ATOM 1 N MET A 1 73.886 27.524 15.764 1.00 38.92 N ANISOU 1 N MET A 1 5098 6097 3592 -1489 447 362 N ATOM 2 CA MET A 1 75.017 28.339 16.187 1.00 39.64 C ANISOU 2 CA MET A 1 4671 6407 3983 -879 140 -405 C ATOM 3 C MET A 1 76.043 27.410 16.820 1.00 37.92 C ANISOU 3 C MET A 1 4914 5679 3813 -933 633 -168 C ATOM 4 O MET A 1 75.639 26.473 17.535 1.00 46.58 O ANISOU 4 O MET A 1 5309 7754 4636 -2033 -63 1256 O ATOM 5 CB MET A 1 74.619 29.419 17.200 1.00 40.12 C ANISOU 5 CB MET A 1 4934 6308 4004 -354 -109 -293 C ATOM 6 CG MET A 1 75.855 30.097 17.786 1.00 43.45 C ANISOU 6 CG MET A 1 5363 6642 4505 -613 -169 -839 C ATOM 7 SD MET A 1 75.460 31.308 19.088 1.00 40.76 S ANISOU 7 SD MET A 1 5716 5321 4449 -844 351 -81 S ATOM 8 CE MET A 1 74.736 32.560 17.975 1.00 40.89 C ANISOU 8 CE MET A 1 5132 5850 4556 -1337 -1383 -497 C ATOM 9 N ARG A 2 77.319 27.649 16.569 1.00 32.45 N ANISOU 9 N ARG A 2 4810 4307 3211 -795 419 -513 N ATOM 10 CA ARG A 2 78.338 26.836 17.234 1.00 31.91 C ANISOU 10 CA ARG A 2 5037 4272 2817 -1111 367 -36 C ATOM 11 C ARG A 2 79.000 27.706 18.296 1.00 31.66 C ANISOU 11 C ARG A 2 4806 4445 2778 -1169 640 -178 C ATOM 12 O ARG A 2 79.134 28.914 18.126 1.00 35.19 O ANISOU 12 O ARG A 2 5848 4297 3224 -928 50 -345 O ATOM 13 CB ARG A 2 79.346 26.287 16.232 1.00 30.78 C ANISOU 13 CB ARG A 2 5683 3264 2747 -322 224 278 C ATOM 14 CG ARG A 2 78.763 25.410 15.130 1.00 31.74 C ANISOU 14 CG ARG A 2 6052 3464 2546 -297 -63 449 C ATOM 15 CD ARG A 2 79.825 25.063 14.088 1.00 34.98 C ANISOU 15 CD ARG A 2 6719 3922 2652 -266 253 153 C ATOM 16 NE ARG A 2 80.869 24.227 14.691 1.00 34.41 N ANISOU 16 NE ARG A 2 6379 4594 2103 -53 429 -191 N ATOM 17 CZ ARG A 2 82.045 23.971 14.154 1.00 36.03 C ANISOU 17 CZ ARG A 2 5807 4903 2981 -919 503 344 C ATOM 18 NH1 ARG A 2 82.323 24.498 12.980 1.00 40.91 N ANISOU 18 NH1 ARG A 2 6260 5762 3522 -1418 799 915 N ATOM 19 NH2 ARG A 2 82.951 23.206 14.749 1.00 34.88 N ANISOU 19 NH2 ARG A 2 5784 4351 3119 -751 335 -382 N ATOM 20 N LEU A 3 79.388 27.089 19.404 1.00 31.74 N ANISOU 20 N LEU A 3 4926 4478 2657 -969 591 -365 N ATOM 21 CA LEU A 3 80.213 27.752 20.403 1.00 30.10 C ANISOU 21 CA LEU A 3 4287 4342 2806 -471 790 -760 C ATOM 22 C LEU A 3 81.495 26.917 20.526 1.00 29.83 C ANISOU 22 C LEU A 3 4583 3777 2975 -455 909 -446 C ATOM 23 O LEU A 3 81.358 25.730 20.826 1.00 32.73 O ANISOU 23 O LEU A 3 5431 3887 3119 -772 569 -246 O ATOM 24 CB LEU A 3 79.522 27.897 21.755 1.00 28.39 C ANISOU 24 CB LEU A 3 3943 4351 2491 -526 530 -177 C ATOM 25 CG LEU A 3 80.334 28.476 22.922 1.00 30.84 C ANISOU 25 CG LEU A 3 4457 4660 2600 -868 475 -330 C ATOM 26 CD1 LEU A 3 80.754 29.901 22.640 1.00 32.59 C ANISOU 26 CD1 LEU A 3 4263 4270 3850 -374 15 -436 C ATOM 27 CD2 LEU A 3 79.534 28.460 24.214 1.00 31.39 C ANISOU 27 CD2 LEU A 3 3956 5259 2710 -90 417 -825 C ATOM 28 N ILE A 4 82.641 27.531 20.272 1.00 29.63 N ANISOU 28 N ILE A 4 4344 3841 3072 -259 982 -342 N ATOM 29 CA ILE A 4 83.914 26.828 20.403 1.00 29.55 C ANISOU 29 CA ILE A 4 4606 3487 3133 -143 936 162 C ATOM 30 C ILE A 4 84.572 27.299 21.691 1.00 30.18 C ANISOU 30 C ILE A 4 4166 4260 3043 -442 1143 178 C ATOM 31 O ILE A 4 85.135 28.408 21.761 1.00 32.25 O ANISOU 31 O ILE A 4 4551 4378 3323 -649 453 454 O ATOM 32 CB ILE A 4 84.857 27.079 19.219 1.00 27.05 C ANISOU 32 CB ILE A 4 3924 3415 2937 -176 550 63 C ATOM 33 CG1 ILE A 4 84.196 27.038 17.840 1.00 29.47 C ANISOU 33 CG1 ILE A 4 4697 3441 3059 -175 216 596 C ATOM 34 CG2 ILE A 4 86.056 26.122 19.281 1.00 27.89 C ANISOU 34 CG2 ILE A 4 4136 3481 2980 -8 132 -560 C ATOM 35 CD1 ILE A 4 83.436 25.774 17.514 1.00 33.52 C ANISOU 35 CD1 ILE A 4 5050 4991 2694 -1287 715 -196 C ATOM 36 N PRO A 5 84.479 26.522 22.757 1.00 32.38 N ANISOU 36 N PRO A 5 4856 4317 3131 -679 830 285 N ATOM 37 CA PRO A 5 85.002 26.971 24.053 1.00 30.96 C ANISOU 37 CA PRO A 5 4547 3924 3290 -305 590 340 C ATOM 38 C PRO A 5 86.470 26.581 24.178 1.00 32.73 C ANISOU 38 C PRO A 5 4676 3912 3847 7 682 -203 C ATOM 39 O PRO A 5 86.785 25.393 24.330 1.00 41.35 O ANISOU 39 O PRO A 5 5900 4187 5623 717 832 -29 O ATOM 40 CB PRO A 5 84.146 26.216 25.062 1.00 31.19 C ANISOU 40 CB PRO A 5 4759 4059 3031 -415 332 559 C ATOM 41 CG PRO A 5 83.260 25.315 24.275 1.00 36.93 C ANISOU 41 CG PRO A 5 6032 5134 2865 -1639 480 549 C ATOM 42 CD PRO A 5 83.873 25.194 22.902 1.00 33.62 C ANISOU 42 CD PRO A 5 5289 4328 3157 -800 506 366 C ATOM 43 N LEU A 6 87.330 27.589 24.100 1.00 33.33 N ANISOU 43 N LEU A 6 4570 4819 3274 -481 776 -193 N ATOM 44 CA LEU A 6 88.751 27.362 24.274 1.00 33.33 C ANISOU 44 CA LEU A 6 4731 4654 3278 -246 525 613 C ATOM 45 C LEU A 6 89.258 28.041 25.537 1.00 31.09 C ANISOU 45 C LEU A 6 4147 4368 3297 279 673 476 C ATOM 46 O LEU A 6 88.590 28.759 26.261 1.00 32.27 O ANISOU 46 O LEU A 6 4119 4542 3601 99 1150 523 O ATOM 47 CB LEU A 6 89.500 27.852 23.012 1.00 30.93 C ANISOU 47 CB LEU A 6 3860 4785 3106 349 44 1093 C ATOM 48 CG LEU A 6 89.072 27.094 21.746 1.00 32.11 C ANISOU 48 CG LEU A 6 4765 4312 3124 71 328 1115 C ATOM 49 CD1 LEU A 6 89.503 27.831 20.486 1.00 35.25 C ANISOU 49 CD1 LEU A 6 5001 5247 3147 -439 1216 761 C ATOM 50 CD2 LEU A 6 89.593 25.659 21.752 1.00 35.77 C ANISOU 50 CD2 LEU A 6 4293 4843 4453 743 779 713 C ATOM 51 N THR A 7 90.546 27.815 25.835 1.00 31.68 N ANISOU 51 N THR A 7 4224 4112 3701 321 509 420 N ATOM 52 CA THR A 7 91.121 28.361 27.054 1.00 33.08 C ANISOU 52 CA THR A 7 4689 4514 3367 118 295 845 C ATOM 53 C THR A 7 91.740 29.731 26.857 1.00 31.24 C ANISOU 53 C THR A 7 3910 4252 3706 464 192 409 C ATOM 54 O THR A 7 91.330 30.641 27.582 1.00 35.37 O ANISOU 54 O THR A 7 6266 4839 2335 243 238 189 O ATOM 55 CB THR A 7 92.190 27.399 27.608 1.00 35.77 C ANISOU 55 CB THR A 7 5099 4124 4366 201 -284 440 C ATOM 56 OG1 THR A 7 91.610 26.092 27.664 1.00 47.75 O ANISOU 56 OG1 THR A 7 8771 4110 5264 -541 -867 1016 O ATOM 57 CG2 THR A 7 92.569 27.792 29.029 1.00 37.28 C ANISOU 57 CG2 THR A 7 4307 5762 4097 -525 -261 1003 C ATOM 58 N THR A 8 92.686 29.876 25.928 1.00 30.84 N ANISOU 58 N THR A 8 4104 4019 3596 438 215 699 N ATOM 59 CA THR A 8 93.446 31.109 25.791 1.00 31.16 C ANISOU 59 CA THR A 8 4406 3978 3457 355 94 571 C ATOM 60 C THR A 8 93.150 31.797 24.451 1.00 30.18 C ANISOU 60 C THR A 8 4125 4102 3240 241 452 507 C ATOM 61 O THR A 8 92.632 31.214 23.508 1.00 31.39 O ANISOU 61 O THR A 8 4238 4017 3672 414 -241 687 O ATOM 62 CB THR A 8 94.959 30.857 25.861 1.00 35.03 C ANISOU 62 CB THR A 8 4296 4909 4104 3 -51 1001 C ATOM 63 OG1 THR A 8 95.295 30.102 24.673 1.00 34.44 O ANISOU 63 OG1 THR A 8 4112 4849 4124 424 677 1479 O ATOM 64 CG2 THR A 8 95.375 29.996 27.046 1.00 37.97 C ANISOU 64 CG2 THR A 8 4096 6196 4135 368 -39 1312 C ATOM 65 N ALA A 9 93.505 33.084 24.418 1.00 32.06 N ANISOU 65 N ALA A 9 4160 4378 3641 -281 174 869 N ATOM 66 CA ALA A 9 93.449 33.861 23.192 1.00 31.04 C ANISOU 66 CA ALA A 9 4421 4042 3330 54 124 490 C ATOM 67 C ALA A 9 94.273 33.204 22.089 1.00 32.92 C ANISOU 67 C ALA A 9 3707 5331 3470 167 -40 180 C ATOM 68 O ALA A 9 93.888 33.213 20.915 1.00 32.03 O ANISOU 68 O ALA A 9 3626 5124 3421 -138 -7 107 O ATOM 69 CB ALA A 9 93.940 35.275 23.456 1.00 30.59 C ANISOU 69 CB ALA A 9 3188 4023 4410 94 -250 811 C ATOM 70 N GLU A 10 95.433 32.627 22.434 1.00 33.85 N ANISOU 70 N GLU A 10 3775 5271 3814 125 16 681 N ATOM 71 CA GLU A 10 96.246 32.055 21.361 1.00 39.43 C ANISOU 71 CA GLU A 10 3560 5969 5451 -195 889 8 C ATOM 72 C GLU A 10 95.497 30.876 20.749 1.00 37.01 C ANISOU 72 C GLU A 10 4141 5260 4661 -46 1227 292 C ATOM 73 O GLU A 10 95.535 30.736 19.527 1.00 32.98 O ANISOU 73 O GLU A 10 3149 4745 4635 151 1622 525 O ATOM 74 CB GLU A 10 97.615 31.568 21.792 1.00 42.67 C ANISOU 74 CB GLU A 10 4032 6783 5397 396 705 329 C ATOM 75 CG GLU A 10 97.958 31.594 23.251 1.00 55.83 C ANISOU 75 CG GLU A 10 6703 8353 6159 -877 -1108 26 C ATOM 76 CD GLU A 10 98.041 32.956 23.906 1.00 68.33 C ANISOU 76 CD GLU A 10 9689 9367 6907 -3509 778 -1069 C ATOM 77 OE1 GLU A 10 97.322 33.133 24.915 1.00 57.50 O ANISOU 77 OE1 GLU A 10 7455 8986 5406 -2363 -1163 -518 O ATOM 78 OE2 GLU A 10 98.816 33.817 23.422 1.00 89.46 O ANISOU 78 OE2 GLU A 10 12970 11278 9744 -5873 3114 -2031 O ATOM 79 N GLN A 11 94.849 30.074 21.586 1.00 33.27 N ANISOU 79 N GLN A 11 4292 4510 3841 620 787 482 N ATOM 80 CA GLN A 11 94.067 28.997 21.005 1.00 33.41 C ANISOU 80 CA GLN A 11 4958 4221 3514 370 560 1011 C ATOM 81 C GLN A 11 92.905 29.552 20.184 1.00 32.06 C ANISOU 81 C GLN A 11 5269 3696 3218 185 402 974 C ATOM 82 O GLN A 11 92.542 29.018 19.130 1.00 32.12 O ANISOU 82 O GLN A 11 4172 4714 3319 -288 990 514 O ATOM 83 CB GLN A 11 93.452 28.088 22.067 1.00 34.19 C ANISOU 83 CB GLN A 11 5234 4412 3344 568 454 1209 C ATOM 84 CG GLN A 11 94.385 27.143 22.799 1.00 37.54 C ANISOU 84 CG GLN A 11 5259 4933 4070 883 549 1570 C ATOM 85 CD GLN A 11 93.637 26.477 23.945 1.00 38.16 C ANISOU 85 CD GLN A 11 6373 4487 3639 963 681 1402 C ATOM 86 OE1 GLN A 11 93.118 27.171 24.813 1.00 42.48 O ANISOU 86 OE1 GLN A 11 6455 5597 4087 -229 922 138 O ATOM 87 NE2 GLN A 11 93.549 25.165 23.965 1.00 52.12 N ANISOU 87 NE2 GLN A 11 9658 4581 5564 324 2102 1353 N ATOM 88 N VAL A 12 92.265 30.612 20.666 1.00 32.02 N ANISOU 88 N VAL A 12 4669 3928 3568 125 474 777 N ATOM 89 CA VAL A 12 91.156 31.147 19.858 1.00 30.86 C ANISOU 89 CA VAL A 12 4315 4473 2937 105 733 602 C ATOM 90 C VAL A 12 91.646 31.589 18.491 1.00 31.72 C ANISOU 90 C VAL A 12 4118 4969 2964 -299 730 513 C ATOM 91 O VAL A 12 91.042 31.303 17.431 1.00 33.07 O ANISOU 91 O VAL A 12 5054 4690 2820 -1018 1080 -72 O ATOM 92 CB VAL A 12 90.501 32.320 20.600 1.00 30.93 C ANISOU 92 CB VAL A 12 4292 4529 2930 249 606 644 C ATOM 93 CG1 VAL A 12 89.601 33.154 19.687 1.00 26.77 C ANISOU 93 CG1 VAL A 12 2518 4821 2832 -406 1004 825 C ATOM 94 CG2 VAL A 12 89.722 31.772 21.799 1.00 27.85 C ANISOU 94 CG2 VAL A 12 4346 3318 2917 63 533 331 C ATOM 95 N GLY A 13 92.765 32.322 18.433 1.00 34.20 N ANISOU 95 N GLY A 13 4049 5732 3212 -520 779 305 N ATOM 96 CA GLY A 13 93.261 32.745 17.110 1.00 29.99 C ANISOU 96 CA GLY A 13 3565 4722 3108 -212 638 236 C ATOM 97 C GLY A 13 93.640 31.543 16.266 1.00 32.48 C ANISOU 97 C GLY A 13 4481 4605 3254 -5 535 274 C ATOM 98 O GLY A 13 93.433 31.523 15.046 1.00 29.43 O ANISOU 98 O GLY A 13 3679 4384 3119 -135 1000 386 O ATOM 99 N LYS A 14 94.208 30.477 16.857 1.00 34.10 N ANISOU 99 N LYS A 14 4805 4698 3454 70 236 279 N ATOM 100 CA LYS A 14 94.589 29.367 15.968 1.00 33.19 C ANISOU 100 CA LYS A 14 3933 4702 3977 -10 646 255 C ATOM 101 C LYS A 14 93.361 28.698 15.380 1.00 32.13 C ANISOU 101 C LYS A 14 3945 4509 3753 -74 844 197 C ATOM 102 O LYS A 14 93.336 28.269 14.227 1.00 30.73 O ANISOU 102 O LYS A 14 3695 4154 3826 518 707 190 O ATOM 103 CB LYS A 14 95.467 28.348 16.707 1.00 35.28 C ANISOU 103 CB LYS A 14 3443 5482 4479 324 1177 812 C ATOM 104 CG LYS A 14 96.887 28.881 16.868 1.00 44.78 C ANISOU 104 CG LYS A 14 3870 7448 5695 -306 234 716 C ATOM 105 CD LYS A 14 97.734 28.140 17.881 1.00 51.11 C ANISOU 105 CD LYS A 14 4335 7781 7302 381 -432 799 C ATOM 106 CE LYS A 14 99.202 28.551 17.790 1.00 59.42 C ANISOU 106 CE LYS A 14 4853 9178 8545 -1037 -1909 511 C ATOM 107 NZ LYS A 14 99.624 29.411 18.938 1.00 82.88 N ANISOU 107 NZ LYS A 14 9491 12124 9874 -4405 -260 -1517 N ATOM 108 N TRP A 15 92.319 28.602 16.188 1.00 32.83 N ANISOU 108 N TRP A 15 3964 4686 3826 16 920 319 N ATOM 109 CA TRP A 15 91.093 27.929 15.770 1.00 31.38 C ANISOU 109 CA TRP A 15 3957 4475 3492 36 838 671 C ATOM 110 C TRP A 15 90.442 28.721 14.644 1.00 30.90 C ANISOU 110 C TRP A 15 4466 4001 3273 -274 838 651 C ATOM 111 O TRP A 15 90.058 28.207 13.587 1.00 30.21 O ANISOU 111 O TRP A 15 3919 3861 3699 -145 576 482 O ATOM 112 CB TRP A 15 90.091 27.742 16.946 1.00 32.35 C ANISOU 112 CB TRP A 15 4518 4618 3156 -598 816 601 C ATOM 113 CG TRP A 15 89.032 26.726 16.554 1.00 32.69 C ANISOU 113 CG TRP A 15 4393 4590 3440 -423 1089 0 C ATOM 114 CD1 TRP A 15 89.026 25.395 16.869 1.00 33.69 C ANISOU 114 CD1 TRP A 15 4677 4557 3565 -529 1072 -65 C ATOM 115 CD2 TRP A 15 87.838 26.952 15.778 1.00 33.36 C ANISOU 115 CD2 TRP A 15 4267 4495 3913 -175 1017 -585 C ATOM 116 NE1 TRP A 15 87.912 24.776 16.343 1.00 35.12 N ANISOU 116 NE1 TRP A 15 4626 4609 4109 -443 1009 -286 N ATOM 117 CE2 TRP A 15 87.166 25.710 15.670 1.00 34.81 C ANISOU 117 CE2 TRP A 15 4363 4726 4137 -481 1105 -233 C ATOM 118 CE3 TRP A 15 87.260 28.073 15.164 1.00 29.62 C ANISOU 118 CE3 TRP A 15 3588 4554 3111 -87 1519 -713 C ATOM 119 CZ2 TRP A 15 85.964 25.555 14.979 1.00 32.81 C ANISOU 119 CZ2 TRP A 15 3755 4507 4204 -110 1598 -773 C ATOM 120 CZ3 TRP A 15 86.074 27.922 14.481 1.00 33.75 C ANISOU 120 CZ3 TRP A 15 4283 5014 3525 -980 862 188 C ATOM 121 CH2 TRP A 15 85.436 26.671 14.396 1.00 35.37 C ANISOU 121 CH2 TRP A 15 4813 4770 3856 -814 679 -158 C ATOM 122 N ALA A 16 90.298 30.016 14.909 1.00 30.94 N ANISOU 122 N ALA A 16 4454 4063 3239 -229 793 488 N ATOM 123 CA ALA A 16 89.678 30.912 13.923 1.00 29.29 C ANISOU 123 CA ALA A 16 3856 4129 3145 116 1164 397 C ATOM 124 C ALA A 16 90.463 30.933 12.623 1.00 29.05 C ANISOU 124 C ALA A 16 3699 4539 2798 -316 790 36 C ATOM 125 O ALA A 16 89.958 30.827 11.508 1.00 33.29 O ANISOU 125 O ALA A 16 4768 4944 2935 -1247 418 291 O ATOM 126 CB ALA A 16 89.597 32.300 14.538 1.00 26.10 C ANISOU 126 CB ALA A 16 2751 4510 2657 366 -21 59 C ATOM 127 N ALA A 17 91.787 31.070 12.753 1.00 30.90 N ANISOU 127 N ALA A 17 3685 4787 3270 -548 1021 78 N ATOM 128 CA ALA A 17 92.625 31.074 11.554 1.00 29.58 C ANISOU 128 CA ALA A 17 3656 4664 2920 9 781 291 C ATOM 129 C ALA A 17 92.506 29.741 10.835 1.00 30.77 C ANISOU 129 C ALA A 17 3429 4455 3808 304 1037 159 C ATOM 130 O ALA A 17 92.382 29.697 9.597 1.00 33.56 O ANISOU 130 O ALA A 17 5242 3549 3961 322 391 -19 O ATOM 131 CB ALA A 17 94.057 31.411 11.930 1.00 31.67 C ANISOU 131 CB ALA A 17 3817 5595 2621 -705 945 938 C ATOM 132 N ARG A 18 92.518 28.614 11.527 1.00 33.37 N ANISOU 132 N ARG A 18 4138 4690 3852 -305 976 359 N ATOM 133 CA ARG A 18 92.355 27.327 10.850 1.00 32.76 C ANISOU 133 CA ARG A 18 3847 4462 4140 76 1273 399 C ATOM 134 C ARG A 18 90.992 27.243 10.164 1.00 31.33 C ANISOU 134 C ARG A 18 4125 3797 3982 276 1024 85 C ATOM 135 O ARG A 18 90.892 26.668 9.055 1.00 36.95 O ANISOU 135 O ARG A 18 4887 4509 4643 82 1079 -703 O ATOM 136 CB ARG A 18 92.540 26.186 11.848 1.00 33.91 C ANISOU 136 CB ARG A 18 3988 4728 4170 240 1013 497 C ATOM 137 CG ARG A 18 92.586 24.801 11.211 1.00 37.46 C ANISOU 137 CG ARG A 18 4925 4534 4776 327 1308 593 C ATOM 138 CD ARG A 18 92.844 23.741 12.285 1.00 41.00 C ANISOU 138 CD ARG A 18 5949 4767 4862 140 1220 802 C ATOM 139 NE ARG A 18 91.681 23.589 13.166 1.00 45.31 N ANISOU 139 NE ARG A 18 6946 5829 4442 -324 1671 479 N ATOM 140 CZ ARG A 18 91.526 22.671 14.098 1.00 50.53 C ANISOU 140 CZ ARG A 18 7873 6006 5319 -150 2270 950 C ATOM 141 NH1 ARG A 18 92.484 21.776 14.305 1.00 60.56 N ANISOU 141 NH1 ARG A 18 8888 7188 6934 529 1145 1804 N ATOM 142 NH2 ARG A 18 90.419 22.651 14.822 1.00 58.04 N ANISOU 142 NH2 ARG A 18 9870 5866 6316 -870 4164 -161 N ATOM 143 N HIS A 19 89.942 27.794 10.773 1.00 30.93 N ANISOU 143 N HIS A 19 4001 3875 3875 385 985 358 N ATOM 144 CA HIS A 19 88.599 27.786 10.178 1.00 29.19 C ANISOU 144 CA HIS A 19 4131 3571 3390 299 962 56 C ATOM 145 C HIS A 19 88.612 28.557 8.860 1.00 30.19 C ANISOU 145 C HIS A 19 4403 3642 3426 10 894 90 C ATOM 146 O HIS A 19 88.139 28.141 7.796 1.00 36.06 O ANISOU 146 O HIS A 19 6311 3812 3577 -286 289 203 O ATOM 147 CB HIS A 19 87.559 28.374 11.144 1.00 28.79 C ANISOU 147 CB HIS A 19 4045 3511 3382 510 825 102 C ATOM 148 CG HIS A 19 86.151 28.167 10.684 1.00 30.50 C ANISOU 148 CG HIS A 19 4090 3803 3695 373 813 -201 C ATOM 149 ND1 HIS A 19 85.555 26.935 10.577 1.00 33.56 N ANISOU 149 ND1 HIS A 19 4787 3990 3973 -5 382 44 N ATOM 150 CD2 HIS A 19 85.196 29.052 10.285 1.00 31.72 C ANISOU 150 CD2 HIS A 19 3922 3984 4146 448 549 -610 C ATOM 151 CE1 HIS A 19 84.311 27.049 10.146 1.00 34.20 C ANISOU 151 CE1 HIS A 19 4915 4265 3813 -128 130 -220 C ATOM 152 NE2 HIS A 19 84.069 28.334 9.959 1.00 34.50 N ANISOU 152 NE2 HIS A 19 4320 4316 4472 92 236 -445 N ATOM 153 N ILE A 20 89.198 29.755 8.918 1.00 33.50 N ANISOU 153 N ILE A 20 4840 4222 3665 -726 1231 153 N ATOM 154 CA ILE A 20 89.310 30.603 7.717 1.00 32.34 C ANISOU 154 CA ILE A 20 4869 3846 3575 -275 1542 -52 C ATOM 155 C ILE A 20 90.043 29.836 6.629 1.00 33.02 C ANISOU 155 C ILE A 20 4689 4221 3637 -170 1282 -341 C ATOM 156 O ILE A 20 89.535 29.758 5.507 1.00 35.06 O ANISOU 156 O ILE A 20 5147 4395 3778 -369 1052 -545 O ATOM 157 CB ILE A 20 90.000 31.941 8.049 1.00 31.64 C ANISOU 157 CB ILE A 20 4972 3796 3253 -249 1104 99 C ATOM 158 CG1 ILE A 20 89.183 32.848 8.978 1.00 27.21 C ANISOU 158 CG1 ILE A 20 4083 3578 2679 -480 788 382 C ATOM 159 CG2 ILE A 20 90.379 32.667 6.768 1.00 30.74 C ANISOU 159 CG2 ILE A 20 4222 4101 3356 -234 1397 63 C ATOM 160 CD1 ILE A 20 89.917 34.046 9.539 1.00 27.95 C ANISOU 160 CD1 ILE A 20 3960 3676 2983 -143 98 227 C ATOM 161 N VAL A 21 91.191 29.265 6.964 1.00 33.86 N ANISOU 161 N VAL A 21 4471 4460 3934 -273 1515 -76 N ATOM 162 CA VAL A 21 91.984 28.511 5.993 1.00 34.17 C ANISOU 162 CA VAL A 21 4534 4381 4068 -123 1204 -318 C ATOM 163 C VAL A 21 91.187 27.368 5.373 1.00 36.10 C ANISOU 163 C VAL A 21 5749 4619 3350 -662 814 77 C ATOM 164 O VAL A 21 91.172 27.099 4.165 1.00 37.00 O ANISOU 164 O VAL A 21 6030 4317 3713 -347 2338 -810 O ATOM 165 CB VAL A 21 93.264 27.964 6.663 1.00 37.20 C ANISOU 165 CB VAL A 21 4646 4993 4495 100 1086 -325 C ATOM 166 CG1 VAL A 21 93.908 26.903 5.769 1.00 33.39 C ANISOU 166 CG1 VAL A 21 3606 5524 3557 -231 1759 143 C ATOM 167 CG2 VAL A 21 94.219 29.104 6.988 1.00 37.04 C ANISOU 167 CG2 VAL A 21 4146 5571 4354 -179 1433 -119 C ATOM 168 N ASN A 22 90.472 26.638 6.221 1.00 35.42 N ANISOU 168 N ASN A 22 5578 4810 3072 -833 684 -45 N ATOM 169 CA ASN A 22 89.694 25.515 5.709 1.00 36.23 C ANISOU 169 CA ASN A 22 5802 4366 3596 -598 428 13 C ATOM 170 C ASN A 22 88.552 26.003 4.835 1.00 35.13 C ANISOU 170 C ASN A 22 5692 4331 3324 -622 502 -178 C ATOM 171 O ASN A 22 88.227 25.385 3.817 1.00 37.68 O ANISOU 171 O ASN A 22 5612 5340 3365 -947 734 -548 O ATOM 172 CB ASN A 22 89.211 24.667 6.888 1.00 39.79 C ANISOU 172 CB ASN A 22 6436 4639 4041 -967 142 475 C ATOM 173 CG ASN A 22 90.333 23.912 7.582 1.00 45.83 C ANISOU 173 CG ASN A 22 7258 5374 4783 -947 -662 925 C ATOM 174 OD1 ASN A 22 90.076 23.299 8.618 1.00 54.80 O ANISOU 174 OD1 ASN A 22 8143 7299 5378 -1210 -963 2065 O ATOM 175 ND2 ASN A 22 91.558 23.916 7.072 1.00 45.89 N ANISOU 175 ND2 ASN A 22 7308 5443 4685 354 -589 472 N ATOM 176 N ARG A 23 87.906 27.118 5.167 1.00 35.83 N ANISOU 176 N ARG A 23 5833 4392 3389 -470 976 198 N ATOM 177 CA ARG A 23 86.873 27.607 4.253 1.00 33.81 C ANISOU 177 CA ARG A 23 5251 4775 2818 -351 1334 -299 C ATOM 178 C ARG A 23 87.486 28.020 2.927 1.00 34.96 C ANISOU 178 C ARG A 23 5254 5289 2741 -722 1197 -306 C ATOM 179 O ARG A 23 86.944 27.705 1.869 1.00 36.82 O ANISOU 179 O ARG A 23 5818 5426 2745 -279 1168 -752 O ATOM 180 CB ARG A 23 86.143 28.803 4.866 1.00 35.25 C ANISOU 180 CB ARG A 23 5146 4909 3337 -363 1235 -638 C ATOM 181 CG ARG A 23 85.272 28.311 6.006 1.00 30.89 C ANISOU 181 CG ARG A 23 4207 4471 3060 112 732 -412 C ATOM 182 CD ARG A 23 84.107 27.471 5.461 1.00 38.51 C ANISOU 182 CD ARG A 23 5582 5100 3950 -1057 249 -41 C ATOM 183 NE ARG A 23 83.124 27.351 6.551 1.00 40.05 N ANISOU 183 NE ARG A 23 4953 5583 4681 -1159 237 382 N ATOM 184 CZ ARG A 23 82.413 26.270 6.836 1.00 46.54 C ANISOU 184 CZ ARG A 23 6432 5918 5332 -1957 791 -23 C ATOM 185 NH1 ARG A 23 82.581 25.183 6.078 1.00 45.47 N ANISOU 185 NH1 ARG A 23 6255 5597 5424 -1602 1236 316 N ATOM 186 NH2 ARG A 23 81.561 26.295 7.857 1.00 39.35 N ANISOU 186 NH2 ARG A 23 5844 4406 4700 -1401 167 496 N ATOM 187 N ILE A 24 88.616 28.728 2.986 1.00 36.60 N ANISOU 187 N ILE A 24 5032 5082 3794 -531 1463 -307 N ATOM 188 CA ILE A 24 89.231 29.130 1.727 1.00 36.12 C ANISOU 188 CA ILE A 24 4944 4952 3828 -444 1575 -410 C ATOM 189 C ILE A 24 89.668 27.921 0.917 1.00 37.86 C ANISOU 189 C ILE A 24 5388 5292 3707 -139 1001 -707 C ATOM 190 O ILE A 24 89.477 27.810 -0.298 1.00 43.09 O ANISOU 190 O ILE A 24 6870 5635 3868 -744 545 -885 O ATOM 191 CB ILE A 24 90.438 30.048 1.987 1.00 33.76 C ANISOU 191 CB ILE A 24 4106 5106 3616 84 1724 -768 C ATOM 192 CG1 ILE A 24 90.045 31.410 2.548 1.00 32.78 C ANISOU 192 CG1 ILE A 24 4389 4766 3300 68 1392 -388 C ATOM 193 CG2 ILE A 24 91.278 30.191 0.709 1.00 35.69 C ANISOU 193 CG2 ILE A 24 3904 6526 3130 -272 1273 -1019 C ATOM 194 CD1 ILE A 24 91.165 32.174 3.200 1.00 33.70 C ANISOU 194 CD1 ILE A 24 4440 4508 3855 -216 1429 -75 C ATOM 195 N ASN A 25 90.295 26.930 1.557 1.00 39.70 N ANISOU 195 N ASN A 25 5448 5176 4462 -73 823 -715 N ATOM 196 CA ASN A 25 90.820 25.829 0.743 1.00 38.29 C ANISOU 196 CA ASN A 25 4951 5480 4118 -75 1363 -477 C ATOM 197 C ASN A 25 89.678 24.985 0.207 1.00 38.36 C ANISOU 197 C ASN A 25 5064 5487 4025 -82 1665 -1018 C ATOM 198 O ASN A 25 89.736 24.399 -0.884 1.00 45.52 O ANISOU 198 O ASN A 25 6670 6190 4436 -504 2035 -1597 O ATOM 199 CB ASN A 25 91.847 25.028 1.545 1.00 38.75 C ANISOU 199 CB ASN A 25 5514 5043 4167 -147 1240 -254 C ATOM 200 CG ASN A 25 93.174 25.746 1.724 1.00 37.94 C ANISOU 200 CG ASN A 25 4753 5011 4650 399 1590 199 C ATOM 201 OD1 ASN A 25 93.513 26.640 0.942 1.00 43.68 O ANISOU 201 OD1 ASN A 25 5939 5284 5373 -193 1400 577 O ATOM 202 ND2 ASN A 25 93.978 25.418 2.725 1.00 38.06 N ANISOU 202 ND2 ASN A 25 5159 4318 4983 639 1083 -371 N ATOM 203 N ALA A 26 88.550 24.890 0.909 1.00 39.03 N ANISOU 203 N ALA A 26 5387 5650 3794 -559 1731 -124 N ATOM 204 CA ALA A 26 87.475 24.055 0.356 1.00 39.56 C ANISOU 204 CA ALA A 26 5776 5022 4232 -740 1787 -16 C ATOM 205 C ALA A 26 86.755 24.756 -0.785 1.00 39.68 C ANISOU 205 C ALA A 26 6338 4625 4112 -760 1116 -698 C ATOM 206 O ALA A 26 86.208 24.106 -1.665 1.00 47.53 O ANISOU 206 O ALA A 26 9724 4861 3475 -1902 1068 -498 O ATOM 207 CB ALA A 26 86.466 23.705 1.440 1.00 36.18 C ANISOU 207 CB ALA A 26 5123 4342 4282 -55 1936 -723 C ATOM 208 N PHE A 27 86.749 26.085 -0.747 1.00 38.35 N ANISOU 208 N PHE A 27 5942 4615 4013 -405 1029 -920 N ATOM 209 CA PHE A 27 86.069 26.904 -1.742 1.00 40.04 C ANISOU 209 CA PHE A 27 6188 5010 4013 -384 1177 -579 C ATOM 210 C PHE A 27 86.834 26.957 -3.060 1.00 41.26 C ANISOU 210 C PHE A 27 6808 4817 4051 -346 1448 -885 C ATOM 211 O PHE A 27 86.214 27.059 -4.118 1.00 41.16 O ANISOU 211 O PHE A 27 7394 4144 4103 -954 1316 -139 O ATOM 212 CB PHE A 27 85.906 28.327 -1.233 1.00 37.50 C ANISOU 212 CB PHE A 27 5627 5273 3349 184 623 -681 C ATOM 213 CG PHE A 27 85.154 29.329 -2.088 1.00 36.10 C ANISOU 213 CG PHE A 27 4925 5379 3413 -351 584 -349 C ATOM 214 CD1 PHE A 27 83.791 29.480 -1.918 1.00 36.57 C ANISOU 214 CD1 PHE A 27 4890 5474 3529 -493 506 -721 C ATOM 215 CD2 PHE A 27 85.803 30.107 -3.031 1.00 37.55 C ANISOU 215 CD2 PHE A 27 5136 5593 3540 -1063 296 -375 C ATOM 216 CE1 PHE A 27 83.090 30.386 -2.673 1.00 37.05 C ANISOU 216 CE1 PHE A 27 4493 5781 3805 -495 810 -343 C ATOM 217 CE2 PHE A 27 85.104 31.031 -3.791 1.00 38.14 C ANISOU 217 CE2 PHE A 27 4737 5829 3926 -1438 374 177 C ATOM 218 CZ PHE A 27 83.741 31.183 -3.601 1.00 39.50 C ANISOU 218 CZ PHE A 27 4809 6140 4058 -1157 437 -99 C ATOM 219 N LYS A 28 88.155 26.900 -2.963 1.00 44.61 N ANISOU 219 N LYS A 28 6756 5747 4445 -570 1777 -641 N ATOM 220 CA LYS A 28 89.013 26.896 -4.151 1.00 46.21 C ANISOU 220 CA LYS A 28 7387 5462 4708 -684 2205 -620 C ATOM 221 C LYS A 28 88.821 28.146 -5.006 1.00 44.35 C ANISOU 221 C LYS A 28 7283 5607 3960 -986 1123 -833 C ATOM 222 O LYS A 28 88.325 28.055 -6.132 1.00 49.03 O ANISOU 222 O LYS A 28 8259 6865 3505 -1735 1498 -1172 O ATOM 223 CB LYS A 28 88.742 25.646 -4.998 1.00 52.78 C ANISOU 223 CB LYS A 28 8806 5571 5675 -713 2907 -1237 C ATOM 224 CG LYS A 28 89.209 24.366 -4.336 1.00 62.04 C ANISOU 224 CG LYS A 28 10735 5380 7459 -1095 2638 -533 C ATOM 225 CD LYS A 28 88.149 23.271 -4.342 1.00 83.37 C ANISOU 225 CD LYS A 28 14704 6945 10028 -3815 2545 -213 C ATOM 226 CE LYS A 28 88.094 22.536 -3.007 1.00 92.61 C ANISOU 226 CE LYS A 28 16511 7514 11163 -4622 2424 933 C ATOM 227 NZ LYS A 28 86.787 21.880 -2.720 1.00103.41 N ANISOU 227 NZ LYS A 28 18273 7587 13433 -5443 6133 -1423 N ATOM 228 N PRO A 29 89.213 29.296 -4.467 1.00 39.46 N ANISOU 228 N PRO A 29 5785 5362 3845 -424 1002 -725 N ATOM 229 CA PRO A 29 88.938 30.583 -5.105 1.00 37.54 C ANISOU 229 CA PRO A 29 5009 5543 3711 -230 939 -695 C ATOM 230 C PRO A 29 89.768 30.787 -6.363 1.00 41.25 C ANISOU 230 C PRO A 29 6231 5831 3612 -708 1172 -774 C ATOM 231 O PRO A 29 90.880 30.266 -6.441 1.00 43.73 O ANISOU 231 O PRO A 29 5745 6606 4264 -1134 1934 -461 O ATOM 232 CB PRO A 29 89.391 31.591 -4.037 1.00 35.65 C ANISOU 232 CB PRO A 29 4574 5268 3702 -35 1111 -669 C ATOM 233 CG PRO A 29 90.476 30.857 -3.307 1.00 36.41 C ANISOU 233 CG PRO A 29 5121 5152 3560 33 908 -576 C ATOM 234 CD PRO A 29 89.953 29.444 -3.199 1.00 38.15 C ANISOU 234 CD PRO A 29 5260 5248 3985 -108 942 -559 C ATOM 235 N THR A 30 89.213 31.544 -7.303 1.00 45.50 N ANISOU 235 N THR A 30 7490 6010 3786 -1299 469 -481 N ATOM 236 CA THR A 30 89.939 31.910 -8.513 1.00 46.83 C ANISOU 236 CA THR A 30 7609 6480 3702 -1843 299 -454 C ATOM 237 C THR A 30 89.757 33.396 -8.814 1.00 50.02 C ANISOU 237 C THR A 30 8268 6557 4179 -1744 797 -198 C ATOM 238 O THR A 30 88.984 34.085 -8.143 1.00 52.51 O ANISOU 238 O THR A 30 8664 6438 4849 -1677 1162 -222 O ATOM 239 CB THR A 30 89.483 31.092 -9.736 1.00 44.09 C ANISOU 239 CB THR A 30 6711 6582 3459 -1159 -332 -109 C ATOM 240 OG1 THR A 30 88.101 31.367 -9.987 1.00 46.64 O ANISOU 240 OG1 THR A 30 6551 7076 4093 -953 237 201 O ATOM 241 CG2 THR A 30 89.586 29.601 -9.459 1.00 42.08 C ANISOU 241 CG2 THR A 30 7296 6431 2261 -443 1449 -777 C ATOM 242 N ALA A 31 90.477 33.865 -9.833 1.00 52.97 N ANISOU 242 N ALA A 31 8827 7004 4296 -1634 985 127 N ATOM 243 CA ALA A 31 90.433 35.260 -10.249 1.00 53.78 C ANISOU 243 CA ALA A 31 9115 6975 4346 -1331 1698 68 C ATOM 244 C ALA A 31 88.995 35.728 -10.457 1.00 54.14 C ANISOU 244 C ALA A 31 9096 7145 4330 -1356 1670 468 C ATOM 245 O ALA A 31 88.646 36.856 -10.116 1.00 56.11 O ANISOU 245 O ALA A 31 9632 7247 4442 -738 -88 303 O ATOM 246 CB ALA A 31 91.236 35.474 -11.528 1.00 55.18 C ANISOU 246 CB ALA A 31 9035 7432 4499 -1937 1730 -40 C ATOM 247 N ASP A 32 88.184 34.840 -11.027 1.00 54.17 N ANISOU 247 N ASP A 32 8981 7218 4383 -1307 1864 231 N ATOM 248 CA ASP A 32 86.805 35.163 -11.381 1.00 56.83 C ANISOU 248 CA ASP A 32 9268 7418 4908 -1227 1294 339 C ATOM 249 C ASP A 32 85.808 34.687 -10.328 1.00 53.60 C ANISOU 249 C ASP A 32 8274 6953 5141 -1152 740 731 C ATOM 250 O ASP A 32 84.615 35.004 -10.409 1.00 51.86 O ANISOU 250 O ASP A 32 8029 7728 3949 -1792 -388 384 O ATOM 251 CB ASP A 32 86.477 34.574 -12.756 1.00 62.94 C ANISOU 251 CB ASP A 32 10524 8347 5042 -1065 743 143 C ATOM 252 CG ASP A 32 87.205 35.324 -13.863 1.00 73.31 C ANISOU 252 CG ASP A 32 14176 8786 4892 -2321 1926 -630 C ATOM 253 OD1 ASP A 32 87.268 36.580 -13.833 1.00 85.57 O ANISOU 253 OD1 ASP A 32 18137 8895 5480 -4880 594 -885 O ATOM 254 OD2 ASP A 32 87.738 34.671 -14.794 1.00102.79 O ANISOU 254 OD2 ASP A 32 18775 12167 8113 -4367 5851 -3177 O ATOM 255 N ARG A 33 86.291 33.935 -9.342 1.00 47.75 N ANISOU 255 N ARG A 33 7703 6550 3890 -716 804 -507 N ATOM 256 CA ARG A 33 85.441 33.504 -8.237 1.00 44.00 C ANISOU 256 CA ARG A 33 6663 6144 3912 -801 287 -402 C ATOM 257 C ARG A 33 86.283 33.552 -6.962 1.00 42.40 C ANISOU 257 C ARG A 33 6310 5814 3985 -788 346 -194 C ATOM 258 O ARG A 33 86.783 32.519 -6.509 1.00 42.09 O ANISOU 258 O ARG A 33 6755 5625 3612 -979 834 113 O ATOM 259 CB ARG A 33 84.844 32.114 -8.450 1.00 46.13 C ANISOU 259 CB ARG A 33 6191 6304 5030 -675 436 -1107 C ATOM 260 CG ARG A 33 83.569 31.905 -7.647 1.00 48.91 C ANISOU 260 CG ARG A 33 5890 6223 6471 -488 610 -650 C ATOM 261 CD ARG A 33 83.180 30.430 -7.574 1.00 50.23 C ANISOU 261 CD ARG A 33 5725 6018 7342 -54 992 -652 C ATOM 262 NE ARG A 33 84.348 29.625 -7.268 1.00 54.48 N ANISOU 262 NE ARG A 33 6214 6723 7762 313 312 -655 N ATOM 263 CZ ARG A 33 84.512 28.676 -6.365 1.00 51.40 C ANISOU 263 CZ ARG A 33 5936 6491 7104 380 692 -1028 C ATOM 264 NH1 ARG A 33 83.574 28.271 -5.531 1.00 45.95 N ANISOU 264 NH1 ARG A 33 5864 5661 5935 -359 383 -2613 N ATOM 265 NH2 ARG A 33 85.717 28.113 -6.324 1.00 51.57 N ANISOU 265 NH2 ARG A 33 6382 6499 6714 886 1086 -1189 N ATOM 266 N PRO A 34 86.435 34.767 -6.450 1.00 38.08 N ANISOU 266 N PRO A 34 5036 5895 3539 -293 777 -377 N ATOM 267 CA PRO A 34 87.216 34.960 -5.230 1.00 37.24 C ANISOU 267 CA PRO A 34 5165 5475 3510 -542 698 62 C ATOM 268 C PRO A 34 86.453 34.532 -3.981 1.00 37.15 C ANISOU 268 C PRO A 34 4964 5495 3654 -911 572 154 C ATOM 269 O PRO A 34 85.227 34.548 -3.978 1.00 34.83 O ANISOU 269 O PRO A 34 4961 4858 3415 -1190 232 197 O ATOM 270 CB PRO A 34 87.407 36.482 -5.192 1.00 34.64 C ANISOU 270 CB PRO A 34 3958 5439 3767 -423 591 302 C ATOM 271 CG PRO A 34 86.199 37.026 -5.894 1.00 34.98 C ANISOU 271 CG PRO A 34 4129 5589 3573 -786 -2 -77 C ATOM 272 CD PRO A 34 85.905 36.032 -6.978 1.00 35.93 C ANISOU 272 CD PRO A 34 4820 5946 2885 -437 898 -291 C ATOM 273 N PHE A 35 87.173 34.180 -2.927 1.00 33.50 N ANISOU 273 N PHE A 35 4323 4795 3610 -209 1093 92 N ATOM 274 CA PHE A 35 86.640 34.012 -1.582 1.00 34.47 C ANISOU 274 CA PHE A 35 4715 4901 3480 -303 1108 -166 C ATOM 275 C PHE A 35 86.574 35.381 -0.920 1.00 30.80 C ANISOU 275 C PHE A 35 3745 4708 3249 -133 283 80 C ATOM 276 O PHE A 35 87.579 36.103 -0.859 1.00 34.69 O ANISOU 276 O PHE A 35 4370 5498 3313 -953 865 102 O ATOM 277 CB PHE A 35 87.526 33.090 -0.763 1.00 31.19 C ANISOU 277 CB PHE A 35 4628 4378 2845 -147 1408 -659 C ATOM 278 CG PHE A 35 86.882 32.720 0.575 1.00 32.85 C ANISOU 278 CG PHE A 35 4726 4756 2998 -563 1396 -552 C ATOM 279 CD1 PHE A 35 86.031 31.635 0.648 1.00 34.09 C ANISOU 279 CD1 PHE A 35 4555 4989 3409 -659 1006 -231 C ATOM 280 CD2 PHE A 35 87.155 33.469 1.701 1.00 32.16 C ANISOU 280 CD2 PHE A 35 4104 5072 3044 -292 1803 -911 C ATOM 281 CE1 PHE A 35 85.433 31.286 1.844 1.00 36.47 C ANISOU 281 CE1 PHE A 35 5383 4816 3659 -970 1408 -344 C ATOM 282 CE2 PHE A 35 86.555 33.117 2.908 1.00 32.59 C ANISOU 282 CE2 PHE A 35 4209 5400 2773 -710 1003 -232 C ATOM 283 CZ PHE A 35 85.702 32.023 2.986 1.00 31.87 C ANISOU 283 CZ PHE A 35 4006 4644 3461 -139 1146 -158 C ATOM 284 N VAL A 36 85.407 35.760 -0.421 1.00 31.61 N ANISOU 284 N VAL A 36 4174 4493 3343 -147 942 418 N ATOM 285 CA VAL A 36 85.235 37.101 0.130 1.00 31.43 C ANISOU 285 CA VAL A 36 4778 4483 2682 123 698 564 C ATOM 286 C VAL A 36 85.199 37.031 1.656 1.00 32.63 C ANISOU 286 C VAL A 36 5038 4700 2660 -862 252 757 C ATOM 287 O VAL A 36 84.332 36.337 2.212 1.00 32.32 O ANISOU 287 O VAL A 36 4713 5181 2386 -1089 704 -255 O ATOM 288 CB VAL A 36 83.985 37.798 -0.432 1.00 31.27 C ANISOU 288 CB VAL A 36 4827 4559 2494 99 136 -277 C ATOM 289 CG1 VAL A 36 83.889 39.225 0.092 1.00 27.48 C ANISOU 289 CG1 VAL A 36 3380 4632 2430 -165 -163 -417 C ATOM 290 CG2 VAL A 36 84.006 37.784 -1.975 1.00 28.93 C ANISOU 290 CG2 VAL A 36 3655 4842 2496 -270 474 -500 C ATOM 291 N LEU A 37 86.137 37.725 2.289 1.00 30.67 N ANISOU 291 N LEU A 37 4517 4144 2994 -623 685 483 N ATOM 292 CA LEU A 37 86.402 37.654 3.714 1.00 28.29 C ANISOU 292 CA LEU A 37 3603 4101 3043 -644 539 372 C ATOM 293 C LEU A 37 86.160 38.996 4.386 1.00 28.55 C ANISOU 293 C LEU A 37 3493 4173 3181 -461 441 330 C ATOM 294 O LEU A 37 86.843 39.945 3.993 1.00 29.10 O ANISOU 294 O LEU A 37 3783 3994 3281 -337 844 224 O ATOM 295 CB LEU A 37 87.864 37.336 3.977 1.00 32.82 C ANISOU 295 CB LEU A 37 3775 4139 4557 -272 387 425 C ATOM 296 CG LEU A 37 88.391 36.288 4.940 1.00 32.63 C ANISOU 296 CG LEU A 37 3723 5069 3608 -636 -25 474 C ATOM 297 CD1 LEU A 37 89.815 36.658 5.353 1.00 32.91 C ANISOU 297 CD1 LEU A 37 4935 4662 2905 -2002 -779 347 C ATOM 298 CD2 LEU A 37 87.535 36.051 6.170 1.00 28.13 C ANISOU 298 CD2 LEU A 37 4074 4126 2488 234 -64 -1156 C ATOM 299 N GLY A 38 85.273 39.070 5.367 1.00 29.00 N ANISOU 299 N GLY A 38 3598 4227 3192 -802 506 96 N ATOM 300 CA GLY A 38 85.070 40.306 6.116 1.00 27.79 C ANISOU 300 CA GLY A 38 3542 4232 2786 -519 8 203 C ATOM 301 C GLY A 38 85.936 40.280 7.378 1.00 28.30 C ANISOU 301 C GLY A 38 3406 4072 3273 -349 -292 388 C ATOM 302 O GLY A 38 86.085 39.224 8.007 1.00 26.56 O ANISOU 302 O GLY A 38 3348 4128 2614 -59 648 328 O ATOM 303 N LEU A 39 86.527 41.420 7.737 1.00 26.66 N ANISOU 303 N LEU A 39 3158 3916 3056 106 -40 -130 N ATOM 304 CA LEU A 39 87.551 41.446 8.770 1.00 26.08 C ANISOU 304 CA LEU A 39 2896 3741 3271 159 -45 -11 C ATOM 305 C LEU A 39 87.395 42.588 9.751 1.00 25.74 C ANISOU 305 C LEU A 39 3267 3450 3064 -333 27 177 C ATOM 306 O LEU A 39 86.958 43.677 9.390 1.00 27.38 O ANISOU 306 O LEU A 39 3133 3840 3430 335 36 -56 O ATOM 307 CB LEU A 39 88.936 41.586 8.105 1.00 28.35 C ANISOU 307 CB LEU A 39 3119 4457 3196 -71 160 283 C ATOM 308 CG LEU A 39 89.359 40.380 7.265 1.00 29.90 C ANISOU 308 CG LEU A 39 3207 4583 3570 -75 755 292 C ATOM 309 CD1 LEU A 39 90.745 40.602 6.651 1.00 28.57 C ANISOU 309 CD1 LEU A 39 3188 5131 2536 -340 361 570 C ATOM 310 CD2 LEU A 39 89.337 39.092 8.084 1.00 29.84 C ANISOU 310 CD2 LEU A 39 3316 4361 3659 -386 957 143 C ATOM 311 N PRO A 40 87.741 42.372 11.005 1.00 27.30 N ANISOU 311 N PRO A 40 3357 4166 2850 -156 495 260 N ATOM 312 CA PRO A 40 87.795 43.438 12.005 1.00 27.80 C ANISOU 312 CA PRO A 40 3695 4172 2697 -269 673 271 C ATOM 313 C PRO A 40 89.201 43.833 12.426 1.00 29.36 C ANISOU 313 C PRO A 40 3953 3855 3348 -565 426 409 C ATOM 314 O PRO A 40 90.193 43.211 12.023 1.00 28.16 O ANISOU 314 O PRO A 40 3646 3956 3097 -554 -80 202 O ATOM 315 CB PRO A 40 87.133 42.699 13.188 1.00 26.34 C ANISOU 315 CB PRO A 40 3850 3430 2729 -341 378 300 C ATOM 316 CG PRO A 40 87.726 41.330 13.079 1.00 26.74 C ANISOU 316 CG PRO A 40 3569 3895 2697 62 756 21 C ATOM 317 CD PRO A 40 88.037 41.065 11.617 1.00 26.74 C ANISOU 317 CD PRO A 40 3568 4218 2373 -160 163 111 C ATOM 318 N THR A 41 89.290 44.869 13.253 1.00 30.65 N ANISOU 318 N THR A 41 4076 4449 3119 -593 654 129 N ATOM 319 CA THR A 41 90.554 45.349 13.782 1.00 32.57 C ANISOU 319 CA THR A 41 4423 4492 3462 -721 316 55 C ATOM 320 C THR A 41 90.480 45.324 15.309 1.00 34.25 C ANISOU 320 C THR A 41 4493 5077 3445 -735 278 149 C ATOM 321 O THR A 41 89.474 44.872 15.870 1.00 39.20 O ANISOU 321 O THR A 41 4684 6525 3685 -983 561 213 O ATOM 322 CB THR A 41 90.949 46.766 13.323 1.00 33.71 C ANISOU 322 CB THR A 41 5253 4338 3216 -1003 374 -341 C ATOM 323 OG1 THR A 41 89.957 47.696 13.779 1.00 36.62 O ANISOU 323 OG1 THR A 41 6285 4357 3273 -747 1025 -314 O ATOM 324 CG2 THR A 41 90.977 46.929 11.816 1.00 31.31 C ANISOU 324 CG2 THR A 41 5179 3499 3219 550 189 -159 C ATOM 325 N GLY A 42 91.514 45.792 15.981 1.00 36.09 N ANISOU 325 N GLY A 42 4541 5612 3561 -598 114 26 N ATOM 326 CA GLY A 42 91.569 45.864 17.422 1.00 36.71 C ANISOU 326 CA GLY A 42 4990 5433 3523 -684 16 166 C ATOM 327 C GLY A 42 92.370 44.743 18.036 1.00 35.57 C ANISOU 327 C GLY A 42 4942 5088 3485 -742 147 -25 C ATOM 328 O GLY A 42 92.964 43.895 17.403 1.00 35.05 O ANISOU 328 O GLY A 42 5529 4786 3001 -940 306 113 O ATOM 329 N GLY A 43 92.418 44.707 19.365 1.00 34.07 N ANISOU 329 N GLY A 43 4938 4519 3487 -272 530 59 N ATOM 330 CA GLY A 43 93.203 43.700 20.069 1.00 33.79 C ANISOU 330 CA GLY A 43 4362 4499 3976 -767 424 439 C ATOM 331 C GLY A 43 92.603 42.312 19.931 1.00 31.78 C ANISOU 331 C GLY A 43 4012 4468 3594 -551 440 29 C ATOM 332 O GLY A 43 93.338 41.325 19.951 1.00 32.96 O ANISOU 332 O GLY A 43 4103 4546 3873 -467 797 284 O ATOM 333 N THR A 44 91.287 42.204 19.795 1.00 30.70 N ANISOU 333 N THR A 44 3928 4790 2946 -615 788 -67 N ATOM 334 CA THR A 44 90.646 40.888 19.768 1.00 31.56 C ANISOU 334 CA THR A 44 4083 4857 3050 -743 580 -30 C ATOM 335 C THR A 44 91.109 39.998 18.637 1.00 27.57 C ANISOU 335 C THR A 44 3397 4242 2838 -98 107 451 C ATOM 336 O THR A 44 91.453 38.837 18.901 1.00 29.25 O ANISOU 336 O THR A 44 2870 4461 3782 -108 348 1007 O ATOM 337 CB THR A 44 89.107 41.052 19.703 1.00 32.96 C ANISOU 337 CB THR A 44 4063 4366 4094 -645 1021 -659 C ATOM 338 OG1 THR A 44 88.657 41.577 20.965 1.00 40.12 O ANISOU 338 OG1 THR A 44 5055 5581 4609 -1401 1930 -1118 O ATOM 339 CG2 THR A 44 88.401 39.724 19.525 1.00 30.57 C ANISOU 339 CG2 THR A 44 4264 4209 3141 -760 433 432 C ATOM 340 N PRO A 45 91.125 40.392 17.366 1.00 27.52 N ANISOU 340 N PRO A 45 3448 4170 2840 -157 392 440 N ATOM 341 CA PRO A 45 91.638 39.466 16.355 1.00 28.21 C ANISOU 341 CA PRO A 45 3447 4269 3002 63 271 322 C ATOM 342 C PRO A 45 93.157 39.372 16.276 1.00 28.67 C ANISOU 342 C PRO A 45 3466 4244 3183 199 52 130 C ATOM 343 O PRO A 45 93.654 38.700 15.366 1.00 29.73 O ANISOU 343 O PRO A 45 3427 4747 3122 -639 856 110 O ATOM 344 CB PRO A 45 91.103 40.090 15.047 1.00 26.66 C ANISOU 344 CB PRO A 45 3291 3904 2934 -104 69 9 C ATOM 345 CG PRO A 45 90.992 41.560 15.340 1.00 26.85 C ANISOU 345 CG PRO A 45 3873 3958 2372 -165 -185 -94 C ATOM 346 CD PRO A 45 90.629 41.660 16.809 1.00 28.88 C ANISOU 346 CD PRO A 45 4611 3828 2536 -229 346 252 C ATOM 347 N MET A 46 93.980 39.975 17.119 1.00 31.24 N ANISOU 347 N MET A 46 3654 5111 3103 -530 326 104 N ATOM 348 CA MET A 46 95.439 39.877 16.940 1.00 32.62 C ANISOU 348 CA MET A 46 3597 4831 3968 -342 -49 882 C ATOM 349 C MET A 46 95.991 38.456 16.873 1.00 34.04 C ANISOU 349 C MET A 46 4307 4874 3754 -194 1028 833 C ATOM 350 O MET A 46 96.785 38.134 15.990 1.00 36.82 O ANISOU 350 O MET A 46 4296 5735 3957 -568 1120 309 O ATOM 351 CB MET A 46 96.221 40.581 18.061 1.00 32.57 C ANISOU 351 CB MET A 46 3155 5559 3662 142 294 281 C ATOM 352 CG MET A 46 96.095 42.093 18.040 1.00 39.33 C ANISOU 352 CG MET A 46 4828 5541 4573 142 -53 -347 C ATOM 353 SD MET A 46 97.013 42.769 16.641 1.00 54.33 S ANISOU 353 SD MET A 46 6699 6308 7636 -571 996 1817 S ATOM 354 CE MET A 46 98.695 42.576 17.213 1.00 56.96 C ANISOU 354 CE MET A 46 5802 8021 7819 43 2212 -1512 C ATOM 355 N THR A 47 95.607 37.562 17.789 1.00 32.40 N ANISOU 355 N THR A 47 3999 4720 3590 -566 433 774 N ATOM 356 CA THR A 47 96.200 36.224 17.688 1.00 31.89 C ANISOU 356 CA THR A 47 3595 4904 3620 -412 345 823 C ATOM 357 C THR A 47 95.688 35.501 16.452 1.00 32.90 C ANISOU 357 C THR A 47 4405 4460 3634 -205 58 935 C ATOM 358 O THR A 47 96.355 34.582 15.945 1.00 33.63 O ANISOU 358 O THR A 47 4046 4683 4048 -241 43 705 O ATOM 359 CB THR A 47 95.924 35.342 18.923 1.00 30.82 C ANISOU 359 CB THR A 47 4163 4178 3369 -198 1031 189 C ATOM 360 OG1 THR A 47 94.494 35.231 19.088 1.00 33.92 O ANISOU 360 OG1 THR A 47 4147 5056 3687 -660 646 709 O ATOM 361 CG2 THR A 47 96.515 35.912 20.214 1.00 31.26 C ANISOU 361 CG2 THR A 47 3715 4857 3305 -117 1007 160 C ATOM 362 N THR A 48 94.515 35.865 15.929 1.00 29.54 N ANISOU 362 N THR A 48 4228 3914 3080 -357 324 878 N ATOM 363 CA THR A 48 94.053 35.214 14.694 1.00 27.79 C ANISOU 363 CA THR A 48 3417 3989 3153 -39 813 442 C ATOM 364 C THR A 48 94.907 35.601 13.488 1.00 28.17 C ANISOU 364 C THR A 48 3178 4078 3446 -129 980 221 C ATOM 365 O THR A 48 95.287 34.748 12.690 1.00 30.90 O ANISOU 365 O THR A 48 4012 4516 3213 -461 995 -116 O ATOM 366 CB THR A 48 92.572 35.551 14.439 1.00 28.55 C ANISOU 366 CB THR A 48 3209 4227 3412 -173 1019 -331 C ATOM 367 OG1 THR A 48 91.781 35.040 15.518 1.00 29.67 O ANISOU 367 OG1 THR A 48 3288 4736 3250 -144 689 174 O ATOM 368 CG2 THR A 48 92.051 34.878 13.180 1.00 27.34 C ANISOU 368 CG2 THR A 48 3844 3330 3213 -240 602 305 C ATOM 369 N TYR A 49 95.231 36.875 13.318 1.00 29.41 N ANISOU 369 N TYR A 49 3728 4195 3251 -350 798 446 N ATOM 370 CA TYR A 49 96.080 37.380 12.243 1.00 29.62 C ANISOU 370 CA TYR A 49 3529 4508 3217 -357 716 488 C ATOM 371 C TYR A 49 97.471 36.758 12.350 1.00 31.06 C ANISOU 371 C TYR A 49 3479 4980 3342 -281 483 -129 C ATOM 372 O TYR A 49 98.057 36.281 11.373 1.00 32.01 O ANISOU 372 O TYR A 49 3581 5256 3326 -193 493 -166 O ATOM 373 CB TYR A 49 96.153 38.909 12.268 1.00 28.70 C ANISOU 373 CB TYR A 49 3729 4516 2661 -593 763 432 C ATOM 374 CG TYR A 49 94.855 39.551 11.826 1.00 28.86 C ANISOU 374 CG TYR A 49 3899 4225 2843 -562 643 535 C ATOM 375 CD1 TYR A 49 94.228 39.150 10.644 1.00 29.67 C ANISOU 375 CD1 TYR A 49 3644 4428 3202 -472 600 139 C ATOM 376 CD2 TYR A 49 94.245 40.555 12.570 1.00 28.94 C ANISOU 376 CD2 TYR A 49 4228 4131 2636 -369 435 627 C ATOM 377 CE1 TYR A 49 93.037 39.738 10.233 1.00 30.68 C ANISOU 377 CE1 TYR A 49 4273 3965 3417 -273 178 282 C ATOM 378 CE2 TYR A 49 93.045 41.156 12.173 1.00 29.44 C ANISOU 378 CE2 TYR A 49 4204 4244 2736 -319 475 638 C ATOM 379 CZ TYR A 49 92.457 40.731 11.004 1.00 30.49 C ANISOU 379 CZ TYR A 49 4441 3847 3297 -119 27 397 C ATOM 380 OH TYR A 49 91.280 41.298 10.581 1.00 29.81 O ANISOU 380 OH TYR A 49 4119 4185 3023 -249 372 598 O ATOM 381 N LYS A 50 98.001 36.738 13.578 1.00 30.55 N ANISOU 381 N LYS A 50 3676 4614 3316 -206 455 -43 N ATOM 382 CA LYS A 50 99.303 36.109 13.797 1.00 33.48 C ANISOU 382 CA LYS A 50 3763 4868 4090 -138 300 528 C ATOM 383 C LYS A 50 99.262 34.658 13.330 1.00 34.21 C ANISOU 383 C LYS A 50 3396 4891 4709 5 747 390 C ATOM 384 O LYS A 50 100.190 34.205 12.637 1.00 34.90 O ANISOU 384 O LYS A 50 3537 5537 4188 130 643 348 O ATOM 385 CB LYS A 50 99.711 36.215 15.265 1.00 36.30 C ANISOU 385 CB LYS A 50 3582 6026 4183 140 229 363 C ATOM 386 CG LYS A 50 100.833 35.266 15.652 1.00 44.99 C ANISOU 386 CG LYS A 50 4759 6862 5473 802 -824 439 C ATOM 387 CD LYS A 50 100.954 35.133 17.164 1.00 58.15 C ANISOU 387 CD LYS A 50 7857 8435 5801 -219 -2354 1304 C ATOM 388 CE LYS A 50 102.196 34.388 17.640 1.00 62.07 C ANISOU 388 CE LYS A 50 7631 9259 6695 -492 -3182 1119 C ATOM 389 NZ LYS A 50 103.077 35.187 18.534 1.00 67.58 N ANISOU 389 NZ LYS A 50 6656 10188 8835 -1236 -2240 -114 N ATOM 390 N ALA A 51 98.222 33.903 13.672 1.00 33.07 N ANISOU 390 N ALA A 51 3618 4766 4180 -56 576 739 N ATOM 391 CA ALA A 51 98.145 32.518 13.222 1.00 38.48 C ANISOU 391 CA ALA A 51 5429 4882 4308 -518 249 671 C ATOM 392 C ALA A 51 97.871 32.391 11.729 1.00 37.45 C ANISOU 392 C ALA A 51 5427 4726 4077 -234 819 774 C ATOM 393 O ALA A 51 98.395 31.496 11.043 1.00 39.04 O ANISOU 393 O ALA A 51 5435 4712 4686 -181 578 452 O ATOM 394 CB ALA A 51 97.054 31.778 13.994 1.00 38.64 C ANISOU 394 CB ALA A 51 6696 4148 3837 -483 1315 -169 C ATOM 395 N LEU A 52 97.032 33.273 11.173 1.00 35.68 N ANISOU 395 N LEU A 52 5046 4696 3814 -349 927 699 N ATOM 396 CA LEU A 52 96.816 33.226 9.728 1.00 33.57 C ANISOU 396 CA LEU A 52 4097 4791 3867 -151 930 194 C ATOM 397 C LEU A 52 98.139 33.440 8.991 1.00 36.49 C ANISOU 397 C LEU A 52 4286 5492 4087 -463 1111 -39 C ATOM 398 O LEU A 52 98.481 32.734 8.037 1.00 38.80 O ANISOU 398 O LEU A 52 4941 5301 4500 -245 1690 70 O ATOM 399 CB LEU A 52 95.817 34.295 9.300 1.00 35.41 C ANISOU 399 CB LEU A 52 4291 4751 4413 -274 184 39 C ATOM 400 CG LEU A 52 94.345 33.936 9.214 1.00 38.29 C ANISOU 400 CG LEU A 52 4407 4980 5163 -433 -340 505 C ATOM 401 CD1 LEU A 52 93.521 35.164 8.848 1.00 45.21 C ANISOU 401 CD1 LEU A 52 4596 5953 6630 -275 -507 2054 C ATOM 402 CD2 LEU A 52 94.135 32.797 8.216 1.00 41.23 C ANISOU 402 CD2 LEU A 52 5482 6511 3672 -1048 -925 517 C ATOM 403 N VAL A 53 98.902 34.440 9.430 1.00 34.15 N ANISOU 403 N VAL A 53 3484 5648 3844 -77 -36 542 N ATOM 404 CA VAL A 53 100.184 34.692 8.767 1.00 34.02 C ANISOU 404 CA VAL A 53 3492 5687 3746 6 -38 663 C ATOM 405 C VAL A 53 101.101 33.474 8.776 1.00 35.71 C ANISOU 405 C VAL A 53 3968 5688 3913 210 505 903 C ATOM 406 O VAL A 53 101.787 33.117 7.800 1.00 37.15 O ANISOU 406 O VAL A 53 5239 5205 3671 335 614 801 O ATOM 407 CB VAL A 53 100.838 35.891 9.469 1.00 34.43 C ANISOU 407 CB VAL A 53 3146 5744 4193 115 -316 640 C ATOM 408 CG1 VAL A 53 102.305 36.004 9.082 1.00 34.38 C ANISOU 408 CG1 VAL A 53 3037 5677 4350 336 -480 1600 C ATOM 409 CG2 VAL A 53 100.056 37.146 9.113 1.00 32.94 C ANISOU 409 CG2 VAL A 53 3012 5751 3754 300 394 532 C ATOM 410 N GLU A 54 101.097 32.801 9.926 1.00 36.62 N ANISOU 410 N GLU A 54 4243 5648 4023 367 921 994 N ATOM 411 CA GLU A 54 101.914 31.627 10.164 1.00 37.38 C ANISOU 411 CA GLU A 54 4634 5511 4059 340 472 836 C ATOM 412 C GLU A 54 101.557 30.515 9.174 1.00 38.61 C ANISOU 412 C GLU A 54 4553 5914 4205 351 560 489 C ATOM 413 O GLU A 54 102.425 29.889 8.550 1.00 41.06 O ANISOU 413 O GLU A 54 4916 6097 4589 -34 1338 407 O ATOM 414 CB GLU A 54 101.772 31.108 11.605 1.00 41.10 C ANISOU 414 CB GLU A 54 5125 6523 3967 353 -3 1093 C ATOM 415 CG GLU A 54 102.880 31.478 12.560 1.00 58.89 C ANISOU 415 CG GLU A 54 8324 8511 5542 -1348 -2116 1608 C ATOM 416 CD GLU A 54 102.507 31.323 14.025 1.00 65.60 C ANISOU 416 CD GLU A 54 9639 10092 5195 -2264 -2694 1559 C ATOM 417 OE1 GLU A 54 101.391 30.874 14.376 1.00 88.06 O ANISOU 417 OE1 GLU A 54 13342 12442 7675 -5923 49 1437 O ATOM 418 OE2 GLU A 54 103.350 31.656 14.894 1.00 87.65 O ANISOU 418 OE2 GLU A 54 14582 11984 6736 -3012 -5420 578 O ATOM 419 N MET A 55 100.255 30.285 9.055 1.00 39.25 N ANISOU 419 N MET A 55 4572 5933 4408 388 290 604 N ATOM 420 CA MET A 55 99.778 29.243 8.151 1.00 40.82 C ANISOU 420 CA MET A 55 5468 5886 4156 -399 382 995 C ATOM 421 C MET A 55 100.112 29.541 6.695 1.00 40.32 C ANISOU 421 C MET A 55 5277 5804 4237 -258 593 957 C ATOM 422 O MET A 55 100.379 28.662 5.857 1.00 41.77 O ANISOU 422 O MET A 55 5137 5985 4748 -205 1262 839 O ATOM 423 CB MET A 55 98.261 29.120 8.352 1.00 37.31 C ANISOU 423 CB MET A 55 5429 5474 3274 -54 447 305 C ATOM 424 CG MET A 55 97.929 28.628 9.759 1.00 37.55 C ANISOU 424 CG MET A 55 5293 5936 3040 76 223 264 C ATOM 425 SD MET A 55 96.152 28.406 9.976 1.00 42.14 S ANISOU 425 SD MET A 55 5526 5570 4915 -157 981 545 S ATOM 426 CE MET A 55 95.890 26.845 9.118 1.00 45.49 C ANISOU 426 CE MET A 55 6271 6996 4015 -1031 738 -217 C ATOM 427 N HIS A 56 100.075 30.839 6.380 1.00 40.28 N ANISOU 427 N HIS A 56 4606 5840 4861 -327 1653 1152 N ATOM 428 CA HIS A 56 100.407 31.308 5.032 1.00 36.50 C ANISOU 428 CA HIS A 56 4299 5254 4317 438 1371 679 C ATOM 429 C HIS A 56 101.869 31.003 4.766 1.00 37.39 C ANISOU 429 C HIS A 56 4325 5505 4376 325 1460 -163 C ATOM 430 O HIS A 56 102.331 30.478 3.753 1.00 42.59 O ANISOU 430 O HIS A 56 5264 6224 4696 -194 2341 -302 O ATOM 431 CB HIS A 56 100.155 32.815 4.898 1.00 35.48 C ANISOU 431 CB HIS A 56 4505 5119 3858 263 1363 337 C ATOM 432 CG HIS A 56 100.682 33.325 3.584 1.00 35.58 C ANISOU 432 CG HIS A 56 4589 4952 3976 201 1449 293 C ATOM 433 ND1 HIS A 56 100.259 32.833 2.365 1.00 35.66 N ANISOU 433 ND1 HIS A 56 4452 5245 3851 87 1267 567 N ATOM 434 CD2 HIS A 56 101.616 34.261 3.303 1.00 37.60 C ANISOU 434 CD2 HIS A 56 5221 4959 4106 -114 1382 360 C ATOM 435 CE1 HIS A 56 100.898 33.452 1.391 1.00 37.12 C ANISOU 435 CE1 HIS A 56 4915 5180 4010 -158 1590 277 C ATOM 436 NE2 HIS A 56 101.732 34.330 1.925 1.00 37.17 N ANISOU 436 NE2 HIS A 56 4672 5325 4126 -86 1582 188 N ATOM 437 N LYS A 57 102.669 31.367 5.779 1.00 41.30 N ANISOU 437 N LYS A 57 4464 6290 4937 -121 1128 -94 N ATOM 438 CA LYS A 57 104.113 31.153 5.605 1.00 43.41 C ANISOU 438 CA LYS A 57 4456 6226 5813 -116 1049 104 C ATOM 439 C LYS A 57 104.407 29.669 5.557 1.00 44.80 C ANISOU 439 C LYS A 57 4939 6334 5749 138 1462 5 C ATOM 440 O LYS A 57 105.358 29.227 4.911 1.00 50.05 O ANISOU 440 O LYS A 57 5462 6879 6674 355 2127 44 O ATOM 441 CB LYS A 57 104.873 31.910 6.701 1.00 44.48 C ANISOU 441 CB LYS A 57 4340 6575 5985 166 906 -158 C ATOM 442 CG LYS A 57 104.549 33.404 6.643 1.00 51.01 C ANISOU 442 CG LYS A 57 6070 6341 6971 -158 1498 -455 C ATOM 443 CD LYS A 57 105.436 34.189 7.588 1.00 56.88 C ANISOU 443 CD LYS A 57 6968 7301 7343 -997 1728 -1021 C ATOM 444 CE LYS A 57 105.879 35.494 6.938 1.00 64.05 C ANISOU 444 CE LYS A 57 8349 7361 8627 -1687 2644 -1279 C ATOM 445 NZ LYS A 57 106.573 36.392 7.922 1.00 78.18 N ANISOU 445 NZ LYS A 57 13083 8827 7794 -4030 3470 -2024 N ATOM 446 N ALA A 58 103.596 28.834 6.192 1.00 42.30 N ANISOU 446 N ALA A 58 4369 5980 5724 145 968 -91 N ATOM 447 CA ALA A 58 103.875 27.407 6.174 1.00 42.20 C ANISOU 447 CA ALA A 58 3914 6116 6006 458 1348 -142 C ATOM 448 C ALA A 58 103.376 26.801 4.876 1.00 43.86 C ANISOU 448 C ALA A 58 5241 5672 5750 264 1375 67 C ATOM 449 O ALA A 58 103.443 25.587 4.681 1.00 47.11 O ANISOU 449 O ALA A 58 5609 5777 6512 631 1364 -245 O ATOM 450 CB ALA A 58 103.216 26.731 7.367 1.00 40.88 C ANISOU 450 CB ALA A 58 4030 5802 5701 512 1062 -162 C ATOM 451 N GLY A 59 102.865 27.643 3.990 1.00 42.92 N ANISOU 451 N GLY A 59 4849 5919 5541 87 1691 300 N ATOM 452 CA GLY A 59 102.358 27.181 2.716 1.00 41.52 C ANISOU 452 CA GLY A 59 5229 5218 5327 449 1947 220 C ATOM 453 C GLY A 59 100.997 26.523 2.827 1.00 42.22 C ANISOU 453 C GLY A 59 5145 5719 5179 358 1743 -268 C ATOM 454 O GLY A 59 100.669 25.694 1.958 1.00 50.77 O ANISOU 454 O GLY A 59 6546 7108 5637 -812 2419 -1105 O ATOM 455 N GLN A 60 100.177 26.843 3.840 1.00 40.36 N ANISOU 455 N GLN A 60 5158 5593 4585 343 1617 281 N ATOM 456 CA GLN A 60 98.891 26.141 3.927 1.00 42.17 C ANISOU 456 CA GLN A 60 5305 5372 5345 297 1772 391 C ATOM 457 C GLN A 60 97.738 26.914 3.298 1.00 42.03 C ANISOU 457 C GLN A 60 5129 5202 5637 118 1539 193 C ATOM 458 O GLN A 60 96.607 26.450 3.110 1.00 41.80 O ANISOU 458 O GLN A 60 5215 5402 5265 4 1695 -339 O ATOM 459 CB GLN A 60 98.573 25.840 5.389 1.00 43.43 C ANISOU 459 CB GLN A 60 4704 6522 5274 -49 1679 279 C ATOM 460 CG GLN A 60 99.629 25.031 6.130 1.00 49.81 C ANISOU 460 CG GLN A 60 5483 7271 6171 -728 312 1074 C ATOM 461 CD GLN A 60 99.407 25.072 7.631 1.00 56.33 C ANISOU 461 CD GLN A 60 6998 8291 6113 -1600 309 1365 C ATOM 462 OE1 GLN A 60 98.296 24.852 8.111 1.00 64.84 O ANISOU 462 OE1 GLN A 60 8153 10132 6352 -3034 1176 828 O ATOM 463 NE2 GLN A 60 100.426 25.362 8.425 1.00 65.00 N ANISOU 463 NE2 GLN A 60 7738 10357 6604 -1472 135 -715 N ATOM 464 N VAL A 61 98.009 28.172 2.937 1.00 40.33 N ANISOU 464 N VAL A 61 4988 4883 5451 458 1903 -213 N ATOM 465 CA VAL A 61 96.935 28.997 2.389 1.00 38.51 C ANISOU 465 CA VAL A 61 4772 5192 4668 108 1718 -6 C ATOM 466 C VAL A 61 97.516 30.130 1.554 1.00 38.79 C ANISOU 466 C VAL A 61 4662 5459 4616 53 1839 17 C ATOM 467 O VAL A 61 98.580 30.695 1.790 1.00 38.01 O ANISOU 467 O VAL A 61 5177 5154 4111 -178 1776 -439 O ATOM 468 CB VAL A 61 96.057 29.545 3.533 1.00 35.87 C ANISOU 468 CB VAL A 61 3459 5851 4319 38 1149 136 C ATOM 469 CG1 VAL A 61 96.828 30.552 4.379 1.00 34.05 C ANISOU 469 CG1 VAL A 61 3899 4739 4300 -57 1588 390 C ATOM 470 CG2 VAL A 61 94.771 30.211 3.048 1.00 38.36 C ANISOU 470 CG2 VAL A 61 4114 5000 5463 207 905 784 C ATOM 471 N SER A 62 96.777 30.494 0.518 1.00 37.71 N ANISOU 471 N SER A 62 5016 5335 3977 -210 1931 -311 N ATOM 472 CA SER A 62 97.147 31.644 -0.292 1.00 37.37 C ANISOU 472 CA SER A 62 5117 5136 3946 -253 1835 -455 C ATOM 473 C SER A 62 96.002 32.655 -0.320 1.00 36.60 C ANISOU 473 C SER A 62 4929 5187 3790 -330 1269 -663 C ATOM 474 O SER A 62 94.837 32.242 -0.397 1.00 36.49 O ANISOU 474 O SER A 62 5074 5273 3517 -543 949 191 O ATOM 475 CB SER A 62 97.520 31.179 -1.702 1.00 38.05 C ANISOU 475 CB SER A 62 5419 5105 3934 -500 1942 -461 C ATOM 476 OG SER A 62 97.841 32.321 -2.474 1.00 39.31 O ANISOU 476 OG SER A 62 5994 5146 3794 -33 1566 -189 O ATOM 477 N PHE A 63 96.325 33.939 -0.266 1.00 34.91 N ANISOU 477 N PHE A 63 4813 5129 3321 -286 441 -70 N ATOM 478 CA PHE A 63 95.305 34.976 -0.334 1.00 36.39 C ANISOU 478 CA PHE A 63 4612 5181 4035 -376 400 135 C ATOM 479 C PHE A 63 95.255 35.649 -1.705 1.00 36.50 C ANISOU 479 C PHE A 63 4735 4958 4175 -34 786 186 C ATOM 480 O PHE A 63 94.603 36.699 -1.811 1.00 38.39 O ANISOU 480 O PHE A 63 5144 4391 5052 -390 1827 750 O ATOM 481 CB PHE A 63 95.561 36.008 0.772 1.00 36.21 C ANISOU 481 CB PHE A 63 4572 4909 4277 -185 524 46 C ATOM 482 CG PHE A 63 95.373 35.346 2.144 1.00 36.61 C ANISOU 482 CG PHE A 63 4825 4951 4133 -434 306 -78 C ATOM 483 CD1 PHE A 63 94.114 35.147 2.679 1.00 36.87 C ANISOU 483 CD1 PHE A 63 5009 5238 3761 -73 617 -241 C ATOM 484 CD2 PHE A 63 96.473 34.928 2.864 1.00 37.65 C ANISOU 484 CD2 PHE A 63 5038 4681 4585 -129 290 152 C ATOM 485 CE1 PHE A 63 93.902 34.527 3.901 1.00 33.38 C ANISOU 485 CE1 PHE A 63 4701 4616 3368 641 566 -647 C ATOM 486 CE2 PHE A 63 96.298 34.316 4.078 1.00 35.30 C ANISOU 486 CE2 PHE A 63 4691 4592 4131 692 760 -337 C ATOM 487 CZ PHE A 63 95.027 34.122 4.598 1.00 35.04 C ANISOU 487 CZ PHE A 63 4500 4689 4124 616 532 -552 C ATOM 488 N LYS A 64 95.901 35.079 -2.711 1.00 38.20 N ANISOU 488 N LYS A 64 5030 5353 4130 -38 730 -177 N ATOM 489 CA LYS A 64 95.925 35.598 -4.068 1.00 40.02 C ANISOU 489 CA LYS A 64 5502 5507 4198 300 823 -81 C ATOM 490 C LYS A 64 94.537 35.872 -4.637 1.00 37.29 C ANISOU 490 C LYS A 64 5325 4801 4043 -159 918 157 C ATOM 491 O LYS A 64 94.320 36.853 -5.340 1.00 38.94 O ANISOU 491 O LYS A 64 5244 5721 3830 -406 1042 819 O ATOM 492 CB LYS A 64 96.585 34.582 -5.013 1.00 46.94 C ANISOU 492 CB LYS A 64 5209 7329 5298 -39 2426 -724 C ATOM 493 CG LYS A 64 97.761 35.088 -5.818 1.00 63.62 C ANISOU 493 CG LYS A 64 6935 9358 7882 -2352 3791 -1694 C ATOM 494 CD LYS A 64 98.914 35.503 -4.914 1.00 78.52 C ANISOU 494 CD LYS A 64 7690 11352 10791 -3655 2791 -1979 C ATOM 495 CE LYS A 64 100.242 35.566 -5.652 1.00 84.39 C ANISOU 495 CE LYS A 64 7679 12216 12171 -4131 3197 -2918 C ATOM 496 NZ LYS A 64 100.907 36.896 -5.479 1.00 86.17 N ANISOU 496 NZ LYS A 64 6178 12119 14443 -3347 2915 -3978 N ATOM 497 N HIS A 65 93.581 34.981 -4.347 1.00 36.57 N ANISOU 497 N HIS A 65 5551 4340 4002 -26 1786 -468 N ATOM 498 CA HIS A 65 92.221 35.211 -4.842 1.00 38.83 C ANISOU 498 CA HIS A 65 5328 5346 4082 -462 1852 -408 C ATOM 499 C HIS A 65 91.238 35.346 -3.686 1.00 38.25 C ANISOU 499 C HIS A 65 5120 5684 3728 -1069 1583 -694 C ATOM 500 O HIS A 65 90.097 34.876 -3.718 1.00 41.41 O ANISOU 500 O HIS A 65 5806 6432 3494 -2087 1577 86 O ATOM 501 CB HIS A 65 91.792 34.100 -5.813 1.00 40.34 C ANISOU 501 CB HIS A 65 5878 5839 3610 -755 1960 -446 C ATOM 502 CG HIS A 65 92.770 34.068 -6.965 1.00 40.80 C ANISOU 502 CG HIS A 65 5719 5801 3983 -378 2110 -308 C ATOM 503 ND1 HIS A 65 93.060 35.206 -7.684 1.00 43.19 N ANISOU 503 ND1 HIS A 65 6066 5694 4649 -380 2888 -350 N ATOM 504 CD2 HIS A 65 93.521 33.090 -7.498 1.00 40.00 C ANISOU 504 CD2 HIS A 65 5536 5771 3890 -317 1611 -476 C ATOM 505 CE1 HIS A 65 93.943 34.931 -8.629 1.00 42.44 C ANISOU 505 CE1 HIS A 65 5471 5790 4863 -448 2721 -458 C ATOM 506 NE2 HIS A 65 94.242 33.648 -8.538 1.00 41.61 N ANISOU 506 NE2 HIS A 65 5402 5891 4518 -294 2141 -579 N ATOM 507 N VAL A 66 91.693 36.010 -2.627 1.00 37.49 N ANISOU 507 N VAL A 66 5759 5103 3382 -1048 1137 -45 N ATOM 508 CA VAL A 66 90.832 36.319 -1.486 1.00 32.58 C ANISOU 508 CA VAL A 66 4729 4641 3010 -406 319 -29 C ATOM 509 C VAL A 66 90.571 37.823 -1.533 1.00 33.64 C ANISOU 509 C VAL A 66 4180 4617 3983 -624 -195 260 C ATOM 510 O VAL A 66 91.503 38.615 -1.667 1.00 33.70 O ANISOU 510 O VAL A 66 4237 4861 3709 -609 849 178 O ATOM 511 CB VAL A 66 91.429 35.890 -0.138 1.00 30.79 C ANISOU 511 CB VAL A 66 3995 4534 3171 -53 257 -274 C ATOM 512 CG1 VAL A 66 90.560 36.402 0.999 1.00 28.54 C ANISOU 512 CG1 VAL A 66 3481 4398 2965 -354 114 -163 C ATOM 513 CG2 VAL A 66 91.547 34.375 -0.081 1.00 30.17 C ANISOU 513 CG2 VAL A 66 4545 4483 2433 -485 1011 -15 C ATOM 514 N VAL A 67 89.307 38.193 -1.450 1.00 31.87 N ANISOU 514 N VAL A 67 4128 4521 3461 -709 -113 361 N ATOM 515 CA VAL A 67 88.916 39.602 -1.425 1.00 30.76 C ANISOU 515 CA VAL A 67 4351 4529 2807 -642 557 496 C ATOM 516 C VAL A 67 88.491 39.919 -0.004 1.00 32.92 C ANISOU 516 C VAL A 67 5272 4611 2623 -1317 528 447 C ATOM 517 O VAL A 67 87.809 39.079 0.571 1.00 30.50 O ANISOU 517 O VAL A 67 4243 4471 2876 -943 593 329 O ATOM 518 CB VAL A 67 87.771 39.881 -2.413 1.00 29.57 C ANISOU 518 CB VAL A 67 4338 4257 2639 -267 644 21 C ATOM 519 CG1 VAL A 67 87.045 41.185 -2.135 1.00 30.25 C ANISOU 519 CG1 VAL A 67 3849 4230 3417 -556 1119 -73 C ATOM 520 CG2 VAL A 67 88.332 39.840 -3.844 1.00 30.09 C ANISOU 520 CG2 VAL A 67 4433 4375 2624 -348 692 -66 C ATOM 521 N THR A 68 88.883 41.063 0.535 1.00 28.03 N ANISOU 521 N THR A 68 3537 4225 2890 -529 249 556 N ATOM 522 CA THR A 68 88.509 41.383 1.895 1.00 29.02 C ANISOU 522 CA THR A 68 3571 4427 3030 -384 231 247 C ATOM 523 C THR A 68 87.776 42.721 1.988 1.00 30.37 C ANISOU 523 C THR A 68 3931 4335 3271 -363 415 481 C ATOM 524 O THR A 68 88.044 43.620 1.191 1.00 30.55 O ANISOU 524 O THR A 68 3681 5014 2912 -8 120 888 O ATOM 525 CB THR A 68 89.730 41.466 2.840 1.00 29.30 C ANISOU 525 CB THR A 68 3836 4069 3229 -676 13 152 C ATOM 526 OG1 THR A 68 90.581 42.535 2.379 1.00 32.78 O ANISOU 526 OG1 THR A 68 4298 4521 3636 -1125 476 -23 O ATOM 527 CG2 THR A 68 90.564 40.200 2.840 1.00 29.46 C ANISOU 527 CG2 THR A 68 3888 4619 2685 -190 116 216 C ATOM 528 N PHE A 69 86.903 42.808 2.988 1.00 26.17 N ANISOU 528 N PHE A 69 3142 3973 2828 -405 -171 461 N ATOM 529 CA PHE A 69 86.149 43.982 3.380 1.00 28.36 C ANISOU 529 CA PHE A 69 4053 3805 2918 -327 39 377 C ATOM 530 C PHE A 69 86.339 44.204 4.874 1.00 28.95 C ANISOU 530 C PHE A 69 4260 3775 2963 -296 -115 416 C ATOM 531 O PHE A 69 86.036 43.280 5.664 1.00 28.25 O ANISOU 531 O PHE A 69 3897 3916 2922 -395 166 336 O ATOM 532 CB PHE A 69 84.662 43.812 3.073 1.00 27.11 C ANISOU 532 CB PHE A 69 3946 3445 2910 366 -37 248 C ATOM 533 CG PHE A 69 84.328 43.930 1.589 1.00 29.98 C ANISOU 533 CG PHE A 69 4332 4143 2916 -201 -101 390 C ATOM 534 CD1 PHE A 69 84.224 42.812 0.778 1.00 28.94 C ANISOU 534 CD1 PHE A 69 3373 4621 3001 -218 45 10 C ATOM 535 CD2 PHE A 69 84.118 45.180 1.011 1.00 29.05 C ANISOU 535 CD2 PHE A 69 3395 4491 3153 -163 -363 721 C ATOM 536 CE1 PHE A 69 83.928 42.951 -0.580 1.00 32.19 C ANISOU 536 CE1 PHE A 69 4194 4791 3244 -637 -524 139 C ATOM 537 CE2 PHE A 69 83.826 45.326 -0.347 1.00 29.75 C ANISOU 537 CE2 PHE A 69 3479 4711 3115 -454 -360 666 C ATOM 538 CZ PHE A 69 83.729 44.197 -1.150 1.00 30.71 C ANISOU 538 CZ PHE A 69 3704 4962 3002 -824 566 495 C ATOM 539 N ASN A 70 86.821 45.374 5.274 1.00 30.06 N ANISOU 539 N ASN A 70 4586 4001 2834 -680 375 281 N ATOM 540 CA ASN A 70 86.961 45.642 6.713 1.00 29.07 C ANISOU 540 CA ASN A 70 4588 3587 2872 -24 68 333 C ATOM 541 C ASN A 70 85.709 46.311 7.269 1.00 29.49 C ANISOU 541 C ASN A 70 4517 3953 2734 -58 233 569 C ATOM 542 O ASN A 70 84.983 47.008 6.548 1.00 31.09 O ANISOU 542 O ASN A 70 3473 5192 3147 -294 65 920 O ATOM 543 CB ASN A 70 88.192 46.511 6.953 1.00 29.68 C ANISOU 543 CB ASN A 70 4644 4010 2622 -236 660 -339 C ATOM 544 CG ASN A 70 89.341 45.656 7.445 1.00 30.70 C ANISOU 544 CG ASN A 70 4485 4351 2830 -322 261 -659 C ATOM 545 OD1 ASN A 70 89.989 44.981 6.643 1.00 29.40 O ANISOU 545 OD1 ASN A 70 3944 4144 3082 -610 749 -266 O ATOM 546 ND2 ASN A 70 89.590 45.688 8.759 1.00 31.69 N ANISOU 546 ND2 ASN A 70 4365 4965 2709 -885 503 -33 N ATOM 547 N MET A 71 85.428 46.124 8.548 1.00 30.26 N ANISOU 547 N MET A 71 4718 4257 2522 -619 19 126 N ATOM 548 CA MET A 71 84.219 46.614 9.188 1.00 35.32 C ANISOU 548 CA MET A 71 5264 4956 3202 -786 731 -453 C ATOM 549 C MET A 71 84.156 48.134 9.307 1.00 33.84 C ANISOU 549 C MET A 71 4434 4942 3480 -273 159 -110 C ATOM 550 O MET A 71 83.065 48.709 9.244 1.00 34.08 O ANISOU 550 O MET A 71 4080 5334 3533 -667 -539 991 O ATOM 551 CB MET A 71 84.073 46.037 10.622 1.00 33.33 C ANISOU 551 CB MET A 71 4725 4761 3178 347 567 -368 C ATOM 552 CG MET A 71 83.829 44.548 10.695 1.00 39.27 C ANISOU 552 CG MET A 71 5876 5010 4034 -447 1789 -208 C ATOM 553 SD MET A 71 83.254 43.952 12.304 1.00 43.40 S ANISOU 553 SD MET A 71 6840 5791 3859 -207 1793 -100 S ATOM 554 CE MET A 71 83.967 45.200 13.383 1.00 41.95 C ANISOU 554 CE MET A 71 7854 4657 3430 -390 565 1391 C ATOM 555 N ASP A 72 85.312 48.784 9.521 1.00 27.73 N ANISOU 555 N ASP A 72 3999 3840 2697 424 -414 894 N ATOM 556 CA ASP A 72 85.237 50.205 9.819 1.00 33.08 C ANISOU 556 CA ASP A 72 4116 4226 4227 316 867 -224 C ATOM 557 C ASP A 72 86.550 50.955 9.609 1.00 34.95 C ANISOU 557 C ASP A 72 4227 4434 4617 -87 -49 -111 C ATOM 558 O ASP A 72 87.585 50.351 9.303 1.00 34.87 O ANISOU 558 O ASP A 72 4536 4410 4302 -599 1563 41 O ATOM 559 CB ASP A 72 84.761 50.346 11.266 1.00 44.06 C ANISOU 559 CB ASP A 72 8100 4460 4179 -904 1573 -158 C ATOM 560 CG ASP A 72 85.301 49.312 12.227 1.00 45.45 C ANISOU 560 CG ASP A 72 7717 5146 4405 -817 1610 227 C ATOM 561 OD1 ASP A 72 86.448 48.825 12.074 1.00 53.37 O ANISOU 561 OD1 ASP A 72 7062 6641 6577 -863 359 -146 O ATOM 562 OD2 ASP A 72 84.569 48.972 13.176 1.00 51.96 O ANISOU 562 OD2 ASP A 72 9349 5745 4650 -1909 1927 489 O ATOM 563 N GLU A 73 86.480 52.279 9.770 1.00 36.89 N ANISOU 563 N GLU A 73 5316 4442 4257 -233 830 -91 N ATOM 564 CA GLU A 73 87.599 53.210 9.672 1.00 39.23 C ANISOU 564 CA GLU A 73 6067 4619 4219 -758 722 -146 C ATOM 565 C GLU A 73 87.251 54.534 10.352 1.00 37.56 C ANISOU 565 C GLU A 73 5713 4623 3935 -492 333 21 C ATOM 566 O GLU A 73 86.094 54.970 10.394 1.00 40.77 O ANISOU 566 O GLU A 73 5444 5701 4344 -700 972 -594 O ATOM 567 CB GLU A 73 88.006 53.423 8.209 1.00 34.97 C ANISOU 567 CB GLU A 73 4785 4198 4304 107 553 228 C ATOM 568 CG GLU A 73 89.226 54.298 7.972 1.00 42.01 C ANISOU 568 CG GLU A 73 5410 5682 4869 -845 554 426 C ATOM 569 CD GLU A 73 90.519 53.803 8.617 1.00 41.86 C ANISOU 569 CD GLU A 73 5233 6069 4603 -1168 280 -224 C ATOM 570 OE1 GLU A 73 90.669 54.017 9.849 1.00 39.20 O ANISOU 570 OE1 GLU A 73 4960 5439 4493 -1399 763 -263 O ATOM 571 OE2 GLU A 73 91.357 53.220 7.857 1.00 38.00 O ANISOU 571 OE2 GLU A 73 4982 6112 3345 -1143 204 643 O ATOM 572 N TYR A 74 88.281 55.183 10.910 1.00 37.36 N ANISOU 572 N TYR A 74 5673 4875 3647 -565 541 -202 N ATOM 573 CA TYR A 74 88.098 56.509 11.479 1.00 41.28 C ANISOU 573 CA TYR A 74 5667 5053 4964 -481 541 -711 C ATOM 574 C TYR A 74 87.886 57.559 10.397 1.00 41.19 C ANISOU 574 C TYR A 74 5495 4709 5448 -293 751 -648 C ATOM 575 O TYR A 74 88.491 57.522 9.312 1.00 39.71 O ANISOU 575 O TYR A 74 5055 4567 5465 -126 667 -328 O ATOM 576 CB TYR A 74 89.307 56.947 12.294 1.00 41.08 C ANISOU 576 CB TYR A 74 5489 4886 5233 -454 679 -990 C ATOM 577 CG TYR A 74 89.440 56.265 13.631 1.00 43.17 C ANISOU 577 CG TYR A 74 6067 5477 4860 -1198 336 -1187 C ATOM 578 CD1 TYR A 74 88.460 56.345 14.604 1.00 45.76 C ANISOU 578 CD1 TYR A 74 6685 5643 5060 -1237 755 -1295 C ATOM 579 CD2 TYR A 74 90.584 55.526 13.908 1.00 43.30 C ANISOU 579 CD2 TYR A 74 5970 6098 4385 -1347 42 -628 C ATOM 580 CE1 TYR A 74 88.638 55.697 15.813 1.00 50.27 C ANISOU 580 CE1 TYR A 74 7361 6441 5297 -1381 916 -798 C ATOM 581 CE2 TYR A 74 90.768 54.879 15.110 1.00 46.74 C ANISOU 581 CE2 TYR A 74 6844 6625 4291 -1476 254 -474 C ATOM 582 CZ TYR A 74 89.781 54.967 16.071 1.00 50.91 C ANISOU 582 CZ TYR A 74 7258 7085 5001 -1429 845 -134 C ATOM 583 OH TYR A 74 89.960 54.322 17.280 1.00 55.75 O ANISOU 583 OH TYR A 74 8276 8611 4294 -813 895 -463 O ATOM 584 N VAL A 75 87.016 58.506 10.726 1.00 42.13 N ANISOU 584 N VAL A 75 4919 5224 5863 -261 738 -759 N ATOM 585 CA VAL A 75 86.759 59.617 9.806 1.00 47.19 C ANISOU 585 CA VAL A 75 5788 5097 7045 -33 166 -493 C ATOM 586 C VAL A 75 87.784 60.723 10.055 1.00 48.55 C ANISOU 586 C VAL A 75 6285 5224 6940 -454 735 -542 C ATOM 587 O VAL A 75 88.037 61.002 11.238 1.00 48.47 O ANISOU 587 O VAL A 75 5693 5860 6862 -1170 726 -226 O ATOM 588 CB VAL A 75 85.329 60.161 9.982 1.00 48.86 C ANISOU 588 CB VAL A 75 6013 5205 7348 131 647 -104 C ATOM 589 CG1 VAL A 75 85.209 61.547 9.356 1.00 53.29 C ANISOU 589 CG1 VAL A 75 6667 5126 8455 481 1334 91 C ATOM 590 CG2 VAL A 75 84.279 59.213 9.404 1.00 43.92 C ANISOU 590 CG2 VAL A 75 5319 5653 5715 67 1547 -167 C ATOM 591 N GLY A 76 88.358 61.313 9.021 1.00 50.75 N ANISOU 591 N GLY A 76 7221 5344 6717 -516 356 -120 N ATOM 592 CA GLY A 76 89.258 62.447 9.073 1.00 50.36 C ANISOU 592 CA GLY A 76 6827 5542 6765 -498 1207 -437 C ATOM 593 C GLY A 76 90.659 62.157 9.554 1.00 52.70 C ANISOU 593 C GLY A 76 6657 6001 7365 -559 1338 -104 C ATOM 594 O GLY A 76 91.507 63.027 9.776 1.00 53.35 O ANISOU 594 O GLY A 76 6451 6305 7513 -727 1657 -39 O ATOM 595 N LEU A 77 90.978 60.885 9.753 1.00 51.62 N ANISOU 595 N LEU A 77 6184 6058 7372 -182 2057 -442 N ATOM 596 CA LEU A 77 92.326 60.516 10.181 1.00 51.42 C ANISOU 596 CA LEU A 77 6268 6170 7100 -353 1735 -602 C ATOM 597 C LEU A 77 93.111 60.225 8.916 1.00 48.97 C ANISOU 597 C LEU A 77 5514 6321 6772 -359 1217 -704 C ATOM 598 O LEU A 77 92.548 59.512 8.071 1.00 53.77 O ANISOU 598 O LEU A 77 7868 6544 6016 -2227 1383 112 O ATOM 599 CB LEU A 77 92.225 59.308 11.086 1.00 52.44 C ANISOU 599 CB LEU A 77 7136 6167 6620 -351 1335 -752 C ATOM 600 CG LEU A 77 93.137 59.150 12.291 1.00 54.52 C ANISOU 600 CG LEU A 77 7227 5709 7779 133 600 -1018 C ATOM 601 CD1 LEU A 77 93.867 57.813 12.216 1.00 54.85 C ANISOU 601 CD1 LEU A 77 5875 7127 7838 795 1700 -2120 C ATOM 602 CD2 LEU A 77 94.132 60.290 12.405 1.00 59.94 C ANISOU 602 CD2 LEU A 77 7100 6902 8774 -680 -44 781 C ATOM 603 N PRO A 78 94.322 60.725 8.715 1.00 49.97 N ANISOU 603 N PRO A 78 5464 6640 6884 -337 1061 -178 N ATOM 604 CA PRO A 78 95.054 60.348 7.489 1.00 51.66 C ANISOU 604 CA PRO A 78 5460 6928 7242 -311 1309 -262 C ATOM 605 C PRO A 78 95.295 58.839 7.428 1.00 48.74 C ANISOU 605 C PRO A 78 5262 6812 6445 -642 1623 -73 C ATOM 606 O PRO A 78 95.712 58.261 8.437 1.00 51.65 O ANISOU 606 O PRO A 78 6508 6970 6146 -1049 2070 410 O ATOM 607 CB PRO A 78 96.374 61.100 7.624 1.00 54.45 C ANISOU 607 CB PRO A 78 6132 6946 7612 -961 1705 -379 C ATOM 608 CG PRO A 78 96.112 62.192 8.605 1.00 52.18 C ANISOU 608 CG PRO A 78 5589 6980 7258 -538 1438 -211 C ATOM 609 CD PRO A 78 95.081 61.659 9.559 1.00 49.69 C ANISOU 609 CD PRO A 78 5322 6615 6941 -498 978 73 C ATOM 610 N LYS A 79 95.051 58.195 6.295 1.00 48.19 N ANISOU 610 N LYS A 79 5083 7123 6104 -876 2386 -94 N ATOM 611 CA LYS A 79 95.235 56.757 6.153 1.00 54.40 C ANISOU 611 CA LYS A 79 7407 6964 6298 -1288 1942 -134 C ATOM 612 C LYS A 79 96.591 56.284 6.664 1.00 53.90 C ANISOU 612 C LYS A 79 7398 6095 6984 -536 2690 4 C ATOM 613 O LYS A 79 96.702 55.240 7.318 1.00 58.96 O ANISOU 613 O LYS A 79 8627 5807 7968 -892 2034 91 O ATOM 614 CB LYS A 79 95.078 56.340 4.687 1.00 64.52 C ANISOU 614 CB LYS A 79 10277 7584 6653 -3394 1702 -620 C ATOM 615 CG LYS A 79 93.654 56.018 4.264 1.00 81.09 C ANISOU 615 CG LYS A 79 12443 9681 8687 -6045 205 -51 C ATOM 616 CD LYS A 79 93.630 55.157 3.000 1.00 94.67 C ANISOU 616 CD LYS A 79 16385 10464 9120 -7758 -149 -552 C ATOM 617 CE LYS A 79 92.217 54.704 2.648 1.00100.31 C ANISOU 617 CE LYS A 79 17239 10681 10196 -8238 -1562 180 C ATOM 618 NZ LYS A 79 92.093 53.263 2.259 1.00 99.23 N ANISOU 618 NZ LYS A 79 16487 9198 12017 -7898 -3093 3219 N ATOM 619 N GLU A 80 97.664 57.018 6.389 1.00 55.66 N ANISOU 619 N GLU A 80 7175 6753 7220 -583 2365 620 N ATOM 620 CA GLU A 80 98.980 56.592 6.860 1.00 59.52 C ANISOU 620 CA GLU A 80 7348 7740 7526 -424 2377 1678 C ATOM 621 C GLU A 80 99.204 56.896 8.335 1.00 58.33 C ANISOU 621 C GLU A 80 7538 6988 7636 -723 2023 1750 C ATOM 622 O GLU A 80 100.290 56.605 8.853 1.00 60.27 O ANISOU 622 O GLU A 80 7470 6869 8561 -1035 1553 1201 O ATOM 623 CB GLU A 80 100.129 57.224 6.058 1.00 68.18 C ANISOU 623 CB GLU A 80 7326 10033 8545 -363 3156 1880 C ATOM 624 CG GLU A 80 100.962 56.191 5.308 1.00 79.36 C ANISOU 624 CG GLU A 80 8602 11058 10492 -46 4197 1108 C ATOM 625 CD GLU A 80 102.345 55.896 5.849 1.00 85.38 C ANISOU 625 CD GLU A 80 8638 11323 12480 946 4294 1367 C ATOM 626 OE1 GLU A 80 103.357 56.114 5.127 1.00 99.94 O ANISOU 626 OE1 GLU A 80 8592 11873 17506 -1411 5570 441 O ATOM 627 OE2 GLU A 80 102.449 55.427 7.010 1.00102.82 O ANISOU 627 OE2 GLU A 80 12178 12381 14509 1275 2104 3815 O ATOM 628 N HIS A 81 98.246 57.462 9.060 1.00 57.52 N ANISOU 628 N HIS A 81 7404 6948 7504 -1180 1928 1251 N ATOM 629 CA HIS A 81 98.450 57.509 10.517 1.00 55.43 C ANISOU 629 CA HIS A 81 5668 7555 7838 -647 972 401 C ATOM 630 C HIS A 81 98.585 56.072 11.004 1.00 51.01 C ANISOU 630 C HIS A 81 5461 7634 6288 -559 567 149 C ATOM 631 O HIS A 81 97.871 55.158 10.580 1.00 45.52 O ANISOU 631 O HIS A 81 5018 7368 4909 -184 648 374 O ATOM 632 CB HIS A 81 97.304 58.250 11.200 1.00 57.02 C ANISOU 632 CB HIS A 81 6080 7270 8314 -800 939 -523 C ATOM 633 CG HIS A 81 97.445 58.370 12.685 1.00 60.06 C ANISOU 633 CG HIS A 81 6354 8163 8302 -1518 1174 -661 C ATOM 634 ND1 HIS A 81 97.750 59.569 13.301 1.00 61.95 N ANISOU 634 ND1 HIS A 81 6815 8307 8417 -1426 1148 -885 N ATOM 635 CD2 HIS A 81 97.345 57.492 13.701 1.00 60.36 C ANISOU 635 CD2 HIS A 81 6050 8619 8265 -1854 520 -442 C ATOM 636 CE1 HIS A 81 97.823 59.406 14.615 1.00 62.89 C ANISOU 636 CE1 HIS A 81 6559 8713 8624 -1590 -243 -604 C ATOM 637 NE2 HIS A 81 97.577 58.133 14.890 1.00 62.21 N ANISOU 637 NE2 HIS A 81 6300 8795 8540 -1619 -512 -427 N ATOM 638 N PRO A 82 99.495 55.772 11.915 1.00 54.15 N ANISOU 638 N PRO A 82 6012 8050 6511 -1228 -93 49 N ATOM 639 CA PRO A 82 99.721 54.384 12.311 1.00 54.66 C ANISOU 639 CA PRO A 82 6053 8363 6353 -1964 -1118 871 C ATOM 640 C PRO A 82 98.544 53.730 13.037 1.00 58.22 C ANISOU 640 C PRO A 82 6080 9549 6492 -2448 -1232 928 C ATOM 641 O PRO A 82 98.502 52.494 13.125 1.00 65.27 O ANISOU 641 O PRO A 82 6657 9514 8628 -3346 -253 386 O ATOM 642 CB PRO A 82 100.890 54.490 13.297 1.00 57.60 C ANISOU 642 CB PRO A 82 6202 8897 6785 -2495 -1300 694 C ATOM 643 CG PRO A 82 101.507 55.821 13.032 1.00 61.64 C ANISOU 643 CG PRO A 82 7485 8655 7281 -2687 -1574 473 C ATOM 644 CD PRO A 82 100.366 56.720 12.616 1.00 61.44 C ANISOU 644 CD PRO A 82 7545 8452 7347 -2048 -486 -22 C ATOM 645 N GLU A 83 97.620 54.523 13.552 1.00 60.08 N ANISOU 645 N GLU A 83 6911 10136 5779 -2649 -491 346 N ATOM 646 CA GLU A 83 96.436 54.077 14.266 1.00 58.75 C ANISOU 646 CA GLU A 83 7323 9833 5165 -2875 -527 401 C ATOM 647 C GLU A 83 95.202 54.024 13.380 1.00 49.36 C ANISOU 647 C GLU A 83 6323 7416 5015 -1136 126 106 C ATOM 648 O GLU A 83 94.113 53.625 13.809 1.00 47.67 O ANISOU 648 O GLU A 83 6268 7574 4270 -680 229 332 O ATOM 649 CB GLU A 83 96.152 54.980 15.469 1.00 72.69 C ANISOU 649 CB GLU A 83 9982 12292 5346 -5237 740 -929 C ATOM 650 CG GLU A 83 97.062 54.709 16.659 1.00 77.05 C ANISOU 650 CG GLU A 83 10408 13710 5159 -4911 703 -1110 C ATOM 651 CD GLU A 83 97.444 53.248 16.802 1.00 80.81 C ANISOU 651 CD GLU A 83 10734 13895 6074 -4907 -9 -221 C ATOM 652 OE1 GLU A 83 96.564 52.362 16.860 1.00 89.49 O ANISOU 652 OE1 GLU A 83 13427 14399 6175 -6529 -398 -45 O ATOM 653 OE2 GLU A 83 98.665 52.963 16.866 1.00 90.04 O ANISOU 653 OE2 GLU A 83 11351 16138 6721 -3189 509 -996 O ATOM 654 N SER A 84 95.288 54.393 12.113 1.00 40.77 N ANISOU 654 N SER A 84 4873 5560 5057 -332 490 -137 N ATOM 655 CA SER A 84 94.155 54.157 11.220 1.00 39.95 C ANISOU 655 CA SER A 84 4506 6067 4608 -437 974 -437 C ATOM 656 C SER A 84 93.899 52.662 11.126 1.00 40.12 C ANISOU 656 C SER A 84 4629 6113 4502 -706 506 137 C ATOM 657 O SER A 84 94.789 51.858 11.438 1.00 39.83 O ANISOU 657 O SER A 84 4325 5873 4937 -1163 135 309 O ATOM 658 CB SER A 84 94.448 54.720 9.832 1.00 36.56 C ANISOU 658 CB SER A 84 3963 5194 4736 -166 963 -458 C ATOM 659 OG SER A 84 95.455 53.959 9.184 1.00 34.84 O ANISOU 659 OG SER A 84 4221 4760 4256 -13 543 -616 O ATOM 660 N TYR A 85 92.697 52.277 10.696 1.00 36.91 N ANISOU 660 N TYR A 85 4557 5925 3540 -512 460 563 N ATOM 661 CA TYR A 85 92.465 50.832 10.579 1.00 38.87 C ANISOU 661 CA TYR A 85 4545 6043 4179 -825 976 304 C ATOM 662 C TYR A 85 93.181 50.297 9.343 1.00 36.56 C ANISOU 662 C TYR A 85 4016 5694 4181 -729 923 584 C ATOM 663 O TYR A 85 93.624 49.143 9.334 1.00 35.47 O ANISOU 663 O TYR A 85 4698 5285 3494 -1150 601 460 O ATOM 664 CB TYR A 85 90.961 50.525 10.600 1.00 41.00 C ANISOU 664 CB TYR A 85 4519 6535 4525 -762 1324 -738 C ATOM 665 CG TYR A 85 90.335 50.723 11.976 1.00 45.44 C ANISOU 665 CG TYR A 85 5347 7087 4830 -1091 1841 -806 C ATOM 666 CD1 TYR A 85 91.145 51.060 13.060 1.00 45.44 C ANISOU 666 CD1 TYR A 85 5931 6893 4440 -1465 2026 -799 C ATOM 667 CD2 TYR A 85 88.983 50.582 12.213 1.00 45.14 C ANISOU 667 CD2 TYR A 85 5301 7010 4841 -551 1953 211 C ATOM 668 CE1 TYR A 85 90.619 51.245 14.312 1.00 45.55 C ANISOU 668 CE1 TYR A 85 5920 6908 4481 -1493 2272 -227 C ATOM 669 CE2 TYR A 85 88.430 50.770 13.461 1.00 45.60 C ANISOU 669 CE2 TYR A 85 5642 6929 4757 -819 2032 397 C ATOM 670 CZ TYR A 85 89.259 51.100 14.497 1.00 46.45 C ANISOU 670 CZ TYR A 85 5882 6851 4915 -1443 2206 28 C ATOM 671 OH TYR A 85 88.756 51.295 15.757 1.00 44.32 O ANISOU 671 OH TYR A 85 5391 6372 5076 -1046 2153 -207 O ATOM 672 N TYR A 86 93.315 51.112 8.293 1.00 34.54 N ANISOU 672 N TYR A 86 3497 5354 4274 -575 813 547 N ATOM 673 CA TYR A 86 94.181 50.799 7.170 1.00 33.41 C ANISOU 673 CA TYR A 86 4260 4623 3814 -451 688 435 C ATOM 674 C TYR A 86 95.542 50.345 7.706 1.00 31.85 C ANISOU 674 C TYR A 86 3948 4639 3515 -459 1061 145 C ATOM 675 O TYR A 86 96.083 49.285 7.341 1.00 35.51 O ANISOU 675 O TYR A 86 3996 5070 4426 -291 1607 -120 O ATOM 676 CB TYR A 86 94.312 52.038 6.291 1.00 36.45 C ANISOU 676 CB TYR A 86 5065 4979 3806 -845 382 679 C ATOM 677 CG TYR A 86 95.470 52.015 5.313 1.00 37.16 C ANISOU 677 CG TYR A 86 5383 4560 4175 -1000 727 667 C ATOM 678 CD1 TYR A 86 95.272 51.452 4.054 1.00 37.49 C ANISOU 678 CD1 TYR A 86 5644 4405 4197 -694 821 588 C ATOM 679 CD2 TYR A 86 96.730 52.543 5.592 1.00 37.27 C ANISOU 679 CD2 TYR A 86 4696 4538 4927 -73 415 567 C ATOM 680 CE1 TYR A 86 96.281 51.401 3.109 1.00 39.99 C ANISOU 680 CE1 TYR A 86 5869 5350 3974 -1235 886 920 C ATOM 681 CE2 TYR A 86 97.747 52.494 4.661 1.00 37.76 C ANISOU 681 CE2 TYR A 86 4554 4612 5179 237 399 437 C ATOM 682 CZ TYR A 86 97.515 51.925 3.424 1.00 41.68 C ANISOU 682 CZ TYR A 86 5611 5481 4744 -869 767 708 C ATOM 683 OH TYR A 86 98.524 51.875 2.486 1.00 41.02 O ANISOU 683 OH TYR A 86 4878 5730 4978 98 398 544 O ATOM 684 N SER A 87 96.125 51.168 8.584 1.00 34.05 N ANISOU 684 N SER A 87 4519 4337 4081 -1045 546 605 N ATOM 685 CA SER A 87 97.484 50.916 9.060 1.00 35.21 C ANISOU 685 CA SER A 87 4647 4861 3871 -770 492 380 C ATOM 686 C SER A 87 97.556 49.650 9.905 1.00 33.45 C ANISOU 686 C SER A 87 4273 4825 3612 -579 739 247 C ATOM 687 O SER A 87 98.490 48.871 9.712 1.00 33.44 O ANISOU 687 O SER A 87 3240 5338 4128 -807 228 544 O ATOM 688 CB SER A 87 98.037 52.097 9.861 1.00 36.43 C ANISOU 688 CB SER A 87 4146 4853 4842 -654 427 102 C ATOM 689 OG SER A 87 98.331 53.163 8.965 1.00 40.72 O ANISOU 689 OG SER A 87 5011 5327 5135 -1476 -398 470 O ATOM 690 N PHE A 88 96.587 49.497 10.807 1.00 33.41 N ANISOU 690 N PHE A 88 3834 4886 3972 -1075 640 82 N ATOM 691 CA PHE A 88 96.479 48.277 11.586 1.00 30.53 C ANISOU 691 CA PHE A 88 3381 4744 3476 -631 655 -81 C ATOM 692 C PHE A 88 96.483 47.089 10.631 1.00 27.74 C ANISOU 692 C PHE A 88 2666 4843 3031 -313 829 50 C ATOM 693 O PHE A 88 97.186 46.114 10.888 1.00 30.41 O ANISOU 693 O PHE A 88 3926 4671 2959 -249 399 384 O ATOM 694 CB PHE A 88 95.189 48.260 12.412 1.00 28.25 C ANISOU 694 CB PHE A 88 3563 3873 3299 -85 756 -130 C ATOM 695 CG PHE A 88 94.925 46.952 13.163 1.00 30.86 C ANISOU 695 CG PHE A 88 3418 4455 3853 -457 419 466 C ATOM 696 CD1 PHE A 88 94.305 45.802 12.654 1.00 31.31 C ANISOU 696 CD1 PHE A 88 4064 4487 3345 -831 875 514 C ATOM 697 CD2 PHE A 88 95.352 46.907 14.487 1.00 32.13 C ANISOU 697 CD2 PHE A 88 3623 4395 4192 -326 -162 629 C ATOM 698 CE1 PHE A 88 94.154 44.658 13.406 1.00 36.09 C ANISOU 698 CE1 PHE A 88 4567 5131 4015 -1525 -609 1295 C ATOM 699 CE2 PHE A 88 95.185 45.774 15.249 1.00 31.90 C ANISOU 699 CE2 PHE A 88 3708 4616 3796 -736 341 500 C ATOM 700 CZ PHE A 88 94.585 44.645 14.732 1.00 33.19 C ANISOU 700 CZ PHE A 88 3783 5050 3779 -1242 -189 845 C ATOM 701 N MET A 89 95.612 47.066 9.621 1.00 29.41 N ANISOU 701 N MET A 89 2935 4876 3362 -421 500 79 N ATOM 702 CA MET A 89 95.398 45.875 8.793 1.00 29.82 C ANISOU 702 CA MET A 89 2897 4849 3585 -631 451 92 C ATOM 703 C MET A 89 96.640 45.510 7.983 1.00 28.85 C ANISOU 703 C MET A 89 3158 4680 3123 -736 546 107 C ATOM 704 O MET A 89 96.958 44.325 7.815 1.00 29.56 O ANISOU 704 O MET A 89 3066 4752 3415 -354 467 598 O ATOM 705 CB MET A 89 94.199 46.053 7.844 1.00 30.13 C ANISOU 705 CB MET A 89 3193 4668 3586 -720 301 308 C ATOM 706 CG MET A 89 92.863 46.029 8.593 1.00 30.03 C ANISOU 706 CG MET A 89 2944 4561 3905 -524 144 731 C ATOM 707 SD MET A 89 92.610 44.446 9.434 1.00 31.40 S ANISOU 707 SD MET A 89 4243 4373 3316 -908 432 245 S ATOM 708 CE MET A 89 92.836 43.300 8.082 1.00 30.87 C ANISOU 708 CE MET A 89 4601 4671 2457 -598 -366 517 C ATOM 709 N HIS A 90 97.347 46.524 7.464 1.00 30.25 N ANISOU 709 N HIS A 90 3395 4865 3233 -852 488 354 N ATOM 710 CA HIS A 90 98.576 46.220 6.726 1.00 31.13 C ANISOU 710 CA HIS A 90 3569 5055 3205 -723 689 800 C ATOM 711 C HIS A 90 99.646 45.678 7.660 1.00 30.39 C ANISOU 711 C HIS A 90 3538 4858 3150 -617 691 477 C ATOM 712 O HIS A 90 100.269 44.635 7.462 1.00 32.67 O ANISOU 712 O HIS A 90 3926 4798 3690 -483 810 703 O ATOM 713 CB HIS A 90 99.047 47.484 5.974 1.00 31.72 C ANISOU 713 CB HIS A 90 3515 5022 3515 -1054 337 785 C ATOM 714 CG HIS A 90 98.171 47.697 4.768 1.00 32.17 C ANISOU 714 CG HIS A 90 4100 4569 3556 -480 217 674 C ATOM 715 ND1 HIS A 90 98.319 46.989 3.592 1.00 29.81 N ANISOU 715 ND1 HIS A 90 3433 4288 3604 -380 177 698 N ATOM 716 CD2 HIS A 90 97.115 48.518 4.551 1.00 33.01 C ANISOU 716 CD2 HIS A 90 4532 4539 3470 -153 107 233 C ATOM 717 CE1 HIS A 90 97.404 47.377 2.712 1.00 28.80 C ANISOU 717 CE1 HIS A 90 3279 3942 3724 65 245 308 C ATOM 718 NE2 HIS A 90 96.659 48.310 3.267 1.00 30.26 N ANISOU 718 NE2 HIS A 90 3720 4212 3567 -19 255 -218 N ATOM 719 N ARG A 91 99.895 46.390 8.750 1.00 33.11 N ANISOU 719 N ARG A 91 4353 4960 3268 -1110 444 493 N ATOM 720 CA ARG A 91 100.932 46.004 9.717 1.00 36.54 C ANISOU 720 CA ARG A 91 4700 5273 3912 -1226 -152 447 C ATOM 721 C ARG A 91 100.715 44.636 10.332 1.00 36.40 C ANISOU 721 C ARG A 91 4322 5316 4192 -652 20 690 C ATOM 722 O ARG A 91 101.689 43.920 10.565 1.00 35.21 O ANISOU 722 O ARG A 91 3853 6253 3272 -721 142 1023 O ATOM 723 CB ARG A 91 100.962 47.067 10.812 1.00 43.09 C ANISOU 723 CB ARG A 91 6615 5891 3866 -2657 -136 202 C ATOM 724 CG ARG A 91 101.679 46.729 12.090 1.00 43.92 C ANISOU 724 CG ARG A 91 6204 5813 4670 -1722 -732 -351 C ATOM 725 CD ARG A 91 101.732 47.976 12.974 1.00 46.77 C ANISOU 725 CD ARG A 91 5724 6840 5208 -1314 -893 -1308 C ATOM 726 NE ARG A 91 100.449 48.386 13.522 1.00 47.83 N ANISOU 726 NE ARG A 91 5608 7281 5286 -1124 -1010 -968 N ATOM 727 CZ ARG A 91 99.804 49.539 13.419 1.00 48.30 C ANISOU 727 CZ ARG A 91 5533 7333 5485 -1133 -564 -607 C ATOM 728 NH1 ARG A 91 100.286 50.568 12.732 1.00 47.57 N ANISOU 728 NH1 ARG A 91 4548 7368 6160 -1242 -543 -593 N ATOM 729 NH2 ARG A 91 98.629 49.639 14.036 1.00 47.84 N ANISOU 729 NH2 ARG A 91 6123 6762 5292 -1219 -18 -561 N ATOM 730 N ASN A 92 99.478 44.246 10.619 1.00 32.32 N ANISOU 730 N ASN A 92 4072 4467 3741 -99 -65 946 N ATOM 731 CA ASN A 92 99.183 42.965 11.267 1.00 30.99 C ANISOU 731 CA ASN A 92 4345 4296 3134 -55 -210 654 C ATOM 732 C ASN A 92 98.841 41.848 10.294 1.00 31.42 C ANISOU 732 C ASN A 92 3701 4645 3593 -93 -208 329 C ATOM 733 O ASN A 92 98.839 40.660 10.648 1.00 32.32 O ANISOU 733 O ASN A 92 4081 4476 3724 -48 596 108 O ATOM 734 CB ASN A 92 98.035 43.144 12.288 1.00 35.51 C ANISOU 734 CB ASN A 92 5302 5141 3048 -289 344 650 C ATOM 735 CG ASN A 92 98.524 43.977 13.457 1.00 38.19 C ANISOU 735 CG ASN A 92 5988 5080 3443 157 113 269 C ATOM 736 OD1 ASN A 92 99.411 43.533 14.191 1.00 43.56 O ANISOU 736 OD1 ASN A 92 7035 5406 4112 539 -878 -301 O ATOM 737 ND2 ASN A 92 98.003 45.173 13.653 1.00 37.21 N ANISOU 737 ND2 ASN A 92 6000 4543 3596 -327 826 925 N ATOM 738 N PHE A 93 98.553 42.158 9.034 1.00 31.32 N ANISOU 738 N PHE A 93 3640 5181 3080 -457 518 137 N ATOM 739 CA PHE A 93 98.167 41.049 8.147 1.00 28.57 C ANISOU 739 CA PHE A 93 3360 4444 3050 -53 634 424 C ATOM 740 C PHE A 93 98.610 41.246 6.708 1.00 29.40 C ANISOU 740 C PHE A 93 3412 4803 2958 61 460 346 C ATOM 741 O PHE A 93 99.368 40.444 6.161 1.00 31.72 O ANISOU 741 O PHE A 93 4734 4118 3201 -208 1108 177 O ATOM 742 CB PHE A 93 96.644 40.924 8.229 1.00 30.39 C ANISOU 742 CB PHE A 93 3405 4753 3391 -284 565 244 C ATOM 743 CG PHE A 93 96.036 39.796 7.420 1.00 31.25 C ANISOU 743 CG PHE A 93 3730 4660 3483 -377 581 243 C ATOM 744 CD1 PHE A 93 96.566 38.515 7.506 1.00 29.95 C ANISOU 744 CD1 PHE A 93 3466 4815 3097 -206 1137 161 C ATOM 745 CD2 PHE A 93 94.943 40.039 6.593 1.00 30.73 C ANISOU 745 CD2 PHE A 93 3209 4834 3633 -91 802 -453 C ATOM 746 CE1 PHE A 93 96.004 37.486 6.779 1.00 31.44 C ANISOU 746 CE1 PHE A 93 3859 4705 3380 -265 1086 121 C ATOM 747 CE2 PHE A 93 94.377 39.013 5.861 1.00 31.69 C ANISOU 747 CE2 PHE A 93 3531 4731 3780 -329 747 -274 C ATOM 748 CZ PHE A 93 94.917 37.742 5.959 1.00 30.27 C ANISOU 748 CZ PHE A 93 3337 4728 3437 -361 1314 -233 C ATOM 749 N PHE A 94 98.135 42.303 6.043 1.00 30.65 N ANISOU 749 N PHE A 94 3692 4745 3207 -184 587 693 N ATOM 750 CA PHE A 94 98.383 42.374 4.605 1.00 30.56 C ANISOU 750 CA PHE A 94 3572 4889 3150 -114 485 514 C ATOM 751 C PHE A 94 99.882 42.472 4.319 1.00 30.65 C ANISOU 751 C PHE A 94 3623 4807 3218 -236 584 160 C ATOM 752 O PHE A 94 100.331 41.893 3.318 1.00 33.71 O ANISOU 752 O PHE A 94 4416 4812 3580 -311 1262 241 O ATOM 753 CB PHE A 94 97.655 43.540 3.947 1.00 30.31 C ANISOU 753 CB PHE A 94 3761 4790 2966 -302 103 374 C ATOM 754 CG PHE A 94 96.150 43.589 4.117 1.00 30.45 C ANISOU 754 CG PHE A 94 3625 4942 3003 -409 -384 421 C ATOM 755 CD1 PHE A 94 95.378 42.444 3.974 1.00 33.40 C ANISOU 755 CD1 PHE A 94 4161 5402 3128 -855 168 -429 C ATOM 756 CD2 PHE A 94 95.524 44.794 4.416 1.00 30.80 C ANISOU 756 CD2 PHE A 94 3484 5250 2967 -482 9 -58 C ATOM 757 CE1 PHE A 94 93.995 42.509 4.128 1.00 33.70 C ANISOU 757 CE1 PHE A 94 4110 5756 2937 -1099 -5 -243 C ATOM 758 CE2 PHE A 94 94.142 44.866 4.567 1.00 31.73 C ANISOU 758 CE2 PHE A 94 3582 5591 2883 -645 582 43 C ATOM 759 CZ PHE A 94 93.381 43.717 4.414 1.00 31.82 C ANISOU 759 CZ PHE A 94 3680 5899 2510 -850 -114 199 C ATOM 760 N ASP A 95 100.692 43.125 5.135 1.00 34.08 N ANISOU 760 N ASP A 95 4049 5597 3304 -634 -44 629 N ATOM 761 CA ASP A 95 102.130 43.207 4.906 1.00 34.35 C ANISOU 761 CA ASP A 95 4079 5311 3660 -767 150 542 C ATOM 762 C ASP A 95 102.783 41.833 4.841 1.00 36.57 C ANISOU 762 C ASP A 95 4287 5317 4292 -783 779 50 C ATOM 763 O ASP A 95 103.903 41.736 4.337 1.00 39.69 O ANISOU 763 O ASP A 95 4476 5756 4849 -983 1093 -549 O ATOM 764 CB ASP A 95 102.848 43.966 6.024 1.00 35.67 C ANISOU 764 CB ASP A 95 3774 5708 4073 -1030 780 -226 C ATOM 765 CG ASP A 95 102.668 45.465 5.996 1.00 34.99 C ANISOU 765 CG ASP A 95 3899 5693 3703 -1159 304 312 C ATOM 766 OD1 ASP A 95 102.036 46.006 5.067 1.00 35.39 O ANISOU 766 OD1 ASP A 95 4277 6282 2888 -1864 648 822 O ATOM 767 OD2 ASP A 95 103.174 46.126 6.929 1.00 33.74 O ANISOU 767 OD2 ASP A 95 4027 5208 3586 -667 131 421 O ATOM 768 N HIS A 96 102.140 40.790 5.346 1.00 36.46 N ANISOU 768 N HIS A 96 4684 5293 3875 -526 734 493 N ATOM 769 CA HIS A 96 102.776 39.485 5.442 1.00 35.36 C ANISOU 769 CA HIS A 96 4348 5461 3624 -367 1275 209 C ATOM 770 C HIS A 96 102.165 38.416 4.562 1.00 35.19 C ANISOU 770 C HIS A 96 4029 5694 3647 -425 1626 -52 C ATOM 771 O HIS A 96 102.639 37.273 4.638 1.00 39.30 O ANISOU 771 O HIS A 96 4650 5773 4509 -187 730 -354 O ATOM 772 CB HIS A 96 102.697 38.995 6.909 1.00 33.49 C ANISOU 772 CB HIS A 96 4456 4624 3644 -211 1455 117 C ATOM 773 CG HIS A 96 103.120 40.127 7.808 1.00 38.62 C ANISOU 773 CG HIS A 96 4939 5649 4085 -462 1172 -559 C ATOM 774 ND1 HIS A 96 104.432 40.517 7.953 1.00 40.50 N ANISOU 774 ND1 HIS A 96 4989 6057 4344 -654 1265 -701 N ATOM 775 CD2 HIS A 96 102.390 40.961 8.585 1.00 40.14 C ANISOU 775 CD2 HIS A 96 5023 6117 4113 -720 1221 -1071 C ATOM 776 CE1 HIS A 96 104.513 41.533 8.782 1.00 39.67 C ANISOU 776 CE1 HIS A 96 4932 6129 4012 -470 882 -603 C ATOM 777 NE2 HIS A 96 103.281 41.822 9.185 1.00 37.90 N ANISOU 777 NE2 HIS A 96 4805 5639 3956 -144 387 -484 N ATOM 778 N VAL A 97 101.152 38.745 3.767 1.00 34.62 N ANISOU 778 N VAL A 97 4461 5321 3373 -477 1494 54 N ATOM 779 CA VAL A 97 100.552 37.700 2.933 1.00 36.46 C ANISOU 779 CA VAL A 97 4874 5289 3692 -460 1178 36 C ATOM 780 C VAL A 97 100.493 38.127 1.470 1.00 35.96 C ANISOU 780 C VAL A 97 4654 5581 3426 -439 1679 -336 C ATOM 781 O VAL A 97 100.910 39.236 1.131 1.00 39.41 O ANISOU 781 O VAL A 97 5804 5797 3372 -914 25 271 O ATOM 782 CB VAL A 97 99.157 37.314 3.453 1.00 35.14 C ANISOU 782 CB VAL A 97 5139 5045 3167 -785 1099 236 C ATOM 783 CG1 VAL A 97 99.247 36.801 4.888 1.00 33.93 C ANISOU 783 CG1 VAL A 97 5390 4646 2856 -222 961 -318 C ATOM 784 CG2 VAL A 97 98.196 38.490 3.360 1.00 34.92 C ANISOU 784 CG2 VAL A 97 4327 5855 3086 -666 223 72 C ATOM 785 N ASP A 98 99.997 37.245 0.604 1.00 36.74 N ANISOU 785 N ASP A 98 4927 5302 3730 -197 1333 -352 N ATOM 786 CA ASP A 98 100.100 37.473 -0.836 1.00 34.71 C ANISOU 786 CA ASP A 98 4702 4779 3708 -54 1044 -383 C ATOM 787 C ASP A 98 98.822 38.033 -1.456 1.00 35.19 C ANISOU 787 C ASP A 98 4413 4907 4051 -182 914 -851 C ATOM 788 O ASP A 98 98.515 37.725 -2.610 1.00 35.65 O ANISOU 788 O ASP A 98 4240 5630 3677 -138 1218 -561 O ATOM 789 CB ASP A 98 100.483 36.183 -1.575 1.00 34.30 C ANISOU 789 CB ASP A 98 4389 4744 3901 -267 1045 -509 C ATOM 790 CG ASP A 98 99.494 35.055 -1.319 1.00 42.85 C ANISOU 790 CG ASP A 98 6236 5461 4584 -1451 1620 -797 C ATOM 791 OD1 ASP A 98 98.643 35.192 -0.405 1.00 41.13 O ANISOU 791 OD1 ASP A 98 5685 5525 4418 -1274 1366 -182 O ATOM 792 OD2 ASP A 98 99.575 34.030 -2.032 1.00 40.73 O ANISOU 792 OD2 ASP A 98 6312 4815 4350 -870 814 -248 O ATOM 793 N ILE A 99 98.099 38.858 -0.700 1.00 33.19 N ANISOU 793 N ILE A 99 4298 4713 3599 -396 1533 -192 N ATOM 794 CA ILE A 99 96.904 39.456 -1.276 1.00 33.90 C ANISOU 794 CA ILE A 99 4695 4378 3809 -187 1492 28 C ATOM 795 C ILE A 99 97.206 40.725 -2.084 1.00 36.58 C ANISOU 795 C ILE A 99 5231 4990 3677 -1364 534 289 C ATOM 796 O ILE A 99 97.927 41.641 -1.689 1.00 35.36 O ANISOU 796 O ILE A 99 4707 4851 3876 -930 742 -274 O ATOM 797 CB ILE A 99 95.913 39.802 -0.158 1.00 35.18 C ANISOU 797 CB ILE A 99 3998 5274 4095 -492 1345 -288 C ATOM 798 CG1 ILE A 99 94.511 40.202 -0.634 1.00 34.23 C ANISOU 798 CG1 ILE A 99 4305 4669 4033 -422 1095 -6 C ATOM 799 CG2 ILE A 99 96.507 40.903 0.720 1.00 37.02 C ANISOU 799 CG2 ILE A 99 5269 6154 2643 -704 911 -99 C ATOM 800 CD1 ILE A 99 93.537 40.359 0.536 1.00 34.84 C ANISOU 800 CD1 ILE A 99 4107 4388 4744 -137 1473 605 C ATOM 801 N PRO A 100 96.612 40.812 -3.276 1.00 36.88 N ANISOU 801 N PRO A 100 5587 5329 3097 -1531 930 -61 N ATOM 802 CA PRO A 100 96.778 41.987 -4.116 1.00 35.29 C ANISOU 802 CA PRO A 100 4840 5035 3535 -1196 356 54 C ATOM 803 C PRO A 100 95.986 43.200 -3.644 1.00 36.36 C ANISOU 803 C PRO A 100 4851 5250 3715 -1543 965 -480 C ATOM 804 O PRO A 100 94.884 43.074 -3.118 1.00 39.45 O ANISOU 804 O PRO A 100 5703 5877 3407 -1736 1727 -330 O ATOM 805 CB PRO A 100 96.224 41.559 -5.486 1.00 33.85 C ANISOU 805 CB PRO A 100 4530 5161 3171 -1211 970 -90 C ATOM 806 CG PRO A 100 95.451 40.312 -5.246 1.00 37.64 C ANISOU 806 CG PRO A 100 5633 5438 3229 -1814 917 -195 C ATOM 807 CD PRO A 100 95.763 39.779 -3.869 1.00 36.80 C ANISOU 807 CD PRO A 100 5032 5463 3487 -1619 913 121 C ATOM 808 N ALA A 101 96.536 44.397 -3.856 1.00 30.99 N ANISOU 808 N ALA A 101 3433 5040 3303 -898 -430 305 N ATOM 809 CA ALA A 101 95.881 45.634 -3.462 1.00 33.72 C ANISOU 809 CA ALA A 101 4081 5089 3640 -619 200 736 C ATOM 810 C ALA A 101 94.464 45.710 -4.004 1.00 30.88 C ANISOU 810 C ALA A 101 3919 4368 3448 -629 404 347 C ATOM 811 O ALA A 101 93.541 46.194 -3.352 1.00 32.77 O ANISOU 811 O ALA A 101 4178 4764 3512 -566 682 392 O ATOM 812 CB ALA A 101 96.681 46.836 -3.950 1.00 33.55 C ANISOU 812 CB ALA A 101 3964 5017 3766 -861 593 -5 C ATOM 813 N GLU A 102 94.261 45.236 -5.235 1.00 30.35 N ANISOU 813 N GLU A 102 4106 4392 3032 -846 605 806 N ATOM 814 CA GLU A 102 92.919 45.441 -5.775 1.00 32.82 C ANISOU 814 CA GLU A 102 4063 5216 3191 -999 506 481 C ATOM 815 C GLU A 102 91.904 44.588 -5.032 1.00 31.46 C ANISOU 815 C GLU A 102 3864 4733 3355 -396 864 489 C ATOM 816 O GLU A 102 90.708 44.848 -5.139 1.00 34.82 O ANISOU 816 O GLU A 102 3726 5192 4311 -1043 -26 703 O ATOM 817 CB GLU A 102 92.894 45.116 -7.265 1.00 35.90 C ANISOU 817 CB GLU A 102 4640 5930 3070 -1466 471 632 C ATOM 818 CG GLU A 102 93.460 43.721 -7.511 1.00 42.27 C ANISOU 818 CG GLU A 102 6742 5952 3365 -1389 507 -204 C ATOM 819 CD GLU A 102 93.805 43.549 -8.983 1.00 50.47 C ANISOU 819 CD GLU A 102 7995 7533 3648 -1747 1074 -687 C ATOM 820 OE1 GLU A 102 95.016 43.475 -9.319 1.00 57.34 O ANISOU 820 OE1 GLU A 102 8278 9155 4353 -1924 1846 -96 O ATOM 821 OE2 GLU A 102 92.843 43.495 -9.793 1.00 60.07 O ANISOU 821 OE2 GLU A 102 8655 10831 3336 -3672 902 -1579 O ATOM 822 N ASN A 103 92.356 43.584 -4.287 1.00 32.64 N ANISOU 822 N ASN A 103 4396 4734 3272 -404 598 409 N ATOM 823 CA ASN A 103 91.444 42.726 -3.540 1.00 33.57 C ANISOU 823 CA ASN A 103 5275 4740 2740 -1027 431 227 C ATOM 824 C ASN A 103 91.098 43.268 -2.161 1.00 31.50 C ANISOU 824 C ASN A 103 4370 4610 2987 -737 366 81 C ATOM 825 O ASN A 103 90.249 42.693 -1.467 1.00 32.15 O ANISOU 825 O ASN A 103 4006 4785 3422 -525 691 -130 O ATOM 826 CB ASN A 103 92.072 41.334 -3.394 1.00 34.34 C ANISOU 826 CB ASN A 103 5232 4745 3072 -912 1374 133 C ATOM 827 CG ASN A 103 91.952 40.500 -4.653 1.00 36.60 C ANISOU 827 CG ASN A 103 5288 5096 3522 -883 519 -207 C ATOM 828 OD1 ASN A 103 91.599 41.027 -5.715 1.00 35.71 O ANISOU 828 OD1 ASN A 103 5044 5400 3123 -644 1347 -82 O ATOM 829 ND2 ASN A 103 92.240 39.210 -4.590 1.00 35.38 N ANISOU 829 ND2 ASN A 103 5136 5176 3130 -685 1303 -224 N ATOM 830 N ILE A 104 91.719 44.355 -1.700 1.00 32.91 N ANISOU 830 N ILE A 104 4556 4661 3286 -737 274 -56 N ATOM 831 CA ILE A 104 91.546 44.855 -0.334 1.00 31.09 C ANISOU 831 CA ILE A 104 4505 4217 3091 -847 319 231 C ATOM 832 C ILE A 104 90.556 46.002 -0.316 1.00 31.25 C ANISOU 832 C ILE A 104 4575 3985 3313 -949 706 460 C ATOM 833 O ILE A 104 90.694 46.982 -1.052 1.00 32.27 O ANISOU 833 O ILE A 104 4783 4728 2752 -686 460 863 O ATOM 834 CB ILE A 104 92.869 45.329 0.293 1.00 31.31 C ANISOU 834 CB ILE A 104 4726 4326 2846 -1181 253 675 C ATOM 835 CG1 ILE A 104 93.900 44.200 0.402 1.00 31.28 C ANISOU 835 CG1 ILE A 104 4403 4559 2921 -1144 164 242 C ATOM 836 CG2 ILE A 104 92.657 46.004 1.648 1.00 29.67 C ANISOU 836 CG2 ILE A 104 4248 4267 2758 -881 104 781 C ATOM 837 CD1 ILE A 104 95.295 44.688 0.713 1.00 32.42 C ANISOU 837 CD1 ILE A 104 4680 4730 2907 -1500 -179 876 C ATOM 838 N ASN A 105 89.534 45.885 0.521 1.00 30.46 N ANISOU 838 N ASN A 105 4248 4407 2918 -945 333 590 N ATOM 839 CA ASN A 105 88.568 46.967 0.589 1.00 32.34 C ANISOU 839 CA ASN A 105 4321 4452 3516 -907 626 520 C ATOM 840 C ASN A 105 88.464 47.446 2.034 1.00 33.61 C ANISOU 840 C ASN A 105 4711 4436 3624 -724 491 392 C ATOM 841 O ASN A 105 88.244 46.700 2.985 1.00 30.80 O ANISOU 841 O ASN A 105 4042 4434 3227 -644 -297 398 O ATOM 842 CB ASN A 105 87.211 46.496 0.090 1.00 32.61 C ANISOU 842 CB ASN A 105 4246 4368 3777 -697 574 342 C ATOM 843 CG ASN A 105 87.221 46.091 -1.361 1.00 35.09 C ANISOU 843 CG ASN A 105 4708 5076 3550 -880 272 688 C ATOM 844 OD1 ASN A 105 87.061 46.972 -2.211 1.00 39.39 O ANISOU 844 OD1 ASN A 105 5905 5078 3981 -569 731 944 O ATOM 845 ND2 ASN A 105 87.405 44.807 -1.663 1.00 29.24 N ANISOU 845 ND2 ASN A 105 3888 5167 2057 -734 610 859 N ATOM 846 N LEU A 106 88.651 48.756 2.154 1.00 31.95 N ANISOU 846 N LEU A 106 3952 4279 3909 -177 439 403 N ATOM 847 CA LEU A 106 88.611 49.463 3.421 1.00 34.22 C ANISOU 847 CA LEU A 106 4400 4562 4040 -423 543 158 C ATOM 848 C LEU A 106 87.784 50.726 3.216 1.00 34.71 C ANISOU 848 C LEU A 106 4913 4364 3913 -388 534 20 C ATOM 849 O LEU A 106 87.858 51.296 2.130 1.00 36.23 O ANISOU 849 O LEU A 106 4968 4770 4027 -138 604 233 O ATOM 850 CB LEU A 106 90.001 49.833 3.924 1.00 36.38 C ANISOU 850 CB LEU A 106 4510 4684 4630 -584 565 -435 C ATOM 851 CG LEU A 106 90.804 48.750 4.654 1.00 35.72 C ANISOU 851 CG LEU A 106 3771 5352 4451 -70 829 -681 C ATOM 852 CD1 LEU A 106 92.243 48.776 4.144 1.00 42.00 C ANISOU 852 CD1 LEU A 106 3910 6757 5290 -647 1129 138 C ATOM 853 CD2 LEU A 106 90.766 48.914 6.163 1.00 35.07 C ANISOU 853 CD2 LEU A 106 4779 4133 4415 -597 761 -603 C ATOM 854 N LEU A 107 87.015 51.164 4.196 1.00 34.53 N ANISOU 854 N LEU A 107 4691 4414 4014 -459 540 -33 N ATOM 855 CA LEU A 107 86.283 52.416 4.074 1.00 35.05 C ANISOU 855 CA LEU A 107 4619 4356 4344 -516 1190 479 C ATOM 856 C LEU A 107 87.228 53.609 4.022 1.00 37.46 C ANISOU 856 C LEU A 107 4938 4618 4678 -787 937 911 C ATOM 857 O LEU A 107 88.222 53.687 4.760 1.00 38.05 O ANISOU 857 O LEU A 107 5313 4559 4585 -800 755 183 O ATOM 858 CB LEU A 107 85.294 52.502 5.250 1.00 34.30 C ANISOU 858 CB LEU A 107 4586 4483 3964 -534 928 451 C ATOM 859 CG LEU A 107 84.008 51.702 4.973 1.00 34.06 C ANISOU 859 CG LEU A 107 4502 4681 3757 -547 836 807 C ATOM 860 CD1 LEU A 107 83.281 51.362 6.275 1.00 29.82 C ANISOU 860 CD1 LEU A 107 3380 4872 3080 -19 332 269 C ATOM 861 CD2 LEU A 107 83.120 52.457 4.001 1.00 33.01 C ANISOU 861 CD2 LEU A 107 5034 4156 3351 -512 683 489 C ATOM 862 N ASN A 108 86.939 54.562 3.121 1.00 39.13 N ANISOU 862 N ASN A 108 5989 4292 4588 -435 1104 684 N ATOM 863 CA ASN A 108 87.757 55.770 3.021 1.00 39.84 C ANISOU 863 CA ASN A 108 6362 4176 4599 -440 1482 556 C ATOM 864 C ASN A 108 87.255 56.829 3.994 1.00 40.69 C ANISOU 864 C ASN A 108 6208 4324 4928 -519 1857 483 C ATOM 865 O ASN A 108 86.309 57.575 3.727 1.00 43.29 O ANISOU 865 O ASN A 108 6790 3902 5756 -377 1638 598 O ATOM 866 CB ASN A 108 87.764 56.305 1.589 1.00 40.41 C ANISOU 866 CB ASN A 108 6331 4262 4760 21 1660 794 C ATOM 867 CG ASN A 108 88.702 57.477 1.399 1.00 38.84 C ANISOU 867 CG ASN A 108 5505 4307 4946 398 2042 806 C ATOM 868 OD1 ASN A 108 89.345 57.976 2.334 1.00 53.94 O ANISOU 868 OD1 ASN A 108 10729 5477 4290 -2612 3158 -571 O ATOM 869 ND2 ASN A 108 88.776 57.938 0.144 1.00 46.61 N ANISOU 869 ND2 ASN A 108 7358 5603 4750 -825 2625 612 N ATOM 870 N GLY A 109 87.893 56.917 5.159 1.00 40.85 N ANISOU 870 N GLY A 109 6270 4240 5010 -754 1842 113 N ATOM 871 CA GLY A 109 87.471 57.863 6.181 1.00 39.63 C ANISOU 871 CA GLY A 109 5024 4631 5402 78 1429 -31 C ATOM 872 C GLY A 109 87.745 59.300 5.785 1.00 42.22 C ANISOU 872 C GLY A 109 5622 4535 5887 -177 1869 -417 C ATOM 873 O GLY A 109 87.315 60.242 6.446 1.00 38.25 O ANISOU 873 O GLY A 109 4210 4790 5534 -176 293 -952 O ATOM 874 N ASN A 110 88.467 59.471 4.681 1.00 44.46 N ANISOU 874 N ASN A 110 5804 4980 6109 -380 1982 -24 N ATOM 875 CA ASN A 110 88.776 60.799 4.181 1.00 48.58 C ANISOU 875 CA ASN A 110 6429 5414 6615 -1018 1249 443 C ATOM 876 C ASN A 110 87.954 61.118 2.948 1.00 50.82 C ANISOU 876 C ASN A 110 6823 5772 6715 -709 1144 566 C ATOM 877 O ASN A 110 88.194 62.146 2.314 1.00 48.88 O ANISOU 877 O ASN A 110 7062 4473 7037 13 812 -66 O ATOM 878 CB ASN A 110 90.289 60.910 3.907 1.00 50.36 C ANISOU 878 CB ASN A 110 6487 5502 7146 -1451 1298 21 C ATOM 879 CG ASN A 110 91.081 60.878 5.207 1.00 50.62 C ANISOU 879 CG ASN A 110 6301 5774 7159 -1249 1332 -411 C ATOM 880 OD1 ASN A 110 90.901 61.748 6.065 1.00 52.61 O ANISOU 880 OD1 ASN A 110 6575 6222 7194 -811 1545 -529 O ATOM 881 ND2 ASN A 110 91.959 59.898 5.397 1.00 48.08 N ANISOU 881 ND2 ASN A 110 6147 5904 6217 -1209 1853 -182 N ATOM 882 N ALA A 111 86.983 60.283 2.577 1.00 46.92 N ANISOU 882 N ALA A 111 5573 5931 6322 -309 1461 920 N ATOM 883 CA ALA A 111 86.198 60.608 1.381 1.00 48.47 C ANISOU 883 CA ALA A 111 5790 6212 6414 129 1455 1048 C ATOM 884 C ALA A 111 85.509 61.964 1.551 1.00 52.94 C ANISOU 884 C ALA A 111 6797 6316 7001 455 1192 819 C ATOM 885 O ALA A 111 85.078 62.368 2.636 1.00 54.44 O ANISOU 885 O ALA A 111 7637 5640 7410 41 1768 691 O ATOM 886 CB ALA A 111 85.183 59.530 1.041 1.00 45.03 C ANISOU 886 CB ALA A 111 3698 5647 7765 1271 726 1998 C ATOM 887 N PRO A 112 85.424 62.685 0.434 1.00 55.19 N ANISOU 887 N PRO A 112 7572 6396 7003 848 638 742 N ATOM 888 CA PRO A 112 84.807 64.018 0.444 1.00 54.22 C ANISOU 888 CA PRO A 112 6868 6455 7279 743 569 625 C ATOM 889 C PRO A 112 83.297 63.900 0.638 1.00 59.71 C ANISOU 889 C PRO A 112 7025 6982 8682 359 1164 -242 C ATOM 890 O PRO A 112 82.712 64.668 1.410 1.00 77.93 O ANISOU 890 O PRO A 112 8031 7763 13817 567 2677 -2149 O ATOM 891 CB PRO A 112 85.161 64.583 -0.933 1.00 57.18 C ANISOU 891 CB PRO A 112 7833 6256 7639 966 1000 896 C ATOM 892 CG PRO A 112 85.243 63.358 -1.791 1.00 54.16 C ANISOU 892 CG PRO A 112 7183 6144 7253 1389 1098 1162 C ATOM 893 CD PRO A 112 85.884 62.312 -0.913 1.00 53.80 C ANISOU 893 CD PRO A 112 6856 6468 7117 1172 1100 1377 C ATOM 894 N ASP A 113 82.656 62.942 -0.025 1.00 58.97 N ANISOU 894 N ASP A 113 7871 6976 7558 -703 978 1015 N ATOM 895 CA ASP A 113 81.230 62.706 0.177 1.00 54.23 C ANISOU 895 CA ASP A 113 7651 6420 6535 -174 564 1816 C ATOM 896 C ASP A 113 81.002 61.413 0.963 1.00 52.93 C ANISOU 896 C ASP A 113 7586 6363 6163 180 639 1741 C ATOM 897 O ASP A 113 80.907 60.341 0.362 1.00 44.98 O ANISOU 897 O ASP A 113 5320 6095 5676 1212 693 1948 O ATOM 898 CB ASP A 113 80.499 62.625 -1.160 1.00 54.08 C ANISOU 898 CB ASP A 113 7975 6588 5985 -110 988 1859 C ATOM 899 CG ASP A 113 78.994 62.556 -1.007 1.00 58.32 C ANISOU 899 CG ASP A 113 7835 7247 7078 -138 293 1121 C ATOM 900 OD1 ASP A 113 78.497 62.317 0.107 1.00 53.98 O ANISOU 900 OD1 ASP A 113 5905 7266 7339 387 -41 1707 O ATOM 901 OD2 ASP A 113 78.289 62.752 -2.019 1.00 61.72 O ANISOU 901 OD2 ASP A 113 8558 8578 6314 -863 -16 -699 O ATOM 902 N ILE A 114 80.918 61.548 2.281 1.00 51.56 N ANISOU 902 N ILE A 114 6967 6312 6311 -162 1211 1397 N ATOM 903 CA ILE A 114 80.756 60.416 3.185 1.00 52.94 C ANISOU 903 CA ILE A 114 7380 6739 5997 -693 1291 1417 C ATOM 904 C ILE A 114 79.586 59.512 2.839 1.00 49.80 C ANISOU 904 C ILE A 114 7019 5918 5983 -7 1190 1105 C ATOM 905 O ILE A 114 79.750 58.286 2.773 1.00 49.57 O ANISOU 905 O ILE A 114 6631 5887 6317 133 1737 1794 O ATOM 906 CB ILE A 114 80.579 60.919 4.633 1.00 55.04 C ANISOU 906 CB ILE A 114 7595 7188 6129 -1136 1136 1055 C ATOM 907 CG1 ILE A 114 81.847 61.581 5.183 1.00 59.43 C ANISOU 907 CG1 ILE A 114 8000 7943 6638 -2048 1462 914 C ATOM 908 CG2 ILE A 114 80.106 59.795 5.542 1.00 45.34 C ANISOU 908 CG2 ILE A 114 6371 5895 4960 -544 270 324 C ATOM 909 CD1 ILE A 114 83.065 60.695 4.952 1.00 67.13 C ANISOU 909 CD1 ILE A 114 7512 7919 10077 -1945 751 1921 C ATOM 910 N ASP A 115 78.387 60.050 2.616 1.00 48.77 N ANISOU 910 N ASP A 115 7171 5406 5955 66 1323 1323 N ATOM 911 CA ASP A 115 77.297 59.118 2.315 1.00 48.39 C ANISOU 911 CA ASP A 115 7228 5264 5896 282 442 1777 C ATOM 912 C ASP A 115 77.558 58.341 1.036 1.00 47.13 C ANISOU 912 C ASP A 115 6772 5891 5245 168 83 1979 C ATOM 913 O ASP A 115 77.146 57.188 0.939 1.00 40.86 O ANISOU 913 O ASP A 115 4896 6366 4264 -85 440 1617 O ATOM 914 CB ASP A 115 75.958 59.849 2.214 1.00 54.10 C ANISOU 914 CB ASP A 115 7425 5973 7156 638 193 1521 C ATOM 915 CG ASP A 115 75.566 60.372 3.588 1.00 57.98 C ANISOU 915 CG ASP A 115 7268 7039 7724 782 726 1041 C ATOM 916 OD1 ASP A 115 76.357 60.199 4.542 1.00 63.54 O ANISOU 916 OD1 ASP A 115 8889 7752 7500 -32 -83 573 O ATOM 917 OD2 ASP A 115 74.471 60.957 3.704 1.00 72.11 O ANISOU 917 OD2 ASP A 115 8323 7947 11127 1838 1191 119 O ATOM 918 N ALA A 116 78.234 58.989 0.101 1.00 45.03 N ANISOU 918 N ALA A 116 6608 5130 5370 362 -231 2216 N ATOM 919 CA ALA A 116 78.573 58.330 -1.156 1.00 46.84 C ANISOU 919 CA ALA A 116 7112 5580 5106 -215 11 2295 C ATOM 920 C ALA A 116 79.560 57.181 -0.955 1.00 42.63 C ANISOU 920 C ALA A 116 6829 5093 4274 -485 416 1882 C ATOM 921 O ALA A 116 79.402 56.087 -1.529 1.00 43.65 O ANISOU 921 O ALA A 116 6664 5785 4135 -790 1404 1188 O ATOM 922 CB ALA A 116 79.129 59.371 -2.109 1.00 45.03 C ANISOU 922 CB ALA A 116 5193 5521 6397 378 640 2551 C ATOM 923 N GLU A 117 80.577 57.437 -0.142 1.00 40.19 N ANISOU 923 N GLU A 117 5901 5384 3985 -321 1107 1559 N ATOM 924 CA GLU A 117 81.569 56.426 0.242 1.00 42.41 C ANISOU 924 CA GLU A 117 6550 5019 4547 -371 582 1690 C ATOM 925 C GLU A 117 80.847 55.197 0.791 1.00 40.28 C ANISOU 925 C GLU A 117 6191 4878 4236 -462 829 1007 C ATOM 926 O GLU A 117 81.119 54.061 0.375 1.00 37.84 O ANISOU 926 O GLU A 117 5358 4923 4096 -54 799 1325 O ATOM 927 CB GLU A 117 82.541 57.025 1.250 1.00 41.10 C ANISOU 927 CB GLU A 117 6379 4044 5193 -218 420 1696 C ATOM 928 CG GLU A 117 83.604 56.154 1.886 1.00 39.62 C ANISOU 928 CG GLU A 117 5565 4581 4906 -77 1126 1712 C ATOM 929 CD GLU A 117 84.501 55.500 0.852 1.00 43.56 C ANISOU 929 CD GLU A 117 6478 4914 5158 -169 1533 1396 C ATOM 930 OE1 GLU A 117 84.641 56.086 -0.248 1.00 40.98 O ANISOU 930 OE1 GLU A 117 5095 5747 4727 12 796 1432 O ATOM 931 OE2 GLU A 117 85.043 54.408 1.144 1.00 41.60 O ANISOU 931 OE2 GLU A 117 5582 5443 4780 120 1472 1403 O ATOM 932 N CYS A 118 79.915 55.430 1.719 1.00 36.59 N ANISOU 932 N CYS A 118 5340 4757 3805 -197 141 868 N ATOM 933 CA CYS A 118 79.217 54.335 2.386 1.00 35.42 C ANISOU 933 CA CYS A 118 4597 4601 4259 145 389 845 C ATOM 934 C CYS A 118 78.355 53.567 1.397 1.00 35.22 C ANISOU 934 C CYS A 118 4292 4824 4266 153 357 926 C ATOM 935 O CYS A 118 78.341 52.335 1.393 1.00 36.37 O ANISOU 935 O CYS A 118 5254 4837 3727 -302 589 909 O ATOM 936 CB CYS A 118 78.399 54.880 3.562 1.00 38.72 C ANISOU 936 CB CYS A 118 6019 4186 4508 272 977 881 C ATOM 937 SG CYS A 118 79.476 55.532 4.887 1.00 42.29 S ANISOU 937 SG CYS A 118 6457 5128 4485 -445 1404 310 S ATOM 938 N ARG A 119 77.639 54.264 0.533 1.00 39.08 N ANISOU 938 N ARG A 119 3719 5677 5451 379 14 1271 N ATOM 939 CA ARG A 119 76.899 53.630 -0.554 1.00 44.31 C ANISOU 939 CA ARG A 119 4903 5728 6206 455 -1119 1422 C ATOM 940 C ARG A 119 77.728 52.770 -1.498 1.00 43.76 C ANISOU 940 C ARG A 119 5164 6305 5159 166 -1336 1150 C ATOM 941 O ARG A 119 77.366 51.670 -1.940 1.00 41.45 O ANISOU 941 O ARG A 119 5564 6327 3860 16 -1556 1553 O ATOM 942 CB ARG A 119 76.232 54.770 -1.349 1.00 52.18 C ANISOU 942 CB ARG A 119 6079 6237 7511 557 -1925 2009 C ATOM 943 CG ARG A 119 74.905 54.397 -1.982 1.00 62.59 C ANISOU 943 CG ARG A 119 7520 7269 8992 -116 -3727 3064 C ATOM 944 CD ARG A 119 74.296 55.590 -2.738 1.00 70.06 C ANISOU 944 CD ARG A 119 8623 7363 10634 217 -4665 3157 C ATOM 945 NE ARG A 119 74.336 56.785 -1.889 1.00 77.92 N ANISOU 945 NE ARG A 119 10834 7176 11594 33 -3455 2858 N ATOM 946 CZ ARG A 119 74.839 57.971 -2.201 1.00 81.38 C ANISOU 946 CZ ARG A 119 11888 7786 11248 -990 -3153 2568 C ATOM 947 NH1 ARG A 119 75.377 58.190 -3.402 1.00 79.87 N ANISOU 947 NH1 ARG A 119 11090 9685 9573 -1384 -5734 3721 N ATOM 948 NH2 ARG A 119 74.795 58.956 -1.302 1.00 78.89 N ANISOU 948 NH2 ARG A 119 10717 8579 10677 -1734 -5670 2193 N ATOM 949 N GLN A 120 78.908 53.262 -1.869 1.00 43.70 N ANISOU 949 N GLN A 120 5581 6454 4567 -50 -1033 1137 N ATOM 950 CA GLN A 120 79.783 52.522 -2.779 1.00 43.77 C ANISOU 950 CA GLN A 120 6264 6209 4159 -91 -698 1472 C ATOM 951 C GLN A 120 80.324 51.240 -2.159 1.00 42.63 C ANISOU 951 C GLN A 120 6254 5980 3964 -171 -1138 1024 C ATOM 952 O GLN A 120 80.445 50.200 -2.818 1.00 40.35 O ANISOU 952 O GLN A 120 5549 6318 3463 -59 -564 1020 O ATOM 953 CB GLN A 120 80.943 53.434 -3.209 1.00 51.15 C ANISOU 953 CB GLN A 120 8110 6639 4685 -934 797 1022 C ATOM 954 CG GLN A 120 80.476 54.617 -4.032 1.00 60.59 C ANISOU 954 CG GLN A 120 10526 6828 5666 -1654 -68 1791 C ATOM 955 CD GLN A 120 81.534 55.687 -4.214 1.00 66.38 C ANISOU 955 CD GLN A 120 11134 7736 6353 -2259 807 2050 C ATOM 956 OE1 GLN A 120 82.727 55.445 -4.011 1.00 80.51 O ANISOU 956 OE1 GLN A 120 11531 10907 8151 -3681 -1848 4294 O ATOM 957 NE2 GLN A 120 81.084 56.883 -4.597 1.00 65.48 N ANISOU 957 NE2 GLN A 120 12268 6515 6094 -1355 4376 647 N ATOM 958 N TYR A 121 80.657 51.324 -0.864 1.00 39.41 N ANISOU 958 N TYR A 121 5523 5545 3904 -557 -941 999 N ATOM 959 CA TYR A 121 81.121 50.135 -0.151 1.00 37.24 C ANISOU 959 CA TYR A 121 4934 5576 3642 -351 -578 889 C ATOM 960 C TYR A 121 80.094 49.009 -0.249 1.00 35.57 C ANISOU 960 C TYR A 121 4686 5266 3564 -56 -151 609 C ATOM 961 O TYR A 121 80.427 47.876 -0.603 1.00 39.31 O ANISOU 961 O TYR A 121 5066 5420 4451 -17 279 342 O ATOM 962 CB TYR A 121 81.400 50.485 1.307 1.00 32.78 C ANISOU 962 CB TYR A 121 4529 4380 3547 235 -18 741 C ATOM 963 CG TYR A 121 82.460 49.676 2.015 1.00 32.72 C ANISOU 963 CG TYR A 121 4195 4876 3362 79 -13 842 C ATOM 964 CD1 TYR A 121 83.772 49.688 1.545 1.00 32.38 C ANISOU 964 CD1 TYR A 121 4294 4542 3467 -45 155 697 C ATOM 965 CD2 TYR A 121 82.144 48.910 3.141 1.00 29.32 C ANISOU 965 CD2 TYR A 121 4353 3681 3105 719 514 215 C ATOM 966 CE1 TYR A 121 84.756 48.959 2.172 1.00 29.55 C ANISOU 966 CE1 TYR A 121 4346 3796 3086 310 491 52 C ATOM 967 CE2 TYR A 121 83.122 48.180 3.779 1.00 26.68 C ANISOU 967 CE2 TYR A 121 4082 3327 2727 406 295 -193 C ATOM 968 CZ TYR A 121 84.407 48.212 3.287 1.00 29.38 C ANISOU 968 CZ TYR A 121 4160 3638 3366 350 482 232 C ATOM 969 OH TYR A 121 85.412 47.493 3.907 1.00 30.92 O ANISOU 969 OH TYR A 121 3871 4298 3580 135 349 502 O ATOM 970 N GLU A 122 78.834 49.306 0.065 1.00 34.29 N ANISOU 970 N GLU A 122 4451 5144 3434 344 -834 1356 N ATOM 971 CA GLU A 122 77.775 48.302 -0.034 1.00 37.50 C ANISOU 971 CA GLU A 122 4800 5818 3630 -156 498 -49 C ATOM 972 C GLU A 122 77.651 47.834 -1.481 1.00 36.58 C ANISOU 972 C GLU A 122 4713 5633 3554 185 412 101 C ATOM 973 O GLU A 122 77.439 46.659 -1.780 1.00 38.91 O ANISOU 973 O GLU A 122 4594 6036 4155 -416 -691 -119 O ATOM 974 CB GLU A 122 76.415 48.829 0.422 1.00 37.54 C ANISOU 974 CB GLU A 122 4948 5625 3692 -122 635 -69 C ATOM 975 CG GLU A 122 76.357 49.173 1.907 1.00 35.43 C ANISOU 975 CG GLU A 122 4337 5596 3529 370 210 271 C ATOM 976 CD GLU A 122 76.170 47.965 2.797 1.00 39.13 C ANISOU 976 CD GLU A 122 5390 5602 3876 -300 368 243 C ATOM 977 OE1 GLU A 122 75.882 46.869 2.271 1.00 40.51 O ANISOU 977 OE1 GLU A 122 5324 5966 4101 -741 -1057 413 O ATOM 978 OE2 GLU A 122 76.327 48.150 4.033 1.00 37.69 O ANISOU 978 OE2 GLU A 122 5819 4757 3746 -47 903 257 O ATOM 979 N GLU A 123 77.785 48.813 -2.388 1.00 41.44 N ANISOU 979 N GLU A 123 5037 6678 4029 -410 -421 951 N ATOM 980 CA GLU A 123 77.683 48.378 -3.789 1.00 45.19 C ANISOU 980 CA GLU A 123 6449 6777 3942 -681 -248 1030 C ATOM 981 C GLU A 123 78.822 47.447 -4.172 1.00 44.81 C ANISOU 981 C GLU A 123 5963 7095 3967 -1105 -108 473 C ATOM 982 O GLU A 123 78.639 46.466 -4.898 1.00 42.83 O ANISOU 982 O GLU A 123 6460 6124 3688 -484 -1306 1300 O ATOM 983 CB GLU A 123 77.643 49.613 -4.693 1.00 52.97 C ANISOU 983 CB GLU A 123 7888 7594 4642 -1002 -1478 1840 C ATOM 984 CG GLU A 123 76.211 49.961 -5.065 1.00 62.88 C ANISOU 984 CG GLU A 123 8488 7466 7937 376 -1773 1479 C ATOM 985 CD GLU A 123 75.741 51.300 -4.544 1.00 75.26 C ANISOU 985 CD GLU A 123 10105 7469 11021 -13 -239 782 C ATOM 986 OE1 GLU A 123 76.201 52.343 -5.059 1.00 94.72 O ANISOU 986 OE1 GLU A 123 15817 7792 12381 -1954 62 894 O ATOM 987 OE2 GLU A 123 74.896 51.311 -3.610 1.00108.70 O ANISOU 987 OE2 GLU A 123 15891 10579 14830 -1925 4492 -3558 O ATOM 988 N LYS A 124 80.033 47.746 -3.684 1.00 43.43 N ANISOU 988 N LYS A 124 6342 6311 3849 -1081 -739 1307 N ATOM 989 CA LYS A 124 81.154 46.865 -4.026 1.00 43.60 C ANISOU 989 CA LYS A 124 5986 6783 3799 -1212 -366 1516 C ATOM 990 C LYS A 124 80.924 45.456 -3.483 1.00 41.43 C ANISOU 990 C LYS A 124 6080 6378 3283 -809 740 844 C ATOM 991 O LYS A 124 81.202 44.473 -4.171 1.00 39.70 O ANISOU 991 O LYS A 124 5588 6905 2593 -416 174 717 O ATOM 992 CB LYS A 124 82.474 47.448 -3.514 1.00 48.70 C ANISOU 992 CB LYS A 124 6154 7889 4462 -1797 -661 2218 C ATOM 993 CG LYS A 124 83.511 47.736 -4.582 1.00 63.43 C ANISOU 993 CG LYS A 124 7294 10431 6376 -3061 617 2158 C ATOM 994 CD LYS A 124 84.928 47.452 -4.104 1.00 65.56 C ANISOU 994 CD LYS A 124 7032 11017 6862 -1995 1436 1559 C ATOM 995 CE LYS A 124 85.760 46.808 -5.205 1.00 69.50 C ANISOU 995 CE LYS A 124 8209 12180 6018 -2846 2079 1601 C ATOM 996 NZ LYS A 124 87.194 46.625 -4.814 1.00 75.15 N ANISOU 996 NZ LYS A 124 7038 17031 4484 -4576 3724 -1262 N ATOM 997 N ILE A 125 80.415 45.323 -2.257 1.00 38.54 N ANISOU 997 N ILE A 125 4878 6076 3689 -691 1108 567 N ATOM 998 CA ILE A 125 80.150 43.971 -1.737 1.00 34.53 C ANISOU 998 CA ILE A 125 3711 6172 3237 -519 393 769 C ATOM 999 C ILE A 125 79.195 43.236 -2.678 1.00 38.08 C ANISOU 999 C ILE A 125 4373 6461 3635 -657 3 649 C ATOM 1000 O ILE A 125 79.435 42.101 -3.113 1.00 40.44 O ANISOU 1000 O ILE A 125 5635 6242 3488 -613 -524 843 O ATOM 1001 CB ILE A 125 79.574 44.022 -0.315 1.00 38.18 C ANISOU 1001 CB ILE A 125 4638 6414 3453 -940 800 561 C ATOM 1002 CG1 ILE A 125 80.563 44.532 0.727 1.00 37.72 C ANISOU 1002 CG1 ILE A 125 4797 6191 3344 -1317 1369 -151 C ATOM 1003 CG2 ILE A 125 79.037 42.650 0.076 1.00 31.39 C ANISOU 1003 CG2 ILE A 125 3778 5944 2204 -412 106 304 C ATOM 1004 CD1 ILE A 125 79.942 45.166 1.949 1.00 33.33 C ANISOU 1004 CD1 ILE A 125 3304 5887 3474 -140 1071 460 C ATOM 1005 N ARG A 126 78.097 43.934 -3.012 1.00 39.91 N ANISOU 1005 N ARG A 126 5093 6528 3541 -592 -799 1236 N ATOM 1006 CA ARG A 126 77.105 43.328 -3.906 1.00 41.68 C ANISOU 1006 CA ARG A 126 4615 6590 4630 -591 -504 396 C ATOM 1007 C ARG A 126 77.729 43.068 -5.266 1.00 42.83 C ANISOU 1007 C ARG A 126 6096 6161 4016 -833 -706 654 C ATOM 1008 O ARG A 126 77.284 42.168 -5.978 1.00 50.68 O ANISOU 1008 O ARG A 126 8113 7268 3876 -1592 -1649 650 O ATOM 1009 CB ARG A 126 75.840 44.181 -4.040 1.00 49.83 C ANISOU 1009 CB ARG A 126 4423 7446 7066 -493 -945 639 C ATOM 1010 CG ARG A 126 75.135 44.379 -2.704 1.00 61.30 C ANISOU 1010 CG ARG A 126 5305 8610 9378 -150 1073 -467 C ATOM 1011 CD ARG A 126 73.913 45.280 -2.772 1.00 70.98 C ANISOU 1011 CD ARG A 126 6066 8802 12102 403 337 -1383 C ATOM 1012 NE ARG A 126 73.644 46.003 -1.522 1.00 75.78 N ANISOU 1012 NE ARG A 126 6410 9126 13256 732 279 -2434 N ATOM 1013 CZ ARG A 126 73.503 47.327 -1.464 1.00 80.52 C ANISOU 1013 CZ ARG A 126 7729 9012 13852 270 -308 -2303 C ATOM 1014 NH1 ARG A 126 73.605 48.060 -2.573 1.00 75.26 N ANISOU 1014 NH1 ARG A 126 3984 10070 14544 614 -1937 -1211 N ATOM 1015 NH2 ARG A 126 73.259 47.935 -0.304 1.00 84.71 N ANISOU 1015 NH2 ARG A 126 8443 9133 14609 154 -560 -3265 N ATOM 1016 N SER A 127 78.763 43.804 -5.680 1.00 45.17 N ANISOU 1016 N SER A 127 6405 6105 4654 -537 272 666 N ATOM 1017 CA SER A 127 79.296 43.483 -7.022 1.00 45.18 C ANISOU 1017 CA SER A 127 6382 6517 4269 -264 -284 650 C ATOM 1018 C SER A 127 79.889 42.083 -7.002 1.00 44.06 C ANISOU 1018 C SER A 127 5846 6620 4274 -268 -1001 7 C ATOM 1019 O SER A 127 79.849 41.390 -8.010 1.00 51.05 O ANISOU 1019 O SER A 127 9415 6449 3533 -269 -623 590 O ATOM 1020 CB SER A 127 80.332 44.497 -7.492 1.00 46.96 C ANISOU 1020 CB SER A 127 6559 6827 4457 -337 566 241 C ATOM 1021 OG SER A 127 81.505 44.401 -6.680 1.00 47.73 O ANISOU 1021 OG SER A 127 5686 6576 5873 44 856 1070 O ATOM 1022 N TYR A 128 80.434 41.634 -5.874 1.00 41.48 N ANISOU 1022 N TYR A 128 5253 6118 4389 -622 -1232 -208 N ATOM 1023 CA TYR A 128 80.984 40.291 -5.817 1.00 41.75 C ANISOU 1023 CA TYR A 128 5167 6292 4404 -421 -748 -126 C ATOM 1024 C TYR A 128 79.887 39.294 -5.473 1.00 43.28 C ANISOU 1024 C TYR A 128 5150 5889 5406 -311 -543 -473 C ATOM 1025 O TYR A 128 80.031 38.109 -5.751 1.00 50.69 O ANISOU 1025 O TYR A 128 6660 5912 6687 -290 -152 -716 O ATOM 1026 CB TYR A 128 82.072 40.151 -4.758 1.00 40.32 C ANISOU 1026 CB TYR A 128 5256 6154 3908 -642 -520 476 C ATOM 1027 CG TYR A 128 83.383 40.823 -5.096 1.00 38.84 C ANISOU 1027 CG TYR A 128 5027 5838 3892 -375 -576 486 C ATOM 1028 CD1 TYR A 128 84.298 40.215 -5.944 1.00 40.46 C ANISOU 1028 CD1 TYR A 128 5413 5790 4169 -563 -303 184 C ATOM 1029 CD2 TYR A 128 83.686 42.073 -4.549 1.00 36.34 C ANISOU 1029 CD2 TYR A 128 4779 5615 3412 -143 -577 724 C ATOM 1030 CE1 TYR A 128 85.495 40.825 -6.255 1.00 41.77 C ANISOU 1030 CE1 TYR A 128 6297 5884 3690 -902 535 585 C ATOM 1031 CE2 TYR A 128 84.887 42.680 -4.863 1.00 39.91 C ANISOU 1031 CE2 TYR A 128 4938 5837 4389 -371 -305 415 C ATOM 1032 CZ TYR A 128 85.778 42.054 -5.711 1.00 41.74 C ANISOU 1032 CZ TYR A 128 6221 6101 3537 -1268 787 509 C ATOM 1033 OH TYR A 128 86.967 42.693 -5.994 1.00 42.11 O ANISOU 1033 OH TYR A 128 6000 5514 4487 -746 719 1670 O ATOM 1034 N GLY A 129 78.813 39.779 -4.848 1.00 42.11 N ANISOU 1034 N GLY A 129 5664 6058 4278 -85 -183 498 N ATOM 1035 CA GLY A 129 77.710 38.866 -4.579 1.00 40.48 C ANISOU 1035 CA GLY A 129 6175 6021 3184 -368 176 -100 C ATOM 1036 C GLY A 129 77.512 38.713 -3.090 1.00 37.91 C ANISOU 1036 C GLY A 129 5236 6069 3100 293 -58 -536 C ATOM 1037 O GLY A 129 76.459 39.052 -2.568 1.00 40.86 O ANISOU 1037 O GLY A 129 5364 6091 4071 -64 550 -542 O ATOM 1038 N LYS A 130 78.512 38.211 -2.364 1.00 41.09 N ANISOU 1038 N LYS A 130 5571 6204 3836 -158 -867 -467 N ATOM 1039 CA LYS A 130 78.282 38.086 -0.930 1.00 39.33 C ANISOU 1039 CA LYS A 130 5076 5865 4003 -166 -797 221 C ATOM 1040 C LYS A 130 79.607 37.873 -0.209 1.00 34.07 C ANISOU 1040 C LYS A 130 4613 4869 3463 492 -65 -221 C ATOM 1041 O LYS A 130 80.550 37.419 -0.856 1.00 37.69 O ANISOU 1041 O LYS A 130 4983 5663 3676 -107 1081 345 O ATOM 1042 CB LYS A 130 77.378 36.900 -0.611 1.00 48.04 C ANISOU 1042 CB LYS A 130 6199 6826 5226 -1318 -1696 846 C ATOM 1043 CG LYS A 130 78.091 35.589 -0.956 1.00 56.92 C ANISOU 1043 CG LYS A 130 8814 5910 6904 -696 -2458 1845 C ATOM 1044 CD LYS A 130 77.210 34.420 -0.525 1.00 64.23 C ANISOU 1044 CD LYS A 130 10079 6950 7377 -1460 -1556 2019 C ATOM 1045 CE LYS A 130 75.832 34.944 -0.131 1.00 66.12 C ANISOU 1045 CE LYS A 130 10805 8179 6139 -1726 -125 739 C ATOM 1046 NZ LYS A 130 75.733 35.240 1.327 1.00 77.00 N ANISOU 1046 NZ LYS A 130 14511 8537 6209 -992 -1736 -441 N ATOM 1047 N ILE A 131 79.594 38.202 1.065 1.00 31.02 N ANISOU 1047 N ILE A 131 3861 4582 3345 -482 133 -47 N ATOM 1048 CA ILE A 131 80.753 37.888 1.903 1.00 31.31 C ANISOU 1048 CA ILE A 131 4012 4209 3678 -423 -81 -152 C ATOM 1049 C ILE A 131 80.609 36.436 2.323 1.00 30.73 C ANISOU 1049 C ILE A 131 3753 4269 3654 -517 150 -164 C ATOM 1050 O ILE A 131 79.557 36.066 2.853 1.00 34.14 O ANISOU 1050 O ILE A 131 3854 5108 4008 -791 188 99 O ATOM 1051 CB ILE A 131 80.824 38.877 3.083 1.00 33.63 C ANISOU 1051 CB ILE A 131 5058 4285 3436 -1033 -124 -9 C ATOM 1052 CG1 ILE A 131 81.070 40.308 2.585 1.00 31.40 C ANISOU 1052 CG1 ILE A 131 4514 4086 3331 -270 -208 42 C ATOM 1053 CG2 ILE A 131 81.857 38.446 4.110 1.00 25.43 C ANISOU 1053 CG2 ILE A 131 4033 3240 2391 138 1295 -502 C ATOM 1054 CD1 ILE A 131 80.923 41.405 3.589 1.00 29.42 C ANISOU 1054 CD1 ILE A 131 4061 4050 3066 284 -38 314 C ATOM 1055 N HIS A 132 81.598 35.578 2.084 1.00 28.52 N ANISOU 1055 N HIS A 132 4089 4323 2422 -235 -296 -275 N ATOM 1056 CA HIS A 132 81.458 34.175 2.464 1.00 30.32 C ANISOU 1056 CA HIS A 132 4157 4435 2930 -299 71 -4 C ATOM 1057 C HIS A 132 81.655 33.930 3.951 1.00 31.66 C ANISOU 1057 C HIS A 132 4407 4647 2975 -666 86 210 C ATOM 1058 O HIS A 132 81.020 33.027 4.513 1.00 33.63 O ANISOU 1058 O HIS A 132 5439 4291 3048 -711 1019 -321 O ATOM 1059 CB HIS A 132 82.473 33.337 1.676 1.00 30.62 C ANISOU 1059 CB HIS A 132 4246 4205 3184 -277 46 -46 C ATOM 1060 CG HIS A 132 82.230 33.498 0.198 1.00 32.30 C ANISOU 1060 CG HIS A 132 4720 4451 3103 -214 79 -368 C ATOM 1061 ND1 HIS A 132 81.185 32.882 -0.455 1.00 37.74 N ANISOU 1061 ND1 HIS A 132 5939 5256 3143 -1222 -185 -328 N ATOM 1062 CD2 HIS A 132 82.895 34.199 -0.731 1.00 30.12 C ANISOU 1062 CD2 HIS A 132 4730 4248 2467 -1 741 -1297 C ATOM 1063 CE1 HIS A 132 81.218 33.202 -1.740 1.00 40.61 C ANISOU 1063 CE1 HIS A 132 6737 5694 3000 -1929 -57 -571 C ATOM 1064 NE2 HIS A 132 82.253 34.006 -1.925 1.00 40.22 N ANISOU 1064 NE2 HIS A 132 6345 5845 3092 -1717 -282 -259 N ATOM 1065 N LEU A 133 82.537 34.725 4.553 1.00 31.59 N ANISOU 1065 N LEU A 133 4605 4354 3043 -380 -89 -26 N ATOM 1066 CA LEU A 133 82.848 34.599 5.968 1.00 28.37 C ANISOU 1066 CA LEU A 133 3938 3870 2972 -91 196 10 C ATOM 1067 C LEU A 133 83.174 35.971 6.542 1.00 28.98 C ANISOU 1067 C LEU A 133 3357 4254 3399 -330 353 -398 C ATOM 1068 O LEU A 133 84.132 36.600 6.068 1.00 32.62 O ANISOU 1068 O LEU A 133 4510 4525 3358 -792 898 -113 O ATOM 1069 CB LEU A 133 84.023 33.664 6.181 1.00 29.90 C ANISOU 1069 CB LEU A 133 3627 4260 3473 -104 292 -72 C ATOM 1070 CG LEU A 133 84.556 33.506 7.607 1.00 30.77 C ANISOU 1070 CG LEU A 133 3544 4725 3421 360 627 493 C ATOM 1071 CD1 LEU A 133 83.483 33.043 8.574 1.00 30.36 C ANISOU 1071 CD1 LEU A 133 3154 5025 3356 -426 420 -419 C ATOM 1072 CD2 LEU A 133 85.725 32.512 7.590 1.00 30.54 C ANISOU 1072 CD2 LEU A 133 3610 4669 3327 357 529 -212 C ATOM 1073 N PHE A 134 82.378 36.409 7.515 1.00 30.24 N ANISOU 1073 N PHE A 134 4088 4159 3241 -390 666 -253 N ATOM 1074 CA PHE A 134 82.629 37.696 8.152 1.00 27.13 C ANISOU 1074 CA PHE A 134 3676 3832 2800 -121 279 137 C ATOM 1075 C PHE A 134 83.094 37.414 9.583 1.00 27.18 C ANISOU 1075 C PHE A 134 3808 3450 3069 -186 63 527 C ATOM 1076 O PHE A 134 82.336 36.871 10.382 1.00 27.06 O ANISOU 1076 O PHE A 134 3762 3739 2780 -314 182 84 O ATOM 1077 CB PHE A 134 81.394 38.596 8.159 1.00 26.18 C ANISOU 1077 CB PHE A 134 3256 3825 2867 -375 109 415 C ATOM 1078 CG PHE A 134 81.690 40.082 8.065 1.00 28.15 C ANISOU 1078 CG PHE A 134 3764 3739 3192 -258 -66 289 C ATOM 1079 CD1 PHE A 134 82.670 40.669 8.857 1.00 27.28 C ANISOU 1079 CD1 PHE A 134 3910 3496 2959 7 63 -133 C ATOM 1080 CD2 PHE A 134 80.984 40.897 7.173 1.00 26.16 C ANISOU 1080 CD2 PHE A 134 3356 3681 2900 -3 414 148 C ATOM 1081 CE1 PHE A 134 82.930 42.019 8.752 1.00 29.02 C ANISOU 1081 CE1 PHE A 134 4191 3644 3192 -273 60 88 C ATOM 1082 CE2 PHE A 134 81.253 42.254 7.054 1.00 28.76 C ANISOU 1082 CE2 PHE A 134 4500 3692 2734 -148 175 169 C ATOM 1083 CZ PHE A 134 82.241 42.820 7.845 1.00 30.25 C ANISOU 1083 CZ PHE A 134 4737 3547 3210 -171 -64 52 C ATOM 1084 N MET A 135 84.321 37.761 9.905 1.00 26.32 N ANISOU 1084 N MET A 135 3595 3693 2714 -5 367 190 N ATOM 1085 CA MET A 135 84.901 37.636 11.217 1.00 25.09 C ANISOU 1085 CA MET A 135 3269 3703 2560 -166 605 448 C ATOM 1086 C MET A 135 84.757 38.954 11.957 1.00 25.40 C ANISOU 1086 C MET A 135 3207 3842 2601 -266 460 287 C ATOM 1087 O MET A 135 85.000 40.029 11.409 1.00 25.93 O ANISOU 1087 O MET A 135 3696 3701 2456 163 571 289 O ATOM 1088 CB MET A 135 86.392 37.263 11.129 1.00 25.32 C ANISOU 1088 CB MET A 135 3207 4013 2401 -318 701 302 C ATOM 1089 CG MET A 135 86.939 37.027 12.544 1.00 28.15 C ANISOU 1089 CG MET A 135 3367 4549 2781 -814 4 125 C ATOM 1090 SD MET A 135 88.592 36.297 12.489 1.00 31.02 S ANISOU 1090 SD MET A 135 3750 4653 3384 -375 -86 334 S ATOM 1091 CE MET A 135 89.543 37.757 11.998 1.00 28.43 C ANISOU 1091 CE MET A 135 3016 4068 3717 -83 256 -533 C ATOM 1092 N GLY A 136 84.352 38.930 13.227 1.00 24.78 N ANISOU 1092 N GLY A 136 3188 3786 2439 -503 167 240 N ATOM 1093 CA GLY A 136 84.228 40.183 13.975 1.00 27.87 C ANISOU 1093 CA GLY A 136 3717 4095 2776 -678 220 -175 C ATOM 1094 C GLY A 136 84.449 39.935 15.458 1.00 26.53 C ANISOU 1094 C GLY A 136 3610 3703 2768 -44 526 -170 C ATOM 1095 O GLY A 136 84.705 38.803 15.894 1.00 27.86 O ANISOU 1095 O GLY A 136 3389 3779 3417 81 -146 -182 O ATOM 1096 N GLY A 137 84.352 40.993 16.248 1.00 29.09 N ANISOU 1096 N GLY A 137 4509 3712 2831 -273 435 -262 N ATOM 1097 CA GLY A 137 84.316 40.875 17.709 1.00 28.89 C ANISOU 1097 CA GLY A 137 4062 4089 2827 -596 602 -311 C ATOM 1098 C GLY A 137 82.955 41.361 18.223 1.00 28.78 C ANISOU 1098 C GLY A 137 3846 4271 2819 -450 276 -211 C ATOM 1099 O GLY A 137 82.021 41.529 17.432 1.00 29.61 O ANISOU 1099 O GLY A 137 4311 4132 2806 -454 18 -10 O ATOM 1100 N VAL A 138 82.844 41.589 19.535 1.00 26.82 N ANISOU 1100 N VAL A 138 3435 3959 2794 -174 231 -77 N ATOM 1101 CA VAL A 138 81.556 42.055 20.061 1.00 24.45 C ANISOU 1101 CA VAL A 138 3353 3292 2644 -155 53 295 C ATOM 1102 C VAL A 138 81.813 43.036 21.198 1.00 24.17 C ANISOU 1102 C VAL A 138 3323 3399 2464 47 -81 329 C ATOM 1103 O VAL A 138 82.775 42.878 21.955 1.00 26.46 O ANISOU 1103 O VAL A 138 3429 3798 2826 -189 -351 516 O ATOM 1104 CB VAL A 138 80.693 40.847 20.481 1.00 25.77 C ANISOU 1104 CB VAL A 138 3325 3426 3039 -172 -199 611 C ATOM 1105 CG1 VAL A 138 81.411 40.032 21.553 1.00 28.40 C ANISOU 1105 CG1 VAL A 138 4717 3466 2609 121 -305 480 C ATOM 1106 CG2 VAL A 138 79.312 41.256 20.973 1.00 26.22 C ANISOU 1106 CG2 VAL A 138 3531 4230 2201 -424 148 240 C ATOM 1107 N GLY A 139 80.972 44.068 21.298 1.00 24.37 N ANISOU 1107 N GLY A 139 3893 2966 2402 32 106 679 N ATOM 1108 CA GLY A 139 81.150 45.051 22.356 1.00 26.69 C ANISOU 1108 CA GLY A 139 4036 3470 2635 13 248 245 C ATOM 1109 C GLY A 139 80.718 44.448 23.688 1.00 27.30 C ANISOU 1109 C GLY A 139 4457 3318 2597 -329 173 122 C ATOM 1110 O GLY A 139 80.039 43.408 23.748 1.00 28.89 O ANISOU 1110 O GLY A 139 4748 3244 2984 -395 -207 425 O ATOM 1111 N ASN A 140 81.107 45.094 24.795 1.00 25.69 N ANISOU 1111 N ASN A 140 3631 3502 2629 48 -42 124 N ATOM 1112 CA ASN A 140 80.712 44.653 26.116 1.00 27.00 C ANISOU 1112 CA ASN A 140 3575 4061 2622 -548 93 -99 C ATOM 1113 C ASN A 140 79.183 44.654 26.234 1.00 28.54 C ANISOU 1113 C ASN A 140 3580 3849 3413 -564 68 141 C ATOM 1114 O ASN A 140 78.614 43.856 26.998 1.00 26.79 O ANISOU 1114 O ASN A 140 3564 3855 2759 -580 23 -128 O ATOM 1115 CB ASN A 140 81.298 45.561 27.197 1.00 24.74 C ANISOU 1115 CB ASN A 140 3986 2859 2555 -398 -275 507 C ATOM 1116 CG ASN A 140 82.803 45.478 27.317 1.00 27.52 C ANISOU 1116 CG ASN A 140 4084 3268 3104 -302 -543 -183 C ATOM 1117 OD1 ASN A 140 83.491 44.716 26.617 1.00 28.78 O ANISOU 1117 OD1 ASN A 140 4295 4160 2480 -141 170 318 O ATOM 1118 ND2 ASN A 140 83.367 46.281 28.214 1.00 32.68 N ANISOU 1118 ND2 ASN A 140 4801 4318 3298 -1401 -449 -329 N ATOM 1119 N ASP A 141 78.534 45.550 25.504 1.00 25.43 N ANISOU 1119 N ASP A 141 3624 3714 2323 -341 347 -354 N ATOM 1120 CA ASP A 141 77.072 45.580 25.582 1.00 26.26 C ANISOU 1120 CA ASP A 141 3642 3814 2522 -331 355 -36 C ATOM 1121 C ASP A 141 76.436 44.807 24.437 1.00 26.49 C ANISOU 1121 C ASP A 141 3569 3491 3006 -170 94 -156 C ATOM 1122 O ASP A 141 75.252 45.025 24.136 1.00 25.75 O ANISOU 1122 O ASP A 141 3565 3223 2995 -391 112 560 O ATOM 1123 CB ASP A 141 76.557 47.025 25.582 1.00 26.72 C ANISOU 1123 CB ASP A 141 3547 3842 2765 -309 -249 -384 C ATOM 1124 CG ASP A 141 76.973 47.741 24.308 1.00 26.06 C ANISOU 1124 CG ASP A 141 3097 3817 2989 461 -314 22 C ATOM 1125 OD1 ASP A 141 76.699 48.954 24.175 1.00 34.78 O ANISOU 1125 OD1 ASP A 141 5599 3472 4144 141 402 -150 O ATOM 1126 OD2 ASP A 141 77.592 47.129 23.417 1.00 30.28 O ANISOU 1126 OD2 ASP A 141 4384 3992 3130 256 314 -130 O ATOM 1127 N GLY A 142 77.194 43.937 23.779 1.00 26.48 N ANISOU 1127 N GLY A 142 3962 3312 2788 -208 434 86 N ATOM 1128 CA GLY A 142 76.656 43.082 22.717 1.00 25.59 C ANISOU 1128 CA GLY A 142 3756 3176 2790 -148 467 139 C ATOM 1129 C GLY A 142 76.613 43.731 21.358 1.00 25.67 C ANISOU 1129 C GLY A 142 3392 3211 3151 224 -423 428 C ATOM 1130 O GLY A 142 76.196 43.087 20.366 1.00 27.27 O ANISOU 1130 O GLY A 142 3583 3831 2948 -36 154 66 O ATOM 1131 N HIS A 143 77.021 44.999 21.210 1.00 26.81 N ANISOU 1131 N HIS A 143 3542 3427 3216 -44 -50 594 N ATOM 1132 CA HIS A 143 76.929 45.670 19.896 1.00 27.70 C ANISOU 1132 CA HIS A 143 3694 3720 3113 -107 -43 623 C ATOM 1133 C HIS A 143 77.972 45.159 18.912 1.00 28.72 C ANISOU 1133 C HIS A 143 3819 4031 3063 -16 -117 490 C ATOM 1134 O HIS A 143 78.963 44.526 19.287 1.00 28.56 O ANISOU 1134 O HIS A 143 3322 4544 2984 -223 -216 252 O ATOM 1135 CB HIS A 143 77.094 47.189 20.030 1.00 28.55 C ANISOU 1135 CB HIS A 143 4574 3745 2530 -324 194 700 C ATOM 1136 CG HIS A 143 78.493 47.678 20.250 1.00 35.65 C ANISOU 1136 CG HIS A 143 5284 4866 3394 -1553 -40 960 C ATOM 1137 ND1 HIS A 143 79.008 47.887 21.516 1.00 33.00 N ANISOU 1137 ND1 HIS A 143 4485 4459 3595 -302 -143 483 N ATOM 1138 CD2 HIS A 143 79.495 48.031 19.391 1.00 39.21 C ANISOU 1138 CD2 HIS A 143 5260 5829 3811 -1714 220 735 C ATOM 1139 CE1 HIS A 143 80.248 48.329 21.458 1.00 33.43 C ANISOU 1139 CE1 HIS A 143 4082 4472 4145 252 -361 928 C ATOM 1140 NE2 HIS A 143 80.573 48.419 20.173 1.00 38.04 N ANISOU 1140 NE2 HIS A 143 4721 5393 4340 -876 -18 943 N ATOM 1141 N ILE A 144 77.764 45.491 17.638 1.00 27.69 N ANISOU 1141 N ILE A 144 4000 3529 2989 -166 -216 269 N ATOM 1142 CA ILE A 144 78.673 45.046 16.579 1.00 30.21 C ANISOU 1142 CA ILE A 144 4441 3961 3078 -20 -40 137 C ATOM 1143 C ILE A 144 79.288 46.221 15.841 1.00 30.24 C ANISOU 1143 C ILE A 144 4207 4313 2970 29 -24 347 C ATOM 1144 O ILE A 144 78.572 47.181 15.501 1.00 28.53 O ANISOU 1144 O ILE A 144 3824 4341 2677 -185 -149 407 O ATOM 1145 CB ILE A 144 77.887 44.107 15.654 1.00 35.87 C ANISOU 1145 CB ILE A 144 5317 5273 3038 -1017 499 -391 C ATOM 1146 CG1 ILE A 144 77.666 42.746 16.339 1.00 39.81 C ANISOU 1146 CG1 ILE A 144 6210 5401 3515 -2039 1688 -660 C ATOM 1147 CG2 ILE A 144 78.549 43.992 14.284 1.00 38.08 C ANISOU 1147 CG2 ILE A 144 5980 5485 3002 -1448 680 -144 C ATOM 1148 CD1 ILE A 144 76.723 41.830 15.611 1.00 44.89 C ANISOU 1148 CD1 ILE A 144 5198 7047 4812 -2738 1919 -773 C ATOM 1149 N ALA A 145 80.603 46.146 15.616 1.00 30.04 N ANISOU 1149 N ALA A 145 4019 4709 2687 51 -574 734 N ATOM 1150 CA ALA A 145 81.327 47.217 14.933 1.00 33.88 C ANISOU 1150 CA ALA A 145 4272 4899 3700 -516 -314 528 C ATOM 1151 C ALA A 145 81.013 48.538 15.611 1.00 32.88 C ANISOU 1151 C ALA A 145 3871 4994 3626 -722 282 533 C ATOM 1152 O ALA A 145 81.079 48.591 16.850 1.00 37.05 O ANISOU 1152 O ALA A 145 5636 4738 3703 -722 -285 559 O ATOM 1153 CB ALA A 145 80.967 47.256 13.454 1.00 31.60 C ANISOU 1153 CB ALA A 145 4304 4341 3363 -118 479 935 C ATOM 1154 N PHE A 146 80.659 49.587 14.871 1.00 32.14 N ANISOU 1154 N PHE A 146 4142 4992 3078 -336 1125 474 N ATOM 1155 CA PHE A 146 80.285 50.823 15.556 1.00 32.43 C ANISOU 1155 CA PHE A 146 4183 5097 3041 -475 853 228 C ATOM 1156 C PHE A 146 78.765 50.975 15.593 1.00 31.27 C ANISOU 1156 C PHE A 146 4169 4422 3293 -471 846 212 C ATOM 1157 O PHE A 146 78.260 52.065 15.907 1.00 35.15 O ANISOU 1157 O PHE A 146 4625 4822 3907 -252 620 -501 O ATOM 1158 CB PHE A 146 80.871 52.096 14.938 1.00 32.34 C ANISOU 1158 CB PHE A 146 4126 5133 3028 -936 384 31 C ATOM 1159 CG PHE A 146 82.352 52.229 15.264 1.00 36.84 C ANISOU 1159 CG PHE A 146 4333 5777 3886 -1021 -100 160 C ATOM 1160 CD1 PHE A 146 82.755 52.675 16.508 1.00 42.68 C ANISOU 1160 CD1 PHE A 146 4466 7257 4494 -1295 -187 -795 C ATOM 1161 CD2 PHE A 146 83.303 51.904 14.317 1.00 34.07 C ANISOU 1161 CD2 PHE A 146 3601 5135 4210 121 -789 -10 C ATOM 1162 CE1 PHE A 146 84.102 52.793 16.799 1.00 45.34 C ANISOU 1162 CE1 PHE A 146 4476 7702 5049 -1527 -157 -1240 C ATOM 1163 CE2 PHE A 146 84.647 52.019 14.589 1.00 35.10 C ANISOU 1163 CE2 PHE A 146 3813 5445 4079 116 -1337 176 C ATOM 1164 CZ PHE A 146 85.035 52.468 15.834 1.00 39.62 C ANISOU 1164 CZ PHE A 146 4236 6578 4238 -695 -785 -513 C ATOM 1165 N ASN A 147 78.041 49.907 15.286 1.00 31.88 N ANISOU 1165 N ASN A 147 4445 4628 3040 -483 137 78 N ATOM 1166 CA ASN A 147 76.591 50.015 15.452 1.00 31.70 C ANISOU 1166 CA ASN A 147 4438 4565 3042 -688 276 -26 C ATOM 1167 C ASN A 147 76.203 50.145 16.918 1.00 34.38 C ANISOU 1167 C ASN A 147 4673 5296 3095 -405 194 -487 C ATOM 1168 O ASN A 147 76.833 49.620 17.845 1.00 40.03 O ANISOU 1168 O ASN A 147 6438 5686 3087 254 632 390 O ATOM 1169 CB ASN A 147 75.926 48.769 14.862 1.00 30.43 C ANISOU 1169 CB ASN A 147 4384 4252 2927 -123 -373 45 C ATOM 1170 CG ASN A 147 76.209 48.688 13.373 1.00 30.24 C ANISOU 1170 CG ASN A 147 4651 3873 2967 1 -136 262 C ATOM 1171 OD1 ASN A 147 75.446 49.307 12.618 1.00 32.49 O ANISOU 1171 OD1 ASN A 147 4299 4953 3093 -219 -486 341 O ATOM 1172 ND2 ASN A 147 77.258 47.967 12.993 1.00 30.25 N ANISOU 1172 ND2 ASN A 147 4554 3366 3574 -380 304 317 N ATOM 1173 N GLU A 148 75.112 50.854 17.218 1.00 36.52 N ANISOU 1173 N GLU A 148 4784 5165 3926 -576 621 -647 N ATOM 1174 CA GLU A 148 74.754 50.978 18.619 1.00 37.62 C ANISOU 1174 CA GLU A 148 4800 5496 3996 -506 795 -628 C ATOM 1175 C GLU A 148 73.748 49.927 19.040 1.00 35.13 C ANISOU 1175 C GLU A 148 4193 5501 3653 -282 383 -550 C ATOM 1176 O GLU A 148 73.147 49.292 18.181 1.00 36.10 O ANISOU 1176 O GLU A 148 4942 5346 3428 -441 92 -134 O ATOM 1177 CB GLU A 148 74.253 52.413 18.839 1.00 44.63 C ANISOU 1177 CB GLU A 148 6139 5477 5341 -679 1299 -1418 C ATOM 1178 CG GLU A 148 75.403 53.126 19.571 1.00 62.51 C ANISOU 1178 CG GLU A 148 10150 6335 7266 -2672 -1198 -738 C ATOM 1179 CD GLU A 148 75.206 54.618 19.703 1.00 62.28 C ANISOU 1179 CD GLU A 148 10737 6366 6563 -2751 -91 -994 C ATOM 1180 OE1 GLU A 148 74.761 54.994 20.814 1.00 58.46 O ANISOU 1180 OE1 GLU A 148 8529 7728 5956 -589 -931 32 O ATOM 1181 OE2 GLU A 148 75.502 55.318 18.705 1.00 53.92 O ANISOU 1181 OE2 GLU A 148 7807 6685 5995 -228 -852 -345 O ATOM 1182 N PRO A 149 73.582 49.751 20.339 1.00 32.87 N ANISOU 1182 N PRO A 149 3807 5083 3601 -97 -179 -132 N ATOM 1183 CA PRO A 149 72.502 48.911 20.839 1.00 32.24 C ANISOU 1183 CA PRO A 149 4390 4418 3444 -319 -805 463 C ATOM 1184 C PRO A 149 71.184 49.423 20.255 1.00 31.02 C ANISOU 1184 C PRO A 149 3812 4107 3866 -8 -140 -98 C ATOM 1185 O PRO A 149 71.021 50.630 20.079 1.00 30.07 O ANISOU 1185 O PRO A 149 3975 4089 3359 -109 69 11 O ATOM 1186 CB PRO A 149 72.553 49.175 22.333 1.00 31.62 C ANISOU 1186 CB PRO A 149 4043 4309 3661 -329 -144 -207 C ATOM 1187 CG PRO A 149 73.976 49.543 22.617 1.00 34.44 C ANISOU 1187 CG PRO A 149 4321 5187 3579 -832 -344 -382 C ATOM 1188 CD PRO A 149 74.379 50.361 21.417 1.00 35.77 C ANISOU 1188 CD PRO A 149 4150 5686 3756 -783 18 -291 C ATOM 1189 N ALA A 150 70.271 48.521 19.945 1.00 31.18 N ANISOU 1189 N ALA A 150 3700 4110 4039 -107 -144 333 N ATOM 1190 CA ALA A 150 68.957 48.753 19.340 1.00 28.85 C ANISOU 1190 CA ALA A 150 3788 3648 3525 217 -129 -142 C ATOM 1191 C ALA A 150 69.124 49.253 17.913 1.00 30.57 C ANISOU 1191 C ALA A 150 4376 3691 3548 371 -19 -112 C ATOM 1192 O ALA A 150 68.198 49.855 17.373 1.00 31.66 O ANISOU 1192 O ALA A 150 4014 4233 3783 29 -88 363 O ATOM 1193 CB ALA A 150 68.087 49.710 20.139 1.00 31.71 C ANISOU 1193 CB ALA A 150 3074 4424 4551 -839 652 -1116 C ATOM 1194 N SER A 151 70.287 48.998 17.305 1.00 29.94 N ANISOU 1194 N SER A 151 3870 4227 3279 -100 -355 23 N ATOM 1195 CA SER A 151 70.411 49.245 15.883 1.00 28.79 C ANISOU 1195 CA SER A 151 3667 3912 3359 -130 -366 214 C ATOM 1196 C SER A 151 69.402 48.359 15.146 1.00 27.85 C ANISOU 1196 C SER A 151 3270 4162 3148 -5 -137 69 C ATOM 1197 O SER A 151 69.165 47.255 15.640 1.00 28.87 O ANISOU 1197 O SER A 151 3544 4607 2820 -650 -615 285 O ATOM 1198 CB SER A 151 71.785 48.877 15.314 1.00 29.68 C ANISOU 1198 CB SER A 151 3367 4612 3298 -169 -518 533 C ATOM 1199 OG SER A 151 72.784 49.833 15.637 1.00 34.72 O ANISOU 1199 OG SER A 151 3690 4948 4553 -486 -1143 1135 O ATOM 1200 N SER A 152 68.896 48.826 14.018 1.00 29.45 N ANISOU 1200 N SER A 152 3378 3942 3869 9 -659 386 N ATOM 1201 CA SER A 152 68.153 47.982 13.091 1.00 29.19 C ANISOU 1201 CA SER A 152 3469 4067 3556 16 -643 433 C ATOM 1202 C SER A 152 68.996 46.794 12.651 1.00 29.48 C ANISOU 1202 C SER A 152 3728 3893 3582 34 -663 526 C ATOM 1203 O SER A 152 70.201 46.925 12.364 1.00 29.07 O ANISOU 1203 O SER A 152 3750 3599 3698 168 -539 744 O ATOM 1204 CB SER A 152 67.720 48.780 11.852 1.00 24.29 C ANISOU 1204 CB SER A 152 2261 4031 2936 151 489 373 C ATOM 1205 OG SER A 152 67.194 47.864 10.892 1.00 30.65 O ANISOU 1205 OG SER A 152 4423 4323 2899 148 -104 292 O ATOM 1206 N LEU A 153 68.383 45.610 12.561 1.00 29.06 N ANISOU 1206 N LEU A 153 4048 4037 2954 -219 -370 477 N ATOM 1207 CA LEU A 153 69.119 44.429 12.103 1.00 29.26 C ANISOU 1207 CA LEU A 153 3685 3994 3440 -261 -742 284 C ATOM 1208 C LEU A 153 69.327 44.521 10.600 1.00 29.11 C ANISOU 1208 C LEU A 153 3316 4253 3491 209 -558 101 C ATOM 1209 O LEU A 153 70.027 43.703 9.999 1.00 34.08 O ANISOU 1209 O LEU A 153 4357 4097 4497 304 441 284 O ATOM 1210 CB LEU A 153 68.369 43.155 12.436 1.00 33.10 C ANISOU 1210 CB LEU A 153 3749 4053 4775 -216 131 228 C ATOM 1211 CG LEU A 153 68.733 42.384 13.711 1.00 40.02 C ANISOU 1211 CG LEU A 153 5950 5263 3992 -2329 133 679 C ATOM 1212 CD1 LEU A 153 69.343 43.266 14.783 1.00 36.67 C ANISOU 1212 CD1 LEU A 153 6870 4004 3059 -1329 1626 -51 C ATOM 1213 CD2 LEU A 153 67.516 41.650 14.268 1.00 35.55 C ANISOU 1213 CD2 LEU A 153 2763 5853 4889 200 331 967 C ATOM 1214 N ALA A 154 68.701 45.511 9.970 1.00 28.86 N ANISOU 1214 N ALA A 154 3772 3811 3384 -100 -231 365 N ATOM 1215 CA ALA A 154 68.950 45.719 8.545 1.00 30.37 C ANISOU 1215 CA ALA A 154 3746 4496 3297 -369 -386 198 C ATOM 1216 C ALA A 154 69.783 46.967 8.328 1.00 31.22 C ANISOU 1216 C ALA A 154 4347 4666 2850 -661 -348 317 C ATOM 1217 O ALA A 154 69.810 47.497 7.212 1.00 34.75 O ANISOU 1217 O ALA A 154 5023 4855 3323 -392 -1059 947 O ATOM 1218 CB ALA A 154 67.633 45.838 7.787 1.00 34.29 C ANISOU 1218 CB ALA A 154 4068 5230 3729 -356 -793 160 C ATOM 1219 N SER A 155 70.462 47.491 9.362 1.00 27.85 N ANISOU 1219 N SER A 155 3657 4121 2802 -121 7 9 N ATOM 1220 CA SER A 155 71.157 48.768 9.111 1.00 29.11 C ANISOU 1220 CA SER A 155 3680 4341 3039 -299 -34 162 C ATOM 1221 C SER A 155 72.310 48.538 8.149 1.00 31.02 C ANISOU 1221 C SER A 155 3935 4240 3611 -131 316 360 C ATOM 1222 O SER A 155 72.764 47.408 7.965 1.00 29.07 O ANISOU 1222 O SER A 155 4093 3993 2960 -410 506 489 O ATOM 1223 CB SER A 155 71.576 49.345 10.463 1.00 28.66 C ANISOU 1223 CB SER A 155 3994 4035 2860 -630 -380 718 C ATOM 1224 OG SER A 155 72.317 48.324 11.146 1.00 30.95 O ANISOU 1224 OG SER A 155 3936 4581 3242 -12 18 839 O ATOM 1225 N ARG A 156 72.816 49.580 7.497 1.00 27.27 N ANISOU 1225 N ARG A 156 3264 3955 3142 464 -1 470 N ATOM 1226 CA ARG A 156 73.836 49.491 6.462 1.00 28.27 C ANISOU 1226 CA ARG A 156 3079 4309 3353 470 18 544 C ATOM 1227 C ARG A 156 75.025 50.404 6.758 1.00 27.82 C ANISOU 1227 C ARG A 156 2907 3931 3731 789 -28 347 C ATOM 1228 O ARG A 156 74.971 51.167 7.729 1.00 31.42 O ANISOU 1228 O ARG A 156 4483 3701 3754 -136 705 427 O ATOM 1229 CB ARG A 156 73.229 49.887 5.109 1.00 30.35 C ANISOU 1229 CB ARG A 156 4010 4532 2991 289 -109 187 C ATOM 1230 CG ARG A 156 72.154 48.903 4.627 1.00 32.56 C ANISOU 1230 CG ARG A 156 4808 4586 2978 -232 -361 625 C ATOM 1231 CD ARG A 156 72.897 47.692 4.061 1.00 36.21 C ANISOU 1231 CD ARG A 156 5806 4472 3480 -146 -508 297 C ATOM 1232 NE ARG A 156 72.103 46.478 4.123 1.00 40.57 N ANISOU 1232 NE ARG A 156 6347 4722 4348 -532 -933 182 N ATOM 1233 CZ ARG A 156 72.546 45.287 3.735 1.00 40.13 C ANISOU 1233 CZ ARG A 156 5796 4720 4733 -761 -573 57 C ATOM 1234 NH1 ARG A 156 73.777 45.151 3.260 1.00 37.87 N ANISOU 1234 NH1 ARG A 156 5173 5635 3582 -493 -1594 379 N ATOM 1235 NH2 ARG A 156 71.721 44.258 3.839 1.00 40.93 N ANISOU 1235 NH2 ARG A 156 6082 4379 5092 -499 -635 1412 N ATOM 1236 N THR A 157 76.065 50.325 5.917 1.00 30.93 N ANISOU 1236 N THR A 157 3402 4458 3890 186 411 340 N ATOM 1237 CA THR A 157 77.307 51.060 6.105 1.00 31.02 C ANISOU 1237 CA THR A 157 3752 4415 3620 -155 491 575 C ATOM 1238 C THR A 157 77.017 52.543 6.249 1.00 30.19 C ANISOU 1238 C THR A 157 3483 4497 3492 48 735 555 C ATOM 1239 O THR A 157 76.230 53.075 5.454 1.00 35.36 O ANISOU 1239 O THR A 157 4388 4808 4240 93 111 919 O ATOM 1240 CB THR A 157 78.279 50.839 4.930 1.00 30.76 C ANISOU 1240 CB THR A 157 3447 4291 3950 77 433 279 C ATOM 1241 OG1 THR A 157 78.561 49.437 4.848 1.00 35.13 O ANISOU 1241 OG1 THR A 157 6169 4069 3109 -194 326 -108 O ATOM 1242 CG2 THR A 157 79.585 51.570 5.165 1.00 28.06 C ANISOU 1242 CG2 THR A 157 3457 4294 2910 150 280 74 C ATOM 1243 N ARG A 158 77.603 53.201 7.242 1.00 30.88 N ANISOU 1243 N ARG A 158 3677 4516 3538 -184 889 460 N ATOM 1244 CA ARG A 158 77.223 54.582 7.520 1.00 31.76 C ANISOU 1244 CA ARG A 158 3594 4736 3736 29 1033 278 C ATOM 1245 C ARG A 158 78.188 55.227 8.509 1.00 32.73 C ANISOU 1245 C ARG A 158 3919 4475 4043 -104 855 287 C ATOM 1246 O ARG A 158 78.974 54.547 9.149 1.00 34.08 O ANISOU 1246 O ARG A 158 4434 4672 3844 -90 510 247 O ATOM 1247 CB ARG A 158 75.798 54.657 8.083 1.00 34.38 C ANISOU 1247 CB ARG A 158 3660 5187 4217 9 1226 540 C ATOM 1248 CG ARG A 158 75.635 54.179 9.524 1.00 36.00 C ANISOU 1248 CG ARG A 158 4251 5275 4153 -123 1535 379 C ATOM 1249 CD ARG A 158 74.192 53.786 9.810 1.00 34.46 C ANISOU 1249 CD ARG A 158 4145 5227 3722 -368 735 1012 C ATOM 1250 NE ARG A 158 73.928 53.356 11.197 1.00 33.95 N ANISOU 1250 NE ARG A 158 4630 4450 3821 -159 1221 798 N ATOM 1251 CZ ARG A 158 74.159 52.107 11.608 1.00 36.78 C ANISOU 1251 CZ ARG A 158 6016 4217 3740 -394 521 541 C ATOM 1252 NH1 ARG A 158 74.653 51.242 10.717 1.00 31.31 N ANISOU 1252 NH1 ARG A 158 3855 4426 3616 -117 9 704 N ATOM 1253 NH2 ARG A 158 73.916 51.736 12.845 1.00 31.35 N ANISOU 1253 NH2 ARG A 158 3919 4507 3486 432 -249 696 N ATOM 1254 N ILE A 159 78.109 56.543 8.632 1.00 35.47 N ANISOU 1254 N ILE A 159 4542 4492 4441 -50 1111 179 N ATOM 1255 CA ILE A 159 78.938 57.268 9.573 1.00 35.07 C ANISOU 1255 CA ILE A 159 4407 4135 4782 416 896 -14 C ATOM 1256 C ILE A 159 78.253 57.244 10.945 1.00 37.45 C ANISOU 1256 C ILE A 159 4806 4741 4684 -268 875 -130 C ATOM 1257 O ILE A 159 77.022 57.290 11.004 1.00 39.31 O ANISOU 1257 O ILE A 159 4878 5013 5044 341 1309 -5 O ATOM 1258 CB ILE A 159 79.171 58.733 9.182 1.00 39.65 C ANISOU 1258 CB ILE A 159 5410 4542 5112 -294 284 485 C ATOM 1259 CG1 ILE A 159 80.248 59.405 10.040 1.00 41.71 C ANISOU 1259 CG1 ILE A 159 5362 5294 5191 -823 877 -95 C ATOM 1260 CG2 ILE A 159 77.866 59.515 9.232 1.00 38.23 C ANISOU 1260 CG2 ILE A 159 5699 3317 5509 -405 418 757 C ATOM 1261 CD1 ILE A 159 80.724 60.728 9.476 1.00 40.62 C ANISOU 1261 CD1 ILE A 159 5716 4824 4893 -491 821 -362 C ATOM 1262 N LYS A 160 79.068 57.173 11.978 1.00 40.97 N ANISOU 1262 N LYS A 160 5651 5057 4861 -739 423 378 N ATOM 1263 CA LYS A 160 78.687 57.138 13.365 1.00 43.00 C ANISOU 1263 CA LYS A 160 6809 4735 4795 -446 519 202 C ATOM 1264 C LYS A 160 79.538 58.113 14.195 1.00 44.52 C ANISOU 1264 C LYS A 160 6225 5368 5323 -675 1661 -868 C ATOM 1265 O LYS A 160 80.719 58.309 13.895 1.00 46.37 O ANISOU 1265 O LYS A 160 6438 5703 5476 -894 1992 -589 O ATOM 1266 CB LYS A 160 78.855 55.742 13.992 1.00 40.85 C ANISOU 1266 CB LYS A 160 5643 4962 4918 -153 508 397 C ATOM 1267 CG LYS A 160 77.942 54.644 13.487 1.00 43.72 C ANISOU 1267 CG LYS A 160 6473 4746 5394 -387 258 512 C ATOM 1268 CD LYS A 160 76.516 55.144 13.331 1.00 47.22 C ANISOU 1268 CD LYS A 160 5920 5840 6181 -889 443 211 C ATOM 1269 CE LYS A 160 75.661 54.759 14.518 1.00 51.24 C ANISOU 1269 CE LYS A 160 6579 6643 6247 -1400 612 143 C ATOM 1270 NZ LYS A 160 76.060 55.354 15.820 1.00 52.76 N ANISOU 1270 NZ LYS A 160 8506 5514 6026 -562 306 357 N ATOM 1271 N THR A 161 78.881 58.653 15.224 1.00 46.07 N ANISOU 1271 N THR A 161 6196 5573 5734 95 1582 -914 N ATOM 1272 CA THR A 161 79.524 59.461 16.249 1.00 50.03 C ANISOU 1272 CA THR A 161 6913 6464 5630 -308 1964 -1436 C ATOM 1273 C THR A 161 80.006 58.587 17.393 1.00 49.72 C ANISOU 1273 C THR A 161 6611 6875 5404 41 1749 -1746 C ATOM 1274 O THR A 161 79.200 57.986 18.095 1.00 51.50 O ANISOU 1274 O THR A 161 5747 7772 6050 61 770 -337 O ATOM 1275 CB THR A 161 78.544 60.503 16.808 1.00 50.46 C ANISOU 1275 CB THR A 161 6768 6590 5816 -161 1539 -1616 C ATOM 1276 OG1 THR A 161 78.042 61.276 15.708 1.00 55.20 O ANISOU 1276 OG1 THR A 161 6600 7971 6401 191 1818 -728 O ATOM 1277 CG2 THR A 161 79.249 61.459 17.756 1.00 52.69 C ANISOU 1277 CG2 THR A 161 4577 8539 6904 -166 2426 -3197 C ATOM 1278 N LEU A 162 81.304 58.461 17.602 1.00 50.34 N ANISOU 1278 N LEU A 162 6449 7256 5423 -457 1918 -1694 N ATOM 1279 CA LEU A 162 81.764 57.447 18.554 1.00 52.65 C ANISOU 1279 CA LEU A 162 6286 8091 5628 -161 1548 -1472 C ATOM 1280 C LEU A 162 81.256 57.672 19.967 1.00 52.23 C ANISOU 1280 C LEU A 162 5897 8430 5516 386 1306 -1358 C ATOM 1281 O LEU A 162 80.958 58.824 20.308 1.00 62.49 O ANISOU 1281 O LEU A 162 8039 8700 7004 -362 1496 -2942 O ATOM 1282 CB LEU A 162 83.298 57.440 18.503 1.00 53.19 C ANISOU 1282 CB LEU A 162 6314 8196 5699 -499 1777 -1522 C ATOM 1283 CG LEU A 162 83.867 57.169 17.107 1.00 52.93 C ANISOU 1283 CG LEU A 162 6606 7838 5667 13 1777 -1363 C ATOM 1284 CD1 LEU A 162 85.372 57.026 17.187 1.00 55.07 C ANISOU 1284 CD1 LEU A 162 6561 7050 7311 156 2360 -995 C ATOM 1285 CD2 LEU A 162 83.168 55.945 16.541 1.00 57.05 C ANISOU 1285 CD2 LEU A 162 8865 8972 3838 -1552 778 -482 C ATOM 1286 N THR A 163 81.141 56.636 20.802 1.00 59.10 N ANISOU 1286 N THR A 163 6302 9840 6313 -767 1535 -340 N ATOM 1287 CA THR A 163 80.708 56.877 22.184 1.00 67.97 C ANISOU 1287 CA THR A 163 8737 10769 6321 -2093 2043 -691 C ATOM 1288 C THR A 163 81.901 57.221 23.078 1.00 72.03 C ANISOU 1288 C THR A 163 9650 11375 6344 -2327 1519 -773 C ATOM 1289 O THR A 163 83.011 56.753 22.824 1.00 63.46 O ANISOU 1289 O THR A 163 9754 9523 4834 -2098 377 -773 O ATOM 1290 CB THR A 163 79.972 55.681 22.814 1.00 67.87 C ANISOU 1290 CB THR A 163 8532 10536 6719 -1473 2303 -297 C ATOM 1291 OG1 THR A 163 80.922 54.654 23.157 1.00 77.41 O ANISOU 1291 OG1 THR A 163 9711 11701 8001 -1467 -319 417 O ATOM 1292 CG2 THR A 163 78.967 55.043 21.859 1.00 61.67 C ANISOU 1292 CG2 THR A 163 6295 9323 7815 -351 2422 -293 C ATOM 1293 N HIS A 164 81.684 58.021 24.109 1.00 73.18 N ANISOU 1293 N HIS A 164 8953 11950 6903 -2104 1660 -1261 N ATOM 1294 CA HIS A 164 82.708 58.373 25.083 1.00 79.94 C ANISOU 1294 CA HIS A 164 10826 12269 7277 -2713 673 -1193 C ATOM 1295 C HIS A 164 83.459 57.131 25.548 1.00 75.86 C ANISOU 1295 C HIS A 164 10789 12290 5744 -2880 480 -1278 C ATOM 1296 O HIS A 164 84.682 57.078 25.530 1.00 68.07 O ANISOU 1296 O HIS A 164 10732 12117 3012 -3617 -310 -48 O ATOM 1297 CB HIS A 164 82.077 59.053 26.288 1.00 86.94 C ANISOU 1297 CB HIS A 164 11525 12664 8842 -3047 658 -3009 C ATOM 1298 CG HIS A 164 82.882 60.137 26.930 1.00 98.83 C ANISOU 1298 CG HIS A 164 13596 13511 10445 -4228 -13 -3227 C ATOM 1299 ND1 HIS A 164 83.673 61.020 26.218 1.00104.21 N ANISOU 1299 ND1 HIS A 164 14138 14089 11368 -5006 -781 -2512 N ATOM 1300 CD2 HIS A 164 83.010 60.483 28.240 1.00102.90 C ANISOU 1300 CD2 HIS A 164 14181 14168 10747 -4985 -1232 -3005 C ATOM 1301 CE1 HIS A 164 84.255 61.866 27.060 1.00107.01 C ANISOU 1301 CE1 HIS A 164 14524 14378 11757 -5151 -1430 -2348 C ATOM 1302 NE2 HIS A 164 83.869 61.562 28.295 1.00106.55 N ANISOU 1302 NE2 HIS A 164 14544 14352 11590 -5250 -1668 -2462 N ATOM 1303 N ASP A 165 82.703 56.110 25.940 1.00 72.18 N ANISOU 1303 N ASP A 165 9561 12182 5684 -2138 1484 -1623 N ATOM 1304 CA ASP A 165 83.320 54.832 26.291 1.00 77.60 C ANISOU 1304 CA ASP A 165 11006 12333 6146 -1786 1999 -1092 C ATOM 1305 C ASP A 165 84.253 54.331 25.201 1.00 74.61 C ANISOU 1305 C ASP A 165 9901 12590 5858 -1162 1374 -630 C ATOM 1306 O ASP A 165 85.269 53.675 25.452 1.00 76.73 O ANISOU 1306 O ASP A 165 10896 11798 6461 -813 831 -553 O ATOM 1307 CB ASP A 165 82.212 53.812 26.559 1.00 85.81 C ANISOU 1307 CB ASP A 165 12889 12470 7243 -2487 3699 -1308 C ATOM 1308 CG ASP A 165 81.297 54.304 27.670 1.00 94.21 C ANISOU 1308 CG ASP A 165 14915 12585 8295 -2725 5300 -1274 C ATOM 1309 OD1 ASP A 165 81.091 55.536 27.749 1.00108.17 O ANISOU 1309 OD1 ASP A 165 16354 12710 12037 -2263 7768 -1380 O ATOM 1310 OD2 ASP A 165 80.806 53.465 28.455 1.00 97.35 O ANISOU 1310 OD2 ASP A 165 17132 13617 6241 -2539 4483 -704 O ATOM 1311 N THR A 166 83.924 54.632 23.941 1.00 74.67 N ANISOU 1311 N THR A 166 9546 12954 5873 -1010 1398 -554 N ATOM 1312 CA THR A 166 84.799 54.151 22.873 1.00 68.60 C ANISOU 1312 CA THR A 166 7758 12833 5476 -437 336 -156 C ATOM 1313 C THR A 166 85.987 55.081 22.653 1.00 68.94 C ANISOU 1313 C THR A 166 7970 12883 5341 -542 -156 716 C ATOM 1314 O THR A 166 87.090 54.589 22.416 1.00 68.20 O ANISOU 1314 O THR A 166 7559 12731 5624 -692 -530 1061 O ATOM 1315 CB THR A 166 84.085 53.979 21.516 1.00 72.37 C ANISOU 1315 CB THR A 166 9155 12702 5639 -1043 -61 -362 C ATOM 1316 OG1 THR A 166 82.922 53.153 21.665 1.00 75.94 O ANISOU 1316 OG1 THR A 166 8668 12928 7257 -920 327 -1882 O ATOM 1317 CG2 THR A 166 85.039 53.287 20.546 1.00 74.00 C ANISOU 1317 CG2 THR A 166 9650 13247 5218 -1212 624 39 C ATOM 1318 N ARG A 167 85.772 56.393 22.713 1.00 69.78 N ANISOU 1318 N ARG A 167 8682 12889 4941 -548 562 511 N ATOM 1319 CA ARG A 167 86.926 57.275 22.538 1.00 71.95 C ANISOU 1319 CA ARG A 167 8780 12745 5814 -629 917 -407 C ATOM 1320 C ARG A 167 87.882 57.005 23.705 1.00 74.23 C ANISOU 1320 C ARG A 167 8941 13769 5493 -1343 846 -439 C ATOM 1321 O ARG A 167 89.082 56.783 23.554 1.00 78.16 O ANISOU 1321 O ARG A 167 8228 14833 6636 -2496 226 -189 O ATOM 1322 CB ARG A 167 86.573 58.750 22.493 1.00 77.63 C ANISOU 1322 CB ARG A 167 9638 12639 7221 -665 1124 -961 C ATOM 1323 CG ARG A 167 85.201 59.158 22.027 1.00 81.73 C ANISOU 1323 CG ARG A 167 10758 12178 8116 -257 -90 -165 C ATOM 1324 CD ARG A 167 85.144 59.545 20.563 1.00 87.05 C ANISOU 1324 CD ARG A 167 12778 11970 8326 -590 -56 301 C ATOM 1325 NE ARG A 167 84.548 60.830 20.251 1.00 92.77 N ANISOU 1325 NE ARG A 167 14409 11696 9144 -662 -296 517 N ATOM 1326 CZ ARG A 167 83.438 61.162 19.622 1.00 95.37 C ANISOU 1326 CZ ARG A 167 15380 11275 9580 -374 -904 1145 C ATOM 1327 NH1 ARG A 167 82.584 60.281 19.121 1.00 94.39 N ANISOU 1327 NH1 ARG A 167 15117 11435 9312 -231 -1424 1589 N ATOM 1328 NH2 ARG A 167 83.111 62.447 19.464 1.00110.50 N ANISOU 1328 NH2 ARG A 167 19973 11216 10798 -1808 -3257 4175 N ATOM 1329 N VAL A 168 87.262 57.025 24.878 1.00 80.95 N ANISOU 1329 N VAL A 168 10812 14447 5497 -2185 1339 -777 N ATOM 1330 CA VAL A 168 87.936 56.712 26.118 1.00 84.04 C ANISOU 1330 CA VAL A 168 12024 14446 5461 -2415 1114 -475 C ATOM 1331 C VAL A 168 88.758 55.441 25.982 1.00 84.40 C ANISOU 1331 C VAL A 168 12875 13943 5251 -2397 603 -261 C ATOM 1332 O VAL A 168 89.970 55.485 26.164 1.00 89.82 O ANISOU 1332 O VAL A 168 12314 15343 6472 -1740 2248 -1764 O ATOM 1333 CB VAL A 168 86.930 56.519 27.269 1.00 88.21 C ANISOU 1333 CB VAL A 168 13524 14378 5615 -3379 1719 -807 C ATOM 1334 CG1 VAL A 168 87.516 55.582 28.315 1.00 86.04 C ANISOU 1334 CG1 VAL A 168 14085 12505 6102 -3940 1902 -833 C ATOM 1335 CG2 VAL A 168 86.559 57.872 27.856 1.00 86.16 C ANISOU 1335 CG2 VAL A 168 11934 14947 5855 -1949 1013 -643 C ATOM 1336 N ALA A 169 88.112 54.333 25.658 1.00 91.57 N ANISOU 1336 N ALA A 169 15364 13755 5673 -3339 -113 804 N ATOM 1337 CA ALA A 169 88.831 53.069 25.512 1.00 95.17 C ANISOU 1337 CA ALA A 169 16049 13584 6528 -3524 1372 390 C ATOM 1338 C ALA A 169 89.746 53.012 24.292 1.00102.07 C ANISOU 1338 C ALA A 169 17256 14134 7393 -4115 2423 545 C ATOM 1339 O ALA A 169 90.382 51.992 23.991 1.00106.85 O ANISOU 1339 O ALA A 169 19119 13265 8212 -5055 4172 -586 O ATOM 1340 CB ALA A 169 87.803 51.943 25.478 1.00103.83 C ANISOU 1340 CB ALA A 169 17666 14087 7697 -4586 2652 87 C ATOM 1341 N ASN A 170 89.856 54.110 23.534 1.00106.51 N ANISOU 1341 N ASN A 170 18134 14836 7500 -4499 2029 1062 N ATOM 1342 CA ASN A 170 90.772 54.067 22.387 1.00109.84 C ANISOU 1342 CA ASN A 170 18334 15718 7681 -5454 2226 978 C ATOM 1343 C ASN A 170 91.777 55.213 22.468 1.00112.59 C ANISOU 1343 C ASN A 170 18483 15901 8396 -5599 1805 941 C ATOM 1344 O ASN A 170 92.776 55.242 21.725 1.00116.92 O ANISOU 1344 O ASN A 170 21676 16275 6474 -7495 3171 1897 O ATOM 1345 CB ASN A 170 90.001 54.087 21.067 1.00107.00 C ANISOU 1345 CB ASN A 170 17223 15854 7580 -4994 2601 690 C ATOM 1346 CG ASN A 170 89.476 52.737 20.616 1.00104.44 C ANISOU 1346 CG ASN A 170 16237 15763 7682 -4573 2828 452 C ATOM 1347 OD1 ASN A 170 89.789 51.687 21.169 1.00109.05 O ANISOU 1347 OD1 ASN A 170 16961 15826 8648 -4927 1518 639 O ATOM 1348 ND2 ASN A 170 88.635 52.728 19.577 1.00 90.72 N ANISOU 1348 ND2 ASN A 170 11283 14971 8214 -2336 4491 -806 N ATOM 1349 N SER A 171 91.561 56.163 23.375 1.00110.23 N ANISOU 1349 N SER A 171 17178 15892 8812 -4576 354 679 N ATOM 1350 CA SER A 171 92.460 57.309 23.526 1.00111.31 C ANISOU 1350 CA SER A 171 17038 15580 9674 -4280 -170 887 C ATOM 1351 C SER A 171 93.923 56.905 23.690 1.00111.01 C ANISOU 1351 C SER A 171 17047 15238 9894 -4199 -5 780 C ATOM 1352 O SER A 171 94.804 57.708 23.354 1.00115.28 O ANISOU 1352 O SER A 171 17036 16296 10469 -5295 -2437 1977 O ATOM 1353 CB SER A 171 92.033 58.181 24.715 1.00111.07 C ANISOU 1353 CB SER A 171 16913 15240 10048 -3695 -673 693 C ATOM 1354 OG SER A 171 90.928 57.634 25.421 1.00113.97 O ANISOU 1354 OG SER A 171 18978 14524 9800 -4234 653 538 O ATOM 1355 N ARG A 172 94.182 55.705 24.190 1.00110.85 N ANISOU 1355 N ARG A 172 17451 14821 9847 -3968 200 169 N ATOM 1356 CA ARG A 172 95.481 55.089 24.405 1.00111.98 C ANISOU 1356 CA ARG A 172 17665 14906 9976 -4058 -794 10 C ATOM 1357 C ARG A 172 96.278 55.020 23.110 1.00111.03 C ANISOU 1357 C ARG A 172 16172 15559 10454 -3932 -939 -262 C ATOM 1358 O ARG A 172 97.473 55.302 23.006 1.00112.06 O ANISOU 1358 O ARG A 172 16730 16836 9010 -5744 -1975 -11 O ATOM 1359 CB ARG A 172 95.335 53.688 25.003 1.00116.98 C ANISOU 1359 CB ARG A 172 19431 14785 10230 -3822 -1089 65 C ATOM 1360 CG ARG A 172 94.751 52.618 24.102 1.00128.53 C ANISOU 1360 CG ARG A 172 22686 15019 11132 -4938 -1604 -14 C ATOM 1361 CD ARG A 172 95.701 51.453 23.874 1.00133.23 C ANISOU 1361 CD ARG A 172 24043 14646 11932 -4849 -1006 -529 C ATOM 1362 NE ARG A 172 95.075 50.156 24.099 1.00140.27 N ANISOU 1362 NE ARG A 172 25830 14832 12636 -5439 -672 -487 N ATOM 1363 CZ ARG A 172 95.655 48.959 24.135 1.00142.46 C ANISOU 1363 CZ ARG A 172 26138 14766 13223 -5418 -605 -69 C ATOM 1364 NH1 ARG A 172 96.975 48.814 23.953 1.00146.19 N ANISOU 1364 NH1 ARG A 172 26094 15488 13962 -4749 -833 543 N ATOM 1365 NH2 ARG A 172 94.929 47.862 24.354 1.00148.11 N ANISOU 1365 NH2 ARG A 172 27294 15026 13955 -5942 -745 288 N ATOM 1366 N PHE A 173 95.571 54.624 22.045 1.00 99.08 N ANISOU 1366 N PHE A 173 12166 15154 10327 -1652 -98 -625 N ATOM 1367 CA PHE A 173 96.279 54.681 20.772 1.00 95.56 C ANISOU 1367 CA PHE A 173 11181 14684 10441 -1264 -294 -16 C ATOM 1368 C PHE A 173 96.501 56.131 20.411 1.00 93.43 C ANISOU 1368 C PHE A 173 10204 14403 10892 -1050 -663 -317 C ATOM 1369 O PHE A 173 97.552 56.492 19.877 1.00 90.44 O ANISOU 1369 O PHE A 173 8772 14217 11373 -1673 -2556 -482 O ATOM 1370 CB PHE A 173 95.481 53.937 19.707 1.00 90.93 C ANISOU 1370 CB PHE A 173 10884 13929 9734 -1337 138 461 C ATOM 1371 CG PHE A 173 95.098 52.557 20.235 1.00 92.38 C ANISOU 1371 CG PHE A 173 11175 14171 9755 -1241 -225 1018 C ATOM 1372 CD1 PHE A 173 95.925 51.469 20.036 1.00 91.14 C ANISOU 1372 CD1 PHE A 173 11094 14284 9251 -1076 -347 1420 C ATOM 1373 CD2 PHE A 173 93.913 52.394 20.923 1.00 91.66 C ANISOU 1373 CD2 PHE A 173 10907 13980 9941 -1040 -423 1644 C ATOM 1374 CE1 PHE A 173 95.571 50.223 20.518 1.00 91.11 C ANISOU 1374 CE1 PHE A 173 11004 14444 9172 -992 -551 1730 C ATOM 1375 CE2 PHE A 173 93.553 51.148 21.406 1.00 91.80 C ANISOU 1375 CE2 PHE A 173 10541 14096 10243 -794 -985 2187 C ATOM 1376 CZ PHE A 173 94.381 50.062 21.202 1.00 90.64 C ANISOU 1376 CZ PHE A 173 10223 14319 9898 -703 -1053 2344 C ATOM 1377 N PHE A 174 95.555 57.027 20.698 1.00 98.63 N ANISOU 1377 N PHE A 174 10789 14856 11831 -833 -369 -1379 N ATOM 1378 CA PHE A 174 95.872 58.421 20.311 1.00102.64 C ANISOU 1378 CA PHE A 174 12059 14291 12650 -629 -398 -2078 C ATOM 1379 C PHE A 174 96.686 59.045 21.438 1.00108.34 C ANISOU 1379 C PHE A 174 12786 14844 13533 -651 -1222 -2243 C ATOM 1380 O PHE A 174 96.234 59.936 22.143 1.00113.25 O ANISOU 1380 O PHE A 174 14713 14498 13819 212 -2451 -2631 O ATOM 1381 CB PHE A 174 94.602 59.179 19.948 1.00100.89 C ANISOU 1381 CB PHE A 174 12146 13993 12196 -438 -292 -2674 C ATOM 1382 CG PHE A 174 94.162 58.938 18.499 1.00101.23 C ANISOU 1382 CG PHE A 174 11869 14360 12232 -610 -257 -2760 C ATOM 1383 CD1 PHE A 174 93.639 57.711 18.126 1.00101.15 C ANISOU 1383 CD1 PHE A 174 11722 14554 12156 -813 146 -2915 C ATOM 1384 CD2 PHE A 174 94.293 59.932 17.541 1.00 99.50 C ANISOU 1384 CD2 PHE A 174 11610 14369 11828 -479 172 -2977 C ATOM 1385 CE1 PHE A 174 93.243 57.484 16.822 1.00100.80 C ANISOU 1385 CE1 PHE A 174 11514 14644 12141 -931 174 -2836 C ATOM 1386 CE2 PHE A 174 93.910 59.715 16.232 1.00 98.42 C ANISOU 1386 CE2 PHE A 174 11506 14380 11508 -655 925 -3316 C ATOM 1387 CZ PHE A 174 93.406 58.482 15.874 1.00100.40 C ANISOU 1387 CZ PHE A 174 11676 14579 11892 -1087 596 -3021 C ATOM 1388 N ASP A 175 97.894 58.527 21.539 1.00112.09 N ANISOU 1388 N ASP A 175 12995 15173 14422 -436 -1786 -1485 N ATOM 1389 CA ASP A 175 98.758 58.244 22.652 1.00115.08 C ANISOU 1389 CA ASP A 175 13761 15399 14564 -948 -2093 -893 C ATOM 1390 C ASP A 175 98.078 58.814 23.915 1.00115.71 C ANISOU 1390 C ASP A 175 14276 15528 14161 -1845 -1488 -256 C ATOM 1391 O ASP A 175 98.332 59.923 24.353 1.00101.68 O ANISOU 1391 O ASP A 175 8131 15542 14961 -499 -1721 -833 O ATOM 1392 CB ASP A 175 100.204 58.732 22.556 1.00113.42 C ANISOU 1392 CB ASP A 175 13335 15222 14536 -254 -2220 -790 C ATOM 1393 CG ASP A 175 101.208 57.633 22.919 1.00114.59 C ANISOU 1393 CG ASP A 175 14314 14779 14446 34 -1892 -751 C ATOM 1394 OD1 ASP A 175 100.775 56.487 23.212 1.00117.13 O ANISOU 1394 OD1 ASP A 175 16380 14695 13429 52 333 -1017 O ATOM 1395 OD2 ASP A 175 102.435 57.889 22.927 1.00114.39 O ANISOU 1395 OD2 ASP A 175 13894 14998 14569 1145 -918 -1667 O ATOM 1396 N ASN A 176 97.212 57.923 24.383 1.00121.11 N ANISOU 1396 N ASN A 176 16259 15316 14442 -2523 -1645 359 N ATOM 1397 CA ASN A 176 96.486 57.971 25.641 1.00119.04 C ANISOU 1397 CA ASN A 176 16189 14492 14550 -2736 -1505 839 C ATOM 1398 C ASN A 176 95.868 59.340 25.886 1.00119.68 C ANISOU 1398 C ASN A 176 16495 14491 14488 -2749 -1624 469 C ATOM 1399 O ASN A 176 95.765 59.822 27.011 1.00124.72 O ANISOU 1399 O ASN A 176 17735 14741 14911 -3286 -2318 -305 O ATOM 1400 CB ASN A 176 97.468 57.541 26.744 1.00122.57 C ANISOU 1400 CB ASN A 176 17638 13976 14957 -3487 -2272 1753 C ATOM 1401 CG ASN A 176 98.459 56.505 26.223 1.00119.83 C ANISOU 1401 CG ASN A 176 17236 13557 14738 -3318 -2834 2375 C ATOM 1402 OD1 ASN A 176 99.617 56.815 25.937 1.00112.39 O ANISOU 1402 OD1 ASN A 176 17127 13114 12463 -3026 -3341 3384 O ATOM 1403 ND2 ASN A 176 98.014 55.263 26.070 1.00118.58 N ANISOU 1403 ND2 ASN A 176 15982 13336 15738 -2785 -4764 2945 N ATOM 1404 N ASP A 177 95.446 59.947 24.787 1.00121.16 N ANISOU 1404 N ASP A 177 16699 14395 14941 -2643 -2025 583 N ATOM 1405 CA ASP A 177 94.992 61.326 24.703 1.00120.08 C ANISOU 1405 CA ASP A 177 16473 14274 14877 -2799 -2648 -20 C ATOM 1406 C ASP A 177 93.599 61.396 24.090 1.00116.88 C ANISOU 1406 C ASP A 177 16061 14590 13758 -2498 -1936 -826 C ATOM 1407 O ASP A 177 93.444 61.466 22.868 1.00116.90 O ANISOU 1407 O ASP A 177 15584 15979 12852 -4161 -1973 -6623 O ATOM 1408 CB ASP A 177 96.042 62.097 23.907 1.00123.47 C ANISOU 1408 CB ASP A 177 16783 14388 15742 -4064 -3476 197 C ATOM 1409 CG ASP A 177 95.596 63.431 23.336 1.00128.08 C ANISOU 1409 CG ASP A 177 17759 14285 16618 -4454 -4378 444 C ATOM 1410 OD1 ASP A 177 94.671 64.039 23.923 1.00128.91 O ANISOU 1410 OD1 ASP A 177 17629 14208 17141 -3845 -5296 -103 O ATOM 1411 OD2 ASP A 177 96.177 63.871 22.308 1.00134.42 O ANISOU 1411 OD2 ASP A 177 18686 14781 17606 -5619 -4369 1175 O ATOM 1412 N VAL A 178 92.586 61.371 24.952 1.00118.66 N ANISOU 1412 N VAL A 178 16676 14823 13586 -3116 -1669 -593 N ATOM 1413 CA VAL A 178 91.179 61.433 24.606 1.00114.96 C ANISOU 1413 CA VAL A 178 16440 14173 13065 -2790 -1097 -961 C ATOM 1414 C VAL A 178 90.739 62.844 24.211 1.00114.77 C ANISOU 1414 C VAL A 178 16742 13959 12908 -3083 -1201 -979 C ATOM 1415 O VAL A 178 89.916 63.452 24.901 1.00114.89 O ANISOU 1415 O VAL A 178 16482 13515 13656 -3279 -892 -779 O ATOM 1416 CB VAL A 178 90.297 60.970 25.788 1.00114.12 C ANISOU 1416 CB VAL A 178 16879 14133 12349 -2691 -1395 -955 C ATOM 1417 CG1 VAL A 178 89.296 59.910 25.360 1.00100.42 C ANISOU 1417 CG1 VAL A 178 16419 12787 8949 -1649 -3 -1912 C ATOM 1418 CG2 VAL A 178 91.185 60.455 26.927 1.00108.95 C ANISOU 1418 CG2 VAL A 178 14263 13668 13463 -2327 -635 -648 C ATOM 1419 N ASN A 179 91.279 63.355 23.114 1.00116.58 N ANISOU 1419 N ASN A 179 17945 13795 12556 -3598 -1127 -1455 N ATOM 1420 CA ASN A 179 90.963 64.662 22.556 1.00116.97 C ANISOU 1420 CA ASN A 179 19049 13285 12108 -3906 -966 -1844 C ATOM 1421 C ASN A 179 91.302 64.687 21.061 1.00115.42 C ANISOU 1421 C ASN A 179 18661 12859 12334 -4366 -546 -1960 C ATOM 1422 O ASN A 179 90.842 65.548 20.322 1.00111.17 O ANISOU 1422 O ASN A 179 18670 11973 11594 -4270 -82 -2598 O ATOM 1423 CB ASN A 179 91.733 65.786 23.249 1.00126.19 C ANISOU 1423 CB ASN A 179 20612 14193 13140 -4450 -586 -3101 C ATOM 1424 CG ASN A 179 91.048 66.346 24.480 1.00133.83 C ANISOU 1424 CG ASN A 179 21547 15588 13714 -4664 -1 -3782 C ATOM 1425 OD1 ASN A 179 89.872 66.725 24.449 1.00141.47 O ANISOU 1425 OD1 ASN A 179 22131 16168 15453 -3717 104 -5270 O ATOM 1426 ND2 ASN A 179 91.783 66.411 25.588 1.00140.96 N ANISOU 1426 ND2 ASN A 179 22307 17586 13667 -5567 -254 -4832 N ATOM 1427 N GLN A 180 92.121 63.715 20.695 1.00113.09 N ANISOU 1427 N GLN A 180 18065 12522 12383 -4550 -539 -1364 N ATOM 1428 CA GLN A 180 92.619 63.521 19.345 1.00111.28 C ANISOU 1428 CA GLN A 180 17368 12221 12694 -4603 -233 -1241 C ATOM 1429 C GLN A 180 91.906 62.368 18.637 1.00107.47 C ANISOU 1429 C GLN A 180 16498 11752 12582 -4276 637 -1433 C ATOM 1430 O GLN A 180 91.761 62.399 17.414 1.00110.04 O ANISOU 1430 O GLN A 180 17836 11203 12770 -6924 -34 -201 O ATOM 1431 CB GLN A 180 94.132 63.269 19.373 1.00115.85 C ANISOU 1431 CB GLN A 180 17179 13290 13550 -5064 -396 -286 C ATOM 1432 CG GLN A 180 94.909 64.225 18.473 1.00120.97 C ANISOU 1432 CG GLN A 180 17873 13992 14097 -4886 274 156 C ATOM 1433 CD GLN A 180 94.016 64.879 17.424 1.00126.63 C ANISOU 1433 CD GLN A 180 19208 14437 14468 -4872 -191 735 C ATOM 1434 OE1 GLN A 180 93.817 64.332 16.340 1.00134.88 O ANISOU 1434 OE1 GLN A 180 21173 16732 13344 -5194 390 1458 O ATOM 1435 NE2 GLN A 180 93.465 66.045 17.750 1.00134.37 N ANISOU 1435 NE2 GLN A 180 20493 13494 17068 -4682 -570 1136 N ATOM 1436 N VAL A 181 91.488 61.393 19.438 1.00 91.41 N ANISOU 1436 N VAL A 181 12209 11447 11077 -2514 -691 -1245 N ATOM 1437 CA VAL A 181 90.629 60.294 19.007 1.00 87.48 C ANISOU 1437 CA VAL A 181 12009 11197 10032 -2443 244 -1415 C ATOM 1438 C VAL A 181 89.538 60.838 18.087 1.00 80.41 C ANISOU 1438 C VAL A 181 10823 10634 9095 -1836 1155 -2706 C ATOM 1439 O VAL A 181 88.761 61.671 18.566 1.00 92.19 O ANISOU 1439 O VAL A 181 11677 11840 11511 -1460 997 -4631 O ATOM 1440 CB VAL A 181 89.975 59.575 20.203 1.00 90.28 C ANISOU 1440 CB VAL A 181 12256 11761 10287 -2070 945 -1371 C ATOM 1441 CG1 VAL A 181 89.408 58.221 19.779 1.00 79.58 C ANISOU 1441 CG1 VAL A 181 8542 12793 8903 -2166 3719 -2698 C ATOM 1442 CG2 VAL A 181 90.966 59.443 21.354 1.00 90.23 C ANISOU 1442 CG2 VAL A 181 13190 11625 9469 -2396 839 -1705 C ATOM 1443 N PRO A 182 89.479 60.414 16.838 1.00 78.75 N ANISOU 1443 N PRO A 182 10355 10446 9119 -2988 1354 -2686 N ATOM 1444 CA PRO A 182 88.559 61.026 15.859 1.00 76.52 C ANISOU 1444 CA PRO A 182 10676 9754 8644 -3288 1639 -2374 C ATOM 1445 C PRO A 182 87.138 61.025 16.396 1.00 71.68 C ANISOU 1445 C PRO A 182 10376 9002 7857 -3382 1082 -2873 C ATOM 1446 O PRO A 182 86.774 60.167 17.209 1.00 66.00 O ANISOU 1446 O PRO A 182 9654 8907 6513 -1321 1615 -2978 O ATOM 1447 CB PRO A 182 88.721 60.114 14.642 1.00 75.44 C ANISOU 1447 CB PRO A 182 10308 9585 8770 -2867 1719 -2322 C ATOM 1448 CG PRO A 182 90.101 59.554 14.774 1.00 76.20 C ANISOU 1448 CG PRO A 182 10118 9995 8838 -3110 1344 -2279 C ATOM 1449 CD PRO A 182 90.253 59.312 16.256 1.00 76.74 C ANISOU 1449 CD PRO A 182 10206 10234 8719 -3262 1277 -2719 C ATOM 1450 N LYS A 183 86.302 61.987 16.021 1.00 66.25 N ANISOU 1450 N LYS A 183 10340 8136 6695 -4050 1488 -2470 N ATOM 1451 CA LYS A 183 84.992 62.008 16.668 1.00 67.52 C ANISOU 1451 CA LYS A 183 10571 8502 6581 -3366 1692 -1915 C ATOM 1452 C LYS A 183 84.052 61.008 16.007 1.00 61.25 C ANISOU 1452 C LYS A 183 9080 8020 6172 -2590 2056 -1793 C ATOM 1453 O LYS A 183 83.104 60.535 16.630 1.00 62.32 O ANISOU 1453 O LYS A 183 8010 8614 7056 -1762 3204 -3628 O ATOM 1454 CB LYS A 183 84.380 63.405 16.621 1.00 75.36 C ANISOU 1454 CB LYS A 183 12471 8389 7774 -2993 2715 -2713 C ATOM 1455 CG LYS A 183 84.807 64.254 17.819 1.00 84.45 C ANISOU 1455 CG LYS A 183 14227 9329 8531 -2830 1521 -3164 C ATOM 1456 CD LYS A 183 86.057 63.688 18.472 1.00 95.52 C ANISOU 1456 CD LYS A 183 15282 11438 9573 -3046 265 -1703 C ATOM 1457 CE LYS A 183 86.012 63.729 19.991 1.00101.86 C ANISOU 1457 CE LYS A 183 16632 12453 9618 -3588 396 -1398 C ATOM 1458 NZ LYS A 183 87.005 62.787 20.593 1.00102.56 N ANISOU 1458 NZ LYS A 183 16349 13890 8727 -3036 990 -1168 N ATOM 1459 N TYR A 184 84.341 60.709 14.746 1.00 51.83 N ANISOU 1459 N TYR A 184 7385 6107 6202 -1451 1991 -1376 N ATOM 1460 CA TYR A 184 83.439 59.906 13.945 1.00 55.27 C ANISOU 1460 CA TYR A 184 8249 6086 6665 -1439 1539 -1697 C ATOM 1461 C TYR A 184 84.158 58.737 13.276 1.00 50.14 C ANISOU 1461 C TYR A 184 7486 5664 5900 -936 511 -893 C ATOM 1462 O TYR A 184 85.381 58.722 13.125 1.00 48.87 O ANISOU 1462 O TYR A 184 7286 5065 6217 -912 -386 -628 O ATOM 1463 CB TYR A 184 82.790 60.730 12.838 1.00 53.58 C ANISOU 1463 CB TYR A 184 6222 6312 7825 -223 1467 -2105 C ATOM 1464 CG TYR A 184 82.090 61.992 13.261 1.00 65.46 C ANISOU 1464 CG TYR A 184 7173 6790 10910 -60 1811 -3275 C ATOM 1465 CD1 TYR A 184 80.708 62.113 13.178 1.00 67.60 C ANISOU 1465 CD1 TYR A 184 6973 7049 11662 58 3033 -3556 C ATOM 1466 CD2 TYR A 184 82.816 63.082 13.732 1.00 73.31 C ANISOU 1466 CD2 TYR A 184 8066 7074 12715 -474 2087 -4017 C ATOM 1467 CE1 TYR A 184 80.066 63.277 13.563 1.00 72.07 C ANISOU 1467 CE1 TYR A 184 7801 7118 12467 126 3804 -3699 C ATOM 1468 CE2 TYR A 184 82.192 64.249 14.125 1.00 77.62 C ANISOU 1468 CE2 TYR A 184 8961 6918 13614 -526 2886 -4002 C ATOM 1469 CZ TYR A 184 80.819 64.336 14.035 1.00 77.23 C ANISOU 1469 CZ TYR A 184 8779 7214 13351 -254 4043 -4133 C ATOM 1470 OH TYR A 184 80.207 65.507 14.422 1.00 81.19 O ANISOU 1470 OH TYR A 184 9978 6232 14639 -89 4148 -3058 O ATOM 1471 N ALA A 185 83.347 57.761 12.865 1.00 44.28 N ANISOU 1471 N ALA A 185 6583 5134 5106 -446 559 -397 N ATOM 1472 CA ALA A 185 83.877 56.599 12.164 1.00 41.54 C ANISOU 1472 CA ALA A 185 6004 5031 4749 -416 508 -104 C ATOM 1473 C ALA A 185 82.888 56.142 11.101 1.00 39.24 C ANISOU 1473 C ALA A 185 5740 4871 4300 -717 912 133 C ATOM 1474 O ALA A 185 81.705 56.432 11.257 1.00 40.15 O ANISOU 1474 O ALA A 185 5793 5070 4394 -630 878 -475 O ATOM 1475 CB ALA A 185 84.154 55.449 13.115 1.00 40.34 C ANISOU 1475 CB ALA A 185 5188 5388 4751 -438 771 151 C ATOM 1476 N LEU A 186 83.418 55.455 10.106 1.00 37.19 N ANISOU 1476 N LEU A 186 5393 4789 3950 -862 1160 535 N ATOM 1477 CA LEU A 186 82.570 54.767 9.130 1.00 35.06 C ANISOU 1477 CA LEU A 186 4702 4519 4100 -214 1223 282 C ATOM 1478 C LEU A 186 82.454 53.309 9.579 1.00 33.86 C ANISOU 1478 C LEU A 186 4382 4655 3830 -287 401 524 C ATOM 1479 O LEU A 186 83.489 52.759 9.978 1.00 34.53 O ANISOU 1479 O LEU A 186 4199 5283 3639 -774 52 1064 O ATOM 1480 CB LEU A 186 83.132 54.839 7.720 1.00 36.12 C ANISOU 1480 CB LEU A 186 4452 5494 3779 94 711 865 C ATOM 1481 CG LEU A 186 82.603 55.960 6.830 1.00 39.23 C ANISOU 1481 CG LEU A 186 6353 4183 4371 259 794 461 C ATOM 1482 CD1 LEU A 186 82.232 57.157 7.673 1.00 42.75 C ANISOU 1482 CD1 LEU A 186 9437 3566 3240 -1441 -472 -47 C ATOM 1483 CD2 LEU A 186 83.605 56.317 5.729 1.00 40.18 C ANISOU 1483 CD2 LEU A 186 6145 4354 4767 -1365 226 1002 C ATOM 1484 N THR A 187 81.267 52.711 9.530 1.00 30.92 N ANISOU 1484 N THR A 187 4133 4155 3461 94 150 309 N ATOM 1485 CA THR A 187 81.160 51.311 9.950 1.00 32.43 C ANISOU 1485 CA THR A 187 4606 4346 3371 -190 -100 590 C ATOM 1486 C THR A 187 80.193 50.532 9.095 1.00 30.01 C ANISOU 1486 C THR A 187 4081 4157 3164 -36 197 666 C ATOM 1487 O THR A 187 79.145 51.052 8.683 1.00 30.48 O ANISOU 1487 O THR A 187 3846 4335 3400 -14 462 717 O ATOM 1488 CB THR A 187 80.697 51.255 11.421 1.00 33.44 C ANISOU 1488 CB THR A 187 4926 4319 3459 -409 73 284 C ATOM 1489 OG1 THR A 187 80.599 49.903 11.896 1.00 37.26 O ANISOU 1489 OG1 THR A 187 6156 4383 3620 301 1094 527 O ATOM 1490 CG2 THR A 187 79.303 51.880 11.585 1.00 33.76 C ANISOU 1490 CG2 THR A 187 5268 4475 3086 12 -123 -62 C ATOM 1491 N VAL A 188 80.473 49.268 8.801 1.00 28.57 N ANISOU 1491 N VAL A 188 3740 4203 2911 -94 603 608 N ATOM 1492 CA VAL A 188 79.415 48.485 8.164 1.00 29.31 C ANISOU 1492 CA VAL A 188 3735 4253 3147 34 387 510 C ATOM 1493 C VAL A 188 78.212 48.374 9.090 1.00 30.26 C ANISOU 1493 C VAL A 188 3591 4490 3416 -170 473 -521 C ATOM 1494 O VAL A 188 78.311 48.543 10.320 1.00 29.19 O ANISOU 1494 O VAL A 188 3485 4361 3245 -525 366 186 O ATOM 1495 CB VAL A 188 79.901 47.065 7.822 1.00 29.17 C ANISOU 1495 CB VAL A 188 4038 4367 2679 -104 1059 342 C ATOM 1496 CG1 VAL A 188 81.060 47.137 6.831 1.00 31.08 C ANISOU 1496 CG1 VAL A 188 3683 4932 3194 -158 1065 776 C ATOM 1497 CG2 VAL A 188 80.308 46.320 9.090 1.00 28.12 C ANISOU 1497 CG2 VAL A 188 3455 4019 3209 -169 1025 629 C ATOM 1498 N GLY A 189 77.056 48.079 8.499 1.00 28.38 N ANISOU 1498 N GLY A 189 3717 3841 3224 -117 155 384 N ATOM 1499 CA GLY A 189 75.853 47.938 9.300 1.00 28.02 C ANISOU 1499 CA GLY A 189 3469 4112 3066 46 -121 769 C ATOM 1500 C GLY A 189 75.591 46.533 9.801 1.00 27.71 C ANISOU 1500 C GLY A 189 3463 3891 3172 18 212 417 C ATOM 1501 O GLY A 189 76.309 45.593 9.425 1.00 27.45 O ANISOU 1501 O GLY A 189 3160 3989 3282 -145 31 50 O ATOM 1502 N VAL A 190 74.565 46.385 10.637 1.00 26.82 N ANISOU 1502 N VAL A 190 3465 3926 2798 112 107 420 N ATOM 1503 CA VAL A 190 74.253 45.044 11.142 1.00 26.93 C ANISOU 1503 CA VAL A 190 3389 4048 2796 131 90 577 C ATOM 1504 C VAL A 190 73.752 44.162 10.013 1.00 28.09 C ANISOU 1504 C VAL A 190 3785 3971 2918 -213 119 637 C ATOM 1505 O VAL A 190 74.049 42.971 9.936 1.00 30.94 O ANISOU 1505 O VAL A 190 4716 3911 3129 -189 60 682 O ATOM 1506 CB VAL A 190 73.221 45.092 12.284 1.00 26.99 C ANISOU 1506 CB VAL A 190 3112 3553 3590 -134 386 136 C ATOM 1507 CG1 VAL A 190 72.888 43.686 12.789 1.00 25.38 C ANISOU 1507 CG1 VAL A 190 2744 3342 3558 112 575 -44 C ATOM 1508 CG2 VAL A 190 73.713 45.956 13.444 1.00 27.32 C ANISOU 1508 CG2 VAL A 190 4403 2881 3095 133 365 484 C ATOM 1509 N GLY A 191 72.977 44.736 9.099 1.00 28.27 N ANISOU 1509 N GLY A 191 3208 4106 3427 -304 -227 355 N ATOM 1510 CA GLY A 191 72.476 44.060 7.904 1.00 28.37 C ANISOU 1510 CA GLY A 191 3342 3994 3444 -476 -138 303 C ATOM 1511 C GLY A 191 73.640 43.629 7.028 1.00 28.92 C ANISOU 1511 C GLY A 191 3516 4195 3278 -472 -45 463 C ATOM 1512 O GLY A 191 73.666 42.535 6.459 1.00 30.95 O ANISOU 1512 O GLY A 191 3779 4123 3859 -480 519 391 O ATOM 1513 N THR A 192 74.637 44.508 6.917 1.00 29.18 N ANISOU 1513 N THR A 192 3439 4502 3147 -591 -134 402 N ATOM 1514 CA THR A 192 75.843 44.170 6.161 1.00 29.81 C ANISOU 1514 CA THR A 192 3857 4395 3073 -556 226 626 C ATOM 1515 C THR A 192 76.469 42.891 6.706 1.00 29.87 C ANISOU 1515 C THR A 192 4123 4135 3090 -435 71 136 C ATOM 1516 O THR A 192 76.852 41.965 5.992 1.00 30.88 O ANISOU 1516 O THR A 192 3359 4959 3417 -200 564 -87 O ATOM 1517 CB THR A 192 76.883 45.299 6.261 1.00 30.46 C ANISOU 1517 CB THR A 192 3949 4135 3491 -437 1053 19 C ATOM 1518 OG1 THR A 192 76.214 46.563 6.176 1.00 30.94 O ANISOU 1518 OG1 THR A 192 4233 4289 3235 -315 469 522 O ATOM 1519 CG2 THR A 192 77.877 45.228 5.106 1.00 28.56 C ANISOU 1519 CG2 THR A 192 3804 4881 2167 -406 239 587 C ATOM 1520 N LEU A 193 76.583 42.839 8.041 1.00 29.30 N ANISOU 1520 N LEU A 193 3907 4130 3097 -445 -282 243 N ATOM 1521 CA LEU A 193 77.164 41.648 8.666 1.00 28.61 C ANISOU 1521 CA LEU A 193 3432 4212 3224 9 467 216 C ATOM 1522 C LEU A 193 76.249 40.452 8.467 1.00 28.75 C ANISOU 1522 C LEU A 193 3528 4125 3272 31 128 531 C ATOM 1523 O LEU A 193 76.735 39.376 8.094 1.00 29.30 O ANISOU 1523 O LEU A 193 4126 4214 2793 -10 282 293 O ATOM 1524 CB LEU A 193 77.360 41.932 10.133 1.00 31.34 C ANISOU 1524 CB LEU A 193 4114 4565 3228 132 -171 407 C ATOM 1525 CG LEU A 193 78.223 41.162 11.109 1.00 35.04 C ANISOU 1525 CG LEU A 193 5419 4216 3677 812 52 819 C ATOM 1526 CD1 LEU A 193 77.354 40.380 12.104 1.00 39.91 C ANISOU 1526 CD1 LEU A 193 4504 3781 6878 259 -509 2372 C ATOM 1527 CD2 LEU A 193 79.226 40.229 10.453 1.00 40.58 C ANISOU 1527 CD2 LEU A 193 7843 3165 4409 1560 41 377 C ATOM 1528 N LEU A 194 74.946 40.627 8.726 1.00 28.35 N ANISOU 1528 N LEU A 194 3406 4654 2710 -78 -153 487 N ATOM 1529 CA LEU A 194 74.056 39.466 8.657 1.00 29.18 C ANISOU 1529 CA LEU A 194 3512 4386 3188 42 788 217 C ATOM 1530 C LEU A 194 73.919 38.910 7.255 1.00 27.64 C ANISOU 1530 C LEU A 194 3308 3882 3311 13 459 277 C ATOM 1531 O LEU A 194 73.572 37.740 7.044 1.00 32.48 O ANISOU 1531 O LEU A 194 4441 4208 3691 -751 230 449 O ATOM 1532 CB LEU A 194 72.663 39.835 9.203 1.00 30.39 C ANISOU 1532 CB LEU A 194 3416 4337 3793 268 610 -13 C ATOM 1533 CG LEU A 194 72.629 39.998 10.732 1.00 32.67 C ANISOU 1533 CG LEU A 194 4476 4134 3803 244 1480 184 C ATOM 1534 CD1 LEU A 194 71.266 40.477 11.219 1.00 33.19 C ANISOU 1534 CD1 LEU A 194 3856 4679 4076 -249 1257 200 C ATOM 1535 CD2 LEU A 194 73.033 38.691 11.403 1.00 37.87 C ANISOU 1535 CD2 LEU A 194 5689 4563 4135 478 209 271 C ATOM 1536 N ASP A 195 74.167 39.720 6.238 1.00 30.12 N ANISOU 1536 N ASP A 195 4211 4072 3163 -662 590 131 N ATOM 1537 CA ASP A 195 74.110 39.205 4.882 1.00 29.64 C ANISOU 1537 CA ASP A 195 4302 3758 3203 98 -79 213 C ATOM 1538 C ASP A 195 75.264 38.253 4.589 1.00 29.57 C ANISOU 1538 C ASP A 195 4117 3778 3340 -45 -78 100 C ATOM 1539 O ASP A 195 75.234 37.574 3.549 1.00 32.41 O ANISOU 1539 O ASP A 195 4205 4517 3592 -211 318 -376 O ATOM 1540 CB ASP A 195 74.208 40.356 3.870 1.00 32.84 C ANISOU 1540 CB ASP A 195 4666 4408 3404 87 -719 714 C ATOM 1541 CG ASP A 195 72.921 41.118 3.713 1.00 36.78 C ANISOU 1541 CG ASP A 195 5311 4142 4521 658 -307 529 C ATOM 1542 OD1 ASP A 195 71.909 40.619 4.246 1.00 41.73 O ANISOU 1542 OD1 ASP A 195 4379 5412 6064 -338 -1138 -93 O ATOM 1543 OD2 ASP A 195 72.950 42.181 3.066 1.00 46.56 O ANISOU 1543 OD2 ASP A 195 7158 4576 5955 488 -1854 1342 O ATOM 1544 N ALA A 196 76.289 38.181 5.432 1.00 29.67 N ANISOU 1544 N ALA A 196 3714 4500 3058 -289 263 755 N ATOM 1545 CA ALA A 196 77.369 37.225 5.120 1.00 27.17 C ANISOU 1545 CA ALA A 196 3566 4341 2418 -493 286 664 C ATOM 1546 C ALA A 196 76.873 35.788 5.217 1.00 28.00 C ANISOU 1546 C ALA A 196 3307 4465 2866 -680 569 151 C ATOM 1547 O ALA A 196 75.912 35.483 5.925 1.00 28.87 O ANISOU 1547 O ALA A 196 3380 4911 2678 -817 407 523 O ATOM 1548 CB ALA A 196 78.532 37.419 6.057 1.00 26.85 C ANISOU 1548 CB ALA A 196 3786 3619 2796 -451 4 594 C ATOM 1549 N GLU A 197 77.504 34.877 4.506 1.00 27.17 N ANISOU 1549 N GLU A 197 3167 4506 2651 43 -131 398 N ATOM 1550 CA GLU A 197 77.138 33.476 4.475 1.00 30.24 C ANISOU 1550 CA GLU A 197 3681 4448 3362 63 432 377 C ATOM 1551 C GLU A 197 77.402 32.819 5.821 1.00 30.02 C ANISOU 1551 C GLU A 197 3932 4152 3320 -495 120 257 C ATOM 1552 O GLU A 197 76.644 31.955 6.269 1.00 29.71 O ANISOU 1552 O GLU A 197 3706 5116 2466 -914 330 -139 O ATOM 1553 CB GLU A 197 77.976 32.767 3.410 1.00 40.52 C ANISOU 1553 CB GLU A 197 6248 5074 4074 -980 1874 -674 C ATOM 1554 CG GLU A 197 77.428 31.434 2.949 1.00 60.69 C ANISOU 1554 CG GLU A 197 10960 5871 6230 -2159 2147 -1972 C ATOM 1555 CD GLU A 197 78.123 30.910 1.705 1.00 66.66 C ANISOU 1555 CD GLU A 197 12361 6294 6674 -1720 2370 -2598 C ATOM 1556 OE1 GLU A 197 78.087 31.620 0.668 1.00 68.95 O ANISOU 1556 OE1 GLU A 197 12681 6424 7091 -1696 3962 -2134 O ATOM 1557 OE2 GLU A 197 78.694 29.795 1.783 1.00 72.08 O ANISOU 1557 OE2 GLU A 197 12903 7065 7420 -834 2072 -2632 O ATOM 1558 N GLU A 198 78.493 33.204 6.462 1.00 29.40 N ANISOU 1558 N GLU A 198 4080 4111 2979 -884 400 26 N ATOM 1559 CA GLU A 198 78.884 32.680 7.773 1.00 29.14 C ANISOU 1559 CA GLU A 198 3686 4407 2976 -596 412 4 C ATOM 1560 C GLU A 198 79.470 33.825 8.587 1.00 30.64 C ANISOU 1560 C GLU A 198 3990 4706 2945 -952 421 17 C ATOM 1561 O GLU A 198 80.182 34.674 8.024 1.00 26.56 O ANISOU 1561 O GLU A 198 3260 4014 2819 -140 508 -1 O ATOM 1562 CB GLU A 198 79.879 31.537 7.610 1.00 29.18 C ANISOU 1562 CB GLU A 198 3211 4607 3268 -706 933 303 C ATOM 1563 CG GLU A 198 80.375 30.917 8.918 1.00 32.96 C ANISOU 1563 CG GLU A 198 3877 4954 3691 -308 357 332 C ATOM 1564 CD GLU A 198 81.225 29.690 8.634 1.00 36.62 C ANISOU 1564 CD GLU A 198 5000 4709 4204 -89 1011 746 C ATOM 1565 OE1 GLU A 198 82.012 29.725 7.664 1.00 36.61 O ANISOU 1565 OE1 GLU A 198 5321 4283 4307 -280 1223 248 O ATOM 1566 OE2 GLU A 198 81.131 28.669 9.352 1.00 43.85 O ANISOU 1566 OE2 GLU A 198 7564 4664 4432 -101 1557 743 O ATOM 1567 N VAL A 199 79.157 33.869 9.876 1.00 28.01 N ANISOU 1567 N VAL A 199 3735 3995 2911 -590 355 193 N ATOM 1568 CA VAL A 199 79.634 34.921 10.764 1.00 28.79 C ANISOU 1568 CA VAL A 199 4099 3913 2926 -422 35 243 C ATOM 1569 C VAL A 199 80.401 34.258 11.900 1.00 26.71 C ANISOU 1569 C VAL A 199 3439 3620 3092 -347 251 296 C ATOM 1570 O VAL A 199 79.833 33.367 12.558 1.00 28.14 O ANISOU 1570 O VAL A 199 3635 4215 2844 -635 380 363 O ATOM 1571 CB VAL A 199 78.481 35.753 11.342 1.00 26.90 C ANISOU 1571 CB VAL A 199 3876 3732 2611 -293 -478 289 C ATOM 1572 CG1 VAL A 199 78.981 36.774 12.349 1.00 26.66 C ANISOU 1572 CG1 VAL A 199 4317 4077 1737 -515 -252 492 C ATOM 1573 CG2 VAL A 199 77.747 36.467 10.224 1.00 26.84 C ANISOU 1573 CG2 VAL A 199 3784 4224 2189 -724 -423 415 C ATOM 1574 N MET A 200 81.639 34.672 12.113 1.00 25.82 N ANISOU 1574 N MET A 200 3405 3339 3067 -293 498 -199 N ATOM 1575 CA MET A 200 82.445 34.094 13.193 1.00 26.13 C ANISOU 1575 CA MET A 200 3086 3834 3009 -311 524 -191 C ATOM 1576 C MET A 200 82.878 35.210 14.133 1.00 26.51 C ANISOU 1576 C MET A 200 3359 3860 2853 -621 688 -45 C ATOM 1577 O MET A 200 83.614 36.124 13.731 1.00 26.60 O ANISOU 1577 O MET A 200 3277 3787 3044 -483 920 -67 O ATOM 1578 CB MET A 200 83.651 33.335 12.620 1.00 25.55 C ANISOU 1578 CB MET A 200 3154 3628 2926 -420 893 307 C ATOM 1579 CG MET A 200 84.632 32.810 13.667 1.00 27.01 C ANISOU 1579 CG MET A 200 3214 3595 3455 -318 604 244 C ATOM 1580 SD MET A 200 85.904 31.745 12.964 1.00 28.73 S ANISOU 1580 SD MET A 200 3551 3918 3448 -104 689 149 S ATOM 1581 CE MET A 200 86.883 32.923 12.016 1.00 26.69 C ANISOU 1581 CE MET A 200 2874 4794 2472 -335 27 342 C ATOM 1582 N ILE A 201 82.411 35.159 15.388 1.00 23.46 N ANISOU 1582 N ILE A 201 2655 3502 2756 -211 435 140 N ATOM 1583 CA ILE A 201 82.696 36.208 16.349 1.00 24.79 C ANISOU 1583 CA ILE A 201 3173 3587 2659 -135 141 166 C ATOM 1584 C ILE A 201 83.729 35.707 17.351 1.00 26.52 C ANISOU 1584 C ILE A 201 3302 3637 3138 -120 -129 255 C ATOM 1585 O ILE A 201 83.548 34.633 17.931 1.00 27.81 O ANISOU 1585 O ILE A 201 4090 3835 2643 -342 -290 292 O ATOM 1586 CB ILE A 201 81.427 36.641 17.097 1.00 27.24 C ANISOU 1586 CB ILE A 201 3374 3618 3356 163 152 -363 C ATOM 1587 CG1 ILE A 201 80.306 37.030 16.123 1.00 27.24 C ANISOU 1587 CG1 ILE A 201 3081 3946 3322 -139 251 -186 C ATOM 1588 CG2 ILE A 201 81.744 37.754 18.088 1.00 25.31 C ANISOU 1588 CG2 ILE A 201 3326 3157 3136 -130 215 74 C ATOM 1589 CD1 ILE A 201 80.665 38.295 15.350 1.00 28.28 C ANISOU 1589 CD1 ILE A 201 3584 4313 2850 -494 -85 -87 C ATOM 1590 N LEU A 202 84.777 36.489 17.509 1.00 26.31 N ANISOU 1590 N LEU A 202 3092 3731 3174 -22 64 -128 N ATOM 1591 CA LEU A 202 85.835 36.224 18.459 1.00 26.30 C ANISOU 1591 CA LEU A 202 3483 3728 2784 -398 -43 153 C ATOM 1592 C LEU A 202 85.438 36.839 19.804 1.00 27.46 C ANISOU 1592 C LEU A 202 3413 4048 2970 -16 191 179 C ATOM 1593 O LEU A 202 85.148 38.039 19.863 1.00 28.40 O ANISOU 1593 O LEU A 202 3715 3947 3129 -232 511 123 O ATOM 1594 CB LEU A 202 87.149 36.844 18.019 1.00 27.98 C ANISOU 1594 CB LEU A 202 3026 4205 3402 -8 200 67 C ATOM 1595 CG LEU A 202 88.120 36.122 17.089 1.00 32.57 C ANISOU 1595 CG LEU A 202 4884 4340 3151 -665 1223 -340 C ATOM 1596 CD1 LEU A 202 87.470 35.010 16.302 1.00 29.03 C ANISOU 1596 CD1 LEU A 202 4459 5402 1168 -774 316 322 C ATOM 1597 CD2 LEU A 202 88.804 37.123 16.174 1.00 28.96 C ANISOU 1597 CD2 LEU A 202 4928 4324 1753 -81 81 254 C ATOM 1598 N VAL A 203 85.457 36.022 20.845 1.00 27.08 N ANISOU 1598 N VAL A 203 3379 4070 2841 -319 158 136 N ATOM 1599 CA VAL A 203 85.060 36.531 22.156 1.00 28.32 C ANISOU 1599 CA VAL A 203 3361 4483 2917 -368 193 -54 C ATOM 1600 C VAL A 203 86.151 36.291 23.208 1.00 28.11 C ANISOU 1600 C VAL A 203 3351 4416 2913 -207 204 -341 C ATOM 1601 O VAL A 203 86.353 35.132 23.600 1.00 31.28 O ANISOU 1601 O VAL A 203 4296 4820 2771 -986 -232 601 O ATOM 1602 CB VAL A 203 83.737 35.878 22.598 1.00 31.03 C ANISOU 1602 CB VAL A 203 3660 5547 2583 -1005 156 -265 C ATOM 1603 CG1 VAL A 203 83.233 36.570 23.887 1.00 27.47 C ANISOU 1603 CG1 VAL A 203 3351 4595 2491 -504 -35 175 C ATOM 1604 CG2 VAL A 203 82.662 35.897 21.515 1.00 29.06 C ANISOU 1604 CG2 VAL A 203 3679 5007 2355 -1074 283 118 C ATOM 1605 N LEU A 204 86.833 37.357 23.641 1.00 30.58 N ANISOU 1605 N LEU A 204 3955 4885 2778 -1079 110 214 N ATOM 1606 CA LEU A 204 87.963 37.300 24.546 1.00 30.91 C ANISOU 1606 CA LEU A 204 3857 4859 3028 -978 77 43 C ATOM 1607 C LEU A 204 87.772 38.165 25.781 1.00 29.57 C ANISOU 1607 C LEU A 204 3398 4788 3048 -201 -283 88 C ATOM 1608 O LEU A 204 87.451 39.347 25.675 1.00 31.99 O ANISOU 1608 O LEU A 204 4527 4559 3069 -551 -246 384 O ATOM 1609 CB LEU A 204 89.241 37.779 23.838 1.00 31.23 C ANISOU 1609 CB LEU A 204 3744 4804 3316 -564 188 378 C ATOM 1610 CG LEU A 204 89.706 36.963 22.632 1.00 34.71 C ANISOU 1610 CG LEU A 204 4546 4360 4282 -557 1005 214 C ATOM 1611 CD1 LEU A 204 90.968 37.577 22.045 1.00 33.44 C ANISOU 1611 CD1 LEU A 204 3953 5118 3633 -175 495 933 C ATOM 1612 CD2 LEU A 204 89.924 35.494 23.005 1.00 31.49 C ANISOU 1612 CD2 LEU A 204 4245 4809 2909 -221 105 641 C ATOM 1613 N GLY A 205 87.990 37.612 26.982 1.00 29.39 N ANISOU 1613 N GLY A 205 3684 4477 3005 108 341 145 N ATOM 1614 CA GLY A 205 88.012 38.466 28.163 1.00 29.33 C ANISOU 1614 CA GLY A 205 3309 4893 2943 -186 184 46 C ATOM 1615 C GLY A 205 86.708 38.382 28.931 1.00 29.69 C ANISOU 1615 C GLY A 205 3654 4708 2919 -229 429 95 C ATOM 1616 O GLY A 205 85.637 38.250 28.359 1.00 28.46 O ANISOU 1616 O GLY A 205 3423 4190 3199 -544 655 -51 O ATOM 1617 N SER A 206 86.838 38.448 30.258 1.00 31.83 N ANISOU 1617 N SER A 206 4673 4502 2919 -549 548 -276 N ATOM 1618 CA SER A 206 85.645 38.416 31.102 1.00 29.80 C ANISOU 1618 CA SER A 206 4041 4962 2320 -526 -102 -270 C ATOM 1619 C SER A 206 84.789 39.650 30.872 1.00 31.69 C ANISOU 1619 C SER A 206 4450 4768 2821 -451 78 -368 C ATOM 1620 O SER A 206 83.600 39.626 31.195 1.00 28.29 O ANISOU 1620 O SER A 206 4255 4279 2215 -476 -394 268 O ATOM 1621 CB SER A 206 86.030 38.282 32.585 1.00 33.90 C ANISOU 1621 CB SER A 206 4494 6018 2369 -833 -305 -238 C ATOM 1622 OG SER A 206 86.706 39.476 32.971 1.00 38.87 O ANISOU 1622 OG SER A 206 5664 6409 2695 -1460 -1342 262 O ATOM 1623 N GLN A 207 85.330 40.731 30.310 1.00 30.40 N ANISOU 1623 N GLN A 207 3695 4607 3248 -457 63 -618 N ATOM 1624 CA GLN A 207 84.447 41.857 30.016 1.00 32.40 C ANISOU 1624 CA GLN A 207 4520 4248 3542 -300 14 -920 C ATOM 1625 C GLN A 207 83.410 41.525 28.941 1.00 29.27 C ANISOU 1625 C GLN A 207 4194 3487 3441 -283 30 -247 C ATOM 1626 O GLN A 207 82.432 42.282 28.802 1.00 29.03 O ANISOU 1626 O GLN A 207 4537 3459 3036 -42 551 326 O ATOM 1627 CB GLN A 207 85.268 43.091 29.620 1.00 36.95 C ANISOU 1627 CB GLN A 207 4455 5029 4553 -804 -1270 278 C ATOM 1628 CG GLN A 207 85.770 43.086 28.189 1.00 47.12 C ANISOU 1628 CG GLN A 207 5195 7212 5495 -2280 256 49 C ATOM 1629 CD GLN A 207 87.187 42.556 28.062 1.00 58.32 C ANISOU 1629 CD GLN A 207 5271 8711 8178 -2199 1161 -85 C ATOM 1630 OE1 GLN A 207 87.603 41.650 28.810 1.00 66.79 O ANISOU 1630 OE1 GLN A 207 6080 5957 13342 -1004 1966 -111 O ATOM 1631 NE2 GLN A 207 87.926 43.133 27.106 1.00 76.22 N ANISOU 1631 NE2 GLN A 207 4748 13694 10520 -4923 636 1575 N ATOM 1632 N LYS A 208 83.560 40.447 28.178 1.00 25.90 N ANISOU 1632 N LYS A 208 4036 3076 2728 -346 -118 256 N ATOM 1633 CA LYS A 208 82.603 40.038 27.161 1.00 26.11 C ANISOU 1633 CA LYS A 208 3765 3732 2423 -458 139 294 C ATOM 1634 C LYS A 208 81.630 38.976 27.648 1.00 26.21 C ANISOU 1634 C LYS A 208 3512 3888 2558 -387 -252 646 C ATOM 1635 O LYS A 208 80.802 38.427 26.922 1.00 26.03 O ANISOU 1635 O LYS A 208 3872 3305 2713 -291 -176 195 O ATOM 1636 CB LYS A 208 83.367 39.439 25.972 1.00 26.25 C ANISOU 1636 CB LYS A 208 3674 3411 2887 -397 148 -17 C ATOM 1637 CG LYS A 208 84.494 40.359 25.499 1.00 30.23 C ANISOU 1637 CG LYS A 208 4395 3646 3444 -621 1015 -299 C ATOM 1638 CD LYS A 208 83.952 41.693 25.007 1.00 31.45 C ANISOU 1638 CD LYS A 208 4882 3749 3319 -1187 -14 134 C ATOM 1639 CE LYS A 208 85.063 42.415 24.249 1.00 33.73 C ANISOU 1639 CE LYS A 208 4506 4101 4209 -1327 -214 329 C ATOM 1640 NZ LYS A 208 84.645 43.774 23.840 1.00 36.37 N ANISOU 1640 NZ LYS A 208 5786 3210 4825 -1811 65 -212 N ATOM 1641 N ALA A 209 81.730 38.624 28.914 1.00 27.52 N ANISOU 1641 N ALA A 209 3856 3895 2704 -341 -333 905 N ATOM 1642 CA ALA A 209 80.961 37.492 29.425 1.00 25.88 C ANISOU 1642 CA ALA A 209 3565 3497 2773 -123 -826 957 C ATOM 1643 C ALA A 209 79.463 37.729 29.334 1.00 25.14 C ANISOU 1643 C ALA A 209 3546 3492 2513 -82 -760 754 C ATOM 1644 O ALA A 209 78.712 36.800 28.991 1.00 26.85 O ANISOU 1644 O ALA A 209 3455 3812 2936 -140 -241 8 O ATOM 1645 CB ALA A 209 81.402 37.169 30.860 1.00 23.02 C ANISOU 1645 CB ALA A 209 2921 3511 2316 25 -299 546 C ATOM 1646 N LEU A 210 79.000 38.935 29.629 1.00 25.44 N ANISOU 1646 N LEU A 210 3524 3670 2471 -183 -458 358 N ATOM 1647 CA LEU A 210 77.541 39.166 29.529 1.00 25.96 C ANISOU 1647 CA LEU A 210 3513 3934 2415 -72 -197 183 C ATOM 1648 C LEU A 210 77.084 39.115 28.079 1.00 25.20 C ANISOU 1648 C LEU A 210 3328 3734 2514 20 -310 632 C ATOM 1649 O LEU A 210 75.986 38.647 27.764 1.00 31.16 O ANISOU 1649 O LEU A 210 4203 4560 3078 -900 -917 898 O ATOM 1650 CB LEU A 210 77.126 40.505 30.145 1.00 27.50 C ANISOU 1650 CB LEU A 210 3969 3660 2821 -64 138 434 C ATOM 1651 CG LEU A 210 77.074 40.536 31.671 1.00 30.14 C ANISOU 1651 CG LEU A 210 4555 3985 2914 -429 747 -23 C ATOM 1652 CD1 LEU A 210 76.961 41.966 32.182 1.00 40.51 C ANISOU 1652 CD1 LEU A 210 6486 4436 4470 -530 822 -963 C ATOM 1653 CD2 LEU A 210 75.919 39.700 32.196 1.00 33.37 C ANISOU 1653 CD2 LEU A 210 4280 4458 3940 -58 1358 352 C ATOM 1654 N ALA A 211 77.948 39.614 27.183 1.00 27.48 N ANISOU 1654 N ALA A 211 4486 3291 2663 -308 115 631 N ATOM 1655 CA ALA A 211 77.608 39.539 25.774 1.00 28.29 C ANISOU 1655 CA ALA A 211 3993 4123 2631 -618 294 169 C ATOM 1656 C ALA A 211 77.552 38.091 25.304 1.00 28.10 C ANISOU 1656 C ALA A 211 4031 3919 2728 -565 200 406 C ATOM 1657 O ALA A 211 76.665 37.750 24.509 1.00 28.25 O ANISOU 1657 O ALA A 211 3966 3542 3227 -506 8 452 O ATOM 1658 CB ALA A 211 78.622 40.346 24.985 1.00 25.95 C ANISOU 1658 CB ALA A 211 3715 3845 2298 -492 -138 300 C ATOM 1659 N LEU A 212 78.471 37.241 25.763 1.00 29.74 N ANISOU 1659 N LEU A 212 4595 4129 2575 -549 -229 649 N ATOM 1660 CA LEU A 212 78.512 35.842 25.359 1.00 25.23 C ANISOU 1660 CA LEU A 212 3555 4092 1940 -464 -338 834 C ATOM 1661 C LEU A 212 77.230 35.150 25.822 1.00 26.45 C ANISOU 1661 C LEU A 212 3253 4091 2706 -119 118 416 C ATOM 1662 O LEU A 212 76.649 34.339 25.106 1.00 26.73 O ANISOU 1662 O LEU A 212 3539 3928 2690 -461 108 723 O ATOM 1663 CB LEU A 212 79.661 35.075 25.979 1.00 26.14 C ANISOU 1663 CB LEU A 212 3254 5074 1604 -148 130 1069 C ATOM 1664 CG LEU A 212 80.459 34.083 25.164 1.00 31.40 C ANISOU 1664 CG LEU A 212 4836 4104 2990 228 -696 230 C ATOM 1665 CD1 LEU A 212 80.921 32.915 26.030 1.00 31.16 C ANISOU 1665 CD1 LEU A 212 5718 3975 2147 -356 505 747 C ATOM 1666 CD2 LEU A 212 79.735 33.550 23.931 1.00 29.99 C ANISOU 1666 CD2 LEU A 212 3747 2975 4675 428 -1429 -231 C ATOM 1667 N GLN A 213 76.875 35.510 27.050 1.00 28.60 N ANISOU 1667 N GLN A 213 3647 4297 2922 23 421 291 N ATOM 1668 CA GLN A 213 75.644 34.932 27.612 1.00 28.27 C ANISOU 1668 CA GLN A 213 3770 4308 2664 43 296 648 C ATOM 1669 C GLN A 213 74.420 35.358 26.796 1.00 27.90 C ANISOU 1669 C GLN A 213 3697 3508 3397 162 48 28 C ATOM 1670 O GLN A 213 73.538 34.527 26.539 1.00 26.94 O ANISOU 1670 O GLN A 213 3530 3710 2995 -146 559 542 O ATOM 1671 CB GLN A 213 75.492 35.307 29.098 1.00 29.86 C ANISOU 1671 CB GLN A 213 4273 4258 2815 304 573 427 C ATOM 1672 CG GLN A 213 74.522 34.374 29.826 1.00 39.30 C ANISOU 1672 CG GLN A 213 6207 5403 3322 -880 1789 -170 C ATOM 1673 CD GLN A 213 73.096 34.886 29.763 1.00 45.82 C ANISOU 1673 CD GLN A 213 5764 6136 5508 -1206 2816 22 C ATOM 1674 OE1 GLN A 213 72.915 36.056 29.416 1.00 53.98 O ANISOU 1674 OE1 GLN A 213 5710 6244 8557 -370 2661 187 O ATOM 1675 NE2 GLN A 213 72.088 34.075 30.040 1.00 57.17 N ANISOU 1675 NE2 GLN A 213 6683 8012 7026 -2886 1918 53 N ATOM 1676 N ALA A 214 74.381 36.638 26.426 1.00 28.99 N ANISOU 1676 N ALA A 214 4033 3798 3185 -353 -195 686 N ATOM 1677 CA ALA A 214 73.242 37.125 25.654 1.00 28.54 C ANISOU 1677 CA ALA A 214 3677 3693 3475 -175 -111 350 C ATOM 1678 C ALA A 214 73.228 36.457 24.287 1.00 28.15 C ANISOU 1678 C ALA A 214 3485 3684 3525 -42 -286 270 C ATOM 1679 O ALA A 214 72.128 36.181 23.775 1.00 32.38 O ANISOU 1679 O ALA A 214 3423 5591 3289 -771 170 210 O ATOM 1680 CB ALA A 214 73.258 38.630 25.455 1.00 28.84 C ANISOU 1680 CB ALA A 214 3188 3675 4096 -530 -1297 130 C ATOM 1681 N ALA A 215 74.398 36.199 23.707 1.00 26.92 N ANISOU 1681 N ALA A 215 3358 3711 3160 20 -495 438 N ATOM 1682 CA ALA A 215 74.459 35.553 22.393 1.00 30.50 C ANISOU 1682 CA ALA A 215 4225 3758 3604 -113 -91 36 C ATOM 1683 C ALA A 215 73.986 34.102 22.453 1.00 27.87 C ANISOU 1683 C ALA A 215 3067 3676 3846 215 -514 194 C ATOM 1684 O ALA A 215 73.242 33.648 21.584 1.00 28.10 O ANISOU 1684 O ALA A 215 3415 4015 3248 -44 -217 177 O ATOM 1685 CB ALA A 215 75.866 35.616 21.796 1.00 26.25 C ANISOU 1685 CB ALA A 215 4114 3604 2255 -51 -540 938 C ATOM 1686 N VAL A 216 74.417 33.357 23.470 1.00 26.01 N ANISOU 1686 N VAL A 216 2832 4068 2981 93 223 219 N ATOM 1687 CA VAL A 216 74.253 31.915 23.491 1.00 28.99 C ANISOU 1687 CA VAL A 216 3507 4112 3397 -225 178 765 C ATOM 1688 C VAL A 216 73.038 31.485 24.297 1.00 28.46 C ANISOU 1688 C VAL A 216 3112 4337 3362 -369 41 110 C ATOM 1689 O VAL A 216 72.270 30.618 23.830 1.00 31.65 O ANISOU 1689 O VAL A 216 3387 4551 4086 -556 -656 424 O ATOM 1690 CB VAL A 216 75.522 31.263 24.084 1.00 29.65 C ANISOU 1690 CB VAL A 216 3251 3832 4183 68 523 354 C ATOM 1691 CG1 VAL A 216 75.365 29.765 24.327 1.00 29.03 C ANISOU 1691 CG1 VAL A 216 3443 3719 3869 105 375 13 C ATOM 1692 CG2 VAL A 216 76.722 31.512 23.168 1.00 30.11 C ANISOU 1692 CG2 VAL A 216 3985 3878 3576 615 904 487 C ATOM 1693 N GLU A 217 72.803 32.021 25.491 1.00 29.52 N ANISOU 1693 N GLU A 217 3976 4112 3127 260 137 542 N ATOM 1694 CA GLU A 217 71.728 31.490 26.336 1.00 27.64 C ANISOU 1694 CA GLU A 217 3965 3921 2615 -127 -259 328 C ATOM 1695 C GLU A 217 70.539 32.434 26.376 1.00 27.57 C ANISOU 1695 C GLU A 217 3324 3921 3230 -513 -371 158 C ATOM 1696 O GLU A 217 69.434 32.012 26.691 1.00 30.82 O ANISOU 1696 O GLU A 217 3867 4616 3227 -699 388 516 O ATOM 1697 CB GLU A 217 72.125 31.300 27.806 1.00 28.51 C ANISOU 1697 CB GLU A 217 4447 3723 2661 -394 -510 230 C ATOM 1698 CG GLU A 217 72.926 30.071 28.134 1.00 31.72 C ANISOU 1698 CG GLU A 217 5028 3915 3109 -231 -796 545 C ATOM 1699 CD GLU A 217 73.510 30.118 29.532 1.00 30.22 C ANISOU 1699 CD GLU A 217 4414 4065 3004 153 -513 122 C ATOM 1700 OE1 GLU A 217 73.168 31.034 30.313 1.00 35.52 O ANISOU 1700 OE1 GLU A 217 5903 4209 3386 209 -68 -39 O ATOM 1701 OE2 GLU A 217 74.329 29.259 29.916 1.00 30.37 O ANISOU 1701 OE2 GLU A 217 4816 3827 2895 -71 -240 972 O ATOM 1702 N GLY A 218 70.748 33.711 26.091 1.00 27.03 N ANISOU 1702 N GLY A 218 3319 3806 3146 -253 182 24 N ATOM 1703 CA GLY A 218 69.611 34.618 26.211 1.00 27.96 C ANISOU 1703 CA GLY A 218 3346 4040 3238 -207 332 -278 C ATOM 1704 C GLY A 218 68.645 34.513 25.052 1.00 26.15 C ANISOU 1704 C GLY A 218 3303 3304 3330 261 346 -666 C ATOM 1705 O GLY A 218 68.827 33.745 24.123 1.00 26.74 O ANISOU 1705 O GLY A 218 3373 3412 3376 240 541 -709 O ATOM 1706 N CYS A 219 67.572 35.305 25.087 1.00 24.88 N ANISOU 1706 N CYS A 219 3568 2925 2958 352 743 37 N ATOM 1707 CA CYS A 219 66.646 35.292 23.984 1.00 30.38 C ANISOU 1707 CA CYS A 219 4496 3078 3969 623 -280 303 C ATOM 1708 C CYS A 219 66.993 36.395 22.975 1.00 30.85 C ANISOU 1708 C CYS A 219 4438 3599 3682 74 -540 392 C ATOM 1709 O CYS A 219 67.787 37.295 23.250 1.00 25.68 O ANISOU 1709 O CYS A 219 3123 3511 3124 661 -12 78 O ATOM 1710 CB CYS A 219 65.205 35.494 24.460 1.00 37.11 C ANISOU 1710 CB CYS A 219 3936 4930 5235 -330 -381 641 C ATOM 1711 SG CYS A 219 64.533 34.107 25.414 1.00 58.04 S ANISOU 1711 SG CYS A 219 7872 5748 8434 -1355 2190 1007 S ATOM 1712 N VAL A 220 66.366 36.306 21.814 1.00 27.88 N ANISOU 1712 N VAL A 220 3496 3703 3394 104 59 -12 N ATOM 1713 CA VAL A 220 66.590 37.305 20.771 1.00 26.75 C ANISOU 1713 CA VAL A 220 3323 3784 3057 282 28 -76 C ATOM 1714 C VAL A 220 66.054 38.677 21.176 1.00 26.58 C ANISOU 1714 C VAL A 220 3305 3766 3028 181 527 46 C ATOM 1715 O VAL A 220 64.885 38.871 21.528 1.00 26.98 O ANISOU 1715 O VAL A 220 3141 3674 3436 -52 435 -131 O ATOM 1716 CB VAL A 220 65.958 36.840 19.448 1.00 33.69 C ANISOU 1716 CB VAL A 220 5260 4232 3308 -763 -327 -237 C ATOM 1717 CG1 VAL A 220 66.095 37.953 18.400 1.00 29.53 C ANISOU 1717 CG1 VAL A 220 4246 4100 2875 -432 -540 -467 C ATOM 1718 CG2 VAL A 220 66.608 35.545 18.990 1.00 29.12 C ANISOU 1718 CG2 VAL A 220 4256 4208 2601 -760 -991 -56 C ATOM 1719 N ASN A 221 66.933 39.688 21.136 1.00 23.80 N ANISOU 1719 N ASN A 221 2734 3576 2733 519 250 357 N ATOM 1720 CA ASN A 221 66.438 41.029 21.411 1.00 26.01 C ANISOU 1720 CA ASN A 221 2969 3599 3315 539 773 400 C ATOM 1721 C ASN A 221 67.391 42.061 20.821 1.00 28.17 C ANISOU 1721 C ASN A 221 2942 3749 4012 85 133 543 C ATOM 1722 O ASN A 221 68.602 41.851 20.806 1.00 30.71 O ANISOU 1722 O ASN A 221 3047 3707 4914 270 773 475 O ATOM 1723 CB ASN A 221 66.242 41.257 22.909 1.00 33.22 C ANISOU 1723 CB ASN A 221 5329 3818 3475 153 881 -227 C ATOM 1724 CG ASN A 221 67.591 41.578 23.511 1.00 39.44 C ANISOU 1724 CG ASN A 221 6876 4170 3941 -916 -536 452 C ATOM 1725 OD1 ASN A 221 67.921 42.754 23.632 1.00 50.59 O ANISOU 1725 OD1 ASN A 221 9635 4632 4955 -1970 -966 36 O ATOM 1726 ND2 ASN A 221 68.322 40.526 23.845 1.00 39.14 N ANISOU 1726 ND2 ASN A 221 4934 5456 4482 -196 908 529 N ATOM 1727 N HIS A 222 66.845 43.166 20.318 1.00 24.93 N ANISOU 1727 N HIS A 222 3292 3123 3055 99 244 -201 N ATOM 1728 CA HIS A 222 67.696 44.113 19.607 1.00 28.03 C ANISOU 1728 CA HIS A 222 3672 3846 3130 -342 -116 313 C ATOM 1729 C HIS A 222 68.601 44.912 20.526 1.00 25.51 C ANISOU 1729 C HIS A 222 3150 3788 2756 -191 167 370 C ATOM 1730 O HIS A 222 69.486 45.624 20.069 1.00 26.47 O ANISOU 1730 O HIS A 222 3347 4108 2601 -357 606 -136 O ATOM 1731 CB HIS A 222 66.800 45.047 18.775 1.00 27.71 C ANISOU 1731 CB HIS A 222 3610 4005 2913 -335 -149 269 C ATOM 1732 CG HIS A 222 65.987 46.002 19.595 1.00 30.41 C ANISOU 1732 CG HIS A 222 4463 3639 3452 -122 171 392 C ATOM 1733 ND1 HIS A 222 65.524 47.164 19.040 1.00 30.51 N ANISOU 1733 ND1 HIS A 222 4026 3751 3813 -351 -41 647 N ATOM 1734 CD2 HIS A 222 65.526 46.000 20.888 1.00 28.37 C ANISOU 1734 CD2 HIS A 222 3804 3680 3294 164 -146 175 C ATOM 1735 CE1 HIS A 222 64.833 47.849 19.938 1.00 29.61 C ANISOU 1735 CE1 HIS A 222 3212 3860 4178 -174 -48 794 C ATOM 1736 NE2 HIS A 222 64.817 47.171 21.075 1.00 27.77 N ANISOU 1736 NE2 HIS A 222 3066 3834 3652 142 -437 335 N ATOM 1737 N MET A 223 68.396 44.857 21.846 1.00 25.07 N ANISOU 1737 N MET A 223 3191 3482 2852 -2 648 90 N ATOM 1738 CA MET A 223 69.259 45.680 22.697 1.00 27.84 C ANISOU 1738 CA MET A 223 3817 3836 2926 20 235 -63 C ATOM 1739 C MET A 223 70.652 45.042 22.815 1.00 28.01 C ANISOU 1739 C MET A 223 3332 3791 3519 -420 477 -313 C ATOM 1740 O MET A 223 71.648 45.752 23.010 1.00 32.61 O ANISOU 1740 O MET A 223 4043 4364 3982 -827 -476 -588 O ATOM 1741 CB MET A 223 68.661 45.914 24.082 1.00 31.81 C ANISOU 1741 CB MET A 223 3759 4994 3335 -137 569 -704 C ATOM 1742 CG MET A 223 67.504 46.874 24.232 1.00 35.49 C ANISOU 1742 CG MET A 223 4971 4284 4229 278 1229 -251 C ATOM 1743 SD MET A 223 67.841 48.620 23.909 1.00 45.43 S ANISOU 1743 SD MET A 223 7173 4720 5367 -457 4 786 S ATOM 1744 CE MET A 223 69.446 48.815 24.647 1.00 45.69 C ANISOU 1744 CE MET A 223 6965 6223 4174 -1548 947 -545 C ATOM 1745 N TRP A 224 70.742 43.722 22.709 1.00 26.46 N ANISOU 1745 N TRP A 224 3248 3792 3012 -210 580 -393 N ATOM 1746 CA TRP A 224 71.986 42.977 22.631 1.00 25.51 C ANISOU 1746 CA TRP A 224 2915 3982 2794 -399 599 -47 C ATOM 1747 C TRP A 224 72.096 42.457 21.203 1.00 23.92 C ANISOU 1747 C TRP A 224 2798 3541 2750 126 299 111 C ATOM 1748 O TRP A 224 71.635 41.344 20.922 1.00 28.18 O ANISOU 1748 O TRP A 224 4073 4026 2607 -664 -261 251 O ATOM 1749 CB TRP A 224 72.009 41.820 23.630 1.00 26.22 C ANISOU 1749 CB TRP A 224 3118 4195 2652 -420 353 18 C ATOM 1750 CG TRP A 224 72.048 42.328 25.057 1.00 27.79 C ANISOU 1750 CG TRP A 224 3388 4375 2797 -169 32 -98 C ATOM 1751 CD1 TRP A 224 70.987 42.764 25.792 1.00 28.37 C ANISOU 1751 CD1 TRP A 224 3671 4310 2800 -9 -75 -617 C ATOM 1752 CD2 TRP A 224 73.183 42.453 25.917 1.00 28.12 C ANISOU 1752 CD2 TRP A 224 3668 4114 2901 -141 -221 210 C ATOM 1753 NE1 TRP A 224 71.375 43.150 27.039 1.00 29.97 N ANISOU 1753 NE1 TRP A 224 3806 4833 2747 -261 -224 -395 N ATOM 1754 CE2 TRP A 224 72.734 42.970 27.146 1.00 30.42 C ANISOU 1754 CE2 TRP A 224 3885 4698 2975 -218 -329 -98 C ATOM 1755 CE3 TRP A 224 74.542 42.185 25.783 1.00 27.83 C ANISOU 1755 CE3 TRP A 224 3701 3809 3064 31 -475 414 C ATOM 1756 CZ2 TRP A 224 73.592 43.219 28.216 1.00 30.60 C ANISOU 1756 CZ2 TRP A 224 3923 4616 3087 -197 -442 -43 C ATOM 1757 CZ3 TRP A 224 75.404 42.428 26.838 1.00 28.39 C ANISOU 1757 CZ3 TRP A 224 3913 3697 3177 -26 -548 146 C ATOM 1758 CH2 TRP A 224 74.923 42.945 28.052 1.00 29.45 C ANISOU 1758 CH2 TRP A 224 3780 4361 3050 -619 -160 298 C ATOM 1759 N THR A 225 72.655 43.264 20.298 1.00 24.46 N ANISOU 1759 N THR A 225 2994 3587 2711 71 623 -144 N ATOM 1760 CA THR A 225 72.657 42.964 18.872 1.00 23.89 C ANISOU 1760 CA THR A 225 2936 3457 2683 -37 365 -176 C ATOM 1761 C THR A 225 73.162 41.555 18.595 1.00 23.19 C ANISOU 1761 C THR A 225 3060 3332 2421 -189 -249 -227 C ATOM 1762 O THR A 225 72.606 40.846 17.758 1.00 24.92 O ANISOU 1762 O THR A 225 3742 3616 2112 -581 -167 -160 O ATOM 1763 CB THR A 225 73.536 43.982 18.117 1.00 28.76 C ANISOU 1763 CB THR A 225 5097 3622 2209 -1100 151 -226 C ATOM 1764 OG1 THR A 225 73.076 45.294 18.442 1.00 26.14 O ANISOU 1764 OG1 THR A 225 3254 3870 2808 -573 134 514 O ATOM 1765 CG2 THR A 225 73.383 43.818 16.610 1.00 25.10 C ANISOU 1765 CG2 THR A 225 3289 3990 2260 -19 -1080 637 C ATOM 1766 N ILE A 226 74.207 41.150 19.295 1.00 23.82 N ANISOU 1766 N ILE A 226 3298 3556 2197 -70 -148 250 N ATOM 1767 CA ILE A 226 74.808 39.831 19.121 1.00 26.22 C ANISOU 1767 CA ILE A 226 3673 3367 2922 -125 -323 466 C ATOM 1768 C ILE A 226 73.790 38.710 19.301 1.00 27.08 C ANISOU 1768 C ILE A 226 3529 3616 3145 -236 -8 -107 C ATOM 1769 O ILE A 226 73.955 37.628 18.699 1.00 25.56 O ANISOU 1769 O ILE A 226 3398 3644 2671 -280 170 31 O ATOM 1770 CB ILE A 226 75.997 39.623 20.089 1.00 24.10 C ANISOU 1770 CB ILE A 226 3102 3689 2368 264 168 -148 C ATOM 1771 CG1 ILE A 226 76.909 38.459 19.670 1.00 26.09 C ANISOU 1771 CG1 ILE A 226 2996 3888 3031 95 447 -573 C ATOM 1772 CG2 ILE A 226 75.550 39.439 21.553 1.00 22.86 C ANISOU 1772 CG2 ILE A 226 2494 3551 2642 498 325 295 C ATOM 1773 CD1 ILE A 226 77.729 38.773 18.426 1.00 30.57 C ANISOU 1773 CD1 ILE A 226 3755 4324 3538 229 1015 -389 C ATOM 1774 N SER A 227 72.735 38.918 20.102 1.00 25.04 N ANISOU 1774 N SER A 227 3424 3454 2636 -15 -298 -68 N ATOM 1775 CA SER A 227 71.725 37.867 20.256 1.00 26.89 C ANISOU 1775 CA SER A 227 3845 3709 2662 -327 253 -370 C ATOM 1776 C SER A 227 71.011 37.575 18.936 1.00 27.33 C ANISOU 1776 C SER A 227 3780 3607 2999 -575 -69 -80 C ATOM 1777 O SER A 227 70.470 36.490 18.735 1.00 25.90 O ANISOU 1777 O SER A 227 3228 3565 3048 -395 43 -78 O ATOM 1778 CB SER A 227 70.682 38.232 21.315 1.00 28.65 C ANISOU 1778 CB SER A 227 3612 3899 3375 57 326 -525 C ATOM 1779 OG SER A 227 69.801 39.250 20.837 1.00 29.28 O ANISOU 1779 OG SER A 227 4302 3703 3122 -12 499 -34 O ATOM 1780 N CYS A 228 70.997 38.557 18.007 1.00 27.72 N ANISOU 1780 N CYS A 228 3531 3482 3517 -138 -413 144 N ATOM 1781 CA CYS A 228 70.228 38.221 16.802 1.00 30.52 C ANISOU 1781 CA CYS A 228 3796 4297 3502 -259 -491 167 C ATOM 1782 C CYS A 228 71.021 37.261 15.918 1.00 28.64 C ANISOU 1782 C CYS A 228 4034 3652 3198 -282 -635 375 C ATOM 1783 O CYS A 228 70.460 36.724 14.956 1.00 28.04 O ANISOU 1783 O CYS A 228 4053 4283 2318 -141 -620 895 O ATOM 1784 CB CYS A 228 69.744 39.518 16.139 1.00 35.97 C ANISOU 1784 CB CYS A 228 4947 4097 4625 374 -2151 -672 C ATOM 1785 SG CYS A 228 68.773 40.529 17.387 1.00 44.93 S ANISOU 1785 SG CYS A 228 6784 4787 5499 995 -101 253 S ATOM 1786 N LEU A 229 72.286 36.958 16.226 1.00 25.14 N ANISOU 1786 N LEU A 229 3768 3358 2425 -601 -289 556 N ATOM 1787 CA LEU A 229 72.978 35.909 15.465 1.00 26.01 C ANISOU 1787 CA LEU A 229 3763 3876 2245 -645 -166 307 C ATOM 1788 C LEU A 229 72.357 34.536 15.653 1.00 27.05 C ANISOU 1788 C LEU A 229 3811 3617 2851 -359 608 -10 C ATOM 1789 O LEU A 229 72.632 33.610 14.877 1.00 25.11 O ANISOU 1789 O LEU A 229 3310 3704 2526 -28 400 164 O ATOM 1790 CB LEU A 229 74.468 35.854 15.841 1.00 27.99 C ANISOU 1790 CB LEU A 229 3715 4359 2561 -462 -105 389 C ATOM 1791 CG LEU A 229 75.281 37.027 15.265 1.00 35.45 C ANISOU 1791 CG LEU A 229 4502 5677 3289 -1842 -283 498 C ATOM 1792 CD1 LEU A 229 76.732 36.940 15.687 1.00 35.34 C ANISOU 1792 CD1 LEU A 229 4276 6000 3152 -1493 117 -705 C ATOM 1793 CD2 LEU A 229 75.178 37.030 13.747 1.00 30.45 C ANISOU 1793 CD2 LEU A 229 3824 4477 3267 -1275 323 542 C ATOM 1794 N GLN A 230 71.505 34.370 16.659 1.00 26.40 N ANISOU 1794 N GLN A 230 3851 3533 2648 -560 549 -290 N ATOM 1795 CA GLN A 230 70.758 33.132 16.824 1.00 25.65 C ANISOU 1795 CA GLN A 230 3857 3443 2445 -411 8 347 C ATOM 1796 C GLN A 230 69.869 32.854 15.608 1.00 24.61 C ANISOU 1796 C GLN A 230 3239 3277 2836 167 82 -266 C ATOM 1797 O GLN A 230 69.506 31.712 15.336 1.00 26.95 O ANISOU 1797 O GLN A 230 3802 3453 2986 -187 192 -316 O ATOM 1798 CB GLN A 230 69.856 33.184 18.068 1.00 25.56 C ANISOU 1798 CB GLN A 230 4034 3023 2655 -236 224 432 C ATOM 1799 CG GLN A 230 70.619 33.193 19.382 1.00 25.03 C ANISOU 1799 CG GLN A 230 3973 3053 2486 296 372 499 C ATOM 1800 CD GLN A 230 69.703 33.241 20.590 1.00 27.22 C ANISOU 1800 CD GLN A 230 3859 3743 2742 -48 491 -185 C ATOM 1801 OE1 GLN A 230 68.574 32.734 20.530 1.00 28.77 O ANISOU 1801 OE1 GLN A 230 3961 3766 3204 -190 487 95 O ATOM 1802 NE2 GLN A 230 70.175 33.842 21.686 1.00 31.30 N ANISOU 1802 NE2 GLN A 230 4572 4527 2795 -375 440 -383 N ATOM 1803 N LEU A 231 69.506 33.927 14.901 1.00 25.39 N ANISOU 1803 N LEU A 231 3599 3562 2485 206 -28 -133 N ATOM 1804 CA LEU A 231 68.640 33.785 13.745 1.00 24.25 C ANISOU 1804 CA LEU A 231 3256 3484 2474 130 188 -459 C ATOM 1805 C LEU A 231 69.463 33.651 12.464 1.00 24.06 C ANISOU 1805 C LEU A 231 3218 3411 2514 113 235 -303 C ATOM 1806 O LEU A 231 68.918 33.443 11.372 1.00 31.82 O ANISOU 1806 O LEU A 231 4543 5218 2330 -1154 174 -216 O ATOM 1807 CB LEU A 231 67.708 34.993 13.605 1.00 25.21 C ANISOU 1807 CB LEU A 231 2684 3926 2969 149 149 -360 C ATOM 1808 CG LEU A 231 66.835 35.246 14.836 1.00 27.06 C ANISOU 1808 CG LEU A 231 3295 3610 3378 173 658 -285 C ATOM 1809 CD1 LEU A 231 65.958 36.464 14.581 1.00 28.51 C ANISOU 1809 CD1 LEU A 231 3502 4002 3326 534 145 -685 C ATOM 1810 CD2 LEU A 231 66.052 33.981 15.155 1.00 28.42 C ANISOU 1810 CD2 LEU A 231 3397 4006 3397 -320 521 -514 C ATOM 1811 N HIS A 232 70.778 33.768 12.598 1.00 26.95 N ANISOU 1811 N HIS A 232 3167 3463 3609 -99 451 265 N ATOM 1812 CA HIS A 232 71.592 33.694 11.377 1.00 26.73 C ANISOU 1812 CA HIS A 232 2986 3787 3384 -101 213 -20 C ATOM 1813 C HIS A 232 71.786 32.253 10.952 1.00 25.36 C ANISOU 1813 C HIS A 232 3199 3722 2714 -146 -298 93 C ATOM 1814 O HIS A 232 71.945 31.344 11.761 1.00 29.30 O ANISOU 1814 O HIS A 232 4631 3628 2874 -997 159 409 O ATOM 1815 CB HIS A 232 72.922 34.414 11.643 1.00 24.21 C ANISOU 1815 CB HIS A 232 3148 3584 2465 -189 147 217 C ATOM 1816 CG HIS A 232 73.710 34.585 10.381 1.00 24.58 C ANISOU 1816 CG HIS A 232 3459 3392 2489 -228 314 -9 C ATOM 1817 ND1 HIS A 232 74.536 33.586 9.914 1.00 24.87 N ANISOU 1817 ND1 HIS A 232 3275 3272 2904 -316 339 11 N ATOM 1818 CD2 HIS A 232 73.777 35.611 9.507 1.00 23.99 C ANISOU 1818 CD2 HIS A 232 3153 3477 2487 -108 361 69 C ATOM 1819 CE1 HIS A 232 75.097 33.997 8.781 1.00 27.11 C ANISOU 1819 CE1 HIS A 232 3390 3582 3326 73 781 245 C ATOM 1820 NE2 HIS A 232 74.656 35.217 8.514 1.00 27.56 N ANISOU 1820 NE2 HIS A 232 3913 3291 3266 -106 1117 149 N ATOM 1821 N PRO A 233 71.759 31.969 9.647 1.00 29.85 N ANISOU 1821 N PRO A 233 4389 4130 2825 -525 -831 -39 N ATOM 1822 CA PRO A 233 71.906 30.578 9.200 1.00 29.55 C ANISOU 1822 CA PRO A 233 4353 4227 2648 -629 20 -135 C ATOM 1823 C PRO A 233 73.210 29.930 9.651 1.00 30.17 C ANISOU 1823 C PRO A 233 4240 3997 3226 -655 269 54 C ATOM 1824 O PRO A 233 73.233 28.702 9.836 1.00 30.28 O ANISOU 1824 O PRO A 233 4342 3887 3276 -373 1171 -270 O ATOM 1825 CB PRO A 233 71.888 30.671 7.673 1.00 29.53 C ANISOU 1825 CB PRO A 233 4372 4156 2691 -1082 502 167 C ATOM 1826 CG PRO A 233 71.925 32.106 7.331 1.00 33.98 C ANISOU 1826 CG PRO A 233 5727 4093 3092 -287 649 102 C ATOM 1827 CD PRO A 233 71.555 32.911 8.541 1.00 31.71 C ANISOU 1827 CD PRO A 233 5181 4341 2525 -575 -100 46 C ATOM 1828 N LYS A 234 74.309 30.655 9.831 1.00 28.88 N ANISOU 1828 N LYS A 234 3639 4258 3076 -531 1301 -227 N ATOM 1829 CA LYS A 234 75.585 29.984 10.091 1.00 29.54 C ANISOU 1829 CA LYS A 234 3940 4172 3110 -404 1065 -86 C ATOM 1830 C LYS A 234 76.528 30.862 10.907 1.00 33.54 C ANISOU 1830 C LYS A 234 4515 4743 3485 -914 306 503 C ATOM 1831 O LYS A 234 77.398 31.560 10.360 1.00 27.61 O ANISOU 1831 O LYS A 234 2921 4179 3391 248 464 169 O ATOM 1832 CB LYS A 234 76.258 29.601 8.766 1.00 30.48 C ANISOU 1832 CB LYS A 234 3351 4769 3459 -536 1563 245 C ATOM 1833 CG LYS A 234 77.067 28.326 8.896 1.00 38.16 C ANISOU 1833 CG LYS A 234 4449 4908 5142 -7 2316 -28 C ATOM 1834 CD LYS A 234 77.956 28.113 7.683 1.00 47.81 C ANISOU 1834 CD LYS A 234 6546 5808 5814 -229 3168 -1844 C ATOM 1835 CE LYS A 234 77.082 27.965 6.450 1.00 54.11 C ANISOU 1835 CE LYS A 234 8746 6080 5734 -1419 2641 -2081 C ATOM 1836 NZ LYS A 234 77.326 26.614 5.859 1.00 66.62 N ANISOU 1836 NZ LYS A 234 10734 5787 8791 -2122 2186 -2864 N ATOM 1837 N ALA A 235 76.335 30.823 12.218 1.00 27.96 N ANISOU 1837 N ALA A 235 3557 3681 3387 -288 66 568 N ATOM 1838 CA ALA A 235 77.081 31.633 13.166 1.00 31.58 C ANISOU 1838 CA ALA A 235 3988 4098 3913 -355 -424 435 C ATOM 1839 C ALA A 235 77.917 30.786 14.127 1.00 29.07 C ANISOU 1839 C ALA A 235 3748 3818 3480 -355 -57 357 C ATOM 1840 O ALA A 235 77.571 29.687 14.604 1.00 31.00 O ANISOU 1840 O ALA A 235 3926 3599 4253 -14 747 353 O ATOM 1841 CB ALA A 235 76.117 32.525 13.944 1.00 30.40 C ANISOU 1841 CB ALA A 235 4795 3101 3656 -216 -579 613 C ATOM 1842 N ILE A 236 79.106 31.326 14.425 1.00 26.94 N ANISOU 1842 N ILE A 236 3158 3904 3176 100 507 -133 N ATOM 1843 CA ILE A 236 80.054 30.652 15.294 1.00 31.10 C ANISOU 1843 CA ILE A 236 3868 4157 3793 175 -244 -227 C ATOM 1844 C ILE A 236 80.637 31.637 16.293 1.00 29.56 C ANISOU 1844 C ILE A 236 3757 4065 3411 -181 121 1 C ATOM 1845 O ILE A 236 81.093 32.681 15.846 1.00 33.00 O ANISOU 1845 O ILE A 236 5284 4375 2879 -612 -69 189 O ATOM 1846 CB ILE A 236 81.209 30.047 14.474 1.00 31.23 C ANISOU 1846 CB ILE A 236 3621 4325 3921 596 -804 -478 C ATOM 1847 CG1 ILE A 236 80.720 29.286 13.249 1.00 35.13 C ANISOU 1847 CG1 ILE A 236 3770 5456 4123 385 -695 -1035 C ATOM 1848 CG2 ILE A 236 82.106 29.170 15.333 1.00 31.42 C ANISOU 1848 CG2 ILE A 236 2994 5127 3817 -118 -89 1014 C ATOM 1849 CD1 ILE A 236 81.806 28.667 12.385 1.00 55.06 C ANISOU 1849 CD1 ILE A 236 7612 6737 6571 -825 3180 -2168 C ATOM 1850 N MET A 237 80.606 31.293 17.563 1.00 29.36 N ANISOU 1850 N MET A 237 3617 4074 3464 -752 422 95 N ATOM 1851 CA MET A 237 81.266 32.040 18.614 1.00 30.49 C ANISOU 1851 CA MET A 237 3624 4555 3407 -270 224 -150 C ATOM 1852 C MET A 237 82.525 31.260 19.038 1.00 30.72 C ANISOU 1852 C MET A 237 3624 4444 3602 -190 392 -60 C ATOM 1853 O MET A 237 82.388 30.076 19.377 1.00 31.33 O ANISOU 1853 O MET A 237 3859 4527 3519 -259 548 85 O ATOM 1854 CB MET A 237 80.434 32.239 19.871 1.00 32.89 C ANISOU 1854 CB MET A 237 3613 4865 4018 -523 678 -645 C ATOM 1855 CG MET A 237 79.020 32.728 19.725 1.00 37.03 C ANISOU 1855 CG MET A 237 3307 5944 4817 -827 797 294 C ATOM 1856 SD MET A 237 78.882 34.311 18.921 1.00 48.54 S ANISOU 1856 SD MET A 237 5863 5740 6841 -99 -1040 349 S ATOM 1857 CE MET A 237 79.239 35.507 20.192 1.00 42.25 C ANISOU 1857 CE MET A 237 6070 5304 4680 934 -1908 1637 C ATOM 1858 N VAL A 238 83.656 31.941 18.993 1.00 29.35 N ANISOU 1858 N VAL A 238 3627 4330 3193 -186 196 -143 N ATOM 1859 CA VAL A 238 84.925 31.319 19.392 1.00 28.91 C ANISOU 1859 CA VAL A 238 3688 4254 3042 -176 227 13 C ATOM 1860 C VAL A 238 85.429 32.030 20.642 1.00 28.28 C ANISOU 1860 C VAL A 238 3595 4044 3107 -184 263 -10 C ATOM 1861 O VAL A 238 85.695 33.234 20.601 1.00 28.31 O ANISOU 1861 O VAL A 238 3533 4080 3146 -227 80 217 O ATOM 1862 CB VAL A 238 85.978 31.373 18.278 1.00 29.24 C ANISOU 1862 CB VAL A 238 3648 4347 3114 -173 238 -121 C ATOM 1863 CG1 VAL A 238 87.175 30.480 18.604 1.00 27.27 C ANISOU 1863 CG1 VAL A 238 3419 4035 2908 -480 56 -206 C ATOM 1864 CG2 VAL A 238 85.331 30.993 16.948 1.00 26.61 C ANISOU 1864 CG2 VAL A 238 3134 3775 3200 279 288 -355 C ATOM 1865 N CYS A 239 85.537 31.299 21.762 1.00 25.74 N ANISOU 1865 N CYS A 239 3053 3681 3047 -106 288 -148 N ATOM 1866 CA CYS A 239 85.764 32.097 22.965 1.00 29.29 C ANISOU 1866 CA CYS A 239 3473 4457 3199 307 101 -600 C ATOM 1867 C CYS A 239 86.860 31.539 23.854 1.00 28.69 C ANISOU 1867 C CYS A 239 4053 3961 2886 -135 87 142 C ATOM 1868 O CYS A 239 87.266 30.370 23.783 1.00 29.05 O ANISOU 1868 O CYS A 239 3648 3928 3461 -210 517 295 O ATOM 1869 CB CYS A 239 84.406 32.181 23.676 1.00 34.03 C ANISOU 1869 CB CYS A 239 4347 3865 4719 742 1239 -760 C ATOM 1870 SG CYS A 239 83.927 30.665 24.547 1.00 39.99 S ANISOU 1870 SG CYS A 239 5272 5296 4628 -462 850 -44 S ATOM 1871 N ASP A 240 87.371 32.428 24.734 1.00 26.15 N ANISOU 1871 N ASP A 240 3033 4251 2650 -398 564 161 N ATOM 1872 CA ASP A 240 88.380 31.966 25.678 1.00 29.09 C ANISOU 1872 CA ASP A 240 3413 4564 3075 -481 205 457 C ATOM 1873 C ASP A 240 87.734 31.672 27.024 1.00 28.66 C ANISOU 1873 C ASP A 240 3324 4458 3108 105 229 659 C ATOM 1874 O ASP A 240 86.530 31.868 27.193 1.00 28.38 O ANISOU 1874 O ASP A 240 3477 3970 3336 387 396 598 O ATOM 1875 CB ASP A 240 89.489 32.984 25.842 1.00 29.89 C ANISOU 1875 CB ASP A 240 3770 4689 2899 -685 -195 549 C ATOM 1876 CG ASP A 240 89.104 34.277 26.495 1.00 31.16 C ANISOU 1876 CG ASP A 240 4159 4670 3010 -564 -486 520 C ATOM 1877 OD1 ASP A 240 87.933 34.503 26.852 1.00 32.48 O ANISOU 1877 OD1 ASP A 240 4104 4798 3439 -167 -804 258 O ATOM 1878 OD2 ASP A 240 90.034 35.097 26.653 1.00 31.57 O ANISOU 1878 OD2 ASP A 240 4681 4817 2497 -942 -278 564 O ATOM 1879 N GLU A 241 88.524 31.194 27.973 1.00 29.71 N ANISOU 1879 N GLU A 241 3604 4350 3333 116 44 789 N ATOM 1880 CA GLU A 241 87.933 30.805 29.270 1.00 31.31 C ANISOU 1880 CA GLU A 241 4200 4568 3129 131 101 643 C ATOM 1881 C GLU A 241 87.327 31.955 30.054 1.00 29.43 C ANISOU 1881 C GLU A 241 3646 4509 3026 -128 -340 422 C ATOM 1882 O GLU A 241 86.179 31.859 30.523 1.00 29.66 O ANISOU 1882 O GLU A 241 4029 4344 2898 -75 59 731 O ATOM 1883 CB GLU A 241 89.010 30.086 30.101 1.00 31.59 C ANISOU 1883 CB GLU A 241 4093 5054 2857 382 334 599 C ATOM 1884 CG GLU A 241 88.609 29.822 31.545 1.00 39.18 C ANISOU 1884 CG GLU A 241 6070 5726 3091 -330 353 1361 C ATOM 1885 CD GLU A 241 89.777 29.153 32.259 1.00 49.17 C ANISOU 1885 CD GLU A 241 8485 5771 4425 -723 -2413 1325 C ATOM 1886 OE1 GLU A 241 90.005 27.960 31.975 1.00 58.40 O ANISOU 1886 OE1 GLU A 241 8545 5563 8081 -181 -2846 1624 O ATOM 1887 OE2 GLU A 241 90.468 29.813 33.072 1.00 68.54 O ANISOU 1887 OE2 GLU A 241 9711 9225 7105 -1444 -3487 -521 O ATOM 1888 N PRO A 242 88.008 33.080 30.278 1.00 30.69 N ANISOU 1888 N PRO A 242 4110 4639 2911 -380 -720 663 N ATOM 1889 CA PRO A 242 87.419 34.152 31.074 1.00 31.27 C ANISOU 1889 CA PRO A 242 4644 4100 3136 -448 -489 889 C ATOM 1890 C PRO A 242 86.111 34.682 30.492 1.00 29.98 C ANISOU 1890 C PRO A 242 4208 4477 2705 -484 -265 214 C ATOM 1891 O PRO A 242 85.293 35.216 31.265 1.00 31.45 O ANISOU 1891 O PRO A 242 4778 4586 2587 -409 303 684 O ATOM 1892 CB PRO A 242 88.448 35.274 31.029 1.00 33.73 C ANISOU 1892 CB PRO A 242 4340 4658 3819 -618 -690 612 C ATOM 1893 CG PRO A 242 89.691 34.704 30.428 1.00 34.64 C ANISOU 1893 CG PRO A 242 4523 4941 3700 -700 -610 174 C ATOM 1894 CD PRO A 242 89.376 33.376 29.835 1.00 34.24 C ANISOU 1894 CD PRO A 242 5007 5146 2856 -1301 125 244 C ATOM 1895 N SER A 243 85.896 34.567 29.185 1.00 29.23 N ANISOU 1895 N SER A 243 3971 4416 2718 -540 -182 61 N ATOM 1896 CA SER A 243 84.654 35.076 28.605 1.00 27.31 C ANISOU 1896 CA SER A 243 3917 4111 2349 -525 14 50 C ATOM 1897 C SER A 243 83.433 34.240 28.987 1.00 27.62 C ANISOU 1897 C SER A 243 3848 3712 2935 -250 285 29 C ATOM 1898 O SER A 243 82.292 34.661 28.769 1.00 26.17 O ANISOU 1898 O SER A 243 3898 3493 2554 -331 352 425 O ATOM 1899 CB SER A 243 84.787 35.128 27.074 1.00 29.73 C ANISOU 1899 CB SER A 243 4950 3969 2378 -585 1 256 C ATOM 1900 OG SER A 243 84.650 33.816 26.526 1.00 27.83 O ANISOU 1900 OG SER A 243 3599 4346 2629 -370 39 -250 O ATOM 1901 N THR A 244 83.649 33.044 29.542 1.00 26.75 N ANISOU 1901 N THR A 244 3617 3871 2676 -168 129 104 N ATOM 1902 CA THR A 244 82.542 32.131 29.808 1.00 27.91 C ANISOU 1902 CA THR A 244 4136 3994 2473 -596 -30 87 C ATOM 1903 C THR A 244 81.912 32.314 31.190 1.00 25.34 C ANISOU 1903 C THR A 244 3259 3619 2751 131 26 212 C ATOM 1904 O THR A 244 81.070 31.469 31.534 1.00 30.29 O ANISOU 1904 O THR A 244 4601 4276 2633 -678 -13 649 O ATOM 1905 CB THR A 244 82.956 30.643 29.727 1.00 28.25 C ANISOU 1905 CB THR A 244 4132 4062 2537 -640 618 -320 C ATOM 1906 OG1 THR A 244 83.943 30.388 30.745 1.00 31.66 O ANISOU 1906 OG1 THR A 244 4688 4038 3302 -486 317 809 O ATOM 1907 CG2 THR A 244 83.560 30.269 28.372 1.00 32.74 C ANISOU 1907 CG2 THR A 244 4748 4681 3012 -1123 1583 -177 C ATOM 1908 N MET A 245 82.276 33.335 31.947 1.00 27.73 N ANISOU 1908 N MET A 245 3833 3638 3063 254 323 -141 N ATOM 1909 CA MET A 245 81.905 33.532 33.347 1.00 29.15 C ANISOU 1909 CA MET A 245 3841 4124 3111 -106 489 -229 C ATOM 1910 C MET A 245 80.398 33.581 33.597 1.00 28.19 C ANISOU 1910 C MET A 245 3793 3985 2932 -127 329 146 C ATOM 1911 O MET A 245 79.916 33.168 34.667 1.00 28.07 O ANISOU 1911 O MET A 245 3395 4168 3100 -545 -121 637 O ATOM 1912 CB MET A 245 82.509 34.835 33.924 1.00 32.08 C ANISOU 1912 CB MET A 245 4907 4979 2302 -1388 557 16 C ATOM 1913 CG MET A 245 83.999 34.771 34.202 1.00 33.99 C ANISOU 1913 CG MET A 245 4894 4983 3038 -1511 528 382 C ATOM 1914 SD MET A 245 84.508 33.426 35.299 1.00 43.11 S ANISOU 1914 SD MET A 245 7059 5708 3614 -496 -528 370 S ATOM 1915 CE MET A 245 85.039 32.144 34.169 1.00 42.86 C ANISOU 1915 CE MET A 245 5039 5972 5272 -297 -1271 -500 C ATOM 1916 N GLU A 246 79.612 34.102 32.661 1.00 27.84 N ANISOU 1916 N GLU A 246 3908 3836 2832 -253 438 416 N ATOM 1917 CA GLU A 246 78.184 34.274 32.899 1.00 27.58 C ANISOU 1917 CA GLU A 246 3866 3777 2835 -124 306 269 C ATOM 1918 C GLU A 246 77.371 33.130 32.317 1.00 27.70 C ANISOU 1918 C GLU A 246 3831 3611 3081 5 87 364 C ATOM 1919 O GLU A 246 76.137 33.153 32.416 1.00 30.01 O ANISOU 1919 O GLU A 246 3882 4391 3127 -343 502 121 O ATOM 1920 CB GLU A 246 77.728 35.598 32.286 1.00 26.55 C ANISOU 1920 CB GLU A 246 3614 3741 2732 -456 483 478 C ATOM 1921 CG GLU A 246 78.421 36.801 32.924 1.00 29.45 C ANISOU 1921 CG GLU A 246 4390 3866 2933 -516 254 251 C ATOM 1922 CD GLU A 246 77.791 37.207 34.238 1.00 29.68 C ANISOU 1922 CD GLU A 246 3787 4147 3342 -285 257 -45 C ATOM 1923 OE1 GLU A 246 76.811 36.545 34.661 1.00 32.95 O ANISOU 1923 OE1 GLU A 246 4022 4907 3589 -275 356 926 O ATOM 1924 OE2 GLU A 246 78.267 38.187 34.855 1.00 32.32 O ANISOU 1924 OE2 GLU A 246 4831 3772 3677 228 -161 -223 O ATOM 1925 N LEU A 247 78.012 32.130 31.714 1.00 27.85 N ANISOU 1925 N LEU A 247 4243 3797 2543 -168 485 316 N ATOM 1926 CA LEU A 247 77.262 30.983 31.189 1.00 26.84 C ANISOU 1926 CA LEU A 247 4342 3880 1975 -95 222 389 C ATOM 1927 C LEU A 247 76.912 29.986 32.275 1.00 28.12 C ANISOU 1927 C LEU A 247 4599 4000 2084 -399 350 412 C ATOM 1928 O LEU A 247 77.640 29.934 33.271 1.00 27.40 O ANISOU 1928 O LEU A 247 4793 3795 1823 -571 446 390 O ATOM 1929 CB LEU A 247 78.070 30.238 30.112 1.00 26.12 C ANISOU 1929 CB LEU A 247 3883 3889 2151 -158 258 429 C ATOM 1930 CG LEU A 247 78.419 31.038 28.857 1.00 27.37 C ANISOU 1930 CG LEU A 247 4202 4010 2188 143 419 533 C ATOM 1931 CD1 LEU A 247 79.262 30.164 27.924 1.00 25.57 C ANISOU 1931 CD1 LEU A 247 2934 4540 2240 -178 83 230 C ATOM 1932 CD2 LEU A 247 77.146 31.524 28.195 1.00 24.81 C ANISOU 1932 CD2 LEU A 247 3837 3233 2357 45 816 662 C ATOM 1933 N LYS A 248 75.879 29.175 32.112 1.00 28.25 N ANISOU 1933 N LYS A 248 4041 4115 2577 -83 270 586 N ATOM 1934 CA LYS A 248 75.720 28.091 33.086 1.00 27.77 C ANISOU 1934 CA LYS A 248 3864 3955 2733 -359 -276 579 C ATOM 1935 C LYS A 248 76.762 27.004 32.831 1.00 27.06 C ANISOU 1935 C LYS A 248 3758 4145 2381 -282 -377 518 C ATOM 1936 O LYS A 248 77.162 26.781 31.684 1.00 27.94 O ANISOU 1936 O LYS A 248 3636 4469 2510 -630 -64 591 O ATOM 1937 CB LYS A 248 74.351 27.443 33.053 1.00 27.56 C ANISOU 1937 CB LYS A 248 3811 4018 2643 -336 130 12 C ATOM 1938 CG LYS A 248 73.190 28.346 33.462 1.00 30.94 C ANISOU 1938 CG LYS A 248 3946 4092 3718 324 -465 382 C ATOM 1939 CD LYS A 248 71.915 27.543 33.205 1.00 36.79 C ANISOU 1939 CD LYS A 248 3777 4469 5732 267 -268 248 C ATOM 1940 CE LYS A 248 70.673 28.389 33.453 1.00 41.56 C ANISOU 1940 CE LYS A 248 3895 5194 6701 316 1231 655 C ATOM 1941 NZ LYS A 248 69.759 27.654 34.388 1.00 64.44 N ANISOU 1941 NZ LYS A 248 7675 7829 8980 -1186 4287 57 N ATOM 1942 N VAL A 249 77.185 26.347 33.893 1.00 27.82 N ANISOU 1942 N VAL A 249 4064 3966 2541 -418 -418 653 N ATOM 1943 CA VAL A 249 78.122 25.231 33.803 1.00 29.14 C ANISOU 1943 CA VAL A 249 4339 3867 2865 -364 -622 687 C ATOM 1944 C VAL A 249 77.633 24.217 32.792 1.00 29.69 C ANISOU 1944 C VAL A 249 4243 4183 2856 -604 51 363 C ATOM 1945 O VAL A 249 78.388 23.665 31.988 1.00 29.65 O ANISOU 1945 O VAL A 249 4190 4321 2753 -180 -49 692 O ATOM 1946 CB VAL A 249 78.284 24.601 35.205 1.00 30.17 C ANISOU 1946 CB VAL A 249 4621 3819 3023 -532 -573 890 C ATOM 1947 CG1 VAL A 249 78.980 23.251 35.111 1.00 29.07 C ANISOU 1947 CG1 VAL A 249 5318 3551 2176 -649 -309 701 C ATOM 1948 CG2 VAL A 249 79.044 25.530 36.142 1.00 24.16 C ANISOU 1948 CG2 VAL A 249 3130 3405 2647 514 -231 679 C ATOM 1949 N LYS A 250 76.341 23.906 32.764 1.00 27.54 N ANISOU 1949 N LYS A 250 3970 4005 2488 39 -519 338 N ATOM 1950 CA LYS A 250 75.908 22.857 31.819 1.00 27.82 C ANISOU 1950 CA LYS A 250 4165 3806 2600 -394 167 308 C ATOM 1951 C LYS A 250 75.968 23.308 30.362 1.00 27.22 C ANISOU 1951 C LYS A 250 4222 3668 2452 -25 224 26 C ATOM 1952 O LYS A 250 76.099 22.493 29.422 1.00 28.24 O ANISOU 1952 O LYS A 250 3419 4438 2873 -240 412 -535 O ATOM 1953 CB LYS A 250 74.481 22.404 32.126 1.00 30.23 C ANISOU 1953 CB LYS A 250 4164 4250 3073 -540 123 477 C ATOM 1954 CG LYS A 250 73.466 23.546 31.972 1.00 31.70 C ANISOU 1954 CG LYS A 250 4092 4896 3057 -244 -261 487 C ATOM 1955 CD LYS A 250 72.072 22.932 32.125 1.00 35.06 C ANISOU 1955 CD LYS A 250 4216 5425 3681 -254 811 324 C ATOM 1956 CE LYS A 250 70.983 23.954 31.861 1.00 36.44 C ANISOU 1956 CE LYS A 250 4030 6135 3681 24 798 111 C ATOM 1957 NZ LYS A 250 69.643 23.340 32.082 1.00 41.29 N ANISOU 1957 NZ LYS A 250 4044 7263 4381 -820 -949 157 N ATOM 1958 N THR A 251 75.849 24.619 30.149 1.00 27.37 N ANISOU 1958 N THR A 251 3712 3797 2891 137 196 475 N ATOM 1959 CA THR A 251 75.942 25.148 28.794 1.00 31.40 C ANISOU 1959 CA THR A 251 4784 4275 2872 -274 472 537 C ATOM 1960 C THR A 251 77.360 24.971 28.272 1.00 29.52 C ANISOU 1960 C THR A 251 4861 3738 2619 -202 455 249 C ATOM 1961 O THR A 251 77.569 24.524 27.146 1.00 32.25 O ANISOU 1961 O THR A 251 5614 3891 2749 -72 548 83 O ATOM 1962 CB THR A 251 75.602 26.647 28.776 1.00 28.46 C ANISOU 1962 CB THR A 251 4228 4524 2061 80 99 797 C ATOM 1963 OG1 THR A 251 74.266 26.806 29.251 1.00 29.70 O ANISOU 1963 OG1 THR A 251 4389 4539 2356 -373 456 437 O ATOM 1964 CG2 THR A 251 75.671 27.194 27.348 1.00 31.07 C ANISOU 1964 CG2 THR A 251 5112 4743 1949 -1025 259 640 C ATOM 1965 N LEU A 252 78.323 25.339 29.124 1.00 29.85 N ANISOU 1965 N LEU A 252 4893 3879 2568 -589 377 794 N ATOM 1966 CA LEU A 252 79.731 25.217 28.739 1.00 34.76 C ANISOU 1966 CA LEU A 252 4921 5004 3281 -1060 667 206 C ATOM 1967 C LEU A 252 80.078 23.750 28.543 1.00 33.21 C ANISOU 1967 C LEU A 252 3835 5125 3657 -622 356 619 C ATOM 1968 O LEU A 252 80.767 23.346 27.598 1.00 35.21 O ANISOU 1968 O LEU A 252 4810 5168 3402 -383 402 545 O ATOM 1969 CB LEU A 252 80.605 25.937 29.773 1.00 36.74 C ANISOU 1969 CB LEU A 252 5077 5825 3058 -1259 574 306 C ATOM 1970 CG LEU A 252 82.089 26.095 29.441 1.00 39.19 C ANISOU 1970 CG LEU A 252 5216 5905 3768 -1667 697 -49 C ATOM 1971 CD1 LEU A 252 82.286 26.867 28.127 1.00 34.52 C ANISOU 1971 CD1 LEU A 252 4461 5526 3128 -1047 903 -630 C ATOM 1972 CD2 LEU A 252 82.854 26.724 30.607 1.00 35.04 C ANISOU 1972 CD2 LEU A 252 4735 5034 3545 -297 241 214 C ATOM 1973 N ARG A 253 79.591 22.864 29.407 1.00 36.36 N ANISOU 1973 N ARG A 253 5121 5135 3561 -1103 453 433 N ATOM 1974 CA ARG A 253 79.812 21.421 29.300 1.00 38.59 C ANISOU 1974 CA ARG A 253 6027 5184 3451 -732 264 695 C ATOM 1975 C ARG A 253 79.210 20.825 28.029 1.00 38.93 C ANISOU 1975 C ARG A 253 6532 4733 3528 -872 285 679 C ATOM 1976 O ARG A 253 79.802 19.959 27.370 1.00 43.82 O ANISOU 1976 O ARG A 253 8345 4533 3773 -354 382 699 O ATOM 1977 CB ARG A 253 79.255 20.725 30.570 1.00 39.74 C ANISOU 1977 CB ARG A 253 6022 5503 3574 -39 425 1090 C ATOM 1978 CG ARG A 253 79.394 19.219 30.487 1.00 54.89 C ANISOU 1978 CG ARG A 253 9916 5416 5523 -414 1567 1488 C ATOM 1979 CD ARG A 253 78.613 18.467 31.551 1.00 78.02 C ANISOU 1979 CD ARG A 253 15665 7538 6442 -2471 1999 2875 C ATOM 1980 NE ARG A 253 79.551 17.781 32.452 1.00 91.76 N ANISOU 1980 NE ARG A 253 18216 8596 8054 -2693 518 4537 N ATOM 1981 CZ ARG A 253 79.765 16.482 32.543 1.00 97.65 C ANISOU 1981 CZ ARG A 253 19916 8465 8723 -3233 -1149 4968 C ATOM 1982 NH1 ARG A 253 79.099 15.606 31.802 1.00111.61 N ANISOU 1982 NH1 ARG A 253 22556 9699 10151 -3763 -1219 3091 N ATOM 1983 NH2 ARG A 253 80.668 16.038 33.420 1.00109.51 N ANISOU 1983 NH2 ARG A 253 21238 10420 9950 -2615 -1744 6339 N ATOM 1984 N TYR A 254 78.012 21.270 27.644 1.00 37.12 N ANISOU 1984 N TYR A 254 6131 4846 3126 -1609 379 1414 N ATOM 1985 CA TYR A 254 77.348 20.836 26.422 1.00 35.87 C ANISOU 1985 CA TYR A 254 5615 4834 3181 -1309 945 472 C ATOM 1986 C TYR A 254 78.167 21.119 25.162 1.00 37.91 C ANISOU 1986 C TYR A 254 6403 4597 3404 -1551 1324 326 C ATOM 1987 O TYR A 254 78.370 20.271 24.269 1.00 40.95 O ANISOU 1987 O TYR A 254 6914 4843 3804 -1788 1812 35 O ATOM 1988 CB TYR A 254 75.983 21.529 26.302 1.00 36.39 C ANISOU 1988 CB TYR A 254 5681 4772 3376 -1304 537 241 C ATOM 1989 CG TYR A 254 75.307 21.303 24.957 1.00 38.96 C ANISOU 1989 CG TYR A 254 6344 4956 3504 -1260 251 145 C ATOM 1990 CD1 TYR A 254 74.753 20.061 24.641 1.00 39.58 C ANISOU 1990 CD1 TYR A 254 6319 5114 3605 -1409 243 101 C ATOM 1991 CD2 TYR A 254 75.210 22.317 24.002 1.00 38.99 C ANISOU 1991 CD2 TYR A 254 6008 5015 3791 -1020 -21 264 C ATOM 1992 CE1 TYR A 254 74.129 19.833 23.423 1.00 39.41 C ANISOU 1992 CE1 TYR A 254 5976 4999 3999 -1329 -150 339 C ATOM 1993 CE2 TYR A 254 74.590 22.103 22.782 1.00 38.40 C ANISOU 1993 CE2 TYR A 254 5911 4858 3822 -1107 9 202 C ATOM 1994 CZ TYR A 254 74.052 20.861 22.499 1.00 40.32 C ANISOU 1994 CZ TYR A 254 6003 4892 4425 -1207 -391 446 C ATOM 1995 OH TYR A 254 73.431 20.620 21.299 1.00 45.13 O ANISOU 1995 OH TYR A 254 8431 4773 3942 -2493 -374 763 O ATOM 1996 N PHE A 255 78.649 22.372 25.067 1.00 35.08 N ANISOU 1996 N PHE A 255 5750 4409 3169 -1228 493 761 N ATOM 1997 CA PHE A 255 79.400 22.733 23.868 1.00 35.31 C ANISOU 1997 CA PHE A 255 6118 3955 3345 -899 881 713 C ATOM 1998 C PHE A 255 80.796 22.128 23.912 1.00 37.20 C ANISOU 1998 C PHE A 255 6690 3719 3723 -226 1206 146 C ATOM 1999 O PHE A 255 81.373 21.825 22.863 1.00 43.90 O ANISOU 1999 O PHE A 255 7467 5107 4107 -410 1880 93 O ATOM 2000 CB PHE A 255 79.498 24.256 23.723 1.00 30.76 C ANISOU 2000 CB PHE A 255 5648 3871 2168 -513 606 429 C ATOM 2001 CG PHE A 255 78.162 24.856 23.311 1.00 32.15 C ANISOU 2001 CG PHE A 255 5329 4350 2537 -747 575 341 C ATOM 2002 CD1 PHE A 255 77.716 24.705 22.005 1.00 32.72 C ANISOU 2002 CD1 PHE A 255 5091 4551 2790 -971 383 146 C ATOM 2003 CD2 PHE A 255 77.369 25.556 24.201 1.00 33.72 C ANISOU 2003 CD2 PHE A 255 5637 4575 2600 -310 721 593 C ATOM 2004 CE1 PHE A 255 76.496 25.240 21.597 1.00 33.26 C ANISOU 2004 CE1 PHE A 255 5722 4267 2648 -363 397 298 C ATOM 2005 CE2 PHE A 255 76.157 26.092 23.806 1.00 33.15 C ANISOU 2005 CE2 PHE A 255 5674 4244 2679 -442 398 229 C ATOM 2006 CZ PHE A 255 75.711 25.951 22.500 1.00 33.28 C ANISOU 2006 CZ PHE A 255 5897 4050 2699 -507 396 102 C ATOM 2007 N ASN A 256 81.343 21.963 25.114 1.00 37.09 N ANISOU 2007 N ASN A 256 6241 3836 4015 42 1174 699 N ATOM 2008 CA ASN A 256 82.661 21.357 25.239 1.00 42.58 C ANISOU 2008 CA ASN A 256 6272 5204 4702 471 1442 342 C ATOM 2009 C ASN A 256 82.592 19.903 24.788 1.00 43.82 C ANISOU 2009 C ASN A 256 5694 5102 5854 798 1520 286 C ATOM 2010 O ASN A 256 83.600 19.432 24.256 1.00 49.55 O ANISOU 2010 O ASN A 256 5990 5059 7777 1151 2251 909 O ATOM 2011 CB ASN A 256 83.235 21.413 26.654 1.00 45.84 C ANISOU 2011 CB ASN A 256 7020 5227 5172 1072 563 854 C ATOM 2012 CG ASN A 256 84.190 22.586 26.798 1.00 51.15 C ANISOU 2012 CG ASN A 256 7453 6339 5643 319 -365 978 C ATOM 2013 OD1 ASN A 256 85.303 22.619 26.255 1.00 63.15 O ANISOU 2013 OD1 ASN A 256 7543 8146 8305 -609 370 -352 O ATOM 2014 ND2 ASN A 256 83.738 23.593 27.526 1.00 59.01 N ANISOU 2014 ND2 ASN A 256 10319 7443 4660 -2024 1467 -407 N ATOM 2015 N GLU A 257 81.444 19.251 24.989 1.00 43.26 N ANISOU 2015 N GLU A 257 6315 5509 4613 250 2117 -95 N ATOM 2016 CA GLU A 257 81.359 17.869 24.506 1.00 46.91 C ANISOU 2016 CA GLU A 257 6788 5798 5238 -98 2812 -601 C ATOM 2017 C GLU A 257 81.031 17.825 23.022 1.00 49.57 C ANISOU 2017 C GLU A 257 8194 5336 5303 -921 2507 -405 C ATOM 2018 O GLU A 257 81.597 17.070 22.218 1.00 49.09 O ANISOU 2018 O GLU A 257 8394 5604 4654 -481 2513 81 O ATOM 2019 CB GLU A 257 80.352 17.113 25.389 1.00 57.48 C ANISOU 2019 CB GLU A 257 9569 6628 5642 -1616 3645 -717 C ATOM 2020 CG GLU A 257 80.802 17.137 26.859 1.00 69.57 C ANISOU 2020 CG GLU A 257 11906 8594 5933 -2785 2731 806 C ATOM 2021 CD GLU A 257 79.874 16.391 27.790 1.00 79.02 C ANISOU 2021 CD GLU A 257 13844 9722 6456 -4129 2561 1566 C ATOM 2022 OE1 GLU A 257 78.735 16.101 27.351 1.00 96.05 O ANISOU 2022 OE1 GLU A 257 16292 11402 8801 -8311 1429 2019 O ATOM 2023 OE2 GLU A 257 80.248 16.074 28.949 1.00 89.60 O ANISOU 2023 OE2 GLU A 257 17551 9594 6899 -4298 1870 2295 O ATOM 2024 N LEU A 258 80.094 18.649 22.565 1.00 47.38 N ANISOU 2024 N LEU A 258 8517 4891 4593 -940 2611 -410 N ATOM 2025 CA LEU A 258 79.724 18.661 21.164 1.00 50.87 C ANISOU 2025 CA LEU A 258 9305 5186 4839 -1285 2010 -881 C ATOM 2026 C LEU A 258 80.864 19.041 20.229 1.00 50.46 C ANISOU 2026 C LEU A 258 9888 5220 4064 -1167 1960 -398 C ATOM 2027 O LEU A 258 80.872 18.711 19.039 1.00 56.43 O ANISOU 2027 O LEU A 258 11745 5327 4367 -475 2277 -1063 O ATOM 2028 CB LEU A 258 78.558 19.652 21.020 1.00 51.82 C ANISOU 2028 CB LEU A 258 9073 5350 5265 -1419 867 -1596 C ATOM 2029 CG LEU A 258 77.984 19.815 19.610 1.00 55.99 C ANISOU 2029 CG LEU A 258 10130 5524 5618 -1907 118 -1687 C ATOM 2030 CD1 LEU A 258 77.296 18.525 19.192 1.00 64.99 C ANISOU 2030 CD1 LEU A 258 12598 5423 6671 -2252 -809 -1670 C ATOM 2031 CD2 LEU A 258 77.008 20.980 19.526 1.00 50.86 C ANISOU 2031 CD2 LEU A 258 8474 5253 5598 -2781 244 -1079 C ATOM 2032 N GLU A 259 81.883 19.768 20.691 1.00 46.86 N ANISOU 2032 N GLU A 259 8842 4555 4407 -487 1357 1040 N ATOM 2033 CA GLU A 259 82.857 20.303 19.732 1.00 45.60 C ANISOU 2033 CA GLU A 259 8904 4446 3977 14 1545 864 C ATOM 2034 C GLU A 259 84.230 19.728 20.030 1.00 49.17 C ANISOU 2034 C GLU A 259 8743 5471 4468 -133 1080 653 C ATOM 2035 O GLU A 259 85.254 20.143 19.482 1.00 48.07 O ANISOU 2035 O GLU A 259 8710 5793 3760 -122 724 1091 O ATOM 2036 CB GLU A 259 82.815 21.840 19.803 1.00 46.80 C ANISOU 2036 CB GLU A 259 8304 4519 4958 -451 4472 -385 C ATOM 2037 CG GLU A 259 82.985 22.490 18.422 1.00 57.76 C ANISOU 2037 CG GLU A 259 11515 4176 6255 -917 2905 1180 C ATOM 2038 CD GLU A 259 81.660 22.721 17.729 1.00 55.12 C ANISOU 2038 CD GLU A 259 11185 3572 6186 -78 3406 341 C ATOM 2039 OE1 GLU A 259 81.465 22.212 16.628 1.00 65.96 O ANISOU 2039 OE1 GLU A 259 14529 6178 4355 450 2391 1987 O ATOM 2040 OE2 GLU A 259 80.749 23.363 18.279 1.00 69.79 O ANISOU 2040 OE2 GLU A 259 9600 4789 12129 -2508 6009 -1473 O ATOM 2041 N ALA A 260 84.245 18.744 20.948 1.00 44.52 N ANISOU 2041 N ALA A 260 7647 4863 4406 659 1995 297 N ATOM 2042 CA ALA A 260 85.509 18.182 21.408 1.00 46.86 C ANISOU 2042 CA ALA A 260 7440 5203 5160 694 2246 501 C ATOM 2043 C ALA A 260 86.444 17.748 20.285 1.00 49.08 C ANISOU 2043 C ALA A 260 7882 5158 5608 701 2566 260 C ATOM 2044 O ALA A 260 87.649 17.988 20.320 1.00 49.48 O ANISOU 2044 O ALA A 260 7474 4853 6474 1891 2292 -515 O ATOM 2045 CB ALA A 260 85.258 16.981 22.319 1.00 45.90 C ANISOU 2045 CB ALA A 260 7330 5013 5096 694 1846 434 C ATOM 2046 N GLU A 261 85.893 17.092 19.277 1.00 49.76 N ANISOU 2046 N GLU A 261 8015 5128 5762 1212 2289 43 N ATOM 2047 CA GLU A 261 86.736 16.521 18.224 1.00 58.83 C ANISOU 2047 CA GLU A 261 10236 5801 6317 766 3757 -241 C ATOM 2048 C GLU A 261 87.360 17.634 17.388 1.00 57.24 C ANISOU 2048 C GLU A 261 9715 5717 6317 1168 3269 162 C ATOM 2049 O GLU A 261 88.403 17.481 16.753 1.00 52.72 O ANISOU 2049 O GLU A 261 9668 4880 5484 1062 2959 9 O ATOM 2050 CB GLU A 261 85.922 15.583 17.339 1.00 65.59 C ANISOU 2050 CB GLU A 261 11761 5403 7757 725 3823 -1336 C ATOM 2051 CG GLU A 261 86.134 14.097 17.498 1.00 78.63 C ANISOU 2051 CG GLU A 261 14955 5645 9274 230 1777 93 C ATOM 2052 CD GLU A 261 87.268 13.613 18.382 1.00 90.73 C ANISOU 2052 CD GLU A 261 17714 6934 9826 -99 89 1602 C ATOM 2053 OE1 GLU A 261 88.399 13.366 17.892 1.00 93.00 O ANISOU 2053 OE1 GLU A 261 17444 7105 10786 2597 -995 2857 O ATOM 2054 OE2 GLU A 261 87.040 13.449 19.608 1.00105.06 O ANISOU 2054 OE2 GLU A 261 22097 7991 9831 -725 257 1875 O ATOM 2055 N ASN A 262 86.651 18.762 17.426 1.00 55.39 N ANISOU 2055 N ASN A 262 8542 6013 6493 1073 2350 -29 N ATOM 2056 CA ASN A 262 86.991 19.905 16.595 1.00 49.60 C ANISOU 2056 CA ASN A 262 7153 5570 6124 1345 2237 -416 C ATOM 2057 C ASN A 262 87.940 20.867 17.278 1.00 51.02 C ANISOU 2057 C ASN A 262 6661 6390 6334 1264 2201 -590 C ATOM 2058 O ASN A 262 88.324 21.873 16.677 1.00 50.52 O ANISOU 2058 O ASN A 262 5771 7727 5697 206 2684 -634 O ATOM 2059 CB ASN A 262 85.718 20.689 16.217 1.00 44.56 C ANISOU 2059 CB ASN A 262 6658 5448 4826 1299 2615 -1416 C ATOM 2060 CG ASN A 262 84.710 19.810 15.506 1.00 50.37 C ANISOU 2060 CG ASN A 262 7736 5882 5522 772 1870 -1257 C ATOM 2061 OD1 ASN A 262 85.077 19.090 14.579 1.00 60.86 O ANISOU 2061 OD1 ASN A 262 7865 6632 8626 255 2311 -3505 O ATOM 2062 ND2 ASN A 262 83.451 19.837 15.906 1.00 53.11 N ANISOU 2062 ND2 ASN A 262 7280 5719 7181 968 1356 -2464 N ATOM 2063 N ILE A 263 88.316 20.619 18.533 1.00 54.88 N ANISOU 2063 N ILE A 263 7854 6657 6339 921 1957 -511 N ATOM 2064 CA ILE A 263 89.177 21.678 19.087 1.00 58.84 C ANISOU 2064 CA ILE A 263 9072 7101 6182 199 1693 -315 C ATOM 2065 C ILE A 263 90.545 21.106 19.398 1.00 61.53 C ANISOU 2065 C ILE A 263 8805 8054 6522 -134 1228 -518 C ATOM 2066 O ILE A 263 91.336 21.639 20.169 1.00 73.30 O ANISOU 2066 O ILE A 263 11969 8937 6945 -1392 -1345 1505 O ATOM 2067 CB ILE A 263 88.531 22.303 20.318 1.00 60.11 C ANISOU 2067 CB ILE A 263 9075 7875 5889 -323 1516 -647 C ATOM 2068 CG1 ILE A 263 88.210 21.279 21.407 1.00 60.97 C ANISOU 2068 CG1 ILE A 263 8141 8593 6432 -189 1709 -123 C ATOM 2069 CG2 ILE A 263 87.258 23.047 19.961 1.00 53.81 C ANISOU 2069 CG2 ILE A 263 7700 7705 5041 -1213 2539 -212 C ATOM 2070 CD1 ILE A 263 86.750 21.421 21.809 1.00 73.31 C ANISOU 2070 CD1 ILE A 263 6995 13184 7674 -2081 804 -698 C ATOM 2071 N LYS A 264 90.837 19.976 18.763 1.00 68.81 N ANISOU 2071 N LYS A 264 9647 7885 8611 823 2206 -294 N ATOM 2072 CA LYS A 264 92.183 19.410 18.876 1.00 76.55 C ANISOU 2072 CA LYS A 264 9629 8575 10881 860 1904 544 C ATOM 2073 C LYS A 264 93.107 19.942 17.785 1.00 77.52 C ANISOU 2073 C LYS A 264 8825 8920 11709 1188 1942 1056 C ATOM 2074 O LYS A 264 92.738 20.190 16.639 1.00 75.36 O ANISOU 2074 O LYS A 264 8680 8512 11443 798 2272 1025 O ATOM 2075 CB LYS A 264 92.104 17.880 18.836 1.00 76.51 C ANISOU 2075 CB LYS A 264 8786 8559 11725 1096 2521 342 C ATOM 2076 CG LYS A 264 90.858 17.295 19.487 1.00 80.69 C ANISOU 2076 CG LYS A 264 9279 9173 12207 413 2836 -39 C ATOM 2077 CD LYS A 264 90.734 15.807 19.187 1.00 78.42 C ANISOU 2077 CD LYS A 264 8394 9101 12301 798 3041 -22 C ATOM 2078 CE LYS A 264 90.295 15.052 20.433 1.00 78.43 C ANISOU 2078 CE LYS A 264 8762 8938 12101 682 3169 -309 C ATOM 2079 NZ LYS A 264 89.480 15.915 21.333 1.00 84.34 N ANISOU 2079 NZ LYS A 264 9861 10332 11853 -92 2924 -2156 N ATOM 2080 N GLY A 265 94.376 20.135 18.141 1.00 83.82 N ANISOU 2080 N GLY A 265 9209 9687 12953 641 1313 1474 N ATOM 2081 CA GLY A 265 95.358 20.599 17.170 1.00 83.43 C ANISOU 2081 CA GLY A 265 8380 9797 13523 1086 1098 2205 C ATOM 2082 C GLY A 265 95.291 22.114 17.043 1.00 87.07 C ANISOU 2082 C GLY A 265 9740 9860 13482 955 155 2653 C ATOM 2083 O GLY A 265 96.301 22.797 17.224 1.00 86.51 O ANISOU 2083 O GLY A 265 9490 9550 13831 1140 650 2459 O ATOM 2084 N LEU A 266 94.083 22.576 16.740 1.00 87.12 N ANISOU 2084 N LEU A 266 10153 9542 13408 970 -584 2410 N ATOM 2085 CA LEU A 266 93.773 23.993 16.591 1.00 89.29 C ANISOU 2085 CA LEU A 266 11062 9587 13277 985 -987 2797 C ATOM 2086 C LEU A 266 94.211 24.533 15.236 1.00 94.29 C ANISOU 2086 C LEU A 266 12132 10436 13258 560 -957 2916 C ATOM 2087 O LEU A 266 95.342 24.461 14.762 1.00101.99 O ANISOU 2087 O LEU A 266 13306 11900 13546 462 432 1647 O ATOM 2088 CB LEU A 266 94.404 24.784 17.740 1.00 91.54 C ANISOU 2088 CB LEU A 266 12387 9172 13221 91 -931 3141 C ATOM 2089 CG LEU A 266 93.707 24.701 19.097 1.00 90.13 C ANISOU 2089 CG LEU A 266 12137 8943 13166 180 -1012 3032 C ATOM 2090 CD1 LEU A 266 92.203 24.707 18.915 1.00 80.49 C ANISOU 2090 CD1 LEU A 266 12358 8433 9792 236 -1914 3047 C ATOM 2091 CD2 LEU A 266 94.143 23.464 19.869 1.00 86.96 C ANISOU 2091 CD2 LEU A 266 10986 9425 12628 351 -1463 2828 C ATOM 2092 OXT LEU A 266 92.687 24.863 15.393 1.00 99.16 O ANISOU 2092 OXT LEU A 266 11642 11558 14475 367 -2546 3302 O TER 2093 LEU A 266 ATOM 1 N MET A 1 65.897 50.225 15.764 1.00 38.92 N ANISOU 1 N MET B 1 5098 6097 3592 -1489 447 362 N ATOM 2 CA MET A 1 64.625 50.797 16.187 1.00 39.64 C ANISOU 2 CA MET B 1 4671 6407 3983 -879 140 -405 C ATOM 3 C MET A 1 64.917 52.150 16.820 1.00 37.92 C ANISOU 3 C MET B 1 4914 5679 3813 -933 633 -168 C ATOM 4 O MET A 1 65.930 52.269 17.535 1.00 46.58 O ANISOU 4 O MET B 1 5309 7754 4636 -2033 -63 1256 O ATOM 5 CB MET A 1 63.889 49.912 17.200 1.00 40.12 C ANISOU 5 CB MET B 1 4934 6308 4004 -354 -109 -293 C ATOM 6 CG MET A 1 62.684 50.644 17.786 1.00 43.45 C ANISOU 6 CG MET B 1 5363 6642 4505 -613 -169 -839 C ATOM 7 SD MET A 1 61.832 49.696 19.088 1.00 40.76 S ANISOU 7 SD MET B 1 5716 5321 4449 -844 351 -81 S ATOM 8 CE MET A 1 61.110 48.443 17.975 1.00 40.89 C ANISOU 8 CE MET B 1 5132 5850 4556 -1337 -1383 -497 C ATOM 9 N ARG A 2 64.072 53.136 16.569 1.00 32.45 N ANISOU 9 N ARG B 2 4810 4307 3211 -795 419 -513 N ATOM 10 CA ARG A 2 64.266 54.425 17.234 1.00 31.91 C ANISOU 10 CA ARG B 2 5037 4272 2817 -1111 367 -36 C ATOM 11 C ARG A 2 63.182 54.563 18.296 1.00 31.66 C ANISOU 11 C ARG B 2 4806 4445 2778 -1169 640 -178 C ATOM 12 O ARG A 2 62.069 54.075 18.126 1.00 35.19 O ANISOU 12 O ARG B 2 5848 4297 3224 -928 50 -345 O ATOM 13 CB ARG A 2 64.238 55.572 16.232 1.00 30.78 C ANISOU 13 CB ARG B 2 5683 3264 2747 -322 224 278 C ATOM 14 CG ARG A 2 65.289 55.506 15.130 1.00 31.74 C ANISOU 14 CG ARG B 2 6052 3464 2546 -297 -63 449 C ATOM 15 CD ARG A 2 65.058 56.599 14.088 1.00 34.98 C ANISOU 15 CD ARG B 2 6719 3922 2652 -266 253 153 C ATOM 16 NE ARG A 2 65.260 57.921 14.691 1.00 34.41 N ANISOU 16 NE ARG B 2 6379 4594 2103 -53 429 -191 N ATOM 17 CZ ARG A 2 64.894 59.068 14.154 1.00 36.03 C ANISOU 17 CZ ARG B 2 5807 4903 2981 -919 503 344 C ATOM 18 NH1 ARG A 2 64.299 59.045 12.980 1.00 40.91 N ANISOU 18 NH1 ARG B 2 6260 5762 3522 -1418 799 915 N ATOM 19 NH2 ARG A 2 65.104 60.235 14.749 1.00 34.88 N ANISOU 19 NH2 ARG B 2 5784 4351 3119 -751 335 -382 N ATOM 20 N LEU A 3 63.522 55.208 19.404 1.00 31.74 N ANISOU 20 N LEU B 3 4926 4478 2657 -969 591 -365 N ATOM 21 CA LEU A 3 62.536 55.590 20.403 1.00 30.10 C ANISOU 21 CA LEU B 3 4287 4342 2806 -471 790 -760 C ATOM 22 C LEU A 3 62.618 57.118 20.526 1.00 29.83 C ANISOU 22 C LEU B 3 4583 3777 2975 -455 909 -446 C ATOM 23 O LEU A 3 63.714 57.593 20.826 1.00 32.73 O ANISOU 23 O LEU B 3 5431 3887 3119 -772 569 -246 O ATOM 24 CB LEU A 3 62.756 54.920 21.755 1.00 28.39 C ANISOU 24 CB LEU B 3 3943 4351 2491 -526 530 -177 C ATOM 25 CG LEU A 3 61.848 55.333 22.922 1.00 30.84 C ANISOU 25 CG LEU B 3 4457 4660 2600 -868 475 -330 C ATOM 26 CD1 LEU A 3 60.404 54.985 22.640 1.00 32.59 C ANISOU 26 CD1 LEU B 3 4263 4270 3850 -374 15 -436 C ATOM 27 CD2 LEU A 3 62.262 54.648 24.214 1.00 31.39 C ANISOU 27 CD2 LEU B 3 3956 5259 2710 -90 417 -825 C ATOM 28 N ILE A 4 61.513 57.804 20.272 1.00 29.63 N ANISOU 28 N ILE B 4 4344 3841 3072 -259 982 -342 N ATOM 29 CA ILE A 4 61.485 59.258 20.403 1.00 29.55 C ANISOU 29 CA ILE B 4 4606 3487 3133 -143 936 162 C ATOM 30 C ILE A 4 60.748 59.592 21.691 1.00 30.18 C ANISOU 30 C ILE B 4 4166 4260 3043 -442 1143 178 C ATOM 31 O ILE A 4 59.506 59.525 21.761 1.00 32.25 O ANISOU 31 O ILE B 4 4551 4378 3323 -649 453 454 O ATOM 32 CB ILE A 4 60.796 59.949 19.219 1.00 27.05 C ANISOU 32 CB ILE B 4 3924 3415 2937 -176 550 63 C ATOM 33 CG1 ILE A 4 61.162 59.397 17.840 1.00 29.47 C ANISOU 33 CG1 ILE B 4 4697 3441 3059 -175 216 596 C ATOM 34 CG2 ILE A 4 61.026 61.466 19.281 1.00 27.89 C ANISOU 34 CG2 ILE B 4 4136 3481 2980 -8 132 -560 C ATOM 35 CD1 ILE A 4 62.637 59.371 17.514 1.00 33.52 C ANISOU 35 CD1 ILE B 4 5050 4991 2694 -1287 715 -196 C ATOM 36 N PRO A 5 61.468 59.900 22.757 1.00 32.38 N ANISOU 36 N PRO B 5 4856 4317 3131 -679 830 285 N ATOM 37 CA PRO A 5 60.817 60.128 24.053 1.00 30.96 C ANISOU 37 CA PRO B 5 4547 3924 3290 -305 590 340 C ATOM 38 C PRO A 5 60.421 61.595 24.178 1.00 32.73 C ANISOU 38 C PRO B 5 4676 3912 3847 7 682 -203 C ATOM 39 O PRO A 5 61.293 62.462 24.330 1.00 41.35 O ANISOU 39 O PRO B 5 5900 4187 5623 717 832 -29 O ATOM 40 CB PRO A 5 61.899 59.765 25.062 1.00 31.19 C ANISOU 40 CB PRO B 5 4759 4059 3031 -415 332 559 C ATOM 41 CG PRO A 5 63.123 59.448 24.275 1.00 36.93 C ANISOU 41 CG PRO B 5 6032 5134 2865 -1639 480 549 C ATOM 42 CD PRO A 5 62.921 60.039 22.902 1.00 33.62 C ANISOU 42 CD PRO B 5 5289 4328 3157 -800 506 366 C ATOM 43 N LEU A 6 59.118 61.835 24.100 1.00 33.33 N ANISOU 43 N LEU B 6 4570 4819 3274 -481 776 -193 N ATOM 44 CA LEU A 6 58.604 63.180 24.274 1.00 33.33 C ANISOU 44 CA LEU B 6 4731 4654 3278 -246 525 613 C ATOM 45 C LEU A 6 57.763 63.279 25.537 1.00 31.09 C ANISOU 45 C LEU B 6 4147 4368 3297 279 673 476 C ATOM 46 O LEU A 6 57.475 62.342 26.261 1.00 32.27 O ANISOU 46 O LEU B 6 4119 4542 3601 99 1150 523 O ATOM 47 CB LEU A 6 57.805 63.583 23.012 1.00 30.93 C ANISOU 47 CB LEU B 6 3860 4785 3106 349 44 1093 C ATOM 48 CG LEU A 6 58.676 63.592 21.746 1.00 32.11 C ANISOU 48 CG LEU B 6 4765 4312 3124 71 328 1115 C ATOM 49 CD1 LEU A 6 57.822 63.596 20.486 1.00 35.25 C ANISOU 49 CD1 LEU B 6 5001 5247 3147 -439 1216 761 C ATOM 50 CD2 LEU A 6 59.658 64.760 21.752 1.00 35.77 C ANISOU 50 CD2 LEU B 6 4293 4843 4453 743 779 713 C ATOM 51 N THR A 7 57.315 64.508 25.835 1.00 31.68 N ANISOU 51 N THR B 7 4224 4112 3701 321 509 420 N ATOM 52 CA THR A 7 56.554 64.733 27.054 1.00 33.08 C ANISOU 52 CA THR B 7 4689 4514 3367 118 295 845 C ATOM 53 C THR A 7 55.058 64.584 26.857 1.00 31.24 C ANISOU 53 C THR B 7 3910 4252 3706 464 192 409 C ATOM 54 O THR A 7 54.475 63.774 27.582 1.00 35.37 O ANISOU 54 O THR B 7 6266 4839 2335 243 238 189 O ATOM 55 CB THR A 7 56.853 66.139 27.608 1.00 35.77 C ANISOU 55 CB THR B 7 5099 4124 4366 201 -284 440 C ATOM 56 OG1 THR A 7 58.275 66.291 27.664 1.00 47.75 O ANISOU 56 OG1 THR B 7 8771 4110 5264 -541 -867 1016 O ATOM 57 CG2 THR A 7 56.323 66.271 29.029 1.00 37.28 C ANISOU 57 CG2 THR B 7 4307 5762 4097 -525 -261 1003 C ATOM 58 N THR A 8 54.460 65.330 25.928 1.00 30.84 N ANISOU 58 N THR B 8 4104 4019 3596 438 215 699 N ATOM 59 CA THR A 8 53.012 65.372 25.791 1.00 31.16 C ANISOU 59 CA THR B 8 4406 3978 3457 355 94 571 C ATOM 60 C THR A 8 52.564 64.772 24.451 1.00 30.18 C ANISOU 60 C THR B 8 4125 4102 3240 241 452 507 C ATOM 61 O THR A 8 53.328 64.615 23.508 1.00 31.39 O ANISOU 61 O THR B 8 4238 4017 3672 414 -241 687 O ATOM 62 CB THR A 8 52.474 66.808 25.861 1.00 35.03 C ANISOU 62 CB THR B 8 4296 4909 4104 3 -51 1001 C ATOM 63 OG1 THR A 8 52.959 67.477 24.673 1.00 34.44 O ANISOU 63 OG1 THR B 8 4112 4849 4124 424 677 1479 O ATOM 64 CG2 THR A 8 53.011 67.599 27.046 1.00 37.97 C ANISOU 64 CG2 THR B 8 4096 6196 4135 368 -39 1312 C ATOM 65 N ALA A 9 51.272 64.436 24.418 1.00 32.06 N ANISOU 65 N ALA B 9 4160 4378 3641 -281 174 869 N ATOM 66 CA ALA A 9 50.627 63.999 23.192 1.00 31.04 C ANISOU 66 CA ALA B 9 4421 4042 3330 54 124 490 C ATOM 67 C ALA A 9 50.784 65.041 22.089 1.00 32.92 C ANISOU 67 C ALA B 9 3707 5331 3470 167 -40 180 C ATOM 68 O ALA A 9 50.969 64.703 20.915 1.00 32.03 O ANISOU 68 O ALA B 9 3626 5124 3421 -138 -7 107 O ATOM 69 CB ALA A 9 49.157 63.717 23.456 1.00 30.59 C ANISOU 69 CB ALA B 9 3188 4023 4410 94 -250 811 C ATOM 70 N GLU A 10 50.704 66.334 22.434 1.00 33.85 N ANISOU 70 N GLU B 10 3775 5271 3814 125 16 681 N ATOM 71 CA GLU A 10 50.793 67.324 21.361 1.00 39.43 C ANISOU 71 CA GLU B 10 3560 5969 5451 -195 889 8 C ATOM 72 C GLU A 10 52.188 67.265 20.749 1.00 37.01 C ANISOU 72 C GLU B 10 4141 5260 4661 -46 1227 292 C ATOM 73 O GLU A 10 52.290 67.368 19.527 1.00 32.98 O ANISOU 73 O GLU B 10 3149 4745 4635 151 1622 525 O ATOM 74 CB GLU A 10 50.530 68.753 21.792 1.00 42.67 C ANISOU 74 CB GLU B 10 4032 6783 5397 396 705 329 C ATOM 75 CG GLU A 10 50.336 69.037 23.251 1.00 55.83 C ANISOU 75 CG GLU B 10 6703 8353 6159 -877 -1108 26 C ATOM 76 CD GLU A 10 49.115 68.428 23.906 1.00 68.33 C ANISOU 76 CD GLU B 10 9689 9367 6907 -3509 778 -1069 C ATOM 77 OE1 GLU A 10 49.321 67.717 24.915 1.00 57.50 O ANISOU 77 OE1 GLU B 10 7455 8986 5406 -2363 -1163 -518 O ATOM 78 OE2 GLU A 10 47.982 68.669 23.422 1.00 89.46 O ANISOU 78 OE2 GLU B 10 12970 11278 9744 -5873 3114 -2031 O ATOM 79 N GLN A 11 53.207 67.105 21.586 1.00 33.27 N ANISOU 79 N GLN B 11 4292 4510 3841 620 787 482 N ATOM 80 CA GLN A 11 54.530 66.966 21.005 1.00 33.41 C ANISOU 80 CA GLN B 11 4958 4221 3514 370 560 1011 C ATOM 81 C GLN A 11 54.631 65.682 20.184 1.00 32.06 C ANISOU 81 C GLN B 11 5269 3696 3218 185 402 974 C ATOM 82 O GLN A 11 55.275 65.635 19.130 1.00 32.12 O ANISOU 82 O GLN B 11 4172 4714 3319 -288 990 514 O ATOM 83 CB GLN A 11 55.625 66.888 22.067 1.00 34.19 C ANISOU 83 CB GLN B 11 5234 4412 3344 568 454 1209 C ATOM 84 CG GLN A 11 55.977 68.168 22.799 1.00 37.54 C ANISOU 84 CG GLN B 11 5259 4933 4070 883 549 1570 C ATOM 85 CD GLN A 11 56.928 67.854 23.945 1.00 38.16 C ANISOU 85 CD GLN B 11 6373 4487 3639 963 681 1402 C ATOM 86 OE1 GLN A 11 56.586 67.057 24.813 1.00 42.48 O ANISOU 86 OE1 GLN B 11 6455 5597 4087 -229 922 138 O ATOM 87 NE2 GLN A 11 58.108 68.433 23.965 1.00 52.12 N ANISOU 87 NE2 GLN B 11 9658 4581 5564 324 2102 1353 N ATOM 88 N VAL A 12 54.033 64.598 20.666 1.00 32.02 N ANISOU 88 N VAL B 12 4669 3928 3568 125 474 777 N ATOM 89 CA VAL A 12 54.124 63.370 19.858 1.00 30.86 C ANISOU 89 CA VAL B 12 4315 4473 2937 105 733 602 C ATOM 90 C VAL A 12 53.496 63.573 18.491 1.00 31.72 C ANISOU 90 C VAL B 12 4118 4969 2964 -299 730 513 C ATOM 91 O VAL A 12 54.046 63.193 17.431 1.00 33.07 O ANISOU 91 O VAL B 12 5054 4690 2820 -1018 1080 -72 O ATOM 92 CB VAL A 12 53.436 62.216 20.600 1.00 30.93 C ANISOU 92 CB VAL B 12 4292 4529 2930 249 606 644 C ATOM 93 CG1 VAL A 12 53.163 61.020 19.687 1.00 26.77 C ANISOU 93 CG1 VAL B 12 2518 4821 2832 -406 1004 825 C ATOM 94 CG2 VAL A 12 54.300 61.816 21.799 1.00 27.85 C ANISOU 94 CG2 VAL B 12 4346 3318 2917 63 533 331 C ATOM 95 N GLY A 13 52.302 64.176 18.433 1.00 34.20 N ANISOU 95 N GLY B 13 4049 5732 3212 -520 779 305 N ATOM 96 CA GLY A 13 51.688 64.394 17.110 1.00 29.99 C ANISOU 96 CA GLY B 13 3565 4722 3108 -212 638 236 C ATOM 97 C GLY A 13 52.539 65.323 16.266 1.00 32.48 C ANISOU 97 C GLY B 13 4481 4605 3254 -5 535 274 C ATOM 98 O GLY A 13 52.660 65.154 15.046 1.00 29.43 O ANISOU 98 O GLY B 13 3679 4384 3119 -135 1000 386 O ATOM 99 N LYS A 14 53.178 66.348 16.857 1.00 34.10 N ANISOU 99 N LYS B 14 4805 4698 3454 70 236 279 N ATOM 100 CA LYS A 14 53.949 67.233 15.968 1.00 33.19 C ANISOU 100 CA LYS B 14 3933 4702 3977 -10 646 255 C ATOM 101 C LYS A 14 55.142 66.504 15.380 1.00 32.13 C ANISOU 101 C LYS B 14 3945 4509 3753 -74 844 197 C ATOM 102 O LYS A 14 55.526 66.697 14.227 1.00 30.73 O ANISOU 102 O LYS B 14 3695 4154 3826 518 707 190 O ATOM 103 CB LYS A 14 54.392 68.503 16.707 1.00 35.28 C ANISOU 103 CB LYS B 14 3443 5482 4479 324 1177 812 C ATOM 104 CG LYS A 14 53.221 69.466 16.868 1.00 44.78 C ANISOU 104 CG LYS B 14 3870 7448 5695 -306 234 716 C ATOM 105 CD LYS A 14 53.439 70.570 17.881 1.00 51.11 C ANISOU 105 CD LYS B 14 4335 7781 7302 381 -432 799 C ATOM 106 CE LYS A 14 52.349 71.636 17.790 1.00 59.42 C ANISOU 106 CE LYS B 14 4853 9178 8545 -1037 -1909 511 C ATOM 107 NZ LYS A 14 51.393 71.571 18.938 1.00 82.88 N ANISOU 107 NZ LYS B 14 9491 12124 9874 -4405 -260 -1517 N ATOM 108 N TRP A 15 55.746 65.650 16.188 1.00 32.83 N ANISOU 108 N TRP B 15 3964 4686 3826 16 920 319 N ATOM 109 CA TRP A 15 56.942 64.924 15.770 1.00 31.38 C ANISOU 109 CA TRP B 15 3957 4475 3492 36 838 671 C ATOM 110 C TRP A 15 56.582 63.965 14.644 1.00 30.90 C ANISOU 110 C TRP B 15 4466 4001 3273 -274 838 651 C ATOM 111 O TRP A 15 57.219 63.889 13.587 1.00 30.21 O ANISOU 111 O TRP B 15 3919 3861 3699 -145 576 482 O ATOM 112 CB TRP A 15 57.605 64.150 16.946 1.00 32.35 C ANISOU 112 CB TRP B 15 4518 4618 3156 -598 816 601 C ATOM 113 CG TRP A 15 59.015 63.741 16.554 1.00 32.69 C ANISOU 113 CG TRP B 15 4393 4590 3440 -423 1089 0 C ATOM 114 CD1 TRP A 15 60.170 64.401 16.869 1.00 33.69 C ANISOU 114 CD1 TRP B 15 4677 4557 3565 -529 1072 -65 C ATOM 115 CD2 TRP A 15 59.416 62.594 15.778 1.00 33.36 C ANISOU 115 CD2 TRP B 15 4267 4495 3913 -175 1017 -585 C ATOM 116 NE1 TRP A 15 61.263 63.746 16.343 1.00 35.12 N ANISOU 116 NE1 TRP B 15 4626 4609 4109 -443 1009 -286 N ATOM 117 CE2 TRP A 15 60.828 62.633 15.670 1.00 34.81 C ANISOU 117 CE2 TRP B 15 4363 4726 4137 -481 1105 -233 C ATOM 118 CE3 TRP A 15 58.734 61.533 15.164 1.00 29.62 C ANISOU 118 CE3 TRP B 15 3588 4554 3111 -87 1519 -713 C ATOM 119 CZ2 TRP A 15 61.563 61.670 14.979 1.00 32.81 C ANISOU 119 CZ2 TRP B 15 3755 4507 4204 -110 1598 -773 C ATOM 120 CZ3 TRP A 15 59.458 60.581 14.481 1.00 33.75 C ANISOU 120 CZ3 TRP B 15 4283 5014 3525 -980 862 188 C ATOM 121 CH2 TRP A 15 60.860 60.654 14.396 1.00 35.37 C ANISOU 121 CH2 TRP B 15 4813 4770 3856 -814 679 -158 C ATOM 122 N ALA A 16 55.532 63.192 14.909 1.00 30.94 N ANISOU 122 N ALA B 16 4454 4063 3239 -229 793 488 N ATOM 123 CA ALA A 16 55.066 62.207 13.923 1.00 29.29 C ANISOU 123 CA ALA B 16 3856 4129 3145 116 1164 397 C ATOM 124 C ALA A 16 54.656 62.877 12.623 1.00 29.05 C ANISOU 124 C ALA B 16 3699 4539 2798 -316 790 36 C ATOM 125 O ALA A 16 55.000 62.492 11.508 1.00 33.29 O ANISOU 125 O ALA B 16 4768 4944 2935 -1247 418 291 O ATOM 126 CB ALA A 16 53.905 61.443 14.538 1.00 26.10 C ANISOU 126 CB ALA B 16 2751 4510 2657 366 -21 59 C ATOM 127 N ALA A 17 53.875 63.955 12.753 1.00 30.90 N ANISOU 127 N ALA B 17 3685 4787 3270 -548 1021 78 N ATOM 128 CA ALA A 17 53.453 64.679 11.554 1.00 29.58 C ANISOU 128 CA ALA B 17 3656 4664 2920 9 781 291 C ATOM 129 C ALA A 17 54.667 65.242 10.835 1.00 30.77 C ANISOU 129 C ALA B 17 3429 4455 3808 304 1037 159 C ATOM 130 O ALA A 17 54.767 65.157 9.597 1.00 33.56 O ANISOU 130 O ALA B 17 5242 3549 3961 322 391 -19 O ATOM 131 CB ALA A 17 52.445 65.750 11.930 1.00 31.67 C ANISOU 131 CB ALA B 17 3817 5595 2621 -705 945 938 C ATOM 132 N ARG A 18 55.637 65.816 11.527 1.00 33.37 N ANISOU 132 N ARG B 18 4138 4690 3852 -305 976 359 N ATOM 133 CA ARG A 18 56.833 66.318 10.850 1.00 32.76 C ANISOU 133 CA ARG B 18 3847 4462 4140 76 1273 399 C ATOM 134 C ARG A 18 57.587 65.180 10.164 1.00 31.33 C ANISOU 134 C ARG B 18 4125 3797 3982 276 1024 85 C ATOM 135 O ARG A 18 58.135 65.381 9.055 1.00 36.95 O ANISOU 135 O ARG B 18 4887 4509 4643 82 1079 -703 O ATOM 136 CB ARG A 18 57.728 67.049 11.848 1.00 33.91 C ANISOU 136 CB ARG B 18 3988 4728 4170 240 1013 497 C ATOM 137 CG ARG A 18 58.905 67.781 11.211 1.00 37.46 C ANISOU 137 CG ARG B 18 4925 4534 4776 327 1308 593 C ATOM 138 CD ARG A 18 59.694 68.535 12.285 1.00 41.00 C ANISOU 138 CD ARG B 18 5949 4767 4862 140 1220 802 C ATOM 139 NE ARG A 18 60.407 67.604 13.166 1.00 45.31 N ANISOU 139 NE ARG B 18 6946 5829 4442 -324 1671 479 N ATOM 140 CZ ARG A 18 61.279 67.928 14.098 1.00 50.53 C ANISOU 140 CZ ARG B 18 7873 6006 5319 -150 2270 950 C ATOM 141 NH1 ARG A 18 61.575 69.205 14.305 1.00 60.56 N ANISOU 141 NH1 ARG B 18 8888 7188 6934 529 1145 1804 N ATOM 142 NH2 ARG A 18 61.850 66.980 14.822 1.00 58.04 N ANISOU 142 NH2 ARG B 18 9870 5866 6316 -870 4164 -161 N ATOM 143 N HIS A 19 57.635 63.995 10.773 1.00 30.93 N ANISOU 143 N HIS B 19 4001 3875 3875 385 985 358 N ATOM 144 CA HIS A 19 58.313 62.836 10.178 1.00 29.19 C ANISOU 144 CA HIS B 19 4131 3571 3390 299 962 56 C ATOM 145 C HIS A 19 57.639 62.462 8.860 1.00 30.19 C ANISOU 145 C HIS B 19 4403 3642 3426 10 894 90 C ATOM 146 O HIS A 19 58.236 62.260 7.796 1.00 36.06 O ANISOU 146 O HIS B 19 6311 3812 3577 -286 289 203 O ATOM 147 CB HIS A 19 58.324 61.641 11.144 1.00 28.79 C ANISOU 147 CB HIS B 19 4045 3511 3382 510 825 102 C ATOM 148 CG HIS A 19 59.207 60.525 10.684 1.00 30.50 C ANISOU 148 CG HIS B 19 4090 3803 3695 373 813 -201 C ATOM 149 ND1 HIS A 19 60.572 60.625 10.577 1.00 33.56 N ANISOU 149 ND1 HIS B 19 4787 3990 3973 -5 382 44 N ATOM 150 CD2 HIS A 19 58.918 59.256 10.285 1.00 31.72 C ANISOU 150 CD2 HIS B 19 3922 3984 4146 448 549 -610 C ATOM 151 CE1 HIS A 19 61.095 59.491 10.146 1.00 34.20 C ANISOU 151 CE1 HIS B 19 4915 4265 3813 -128 130 -220 C ATOM 152 NE2 HIS A 19 60.104 58.639 9.959 1.00 34.50 N ANISOU 152 NE2 HIS B 19 4320 4316 4472 92 236 -445 N ATOM 153 N ILE A 20 56.308 62.370 8.918 1.00 33.50 N ANISOU 153 N ILE B 20 4840 4222 3665 -726 1231 153 N ATOM 154 CA ILE A 20 55.518 62.043 7.717 1.00 32.34 C ANISOU 154 CA ILE B 20 4869 3846 3575 -275 1542 -52 C ATOM 155 C ILE A 20 55.816 63.062 6.629 1.00 33.02 C ANISOU 155 C ILE B 20 4689 4221 3637 -170 1282 -341 C ATOM 156 O ILE A 20 56.137 62.661 5.507 1.00 35.06 O ANISOU 156 O ILE B 20 5147 4395 3778 -369 1052 -545 O ATOM 157 CB ILE A 20 54.014 61.972 8.049 1.00 31.64 C ANISOU 157 CB ILE B 20 4972 3796 3253 -249 1104 99 C ATOM 158 CG1 ILE A 20 53.637 60.811 8.978 1.00 27.21 C ANISOU 158 CG1 ILE B 20 4083 3578 2679 -480 788 382 C ATOM 159 CG2 ILE A 20 53.196 61.937 6.768 1.00 30.74 C ANISOU 159 CG2 ILE B 20 4222 4101 3356 -234 1397 63 C ATOM 160 CD1 ILE A 20 52.233 60.847 9.539 1.00 27.95 C ANISOU 160 CD1 ILE B 20 3960 3676 2983 -143 98 227 C ATOM 161 N VAL A 21 55.736 64.341 6.964 1.00 33.86 N ANISOU 161 N VAL B 21 4471 4460 3934 -273 1515 -76 N ATOM 162 CA VAL A 21 55.993 65.405 5.993 1.00 34.17 C ANISOU 162 CA VAL B 21 4534 4381 4068 -123 1204 -318 C ATOM 163 C VAL A 21 57.381 65.286 5.373 1.00 36.10 C ANISOU 163 C VAL B 21 5749 4619 3350 -662 814 77 C ATOM 164 O VAL A 21 57.622 65.408 4.165 1.00 37.00 O ANISOU 164 O VAL B 21 6030 4317 3713 -347 2338 -810 O ATOM 165 CB VAL A 21 55.826 66.787 6.663 1.00 37.20 C ANISOU 165 CB VAL B 21 4646 4993 4495 100 1086 -325 C ATOM 166 CG1 VAL A 21 56.423 67.875 5.769 1.00 33.39 C ANISOU 166 CG1 VAL B 21 3606 5524 3557 -231 1759 143 C ATOM 167 CG2 VAL A 21 54.362 67.044 6.988 1.00 37.04 C ANISOU 167 CG2 VAL B 21 4146 5571 4354 -179 1433 -119 C ATOM 168 N ASN A 22 58.371 65.032 6.221 1.00 35.42 N ANISOU 168 N ASN B 22 5578 4810 3072 -833 684 -45 N ATOM 169 CA ASN A 22 59.732 64.920 5.709 1.00 36.23 C ANISOU 169 CA ASN B 22 5802 4366 3596 -598 428 13 C ATOM 170 C ASN A 22 59.881 63.687 4.835 1.00 35.13 C ANISOU 170 C ASN B 22 5692 4331 3324 -622 502 -178 C ATOM 171 O ASN A 22 60.578 63.714 3.817 1.00 37.68 O ANISOU 171 O ASN B 22 5612 5340 3365 -947 734 -548 O ATOM 172 CB ASN A 22 60.708 64.925 6.888 1.00 39.79 C ANISOU 172 CB ASN B 22 6436 4639 4041 -967 142 475 C ATOM 173 CG ASN A 22 60.801 66.275 7.582 1.00 45.83 C ANISOU 173 CG ASN B 22 7258 5374 4783 -947 -662 925 C ATOM 174 OD1 ASN A 22 61.460 66.359 8.618 1.00 54.80 O ANISOU 174 OD1 ASN B 22 8143 7299 5378 -1210 -963 2065 O ATOM 175 ND2 ASN A 22 60.185 67.334 7.072 1.00 45.89 N ANISOU 175 ND2 ASN B 22 7308 5443 4685 354 -589 472 N ATOM 176 N ARG A 23 59.238 62.570 5.167 1.00 35.83 N ANISOU 176 N ARG B 23 5833 4392 3389 -470 976 198 N ATOM 177 CA ARG A 23 59.331 61.431 4.253 1.00 33.81 C ANISOU 177 CA ARG B 23 5251 4775 2818 -351 1334 -299 C ATOM 178 C ARG A 23 58.667 61.755 2.927 1.00 34.96 C ANISOU 178 C ARG B 23 5254 5289 2741 -722 1197 -306 C ATOM 179 O ARG A 23 59.211 61.443 1.869 1.00 36.82 O ANISOU 179 O ARG B 23 5818 5426 2745 -279 1168 -752 O ATOM 180 CB ARG A 23 58.660 60.201 4.866 1.00 35.25 C ANISOU 180 CB ARG B 23 5146 4909 3337 -363 1235 -638 C ATOM 181 CG ARG A 23 59.522 59.692 6.006 1.00 30.89 C ANISOU 181 CG ARG B 23 4207 4471 3060 112 732 -412 C ATOM 182 CD ARG A 23 60.832 59.103 5.461 1.00 38.51 C ANISOU 182 CD ARG B 23 5582 5100 3950 -1057 249 -41 C ATOM 183 NE ARG A 23 61.427 58.312 6.551 1.00 40.05 N ANISOU 183 NE ARG B 23 4953 5583 4681 -1159 237 382 N ATOM 184 CZ ARG A 23 62.719 58.237 6.836 1.00 46.54 C ANISOU 184 CZ ARG B 23 6432 5918 5332 -1957 791 -23 C ATOM 185 NH1 ARG A 23 63.576 58.926 6.078 1.00 45.47 N ANISOU 185 NH1 ARG B 23 6255 5597 5424 -1602 1236 316 N ATOM 186 NH2 ARG A 23 63.123 57.486 7.857 1.00 39.35 N ANISOU 186 NH2 ARG B 23 5844 4406 4700 -1401 167 496 N ATOM 187 N ILE A 24 57.489 62.380 2.986 1.00 36.60 N ANISOU 187 N ILE B 24 5032 5082 3794 -531 1463 -307 N ATOM 188 CA ILE A 24 56.833 62.711 1.727 1.00 36.12 C ANISOU 188 CA ILE B 24 4944 4952 3828 -444 1575 -410 C ATOM 189 C ILE A 24 57.662 63.694 0.917 1.00 37.86 C ANISOU 189 C ILE B 24 5388 5292 3707 -139 1001 -707 C ATOM 190 O ILE A 24 57.853 63.584 -0.298 1.00 43.09 O ANISOU 190 O ILE B 24 6870 5635 3868 -744 545 -885 O ATOM 191 CB ILE A 24 55.435 63.298 1.987 1.00 33.76 C ANISOU 191 CB ILE B 24 4106 5106 3616 84 1724 -768 C ATOM 192 CG1 ILE A 24 54.452 62.276 2.548 1.00 32.78 C ANISOU 192 CG1 ILE B 24 4389 4766 3300 68 1392 -388 C ATOM 193 CG2 ILE A 24 54.891 63.954 0.709 1.00 35.69 C ANISOU 193 CG2 ILE B 24 3904 6526 3130 -272 1273 -1019 C ATOM 194 CD1 ILE A 24 53.230 62.864 3.200 1.00 33.70 C ANISOU 194 CD1 ILE B 24 4440 4508 3855 -216 1429 -75 C ATOM 195 N ASN A 25 58.206 64.733 1.557 1.00 39.70 N ANISOU 195 N ASN B 25 5448 5176 4462 -73 823 -715 N ATOM 196 CA ASN A 25 58.897 65.738 0.743 1.00 38.29 C ANISOU 196 CA ASN B 25 4951 5480 4118 -75 1363 -477 C ATOM 197 C ASN A 25 60.199 65.171 0.207 1.00 38.36 C ANISOU 197 C ASN B 25 5064 5487 4025 -82 1665 -1018 C ATOM 198 O ASN A 25 60.678 65.514 -0.884 1.00 45.52 O ANISOU 198 O ASN B 25 6670 6190 4436 -504 2035 -1597 O ATOM 199 CB ASN A 25 59.078 67.028 1.545 1.00 38.75 C ANISOU 199 CB ASN B 25 5514 5043 4167 -147 1240 -254 C ATOM 200 CG ASN A 25 57.792 67.818 1.724 1.00 37.94 C ANISOU 200 CG ASN B 25 4753 5011 4650 399 1590 199 C ATOM 201 OD1 ASN A 25 56.849 67.665 0.942 1.00 43.68 O ANISOU 201 OD1 ASN B 25 5939 5284 5373 -193 1400 577 O ATOM 202 ND2 ASN A 25 57.674 68.678 2.725 1.00 38.06 N ANISOU 202 ND2 ASN B 25 5159 4318 4983 639 1083 -371 N ATOM 203 N ALA A 26 60.846 64.242 0.909 1.00 39.03 N ANISOU 203 N ALA B 26 5387 5650 3794 -559 1731 -124 N ATOM 204 CA ALA A 26 62.106 63.728 0.356 1.00 39.56 C ANISOU 204 CA ALA B 26 5776 5022 4232 -740 1787 -16 C ATOM 205 C ALA A 26 61.859 62.754 -0.785 1.00 39.68 C ANISOU 205 C ALA B 26 6338 4625 4112 -760 1116 -698 C ATOM 206 O ALA A 26 62.696 62.605 -1.665 1.00 47.53 O ANISOU 206 O ALA B 26 9724 4861 3475 -1902 1068 -498 O ATOM 207 CB ALA A 26 62.914 63.029 1.440 1.00 36.18 C ANISOU 207 CB ALA B 26 5123 4342 4282 -55 1936 -723 C ATOM 208 N PHE A 27 60.711 62.084 -0.747 1.00 38.35 N ANISOU 208 N PHE B 27 5942 4615 4013 -405 1029 -920 N ATOM 209 CA PHE A 27 60.342 61.086 -1.742 1.00 40.04 C ANISOU 209 CA PHE B 27 6188 5010 4013 -384 1177 -579 C ATOM 210 C PHE A 27 59.914 61.722 -3.060 1.00 41.26 C ANISOU 210 C PHE B 27 6808 4817 4051 -346 1448 -885 C ATOM 211 O PHE A 27 60.135 61.134 -4.118 1.00 41.16 O ANISOU 211 O PHE B 27 7394 4144 4103 -954 1316 -139 O ATOM 212 CB PHE A 27 59.191 60.233 -1.233 1.00 37.50 C ANISOU 212 CB PHE B 27 5627 5273 3349 184 623 -681 C ATOM 213 CG PHE A 27 58.699 59.081 -2.088 1.00 36.10 C ANISOU 213 CG PHE B 27 4925 5379 3413 -351 584 -349 C ATOM 214 CD1 PHE A 27 59.250 57.825 -1.918 1.00 36.57 C ANISOU 214 CD1 PHE B 27 4890 5474 3529 -493 506 -721 C ATOM 215 CD2 PHE A 27 57.701 59.254 -3.031 1.00 37.55 C ANISOU 215 CD2 PHE B 27 5136 5593 3540 -1063 296 -375 C ATOM 216 CE1 PHE A 27 58.816 56.765 -2.673 1.00 37.05 C ANISOU 216 CE1 PHE B 27 4493 5781 3805 -495 810 -343 C ATOM 217 CE2 PHE A 27 57.250 58.187 -3.791 1.00 38.14 C ANISOU 217 CE2 PHE B 27 4737 5829 3926 -1438 374 177 C ATOM 218 CZ PHE A 27 57.800 56.930 -3.601 1.00 39.50 C ANISOU 218 CZ PHE B 27 4809 6140 4058 -1157 437 -99 C ATOM 219 N LYS A 28 59.302 62.894 -2.963 1.00 44.61 N ANISOU 219 N LYS B 28 6756 5747 4445 -570 1777 -641 N ATOM 220 CA LYS A 28 58.877 63.640 -4.151 1.00 46.21 C ANISOU 220 CA LYS B 28 7387 5462 4708 -684 2205 -620 C ATOM 221 C LYS A 28 57.890 62.848 -5.006 1.00 44.35 C ANISOU 221 C LYS B 28 7283 5607 3960 -986 1123 -833 C ATOM 222 O LYS A 28 58.217 62.464 -6.132 1.00 49.03 O ANISOU 222 O LYS B 28 8259 6865 3505 -1735 1498 -1172 O ATOM 223 CB LYS A 28 60.095 64.030 -4.998 1.00 52.78 C ANISOU 223 CB LYS B 28 8806 5571 5675 -713 2907 -1237 C ATOM 224 CG LYS A 28 60.970 65.074 -4.336 1.00 62.04 C ANISOU 224 CG LYS B 28 10735 5380 7459 -1095 2638 -533 C ATOM 225 CD LYS A 28 62.448 64.704 -4.342 1.00 83.37 C ANISOU 225 CD LYS B 28 14704 6945 10028 -3815 2545 -213 C ATOM 226 CE LYS A 28 63.112 65.024 -3.007 1.00 92.61 C ANISOU 226 CE LYS B 28 16511 7514 11163 -4622 2424 933 C ATOM 227 NZ LYS A 28 64.334 64.220 -2.720 1.00103.41 N ANISOU 227 NZ LYS B 28 18273 7587 13433 -5443 6133 -1423 N ATOM 228 N PRO A 29 56.698 62.613 -4.467 1.00 39.46 N ANISOU 228 N PRO B 29 5785 5362 3845 -424 1002 -725 N ATOM 229 CA PRO A 29 55.721 61.731 -5.105 1.00 37.54 C ANISOU 229 CA PRO B 29 5009 5543 3711 -230 939 -695 C ATOM 230 C PRO A 29 55.130 62.348 -6.363 1.00 41.25 C ANISOU 230 C PRO B 29 6231 5831 3612 -708 1172 -774 C ATOM 231 O PRO A 29 55.025 63.571 -6.441 1.00 43.73 O ANISOU 231 O PRO B 29 5745 6606 4264 -1134 1934 -461 O ATOM 232 CB PRO A 29 54.622 61.619 -4.037 1.00 35.65 C ANISOU 232 CB PRO B 29 4574 5268 3702 -35 1111 -669 C ATOM 233 CG PRO A 29 54.715 62.926 -3.307 1.00 36.41 C ANISOU 233 CG PRO B 29 5121 5152 3560 33 908 -576 C ATOM 234 CD PRO A 29 56.200 63.180 -3.199 1.00 38.15 C ANISOU 234 CD PRO B 29 5260 5248 3985 -108 942 -559 C ATOM 235 N THR A 30 54.752 61.489 -7.303 1.00 45.50 N ANISOU 235 N THR B 30 7490 6010 3786 -1299 469 -481 N ATOM 236 CA THR A 30 54.072 61.934 -8.513 1.00 46.83 C ANISOU 236 CA THR B 30 7609 6480 3702 -1843 299 -454 C ATOM 237 C THR A 30 52.876 61.034 -8.814 1.00 50.02 C ANISOU 237 C THR B 30 8268 6557 4179 -1744 797 -198 C ATOM 238 O THR A 30 52.666 60.020 -8.143 1.00 52.51 O ANISOU 238 O THR B 30 8664 6438 4849 -1677 1162 -222 O ATOM 239 CB THR A 30 55.008 61.949 -9.736 1.00 44.09 C ANISOU 239 CB THR B 30 6711 6582 3459 -1159 -332 -109 C ATOM 240 OG1 THR A 30 55.461 60.614 -9.987 1.00 46.64 O ANISOU 240 OG1 THR B 30 6551 7076 4093 -953 237 201 O ATOM 241 CG2 THR A 30 56.248 62.783 -9.459 1.00 42.08 C ANISOU 241 CG2 THR B 30 7296 6431 2261 -443 1449 -777 C ATOM 242 N ALA A 31 52.110 61.423 -9.833 1.00 52.97 N ANISOU 242 N ALA B 31 8827 7004 4296 -1634 985 127 N ATOM 243 CA ALA A 31 50.923 60.687 -10.249 1.00 53.78 C ANISOU 243 CA ALA B 31 9115 6975 4346 -1331 1698 68 C ATOM 244 C ALA A 31 51.237 59.208 -10.457 1.00 54.14 C ANISOU 244 C ALA B 31 9096 7145 4330 -1356 1670 468 C ATOM 245 O ALA A 31 50.435 58.342 -10.116 1.00 56.11 O ANISOU 245 O ALA B 31 9632 7247 4442 -738 -88 303 O ATOM 246 CB ALA A 31 50.337 61.276 -11.528 1.00 55.18 C ANISOU 246 CB ALA B 31 9035 7432 4499 -1937 1730 -40 C ATOM 247 N ASP A 32 52.412 58.950 -11.027 1.00 54.17 N ANISOU 247 N ASP B 32 8981 7218 4383 -1307 1864 231 N ATOM 248 CA ASP A 32 52.821 57.594 -11.381 1.00 56.83 C ANISOU 248 CA ASP B 32 9268 7418 4908 -1227 1294 339 C ATOM 249 C ASP A 32 53.732 56.968 -10.328 1.00 53.60 C ANISOU 249 C ASP B 32 8274 6953 5141 -1152 740 731 C ATOM 250 O ASP A 32 54.054 55.777 -10.409 1.00 51.86 O ANISOU 250 O ASP B 32 8029 7728 3949 -1792 -388 384 O ATOM 251 CB ASP A 32 53.496 57.604 -12.756 1.00 62.94 C ANISOU 251 CB ASP B 32 10524 8347 5042 -1065 743 143 C ATOM 252 CG ASP A 32 52.482 57.860 -13.863 1.00 73.31 C ANISOU 252 CG ASP B 32 14176 8786 4892 -2321 1926 -630 C ATOM 253 OD1 ASP A 32 51.363 57.286 -13.833 1.00 85.57 O ANISOU 253 OD1 ASP B 32 18137 8895 5480 -4880 594 -885 O ATOM 254 OD2 ASP A 32 52.781 58.648 -14.794 1.00102.79 O ANISOU 254 OD2 ASP B 32 18775 12167 8113 -4367 5851 -3177 O ATOM 255 N ARG A 33 54.142 57.763 -9.342 1.00 47.75 N ANISOU 255 N ARG B 33 7703 6550 3890 -716 804 -507 N ATOM 256 CA ARG A 33 54.940 57.242 -8.237 1.00 44.00 C ANISOU 256 CA ARG B 33 6663 6144 3912 -801 287 -402 C ATOM 257 C ARG A 33 54.478 57.947 -6.962 1.00 42.40 C ANISOU 257 C ARG B 33 6310 5814 3985 -788 346 -194 C ATOM 258 O ARG A 33 55.122 58.897 -6.509 1.00 42.09 O ANISOU 258 O ARG B 33 6755 5625 3612 -979 834 113 O ATOM 259 CB ARG A 33 56.442 57.420 -8.450 1.00 46.13 C ANISOU 259 CB ARG B 33 6191 6304 5030 -675 436 -1107 C ATOM 260 CG ARG A 33 57.261 56.420 -7.647 1.00 48.91 C ANISOU 260 CG ARG B 33 5890 6223 6471 -488 610 -650 C ATOM 261 CD ARG A 33 58.733 56.821 -7.574 1.00 50.23 C ANISOU 261 CD ARG B 33 5725 6018 7342 -54 992 -652 C ATOM 262 NE ARG A 33 58.846 58.235 -7.268 1.00 54.48 N ANISOU 262 NE ARG B 33 6214 6723 7762 313 312 -655 N ATOM 263 CZ ARG A 33 59.586 58.852 -6.365 1.00 51.40 C ANISOU 263 CZ ARG B 33 5936 6491 7104 380 692 -1028 C ATOM 264 NH1 ARG A 33 60.406 58.242 -5.531 1.00 45.95 N ANISOU 264 NH1 ARG B 33 5864 5661 5935 -359 383 -2613 N ATOM 265 NH2 ARG A 33 59.471 60.177 -6.324 1.00 51.57 N ANISOU 265 NH2 ARG B 33 6382 6499 6714 886 1086 -1189 N ATOM 266 N PRO A 34 53.349 57.471 -6.450 1.00 38.08 N ANISOU 266 N PRO B 34 5036 5895 3539 -293 777 -377 N ATOM 267 CA PRO A 34 52.792 58.051 -5.230 1.00 37.24 C ANISOU 267 CA PRO B 34 5165 5475 3510 -542 698 62 C ATOM 268 C PRO A 34 53.544 57.604 -3.981 1.00 37.15 C ANISOU 268 C PRO B 34 4964 5495 3654 -911 572 154 C ATOM 269 O PRO A 34 54.143 56.535 -3.978 1.00 34.83 O ANISOU 269 O PRO B 34 4961 4858 3415 -1190 232 197 O ATOM 270 CB PRO A 34 51.378 57.456 -5.192 1.00 34.64 C ANISOU 270 CB PRO B 34 3958 5439 3767 -423 591 302 C ATOM 271 CG PRO A 34 51.511 56.138 -5.894 1.00 34.98 C ANISOU 271 CG PRO B 34 4129 5589 3573 -786 -2 -77 C ATOM 272 CD PRO A 34 52.519 56.380 -6.978 1.00 35.93 C ANISOU 272 CD PRO B 34 4820 5946 2885 -437 898 -291 C ATOM 273 N PHE A 35 53.489 58.404 -2.927 1.00 33.50 N ANISOU 273 N PHE B 35 4323 4795 3610 -209 1093 92 N ATOM 274 CA PHE A 35 53.901 58.026 -1.582 1.00 34.47 C ANISOU 274 CA PHE B 35 4715 4901 3480 -303 1108 -166 C ATOM 275 C PHE A 35 52.748 57.285 -0.920 1.00 30.80 C ANISOU 275 C PHE B 35 3745 4708 3249 -133 283 80 C ATOM 276 O PHE A 35 51.620 57.794 -0.859 1.00 34.69 O ANISOU 276 O PHE B 35 4370 5498 3313 -953 865 102 O ATOM 277 CB PHE A 35 54.256 59.255 -0.763 1.00 31.19 C ANISOU 277 CB PHE B 35 4628 4378 2845 -147 1408 -659 C ATOM 278 CG PHE A 35 54.899 58.882 0.575 1.00 32.85 C ANISOU 278 CG PHE B 35 4726 4756 2998 -563 1396 -552 C ATOM 279 CD1 PHE A 35 56.264 58.688 0.648 1.00 34.09 C ANISOU 279 CD1 PHE B 35 4555 4989 3409 -659 1006 -231 C ATOM 280 CD2 PHE A 35 54.114 58.744 1.701 1.00 32.16 C ANISOU 280 CD2 PHE B 35 4104 5072 3044 -292 1803 -911 C ATOM 281 CE1 PHE A 35 56.865 58.344 1.844 1.00 36.47 C ANISOU 281 CE1 PHE B 35 5383 4816 3659 -970 1408 -344 C ATOM 282 CE2 PHE A 35 54.718 58.400 2.908 1.00 32.59 C ANISOU 282 CE2 PHE B 35 4209 5400 2773 -710 1003 -232 C ATOM 283 CZ PHE A 35 56.092 58.209 2.986 1.00 31.87 C ANISOU 283 CZ PHE B 35 4006 4644 3461 -139 1146 -158 C ATOM 284 N VAL A 36 53.003 56.085 -0.421 1.00 31.61 N ANISOU 284 N VAL B 36 4174 4493 3343 -147 942 418 N ATOM 285 CA VAL A 36 51.928 55.265 0.130 1.00 31.43 C ANISOU 285 CA VAL B 36 4778 4483 2682 123 698 564 C ATOM 286 C VAL A 36 52.007 55.269 1.656 1.00 32.63 C ANISOU 286 C VAL B 36 5038 4700 2660 -862 252 757 C ATOM 287 O VAL A 36 53.041 54.865 2.212 1.00 32.32 O ANISOU 287 O VAL B 36 4713 5181 2386 -1089 704 -255 O ATOM 288 CB VAL A 36 51.949 53.834 -0.432 1.00 31.27 C ANISOU 288 CB VAL B 36 4827 4559 2494 99 136 -277 C ATOM 289 CG1 VAL A 36 50.762 53.038 0.092 1.00 27.48 C ANISOU 289 CG1 VAL B 36 3380 4632 2430 -165 -163 -417 C ATOM 290 CG2 VAL A 36 51.951 53.859 -1.975 1.00 28.93 C ANISOU 290 CG2 VAL B 36 3655 4842 2496 -270 474 -500 C ATOM 291 N LEU A 37 50.937 55.734 2.289 1.00 30.67 N ANISOU 291 N LEU B 37 4517 4144 2994 -623 685 483 N ATOM 292 CA LEU A 37 50.866 55.999 3.714 1.00 28.29 C ANISOU 292 CA LEU B 37 3603 4101 3043 -644 539 372 C ATOM 293 C LEU A 37 49.824 55.119 4.386 1.00 28.55 C ANISOU 293 C LEU B 37 3493 4173 3181 -461 441 330 C ATOM 294 O LEU A 37 48.661 55.236 3.993 1.00 29.10 O ANISOU 294 O LEU B 37 3783 3994 3281 -337 844 224 O ATOM 295 CB LEU A 37 50.410 57.424 3.977 1.00 32.82 C ANISOU 295 CB LEU B 37 3775 4139 4557 -272 387 425 C ATOM 296 CG LEU A 37 51.054 58.405 4.940 1.00 32.63 C ANISOU 296 CG LEU B 37 3723 5069 3608 -636 -25 474 C ATOM 297 CD1 LEU A 37 50.022 59.453 5.353 1.00 32.91 C ANISOU 297 CD1 LEU B 37 4935 4662 2905 -2002 -779 347 C ATOM 298 CD2 LEU A 37 51.687 57.782 6.170 1.00 28.13 C ANISOU 298 CD2 LEU B 37 4074 4126 2488 234 -64 -1156 C ATOM 299 N GLY A 38 50.204 54.314 5.367 1.00 29.00 N ANISOU 299 N GLY B 38 3598 4227 3192 -802 506 96 N ATOM 300 CA GLY A 38 49.235 53.520 6.116 1.00 27.79 C ANISOU 300 CA GLY B 38 3542 4232 2786 -519 8 203 C ATOM 301 C GLY A 38 48.825 54.283 7.378 1.00 28.30 C ANISOU 301 C GLY B 38 3406 4072 3273 -349 -292 388 C ATOM 302 O GLY A 38 49.665 54.940 8.007 1.00 26.56 O ANISOU 302 O GLY B 38 3348 4128 2614 -59 648 328 O ATOM 303 N LEU A 39 47.542 54.225 7.737 1.00 26.66 N ANISOU 303 N LEU B 39 3158 3916 3056 106 -40 -130 N ATOM 304 CA LEU A 39 47.007 55.098 8.770 1.00 26.08 C ANISOU 304 CA LEU B 39 2896 3741 3271 159 -45 -11 C ATOM 305 C LEU A 39 46.096 54.392 9.751 1.00 25.74 C ANISOU 305 C LEU B 39 3267 3450 3064 -333 27 177 C ATOM 306 O LEU A 39 45.372 53.469 9.390 1.00 27.38 O ANISOU 306 O LEU B 39 3133 3840 3430 335 36 -56 O ATOM 307 CB LEU A 39 46.193 56.228 8.105 1.00 28.35 C ANISOU 307 CB LEU B 39 3119 4457 3196 -71 160 283 C ATOM 308 CG LEU A 39 47.026 57.197 7.265 1.00 29.90 C ANISOU 308 CG LEU B 39 3207 4583 3570 -75 755 292 C ATOM 309 CD1 LEU A 39 46.141 58.286 6.651 1.00 28.57 C ANISOU 309 CD1 LEU B 39 3188 5131 2536 -340 361 570 C ATOM 310 CD2 LEU A 39 48.153 57.822 8.084 1.00 29.84 C ANISOU 310 CD2 LEU B 39 3316 4361 3659 -386 957 143 C ATOM 311 N PRO A 40 46.110 54.800 11.005 1.00 27.30 N ANISOU 311 N PRO B 40 3357 4166 2850 -156 495 260 N ATOM 312 CA PRO A 40 45.160 54.314 12.005 1.00 27.80 C ANISOU 312 CA PRO B 40 3695 4172 2697 -269 673 271 C ATOM 313 C PRO A 40 44.115 55.334 12.426 1.00 29.36 C ANISOU 313 C PRO B 40 3953 3855 3348 -565 426 409 C ATOM 314 O PRO A 40 44.158 56.504 12.023 1.00 28.16 O ANISOU 314 O PRO B 40 3646 3956 3097 -554 -80 202 O ATOM 315 CB PRO A 40 46.131 54.110 13.188 1.00 26.34 C ANISOU 315 CB PRO B 40 3850 3430 2729 -341 378 300 C ATOM 316 CG PRO A 40 47.020 55.308 13.079 1.00 26.74 C ANISOU 316 CG PRO B 40 3569 3895 2697 62 756 21 C ATOM 317 CD PRO A 40 47.094 55.710 11.617 1.00 26.74 C ANISOU 317 CD PRO B 40 3568 4218 2373 -160 163 111 C ATOM 318 N THR A 41 43.173 54.893 13.253 1.00 30.65 N ANISOU 318 N THR B 41 4076 4449 3119 -593 654 129 N ATOM 319 CA THR A 41 42.126 55.748 13.782 1.00 32.57 C ANISOU 319 CA THR B 41 4423 4492 3462 -721 316 55 C ATOM 320 C THR A 41 42.184 55.696 15.309 1.00 34.25 C ANISOU 320 C THR B 41 4493 5077 3445 -735 278 149 C ATOM 321 O THR A 41 43.079 55.051 15.870 1.00 39.20 O ANISOU 321 O THR B 41 4684 6525 3685 -983 561 213 O ATOM 322 CB THR A 41 40.701 55.381 13.323 1.00 33.71 C ANISOU 322 CB THR B 41 5253 4338 3216 -1003 374 -341 C ATOM 323 OG1 THR A 41 40.392 54.057 13.779 1.00 36.62 O ANISOU 323 OG1 THR B 41 6285 4357 3273 -747 1025 -314 O ATOM 324 CG2 THR A 41 40.546 55.324 11.816 1.00 31.31 C ANISOU 324 CG2 THR B 41 5179 3499 3219 550 189 -159 C ATOM 325 N GLY A 42 41.262 56.357 15.981 1.00 36.09 N ANISOU 325 N GLY B 42 4541 5612 3561 -598 114 26 N ATOM 326 CA GLY A 42 41.172 56.369 17.422 1.00 36.71 C ANISOU 326 CA GLY B 42 4990 5433 3523 -684 16 166 C ATOM 327 C GLY A 42 41.742 57.623 18.036 1.00 35.57 C ANISOU 327 C GLY B 42 4942 5088 3485 -742 147 -25 C ATOM 328 O GLY A 42 42.180 58.562 17.403 1.00 35.05 O ANISOU 328 O GLY B 42 5529 4786 3001 -940 306 113 O ATOM 329 N GLY A 43 41.750 57.683 19.365 1.00 34.07 N ANISOU 329 N GLY B 43 4938 4519 3487 -272 530 59 N ATOM 330 CA GLY A 43 42.229 58.866 20.069 1.00 33.79 C ANISOU 330 CA GLY B 43 4362 4499 3976 -767 424 439 C ATOM 331 C GLY A 43 43.731 59.041 19.931 1.00 31.78 C ANISOU 331 C GLY B 43 4012 4468 3594 -551 440 29 C ATOM 332 O GLY A 43 44.219 60.171 19.951 1.00 32.96 O ANISOU 332 O GLY B 43 4103 4546 3873 -467 797 284 O ATOM 333 N THR A 44 44.483 57.955 19.795 1.00 30.70 N ANISOU 333 N THR B 44 3928 4790 2946 -615 788 -67 N ATOM 334 CA THR A 44 45.943 58.058 19.768 1.00 31.56 C ANISOU 334 CA THR B 44 4083 4857 3050 -743 580 -30 C ATOM 335 C THR A 44 46.482 58.904 18.637 1.00 27.57 C ANISOU 335 C THR B 44 3397 4242 2838 -98 107 451 C ATOM 336 O THR A 44 47.316 59.782 18.901 1.00 29.25 O ANISOU 336 O THR B 44 2870 4461 3782 -108 348 1007 O ATOM 337 CB THR A 44 46.570 56.643 19.703 1.00 32.96 C ANISOU 337 CB THR B 44 4063 4366 4094 -645 1021 -659 C ATOM 338 OG1 THR A 44 46.341 55.991 20.965 1.00 40.12 O ANISOU 338 OG1 THR B 44 5055 5581 4609 -1401 1930 -1118 O ATOM 339 CG2 THR A 44 48.074 56.695 19.525 1.00 30.57 C ANISOU 339 CG2 THR B 44 4264 4209 3141 -760 433 432 C ATOM 340 N PRO A 45 46.133 58.721 17.366 1.00 27.52 N ANISOU 340 N PRO B 45 3448 4170 2840 -157 392 440 N ATOM 341 CA PRO A 45 46.678 59.628 16.355 1.00 28.21 C ANISOU 341 CA PRO B 45 3447 4269 3002 63 271 322 C ATOM 342 C PRO A 45 46.000 60.990 16.276 1.00 28.67 C ANISOU 342 C PRO B 45 3466 4244 3183 199 52 130 C ATOM 343 O PRO A 45 46.334 61.757 15.366 1.00 29.73 O ANISOU 343 O PRO B 45 3427 4747 3122 -639 856 110 O ATOM 344 CB PRO A 45 46.406 58.853 15.047 1.00 26.66 C ANISOU 344 CB PRO B 45 3291 3904 2934 -104 69 9 C ATOM 345 CG PRO A 45 45.188 58.021 15.340 1.00 26.85 C ANISOU 345 CG PRO B 45 3873 3958 2372 -165 -185 -94 C ATOM 346 CD PRO A 45 45.283 57.657 16.809 1.00 28.88 C ANISOU 346 CD PRO B 45 4611 3828 2536 -229 346 252 C ATOM 347 N MET A 46 45.067 61.402 17.119 1.00 31.24 N ANISOU 347 N MET B 46 3654 5111 3103 -530 326 104 N ATOM 348 CA MET A 46 44.422 62.714 16.940 1.00 32.62 C ANISOU 348 CA MET B 46 3597 4831 3968 -342 -49 882 C ATOM 349 C MET A 46 45.377 63.903 16.873 1.00 34.04 C ANISOU 349 C MET B 46 4307 4874 3754 -194 1028 833 C ATOM 350 O MET A 46 45.259 64.751 15.990 1.00 36.82 O ANISOU 350 O MET B 46 4296 5735 3957 -568 1120 309 O ATOM 351 CB MET A 46 43.421 63.039 18.061 1.00 32.57 C ANISOU 351 CB MET B 46 3155 5559 3662 142 294 281 C ATOM 352 CG MET A 46 42.175 62.174 18.040 1.00 39.33 C ANISOU 352 CG MET B 46 4828 5541 4573 142 -53 -347 C ATOM 353 SD MET A 46 41.130 62.631 16.641 1.00 54.33 S ANISOU 353 SD MET B 46 6699 6308 7636 -571 996 1817 S ATOM 354 CE MET A 46 40.457 64.184 17.213 1.00 56.96 C ANISOU 354 CE MET B 46 5802 8021 7819 43 2212 -1512 C ATOM 355 N THR A 47 46.343 64.017 17.789 1.00 32.40 N ANISOU 355 N THR B 47 3999 4720 3590 -566 433 774 N ATOM 356 CA THR A 47 47.205 65.200 17.688 1.00 31.89 C ANISOU 356 CA THR B 47 3595 4904 3620 -412 345 823 C ATOM 357 C THR A 47 48.087 65.118 16.452 1.00 32.90 C ANISOU 357 C THR B 47 4405 4460 3634 -205 58 935 C ATOM 358 O THR A 47 48.550 66.155 15.945 1.00 33.63 O ANISOU 358 O THR B 47 4046 4683 4048 -241 43 705 O ATOM 359 CB THR A 47 48.107 65.402 18.923 1.00 30.82 C ANISOU 359 CB THR B 47 4163 4178 3369 -198 1031 189 C ATOM 360 OG1 THR A 47 48.918 64.219 19.088 1.00 33.92 O ANISOU 360 OG1 THR B 47 4147 5056 3687 -660 646 709 O ATOM 361 CG2 THR A 47 47.318 65.628 20.214 1.00 31.26 C ANISOU 361 CG2 THR B 47 3715 4857 3305 -117 1007 160 C ATOM 362 N THR A 48 48.359 63.920 15.929 1.00 29.54 N ANISOU 362 N THR B 48 4228 3914 3080 -357 324 878 N ATOM 363 CA THR A 48 49.153 63.845 14.694 1.00 27.79 C ANISOU 363 CA THR B 48 3417 3989 3153 -39 813 442 C ATOM 364 C THR A 48 48.391 64.391 13.488 1.00 28.17 C ANISOU 364 C THR B 48 3178 4078 3446 -129 980 221 C ATOM 365 O THR A 48 48.940 65.147 12.690 1.00 30.90 O ANISOU 365 O THR B 48 4012 4516 3213 -461 995 -116 O ATOM 366 CB THR A 48 49.602 62.394 14.439 1.00 28.55 C ANISOU 366 CB THR B 48 3209 4227 3412 -173 1019 -331 C ATOM 367 OG1 THR A 48 50.440 61.965 15.518 1.00 29.67 O ANISOU 367 OG1 THR B 48 3288 4736 3250 -144 689 174 O ATOM 368 CG2 THR A 48 50.445 62.280 13.180 1.00 27.34 C ANISOU 368 CG2 THR B 48 3844 3330 3213 -240 602 305 C ATOM 369 N TYR A 49 47.126 64.035 13.318 1.00 29.41 N ANISOU 369 N TYR B 49 3728 4195 3251 -350 798 446 N ATOM 370 CA TYR A 49 46.264 64.518 12.243 1.00 29.62 C ANISOU 370 CA TYR B 49 3529 4508 3217 -357 716 488 C ATOM 371 C TYR A 49 46.107 66.033 12.350 1.00 31.06 C ANISOU 371 C TYR B 49 3479 4980 3342 -281 483 -129 C ATOM 372 O TYR A 49 46.227 66.779 11.373 1.00 32.01 O ANISOU 372 O TYR B 49 3581 5256 3326 -193 493 -166 O ATOM 373 CB TYR A 49 44.903 63.816 12.268 1.00 28.70 C ANISOU 373 CB TYR B 49 3729 4516 2661 -593 763 432 C ATOM 374 CG TYR A 49 44.996 62.371 11.826 1.00 28.86 C ANISOU 374 CG TYR B 49 3899 4225 2843 -562 643 535 C ATOM 375 CD1 TYR A 49 45.657 62.029 10.644 1.00 29.67 C ANISOU 375 CD1 TYR B 49 3644 4428 3202 -472 600 139 C ATOM 376 CD2 TYR A 49 44.432 61.341 12.570 1.00 28.94 C ANISOU 376 CD2 TYR B 49 4228 4131 2636 -369 435 627 C ATOM 377 CE1 TYR A 49 45.743 60.703 10.233 1.00 30.68 C ANISOU 377 CE1 TYR B 49 4273 3965 3417 -273 178 282 C ATOM 378 CE2 TYR A 49 44.511 60.001 12.173 1.00 29.44 C ANISOU 378 CE2 TYR B 49 4204 4244 2736 -319 475 638 C ATOM 379 CZ TYR A 49 45.173 59.705 11.004 1.00 30.49 C ANISOU 379 CZ TYR B 49 4441 3847 3297 -119 27 397 C ATOM 380 OH TYR A 49 45.271 58.402 10.581 1.00 29.81 O ANISOU 380 OH TYR B 49 4119 4185 3023 -249 372 598 O ATOM 381 N LYS A 50 45.859 66.502 13.578 1.00 30.55 N ANISOU 381 N LYS B 50 3676 4614 3316 -206 455 -43 N ATOM 382 CA LYS A 50 45.753 67.944 13.797 1.00 33.48 C ANISOU 382 CA LYS B 50 3763 4868 4090 -138 300 528 C ATOM 383 C LYS A 50 47.030 68.634 13.330 1.00 34.21 C ANISOU 383 C LYS B 50 3396 4891 4709 5 747 390 C ATOM 384 O LYS A 50 46.959 69.665 12.637 1.00 34.90 O ANISOU 384 O LYS B 50 3537 5537 4188 130 643 348 O ATOM 385 CB LYS A 50 45.457 68.245 15.265 1.00 36.30 C ANISOU 385 CB LYS B 50 3582 6026 4183 140 229 363 C ATOM 386 CG LYS A 50 45.718 69.691 15.652 1.00 44.99 C ANISOU 386 CG LYS B 50 4759 6862 5473 802 -824 439 C ATOM 387 CD LYS A 50 45.773 69.862 17.164 1.00 58.15 C ANISOU 387 CD LYS B 50 7857 8435 5801 -219 -2354 1304 C ATOM 388 CE LYS A 50 45.797 71.310 17.640 1.00 62.07 C ANISOU 388 CE LYS B 50 7631 9259 6695 -492 -3182 1119 C ATOM 389 NZ LYS A 50 44.665 71.674 18.534 1.00 67.58 N ANISOU 389 NZ LYS B 50 6656 10188 8835 -1236 -2240 -114 N ATOM 390 N ALA A 51 48.204 68.111 13.672 1.00 33.07 N ANISOU 390 N ALA B 51 3618 4766 4180 -56 576 739 N ATOM 391 CA ALA A 51 49.442 68.737 13.222 1.00 38.48 C ANISOU 391 CA ALA B 51 5429 4882 4308 -518 249 671 C ATOM 392 C ALA A 51 49.689 68.563 11.729 1.00 37.45 C ANISOU 392 C ALA B 51 5427 4726 4077 -234 819 774 C ATOM 393 O ALA A 51 50.202 69.465 11.043 1.00 39.04 O ANISOU 393 O ALA B 51 5435 4712 4686 -181 578 452 O ATOM 394 CB ALA A 51 50.628 68.162 13.994 1.00 38.64 C ANISOU 394 CB ALA B 51 6696 4148 3837 -483 1315 -169 C ATOM 395 N LEU A 52 49.345 67.396 11.173 1.00 35.68 N ANISOU 395 N LEU B 52 5046 4696 3814 -349 927 699 N ATOM 396 CA LEU A 52 49.493 67.232 9.728 1.00 33.57 C ANISOU 396 CA LEU B 52 4097 4791 3867 -151 930 194 C ATOM 397 C LEU A 52 48.647 68.271 8.991 1.00 36.49 C ANISOU 397 C LEU B 52 4286 5492 4087 -463 1111 -39 C ATOM 398 O LEU A 52 49.087 68.920 8.037 1.00 38.80 O ANISOU 398 O LEU B 52 4941 5301 4500 -245 1690 70 O ATOM 399 CB LEU A 52 49.067 65.832 9.300 1.00 35.41 C ANISOU 399 CB LEU B 52 4291 4751 4413 -274 184 39 C ATOM 400 CG LEU A 52 50.114 64.737 9.214 1.00 38.29 C ANISOU 400 CG LEU B 52 4407 4980 5163 -433 -340 505 C ATOM 401 CD1 LEU A 52 49.463 63.410 8.848 1.00 45.21 C ANISOU 401 CD1 LEU B 52 4596 5953 6630 -275 -507 2054 C ATOM 402 CD2 LEU A 52 51.205 65.125 8.216 1.00 41.23 C ANISOU 402 CD2 LEU B 52 5482 6511 3672 -1048 -925 517 C ATOM 403 N VAL A 53 47.399 68.432 9.430 1.00 34.15 N ANISOU 403 N VAL B 53 3484 5648 3844 -77 -36 542 N ATOM 404 CA VAL A 53 46.540 69.416 8.767 1.00 34.02 C ANISOU 404 CA VAL B 53 3492 5687 3746 6 -38 663 C ATOM 405 C VAL A 53 47.136 70.819 8.776 1.00 35.71 C ANISOU 405 C VAL B 53 3968 5688 3913 210 505 903 C ATOM 406 O VAL A 53 47.102 71.592 7.800 1.00 37.15 O ANISOU 406 O VAL B 53 5239 5205 3671 335 614 801 O ATOM 407 CB VAL A 53 45.174 69.383 9.469 1.00 34.43 C ANISOU 407 CB VAL B 53 3146 5744 4193 115 -316 640 C ATOM 408 CG1 VAL A 53 44.343 70.597 9.082 1.00 34.38 C ANISOU 408 CG1 VAL B 53 3037 5677 4350 336 -480 1600 C ATOM 409 CG2 VAL A 53 44.479 68.078 9.113 1.00 32.94 C ANISOU 409 CG2 VAL B 53 3012 5751 3754 300 394 532 C ATOM 410 N GLU A 54 47.721 71.152 9.926 1.00 36.62 N ANISOU 410 N GLU B 54 4243 5648 4023 367 921 994 N ATOM 411 CA GLU A 54 48.329 72.447 10.164 1.00 37.38 C ANISOU 411 CA GLU B 54 4634 5511 4059 340 472 836 C ATOM 412 C GLU A 54 49.471 72.693 9.174 1.00 38.61 C ANISOU 412 C GLU B 54 4553 5914 4205 351 560 489 C ATOM 413 O GLU A 54 49.579 73.758 8.550 1.00 41.06 O ANISOU 413 O GLU B 54 4916 6097 4589 -34 1338 407 O ATOM 414 CB GLU A 54 48.850 72.583 11.605 1.00 41.10 C ANISOU 414 CB GLU B 54 5125 6523 3967 353 -3 1093 C ATOM 415 CG GLU A 54 47.975 73.358 12.560 1.00 58.89 C ANISOU 415 CG GLU B 54 8324 8511 5542 -1348 -2116 1608 C ATOM 416 CD GLU A 54 48.296 73.112 14.025 1.00 65.60 C ANISOU 416 CD GLU B 54 9639 10092 5195 -2264 -2694 1559 C ATOM 417 OE1 GLU A 54 49.243 72.370 14.376 1.00 88.06 O ANISOU 417 OE1 GLU B 54 13342 12442 7675 -5923 49 1437 O ATOM 418 OE2 GLU A 54 47.586 73.676 14.894 1.00 87.65 O ANISOU 418 OE2 GLU B 54 14582 11984 6736 -3012 -5420 578 O ATOM 419 N MET A 55 50.321 71.681 9.055 1.00 39.25 N ANISOU 419 N MET B 55 4572 5933 4408 388 290 604 N ATOM 420 CA MET A 55 51.462 71.789 8.151 1.00 40.82 C ANISOU 420 CA MET B 55 5468 5886 4156 -399 382 995 C ATOM 421 C MET A 55 51.037 71.929 6.695 1.00 40.32 C ANISOU 421 C MET B 55 5277 5804 4237 -258 593 957 C ATOM 422 O MET A 55 51.664 72.600 5.857 1.00 41.77 O ANISOU 422 O MET B 55 5137 5985 4748 -205 1262 839 O ATOM 423 CB MET A 55 52.327 70.537 8.352 1.00 37.31 C ANISOU 423 CB MET B 55 5429 5474 3274 -54 447 305 C ATOM 424 CG MET A 55 52.919 70.495 9.759 1.00 37.55 C ANISOU 424 CG MET B 55 5293 5936 3040 76 223 264 C ATOM 425 SD MET A 55 54.000 69.067 9.976 1.00 42.14 S ANISOU 425 SD MET B 55 5526 5570 4915 -157 981 545 S ATOM 426 CE MET A 55 55.483 69.621 9.118 1.00 45.49 C ANISOU 426 CE MET B 55 6271 6996 4015 -1031 738 -217 C ATOM 427 N HIS A 56 49.931 71.248 6.380 1.00 40.28 N ANISOU 427 N HIS B 56 4606 5840 4861 -327 1653 1152 N ATOM 428 CA HIS A 56 49.359 71.301 5.032 1.00 36.50 C ANISOU 428 CA HIS B 56 4299 5254 4317 438 1371 679 C ATOM 429 C HIS A 56 48.892 72.720 4.766 1.00 37.39 C ANISOU 429 C HIS B 56 4325 5505 4376 325 1460 -163 C ATOM 430 O HIS A 56 49.116 73.382 3.753 1.00 42.59 O ANISOU 430 O HIS B 56 5264 6224 4696 -194 2341 -302 O ATOM 431 CB HIS A 56 48.180 70.329 4.898 1.00 35.48 C ANISOU 431 CB HIS B 56 4505 5119 3858 263 1363 337 C ATOM 432 CG HIS A 56 47.475 70.531 3.584 1.00 35.58 C ANISOU 432 CG HIS B 56 4589 4952 3976 201 1449 293 C ATOM 433 ND1 HIS A 56 48.112 70.410 2.365 1.00 35.66 N ANISOU 433 ND1 HIS B 56 4452 5245 3851 87 1267 567 N ATOM 434 CD2 HIS A 56 46.197 70.872 3.303 1.00 37.60 C ANISOU 434 CD2 HIS B 56 5221 4959 4106 -114 1382 360 C ATOM 435 CE1 HIS A 56 47.257 70.654 1.391 1.00 37.12 C ANISOU 435 CE1 HIS B 56 4915 5180 4010 -158 1590 277 C ATOM 436 NE2 HIS A 56 46.079 70.937 1.925 1.00 37.17 N ANISOU 436 NE2 HIS B 56 4672 5325 4126 -86 1582 188 N ATOM 437 N LYS A 57 48.177 73.230 5.779 1.00 41.30 N ANISOU 437 N LYS B 57 4464 6290 4937 -121 1128 -94 N ATOM 438 CA LYS A 57 47.640 74.588 5.605 1.00 43.41 C ANISOU 438 CA LYS B 57 4456 6226 5813 -116 1049 104 C ATOM 439 C LYS A 57 48.778 75.585 5.557 1.00 44.80 C ANISOU 439 C LYS B 57 4939 6334 5749 138 1462 5 C ATOM 440 O LYS A 57 48.686 76.629 4.911 1.00 50.05 O ANISOU 440 O LYS B 57 5462 6879 6674 355 2127 44 O ATOM 441 CB LYS A 57 46.605 74.868 6.701 1.00 44.48 C ANISOU 441 CB LYS B 57 4340 6575 5985 166 906 -158 C ATOM 442 CG LYS A 57 45.473 73.840 6.643 1.00 51.01 C ANISOU 442 CG LYS B 57 6070 6341 6971 -158 1498 -455 C ATOM 443 CD LYS A 57 44.349 74.216 7.588 1.00 56.88 C ANISOU 443 CD LYS B 57 6968 7301 7343 -997 1728 -1021 C ATOM 444 CE LYS A 57 42.998 73.947 6.938 1.00 64.05 C ANISOU 444 CE LYS B 57 8349 7361 8627 -1687 2644 -1279 C ATOM 445 NZ LYS A 57 41.873 74.099 7.922 1.00 78.18 N ANISOU 445 NZ LYS B 57 13083 8827 7794 -4030 3470 -2024 N ATOM 446 N ALA A 58 49.907 75.300 6.192 1.00 42.30 N ANISOU 446 N ALA B 58 4369 5980 5724 145 968 -91 N ATOM 447 CA ALA A 58 51.003 76.255 6.174 1.00 42.20 C ANISOU 447 CA ALA B 58 3914 6116 6006 458 1348 -142 C ATOM 448 C ALA A 58 51.778 76.126 4.876 1.00 43.86 C ANISOU 448 C ALA B 58 5241 5672 5750 264 1375 67 C ATOM 449 O ALA A 58 52.796 76.791 4.681 1.00 47.11 O ANISOU 449 O ALA B 58 5609 5777 6512 631 1364 -245 O ATOM 450 CB ALA A 58 51.918 76.022 7.367 1.00 40.88 C ANISOU 450 CB ALA B 58 4030 5802 5701 512 1062 -162 C ATOM 451 N GLY A 59 51.304 75.262 3.990 1.00 42.92 N ANISOU 451 N GLY B 59 4849 5919 5541 87 1691 300 N ATOM 452 CA GLY A 59 51.958 75.054 2.716 1.00 41.52 C ANISOU 452 CA GLY B 59 5229 5218 5327 449 1947 220 C ATOM 453 C GLY A 59 53.208 74.204 2.827 1.00 42.22 C ANISOU 453 C GLY B 59 5145 5719 5179 358 1743 -268 C ATOM 454 O GLY A 59 54.090 74.335 1.958 1.00 50.77 O ANISOU 454 O GLY B 59 6546 7108 5637 -812 2419 -1105 O ATOM 455 N GLN A 60 53.341 73.334 3.840 1.00 40.36 N ANISOU 455 N GLN B 60 5158 5593 4585 343 1617 281 N ATOM 456 CA GLN A 60 54.592 72.572 3.927 1.00 42.17 C ANISOU 456 CA GLN B 60 5305 5372 5345 297 1772 391 C ATOM 457 C GLN A 60 54.499 71.187 3.298 1.00 42.03 C ANISOU 457 C GLN B 60 5129 5202 5637 118 1539 193 C ATOM 458 O GLN A 60 55.466 70.439 3.110 1.00 41.80 O ANISOU 458 O GLN B 60 5215 5402 5265 4 1695 -339 O ATOM 459 CB GLN A 60 55.011 72.447 5.389 1.00 43.43 C ANISOU 459 CB GLN B 60 4704 6522 5274 -49 1679 279 C ATOM 460 CG GLN A 60 55.184 73.766 6.130 1.00 49.81 C ANISOU 460 CG GLN B 60 5483 7271 6171 -728 312 1074 C ATOM 461 CD GLN A 60 55.260 73.553 7.631 1.00 56.33 C ANISOU 461 CD GLN B 60 6998 8291 6113 -1600 309 1365 C ATOM 462 OE1 GLN A 60 56.006 72.701 8.111 1.00 64.84 O ANISOU 462 OE1 GLN B 60 8153 10132 6352 -3034 1176 828 O ATOM 463 NE2 GLN A 60 54.499 74.290 8.425 1.00 65.00 N ANISOU 463 NE2 GLN B 60 7738 10357 6604 -1472 135 -715 N ATOM 464 N VAL A 61 53.274 70.792 2.937 1.00 40.33 N ANISOU 464 N VAL B 61 4988 4883 5451 458 1903 -213 N ATOM 465 CA VAL A 61 53.096 69.450 2.389 1.00 38.51 C ANISOU 465 CA VAL B 61 4772 5192 4668 108 1718 -6 C ATOM 466 C VAL A 61 51.825 69.386 1.554 1.00 38.79 C ANISOU 466 C VAL B 61 4662 5459 4616 53 1839 17 C ATOM 467 O VAL A 61 50.803 70.025 1.790 1.00 38.01 O ANISOU 467 O VAL B 61 5177 5154 4111 -178 1776 -439 O ATOM 468 CB VAL A 61 53.061 68.415 3.533 1.00 35.87 C ANISOU 468 CB VAL B 61 3459 5851 4319 38 1149 136 C ATOM 469 CG1 VAL A 61 51.803 68.580 4.379 1.00 34.05 C ANISOU 469 CG1 VAL B 61 3899 4739 4300 -57 1588 390 C ATOM 470 CG2 VAL A 61 53.127 66.969 3.048 1.00 38.36 C ANISOU 470 CG2 VAL B 61 4114 5000 5463 207 905 784 C ATOM 471 N SER A 62 51.879 68.564 0.518 1.00 37.71 N ANISOU 471 N SER B 62 5016 5335 3977 -210 1931 -311 N ATOM 472 CA SER A 62 50.698 68.310 -0.292 1.00 37.37 C ANISOU 472 CA SER B 62 5117 5136 3946 -253 1835 -455 C ATOM 473 C SER A 62 50.395 66.813 -0.320 1.00 36.60 C ANISOU 473 C SER B 62 4929 5187 3790 -330 1269 -663 C ATOM 474 O SER A 62 51.335 66.010 -0.397 1.00 36.49 O ANISOU 474 O SER B 62 5074 5273 3517 -543 949 191 O ATOM 475 CB SER A 62 50.914 68.865 -1.702 1.00 38.05 C ANISOU 475 CB SER B 62 5419 5105 3934 -500 1942 -461 C ATOM 476 OG SER A 62 49.765 68.572 -2.474 1.00 39.31 O ANISOU 476 OG SER B 62 5994 5146 3794 -33 1566 -189 O ATOM 477 N PHE A 63 49.121 66.450 -0.266 1.00 34.91 N ANISOU 477 N PHE B 63 4813 5129 3321 -286 441 -70 N ATOM 478 CA PHE A 63 48.733 65.049 -0.334 1.00 36.39 C ANISOU 478 CA PHE B 63 4612 5181 4035 -376 400 135 C ATOM 479 C PHE A 63 48.176 64.669 -1.705 1.00 36.50 C ANISOU 479 C PHE B 63 4735 4958 4175 -34 786 186 C ATOM 480 O PHE A 63 47.592 63.579 -1.811 1.00 38.39 O ANISOU 480 O PHE B 63 5144 4391 5052 -390 1827 750 O ATOM 481 CB PHE A 63 47.712 64.754 0.772 1.00 36.21 C ANISOU 481 CB PHE B 63 4572 4909 4277 -185 524 46 C ATOM 482 CG PHE A 63 48.379 64.922 2.144 1.00 36.61 C ANISOU 482 CG PHE B 63 4825 4951 4133 -434 306 -78 C ATOM 483 CD1 PHE A 63 49.181 63.932 2.679 1.00 36.87 C ANISOU 483 CD1 PHE B 63 5009 5238 3761 -73 617 -241 C ATOM 484 CD2 PHE A 63 48.191 66.084 2.864 1.00 37.65 C ANISOU 484 CD2 PHE B 63 5038 4681 4585 -129 290 152 C ATOM 485 CE1 PHE A 63 49.824 64.058 3.901 1.00 33.38 C ANISOU 485 CE1 PHE B 63 4701 4616 3368 641 566 -647 C ATOM 486 CE2 PHE A 63 48.808 66.239 4.078 1.00 35.30 C ANISOU 486 CE2 PHE B 63 4691 4592 4131 692 760 -337 C ATOM 487 CZ PHE A 63 49.612 65.235 4.598 1.00 35.04 C ANISOU 487 CZ PHE B 63 4500 4689 4124 616 532 -552 C ATOM 488 N LYS A 64 48.346 65.513 -2.711 1.00 38.20 N ANISOU 488 N LYS B 64 5030 5353 4130 -38 730 -177 N ATOM 489 CA LYS A 64 47.885 65.274 -4.068 1.00 40.02 C ANISOU 489 CA LYS B 64 5502 5507 4198 300 823 -81 C ATOM 490 C LYS A 64 48.341 63.935 -4.637 1.00 37.29 C ANISOU 490 C LYS B 64 5325 4801 4043 -159 918 157 C ATOM 491 O LYS A 64 47.600 63.257 -5.340 1.00 38.94 O ANISOU 491 O LYS B 64 5244 5721 3830 -406 1042 819 O ATOM 492 CB LYS A 64 48.435 66.354 -5.013 1.00 46.94 C ANISOU 492 CB LYS B 64 5209 7329 5298 -39 2426 -724 C ATOM 493 CG LYS A 64 47.408 67.119 -5.818 1.00 63.62 C ANISOU 493 CG LYS B 64 6935 9358 7882 -2352 3791 -1694 C ATOM 494 CD LYS A 64 46.473 67.911 -4.914 1.00 78.52 C ANISOU 494 CD LYS B 64 7690 11352 10791 -3655 2791 -1979 C ATOM 495 CE LYS A 64 45.754 69.029 -5.652 1.00 84.39 C ANISOU 495 CE LYS B 64 7679 12216 12171 -4131 3197 -2918 C ATOM 496 NZ LYS A 64 44.270 68.940 -5.479 1.00 86.17 N ANISOU 496 NZ LYS B 64 6178 12119 14443 -3347 2915 -3978 N ATOM 497 N HIS A 65 49.591 63.553 -4.347 1.00 36.57 N ANISOU 497 N HIS B 65 5551 4340 4002 -26 1786 -468 N ATOM 498 CA HIS A 65 50.072 62.260 -4.842 1.00 38.83 C ANISOU 498 CA HIS B 65 5328 5346 4082 -462 1852 -408 C ATOM 499 C HIS A 65 50.446 61.341 -3.686 1.00 38.25 C ANISOU 499 C HIS B 65 5120 5684 3728 -1069 1583 -694 C ATOM 500 O HIS A 65 51.424 60.588 -3.718 1.00 41.41 O ANISOU 500 O HIS B 65 5806 6432 3494 -2087 1577 86 O ATOM 501 CB HIS A 65 51.249 62.444 -5.813 1.00 40.34 C ANISOU 501 CB HIS B 65 5878 5839 3610 -755 1960 -446 C ATOM 502 CG HIS A 65 50.787 63.307 -6.965 1.00 40.80 C ANISOU 502 CG HIS B 65 5719 5801 3983 -378 2110 -308 C ATOM 503 ND1 HIS A 65 49.657 62.989 -7.684 1.00 43.19 N ANISOU 503 ND1 HIS B 65 6066 5694 4649 -380 2888 -350 N ATOM 504 CD2 HIS A 65 51.259 64.447 -7.498 1.00 40.00 C ANISOU 504 CD2 HIS B 65 5536 5771 3890 -317 1611 -476 C ATOM 505 CE1 HIS A 65 49.453 63.892 -8.629 1.00 42.44 C ANISOU 505 CE1 HIS B 65 5471 5790 4863 -448 2721 -458 C ATOM 506 NE2 HIS A 65 50.415 64.792 -8.538 1.00 41.61 N ANISOU 506 NE2 HIS B 65 5402 5891 4518 -294 2141 -579 N ATOM 507 N VAL A 66 49.644 61.403 -2.627 1.00 37.49 N ANISOU 507 N VAL B 66 5759 5103 3382 -1048 1137 -45 N ATOM 508 CA VAL A 66 49.807 60.503 -1.486 1.00 32.58 C ANISOU 508 CA VAL B 66 4729 4641 3010 -406 319 -29 C ATOM 509 C VAL A 66 48.635 59.525 -1.533 1.00 33.64 C ANISOU 509 C VAL B 66 4180 4617 3983 -624 -195 260 C ATOM 510 O VAL A 66 47.483 59.936 -1.667 1.00 33.70 O ANISOU 510 O VAL B 66 4237 4861 3709 -609 849 178 O ATOM 511 CB VAL A 66 49.880 61.235 -0.138 1.00 30.79 C ANISOU 511 CB VAL B 66 3995 4534 3171 -53 257 -274 C ATOM 512 CG1 VAL A 66 49.871 60.226 0.999 1.00 28.54 C ANISOU 512 CG1 VAL B 66 3481 4398 2965 -354 114 -163 C ATOM 513 CG2 VAL A 66 51.133 62.095 -0.081 1.00 30.17 C ANISOU 513 CG2 VAL B 66 4545 4483 2433 -485 1011 -15 C ATOM 514 N VAL A 67 48.946 58.246 -1.450 1.00 31.87 N ANISOU 514 N VAL B 67 4128 4521 3461 -709 -113 361 N ATOM 515 CA VAL A 67 47.922 57.203 -1.425 1.00 30.76 C ANISOU 515 CA VAL B 67 4351 4529 2807 -642 557 496 C ATOM 516 C VAL A 67 47.860 56.676 -0.004 1.00 32.92 C ANISOU 516 C VAL B 67 5272 4611 2623 -1317 528 447 C ATOM 517 O VAL A 67 48.928 56.505 0.571 1.00 30.50 O ANISOU 517 O VAL B 67 4243 4471 2876 -943 593 329 O ATOM 518 CB VAL A 67 48.253 56.071 -2.413 1.00 29.57 C ANISOU 518 CB VAL B 67 4338 4257 2639 -267 644 21 C ATOM 519 CG1 VAL A 67 47.486 54.791 -2.135 1.00 30.25 C ANISOU 519 CG1 VAL B 67 3849 4230 3417 -556 1119 -73 C ATOM 520 CG2 VAL A 67 48.008 56.578 -3.844 1.00 30.09 C ANISOU 520 CG2 VAL B 67 4433 4375 2624 -348 692 -66 C ATOM 521 N THR A 68 46.673 56.443 0.535 1.00 28.03 N ANISOU 521 N THR B 68 3537 4225 2890 -529 249 556 N ATOM 522 CA THR A 68 46.583 55.960 1.895 1.00 29.02 C ANISOU 522 CA THR B 68 3571 4427 3030 -384 231 247 C ATOM 523 C THR A 68 45.791 54.656 1.988 1.00 30.37 C ANISOU 523 C THR B 68 3931 4335 3271 -363 415 481 C ATOM 524 O THR A 68 44.878 54.438 1.191 1.00 30.55 O ANISOU 524 O THR B 68 3681 5014 2912 -8 120 888 O ATOM 525 CB THR A 68 45.900 56.975 2.840 1.00 29.30 C ANISOU 525 CB THR B 68 3836 4069 3229 -676 13 152 C ATOM 526 OG1 THR A 68 44.549 57.178 2.379 1.00 32.78 O ANISOU 526 OG1 THR B 68 4298 4521 3636 -1125 476 -23 O ATOM 527 CG2 THR A 68 46.580 58.331 2.840 1.00 29.46 C ANISOU 527 CG2 THR B 68 3888 4619 2685 -190 116 216 C ATOM 528 N PHE A 69 46.152 53.856 2.988 1.00 26.17 N ANISOU 528 N PHE B 69 3142 3973 2828 -405 -171 461 N ATOM 529 CA PHE A 69 45.512 52.616 3.380 1.00 28.36 C ANISOU 529 CA PHE B 69 4053 3805 2918 -327 39 377 C ATOM 530 C PHE A 69 45.225 52.670 4.874 1.00 28.95 C ANISOU 530 C PHE B 69 4260 3775 2963 -296 -115 416 C ATOM 531 O PHE A 69 46.176 52.869 5.664 1.00 28.25 O ANISOU 531 O PHE B 69 3897 3916 2922 -395 166 336 O ATOM 532 CB PHE A 69 46.403 51.413 3.073 1.00 27.11 C ANISOU 532 CB PHE B 69 3946 3445 2910 366 -37 248 C ATOM 533 CG PHE A 69 46.468 51.065 1.589 1.00 29.98 C ANISOU 533 CG PHE B 69 4332 4143 2916 -201 -101 390 C ATOM 534 CD1 PHE A 69 47.488 51.534 0.778 1.00 28.94 C ANISOU 534 CD1 PHE B 69 3373 4621 3001 -218 45 10 C ATOM 535 CD2 PHE A 69 45.490 50.258 1.011 1.00 29.05 C ANISOU 535 CD2 PHE B 69 3395 4491 3153 -163 -363 721 C ATOM 536 CE1 PHE A 69 47.515 51.208 -0.580 1.00 32.19 C ANISOU 536 CE1 PHE B 69 4194 4791 3244 -637 -524 139 C ATOM 537 CE2 PHE A 69 45.510 49.932 -0.347 1.00 29.75 C ANISOU 537 CE2 PHE B 69 3479 4711 3115 -454 -360 666 C ATOM 538 CZ PHE A 69 46.536 50.413 -1.150 1.00 30.71 C ANISOU 538 CZ PHE B 69 3704 4962 3002 -824 566 495 C ATOM 539 N ASN A 70 43.970 52.502 5.274 1.00 30.06 N ANISOU 539 N ASN B 70 4586 4001 2834 -680 375 281 N ATOM 540 CA ASN A 70 43.668 52.489 6.713 1.00 29.07 C ANISOU 540 CA ASN B 70 4588 3587 2872 -24 68 333 C ATOM 541 C ASN A 70 43.715 51.071 7.269 1.00 29.49 C ANISOU 541 C ASN B 70 4517 3953 2734 -58 233 569 C ATOM 542 O ASN A 70 43.474 50.093 6.548 1.00 31.09 O ANISOU 542 O ASN B 70 3473 5192 3147 -294 65 920 O ATOM 543 CB ASN A 70 42.300 53.121 6.953 1.00 29.68 C ANISOU 543 CB ASN B 70 4644 4010 2622 -236 660 -339 C ATOM 544 CG ASN A 70 42.466 54.544 7.445 1.00 30.70 C ANISOU 544 CG ASN B 70 4485 4351 2830 -322 261 -659 C ATOM 545 OD1 ASN A 70 42.727 55.442 6.643 1.00 29.40 O ANISOU 545 OD1 ASN B 70 3944 4144 3082 -610 749 -266 O ATOM 546 ND2 ASN A 70 42.314 54.743 8.759 1.00 31.69 N ANISOU 546 ND2 ASN B 70 4365 4965 2709 -885 503 -33 N ATOM 547 N MET A 71 44.017 50.921 8.548 1.00 30.26 N ANISOU 547 N MET B 71 4718 4257 2522 -619 19 126 N ATOM 548 CA MET A 71 44.198 49.629 9.188 1.00 35.32 C ANISOU 548 CA MET B 71 5264 4956 3202 -786 731 -453 C ATOM 549 C MET A 71 42.913 48.814 9.307 1.00 33.84 C ANISOU 549 C MET B 71 4434 4942 3480 -273 159 -110 C ATOM 550 O MET A 71 42.960 47.582 9.244 1.00 34.08 O ANISOU 550 O MET B 71 4080 5334 3533 -667 -539 991 O ATOM 551 CB MET A 71 44.770 49.791 10.622 1.00 33.33 C ANISOU 551 CB MET B 71 4725 4761 3178 347 567 -368 C ATOM 552 CG MET A 71 46.182 50.324 10.695 1.00 39.27 C ANISOU 552 CG MET B 71 5876 5010 4034 -447 1789 -208 C ATOM 553 SD MET A 71 46.985 50.124 12.304 1.00 43.40 S ANISOU 553 SD MET B 71 6840 5791 3859 -207 1793 -100 S ATOM 554 CE MET A 71 45.548 50.118 13.383 1.00 41.95 C ANISOU 554 CE MET B 71 7854 4657 3430 -390 565 1391 C ATOM 555 N ASP A 72 41.772 49.490 9.521 1.00 27.73 N ANISOU 555 N ASP B 72 3999 3840 2697 424 -414 894 N ATOM 556 CA ASP A 72 40.579 48.715 9.819 1.00 33.08 C ANISOU 556 CA ASP B 72 4116 4226 4227 316 867 -224 C ATOM 557 C ASP A 72 39.273 49.477 9.609 1.00 34.95 C ANISOU 557 C ASP B 72 4227 4434 4617 -87 -49 -111 C ATOM 558 O ASP A 72 39.278 50.675 9.303 1.00 34.87 O ANISOU 558 O ASP B 72 4536 4410 4302 -599 1563 41 O ATOM 559 CB ASP A 72 40.695 48.232 11.266 1.00 44.06 C ANISOU 559 CB ASP B 72 8100 4460 4179 -904 1573 -158 C ATOM 560 CG ASP A 72 41.320 49.217 12.227 1.00 45.45 C ANISOU 560 CG ASP B 72 7717 5146 4405 -817 1610 227 C ATOM 561 OD1 ASP A 72 41.168 50.454 12.074 1.00 53.37 O ANISOU 561 OD1 ASP B 72 7062 6641 6577 -863 359 -146 O ATOM 562 OD2 ASP A 72 41.981 48.753 13.176 1.00 51.96 O ANISOU 562 OD2 ASP B 72 9349 5745 4650 -1909 1927 489 O ATOM 563 N GLU A 73 38.161 48.754 9.770 1.00 36.89 N ANISOU 563 N GLU B 73 5316 4442 4257 -233 830 -91 N ATOM 564 CA GLU A 73 36.795 49.258 9.672 1.00 39.23 C ANISOU 564 CA GLU B 73 6067 4619 4219 -758 722 -146 C ATOM 565 C GLU A 73 35.823 48.295 10.352 1.00 37.56 C ANISOU 565 C GLU B 73 5713 4623 3935 -492 333 21 C ATOM 566 O GLU A 73 36.024 47.075 10.394 1.00 40.77 O ANISOU 566 O GLU B 73 5444 5701 4344 -700 972 -594 O ATOM 567 CB GLU A 73 36.407 49.504 8.209 1.00 34.97 C ANISOU 567 CB GLU B 73 4785 4198 4304 107 553 228 C ATOM 568 CG GLU A 73 35.040 50.123 7.972 1.00 42.01 C ANISOU 568 CG GLU B 73 5410 5682 4869 -845 554 426 C ATOM 569 CD GLU A 73 34.822 51.490 8.617 1.00 41.86 C ANISOU 569 CD GLU B 73 5233 6069 4603 -1168 280 -224 C ATOM 570 OE1 GLU A 73 34.561 51.513 9.849 1.00 39.20 O ANISOU 570 OE1 GLU B 73 4960 5439 4493 -1399 763 -263 O ATOM 571 OE2 GLU A 73 34.908 52.507 7.857 1.00 38.00 O ANISOU 571 OE2 GLU B 73 4982 6112 3345 -1143 204 643 O ATOM 572 N TYR A 74 34.746 48.862 10.910 1.00 37.36 N ANISOU 572 N TYR B 74 5673 4875 3647 -565 541 -202 N ATOM 573 CA TYR A 74 33.689 48.041 11.479 1.00 41.28 C ANISOU 573 CA TYR B 74 5667 5053 4964 -481 541 -711 C ATOM 574 C TYR A 74 32.885 47.332 10.397 1.00 41.19 C ANISOU 574 C TYR B 74 5495 4709 5448 -293 751 -648 C ATOM 575 O TYR A 74 32.615 47.874 9.312 1.00 39.71 O ANISOU 575 O TYR B 74 5055 4567 5465 -126 667 -328 O ATOM 576 CB TYR A 74 32.705 48.869 12.294 1.00 41.08 C ANISOU 576 CB TYR B 74 5489 4886 5233 -454 679 -990 C ATOM 577 CG TYR A 74 33.229 49.325 13.631 1.00 43.17 C ANISOU 577 CG TYR B 74 6067 5477 4860 -1198 336 -1187 C ATOM 578 CD1 TYR A 74 33.650 48.436 14.604 1.00 45.76 C ANISOU 578 CD1 TYR B 74 6685 5643 5060 -1237 755 -1295 C ATOM 579 CD2 TYR A 74 33.297 50.685 13.908 1.00 43.30 C ANISOU 579 CD2 TYR B 74 5970 6098 4385 -1347 42 -628 C ATOM 580 CE1 TYR A 74 34.122 48.914 15.813 1.00 50.27 C ANISOU 580 CE1 TYR B 74 7361 6441 5297 -1381 916 -798 C ATOM 581 CE2 TYR A 74 33.765 51.168 15.110 1.00 46.74 C ANISOU 581 CE2 TYR B 74 6844 6625 4291 -1476 254 -474 C ATOM 582 CZ TYR A 74 34.183 50.269 16.071 1.00 50.91 C ANISOU 582 CZ TYR B 74 7258 7085 5001 -1429 845 -134 C ATOM 583 OH TYR A 74 34.652 50.747 17.280 1.00 55.75 O ANISOU 583 OH TYR B 74 8276 8611 4294 -813 895 -463 O ATOM 584 N VAL A 75 32.500 46.105 10.726 1.00 42.13 N ANISOU 584 N VAL B 75 4919 5224 5863 -261 738 -759 N ATOM 585 CA VAL A 75 31.667 45.327 9.806 1.00 47.19 C ANISOU 585 CA VAL B 75 5788 5097 7045 -33 166 -493 C ATOM 586 C VAL A 75 30.196 45.662 10.055 1.00 48.55 C ANISOU 586 C VAL B 75 6285 5224 6940 -454 735 -542 C ATOM 587 O VAL A 75 29.828 45.741 11.238 1.00 48.47 O ANISOU 587 O VAL B 75 5693 5860 6862 -1170 726 -226 O ATOM 588 CB VAL A 75 31.911 43.817 9.982 1.00 48.86 C ANISOU 588 CB VAL B 75 6013 5205 7348 131 647 -104 C ATOM 589 CG1 VAL A 75 30.770 43.020 9.356 1.00 53.29 C ANISOU 589 CG1 VAL B 75 6667 5126 8455 481 1334 91 C ATOM 590 CG2 VAL A 75 33.257 43.381 9.404 1.00 43.92 C ANISOU 590 CG2 VAL B 75 5319 5653 5715 67 1547 -167 C ATOM 591 N GLY A 76 29.398 45.864 9.021 1.00 50.75 N ANISOU 591 N GLY B 76 7221 5344 6717 -516 356 -120 N ATOM 592 CA GLY A 76 27.966 46.076 9.073 1.00 50.36 C ANISOU 592 CA GLY B 76 6827 5542 6765 -498 1207 -437 C ATOM 593 C GLY A 76 27.517 47.434 9.554 1.00 52.70 C ANISOU 593 C GLY B 76 6657 6001 7365 -559 1338 -104 C ATOM 594 O GLY A 76 26.340 47.734 9.776 1.00 53.35 O ANISOU 594 O GLY B 76 6451 6305 7513 -727 1657 -39 O ATOM 595 N LEU A 77 28.459 48.347 9.753 1.00 51.62 N ANISOU 595 N LEU B 77 6184 6058 7372 -182 2057 -442 N ATOM 596 CA LEU A 77 28.105 49.699 10.181 1.00 51.42 C ANISOU 596 CA LEU B 77 6268 6170 7100 -353 1735 -602 C ATOM 597 C LEU A 77 27.964 50.524 8.916 1.00 48.97 C ANISOU 597 C LEU B 77 5514 6321 6772 -359 1217 -704 C ATOM 598 O LEU A 77 28.863 50.393 8.071 1.00 53.77 O ANISOU 598 O LEU B 77 7868 6544 6016 -2227 1383 112 O ATOM 599 CB LEU A 77 29.201 50.215 11.086 1.00 52.44 C ANISOU 599 CB LEU B 77 7136 6167 6620 -351 1335 -752 C ATOM 600 CG LEU A 77 28.882 51.084 12.291 1.00 54.52 C ANISOU 600 CG LEU B 77 7227 5709 7779 133 600 -1018 C ATOM 601 CD1 LEU A 77 29.675 52.385 12.216 1.00 54.85 C ANISOU 601 CD1 LEU B 77 5875 7127 7838 795 1700 -2120 C ATOM 602 CD2 LEU A 77 27.397 51.376 12.405 1.00 59.94 C ANISOU 602 CD2 LEU B 77 7100 6902 8774 -680 -44 781 C ATOM 603 N PRO A 78 26.926 51.323 8.715 1.00 49.97 N ANISOU 603 N PRO B 78 5464 6640 6884 -337 1061 -178 N ATOM 604 CA PRO A 78 26.886 52.145 7.489 1.00 51.66 C ANISOU 604 CA PRO B 78 5460 6928 7242 -311 1309 -262 C ATOM 605 C PRO A 78 28.072 53.108 7.428 1.00 48.74 C ANISOU 605 C PRO B 78 5262 6812 6445 -642 1623 -73 C ATOM 606 O PRO A 78 28.365 53.759 8.437 1.00 51.65 O ANISOU 606 O PRO B 78 6508 6970 6146 -1049 2070 410 O ATOM 607 CB PRO A 78 25.575 52.912 7.624 1.00 54.45 C ANISOU 607 CB PRO B 78 6132 6946 7612 -961 1705 -379 C ATOM 608 CG PRO A 78 24.760 52.139 8.605 1.00 52.18 C ANISOU 608 CG PRO B 78 5589 6980 7258 -538 1438 -211 C ATOM 609 CD PRO A 78 25.737 51.513 9.559 1.00 49.69 C ANISOU 609 CD PRO B 78 5322 6615 6941 -498 978 73 C ATOM 610 N LYS A 79 28.752 53.219 6.295 1.00 48.19 N ANISOU 610 N LYS B 79 5083 7123 6104 -876 2386 -94 N ATOM 611 CA LYS A 79 29.906 54.097 6.153 1.00 54.40 C ANISOU 611 CA LYS B 79 7407 6964 6298 -1288 1942 -134 C ATOM 612 C LYS A 79 29.637 55.508 6.664 1.00 53.90 C ANISOU 612 C LYS B 79 7398 6095 6984 -536 2690 4 C ATOM 613 O LYS A 79 30.486 56.126 7.318 1.00 58.96 O ANISOU 613 O LYS B 79 8627 5807 7968 -892 2034 91 O ATOM 614 CB LYS A 79 30.345 54.170 4.687 1.00 64.52 C ANISOU 614 CB LYS B 79 10277 7584 6653 -3394 1702 -620 C ATOM 615 CG LYS A 79 31.336 53.098 4.264 1.00 81.09 C ANISOU 615 CG LYS B 79 12443 9681 8687 -6045 205 -51 C ATOM 616 CD LYS A 79 32.094 53.507 3.000 1.00 94.67 C ANISOU 616 CD LYS B 79 16385 10464 9120 -7758 -149 -552 C ATOM 617 CE LYS A 79 33.192 52.510 2.648 1.00100.31 C ANISOU 617 CE LYS B 79 17239 10681 10196 -8238 -1562 180 C ATOM 618 NZ LYS A 79 34.502 53.123 2.259 1.00 99.23 N ANISOU 618 NZ LYS B 79 16487 9198 12017 -7898 -3093 3219 N ATOM 619 N GLU A 80 28.465 56.070 6.389 1.00 55.66 N ANISOU 619 N GLU B 80 7175 6753 7220 -583 2365 620 N ATOM 620 CA GLU A 80 28.176 57.423 6.860 1.00 59.52 C ANISOU 620 CA GLU B 80 7348 7740 7526 -424 2377 1678 C ATOM 621 C GLU A 80 27.801 57.465 8.335 1.00 58.33 C ANISOU 621 C GLU B 80 7538 6988 7636 -723 2023 1750 C ATOM 622 O GLU A 80 27.510 58.551 8.853 1.00 60.27 O ANISOU 622 O GLU B 80 7470 6869 8561 -1035 1553 1201 O ATOM 623 CB GLU A 80 27.054 58.102 6.058 1.00 68.18 C ANISOU 623 CB GLU B 80 7326 10033 8545 -363 3156 1880 C ATOM 624 CG GLU A 80 27.532 59.340 5.308 1.00 79.36 C ANISOU 624 CG GLU B 80 8602 11058 10492 -46 4197 1108 C ATOM 625 CD GLU A 80 27.096 60.685 5.849 1.00 85.38 C ANISOU 625 CD GLU B 80 8638 11323 12480 946 4294 1367 C ATOM 626 OE1 GLU A 80 26.401 61.453 5.127 1.00 99.94 O ANISOU 626 OE1 GLU B 80 8592 11873 17506 -1411 5570 441 O ATOM 627 OE2 GLU A 80 27.450 61.010 7.010 1.00102.82 O ANISOU 627 OE2 GLU B 80 12178 12381 14509 1275 2104 3815 O ATOM 628 N HIS A 81 27.789 56.353 9.060 1.00 57.52 N ANISOU 628 N HIS B 81 7404 6948 7504 -1180 1928 1251 N ATOM 629 CA HIS A 81 27.647 56.506 10.517 1.00 55.43 C ANISOU 629 CA HIS B 81 5668 7555 7838 -647 972 401 C ATOM 630 C HIS A 81 28.824 57.341 11.004 1.00 51.01 C ANISOU 630 C HIS B 81 5461 7634 6288 -559 567 149 C ATOM 631 O HIS A 81 29.972 57.180 10.580 1.00 45.52 O ANISOU 631 O HIS B 81 5018 7368 4909 -184 648 374 O ATOM 632 CB HIS A 81 27.578 55.143 11.200 1.00 57.02 C ANISOU 632 CB HIS B 81 6080 7270 8314 -800 939 -523 C ATOM 633 CG HIS A 81 27.404 55.205 12.685 1.00 60.06 C ANISOU 633 CG HIS B 81 6354 8163 8302 -1518 1174 -661 C ATOM 634 ND1 HIS A 81 26.213 54.869 13.301 1.00 61.95 N ANISOU 634 ND1 HIS B 81 6815 8307 8417 -1426 1148 -885 N ATOM 635 CD2 HIS A 81 28.214 55.557 13.701 1.00 60.36 C ANISOU 635 CD2 HIS B 81 6050 8619 8265 -1854 520 -442 C ATOM 636 CE1 HIS A 81 26.317 55.014 14.615 1.00 62.89 C ANISOU 636 CE1 HIS B 81 6559 8713 8624 -1590 -243 -604 C ATOM 637 NE2 HIS A 81 27.543 55.438 14.890 1.00 62.21 N ANISOU 637 NE2 HIS B 81 6300 8795 8540 -1619 -512 -427 N ATOM 638 N PRO A 82 28.629 58.279 11.915 1.00 54.15 N ANISOU 638 N PRO B 82 6012 8050 6511 -1228 -93 49 N ATOM 639 CA PRO A 82 29.718 59.169 12.311 1.00 54.66 C ANISOU 639 CA PRO B 82 6053 8363 6353 -1964 -1118 871 C ATOM 640 C PRO A 82 30.872 58.477 13.037 1.00 58.22 C ANISOU 640 C PRO B 82 6080 9549 6492 -2448 -1232 928 C ATOM 641 O PRO A 82 31.964 59.058 13.125 1.00 65.27 O ANISOU 641 O PRO B 82 6657 9514 8628 -3346 -253 386 O ATOM 642 CB PRO A 82 29.041 60.128 13.297 1.00 57.60 C ANISOU 642 CB PRO B 82 6202 8897 6785 -2495 -1300 694 C ATOM 643 CG PRO A 82 27.580 59.997 13.032 1.00 61.64 C ANISOU 643 CG PRO B 82 7485 8655 7281 -2687 -1574 473 C ATOM 644 CD PRO A 82 27.372 58.560 12.616 1.00 61.44 C ANISOU 644 CD PRO B 82 7545 8452 7347 -2048 -486 -22 C ATOM 645 N GLU A 83 30.648 57.280 13.552 1.00 60.08 N ANISOU 645 N GLU B 83 6911 10136 5779 -2649 -491 346 N ATOM 646 CA GLU A 83 31.626 56.478 14.266 1.00 58.75 C ANISOU 646 CA GLU B 83 7323 9833 5165 -2875 -527 401 C ATOM 647 C GLU A 83 32.289 55.435 13.380 1.00 49.36 C ANISOU 647 C GLU B 83 6323 7416 5015 -1136 126 106 C ATOM 648 O GLU A 83 33.179 54.692 13.809 1.00 47.67 O ANISOU 648 O GLU B 83 6268 7574 4270 -680 229 332 O ATOM 649 CB GLU A 83 30.986 55.780 15.469 1.00 72.69 C ANISOU 649 CB GLU B 83 9982 12292 5346 -5237 740 -929 C ATOM 650 CG GLU A 83 30.766 56.704 16.659 1.00 77.05 C ANISOU 650 CG GLU B 83 10408 13710 5159 -4911 703 -1110 C ATOM 651 CD GLU A 83 31.840 57.765 16.802 1.00 80.81 C ANISOU 651 CD GLU B 83 10734 13895 6074 -4907 -9 -221 C ATOM 652 OE1 GLU A 83 33.047 57.446 16.860 1.00 89.49 O ANISOU 652 OE1 GLU B 83 13427 14399 6175 -6529 -398 -45 O ATOM 653 OE2 GLU A 83 31.476 58.965 16.866 1.00 90.04 O ANISOU 653 OE2 GLU B 83 11351 16138 6721 -3189 509 -996 O ATOM 654 N SER A 84 31.926 55.325 12.113 1.00 40.77 N ANISOU 654 N SER B 84 4873 5560 5057 -332 490 -137 N ATOM 655 CA SER A 84 32.697 54.462 11.220 1.00 39.95 C ANISOU 655 CA SER B 84 4506 6067 4608 -437 974 -437 C ATOM 656 C SER A 84 34.120 54.988 11.126 1.00 40.12 C ANISOU 656 C SER B 84 4629 6113 4502 -706 506 137 C ATOM 657 O SER A 84 34.371 56.161 11.438 1.00 39.83 O ANISOU 657 O SER B 84 4325 5873 4937 -1163 135 309 O ATOM 658 CB SER A 84 32.063 54.434 9.832 1.00 36.56 C ANISOU 658 CB SER B 84 3963 5194 4736 -166 963 -458 C ATOM 659 OG SER A 84 32.219 55.687 9.184 1.00 34.84 O ANISOU 659 OG SER B 84 4221 4760 4256 -13 543 -616 O ATOM 660 N TYR A 85 35.054 54.139 10.696 1.00 36.91 N ANISOU 660 N TYR B 85 4557 5925 3540 -512 460 563 N ATOM 661 CA TYR A 85 36.422 54.661 10.579 1.00 38.87 C ANISOU 661 CA TYR B 85 4545 6043 4179 -825 976 304 C ATOM 662 C TYR A 85 36.527 55.549 9.343 1.00 36.56 C ANISOU 662 C TYR B 85 4016 5694 4181 -729 923 584 C ATOM 663 O TYR A 85 37.305 56.509 9.334 1.00 35.47 O ANISOU 663 O TYR B 85 4698 5285 3494 -1150 601 460 O ATOM 664 CB TYR A 85 37.440 53.512 10.600 1.00 41.00 C ANISOU 664 CB TYR B 85 4519 6535 4525 -762 1324 -738 C ATOM 665 CG TYR A 85 37.581 52.871 11.976 1.00 45.44 C ANISOU 665 CG TYR B 85 5347 7087 4830 -1091 1841 -806 C ATOM 666 CD1 TYR A 85 36.884 53.404 13.060 1.00 45.44 C ANISOU 666 CD1 TYR B 85 5931 6893 4440 -1465 2026 -799 C ATOM 667 CD2 TYR A 85 38.379 51.771 12.213 1.00 45.14 C ANISOU 667 CD2 TYR B 85 5301 7010 4841 -551 1953 211 C ATOM 668 CE1 TYR A 85 36.987 52.856 14.312 1.00 45.55 C ANISOU 668 CE1 TYR B 85 5920 6908 4481 -1493 2272 -227 C ATOM 669 CE2 TYR A 85 38.493 51.198 13.461 1.00 45.60 C ANISOU 669 CE2 TYR B 85 5642 6929 4757 -819 2032 397 C ATOM 670 CZ TYR A 85 37.793 51.751 14.497 1.00 46.45 C ANISOU 670 CZ TYR B 85 5882 6851 4915 -1443 2206 28 C ATOM 671 OH TYR A 85 37.875 51.217 15.757 1.00 44.32 O ANISOU 671 OH TYR B 85 5391 6372 5076 -1046 2153 -207 O ATOM 672 N TYR A 86 35.754 55.257 8.293 1.00 34.54 N ANISOU 672 N TYR B 86 3497 5354 4274 -575 813 547 N ATOM 673 CA TYR A 86 35.592 56.164 7.170 1.00 33.41 C ANISOU 673 CA TYR B 86 4260 4623 3814 -451 688 435 C ATOM 674 C TYR A 86 35.305 57.569 7.706 1.00 31.85 C ANISOU 674 C TYR B 86 3948 4639 3515 -459 1061 145 C ATOM 675 O TYR A 86 35.952 58.568 7.341 1.00 35.51 O ANISOU 675 O TYR B 86 3996 5070 4426 -291 1607 -120 O ATOM 676 CB TYR A 86 34.454 55.658 6.291 1.00 36.45 C ANISOU 676 CB TYR B 86 5065 4979 3806 -845 382 679 C ATOM 677 CG TYR A 86 33.895 56.672 5.313 1.00 37.16 C ANISOU 677 CG TYR B 86 5383 4560 4175 -1000 727 667 C ATOM 678 CD1 TYR A 86 34.481 56.782 4.054 1.00 37.49 C ANISOU 678 CD1 TYR B 86 5644 4405 4197 -694 821 588 C ATOM 679 CD2 TYR A 86 32.807 57.499 5.592 1.00 37.27 C ANISOU 679 CD2 TYR B 86 4696 4538 4927 -73 415 567 C ATOM 680 CE1 TYR A 86 34.021 57.681 3.109 1.00 39.99 C ANISOU 680 CE1 TYR B 86 5869 5350 3974 -1235 886 920 C ATOM 681 CE2 TYR A 86 32.341 58.404 4.661 1.00 37.76 C ANISOU 681 CE2 TYR B 86 4554 4612 5179 237 399 437 C ATOM 682 CZ TYR A 86 32.950 58.488 3.424 1.00 41.68 C ANISOU 682 CZ TYR B 86 5611 5481 4744 -869 767 708 C ATOM 683 OH TYR A 86 32.489 59.387 2.486 1.00 41.02 O ANISOU 683 OH TYR B 86 4878 5730 4978 98 398 544 O ATOM 684 N SER A 87 34.301 57.663 8.584 1.00 34.05 N ANISOU 684 N SER B 87 4519 4337 4081 -1045 546 605 N ATOM 685 CA SER A 87 33.839 58.966 9.060 1.00 35.21 C ANISOU 685 CA SER B 87 4647 4861 3871 -770 492 380 C ATOM 686 C SER A 87 34.900 59.661 9.905 1.00 33.45 C ANISOU 686 C SER B 87 4273 4825 3612 -579 739 247 C ATOM 687 O SER A 87 35.107 60.859 9.712 1.00 33.44 O ANISOU 687 O SER B 87 3240 5338 4128 -807 228 544 O ATOM 688 CB SER A 87 32.540 58.854 9.861 1.00 36.43 C ANISOU 688 CB SER B 87 4146 4853 4842 -654 427 102 C ATOM 689 OG SER A 87 31.470 58.576 8.965 1.00 40.72 O ANISOU 689 OG SER B 87 5011 5327 5135 -1476 -398 470 O ATOM 690 N PHE A 88 35.517 58.898 10.807 1.00 33.41 N ANISOU 690 N PHE B 88 3834 4886 3972 -1075 640 82 N ATOM 691 CA PHE A 88 36.627 59.415 11.586 1.00 30.53 C ANISOU 691 CA PHE B 88 3381 4744 3476 -631 655 -81 C ATOM 692 C PHE A 88 37.654 60.012 10.631 1.00 27.74 C ANISOU 692 C PHE B 88 2666 4843 3031 -313 829 50 C ATOM 693 O PHE A 88 38.147 61.109 10.888 1.00 30.41 O ANISOU 693 O PHE B 88 3926 4671 2959 -249 399 384 O ATOM 694 CB PHE A 88 37.287 58.306 12.412 1.00 28.25 C ANISOU 694 CB PHE B 88 3563 3873 3299 -85 756 -130 C ATOM 695 CG PHE A 88 38.552 58.731 13.163 1.00 30.86 C ANISOU 695 CG PHE B 88 3418 4455 3853 -457 419 466 C ATOM 696 CD1 PHE A 88 39.858 58.770 12.654 1.00 31.31 C ANISOU 696 CD1 PHE B 88 4064 4487 3345 -831 875 514 C ATOM 697 CD2 PHE A 88 38.377 59.124 14.487 1.00 32.13 C ANISOU 697 CD2 PHE B 88 3623 4395 4192 -326 -162 629 C ATOM 698 CE1 PHE A 88 40.924 59.211 13.406 1.00 36.09 C ANISOU 698 CE1 PHE B 88 4567 5131 4015 -1525 -609 1295 C ATOM 699 CE2 PHE A 88 39.442 59.546 15.249 1.00 31.90 C ANISOU 699 CE2 PHE B 88 3708 4616 3796 -736 341 500 C ATOM 700 CZ PHE A 88 40.720 59.591 14.732 1.00 33.19 C ANISOU 700 CZ PHE B 88 3783 5050 3779 -1242 -189 845 C ATOM 701 N MET A 89 38.110 59.269 9.621 1.00 29.41 N ANISOU 701 N MET B 89 2935 4876 3362 -421 500 79 N ATOM 702 CA MET A 89 39.248 59.680 8.793 1.00 29.82 C ANISOU 702 CA MET B 89 2897 4849 3585 -631 451 92 C ATOM 703 C MET A 89 38.943 60.938 7.983 1.00 28.85 C ANISOU 703 C MET B 89 3158 4680 3123 -736 546 107 C ATOM 704 O MET A 89 39.810 61.806 7.815 1.00 29.56 O ANISOU 704 O MET B 89 3066 4752 3415 -354 467 598 O ATOM 705 CB MET A 89 39.693 58.552 7.844 1.00 30.13 C ANISOU 705 CB MET B 89 3193 4668 3586 -720 301 308 C ATOM 706 CG MET A 89 40.382 57.407 8.593 1.00 30.03 C ANISOU 706 CG MET B 89 2944 4561 3905 -524 144 731 C ATOM 707 SD MET A 89 41.880 57.980 9.434 1.00 31.40 S ANISOU 707 SD MET B 89 4243 4373 3316 -908 432 245 S ATOM 708 CE MET A 89 42.759 58.748 8.082 1.00 30.87 C ANISOU 708 CE MET B 89 4601 4671 2457 -598 -366 517 C ATOM 709 N HIS A 90 37.712 61.043 7.464 1.00 30.25 N ANISOU 709 N HIS B 90 3395 4865 3233 -852 488 354 N ATOM 710 CA HIS A 90 37.360 62.259 6.726 1.00 31.13 C ANISOU 710 CA HIS B 90 3569 5055 3205 -723 689 800 C ATOM 711 C HIS A 90 37.295 63.457 7.660 1.00 30.39 C ANISOU 711 C HIS B 90 3538 4858 3150 -617 691 477 C ATOM 712 O HIS A 90 37.886 64.518 7.462 1.00 32.67 O ANISOU 712 O HIS B 90 3926 4798 3690 -483 810 703 O ATOM 713 CB HIS A 90 36.030 62.035 5.974 1.00 31.72 C ANISOU 713 CB HIS B 90 3515 5022 3515 -1054 337 785 C ATOM 714 CG HIS A 90 36.284 61.170 4.768 1.00 32.17 C ANISOU 714 CG HIS B 90 4100 4569 3556 -480 217 674 C ATOM 715 ND1 HIS A 90 36.823 61.652 3.592 1.00 29.81 N ANISOU 715 ND1 HIS B 90 3433 4288 3604 -380 177 698 N ATOM 716 CD2 HIS A 90 36.101 59.845 4.551 1.00 33.01 C ANISOU 716 CD2 HIS B 90 4532 4539 3470 -153 107 233 C ATOM 717 CE1 HIS A 90 36.944 60.666 2.712 1.00 28.80 C ANISOU 717 CE1 HIS B 90 3279 3942 3724 65 245 308 C ATOM 718 NE2 HIS A 90 36.509 59.554 3.267 1.00 30.26 N ANISOU 718 NE2 HIS B 90 3720 4212 3567 -19 255 -218 N ATOM 719 N ARG A 91 36.554 63.317 8.750 1.00 33.11 N ANISOU 719 N ARG B 91 4353 4960 3268 -1110 444 493 N ATOM 720 CA ARG A 91 36.369 64.408 9.717 1.00 36.54 C ANISOU 720 CA ARG B 91 4700 5273 3912 -1226 -152 447 C ATOM 721 C ARG A 91 37.663 64.904 10.332 1.00 36.40 C ANISOU 721 C ARG B 91 4322 5316 4192 -652 20 690 C ATOM 722 O ARG A 91 37.796 66.105 10.565 1.00 35.21 O ANISOU 722 O ARG B 91 3853 6253 3272 -721 142 1023 O ATOM 723 CB ARG A 91 35.434 63.902 10.812 1.00 43.09 C ANISOU 723 CB ARG B 91 6615 5891 3866 -2657 -136 202 C ATOM 724 CG ARG A 91 35.368 64.692 12.090 1.00 43.92 C ANISOU 724 CG ARG B 91 6204 5813 4670 -1722 -732 -351 C ATOM 725 CD ARG A 91 34.262 64.114 12.974 1.00 46.77 C ANISOU 725 CD ARG B 91 5724 6840 5208 -1314 -893 -1308 C ATOM 726 NE ARG A 91 34.548 62.798 13.522 1.00 47.83 N ANISOU 726 NE ARG B 91 5608 7281 5286 -1124 -1010 -968 N ATOM 727 CZ ARG A 91 33.872 61.663 13.419 1.00 48.30 C ANISOU 727 CZ ARG B 91 5533 7333 5485 -1133 -564 -607 C ATOM 728 NH1 ARG A 91 32.740 61.566 12.732 1.00 47.57 N ANISOU 728 NH1 ARG B 91 4548 7368 6160 -1242 -543 -593 N ATOM 729 NH2 ARG A 91 34.373 60.596 14.036 1.00 47.84 N ANISOU 729 NH2 ARG B 91 6123 6762 5292 -1219 -18 -561 N ATOM 730 N ASN A 92 38.619 64.027 10.619 1.00 32.32 N ANISOU 730 N ASN B 92 4072 4467 3741 -99 -65 946 N ATOM 731 CA ASN A 92 39.876 64.412 11.267 1.00 30.99 C ANISOU 731 CA ASN B 92 4345 4296 3134 -55 -210 654 C ATOM 732 C ASN A 92 41.014 64.675 10.294 1.00 31.42 C ANISOU 732 C ASN B 92 3701 4645 3593 -93 -208 329 C ATOM 733 O ASN A 92 42.044 65.267 10.648 1.00 32.32 O ANISOU 733 O ASN B 92 4081 4476 3724 -48 596 108 O ATOM 734 CB ASN A 92 40.295 63.329 12.288 1.00 35.51 C ANISOU 734 CB ASN B 92 5302 5141 3048 -289 344 650 C ATOM 735 CG ASN A 92 39.329 63.336 13.457 1.00 38.19 C ANISOU 735 CG ASN B 92 5988 5080 3443 157 113 269 C ATOM 736 OD1 ASN A 92 39.270 64.326 14.191 1.00 43.56 O ANISOU 736 OD1 ASN B 92 7035 5406 4112 539 -878 -301 O ATOM 737 ND2 ASN A 92 38.554 62.287 13.653 1.00 37.21 N ANISOU 737 ND2 ASN B 92 6000 4543 3596 -327 826 925 N ATOM 738 N PHE A 93 40.890 64.270 9.034 1.00 31.32 N ANISOU 738 N PHE B 93 3640 5181 3080 -457 518 137 N ATOM 739 CA PHE A 93 42.043 64.491 8.147 1.00 28.57 C ANISOU 739 CA PHE B 93 3360 4444 3050 -53 634 424 C ATOM 740 C PHE A 93 41.651 64.776 6.708 1.00 29.40 C ANISOU 740 C PHE B 93 3412 4803 2958 61 460 346 C ATOM 741 O PHE A 93 41.966 65.833 6.161 1.00 31.72 O ANISOU 741 O PHE B 93 4734 4118 3201 -208 1108 177 O ATOM 742 CB PHE A 93 42.913 63.234 8.229 1.00 30.39 C ANISOU 742 CB PHE B 93 3405 4753 3391 -284 565 244 C ATOM 743 CG PHE A 93 44.194 63.272 7.420 1.00 31.25 C ANISOU 743 CG PHE B 93 3730 4660 3483 -377 581 243 C ATOM 744 CD1 PHE A 93 45.038 64.371 7.506 1.00 29.95 C ANISOU 744 CD1 PHE B 93 3466 4815 3097 -206 1137 161 C ATOM 745 CD2 PHE A 93 44.530 62.204 6.593 1.00 30.73 C ANISOU 745 CD2 PHE B 93 3209 4834 3633 -91 802 -453 C ATOM 746 CE1 PHE A 93 46.210 64.399 6.779 1.00 31.44 C ANISOU 746 CE1 PHE B 93 3859 4705 3380 -265 1086 121 C ATOM 747 CE2 PHE A 93 45.701 62.226 5.861 1.00 31.69 C ANISOU 747 CE2 PHE B 93 3531 4731 3780 -329 747 -274 C ATOM 748 CZ PHE A 93 46.532 63.330 5.959 1.00 30.27 C ANISOU 748 CZ PHE B 93 3337 4728 3437 -361 1314 -233 C ATOM 749 N PHE A 94 40.973 63.836 6.043 1.00 30.65 N ANISOU 749 N PHE B 94 3692 4745 3207 -184 587 693 N ATOM 750 CA PHE A 94 40.788 64.015 4.605 1.00 30.56 C ANISOU 750 CA PHE B 94 3572 4889 3150 -114 485 514 C ATOM 751 C PHE A 94 39.953 65.264 4.319 1.00 30.65 C ANISOU 751 C PHE B 94 3623 4807 3218 -236 584 160 C ATOM 752 O PHE A 94 40.230 65.943 3.318 1.00 33.71 O ANISOU 752 O PHE B 94 4416 4812 3580 -311 1262 241 O ATOM 753 CB PHE A 94 40.142 62.802 3.947 1.00 30.31 C ANISOU 753 CB PHE B 94 3761 4790 2966 -302 103 374 C ATOM 754 CG PHE A 94 40.852 61.474 4.117 1.00 30.45 C ANISOU 754 CG PHE B 94 3625 4942 3003 -409 -384 421 C ATOM 755 CD1 PHE A 94 42.229 61.378 3.974 1.00 33.40 C ANISOU 755 CD1 PHE B 94 4161 5402 3128 -855 168 -429 C ATOM 756 CD2 PHE A 94 40.121 60.329 4.416 1.00 30.80 C ANISOU 756 CD2 PHE B 94 3484 5250 2967 -482 9 -58 C ATOM 757 CE1 PHE A 94 42.865 60.148 4.128 1.00 33.70 C ANISOU 757 CE1 PHE B 94 4110 5756 2937 -1099 -5 -243 C ATOM 758 CE2 PHE A 94 40.750 59.096 4.567 1.00 31.73 C ANISOU 758 CE2 PHE B 94 3582 5591 2883 -645 582 43 C ATOM 759 CZ PHE A 94 42.125 59.012 4.414 1.00 31.82 C ANISOU 759 CZ PHE B 94 3680 5899 2510 -850 -114 199 C ATOM 760 N ASP A 95 38.983 65.639 5.135 1.00 34.08 N ANISOU 760 N ASP B 95 4049 5597 3304 -634 -44 629 N ATOM 761 CA ASP A 95 38.193 66.844 4.906 1.00 34.35 C ANISOU 761 CA ASP B 95 4079 5311 3660 -767 150 542 C ATOM 762 C ASP A 95 39.056 68.096 4.841 1.00 36.57 C ANISOU 762 C ASP B 95 4287 5317 4292 -783 779 50 C ATOM 763 O ASP A 95 38.580 69.115 4.337 1.00 39.69 O ANISOU 763 O ASP B 95 4476 5756 4849 -983 1093 -549 O ATOM 764 CB ASP A 95 37.176 67.086 6.024 1.00 35.67 C ANISOU 764 CB ASP B 95 3774 5708 4073 -1030 780 -226 C ATOM 765 CG ASP A 95 35.968 66.181 5.996 1.00 34.99 C ANISOU 765 CG ASP B 95 3899 5693 3703 -1159 304 312 C ATOM 766 OD1 ASP A 95 35.816 65.363 5.067 1.00 35.39 O ANISOU 766 OD1 ASP B 95 4277 6282 2888 -1864 648 822 O ATOM 767 OD2 ASP A 95 35.143 66.288 6.929 1.00 33.74 O ANISOU 767 OD2 ASP B 95 4027 5208 3586 -667 131 421 O ATOM 768 N HIS A 96 40.281 68.061 5.346 1.00 36.46 N ANISOU 768 N HIS B 96 4684 5293 3875 -526 734 493 N ATOM 769 CA HIS A 96 41.093 69.264 5.442 1.00 35.36 C ANISOU 769 CA HIS B 96 4348 5461 3624 -367 1275 209 C ATOM 770 C HIS A 96 42.324 69.269 4.562 1.00 35.19 C ANISOU 770 C HIS B 96 4029 5694 3647 -425 1626 -52 C ATOM 771 O HIS A 96 43.077 70.251 4.638 1.00 39.30 O ANISOU 771 O HIS B 96 4650 5773 4509 -187 730 -354 O ATOM 772 CB HIS A 96 41.557 69.441 6.909 1.00 33.49 C ANISOU 772 CB HIS B 96 4456 4624 3644 -211 1455 117 C ATOM 773 CG HIS A 96 40.365 69.241 7.808 1.00 38.62 C ANISOU 773 CG HIS B 96 4939 5649 4085 -462 1172 -559 C ATOM 774 ND1 HIS A 96 39.371 70.182 7.953 1.00 40.50 N ANISOU 774 ND1 HIS B 96 4989 6057 4344 -654 1265 -701 N ATOM 775 CD2 HIS A 96 40.008 68.192 8.585 1.00 40.14 C ANISOU 775 CD2 HIS B 96 5023 6117 4113 -720 1221 -1071 C ATOM 776 CE1 HIS A 96 38.451 69.744 8.782 1.00 39.67 C ANISOU 776 CE1 HIS B 96 4932 6129 4012 -470 882 -603 C ATOM 777 NE2 HIS A 96 38.817 68.533 9.185 1.00 37.90 N ANISOU 777 NE2 HIS B 96 4805 5639 3956 -144 387 -484 N ATOM 778 N VAL A 97 42.546 68.228 3.767 1.00 34.62 N ANISOU 778 N VAL B 97 4461 5321 3373 -477 1494 54 N ATOM 779 CA VAL A 97 43.751 68.231 2.933 1.00 36.46 C ANISOU 779 CA VAL B 97 4874 5289 3692 -460 1178 36 C ATOM 780 C VAL A 97 43.411 67.966 1.470 1.00 35.96 C ANISOU 780 C VAL B 97 4654 5581 3426 -439 1679 -336 C ATOM 781 O VAL A 97 42.242 67.773 1.131 1.00 39.41 O ANISOU 781 O VAL B 97 5804 5797 3372 -914 25 271 O ATOM 782 CB VAL A 97 44.783 67.215 3.453 1.00 35.14 C ANISOU 782 CB VAL B 97 5139 5045 3167 -785 1099 236 C ATOM 783 CG1 VAL A 97 45.182 67.550 4.888 1.00 33.93 C ANISOU 783 CG1 VAL B 97 5390 4646 2856 -222 961 -318 C ATOM 784 CG2 VAL A 97 44.245 65.795 3.360 1.00 34.92 C ANISOU 784 CG2 VAL B 97 4327 5855 3086 -666 223 72 C ATOM 785 N ASP A 98 44.422 67.977 0.604 1.00 36.74 N ANISOU 785 N ASP B 98 4927 5302 3730 -197 1333 -352 N ATOM 786 CA ASP A 98 44.173 67.953 -0.836 1.00 34.71 C ANISOU 786 CA ASP B 98 4702 4779 3708 -54 1044 -383 C ATOM 787 C ASP A 98 44.327 66.566 -1.456 1.00 35.19 C ANISOU 787 C ASP B 98 4413 4907 4051 -182 914 -851 C ATOM 788 O ASP A 98 44.748 66.454 -2.610 1.00 35.65 O ANISOU 788 O ASP B 98 4240 5630 3677 -138 1218 -561 O ATOM 789 CB ASP A 98 45.099 68.929 -1.575 1.00 34.30 C ANISOU 789 CB ASP B 98 4389 4744 3901 -267 1045 -509 C ATOM 790 CG ASP A 98 46.570 68.637 -1.319 1.00 42.85 C ANISOU 790 CG ASP B 98 6236 5461 4584 -1451 1620 -797 C ATOM 791 OD1 ASP A 98 46.877 67.831 -0.405 1.00 41.13 O ANISOU 791 OD1 ASP B 98 5685 5525 4418 -1274 1366 -182 O ATOM 792 OD2 ASP A 98 47.418 69.219 -2.032 1.00 40.73 O ANISOU 792 OD2 ASP B 98 6312 4815 4350 -870 814 -248 O ATOM 793 N ILE A 99 43.974 65.527 -0.700 1.00 33.19 N ANISOU 793 N ILE B 99 4298 4713 3599 -396 1533 -192 N ATOM 794 CA ILE A 99 44.054 64.193 -1.276 1.00 33.90 C ANISOU 794 CA ILE B 99 4695 4378 3809 -187 1492 28 C ATOM 795 C ILE A 99 42.804 63.820 -2.084 1.00 36.58 C ANISOU 795 C ILE B 99 5231 4990 3677 -1364 534 289 C ATOM 796 O ILE A 99 41.650 63.987 -1.689 1.00 35.36 O ANISOU 796 O ILE B 99 4707 4851 3876 -930 742 -274 O ATOM 797 CB ILE A 99 44.250 63.162 -0.158 1.00 35.18 C ANISOU 797 CB ILE B 99 3998 5274 4095 -492 1345 -288 C ATOM 798 CG1 ILE A 99 44.605 61.748 -0.634 1.00 34.23 C ANISOU 798 CG1 ILE B 99 4305 4669 4033 -422 1095 -6 C ATOM 799 CG2 ILE A 99 42.999 63.126 0.720 1.00 37.02 C ANISOU 799 CG2 ILE B 99 5269 6154 2643 -704 911 -99 C ATOM 800 CD1 ILE A 99 44.956 60.826 0.536 1.00 34.84 C ANISOU 800 CD1 ILE B 99 4107 4388 4744 -137 1473 605 C ATOM 801 N PRO A 100 43.026 63.262 -3.276 1.00 36.88 N ANISOU 801 N PRO B 100 5587 5329 3097 -1531 930 -61 N ATOM 802 CA PRO A 100 41.925 62.819 -4.116 1.00 35.29 C ANISOU 802 CA PRO B 100 4840 5035 3535 -1196 356 54 C ATOM 803 C PRO A 100 41.271 61.526 -3.644 1.00 36.36 C ANISOU 803 C PRO B 100 4851 5250 3715 -1543 965 -480 C ATOM 804 O PRO A 100 41.931 60.635 -3.118 1.00 39.45 O ANISOU 804 O PRO B 100 5703 5877 3407 -1736 1727 -330 O ATOM 805 CB PRO A 100 42.573 62.553 -5.486 1.00 33.85 C ANISOU 805 CB PRO B 100 4530 5161 3171 -1211 970 -90 C ATOM 806 CG PRO A 100 44.039 62.507 -5.246 1.00 37.64 C ANISOU 806 CG PRO B 100 5633 5438 3229 -1814 917 -195 C ATOM 807 CD PRO A 100 44.345 63.044 -3.869 1.00 36.80 C ANISOU 807 CD PRO B 100 5032 5463 3487 -1619 913 121 C ATOM 808 N ALA A 101 39.959 61.404 -3.856 1.00 30.99 N ANISOU 808 N ALA B 101 3433 5040 3303 -898 -430 305 N ATOM 809 CA ALA A 101 39.215 60.218 -3.462 1.00 33.72 C ANISOU 809 CA ALA B 101 4081 5089 3640 -619 200 736 C ATOM 810 C ALA A 101 39.858 58.953 -4.004 1.00 30.88 C ANISOU 810 C ALA B 101 3919 4368 3448 -629 404 347 C ATOM 811 O ALA A 101 39.900 57.912 -3.352 1.00 32.77 O ANISOU 811 O ALA B 101 4178 4764 3512 -566 682 392 O ATOM 812 CB ALA A 101 37.774 60.310 -3.950 1.00 33.55 C ANISOU 812 CB ALA B 101 3964 5017 3766 -861 593 -5 C ATOM 813 N GLU A 102 40.370 59.014 -5.235 1.00 30.35 N ANISOU 813 N GLU B 102 4106 4392 3032 -846 605 806 N ATOM 814 CA GLU A 102 40.863 57.750 -5.775 1.00 32.82 C ANISOU 814 CA GLU B 102 4063 5216 3191 -999 506 481 C ATOM 815 C GLU A 102 42.110 57.297 -5.032 1.00 31.46 C ANISOU 815 C GLU B 102 3864 4733 3355 -396 864 489 C ATOM 816 O GLU A 102 42.483 56.131 -5.139 1.00 34.82 O ANISOU 816 O GLU B 102 3726 5192 4311 -1043 -26 703 O ATOM 817 CB GLU A 102 41.157 57.891 -7.265 1.00 35.90 C ANISOU 817 CB GLU B 102 4640 5930 3070 -1466 471 632 C ATOM 818 CG GLU A 102 42.083 59.078 -7.511 1.00 42.27 C ANISOU 818 CG GLU B 102 6742 5952 3365 -1389 507 -204 C ATOM 819 CD GLU A 102 42.059 59.463 -8.983 1.00 50.47 C ANISOU 819 CD GLU B 102 7995 7533 3648 -1747 1074 -687 C ATOM 820 OE1 GLU A 102 41.518 60.549 -9.319 1.00 57.34 O ANISOU 820 OE1 GLU B 102 8278 9155 4353 -1924 1846 -96 O ATOM 821 OE2 GLU A 102 42.587 58.657 -9.793 1.00 60.07 O ANISOU 821 OE2 GLU B 102 8655 10831 3336 -3672 902 -1579 O ATOM 822 N ASN A 103 42.753 58.191 -4.287 1.00 32.64 N ANISOU 822 N ASN B 103 4396 4734 3272 -404 598 409 N ATOM 823 CA ASN A 103 43.952 57.830 -3.540 1.00 33.57 C ANISOU 823 CA ASN B 103 5275 4740 2740 -1027 431 227 C ATOM 824 C ASN A 103 43.656 57.259 -2.161 1.00 31.50 C ANISOU 824 C ASN B 103 4370 4610 2987 -737 366 81 C ATOM 825 O ASN A 103 44.578 56.811 -1.467 1.00 32.15 O ANISOU 825 O ASN B 103 4006 4785 3422 -525 691 -130 O ATOM 826 CB ASN A 103 44.844 59.070 -3.394 1.00 34.34 C ANISOU 826 CB ASN B 103 5232 4745 3072 -912 1374 133 C ATOM 827 CG ASN A 103 45.626 59.383 -4.653 1.00 36.60 C ANISOU 827 CG ASN B 103 5288 5096 3522 -883 519 -207 C ATOM 828 OD1 ASN A 103 45.346 58.814 -5.715 1.00 35.71 O ANISOU 828 OD1 ASN B 103 5044 5400 3123 -644 1347 -82 O ATOM 829 ND2 ASN A 103 46.599 60.277 -4.590 1.00 35.38 N ANISOU 829 ND2 ASN B 103 5136 5176 3130 -685 1303 -224 N ATOM 830 N ILE A 104 42.404 57.253 -1.700 1.00 32.91 N ANISOU 830 N ILE B 104 4556 4661 3286 -737 274 -56 N ATOM 831 CA ILE A 104 42.057 56.854 -0.334 1.00 31.09 C ANISOU 831 CA ILE B 104 4505 4217 3091 -847 319 231 C ATOM 832 C ILE A 104 41.559 55.423 -0.316 1.00 31.25 C ANISOU 832 C ILE B 104 4575 3985 3313 -949 706 460 C ATOM 833 O ILE A 104 40.641 55.052 -1.052 1.00 32.27 O ANISOU 833 O ILE B 104 4783 4728 2752 -686 460 863 O ATOM 834 CB ILE A 104 40.985 57.762 0.293 1.00 31.31 C ANISOU 834 CB ILE B 104 4726 4326 2846 -1181 253 675 C ATOM 835 CG1 ILE A 104 41.448 59.220 0.402 1.00 31.28 C ANISOU 835 CG1 ILE B 104 4403 4559 2921 -1144 164 242 C ATOM 836 CG2 ILE A 104 40.507 57.241 1.648 1.00 29.67 C ANISOU 836 CG2 ILE B 104 4248 4267 2758 -881 104 781 C ATOM 837 CD1 ILE A 104 40.328 60.184 0.713 1.00 32.42 C ANISOU 837 CD1 ILE B 104 4680 4730 2907 -1500 -179 876 C ATOM 838 N ASN A 105 42.171 54.596 0.521 1.00 30.46 N ANISOU 838 N ASN B 105 4248 4407 2918 -945 333 590 N ATOM 839 CA ASN A 105 41.717 53.219 0.589 1.00 32.34 C ANISOU 839 CA ASN B 105 4321 4452 3516 -907 626 520 C ATOM 840 C ASN A 105 41.355 52.889 2.034 1.00 33.61 C ANISOU 840 C ASN B 105 4711 4436 3624 -724 491 392 C ATOM 841 O ASN A 105 42.111 53.072 2.985 1.00 30.80 O ANISOU 841 O ASN B 105 4042 4434 3227 -644 -297 398 O ATOM 842 CB ASN A 105 42.804 52.279 0.090 1.00 32.61 C ANISOU 842 CB ASN B 105 4246 4368 3777 -697 574 342 C ATOM 843 CG ASN A 105 43.150 52.490 -1.361 1.00 35.09 C ANISOU 843 CG ASN B 105 4708 5076 3550 -880 272 688 C ATOM 844 OD1 ASN A 105 42.467 51.911 -2.211 1.00 39.39 O ANISOU 844 OD1 ASN B 105 5905 5078 3981 -569 731 944 O ATOM 845 ND2 ASN A 105 44.170 53.291 -1.663 1.00 29.24 N ANISOU 845 ND2 ASN B 105 3888 5167 2057 -734 610 859 N ATOM 846 N LEU A 106 40.127 52.396 2.154 1.00 31.95 N ANISOU 846 N LEU B 106 3952 4279 3909 -177 439 403 N ATOM 847 CA LEU A 106 39.534 52.008 3.421 1.00 34.22 C ANISOU 847 CA LEU B 106 4400 4562 4040 -423 543 158 C ATOM 848 C LEU A 106 38.854 50.660 3.216 1.00 34.71 C ANISOU 848 C LEU B 106 4913 4364 3913 -388 534 20 C ATOM 849 O LEU A 106 38.323 50.439 2.130 1.00 36.23 O ANISOU 849 O LEU B 106 4968 4770 4027 -138 604 233 O ATOM 850 CB LEU A 106 38.519 53.027 3.924 1.00 36.38 C ANISOU 850 CB LEU B 106 4510 4684 4630 -584 565 -435 C ATOM 851 CG LEU A 106 39.055 54.264 4.654 1.00 35.72 C ANISOU 851 CG LEU B 106 3771 5352 4451 -70 829 -681 C ATOM 852 CD1 LEU A 106 38.313 55.497 4.144 1.00 42.00 C ANISOU 852 CD1 LEU B 106 3910 6757 5290 -647 1129 138 C ATOM 853 CD2 LEU A 106 38.932 54.149 6.163 1.00 35.07 C ANISOU 853 CD2 LEU B 106 4779 4133 4415 -597 761 -603 C ATOM 854 N LEU A 107 38.859 49.775 4.196 1.00 34.53 N ANISOU 854 N LEU B 107 4691 4414 4014 -459 540 -33 N ATOM 855 CA LEU A 107 38.141 48.515 4.074 1.00 35.05 C ANISOU 855 CA LEU B 107 4619 4356 4344 -516 1190 479 C ATOM 856 C LEU A 107 36.635 48.737 4.022 1.00 37.46 C ANISOU 856 C LEU B 107 4938 4618 4678 -787 937 911 C ATOM 857 O LEU A 107 36.071 49.559 4.760 1.00 38.05 O ANISOU 857 O LEU B 107 5313 4559 4585 -800 755 183 O ATOM 858 CB LEU A 107 38.561 47.616 5.250 1.00 34.30 C ANISOU 858 CB LEU B 107 4586 4483 3964 -534 928 451 C ATOM 859 CG LEU A 107 39.897 46.902 4.973 1.00 34.06 C ANISOU 859 CG LEU B 107 4502 4681 3757 -547 836 807 C ATOM 860 CD1 LEU A 107 40.555 46.442 6.275 1.00 29.82 C ANISOU 860 CD1 LEU B 107 3380 4872 3080 -19 332 269 C ATOM 861 CD2 LEU A 107 39.687 45.756 4.001 1.00 33.01 C ANISOU 861 CD2 LEU B 107 5034 4156 3351 -512 683 489 C ATOM 862 N ASN A 108 35.954 48.010 3.121 1.00 39.13 N ANISOU 862 N ASN B 108 5989 4292 4588 -435 1104 684 N ATOM 863 CA ASN A 108 34.499 48.115 3.021 1.00 39.84 C ANISOU 863 CA ASN B 108 6362 4176 4599 -440 1482 556 C ATOM 864 C ASN A 108 33.833 47.151 3.994 1.00 40.69 C ANISOU 864 C ASN B 108 6208 4324 4928 -519 1857 483 C ATOM 865 O ASN A 108 33.660 45.958 3.727 1.00 43.29 O ANISOU 865 O ASN B 108 6790 3902 5756 -377 1638 598 O ATOM 866 CB ASN A 108 34.032 47.853 1.589 1.00 40.41 C ANISOU 866 CB ASN B 108 6331 4262 4760 21 1660 794 C ATOM 867 CG ASN A 108 32.548 48.080 1.399 1.00 38.84 C ANISOU 867 CG ASN B 108 5505 4307 4946 398 2042 806 C ATOM 868 OD1 ASN A 108 31.795 48.387 2.334 1.00 53.94 O ANISOU 868 OD1 ASN B 108 10729 5477 4290 -2612 3158 -571 O ATOM 869 ND2 ASN A 108 32.112 47.913 0.144 1.00 46.61 N ANISOU 869 ND2 ASN B 108 7358 5603 4750 -825 2625 612 N ATOM 870 N GLY A 109 33.438 47.659 5.159 1.00 40.85 N ANISOU 870 N GLY B 109 6270 4240 5010 -754 1842 113 N ATOM 871 CA GLY A 109 32.830 46.821 6.181 1.00 39.63 C ANISOU 871 CA GLY B 109 5024 4631 5402 78 1429 -31 C ATOM 872 C GLY A 109 31.448 46.339 5.785 1.00 42.22 C ANISOU 872 C GLY B 109 5622 4535 5887 -177 1869 -417 C ATOM 873 O GLY A 109 30.847 45.496 6.446 1.00 38.25 O ANISOU 873 O GLY B 109 4210 4790 5534 -176 293 -952 O ATOM 874 N ASN A 110 30.939 46.879 4.681 1.00 44.46 N ANISOU 874 N ASN B 110 5804 4980 6109 -380 1982 -24 N ATOM 875 CA ASN A 110 29.635 46.483 4.181 1.00 48.58 C ANISOU 875 CA ASN B 110 6429 5414 6615 -1018 1249 443 C ATOM 876 C ASN A 110 29.769 45.611 2.948 1.00 50.82 C ANISOU 876 C ASN B 110 6823 5772 6715 -709 1144 566 C ATOM 877 O ASN A 110 28.759 45.305 2.314 1.00 48.88 O ANISOU 877 O ASN B 110 7062 4473 7037 13 812 -66 O ATOM 878 CB ASN A 110 28.782 47.738 3.907 1.00 50.36 C ANISOU 878 CB ASN B 110 6487 5502 7146 -1451 1298 21 C ATOM 879 CG ASN A 110 28.414 48.439 5.207 1.00 50.62 C ANISOU 879 CG ASN B 110 6301 5774 7159 -1249 1332 -411 C ATOM 880 OD1 ASN A 110 27.750 47.849 6.065 1.00 52.61 O ANISOU 880 OD1 ASN B 110 6575 6222 7194 -811 1545 -529 O ATOM 881 ND2 ASN A 110 28.823 49.690 5.397 1.00 48.08 N ANISOU 881 ND2 ASN B 110 6147 5904 6217 -1209 1853 -182 N ATOM 882 N ALA A 111 30.978 45.188 2.577 1.00 46.92 N ANISOU 882 N ALA B 111 5573 5931 6322 -309 1461 920 N ATOM 883 CA ALA A 111 31.089 44.346 1.381 1.00 48.47 C ANISOU 883 CA ALA B 111 5790 6212 6414 129 1455 1048 C ATOM 884 C ALA A 111 30.259 43.071 1.551 1.00 52.94 C ANISOU 884 C ALA B 111 6797 6316 7001 455 1192 819 C ATOM 885 O ALA A 111 30.125 42.496 2.636 1.00 54.44 O ANISOU 885 O ALA B 111 7637 5640 7410 41 1768 691 O ATOM 886 CB ALA A 111 32.530 44.006 1.041 1.00 45.03 C ANISOU 886 CB ALA B 111 3698 5647 7765 1271 726 1998 C ATOM 887 N PRO A 112 29.677 42.637 0.434 1.00 55.19 N ANISOU 887 N PRO B 112 7572 6396 7003 848 638 742 N ATOM 888 CA PRO A 112 28.831 41.436 0.444 1.00 54.22 C ANISOU 888 CA PRO B 112 6868 6455 7279 743 569 625 C ATOM 889 C PRO A 112 29.688 40.187 0.638 1.00 59.71 C ANISOU 889 C PRO B 112 7025 6982 8682 359 1164 -242 C ATOM 890 O PRO A 112 29.316 39.297 1.410 1.00 77.93 O ANISOU 890 O PRO B 112 8031 7763 13817 567 2677 -2149 O ATOM 891 CB PRO A 112 28.165 41.460 -0.933 1.00 57.18 C ANISOU 891 CB PRO B 112 7833 6256 7639 966 1000 896 C ATOM 892 CG PRO A 112 29.185 42.144 -1.791 1.00 54.16 C ANISOU 892 CG PRO B 112 7183 6144 7253 1389 1098 1162 C ATOM 893 CD PRO A 112 29.770 43.222 -0.913 1.00 53.80 C ANISOU 893 CD PRO B 112 6856 6468 7117 1172 1100 1377 C ATOM 894 N ASP A 113 30.839 40.111 -0.025 1.00 58.97 N ANISOU 894 N ASP B 113 7871 6976 7558 -703 978 1015 N ATOM 895 CA ASP A 113 31.756 38.994 0.177 1.00 54.23 C ANISOU 895 CA ASP B 113 7651 6420 6535 -174 564 1816 C ATOM 896 C ASP A 113 32.990 39.443 0.963 1.00 52.93 C ANISOU 896 C ASP B 113 7586 6363 6163 180 639 1741 C ATOM 897 O ASP A 113 33.966 39.897 0.362 1.00 44.98 O ANISOU 897 O ASP B 113 5320 6095 5676 1212 693 1948 O ATOM 898 CB ASP A 113 32.192 38.402 -1.160 1.00 54.08 C ANISOU 898 CB ASP B 113 7975 6588 5985 -110 988 1859 C ATOM 899 CG ASP A 113 33.004 37.133 -1.007 1.00 58.32 C ANISOU 899 CG ASP B 113 7835 7247 7078 -138 293 1121 C ATOM 900 OD1 ASP A 113 33.459 36.822 0.107 1.00 53.98 O ANISOU 900 OD1 ASP B 113 5905 7266 7339 387 -41 1707 O ATOM 901 OD2 ASP A 113 33.187 36.424 -2.019 1.00 61.72 O ANISOU 901 OD2 ASP B 113 8558 8578 6314 -863 -16 -699 O ATOM 902 N ILE A 114 32.915 39.303 2.281 1.00 51.56 N ANISOU 902 N ILE B 114 6967 6312 6311 -162 1211 1397 N ATOM 903 CA ILE A 114 33.976 39.729 3.185 1.00 52.94 C ANISOU 903 CA ILE B 114 7380 6739 5997 -693 1291 1417 C ATOM 904 C ILE A 114 35.344 39.167 2.839 1.00 49.80 C ANISOU 904 C ILE B 114 7019 5918 5983 -7 1190 1105 C ATOM 905 O ILE A 114 36.324 39.923 2.773 1.00 49.57 O ANISOU 905 O ILE B 114 6631 5887 6317 133 1737 1794 O ATOM 906 CB ILE A 114 33.629 39.324 4.633 1.00 55.04 C ANISOU 906 CB ILE B 114 7595 7188 6129 -1136 1136 1055 C ATOM 907 CG1 ILE A 114 32.422 40.091 5.183 1.00 59.43 C ANISOU 907 CG1 ILE B 114 8000 7943 6638 -2048 1462 914 C ATOM 908 CG2 ILE A 114 34.839 39.476 5.542 1.00 45.34 C ANISOU 908 CG2 ILE B 114 6371 5895 4960 -544 270 324 C ATOM 909 CD1 ILE A 114 32.580 41.589 4.952 1.00 67.13 C ANISOU 909 CD1 ILE B 114 7512 7919 10077 -1945 751 1921 C ATOM 910 N ASP A 115 35.478 37.860 2.616 1.00 48.77 N ANISOU 910 N ASP B 115 7171 5406 5955 66 1323 1323 N ATOM 911 CA ASP A 115 36.830 37.382 2.315 1.00 48.39 C ANISOU 911 CA ASP B 115 7228 5264 5896 282 442 1777 C ATOM 912 C ASP A 115 37.372 37.997 1.036 1.00 47.13 C ANISOU 912 C ASP B 115 6772 5891 5245 168 83 1979 C ATOM 913 O ASP A 115 38.577 38.216 0.939 1.00 40.86 O ANISOU 913 O ASP B 115 4896 6366 4264 -85 440 1617 O ATOM 914 CB ASP A 115 36.866 35.857 2.214 1.00 54.10 C ANISOU 914 CB ASP B 115 7425 5973 7156 638 193 1521 C ATOM 915 CG ASP A 115 36.609 35.256 3.588 1.00 57.98 C ANISOU 915 CG ASP B 115 7268 7039 7724 782 726 1041 C ATOM 916 OD1 ASP A 115 36.364 36.028 4.542 1.00 63.54 O ANISOU 916 OD1 ASP B 115 8889 7752 7500 -32 -83 573 O ATOM 917 OD2 ASP A 115 36.650 34.015 3.704 1.00 72.11 O ANISOU 917 OD2 ASP B 115 8323 7947 11127 1838 1191 119 O ATOM 918 N ALA A 116 36.473 38.258 0.101 1.00 45.03 N ANISOU 918 N ALA B 116 6608 5130 5370 362 -231 2216 N ATOM 919 CA ALA A 116 36.874 38.881 -1.156 1.00 46.84 C ANISOU 919 CA ALA B 116 7112 5580 5106 -215 11 2295 C ATOM 920 C ALA A 116 37.376 40.310 -0.955 1.00 42.63 C ANISOU 920 C ALA B 116 6829 5093 4274 -485 416 1882 C ATOM 921 O ALA A 116 38.402 40.721 -1.529 1.00 43.65 O ANISOU 921 O ALA B 116 6664 5785 4135 -790 1404 1188 O ATOM 922 CB ALA A 116 35.695 38.842 -2.109 1.00 45.03 C ANISOU 922 CB ALA B 116 5193 5521 6397 378 640 2551 C ATOM 923 N GLU A 117 36.646 41.063 -0.142 1.00 40.19 N ANISOU 923 N GLU B 117 5901 5384 3985 -321 1107 1559 N ATOM 924 CA GLU A 117 37.025 42.428 0.242 1.00 42.41 C ANISOU 924 CA GLU B 117 6550 5019 4547 -371 582 1690 C ATOM 925 C GLU A 117 38.451 42.417 0.791 1.00 40.28 C ANISOU 925 C GLU B 117 6191 4878 4236 -462 829 1007 C ATOM 926 O GLU A 117 39.298 43.221 0.375 1.00 37.84 O ANISOU 926 O GLU B 117 5358 4923 4096 -54 799 1325 O ATOM 927 CB GLU A 117 36.020 42.970 1.250 1.00 41.10 C ANISOU 927 CB GLU B 117 6379 4044 5193 -218 420 1696 C ATOM 928 CG GLU A 117 36.243 44.326 1.886 1.00 39.62 C ANISOU 928 CG GLU B 117 5565 4581 4906 -77 1126 1712 C ATOM 929 CD GLU A 117 36.361 45.430 0.852 1.00 43.56 C ANISOU 929 CD GLU B 117 6478 4914 5158 -169 1533 1396 C ATOM 930 OE1 GLU A 117 35.784 45.258 -0.248 1.00 40.98 O ANISOU 930 OE1 GLU B 117 5095 5747 4727 12 796 1432 O ATOM 931 OE2 GLU A 117 37.036 46.445 1.144 1.00 41.60 O ANISOU 931 OE2 GLU B 117 5582 5443 4780 120 1472 1403 O ATOM 932 N CYS A 118 38.715 41.493 1.719 1.00 36.59 N ANISOU 932 N CYS B 118 5340 4757 3805 -197 141 868 N ATOM 933 CA CYS A 118 40.012 41.436 2.386 1.00 35.42 C ANISOU 933 CA CYS B 118 4597 4601 4259 145 389 845 C ATOM 934 C CYS A 118 41.108 41.074 1.397 1.00 35.22 C ANISOU 934 C CYS B 118 4292 4824 4266 153 357 926 C ATOM 935 O CYS A 118 42.182 41.678 1.393 1.00 36.37 O ANISOU 935 O CYS B 118 5254 4837 3727 -302 589 909 O ATOM 936 CB CYS A 118 39.949 40.456 3.562 1.00 38.72 C ANISOU 936 CB CYS B 118 6019 4186 4508 272 977 881 C ATOM 937 SG CYS A 118 38.846 41.062 4.887 1.00 42.29 S ANISOU 937 SG CYS B 118 6457 5128 4485 -445 1404 310 S ATOM 938 N ARG A 119 40.863 40.105 0.533 1.00 39.08 N ANISOU 938 N ARG B 119 3719 5677 5451 379 14 1271 N ATOM 939 CA ARG A 119 41.782 39.781 -0.554 1.00 44.31 C ANISOU 939 CA ARG B 119 4903 5728 6206 455 -1119 1422 C ATOM 940 C ARG A 119 42.112 40.929 -1.498 1.00 43.76 C ANISOU 940 C ARG B 119 5164 6305 5159 166 -1336 1150 C ATOM 941 O ARG A 119 43.245 41.166 -1.940 1.00 41.45 O ANISOU 941 O ARG B 119 5564 6327 3860 16 -1556 1553 O ATOM 942 CB ARG A 119 41.128 38.634 -1.349 1.00 52.18 C ANISOU 942 CB ARG B 119 6079 6237 7511 557 -1925 2009 C ATOM 943 CG ARG A 119 42.114 37.671 -1.982 1.00 62.59 C ANISOU 943 CG ARG B 119 7520 7269 8992 -116 -3727 3064 C ATOM 944 CD ARG A 119 41.386 36.547 -2.738 1.00 70.06 C ANISOU 944 CD ARG B 119 8623 7363 10634 217 -4665 3157 C ATOM 945 NE ARG A 119 40.331 35.984 -1.889 1.00 77.92 N ANISOU 945 NE ARG B 119 10834 7176 11594 33 -3455 2858 N ATOM 946 CZ ARG A 119 39.052 35.827 -2.201 1.00 81.38 C ANISOU 946 CZ ARG B 119 11888 7786 11248 -990 -3153 2568 C ATOM 947 NH1 ARG A 119 38.593 36.183 -3.402 1.00 79.87 N ANISOU 947 NH1 ARG B 119 11090 9685 9573 -1384 -5734 3721 N ATOM 948 NH2 ARG A 119 38.221 35.296 -1.302 1.00 78.89 N ANISOU 948 NH2 ARG B 119 10717 8579 10677 -1734 -5670 2193 N ATOM 949 N GLN A 120 41.096 41.705 -1.869 1.00 43.70 N ANISOU 949 N GLN B 120 5581 6454 4567 -50 -1033 1137 N ATOM 950 CA GLN A 120 41.299 42.833 -2.779 1.00 43.77 C ANISOU 950 CA GLN B 120 6264 6209 4159 -91 -698 1472 C ATOM 951 C GLN A 120 42.139 43.943 -2.159 1.00 42.63 C ANISOU 951 C GLN B 120 6254 5980 3964 -171 -1138 1024 C ATOM 952 O GLN A 120 42.979 44.567 -2.818 1.00 40.35 O ANISOU 952 O GLN B 120 5549 6318 3463 -59 -564 1020 O ATOM 953 CB GLN A 120 39.929 43.382 -3.209 1.00 51.15 C ANISOU 953 CB GLN B 120 8110 6639 4685 -934 797 1022 C ATOM 954 CG GLN A 120 39.138 42.386 -4.032 1.00 60.59 C ANISOU 954 CG GLN B 120 10526 6828 5666 -1654 -68 1791 C ATOM 955 CD GLN A 120 37.683 42.767 -4.214 1.00 66.38 C ANISOU 955 CD GLN B 120 11134 7736 6353 -2259 807 2050 C ATOM 956 OE1 GLN A 120 37.296 43.921 -4.011 1.00 80.51 O ANISOU 956 OE1 GLN B 120 11531 10907 8151 -3681 -1848 4294 O ATOM 957 NE2 GLN A 120 36.872 41.779 -4.597 1.00 65.48 N ANISOU 957 NE2 GLN B 120 12268 6515 6094 -1355 4376 647 N ATOM 958 N TYR A 121 41.900 44.189 -0.864 1.00 39.41 N ANISOU 958 N TYR B 121 5523 5545 3904 -557 -941 999 N ATOM 959 CA TYR A 121 42.697 45.185 -0.151 1.00 37.24 C ANISOU 959 CA TYR B 121 4934 5576 3642 -351 -578 889 C ATOM 960 C TYR A 121 44.186 44.859 -0.249 1.00 35.57 C ANISOU 960 C TYR B 121 4686 5266 3564 -56 -151 609 C ATOM 961 O TYR A 121 45.001 45.714 -0.603 1.00 39.31 O ANISOU 961 O TYR B 121 5066 5420 4451 -17 279 342 O ATOM 962 CB TYR A 121 42.255 45.252 1.307 1.00 32.78 C ANISOU 962 CB TYR B 121 4529 4380 3547 235 -18 741 C ATOM 963 CG TYR A 121 42.425 46.574 2.015 1.00 32.72 C ANISOU 963 CG TYR B 121 4195 4876 3362 79 -13 842 C ATOM 964 CD1 TYR A 121 41.759 47.705 1.545 1.00 32.38 C ANISOU 964 CD1 TYR B 121 4294 4542 3467 -45 155 697 C ATOM 965 CD2 TYR A 121 43.247 46.684 3.141 1.00 29.32 C ANISOU 965 CD2 TYR B 121 4353 3681 3105 719 514 215 C ATOM 966 CE1 TYR A 121 41.898 48.921 2.172 1.00 29.55 C ANISOU 966 CE1 TYR B 121 4346 3796 3086 310 491 52 C ATOM 967 CE2 TYR A 121 43.390 47.896 3.779 1.00 26.68 C ANISOU 967 CE2 TYR B 121 4082 3327 2727 406 295 -193 C ATOM 968 CZ TYR A 121 42.720 48.993 3.287 1.00 29.38 C ANISOU 968 CZ TYR B 121 4160 3638 3366 350 482 232 C ATOM 969 OH TYR A 121 42.840 50.222 3.907 1.00 30.92 O ANISOU 969 OH TYR B 121 3871 4298 3580 135 349 502 O ATOM 970 N GLU A 122 44.559 43.619 0.065 1.00 34.29 N ANISOU 970 N GLU B 122 4451 5144 3434 344 -834 1356 N ATOM 971 CA GLU A 122 45.958 43.204 -0.034 1.00 37.50 C ANISOU 971 CA GLU B 122 4800 5818 3630 -156 498 -49 C ATOM 972 C GLU A 122 46.425 43.331 -1.481 1.00 36.58 C ANISOU 972 C GLU B 122 4713 5633 3554 185 412 101 C ATOM 973 O GLU A 122 47.549 43.735 -1.780 1.00 38.91 O ANISOU 973 O GLU B 122 4594 6036 4155 -416 -691 -119 O ATOM 974 CB GLU A 122 46.181 41.763 0.422 1.00 37.54 C ANISOU 974 CB GLU B 122 4948 5625 3692 -122 635 -69 C ATOM 975 CG GLU A 122 45.912 41.541 1.907 1.00 35.43 C ANISOU 975 CG GLU B 122 4337 5596 3529 370 210 271 C ATOM 976 CD GLU A 122 47.052 41.983 2.797 1.00 39.13 C ANISOU 976 CD GLU B 122 5390 5602 3876 -300 368 243 C ATOM 977 OE1 GLU A 122 48.145 42.281 2.271 1.00 40.51 O ANISOU 977 OE1 GLU B 122 5324 5966 4101 -741 -1057 413 O ATOM 978 OE2 GLU A 122 46.813 42.026 4.033 1.00 37.69 O ANISOU 978 OE2 GLU B 122 5819 4757 3746 -47 903 257 O ATOM 979 N GLU A 123 45.510 42.957 -2.388 1.00 41.44 N ANISOU 979 N GLU B 123 5037 6678 4029 -410 -421 951 N ATOM 980 CA GLU A 123 45.938 43.086 -3.789 1.00 45.19 C ANISOU 980 CA GLU B 123 6449 6777 3942 -681 -248 1030 C ATOM 981 C GLU A 123 46.175 44.538 -4.172 1.00 44.81 C ANISOU 981 C GLU B 123 5963 7095 3967 -1105 -108 473 C ATOM 982 O GLU A 123 47.116 44.870 -4.898 1.00 42.83 O ANISOU 982 O GLU B 123 6460 6124 3688 -484 -1306 1300 O ATOM 983 CB GLU A 123 44.888 42.434 -4.693 1.00 52.97 C ANISOU 983 CB GLU B 123 7888 7594 4642 -1002 -1478 1840 C ATOM 984 CG GLU A 123 45.303 41.020 -5.065 1.00 62.88 C ANISOU 984 CG GLU B 123 8488 7466 7937 376 -1773 1479 C ATOM 985 CD GLU A 123 44.378 39.944 -4.544 1.00 75.26 C ANISOU 985 CD GLU B 123 10105 7469 11021 -13 -239 782 C ATOM 986 OE1 GLU A 123 43.245 39.820 -5.059 1.00 94.72 O ANISOU 986 OE1 GLU B 123 15817 7792 12381 -1954 62 894 O ATOM 987 OE2 GLU A 123 44.791 39.206 -3.610 1.00108.70 O ANISOU 987 OE2 GLU B 123 15891 10579 14830 -1925 4492 -3558 O ATOM 988 N LYS A 124 45.310 45.438 -3.684 1.00 43.43 N ANISOU 988 N LYS B 124 6342 6311 3849 -1081 -739 1307 N ATOM 989 CA LYS A 124 45.513 46.849 -4.026 1.00 43.60 C ANISOU 989 CA LYS B 124 5986 6783 3799 -1212 -366 1516 C ATOM 990 C LYS A 124 46.848 47.354 -3.483 1.00 41.43 C ANISOU 990 C LYS B 124 6080 6378 3283 -809 740 844 C ATOM 991 O LYS A 124 47.560 48.086 -4.171 1.00 39.70 O ANISOU 991 O LYS B 124 5588 6905 2593 -416 174 717 O ATOM 992 CB LYS A 124 44.348 47.701 -3.514 1.00 48.70 C ANISOU 992 CB LYS B 124 6154 7889 4462 -1797 -661 2218 C ATOM 993 CG LYS A 124 43.580 48.455 -4.582 1.00 63.43 C ANISOU 993 CG LYS B 124 7294 10431 6376 -3061 617 2158 C ATOM 994 CD LYS A 124 43.117 49.824 -4.104 1.00 65.56 C ANISOU 994 CD LYS B 124 7032 11017 6862 -1995 1436 1559 C ATOM 995 CE LYS A 124 43.259 50.866 -5.205 1.00 69.50 C ANISOU 995 CE LYS B 124 8209 12180 6018 -2846 2079 1601 C ATOM 996 NZ LYS A 124 42.701 52.200 -4.814 1.00 75.15 N ANISOU 996 NZ LYS B 124 7038 17031 4484 -4576 3724 -1262 N ATOM 997 N ILE A 125 47.218 46.980 -2.257 1.00 38.54 N ANISOU 997 N ILE B 125 4878 6076 3689 -691 1108 567 N ATOM 998 CA ILE A 125 48.521 47.426 -1.737 1.00 34.53 C ANISOU 998 CA ILE B 125 3711 6172 3237 -519 393 769 C ATOM 999 C ILE A 125 49.635 46.967 -2.678 1.00 38.08 C ANISOU 999 C ILE B 125 4373 6461 3635 -657 3 649 C ATOM 1000 O ILE A 125 50.498 47.742 -3.113 1.00 40.44 O ANISOU 1000 O ILE B 125 5635 6242 3488 -613 -524 843 O ATOM 1001 CB ILE A 125 48.765 46.902 -0.315 1.00 38.18 C ANISOU 1001 CB ILE B 125 4638 6414 3453 -940 800 561 C ATOM 1002 CG1 ILE A 125 47.829 47.504 0.727 1.00 37.72 C ANISOU 1002 CG1 ILE B 125 4797 6191 3344 -1317 1369 -151 C ATOM 1003 CG2 ILE A 125 50.222 47.123 0.076 1.00 31.39 C ANISOU 1003 CG2 ILE B 125 3778 5944 2204 -412 106 304 C ATOM 1004 CD1 ILE A 125 47.590 46.649 1.949 1.00 33.33 C ANISOU 1004 CD1 ILE B 125 3304 5887 3474 -140 1071 460 C ATOM 1005 N ARG A 126 49.580 45.667 -3.012 1.00 39.91 N ANISOU 1005 N ARG B 126 5093 6528 3541 -592 -799 1236 N ATOM 1006 CA ARG A 126 50.600 45.111 -3.906 1.00 41.68 C ANISOU 1006 CA ARG B 126 4615 6590 4630 -591 -504 396 C ATOM 1007 C ARG A 126 50.514 45.781 -5.266 1.00 42.83 C ANISOU 1007 C ARG B 126 6096 6161 4016 -833 -706 654 C ATOM 1008 O ARG A 126 51.515 45.846 -5.978 1.00 50.68 O ANISOU 1008 O ARG B 126 8113 7268 3876 -1592 -1649 650 O ATOM 1009 CB ARG A 126 50.494 43.589 -4.040 1.00 49.83 C ANISOU 1009 CB ARG B 126 4423 7446 7066 -493 -945 639 C ATOM 1010 CG ARG A 126 50.675 42.879 -2.704 1.00 61.30 C ANISOU 1010 CG ARG B 126 5305 8610 9378 -150 1073 -467 C ATOM 1011 CD ARG A 126 50.506 41.371 -2.772 1.00 70.98 C ANISOU 1011 CD ARG B 126 6066 8802 12102 403 337 -1383 C ATOM 1012 NE ARG A 126 50.014 40.776 -1.522 1.00 75.78 N ANISOU 1012 NE ARG B 126 6410 9126 13256 732 279 -2434 N ATOM 1013 CZ ARG A 126 48.938 39.992 -1.464 1.00 80.52 C ANISOU 1013 CZ ARG B 126 7729 9012 13852 270 -308 -2303 C ATOM 1014 NH1 ARG A 126 48.252 39.714 -2.573 1.00 75.26 N ANISOU 1014 NH1 ARG B 126 3984 10070 14544 614 -1937 -1211 N ATOM 1015 NH2 ARG A 126 48.534 39.477 -0.304 1.00 84.71 N ANISOU 1015 NH2 ARG B 126 8443 9133 14609 154 -560 -3265 N ATOM 1016 N SER A 127 49.359 46.309 -5.680 1.00 45.17 N ANISOU 1016 N SER B 127 6405 6105 4654 -537 272 666 N ATOM 1017 CA SER A 127 49.371 46.931 -7.022 1.00 45.18 C ANISOU 1017 CA SER B 127 6382 6517 4269 -264 -284 650 C ATOM 1018 C SER A 127 50.287 48.144 -7.002 1.00 44.06 C ANISOU 1018 C SER B 127 5846 6620 4274 -268 -1001 7 C ATOM 1019 O SER A 127 50.907 48.456 -8.010 1.00 51.05 O ANISOU 1019 O SER B 127 9415 6449 3533 -269 -623 590 O ATOM 1020 CB SER A 127 47.974 47.321 -7.492 1.00 46.96 C ANISOU 1020 CB SER B 127 6559 6827 4457 -337 566 241 C ATOM 1021 OG SER A 127 47.471 48.385 -6.680 1.00 47.73 O ANISOU 1021 OG SER B 127 5686 6576 5873 44 856 1070 O ATOM 1022 N TYR A 128 50.403 48.841 -5.874 1.00 41.48 N ANISOU 1022 N TYR B 128 5253 6118 4389 -622 -1232 -208 N ATOM 1023 CA TYR A 128 51.291 49.989 -5.817 1.00 41.75 C ANISOU 1023 CA TYR B 128 5167 6292 4404 -421 -748 -126 C ATOM 1024 C TYR A 128 52.703 49.537 -5.473 1.00 43.28 C ANISOU 1024 C TYR B 128 5150 5889 5406 -311 -543 -473 C ATOM 1025 O TYR A 128 53.657 50.254 -5.751 1.00 50.69 O ANISOU 1025 O TYR B 128 6660 5912 6687 -290 -152 -716 O ATOM 1026 CB TYR A 128 50.868 51.001 -4.758 1.00 40.32 C ANISOU 1026 CB TYR B 128 5256 6154 3908 -642 -520 476 C ATOM 1027 CG TYR A 128 49.631 51.800 -5.096 1.00 38.84 C ANISOU 1027 CG TYR B 128 5027 5838 3892 -375 -576 486 C ATOM 1028 CD1 TYR A 128 49.700 52.897 -5.944 1.00 40.46 C ANISOU 1028 CD1 TYR B 128 5413 5790 4169 -563 -303 184 C ATOM 1029 CD2 TYR A 128 48.397 51.438 -4.549 1.00 36.34 C ANISOU 1029 CD2 TYR B 128 4779 5615 3412 -143 -577 724 C ATOM 1030 CE1 TYR A 128 48.573 53.628 -6.255 1.00 41.77 C ANISOU 1030 CE1 TYR B 128 6297 5884 3690 -902 535 585 C ATOM 1031 CE2 TYR A 128 47.271 52.174 -4.863 1.00 39.91 C ANISOU 1031 CE2 TYR B 128 4938 5837 4389 -371 -305 415 C ATOM 1032 CZ TYR A 128 47.367 53.259 -5.711 1.00 41.74 C ANISOU 1032 CZ TYR B 128 6221 6101 3537 -1268 787 509 C ATOM 1033 OH TYR A 128 46.219 53.969 -5.994 1.00 42.11 O ANISOU 1033 OH TYR B 128 6000 5514 4487 -746 719 1670 O ATOM 1034 N GLY A 129 52.820 48.365 -4.848 1.00 42.11 N ANISOU 1034 N GLY B 129 5664 6058 4278 -85 -183 498 N ATOM 1035 CA GLY A 129 54.162 47.866 -4.579 1.00 40.48 C ANISOU 1035 CA GLY B 129 6175 6021 3184 -368 176 -100 C ATOM 1036 C GLY A 129 54.394 47.771 -3.090 1.00 37.91 C ANISOU 1036 C GLY B 129 5236 6069 3100 293 -58 -536 C ATOM 1037 O GLY A 129 54.626 46.689 -2.568 1.00 40.86 O ANISOU 1037 O GLY B 129 5364 6091 4071 -64 550 -542 O ATOM 1038 N LYS A 130 54.328 48.888 -2.364 1.00 41.09 N ANISOU 1038 N LYS B 130 5571 6204 3836 -158 -867 -467 N ATOM 1039 CA LYS A 130 54.552 48.751 -0.930 1.00 39.33 C ANISOU 1039 CA LYS B 130 5076 5865 4003 -166 -797 221 C ATOM 1040 C LYS A 130 54.074 50.005 -0.209 1.00 34.07 C ANISOU 1040 C LYS B 130 4613 4869 3463 492 -65 -221 C ATOM 1041 O LYS A 130 53.995 51.049 -0.856 1.00 37.69 O ANISOU 1041 O LYS B 130 4983 5663 3676 -107 1081 345 O ATOM 1042 CB LYS A 130 56.031 48.561 -0.611 1.00 48.04 C ANISOU 1042 CB LYS B 130 6199 6826 5226 -1318 -1696 846 C ATOM 1043 CG LYS A 130 56.810 49.834 -0.956 1.00 56.92 C ANISOU 1043 CG LYS B 130 8814 5910 6904 -696 -2458 1845 C ATOM 1044 CD LYS A 130 58.262 49.656 -0.525 1.00 64.23 C ANISOU 1044 CD LYS B 130 10079 6950 7377 -1460 -1556 2019 C ATOM 1045 CE LYS A 130 58.498 48.200 -0.131 1.00 66.12 C ANISOU 1045 CE LYS B 130 10805 8179 6139 -1726 -125 739 C ATOM 1046 NZ LYS A 130 58.291 47.967 1.327 1.00 77.00 N ANISOU 1046 NZ LYS B 130 14511 8537 6209 -992 -1736 -441 N ATOM 1047 N ILE A 131 53.795 49.829 1.065 1.00 31.02 N ANISOU 1047 N ILE B 131 3861 4582 3345 -482 133 -47 N ATOM 1048 CA ILE A 131 53.488 50.990 1.903 1.00 31.31 C ANISOU 1048 CA ILE B 131 4012 4209 3678 -423 -81 -152 C ATOM 1049 C ILE A 131 54.817 51.591 2.323 1.00 30.73 C ANISOU 1049 C ILE B 131 3753 4269 3654 -517 150 -164 C ATOM 1050 O ILE A 131 55.663 50.865 2.853 1.00 34.14 O ANISOU 1050 O ILE B 131 3854 5108 4008 -791 188 99 O ATOM 1051 CB ILE A 131 52.596 50.557 3.083 1.00 33.63 C ANISOU 1051 CB ILE B 131 5058 4285 3436 -1033 -124 -9 C ATOM 1052 CG1 ILE A 131 51.233 50.055 2.585 1.00 31.40 C ANISOU 1052 CG1 ILE B 131 4514 4086 3331 -270 -208 42 C ATOM 1053 CG2 ILE A 131 52.452 51.667 4.110 1.00 25.43 C ANISOU 1053 CG2 ILE B 131 4033 3240 2391 138 1295 -502 C ATOM 1054 CD1 ILE A 131 50.357 49.379 3.589 1.00 29.42 C ANISOU 1054 CD1 ILE B 131 4061 4050 3066 284 -38 314 C ATOM 1055 N HIS A 132 55.066 52.877 2.084 1.00 28.52 N ANISOU 1055 N HIS B 132 4089 4323 2422 -235 -296 -275 N ATOM 1056 CA HIS A 132 56.351 53.457 2.464 1.00 30.32 C ANISOU 1056 CA HIS B 132 4157 4435 2930 -299 71 -4 C ATOM 1057 C HIS A 132 56.464 53.750 3.951 1.00 31.66 C ANISOU 1057 C HIS B 132 4407 4647 2975 -666 86 210 C ATOM 1058 O HIS A 132 57.564 53.652 4.513 1.00 33.63 O ANISOU 1058 O HIS B 132 5439 4291 3048 -711 1019 -321 O ATOM 1059 CB HIS A 132 56.569 54.755 1.676 1.00 30.62 C ANISOU 1059 CB HIS B 132 4246 4205 3184 -277 46 -46 C ATOM 1060 CG HIS A 132 56.551 54.464 0.198 1.00 32.30 C ANISOU 1060 CG HIS B 132 4720 4451 3103 -214 79 -368 C ATOM 1061 ND1 HIS A 132 57.607 53.867 -0.455 1.00 37.74 N ANISOU 1061 ND1 HIS B 132 5939 5256 3143 -1222 -185 -328 N ATOM 1062 CD2 HIS A 132 55.611 54.690 -0.731 1.00 30.12 C ANISOU 1062 CD2 HIS B 132 4730 4248 2467 -1 741 -1297 C ATOM 1063 CE1 HIS A 132 57.313 53.736 -1.740 1.00 40.61 C ANISOU 1063 CE1 HIS B 132 6737 5694 3000 -1929 -57 -571 C ATOM 1064 NE2 HIS A 132 56.099 54.230 -1.925 1.00 40.22 N ANISOU 1064 NE2 HIS B 132 6345 5845 3092 -1717 -282 -259 N ATOM 1065 N LEU A 133 55.335 54.117 4.553 1.00 31.59 N ANISOU 1065 N LEU B 133 4605 4354 3043 -380 -89 -26 N ATOM 1066 CA LEU A 133 55.288 54.449 5.968 1.00 28.37 C ANISOU 1066 CA LEU B 133 3938 3870 2972 -91 196 10 C ATOM 1067 C LEU A 133 53.937 54.045 6.542 1.00 28.98 C ANISOU 1067 C LEU B 133 3357 4254 3399 -330 353 -398 C ATOM 1068 O LEU A 133 52.913 54.560 6.068 1.00 32.62 O ANISOU 1068 O LEU B 133 4510 4525 3358 -792 898 -113 O ATOM 1069 CB LEU A 133 55.511 55.934 6.181 1.00 29.90 C ANISOU 1069 CB LEU B 133 3627 4260 3473 -104 292 -72 C ATOM 1070 CG LEU A 133 55.381 56.475 7.607 1.00 30.77 C ANISOU 1070 CG LEU B 133 3544 4725 3421 360 627 493 C ATOM 1071 CD1 LEU A 133 56.318 55.777 8.574 1.00 30.36 C ANISOU 1071 CD1 LEU B 133 3154 5025 3356 -426 420 -419 C ATOM 1072 CD2 LEU A 133 55.657 57.984 7.590 1.00 30.54 C ANISOU 1072 CD2 LEU B 133 3610 4669 3327 357 529 -212 C ATOM 1073 N PHE A 134 53.956 53.137 7.515 1.00 30.24 N ANISOU 1073 N PHE B 134 4088 4159 3241 -390 666 -253 N ATOM 1074 CA PHE A 134 52.716 52.711 8.152 1.00 27.13 C ANISOU 1074 CA PHE B 134 3676 3832 2800 -121 279 137 C ATOM 1075 C PHE A 134 52.728 53.255 9.583 1.00 27.18 C ANISOU 1075 C PHE B 134 3808 3450 3069 -186 63 527 C ATOM 1076 O PHE A 134 53.577 52.870 10.382 1.00 27.06 O ANISOU 1076 O PHE B 134 3762 3739 2780 -314 182 84 O ATOM 1077 CB PHE A 134 52.554 51.191 8.159 1.00 26.18 C ANISOU 1077 CB PHE B 134 3256 3825 2867 -375 109 415 C ATOM 1078 CG PHE A 134 51.119 50.705 8.065 1.00 28.15 C ANISOU 1078 CG PHE B 134 3764 3739 3192 -258 -66 289 C ATOM 1079 CD1 PHE A 134 50.121 51.260 8.857 1.00 27.28 C ANISOU 1079 CD1 PHE B 134 3910 3496 2959 7 63 -133 C ATOM 1080 CD2 PHE A 134 50.766 49.686 7.173 1.00 26.16 C ANISOU 1080 CD2 PHE B 134 3356 3681 2900 -3 414 148 C ATOM 1081 CE1 PHE A 134 48.821 50.810 8.752 1.00 29.02 C ANISOU 1081 CE1 PHE B 134 4191 3644 3192 -273 60 88 C ATOM 1082 CE2 PHE A 134 49.456 49.240 7.054 1.00 28.76 C ANISOU 1082 CE2 PHE B 134 4500 3692 2734 -148 175 169 C ATOM 1083 CZ PHE A 134 48.472 49.813 7.845 1.00 30.25 C ANISOU 1083 CZ PHE B 134 4737 3547 3210 -171 -64 52 C ATOM 1084 N MET A 135 51.814 54.144 9.905 1.00 26.32 N ANISOU 1084 N MET B 135 3595 3693 2714 -5 367 190 N ATOM 1085 CA MET A 135 51.632 54.708 11.217 1.00 25.09 C ANISOU 1085 CA MET B 135 3269 3703 2560 -166 605 448 C ATOM 1086 C MET A 135 50.562 53.925 11.957 1.00 25.40 C ANISOU 1086 C MET B 135 3207 3842 2601 -266 460 287 C ATOM 1087 O MET A 135 49.510 53.598 11.409 1.00 25.93 O ANISOU 1087 O MET B 135 3696 3701 2456 163 571 289 O ATOM 1088 CB MET A 135 51.209 56.186 11.129 1.00 25.32 C ANISOU 1088 CB MET B 135 3207 4013 2401 -318 701 302 C ATOM 1089 CG MET A 135 51.140 56.778 12.544 1.00 28.15 C ANISOU 1089 CG MET B 135 3367 4549 2781 -814 4 125 C ATOM 1090 SD MET A 135 50.946 58.574 12.489 1.00 31.02 S ANISOU 1090 SD MET B 135 3750 4653 3384 -375 -86 334 S ATOM 1091 CE MET A 135 49.206 58.668 11.998 1.00 28.43 C ANISOU 1091 CE MET B 135 3016 4068 3717 -83 256 -533 C ATOM 1092 N GLY A 136 50.786 53.586 13.227 1.00 24.78 N ANISOU 1092 N GLY B 136 3188 3786 2439 -503 167 240 N ATOM 1093 CA GLY A 136 49.763 52.852 13.975 1.00 27.87 C ANISOU 1093 CA GLY B 136 3717 4095 2776 -678 220 -175 C ATOM 1094 C GLY A 136 49.867 53.167 15.458 1.00 26.53 C ANISOU 1094 C GLY B 136 3610 3703 2768 -44 526 -170 C ATOM 1095 O GLY A 136 50.719 53.955 15.894 1.00 27.86 O ANISOU 1095 O GLY B 136 3389 3779 3417 81 -146 -182 O ATOM 1096 N GLY A 137 48.999 52.554 16.248 1.00 29.09 N ANISOU 1096 N GLY B 137 4509 3712 2831 -273 435 -262 N ATOM 1097 CA GLY A 137 49.119 52.582 17.709 1.00 28.89 C ANISOU 1097 CA GLY B 137 4062 4089 2827 -596 602 -311 C ATOM 1098 C GLY A 137 49.379 51.161 18.223 1.00 28.78 C ANISOU 1098 C GLY B 137 3846 4271 2819 -450 276 -211 C ATOM 1099 O GLY A 137 49.700 50.268 17.432 1.00 29.61 O ANISOU 1099 O GLY B 137 4311 4132 2806 -454 18 -10 O ATOM 1100 N VAL A 138 49.237 50.951 19.535 1.00 26.82 N ANISOU 1100 N VAL B 138 3435 3959 2794 -174 231 -77 N ATOM 1101 CA VAL A 138 49.477 49.602 20.061 1.00 24.45 C ANISOU 1101 CA VAL B 138 3353 3292 2644 -155 53 295 C ATOM 1102 C VAL A 138 48.499 49.334 21.198 1.00 24.17 C ANISOU 1102 C VAL B 138 3323 3399 2464 47 -81 329 C ATOM 1103 O VAL A 138 48.155 50.246 21.955 1.00 26.46 O ANISOU 1103 O VAL B 138 3429 3798 2826 -189 -351 516 O ATOM 1104 CB VAL A 138 50.955 49.459 20.481 1.00 25.77 C ANISOU 1104 CB VAL B 138 3325 3426 3039 -172 -199 611 C ATOM 1105 CG1 VAL A 138 51.302 50.488 21.553 1.00 28.40 C ANISOU 1105 CG1 VAL B 138 4717 3466 2609 121 -305 480 C ATOM 1106 CG2 VAL A 138 51.291 48.058 20.973 1.00 26.22 C ANISOU 1106 CG2 VAL B 138 3531 4230 2201 -424 148 240 C ATOM 1107 N GLY A 139 48.026 48.090 21.298 1.00 24.37 N ANISOU 1107 N GLY B 139 3893 2966 2402 32 106 679 N ATOM 1108 CA GLY A 139 47.086 47.752 22.356 1.00 26.69 C ANISOU 1108 CA GLY B 139 4036 3470 2635 13 248 245 C ATOM 1109 C GLY A 139 47.824 47.680 23.688 1.00 27.30 C ANISOU 1109 C GLY B 139 4457 3318 2597 -329 173 122 C ATOM 1110 O GLY A 139 49.064 47.612 23.748 1.00 28.89 O ANISOU 1110 O GLY B 139 4748 3244 2984 -395 -207 425 O ATOM 1111 N ASN A 140 47.070 47.694 24.795 1.00 25.69 N ANISOU 1111 N ASN B 140 3631 3502 2629 48 -42 124 N ATOM 1112 CA ASN A 140 47.649 47.572 26.116 1.00 27.00 C ANISOU 1112 CA ASN B 140 3575 4061 2622 -548 93 -99 C ATOM 1113 C ASN A 140 48.413 46.247 26.234 1.00 28.54 C ANISOU 1113 C ASN B 140 3580 3849 3413 -564 68 141 C ATOM 1114 O ASN A 140 49.389 46.154 26.998 1.00 26.79 O ANISOU 1114 O ASN B 140 3564 3855 2759 -580 23 -128 O ATOM 1115 CB ASN A 140 46.570 47.626 27.197 1.00 24.74 C ANISOU 1115 CB ASN B 140 3986 2859 2555 -398 -275 507 C ATOM 1116 CG ASN A 140 45.889 48.970 27.317 1.00 27.52 C ANISOU 1116 CG ASN B 140 4084 3268 3104 -302 -543 -183 C ATOM 1117 OD1 ASN A 140 46.205 49.947 26.617 1.00 28.78 O ANISOU 1117 OD1 ASN B 140 4295 4160 2480 -141 170 318 O ATOM 1118 ND2 ASN A 140 44.912 49.057 28.214 1.00 32.68 N ANISOU 1118 ND2 ASN B 140 4801 4318 3298 -1401 -449 -329 N ATOM 1119 N ASP A 141 47.962 45.237 25.504 1.00 25.43 N ANISOU 1119 N ASP B 141 3624 3714 2323 -341 347 -354 N ATOM 1120 CA ASP A 141 48.667 43.956 25.582 1.00 26.26 C ANISOU 1120 CA ASP B 141 3642 3814 2522 -331 355 -36 C ATOM 1121 C ASP A 141 49.654 43.792 24.437 1.00 26.49 C ANISOU 1121 C ASP B 141 3569 3491 3006 -170 94 -156 C ATOM 1122 O ASP A 141 50.057 42.658 24.136 1.00 25.75 O ANISOU 1122 O ASP B 141 3565 3223 2995 -391 112 560 O ATOM 1123 CB ASP A 141 47.673 42.788 25.582 1.00 26.72 C ANISOU 1123 CB ASP B 141 3547 3842 2765 -309 -249 -384 C ATOM 1124 CG ASP A 141 46.845 42.790 24.308 1.00 26.06 C ANISOU 1124 CG ASP B 141 3097 3817 2989 461 -314 22 C ATOM 1125 OD1 ASP A 141 45.931 41.946 24.175 1.00 34.78 O ANISOU 1125 OD1 ASP B 141 5599 3472 4144 141 402 -150 O ATOM 1126 OD2 ASP A 141 47.065 43.632 23.417 1.00 30.28 O ANISOU 1126 OD2 ASP B 141 4384 3992 3130 256 314 -130 O ATOM 1127 N GLY A 142 50.028 44.883 23.779 1.00 26.48 N ANISOU 1127 N GLY B 142 3962 3312 2788 -208 434 86 N ATOM 1128 CA GLY A 142 51.038 44.845 22.717 1.00 25.59 C ANISOU 1128 CA GLY B 142 3756 3176 2790 -148 467 139 C ATOM 1129 C GLY A 142 50.497 44.483 21.358 1.00 25.67 C ANISOU 1129 C GLY B 142 3392 3211 3151 224 -423 428 C ATOM 1130 O GLY A 142 51.264 44.444 20.366 1.00 27.27 O ANISOU 1130 O GLY B 142 3583 3831 2948 -36 154 66 O ATOM 1131 N HIS A 143 49.195 44.203 21.210 1.00 26.81 N ANISOU 1131 N HIS B 143 3542 3427 3216 -44 -50 594 N ATOM 1132 CA HIS A 143 48.660 43.787 19.896 1.00 27.70 C ANISOU 1132 CA HIS B 143 3694 3720 3113 -107 -43 623 C ATOM 1133 C HIS A 143 48.581 44.946 18.912 1.00 28.72 C ANISOU 1133 C HIS B 143 3819 4031 3063 -16 -117 490 C ATOM 1134 O HIS A 143 48.634 46.121 19.287 1.00 28.56 O ANISOU 1134 O HIS B 143 3322 4544 2984 -223 -216 252 O ATOM 1135 CB HIS A 143 47.262 43.171 20.030 1.00 28.55 C ANISOU 1135 CB HIS B 143 4574 3745 2530 -324 194 700 C ATOM 1136 CG HIS A 143 46.139 44.138 20.250 1.00 35.65 C ANISOU 1136 CG HIS B 143 5284 4866 3394 -1553 -40 960 C ATOM 1137 ND1 HIS A 143 45.701 44.479 21.516 1.00 33.00 N ANISOU 1137 ND1 HIS B 143 4485 4459 3595 -302 -143 483 N ATOM 1138 CD2 HIS A 143 45.332 44.829 19.391 1.00 39.21 C ANISOU 1138 CD2 HIS B 143 5260 5829 3811 -1714 220 735 C ATOM 1139 CE1 HIS A 143 44.698 45.332 21.458 1.00 33.43 C ANISOU 1139 CE1 HIS B 143 4082 4472 4145 252 -361 928 C ATOM 1140 NE2 HIS A 143 44.457 45.569 20.173 1.00 38.04 N ANISOU 1140 NE2 HIS B 143 4721 5393 4340 -876 -18 943 N ATOM 1141 N ILE A 144 48.398 44.600 17.638 1.00 27.69 N ANISOU 1141 N ILE B 144 4000 3529 2989 -166 -216 269 N ATOM 1142 CA ILE A 144 48.329 45.610 16.579 1.00 30.21 C ANISOU 1142 CA ILE B 144 4441 3961 3078 -20 -40 137 C ATOM 1143 C ILE A 144 47.003 45.555 15.841 1.00 30.24 C ANISOU 1143 C ILE B 144 4207 4313 2970 29 -24 347 C ATOM 1144 O ILE A 144 46.530 44.455 15.501 1.00 28.53 O ANISOU 1144 O ILE B 144 3824 4341 2677 -185 -149 407 O ATOM 1145 CB ILE A 144 49.535 45.399 15.654 1.00 35.87 C ANISOU 1145 CB ILE B 144 5317 5273 3038 -1017 499 -391 C ATOM 1146 CG1 ILE A 144 50.824 45.888 16.339 1.00 39.81 C ANISOU 1146 CG1 ILE B 144 6210 5401 3515 -2039 1688 -660 C ATOM 1147 CG2 ILE A 144 49.303 46.029 14.284 1.00 38.08 C ANISOU 1147 CG2 ILE B 144 5980 5485 3002 -1448 680 -144 C ATOM 1148 CD1 ILE A 144 52.089 45.529 15.611 1.00 44.89 C ANISOU 1148 CD1 ILE B 144 5198 7047 4812 -2738 1919 -773 C ATOM 1149 N ALA A 145 46.411 46.731 15.616 1.00 30.04 N ANISOU 1149 N ALA B 145 4019 4709 2687 51 -574 734 N ATOM 1150 CA ALA A 145 45.121 46.823 14.933 1.00 33.88 C ANISOU 1150 CA ALA B 145 4272 4899 3700 -516 -314 528 C ATOM 1151 C ALA A 145 44.134 45.890 15.611 1.00 32.88 C ANISOU 1151 C ALA B 145 3871 4994 3626 -722 282 533 C ATOM 1152 O ALA A 145 44.055 45.921 16.850 1.00 37.05 O ANISOU 1152 O ALA B 145 5636 4738 3703 -722 -285 559 O ATOM 1153 CB ALA A 145 45.268 46.491 13.454 1.00 31.60 C ANISOU 1153 CB ALA B 145 4304 4341 3363 -118 479 935 C ATOM 1154 N PHE A 146 43.403 45.059 14.871 1.00 32.14 N ANISOU 1154 N PHE B 146 4142 4992 3078 -336 1125 474 N ATOM 1155 CA PHE A 146 42.519 44.117 15.556 1.00 32.43 C ANISOU 1155 CA PHE B 146 4183 5097 3041 -475 853 228 C ATOM 1156 C PHE A 146 43.148 42.725 15.593 1.00 31.27 C ANISOU 1156 C PHE B 146 4169 4422 3293 -471 846 212 C ATOM 1157 O PHE A 146 42.456 41.743 15.907 1.00 35.15 O ANISOU 1157 O PHE B 146 4625 4822 3907 -252 620 -501 O ATOM 1158 CB PHE A 146 41.124 43.988 14.938 1.00 32.34 C ANISOU 1158 CB PHE B 146 4126 5133 3028 -936 384 31 C ATOM 1159 CG PHE A 146 40.268 45.204 15.264 1.00 36.84 C ANISOU 1159 CG PHE B 146 4333 5777 3886 -1021 -100 160 C ATOM 1160 CD1 PHE A 146 39.681 45.330 16.508 1.00 42.68 C ANISOU 1160 CD1 PHE B 146 4466 7257 4494 -1295 -187 -795 C ATOM 1161 CD2 PHE A 146 40.074 46.191 14.317 1.00 34.07 C ANISOU 1161 CD2 PHE B 146 3601 5135 4210 121 -789 -10 C ATOM 1162 CE1 PHE A 146 38.905 46.438 16.799 1.00 45.34 C ANISOU 1162 CE1 PHE B 146 4476 7702 5049 -1527 -157 -1240 C ATOM 1163 CE2 PHE A 146 39.303 47.297 14.589 1.00 35.10 C ANISOU 1163 CE2 PHE B 146 3813 5445 4079 116 -1337 176 C ATOM 1164 CZ PHE A 146 38.720 47.408 15.834 1.00 39.62 C ANISOU 1164 CZ PHE B 146 4236 6578 4238 -695 -785 -513 C ATOM 1165 N ASN A 147 44.435 42.632 15.286 1.00 31.88 N ANISOU 1165 N ASN B 147 4445 4628 3040 -483 137 78 N ATOM 1166 CA ASN A 147 45.066 41.322 15.452 1.00 31.70 C ANISOU 1166 CA ASN B 147 4438 4565 3042 -688 276 -26 C ATOM 1167 C ASN A 147 45.148 40.921 16.918 1.00 34.38 C ANISOU 1167 C ASN B 147 4673 5296 3095 -405 194 -487 C ATOM 1168 O ASN A 147 45.287 41.729 17.845 1.00 40.03 O ANISOU 1168 O ASN B 147 6438 5686 3087 254 632 390 O ATOM 1169 CB ASN A 147 46.478 41.369 14.862 1.00 30.43 C ANISOU 1169 CB ASN B 147 4384 4252 2927 -123 -373 45 C ATOM 1170 CG ASN A 147 46.406 41.655 13.373 1.00 30.24 C ANISOU 1170 CG ASN B 147 4651 3873 2967 1 -136 262 C ATOM 1171 OD1 ASN A 147 46.252 40.685 12.618 1.00 32.49 O ANISOU 1171 OD1 ASN B 147 4299 4953 3093 -219 -486 341 O ATOM 1172 ND2 ASN A 147 46.506 42.924 12.993 1.00 30.25 N ANISOU 1172 ND2 ASN B 147 4554 3366 3574 -380 304 317 N ATOM 1173 N GLU A 148 45.079 39.622 17.218 1.00 36.52 N ANISOU 1173 N GLU B 148 4784 5165 3926 -576 621 -647 N ATOM 1174 CA GLU A 148 45.151 39.250 18.619 1.00 37.62 C ANISOU 1174 CA GLU B 148 4800 5496 3996 -506 795 -628 C ATOM 1175 C GLU A 148 46.564 38.904 19.040 1.00 35.13 C ANISOU 1175 C GLU B 148 4193 5501 3653 -282 383 -550 C ATOM 1176 O GLU A 148 47.414 38.701 18.181 1.00 36.10 O ANISOU 1176 O GLU B 148 4942 5346 3428 -441 92 -134 O ATOM 1177 CB GLU A 148 44.159 38.098 18.839 1.00 44.63 C ANISOU 1177 CB GLU B 148 6139 5477 5341 -679 1299 -1418 C ATOM 1178 CG GLU A 148 42.966 38.738 19.571 1.00 62.51 C ANISOU 1178 CG GLU B 148 10150 6335 7266 -2672 -1198 -738 C ATOM 1179 CD GLU A 148 41.772 37.821 19.703 1.00 62.28 C ANISOU 1179 CD GLU B 148 10737 6366 6563 -2751 -91 -994 C ATOM 1180 OE1 GLU A 148 41.669 37.248 20.814 1.00 58.46 O ANISOU 1180 OE1 GLU B 148 8529 7728 5956 -589 -931 32 O ATOM 1181 OE2 GLU A 148 41.018 37.728 18.705 1.00 53.92 O ANISOU 1181 OE2 GLU B 148 7807 6685 5995 -228 -852 -345 O ATOM 1182 N PRO A 149 46.799 38.848 20.339 1.00 32.87 N ANISOU 1182 N PRO B 149 3807 5083 3601 -97 -179 -132 N ATOM 1183 CA PRO A 149 48.067 38.333 20.839 1.00 32.24 C ANISOU 1183 CA PRO B 149 4390 4418 3444 -319 -805 463 C ATOM 1184 C PRO A 149 48.282 36.936 20.255 1.00 31.02 C ANISOU 1184 C PRO B 149 3812 4107 3866 -8 -140 -98 C ATOM 1185 O PRO A 149 47.319 36.191 20.079 1.00 30.07 O ANISOU 1185 O PRO B 149 3975 4089 3359 -109 69 11 O ATOM 1186 CB PRO A 149 47.813 38.245 22.333 1.00 31.62 C ANISOU 1186 CB PRO B 149 4043 4309 3661 -329 -144 -207 C ATOM 1187 CG PRO A 149 46.783 39.294 22.617 1.00 34.44 C ANISOU 1187 CG PRO B 149 4321 5187 3579 -832 -344 -382 C ATOM 1188 CD PRO A 149 45.873 39.234 21.417 1.00 35.77 C ANISOU 1188 CD PRO B 149 4150 5686 3756 -783 18 -291 C ATOM 1189 N ALA A 150 49.520 36.596 19.945 1.00 31.18 N ANISOU 1189 N ALA B 150 3700 4110 4039 -107 -144 333 N ATOM 1190 CA ALA A 150 49.976 35.342 19.340 1.00 28.85 C ANISOU 1190 CA ALA B 150 3788 3648 3525 217 -129 -142 C ATOM 1191 C ALA A 150 49.460 35.237 17.913 1.00 30.57 C ANISOU 1191 C ALA B 150 4376 3691 3548 371 -19 -112 C ATOM 1192 O ALA A 150 49.401 34.134 17.373 1.00 31.66 O ANISOU 1192 O ALA B 150 4014 4233 3783 29 -88 363 O ATOM 1193 CB ALA A 150 49.582 34.110 20.139 1.00 31.71 C ANISOU 1193 CB ALA B 150 3074 4424 4551 -839 652 -1116 C ATOM 1194 N SER A 151 49.099 36.371 17.305 1.00 29.94 N ANISOU 1194 N SER B 151 3870 4227 3279 -100 -355 23 N ATOM 1195 CA SER A 151 48.823 36.355 15.883 1.00 28.79 C ANISOU 1195 CA SER B 151 3667 3912 3359 -130 -366 214 C ATOM 1196 C SER A 151 50.095 35.924 15.146 1.00 27.85 C ANISOU 1196 C SER B 151 3270 4162 3148 -5 -137 69 C ATOM 1197 O SER A 151 51.169 36.271 15.640 1.00 28.87 O ANISOU 1197 O SER B 151 3544 4607 2820 -650 -615 285 O ATOM 1198 CB SER A 151 48.455 37.729 15.314 1.00 29.68 C ANISOU 1198 CB SER B 151 3367 4612 3298 -169 -518 533 C ATOM 1199 OG SER A 151 47.127 38.116 15.637 1.00 34.72 O ANISOU 1199 OG SER B 151 3690 4948 4553 -486 -1143 1135 O ATOM 1200 N SER A 152 49.943 35.253 14.018 1.00 29.45 N ANISOU 1200 N SER B 152 3378 3942 3869 9 -659 386 N ATOM 1201 CA SER A 152 51.046 35.031 13.091 1.00 29.19 C ANISOU 1201 CA SER B 152 3469 4067 3556 16 -643 433 C ATOM 1202 C SER A 152 51.653 36.355 12.651 1.00 29.48 C ANISOU 1202 C SER B 152 3728 3893 3582 34 -663 526 C ATOM 1203 O SER A 152 50.937 37.333 12.364 1.00 29.07 O ANISOU 1203 O SER B 152 3750 3599 3698 168 -539 744 O ATOM 1204 CB SER A 152 50.571 34.257 11.852 1.00 24.29 C ANISOU 1204 CB SER B 152 2261 4031 2936 151 489 373 C ATOM 1205 OG SER A 152 51.628 34.260 10.892 1.00 30.65 O ANISOU 1205 OG SER B 152 4423 4323 2899 148 -104 292 O ATOM 1206 N LEU A 153 52.985 36.416 12.561 1.00 29.06 N ANISOU 1206 N LEU B 153 4048 4037 2954 -219 -370 477 N ATOM 1207 CA LEU A 153 53.640 37.644 12.103 1.00 29.26 C ANISOU 1207 CA LEU B 153 3685 3994 3440 -261 -742 284 C ATOM 1208 C LEU A 153 53.456 37.778 10.600 1.00 29.11 C ANISOU 1208 C LEU B 153 3316 4253 3491 209 -558 101 C ATOM 1209 O LEU A 153 53.815 38.794 9.999 1.00 34.08 O ANISOU 1209 O LEU B 153 4357 4097 4497 304 441 284 O ATOM 1210 CB LEU A 153 55.118 37.632 12.436 1.00 33.10 C ANISOU 1210 CB LEU B 153 3749 4053 4775 -216 131 228 C ATOM 1211 CG LEU A 153 55.604 38.333 13.711 1.00 40.02 C ANISOU 1211 CG LEU B 153 5950 5263 3992 -2329 133 679 C ATOM 1212 CD1 LEU A 153 54.535 38.420 14.783 1.00 36.67 C ANISOU 1212 CD1 LEU B 153 6870 4004 3059 -1329 1626 -51 C ATOM 1213 CD2 LEU A 153 56.848 37.646 14.268 1.00 35.55 C ANISOU 1213 CD2 LEU B 153 2763 5853 4889 200 331 967 C ATOM 1214 N ALA A 154 52.912 36.741 9.970 1.00 28.86 N ANISOU 1214 N ALA B 154 3772 3811 3384 -100 -231 365 N ATOM 1215 CA ALA A 154 52.607 36.853 8.545 1.00 30.37 C ANISOU 1215 CA ALA B 154 3746 4496 3297 -369 -386 198 C ATOM 1216 C ALA A 154 51.110 36.950 8.328 1.00 31.22 C ANISOU 1216 C ALA B 154 4347 4666 2850 -661 -348 317 C ATOM 1217 O ALA A 154 50.637 36.709 7.212 1.00 34.75 O ANISOU 1217 O ALA B 154 5023 4855 3323 -392 -1059 947 O ATOM 1218 CB ALA A 154 53.163 35.653 7.787 1.00 34.29 C ANISOU 1218 CB ALA B 154 4068 5230 3729 -356 -793 160 C ATOM 1219 N SER A 155 50.317 37.276 9.362 1.00 27.85 N ANISOU 1219 N SER B 155 3657 4121 2802 -121 7 9 N ATOM 1220 CA SER A 155 48.863 37.240 9.111 1.00 29.11 C ANISOU 1220 CA SER B 155 3680 4341 3039 -299 -34 162 C ATOM 1221 C SER A 155 48.486 38.353 8.149 1.00 31.02 C ANISOU 1221 C SER B 155 3935 4240 3611 -131 316 360 C ATOM 1222 O SER A 155 49.237 39.311 7.965 1.00 29.07 O ANISOU 1222 O SER B 155 4093 3993 2960 -410 506 489 O ATOM 1223 CB SER A 155 48.154 37.314 10.463 1.00 28.66 C ANISOU 1223 CB SER B 155 3994 4035 2860 -630 -380 718 C ATOM 1224 OG SER A 155 48.668 38.466 11.146 1.00 30.95 O ANISOU 1224 OG SER B 155 3936 4581 3242 -12 18 839 O ATOM 1225 N ARG A 156 47.330 38.271 7.497 1.00 27.27 N ANISOU 1225 N ARG B 156 3264 3955 3142 464 -1 470 N ATOM 1226 CA ARG A 156 46.898 39.198 6.462 1.00 28.27 C ANISOU 1226 CA ARG B 156 3079 4309 3353 470 18 544 C ATOM 1227 C ARG A 156 45.512 39.772 6.758 1.00 27.82 C ANISOU 1227 C ARG B 156 2907 3931 3731 789 -28 347 C ATOM 1228 O ARG A 156 44.879 39.343 7.729 1.00 31.42 O ANISOU 1228 O ARG B 156 4483 3701 3754 -136 705 427 O ATOM 1229 CB ARG A 156 46.858 38.475 5.109 1.00 30.35 C ANISOU 1229 CB ARG B 156 4010 4532 2991 289 -109 187 C ATOM 1230 CG ARG A 156 48.248 38.036 4.627 1.00 32.56 C ANISOU 1230 CG ARG B 156 4808 4586 2978 -232 -361 625 C ATOM 1231 CD ARG A 156 48.925 39.285 4.061 1.00 36.21 C ANISOU 1231 CD ARG B 156 5806 4472 3480 -146 -508 297 C ATOM 1232 NE ARG A 156 50.373 39.204 4.123 1.00 40.57 N ANISOU 1232 NE ARG B 156 6347 4722 4348 -532 -933 182 N ATOM 1233 CZ ARG A 156 51.183 40.183 3.735 1.00 40.13 C ANISOU 1233 CZ ARG B 156 5796 4720 4733 -761 -573 57 C ATOM 1234 NH1 ARG A 156 50.686 41.317 3.260 1.00 37.87 N ANISOU 1234 NH1 ARG B 156 5173 5635 3582 -493 -1594 379 N ATOM 1235 NH2 ARG A 156 52.487 39.983 3.839 1.00 40.93 N ANISOU 1235 NH2 ARG B 156 6082 4379 5092 -499 -635 1412 N ATOM 1236 N THR A 157 45.061 40.712 5.917 1.00 30.93 N ANISOU 1236 N THR B 157 3402 4458 3890 186 411 340 N ATOM 1237 CA THR A 157 43.803 41.420 6.105 1.00 31.02 C ANISOU 1237 CA THR B 157 3752 4415 3620 -155 491 575 C ATOM 1238 C THR A 157 42.664 40.427 6.249 1.00 30.19 C ANISOU 1238 C THR B 157 3483 4497 3492 48 735 555 C ATOM 1239 O THR A 157 42.597 39.480 5.454 1.00 35.36 O ANISOU 1239 O THR B 157 4388 4808 4240 93 111 919 O ATOM 1240 CB THR A 157 43.509 42.372 4.930 1.00 30.76 C ANISOU 1240 CB THR B 157 3447 4291 3950 77 433 279 C ATOM 1241 OG1 THR A 157 44.582 43.317 4.848 1.00 35.13 O ANISOU 1241 OG1 THR B 157 6169 4069 3109 -194 326 -108 O ATOM 1242 CG2 THR A 157 42.223 43.138 5.165 1.00 28.06 C ANISOU 1242 CG2 THR B 157 3457 4294 2910 150 280 74 C ATOM 1243 N ARG A 158 41.801 40.606 7.242 1.00 30.88 N ANISOU 1243 N ARG B 158 3677 4516 3538 -184 889 460 N ATOM 1244 CA ARG A 158 40.795 39.586 7.520 1.00 31.76 C ANISOU 1244 CA ARG B 158 3594 4736 3736 29 1033 278 C ATOM 1245 C ARG A 158 39.754 40.099 8.509 1.00 32.73 C ANISOU 1245 C ARG B 158 3919 4475 4043 -104 855 287 C ATOM 1246 O ARG A 158 39.950 41.120 9.149 1.00 34.08 O ANISOU 1246 O ARG B 158 4434 4672 3844 -90 510 247 O ATOM 1247 CB ARG A 158 41.443 38.314 8.083 1.00 34.38 C ANISOU 1247 CB ARG B 158 3660 5187 4217 9 1226 540 C ATOM 1248 CG ARG A 158 41.938 38.412 9.524 1.00 36.00 C ANISOU 1248 CG ARG B 158 4251 5275 4153 -123 1535 379 C ATOM 1249 CD ARG A 158 43.000 37.359 9.810 1.00 34.46 C ANISOU 1249 CD ARG B 158 4145 5227 3722 -368 735 1012 C ATOM 1250 NE ARG A 158 43.504 37.346 11.197 1.00 33.95 N ANISOU 1250 NE ARG B 158 4630 4450 3821 -159 1221 798 N ATOM 1251 CZ ARG A 158 44.471 38.170 11.608 1.00 36.78 C ANISOU 1251 CZ ARG B 158 6016 4217 3740 -394 521 541 C ATOM 1252 NH1 ARG A 158 44.973 39.030 10.717 1.00 31.31 N ANISOU 1252 NH1 ARG B 158 3855 4426 3616 -117 9 704 N ATOM 1253 NH2 ARG A 158 44.913 38.145 12.845 1.00 31.35 N ANISOU 1253 NH2 ARG B 158 3919 4507 3486 432 -249 696 N ATOM 1254 N ILE A 159 38.654 39.373 8.632 1.00 35.47 N ANISOU 1254 N ILE B 159 4542 4492 4441 -50 1111 179 N ATOM 1255 CA ILE A 159 37.611 39.728 9.573 1.00 35.07 C ANISOU 1255 CA ILE B 159 4407 4135 4782 416 896 -14 C ATOM 1256 C ILE A 159 37.975 39.147 10.945 1.00 37.45 C ANISOU 1256 C ILE B 159 4806 4741 4684 -268 875 -130 C ATOM 1257 O ILE A 159 38.550 38.058 11.004 1.00 39.31 O ANISOU 1257 O ILE B 159 4878 5013 5044 341 1309 -5 O ATOM 1258 CB ILE A 159 36.226 39.198 9.182 1.00 39.65 C ANISOU 1258 CB ILE B 159 5410 4542 5112 -294 284 485 C ATOM 1259 CG1 ILE A 159 35.106 39.794 10.040 1.00 41.71 C ANISOU 1259 CG1 ILE B 159 5362 5294 5191 -823 877 -95 C ATOM 1260 CG2 ILE A 159 36.201 37.676 9.232 1.00 38.23 C ANISOU 1260 CG2 ILE B 159 5699 3317 5509 -405 418 757 C ATOM 1261 CD1 ILE A 159 33.722 39.545 9.476 1.00 40.62 C ANISOU 1261 CD1 ILE B 159 5716 4824 4893 -491 821 -362 C ATOM 1262 N LYS A 160 37.629 39.888 11.978 1.00 40.97 N ANISOU 1262 N LYS B 160 5651 5057 4861 -739 423 378 N ATOM 1263 CA LYS A 160 37.850 39.576 13.365 1.00 43.00 C ANISOU 1263 CA LYS B 160 6809 4735 4795 -446 519 202 C ATOM 1264 C LYS A 160 36.580 39.825 14.195 1.00 44.52 C ANISOU 1264 C LYS B 160 6225 5368 5323 -675 1661 -868 C ATOM 1265 O LYS A 160 35.819 40.750 13.895 1.00 46.37 O ANISOU 1265 O LYS B 160 6438 5703 5476 -894 1992 -589 O ATOM 1266 CB LYS A 160 38.975 40.419 13.992 1.00 40.85 C ANISOU 1266 CB LYS B 160 5643 4962 4918 -153 508 397 C ATOM 1267 CG LYS A 160 40.382 40.178 13.487 1.00 43.72 C ANISOU 1267 CG LYS B 160 6473 4746 5394 -387 258 512 C ATOM 1268 CD LYS A 160 40.662 38.693 13.331 1.00 47.22 C ANISOU 1268 CD LYS B 160 5920 5840 6181 -889 443 211 C ATOM 1269 CE LYS A 160 41.423 38.145 14.518 1.00 51.24 C ANISOU 1269 CE LYS B 160 6579 6643 6247 -1400 612 143 C ATOM 1270 NZ LYS A 160 40.708 38.193 15.820 1.00 52.76 N ANISOU 1270 NZ LYS B 160 8506 5514 6026 -562 306 357 N ATOM 1271 N THR A 161 36.441 38.986 15.224 1.00 46.07 N ANISOU 1271 N THR B 161 6196 5573 5734 95 1582 -914 N ATOM 1272 CA THR A 161 35.419 39.139 16.249 1.00 50.03 C ANISOU 1272 CA THR B 161 6913 6464 5630 -308 1964 -1436 C ATOM 1273 C THR A 161 35.935 39.994 17.393 1.00 49.72 C ANISOU 1273 C THR B 161 6611 6875 5404 41 1749 -1746 C ATOM 1274 O THR A 161 36.859 39.596 18.095 1.00 51.50 O ANISOU 1274 O THR B 161 5747 7772 6050 61 770 -337 O ATOM 1275 CB THR A 161 35.007 37.770 16.808 1.00 50.46 C ANISOU 1275 CB THR B 161 6768 6590 5816 -161 1539 -1616 C ATOM 1276 OG1 THR A 161 34.588 36.948 15.708 1.00 55.20 O ANISOU 1276 OG1 THR B 161 6600 7971 6401 191 1818 -728 O ATOM 1277 CG2 THR A 161 33.826 37.902 17.756 1.00 52.69 C ANISOU 1277 CG2 THR B 161 4577 8539 6904 -166 2426 -3197 C ATOM 1278 N LEU A 162 35.395 41.181 17.602 1.00 50.34 N ANISOU 1278 N LEU B 162 6449 7256 5423 -457 1918 -1694 N ATOM 1279 CA LEU A 162 36.043 42.086 18.554 1.00 52.65 C ANISOU 1279 CA LEU B 162 6286 8091 5628 -161 1548 -1472 C ATOM 1280 C LEU A 162 36.103 41.534 19.967 1.00 52.23 C ANISOU 1280 C LEU B 162 5897 8430 5516 386 1306 -1358 C ATOM 1281 O LEU A 162 35.254 40.700 20.308 1.00 62.49 O ANISOU 1281 O LEU B 162 8039 8700 7004 -362 1496 -2942 O ATOM 1282 CB LEU A 162 35.283 43.418 18.503 1.00 53.19 C ANISOU 1282 CB LEU B 162 6314 8196 5699 -499 1777 -1522 C ATOM 1283 CG LEU A 162 35.233 44.046 17.107 1.00 52.93 C ANISOU 1283 CG LEU B 162 6606 7838 5667 13 1777 -1363 C ATOM 1284 CD1 LEU A 162 34.604 45.421 17.187 1.00 55.07 C ANISOU 1284 CD1 LEU B 162 6561 7050 7311 156 2360 -995 C ATOM 1285 CD2 LEU A 162 36.642 44.053 16.541 1.00 57.05 C ANISOU 1285 CD2 LEU B 162 8865 8972 3838 -1552 778 -482 C ATOM 1286 N THR A 163 37.057 41.952 20.802 1.00 59.10 N ANISOU 1286 N THR B 163 6302 9840 6313 -767 1535 -340 N ATOM 1287 CA THR A 163 37.065 41.457 22.184 1.00 67.97 C ANISOU 1287 CA THR B 163 8737 10769 6321 -2093 2043 -691 C ATOM 1288 C THR A 163 36.171 42.318 23.078 1.00 72.03 C ANISOU 1288 C THR B 163 9650 11375 6344 -2327 1519 -773 C ATOM 1289 O THR A 163 36.021 43.513 22.824 1.00 63.46 O ANISOU 1289 O THR B 163 9754 9523 4834 -2098 377 -773 O ATOM 1290 CB THR A 163 38.469 41.417 22.814 1.00 67.87 C ANISOU 1290 CB THR B 163 8532 10536 6719 -1473 2303 -297 C ATOM 1291 OG1 THR A 163 38.883 42.754 23.157 1.00 77.41 O ANISOU 1291 OG1 THR B 163 9711 11701 8001 -1467 -319 417 O ATOM 1292 CG2 THR A 163 39.524 40.866 21.859 1.00 61.67 C ANISOU 1292 CG2 THR B 163 6295 9323 7815 -351 2422 -293 C ATOM 1293 N HIS A 164 35.586 41.730 24.109 1.00 73.18 N ANISOU 1293 N HIS B 164 8953 11950 6903 -2104 1660 -1261 N ATOM 1294 CA HIS A 164 34.770 42.441 25.083 1.00 79.94 C ANISOU 1294 CA HIS B 164 10826 12269 7277 -2713 673 -1193 C ATOM 1295 C HIS A 164 35.470 43.712 25.548 1.00 75.86 C ANISOU 1295 C HIS B 164 10789 12290 5744 -2880 480 -1278 C ATOM 1296 O HIS A 164 34.904 44.798 25.530 1.00 68.07 O ANISOU 1296 O HIS B 164 10732 12117 3012 -3617 -310 -48 O ATOM 1297 CB HIS A 164 34.496 41.554 26.288 1.00 86.94 C ANISOU 1297 CB HIS B 164 11525 12664 8842 -3047 658 -3009 C ATOM 1298 CG HIS A 164 33.155 41.709 26.930 1.00 98.83 C ANISOU 1298 CG HIS B 164 13596 13511 10445 -4228 -13 -3227 C ATOM 1299 ND1 HIS A 164 31.995 41.953 26.218 1.00104.21 N ANISOU 1299 ND1 HIS B 164 14138 14089 11368 -5006 -781 -2512 N ATOM 1300 CD2 HIS A 164 32.791 41.647 28.240 1.00102.90 C ANISOU 1300 CD2 HIS B 164 14181 14168 10747 -4985 -1232 -3005 C ATOM 1301 CE1 HIS A 164 30.971 42.034 27.060 1.00107.01 C ANISOU 1301 CE1 HIS B 164 14524 14378 11757 -5151 -1430 -2348 C ATOM 1302 NE2 HIS A 164 31.427 41.852 28.295 1.00106.55 N ANISOU 1302 NE2 HIS B 164 14544 14352 11590 -5250 -1668 -2462 N ATOM 1303 N ASP A 165 36.732 43.568 25.940 1.00 72.18 N ANISOU 1303 N ASP B 165 9561 12182 5684 -2138 1484 -1623 N ATOM 1304 CA ASP A 165 37.530 44.741 26.291 1.00 77.60 C ANISOU 1304 CA ASP B 165 11006 12333 6146 -1786 1999 -1092 C ATOM 1305 C ASP A 165 37.497 45.800 25.201 1.00 74.61 C ANISOU 1305 C ASP B 165 9901 12590 5858 -1162 1374 -630 C ATOM 1306 O ASP A 165 37.558 47.008 25.452 1.00 76.73 O ANISOU 1306 O ASP B 165 10896 11798 6461 -813 831 -553 O ATOM 1307 CB ASP A 165 38.967 44.292 26.559 1.00 85.81 C ANISOU 1307 CB ASP B 165 12889 12470 7243 -2487 3699 -1308 C ATOM 1308 CG ASP A 165 38.999 43.253 27.670 1.00 94.21 C ANISOU 1308 CG ASP B 165 14915 12585 8295 -2725 5300 -1274 C ATOM 1309 OD1 ASP A 165 38.035 42.459 27.749 1.00108.17 O ANISOU 1309 OD1 ASP B 165 16354 12710 12037 -2263 7768 -1380 O ATOM 1310 OD2 ASP A 165 39.971 43.248 28.455 1.00 97.35 O ANISOU 1310 OD2 ASP B 165 17132 13617 6241 -2539 4483 -704 O ATOM 1311 N THR A 166 37.401 45.364 23.941 1.00 74.67 N ANISOU 1311 N THR B 166 9546 12954 5873 -1010 1398 -554 N ATOM 1312 CA THR A 166 37.380 46.363 22.873 1.00 68.60 C ANISOU 1312 CA THR B 166 7758 12833 5476 -437 336 -156 C ATOM 1313 C THR A 166 35.981 46.926 22.653 1.00 68.94 C ANISOU 1313 C THR B 166 7970 12883 5341 -542 -156 716 C ATOM 1314 O THR A 166 35.856 48.128 22.416 1.00 68.20 O ANISOU 1314 O THR B 166 7559 12731 5624 -692 -530 1061 O ATOM 1315 CB THR A 166 37.886 45.830 21.516 1.00 72.37 C ANISOU 1315 CB THR B 166 9155 12702 5639 -1043 -61 -362 C ATOM 1316 OG1 THR A 166 39.183 45.236 21.665 1.00 75.94 O ANISOU 1316 OG1 THR B 166 8668 12928 7257 -920 327 -1882 O ATOM 1317 CG2 THR A 166 38.009 47.002 20.546 1.00 74.00 C ANISOU 1317 CG2 THR B 166 9650 13247 5218 -1212 624 39 C ATOM 1318 N ARG A 167 34.952 46.084 22.713 1.00 69.78 N ANISOU 1318 N ARG B 167 8682 12889 4941 -548 562 511 N ATOM 1319 CA ARG A 167 33.611 46.643 22.538 1.00 71.95 C ANISOU 1319 CA ARG B 167 8780 12745 5814 -629 917 -407 C ATOM 1320 C ARG A 167 33.367 47.606 23.705 1.00 74.23 C ANISOU 1320 C ARG B 167 8941 13769 5493 -1343 846 -439 C ATOM 1321 O ARG A 167 32.959 48.756 23.554 1.00 78.16 O ANISOU 1321 O ARG B 167 8228 14833 6636 -2496 226 -189 O ATOM 1322 CB ARG A 167 32.511 45.599 22.493 1.00 77.63 C ANISOU 1322 CB ARG B 167 9638 12639 7221 -665 1124 -961 C ATOM 1323 CG ARG A 167 32.843 44.207 22.027 1.00 81.73 C ANISOU 1323 CG ARG B 167 10758 12178 8116 -257 -90 -165 C ATOM 1324 CD ARG A 167 32.537 43.964 20.563 1.00 87.05 C ANISOU 1324 CD ARG B 167 12778 11970 8326 -590 -56 301 C ATOM 1325 NE ARG A 167 31.722 42.806 20.251 1.00 92.77 N ANISOU 1325 NE ARG B 167 14409 11696 9144 -662 -296 517 N ATOM 1326 CZ ARG A 167 31.989 41.678 19.622 1.00 95.37 C ANISOU 1326 CZ ARG B 167 15380 11275 9580 -374 -904 1145 C ATOM 1327 NH1 ARG A 167 33.179 41.379 19.121 1.00 94.39 N ANISOU 1327 NH1 ARG B 167 15117 11435 9312 -231 -1424 1589 N ATOM 1328 NH2 ARG A 167 31.040 40.753 19.464 1.00110.50 N ANISOU 1328 NH2 ARG B 167 19973 11216 10798 -1808 -3257 4175 N ATOM 1329 N VAL A 168 33.660 47.059 24.878 1.00 80.95 N ANISOU 1329 N VAL B 168 10812 14447 5497 -2185 1339 -777 N ATOM 1330 CA VAL A 168 33.594 47.799 26.118 1.00 84.04 C ANISOU 1330 CA VAL B 168 12024 14446 5461 -2415 1114 -475 C ATOM 1331 C VAL A 168 34.284 49.146 25.982 1.00 84.40 C ANISOU 1331 C VAL B 168 12875 13943 5251 -2397 603 -261 C ATOM 1332 O VAL A 168 33.640 50.174 26.164 1.00 89.82 O ANISOU 1332 O VAL B 168 12314 15343 6472 -1740 2248 -1764 O ATOM 1333 CB VAL A 168 34.264 47.024 27.269 1.00 88.21 C ANISOU 1333 CB VAL B 168 13524 14378 5615 -3379 1719 -807 C ATOM 1334 CG1 VAL A 168 34.783 48.000 28.315 1.00 86.04 C ANISOU 1334 CG1 VAL B 168 14085 12505 6102 -3940 1902 -833 C ATOM 1335 CG2 VAL A 168 33.278 46.026 27.856 1.00 86.16 C ANISOU 1335 CG2 VAL B 168 11934 14947 5855 -1949 1013 -643 C ATOM 1336 N ALA A 169 35.566 49.141 25.658 1.00 91.57 N ANISOU 1336 N ALA B 169 15364 13755 5673 -3339 -113 804 N ATOM 1337 CA ALA A 169 36.301 50.395 25.512 1.00 95.17 C ANISOU 1337 CA ALA B 169 16049 13584 6528 -3524 1372 390 C ATOM 1338 C ALA A 169 35.893 51.216 24.292 1.00102.07 C ANISOU 1338 C ALA B 169 17256 14134 7393 -4115 2423 545 C ATOM 1339 O ALA A 169 36.459 52.277 23.991 1.00106.85 O ANISOU 1339 O ALA B 169 19119 13265 8212 -5055 4172 -586 O ATOM 1340 CB ALA A 169 37.791 50.068 25.478 1.00103.83 C ANISOU 1340 CB ALA B 169 17666 14087 7697 -4586 2652 87 C ATOM 1341 N ASN A 170 34.887 50.763 23.534 1.00106.51 N ANISOU 1341 N ASN B 170 18134 14836 7500 -4499 2029 1062 N ATOM 1342 CA ASN A 170 34.467 51.577 22.387 1.00109.84 C ANISOU 1342 CA ASN B 170 18334 15718 7681 -5454 2226 978 C ATOM 1343 C ASN A 170 32.972 51.875 22.468 1.00112.59 C ANISOU 1343 C ASN B 170 18483 15901 8396 -5599 1805 941 C ATOM 1344 O ASN A 170 32.447 52.725 21.725 1.00116.92 O ANISOU 1344 O ASN B 170 21676 16275 6474 -7495 3171 1897 O ATOM 1345 CB ASN A 170 34.835 50.900 21.067 1.00107.00 C ANISOU 1345 CB ASN B 170 17223 15854 7580 -4994 2601 690 C ATOM 1346 CG ASN A 170 36.266 51.120 20.616 1.00104.44 C ANISOU 1346 CG ASN B 170 16237 15763 7682 -4573 2828 452 C ATOM 1347 OD1 ASN A 170 37.019 51.916 21.169 1.00109.05 O ANISOU 1347 OD1 ASN B 170 16961 15826 8648 -4927 1518 639 O ATOM 1348 ND2 ASN A 170 36.695 50.396 19.577 1.00 90.72 N ANISOU 1348 ND2 ASN B 170 11283 14971 8214 -2336 4491 -806 N ATOM 1349 N SER A 171 32.257 51.213 23.375 1.00110.23 N ANISOU 1349 N SER B 171 17178 15892 8812 -4576 354 679 N ATOM 1350 CA SER A 171 30.815 51.418 23.526 1.00111.31 C ANISOU 1350 CA SER B 171 17038 15580 9674 -4280 -170 887 C ATOM 1351 C SER A 171 30.433 52.887 23.690 1.00111.01 C ANISOU 1351 C SER B 171 17047 15238 9894 -4199 -5 780 C ATOM 1352 O SER A 171 29.297 53.249 23.354 1.00115.28 O ANISOU 1352 O SER B 171 17036 16296 10469 -5295 -2437 1977 O ATOM 1353 CB SER A 171 30.273 50.612 24.715 1.00111.07 C ANISOU 1353 CB SER B 171 16913 15240 10048 -3695 -673 693 C ATOM 1354 OG SER A 171 31.300 49.929 25.421 1.00113.97 O ANISOU 1354 OG SER B 171 18978 14524 9800 -4234 653 538 O ATOM 1355 N ARG A 172 31.343 53.712 24.190 1.00110.85 N ANISOU 1355 N ARG B 172 17451 14821 9847 -3968 200 169 N ATOM 1356 CA ARG A 172 31.227 55.144 24.405 1.00111.98 C ANISOU 1356 CA ARG B 172 17665 14906 9976 -4058 -794 10 C ATOM 1357 C ARG A 172 30.888 55.869 23.110 1.00111.03 C ANISOU 1357 C ARG B 172 16172 15559 10454 -3932 -939 -262 C ATOM 1358 O ARG A 172 30.047 56.763 23.006 1.00112.06 O ANISOU 1358 O ARG B 172 16730 16836 9010 -5744 -1975 -11 O ATOM 1359 CB ARG A 172 32.513 55.719 25.003 1.00116.98 C ANISOU 1359 CB ARG B 172 19431 14785 10230 -3822 -1089 65 C ATOM 1360 CG ARG A 172 33.732 55.748 24.102 1.00128.53 C ANISOU 1360 CG ARG B 172 22686 15019 11132 -4938 -1604 -14 C ATOM 1361 CD ARG A 172 34.266 57.153 23.874 1.00133.23 C ANISOU 1361 CD ARG B 172 24043 14646 11932 -4849 -1006 -529 C ATOM 1362 NE ARG A 172 35.702 57.259 24.099 1.00140.27 N ANISOU 1362 NE ARG B 172 25830 14832 12636 -5439 -672 -487 N ATOM 1363 CZ ARG A 172 36.449 58.360 24.135 1.00142.46 C ANISOU 1363 CZ ARG B 172 26138 14766 13223 -5418 -605 -69 C ATOM 1364 NH1 ARG A 172 35.914 59.576 23.953 1.00146.19 N ANISOU 1364 NH1 ARG B 172 26094 15488 13962 -4749 -833 543 N ATOM 1365 NH2 ARG A 172 37.762 58.280 24.354 1.00148.11 N ANISOU 1365 NH2 ARG B 172 27294 15026 13955 -5942 -745 288 N ATOM 1366 N PHE A 173 31.585 55.455 22.045 1.00 99.08 N ANISOU 1366 N PHE B 173 12166 15154 10327 -1652 -98 -625 N ATOM 1367 CA PHE A 173 31.181 56.040 20.772 1.00 95.56 C ANISOU 1367 CA PHE B 173 11181 14684 10441 -1264 -294 -16 C ATOM 1368 C PHE A 173 29.815 55.507 20.411 1.00 93.43 C ANISOU 1368 C PHE B 173 10204 14403 10892 -1050 -663 -317 C ATOM 1369 O PHE A 173 28.977 56.237 19.877 1.00 90.44 O ANISOU 1369 O PHE B 173 8772 14217 11373 -1673 -2556 -482 O ATOM 1370 CB PHE A 173 32.225 55.720 19.707 1.00 90.93 C ANISOU 1370 CB PHE B 173 10884 13929 9734 -1337 138 461 C ATOM 1371 CG PHE A 173 33.611 56.079 20.235 1.00 92.38 C ANISOU 1371 CG PHE B 173 11175 14171 9755 -1241 -225 1018 C ATOM 1372 CD1 PHE A 173 34.140 57.339 20.036 1.00 91.14 C ANISOU 1372 CD1 PHE B 173 11094 14284 9251 -1076 -347 1420 C ATOM 1373 CD2 PHE A 173 34.345 55.134 20.923 1.00 91.66 C ANISOU 1373 CD2 PHE B 173 10907 13980 9941 -1040 -423 1644 C ATOM 1374 CE1 PHE A 173 35.396 57.655 20.518 1.00 91.11 C ANISOU 1374 CE1 PHE B 173 11004 14444 9172 -992 -551 1730 C ATOM 1375 CE2 PHE A 173 35.604 55.445 21.406 1.00 91.80 C ANISOU 1375 CE2 PHE B 173 10541 14096 10243 -794 -985 2187 C ATOM 1376 CZ PHE A 173 36.131 56.705 21.202 1.00 90.64 C ANISOU 1376 CZ PHE B 173 10223 14319 9898 -703 -1053 2344 C ATOM 1377 N PHE A 174 29.512 54.240 20.698 1.00 98.63 N ANISOU 1377 N PHE B 174 10789 14856 11831 -833 -369 -1379 N ATOM 1378 CA PHE A 174 28.146 53.817 20.311 1.00102.64 C ANISOU 1378 CA PHE B 174 12059 14291 12650 -629 -398 -2078 C ATOM 1379 C PHE A 174 27.199 54.210 21.438 1.00108.34 C ANISOU 1379 C PHE B 174 12786 14844 13533 -651 -1222 -2243 C ATOM 1380 O PHE A 174 26.653 53.373 22.143 1.00113.25 O ANISOU 1380 O PHE B 174 14713 14498 13819 212 -2451 -2631 O ATOM 1381 CB PHE A 174 28.125 52.338 19.948 1.00100.89 C ANISOU 1381 CB PHE B 174 12146 13993 12196 -438 -292 -2674 C ATOM 1382 CG PHE A 174 28.553 52.078 18.499 1.00101.23 C ANISOU 1382 CG PHE B 174 11869 14360 12232 -610 -257 -2760 C ATOM 1383 CD1 PHE A 174 29.877 52.238 18.126 1.00101.15 C ANISOU 1383 CD1 PHE B 174 11722 14554 12156 -813 146 -2915 C ATOM 1384 CD2 PHE A 174 27.627 51.694 17.541 1.00 99.50 C ANISOU 1384 CD2 PHE B 174 11610 14369 11828 -479 172 -2977 C ATOM 1385 CE1 PHE A 174 30.272 52.009 16.822 1.00100.80 C ANISOU 1385 CE1 PHE B 174 11514 14644 12141 -931 174 -2836 C ATOM 1386 CE2 PHE A 174 28.006 51.471 16.232 1.00 98.42 C ANISOU 1386 CE2 PHE B 174 11506 14380 11508 -655 925 -3316 C ATOM 1387 CZ PHE A 174 29.326 51.651 15.874 1.00100.40 C ANISOU 1387 CZ PHE B 174 11676 14579 11892 -1087 596 -3021 C ATOM 1388 N ASP A 175 27.043 55.515 21.539 1.00112.09 N ANISOU 1388 N ASP B 175 12995 15173 14422 -436 -1786 -1485 N ATOM 1389 CA ASP A 175 26.856 56.405 22.652 1.00115.08 C ANISOU 1389 CA ASP B 175 13761 15399 14564 -948 -2093 -893 C ATOM 1390 C ASP A 175 26.703 55.531 23.915 1.00115.71 C ANISOU 1390 C ASP B 175 14276 15528 14161 -1845 -1488 -256 C ATOM 1391 O ASP A 175 25.615 55.197 24.353 1.00101.68 O ANISOU 1391 O ASP B 175 8131 15542 14961 -499 -1721 -833 O ATOM 1392 CB ASP A 175 25.711 57.413 22.556 1.00113.42 C ANISOU 1392 CB ASP B 175 13335 15222 14536 -254 -2220 -790 C ATOM 1393 CG ASP A 175 26.160 58.832 22.919 1.00114.59 C ANISOU 1393 CG ASP B 175 14314 14779 14446 34 -1892 -751 C ATOM 1394 OD1 ASP A 175 27.369 59.030 23.212 1.00117.13 O ANISOU 1394 OD1 ASP B 175 16380 14695 13429 52 333 -1017 O ATOM 1395 OD2 ASP A 175 25.325 59.767 22.927 1.00114.39 O ANISOU 1395 OD2 ASP B 175 13894 14998 14569 1145 -918 -1667 O ATOM 1396 N ASN A 176 27.907 55.227 24.383 1.00121.11 N ANISOU 1396 N ASN B 176 16259 15316 14442 -2523 -1645 359 N ATOM 1397 CA ASN A 176 28.229 54.574 25.641 1.00119.04 C ANISOU 1397 CA ASN B 176 16189 14492 14550 -2736 -1505 839 C ATOM 1398 C ASN A 176 27.352 53.354 25.886 1.00119.68 C ANISOU 1398 C ASN B 176 16495 14491 14488 -2749 -1624 469 C ATOM 1399 O ASN A 176 26.986 53.024 27.011 1.00124.72 O ANISOU 1399 O ASN B 176 17735 14741 14911 -3286 -2318 -305 O ATOM 1400 CB ASN A 176 28.110 55.639 26.744 1.00122.57 C ANISOU 1400 CB ASN B 176 17638 13976 14957 -3487 -2272 1753 C ATOM 1401 CG ASN A 176 28.512 57.016 26.223 1.00119.83 C ANISOU 1401 CG ASN B 176 17236 13557 14738 -3318 -2834 2375 C ATOM 1402 OD1 ASN A 176 27.664 57.863 25.937 1.00112.39 O ANISOU 1402 OD1 ASN B 176 17127 13114 12463 -3026 -3341 3384 O ATOM 1403 ND2 ASN A 176 29.810 57.251 26.070 1.00118.58 N ANISOU 1403 ND2 ASN B 176 15982 13336 15738 -2785 -4764 2945 N ATOM 1404 N ASP A 177 27.037 52.685 24.787 1.00121.16 N ANISOU 1404 N ASP B 177 16699 14395 14941 -2643 -2025 583 N ATOM 1405 CA ASP A 177 26.070 51.602 24.703 1.00120.08 C ANISOU 1405 CA ASP B 177 16473 14274 14877 -2799 -2648 -20 C ATOM 1406 C ASP A 177 26.706 50.361 24.090 1.00116.88 C ANISOU 1406 C ASP B 177 16061 14590 13758 -2498 -1936 -826 C ATOM 1407 O ASP A 177 26.723 50.192 22.868 1.00116.90 O ANISOU 1407 O ASP B 177 15584 15979 12852 -4161 -1973 -6623 O ATOM 1408 CB ASP A 177 24.877 52.126 23.907 1.00123.47 C ANISOU 1408 CB ASP B 177 16783 14388 15742 -4064 -3476 197 C ATOM 1409 CG ASP A 177 23.945 51.073 23.336 1.00128.08 C ANISOU 1409 CG ASP B 177 17759 14285 16618 -4454 -4378 444 C ATOM 1410 OD1 ASP A 177 23.881 49.968 23.923 1.00128.91 O ANISOU 1410 OD1 ASP B 177 17629 14208 17141 -3845 -5296 -103 O ATOM 1411 OD2 ASP A 177 23.274 51.356 22.308 1.00134.42 O ANISOU 1411 OD2 ASP B 177 18686 14781 17606 -5619 -4369 1175 O ATOM 1412 N VAL A 178 27.234 49.496 24.952 1.00118.66 N ANISOU 1412 N VAL B 178 16676 14823 13586 -3116 -1669 -593 N ATOM 1413 CA VAL A 178 27.884 48.247 24.606 1.00114.96 C ANISOU 1413 CA VAL B 178 16440 14173 13065 -2790 -1097 -961 C ATOM 1414 C VAL A 178 26.882 47.160 24.211 1.00114.77 C ANISOU 1414 C VAL B 178 16742 13959 12908 -3083 -1201 -979 C ATOM 1415 O VAL A 178 26.767 46.144 24.901 1.00114.89 O ANISOU 1415 O VAL B 178 16482 13515 13656 -3279 -892 -779 O ATOM 1416 CB VAL A 178 28.726 47.715 25.788 1.00114.12 C ANISOU 1416 CB VAL B 178 16879 14133 12349 -2691 -1395 -955 C ATOM 1417 CG1 VAL A 178 30.144 47.378 25.360 1.00100.42 C ANISOU 1417 CG1 VAL B 178 16419 12787 8949 -1649 -3 -1912 C ATOM 1418 CG2 VAL A 178 28.728 48.741 26.927 1.00108.95 C ANISOU 1418 CG2 VAL B 178 14263 13668 13463 -2327 -635 -648 C ATOM 1419 N ASN A 179 26.169 47.372 23.114 1.00116.58 N ANISOU 1419 N ASN B 179 17945 13795 12556 -3598 -1127 -1455 N ATOM 1420 CA ASN A 179 25.196 46.445 22.556 1.00116.97 C ANISOU 1420 CA ASN B 179 19049 13285 12108 -3906 -966 -1844 C ATOM 1421 C ASN A 179 25.004 46.726 21.061 1.00115.42 C ANISOU 1421 C ASN B 179 18661 12859 12334 -4366 -546 -1960 C ATOM 1422 O ASN A 179 24.489 45.897 20.322 1.00111.17 O ANISOU 1422 O ASN B 179 18670 11973 11594 -4270 -82 -2598 O ATOM 1423 CB ASN A 179 23.837 46.550 23.249 1.00126.19 C ANISOU 1423 CB ASN B 179 20612 14193 13140 -4450 -586 -3101 C ATOM 1424 CG ASN A 179 23.695 45.677 24.480 1.00133.83 C ANISOU 1424 CG ASN B 179 21547 15588 13714 -4664 -1 -3782 C ATOM 1425 OD1 ASN A 179 23.954 44.469 24.449 1.00141.47 O ANISOU 1425 OD1 ASN B 179 22131 16168 15453 -3717 104 -5270 O ATOM 1426 ND2 ASN A 179 23.271 46.281 25.588 1.00140.96 N ANISOU 1426 ND2 ASN B 179 22307 17586 13667 -5567 -254 -4832 N ATOM 1427 N GLN A 180 25.437 47.922 20.695 1.00113.09 N ANISOU 1427 N GLN B 180 18065 12522 12383 -4550 -539 -1364 N ATOM 1428 CA GLN A 180 25.356 48.450 19.345 1.00111.28 C ANISOU 1428 CA GLN B 180 17368 12221 12694 -4603 -233 -1241 C ATOM 1429 C GLN A 180 26.711 48.409 18.637 1.00107.47 C ANISOU 1429 C GLN B 180 16498 11752 12582 -4276 637 -1433 C ATOM 1430 O GLN A 180 26.756 48.268 17.414 1.00110.04 O ANISOU 1430 O GLN B 180 17836 11203 12770 -6924 -34 -201 O ATOM 1431 CB GLN A 180 24.817 49.886 19.373 1.00115.85 C ANISOU 1431 CB GLN B 180 17179 13290 13550 -5064 -396 -286 C ATOM 1432 CG GLN A 180 23.601 50.081 18.473 1.00120.97 C ANISOU 1432 CG GLN B 180 17873 13992 14097 -4886 274 156 C ATOM 1433 CD GLN A 180 23.481 48.981 17.424 1.00126.63 C ANISOU 1433 CD GLN B 180 19208 14437 14468 -4872 -191 735 C ATOM 1434 OE1 GLN A 180 24.054 49.082 16.340 1.00134.88 O ANISOU 1434 OE1 GLN B 180 21173 16732 13344 -5194 390 1458 O ATOM 1435 NE2 GLN A 180 22.747 47.921 17.750 1.00134.37 N ANISOU 1435 NE2 GLN B 180 20493 13494 17068 -4682 -570 1136 N ATOM 1436 N VAL A 181 27.764 48.534 19.438 1.00 91.41 N ANISOU 1436 N VAL B 181 12209 11447 11077 -2514 -691 -1245 N ATOM 1437 CA VAL A 181 29.145 48.340 19.007 1.00 87.48 C ANISOU 1437 CA VAL B 181 12009 11197 10032 -2443 244 -1415 C ATOM 1438 C VAL A 181 29.220 47.123 18.087 1.00 80.41 C ANISOU 1438 C VAL B 181 10823 10634 9095 -1836 1155 -2706 C ATOM 1439 O VAL A 181 28.887 46.034 18.566 1.00 92.19 O ANISOU 1439 O VAL B 181 11677 11840 11511 -1460 997 -4631 O ATOM 1440 CB VAL A 181 30.095 48.133 20.203 1.00 90.28 C ANISOU 1440 CB VAL B 181 12256 11761 10287 -2070 945 -1371 C ATOM 1441 CG1 VAL A 181 31.551 48.319 19.779 1.00 79.58 C ANISOU 1441 CG1 VAL B 181 8542 12793 8903 -2166 3719 -2698 C ATOM 1442 CG2 VAL A 181 29.714 49.057 21.354 1.00 90.23 C ANISOU 1442 CG2 VAL B 181 13190 11625 9469 -2396 839 -1705 C ATOM 1443 N PRO A 182 29.616 47.284 16.838 1.00 78.75 N ANISOU 1443 N PRO B 182 10355 10446 9119 -2988 1354 -2686 N ATOM 1444 CA PRO A 182 29.546 46.181 15.859 1.00 76.52 C ANISOU 1444 CA PRO B 182 10676 9754 8644 -3288 1639 -2374 C ATOM 1445 C PRO A 182 30.258 44.951 16.396 1.00 71.68 C ANISOU 1445 C PRO B 182 10376 9002 7857 -3382 1082 -2873 C ATOM 1446 O PRO A 182 31.183 45.065 17.209 1.00 66.00 O ANISOU 1446 O PRO B 182 9654 8907 6513 -1321 1615 -2978 O ATOM 1447 CB PRO A 182 30.255 46.778 14.642 1.00 75.44 C ANISOU 1447 CB PRO B 182 10308 9585 8770 -2867 1719 -2322 C ATOM 1448 CG PRO A 182 30.050 48.253 14.774 1.00 76.20 C ANISOU 1448 CG PRO B 182 10118 9995 8838 -3110 1344 -2279 C ATOM 1449 CD PRO A 182 30.184 48.505 16.256 1.00 76.74 C ANISOU 1449 CD PRO B 182 10206 10234 8719 -3262 1277 -2719 C ATOM 1450 N LYS A 183 29.843 43.746 16.021 1.00 66.25 N ANISOU 1450 N LYS B 183 10340 8136 6695 -4050 1488 -2470 N ATOM 1451 CA LYS A 183 30.480 42.601 16.668 1.00 67.52 C ANISOU 1451 CA LYS B 183 10571 8502 6581 -3366 1692 -1915 C ATOM 1452 C LYS A 183 31.816 42.287 16.007 1.00 61.25 C ANISOU 1452 C LYS B 183 9080 8020 6172 -2590 2056 -1793 C ATOM 1453 O LYS A 183 32.699 41.703 16.630 1.00 62.32 O ANISOU 1453 O LYS B 183 8010 8614 7056 -1762 3204 -3628 O ATOM 1454 CB LYS A 183 29.576 41.373 16.621 1.00 75.36 C ANISOU 1454 CB LYS B 183 12471 8389 7774 -2993 2715 -2713 C ATOM 1455 CG LYS A 183 28.627 41.318 17.819 1.00 84.45 C ANISOU 1455 CG LYS B 183 14227 9329 8531 -2830 1521 -3164 C ATOM 1456 CD LYS A 183 28.492 42.684 18.472 1.00 95.52 C ANISOU 1456 CD LYS B 183 15282 11438 9573 -3046 265 -1703 C ATOM 1457 CE LYS A 183 28.479 42.624 19.991 1.00101.86 C ANISOU 1457 CE LYS B 183 16632 12453 9618 -3588 396 -1398 C ATOM 1458 NZ LYS A 183 28.798 43.955 20.593 1.00102.56 N ANISOU 1458 NZ LYS B 183 16349 13890 8727 -3036 990 -1168 N ATOM 1459 N TYR A 184 31.930 42.687 14.746 1.00 51.83 N ANISOU 1459 N TYR B 184 7385 6107 6202 -1451 1991 -1376 N ATOM 1460 CA TYR A 184 33.076 42.307 13.945 1.00 55.27 C ANISOU 1460 CA TYR B 184 8249 6086 6665 -1439 1539 -1697 C ATOM 1461 C TYR A 184 33.729 43.514 13.276 1.00 50.14 C ANISOU 1461 C TYR B 184 7486 5664 5900 -936 511 -893 C ATOM 1462 O TYR A 184 33.131 44.581 13.125 1.00 48.87 O ANISOU 1462 O TYR B 184 7286 5065 6217 -912 -386 -628 O ATOM 1463 CB TYR A 184 32.687 41.333 12.838 1.00 53.58 C ANISOU 1463 CB TYR B 184 6222 6312 7825 -223 1467 -2105 C ATOM 1464 CG TYR A 184 31.944 40.096 13.261 1.00 65.46 C ANISOU 1464 CG TYR B 184 7173 6790 10910 -60 1811 -3275 C ATOM 1465 CD1 TYR A 184 32.531 38.839 13.178 1.00 67.60 C ANISOU 1465 CD1 TYR B 184 6973 7049 11662 58 3033 -3556 C ATOM 1466 CD2 TYR A 184 30.637 40.180 13.732 1.00 73.31 C ANISOU 1466 CD2 TYR B 184 8066 7074 12715 -474 2087 -4017 C ATOM 1467 CE1 TYR A 184 31.844 37.701 13.563 1.00 72.07 C ANISOU 1467 CE1 TYR B 184 7801 7118 12467 126 3804 -3699 C ATOM 1468 CE2 TYR A 184 29.939 39.056 14.125 1.00 77.62 C ANISOU 1468 CE2 TYR B 184 8961 6918 13614 -526 2886 -4002 C ATOM 1469 CZ TYR A 184 30.550 37.823 14.035 1.00 77.23 C ANISOU 1469 CZ TYR B 184 8779 7214 13351 -254 4043 -4133 C ATOM 1470 OH TYR A 184 29.842 36.708 14.422 1.00 81.19 O ANISOU 1470 OH TYR B 184 9978 6232 14639 -89 4148 -3058 O ATOM 1471 N ALA A 185 34.980 43.300 12.865 1.00 44.28 N ANISOU 1471 N ALA B 185 6583 5134 5106 -446 559 -397 N ATOM 1472 CA ALA A 185 35.721 44.340 12.164 1.00 41.54 C ANISOU 1472 CA ALA B 185 6004 5031 4749 -416 508 -104 C ATOM 1473 C ALA A 185 36.612 43.712 11.101 1.00 39.24 C ANISOU 1473 C ALA B 185 5740 4871 4300 -717 912 133 C ATOM 1474 O ALA A 185 36.952 42.543 11.257 1.00 40.15 O ANISOU 1474 O ALA B 185 5793 5070 4394 -630 878 -475 O ATOM 1475 CB ALA A 185 36.579 45.155 13.115 1.00 40.34 C ANISOU 1475 CB ALA B 185 5188 5388 4751 -438 771 151 C ATOM 1476 N LEU A 186 36.942 44.515 10.106 1.00 37.19 N ANISOU 1476 N LEU B 186 5393 4789 3950 -862 1160 535 N ATOM 1477 CA LEU A 186 37.961 44.124 9.130 1.00 35.06 C ANISOU 1477 CA LEU B 186 4702 4519 4100 -214 1223 282 C ATOM 1478 C LEU A 186 39.282 44.753 9.579 1.00 33.86 C ANISOU 1478 C LEU B 186 4382 4655 3830 -287 401 524 C ATOM 1479 O LEU A 186 39.241 45.924 9.978 1.00 34.53 O ANISOU 1479 O LEU B 186 4199 5283 3639 -774 52 1064 O ATOM 1480 CB LEU A 186 37.618 44.575 7.720 1.00 36.12 C ANISOU 1480 CB LEU B 186 4452 5494 3779 94 711 865 C ATOM 1481 CG LEU A 186 36.912 43.556 6.830 1.00 39.23 C ANISOU 1481 CG LEU B 186 6353 4183 4371 259 794 461 C ATOM 1482 CD1 LEU A 186 36.061 42.636 7.673 1.00 42.75 C ANISOU 1482 CD1 LEU B 186 9437 3566 3240 -1441 -472 -47 C ATOM 1483 CD2 LEU A 186 36.102 44.246 5.729 1.00 40.18 C ANISOU 1483 CD2 LEU B 186 6145 4354 4767 -1365 226 1002 C ATOM 1484 N THR A 187 40.393 44.024 9.530 1.00 30.92 N ANISOU 1484 N THR B 187 4133 4155 3461 94 150 309 N ATOM 1485 CA THR A 187 41.659 44.631 9.950 1.00 32.43 C ANISOU 1485 CA THR B 187 4606 4346 3371 -190 -100 590 C ATOM 1486 C THR A 187 42.818 44.183 9.095 1.00 30.01 C ANISOU 1486 C THR B 187 4081 4157 3164 -36 197 666 C ATOM 1487 O THR A 187 42.891 43.016 8.683 1.00 30.48 O ANISOU 1487 O THR B 187 3846 4335 3400 -14 462 717 O ATOM 1488 CB THR A 187 41.939 44.258 11.421 1.00 33.44 C ANISOU 1488 CB THR B 187 4926 4319 3459 -409 73 284 C ATOM 1489 OG1 THR A 187 43.159 44.849 11.896 1.00 37.26 O ANISOU 1489 OG1 THR B 187 6156 4383 3620 301 1094 527 O ATOM 1490 CG2 THR A 187 42.095 42.738 11.585 1.00 33.76 C ANISOU 1490 CG2 THR B 187 5268 4475 3086 12 -123 -62 C ATOM 1491 N VAL A 188 43.772 45.058 8.801 1.00 28.57 N ANISOU 1491 N VAL B 188 3740 4203 2911 -94 603 608 N ATOM 1492 CA VAL A 188 44.979 44.533 8.164 1.00 29.31 C ANISOU 1492 CA VAL B 188 3735 4253 3147 34 387 510 C ATOM 1493 C VAL A 188 45.677 43.547 9.090 1.00 30.26 C ANISOU 1493 C VAL B 188 3591 4490 3416 -170 473 -521 C ATOM 1494 O VAL A 188 45.481 43.548 10.320 1.00 29.19 O ANISOU 1494 O VAL B 188 3485 4361 3245 -525 366 186 O ATOM 1495 CB VAL A 188 45.966 45.664 7.822 1.00 29.17 C ANISOU 1495 CB VAL B 188 4038 4367 2679 -104 1059 342 C ATOM 1496 CG1 VAL A 188 45.324 46.632 6.831 1.00 31.08 C ANISOU 1496 CG1 VAL B 188 3683 4932 3194 -158 1065 776 C ATOM 1497 CG2 VAL A 188 46.408 46.389 9.090 1.00 28.12 C ANISOU 1497 CG2 VAL B 188 3455 4019 3209 -169 1025 629 C ATOM 1498 N GLY A 189 46.510 42.693 8.499 1.00 28.38 N ANISOU 1498 N GLY B 189 3717 3841 3224 -117 155 384 N ATOM 1499 CA GLY A 189 47.234 41.722 9.300 1.00 28.02 C ANISOU 1499 CA GLY B 189 3469 4112 3066 46 -121 769 C ATOM 1500 C GLY A 189 48.582 42.197 9.801 1.00 27.71 C ANISOU 1500 C GLY B 189 3463 3891 3172 18 212 417 C ATOM 1501 O GLY A 189 49.037 43.289 9.425 1.00 27.45 O ANISOU 1501 O GLY B 189 3160 3989 3282 -145 31 50 O ATOM 1502 N VAL A 190 49.223 41.383 10.637 1.00 26.82 N ANISOU 1502 N VAL B 190 3465 3926 2798 112 107 420 N ATOM 1503 CA VAL A 190 50.540 41.783 11.142 1.00 26.93 C ANISOU 1503 CA VAL B 190 3389 4048 2796 131 90 577 C ATOM 1504 C VAL A 190 51.555 41.790 10.013 1.00 28.09 C ANISOU 1504 C VAL B 190 3785 3971 2918 -213 119 637 C ATOM 1505 O VAL A 190 52.438 42.643 9.936 1.00 30.94 O ANISOU 1505 O VAL B 190 4716 3911 3129 -189 60 682 O ATOM 1506 CB VAL A 190 51.015 40.865 12.284 1.00 26.99 C ANISOU 1506 CB VAL B 190 3112 3553 3590 -134 386 136 C ATOM 1507 CG1 VAL A 190 52.399 41.280 12.789 1.00 25.38 C ANISOU 1507 CG1 VAL B 190 2744 3342 3558 112 575 -44 C ATOM 1508 CG2 VAL A 190 50.020 40.859 13.444 1.00 27.32 C ANISOU 1508 CG2 VAL B 190 4403 2881 3095 133 365 484 C ATOM 1509 N GLY A 191 51.445 40.832 9.099 1.00 28.27 N ANISOU 1509 N GLY B 191 3208 4106 3427 -304 -227 355 N ATOM 1510 CA GLY A 191 52.281 40.736 7.904 1.00 28.37 C ANISOU 1510 CA GLY B 191 3342 3994 3444 -476 -138 303 C ATOM 1511 C GLY A 191 52.072 41.960 7.028 1.00 28.92 C ANISOU 1511 C GLY B 191 3516 4195 3278 -472 -45 463 C ATOM 1512 O GLY A 191 53.007 42.529 6.459 1.00 30.95 O ANISOU 1512 O GLY B 191 3779 4123 3859 -480 519 391 O ATOM 1513 N THR A 192 50.812 42.384 6.917 1.00 29.18 N ANISOU 1513 N THR B 192 3439 4502 3147 -591 -134 402 N ATOM 1514 CA THR A 192 50.502 43.597 6.161 1.00 29.81 C ANISOU 1514 CA THR B 192 3857 4395 3073 -556 226 626 C ATOM 1515 C THR A 192 51.297 44.779 6.706 1.00 29.87 C ANISOU 1515 C THR B 192 4123 4135 3090 -435 71 136 C ATOM 1516 O THR A 192 51.907 45.573 5.992 1.00 30.88 O ANISOU 1516 O THR B 192 3359 4959 3417 -200 564 -87 O ATOM 1517 CB THR A 192 49.004 43.933 6.261 1.00 30.46 C ANISOU 1517 CB THR B 192 3949 4135 3491 -437 1053 19 C ATOM 1518 OG1 THR A 192 48.244 42.722 6.176 1.00 30.94 O ANISOU 1518 OG1 THR B 192 4233 4289 3235 -315 469 522 O ATOM 1519 CG2 THR A 192 48.569 44.829 5.106 1.00 28.56 C ANISOU 1519 CG2 THR B 192 3804 4881 2167 -406 239 587 C ATOM 1520 N LEU A 193 51.285 44.903 8.041 1.00 29.30 N ANISOU 1520 N LEU B 193 3907 4130 3097 -445 -282 243 N ATOM 1521 CA LEU A 193 52.026 46.002 8.666 1.00 28.61 C ANISOU 1521 CA LEU B 193 3432 4212 3224 9 467 216 C ATOM 1522 C LEU A 193 53.519 45.808 8.467 1.00 28.75 C ANISOU 1522 C LEU B 193 3528 4125 3272 31 128 531 C ATOM 1523 O LEU A 193 54.208 46.766 8.094 1.00 29.30 O ANISOU 1523 O LEU B 193 4126 4214 2793 -10 282 293 O ATOM 1524 CB LEU A 193 51.682 46.030 10.133 1.00 31.34 C ANISOU 1524 CB LEU B 193 4114 4565 3228 132 -171 407 C ATOM 1525 CG LEU A 193 51.917 47.162 11.109 1.00 35.04 C ANISOU 1525 CG LEU B 193 5419 4216 3677 812 52 819 C ATOM 1526 CD1 LEU A 193 53.029 46.801 12.104 1.00 39.91 C ANISOU 1526 CD1 LEU B 193 4504 3781 6878 259 -509 2372 C ATOM 1527 CD2 LEU A 193 52.224 48.497 10.453 1.00 40.58 C ANISOU 1527 CD2 LEU B 193 7843 3165 4409 1560 41 377 C ATOM 1528 N LEU A 194 54.019 44.592 8.726 1.00 28.35 N ANISOU 1528 N LEU B 194 3406 4654 2710 -78 -153 487 N ATOM 1529 CA LEU A 194 55.469 44.401 8.657 1.00 29.18 C ANISOU 1529 CA LEU B 194 3512 4386 3188 42 788 217 C ATOM 1530 C LEU A 194 56.019 44.561 7.255 1.00 27.64 C ANISOU 1530 C LEU B 194 3308 3882 3311 13 459 277 C ATOM 1531 O LEU A 194 57.206 44.845 7.044 1.00 32.48 O ANISOU 1531 O LEU B 194 4441 4208 3691 -751 230 449 O ATOM 1532 CB LEU A 194 55.846 43.011 9.203 1.00 30.39 C ANISOU 1532 CB LEU B 194 3416 4337 3793 268 610 -13 C ATOM 1533 CG LEU A 194 55.722 42.900 10.732 1.00 32.67 C ANISOU 1533 CG LEU B 194 4476 4134 3803 244 1480 184 C ATOM 1534 CD1 LEU A 194 55.989 41.480 11.219 1.00 33.19 C ANISOU 1534 CD1 LEU B 194 3856 4679 4076 -249 1257 200 C ATOM 1535 CD2 LEU A 194 56.652 43.903 11.403 1.00 37.87 C ANISOU 1535 CD2 LEU B 194 5689 4563 4135 478 209 271 C ATOM 1536 N ASP A 195 55.194 44.371 6.238 1.00 30.12 N ANISOU 1536 N ASP B 195 4211 4072 3163 -662 590 131 N ATOM 1537 CA ASP A 195 55.668 44.579 4.882 1.00 29.64 C ANISOU 1537 CA ASP B 195 4302 3758 3203 98 -79 213 C ATOM 1538 C ASP A 195 55.916 46.054 4.589 1.00 29.57 C ANISOU 1538 C ASP B 195 4117 3778 3340 -45 -78 100 C ATOM 1539 O ASP A 195 56.519 46.368 3.549 1.00 32.41 O ANISOU 1539 O ASP B 195 4205 4517 3592 -211 318 -376 O ATOM 1540 CB ASP A 195 54.623 44.088 3.870 1.00 32.84 C ANISOU 1540 CB ASP B 195 4666 4408 3404 87 -719 714 C ATOM 1541 CG ASP A 195 54.606 42.592 3.713 1.00 36.78 C ANISOU 1541 CG ASP B 195 5311 4142 4521 658 -307 529 C ATOM 1542 OD1 ASP A 195 55.544 41.966 4.246 1.00 41.73 O ANISOU 1542 OD1 ASP B 195 4379 5412 6064 -338 -1138 -93 O ATOM 1543 OD2 ASP A 195 53.671 42.086 3.066 1.00 46.56 O ANISOU 1543 OD2 ASP B 195 7158 4576 5955 488 -1854 1342 O ATOM 1544 N ALA A 196 55.466 46.978 5.432 1.00 29.67 N ANISOU 1544 N ALA B 196 3714 4500 3058 -289 263 755 N ATOM 1545 CA ALA A 196 55.754 48.391 5.120 1.00 27.17 C ANISOU 1545 CA ALA B 196 3566 4341 2418 -493 286 664 C ATOM 1546 C ALA A 196 57.246 48.680 5.217 1.00 28.00 C ANISOU 1546 C ALA B 196 3307 4465 2866 -680 569 151 C ATOM 1547 O ALA A 196 57.991 48.000 5.925 1.00 28.87 O ANISOU 1547 O ALA B 196 3380 4911 2678 -817 407 523 O ATOM 1548 CB ALA A 196 55.004 49.301 6.057 1.00 26.85 C ANISOU 1548 CB ALA B 196 3786 3619 2796 -451 4 594 C ATOM 1549 N GLU A 197 57.720 49.682 4.506 1.00 27.17 N ANISOU 1549 N GLU B 197 3167 4506 2651 43 -131 398 N ATOM 1550 CA GLU A 197 59.116 50.065 4.475 1.00 30.24 C ANISOU 1550 CA GLU B 197 3681 4448 3362 63 432 377 C ATOM 1551 C GLU A 197 59.553 50.623 5.821 1.00 30.02 C ANISOU 1551 C GLU B 197 3932 4152 3320 -495 120 257 C ATOM 1552 O GLU A 197 60.680 50.398 6.269 1.00 29.71 O ANISOU 1552 O GLU B 197 3706 5116 2466 -914 330 -139 O ATOM 1553 CB GLU A 197 59.311 51.146 3.410 1.00 40.52 C ANISOU 1553 CB GLU B 197 6248 5074 4074 -980 1874 -674 C ATOM 1554 CG GLU A 197 60.739 51.338 2.949 1.00 60.69 C ANISOU 1554 CG GLU B 197 10960 5871 6230 -2159 2147 -1972 C ATOM 1555 CD GLU A 197 60.846 52.201 1.705 1.00 66.66 C ANISOU 1555 CD GLU B 197 12361 6294 6674 -1720 2370 -2598 C ATOM 1556 OE1 GLU A 197 60.249 51.815 0.668 1.00 68.95 O ANISOU 1556 OE1 GLU B 197 12681 6424 7091 -1696 3962 -2134 O ATOM 1557 OE2 GLU A 197 61.526 53.253 1.783 1.00 72.08 O ANISOU 1557 OE2 GLU B 197 12903 7065 7420 -834 2072 -2632 O ATOM 1558 N GLU A 198 58.674 51.375 6.462 1.00 29.40 N ANISOU 1558 N GLU B 198 4080 4111 2979 -884 400 26 N ATOM 1559 CA GLU A 198 58.932 51.976 7.773 1.00 29.14 C ANISOU 1559 CA GLU B 198 3686 4407 2976 -596 412 4 C ATOM 1560 C GLU A 198 57.648 51.911 8.587 1.00 30.64 C ANISOU 1560 C GLU B 198 3990 4706 2945 -952 421 17 C ATOM 1561 O GLU A 198 56.556 52.103 8.024 1.00 26.56 O ANISOU 1561 O GLU B 198 3260 4014 2819 -140 508 -1 O ATOM 1562 CB GLU A 198 59.425 53.409 7.610 1.00 29.18 C ANISOU 1562 CB GLU B 198 3211 4607 3268 -706 933 303 C ATOM 1563 CG GLU A 198 59.714 54.148 8.918 1.00 32.96 C ANISOU 1563 CG GLU B 198 3877 4954 3691 -308 357 332 C ATOM 1564 CD GLU A 198 60.351 55.498 8.634 1.00 36.62 C ANISOU 1564 CD GLU B 198 5000 4709 4204 -89 1011 746 C ATOM 1565 OE1 GLU A 198 59.927 56.162 7.664 1.00 36.61 O ANISOU 1565 OE1 GLU B 198 5321 4283 4307 -280 1223 248 O ATOM 1566 OE2 GLU A 198 61.282 55.927 9.352 1.00 43.85 O ANISOU 1566 OE2 GLU B 198 7564 4664 4432 -101 1557 743 O ATOM 1567 N VAL A 199 57.766 51.617 9.876 1.00 28.01 N ANISOU 1567 N VAL B 199 3735 3995 2911 -590 355 193 N ATOM 1568 CA VAL A 199 56.617 51.505 10.764 1.00 28.79 C ANISOU 1568 CA VAL B 199 4099 3913 2926 -422 35 243 C ATOM 1569 C VAL A 199 56.807 52.500 11.900 1.00 26.71 C ANISOU 1569 C VAL B 199 3439 3620 3092 -347 251 296 C ATOM 1570 O VAL A 199 57.863 52.454 12.558 1.00 28.14 O ANISOU 1570 O VAL B 199 3635 4215 2844 -635 380 363 O ATOM 1571 CB VAL A 199 56.473 50.090 11.342 1.00 26.90 C ANISOU 1571 CB VAL B 199 3876 3732 2611 -293 -478 289 C ATOM 1572 CG1 VAL A 199 55.338 50.013 12.349 1.00 26.66 C ANISOU 1572 CG1 VAL B 199 4317 4077 1737 -515 -252 492 C ATOM 1573 CG2 VAL A 199 56.221 49.097 10.224 1.00 26.84 C ANISOU 1573 CG2 VAL B 199 3784 4224 2189 -724 -423 415 C ATOM 1574 N MET A 200 55.830 53.365 12.113 1.00 25.82 N ANISOU 1574 N MET B 200 3405 3339 3067 -293 498 -199 N ATOM 1575 CA MET A 200 55.927 54.352 13.193 1.00 26.13 C ANISOU 1575 CA MET B 200 3086 3834 3009 -311 524 -191 C ATOM 1576 C MET A 200 54.744 54.169 14.133 1.00 26.51 C ANISOU 1576 C MET B 200 3359 3860 2853 -621 688 -45 C ATOM 1577 O MET A 200 53.585 54.350 13.731 1.00 26.60 O ANISOU 1577 O MET B 200 3277 3787 3044 -483 920 -67 O ATOM 1578 CB MET A 200 55.982 55.776 12.620 1.00 25.55 C ANISOU 1578 CB MET B 200 3154 3628 2926 -420 893 307 C ATOM 1579 CG MET A 200 55.946 56.888 13.667 1.00 27.01 C ANISOU 1579 CG MET B 200 3214 3595 3455 -318 604 244 C ATOM 1580 SD MET A 200 56.232 58.523 12.964 1.00 28.73 S ANISOU 1580 SD MET B 200 3551 3918 3448 -104 689 149 S ATOM 1581 CE MET A 200 54.722 58.781 12.016 1.00 26.69 C ANISOU 1581 CE MET B 200 2874 4794 2472 -335 27 342 C ATOM 1582 N ILE A 201 55.022 53.791 15.388 1.00 23.46 N ANISOU 1582 N ILE B 201 2655 3502 2756 -211 435 140 N ATOM 1583 CA ILE A 201 53.971 53.513 16.349 1.00 24.79 C ANISOU 1583 CA ILE B 201 3173 3587 2659 -135 141 166 C ATOM 1584 C ILE A 201 53.888 54.658 17.351 1.00 26.52 C ANISOU 1584 C ILE B 201 3302 3637 3138 -120 -129 255 C ATOM 1585 O ILE A 201 54.909 55.038 17.931 1.00 27.81 O ANISOU 1585 O ILE B 201 4090 3835 2643 -342 -290 292 O ATOM 1586 CB ILE A 201 54.230 52.197 17.097 1.00 27.24 C ANISOU 1586 CB ILE B 201 3374 3618 3356 163 152 -363 C ATOM 1587 CG1 ILE A 201 54.454 51.032 16.123 1.00 27.24 C ANISOU 1587 CG1 ILE B 201 3081 3946 3322 -139 251 -186 C ATOM 1588 CG2 ILE A 201 53.108 51.915 18.088 1.00 25.31 C ANISOU 1588 CG2 ILE B 201 3326 3157 3136 -130 215 74 C ATOM 1589 CD1 ILE A 201 53.179 50.710 15.350 1.00 28.28 C ANISOU 1589 CD1 ILE B 201 3584 4313 2850 -494 -85 -87 C ATOM 1590 N LEU A 202 52.687 55.175 17.509 1.00 26.31 N ANISOU 1590 N LEU B 202 3092 3731 3174 -22 64 -128 N ATOM 1591 CA LEU A 202 52.388 56.223 18.459 1.00 26.30 C ANISOU 1591 CA LEU B 202 3483 3728 2784 -398 -43 153 C ATOM 1592 C LEU A 202 52.054 55.572 19.804 1.00 27.46 C ANISOU 1592 C LEU B 202 3413 4048 2970 -16 191 179 C ATOM 1593 O LEU A 202 51.159 54.721 19.863 1.00 28.40 O ANISOU 1593 O LEU B 202 3715 3947 3129 -232 511 123 O ATOM 1594 CB LEU A 202 51.194 57.051 18.019 1.00 27.98 C ANISOU 1594 CB LEU B 202 3026 4205 3402 -8 200 67 C ATOM 1595 CG LEU A 202 51.333 58.253 17.089 1.00 32.57 C ANISOU 1595 CG LEU B 202 4884 4340 3151 -665 1223 -340 C ATOM 1596 CD1 LEU A 202 52.621 58.246 16.302 1.00 29.03 C ANISOU 1596 CD1 LEU B 202 4459 5402 1168 -774 316 322 C ATOM 1597 CD2 LEU A 202 50.125 58.345 16.174 1.00 28.96 C ANISOU 1597 CD2 LEU B 202 4928 4324 1753 -81 81 254 C ATOM 1598 N VAL A 203 52.752 55.997 20.845 1.00 27.08 N ANISOU 1598 N VAL B 203 3379 4070 2841 -319 158 136 N ATOM 1599 CA VAL A 203 52.509 55.399 22.156 1.00 28.32 C ANISOU 1599 CA VAL B 203 3361 4483 2917 -368 193 -54 C ATOM 1600 C VAL A 203 52.172 56.463 23.208 1.00 28.11 C ANISOU 1600 C VAL B 203 3351 4416 2913 -207 204 -341 C ATOM 1601 O VAL A 203 53.074 57.218 23.600 1.00 31.28 O ANISOU 1601 O VAL B 203 4296 4820 2771 -986 -232 601 O ATOM 1602 CB VAL A 203 53.736 54.579 22.598 1.00 31.03 C ANISOU 1602 CB VAL B 203 3660 5547 2583 -1005 156 -265 C ATOM 1603 CG1 VAL A 203 53.389 53.797 23.887 1.00 27.47 C ANISOU 1603 CG1 VAL B 203 3351 4595 2491 -504 -35 175 C ATOM 1604 CG2 VAL A 203 54.257 53.639 21.515 1.00 29.06 C ANISOU 1604 CG2 VAL B 203 3679 5007 2355 -1074 283 118 C ATOM 1605 N LEU A 204 50.907 56.521 23.641 1.00 30.58 N ANISOU 1605 N LEU B 204 3955 4885 2778 -1079 110 214 N ATOM 1606 CA LEU A 204 50.392 57.528 24.546 1.00 30.91 C ANISOU 1606 CA LEU B 204 3857 4859 3028 -978 77 43 C ATOM 1607 C LEU A 204 49.738 56.930 25.781 1.00 29.57 C ANISOU 1607 C LEU B 204 3398 4788 3048 -201 -283 88 C ATOM 1608 O LEU A 204 48.875 56.061 25.675 1.00 31.99 O ANISOU 1608 O LEU B 204 4527 4559 3069 -551 -246 384 O ATOM 1609 CB LEU A 204 49.338 58.395 23.838 1.00 31.23 C ANISOU 1609 CB LEU B 204 3744 4804 3316 -564 188 378 C ATOM 1610 CG LEU A 204 49.812 59.206 22.632 1.00 34.71 C ANISOU 1610 CG LEU B 204 4546 4360 4282 -557 1005 214 C ATOM 1611 CD1 LEU A 204 48.649 59.992 22.045 1.00 33.44 C ANISOU 1611 CD1 LEU B 204 3953 5118 3633 -175 495 933 C ATOM 1612 CD2 LEU A 204 50.975 60.129 23.005 1.00 31.49 C ANISOU 1612 CD2 LEU B 204 4245 4809 2909 -221 105 641 C ATOM 1613 N GLY A 205 50.108 57.396 26.982 1.00 29.39 N ANISOU 1613 N GLY B 205 3684 4477 3005 108 341 145 N ATOM 1614 CA GLY A 205 49.357 56.988 28.163 1.00 29.33 C ANISOU 1614 CA GLY B 205 3309 4893 2943 -186 184 46 C ATOM 1615 C GLY A 205 50.082 55.900 28.931 1.00 29.69 C ANISOU 1615 C GLY B 205 3654 4708 2919 -229 429 95 C ATOM 1616 O GLY A 205 50.732 55.039 28.359 1.00 28.46 O ANISOU 1616 O GLY B 205 3423 4190 3199 -544 655 -51 O ATOM 1617 N SER A 206 49.960 55.980 30.258 1.00 31.83 N ANISOU 1617 N SER B 206 4673 4502 2919 -549 548 -276 N ATOM 1618 CA SER A 206 50.584 54.963 31.102 1.00 29.80 C ANISOU 1618 CA SER B 206 4041 4962 2320 -526 -102 -270 C ATOM 1619 C SER A 206 49.944 53.604 30.872 1.00 31.69 C ANISOU 1619 C SER B 206 4450 4768 2821 -451 78 -368 C ATOM 1620 O SER A 206 50.559 52.587 31.195 1.00 28.29 O ANISOU 1620 O SER B 206 4255 4279 2215 -476 -394 268 O ATOM 1621 CB SER A 206 50.508 55.363 32.585 1.00 33.90 C ANISOU 1621 CB SER B 206 4494 6018 2369 -833 -305 -238 C ATOM 1622 OG SER A 206 49.136 55.352 32.971 1.00 38.87 O ANISOU 1622 OG SER B 206 5664 6409 2695 -1460 -1342 262 O ATOM 1623 N GLN A 207 48.737 53.532 30.310 1.00 30.40 N ANISOU 1623 N GLN B 207 3695 4607 3248 -457 63 -618 N ATOM 1624 CA GLN A 207 48.203 52.205 30.016 1.00 32.40 C ANISOU 1624 CA GLN B 207 4520 4248 3542 -300 14 -920 C ATOM 1625 C GLN A 207 49.009 51.473 28.941 1.00 29.27 C ANISOU 1625 C GLN B 207 4194 3487 3441 -283 30 -247 C ATOM 1626 O GLN A 207 48.843 50.247 28.802 1.00 29.03 O ANISOU 1626 O GLN B 207 4537 3459 3036 -42 551 326 O ATOM 1627 CB GLN A 207 46.724 52.299 29.620 1.00 36.95 C ANISOU 1627 CB GLN B 207 4455 5029 4553 -804 -1270 278 C ATOM 1628 CG GLN A 207 46.477 52.736 28.189 1.00 47.12 C ANISOU 1628 CG GLN B 207 5195 7212 5495 -2280 256 49 C ATOM 1629 CD GLN A 207 46.228 54.228 28.062 1.00 58.32 C ANISOU 1629 CD GLN B 207 5271 8711 8178 -2199 1161 -85 C ATOM 1630 OE1 GLN A 207 46.805 55.041 28.810 1.00 66.79 O ANISOU 1630 OE1 GLN B 207 6080 5957 13342 -1004 1966 -111 O ATOM 1631 NE2 GLN A 207 45.359 54.580 27.106 1.00 76.22 N ANISOU 1631 NE2 GLN B 207 4748 13694 10520 -4923 636 1575 N ATOM 1632 N LYS A 208 49.868 52.142 28.178 1.00 25.90 N ANISOU 1632 N LYS B 208 4036 3076 2728 -346 -118 256 N ATOM 1633 CA LYS A 208 50.701 51.517 27.161 1.00 26.11 C ANISOU 1633 CA LYS B 208 3765 3732 2423 -458 139 294 C ATOM 1634 C LYS A 208 52.107 51.206 27.648 1.00 26.21 C ANISOU 1634 C LYS B 208 3512 3888 2558 -387 -252 646 C ATOM 1635 O LYS A 208 52.996 50.763 26.922 1.00 26.03 O ANISOU 1635 O LYS B 208 3872 3305 2713 -291 -176 195 O ATOM 1636 CB LYS A 208 50.837 52.478 25.972 1.00 26.25 C ANISOU 1636 CB LYS B 208 3674 3411 2887 -397 148 -17 C ATOM 1637 CG LYS A 208 49.477 52.994 25.499 1.00 30.23 C ANISOU 1637 CG LYS B 208 4395 3646 3444 -621 1015 -299 C ATOM 1638 CD LYS A 208 48.593 51.858 25.007 1.00 31.45 C ANISOU 1638 CD LYS B 208 4882 3749 3319 -1187 -14 134 C ATOM 1639 CE LYS A 208 47.412 52.459 24.249 1.00 33.73 C ANISOU 1639 CE LYS B 208 4506 4101 4209 -1327 -214 329 C ATOM 1640 NZ LYS A 208 46.444 51.418 23.840 1.00 36.37 N ANISOU 1640 NZ LYS B 208 5786 3210 4825 -1811 65 -212 N ATOM 1641 N ALA A 209 52.362 51.468 28.914 1.00 27.52 N ANISOU 1641 N ALA B 209 3856 3895 2704 -341 -333 905 N ATOM 1642 CA ALA A 209 53.726 51.368 29.425 1.00 25.88 C ANISOU 1642 CA ALA B 209 3565 3497 2773 -123 -826 957 C ATOM 1643 C ALA A 209 54.270 49.952 29.334 1.00 25.14 C ANISOU 1643 C ALA B 209 3546 3492 2513 -82 -760 754 C ATOM 1644 O ALA A 209 55.450 49.767 28.991 1.00 26.85 O ANISOU 1644 O ALA B 209 3455 3812 2936 -140 -241 8 O ATOM 1645 CB ALA A 209 53.786 51.912 30.860 1.00 23.02 C ANISOU 1645 CB ALA B 209 2921 3511 2316 25 -299 546 C ATOM 1646 N LEU A 210 53.457 48.949 29.629 1.00 25.44 N ANISOU 1646 N LEU B 210 3524 3670 2471 -183 -458 358 N ATOM 1647 CA LEU A 210 53.987 47.569 29.529 1.00 25.96 C ANISOU 1647 CA LEU B 210 3513 3934 2415 -72 -197 183 C ATOM 1648 C LEU A 210 54.259 47.199 28.079 1.00 25.20 C ANISOU 1648 C LEU B 210 3328 3734 2514 20 -310 632 C ATOM 1649 O LEU A 210 55.214 46.482 27.764 1.00 31.16 O ANISOU 1649 O LEU B 210 4203 4560 3078 -900 -917 898 O ATOM 1650 CB LEU A 210 53.035 46.541 30.145 1.00 27.50 C ANISOU 1650 CB LEU B 210 3969 3660 2821 -64 138 434 C ATOM 1651 CG LEU A 210 53.034 46.480 31.671 1.00 30.14 C ANISOU 1651 CG LEU B 210 4555 3985 2914 -429 747 -23 C ATOM 1652 CD1 LEU A 210 51.852 45.667 32.182 1.00 40.51 C ANISOU 1652 CD1 LEU B 210 6486 4436 4470 -530 822 -963 C ATOM 1653 CD2 LEU A 210 54.335 45.898 32.196 1.00 33.37 C ANISOU 1653 CD2 LEU B 210 4280 4458 3940 -58 1358 352 C ATOM 1654 N ALA A 211 53.395 47.698 27.183 1.00 27.48 N ANISOU 1654 N ALA B 211 4486 3291 2663 -308 115 631 N ATOM 1655 CA ALA A 211 53.630 47.441 25.774 1.00 28.29 C ANISOU 1655 CA ALA B 211 3993 4123 2631 -618 294 169 C ATOM 1656 C ALA A 211 54.912 48.116 25.304 1.00 28.10 C ANISOU 1656 C ALA B 211 4031 3919 2728 -565 200 406 C ATOM 1657 O ALA A 211 55.651 47.519 24.509 1.00 28.25 O ANISOU 1657 O ALA B 211 3966 3542 3227 -506 8 452 O ATOM 1658 CB ALA A 211 52.424 47.916 24.985 1.00 25.95 C ANISOU 1658 CB ALA B 211 3715 3845 2298 -492 -138 300 C ATOM 1659 N LEU A 212 55.189 49.337 25.763 1.00 29.74 N ANISOU 1659 N LEU B 212 4595 4129 2575 -549 -229 649 N ATOM 1660 CA LEU A 212 56.380 50.072 25.359 1.00 25.23 C ANISOU 1660 CA LEU B 212 3555 4092 1940 -464 -338 834 C ATOM 1661 C LEU A 212 57.620 49.308 25.822 1.00 26.45 C ANISOU 1661 C LEU B 212 3253 4091 2706 -119 118 416 C ATOM 1662 O LEU A 212 58.613 49.210 25.106 1.00 26.73 O ANISOU 1662 O LEU B 212 3539 3928 2690 -461 108 723 O ATOM 1663 CB LEU A 212 56.470 51.451 25.979 1.00 26.14 C ANISOU 1663 CB LEU B 212 3254 5074 1604 -148 130 1069 C ATOM 1664 CG LEU A 212 56.930 52.638 25.164 1.00 31.40 C ANISOU 1664 CG LEU B 212 4836 4104 2990 228 -696 230 C ATOM 1665 CD1 LEU A 212 57.710 53.622 26.030 1.00 31.16 C ANISOU 1665 CD1 LEU B 212 5718 3975 2147 -356 505 747 C ATOM 1666 CD2 LEU A 212 57.753 52.278 23.931 1.00 29.99 C ANISOU 1666 CD2 LEU B 212 3747 2975 4675 428 -1429 -231 C ATOM 1667 N GLN A 213 57.486 48.821 27.050 1.00 28.60 N ANISOU 1667 N GLN B 213 3647 4297 2922 23 421 291 N ATOM 1668 CA GLN A 213 58.602 48.044 27.612 1.00 28.27 C ANISOU 1668 CA GLN B 213 3770 4308 2664 43 296 648 C ATOM 1669 C GLN A 213 58.845 46.771 26.796 1.00 27.90 C ANISOU 1669 C GLN B 213 3697 3508 3397 162 48 28 C ATOM 1670 O GLN A 213 60.006 46.422 26.539 1.00 26.94 O ANISOU 1670 O GLN B 213 3530 3710 2995 -146 559 542 O ATOM 1671 CB GLN A 213 58.353 47.724 29.098 1.00 29.86 C ANISOU 1671 CB GLN B 213 4273 4258 2815 304 573 427 C ATOM 1672 CG GLN A 213 59.646 47.351 29.826 1.00 39.30 C ANISOU 1672 CG GLN B 213 6207 5403 3322 -880 1789 -170 C ATOM 1673 CD GLN A 213 59.916 45.860 29.763 1.00 45.82 C ANISOU 1673 CD GLN B 213 5764 6136 5508 -1206 2816 22 C ATOM 1674 OE1 GLN A 213 58.993 45.118 29.416 1.00 53.98 O ANISOU 1674 OE1 GLN B 213 5710 6244 8557 -370 2661 187 O ATOM 1675 NE2 GLN A 213 61.122 45.393 30.040 1.00 57.17 N ANISOU 1675 NE2 GLN B 213 6683 8012 7026 -2886 1918 53 N ATOM 1676 N ALA A 214 57.756 46.097 26.426 1.00 28.99 N ANISOU 1676 N ALA B 214 4033 3798 3185 -353 -195 686 N ATOM 1677 CA ALA A 214 57.904 44.867 25.654 1.00 28.54 C ANISOU 1677 CA ALA B 214 3677 3693 3475 -175 -111 350 C ATOM 1678 C ALA A 214 58.489 45.189 24.287 1.00 28.15 C ANISOU 1678 C ALA B 214 3485 3684 3525 -42 -286 270 C ATOM 1679 O ALA A 214 59.278 44.374 23.775 1.00 32.38 O ANISOU 1679 O ALA B 214 3423 5591 3289 -771 170 210 O ATOM 1680 CB ALA A 214 56.592 44.128 25.455 1.00 28.84 C ANISOU 1680 CB ALA B 214 3188 3675 4096 -530 -1297 130 C ATOM 1681 N ALA A 215 58.128 46.331 23.707 1.00 26.92 N ANISOU 1681 N ALA B 215 3358 3711 3160 20 -495 438 N ATOM 1682 CA ALA A 215 58.657 46.707 22.393 1.00 30.50 C ANISOU 1682 CA ALA B 215 4225 3758 3604 -113 -91 36 C ATOM 1683 C ALA A 215 60.150 47.023 22.453 1.00 27.87 C ANISOU 1683 C ALA B 215 3067 3676 3846 215 -514 194 C ATOM 1684 O ALA A 215 60.915 46.605 21.584 1.00 28.10 O ANISOU 1684 O ALA B 215 3415 4015 3248 -44 -217 177 O ATOM 1685 CB ALA A 215 57.899 47.894 21.796 1.00 26.25 C ANISOU 1685 CB ALA B 215 4114 3604 2255 -51 -540 938 C ATOM 1686 N VAL A 216 60.579 47.769 23.470 1.00 26.01 N ANISOU 1686 N VAL B 216 2832 4068 2981 93 223 219 N ATOM 1687 CA VAL A 216 61.910 48.347 23.491 1.00 28.99 C ANISOU 1687 CA VAL B 216 3507 4112 3397 -225 178 765 C ATOM 1688 C VAL A 216 62.890 47.510 24.297 1.00 28.46 C ANISOU 1688 C VAL B 216 3112 4337 3362 -369 41 110 C ATOM 1689 O VAL A 216 64.025 47.279 23.830 1.00 31.65 O ANISOU 1689 O VAL B 216 3387 4551 4086 -556 -656 424 O ATOM 1690 CB VAL A 216 61.840 49.772 24.084 1.00 29.65 C ANISOU 1690 CB VAL B 216 3251 3832 4183 68 523 354 C ATOM 1691 CG1 VAL A 216 63.216 50.385 24.327 1.00 29.03 C ANISOU 1691 CG1 VAL B 216 3443 3719 3869 105 375 13 C ATOM 1692 CG2 VAL A 216 61.025 50.687 23.168 1.00 30.11 C ANISOU 1692 CG2 VAL B 216 3985 3878 3576 615 904 487 C ATOM 1693 N GLU A 217 62.544 47.039 25.491 1.00 29.52 N ANISOU 1693 N GLU B 217 3976 4112 3127 260 137 542 N ATOM 1694 CA GLU A 217 63.541 46.373 26.336 1.00 27.64 C ANISOU 1694 CA GLU B 217 3965 3921 2615 -127 -259 328 C ATOM 1695 C GLU A 217 63.318 44.872 26.376 1.00 27.57 C ANISOU 1695 C GLU B 217 3324 3921 3230 -513 -371 158 C ATOM 1696 O GLU A 217 64.236 44.126 26.691 1.00 30.82 O ANISOU 1696 O GLU B 217 3867 4616 3227 -699 388 516 O ATOM 1697 CB GLU A 217 63.507 46.812 27.806 1.00 28.51 C ANISOU 1697 CB GLU B 217 4447 3723 2661 -394 -510 230 C ATOM 1698 CG GLU A 217 64.171 48.120 28.134 1.00 31.72 C ANISOU 1698 CG GLU B 217 5028 3915 3109 -231 -796 545 C ATOM 1699 CD GLU A 217 63.838 48.603 29.532 1.00 30.22 C ANISOU 1699 CD GLU B 217 4414 4065 3004 153 -513 122 C ATOM 1700 OE1 GLU A 217 63.216 47.848 30.313 1.00 35.52 O ANISOU 1700 OE1 GLU B 217 5903 4209 3386 209 -68 -39 O ATOM 1701 OE2 GLU A 217 64.172 49.741 29.916 1.00 30.37 O ANISOU 1701 OE2 GLU B 217 4816 3827 2895 -71 -240 972 O ATOM 1702 N GLY A 218 62.107 44.414 26.091 1.00 27.03 N ANISOU 1702 N GLY B 218 3319 3806 3146 -253 182 24 N ATOM 1703 CA GLY A 218 61.890 42.976 26.211 1.00 27.96 C ANISOU 1703 CA GLY B 218 3346 4040 3238 -207 332 -278 C ATOM 1704 C GLY A 218 62.464 42.192 25.052 1.00 26.15 C ANISOU 1704 C GLY B 218 3303 3304 3330 261 346 -666 C ATOM 1705 O GLY A 218 63.038 42.733 24.123 1.00 26.74 O ANISOU 1705 O GLY B 218 3373 3412 3376 240 541 -709 O ATOM 1706 N CYS A 219 62.315 40.867 25.087 1.00 24.88 N ANISOU 1706 N CYS B 219 3568 2925 2958 352 743 37 N ATOM 1707 CA CYS A 219 62.789 40.071 23.984 1.00 30.38 C ANISOU 1707 CA CYS B 219 4496 3078 3969 623 -280 303 C ATOM 1708 C CYS A 219 61.661 39.820 22.975 1.00 30.85 C ANISOU 1708 C CYS B 219 4438 3599 3682 74 -540 392 C ATOM 1709 O CYS A 219 60.484 40.058 23.250 1.00 25.68 O ANISOU 1709 O CYS B 219 3123 3511 3124 661 -12 78 O ATOM 1710 CB CYS A 219 63.335 38.722 24.460 1.00 37.11 C ANISOU 1710 CB CYS B 219 3936 4930 5235 -330 -381 641 C ATOM 1711 SG CYS A 219 64.872 38.834 25.414 1.00 58.04 S ANISOU 1711 SG CYS B 219 7872 5748 8434 -1355 2190 1007 S ATOM 1712 N VAL A 220 62.051 39.322 21.814 1.00 27.88 N ANISOU 1712 N VAL B 220 3496 3703 3394 104 59 -12 N ATOM 1713 CA VAL A 220 61.074 39.016 20.771 1.00 26.75 C ANISOU 1713 CA VAL B 220 3323 3784 3057 282 28 -76 C ATOM 1714 C VAL A 220 60.154 37.866 21.176 1.00 26.58 C ANISOU 1714 C VAL B 220 3305 3766 3028 181 527 46 C ATOM 1715 O VAL A 220 60.570 36.757 21.528 1.00 26.98 O ANISOU 1715 O VAL B 220 3141 3674 3436 -52 435 -131 O ATOM 1716 CB VAL A 220 61.793 38.701 19.448 1.00 33.69 C ANISOU 1716 CB VAL B 220 5260 4232 3308 -763 -327 -237 C ATOM 1717 CG1 VAL A 220 60.760 38.263 18.400 1.00 29.53 C ANISOU 1717 CG1 VAL B 220 4246 4100 2875 -432 -540 -467 C ATOM 1718 CG2 VAL A 220 62.589 39.912 18.990 1.00 29.12 C ANISOU 1718 CG2 VAL B 220 4256 4208 2601 -760 -991 -56 C ATOM 1719 N ASN A 221 58.839 38.122 21.136 1.00 23.80 N ANISOU 1719 N ASN B 221 2734 3576 2733 519 250 357 N ATOM 1720 CA ASN A 221 57.925 37.022 21.411 1.00 26.01 C ANISOU 1720 CA ASN B 221 2969 3599 3315 539 773 400 C ATOM 1721 C ASN A 221 56.555 37.332 20.821 1.00 28.17 C ANISOU 1721 C ASN B 221 2942 3749 4012 85 133 543 C ATOM 1722 O ASN A 221 56.131 38.486 20.806 1.00 30.71 O ANISOU 1722 O ASN B 221 3047 3707 4914 270 773 475 O ATOM 1723 CB ASN A 221 57.825 36.739 22.909 1.00 33.22 C ANISOU 1723 CB ASN B 221 5329 3818 3475 153 881 -227 C ATOM 1724 CG ASN A 221 56.873 37.747 23.511 1.00 39.44 C ANISOU 1724 CG ASN B 221 6876 4170 3941 -916 -536 452 C ATOM 1725 OD1 ASN A 221 55.689 37.444 23.632 1.00 50.59 O ANISOU 1725 OD1 ASN B 221 9635 4632 4955 -1970 -966 36 O ATOM 1726 ND2 ASN A 221 57.418 38.906 23.845 1.00 39.14 N ANISOU 1726 ND2 ASN B 221 4934 5456 4482 -196 908 529 N ATOM 1727 N HIS A 222 55.871 36.306 20.318 1.00 24.93 N ANISOU 1727 N HIS B 222 3292 3123 3055 99 244 -201 N ATOM 1728 CA HIS A 222 54.625 36.570 19.607 1.00 28.03 C ANISOU 1728 CA HIS B 222 3672 3846 3130 -342 -116 313 C ATOM 1729 C HIS A 222 53.481 36.954 20.526 1.00 25.51 C ANISOU 1729 C HIS B 222 3150 3788 2756 -191 167 370 C ATOM 1730 O HIS A 222 52.421 37.365 20.069 1.00 26.47 O ANISOU 1730 O HIS B 222 3347 4108 2601 -357 606 -136 O ATOM 1731 CB HIS A 222 54.264 35.327 18.775 1.00 27.71 C ANISOU 1731 CB HIS B 222 3610 4005 2913 -335 -149 269 C ATOM 1732 CG HIS A 222 53.844 34.145 19.595 1.00 30.41 C ANISOU 1732 CG HIS B 222 4463 3639 3452 -122 171 392 C ATOM 1733 ND1 HIS A 222 53.069 33.163 19.040 1.00 30.51 N ANISOU 1733 ND1 HIS B 222 4026 3751 3813 -351 -41 647 N ATOM 1734 CD2 HIS A 222 54.076 33.747 20.888 1.00 28.37 C ANISOU 1734 CD2 HIS B 222 3804 3680 3294 164 -146 175 C ATOM 1735 CE1 HIS A 222 52.821 32.223 19.938 1.00 29.61 C ANISOU 1735 CE1 HIS B 222 3212 3860 4178 -174 -48 794 C ATOM 1736 NE2 HIS A 222 53.416 32.548 21.075 1.00 27.77 N ANISOU 1736 NE2 HIS B 222 3066 3834 3652 142 -437 335 N ATOM 1737 N MET A 223 53.631 36.804 21.846 1.00 25.07 N ANISOU 1737 N MET B 223 3191 3482 2852 -2 648 90 N ATOM 1738 CA MET A 223 52.486 37.140 22.697 1.00 27.84 C ANISOU 1738 CA MET B 223 3817 3836 2926 20 235 -63 C ATOM 1739 C MET A 223 52.342 38.665 22.815 1.00 28.01 C ANISOU 1739 C MET B 223 3332 3791 3519 -420 477 -313 C ATOM 1740 O MET A 223 51.230 39.173 23.010 1.00 32.61 O ANISOU 1740 O MET B 223 4043 4364 3982 -827 -476 -588 O ATOM 1741 CB MET A 223 52.583 36.505 24.082 1.00 31.81 C ANISOU 1741 CB MET B 223 3759 4994 3335 -137 569 -704 C ATOM 1742 CG MET A 223 52.330 35.023 24.232 1.00 35.49 C ANISOU 1742 CG MET B 223 4971 4284 4229 278 1229 -251 C ATOM 1743 SD MET A 223 50.649 34.442 23.909 1.00 45.43 S ANISOU 1743 SD MET B 223 7173 4720 5367 -457 4 786 S ATOM 1744 CE MET A 223 49.678 35.735 24.647 1.00 45.69 C ANISOU 1744 CE MET B 223 6965 6223 4174 -1548 947 -545 C ATOM 1745 N TRP A 224 53.441 39.403 22.709 1.00 26.46 N ANISOU 1745 N TRP B 224 3248 3792 3012 -210 580 -393 N ATOM 1746 CA TRP A 224 53.464 40.853 22.631 1.00 25.51 C ANISOU 1746 CA TRP B 224 2915 3982 2794 -399 599 -47 C ATOM 1747 C TRP A 224 53.859 41.208 21.203 1.00 23.92 C ANISOU 1747 C TRP B 224 2798 3541 2750 126 299 111 C ATOM 1748 O TRP A 224 55.054 41.366 20.922 1.00 28.18 O ANISOU 1748 O TRP B 224 4073 4026 2607 -664 -261 251 O ATOM 1749 CB TRP A 224 54.454 41.452 23.630 1.00 26.22 C ANISOU 1749 CB TRP B 224 3118 4195 2652 -420 353 18 C ATOM 1750 CG TRP A 224 53.995 41.231 25.057 1.00 27.79 C ANISOU 1750 CG TRP B 224 3388 4375 2797 -169 32 -98 C ATOM 1751 CD1 TRP A 224 54.148 40.095 25.792 1.00 28.37 C ANISOU 1751 CD1 TRP B 224 3671 4310 2800 -9 -75 -617 C ATOM 1752 CD2 TRP A 224 53.319 42.152 25.917 1.00 28.12 C ANISOU 1752 CD2 TRP B 224 3668 4114 2901 -141 -221 210 C ATOM 1753 NE1 TRP A 224 53.620 40.238 27.039 1.00 29.97 N ANISOU 1753 NE1 TRP B 224 3806 4833 2747 -261 -224 -395 N ATOM 1754 CE2 TRP A 224 53.096 41.504 27.146 1.00 30.42 C ANISOU 1754 CE2 TRP B 224 3885 4698 2975 -218 -329 -98 C ATOM 1755 CE3 TRP A 224 52.872 43.463 25.783 1.00 27.83 C ANISOU 1755 CE3 TRP B 224 3701 3809 3064 31 -475 414 C ATOM 1756 CZ2 TRP A 224 52.451 42.123 28.216 1.00 30.60 C ANISOU 1756 CZ2 TRP B 224 3923 4616 3087 -197 -442 -43 C ATOM 1757 CZ3 TRP A 224 52.230 44.088 26.838 1.00 28.39 C ANISOU 1757 CZ3 TRP B 224 3913 3697 3177 -26 -548 146 C ATOM 1758 CH2 TRP A 224 52.023 43.413 28.052 1.00 29.45 C ANISOU 1758 CH2 TRP B 224 3780 4361 3050 -619 -160 298 C ATOM 1759 N THR A 225 52.881 41.289 20.298 1.00 24.46 N ANISOU 1759 N THR B 225 2994 3587 2711 71 623 -144 N ATOM 1760 CA THR A 225 53.140 41.441 18.872 1.00 23.89 C ANISOU 1760 CA THR B 225 2936 3457 2683 -37 365 -176 C ATOM 1761 C THR A 225 54.107 42.583 18.595 1.00 23.19 C ANISOU 1761 C THR B 225 3060 3332 2421 -189 -249 -227 C ATOM 1762 O THR A 225 54.999 42.456 17.758 1.00 24.92 O ANISOU 1762 O THR B 225 3742 3616 2112 -581 -167 -160 O ATOM 1763 CB THR A 225 51.818 41.693 18.117 1.00 28.76 C ANISOU 1763 CB THR B 225 5097 3622 2209 -1100 151 -226 C ATOM 1764 OG1 THR A 225 50.912 40.639 18.442 1.00 26.14 O ANISOU 1764 OG1 THR B 225 3254 3870 2808 -573 134 514 O ATOM 1765 CG2 THR A 225 52.037 41.643 16.610 1.00 25.10 C ANISOU 1765 CG2 THR B 225 3289 3990 2260 -19 -1080 637 C ATOM 1766 N ILE A 226 53.936 43.690 19.295 1.00 23.82 N ANISOU 1766 N ILE B 226 3298 3556 2197 -70 -148 250 N ATOM 1767 CA ILE A 226 54.777 44.870 19.121 1.00 26.22 C ANISOU 1767 CA ILE B 226 3673 3367 2922 -125 -323 466 C ATOM 1768 C ILE A 226 56.257 44.549 19.301 1.00 27.08 C ANISOU 1768 C ILE B 226 3529 3616 3145 -236 -8 -107 C ATOM 1769 O ILE A 226 57.112 45.233 18.699 1.00 25.56 O ANISOU 1769 O ILE B 226 3398 3644 2671 -280 170 31 O ATOM 1770 CB ILE A 226 54.363 46.004 20.089 1.00 24.10 C ANISOU 1770 CB ILE B 226 3102 3689 2368 264 168 -148 C ATOM 1771 CG1 ILE A 226 54.915 47.376 19.670 1.00 26.09 C ANISOU 1771 CG1 ILE B 226 2996 3888 3031 95 447 -573 C ATOM 1772 CG2 ILE A 226 54.746 45.709 21.553 1.00 22.86 C ANISOU 1772 CG2 ILE B 226 2494 3551 2642 498 325 295 C ATOM 1773 CD1 ILE A 226 54.233 47.929 18.426 1.00 30.57 C ANISOU 1773 CD1 ILE B 226 3755 4324 3538 229 1015 -389 C ATOM 1774 N SER A 227 56.605 43.531 20.102 1.00 25.04 N ANISOU 1774 N SER B 227 3424 3454 2636 -15 -298 -68 N ATOM 1775 CA SER A 227 58.020 43.182 20.256 1.00 26.89 C ANISOU 1775 CA SER B 227 3845 3709 2662 -327 253 -370 C ATOM 1776 C SER A 227 58.630 42.710 18.936 1.00 27.33 C ANISOU 1776 C SER B 227 3780 3607 2999 -575 -69 -80 C ATOM 1777 O SER A 227 59.840 42.784 18.735 1.00 25.90 O ANISOU 1777 O SER B 227 3228 3565 3048 -395 43 -78 O ATOM 1778 CB SER A 227 58.225 42.096 21.315 1.00 28.65 C ANISOU 1778 CB SER B 227 3612 3899 3375 57 326 -525 C ATOM 1779 OG SER A 227 57.784 40.824 20.837 1.00 29.28 O ANISOU 1779 OG SER B 227 4302 3703 3122 -12 499 -34 O ATOM 1780 N CYS A 228 57.786 42.207 18.007 1.00 27.72 N ANISOU 1780 N CYS B 228 3531 3482 3517 -138 -413 144 N ATOM 1781 CA CYS A 228 58.462 41.709 16.802 1.00 30.52 C ANISOU 1781 CA CYS B 228 3796 4297 3502 -259 -491 167 C ATOM 1782 C CYS A 228 58.897 42.875 15.918 1.00 28.64 C ANISOU 1782 C CYS B 228 4034 3652 3198 -282 -635 375 C ATOM 1783 O CYS A 228 59.642 42.658 14.956 1.00 28.04 O ANISOU 1783 O CYS B 228 4053 4283 2318 -141 -620 895 O ATOM 1784 CB CYS A 228 57.580 40.641 16.139 1.00 35.97 C ANISOU 1784 CB CYS B 228 4947 4097 4625 374 -2151 -672 C ATOM 1785 SG CYS A 228 57.190 39.295 17.387 1.00 44.93 S ANISOU 1785 SG CYS B 228 6784 4787 5499 995 -101 253 S ATOM 1786 N LEU A 229 58.526 44.123 16.226 1.00 25.14 N ANISOU 1786 N LEU B 229 3768 3358 2425 -601 -289 556 N ATOM 1787 CA LEU A 229 59.089 45.246 15.465 1.00 26.01 C ANISOU 1787 CA LEU B 229 3763 3876 2245 -645 -166 307 C ATOM 1788 C LEU A 229 60.588 45.395 15.653 1.00 27.05 C ANISOU 1788 C LEU B 229 3811 3617 2851 -359 608 -10 C ATOM 1789 O LEU A 229 61.253 46.096 14.877 1.00 25.11 O ANISOU 1789 O LEU B 229 3310 3704 2526 -28 400 164 O ATOM 1790 CB LEU A 229 58.392 46.564 15.841 1.00 27.99 C ANISOU 1790 CB LEU B 229 3715 4359 2561 -462 -105 389 C ATOM 1791 CG LEU A 229 56.969 46.682 15.265 1.00 35.45 C ANISOU 1791 CG LEU B 229 4502 5677 3289 -1842 -283 498 C ATOM 1792 CD1 LEU A 229 56.319 47.982 15.687 1.00 35.34 C ANISOU 1792 CD1 LEU B 229 4276 6000 3152 -1493 117 -705 C ATOM 1793 CD2 LEU A 229 57.018 46.591 13.747 1.00 30.45 C ANISOU 1793 CD2 LEU B 229 3824 4477 3267 -1275 323 542 C ATOM 1794 N GLN A 230 61.158 44.740 16.659 1.00 26.40 N ANISOU 1794 N GLN B 230 3851 3533 2648 -560 549 -290 N ATOM 1795 CA GLN A 230 62.604 44.712 16.824 1.00 25.65 C ANISOU 1795 CA GLN B 230 3857 3443 2445 -411 8 347 C ATOM 1796 C GLN A 230 63.289 44.081 15.608 1.00 24.61 C ANISOU 1796 C GLN B 230 3239 3277 2836 167 82 -266 C ATOM 1797 O GLN A 230 64.460 44.338 15.336 1.00 26.95 O ANISOU 1797 O GLN B 230 3802 3453 2986 -187 192 -316 O ATOM 1798 CB GLN A 230 63.010 43.905 18.068 1.00 25.56 C ANISOU 1798 CB GLN B 230 4034 3023 2655 -236 224 432 C ATOM 1799 CG GLN A 230 62.621 44.561 19.382 1.00 25.03 C ANISOU 1799 CG GLN B 230 3973 3053 2486 296 372 499 C ATOM 1800 CD GLN A 230 63.037 43.744 20.590 1.00 27.22 C ANISOU 1800 CD GLN B 230 3859 3743 2742 -48 491 -185 C ATOM 1801 OE1 GLN A 230 64.041 43.020 20.530 1.00 28.77 O ANISOU 1801 OE1 GLN B 230 3961 3766 3204 -190 487 95 O ATOM 1802 NE2 GLN A 230 62.280 43.852 21.686 1.00 31.30 N ANISOU 1802 NE2 GLN B 230 4572 4527 2795 -375 440 -383 N ATOM 1803 N LEU A 231 62.541 43.230 14.901 1.00 25.39 N ANISOU 1803 N LEU B 231 3599 3562 2485 206 -28 -133 N ATOM 1804 CA LEU A 231 63.097 42.551 13.745 1.00 24.25 C ANISOU 1804 CA LEU B 231 3256 3484 2474 130 188 -459 C ATOM 1805 C LEU A 231 62.802 43.331 12.464 1.00 24.06 C ANISOU 1805 C LEU B 231 3218 3411 2514 113 235 -303 C ATOM 1806 O LEU A 231 63.255 42.963 11.372 1.00 31.82 O ANISOU 1806 O LEU B 231 4543 5218 2330 -1154 174 -216 O ATOM 1807 CB LEU A 231 62.517 41.140 13.605 1.00 25.21 C ANISOU 1807 CB LEU B 231 2684 3926 2969 149 149 -360 C ATOM 1808 CG LEU A 231 62.735 40.258 14.836 1.00 27.06 C ANISOU 1808 CG LEU B 231 3295 3610 3378 173 658 -285 C ATOM 1809 CD1 LEU A 231 62.118 38.889 14.581 1.00 28.51 C ANISOU 1809 CD1 LEU B 231 3502 4002 3326 534 145 -685 C ATOM 1810 CD2 LEU A 231 64.222 40.212 15.155 1.00 28.42 C ANISOU 1810 CD2 LEU B 231 3397 4006 3397 -320 521 -514 C ATOM 1811 N HIS A 232 62.043 44.412 12.598 1.00 26.95 N ANISOU 1811 N HIS B 232 3167 3463 3609 -99 451 265 N ATOM 1812 CA HIS A 232 61.700 45.153 11.377 1.00 26.73 C ANISOU 1812 CA HIS B 232 2986 3787 3384 -101 213 -20 C ATOM 1813 C HIS A 232 62.851 46.042 10.952 1.00 25.36 C ANISOU 1813 C HIS B 232 3199 3722 2714 -146 -298 93 C ATOM 1814 O HIS A 232 63.559 46.634 11.761 1.00 29.30 O ANISOU 1814 O HIS B 232 4631 3628 2874 -997 159 409 O ATOM 1815 CB HIS A 232 60.412 45.945 11.643 1.00 24.21 C ANISOU 1815 CB HIS B 232 3148 3584 2465 -189 147 217 C ATOM 1816 CG HIS A 232 59.870 46.542 10.381 1.00 24.58 C ANISOU 1816 CG HIS B 232 3459 3392 2489 -228 314 -9 C ATOM 1817 ND1 HIS A 232 60.322 47.757 9.914 1.00 24.87 N ANISOU 1817 ND1 HIS B 232 3275 3272 2904 -316 339 11 N ATOM 1818 CD2 HIS A 232 58.947 46.087 9.507 1.00 23.99 C ANISOU 1818 CD2 HIS B 232 3153 3477 2487 -108 361 69 C ATOM 1819 CE1 HIS A 232 59.685 48.037 8.781 1.00 27.11 C ANISOU 1819 CE1 HIS B 232 3390 3582 3326 73 781 245 C ATOM 1820 NE2 HIS A 232 58.849 47.045 8.514 1.00 27.56 N ANISOU 1820 NE2 HIS B 232 3913 3291 3266 -106 1117 149 N ATOM 1821 N PRO A 233 63.111 46.161 9.647 1.00 29.85 N ANISOU 1821 N PRO B 233 4389 4130 2825 -525 -831 -39 N ATOM 1822 CA PRO A 233 64.242 46.983 9.200 1.00 29.55 C ANISOU 1822 CA PRO B 233 4353 4227 2648 -629 20 -135 C ATOM 1823 C PRO A 233 64.151 48.437 9.651 1.00 30.17 C ANISOU 1823 C PRO B 233 4240 3997 3226 -655 269 54 C ATOM 1824 O PRO A 233 65.203 49.071 9.836 1.00 30.28 O ANISOU 1824 O PRO B 233 4342 3887 3276 -373 1171 -270 O ATOM 1825 CB PRO A 233 64.170 46.921 7.673 1.00 29.53 C ANISOU 1825 CB PRO B 233 4372 4156 2691 -1082 502 167 C ATOM 1826 CG PRO A 233 62.909 46.236 7.331 1.00 33.98 C ANISOU 1826 CG PRO B 233 5727 4093 3092 -287 649 102 C ATOM 1827 CD PRO A 233 62.397 45.513 8.541 1.00 31.71 C ANISOU 1827 CD PRO B 233 5181 4341 2525 -575 -100 46 C ATOM 1828 N LYS A 234 62.973 49.026 9.831 1.00 28.88 N ANISOU 1828 N LYS B 234 3639 4258 3076 -531 1301 -227 N ATOM 1829 CA LYS A 234 62.917 50.467 10.091 1.00 29.54 C ANISOU 1829 CA LYS B 234 3940 4172 3110 -404 1065 -86 C ATOM 1830 C LYS A 234 61.685 50.844 10.907 1.00 33.54 C ANISOU 1830 C LYS B 234 4515 4743 3485 -914 306 503 C ATOM 1831 O LYS A 234 60.645 51.249 10.360 1.00 27.61 O ANISOU 1831 O LYS B 234 2921 4179 3391 248 464 169 O ATOM 1832 CB LYS A 234 62.912 51.241 8.766 1.00 30.48 C ANISOU 1832 CB LYS B 234 3351 4769 3459 -536 1563 245 C ATOM 1833 CG LYS A 234 63.611 52.579 8.896 1.00 38.16 C ANISOU 1833 CG LYS B 234 4449 4908 5142 -7 2316 -28 C ATOM 1834 CD LYS A 234 63.351 53.455 7.683 1.00 47.81 C ANISOU 1834 CD LYS B 234 6546 5808 5814 -229 3168 -1844 C ATOM 1835 CE LYS A 234 63.917 52.772 6.450 1.00 54.11 C ANISOU 1835 CE LYS B 234 8746 6080 5734 -1419 2641 -2081 C ATOM 1836 NZ LYS A 234 64.965 53.659 5.859 1.00 66.62 N ANISOU 1836 NZ LYS B 234 10734 5787 8791 -2122 2186 -2864 N ATOM 1837 N ALA A 235 61.815 50.697 12.218 1.00 27.96 N ANISOU 1837 N ALA B 235 3557 3681 3387 -288 66 568 N ATOM 1838 CA ALA A 235 60.741 50.938 13.166 1.00 31.58 C ANISOU 1838 CA ALA B 235 3988 4098 3913 -355 -424 435 C ATOM 1839 C ALA A 235 61.056 52.085 14.127 1.00 29.07 C ANISOU 1839 C ALA B 235 3748 3818 3480 -355 -57 357 C ATOM 1840 O ALA A 235 62.181 52.335 14.604 1.00 31.00 O ANISOU 1840 O ALA B 235 3926 3599 4253 -14 747 353 O ATOM 1841 CB ALA A 235 60.450 49.657 13.944 1.00 30.40 C ANISOU 1841 CB ALA B 235 4795 3101 3656 -216 -579 613 C ATOM 1842 N ILE A 236 59.994 52.845 14.425 1.00 26.94 N ANISOU 1842 N ILE B 236 3158 3904 3176 100 507 -133 N ATOM 1843 CA ILE A 236 60.104 54.003 15.294 1.00 31.10 C ANISOU 1843 CA ILE B 236 3868 4157 3793 175 -244 -227 C ATOM 1844 C ILE A 236 58.959 54.015 16.293 1.00 29.56 C ANISOU 1844 C ILE B 236 3757 4065 3411 -181 121 1 C ATOM 1845 O ILE A 236 57.827 53.888 15.846 1.00 33.00 O ANISOU 1845 O ILE B 236 5284 4375 2879 -612 -69 189 O ATOM 1846 CB ILE A 236 60.050 55.306 14.474 1.00 31.23 C ANISOU 1846 CB ILE B 236 3621 4325 3921 596 -804 -478 C ATOM 1847 CG1 ILE A 236 60.954 55.263 13.249 1.00 35.13 C ANISOU 1847 CG1 ILE B 236 3770 5456 4123 385 -695 -1035 C ATOM 1848 CG2 ILE A 236 60.361 56.521 15.333 1.00 31.42 C ANISOU 1848 CG2 ILE B 236 2994 5127 3817 -118 -89 1014 C ATOM 1849 CD1 ILE A 236 60.947 56.513 12.385 1.00 55.06 C ANISOU 1849 CD1 ILE B 236 7612 6737 6571 -825 3180 -2168 C ATOM 1850 N MET A 237 59.272 54.160 17.563 1.00 29.36 N ANISOU 1850 N MET B 237 3617 4074 3464 -752 422 95 N ATOM 1851 CA MET A 237 58.296 54.358 18.614 1.00 30.49 C ANISOU 1851 CA MET B 237 3624 4555 3407 -270 224 -150 C ATOM 1852 C MET A 237 58.342 55.839 19.038 1.00 30.72 C ANISOU 1852 C MET B 237 3624 4444 3602 -190 392 -60 C ATOM 1853 O MET A 237 59.435 56.312 19.377 1.00 31.33 O ANISOU 1853 O MET B 237 3859 4527 3519 -259 548 85 O ATOM 1854 CB MET A 237 58.539 53.538 19.871 1.00 32.89 C ANISOU 1854 CB MET B 237 3613 4865 4018 -523 678 -645 C ATOM 1855 CG MET A 237 58.823 52.069 19.725 1.00 37.03 C ANISOU 1855 CG MET B 237 3307 5944 4817 -827 797 294 C ATOM 1856 SD MET A 237 57.521 51.158 18.921 1.00 48.54 S ANISOU 1856 SD MET B 237 5863 5740 6841 -99 -1040 349 S ATOM 1857 CE MET A 237 56.307 50.869 20.192 1.00 42.25 C ANISOU 1857 CE MET B 237 6070 5304 4680 934 -1908 1637 C ATOM 1858 N VAL A 238 57.186 56.478 18.993 1.00 29.35 N ANISOU 1858 N VAL B 238 3627 4330 3193 -186 196 -143 N ATOM 1859 CA VAL A 238 57.090 57.888 19.392 1.00 28.91 C ANISOU 1859 CA VAL B 238 3688 4254 3042 -176 227 13 C ATOM 1860 C VAL A 238 56.223 57.969 20.642 1.00 28.28 C ANISOU 1860 C VAL B 238 3595 4044 3107 -184 263 -10 C ATOM 1861 O VAL A 238 55.047 57.597 20.601 1.00 28.31 O ANISOU 1861 O VAL B 238 3533 4080 3146 -227 80 217 O ATOM 1862 CB VAL A 238 56.517 58.773 18.278 1.00 29.24 C ANISOU 1862 CB VAL B 238 3648 4347 3114 -173 238 -121 C ATOM 1863 CG1 VAL A 238 56.692 60.256 18.604 1.00 27.27 C ANISOU 1863 CG1 VAL B 238 3419 4035 2908 -480 56 -206 C ATOM 1864 CG2 VAL A 238 57.170 58.402 16.948 1.00 26.61 C ANISOU 1864 CG2 VAL B 238 3134 3775 3200 279 288 -355 C ATOM 1865 N CYS A 239 56.802 58.428 21.762 1.00 25.74 N ANISOU 1865 N CYS B 239 3053 3681 3047 -106 288 -148 N ATOM 1866 CA CYS A 239 55.997 58.225 22.965 1.00 29.29 C ANISOU 1866 CA CYS B 239 3473 4457 3199 307 101 -600 C ATOM 1867 C CYS A 239 55.932 59.453 23.854 1.00 28.69 C ANISOU 1867 C CYS B 239 4053 3961 2886 -135 87 142 C ATOM 1868 O CYS A 239 56.742 60.390 23.783 1.00 29.05 O ANISOU 1868 O CYS B 239 3648 3928 3461 -210 517 295 O ATOM 1869 CB CYS A 239 56.603 57.007 23.676 1.00 34.03 C ANISOU 1869 CB CYS B 239 4347 3865 4719 742 1239 -760 C ATOM 1870 SG CYS A 239 58.156 57.350 24.547 1.00 39.99 S ANISOU 1870 SG CYS B 239 5272 5296 4628 -462 850 -44 S ATOM 1871 N ASP A 240 54.907 59.451 24.734 1.00 26.15 N ANISOU 1871 N ASP B 240 3033 4251 2650 -398 564 161 N ATOM 1872 CA ASP A 240 54.803 60.556 25.678 1.00 29.09 C ANISOU 1872 CA ASP B 240 3413 4564 3075 -481 205 457 C ATOM 1873 C ASP A 240 55.380 60.144 27.024 1.00 28.66 C ANISOU 1873 C ASP B 240 3324 4458 3108 105 229 659 C ATOM 1874 O ASP A 240 55.813 59.003 27.193 1.00 28.38 O ANISOU 1874 O ASP B 240 3477 3970 3336 387 396 598 O ATOM 1875 CB ASP A 240 53.367 61.008 25.842 1.00 29.89 C ANISOU 1875 CB ASP B 240 3770 4689 2899 -685 -195 549 C ATOM 1876 CG ASP A 240 52.439 60.028 26.495 1.00 31.16 C ANISOU 1876 CG ASP B 240 4159 4670 3010 -564 -486 520 C ATOM 1877 OD1 ASP A 240 52.829 58.901 26.852 1.00 32.48 O ANISOU 1877 OD1 ASP B 240 4104 4798 3439 -167 -804 258 O ATOM 1878 OD2 ASP A 240 51.264 60.423 26.653 1.00 31.57 O ANISOU 1878 OD2 ASP B 240 4681 4817 2497 -942 -278 564 O ATOM 1879 N GLU A 241 55.399 61.067 27.973 1.00 29.71 N ANISOU 1879 N GLU B 241 3604 4350 3333 116 44 789 N ATOM 1880 CA GLU A 241 56.032 60.750 29.270 1.00 31.31 C ANISOU 1880 CA GLU B 241 4200 4568 3129 131 101 643 C ATOM 1881 C GLU A 241 55.339 59.650 30.054 1.00 29.43 C ANISOU 1881 C GLU B 241 3646 4509 3026 -128 -340 422 C ATOM 1882 O GLU A 241 55.996 58.704 30.523 1.00 29.66 O ANISOU 1882 O GLU B 241 4029 4344 2898 -75 59 731 O ATOM 1883 CB GLU A 241 56.116 62.042 30.101 1.00 31.59 C ANISOU 1883 CB GLU B 241 4093 5054 2857 382 334 599 C ATOM 1884 CG GLU A 241 56.545 61.827 31.545 1.00 39.18 C ANISOU 1884 CG GLU B 241 6070 5726 3091 -330 353 1361 C ATOM 1885 CD GLU A 241 56.540 63.173 32.259 1.00 49.17 C ANISOU 1885 CD GLU B 241 8485 5771 4425 -723 -2413 1325 C ATOM 1886 OE1 GLU A 241 57.459 63.967 31.975 1.00 58.40 O ANISOU 1886 OE1 GLU B 241 8545 5563 8081 -181 -2846 1624 O ATOM 1887 OE2 GLU A 241 55.623 63.441 33.072 1.00 68.54 O ANISOU 1887 OE2 GLU B 241 9711 9225 7105 -1444 -3487 -521 O ATOM 1888 N PRO A 242 54.024 59.677 30.278 1.00 30.69 N ANISOU 1888 N PRO B 242 4110 4639 2911 -380 -720 663 N ATOM 1889 CA PRO A 242 53.390 58.631 31.074 1.00 31.27 C ANISOU 1889 CA PRO B 242 4644 4100 3136 -448 -489 889 C ATOM 1890 C PRO A 242 53.585 57.233 30.492 1.00 29.98 C ANISOU 1890 C PRO B 242 4208 4477 2705 -484 -265 214 C ATOM 1891 O PRO A 242 53.532 56.258 31.265 1.00 31.45 O ANISOU 1891 O PRO B 242 4778 4586 2587 -409 303 684 O ATOM 1892 CB PRO A 242 51.904 58.961 31.029 1.00 33.73 C ANISOU 1892 CB PRO B 242 4340 4658 3819 -618 -690 612 C ATOM 1893 CG PRO A 242 51.776 60.323 30.428 1.00 34.64 C ANISOU 1893 CG PRO B 242 4523 4941 3700 -700 -610 174 C ATOM 1894 CD PRO A 242 53.084 60.714 29.835 1.00 34.24 C ANISOU 1894 CD PRO B 242 5007 5146 2856 -1301 125 244 C ATOM 1895 N SER A 243 53.792 57.105 29.185 1.00 29.23 N ANISOU 1895 N SER B 243 3971 4416 2718 -540 -182 61 N ATOM 1896 CA SER A 243 53.972 55.775 28.605 1.00 27.31 C ANISOU 1896 CA SER B 243 3917 4111 2349 -525 14 50 C ATOM 1897 C SER A 243 55.307 55.135 28.987 1.00 27.62 C ANISOU 1897 C SER B 243 3848 3712 2935 -250 285 29 C ATOM 1898 O SER A 243 55.513 53.936 28.769 1.00 26.17 O ANISOU 1898 O SER B 243 3898 3493 2554 -331 352 425 O ATOM 1899 CB SER A 243 53.861 55.864 27.074 1.00 29.73 C ANISOU 1899 CB SER B 243 4950 3969 2378 -585 1 256 C ATOM 1900 OG SER A 243 55.065 56.401 26.526 1.00 27.83 O ANISOU 1900 OG SER B 243 3599 4346 2629 -370 39 -250 O ATOM 1901 N THR A 244 56.235 55.920 29.542 1.00 26.75 N ANISOU 1901 N THR B 244 3617 3871 2676 -168 129 104 N ATOM 1902 CA THR A 244 57.579 55.418 29.808 1.00 27.91 C ANISOU 1902 CA THR B 244 4136 3994 2473 -596 -30 87 C ATOM 1903 C THR A 244 57.735 54.781 31.190 1.00 25.34 C ANISOU 1903 C THR B 244 3259 3619 2751 131 26 212 C ATOM 1904 O THR A 244 58.888 54.474 31.534 1.00 30.29 O ANISOU 1904 O THR B 244 4601 4276 2633 -678 -13 649 O ATOM 1905 CB THR A 244 58.660 56.521 29.727 1.00 28.25 C ANISOU 1905 CB THR B 244 4132 4062 2537 -640 618 -320 C ATOM 1906 OG1 THR A 244 58.388 57.503 30.745 1.00 31.66 O ANISOU 1906 OG1 THR B 244 4688 4038 3302 -486 317 809 O ATOM 1907 CG2 THR A 244 58.682 57.231 28.372 1.00 32.74 C ANISOU 1907 CG2 THR B 244 4748 4681 3012 -1123 1583 -177 C ATOM 1908 N MET A 245 56.669 54.586 31.947 1.00 27.73 N ANISOU 1908 N MET B 245 3833 3638 3063 254 323 -141 N ATOM 1909 CA MET A 245 56.684 54.166 33.347 1.00 29.15 C ANISOU 1909 CA MET B 245 3841 4124 3111 -106 489 -229 C ATOM 1910 C MET A 245 57.395 52.836 33.597 1.00 28.19 C ANISOU 1910 C MET B 245 3793 3985 2932 -127 329 146 C ATOM 1911 O MET A 245 57.994 52.625 34.667 1.00 28.07 O ANISOU 1911 O MET B 245 3395 4168 3100 -545 -121 637 O ATOM 1912 CB MET A 245 55.254 54.037 33.924 1.00 32.08 C ANISOU 1912 CB MET B 245 4907 4979 2302 -1388 557 16 C ATOM 1913 CG MET A 245 54.564 55.360 34.202 1.00 33.99 C ANISOU 1913 CG MET B 245 4894 4983 3038 -1511 528 382 C ATOM 1914 SD MET A 245 55.474 56.473 35.299 1.00 43.11 S ANISOU 1914 SD MET B 245 7059 5708 3614 -496 -528 370 S ATOM 1915 CE MET A 245 56.319 57.574 34.169 1.00 42.86 C ANISOU 1915 CE MET B 245 5039 5972 5272 -297 -1271 -500 C ATOM 1916 N GLU A 246 57.337 51.895 32.661 1.00 27.84 N ANISOU 1916 N GLU B 246 3908 3836 2832 -253 438 416 N ATOM 1917 CA GLU A 246 57.902 50.572 32.899 1.00 27.58 C ANISOU 1917 CA GLU B 246 3866 3777 2835 -124 306 269 C ATOM 1918 C GLU A 246 59.299 50.440 32.317 1.00 27.70 C ANISOU 1918 C GLU B 246 3831 3611 3081 5 87 364 C ATOM 1919 O GLU A 246 59.896 49.360 32.416 1.00 30.01 O ANISOU 1919 O GLU B 246 3882 4391 3127 -343 502 121 O ATOM 1920 CB GLU A 246 56.983 49.515 32.286 1.00 26.55 C ANISOU 1920 CB GLU B 246 3614 3741 2732 -456 483 478 C ATOM 1921 CG GLU A 246 55.595 49.514 32.924 1.00 29.45 C ANISOU 1921 CG GLU B 246 4390 3866 2933 -516 254 251 C ATOM 1922 CD GLU A 246 55.558 48.765 34.238 1.00 29.68 C ANISOU 1922 CD GLU B 246 3787 4147 3342 -285 257 -45 C ATOM 1923 OE1 GLU A 246 56.622 48.248 34.661 1.00 32.95 O ANISOU 1923 OE1 GLU B 246 4022 4907 3589 -275 356 926 O ATOM 1924 OE2 GLU A 246 54.472 48.688 34.855 1.00 32.32 O ANISOU 1924 OE2 GLU B 246 4831 3772 3677 228 -161 -223 O ATOM 1925 N LEU A 247 59.845 51.495 31.714 1.00 27.85 N ANISOU 1925 N LEU B 247 4243 3797 2543 -168 485 316 N ATOM 1926 CA LEU A 247 61.213 51.419 31.189 1.00 26.84 C ANISOU 1926 CA LEU B 247 4342 3880 1975 -95 222 389 C ATOM 1927 C LEU A 247 62.251 51.615 32.275 1.00 28.12 C ANISOU 1927 C LEU B 247 4599 4000 2084 -399 350 412 C ATOM 1928 O LEU A 247 61.932 52.271 33.271 1.00 27.40 O ANISOU 1928 O LEU B 247 4793 3795 1823 -571 446 390 O ATOM 1929 CB LEU A 247 61.454 52.492 30.112 1.00 26.12 C ANISOU 1929 CB LEU B 247 3883 3889 2151 -158 258 429 C ATOM 1930 CG LEU A 247 60.587 52.394 28.857 1.00 27.37 C ANISOU 1930 CG LEU B 247 4202 4010 2188 143 419 533 C ATOM 1931 CD1 LEU A 247 60.922 53.561 27.924 1.00 25.57 C ANISOU 1931 CD1 LEU B 247 2934 4540 2240 -178 83 230 C ATOM 1932 CD2 LEU A 247 60.802 51.048 28.195 1.00 24.81 C ANISOU 1932 CD2 LEU B 247 3837 3233 2357 45 816 662 C ATOM 1933 N LYS A 248 63.470 51.126 32.112 1.00 28.25 N ANISOU 1933 N LYS B 248 4041 4115 2577 -83 270 586 N ATOM 1934 CA LYS A 248 64.488 51.530 33.086 1.00 27.77 C ANISOU 1934 CA LYS B 248 3864 3955 2733 -359 -276 579 C ATOM 1935 C LYS A 248 64.909 52.976 32.831 1.00 27.06 C ANISOU 1935 C LYS B 248 3758 4145 2381 -282 -377 518 C ATOM 1936 O LYS A 248 64.902 53.434 31.684 1.00 27.94 O ANISOU 1936 O LYS B 248 3636 4469 2510 -630 -64 591 O ATOM 1937 CB LYS A 248 65.734 50.668 33.053 1.00 27.56 C ANISOU 1937 CB LYS B 248 3811 4018 2643 -336 130 12 C ATOM 1938 CG LYS A 248 65.533 49.211 33.462 1.00 30.94 C ANISOU 1938 CG LYS B 248 3946 4092 3718 324 -465 382 C ATOM 1939 CD LYS A 248 66.866 48.509 33.205 1.00 36.79 C ANISOU 1939 CD LYS B 248 3777 4469 5732 267 -268 248 C ATOM 1940 CE LYS A 248 66.754 47.010 33.453 1.00 41.56 C ANISOU 1940 CE LYS B 248 3895 5194 6701 316 1231 655 C ATOM 1941 NZ LYS A 248 67.847 46.586 34.388 1.00 64.44 N ANISOU 1941 NZ LYS B 248 7675 7829 8980 -1186 4287 57 N ATOM 1942 N VAL A 249 65.266 53.671 33.893 1.00 27.82 N ANISOU 1942 N VAL B 249 4064 3966 2541 -418 -418 653 N ATOM 1943 CA VAL A 249 65.764 55.040 33.803 1.00 29.14 C ANISOU 1943 CA VAL B 249 4339 3867 2865 -364 -622 687 C ATOM 1944 C VAL A 249 66.887 55.124 32.792 1.00 29.69 C ANISOU 1944 C VAL B 249 4243 4183 2856 -604 51 363 C ATOM 1945 O VAL A 249 66.988 56.053 31.988 1.00 29.65 O ANISOU 1945 O VAL B 249 4190 4321 2753 -180 -49 692 O ATOM 1946 CB VAL A 249 66.229 55.495 35.205 1.00 30.17 C ANISOU 1946 CB VAL B 249 4621 3819 3023 -532 -573 890 C ATOM 1947 CG1 VAL A 249 67.050 56.773 35.111 1.00 29.07 C ANISOU 1947 CG1 VAL B 249 5318 3551 2176 -649 -309 701 C ATOM 1948 CG2 VAL A 249 65.044 55.689 36.142 1.00 24.16 C ANISOU 1948 CG2 VAL B 249 3130 3405 2647 514 -231 679 C ATOM 1949 N LYS A 250 67.802 54.160 32.764 1.00 27.54 N ANISOU 1949 N LYS B 250 3970 4005 2488 39 -519 338 N ATOM 1950 CA LYS A 250 68.927 54.310 31.819 1.00 27.82 C ANISOU 1950 CA LYS B 250 4165 3806 2600 -394 167 308 C ATOM 1951 C LYS A 250 68.507 54.136 30.362 1.00 27.22 C ANISOU 1951 C LYS B 250 4222 3668 2452 -25 224 26 C ATOM 1952 O LYS A 250 69.147 54.657 29.422 1.00 28.24 O ANISOU 1952 O LYS B 250 3419 4438 2873 -240 412 -535 O ATOM 1953 CB LYS A 250 70.033 53.300 32.126 1.00 30.23 C ANISOU 1953 CB LYS B 250 4164 4250 3073 -540 123 477 C ATOM 1954 CG LYS A 250 69.552 51.850 31.972 1.00 31.70 C ANISOU 1954 CG LYS B 250 4092 4896 3057 -244 -261 487 C ATOM 1955 CD LYS A 250 70.780 50.950 32.125 1.00 35.06 C ANISOU 1955 CD LYS B 250 4216 5425 3681 -254 811 324 C ATOM 1956 CE LYS A 250 70.440 49.496 31.861 1.00 36.44 C ANISOU 1956 CE LYS B 250 4030 6135 3681 24 798 111 C ATOM 1957 NZ LYS A 250 71.641 48.643 32.082 1.00 41.29 N ANISOU 1957 NZ LYS B 250 4044 7263 4381 -820 -949 157 N ATOM 1958 N THR A 251 67.431 53.378 30.149 1.00 27.37 N ANISOU 1958 N THR B 251 3712 3797 2891 137 196 475 N ATOM 1959 CA THR A 251 66.926 53.194 28.794 1.00 31.40 C ANISOU 1959 CA THR B 251 4784 4275 2872 -274 472 537 C ATOM 1960 C THR A 251 66.370 54.510 28.272 1.00 29.52 C ANISOU 1960 C THR B 251 4861 3738 2619 -202 455 249 C ATOM 1961 O THR A 251 66.653 54.915 27.146 1.00 32.25 O ANISOU 1961 O THR B 251 5614 3891 2749 -72 548 83 O ATOM 1962 CB THR A 251 65.798 52.150 28.776 1.00 28.46 C ANISOU 1962 CB THR B 251 4228 4524 2061 80 99 797 C ATOM 1963 OG1 THR A 251 66.328 50.913 29.251 1.00 29.70 O ANISOU 1963 OG1 THR B 251 4389 4539 2356 -373 456 437 O ATOM 1964 CG2 THR A 251 65.290 51.936 27.348 1.00 31.07 C ANISOU 1964 CG2 THR B 251 5112 4743 1949 -1025 259 640 C ATOM 1965 N LEU A 252 65.570 55.160 29.124 1.00 29.85 N ANISOU 1965 N LEU B 252 4893 3879 2568 -589 377 794 N ATOM 1966 CA LEU A 252 64.972 56.441 28.739 1.00 34.76 C ANISOU 1966 CA LEU B 252 4921 5004 3281 -1060 667 206 C ATOM 1967 C LEU A 252 66.069 57.475 28.543 1.00 33.21 C ANISOU 1967 C LEU B 252 3835 5125 3657 -622 356 619 C ATOM 1968 O LEU A 252 66.074 58.273 27.598 1.00 35.21 O ANISOU 1968 O LEU B 252 4810 5168 3402 -383 402 545 O ATOM 1969 CB LEU A 252 63.911 56.837 29.773 1.00 36.74 C ANISOU 1969 CB LEU B 252 5077 5825 3058 -1259 574 306 C ATOM 1970 CG LEU A 252 63.033 58.044 29.441 1.00 39.19 C ANISOU 1970 CG LEU B 252 5216 5905 3768 -1667 697 -49 C ATOM 1971 CD1 LEU A 252 62.266 57.828 28.127 1.00 34.52 C ANISOU 1971 CD1 LEU B 252 4461 5526 3128 -1047 903 -630 C ATOM 1972 CD2 LEU A 252 62.105 58.392 30.607 1.00 35.04 C ANISOU 1972 CD2 LEU B 252 4735 5034 3545 -297 241 214 C ATOM 1973 N ARG A 253 67.080 57.496 29.407 1.00 36.36 N ANISOU 1973 N ARG B 253 5121 5135 3561 -1103 453 433 N ATOM 1974 CA ARG A 253 68.219 58.409 29.300 1.00 38.59 C ANISOU 1974 CA ARG B 253 6027 5184 3451 -732 264 695 C ATOM 1975 C ARG A 253 69.036 58.185 28.029 1.00 38.93 C ANISOU 1975 C ARG B 253 6532 4733 3528 -872 285 679 C ATOM 1976 O ARG A 253 69.490 59.131 27.370 1.00 43.82 O ANISOU 1976 O ARG B 253 8345 4533 3773 -354 382 699 O ATOM 1977 CB ARG A 253 69.100 58.274 30.570 1.00 39.74 C ANISOU 1977 CB ARG B 253 6022 5503 3574 -39 425 1090 C ATOM 1978 CG ARG A 253 70.335 59.148 30.487 1.00 54.89 C ANISOU 1978 CG ARG B 253 9916 5416 5523 -414 1567 1488 C ATOM 1979 CD ARG A 253 71.377 58.847 31.551 1.00 78.02 C ANISOU 1979 CD ARG B 253 15665 7538 6442 -2471 1999 2875 C ATOM 1980 NE ARG A 253 71.502 60.003 32.452 1.00 91.76 N ANISOU 1980 NE ARG B 253 18216 8596 8054 -2693 518 4537 N ATOM 1981 CZ ARG A 253 72.520 60.838 32.543 1.00 97.65 C ANISOU 1981 CZ ARG B 253 19916 8465 8723 -3233 -1149 4968 C ATOM 1982 NH1 ARG A 253 73.611 60.699 31.802 1.00111.61 N ANISOU 1982 NH1 ARG B 253 22556 9699 10151 -3763 -1219 3091 N ATOM 1983 NH2 ARG A 253 72.453 61.842 33.420 1.00109.51 N ANISOU 1983 NH2 ARG B 253 21238 10420 9950 -2615 -1744 6339 N ATOM 1984 N TYR A 254 69.250 56.925 27.644 1.00 37.12 N ANISOU 1984 N TYR B 254 6131 4846 3126 -1609 379 1414 N ATOM 1985 CA TYR A 254 69.957 56.567 26.422 1.00 35.87 C ANISOU 1985 CA TYR B 254 5615 4834 3181 -1309 945 472 C ATOM 1986 C TYR A 254 69.303 57.135 25.162 1.00 37.91 C ANISOU 1986 C TYR B 254 6403 4597 3404 -1551 1324 326 C ATOM 1987 O TYR A 254 69.936 57.735 24.269 1.00 40.95 O ANISOU 1987 O TYR B 254 6914 4843 3804 -1788 1812 35 O ATOM 1988 CB TYR A 254 70.040 55.039 26.302 1.00 36.39 C ANISOU 1988 CB TYR B 254 5681 4772 3376 -1304 537 241 C ATOM 1989 CG TYR A 254 70.574 54.566 24.957 1.00 38.96 C ANISOU 1989 CG TYR B 254 6344 4956 3504 -1260 251 145 C ATOM 1990 CD1 TYR A 254 71.926 54.707 24.641 1.00 39.58 C ANISOU 1990 CD1 TYR B 254 6319 5114 3605 -1409 243 101 C ATOM 1991 CD2 TYR A 254 69.744 53.975 24.002 1.00 38.99 C ANISOU 1991 CD2 TYR B 254 6008 5015 3791 -1020 -21 264 C ATOM 1992 CE1 TYR A 254 72.436 54.281 23.423 1.00 39.41 C ANISOU 1992 CE1 TYR B 254 5976 4999 3999 -1329 -150 339 C ATOM 1993 CE2 TYR A 254 70.239 53.545 22.782 1.00 38.40 C ANISOU 1993 CE2 TYR B 254 5911 4858 3822 -1107 9 202 C ATOM 1994 CZ TYR A 254 71.584 53.700 22.499 1.00 40.32 C ANISOU 1994 CZ TYR B 254 6003 4892 4425 -1207 -391 446 C ATOM 1995 OH TYR A 254 72.103 53.283 21.299 1.00 45.13 O ANISOU 1995 OH TYR B 254 8431 4773 3942 -2493 -374 763 O ATOM 1996 N PHE A 255 67.977 56.926 25.067 1.00 35.08 N ANISOU 1996 N PHE B 255 5750 4409 3169 -1228 493 761 N ATOM 1997 CA PHE A 255 67.289 57.396 23.868 1.00 35.31 C ANISOU 1997 CA PHE B 255 6118 3955 3345 -899 881 713 C ATOM 1998 C PHE A 255 67.115 58.907 23.912 1.00 37.20 C ANISOU 1998 C PHE B 255 6690 3719 3723 -226 1206 146 C ATOM 1999 O PHE A 255 67.089 59.559 22.863 1.00 43.90 O ANISOU 1999 O PHE B 255 7467 5107 4107 -410 1880 93 O ATOM 2000 CB PHE A 255 65.921 56.719 23.723 1.00 30.76 C ANISOU 2000 CB PHE B 255 5648 3871 2168 -513 606 429 C ATOM 2001 CG PHE A 255 66.069 55.262 23.311 1.00 32.15 C ANISOU 2001 CG PHE B 255 5329 4350 2537 -747 575 341 C ATOM 2002 CD1 PHE A 255 66.423 54.952 22.005 1.00 32.72 C ANISOU 2002 CD1 PHE B 255 5091 4551 2790 -971 383 146 C ATOM 2003 CD2 PHE A 255 65.859 54.226 24.201 1.00 33.72 C ANISOU 2003 CD2 PHE B 255 5637 4575 2600 -310 721 593 C ATOM 2004 CE1 PHE A 255 66.570 53.627 21.597 1.00 33.26 C ANISOU 2004 CE1 PHE B 255 5722 4267 2648 -363 397 298 C ATOM 2005 CE2 PHE A 255 66.001 52.908 23.806 1.00 33.15 C ANISOU 2005 CE2 PHE B 255 5674 4244 2679 -442 398 229 C ATOM 2006 CZ PHE A 255 66.346 52.592 22.500 1.00 33.28 C ANISOU 2006 CZ PHE B 255 5897 4050 2699 -507 396 102 C ATOM 2007 N ASN A 256 66.984 59.464 25.114 1.00 37.09 N ANISOU 2007 N ASN B 256 6241 3836 4015 42 1174 699 N ATOM 2008 CA ASN A 256 66.850 60.908 25.239 1.00 42.58 C ANISOU 2008 CA ASN B 256 6272 5204 4702 471 1442 342 C ATOM 2009 C ASN A 256 68.143 61.575 24.788 1.00 43.82 C ANISOU 2009 C ASN B 256 5694 5102 5854 798 1520 286 C ATOM 2010 O ASN A 256 68.047 62.684 24.256 1.00 49.55 O ANISOU 2010 O ASN B 256 5990 5059 7777 1151 2251 909 O ATOM 2011 CB ASN A 256 66.514 61.377 26.654 1.00 45.84 C ANISOU 2011 CB ASN B 256 7020 5227 5172 1072 563 854 C ATOM 2012 CG ASN A 256 65.021 61.618 26.798 1.00 51.15 C ANISOU 2012 CG ASN B 256 7453 6339 5643 319 -365 978 C ATOM 2013 OD1 ASN A 256 64.436 62.565 26.255 1.00 63.15 O ANISOU 2013 OD1 ASN B 256 7543 8146 8305 -609 370 -352 O ATOM 2014 ND2 ASN A 256 64.375 60.723 27.526 1.00 59.01 N ANISOU 2014 ND2 ASN B 256 10319 7443 4660 -2024 1467 -407 N ATOM 2015 N GLU A 257 69.282 60.907 24.989 1.00 43.26 N ANISOU 2015 N GLU B 257 6315 5509 4613 250 2117 -95 N ATOM 2016 CA GLU A 257 70.522 61.524 24.506 1.00 46.91 C ANISOU 2016 CA GLU B 257 6788 5798 5238 -98 2812 -601 C ATOM 2017 C GLU A 257 70.724 61.262 23.022 1.00 49.57 C ANISOU 2017 C GLU B 257 8194 5336 5303 -921 2507 -405 C ATOM 2018 O GLU A 257 71.094 62.130 22.218 1.00 49.09 O ANISOU 2018 O GLU B 257 8394 5604 4654 -481 2513 81 O ATOM 2019 CB GLU A 257 71.680 61.030 25.389 1.00 57.48 C ANISOU 2019 CB GLU B 257 9569 6628 5642 -1616 3645 -717 C ATOM 2020 CG GLU A 257 71.434 61.408 26.859 1.00 69.57 C ANISOU 2020 CG GLU B 257 11906 8594 5933 -2785 2731 806 C ATOM 2021 CD GLU A 257 72.544 60.977 27.790 1.00 79.02 C ANISOU 2021 CD GLU B 257 13844 9722 6456 -4129 2561 1566 C ATOM 2022 OE1 GLU A 257 73.365 60.136 27.351 1.00 96.05 O ANISOU 2022 OE1 GLU B 257 16292 11402 8801 -8311 1429 2019 O ATOM 2023 OE2 GLU A 257 72.632 61.460 28.949 1.00 89.60 O ANISOU 2023 OE2 GLU B 257 17551 9594 6899 -4298 1870 2295 O ATOM 2024 N LEU A 258 70.479 60.039 22.565 1.00 47.38 N ANISOU 2024 N LEU B 258 8517 4891 4593 -940 2611 -410 N ATOM 2025 CA LEU A 258 70.653 59.713 21.164 1.00 50.87 C ANISOU 2025 CA LEU B 258 9305 5186 4839 -1285 2010 -881 C ATOM 2026 C LEU A 258 69.754 60.510 20.229 1.00 50.46 C ANISOU 2026 C LEU B 258 9888 5220 4064 -1167 1960 -398 C ATOM 2027 O LEU A 258 70.036 60.682 19.039 1.00 56.43 O ANISOU 2027 O LEU B 258 11745 5327 4367 -475 2277 -1063 O ATOM 2028 CB LEU A 258 70.378 58.207 21.020 1.00 51.82 C ANISOU 2028 CB LEU B 258 9073 5350 5265 -1419 867 -1596 C ATOM 2029 CG LEU A 258 70.524 57.629 19.610 1.00 55.99 C ANISOU 2029 CG LEU B 258 10130 5524 5618 -1907 118 -1687 C ATOM 2030 CD1 LEU A 258 71.985 57.678 19.192 1.00 64.99 C ANISOU 2030 CD1 LEU B 258 12598 5423 6671 -2252 -809 -1670 C ATOM 2031 CD2 LEU A 258 70.003 56.201 19.526 1.00 50.86 C ANISOU 2031 CD2 LEU B 258 8474 5253 5598 -2781 244 -1079 C ATOM 2032 N GLU A 259 68.615 61.029 20.691 1.00 46.86 N ANISOU 2032 N GLU B 259 8842 4555 4407 -487 1357 1040 N ATOM 2033 CA GLU A 259 67.665 61.605 19.732 1.00 45.60 C ANISOU 2033 CA GLU B 259 8904 4446 3977 14 1545 864 C ATOM 2034 C GLU A 259 67.476 63.081 20.030 1.00 49.17 C ANISOU 2034 C GLU B 259 8743 5471 4468 -133 1080 653 C ATOM 2035 O GLU A 259 66.605 63.761 19.482 1.00 48.07 O ANISOU 2035 O GLU B 259 8710 5793 3760 -122 724 1091 O ATOM 2036 CB GLU A 259 66.355 60.800 19.803 1.00 46.80 C ANISOU 2036 CB GLU B 259 8304 4519 4958 -451 4472 -385 C ATOM 2037 CG GLU A 259 65.707 60.622 18.422 1.00 57.76 C ANISOU 2037 CG GLU B 259 11515 4176 6255 -917 2905 1180 C ATOM 2038 CD GLU A 259 66.169 59.359 17.729 1.00 55.12 C ANISOU 2038 CD GLU B 259 11185 3572 6186 -78 3406 341 C ATOM 2039 OE1 GLU A 259 66.707 59.445 16.628 1.00 65.96 O ANISOU 2039 OE1 GLU B 259 14529 6178 4355 450 2391 1987 O ATOM 2040 OE2 GLU A 259 66.069 58.249 18.279 1.00 69.79 O ANISOU 2040 OE2 GLU B 259 9600 4789 12129 -2508 6009 -1473 O ATOM 2041 N ALA A 260 68.321 63.586 20.948 1.00 44.52 N ANISOU 2041 N ALA B 260 7647 4863 4406 659 1995 297 N ATOM 2042 CA ALA A 260 68.175 64.962 21.408 1.00 46.86 C ANISOU 2042 CA ALA B 260 7440 5203 5160 694 2246 501 C ATOM 2043 C ALA A 260 68.084 65.989 20.285 1.00 49.08 C ANISOU 2043 C ALA B 260 7882 5158 5608 701 2566 260 C ATOM 2044 O ALA A 260 67.273 66.912 20.320 1.00 49.48 O ANISOU 2044 O ALA B 260 7474 4853 6474 1891 2292 -515 O ATOM 2045 CB ALA A 260 69.341 65.345 22.319 1.00 45.90 C ANISOU 2045 CB ALA B 260 7330 5013 5096 694 1846 434 C ATOM 2046 N GLU A 261 68.927 65.840 19.277 1.00 49.76 N ANISOU 2046 N GLU B 261 8015 5128 5762 1212 2289 43 N ATOM 2047 CA GLU A 261 69.000 66.855 18.224 1.00 58.83 C ANISOU 2047 CA GLU B 261 10236 5801 6317 766 3757 -241 C ATOM 2048 C GLU A 261 67.725 66.839 17.388 1.00 57.24 C ANISOU 2048 C GLU B 261 9715 5717 6317 1168 3269 162 C ATOM 2049 O GLU A 261 67.336 67.819 16.753 1.00 52.72 O ANISOU 2049 O GLU B 261 9668 4880 5484 1062 2959 9 O ATOM 2050 CB GLU A 261 70.220 66.619 17.339 1.00 65.59 C ANISOU 2050 CB GLU B 261 11761 5403 7757 725 3823 -1336 C ATOM 2051 CG GLU A 261 71.401 67.546 17.498 1.00 78.63 C ANISOU 2051 CG GLU B 261 14955 5645 9274 230 1777 93 C ATOM 2052 CD GLU A 261 71.253 68.770 18.382 1.00 90.73 C ANISOU 2052 CD GLU B 261 17714 6934 9826 -99 89 1602 C ATOM 2053 OE1 GLU A 261 70.901 69.873 17.892 1.00 93.00 O ANISOU 2053 OE1 GLU B 261 17444 7105 10786 2597 -995 2857 O ATOM 2054 OE2 GLU A 261 71.509 68.654 19.608 1.00105.06 O ANISOU 2054 OE2 GLU B 261 22097 7991 9831 -725 257 1875 O ATOM 2055 N ASN A 262 67.102 65.661 17.426 1.00 55.39 N ANISOU 2055 N ASN B 262 8542 6013 6493 1073 2350 -29 N ATOM 2056 CA ASN A 262 65.942 65.384 16.595 1.00 49.60 C ANISOU 2056 CA ASN B 262 7153 5570 6124 1345 2237 -416 C ATOM 2057 C ASN A 262 64.635 65.725 17.278 1.00 51.02 C ANISOU 2057 C ASN B 262 6661 6390 6334 1264 2201 -590 C ATOM 2058 O ASN A 262 63.571 65.554 16.677 1.00 50.52 O ANISOU 2058 O ASN B 262 5771 7727 5697 206 2684 -634 O ATOM 2059 CB ASN A 262 65.900 63.889 16.217 1.00 44.56 C ANISOU 2059 CB ASN B 262 6658 5448 4826 1299 2615 -1416 C ATOM 2060 CG ASN A 262 67.165 63.456 15.506 1.00 50.37 C ANISOU 2060 CG ASN B 262 7736 5882 5522 772 1870 -1257 C ATOM 2061 OD1 ASN A 262 67.605 64.134 14.579 1.00 60.86 O ANISOU 2061 OD1 ASN B 262 7865 6632 8626 255 2311 -3505 O ATOM 2062 ND2 ASN A 262 67.771 62.352 15.906 1.00 53.11 N ANISOU 2062 ND2 ASN B 262 7280 5719 7181 968 1356 -2464 N ATOM 2063 N ILE A 263 64.661 66.174 18.533 1.00 54.88 N ANISOU 2063 N ILE B 263 7854 6657 6339 921 1957 -511 N ATOM 2064 CA ILE A 263 63.314 66.391 19.087 1.00 58.84 C ANISOU 2064 CA ILE B 263 9072 7101 6182 199 1693 -315 C ATOM 2065 C ILE A 263 63.125 67.861 19.398 1.00 61.53 C ANISOU 2065 C ILE B 263 8805 8054 6522 -134 1228 -518 C ATOM 2066 O ILE A 263 62.268 68.280 20.169 1.00 73.30 O ANISOU 2066 O ILE B 263 11969 8937 6945 -1392 -1345 1505 O ATOM 2067 CB ILE A 263 63.096 65.519 20.318 1.00 60.11 C ANISOU 2067 CB ILE B 263 9075 7875 5889 -323 1516 -647 C ATOM 2068 CG1 ILE A 263 64.143 65.753 21.407 1.00 60.97 C ANISOU 2068 CG1 ILE B 263 8141 8593 6432 -189 1709 -123 C ATOM 2069 CG2 ILE A 263 63.088 64.044 19.961 1.00 53.81 C ANISOU 2069 CG2 ILE B 263 7700 7705 5041 -1213 2539 -212 C ATOM 2070 CD1 ILE A 263 64.750 64.417 21.809 1.00 73.31 C ANISOU 2070 CD1 ILE B 263 6995 13184 7674 -2081 804 -698 C ATOM 2071 N LYS A 264 63.958 68.679 18.763 1.00 68.81 N ANISOU 2071 N LYS B 264 9647 7885 8611 823 2206 -294 N ATOM 2072 CA LYS A 264 63.775 70.128 18.876 1.00 76.55 C ANISOU 2072 CA LYS B 264 9629 8575 10881 860 1904 544 C ATOM 2073 C LYS A 264 62.852 70.662 17.785 1.00 77.52 C ANISOU 2073 C LYS B 264 8825 8920 11709 1188 1942 1056 C ATOM 2074 O LYS A 264 62.822 70.218 16.639 1.00 75.36 O ANISOU 2074 O LYS B 264 8680 8512 11443 798 2272 1025 O ATOM 2075 CB LYS A 264 65.139 70.824 18.836 1.00 76.51 C ANISOU 2075 CB LYS B 264 8786 8559 11725 1096 2521 342 C ATOM 2076 CG LYS A 264 66.269 70.038 19.487 1.00 80.69 C ANISOU 2076 CG LYS B 264 9279 9173 12207 413 2836 -39 C ATOM 2077 CD LYS A 264 67.620 70.674 19.187 1.00 78.42 C ANISOU 2077 CD LYS B 264 8394 9101 12301 798 3041 -22 C ATOM 2078 CE LYS A 264 68.493 70.672 20.433 1.00 78.43 C ANISOU 2078 CE LYS B 264 8762 8938 12101 682 3169 -309 C ATOM 2079 NZ LYS A 264 68.153 69.534 21.333 1.00 84.34 N ANISOU 2079 NZ LYS B 264 9861 10332 11853 -92 2924 -2156 N ATOM 2080 N GLY A 265 62.051 71.665 18.141 1.00 83.82 N ANISOU 2080 N GLY B 265 9209 9687 12953 641 1313 1474 N ATOM 2081 CA GLY A 265 61.158 72.283 17.170 1.00 83.43 C ANISOU 2081 CA GLY B 265 8380 9797 13523 1086 1098 2205 C ATOM 2082 C GLY A 265 59.879 71.467 17.043 1.00 87.07 C ANISOU 2082 C GLY B 265 9740 9860 13482 955 155 2653 C ATOM 2083 O GLY A 265 58.783 72.001 17.224 1.00 86.51 O ANISOU 2083 O GLY B 265 9490 9550 13831 1140 650 2459 O ATOM 2084 N LEU A 266 60.083 70.190 16.740 1.00 87.12 N ANISOU 2084 N LEU B 266 10153 9542 13408 970 -584 2410 N ATOM 2085 CA LEU A 266 59.011 69.213 16.591 1.00 89.29 C ANISOU 2085 CA LEU B 266 11062 9587 13277 985 -987 2797 C ATOM 2086 C LEU A 266 58.324 69.323 15.236 1.00 94.29 C ANISOU 2086 C LEU B 266 12132 10436 13258 560 -957 2916 C ATOM 2087 O LEU A 266 57.821 70.338 14.762 1.00101.99 O ANISOU 2087 O LEU B 266 13306 11900 13546 462 432 1647 O ATOM 2088 CB LEU A 266 58.010 69.364 17.740 1.00 91.54 C ANISOU 2088 CB LEU B 266 12387 9172 13221 91 -931 3141 C ATOM 2089 CG LEU A 266 58.431 68.802 19.097 1.00 90.13 C ANISOU 2089 CG LEU B 266 12137 8943 13166 180 -1012 3032 C ATOM 2090 CD1 LEU A 266 59.178 67.497 18.915 1.00 80.49 C ANISOU 2090 CD1 LEU B 266 12358 8433 9792 236 -1914 3047 C ATOM 2091 CD2 LEU A 266 59.284 69.798 19.869 1.00 86.96 C ANISOU 2091 CD2 LEU B 266 10986 9425 12628 351 -1463 2828 C ATOM 2092 OXT LEU A 266 58.801 67.838 15.393 1.00 99.16 O ANISOU 2092 OXT LEU B 266 11642 11558 14475 367 -2546 3302 O TER 2093 LEU B 266 ATOM 1 N MET A 1 50.231 31.955 15.764 1.00 38.92 N ANISOU 1 N MET C 1 5098 6097 3592 -1489 447 362 N ATOM 2 CA MET A 1 50.372 30.569 16.187 1.00 39.64 C ANISOU 2 CA MET C 1 4671 6407 3983 -879 140 -405 C ATOM 3 C MET A 1 49.054 30.144 16.820 1.00 37.92 C ANISOU 3 C MET C 1 4914 5679 3813 -933 633 -168 C ATOM 4 O MET A 1 48.445 30.963 17.535 1.00 46.58 O ANISOU 4 O MET C 1 5309 7754 4636 -2033 -63 1256 O ATOM 5 CB MET A 1 51.506 30.373 17.200 1.00 40.12 C ANISOU 5 CB MET C 1 4934 6308 4004 -354 -109 -293 C ATOM 6 CG MET A 1 51.475 28.964 17.786 1.00 43.45 C ANISOU 6 CG MET C 1 5363 6642 4505 -613 -169 -839 C ATOM 7 SD MET A 1 52.722 28.700 19.088 1.00 40.76 S ANISOU 7 SD MET C 1 5716 5321 4449 -844 351 -81 S ATOM 8 CE MET A 1 54.168 28.701 17.975 1.00 40.89 C ANISOU 8 CE MET C 1 5132 5850 4556 -1337 -1383 -497 C ATOM 9 N ARG A 2 48.623 28.920 16.569 1.00 32.45 N ANISOU 9 N ARG C 2 4810 4307 3211 -795 419 -513 N ATOM 10 CA ARG A 2 47.410 28.444 17.234 1.00 31.91 C ANISOU 10 CA ARG C 2 5037 4272 2817 -1111 367 -36 C ATOM 11 C ARG A 2 47.832 27.436 18.296 1.00 31.66 C ANISOU 11 C ARG C 2 4806 4445 2778 -1169 640 -178 C ATOM 12 O ARG A 2 48.811 26.716 18.126 1.00 35.19 O ANISOU 12 O ARG C 2 5848 4297 3224 -928 50 -345 O ATOM 13 CB ARG A 2 46.430 27.845 16.232 1.00 30.78 C ANISOU 13 CB ARG C 2 5683 3264 2747 -322 224 278 C ATOM 14 CG ARG A 2 45.962 28.789 15.130 1.00 31.74 C ANISOU 14 CG ARG C 2 6052 3464 2546 -297 -63 449 C ATOM 15 CD ARG A 2 45.131 28.043 14.088 1.00 34.98 C ANISOU 15 CD ARG C 2 6719 3922 2652 -266 253 153 C ATOM 16 NE ARG A 2 43.885 27.557 14.691 1.00 34.41 N ANISOU 16 NE ARG C 2 6379 4594 2103 -53 429 -191 N ATOM 17 CZ ARG A 2 43.075 26.666 14.154 1.00 36.03 C ANISOU 17 CZ ARG C 2 5807 4903 2981 -919 503 344 C ATOM 18 NH1 ARG A 2 43.392 26.162 12.980 1.00 40.91 N ANISOU 18 NH1 ARG C 2 6260 5762 3522 -1418 799 915 N ATOM 19 NH2 ARG A 2 41.959 26.264 14.749 1.00 34.88 N ANISOU 19 NH2 ARG C 2 5784 4351 3119 -751 335 -382 N ATOM 20 N LEU A 3 47.104 27.408 19.404 1.00 31.74 N ANISOU 20 N LEU C 3 4926 4478 2657 -969 591 -365 N ATOM 21 CA LEU A 3 47.265 26.362 20.403 1.00 30.10 C ANISOU 21 CA LEU C 3 4287 4342 2806 -471 790 -760 C ATOM 22 C LEU A 3 45.901 25.669 20.526 1.00 29.83 C ANISOU 22 C LEU C 3 4583 3777 2975 -455 909 -446 C ATOM 23 O LEU A 3 44.942 26.382 20.826 1.00 32.73 O ANISOU 23 O LEU C 3 5431 3887 3119 -772 569 -246 O ATOM 24 CB LEU A 3 47.737 26.888 21.755 1.00 28.39 C ANISOU 24 CB LEU C 3 3943 4351 2491 -526 530 -177 C ATOM 25 CG LEU A 3 47.832 25.895 22.922 1.00 30.84 C ANISOU 25 CG LEU C 3 4457 4660 2600 -868 475 -330 C ATOM 26 CD1 LEU A 3 48.856 24.819 22.640 1.00 32.59 C ANISOU 26 CD1 LEU C 3 4263 4270 3850 -374 15 -436 C ATOM 27 CD2 LEU A 3 48.218 26.596 24.214 1.00 31.39 C ANISOU 27 CD2 LEU C 3 3956 5259 2710 -90 417 -825 C ATOM 28 N ILE A 4 45.860 24.370 20.272 1.00 29.63 N ANISOU 28 N ILE C 4 4344 3841 3072 -259 982 -342 N ATOM 29 CA ILE A 4 44.615 23.619 20.403 1.00 29.55 C ANISOU 29 CA ILE C 4 4606 3487 3133 -143 936 162 C ATOM 30 C ILE A 4 44.694 22.814 21.691 1.00 30.18 C ANISOU 30 C ILE C 4 4166 4260 3043 -442 1143 178 C ATOM 31 O ILE A 4 45.373 21.772 21.761 1.00 32.25 O ANISOU 31 O ILE C 4 4551 4378 3323 -649 453 454 O ATOM 32 CB ILE A 4 44.361 22.677 19.219 1.00 27.05 C ANISOU 32 CB ILE C 4 3924 3415 2937 -176 550 63 C ATOM 33 CG1 ILE A 4 44.656 23.270 17.840 1.00 29.47 C ANISOU 33 CG1 ILE C 4 4697 3441 3059 -175 216 596 C ATOM 34 CG2 ILE A 4 42.932 22.117 19.281 1.00 27.89 C ANISOU 34 CG2 ILE C 4 4136 3481 2980 -8 132 -560 C ATOM 35 CD1 ILE A 4 43.941 24.560 17.514 1.00 33.52 C ANISOU 35 CD1 ILE C 4 5050 4991 2694 -1287 715 -196 C ATOM 36 N PRO A 5 44.067 23.283 22.757 1.00 32.38 N ANISOU 36 N PRO C 5 4856 4317 3131 -679 830 285 N ATOM 37 CA PRO A 5 44.195 22.605 24.053 1.00 30.96 C ANISOU 37 CA PRO C 5 4547 3924 3290 -305 590 340 C ATOM 38 C PRO A 5 43.123 21.529 24.178 1.00 32.73 C ANISOU 38 C PRO C 5 4676 3912 3847 7 682 -203 C ATOM 39 O PRO A 5 41.936 21.850 24.330 1.00 41.35 O ANISOU 39 O PRO C 5 5900 4187 5623 717 832 -29 O ATOM 40 CB PRO A 5 43.969 23.724 25.062 1.00 31.19 C ANISOU 40 CB PRO C 5 4759 4059 3031 -415 332 559 C ATOM 41 CG PRO A 5 43.631 24.942 24.275 1.00 36.93 C ANISOU 41 CG PRO C 5 6032 5134 2865 -1639 480 549 C ATOM 42 CD PRO A 5 43.220 24.472 22.902 1.00 33.62 C ANISOU 42 CD PRO C 5 5289 4328 3157 -800 506 366 C ATOM 43 N LEU A 6 43.566 20.280 24.100 1.00 33.33 N ANISOU 43 N LEU C 6 4570 4819 3274 -481 776 -193 N ATOM 44 CA LEU A 6 42.659 19.163 24.274 1.00 33.33 C ANISOU 44 CA LEU C 6 4731 4654 3278 -246 525 613 C ATOM 45 C LEU A 6 42.993 18.384 25.537 1.00 31.09 C ANISOU 45 C LEU C 6 4147 4368 3297 279 673 476 C ATOM 46 O LEU A 6 43.949 18.604 26.261 1.00 32.27 O ANISOU 46 O LEU C 6 4119 4542 3601 99 1150 523 O ATOM 47 CB LEU A 6 42.709 18.269 23.012 1.00 30.93 C ANISOU 47 CB LEU C 6 3860 4785 3106 349 44 1093 C ATOM 48 CG LEU A 6 42.266 19.019 21.746 1.00 32.11 C ANISOU 48 CG LEU C 6 4765 4312 3124 71 328 1115 C ATOM 49 CD1 LEU A 6 42.689 18.277 20.486 1.00 35.25 C ANISOU 49 CD1 LEU C 6 5001 5247 3147 -439 1216 761 C ATOM 50 CD2 LEU A 6 40.763 19.285 21.752 1.00 35.77 C ANISOU 50 CD2 LEU C 6 4293 4843 4453 743 779 713 C ATOM 51 N THR A 7 42.153 17.382 25.835 1.00 31.68 N ANISOU 51 N THR C 7 4224 4112 3701 321 509 420 N ATOM 52 CA THR A 7 42.339 16.611 27.054 1.00 33.08 C ANISOU 52 CA THR C 7 4689 4514 3367 118 295 845 C ATOM 53 C THR A 7 43.216 15.390 26.857 1.00 31.24 C ANISOU 53 C THR C 7 3910 4252 3706 464 192 409 C ATOM 54 O THR A 7 44.209 15.290 27.582 1.00 35.37 O ANISOU 54 O THR C 7 6266 4839 2335 243 238 189 O ATOM 55 CB THR A 7 40.971 16.166 27.608 1.00 35.77 C ANISOU 55 CB THR C 7 5099 4124 4366 201 -284 440 C ATOM 56 OG1 THR A 7 40.129 17.322 27.664 1.00 47.75 O ANISOU 56 OG1 THR C 7 8771 4110 5264 -541 -867 1016 O ATOM 57 CG2 THR A 7 41.122 15.642 29.029 1.00 37.28 C ANISOU 57 CG2 THR C 7 4307 5762 4097 -525 -261 1003 C ATOM 58 N THR A 8 42.868 14.498 25.928 1.00 30.84 N ANISOU 58 N THR C 8 4104 4019 3596 438 215 699 N ATOM 59 CA THR A 8 43.556 13.224 25.791 1.00 31.16 C ANISOU 59 CA THR C 8 4406 3978 3457 355 94 571 C ATOM 60 C THR A 8 44.300 13.136 24.451 1.00 30.18 C ANISOU 60 C THR C 8 4125 4102 3240 241 452 507 C ATOM 61 O THR A 8 44.054 13.876 23.508 1.00 31.39 O ANISOU 61 O THR C 8 4238 4017 3672 414 -241 687 O ATOM 62 CB THR A 8 42.581 12.039 25.861 1.00 35.03 C ANISOU 62 CB THR C 8 4296 4909 4104 3 -51 1001 C ATOM 63 OG1 THR A 8 41.760 12.126 24.673 1.00 34.44 O ANISOU 63 OG1 THR C 8 4112 4849 4124 424 677 1479 O ATOM 64 CG2 THR A 8 41.628 12.109 27.046 1.00 37.97 C ANISOU 64 CG2 THR C 8 4096 6196 4135 368 -39 1312 C ATOM 65 N ALA A 9 45.237 12.185 24.418 1.00 32.06 N ANISOU 65 N ALA C 9 4160 4378 3641 -281 174 869 N ATOM 66 CA ALA A 9 45.938 11.845 23.192 1.00 31.04 C ANISOU 66 CA ALA C 9 4421 4042 3330 54 124 490 C ATOM 67 C ALA A 9 44.957 11.460 22.089 1.00 32.92 C ANISOU 67 C ALA C 9 3707 5331 3470 167 -40 180 C ATOM 68 O ALA A 9 45.157 11.789 20.915 1.00 32.03 O ANISOU 68 O ALA C 9 3626 5124 3421 -138 -7 107 O ATOM 69 CB ALA A 9 46.917 10.713 23.456 1.00 30.59 C ANISOU 69 CB ALA C 9 3188 4023 4410 94 -250 811 C ATOM 70 N GLU A 10 43.877 10.744 22.434 1.00 33.85 N ANISOU 70 N GLU C 10 3775 5271 3814 125 16 681 N ATOM 71 CA GLU A 10 42.975 10.326 21.361 1.00 39.43 C ANISOU 71 CA GLU C 10 3560 5969 5451 -195 889 8 C ATOM 72 C GLU A 10 42.329 11.564 20.749 1.00 37.01 C ANISOU 72 C GLU C 10 4141 5260 4661 -46 1227 292 C ATOM 73 O GLU A 10 42.189 11.601 19.527 1.00 32.98 O ANISOU 73 O GLU C 10 3149 4745 4635 151 1622 525 O ATOM 74 CB GLU A 10 41.869 9.384 21.792 1.00 42.67 C ANISOU 74 CB GLU C 10 4032 6783 5397 396 705 329 C ATOM 75 CG GLU A 10 41.720 9.074 23.251 1.00 55.83 C ANISOU 75 CG GLU C 10 6703 8353 6159 -877 -1108 26 C ATOM 76 CD GLU A 10 42.858 8.321 23.906 1.00 68.33 C ANISOU 76 CD GLU C 10 9689 9367 6907 -3509 778 -1069 C ATOM 77 OE1 GLU A 10 43.371 8.855 24.915 1.00 57.50 O ANISOU 77 OE1 GLU C 10 7455 8986 5406 -2363 -1163 -518 O ATOM 78 OE2 GLU A 10 43.216 7.219 23.422 1.00 89.46 O ANISOU 78 OE2 GLU C 10 12970 11278 9744 -5873 3114 -2031 O ATOM 79 N GLN A 11 41.958 12.526 21.586 1.00 33.27 N ANISOU 79 N GLN C 11 4292 4510 3841 620 787 482 N ATOM 80 CA GLN A 11 41.417 13.742 21.005 1.00 33.41 C ANISOU 80 CA GLN C 11 4958 4221 3514 370 560 1011 C ATOM 81 C GLN A 11 42.478 14.471 20.184 1.00 32.06 C ANISOU 81 C GLN C 11 5269 3696 3218 185 402 974 C ATOM 82 O GLN A 11 42.197 15.052 19.130 1.00 32.12 O ANISOU 82 O GLN C 11 4172 4714 3319 -288 990 514 O ATOM 83 CB GLN A 11 40.937 14.729 22.067 1.00 34.19 C ANISOU 83 CB GLN C 11 5234 4412 3344 568 454 1209 C ATOM 84 CG GLN A 11 39.652 14.393 22.799 1.00 37.54 C ANISOU 84 CG GLN C 11 5259 4933 4070 883 549 1570 C ATOM 85 CD GLN A 11 39.449 15.374 23.945 1.00 38.16 C ANISOU 85 CD GLN C 11 6373 4487 3639 963 681 1402 C ATOM 86 OE1 GLN A 11 40.310 15.477 24.813 1.00 42.48 O ANISOU 86 OE1 GLN C 11 6455 5597 4087 -229 922 138 O ATOM 87 NE2 GLN A 11 38.357 16.106 23.965 1.00 52.12 N ANISOU 87 NE2 GLN C 11 9658 4581 5564 324 2102 1353 N ATOM 88 N VAL A 12 43.716 14.495 20.666 1.00 32.02 N ANISOU 88 N VAL C 12 4669 3928 3568 125 474 777 N ATOM 89 CA VAL A 12 44.734 15.188 19.858 1.00 30.86 C ANISOU 89 CA VAL C 12 4315 4473 2937 105 733 602 C ATOM 90 C VAL A 12 44.872 14.542 18.491 1.00 31.72 C ANISOU 90 C VAL C 12 4118 4969 2964 -299 730 513 C ATOM 91 O VAL A 12 44.926 15.208 17.431 1.00 33.07 O ANISOU 91 O VAL C 12 5054 4690 2820 -1018 1080 -72 O ATOM 92 CB VAL A 12 46.077 15.168 20.600 1.00 30.93 C ANISOU 92 CB VAL C 12 4292 4529 2930 249 606 644 C ATOM 93 CG1 VAL A 12 47.250 15.531 19.687 1.00 26.77 C ANISOU 93 CG1 VAL C 12 2518 4821 2832 -406 1004 825 C ATOM 94 CG2 VAL A 12 45.992 16.117 21.799 1.00 27.85 C ANISOU 94 CG2 VAL C 12 4346 3318 2917 63 533 331 C ATOM 95 N GLY A 13 44.947 13.207 18.433 1.00 34.20 N ANISOU 95 N GLY C 13 4049 5732 3212 -520 779 305 N ATOM 96 CA GLY A 13 45.066 12.566 17.110 1.00 29.99 C ANISOU 96 CA GLY C 13 3565 4722 3108 -212 638 236 C ATOM 97 C GLY A 13 43.835 12.839 16.266 1.00 32.48 C ANISOU 97 C GLY C 13 4481 4605 3254 -5 535 274 C ATOM 98 O GLY A 13 43.921 13.028 15.046 1.00 29.43 O ANISOU 98 O GLY C 13 3679 4384 3119 -135 1000 386 O ATOM 99 N LYS A 14 42.628 12.880 16.857 1.00 34.10 N ANISOU 99 N LYS C 14 4805 4698 3454 70 236 279 N ATOM 100 CA LYS A 14 41.476 13.105 15.968 1.00 33.19 C ANISOU 100 CA LYS C 14 3933 4702 3977 -10 646 255 C ATOM 101 C LYS A 14 41.511 14.503 15.380 1.00 32.13 C ANISOU 101 C LYS C 14 3945 4509 3753 -74 844 197 C ATOM 102 O LYS A 14 41.152 14.739 14.227 1.00 30.73 O ANISOU 102 O LYS C 14 3695 4154 3826 518 707 190 O ATOM 103 CB LYS A 14 40.155 12.854 16.707 1.00 35.28 C ANISOU 103 CB LYS C 14 3443 5482 4479 324 1177 812 C ATOM 104 CG LYS A 14 39.906 11.358 16.868 1.00 44.78 C ANISOU 104 CG LYS C 14 3870 7448 5695 -306 234 716 C ATOM 105 CD LYS A 14 38.841 10.995 17.881 1.00 51.11 C ANISOU 105 CD LYS C 14 4335 7781 7302 381 -432 799 C ATOM 106 CE LYS A 14 38.463 9.518 17.790 1.00 59.42 C ANISOU 106 CE LYS C 14 4853 9178 8545 -1037 -1909 511 C ATOM 107 NZ LYS A 14 38.997 8.722 18.938 1.00 82.88 N ANISOU 107 NZ LYS C 14 9491 12124 9874 -4405 -260 -1517 N ATOM 108 N TRP A 15 41.949 15.453 16.188 1.00 32.83 N ANISOU 108 N TRP C 15 3964 4686 3826 16 920 319 N ATOM 109 CA TRP A 15 41.979 16.851 15.770 1.00 31.38 C ANISOU 109 CA TRP C 15 3957 4475 3492 36 838 671 C ATOM 110 C TRP A 15 42.990 17.019 14.644 1.00 30.90 C ANISOU 110 C TRP C 15 4466 4001 3273 -274 838 651 C ATOM 111 O TRP A 15 42.737 17.609 13.587 1.00 30.21 O ANISOU 111 O TRP C 15 3919 3861 3699 -145 576 482 O ATOM 112 CB TRP A 15 42.318 17.813 16.946 1.00 32.35 C ANISOU 112 CB TRP C 15 4518 4618 3156 -598 816 601 C ATOM 113 CG TRP A 15 41.967 19.238 16.554 1.00 32.69 C ANISOU 113 CG TRP C 15 4393 4590 3440 -423 1089 0 C ATOM 114 CD1 TRP A 15 40.818 19.908 16.869 1.00 33.69 C ANISOU 114 CD1 TRP C 15 4677 4557 3565 -529 1072 -65 C ATOM 115 CD2 TRP A 15 42.760 20.159 15.778 1.00 33.36 C ANISOU 115 CD2 TRP C 15 4267 4495 3913 -175 1017 -585 C ATOM 116 NE1 TRP A 15 40.839 21.183 16.343 1.00 35.12 N ANISOU 116 NE1 TRP C 15 4626 4609 4109 -443 1009 -286 N ATOM 117 CE2 TRP A 15 42.021 21.362 15.670 1.00 34.81 C ANISOU 117 CE2 TRP C 15 4363 4726 4137 -481 1105 -233 C ATOM 118 CE3 TRP A 15 44.020 20.099 15.164 1.00 29.62 C ANISOU 118 CE3 TRP C 15 3588 4554 3111 -87 1519 -713 C ATOM 119 CZ2 TRP A 15 42.487 22.480 14.979 1.00 32.81 C ANISOU 119 CZ2 TRP C 15 3755 4507 4204 -110 1598 -773 C ATOM 120 CZ3 TRP A 15 44.482 21.201 14.481 1.00 33.75 C ANISOU 120 CZ3 TRP C 15 4283 5014 3525 -980 862 188 C ATOM 121 CH2 TRP A 15 43.718 22.379 14.396 1.00 35.37 C ANISOU 121 CH2 TRP C 15 4813 4770 3856 -814 679 -158 C ATOM 122 N ALA A 16 44.184 16.496 14.909 1.00 30.94 N ANISOU 122 N ALA C 16 4454 4063 3239 -229 793 488 N ATOM 123 CA ALA A 16 45.270 16.585 13.923 1.00 29.29 C ANISOU 123 CA ALA C 16 3856 4129 3145 116 1164 397 C ATOM 124 C ALA A 16 44.895 15.895 12.623 1.00 29.05 C ANISOU 124 C ALA C 16 3699 4539 2798 -316 790 36 C ATOM 125 O ALA A 16 45.056 16.385 11.508 1.00 33.29 O ANISOU 125 O ALA C 16 4768 4944 2935 -1247 418 291 O ATOM 126 CB ALA A 16 46.512 15.961 14.538 1.00 26.10 C ANISOU 126 CB ALA C 16 2751 4510 2657 366 -21 59 C ATOM 127 N ALA A 17 44.352 14.680 12.753 1.00 30.90 N ANISOU 127 N ALA C 17 3685 4787 3270 -548 1021 78 N ATOM 128 CA ALA A 17 43.936 13.952 11.554 1.00 29.58 C ANISOU 128 CA ALA C 17 3656 4664 2920 9 781 291 C ATOM 129 C ALA A 17 42.841 14.722 10.835 1.00 30.77 C ANISOU 129 C ALA C 17 3429 4455 3808 304 1037 159 C ATOM 130 O ALA A 17 42.865 14.851 9.597 1.00 33.56 O ANISOU 130 O ALA C 17 5242 3549 3961 322 391 -19 O ATOM 131 CB ALA A 17 43.512 12.543 11.930 1.00 31.67 C ANISOU 131 CB ALA C 17 3817 5595 2621 -705 945 938 C ATOM 132 N ARG A 18 41.859 15.275 11.527 1.00 33.37 N ANISOU 132 N ARG C 18 4138 4690 3852 -305 976 359 N ATOM 133 CA ARG A 18 40.826 16.059 10.850 1.00 32.76 C ANISOU 133 CA ARG C 18 3847 4462 4140 76 1273 399 C ATOM 134 C ARG A 18 41.435 17.282 10.164 1.00 31.33 C ANISOU 134 C ARG C 18 4125 3797 3982 276 1024 85 C ATOM 135 O ARG A 18 40.987 17.656 9.055 1.00 36.95 O ANISOU 135 O ARG C 18 4887 4509 4643 82 1079 -703 O ATOM 136 CB ARG A 18 39.746 16.470 11.848 1.00 33.91 C ANISOU 136 CB ARG C 18 3988 4728 4170 240 1013 497 C ATOM 137 CG ARG A 18 38.523 17.122 11.211 1.00 37.46 C ANISOU 137 CG ARG C 18 4925 4534 4776 327 1308 593 C ATOM 138 CD ARG A 18 37.476 17.429 12.285 1.00 41.00 C ANISOU 138 CD ARG C 18 5949 4767 4862 140 1220 802 C ATOM 139 NE ARG A 18 37.926 18.512 13.166 1.00 45.31 N ANISOU 139 NE ARG C 18 6946 5829 4442 -324 1671 479 N ATOM 140 CZ ARG A 18 37.209 19.105 14.098 1.00 50.53 C ANISOU 140 CZ ARG C 18 7873 6006 5319 -150 2270 950 C ATOM 141 NH1 ARG A 18 35.955 18.723 14.305 1.00 60.56 N ANISOU 141 NH1 ARG C 18 8888 7188 6934 529 1145 1804 N ATOM 142 NH2 ARG A 18 37.745 20.074 14.822 1.00 58.04 N ANISOU 142 NH2 ARG C 18 9870 5866 6316 -870 4164 -161 N ATOM 143 N HIS A 19 42.437 17.916 10.773 1.00 30.93 N ANISOU 143 N HIS C 19 4001 3875 3875 385 985 358 N ATOM 144 CA HIS A 19 43.102 19.083 10.178 1.00 29.19 C ANISOU 144 CA HIS C 19 4131 3571 3390 299 962 56 C ATOM 145 C HIS A 19 43.763 18.686 8.860 1.00 30.19 C ANISOU 145 C HIS C 19 4403 3642 3426 10 894 90 C ATOM 146 O HIS A 19 43.639 19.304 7.796 1.00 36.06 O ANISOU 146 O HIS C 19 6311 3812 3577 -286 289 203 O ATOM 147 CB HIS A 19 44.131 19.689 11.144 1.00 28.79 C ANISOU 147 CB HIS C 19 4045 3511 3382 510 825 102 C ATOM 148 CG HIS A 19 44.656 21.012 10.684 1.00 30.50 C ANISOU 148 CG HIS C 19 4090 3803 3695 373 813 -201 C ATOM 149 ND1 HIS A 19 43.887 22.144 10.577 1.00 33.56 N ANISOU 149 ND1 HIS C 19 4787 3990 3973 -5 382 44 N ATOM 150 CD2 HIS A 19 45.900 21.397 10.285 1.00 31.72 C ANISOU 150 CD2 HIS C 19 3922 3984 4146 448 549 -610 C ATOM 151 CE1 HIS A 19 44.608 23.165 10.146 1.00 34.20 C ANISOU 151 CE1 HIS C 19 4915 4265 3813 -128 130 -220 C ATOM 152 NE2 HIS A 19 45.841 22.732 9.959 1.00 34.50 N ANISOU 152 NE2 HIS C 19 4320 4316 4472 92 236 -445 N ATOM 153 N ILE A 20 44.508 17.579 8.918 1.00 33.50 N ANISOU 153 N ILE C 20 4840 4222 3665 -726 1231 153 N ATOM 154 CA ILE A 20 45.186 17.058 7.717 1.00 32.34 C ANISOU 154 CA ILE C 20 4869 3846 3575 -275 1542 -52 C ATOM 155 C ILE A 20 44.155 16.807 6.629 1.00 33.02 C ANISOU 155 C ILE C 20 4689 4221 3637 -170 1282 -341 C ATOM 156 O ILE A 20 44.342 17.286 5.507 1.00 35.06 O ANISOU 156 O ILE C 20 5147 4395 3778 -369 1052 -545 O ATOM 157 CB ILE A 20 46.000 15.792 8.049 1.00 31.64 C ANISOU 157 CB ILE C 20 4972 3796 3253 -249 1104 99 C ATOM 158 CG1 ILE A 20 47.194 16.046 8.978 1.00 27.21 C ANISOU 158 CG1 ILE C 20 4083 3578 2679 -480 788 382 C ATOM 159 CG2 ILE A 20 46.439 15.101 6.768 1.00 30.74 C ANISOU 159 CG2 ILE C 20 4222 4101 3356 -234 1397 63 C ATOM 160 CD1 ILE A 20 47.864 14.811 9.539 1.00 27.95 C ANISOU 160 CD1 ILE C 20 3960 3676 2983 -143 98 227 C ATOM 161 N VAL A 21 43.087 16.098 6.964 1.00 33.86 N ANISOU 161 N VAL C 21 4471 4460 3934 -273 1515 -76 N ATOM 162 CA VAL A 21 42.037 15.789 5.993 1.00 34.17 C ANISOU 162 CA VAL C 21 4534 4381 4068 -123 1204 -318 C ATOM 163 C VAL A 21 41.446 17.050 5.373 1.00 36.10 C ANISOU 163 C VAL C 21 5749 4619 3350 -662 814 77 C ATOM 164 O VAL A 21 41.220 17.198 4.165 1.00 37.00 O ANISOU 164 O VAL C 21 6030 4317 3713 -347 2338 -810 O ATOM 165 CB VAL A 21 40.924 14.954 6.663 1.00 37.20 C ANISOU 165 CB VAL C 21 4646 4993 4495 100 1086 -325 C ATOM 166 CG1 VAL A 21 39.683 14.926 5.769 1.00 33.39 C ANISOU 166 CG1 VAL C 21 3606 5524 3557 -231 1759 143 C ATOM 167 CG2 VAL A 21 41.433 13.557 6.988 1.00 37.04 C ANISOU 167 CG2 VAL C 21 4146 5571 4354 -179 1433 -119 C ATOM 168 N ASN A 22 41.171 18.035 6.221 1.00 35.42 N ANISOU 168 N ASN C 22 5578 4810 3072 -833 684 -45 N ATOM 169 CA ASN A 22 40.588 19.270 5.709 1.00 36.23 C ANISOU 169 CA ASN C 22 5802 4366 3596 -598 428 13 C ATOM 170 C ASN A 22 41.581 20.015 4.835 1.00 35.13 C ANISOU 170 C ASN C 22 5692 4331 3324 -622 502 -178 C ATOM 171 O ASN A 22 41.209 20.605 3.817 1.00 37.68 O ANISOU 171 O ASN C 22 5612 5340 3365 -947 734 -548 O ATOM 172 CB ASN A 22 40.095 20.112 6.888 1.00 39.79 C ANISOU 172 CB ASN C 22 6436 4639 4041 -967 142 475 C ATOM 173 CG ASN A 22 38.880 19.518 7.582 1.00 45.83 C ANISOU 173 CG ASN C 22 7258 5374 4783 -947 -662 925 C ATOM 174 OD1 ASN A 22 38.478 20.047 8.618 1.00 54.80 O ANISOU 174 OD1 ASN C 22 8143 7299 5378 -1210 -963 2065 O ATOM 175 ND2 ASN A 22 38.271 18.455 7.072 1.00 45.89 N ANISOU 175 ND2 ASN C 22 7308 5443 4685 354 -589 472 N ATOM 176 N ARG A 23 42.870 20.017 5.167 1.00 35.83 N ANISOU 176 N ARG C 23 5833 4392 3389 -470 976 198 N ATOM 177 CA ARG A 23 43.810 20.667 4.253 1.00 33.81 C ANISOU 177 CA ARG C 23 5251 4775 2818 -351 1334 -299 C ATOM 178 C ARG A 23 43.861 19.930 2.927 1.00 34.96 C ANISOU 178 C ARG C 23 5254 5289 2741 -722 1197 -306 C ATOM 179 O ARG A 23 43.859 20.556 1.869 1.00 36.82 O ANISOU 179 O ARG C 23 5818 5426 2745 -279 1168 -752 O ATOM 180 CB ARG A 23 45.211 20.701 4.866 1.00 35.25 C ANISOU 180 CB ARG C 23 5146 4909 3337 -363 1235 -638 C ATOM 181 CG ARG A 23 45.220 21.701 6.006 1.00 30.89 C ANISOU 181 CG ARG C 23 4207 4471 3060 112 732 -412 C ATOM 182 CD ARG A 23 45.075 23.130 5.461 1.00 38.51 C ANISOU 182 CD ARG C 23 5582 5100 3950 -1057 249 -41 C ATOM 183 NE ARG A 23 45.463 24.042 6.551 1.00 40.05 N ANISOU 183 NE ARG C 23 4953 5583 4681 -1159 237 382 N ATOM 184 CZ ARG A 23 44.882 25.198 6.836 1.00 46.54 C ANISOU 184 CZ ARG C 23 6432 5918 5332 -1957 791 -23 C ATOM 185 NH1 ARG A 23 43.857 25.596 6.078 1.00 45.47 N ANISOU 185 NH1 ARG C 23 6255 5597 5424 -1602 1236 316 N ATOM 186 NH2 ARG A 23 45.330 25.923 7.857 1.00 39.35 N ANISOU 186 NH2 ARG C 23 5844 4406 4700 -1401 167 496 N ATOM 187 N ILE A 24 43.909 18.597 2.986 1.00 36.60 N ANISOU 187 N ILE C 24 5032 5082 3794 -531 1463 -307 N ATOM 188 CA ILE A 24 43.950 17.863 1.727 1.00 36.12 C ANISOU 188 CA ILE C 24 4944 4952 3828 -444 1575 -410 C ATOM 189 C ILE A 24 42.684 18.089 0.917 1.00 37.86 C ANISOU 189 C ILE C 24 5388 5292 3707 -139 1001 -707 C ATOM 190 O ILE A 24 42.684 18.310 -0.298 1.00 43.09 O ANISOU 190 O ILE C 24 6870 5635 3868 -744 545 -885 O ATOM 191 CB ILE A 24 44.141 16.359 1.987 1.00 33.76 C ANISOU 191 CB ILE C 24 4106 5106 3616 84 1724 -768 C ATOM 192 CG1 ILE A 24 45.517 16.018 2.548 1.00 32.78 C ANISOU 192 CG1 ILE C 24 4389 4766 3300 68 1392 -388 C ATOM 193 CG2 ILE A 24 43.845 15.560 0.709 1.00 35.69 C ANISOU 193 CG2 ILE C 24 3904 6526 3130 -272 1273 -1019 C ATOM 194 CD1 ILE A 24 45.619 14.666 3.200 1.00 33.70 C ANISOU 194 CD1 ILE C 24 4440 4508 3855 -216 1429 -75 C ATOM 195 N ASN A 25 41.513 18.042 1.557 1.00 39.70 N ANISOU 195 N ASN C 25 5448 5176 4462 -73 823 -715 N ATOM 196 CA ASN A 25 40.297 18.138 0.743 1.00 38.29 C ANISOU 196 CA ASN C 25 4951 5480 4118 -75 1363 -477 C ATOM 197 C ASN A 25 40.137 19.549 0.207 1.00 38.36 C ANISOU 197 C ASN C 25 5064 5487 4025 -82 1665 -1018 C ATOM 198 O ASN A 25 39.600 19.791 -0.884 1.00 45.52 O ANISOU 198 O ASN C 25 6670 6190 4436 -504 2035 -1597 O ATOM 199 CB ASN A 25 39.089 17.649 1.545 1.00 38.75 C ANISOU 199 CB ASN C 25 5514 5043 4167 -147 1240 -254 C ATOM 200 CG ASN A 25 39.048 16.141 1.724 1.00 37.94 C ANISOU 200 CG ASN C 25 4753 5011 4650 399 1590 199 C ATOM 201 OD1 ASN A 25 39.652 15.400 0.942 1.00 43.68 O ANISOU 201 OD1 ASN C 25 5939 5284 5373 -193 1400 577 O ATOM 202 ND2 ASN A 25 38.362 15.608 2.725 1.00 38.06 N ANISOU 202 ND2 ASN C 25 5159 4318 4983 639 1083 -371 N ATOM 203 N ALA A 26 40.618 20.573 0.909 1.00 39.03 N ANISOU 203 N ALA C 26 5387 5650 3794 -559 1731 -124 N ATOM 204 CA ALA A 26 40.433 21.922 0.356 1.00 39.56 C ANISOU 204 CA ALA C 26 5776 5022 4232 -740 1787 -16 C ATOM 205 C ALA A 26 41.400 22.195 -0.785 1.00 39.68 C ANISOU 205 C ALA C 26 6338 4625 4112 -760 1116 -698 C ATOM 206 O ALA A 26 41.110 22.993 -1.665 1.00 47.53 O ANISOU 206 O ALA C 26 9724 4861 3475 -1902 1068 -498 O ATOM 207 CB ALA A 26 40.634 22.970 1.440 1.00 36.18 C ANISOU 207 CB ALA C 26 5123 4342 4282 -55 1936 -723 C ATOM 208 N PHE A 27 42.554 21.535 -0.747 1.00 38.35 N ANISOU 208 N PHE C 27 5942 4615 4013 -405 1029 -920 N ATOM 209 CA PHE A 27 43.603 21.715 -1.742 1.00 40.04 C ANISOU 209 CA PHE C 27 6188 5010 4013 -384 1177 -579 C ATOM 210 C PHE A 27 43.266 21.026 -3.060 1.00 41.26 C ANISOU 210 C PHE C 27 6808 4817 4051 -346 1448 -885 C ATOM 211 O PHE A 27 43.665 21.512 -4.118 1.00 41.16 O ANISOU 211 O PHE C 27 7394 4144 4103 -954 1316 -139 O ATOM 212 CB PHE A 27 44.917 21.144 -1.233 1.00 37.50 C ANISOU 212 CB PHE C 27 5627 5273 3349 184 623 -681 C ATOM 213 CG PHE A 27 46.161 21.295 -2.088 1.00 36.10 C ANISOU 213 CG PHE C 27 4925 5379 3413 -351 584 -349 C ATOM 214 CD1 PHE A 27 46.973 22.400 -1.918 1.00 36.57 C ANISOU 214 CD1 PHE C 27 4890 5474 3529 -493 506 -721 C ATOM 215 CD2 PHE A 27 46.510 20.344 -3.031 1.00 37.55 C ANISOU 215 CD2 PHE C 27 5136 5593 3540 -1063 296 -375 C ATOM 216 CE1 PHE A 27 48.108 22.554 -2.673 1.00 37.05 C ANISOU 216 CE1 PHE C 27 4493 5781 3805 -495 810 -343 C ATOM 217 CE2 PHE A 27 47.660 20.487 -3.791 1.00 38.14 C ANISOU 217 CE2 PHE C 27 4737 5829 3926 -1438 374 177 C ATOM 218 CZ PHE A 27 48.473 21.591 -3.601 1.00 39.50 C ANISOU 218 CZ PHE C 27 4809 6140 4058 -1157 437 -99 C ATOM 219 N LYS A 28 42.557 19.910 -2.963 1.00 44.61 N ANISOU 219 N LYS C 28 6756 5747 4445 -570 1777 -641 N ATOM 220 CA LYS A 28 42.124 19.169 -4.151 1.00 46.21 C ANISOU 220 CA LYS C 28 7387 5462 4708 -684 2205 -620 C ATOM 221 C LYS A 28 43.303 18.710 -5.006 1.00 44.35 C ANISOU 221 C LYS C 28 7283 5607 3960 -986 1123 -833 C ATOM 222 O LYS A 28 43.472 19.185 -6.132 1.00 49.03 O ANISOU 222 O LYS C 28 8259 6865 3505 -1735 1498 -1172 O ATOM 223 CB LYS A 28 41.177 20.029 -4.998 1.00 52.78 C ANISOU 223 CB LYS C 28 8806 5571 5675 -713 2907 -1237 C ATOM 224 CG LYS A 28 39.835 20.264 -4.336 1.00 62.04 C ANISOU 224 CG LYS C 28 10735 5380 7459 -1095 2638 -533 C ATOM 225 CD LYS A 28 39.417 21.730 -4.342 1.00 83.37 C ANISOU 225 CD LYS C 28 14704 6945 10028 -3815 2545 -213 C ATOM 226 CE LYS A 28 38.808 22.145 -3.007 1.00 92.61 C ANISOU 226 CE LYS C 28 16511 7514 11163 -4622 2424 933 C ATOM 227 NZ LYS A 28 38.893 23.605 -2.720 1.00103.41 N ANISOU 227 NZ LYS C 28 18273 7587 13433 -5443 6133 -1423 N ATOM 228 N PRO A 29 44.103 17.796 -4.467 1.00 39.46 N ANISOU 228 N PRO C 29 5785 5362 3845 -424 1002 -725 N ATOM 229 CA PRO A 29 45.355 17.391 -5.105 1.00 37.54 C ANISOU 229 CA PRO C 29 5009 5543 3711 -230 939 -695 C ATOM 230 C PRO A 29 45.116 16.570 -6.363 1.00 41.25 C ANISOU 230 C PRO C 29 6231 5831 3612 -708 1172 -774 C ATOM 231 O PRO A 29 44.109 15.867 -6.441 1.00 43.73 O ANISOU 231 O PRO C 29 5745 6606 4264 -1134 1934 -461 O ATOM 232 CB PRO A 29 46.001 16.494 -4.037 1.00 35.65 C ANISOU 232 CB PRO C 29 4574 5268 3702 -35 1111 -669 C ATOM 233 CG PRO A 29 44.823 15.922 -3.307 1.00 36.41 C ANISOU 233 CG PRO C 29 5121 5152 3560 33 908 -576 C ATOM 234 CD PRO A 29 43.861 17.081 -3.199 1.00 38.15 C ANISOU 234 CD PRO C 29 5260 5248 3985 -108 942 -559 C ATOM 235 N THR A 30 46.049 16.672 -7.303 1.00 45.50 N ANISOU 235 N THR C 30 7490 6010 3786 -1299 469 -481 N ATOM 236 CA THR A 30 46.003 15.860 -8.513 1.00 46.83 C ANISOU 236 CA THR C 30 7609 6480 3702 -1843 299 -454 C ATOM 237 C THR A 30 47.381 15.275 -8.814 1.00 50.02 C ANISOU 237 C THR C 30 8268 6557 4179 -1744 797 -198 C ATOM 238 O THR A 30 48.364 15.600 -8.143 1.00 52.51 O ANISOU 238 O THR C 30 8664 6438 4849 -1677 1162 -222 O ATOM 239 CB THR A 30 45.523 16.664 -9.736 1.00 44.09 C ANISOU 239 CB THR C 30 6711 6582 3459 -1159 -332 -109 C ATOM 240 OG1 THR A 30 46.452 17.723 -9.987 1.00 46.64 O ANISOU 240 OG1 THR C 30 6551 7076 4093 -953 237 201 O ATOM 241 CG2 THR A 30 44.180 17.320 -9.459 1.00 42.08 C ANISOU 241 CG2 THR C 30 7296 6431 2261 -443 1449 -777 C ATOM 242 N ALA A 31 47.427 14.417 -9.833 1.00 52.97 N ANISOU 242 N ALA C 31 8827 7004 4296 -1634 985 127 N ATOM 243 CA ALA A 31 48.658 13.757 -10.249 1.00 53.78 C ANISOU 243 CA ALA C 31 9115 6975 4346 -1331 1698 68 C ATOM 244 C ALA A 31 49.782 14.769 -10.457 1.00 54.14 C ANISOU 244 C ALA C 31 9096 7145 4330 -1356 1670 468 C ATOM 245 O ALA A 31 50.933 14.507 -10.116 1.00 56.11 O ANISOU 245 O ALA C 31 9632 7247 4442 -738 -88 303 O ATOM 246 CB ALA A 31 48.441 12.955 -11.528 1.00 55.18 C ANISOU 246 CB ALA C 31 9035 7432 4499 -1937 1730 -40 C ATOM 247 N ASP A 32 49.418 15.915 -11.027 1.00 54.17 N ANISOU 247 N ASP C 32 8981 7218 4383 -1307 1864 231 N ATOM 248 CA ASP A 32 50.388 16.948 -11.381 1.00 56.83 C ANISOU 248 CA ASP C 32 9268 7418 4908 -1227 1294 339 C ATOM 249 C ASP A 32 50.474 18.049 -10.328 1.00 53.60 C ANISOU 249 C ASP C 32 8274 6953 5141 -1152 740 731 C ATOM 250 O ASP A 32 51.345 18.924 -10.409 1.00 51.86 O ANISOU 250 O ASP C 32 8029 7728 3949 -1792 -388 384 O ATOM 251 CB ASP A 32 50.041 17.526 -12.756 1.00 62.94 C ANISOU 251 CB ASP C 32 10524 8347 5042 -1065 743 143 C ATOM 252 CG ASP A 32 50.327 16.521 -13.863 1.00 73.31 C ANISOU 252 CG ASP C 32 14176 8786 4892 -2321 1926 -630 C ATOM 253 OD1 ASP A 32 51.383 15.838 -13.833 1.00 85.57 O ANISOU 253 OD1 ASP C 32 18137 8895 5480 -4880 594 -885 O ATOM 254 OD2 ASP A 32 49.495 16.386 -14.794 1.00102.79 O ANISOU 254 OD2 ASP C 32 18775 12167 8113 -4367 5851 -3177 O ATOM 255 N ARG A 33 49.581 18.007 -9.342 1.00 47.75 N ANISOU 255 N ARG C 33 7703 6550 3890 -716 804 -507 N ATOM 256 CA ARG A 33 49.633 18.959 -8.237 1.00 44.00 C ANISOU 256 CA ARG C 33 6663 6144 3912 -801 287 -402 C ATOM 257 C ARG A 33 49.253 18.205 -6.962 1.00 42.40 C ANISOU 257 C ARG C 33 6310 5814 3985 -788 346 -194 C ATOM 258 O ARG A 33 48.109 18.289 -6.509 1.00 42.09 O ANISOU 258 O ARG C 33 6755 5625 3612 -979 834 113 O ATOM 259 CB ARG A 33 48.728 20.171 -8.450 1.00 46.13 C ANISOU 259 CB ARG C 33 6191 6304 5030 -675 436 -1107 C ATOM 260 CG ARG A 33 49.184 21.379 -7.647 1.00 48.91 C ANISOU 260 CG ARG C 33 5890 6223 6471 -488 610 -650 C ATOM 261 CD ARG A 33 48.101 22.454 -7.574 1.00 50.23 C ANISOU 261 CD ARG C 33 5725 6018 7342 -54 992 -652 C ATOM 262 NE ARG A 33 46.820 21.845 -7.268 1.00 54.48 N ANISOU 262 NE ARG C 33 6214 6723 7762 313 312 -655 N ATOM 263 CZ ARG A 33 45.916 22.177 -6.365 1.00 51.40 C ANISOU 263 CZ ARG C 33 5936 6491 7104 380 692 -1028 C ATOM 264 NH1 ARG A 33 46.034 23.192 -5.531 1.00 45.95 N ANISOU 264 NH1 ARG C 33 5864 5661 5935 -359 383 -2613 N ATOM 265 NH2 ARG A 33 44.826 21.415 -6.324 1.00 51.57 N ANISOU 265 NH2 ARG C 33 6382 6499 6714 886 1086 -1189 N ATOM 266 N PRO A 34 50.230 17.466 -6.450 1.00 38.08 N ANISOU 266 N PRO C 34 5036 5895 3539 -293 777 -377 N ATOM 267 CA PRO A 34 50.006 16.693 -5.230 1.00 37.24 C ANISOU 267 CA PRO C 34 5165 5475 3510 -542 698 62 C ATOM 268 C PRO A 34 50.017 17.568 -3.981 1.00 37.15 C ANISOU 268 C PRO C 34 4964 5495 3654 -911 572 154 C ATOM 269 O PRO A 34 50.644 18.622 -3.978 1.00 34.83 O ANISOU 269 O PRO C 34 4961 4858 3415 -1190 232 197 O ATOM 270 CB PRO A 34 51.229 15.767 -5.192 1.00 34.64 C ANISOU 270 CB PRO C 34 3958 5439 3767 -423 591 302 C ATOM 271 CG PRO A 34 52.304 16.541 -5.894 1.00 34.98 C ANISOU 271 CG PRO C 34 4129 5589 3573 -786 -2 -77 C ATOM 272 CD PRO A 34 51.590 17.293 -6.978 1.00 35.93 C ANISOU 272 CD PRO C 34 4820 5946 2885 -437 898 -291 C ATOM 273 N PHE A 35 49.352 17.121 -2.927 1.00 33.50 N ANISOU 273 N PHE C 35 4323 4795 3610 -209 1093 92 N ATOM 274 CA PHE A 35 49.473 17.666 -1.582 1.00 34.47 C ANISOU 274 CA PHE C 35 4715 4901 3480 -303 1108 -166 C ATOM 275 C PHE A 35 50.692 17.039 -0.920 1.00 30.80 C ANISOU 275 C PHE C 35 3745 4708 3249 -133 283 80 C ATOM 276 O PHE A 35 50.815 15.808 -0.859 1.00 34.69 O ANISOU 276 O PHE C 35 4370 5498 3313 -953 865 102 O ATOM 277 CB PHE A 35 48.232 17.360 -0.763 1.00 31.19 C ANISOU 277 CB PHE C 35 4628 4378 2845 -147 1408 -659 C ATOM 278 CG PHE A 35 48.233 18.103 0.575 1.00 32.85 C ANISOU 278 CG PHE C 35 4726 4756 2998 -563 1396 -552 C ATOM 279 CD1 PHE A 35 47.719 19.382 0.648 1.00 34.09 C ANISOU 279 CD1 PHE C 35 4555 4989 3409 -659 1006 -231 C ATOM 280 CD2 PHE A 35 48.745 17.492 1.701 1.00 32.16 C ANISOU 280 CD2 PHE C 35 4104 5072 3044 -292 1803 -911 C ATOM 281 CE1 PHE A 35 47.716 20.074 1.844 1.00 36.47 C ANISOU 281 CE1 PHE C 35 5383 4816 3659 -970 1408 -344 C ATOM 282 CE2 PHE A 35 48.741 18.187 2.908 1.00 32.59 C ANISOU 282 CE2 PHE C 35 4209 5400 2773 -710 1003 -232 C ATOM 283 CZ PHE A 35 48.220 19.473 2.986 1.00 31.87 C ANISOU 283 CZ PHE C 35 4006 4644 3461 -139 1146 -158 C ATOM 284 N VAL A 36 51.604 17.860 -0.421 1.00 31.61 N ANISOU 284 N VAL C 36 4174 4493 3343 -147 942 418 N ATOM 285 CA VAL A 36 52.851 17.338 0.130 1.00 31.43 C ANISOU 285 CA VAL C 36 4778 4483 2682 123 698 564 C ATOM 286 C VAL A 36 52.808 17.405 1.656 1.00 32.63 C ANISOU 286 C VAL C 36 5038 4700 2660 -862 252 757 C ATOM 287 O VAL A 36 52.641 18.502 2.212 1.00 32.32 O ANISOU 287 O VAL C 36 4713 5181 2386 -1089 704 -255 O ATOM 288 CB VAL A 36 54.080 18.073 -0.432 1.00 31.27 C ANISOU 288 CB VAL C 36 4827 4559 2494 99 136 -277 C ATOM 289 CG1 VAL A 36 55.363 17.442 0.092 1.00 27.48 C ANISOU 289 CG1 VAL C 36 3380 4632 2430 -165 -163 -417 C ATOM 290 CG2 VAL A 36 54.057 18.061 -1.975 1.00 28.93 C ANISOU 290 CG2 VAL C 36 3655 4842 2496 -270 474 -500 C ATOM 291 N LEU A 37 52.940 16.245 2.289 1.00 30.67 N ANISOU 291 N LEU C 37 4517 4144 2994 -623 685 483 N ATOM 292 CA LEU A 37 52.746 16.051 3.714 1.00 28.29 C ANISOU 292 CA LEU C 37 3603 4101 3043 -644 539 372 C ATOM 293 C LEU A 37 54.030 15.590 4.386 1.00 28.55 C ANISOU 293 C LEU C 37 3493 4173 3181 -461 441 330 C ATOM 294 O LEU A 37 54.510 14.524 3.993 1.00 29.10 O ANISOU 294 O LEU C 37 3783 3994 3281 -337 844 224 O ATOM 295 CB LEU A 37 51.740 14.944 3.977 1.00 32.82 C ANISOU 295 CB LEU C 37 3775 4139 4557 -272 387 425 C ATOM 296 CG LEU A 37 50.569 15.012 4.940 1.00 32.63 C ANISOU 296 CG LEU C 37 3723 5069 3608 -636 -25 474 C ATOM 297 CD1 LEU A 37 50.177 13.594 5.353 1.00 32.91 C ANISOU 297 CD1 LEU C 37 4935 4662 2905 -2002 -779 347 C ATOM 298 CD2 LEU A 37 50.792 15.872 6.170 1.00 28.13 C ANISOU 298 CD2 LEU C 37 4074 4126 2488 234 -64 -1156 C ATOM 299 N GLY A 38 54.537 16.321 5.367 1.00 29.00 N ANISOU 299 N GLY C 38 3598 4227 3192 -802 506 96 N ATOM 300 CA GLY A 38 55.709 15.879 6.116 1.00 27.79 C ANISOU 300 CA GLY C 38 3542 4232 2786 -519 8 203 C ATOM 301 C GLY A 38 55.254 15.142 7.378 1.00 28.30 C ANISOU 301 C GLY C 38 3406 4072 3273 -349 -292 388 C ATOM 302 O GLY A 38 54.264 15.541 8.007 1.00 26.56 O ANISOU 302 O GLY C 38 3348 4128 2614 -59 648 328 O ATOM 303 N LEU A 39 55.945 14.060 7.737 1.00 26.66 N ANISOU 303 N LEU C 39 3158 3916 3056 106 -40 -130 N ATOM 304 CA LEU A 39 55.456 13.160 8.770 1.00 26.08 C ANISOU 304 CA LEU C 39 2896 3741 3271 159 -45 -11 C ATOM 305 C LEU A 39 56.523 12.724 9.751 1.00 25.74 C ANISOU 305 C LEU C 39 3267 3450 3064 -333 27 177 C ATOM 306 O LEU A 39 57.684 12.558 9.390 1.00 27.38 O ANISOU 306 O LEU C 39 3133 3840 3430 335 36 -56 O ATOM 307 CB LEU A 39 54.885 11.891 8.105 1.00 28.35 C ANISOU 307 CB LEU C 39 3119 4457 3196 -71 160 283 C ATOM 308 CG LEU A 39 53.629 12.127 7.265 1.00 29.90 C ANISOU 308 CG LEU C 39 3207 4583 3570 -75 755 292 C ATOM 309 CD1 LEU A 39 53.128 10.816 6.651 1.00 28.57 C ANISOU 309 CD1 LEU C 39 3188 5131 2536 -340 361 570 C ATOM 310 CD2 LEU A 39 52.524 12.791 8.084 1.00 29.84 C ANISOU 310 CD2 LEU C 39 3316 4361 3659 -386 957 143 C ATOM 311 N PRO A 40 56.163 12.533 11.005 1.00 27.30 N ANISOU 311 N PRO C 40 3357 4166 2850 -156 495 260 N ATOM 312 CA PRO A 40 57.059 11.953 12.005 1.00 27.80 C ANISOU 312 CA PRO C 40 3695 4172 2697 -269 673 271 C ATOM 313 C PRO A 40 56.698 10.538 12.426 1.00 29.36 C ANISOU 313 C PRO C 40 3953 3855 3348 -565 426 409 C ATOM 314 O PRO A 40 55.663 9.990 12.023 1.00 28.16 O ANISOU 314 O PRO C 40 3646 3956 3097 -554 -80 202 O ATOM 315 CB PRO A 40 56.750 12.896 13.188 1.00 26.34 C ANISOU 315 CB PRO C 40 3850 3430 2729 -341 378 300 C ATOM 316 CG PRO A 40 55.268 13.067 13.079 1.00 26.74 C ANISOU 316 CG PRO C 40 3569 3895 2697 62 756 21 C ATOM 317 CD PRO A 40 54.883 12.930 11.617 1.00 26.74 C ANISOU 317 CD PRO C 40 3568 4218 2373 -160 163 111 C ATOM 318 N THR A 41 57.551 9.943 13.253 1.00 30.65 N ANISOU 318 N THR C 41 4076 4449 3119 -593 654 129 N ATOM 319 CA THR A 41 57.334 8.608 13.782 1.00 32.57 C ANISOU 319 CA THR C 41 4423 4492 3462 -721 316 55 C ATOM 320 C THR A 41 57.350 8.685 15.309 1.00 34.25 C ANISOU 320 C THR C 41 4493 5077 3445 -735 278 149 C ATOM 321 O THR A 41 57.461 9.782 15.870 1.00 39.20 O ANISOU 321 O THR C 41 4684 6525 3685 -983 561 213 O ATOM 322 CB THR A 41 58.364 7.558 13.323 1.00 33.71 C ANISOU 322 CB THR C 41 5253 4338 3216 -1003 374 -341 C ATOM 323 OG1 THR A 41 59.665 7.952 13.779 1.00 36.62 O ANISOU 323 OG1 THR C 41 6285 4357 3273 -747 1025 -314 O ATOM 324 CG2 THR A 41 58.491 7.452 11.816 1.00 31.31 C ANISOU 324 CG2 THR C 41 5179 3499 3219 550 189 -159 C ATOM 325 N GLY A 42 57.238 7.555 15.981 1.00 36.09 N ANISOU 325 N GLY C 42 4541 5612 3561 -598 114 26 N ATOM 326 CA GLY A 42 57.273 7.472 17.422 1.00 36.71 C ANISOU 326 CA GLY C 42 4990 5433 3523 -684 16 166 C ATOM 327 C GLY A 42 55.902 7.338 18.036 1.00 35.57 C ANISOU 327 C GLY C 42 4942 5088 3485 -742 147 -25 C ATOM 328 O GLY A 42 54.870 7.248 17.403 1.00 35.05 O ANISOU 328 O GLY C 42 5529 4786 3001 -940 306 113 O ATOM 329 N GLY A 43 55.846 7.315 19.365 1.00 34.07 N ANISOU 329 N GLY C 43 4938 4519 3487 -272 530 59 N ATOM 330 CA GLY A 43 54.582 7.138 20.069 1.00 33.79 C ANISOU 330 CA GLY C 43 4362 4499 3976 -767 424 439 C ATOM 331 C GLY A 43 53.680 8.352 19.931 1.00 31.78 C ANISOU 331 C GLY C 43 4012 4468 3594 -551 440 29 C ATOM 332 O GLY A 43 52.457 8.209 19.951 1.00 32.96 O ANISOU 332 O GLY C 43 4103 4546 3873 -467 797 284 O ATOM 333 N THR A 44 54.244 9.546 19.795 1.00 30.70 N ANISOU 333 N THR C 44 3928 4790 2946 -615 788 -67 N ATOM 334 CA THR A 44 53.425 10.759 19.768 1.00 31.56 C ANISOU 334 CA THR C 44 4083 4857 3050 -743 580 -30 C ATOM 335 C THR A 44 52.423 10.803 18.637 1.00 27.57 C ANISOU 335 C THR C 44 3397 4242 2838 -98 107 451 C ATOM 336 O THR A 44 51.245 11.086 18.901 1.00 29.25 O ANISOU 336 O THR C 44 2870 4461 3782 -108 348 1007 O ATOM 337 CB THR A 44 54.337 12.010 19.703 1.00 32.96 C ANISOU 337 CB THR C 44 4063 4366 4094 -645 1021 -659 C ATOM 338 OG1 THR A 44 55.016 12.137 20.965 1.00 40.12 O ANISOU 338 OG1 THR C 44 5055 5581 4609 -1401 1930 -1118 O ATOM 339 CG2 THR A 44 53.539 13.285 19.525 1.00 30.57 C ANISOU 339 CG2 THR C 44 4264 4209 3141 -760 433 432 C ATOM 340 N PRO A 45 52.756 10.592 17.366 1.00 27.52 N ANISOU 340 N PRO C 45 3448 4170 2840 -157 392 440 N ATOM 341 CA PRO A 45 51.698 10.611 16.355 1.00 28.21 C ANISOU 341 CA PRO C 45 3447 4269 3002 63 271 322 C ATOM 342 C PRO A 45 50.857 9.342 16.276 1.00 28.67 C ANISOU 342 C PRO C 45 3466 4244 3183 199 52 130 C ATOM 343 O PRO A 45 50.026 9.248 15.366 1.00 29.73 O ANISOU 343 O PRO C 45 3427 4747 3122 -639 856 110 O ATOM 344 CB PRO A 45 52.505 10.762 15.047 1.00 26.66 C ANISOU 344 CB PRO C 45 3291 3904 2934 -104 69 9 C ATOM 345 CG PRO A 45 53.834 10.123 15.340 1.00 26.85 C ANISOU 345 CG PRO C 45 3873 3958 2372 -165 -185 -94 C ATOM 346 CD PRO A 45 54.102 10.388 16.809 1.00 28.88 C ANISOU 346 CD PRO C 45 4611 3828 2536 -229 346 252 C ATOM 347 N MET A 46 50.967 8.328 17.119 1.00 31.24 N ANISOU 347 N MET C 46 3654 5111 3103 -530 326 104 N ATOM 348 CA MET A 46 50.153 7.114 16.940 1.00 32.62 C ANISOU 348 CA MET C 46 3597 4831 3968 -342 -49 882 C ATOM 349 C MET A 46 48.646 7.346 16.873 1.00 34.04 C ANISOU 349 C MET C 46 4307 4874 3754 -194 1028 833 C ATOM 350 O MET A 46 47.971 6.819 15.990 1.00 36.82 O ANISOU 350 O MET C 46 4296 5735 3957 -568 1120 309 O ATOM 351 CB MET A 46 50.372 6.084 18.061 1.00 32.57 C ANISOU 351 CB MET C 46 3155 5559 3662 142 294 281 C ATOM 352 CG MET A 46 51.744 5.437 18.040 1.00 39.33 C ANISOU 352 CG MET C 46 4828 5541 4573 142 -53 -347 C ATOM 353 SD MET A 46 51.871 4.304 16.641 1.00 54.33 S ANISOU 353 SD MET C 46 6699 6308 7636 -571 996 1817 S ATOM 354 CE MET A 46 50.862 2.944 17.213 1.00 56.96 C ANISOU 354 CE MET C 46 5802 8021 7819 43 2212 -1512 C ATOM 355 N THR A 47 48.064 8.126 17.789 1.00 32.40 N ANISOU 355 N THR C 47 3999 4720 3590 -566 433 774 N ATOM 356 CA THR A 47 46.609 8.281 17.688 1.00 31.89 C ANISOU 356 CA THR C 47 3595 4904 3620 -412 345 823 C ATOM 357 C THR A 47 46.239 9.086 16.452 1.00 32.90 C ANISOU 357 C THR C 47 4405 4460 3634 -205 58 935 C ATOM 358 O THR A 47 45.109 8.968 15.945 1.00 33.63 O ANISOU 358 O THR C 47 4046 4683 4048 -241 43 705 O ATOM 359 CB THR A 47 45.983 8.961 18.923 1.00 30.82 C ANISOU 359 CB THR C 47 4163 4178 3369 -198 1031 189 C ATOM 360 OG1 THR A 47 46.602 10.255 19.088 1.00 33.92 O ANISOU 360 OG1 THR C 47 4147 5056 3687 -660 646 709 O ATOM 361 CG2 THR A 47 46.181 8.164 20.214 1.00 31.26 C ANISOU 361 CG2 THR C 47 3715 4857 3305 -117 1007 160 C ATOM 362 N THR A 48 47.140 9.920 15.929 1.00 29.54 N ANISOU 362 N THR C 48 4228 3914 3080 -357 324 878 N ATOM 363 CA THR A 48 46.808 10.645 14.694 1.00 27.79 C ANISOU 363 CA THR C 48 3417 3989 3153 -39 813 442 C ATOM 364 C THR A 48 46.716 9.712 13.488 1.00 28.17 C ANISOU 364 C THR C 48 3178 4078 3446 -129 980 221 C ATOM 365 O THR A 48 45.787 9.810 12.690 1.00 30.90 O ANISOU 365 O THR C 48 4012 4516 3213 -461 995 -116 O ATOM 366 CB THR A 48 47.840 11.759 14.439 1.00 28.55 C ANISOU 366 CB THR C 48 3209 4227 3412 -173 1019 -331 C ATOM 367 OG1 THR A 48 47.793 12.700 15.518 1.00 29.67 O ANISOU 367 OG1 THR C 48 3288 4736 3250 -144 689 174 O ATOM 368 CG2 THR A 48 47.518 12.547 13.180 1.00 27.34 C ANISOU 368 CG2 THR C 48 3844 3330 3213 -240 602 305 C ATOM 369 N TYR A 49 47.657 8.795 13.318 1.00 29.41 N ANISOU 369 N TYR C 49 3728 4195 3251 -350 798 446 N ATOM 370 CA TYR A 49 47.670 7.807 12.243 1.00 29.62 C ANISOU 370 CA TYR C 49 3529 4508 3217 -357 716 488 C ATOM 371 C TYR A 49 46.436 6.913 12.350 1.00 31.06 C ANISOU 371 C TYR C 49 3479 4980 3342 -281 483 -129 C ATOM 372 O TYR A 49 45.730 6.644 11.373 1.00 32.01 O ANISOU 372 O TYR C 49 3581 5256 3326 -193 493 -166 O ATOM 373 CB TYR A 49 48.958 6.979 12.268 1.00 28.70 C ANISOU 373 CB TYR C 49 3729 4516 2661 -593 763 432 C ATOM 374 CG TYR A 49 50.163 7.782 11.826 1.00 28.86 C ANISOU 374 CG TYR C 49 3899 4225 2843 -562 643 535 C ATOM 375 CD1 TYR A 49 50.129 8.526 10.644 1.00 29.67 C ANISOU 375 CD1 TYR C 49 3644 4428 3202 -472 600 139 C ATOM 376 CD2 TYR A 49 51.337 7.809 12.570 1.00 28.94 C ANISOU 376 CD2 TYR C 49 4228 4131 2636 -369 435 627 C ATOM 377 CE1 TYR A 49 51.234 9.263 10.233 1.00 30.68 C ANISOU 377 CE1 TYR C 49 4273 3965 3417 -273 178 282 C ATOM 378 CE2 TYR A 49 52.458 8.547 12.173 1.00 29.44 C ANISOU 378 CE2 TYR C 49 4204 4244 2736 -319 475 638 C ATOM 379 CZ TYR A 49 52.384 9.269 11.004 1.00 30.49 C ANISOU 379 CZ TYR C 49 4441 3847 3297 -119 27 397 C ATOM 380 OH TYR A 49 53.463 10.005 10.581 1.00 29.81 O ANISOU 380 OH TYR C 49 4119 4185 3023 -249 372 598 O ATOM 381 N LYS A 50 46.154 6.464 13.578 1.00 30.55 N ANISOU 381 N LYS C 50 3676 4614 3316 -206 455 -43 N ATOM 382 CA LYS A 50 44.958 5.651 13.797 1.00 33.48 C ANISOU 382 CA LYS C 50 3763 4868 4090 -138 300 528 C ATOM 383 C LYS A 50 43.722 6.412 13.330 1.00 34.21 C ANISOU 383 C LYS C 50 3396 4891 4709 5 747 390 C ATOM 384 O LYS A 50 42.865 5.835 12.637 1.00 34.90 O ANISOU 384 O LYS C 50 3537 5537 4188 130 643 348 O ATOM 385 CB LYS A 50 44.846 5.245 15.265 1.00 36.30 C ANISOU 385 CB LYS C 50 3582 6026 4183 140 229 363 C ATOM 386 CG LYS A 50 43.463 4.748 15.652 1.00 44.99 C ANISOU 386 CG LYS C 50 4759 6862 5473 802 -824 439 C ATOM 387 CD LYS A 50 43.287 4.709 17.164 1.00 58.15 C ANISOU 387 CD LYS C 50 7857 8435 5801 -219 -2354 1304 C ATOM 388 CE LYS A 50 42.021 4.006 17.640 1.00 62.07 C ANISOU 388 CE LYS C 50 7631 9259 6695 -492 -3182 1119 C ATOM 389 NZ LYS A 50 42.272 2.844 18.534 1.00 67.58 N ANISOU 389 NZ LYS C 50 6656 10188 8835 -1236 -2240 -114 N ATOM 390 N ALA A 51 43.588 7.690 13.672 1.00 33.07 N ANISOU 390 N ALA C 51 3618 4766 4180 -56 576 739 N ATOM 391 CA ALA A 51 42.427 8.450 13.222 1.00 38.48 C ANISOU 391 CA ALA C 51 5429 4882 4308 -518 249 671 C ATOM 392 C ALA A 51 42.454 8.750 11.729 1.00 37.45 C ANISOU 392 C ALA C 51 5427 4726 4077 -234 819 774 C ATOM 393 O ALA A 51 41.417 8.744 11.043 1.00 39.04 O ANISOU 393 O ALA C 51 5435 4712 4686 -181 578 452 O ATOM 394 CB ALA A 51 42.332 9.764 13.994 1.00 38.64 C ANISOU 394 CB ALA C 51 6696 4148 3837 -483 1315 -169 C ATOM 395 N LEU A 52 43.637 9.036 11.173 1.00 35.68 N ANISOU 395 N LEU C 52 5046 4696 3814 -349 927 699 N ATOM 396 CA LEU A 52 43.705 9.247 9.728 1.00 33.57 C ANISOU 396 CA LEU C 52 4097 4791 3867 -151 930 194 C ATOM 397 C LEU A 52 43.228 7.994 8.991 1.00 36.49 C ANISOU 397 C LEU C 52 4286 5492 4087 -463 1111 -39 C ATOM 398 O LEU A 52 42.446 8.051 8.037 1.00 38.80 O ANISOU 398 O LEU C 52 4941 5301 4500 -245 1690 70 O ATOM 399 CB LEU A 52 45.130 9.577 9.300 1.00 35.41 C ANISOU 399 CB LEU C 52 4291 4751 4413 -274 184 39 C ATOM 400 CG LEU A 52 45.555 11.031 9.214 1.00 38.29 C ANISOU 400 CG LEU C 52 4407 4980 5163 -433 -340 505 C ATOM 401 CD1 LEU A 52 47.030 11.131 8.848 1.00 45.21 C ANISOU 401 CD1 LEU C 52 4596 5953 6630 -275 -507 2054 C ATOM 402 CD2 LEU A 52 44.674 11.783 8.216 1.00 41.23 C ANISOU 402 CD2 LEU C 52 5482 6511 3672 -1048 -925 517 C ATOM 403 N VAL A 53 43.713 6.833 9.430 1.00 34.15 N ANISOU 403 N VAL C 53 3484 5648 3844 -77 -36 542 N ATOM 404 CA VAL A 53 43.290 5.597 8.767 1.00 34.02 C ANISOU 404 CA VAL C 53 3492 5687 3746 6 -38 663 C ATOM 405 C VAL A 53 41.777 5.412 8.776 1.00 35.71 C ANISOU 405 C VAL C 53 3968 5688 3913 210 505 903 C ATOM 406 O VAL A 53 41.125 4.996 7.800 1.00 37.15 O ANISOU 406 O VAL C 53 5239 5205 3671 335 614 801 O ATOM 407 CB VAL A 53 44.002 4.431 9.469 1.00 34.43 C ANISOU 407 CB VAL C 53 3146 5744 4193 115 -316 640 C ATOM 408 CG1 VAL A 53 43.366 3.104 9.082 1.00 34.38 C ANISOU 408 CG1 VAL C 53 3037 5677 4350 336 -480 1600 C ATOM 409 CG2 VAL A 53 45.479 4.481 9.113 1.00 32.94 C ANISOU 409 CG2 VAL C 53 3012 5751 3754 300 394 532 C ATOM 410 N GLU A 54 41.196 5.752 9.926 1.00 36.62 N ANISOU 410 N GLU C 54 4243 5648 4023 367 921 994 N ATOM 411 CA GLU A 54 39.771 5.631 10.164 1.00 37.38 C ANISOU 411 CA GLU C 54 4634 5511 4059 340 472 836 C ATOM 412 C GLU A 54 38.986 6.496 9.174 1.00 38.61 C ANISOU 412 C GLU C 54 4553 5914 4205 351 560 489 C ATOM 413 O GLU A 54 38.010 6.057 8.550 1.00 41.06 O ANISOU 413 O GLU C 54 4916 6097 4589 -34 1338 407 O ATOM 414 CB GLU A 54 39.392 6.014 11.605 1.00 41.10 C ANISOU 414 CB GLU C 54 5125 6523 3967 353 -3 1093 C ATOM 415 CG GLU A 54 39.159 4.869 12.560 1.00 58.89 C ANISOU 415 CG GLU C 54 8324 8511 5542 -1348 -2116 1608 C ATOM 416 CD GLU A 54 39.211 5.269 14.025 1.00 65.60 C ANISOU 416 CD GLU C 54 9639 10092 5195 -2264 -2694 1559 C ATOM 417 OE1 GLU A 54 39.380 6.460 14.376 1.00 88.06 O ANISOU 417 OE1 GLU C 54 13342 12442 7675 -5923 49 1437 O ATOM 418 OE2 GLU A 54 39.078 4.373 14.894 1.00 87.65 O ANISOU 418 OE2 GLU C 54 14582 11984 6736 -3012 -5420 578 O ATOM 419 N MET A 55 39.438 7.739 9.055 1.00 39.25 N ANISOU 419 N MET C 55 4572 5933 4408 388 290 604 N ATOM 420 CA MET A 55 38.774 8.673 8.151 1.00 40.82 C ANISOU 420 CA MET C 55 5468 5886 4156 -399 382 995 C ATOM 421 C MET A 55 38.865 8.235 6.695 1.00 40.32 C ANISOU 421 C MET C 55 5277 5804 4237 -258 593 957 C ATOM 422 O MET A 55 37.971 8.443 5.857 1.00 41.77 O ANISOU 422 O MET C 55 5137 5985 4748 -205 1262 839 O ATOM 423 CB MET A 55 39.426 10.048 8.352 1.00 37.31 C ANISOU 423 CB MET C 55 5429 5474 3274 -54 447 305 C ATOM 424 CG MET A 55 39.166 10.582 9.759 1.00 37.55 C ANISOU 424 CG MET C 55 5293 5936 3040 76 223 264 C ATOM 425 SD MET A 55 39.862 12.232 9.976 1.00 42.14 S ANISOU 425 SD MET C 55 5526 5570 4915 -157 981 545 S ATOM 426 CE MET A 55 38.641 13.239 9.118 1.00 45.49 C ANISOU 426 CE MET C 55 6271 6996 4015 -1031 738 -217 C ATOM 427 N HIS A 56 40.008 7.618 6.380 1.00 40.28 N ANISOU 427 N HIS C 56 4606 5840 4861 -327 1653 1152 N ATOM 428 CA HIS A 56 40.248 7.096 5.032 1.00 36.50 C ANISOU 428 CA HIS C 56 4299 5254 4317 438 1371 679 C ATOM 429 C HIS A 56 39.253 5.982 4.766 1.00 37.39 C ANISOU 429 C HIS C 56 4325 5505 4376 325 1460 -163 C ATOM 430 O HIS A 56 38.567 5.844 3.753 1.00 42.59 O ANISOU 430 O HIS C 56 5264 6224 4696 -194 2341 -302 O ATOM 431 CB HIS A 56 41.679 6.560 4.898 1.00 35.48 C ANISOU 431 CB HIS C 56 4505 5119 3858 263 1363 337 C ATOM 432 CG HIS A 56 41.857 5.849 3.584 1.00 35.58 C ANISOU 432 CG HIS C 56 4589 4952 3976 201 1449 293 C ATOM 433 ND1 HIS A 56 41.643 6.461 2.365 1.00 35.66 N ANISOU 433 ND1 HIS C 56 4452 5245 3851 87 1267 567 N ATOM 434 CD2 HIS A 56 42.201 4.572 3.303 1.00 37.60 C ANISOU 434 CD2 HIS C 56 5221 4959 4106 -114 1382 360 C ATOM 435 CE1 HIS A 56 41.859 5.598 1.391 1.00 37.12 C ANISOU 435 CE1 HIS C 56 4915 5180 4010 -158 1590 277 C ATOM 436 NE2 HIS A 56 42.203 4.437 1.925 1.00 37.17 N ANISOU 436 NE2 HIS C 56 4672 5325 4126 -86 1582 188 N ATOM 437 N LYS A 57 39.168 5.107 5.779 1.00 41.30 N ANISOU 437 N LYS C 57 4464 6290 4937 -121 1128 -94 N ATOM 438 CA LYS A 57 38.261 3.964 5.605 1.00 43.41 C ANISOU 438 CA LYS C 57 4456 6226 5813 -116 1049 104 C ATOM 439 C LYS A 57 36.829 4.451 5.557 1.00 44.80 C ANISOU 439 C LYS C 57 4939 6334 5749 138 1462 5 C ATOM 440 O LYS A 57 35.970 3.848 4.911 1.00 50.05 O ANISOU 440 O LYS C 57 5462 6879 6674 355 2127 44 O ATOM 441 CB LYS A 57 38.536 2.927 6.701 1.00 44.48 C ANISOU 441 CB LYS C 57 4340 6575 5985 166 906 -158 C ATOM 442 CG LYS A 57 39.992 2.461 6.643 1.00 51.01 C ANISOU 442 CG LYS C 57 6070 6341 6971 -158 1498 -455 C ATOM 443 CD LYS A 57 40.229 1.300 7.588 1.00 56.88 C ANISOU 443 CD LYS C 57 6968 7301 7343 -997 1728 -1021 C ATOM 444 CE LYS A 57 41.137 0.264 6.938 1.00 64.05 C ANISOU 444 CE LYS C 57 8349 7361 8627 -1687 2644 -1279 C ATOM 445 NZ LYS A 57 41.568 -0.786 7.922 1.00 78.18 N ANISOU 445 NZ LYS C 57 13083 8827 7794 -4030 3470 -2024 N ATOM 446 N ALA A 58 36.511 5.571 6.192 1.00 42.30 N ANISOU 446 N ALA C 58 4369 5980 5724 145 968 -91 N ATOM 447 CA ALA A 58 35.136 6.043 6.174 1.00 42.20 C ANISOU 447 CA ALA C 58 3914 6116 6006 458 1348 -142 C ATOM 448 C ALA A 58 34.860 6.778 4.876 1.00 43.86 C ANISOU 448 C ALA C 58 5241 5672 5750 264 1375 67 C ATOM 449 O ALA A 58 33.775 7.327 4.681 1.00 47.11 O ANISOU 449 O ALA C 58 5609 5777 6512 631 1364 -245 O ATOM 450 CB ALA A 58 34.880 6.951 7.367 1.00 40.88 C ANISOU 450 CB ALA C 58 4030 5802 5701 512 1062 -162 C ATOM 451 N GLY A 59 35.845 6.799 3.990 1.00 42.92 N ANISOU 451 N GLY C 59 4849 5919 5541 87 1691 300 N ATOM 452 CA GLY A 59 35.698 7.470 2.716 1.00 41.52 C ANISOU 452 CA GLY C 59 5229 5218 5327 449 1947 220 C ATOM 453 C GLY A 59 35.809 8.977 2.827 1.00 42.22 C ANISOU 453 C GLY C 59 5145 5719 5179 358 1743 -268 C ATOM 454 O GLY A 59 35.255 9.676 1.958 1.00 50.77 O ANISOU 454 O GLY C 59 6546 7108 5637 -812 2419 -1105 O ATOM 455 N GLN A 60 36.496 9.527 3.840 1.00 40.36 N ANISOU 455 N GLN C 60 5158 5593 4585 343 1617 281 N ATOM 456 CA GLN A 60 36.531 10.992 3.927 1.00 42.17 C ANISOU 456 CA GLN C 60 5305 5372 5345 297 1772 391 C ATOM 457 C GLN A 60 37.777 11.604 3.298 1.00 42.03 C ANISOU 457 C GLN C 60 5129 5202 5637 118 1539 193 C ATOM 458 O GLN A 60 37.941 12.816 3.110 1.00 41.80 O ANISOU 458 O GLN C 60 5215 5402 5265 4 1695 -339 O ATOM 459 CB GLN A 60 36.430 11.418 5.389 1.00 43.43 C ANISOU 459 CB GLN C 60 4704 6522 5274 -49 1679 279 C ATOM 460 CG GLN A 60 35.201 10.908 6.130 1.00 49.81 C ANISOU 460 CG GLN C 60 5483 7271 6171 -728 312 1074 C ATOM 461 CD GLN A 60 35.347 11.080 7.631 1.00 56.33 C ANISOU 461 CD GLN C 60 6998 8291 6113 -1600 309 1365 C ATOM 462 OE1 GLN A 60 35.712 12.152 8.111 1.00 64.84 O ANISOU 462 OE1 GLN C 60 8153 10132 6352 -3034 1176 828 O ATOM 463 NE2 GLN A 60 35.089 10.052 8.425 1.00 65.00 N ANISOU 463 NE2 GLN C 60 7738 10357 6604 -1472 135 -715 N ATOM 464 N VAL A 61 38.731 10.740 2.937 1.00 40.33 N ANISOU 464 N VAL C 61 4988 4883 5451 458 1903 -213 N ATOM 465 CA VAL A 61 39.983 11.258 2.389 1.00 38.51 C ANISOU 465 CA VAL C 61 4772 5192 4668 108 1718 -6 C ATOM 466 C VAL A 61 40.673 10.188 1.554 1.00 38.79 C ANISOU 466 C VAL C 61 4662 5459 4616 53 1839 17 C ATOM 467 O VAL A 61 40.631 8.984 1.790 1.00 38.01 O ANISOU 467 O VAL C 61 5177 5154 4111 -178 1776 -439 O ATOM 468 CB VAL A 61 40.896 11.744 3.533 1.00 35.87 C ANISOU 468 CB VAL C 61 3459 5851 4319 38 1149 136 C ATOM 469 CG1 VAL A 61 41.383 10.573 4.379 1.00 34.05 C ANISOU 469 CG1 VAL C 61 3899 4739 4300 -57 1588 390 C ATOM 470 CG2 VAL A 61 42.116 12.525 3.048 1.00 38.36 C ANISOU 470 CG2 VAL C 61 4114 5000 5463 207 905 784 C ATOM 471 N SER A 62 41.358 10.646 0.518 1.00 37.71 N ANISOU 471 N SER C 62 5016 5335 3977 -210 1931 -311 N ATOM 472 CA SER A 62 42.169 9.751 -0.292 1.00 37.37 C ANISOU 472 CA SER C 62 5117 5136 3946 -253 1835 -455 C ATOM 473 C SER A 62 43.617 10.237 -0.320 1.00 36.60 C ANISOU 473 C SER C 62 4929 5187 3790 -330 1269 -663 C ATOM 474 O SER A 62 43.842 11.452 -0.397 1.00 36.49 O ANISOU 474 O SER C 62 5074 5273 3517 -543 949 191 O ATOM 475 CB SER A 62 41.580 9.660 -1.702 1.00 38.05 C ANISOU 475 CB SER C 62 5419 5105 3934 -500 1942 -461 C ATOM 476 OG SER A 62 42.408 8.811 -2.474 1.00 39.31 O ANISOU 476 OG SER C 62 5994 5146 3794 -33 1566 -189 O ATOM 477 N PHE A 63 44.568 9.315 -0.266 1.00 34.91 N ANISOU 477 N PHE C 63 4813 5129 3321 -286 441 -70 N ATOM 478 CA PHE A 63 45.976 9.680 -0.334 1.00 36.39 C ANISOU 478 CA PHE C 63 4612 5181 4035 -376 400 135 C ATOM 479 C PHE A 63 46.583 9.387 -1.705 1.00 36.50 C ANISOU 479 C PHE C 63 4735 4958 4175 -34 786 186 C ATOM 480 O PHE A 63 47.819 9.427 -1.811 1.00 38.39 O ANISOU 480 O PHE C 63 5144 4391 5052 -390 1827 750 O ATOM 481 CB PHE A 63 46.741 8.942 0.772 1.00 36.21 C ANISOU 481 CB PHE C 63 4572 4909 4277 -185 524 46 C ATOM 482 CG PHE A 63 46.262 9.436 2.144 1.00 36.61 C ANISOU 482 CG PHE C 63 4825 4951 4133 -434 306 -78 C ATOM 483 CD1 PHE A 63 46.719 10.626 2.679 1.00 36.87 C ANISOU 483 CD1 PHE C 63 5009 5238 3761 -73 617 -241 C ATOM 484 CD2 PHE A 63 45.350 8.693 2.864 1.00 37.65 C ANISOU 484 CD2 PHE C 63 5038 4681 4585 -129 290 152 C ATOM 485 CE1 PHE A 63 46.288 11.120 3.901 1.00 33.38 C ANISOU 485 CE1 PHE C 63 4701 4616 3368 641 566 -647 C ATOM 486 CE2 PHE A 63 44.908 9.150 4.078 1.00 35.30 C ANISOU 486 CE2 PHE C 63 4691 4592 4131 692 760 -337 C ATOM 487 CZ PHE A 63 45.375 10.348 4.598 1.00 35.04 C ANISOU 487 CZ PHE C 63 4500 4689 4124 616 532 -552 C ATOM 488 N LYS A 64 45.767 9.112 -2.711 1.00 38.20 N ANISOU 488 N LYS C 64 5030 5353 4130 -38 730 -177 N ATOM 489 CA LYS A 64 46.204 8.832 -4.068 1.00 40.02 C ANISOU 489 CA LYS C 64 5502 5507 4198 300 823 -81 C ATOM 490 C LYS A 64 47.136 9.897 -4.637 1.00 37.29 C ANISOU 490 C LYS C 64 5325 4801 4043 -159 918 157 C ATOM 491 O LYS A 64 48.094 9.595 -5.340 1.00 38.94 O ANISOU 491 O LYS C 64 5244 5721 3830 -406 1042 819 O ATOM 492 CB LYS A 64 44.994 8.769 -5.013 1.00 46.94 C ANISOU 492 CB LYS C 64 5209 7329 5298 -39 2426 -724 C ATOM 493 CG LYS A 64 44.845 7.497 -5.818 1.00 63.62 C ANISOU 493 CG LYS C 64 6935 9358 7882 -2352 3791 -1694 C ATOM 494 CD LYS A 64 44.627 6.291 -4.914 1.00 78.52 C ANISOU 494 CD LYS C 64 7690 11352 10791 -3655 2791 -1979 C ATOM 495 CE LYS A 64 44.018 5.110 -5.652 1.00 84.39 C ANISOU 495 CE LYS C 64 7679 12216 12171 -4131 3197 -2918 C ATOM 496 NZ LYS A 64 44.837 3.869 -5.479 1.00 86.17 N ANISOU 496 NZ LYS C 64 6178 12119 14443 -3347 2915 -3978 N ATOM 497 N HIS A 65 46.842 11.171 -4.347 1.00 36.57 N ANISOU 497 N HIS C 65 5551 4340 4002 -26 1786 -468 N ATOM 498 CA HIS A 65 47.721 12.233 -4.842 1.00 38.83 C ANISOU 498 CA HIS C 65 5328 5346 4082 -462 1852 -408 C ATOM 499 C HIS A 65 48.330 13.017 -3.686 1.00 38.25 C ANISOU 499 C HIS C 65 5120 5684 3728 -1069 1583 -694 C ATOM 500 O HIS A 65 48.493 14.240 -3.718 1.00 41.41 O ANISOU 500 O HIS C 65 5806 6432 3494 -2087 1577 86 O ATOM 501 CB HIS A 65 46.973 13.160 -5.813 1.00 40.34 C ANISOU 501 CB HIS C 65 5878 5839 3610 -755 1960 -446 C ATOM 502 CG HIS A 65 46.457 12.329 -6.965 1.00 40.80 C ANISOU 502 CG HIS C 65 5719 5801 3983 -378 2110 -308 C ATOM 503 ND1 HIS A 65 47.297 11.509 -7.684 1.00 43.19 N ANISOU 503 ND1 HIS C 65 6066 5694 4649 -380 2888 -350 N ATOM 504 CD2 HIS A 65 45.234 12.168 -7.498 1.00 40.00 C ANISOU 504 CD2 HIS C 65 5536 5771 3890 -317 1611 -476 C ATOM 505 CE1 HIS A 65 46.618 10.882 -8.629 1.00 42.44 C ANISOU 505 CE1 HIS C 65 5471 5790 4863 -448 2721 -458 C ATOM 506 NE2 HIS A 65 45.357 11.265 -8.538 1.00 41.61 N ANISOU 506 NE2 HIS C 65 5402 5891 4518 -294 2141 -579 N ATOM 507 N VAL A 66 48.677 12.291 -2.627 1.00 37.49 N ANISOU 507 N VAL C 66 5759 5103 3382 -1048 1137 -45 N ATOM 508 CA VAL A 66 49.375 12.882 -1.486 1.00 32.58 C ANISOU 508 CA VAL C 66 4729 4641 3010 -406 319 -29 C ATOM 509 C VAL A 66 50.808 12.356 -1.533 1.00 33.64 C ANISOU 509 C VAL C 66 4180 4617 3983 -624 -195 260 C ATOM 510 O VAL A 66 51.028 11.153 -1.667 1.00 33.70 O ANISOU 510 O VAL C 66 4237 4861 3709 -609 849 178 O ATOM 511 CB VAL A 66 48.705 12.580 -0.138 1.00 30.79 C ANISOU 511 CB VAL C 66 3995 4534 3171 -53 257 -274 C ATOM 512 CG1 VAL A 66 49.583 13.076 0.999 1.00 28.54 C ANISOU 512 CG1 VAL C 66 3481 4398 2965 -354 114 -163 C ATOM 513 CG2 VAL A 66 47.334 13.235 -0.081 1.00 30.17 C ANISOU 513 CG2 VAL C 66 4545 4483 2433 -485 1011 -15 C ATOM 514 N VAL A 67 51.761 13.266 -1.450 1.00 31.87 N ANISOU 514 N VAL C 67 4128 4521 3461 -709 -113 361 N ATOM 515 CA VAL A 67 53.176 12.900 -1.425 1.00 30.76 C ANISOU 515 CA VAL C 67 4351 4529 2807 -642 557 496 C ATOM 516 C VAL A 67 53.663 13.110 -0.004 1.00 32.92 C ANISOU 516 C VAL C 67 5272 4611 2623 -1317 528 447 C ATOM 517 O VAL A 67 53.277 14.120 0.571 1.00 30.50 O ANISOU 517 O VAL C 67 4243 4471 2876 -943 593 329 O ATOM 518 CB VAL A 67 53.990 13.752 -2.413 1.00 29.57 C ANISOU 518 CB VAL C 67 4338 4257 2639 -267 644 21 C ATOM 519 CG1 VAL A 67 55.483 13.729 -2.135 1.00 30.25 C ANISOU 519 CG1 VAL C 67 3849 4230 3417 -556 1119 -73 C ATOM 520 CG2 VAL A 67 53.674 13.287 -3.844 1.00 30.09 C ANISOU 520 CG2 VAL C 67 4433 4375 2624 -348 692 -66 C ATOM 521 N THR A 68 54.458 12.198 0.535 1.00 28.03 N ANISOU 521 N THR C 68 3537 4225 2890 -529 249 556 N ATOM 522 CA THR A 68 54.922 12.362 1.895 1.00 29.02 C ANISOU 522 CA THR C 68 3571 4427 3030 -384 231 247 C ATOM 523 C THR A 68 56.447 12.328 1.988 1.00 30.37 C ANISOU 523 C THR C 68 3931 4335 3271 -363 415 481 C ATOM 524 O THR A 68 57.092 11.646 1.191 1.00 30.55 O ANISOU 524 O THR C 68 3681 5014 2912 -8 120 888 O ATOM 525 CB THR A 68 54.384 11.263 2.840 1.00 29.30 C ANISOU 525 CB THR C 68 3836 4069 3229 -676 13 152 C ATOM 526 OG1 THR A 68 54.884 9.992 2.379 1.00 32.78 O ANISOU 526 OG1 THR C 68 4298 4521 3636 -1125 476 -23 O ATOM 527 CG2 THR A 68 52.870 11.174 2.840 1.00 29.46 C ANISOU 527 CG2 THR C 68 3888 4619 2685 -190 116 216 C ATOM 528 N PHE A 69 56.959 13.040 2.988 1.00 26.17 N ANISOU 528 N PHE C 69 3142 3973 2828 -405 -171 461 N ATOM 529 CA PHE A 69 58.353 13.106 3.380 1.00 28.36 C ANISOU 529 CA PHE C 69 4053 3805 2918 -327 39 377 C ATOM 530 C PHE A 69 58.450 12.831 4.874 1.00 28.95 C ANISOU 530 C PHE C 69 4260 3775 2963 -296 -115 416 C ATOM 531 O PHE A 69 57.802 13.555 5.664 1.00 28.25 O ANISOU 531 O PHE C 69 3897 3916 2922 -395 166 336 O ATOM 532 CB PHE A 69 58.949 14.479 3.073 1.00 27.11 C ANISOU 532 CB PHE C 69 3946 3445 2910 366 -37 248 C ATOM 533 CG PHE A 69 59.218 14.709 1.589 1.00 29.98 C ANISOU 533 CG PHE C 69 4332 4143 2916 -201 -101 390 C ATOM 534 CD1 PHE A 69 58.302 15.359 0.778 1.00 28.94 C ANISOU 534 CD1 PHE C 69 3373 4621 3001 -218 45 10 C ATOM 535 CD2 PHE A 69 60.406 14.266 1.011 1.00 29.05 C ANISOU 535 CD2 PHE C 69 3395 4491 3153 -163 -363 721 C ATOM 536 CE1 PHE A 69 58.571 15.545 -0.580 1.00 32.19 C ANISOU 536 CE1 PHE C 69 4194 4791 3244 -637 -524 139 C ATOM 537 CE2 PHE A 69 60.678 14.446 -0.347 1.00 29.75 C ANISOU 537 CE2 PHE C 69 3479 4711 3115 -454 -360 666 C ATOM 538 CZ PHE A 69 59.749 15.095 -1.150 1.00 30.71 C ANISOU 538 CZ PHE C 69 3704 4962 3002 -824 566 495 C ATOM 539 N ASN A 70 59.223 11.828 5.274 1.00 30.06 N ANISOU 539 N ASN C 70 4586 4001 2834 -680 375 281 N ATOM 540 CA ASN A 70 59.385 11.573 6.713 1.00 29.07 C ANISOU 540 CA ASN C 70 4588 3587 2872 -24 68 333 C ATOM 541 C ASN A 70 60.590 12.323 7.269 1.00 29.49 C ANISOU 541 C ASN C 70 4517 3953 2734 -58 233 569 C ATOM 542 O ASN A 70 61.557 12.603 6.548 1.00 31.09 O ANISOU 542 O ASN C 70 3473 5192 3147 -294 65 920 O ATOM 543 CB ASN A 70 59.522 10.073 6.953 1.00 29.68 C ANISOU 543 CB ASN C 70 4644 4010 2622 -236 660 -339 C ATOM 544 CG ASN A 70 58.207 9.505 7.445 1.00 30.70 C ANISOU 544 CG ASN C 70 4485 4351 2830 -322 261 -659 C ATOM 545 OD1 ASN A 70 57.298 9.281 6.643 1.00 29.40 O ANISOU 545 OD1 ASN C 70 3944 4144 3082 -610 749 -266 O ATOM 546 ND2 ASN A 70 58.110 9.273 8.759 1.00 31.69 N ANISOU 546 ND2 ASN C 70 4365 4965 2709 -885 503 -33 N ATOM 547 N MET A 71 60.569 12.660 8.548 1.00 30.26 N ANISOU 547 N MET C 71 4718 4257 2522 -619 19 126 N ATOM 548 CA MET A 71 61.597 13.462 9.188 1.00 35.32 C ANISOU 548 CA MET C 71 5264 4956 3202 -786 731 -453 C ATOM 549 C MET A 71 62.945 12.756 9.307 1.00 33.84 C ANISOU 549 C MET C 71 4434 4942 3480 -273 159 -110 C ATOM 550 O MET A 71 63.989 13.414 9.244 1.00 34.08 O ANISOU 550 O MET C 71 4080 5334 3533 -667 -539 991 O ATOM 551 CB MET A 71 61.171 13.877 10.622 1.00 33.33 C ANISOU 551 CB MET C 71 4725 4761 3178 347 567 -368 C ATOM 552 CG MET A 71 60.003 14.833 10.695 1.00 39.27 C ANISOU 552 CG MET C 71 5876 5010 4034 -447 1789 -208 C ATOM 553 SD MET A 71 59.775 15.629 12.304 1.00 43.40 S ANISOU 553 SD MET C 71 6840 5791 3859 -207 1793 -100 S ATOM 554 CE MET A 71 60.499 14.387 13.383 1.00 41.95 C ANISOU 554 CE MET C 71 7854 4657 3430 -390 565 1391 C ATOM 555 N ASP A 72 62.930 11.430 9.521 1.00 27.73 N ANISOU 555 N ASP C 72 3999 3840 2697 424 -414 894 N ATOM 556 CA ASP A 72 64.198 10.785 9.819 1.00 33.08 C ANISOU 556 CA ASP C 72 4116 4226 4227 316 867 -224 C ATOM 557 C ASP A 72 64.191 9.273 9.609 1.00 34.95 C ANISOU 557 C ASP C 72 4227 4434 4617 -87 -49 -111 C ATOM 558 O ASP A 72 63.151 8.678 9.303 1.00 34.87 O ANISOU 558 O ASP C 72 4536 4410 4302 -599 1563 41 O ATOM 559 CB ASP A 72 64.558 11.126 11.266 1.00 44.06 C ANISOU 559 CB ASP C 72 8100 4460 4179 -904 1573 -158 C ATOM 560 CG ASP A 72 63.393 11.176 12.227 1.00 45.45 C ANISOU 560 CG ASP C 72 7717 5146 4405 -817 1610 227 C ATOM 561 OD1 ASP A 72 62.398 10.426 12.074 1.00 53.37 O ANISOU 561 OD1 ASP C 72 7062 6641 6577 -863 359 -146 O ATOM 562 OD2 ASP A 72 63.464 11.980 13.176 1.00 51.96 O ANISOU 562 OD2 ASP C 72 9349 5745 4650 -1909 1927 489 O ATOM 563 N GLU A 73 65.373 8.671 9.770 1.00 36.89 N ANISOU 563 N GLU C 73 5316 4442 4257 -233 830 -91 N ATOM 564 CA GLU A 73 65.620 7.237 9.672 1.00 39.23 C ANISOU 564 CA GLU C 73 6067 4619 4219 -758 722 -146 C ATOM 565 C GLU A 73 66.940 6.876 10.352 1.00 37.56 C ANISOU 565 C GLU C 73 5713 4623 3935 -492 333 21 C ATOM 566 O GLU A 73 67.896 7.660 10.394 1.00 40.77 O ANISOU 566 O GLU C 73 5444 5701 4344 -700 972 -594 O ATOM 567 CB GLU A 73 65.601 6.778 8.209 1.00 34.97 C ANISOU 567 CB GLU C 73 4785 4198 4304 107 553 228 C ATOM 568 CG GLU A 73 65.748 5.284 7.972 1.00 42.01 C ANISOU 568 CG GLU C 73 5410 5682 4869 -845 554 426 C ATOM 569 CD GLU A 73 64.673 4.411 8.617 1.00 41.86 C ANISOU 569 CD GLU C 73 5233 6069 4603 -1168 280 -224 C ATOM 570 OE1 GLU A 73 64.784 4.174 9.849 1.00 39.20 O ANISOU 570 OE1 GLU C 73 4960 5439 4493 -1399 763 -263 O ATOM 571 OE2 GLU A 73 63.749 3.977 7.857 1.00 38.00 O ANISOU 571 OE2 GLU C 73 4982 6112 3345 -1143 204 643 O ATOM 572 N TYR A 74 66.987 5.660 10.910 1.00 37.36 N ANISOU 572 N TYR C 74 5673 4875 3647 -565 541 -202 N ATOM 573 CA TYR A 74 68.227 5.155 11.479 1.00 41.28 C ANISOU 573 CA TYR C 74 5667 5053 4964 -481 541 -711 C ATOM 574 C TYR A 74 69.243 4.814 10.397 1.00 41.19 C ANISOU 574 C TYR C 74 5495 4709 5448 -293 751 -648 C ATOM 575 O TYR A 74 68.908 4.308 9.312 1.00 39.71 O ANISOU 575 O TYR C 74 5055 4567 5465 -126 667 -328 O ATOM 576 CB TYR A 74 68.002 3.889 12.294 1.00 41.08 C ANISOU 576 CB TYR C 74 5489 4886 5233 -454 679 -990 C ATOM 577 CG TYR A 74 67.345 4.115 13.631 1.00 43.17 C ANISOU 577 CG TYR C 74 6067 5477 4860 -1198 336 -1187 C ATOM 578 CD1 TYR A 74 67.904 4.924 14.604 1.00 45.76 C ANISOU 578 CD1 TYR C 74 6685 5643 5060 -1237 755 -1295 C ATOM 579 CD2 TYR A 74 66.133 3.494 13.908 1.00 43.30 C ANISOU 579 CD2 TYR C 74 5970 6098 4385 -1347 42 -628 C ATOM 580 CE1 TYR A 74 67.254 5.093 15.813 1.00 50.27 C ANISOU 580 CE1 TYR C 74 7361 6441 5297 -1381 916 -798 C ATOM 581 CE2 TYR A 74 65.481 3.658 15.110 1.00 46.74 C ANISOU 581 CE2 TYR C 74 6844 6625 4291 -1476 254 -474 C ATOM 582 CZ TYR A 74 66.050 4.469 16.071 1.00 50.91 C ANISOU 582 CZ TYR C 74 7258 7085 5001 -1429 845 -134 C ATOM 583 OH TYR A 74 65.402 4.636 17.280 1.00 55.75 O ANISOU 583 OH TYR C 74 8276 8611 4294 -813 895 -463 O ATOM 584 N VAL A 75 70.498 5.094 10.726 1.00 42.13 N ANISOU 584 N VAL C 75 4919 5224 5863 -261 738 -759 N ATOM 585 CA VAL A 75 71.588 4.761 9.806 1.00 47.19 C ANISOU 585 CA VAL C 75 5788 5097 7045 -33 166 -493 C ATOM 586 C VAL A 75 72.034 3.320 10.055 1.00 48.55 C ANISOU 586 C VAL C 75 6285 5224 6940 -454 735 -542 C ATOM 587 O VAL A 75 72.149 2.961 11.238 1.00 48.47 O ANISOU 587 O VAL C 75 5693 5860 6862 -1170 726 -226 O ATOM 588 CB VAL A 75 72.774 5.727 9.982 1.00 48.86 C ANISOU 588 CB VAL C 75 6013 5205 7348 131 647 -104 C ATOM 589 CG1 VAL A 75 74.035 5.138 9.356 1.00 53.29 C ANISOU 589 CG1 VAL C 75 6667 5126 8455 481 1334 91 C ATOM 590 CG2 VAL A 75 72.478 7.110 9.404 1.00 43.92 C ANISOU 590 CG2 VAL C 75 5319 5653 5715 67 1547 -167 C ATOM 591 N GLY A 76 72.258 2.528 9.021 1.00 50.75 N ANISOU 591 N GLY C 76 7221 5344 6717 -516 356 -120 N ATOM 592 CA GLY A 76 72.790 1.181 9.073 1.00 50.36 C ANISOU 592 CA GLY C 76 6827 5542 6765 -498 1207 -437 C ATOM 593 C GLY A 76 71.838 0.113 9.554 1.00 52.70 C ANISOU 593 C GLY C 76 6657 6001 7365 -559 1338 -104 C ATOM 594 O GLY A 76 72.167 -1.056 9.776 1.00 53.35 O ANISOU 594 O GLY C 76 6451 6305 7513 -727 1657 -39 O ATOM 595 N LEU A 77 70.577 0.473 9.753 1.00 51.62 N ANISOU 595 N LEU C 77 6184 6058 7372 -182 2057 -442 N ATOM 596 CA LEU A 77 69.583 -0.510 10.181 1.00 51.42 C ANISOU 596 CA LEU C 77 6268 6170 7100 -353 1735 -602 C ATOM 597 C LEU A 77 68.939 -1.044 8.916 1.00 48.97 C ANISOU 597 C LEU C 77 5514 6321 6772 -359 1217 -704 C ATOM 598 O LEU A 77 68.603 -0.200 8.071 1.00 53.77 O ANISOU 598 O LEU C 77 7868 6544 6016 -2227 1383 112 O ATOM 599 CB LEU A 77 68.588 0.181 11.086 1.00 52.44 C ANISOU 599 CB LEU C 77 7136 6167 6620 -351 1335 -752 C ATOM 600 CG LEU A 77 67.995 -0.529 12.291 1.00 54.52 C ANISOU 600 CG LEU C 77 7227 5709 7779 133 600 -1018 C ATOM 601 CD1 LEU A 77 66.472 -0.493 12.216 1.00 54.85 C ANISOU 601 CD1 LEU C 77 5875 7127 7838 795 1700 -2120 C ATOM 602 CD2 LEU A 77 68.485 -1.961 12.405 1.00 59.94 C ANISOU 602 CD2 LEU C 77 7100 6902 8774 -680 -44 781 C ATOM 603 N PRO A 78 68.766 -2.343 8.715 1.00 49.97 N ANISOU 603 N PRO C 78 5464 6640 6884 -337 1061 -178 N ATOM 604 CA PRO A 78 68.074 -2.789 7.489 1.00 51.66 C ANISOU 604 CA PRO C 78 5460 6928 7242 -311 1309 -262 C ATOM 605 C PRO A 78 66.647 -2.243 7.428 1.00 48.74 C ANISOU 605 C PRO C 78 5262 6812 6445 -642 1623 -73 C ATOM 606 O PRO A 78 65.937 -2.315 8.437 1.00 51.65 O ANISOU 606 O PRO C 78 6508 6970 6146 -1049 2070 410 O ATOM 607 CB PRO A 78 68.065 -4.308 7.624 1.00 54.45 C ANISOU 607 CB PRO C 78 6132 6946 7612 -961 1705 -379 C ATOM 608 CG PRO A 78 69.142 -4.627 8.605 1.00 52.18 C ANISOU 608 CG PRO C 78 5589 6980 7258 -538 1438 -211 C ATOM 609 CD PRO A 78 69.196 -3.467 9.559 1.00 49.69 C ANISOU 609 CD PRO C 78 5322 6615 6941 -498 978 73 C ATOM 610 N LYS A 79 66.211 -1.709 6.295 1.00 48.19 N ANISOU 610 N LYS C 79 5083 7123 6104 -876 2386 -94 N ATOM 611 CA LYS A 79 64.874 -1.150 6.153 1.00 54.40 C ANISOU 611 CA LYS C 79 7407 6964 6298 -1288 1942 -134 C ATOM 612 C LYS A 79 63.786 -2.088 6.664 1.00 53.90 C ANISOU 612 C LYS C 79 7398 6095 6984 -536 2690 4 C ATOM 613 O LYS A 79 62.826 -1.662 7.318 1.00 58.96 O ANISOU 613 O LYS C 79 8627 5807 7968 -892 2034 91 O ATOM 614 CB LYS A 79 64.591 -0.805 4.687 1.00 64.52 C ANISOU 614 CB LYS C 79 10277 7584 6653 -3394 1702 -620 C ATOM 615 CG LYS A 79 65.024 0.589 4.264 1.00 81.09 C ANISOU 615 CG LYS C 79 12443 9681 8687 -6045 205 -51 C ATOM 616 CD LYS A 79 64.290 1.040 3.000 1.00 94.67 C ANISOU 616 CD LYS C 79 16385 10464 9120 -7758 -149 -552 C ATOM 617 CE LYS A 79 64.605 2.490 2.648 1.00100.31 C ANISOU 617 CE LYS C 79 17239 10681 10196 -8238 -1562 180 C ATOM 618 NZ LYS A 79 63.419 3.318 2.259 1.00 99.23 N ANISOU 618 NZ LYS C 79 16487 9198 12017 -7898 -3093 3219 N ATOM 619 N GLU A 80 63.885 -3.384 6.389 1.00 55.66 N ANISOU 619 N GLU C 80 7175 6753 7220 -583 2365 620 N ATOM 620 CA GLU A 80 62.858 -4.311 6.860 1.00 59.52 C ANISOU 620 CA GLU C 80 7348 7740 7526 -424 2377 1678 C ATOM 621 C GLU A 80 63.009 -4.657 8.335 1.00 58.33 C ANISOU 621 C GLU C 80 7538 6988 7636 -723 2023 1750 C ATOM 622 O GLU A 80 62.214 -5.452 8.853 1.00 60.27 O ANISOU 622 O GLU C 80 7470 6869 8561 -1035 1553 1201 O ATOM 623 CB GLU A 80 62.831 -5.622 6.058 1.00 68.18 C ANISOU 623 CB GLU C 80 7326 10033 8545 -363 3156 1880 C ATOM 624 CG GLU A 80 61.520 -5.827 5.308 1.00 79.36 C ANISOU 624 CG GLU C 80 8602 11058 10492 -46 4197 1108 C ATOM 625 CD GLU A 80 60.573 -6.877 5.849 1.00 85.38 C ANISOU 625 CD GLU C 80 8638 11323 12480 946 4294 1367 C ATOM 626 OE1 GLU A 80 60.256 -7.862 5.127 1.00 99.94 O ANISOU 626 OE1 GLU C 80 8592 11873 17506 -1411 5570 441 O ATOM 627 OE2 GLU A 80 60.115 -6.732 7.010 1.00102.82 O ANISOU 627 OE2 GLU C 80 12178 12381 14509 1275 2104 3815 O ATOM 628 N HIS A 81 63.979 -4.110 9.060 1.00 57.52 N ANISOU 628 N HIS C 81 7404 6948 7504 -1180 1928 1251 N ATOM 629 CA HIS A 81 63.917 -4.310 10.517 1.00 55.43 C ANISOU 629 CA HIS C 81 5668 7555 7838 -647 972 401 C ATOM 630 C HIS A 81 62.605 -3.708 11.004 1.00 51.01 C ANISOU 630 C HIS C 81 5461 7634 6288 -559 567 149 C ATOM 631 O HIS A 81 62.171 -2.633 10.580 1.00 45.52 O ANISOU 631 O HIS C 81 5018 7368 4909 -184 648 374 O ATOM 632 CB HIS A 81 65.132 -3.688 11.200 1.00 57.02 C ANISOU 632 CB HIS C 81 6080 7270 8314 -800 939 -523 C ATOM 633 CG HIS A 81 65.165 -3.870 12.685 1.00 60.06 C ANISOU 633 CG HIS C 81 6354 8163 8302 -1518 1174 -661 C ATOM 634 ND1 HIS A 81 66.051 -4.734 13.301 1.00 61.95 N ANISOU 634 ND1 HIS C 81 6815 8307 8417 -1426 1148 -885 N ATOM 635 CD2 HIS A 81 64.455 -3.345 13.701 1.00 60.36 C ANISOU 635 CD2 HIS C 81 6050 8619 8265 -1854 520 -442 C ATOM 636 CE1 HIS A 81 65.874 -4.716 14.615 1.00 62.89 C ANISOU 636 CE1 HIS C 81 6559 8713 8624 -1590 -243 -604 C ATOM 637 NE2 HIS A 81 64.894 -3.866 14.890 1.00 62.21 N ANISOU 637 NE2 HIS C 81 6300 8795 8540 -1619 -512 -427 N ATOM 638 N PRO A 82 61.890 -4.347 11.915 1.00 54.15 N ANISOU 638 N PRO C 82 6012 8050 6511 -1228 -93 49 N ATOM 639 CA PRO A 82 60.575 -3.848 12.311 1.00 54.66 C ANISOU 639 CA PRO C 82 6053 8363 6353 -1964 -1118 871 C ATOM 640 C PRO A 82 60.598 -2.502 13.037 1.00 58.22 C ANISOU 640 C PRO C 82 6080 9549 6492 -2448 -1232 928 C ATOM 641 O PRO A 82 59.548 -1.848 13.125 1.00 65.27 O ANISOU 641 O PRO C 82 6657 9514 8628 -3346 -253 386 O ATOM 642 CB PRO A 82 60.083 -4.914 13.297 1.00 57.60 C ANISOU 642 CB PRO C 82 6202 8897 6785 -2495 -1300 694 C ATOM 643 CG PRO A 82 60.927 -6.113 13.032 1.00 61.64 C ANISOU 643 CG PRO C 82 7485 8655 7281 -2687 -1574 473 C ATOM 644 CD PRO A 82 62.276 -5.575 12.616 1.00 61.44 C ANISOU 644 CD PRO C 82 7545 8452 7347 -2048 -486 -22 C ATOM 645 N GLU A 83 61.746 -2.098 13.552 1.00 60.08 N ANISOU 645 N GLU C 83 6911 10136 5779 -2649 -491 346 N ATOM 646 CA GLU A 83 61.952 -0.850 14.266 1.00 58.75 C ANISOU 646 CA GLU C 83 7323 9833 5165 -2875 -527 401 C ATOM 647 C GLU A 83 62.523 0.245 13.380 1.00 49.36 C ANISOU 647 C GLU C 83 6323 7416 5015 -1136 126 106 C ATOM 648 O GLU A 83 62.722 1.388 13.809 1.00 47.67 O ANISOU 648 O GLU C 83 6268 7574 4270 -680 229 332 O ATOM 649 CB GLU A 83 62.876 -1.055 15.469 1.00 72.69 C ANISOU 649 CB GLU C 83 9982 12292 5346 -5237 740 -929 C ATOM 650 CG GLU A 83 62.186 -1.708 16.659 1.00 77.05 C ANISOU 650 CG GLU C 83 10408 13710 5159 -4911 703 -1110 C ATOM 651 CD GLU A 83 60.730 -1.308 16.802 1.00 80.81 C ANISOU 651 CD GLU C 83 10734 13895 6074 -4907 -9 -221 C ATOM 652 OE1 GLU A 83 60.403 -0.103 16.860 1.00 89.49 O ANISOU 652 OE1 GLU C 83 13427 14399 6175 -6529 -398 -45 O ATOM 653 OE2 GLU A 83 59.873 -2.223 16.866 1.00 90.04 O ANISOU 653 OE2 GLU C 83 11351 16138 6721 -3189 509 -996 O ATOM 654 N SER A 84 62.800 -0.014 12.113 1.00 40.77 N ANISOU 654 N SER C 84 4873 5560 5057 -332 490 -137 N ATOM 655 CA SER A 84 63.162 1.086 11.220 1.00 39.95 C ANISOU 655 CA SER C 84 4506 6067 4608 -437 974 -437 C ATOM 656 C SER A 84 61.995 2.055 11.126 1.00 40.12 C ANISOU 656 C SER C 84 4629 6113 4502 -706 506 137 C ATOM 657 O SER A 84 60.854 1.686 11.438 1.00 39.83 O ANISOU 657 O SER C 84 4325 5873 4937 -1163 135 309 O ATOM 658 CB SER A 84 63.503 0.550 9.832 1.00 36.56 C ANISOU 658 CB SER C 84 3963 5194 4736 -166 963 -458 C ATOM 659 OG SER A 84 62.340 0.059 9.184 1.00 34.84 O ANISOU 659 OG SER C 84 4221 4760 4256 -13 543 -616 O ATOM 660 N TYR A 85 62.263 3.288 10.696 1.00 36.91 N ANISOU 660 N TYR C 85 4557 5925 3540 -512 460 563 N ATOM 661 CA TYR A 85 61.127 4.212 10.579 1.00 38.87 C ANISOU 661 CA TYR C 85 4545 6043 4179 -825 976 304 C ATOM 662 C TYR A 85 60.306 3.859 9.343 1.00 36.56 C ANISOU 662 C TYR C 85 4016 5694 4181 -729 923 584 C ATOM 663 O TYR A 85 59.085 4.052 9.334 1.00 35.47 O ANISOU 663 O TYR C 85 4698 5285 3494 -1150 601 460 O ATOM 664 CB TYR A 85 61.613 5.668 10.600 1.00 41.00 C ANISOU 664 CB TYR C 85 4519 6535 4525 -762 1324 -738 C ATOM 665 CG TYR A 85 62.098 6.111 11.976 1.00 45.44 C ANISOU 665 CG TYR C 85 5347 7087 4830 -1091 1841 -806 C ATOM 666 CD1 TYR A 85 61.985 5.241 13.060 1.00 45.44 C ANISOU 666 CD1 TYR C 85 5931 6893 4440 -1465 2026 -799 C ATOM 667 CD2 TYR A 85 62.652 7.352 12.213 1.00 45.14 C ANISOU 667 CD2 TYR C 85 5301 7010 4841 -551 1953 211 C ATOM 668 CE1 TYR A 85 62.408 5.604 14.312 1.00 45.55 C ANISOU 668 CE1 TYR C 85 5920 6908 4481 -1493 2272 -227 C ATOM 669 CE2 TYR A 85 63.091 7.737 13.461 1.00 45.60 C ANISOU 669 CE2 TYR C 85 5642 6929 4757 -819 2032 397 C ATOM 670 CZ TYR A 85 62.962 6.854 14.497 1.00 46.45 C ANISOU 670 CZ TYR C 85 5882 6851 4915 -1443 2206 28 C ATOM 671 OH TYR A 85 63.383 7.192 15.757 1.00 44.32 O ANISOU 671 OH TYR C 85 5391 6372 5076 -1046 2153 -207 O ATOM 672 N TYR A 86 60.945 3.335 8.293 1.00 34.54 N ANISOU 672 N TYR C 86 3497 5354 4274 -575 813 547 N ATOM 673 CA TYR A 86 60.241 2.742 7.170 1.00 33.41 C ANISOU 673 CA TYR C 86 4260 4623 3814 -451 688 435 C ATOM 674 C TYR A 86 59.167 1.790 7.706 1.00 31.85 C ANISOU 674 C TYR C 86 3948 4639 3515 -459 1061 145 C ATOM 675 O TYR A 86 57.979 1.852 7.341 1.00 35.51 O ANISOU 675 O TYR C 86 3996 5070 4426 -291 1607 -120 O ATOM 676 CB TYR A 86 61.248 2.009 6.291 1.00 36.45 C ANISOU 676 CB TYR C 86 5065 4979 3806 -845 382 679 C ATOM 677 CG TYR A 86 60.649 1.018 5.313 1.00 37.16 C ANISOU 677 CG TYR C 86 5383 4560 4175 -1000 727 667 C ATOM 678 CD1 TYR A 86 60.261 1.471 4.054 1.00 37.49 C ANISOU 678 CD1 TYR C 86 5644 4405 4197 -694 821 588 C ATOM 679 CD2 TYR A 86 60.477 -0.337 5.592 1.00 37.27 C ANISOU 679 CD2 TYR C 86 4696 4538 4927 -73 415 567 C ATOM 680 CE1 TYR A 86 59.712 0.622 3.109 1.00 39.99 C ANISOU 680 CE1 TYR C 86 5869 5350 3974 -1235 886 920 C ATOM 681 CE2 TYR A 86 59.926 -1.194 4.661 1.00 37.76 C ANISOU 681 CE2 TYR C 86 4554 4612 5179 237 399 437 C ATOM 682 CZ TYR A 86 59.549 -0.708 3.424 1.00 41.68 C ANISOU 682 CZ TYR C 86 5611 5481 4744 -869 767 708 C ATOM 683 OH TYR A 86 59.001 -1.557 2.486 1.00 41.02 O ANISOU 683 OH TYR C 86 4878 5730 4978 98 398 544 O ATOM 684 N SER A 87 59.588 0.874 8.584 1.00 34.05 N ANISOU 684 N SER C 87 4519 4337 4081 -1045 546 605 N ATOM 685 CA SER A 87 58.691 -0.177 9.060 1.00 35.21 C ANISOU 685 CA SER C 87 4647 4861 3871 -770 492 380 C ATOM 686 C SER A 87 57.558 0.394 9.905 1.00 33.45 C ANISOU 686 C SER C 87 4273 4825 3612 -579 739 247 C ATOM 687 O SER A 87 56.417 -0.026 9.712 1.00 33.44 O ANISOU 687 O SER C 87 3240 5338 4128 -807 228 544 O ATOM 688 CB SER A 87 59.437 -1.246 9.861 1.00 36.43 C ANISOU 688 CB SER C 87 4146 4853 4842 -654 427 102 C ATOM 689 OG SER A 87 60.213 -2.034 8.965 1.00 40.72 O ANISOU 689 OG SER C 87 5011 5327 5135 -1476 -398 470 O ATOM 690 N PHE A 88 57.910 1.309 10.807 1.00 33.41 N ANISOU 690 N PHE C 88 3834 4886 3972 -1075 640 82 N ATOM 691 CA PHE A 88 56.908 2.013 11.586 1.00 30.53 C ANISOU 691 CA PHE C 88 3381 4744 3476 -631 655 -81 C ATOM 692 C PHE A 88 55.877 2.603 10.631 1.00 27.74 C ANISOU 692 C PHE C 88 2666 4843 3031 -313 829 50 C ATOM 693 O PHE A 88 54.681 2.482 10.888 1.00 30.41 O ANISOU 693 O PHE C 88 3926 4671 2959 -249 399 384 O ATOM 694 CB PHE A 88 57.538 3.139 12.412 1.00 28.25 C ANISOU 694 CB PHE C 88 3563 3873 3299 -85 756 -130 C ATOM 695 CG PHE A 88 56.537 4.021 13.163 1.00 30.86 C ANISOU 695 CG PHE C 88 3418 4455 3853 -457 419 466 C ATOM 696 CD1 PHE A 88 55.851 5.133 12.654 1.00 31.31 C ANISOU 696 CD1 PHE C 88 4064 4487 3345 -831 875 514 C ATOM 697 CD2 PHE A 88 56.285 3.674 14.487 1.00 32.13 C ANISOU 697 CD2 PHE C 88 3623 4395 4192 -326 -162 629 C ATOM 698 CE1 PHE A 88 54.936 5.836 13.406 1.00 36.09 C ANISOU 698 CE1 PHE C 88 4567 5131 4015 -1525 -609 1295 C ATOM 699 CE2 PHE A 88 55.387 4.385 15.249 1.00 31.90 C ANISOU 699 CE2 PHE C 88 3708 4616 3796 -736 341 500 C ATOM 700 CZ PHE A 88 54.709 5.469 14.732 1.00 33.19 C ANISOU 700 CZ PHE C 88 3783 5050 3779 -1242 -189 845 C ATOM 701 N MET A 89 56.292 3.369 9.621 1.00 29.41 N ANISOU 701 N MET C 89 2935 4876 3362 -421 500 79 N ATOM 702 CA MET A 89 55.368 4.150 8.793 1.00 29.82 C ANISOU 702 CA MET C 89 2897 4849 3585 -631 451 92 C ATOM 703 C MET A 89 54.431 3.257 7.983 1.00 28.85 C ANISOU 703 C MET C 89 3158 4680 3123 -736 546 107 C ATOM 704 O MET A 89 53.246 3.574 7.815 1.00 29.56 O ANISOU 704 O MET C 89 3066 4752 3415 -354 467 598 O ATOM 705 CB MET A 89 56.122 5.099 7.844 1.00 30.13 C ANISOU 705 CB MET C 89 3193 4668 3586 -720 301 308 C ATOM 706 CG MET A 89 56.769 6.268 8.593 1.00 30.03 C ANISOU 706 CG MET C 89 2944 4561 3905 -524 144 731 C ATOM 707 SD MET A 89 55.524 7.279 9.434 1.00 31.40 S ANISOU 707 SD MET C 89 4243 4373 3316 -908 432 245 S ATOM 708 CE MET A 89 54.419 7.656 8.082 1.00 30.87 C ANISOU 708 CE MET C 89 4601 4671 2457 -598 -366 517 C ATOM 709 N HIS A 90 54.955 2.138 7.464 1.00 30.25 N ANISOU 709 N HIS C 90 3395 4865 3233 -852 488 354 N ATOM 710 CA HIS A 90 54.078 1.225 6.726 1.00 31.13 C ANISOU 710 CA HIS C 90 3569 5055 3205 -723 689 800 C ATOM 711 C HIS A 90 53.073 0.570 7.660 1.00 30.39 C ANISOU 711 C HIS C 90 3538 4858 3150 -617 691 477 C ATOM 712 O HIS A 90 51.859 0.552 7.462 1.00 32.67 O ANISOU 712 O HIS C 90 3926 4798 3690 -483 810 703 O ATOM 713 CB HIS A 90 54.937 0.185 5.974 1.00 31.72 C ANISOU 713 CB HIS C 90 3515 5022 3515 -1054 337 785 C ATOM 714 CG HIS A 90 55.559 0.838 4.768 1.00 32.17 C ANISOU 714 CG HIS C 90 4100 4569 3556 -480 217 674 C ATOM 715 ND1 HIS A 90 54.872 1.063 3.592 1.00 29.81 N ANISOU 715 ND1 HIS C 90 3433 4288 3604 -380 177 698 N ATOM 716 CD2 HIS A 90 56.798 1.342 4.551 1.00 33.01 C ANISOU 716 CD2 HIS C 90 4532 4539 3470 -153 107 233 C ATOM 717 CE1 HIS A 90 55.666 1.662 2.712 1.00 28.80 C ANISOU 717 CE1 HIS C 90 3279 3942 3724 65 245 308 C ATOM 718 NE2 HIS A 90 56.846 1.840 3.267 1.00 30.26 N ANISOU 718 NE2 HIS C 90 3720 4212 3567 -19 255 -218 N ATOM 719 N ARG A 91 53.565 -0.002 8.750 1.00 33.11 N ANISOU 719 N ARG C 91 4353 4960 3268 -1110 444 493 N ATOM 720 CA ARG A 91 52.713 -0.707 9.717 1.00 36.54 C ANISOU 720 CA ARG C 91 4700 5273 3912 -1226 -152 447 C ATOM 721 C ARG A 91 51.636 0.165 10.332 1.00 36.40 C ANISOU 721 C ARG C 91 4322 5316 4192 -652 20 690 C ATOM 722 O ARG A 91 50.529 -0.321 10.565 1.00 35.21 O ANISOU 722 O ARG C 91 3853 6253 3272 -721 142 1023 O ATOM 723 CB ARG A 91 53.618 -1.265 10.812 1.00 43.09 C ANISOU 723 CB ARG C 91 6615 5891 3866 -2657 -136 202 C ATOM 724 CG ARG A 91 52.967 -1.716 12.090 1.00 43.92 C ANISOU 724 CG ARG C 91 6204 5813 4670 -1722 -732 -351 C ATOM 725 CD ARG A 91 54.020 -2.386 12.974 1.00 46.77 C ANISOU 725 CD ARG C 91 5724 6840 5208 -1314 -893 -1308 C ATOM 726 NE ARG A 91 55.017 -1.480 13.522 1.00 47.83 N ANISOU 726 NE ARG C 91 5608 7281 5286 -1124 -1010 -968 N ATOM 727 CZ ARG A 91 56.338 -1.498 13.419 1.00 48.30 C ANISOU 727 CZ ARG C 91 5533 7333 5485 -1133 -564 -607 C ATOM 728 NH1 ARG A 91 56.988 -2.430 12.732 1.00 47.57 N ANISOU 728 NH1 ARG C 91 4548 7368 6160 -1242 -543 -593 N ATOM 729 NH2 ARG A 91 57.012 -0.530 14.036 1.00 47.84 N ANISOU 729 NH2 ARG C 91 6123 6762 5292 -1219 -18 -561 N ATOM 730 N ASN A 92 51.917 1.431 10.619 1.00 32.32 N ANISOU 730 N ASN C 92 4072 4467 3741 -99 -65 946 N ATOM 731 CA ASN A 92 50.955 2.327 11.267 1.00 30.99 C ANISOU 731 CA ASN C 92 4345 4296 3134 -55 -210 654 C ATOM 732 C ASN A 92 50.159 3.182 10.294 1.00 31.42 C ANISOU 732 C ASN C 92 3701 4645 3593 -93 -208 329 C ATOM 733 O ASN A 92 49.131 3.778 10.648 1.00 32.32 O ANISOU 733 O ASN C 92 4081 4476 3724 -48 596 108 O ATOM 734 CB ASN A 92 51.684 3.232 12.288 1.00 35.51 C ANISOU 734 CB ASN C 92 5302 5141 3048 -289 344 650 C ATOM 735 CG ASN A 92 52.161 2.392 13.457 1.00 38.19 C ANISOU 735 CG ASN C 92 5988 5080 3443 157 113 269 C ATOM 736 OD1 ASN A 92 51.333 1.846 14.191 1.00 43.56 O ANISOU 736 OD1 ASN C 92 7035 5406 4112 539 -878 -301 O ATOM 737 ND2 ASN A 92 53.457 2.245 13.653 1.00 37.21 N ANISOU 737 ND2 ASN C 92 6000 4543 3596 -327 826 925 N ATOM 738 N PHE A 93 50.571 3.276 9.034 1.00 31.32 N ANISOU 738 N PHE C 93 3640 5181 3080 -457 518 137 N ATOM 739 CA PHE A 93 49.804 4.165 8.147 1.00 28.57 C ANISOU 739 CA PHE C 93 3360 4444 3050 -53 634 424 C ATOM 740 C PHE A 93 49.753 3.683 6.708 1.00 29.40 C ANISOU 740 C PHE C 93 3412 4803 2958 61 460 346 C ATOM 741 O PHE A 93 48.680 3.427 6.161 1.00 31.72 O ANISOU 741 O PHE C 93 4734 4118 3201 -208 1108 177 O ATOM 742 CB PHE A 93 50.457 5.546 8.229 1.00 30.39 C ANISOU 742 CB PHE C 93 3405 4753 3391 -284 565 244 C ATOM 743 CG PHE A 93 49.784 6.637 7.420 1.00 31.25 C ANISOU 743 CG PHE C 93 3730 4660 3483 -377 581 243 C ATOM 744 CD1 PHE A 93 48.410 6.819 7.506 1.00 29.95 C ANISOU 744 CD1 PHE C 93 3466 4815 3097 -206 1137 161 C ATOM 745 CD2 PHE A 93 50.541 7.462 6.593 1.00 30.73 C ANISOU 745 CD2 PHE C 93 3209 4834 3633 -91 802 -453 C ATOM 746 CE1 PHE A 93 47.800 7.820 6.779 1.00 31.44 C ANISOU 746 CE1 PHE C 93 3859 4705 3380 -265 1086 121 C ATOM 747 CE2 PHE A 93 49.936 8.465 5.861 1.00 31.69 C ANISOU 747 CE2 PHE C 93 3531 4731 3780 -329 747 -274 C ATOM 748 CZ PHE A 93 48.565 8.633 5.959 1.00 30.27 C ANISOU 748 CZ PHE C 93 3337 4728 3437 -361 1314 -233 C ATOM 749 N PHE A 94 50.906 3.566 6.043 1.00 30.65 N ANISOU 749 N PHE C 94 3692 4745 3207 -184 587 693 N ATOM 750 CA PHE A 94 50.843 3.315 4.605 1.00 30.56 C ANISOU 750 CA PHE C 94 3572 4889 3150 -114 485 514 C ATOM 751 C PHE A 94 50.179 1.968 4.319 1.00 30.65 C ANISOU 751 C PHE C 94 3623 4807 3218 -236 584 160 C ATOM 752 O PHE A 94 49.453 1.869 3.318 1.00 33.71 O ANISOU 752 O PHE C 94 4416 4812 3580 -311 1262 241 O ATOM 753 CB PHE A 94 52.217 3.363 3.947 1.00 30.31 C ANISOU 753 CB PHE C 94 3761 4790 2966 -302 103 374 C ATOM 754 CG PHE A 94 53.012 4.642 4.117 1.00 30.45 C ANISOU 754 CG PHE C 94 3625 4942 3003 -409 -384 421 C ATOM 755 CD1 PHE A 94 52.407 5.883 3.974 1.00 33.40 C ANISOU 755 CD1 PHE C 94 4161 5402 3128 -855 168 -429 C ATOM 756 CD2 PHE A 94 54.369 4.581 4.416 1.00 30.80 C ANISOU 756 CD2 PHE C 94 3484 5250 2967 -482 9 -58 C ATOM 757 CE1 PHE A 94 53.154 7.048 4.128 1.00 33.70 C ANISOU 757 CE1 PHE C 94 4110 5756 2937 -1099 -5 -243 C ATOM 758 CE2 PHE A 94 55.122 5.742 4.567 1.00 31.73 C ANISOU 758 CE2 PHE C 94 3582 5591 2883 -645 582 43 C ATOM 759 CZ PHE A 94 54.508 6.976 4.414 1.00 31.82 C ANISOU 759 CZ PHE C 94 3680 5899 2510 -850 -114 199 C ATOM 760 N ASP A 95 50.339 0.940 5.135 1.00 34.08 N ANISOU 760 N ASP C 95 4049 5597 3304 -634 -44 629 N ATOM 761 CA ASP A 95 49.691 -0.346 4.906 1.00 34.35 C ANISOU 761 CA ASP C 95 4079 5311 3660 -767 150 542 C ATOM 762 C ASP A 95 48.175 -0.225 4.841 1.00 36.57 C ANISOU 762 C ASP C 95 4287 5317 4292 -783 779 50 C ATOM 763 O ASP A 95 47.531 -1.146 4.337 1.00 39.69 O ANISOU 763 O ASP C 95 4476 5756 4849 -983 1093 -549 O ATOM 764 CB ASP A 95 49.990 -1.347 6.024 1.00 35.67 C ANISOU 764 CB ASP C 95 3774 5708 4073 -1030 780 -226 C ATOM 765 CG ASP A 95 51.378 -1.941 5.996 1.00 34.99 C ANISOU 765 CG ASP C 95 3899 5693 3703 -1159 304 312 C ATOM 766 OD1 ASP A 95 52.162 -1.664 5.067 1.00 35.39 O ANISOU 766 OD1 ASP C 95 4277 6282 2888 -1864 648 822 O ATOM 767 OD2 ASP A 95 51.697 -2.710 6.929 1.00 33.74 O ANISOU 767 OD2 ASP C 95 4027 5208 3586 -667 131 421 O ATOM 768 N HIS A 96 47.593 0.854 5.346 1.00 36.46 N ANISOU 768 N HIS C 96 4684 5293 3875 -526 734 493 N ATOM 769 CA HIS A 96 46.145 0.956 5.442 1.00 35.36 C ANISOU 769 CA HIS C 96 4348 5461 3624 -367 1275 209 C ATOM 770 C HIS A 96 45.525 2.019 4.562 1.00 35.19 C ANISOU 770 C HIS C 96 4029 5694 3647 -425 1626 -52 C ATOM 771 O HIS A 96 44.298 2.180 4.638 1.00 39.30 O ANISOU 771 O HIS C 96 4650 5773 4509 -187 730 -354 O ATOM 772 CB HIS A 96 45.760 1.269 6.909 1.00 33.49 C ANISOU 772 CB HIS C 96 4456 4624 3644 -211 1455 117 C ATOM 773 CG HIS A 96 46.529 0.337 7.808 1.00 38.62 C ANISOU 773 CG HIS C 96 4939 5649 4085 -462 1172 -559 C ATOM 774 ND1 HIS A 96 46.211 -0.995 7.953 1.00 40.50 N ANISOU 774 ND1 HIS C 96 4989 6057 4344 -654 1265 -701 N ATOM 775 CD2 HIS A 96 47.616 0.552 8.585 1.00 40.14 C ANISOU 775 CD2 HIS C 96 5023 6117 4113 -720 1221 -1071 C ATOM 776 CE1 HIS A 96 47.050 -1.573 8.782 1.00 39.67 C ANISOU 776 CE1 HIS C 96 4932 6129 4012 -470 882 -603 C ATOM 777 NE2 HIS A 96 47.916 -0.650 9.185 1.00 37.90 N ANISOU 777 NE2 HIS C 96 4805 5639 3956 -144 387 -484 N ATOM 778 N VAL A 97 46.316 2.732 3.767 1.00 34.62 N ANISOU 778 N VAL C 97 4461 5321 3373 -477 1494 54 N ATOM 779 CA VAL A 97 45.711 3.774 2.933 1.00 36.46 C ANISOU 779 CA VAL C 97 4874 5289 3692 -460 1178 36 C ATOM 780 C VAL A 97 46.110 3.612 1.470 1.00 35.96 C ANISOU 780 C VAL C 97 4654 5581 3426 -439 1679 -336 C ATOM 781 O VAL A 97 46.862 2.696 1.131 1.00 39.41 O ANISOU 781 O VAL C 97 5804 5797 3372 -914 25 271 O ATOM 782 CB VAL A 97 46.074 5.175 3.453 1.00 35.14 C ANISOU 782 CB VAL C 97 5139 5045 3167 -785 1099 236 C ATOM 783 CG1 VAL A 97 45.585 5.354 4.888 1.00 33.93 C ANISOU 783 CG1 VAL C 97 5390 4646 2856 -222 961 -318 C ATOM 784 CG2 VAL A 97 47.573 5.419 3.360 1.00 34.92 C ANISOU 784 CG2 VAL C 97 4327 5855 3086 -666 223 72 C ATOM 785 N ASP A 98 45.595 4.482 0.604 1.00 36.74 N ANISOU 785 N ASP C 98 4927 5302 3730 -197 1333 -352 N ATOM 786 CA ASP A 98 45.741 4.279 -0.836 1.00 34.71 C ANISOU 786 CA ASP C 98 4702 4779 3708 -54 1044 -383 C ATOM 787 C ASP A 98 46.865 5.106 -1.456 1.00 35.19 C ANISOU 787 C ASP C 98 4413 4907 4051 -182 914 -851 C ATOM 788 O ASP A 98 46.751 5.526 -2.610 1.00 35.65 O ANISOU 788 O ASP C 98 4240 5630 3677 -138 1218 -561 O ATOM 789 CB ASP A 98 44.432 4.592 -1.575 1.00 34.30 C ANISOU 789 CB ASP C 98 4389 4744 3901 -267 1045 -509 C ATOM 790 CG ASP A 98 43.950 6.013 -1.319 1.00 42.85 C ANISOU 790 CG ASP C 98 6236 5461 4584 -1451 1620 -797 C ATOM 791 OD1 ASP A 98 44.494 6.681 -0.405 1.00 41.13 O ANISOU 791 OD1 ASP C 98 5685 5525 4418 -1274 1366 -182 O ATOM 792 OD2 ASP A 98 43.021 6.455 -2.032 1.00 40.73 O ANISOU 792 OD2 ASP C 98 6312 4815 4350 -870 814 -248 O ATOM 793 N ILE A 99 47.941 5.319 -0.700 1.00 33.19 N ANISOU 793 N ILE C 99 4298 4713 3599 -396 1533 -192 N ATOM 794 CA ILE A 99 49.056 6.055 -1.276 1.00 33.90 C ANISOU 794 CA ILE C 99 4695 4378 3809 -187 1492 28 C ATOM 795 C ILE A 99 50.004 5.159 -2.084 1.00 36.58 C ANISOU 795 C ILE C 99 5231 4990 3677 -1364 534 289 C ATOM 796 O ILE A 99 50.437 4.077 -1.689 1.00 35.36 O ANISOU 796 O ILE C 99 4707 4851 3876 -930 742 -274 O ATOM 797 CB ILE A 99 49.851 6.741 -0.158 1.00 35.18 C ANISOU 797 CB ILE C 99 3998 5274 4095 -492 1345 -288 C ATOM 798 CG1 ILE A 99 50.898 7.755 -0.634 1.00 34.23 C ANISOU 798 CG1 ILE C 99 4305 4669 4033 -422 1095 -6 C ATOM 799 CG2 ILE A 99 50.508 5.676 0.720 1.00 37.02 C ANISOU 799 CG2 ILE C 99 5269 6154 2643 -704 911 -99 C ATOM 800 CD1 ILE A 99 51.521 8.520 0.536 1.00 34.84 C ANISOU 800 CD1 ILE C 99 4107 4388 4744 -137 1473 605 C ATOM 801 N PRO A 100 50.376 5.630 -3.276 1.00 36.88 N ANISOU 801 N PRO C 100 5587 5329 3097 -1531 930 -61 N ATOM 802 CA PRO A 100 51.311 4.899 -4.116 1.00 35.29 C ANISOU 802 CA PRO C 100 4840 5035 3535 -1196 356 54 C ATOM 803 C PRO A 100 52.757 4.978 -3.644 1.00 36.36 C ANISOU 803 C PRO C 100 4851 5250 3715 -1543 965 -480 C ATOM 804 O PRO A 100 53.199 5.996 -3.118 1.00 39.45 O ANISOU 804 O PRO C 100 5703 5877 3407 -1736 1727 -330 O ATOM 805 CB PRO A 100 51.217 5.593 -5.486 1.00 33.85 C ANISOU 805 CB PRO C 100 4530 5161 3171 -1211 970 -90 C ATOM 806 CG PRO A 100 50.524 6.886 -5.246 1.00 37.64 C ANISOU 806 CG PRO C 100 5633 5438 3229 -1814 917 -195 C ATOM 807 CD PRO A 100 49.906 6.882 -3.869 1.00 36.80 C ANISOU 807 CD PRO C 100 5032 5463 3487 -1619 913 121 C ATOM 808 N ALA A 101 53.519 3.904 -3.856 1.00 30.99 N ANISOU 808 N ALA C 101 3433 5040 3303 -898 -430 305 N ATOM 809 CA ALA A 101 54.918 3.852 -3.462 1.00 33.72 C ANISOU 809 CA ALA C 101 4081 5089 3640 -619 200 736 C ATOM 810 C ALA A 101 55.692 5.041 -4.004 1.00 30.88 C ANISOU 810 C ALA C 101 3919 4368 3448 -629 404 347 C ATOM 811 O ALA A 101 56.573 5.599 -3.352 1.00 32.77 O ANISOU 811 O ALA C 101 4178 4764 3512 -566 682 392 O ATOM 812 CB ALA A 101 55.559 2.558 -3.950 1.00 33.55 C ANISOU 812 CB ALA C 101 3964 5017 3766 -861 593 -5 C ATOM 813 N GLU A 102 55.383 5.454 -5.235 1.00 30.35 N ANISOU 813 N GLU C 102 4106 4392 3032 -846 605 806 N ATOM 814 CA GLU A 102 56.232 6.514 -5.775 1.00 32.82 C ANISOU 814 CA GLU C 102 4063 5216 3191 -999 506 481 C ATOM 815 C GLU A 102 56.000 7.819 -5.032 1.00 31.46 C ANISOU 815 C GLU C 102 3864 4733 3355 -396 864 489 C ATOM 816 O GLU A 102 56.824 8.725 -5.139 1.00 34.82 O ANISOU 816 O GLU C 102 3726 5192 4311 -1043 -26 703 O ATOM 817 CB GLU A 102 55.963 6.698 -7.265 1.00 35.90 C ANISOU 817 CB GLU C 102 4640 5930 3070 -1466 471 632 C ATOM 818 CG GLU A 102 54.471 6.905 -7.511 1.00 42.27 C ANISOU 818 CG GLU C 102 6742 5952 3365 -1389 507 -204 C ATOM 819 CD GLU A 102 54.150 6.693 -8.983 1.00 50.47 C ANISOU 819 CD GLU C 102 7995 7533 3648 -1747 1074 -687 C ATOM 820 OE1 GLU A 102 53.480 5.681 -9.319 1.00 57.34 O ANISOU 820 OE1 GLU C 102 8278 9155 4353 -1924 1846 -96 O ATOM 821 OE2 GLU A 102 54.584 7.553 -9.793 1.00 60.07 O ANISOU 821 OE2 GLU C 102 8655 10831 3336 -3672 902 -1579 O ATOM 822 N ASN A 103 54.905 7.930 -4.287 1.00 32.64 N ANISOU 822 N ASN C 103 4396 4734 3272 -404 598 409 N ATOM 823 CA ASN A 103 54.618 9.149 -3.540 1.00 33.57 C ANISOU 823 CA ASN C 103 5275 4740 2740 -1027 431 227 C ATOM 824 C ASN A 103 55.260 9.177 -2.161 1.00 31.50 C ANISOU 824 C ASN C 103 4370 4610 2987 -737 366 81 C ATOM 825 O ASN A 103 55.187 10.200 -1.467 1.00 32.15 O ANISOU 825 O ASN C 103 4006 4785 3422 -525 691 -130 O ATOM 826 CB ASN A 103 53.098 9.301 -3.394 1.00 34.34 C ANISOU 826 CB ASN C 103 5232 4745 3072 -912 1374 133 C ATOM 827 CG ASN A 103 52.436 9.822 -4.653 1.00 36.60 C ANISOU 827 CG ASN C 103 5288 5096 3522 -883 519 -207 C ATOM 828 OD1 ASN A 103 53.069 9.864 -5.715 1.00 35.71 O ANISOU 828 OD1 ASN C 103 5044 5400 3123 -644 1347 -82 O ATOM 829 ND2 ASN A 103 51.175 10.217 -4.590 1.00 35.38 N ANISOU 829 ND2 ASN C 103 5136 5176 3130 -685 1303 -224 N ATOM 830 N ILE A 104 55.891 8.096 -1.700 1.00 32.91 N ANISOU 830 N ILE C 104 4556 4661 3286 -737 274 -56 N ATOM 831 CA ILE A 104 56.411 7.996 -0.334 1.00 31.09 C ANISOU 831 CA ILE C 104 4505 4217 3091 -847 319 231 C ATOM 832 C ILE A 104 57.899 8.280 -0.316 1.00 31.25 C ANISOU 832 C ILE C 104 4575 3985 3313 -949 706 460 C ATOM 833 O ILE A 104 58.679 7.670 -1.052 1.00 32.27 O ANISOU 833 O ILE C 104 4783 4728 2752 -686 460 863 O ATOM 834 CB ILE A 104 56.160 6.613 0.293 1.00 31.31 C ANISOU 834 CB ILE C 104 4726 4326 2846 -1181 253 675 C ATOM 835 CG1 ILE A 104 54.666 6.285 0.402 1.00 31.28 C ANISOU 835 CG1 ILE C 104 4403 4559 2921 -1144 164 242 C ATOM 836 CG2 ILE A 104 56.850 6.459 1.648 1.00 29.67 C ANISOU 836 CG2 ILE C 104 4248 4267 2758 -881 104 781 C ATOM 837 CD1 ILE A 104 54.391 4.833 0.713 1.00 32.42 C ANISOU 837 CD1 ILE C 104 4680 4730 2907 -1500 -179 876 C ATOM 838 N ASN A 105 58.309 9.223 0.521 1.00 30.46 N ANISOU 838 N ASN C 105 4248 4407 2918 -945 333 590 N ATOM 839 CA ASN A 105 59.729 9.519 0.589 1.00 32.34 C ANISOU 839 CA ASN C 105 4321 4452 3516 -907 626 520 C ATOM 840 C ASN A 105 60.195 9.370 2.034 1.00 33.61 C ANISOU 840 C ASN C 105 4711 4436 3624 -724 491 392 C ATOM 841 O ASN A 105 59.659 9.933 2.985 1.00 30.80 O ANISOU 841 O ASN C 105 4042 4434 3227 -644 -297 398 O ATOM 842 CB ASN A 105 59.999 10.930 0.090 1.00 32.61 C ANISOU 842 CB ASN C 105 4246 4368 3777 -697 574 342 C ATOM 843 CG ASN A 105 59.643 11.124 -1.361 1.00 35.09 C ANISOU 843 CG ASN C 105 4708 5076 3550 -880 272 688 C ATOM 844 OD1 ASN A 105 60.486 10.822 -2.211 1.00 39.39 O ANISOU 844 OD1 ASN C 105 5905 5078 3981 -569 731 944 O ATOM 845 ND2 ASN A 105 58.439 11.606 -1.663 1.00 29.24 N ANISOU 845 ND2 ASN C 105 3888 5167 2057 -734 610 859 N ATOM 846 N LEU A 106 61.236 8.553 2.154 1.00 31.95 N ANISOU 846 N LEU C 106 3952 4279 3909 -177 439 403 N ATOM 847 CA LEU A 106 61.869 8.234 3.421 1.00 34.22 C ANISOU 847 CA LEU C 106 4400 4562 4040 -423 543 158 C ATOM 848 C LEU A 106 63.376 8.318 3.216 1.00 34.71 C ANISOU 848 C LEU C 106 4913 4364 3913 -388 534 20 C ATOM 849 O LEU A 106 63.833 7.969 2.130 1.00 36.23 O ANISOU 849 O LEU C 106 4968 4770 4027 -138 604 233 O ATOM 850 CB LEU A 106 61.494 6.845 3.924 1.00 36.38 C ANISOU 850 CB LEU C 106 4510 4684 4630 -584 565 -435 C ATOM 851 CG LEU A 106 60.155 6.691 4.654 1.00 35.72 C ANISOU 851 CG LEU C 106 3771 5352 4451 -70 829 -681 C ATOM 852 CD1 LEU A 106 59.458 5.432 4.144 1.00 42.00 C ANISOU 852 CD1 LEU C 106 3910 6757 5290 -647 1129 138 C ATOM 853 CD2 LEU A 106 60.316 6.642 6.163 1.00 35.07 C ANISOU 853 CD2 LEU C 106 4779 4133 4415 -597 761 -603 C ATOM 854 N LEU A 107 64.140 8.765 4.196 1.00 34.53 N ANISOU 854 N LEU C 107 4691 4414 4014 -459 540 -33 N ATOM 855 CA LEU A 107 65.590 8.773 4.074 1.00 35.05 C ANISOU 855 CA LEU C 107 4619 4356 4344 -516 1190 479 C ATOM 856 C LEU A 107 66.151 7.358 4.022 1.00 37.46 C ANISOU 856 C LEU C 107 4938 4618 4678 -787 937 911 C ATOM 857 O LEU A 107 65.721 6.459 4.760 1.00 38.05 O ANISOU 857 O LEU C 107 5313 4559 4585 -800 755 183 O ATOM 858 CB LEU A 107 66.159 9.587 5.250 1.00 34.30 C ANISOU 858 CB LEU C 107 4586 4483 3964 -534 928 451 C ATOM 859 CG LEU A 107 66.109 11.101 4.973 1.00 34.06 C ANISOU 859 CG LEU C 107 4502 4681 3757 -547 836 807 C ATOM 860 CD1 LEU A 107 66.178 11.900 6.275 1.00 29.82 C ANISOU 860 CD1 LEU C 107 3380 4872 3080 -19 332 269 C ATOM 861 CD2 LEU A 107 67.207 11.492 4.001 1.00 33.01 C ANISOU 861 CD2 LEU C 107 5034 4156 3351 -512 683 489 C ATOM 862 N ASN A 108 67.121 7.132 3.121 1.00 39.13 N ANISOU 862 N ASN C 108 5989 4292 4588 -435 1104 684 N ATOM 863 CA ASN A 108 67.758 5.820 3.021 1.00 39.84 C ANISOU 863 CA ASN C 108 6362 4176 4599 -440 1482 556 C ATOM 864 C ASN A 108 68.926 5.725 3.994 1.00 40.69 C ANISOU 864 C ASN C 108 6208 4324 4928 -519 1857 483 C ATOM 865 O ASN A 108 70.045 6.171 3.727 1.00 43.29 O ANISOU 865 O ASN C 108 6790 3902 5756 -377 1638 598 O ATOM 866 CB ASN A 108 68.218 5.546 1.589 1.00 40.41 C ANISOU 866 CB ASN C 108 6331 4262 4760 21 1660 794 C ATOM 867 CG ASN A 108 68.764 4.148 1.399 1.00 38.84 C ANISOU 867 CG ASN C 108 5505 4307 4946 398 2042 806 C ATOM 868 OD1 ASN A 108 68.874 3.342 2.334 1.00 53.94 O ANISOU 868 OD1 ASN C 108 10729 5477 4290 -2612 3158 -571 O ATOM 869 ND2 ASN A 108 69.126 3.853 0.144 1.00 46.61 N ANISOU 869 ND2 ASN C 108 7358 5603 4750 -825 2625 612 N ATOM 870 N GLY A 109 68.683 5.129 5.159 1.00 40.85 N ANISOU 870 N GLY C 109 6270 4240 5010 -754 1842 113 N ATOM 871 CA GLY A 109 69.713 5.021 6.181 1.00 39.63 C ANISOU 871 CA GLY C 109 5024 4631 5402 78 1429 -31 C ATOM 872 C GLY A 109 70.821 4.065 5.785 1.00 42.22 C ANISOU 872 C GLY C 109 5622 4535 5887 -177 1869 -417 C ATOM 873 O GLY A 109 71.852 3.967 6.446 1.00 38.25 O ANISOU 873 O GLY C 109 4210 4790 5534 -176 293 -952 O ATOM 874 N ASN A 110 70.608 3.354 4.681 1.00 44.46 N ANISOU 874 N ASN C 110 5804 4980 6109 -380 1982 -24 N ATOM 875 CA ASN A 110 71.603 2.423 4.181 1.00 48.58 C ANISOU 875 CA ASN C 110 6429 5414 6615 -1018 1249 443 C ATOM 876 C ASN A 110 72.291 2.975 2.948 1.00 50.82 C ANISOU 876 C ASN C 110 6823 5772 6715 -709 1144 566 C ATOM 877 O ASN A 110 73.061 2.253 2.314 1.00 48.88 O ANISOU 877 O ASN C 110 7062 4473 7037 13 812 -66 O ATOM 878 CB ASN A 110 70.943 1.057 3.907 1.00 50.36 C ANISOU 878 CB ASN C 110 6487 5502 7146 -1451 1298 21 C ATOM 879 CG ASN A 110 70.519 0.387 5.207 1.00 50.62 C ANISOU 879 CG ASN C 110 6301 5774 7159 -1249 1332 -411 C ATOM 880 OD1 ASN A 110 71.363 0.108 6.065 1.00 52.61 O ANISOU 880 OD1 ASN C 110 6575 6222 7194 -811 1545 -529 O ATOM 881 ND2 ASN A 110 69.232 0.117 5.397 1.00 48.08 N ANISOU 881 ND2 ASN C 110 6147 5904 6217 -1209 1853 -182 N ATOM 882 N ALA A 111 72.053 4.234 2.577 1.00 46.92 N ANISOU 882 N ALA C 111 5573 5931 6322 -309 1461 920 N ATOM 883 CA ALA A 111 72.727 4.751 1.381 1.00 48.47 C ANISOU 883 CA ALA C 111 5790 6212 6414 129 1455 1048 C ATOM 884 C ALA A 111 74.246 4.670 1.551 1.00 52.94 C ANISOU 884 C ALA C 111 6797 6316 7001 455 1192 819 C ATOM 885 O ALA A 111 74.811 4.841 2.636 1.00 54.44 O ANISOU 885 O ALA C 111 7637 5640 7410 41 1768 691 O ATOM 886 CB ALA A 111 72.301 6.169 1.041 1.00 45.03 C ANISOU 886 CB ALA C 111 3698 5647 7765 1271 726 1998 C ATOM 887 N PRO A 112 74.913 4.383 0.434 1.00 55.19 N ANISOU 887 N PRO C 112 7572 6396 7003 848 638 742 N ATOM 888 CA PRO A 112 76.376 4.251 0.444 1.00 54.22 C ANISOU 888 CA PRO C 112 6868 6455 7279 743 569 625 C ATOM 889 C PRO A 112 77.029 5.617 0.638 1.00 59.71 C ANISOU 889 C PRO C 112 7025 6982 8682 359 1164 -242 C ATOM 890 O PRO A 112 77.986 5.740 1.410 1.00 77.93 O ANISOU 890 O PRO C 112 8031 7763 13817 567 2677 -2149 O ATOM 891 CB PRO A 112 76.688 3.662 -0.933 1.00 57.18 C ANISOU 891 CB PRO C 112 7833 6256 7639 966 1000 896 C ATOM 892 CG PRO A 112 75.586 4.203 -1.791 1.00 54.16 C ANISOU 892 CG PRO C 112 7183 6144 7253 1389 1098 1162 C ATOM 893 CD PRO A 112 74.360 4.171 -0.913 1.00 53.80 C ANISOU 893 CD PRO C 112 6856 6468 7117 1172 1100 1377 C ATOM 894 N ASP A 113 76.519 6.651 -0.025 1.00 58.97 N ANISOU 894 N ASP C 113 7871 6976 7558 -703 978 1015 N ATOM 895 CA ASP A 113 77.028 8.004 0.177 1.00 54.23 C ANISOU 895 CA ASP C 113 7651 6420 6535 -174 564 1816 C ATOM 896 C ASP A 113 76.022 8.848 0.963 1.00 52.93 C ANISOU 896 C ASP C 113 7586 6363 6163 180 639 1741 C ATOM 897 O ASP A 113 75.141 9.467 0.362 1.00 44.98 O ANISOU 897 O ASP C 113 5320 6095 5676 1212 693 1948 O ATOM 898 CB ASP A 113 77.323 8.678 -1.160 1.00 54.08 C ANISOU 898 CB ASP C 113 7975 6588 5985 -110 988 1859 C ATOM 899 CG ASP A 113 78.016 10.016 -1.007 1.00 58.32 C ANISOU 899 CG ASP C 113 7835 7247 7078 -138 293 1121 C ATOM 900 OD1 ASP A 113 78.058 10.566 0.107 1.00 53.98 O ANISOU 900 OD1 ASP C 113 5905 7266 7339 387 -41 1707 O ATOM 901 OD2 ASP A 113 78.538 10.528 -2.019 1.00 61.72 O ANISOU 901 OD2 ASP C 113 8558 8578 6314 -863 -16 -699 O ATOM 902 N ILE A 114 76.181 8.854 2.281 1.00 51.56 N ANISOU 902 N ILE C 114 6967 6312 6311 -162 1211 1397 N ATOM 903 CA ILE A 114 75.282 9.560 3.185 1.00 52.94 C ANISOU 903 CA ILE C 114 7380 6739 5997 -693 1291 1417 C ATOM 904 C ILE A 114 75.084 11.025 2.839 1.00 49.80 C ANISOU 904 C ILE C 114 7019 5918 5983 -7 1190 1105 C ATOM 905 O ILE A 114 73.940 11.496 2.773 1.00 49.57 O ANISOU 905 O ILE C 114 6631 5887 6317 133 1737 1794 O ATOM 906 CB ILE A 114 75.806 9.462 4.633 1.00 55.04 C ANISOU 906 CB ILE C 114 7595 7188 6129 -1136 1136 1055 C ATOM 907 CG1 ILE A 114 75.745 8.033 5.183 1.00 59.43 C ANISOU 907 CG1 ILE C 114 8000 7943 6638 -2048 1462 914 C ATOM 908 CG2 ILE A 114 75.069 10.433 5.542 1.00 45.34 C ANISOU 908 CG2 ILE C 114 6371 5895 4960 -544 270 324 C ATOM 909 CD1 ILE A 114 74.369 7.421 4.952 1.00 67.13 C ANISOU 909 CD1 ILE C 114 7512 7919 10077 -1945 751 1921 C ATOM 910 N ASP A 115 76.149 11.795 2.616 1.00 48.77 N ANISOU 910 N ASP C 115 7171 5406 5955 66 1323 1323 N ATOM 911 CA ASP A 115 75.887 13.204 2.315 1.00 48.39 C ANISOU 911 CA ASP C 115 7228 5264 5896 282 442 1777 C ATOM 912 C ASP A 115 75.084 13.367 1.036 1.00 47.13 C ANISOU 912 C ASP C 115 6772 5891 5245 168 83 1979 C ATOM 913 O ASP A 115 74.291 14.300 0.939 1.00 40.86 O ANISOU 913 O ASP C 115 4896 6366 4264 -85 440 1617 O ATOM 914 CB ASP A 115 77.190 13.999 2.214 1.00 54.10 C ANISOU 914 CB ASP C 115 7425 5973 7156 638 193 1521 C ATOM 915 CG ASP A 115 77.839 14.077 3.588 1.00 57.98 C ANISOU 915 CG ASP C 115 7268 7039 7724 782 726 1041 C ATOM 916 OD1 ASP A 115 77.293 13.478 4.542 1.00 63.54 O ANISOU 916 OD1 ASP C 115 8889 7752 7500 -32 -83 573 O ATOM 917 OD2 ASP A 115 78.893 14.732 3.704 1.00 72.11 O ANISOU 917 OD2 ASP C 115 8323 7947 11127 1838 1191 119 O ATOM 918 N ALA A 116 75.307 12.458 0.101 1.00 45.03 N ANISOU 918 N ALA C 116 6608 5130 5370 362 -231 2216 N ATOM 919 CA ALA A 116 74.567 12.493 -1.156 1.00 46.84 C ANISOU 919 CA ALA C 116 7112 5580 5106 -215 11 2295 C ATOM 920 C ALA A 116 73.078 12.213 -0.955 1.00 42.63 C ANISOU 920 C ALA C 116 6829 5093 4274 -485 416 1882 C ATOM 921 O ALA A 116 72.210 12.897 -1.529 1.00 43.65 O ANISOU 921 O ALA C 116 6664 5785 4135 -790 1404 1188 O ATOM 922 CB ALA A 116 75.190 11.491 -2.109 1.00 45.03 C ANISOU 922 CB ALA C 116 5193 5521 6397 378 640 2551 C ATOM 923 N GLU A 117 72.791 11.204 -0.142 1.00 40.19 N ANISOU 923 N GLU C 117 5901 5384 3985 -321 1107 1559 N ATOM 924 CA GLU A 117 71.420 10.851 0.242 1.00 42.41 C ANISOU 924 CA GLU C 117 6550 5019 4547 -371 582 1690 C ATOM 925 C GLU A 117 70.717 12.091 0.791 1.00 40.28 C ANISOU 925 C GLU C 117 6191 4878 4236 -462 829 1007 C ATOM 926 O GLU A 117 69.597 12.423 0.375 1.00 37.84 O ANISOU 926 O GLU C 117 5358 4923 4096 -54 799 1325 O ATOM 927 CB GLU A 117 71.453 9.710 1.250 1.00 41.10 C ANISOU 927 CB GLU C 117 6379 4044 5193 -218 420 1696 C ATOM 928 CG GLU A 117 70.167 9.224 1.886 1.00 39.62 C ANISOU 928 CG GLU C 117 5565 4581 4906 -77 1126 1712 C ATOM 929 CD GLU A 117 69.152 8.775 0.852 1.00 43.56 C ANISOU 929 CD GLU C 117 6478 4914 5158 -169 1533 1396 C ATOM 930 OE1 GLU A 117 69.589 8.360 -0.248 1.00 40.98 O ANISOU 930 OE1 GLU C 117 5095 5747 4727 12 796 1432 O ATOM 931 OE2 GLU A 117 67.935 8.851 1.144 1.00 41.60 O ANISOU 931 OE2 GLU C 117 5582 5443 4780 120 1472 1403 O ATOM 932 N CYS A 118 71.384 12.781 1.719 1.00 36.59 N ANISOU 932 N CYS C 118 5340 4757 3805 -197 141 868 N ATOM 933 CA CYS A 118 70.785 13.933 2.386 1.00 35.42 C ANISOU 933 CA CYS C 118 4597 4601 4259 145 389 845 C ATOM 934 C CYS A 118 70.551 15.064 1.397 1.00 35.22 C ANISOU 934 C CYS C 118 4292 4824 4266 153 357 926 C ATOM 935 O CYS A 118 69.491 15.692 1.393 1.00 36.37 O ANISOU 935 O CYS C 118 5254 4837 3727 -302 589 909 O ATOM 936 CB CYS A 118 71.666 14.369 3.562 1.00 38.72 C ANISOU 936 CB CYS C 118 6019 4186 4508 272 977 881 C ATOM 937 SG CYS A 118 71.692 13.110 4.887 1.00 42.29 S ANISOU 937 SG CYS C 118 6457 5128 4485 -445 1404 310 S ATOM 938 N ARG A 119 71.512 15.335 0.533 1.00 39.08 N ANISOU 938 N ARG C 119 3719 5677 5451 379 14 1271 N ATOM 939 CA ARG A 119 71.333 16.293 -0.554 1.00 44.31 C ANISOU 939 CA ARG C 119 4903 5728 6206 455 -1119 1422 C ATOM 940 C ARG A 119 70.174 16.005 -1.498 1.00 43.76 C ANISOU 940 C ARG C 119 5164 6305 5159 166 -1336 1150 C ATOM 941 O ARG A 119 69.403 16.869 -1.940 1.00 41.45 O ANISOU 941 O ARG C 119 5564 6327 3860 16 -1556 1553 O ATOM 942 CB ARG A 119 72.654 16.301 -1.349 1.00 52.18 C ANISOU 942 CB ARG C 119 6079 6237 7511 557 -1925 2009 C ATOM 943 CG ARG A 119 72.995 17.637 -1.982 1.00 62.59 C ANISOU 943 CG ARG C 119 7520 7269 8992 -116 -3727 3064 C ATOM 944 CD ARG A 119 74.332 17.567 -2.738 1.00 70.06 C ANISOU 944 CD ARG C 119 8623 7363 10634 217 -4665 3157 C ATOM 945 NE ARG A 119 75.347 16.935 -1.889 1.00 77.92 N ANISOU 945 NE ARG C 119 10834 7176 11594 33 -3455 2858 N ATOM 946 CZ ARG A 119 76.123 15.907 -2.201 1.00 81.38 C ANISOU 946 CZ ARG C 119 11888 7786 11248 -990 -3153 2568 C ATOM 947 NH1 ARG A 119 76.044 15.331 -3.402 1.00 79.87 N ANISOU 947 NH1 ARG C 119 11090 9685 9573 -1384 -5734 3721 N ATOM 948 NH2 ARG A 119 76.998 15.452 -1.302 1.00 78.89 N ANISOU 948 NH2 ARG C 119 10717 8579 10677 -1734 -5670 2193 N ATOM 949 N GLN A 120 70.010 14.737 -1.869 1.00 43.70 N ANISOU 949 N GLN C 120 5581 6454 4567 -50 -1033 1137 N ATOM 950 CA GLN A 120 68.932 14.350 -2.779 1.00 43.77 C ANISOU 950 CA GLN C 120 6264 6209 4159 -91 -698 1472 C ATOM 951 C GLN A 120 67.551 14.522 -2.159 1.00 42.63 C ANISOU 951 C GLN C 120 6254 5980 3964 -171 -1138 1024 C ATOM 952 O GLN A 120 66.590 14.937 -2.818 1.00 40.35 O ANISOU 952 O GLN C 120 5549 6318 3463 -59 -564 1020 O ATOM 953 CB GLN A 120 69.142 12.889 -3.209 1.00 51.15 C ANISOU 953 CB GLN C 120 8110 6639 4685 -934 797 1022 C ATOM 954 CG GLN A 120 70.400 12.702 -4.032 1.00 60.59 C ANISOU 954 CG GLN C 120 10526 6828 5666 -1654 -68 1791 C ATOM 955 CD GLN A 120 70.797 11.251 -4.214 1.00 66.38 C ANISOU 955 CD GLN C 120 11134 7736 6353 -2259 807 2050 C ATOM 956 OE1 GLN A 120 69.991 10.338 -4.011 1.00 80.51 O ANISOU 956 OE1 GLN C 120 11531 10907 8151 -3681 -1848 4294 O ATOM 957 NE2 GLN A 120 72.058 11.042 -4.597 1.00 65.48 N ANISOU 957 NE2 GLN C 120 12268 6515 6094 -1355 4376 647 N ATOM 958 N TYR A 121 67.457 14.192 -0.864 1.00 39.41 N ANISOU 958 N TYR C 121 5523 5545 3904 -557 -941 999 N ATOM 959 CA TYR A 121 66.196 14.384 -0.151 1.00 37.24 C ANISOU 959 CA TYR C 121 4934 5576 3642 -351 -578 889 C ATOM 960 C TYR A 121 65.734 15.837 -0.249 1.00 35.57 C ANISOU 960 C TYR C 121 4686 5266 3564 -56 -151 609 C ATOM 961 O TYR A 121 64.586 16.115 -0.603 1.00 39.31 O ANISOU 961 O TYR C 121 5066 5420 4451 -17 279 342 O ATOM 962 CB TYR A 121 66.359 13.968 1.307 1.00 32.78 C ANISOU 962 CB TYR C 121 4529 4380 3547 235 -18 741 C ATOM 963 CG TYR A 121 65.129 13.454 2.015 1.00 32.72 C ANISOU 963 CG TYR C 121 4195 4876 3362 79 -13 842 C ATOM 964 CD1 TYR A 121 64.483 12.312 1.545 1.00 32.38 C ANISOU 964 CD1 TYR C 121 4294 4542 3467 -45 155 697 C ATOM 965 CD2 TYR A 121 64.623 14.111 3.141 1.00 29.32 C ANISOU 965 CD2 TYR C 121 4353 3681 3105 719 514 215 C ATOM 966 CE1 TYR A 121 63.360 11.824 2.172 1.00 29.55 C ANISOU 966 CE1 TYR C 121 4346 3796 3086 310 491 52 C ATOM 967 CE2 TYR A 121 63.502 13.629 3.779 1.00 26.68 C ANISOU 967 CE2 TYR C 121 4082 3327 2727 406 295 -193 C ATOM 968 CZ TYR A 121 62.887 12.500 3.287 1.00 29.38 C ANISOU 968 CZ TYR C 121 4160 3638 3366 350 482 232 C ATOM 969 OH TYR A 121 61.762 11.989 3.907 1.00 30.92 O ANISOU 969 OH TYR C 121 3871 4298 3580 135 349 502 O ATOM 970 N GLU A 122 66.621 16.779 0.065 1.00 34.29 N ANISOU 970 N GLU C 122 4451 5144 3434 344 -834 1356 N ATOM 971 CA GLU A 122 66.281 18.199 -0.034 1.00 37.50 C ANISOU 971 CA GLU C 122 4800 5818 3630 -156 498 -49 C ATOM 972 C GLU A 122 65.938 18.540 -1.481 1.00 36.58 C ANISOU 972 C GLU C 122 4713 5633 3554 185 412 101 C ATOM 973 O GLU A 122 65.026 19.311 -1.780 1.00 38.91 O ANISOU 973 O GLU C 122 4594 6036 4155 -416 -691 -119 O ATOM 974 CB GLU A 122 67.418 19.113 0.422 1.00 37.54 C ANISOU 974 CB GLU C 122 4948 5625 3692 -122 635 -69 C ATOM 975 CG GLU A 122 67.745 18.991 1.907 1.00 35.43 C ANISOU 975 CG GLU C 122 4337 5596 3529 370 210 271 C ATOM 976 CD GLU A 122 66.792 19.757 2.797 1.00 39.13 C ANISOU 976 CD GLU C 122 5390 5602 3876 -300 368 243 C ATOM 977 OE1 GLU A 122 65.987 20.554 2.271 1.00 40.51 O ANISOU 977 OE1 GLU C 122 5324 5966 4101 -741 -1057 413 O ATOM 978 OE2 GLU A 122 66.874 19.529 4.033 1.00 37.69 O ANISOU 978 OE2 GLU C 122 5819 4757 3746 -47 903 257 O ATOM 979 N GLU A 123 66.719 17.934 -2.388 1.00 41.44 N ANISOU 979 N GLU C 123 5037 6678 4029 -410 -421 951 N ATOM 980 CA GLU A 123 66.393 18.240 -3.789 1.00 45.19 C ANISOU 980 CA GLU C 123 6449 6777 3942 -681 -248 1030 C ATOM 981 C GLU A 123 65.017 17.719 -4.172 1.00 44.81 C ANISOU 981 C GLU C 123 5963 7095 3967 -1105 -108 473 C ATOM 982 O GLU A 123 64.259 18.368 -4.898 1.00 42.83 O ANISOU 982 O GLU C 123 6460 6124 3688 -484 -1306 1300 O ATOM 983 CB GLU A 123 67.483 17.657 -4.693 1.00 52.97 C ANISOU 983 CB GLU C 123 7888 7594 4642 -1002 -1478 1840 C ATOM 984 CG GLU A 123 68.500 18.723 -5.065 1.00 62.88 C ANISOU 984 CG GLU C 123 8488 7466 7937 376 -1773 1479 C ATOM 985 CD GLU A 123 69.895 18.461 -4.544 1.00 75.26 C ANISOU 985 CD GLU C 123 10105 7469 11021 -13 -239 782 C ATOM 986 OE1 GLU A 123 70.568 17.541 -5.059 1.00 94.72 O ANISOU 986 OE1 GLU C 123 15817 7792 12381 -1954 62 894 O ATOM 987 OE2 GLU A 123 70.327 19.187 -3.610 1.00108.70 O ANISOU 987 OE2 GLU C 123 15891 10579 14830 -1925 4492 -3558 O ATOM 988 N LYS A 124 64.671 16.521 -3.684 1.00 43.43 N ANISOU 988 N LYS C 124 6342 6311 3849 -1081 -739 1307 N ATOM 989 CA LYS A 124 63.347 15.991 -4.026 1.00 43.60 C ANISOU 989 CA LYS C 124 5986 6783 3799 -1212 -366 1516 C ATOM 990 C LYS A 124 62.242 16.894 -3.483 1.00 41.43 C ANISOU 990 C LYS C 124 6080 6378 3283 -809 740 844 C ATOM 991 O LYS A 124 61.252 17.145 -4.171 1.00 39.70 O ANISOU 991 O LYS C 124 5588 6905 2593 -416 174 717 O ATOM 992 CB LYS A 124 63.192 14.556 -3.514 1.00 48.70 C ANISOU 992 CB LYS C 124 6154 7889 4462 -1797 -661 2218 C ATOM 993 CG LYS A 124 62.923 13.514 -4.582 1.00 63.43 C ANISOU 993 CG LYS C 124 7294 10431 6376 -3061 617 2158 C ATOM 994 CD LYS A 124 61.969 12.429 -4.104 1.00 65.56 C ANISOU 994 CD LYS C 124 7032 11017 6862 -1995 1436 1559 C ATOM 995 CE LYS A 124 60.995 12.030 -5.205 1.00 69.50 C ANISOU 995 CE LYS C 124 8209 12180 6018 -2846 2079 1601 C ATOM 996 NZ LYS A 124 60.119 10.880 -4.814 1.00 75.15 N ANISOU 996 NZ LYS C 124 7038 17031 4484 -4576 3724 -1262 N ATOM 997 N ILE A 125 62.381 17.402 -2.257 1.00 38.54 N ANISOU 997 N ILE C 125 4878 6076 3689 -691 1108 567 N ATOM 998 CA ILE A 125 61.343 18.307 -1.737 1.00 34.53 C ANISOU 998 CA ILE C 125 3711 6172 3237 -519 393 769 C ATOM 999 C ILE A 125 61.184 19.502 -2.678 1.00 38.08 C ANISOU 999 C ILE C 125 4373 6461 3635 -657 3 649 C ATOM 1000 O ILE A 125 60.081 19.861 -3.113 1.00 40.44 O ANISOU 1000 O ILE C 125 5635 6242 3488 -613 -524 843 O ATOM 1001 CB ILE A 125 61.675 18.781 -0.315 1.00 38.18 C ANISOU 1001 CB ILE C 125 4638 6414 3453 -940 800 561 C ATOM 1002 CG1 ILE A 125 61.622 17.669 0.727 1.00 37.72 C ANISOU 1002 CG1 ILE C 125 4797 6191 3344 -1317 1369 -151 C ATOM 1003 CG2 ILE A 125 60.755 19.932 0.076 1.00 31.39 C ANISOU 1003 CG2 ILE C 125 3778 5944 2204 -412 106 304 C ATOM 1004 CD1 ILE A 125 62.482 17.890 1.949 1.00 33.33 C ANISOU 1004 CD1 ILE C 125 3304 5887 3474 -140 1071 460 C ATOM 1005 N ARG A 126 62.337 20.104 -3.012 1.00 39.91 N ANISOU 1005 N ARG C 126 5093 6528 3541 -592 -799 1236 N ATOM 1006 CA ARG A 126 62.309 21.266 -3.906 1.00 41.68 C ANISOU 1006 CA ARG C 126 4615 6590 4630 -591 -504 396 C ATOM 1007 C ARG A 126 61.771 20.855 -5.266 1.00 42.83 C ANISOU 1007 C ARG C 126 6096 6161 4016 -833 -706 654 C ATOM 1008 O ARG A 126 61.215 21.691 -5.978 1.00 50.68 O ANISOU 1008 O ARG C 126 8113 7268 3876 -1592 -1649 650 O ATOM 1009 CB ARG A 126 63.680 21.935 -4.040 1.00 49.83 C ANISOU 1009 CB ARG C 126 4423 7446 7066 -493 -945 639 C ATOM 1010 CG ARG A 126 64.204 22.446 -2.704 1.00 61.30 C ANISOU 1010 CG ARG C 126 5305 8610 9378 -150 1073 -467 C ATOM 1011 CD ARG A 126 65.595 23.054 -2.772 1.00 70.98 C ANISOU 1011 CD ARG C 126 6066 8802 12102 403 337 -1383 C ATOM 1012 NE ARG A 126 66.356 22.926 -1.522 1.00 75.78 N ANISOU 1012 NE ARG C 126 6410 9126 13256 732 279 -2434 N ATOM 1013 CZ ARG A 126 67.573 22.386 -1.464 1.00 80.52 C ANISOU 1013 CZ ARG C 126 7729 9012 13852 270 -308 -2303 C ATOM 1014 NH1 ARG A 126 68.157 21.931 -2.573 1.00 75.26 N ANISOU 1014 NH1 ARG C 126 3984 10070 14544 614 -1937 -1211 N ATOM 1015 NH2 ARG A 126 68.221 22.293 -0.304 1.00 84.71 N ANISOU 1015 NH2 ARG C 126 8443 9133 14609 154 -560 -3265 N ATOM 1016 N SER A 127 61.892 19.592 -5.680 1.00 45.17 N ANISOU 1016 N SER C 127 6405 6105 4654 -537 272 666 N ATOM 1017 CA SER A 127 61.347 19.291 -7.022 1.00 45.18 C ANISOU 1017 CA SER C 127 6382 6517 4269 -264 -284 650 C ATOM 1018 C SER A 127 59.838 19.477 -7.002 1.00 44.06 C ANISOU 1018 C SER C 127 5846 6620 4274 -268 -1001 7 C ATOM 1019 O SER A 127 59.258 19.858 -8.010 1.00 51.05 O ANISOU 1019 O SER C 127 9415 6449 3533 -269 -623 590 O ATOM 1020 CB SER A 127 61.708 17.887 -7.492 1.00 46.96 C ANISOU 1020 CB SER C 127 6559 6827 4457 -337 566 241 C ATOM 1021 OG SER A 127 61.038 16.919 -6.680 1.00 47.73 O ANISOU 1021 OG SER C 127 5686 6576 5873 44 856 1070 O ATOM 1022 N TYR A 128 59.177 19.230 -5.874 1.00 41.48 N ANISOU 1022 N TYR C 128 5253 6118 4389 -622 -1232 -208 N ATOM 1023 CA TYR A 128 57.739 19.425 -5.817 1.00 41.75 C ANISOU 1023 CA TYR C 128 5167 6292 4404 -421 -748 -126 C ATOM 1024 C TYR A 128 57.424 20.873 -5.473 1.00 43.28 C ANISOU 1024 C TYR C 128 5150 5889 5406 -311 -543 -473 C ATOM 1025 O TYR A 128 56.326 21.341 -5.751 1.00 50.69 O ANISOU 1025 O TYR C 128 6660 5912 6687 -290 -152 -716 O ATOM 1026 CB TYR A 128 57.074 18.553 -4.758 1.00 40.32 C ANISOU 1026 CB TYR C 128 5256 6154 3908 -642 -520 476 C ATOM 1027 CG TYR A 128 57.000 17.081 -5.096 1.00 38.84 C ANISOU 1027 CG TYR C 128 5027 5838 3892 -375 -576 486 C ATOM 1028 CD1 TYR A 128 56.016 16.593 -5.944 1.00 40.46 C ANISOU 1028 CD1 TYR C 128 5413 5790 4169 -563 -303 184 C ATOM 1029 CD2 TYR A 128 57.931 16.194 -4.549 1.00 36.34 C ANISOU 1029 CD2 TYR C 128 4779 5615 3412 -143 -577 724 C ATOM 1030 CE1 TYR A 128 55.946 15.251 -6.255 1.00 41.77 C ANISOU 1030 CE1 TYR C 128 6297 5884 3690 -902 535 585 C ATOM 1031 CE2 TYR A 128 57.856 14.850 -4.863 1.00 39.91 C ANISOU 1031 CE2 TYR C 128 4938 5837 4389 -371 -305 415 C ATOM 1032 CZ TYR A 128 56.869 14.392 -5.711 1.00 41.74 C ANISOU 1032 CZ TYR C 128 6221 6101 3537 -1268 787 509 C ATOM 1033 OH TYR A 128 56.828 13.043 -5.994 1.00 42.11 O ANISOU 1033 OH TYR C 128 6000 5514 4487 -746 719 1670 O ATOM 1034 N GLY A 129 58.381 21.561 -4.848 1.00 42.11 N ANISOU 1034 N GLY C 129 5664 6058 4278 -85 -183 498 N ATOM 1035 CA GLY A 129 58.142 22.973 -4.579 1.00 40.48 C ANISOU 1035 CA GLY C 129 6175 6021 3184 -368 176 -100 C ATOM 1036 C GLY A 129 58.108 23.221 -3.090 1.00 37.91 C ANISOU 1036 C GLY C 129 5236 6069 3100 293 -58 -536 C ATOM 1037 O GLY A 129 58.929 23.963 -2.568 1.00 40.86 O ANISOU 1037 O GLY C 129 5364 6091 4071 -64 550 -542 O ATOM 1038 N LYS A 130 57.174 22.606 -2.364 1.00 41.09 N ANISOU 1038 N LYS C 130 5571 6204 3836 -158 -867 -467 N ATOM 1039 CA LYS A 130 57.180 22.867 -0.930 1.00 39.33 C ANISOU 1039 CA LYS C 130 5076 5865 4003 -166 -797 221 C ATOM 1040 C LYS A 130 56.333 21.826 -0.209 1.00 34.07 C ANISOU 1040 C LYS C 130 4613 4869 3463 492 -65 -221 C ATOM 1041 O LYS A 130 55.469 21.237 -0.856 1.00 37.69 O ANISOU 1041 O LYS C 130 4983 5663 3676 -107 1081 345 O ATOM 1042 CB LYS A 130 56.605 24.243 -0.611 1.00 48.04 C ANISOU 1042 CB LYS C 130 6199 6826 5226 -1318 -1696 846 C ATOM 1043 CG LYS A 130 55.113 24.281 -0.956 1.00 56.92 C ANISOU 1043 CG LYS C 130 8814 5910 6904 -696 -2458 1845 C ATOM 1044 CD LYS A 130 54.542 25.629 -0.525 1.00 64.23 C ANISOU 1044 CD LYS C 130 10079 6950 7377 -1460 -1556 2019 C ATOM 1045 CE LYS A 130 55.684 26.560 -0.131 1.00 66.12 C ANISOU 1045 CE LYS C 130 10805 8179 6139 -1726 -125 739 C ATOM 1046 NZ LYS A 130 55.990 26.498 1.327 1.00 77.00 N ANISOU 1046 NZ LYS C 130 14511 8537 6209 -992 -1736 -441 N ATOM 1047 N ILE A 131 56.625 21.673 1.065 1.00 31.02 N ANISOU 1047 N ILE C 131 3861 4582 3345 -482 133 -47 N ATOM 1048 CA ILE A 131 55.773 20.827 1.903 1.00 31.31 C ANISOU 1048 CA ILE C 131 4012 4209 3678 -423 -81 -152 C ATOM 1049 C ILE A 131 54.588 21.677 2.323 1.00 30.73 C ANISOU 1049 C ILE C 131 3753 4269 3654 -517 150 -164 C ATOM 1050 O ILE A 131 54.794 22.773 2.853 1.00 34.14 O ANISOU 1050 O ILE C 131 3854 5108 4008 -791 188 99 O ATOM 1051 CB ILE A 131 56.594 20.271 3.083 1.00 33.63 C ANISOU 1051 CB ILE C 131 5058 4285 3436 -1033 -124 -9 C ATOM 1052 CG1 ILE A 131 57.711 19.342 2.585 1.00 31.40 C ANISOU 1052 CG1 ILE C 131 4514 4086 3331 -270 -208 42 C ATOM 1053 CG2 ILE A 131 55.705 19.591 4.110 1.00 25.43 C ANISOU 1053 CG2 ILE C 131 4033 3240 2391 138 1295 -502 C ATOM 1054 CD1 ILE A 131 58.734 18.921 3.589 1.00 29.42 C ANISOU 1054 CD1 ILE C 131 4061 4050 3066 284 -38 314 C ATOM 1055 N HIS A 132 53.350 21.250 2.084 1.00 28.52 N ANISOU 1055 N HIS C 132 4089 4323 2422 -235 -296 -275 N ATOM 1056 CA HIS A 132 52.205 22.072 2.464 1.00 30.32 C ANISOU 1056 CA HIS C 132 4157 4435 2930 -299 71 -4 C ATOM 1057 C HIS A 132 51.895 22.024 3.951 1.00 31.66 C ANISOU 1057 C HIS C 132 4407 4647 2975 -666 86 210 C ATOM 1058 O HIS A 132 51.430 23.026 4.513 1.00 33.63 O ANISOU 1058 O HIS C 132 5439 4291 3048 -711 1019 -321 O ATOM 1059 CB HIS A 132 50.972 21.612 1.676 1.00 30.62 C ANISOU 1059 CB HIS C 132 4246 4205 3184 -277 46 -46 C ATOM 1060 CG HIS A 132 51.233 21.742 0.198 1.00 32.30 C ANISOU 1060 CG HIS C 132 4720 4451 3103 -214 79 -368 C ATOM 1061 ND1 HIS A 132 51.222 22.955 -0.455 1.00 37.74 N ANISOU 1061 ND1 HIS C 132 5939 5256 3143 -1222 -185 -328 N ATOM 1062 CD2 HIS A 132 51.508 20.816 -0.731 1.00 30.12 C ANISOU 1062 CD2 HIS C 132 4730 4248 2467 -1 741 -1297 C ATOM 1063 CE1 HIS A 132 51.483 22.767 -1.740 1.00 40.61 C ANISOU 1063 CE1 HIS C 132 6737 5694 3000 -1929 -57 -571 C ATOM 1064 NE2 HIS A 132 51.662 21.468 -1.925 1.00 40.22 N ANISOU 1064 NE2 HIS C 132 6345 5845 3092 -1717 -282 -259 N ATOM 1065 N LEU A 133 52.142 20.863 4.553 1.00 31.59 N ANISOU 1065 N LEU C 133 4605 4354 3043 -380 -89 -26 N ATOM 1066 CA LEU A 133 51.878 20.657 5.968 1.00 28.37 C ANISOU 1066 CA LEU C 133 3938 3870 2972 -91 196 10 C ATOM 1067 C LEU A 133 52.903 19.688 6.542 1.00 28.98 C ANISOU 1067 C LEU C 133 3357 4254 3399 -330 353 -398 C ATOM 1068 O LEU A 133 52.969 18.544 6.068 1.00 32.62 O ANISOU 1068 O LEU C 133 4510 4525 3358 -792 898 -113 O ATOM 1069 CB LEU A 133 50.480 20.107 6.181 1.00 29.90 C ANISOU 1069 CB LEU C 133 3627 4260 3473 -104 292 -72 C ATOM 1070 CG LEU A 133 50.077 19.724 7.607 1.00 30.77 C ANISOU 1070 CG LEU C 133 3544 4725 3421 360 627 493 C ATOM 1071 CD1 LEU A 133 50.213 20.885 8.574 1.00 30.36 C ANISOU 1071 CD1 LEU C 133 3154 5025 3356 -426 420 -419 C ATOM 1072 CD2 LEU A 133 48.632 19.209 7.590 1.00 30.54 C ANISOU 1072 CD2 LEU C 133 3610 4669 3327 357 529 -212 C ATOM 1073 N PHE A 134 53.680 20.159 7.515 1.00 30.24 N ANISOU 1073 N PHE C 134 4088 4159 3241 -390 666 -253 N ATOM 1074 CA PHE A 134 54.669 19.298 8.152 1.00 27.13 C ANISOU 1074 CA PHE C 134 3676 3832 2800 -121 279 137 C ATOM 1075 C PHE A 134 54.192 19.036 9.583 1.00 27.18 C ANISOU 1075 C PHE C 134 3808 3450 3069 -186 63 527 C ATOM 1076 O PHE A 134 54.101 19.964 10.382 1.00 27.06 O ANISOU 1076 O PHE C 134 3762 3739 2780 -314 182 84 O ATOM 1077 CB PHE A 134 56.066 19.917 8.159 1.00 26.18 C ANISOU 1077 CB PHE C 134 3256 3825 2867 -375 109 415 C ATOM 1078 CG PHE A 134 57.205 18.918 8.065 1.00 28.15 C ANISOU 1078 CG PHE C 134 3764 3739 3192 -258 -66 289 C ATOM 1079 CD1 PHE A 134 57.223 17.776 8.857 1.00 27.28 C ANISOU 1079 CD1 PHE C 134 3910 3496 2959 7 63 -133 C ATOM 1080 CD2 PHE A 134 58.264 19.122 7.173 1.00 26.16 C ANISOU 1080 CD2 PHE C 134 3356 3681 2900 -3 414 148 C ATOM 1081 CE1 PHE A 134 58.263 16.876 8.752 1.00 29.02 C ANISOU 1081 CE1 PHE C 134 4191 3644 3192 -273 60 88 C ATOM 1082 CE2 PHE A 134 59.305 18.210 7.054 1.00 28.76 C ANISOU 1082 CE2 PHE C 134 4500 3692 2734 -148 175 169 C ATOM 1083 CZ PHE A 134 59.301 17.072 7.845 1.00 30.25 C ANISOU 1083 CZ PHE C 134 4737 3547 3210 -171 -64 52 C ATOM 1084 N MET A 135 53.879 17.800 9.905 1.00 26.32 N ANISOU 1084 N MET C 135 3595 3693 2714 -5 367 190 N ATOM 1085 CA MET A 135 53.481 17.360 11.217 1.00 25.09 C ANISOU 1085 CA MET C 135 3269 3703 2560 -166 605 448 C ATOM 1086 C MET A 135 54.695 16.826 11.957 1.00 25.40 C ANISOU 1086 C MET C 135 3207 3842 2601 -266 460 287 C ATOM 1087 O MET A 135 55.504 16.078 11.409 1.00 25.93 O ANISOU 1087 O MET C 135 3696 3701 2456 163 571 289 O ATOM 1088 CB MET A 135 52.413 16.255 11.129 1.00 25.32 C ANISOU 1088 CB MET C 135 3207 4013 2401 -318 701 302 C ATOM 1089 CG MET A 135 51.935 15.900 12.544 1.00 28.15 C ANISOU 1089 CG MET C 135 3367 4549 2781 -814 4 125 C ATOM 1090 SD MET A 135 50.476 14.833 12.489 1.00 31.02 S ANISOU 1090 SD MET C 135 3750 4653 3384 -375 -86 334 S ATOM 1091 CE MET A 135 51.265 13.280 11.998 1.00 28.43 C ANISOU 1091 CE MET C 135 3016 4068 3717 -83 256 -533 C ATOM 1092 N GLY A 136 54.876 17.189 13.227 1.00 24.78 N ANISOU 1092 N GLY C 136 3188 3786 2439 -503 167 240 N ATOM 1093 CA GLY A 136 56.023 16.670 13.975 1.00 27.87 C ANISOU 1093 CA GLY C 136 3717 4095 2776 -678 220 -175 C ATOM 1094 C GLY A 136 55.698 16.602 15.458 1.00 26.53 C ANISOU 1094 C GLY C 136 3610 3703 2768 -44 526 -170 C ATOM 1095 O GLY A 136 54.590 16.946 15.894 1.00 27.86 O ANISOU 1095 O GLY C 136 3389 3779 3417 81 -146 -182 O ATOM 1096 N GLY A 137 56.663 16.157 16.248 1.00 29.09 N ANISOU 1096 N GLY C 137 4509 3712 2831 -273 435 -262 N ATOM 1097 CA GLY A 137 56.579 16.247 17.709 1.00 28.89 C ANISOU 1097 CA GLY C 137 4062 4089 2827 -596 602 -311 C ATOM 1098 C GLY A 137 57.680 17.183 18.223 1.00 28.78 C ANISOU 1098 C GLY C 137 3846 4271 2819 -450 276 -211 C ATOM 1099 O GLY A 137 58.293 17.908 17.432 1.00 29.61 O ANISOU 1099 O GLY C 137 4311 4132 2806 -454 18 -10 O ATOM 1100 N VAL A 138 57.933 17.165 19.535 1.00 26.82 N ANISOU 1100 N VAL C 138 3435 3959 2794 -174 231 -77 N ATOM 1101 CA VAL A 138 58.981 18.048 20.061 1.00 24.45 C ANISOU 1101 CA VAL C 138 3353 3292 2644 -155 53 295 C ATOM 1102 C VAL A 138 59.702 17.335 21.198 1.00 24.17 C ANISOU 1102 C VAL C 138 3323 3399 2464 47 -81 329 C ATOM 1103 O VAL A 138 59.084 16.580 21.955 1.00 26.46 O ANISOU 1103 O VAL C 138 3429 3798 2826 -189 -351 516 O ATOM 1104 CB VAL A 138 58.366 19.399 20.481 1.00 25.77 C ANISOU 1104 CB VAL C 138 3325 3426 3039 -172 -199 611 C ATOM 1105 CG1 VAL A 138 57.301 19.185 21.553 1.00 28.40 C ANISOU 1105 CG1 VAL C 138 4717 3466 2609 121 -305 480 C ATOM 1106 CG2 VAL A 138 59.411 20.390 20.973 1.00 26.22 C ANISOU 1106 CG2 VAL C 138 3531 4230 2201 -424 148 240 C ATOM 1107 N GLY A 139 61.016 17.547 21.298 1.00 24.37 N ANISOU 1107 N GLY C 139 3893 2966 2402 32 106 679 N ATOM 1108 CA GLY A 139 61.778 16.901 22.356 1.00 26.69 C ANISOU 1108 CA GLY C 139 4036 3470 2635 13 248 245 C ATOM 1109 C GLY A 139 61.472 17.577 23.688 1.00 27.30 C ANISOU 1109 C GLY C 139 4457 3318 2597 -329 173 122 C ATOM 1110 O GLY A 139 60.911 18.685 23.748 1.00 28.89 O ANISOU 1110 O GLY C 139 4748 3244 2984 -395 -207 425 O ATOM 1111 N ASN A 140 61.837 16.917 24.795 1.00 25.69 N ANISOU 1111 N ASN C 140 3631 3502 2629 48 -42 124 N ATOM 1112 CA ASN A 140 61.653 17.480 26.116 1.00 27.00 C ANISOU 1112 CA ASN C 140 3575 4061 2622 -548 93 -99 C ATOM 1113 C ASN A 140 62.418 18.803 26.234 1.00 28.54 C ANISOU 1113 C ASN C 140 3580 3849 3413 -564 68 141 C ATOM 1114 O ASN A 140 62.011 19.695 26.998 1.00 26.79 O ANISOU 1114 O ASN C 140 3564 3855 2759 -580 23 -128 O ATOM 1115 CB ASN A 140 62.146 16.518 27.197 1.00 24.74 C ANISOU 1115 CB ASN C 140 3986 2859 2555 -398 -275 507 C ATOM 1116 CG ASN A 140 61.322 15.256 27.317 1.00 27.52 C ANISOU 1116 CG ASN C 140 4084 3268 3104 -302 -543 -183 C ATOM 1117 OD1 ASN A 140 60.318 15.041 26.617 1.00 28.78 O ANISOU 1117 OD1 ASN C 140 4295 4160 2480 -141 170 318 O ATOM 1118 ND2 ASN A 140 61.735 14.366 28.214 1.00 32.68 N ANISOU 1118 ND2 ASN C 140 4801 4318 3298 -1401 -449 -329 N ATOM 1119 N ASP A 141 63.518 18.917 25.504 1.00 25.43 N ANISOU 1119 N ASP C 141 3624 3714 2323 -341 347 -354 N ATOM 1120 CA ASP A 141 64.275 20.168 25.582 1.00 26.26 C ANISOU 1120 CA ASP C 141 3642 3814 2522 -331 355 -36 C ATOM 1121 C ASP A 141 63.924 21.106 24.437 1.00 26.49 C ANISOU 1121 C ASP C 141 3569 3491 3006 -170 94 -156 C ATOM 1122 O ASP A 141 64.705 22.022 24.136 1.00 25.75 O ANISOU 1122 O ASP C 141 3565 3223 2995 -391 112 560 O ATOM 1123 CB ASP A 141 65.784 19.892 25.582 1.00 26.72 C ANISOU 1123 CB ASP C 141 3547 3842 2765 -309 -249 -384 C ATOM 1124 CG ASP A 141 66.196 19.174 24.308 1.00 26.06 C ANISOU 1124 CG ASP C 141 3097 3817 2989 461 -314 22 C ATOM 1125 OD1 ASP A 141 67.384 18.804 24.175 1.00 34.78 O ANISOU 1125 OD1 ASP C 141 5599 3472 4144 141 402 -150 O ATOM 1126 OD2 ASP A 141 65.357 18.943 23.417 1.00 30.28 O ANISOU 1126 OD2 ASP C 141 4384 3992 3130 256 314 -130 O ATOM 1127 N GLY A 142 62.792 20.884 23.779 1.00 26.48 N ANISOU 1127 N GLY C 142 3962 3312 2788 -208 434 86 N ATOM 1128 CA GLY A 142 62.320 21.778 22.717 1.00 25.59 C ANISOU 1128 CA GLY C 142 3756 3176 2790 -148 467 139 C ATOM 1129 C GLY A 142 62.904 21.490 21.358 1.00 25.67 C ANISOU 1129 C GLY C 142 3392 3211 3151 224 -423 428 C ATOM 1130 O GLY A 142 62.554 22.173 20.366 1.00 27.27 O ANISOU 1130 O GLY C 142 3583 3831 2948 -36 154 66 O ATOM 1131 N HIS A 143 63.798 20.503 21.210 1.00 26.81 N ANISOU 1131 N HIS C 143 3542 3427 3216 -44 -50 594 N ATOM 1132 CA HIS A 143 64.425 20.247 19.896 1.00 27.70 C ANISOU 1132 CA HIS C 143 3694 3720 3113 -107 -43 623 C ATOM 1133 C HIS A 143 63.461 19.599 18.912 1.00 28.72 C ANISOU 1133 C HIS C 143 3819 4031 3063 -16 -117 490 C ATOM 1134 O HIS A 143 62.417 19.058 19.287 1.00 28.56 O ANISOU 1134 O HIS C 143 3322 4544 2984 -223 -216 252 O ATOM 1135 CB HIS A 143 65.658 19.345 20.030 1.00 28.55 C ANISOU 1135 CB HIS C 143 4574 3745 2530 -324 194 700 C ATOM 1136 CG HIS A 143 65.382 17.889 20.250 1.00 35.65 C ANISOU 1136 CG HIS C 143 5284 4866 3394 -1553 -40 960 C ATOM 1137 ND1 HIS A 143 65.305 17.338 21.516 1.00 33.00 N ANISOU 1137 ND1 HIS C 143 4485 4459 3595 -302 -143 483 N ATOM 1138 CD2 HIS A 143 65.187 16.844 19.391 1.00 39.21 C ANISOU 1138 CD2 HIS C 143 5260 5829 3811 -1714 220 735 C ATOM 1139 CE1 HIS A 143 65.068 16.043 21.458 1.00 33.43 C ANISOU 1139 CE1 HIS C 143 4082 4472 4145 252 -361 928 C ATOM 1140 NE2 HIS A 143 64.984 15.717 20.173 1.00 38.04 N ANISOU 1140 NE2 HIS C 143 4721 5393 4340 -876 -18 943 N ATOM 1141 N ILE A 144 63.852 19.614 17.638 1.00 27.69 N ANISOU 1141 N ILE C 144 4000 3529 2989 -166 -216 269 N ATOM 1142 CA ILE A 144 63.012 19.049 16.579 1.00 30.21 C ANISOU 1142 CA ILE C 144 4441 3961 3078 -20 -40 137 C ATOM 1143 C ILE A 144 63.723 17.929 15.841 1.00 30.24 C ANISOU 1143 C ILE C 144 4207 4313 2970 29 -24 347 C ATOM 1144 O ILE A 144 64.912 18.069 15.501 1.00 28.53 O ANISOU 1144 O ILE C 144 3824 4341 2677 -185 -149 407 O ATOM 1145 CB ILE A 144 62.592 20.199 15.654 1.00 35.87 C ANISOU 1145 CB ILE C 144 5317 5273 3038 -1017 499 -391 C ATOM 1146 CG1 ILE A 144 61.524 21.071 16.339 1.00 39.81 C ANISOU 1146 CG1 ILE C 144 6210 5401 3515 -2039 1688 -660 C ATOM 1147 CG2 ILE A 144 62.162 19.683 14.284 1.00 38.08 C ANISOU 1147 CG2 ILE C 144 5980 5485 3002 -1448 680 -144 C ATOM 1148 CD1 ILE A 144 61.202 22.346 15.611 1.00 44.89 C ANISOU 1148 CD1 ILE C 144 5198 7047 4812 -2738 1919 -773 C ATOM 1149 N ALA A 145 63.000 16.827 15.616 1.00 30.04 N ANISOU 1149 N ALA C 145 4019 4709 2687 51 -574 734 N ATOM 1150 CA ALA A 145 63.566 15.665 14.933 1.00 33.88 C ANISOU 1150 CA ALA C 145 4272 4899 3700 -516 -314 528 C ATOM 1151 C ALA A 145 64.867 15.276 15.611 1.00 32.88 C ANISOU 1151 C ALA C 145 3871 4994 3626 -722 282 533 C ATOM 1152 O ALA A 145 64.880 15.193 16.850 1.00 37.05 O ANISOU 1152 O ALA C 145 5636 4738 3703 -722 -285 559 O ATOM 1153 CB ALA A 145 63.779 15.957 13.454 1.00 31.60 C ANISOU 1153 CB ALA C 145 4304 4341 3363 -118 479 935 C ATOM 1154 N PHE A 146 65.952 15.058 14.871 1.00 32.14 N ANISOU 1154 N PHE C 146 4142 4992 3078 -336 1125 474 N ATOM 1155 CA PHE A 146 67.210 14.764 15.556 1.00 32.43 C ANISOU 1155 CA PHE C 146 4183 5097 3041 -475 853 228 C ATOM 1156 C PHE A 146 68.101 16.005 15.593 1.00 31.27 C ANISOU 1156 C PHE C 146 4169 4422 3293 -471 846 212 C ATOM 1157 O PHE A 146 69.298 15.897 15.907 1.00 35.15 O ANISOU 1157 O PHE C 146 4625 4822 3907 -252 620 -501 O ATOM 1158 CB PHE A 146 68.019 13.620 14.938 1.00 32.34 C ANISOU 1158 CB PHE C 146 4126 5133 3028 -936 384 31 C ATOM 1159 CG PHE A 146 67.394 12.271 15.264 1.00 36.84 C ANISOU 1159 CG PHE C 146 4333 5777 3886 -1021 -100 160 C ATOM 1160 CD1 PHE A 146 67.578 11.699 16.508 1.00 42.68 C ANISOU 1160 CD1 PHE C 146 4466 7257 4494 -1295 -187 -795 C ATOM 1161 CD2 PHE A 146 66.637 11.610 14.317 1.00 34.07 C ANISOU 1161 CD2 PHE C 146 3601 5135 4210 121 -789 -10 C ATOM 1162 CE1 PHE A 146 67.007 10.474 16.799 1.00 45.34 C ANISOU 1162 CE1 PHE C 146 4476 7702 5049 -1527 -157 -1240 C ATOM 1163 CE2 PHE A 146 66.064 10.389 14.589 1.00 35.10 C ANISOU 1163 CE2 PHE C 146 3813 5445 4079 116 -1337 176 C ATOM 1164 CZ PHE A 146 66.259 9.828 15.834 1.00 39.62 C ANISOU 1164 CZ PHE C 146 4236 6578 4238 -695 -785 -513 C ATOM 1165 N ASN A 147 67.538 17.166 15.286 1.00 31.88 N ANISOU 1165 N ASN C 147 4445 4628 3040 -483 137 78 N ATOM 1166 CA ASN A 147 68.357 18.367 15.452 1.00 31.70 C ANISOU 1166 CA ASN C 147 4438 4565 3042 -688 276 -26 C ATOM 1167 C ASN A 147 68.663 18.638 16.918 1.00 34.38 C ANISOU 1167 C ASN C 147 4673 5296 3095 -405 194 -487 C ATOM 1168 O ASN A 147 67.894 18.355 17.845 1.00 40.03 O ANISOU 1168 O ASN C 147 6438 5686 3087 254 632 390 O ATOM 1169 CB ASN A 147 67.610 19.566 14.862 1.00 30.43 C ANISOU 1169 CB ASN C 147 4384 4252 2927 -123 -373 45 C ATOM 1170 CG ASN A 147 67.399 19.362 13.373 1.00 30.24 C ANISOU 1170 CG ASN C 147 4651 3873 2967 1 -136 262 C ATOM 1171 OD1 ASN A 147 68.316 19.713 12.618 1.00 32.49 O ANISOU 1171 OD1 ASN C 147 4299 4953 3093 -219 -486 341 O ATOM 1172 ND2 ASN A 147 66.250 18.814 12.993 1.00 30.25 N ANISOU 1172 ND2 ASN C 147 4554 3366 3574 -380 304 317 N ATOM 1173 N GLU A 148 69.823 19.229 17.218 1.00 36.52 N ANISOU 1173 N GLU C 148 4784 5165 3926 -576 621 -647 N ATOM 1174 CA GLU A 148 70.109 19.477 18.619 1.00 37.62 C ANISOU 1174 CA GLU C 148 4800 5496 3996 -506 795 -628 C ATOM 1175 C GLU A 148 69.702 20.874 19.040 1.00 35.13 C ANISOU 1175 C GLU C 148 4193 5501 3653 -282 383 -550 C ATOM 1176 O GLU A 148 69.453 21.711 18.181 1.00 36.10 O ANISOU 1176 O GLU C 148 4942 5346 3428 -441 92 -134 O ATOM 1177 CB GLU A 148 71.602 19.193 18.839 1.00 44.63 C ANISOU 1177 CB GLU C 148 6139 5477 5341 -679 1299 -1418 C ATOM 1178 CG GLU A 148 71.645 17.841 19.571 1.00 62.51 C ANISOU 1178 CG GLU C 148 10150 6335 7266 -2672 -1198 -738 C ATOM 1179 CD GLU A 148 73.036 17.265 19.703 1.00 62.28 C ANISOU 1179 CD GLU C 148 10737 6366 6563 -2751 -91 -994 C ATOM 1180 OE1 GLU A 148 73.584 17.463 20.814 1.00 58.46 O ANISOU 1180 OE1 GLU C 148 8529 7728 5956 -589 -931 32 O ATOM 1181 OE2 GLU A 148 73.494 16.659 18.705 1.00 53.92 O ANISOU 1181 OE2 GLU C 148 7807 6685 5995 -228 -852 -345 O ATOM 1182 N PRO A 149 69.633 21.105 20.339 1.00 32.87 N ANISOU 1182 N PRO C 149 3807 5083 3601 -97 -179 -132 N ATOM 1183 CA PRO A 149 69.445 22.461 20.839 1.00 32.24 C ANISOU 1183 CA PRO C 149 4390 4418 3444 -319 -805 463 C ATOM 1184 C PRO A 149 70.548 23.346 20.255 1.00 31.02 C ANISOU 1184 C PRO C 149 3812 4107 3866 -8 -140 -98 C ATOM 1185 O PRO A 149 71.674 22.884 20.079 1.00 30.07 O ANISOU 1185 O PRO C 149 3975 4089 3359 -109 69 11 O ATOM 1186 CB PRO A 149 69.648 22.284 22.333 1.00 31.62 C ANISOU 1186 CB PRO C 149 4043 4309 3661 -329 -144 -207 C ATOM 1187 CG PRO A 149 69.255 20.868 22.617 1.00 34.44 C ANISOU 1187 CG PRO C 149 4321 5187 3579 -832 -344 -382 C ATOM 1188 CD PRO A 149 69.762 20.110 21.417 1.00 35.77 C ANISOU 1188 CD PRO C 149 4150 5686 3756 -783 18 -291 C ATOM 1189 N ALA A 150 70.223 24.588 19.945 1.00 31.18 N ANISOU 1189 N ALA C 150 3700 4110 4039 -107 -144 333 N ATOM 1190 CA ALA A 150 71.081 25.610 19.340 1.00 28.85 C ANISOU 1190 CA ALA C 150 3788 3648 3525 217 -129 -142 C ATOM 1191 C ALA A 150 71.430 25.215 17.913 1.00 30.57 C ANISOU 1191 C ALA C 150 4376 3691 3548 371 -19 -112 C ATOM 1192 O ALA A 150 72.415 25.716 17.373 1.00 31.66 O ANISOU 1192 O ALA C 150 4014 4233 3783 29 -88 363 O ATOM 1193 CB ALA A 150 72.345 25.885 20.139 1.00 31.71 C ANISOU 1193 CB ALA C 150 3074 4424 4551 -839 652 -1116 C ATOM 1194 N SER A 151 70.628 24.335 17.305 1.00 29.94 N ANISOU 1194 N SER C 151 3870 4227 3279 -100 -355 23 N ATOM 1195 CA SER A 151 70.780 24.104 15.883 1.00 28.79 C ANISOU 1195 CA SER C 151 3667 3912 3359 -130 -366 214 C ATOM 1196 C SER A 151 70.517 25.421 15.146 1.00 27.85 C ANISOU 1196 C SER C 151 3270 4162 3148 -5 -137 69 C ATOM 1197 O SER A 151 69.680 26.178 15.640 1.00 28.87 O ANISOU 1197 O SER C 151 3544 4607 2820 -650 -615 285 O ATOM 1198 CB SER A 151 69.774 23.099 15.314 1.00 29.68 C ANISOU 1198 CB SER C 151 3367 4612 3298 -169 -518 533 C ATOM 1199 OG SER A 151 70.103 21.755 15.637 1.00 34.72 O ANISOU 1199 OG SER C 151 3690 4948 4553 -486 -1143 1135 O ATOM 1200 N SER A 152 71.175 25.626 14.018 1.00 29.45 N ANISOU 1200 N SER C 152 3378 3942 3869 9 -659 386 N ATOM 1201 CA SER A 152 70.815 26.691 13.091 1.00 29.19 C ANISOU 1201 CA SER C 152 3469 4067 3556 16 -643 433 C ATOM 1202 C SER A 152 69.365 26.555 12.651 1.00 29.48 C ANISOU 1202 C SER C 152 3728 3893 3582 34 -663 526 C ATOM 1203 O SER A 152 68.876 25.446 12.364 1.00 29.07 O ANISOU 1203 O SER C 152 3750 3599 3698 168 -539 744 O ATOM 1204 CB SER A 152 71.723 26.667 11.852 1.00 24.29 C ANISOU 1204 CB SER C 152 2261 4031 2936 151 489 373 C ATOM 1205 OG SER A 152 71.192 27.581 10.892 1.00 30.65 O ANISOU 1205 OG SER C 152 4423 4323 2899 148 -104 292 O ATOM 1206 N LEU A 153 68.646 27.678 12.561 1.00 29.06 N ANISOU 1206 N LEU C 153 4048 4037 2954 -219 -370 477 N ATOM 1207 CA LEU A 153 67.255 27.631 12.103 1.00 29.26 C ANISOU 1207 CA LEU C 153 3685 3994 3440 -261 -742 284 C ATOM 1208 C LEU A 153 67.231 27.405 10.600 1.00 29.11 C ANISOU 1208 C LEU C 153 3316 4253 3491 209 -558 101 C ATOM 1209 O LEU A 153 66.172 27.208 9.999 1.00 34.08 O ANISOU 1209 O LEU C 153 4357 4097 4497 304 441 284 O ATOM 1210 CB LEU A 153 66.527 28.918 12.436 1.00 33.10 C ANISOU 1210 CB LEU C 153 3749 4053 4775 -216 131 228 C ATOM 1211 CG LEU A 153 65.677 28.988 13.711 1.00 40.02 C ANISOU 1211 CG LEU C 153 5950 5263 3992 -2329 133 679 C ATOM 1212 CD1 LEU A 153 66.136 28.019 14.783 1.00 36.67 C ANISOU 1212 CD1 LEU C 153 6870 4004 3059 -1329 1626 -51 C ATOM 1213 CD2 LEU A 153 65.650 30.409 14.268 1.00 35.55 C ANISOU 1213 CD2 LEU C 153 2763 5853 4889 200 331 967 C ATOM 1214 N ALA A 154 68.401 27.452 9.970 1.00 28.86 N ANISOU 1214 N ALA C 154 3772 3811 3384 -100 -231 365 N ATOM 1215 CA ALA A 154 68.457 27.133 8.545 1.00 30.37 C ANISOU 1215 CA ALA C 154 3746 4496 3297 -369 -386 198 C ATOM 1216 C ALA A 154 69.121 25.787 8.328 1.00 31.22 C ANISOU 1216 C ALA C 154 4347 4666 2850 -661 -348 317 C ATOM 1217 O ALA A 154 69.567 25.499 7.212 1.00 34.75 O ANISOU 1217 O ALA C 154 5023 4855 3323 -392 -1059 947 O ATOM 1218 CB ALA A 154 69.218 28.214 7.787 1.00 34.29 C ANISOU 1218 CB ALA C 154 4068 5230 3729 -356 -793 160 C ATOM 1219 N SER A 155 69.235 24.937 9.362 1.00 27.85 N ANISOU 1219 N SER C 155 3657 4121 2802 -121 7 9 N ATOM 1220 CA SER A 155 69.994 23.697 9.111 1.00 29.11 C ANISOU 1220 CA SER C 155 3680 4341 3039 -299 -34 162 C ATOM 1221 C SER A 155 69.218 22.813 8.149 1.00 31.02 C ANISOU 1221 C SER C 155 3935 4240 3611 -131 316 360 C ATOM 1222 O SER A 155 68.013 22.985 7.965 1.00 29.07 O ANISOU 1222 O SER C 155 4093 3993 2960 -410 506 489 O ATOM 1223 CB SER A 155 70.284 23.046 10.463 1.00 28.66 C ANISOU 1223 CB SER C 155 3994 4035 2860 -630 -380 718 C ATOM 1224 OG SER A 155 69.029 22.914 11.146 1.00 30.95 O ANISOU 1224 OG SER C 155 3936 4581 3242 -12 18 839 O ATOM 1225 N ARG A 156 69.868 21.854 7.497 1.00 27.27 N ANISOU 1225 N ARG C 156 3264 3955 3142 464 -1 470 N ATOM 1226 CA ARG A 156 69.280 21.015 6.462 1.00 28.27 C ANISOU 1226 CA ARG C 156 3079 4309 3353 470 18 544 C ATOM 1227 C ARG A 156 69.477 19.529 6.758 1.00 27.82 C ANISOU 1227 C ARG C 156 2907 3931 3731 789 -28 347 C ATOM 1228 O ARG A 156 70.164 19.194 7.729 1.00 31.42 O ANISOU 1228 O ARG C 156 4483 3701 3754 -136 705 427 O ATOM 1229 CB ARG A 156 69.927 21.343 5.109 1.00 30.35 C ANISOU 1229 CB ARG C 156 4010 4532 2991 289 -109 187 C ATOM 1230 CG ARG A 156 69.612 22.766 4.627 1.00 32.56 C ANISOU 1230 CG ARG C 156 4808 4586 2978 -232 -361 625 C ATOM 1231 CD ARG A 156 68.192 22.728 4.061 1.00 36.21 C ANISOU 1231 CD ARG C 156 5806 4472 3480 -146 -508 297 C ATOM 1232 NE ARG A 156 67.538 24.023 4.123 1.00 40.57 N ANISOU 1232 NE ARG C 156 6347 4722 4348 -532 -933 182 N ATOM 1233 CZ ARG A 156 66.285 24.234 3.735 1.00 40.13 C ANISOU 1233 CZ ARG C 156 5796 4720 4733 -761 -573 57 C ATOM 1234 NH1 ARG A 156 65.551 23.236 3.260 1.00 37.87 N ANISOU 1234 NH1 ARG C 156 5173 5635 3582 -493 -1594 379 N ATOM 1235 NH2 ARG A 156 65.806 25.463 3.839 1.00 40.93 N ANISOU 1235 NH2 ARG C 156 6082 4379 5092 -499 -635 1412 N ATOM 1236 N THR A 157 68.888 18.668 5.917 1.00 30.93 N ANISOU 1236 N THR C 157 3402 4458 3890 186 411 340 N ATOM 1237 CA THR A 157 68.904 17.225 6.105 1.00 31.02 C ANISOU 1237 CA THR C 157 3752 4415 3620 -155 491 575 C ATOM 1238 C THR A 157 70.333 16.734 6.249 1.00 30.19 C ANISOU 1238 C THR C 157 3483 4497 3492 48 735 555 C ATOM 1239 O THR A 157 71.187 17.150 5.454 1.00 35.36 O ANISOU 1239 O THR C 157 4388 4808 4240 93 111 919 O ATOM 1240 CB THR A 157 68.226 16.494 4.930 1.00 30.76 C ANISOU 1240 CB THR C 157 3447 4291 3950 77 433 279 C ATOM 1241 OG1 THR A 157 66.871 16.950 4.848 1.00 35.13 O ANISOU 1241 OG1 THR C 157 6169 4069 3109 -194 326 -108 O ATOM 1242 CG2 THR A 157 68.206 14.997 5.165 1.00 28.06 C ANISOU 1242 CG2 THR C 157 3457 4294 2910 150 280 74 C ATOM 1243 N ARG A 158 70.610 15.898 7.242 1.00 30.88 N ANISOU 1243 N ARG C 158 3677 4516 3538 -184 889 460 N ATOM 1244 CA ARG A 158 71.996 15.537 7.520 1.00 31.76 C ANISOU 1244 CA ARG C 158 3594 4736 3736 29 1033 278 C ATOM 1245 C ARG A 158 72.072 14.378 8.509 1.00 32.73 C ANISOU 1245 C ARG C 158 3919 4475 4043 -104 855 287 C ATOM 1246 O ARG A 158 71.090 14.038 9.149 1.00 34.08 O ANISOU 1246 O ARG C 158 4434 4672 3844 -90 510 247 O ATOM 1247 CB ARG A 158 72.773 16.733 8.083 1.00 34.38 C ANISOU 1247 CB ARG C 158 3660 5187 4217 9 1226 540 C ATOM 1248 CG ARG A 158 72.441 17.113 9.524 1.00 36.00 C ANISOU 1248 CG ARG C 158 4251 5275 4153 -123 1535 379 C ATOM 1249 CD ARG A 158 72.822 18.559 9.810 1.00 34.46 C ANISOU 1249 CD ARG C 158 4145 5227 3722 -368 735 1012 C ATOM 1250 NE ARG A 158 72.582 19.003 11.197 1.00 33.95 N ANISOU 1250 NE ARG C 158 4630 4450 3821 -159 1221 798 N ATOM 1251 CZ ARG A 158 71.384 19.428 11.608 1.00 36.78 C ANISOU 1251 CZ ARG C 158 6016 4217 3740 -394 521 541 C ATOM 1252 NH1 ARG A 158 70.388 19.432 10.717 1.00 31.31 N ANISOU 1252 NH1 ARG C 158 3855 4426 3616 -117 9 704 N ATOM 1253 NH2 ARG A 158 71.185 19.824 12.845 1.00 31.35 N ANISOU 1253 NH2 ARG C 158 3919 4507 3486 432 -249 696 N ATOM 1254 N ILE A 159 73.251 13.789 8.632 1.00 35.47 N ANISOU 1254 N ILE C 159 4542 4492 4441 -50 1111 179 N ATOM 1255 CA ILE A 159 73.465 12.708 9.573 1.00 35.07 C ANISOU 1255 CA ILE C 159 4407 4135 4782 416 896 -14 C ATOM 1256 C ILE A 159 73.786 13.314 10.945 1.00 37.45 C ANISOU 1256 C ILE C 159 4806 4741 4684 -268 875 -130 C ATOM 1257 O ILE A 159 74.442 14.357 11.004 1.00 39.31 O ANISOU 1257 O ILE C 159 4878 5013 5044 341 1309 -5 O ATOM 1258 CB ILE A 159 74.617 11.774 9.182 1.00 39.65 C ANISOU 1258 CB ILE C 159 5410 4542 5112 -294 284 485 C ATOM 1259 CG1 ILE A 159 74.660 10.505 10.040 1.00 41.71 C ANISOU 1259 CG1 ILE C 159 5362 5294 5191 -823 877 -95 C ATOM 1260 CG2 ILE A 159 75.947 12.513 9.232 1.00 38.23 C ANISOU 1260 CG2 ILE C 159 5699 3317 5509 -405 418 757 C ATOM 1261 CD1 ILE A 159 75.568 9.432 9.476 1.00 40.62 C ANISOU 1261 CD1 ILE C 159 5716 4824 4893 -491 821 -362 C ATOM 1262 N LYS A 160 73.317 12.643 11.978 1.00 40.97 N ANISOU 1262 N LYS C 160 5651 5057 4861 -739 423 378 N ATOM 1263 CA LYS A 160 73.477 12.991 13.365 1.00 43.00 C ANISOU 1263 CA LYS C 160 6809 4735 4795 -446 519 202 C ATOM 1264 C LYS A 160 73.896 11.766 14.195 1.00 44.52 C ANISOU 1264 C LYS C 160 6225 5368 5323 -675 1661 -868 C ATOM 1265 O LYS A 160 73.476 10.645 13.895 1.00 46.37 O ANISOU 1265 O LYS C 160 6438 5703 5476 -894 1992 -589 O ATOM 1266 CB LYS A 160 72.184 13.543 13.992 1.00 40.85 C ANISOU 1266 CB LYS C 160 5643 4962 4918 -153 508 397 C ATOM 1267 CG LYS A 160 71.690 14.883 13.487 1.00 43.72 C ANISOU 1267 CG LYS C 160 6473 4746 5394 -387 258 512 C ATOM 1268 CD LYS A 160 72.836 15.868 13.331 1.00 47.22 C ANISOU 1268 CD LYS C 160 5920 5840 6181 -889 443 211 C ATOM 1269 CE LYS A 160 72.930 16.801 14.518 1.00 51.24 C ANISOU 1269 CE LYS C 160 6579 6643 6247 -1400 612 143 C ATOM 1270 NZ LYS A 160 73.246 16.158 15.820 1.00 52.76 N ANISOU 1270 NZ LYS C 160 8506 5514 6026 -562 306 357 N ATOM 1271 N THR A 161 74.692 12.065 15.224 1.00 46.07 N ANISOU 1271 N THR C 161 6196 5573 5734 95 1582 -914 N ATOM 1272 CA THR A 161 75.071 11.104 16.249 1.00 50.03 C ANISOU 1272 CA THR C 161 6913 6464 5630 -308 1964 -1436 C ATOM 1273 C THR A 161 74.073 11.124 17.393 1.00 49.72 C ANISOU 1273 C THR C 161 6611 6875 5404 41 1749 -1746 C ATOM 1274 O THR A 161 73.955 12.122 18.095 1.00 51.50 O ANISOU 1274 O THR C 161 5747 7772 6050 61 770 -337 O ATOM 1275 CB THR A 161 76.463 11.432 16.808 1.00 50.46 C ANISOU 1275 CB THR C 161 6768 6590 5816 -161 1539 -1616 C ATOM 1276 OG1 THR A 161 77.384 11.480 15.708 1.00 55.20 O ANISOU 1276 OG1 THR C 161 6600 7971 6401 191 1818 -728 O ATOM 1277 CG2 THR A 161 76.939 10.343 17.756 1.00 52.69 C ANISOU 1277 CG2 THR C 161 4577 8539 6904 -166 2426 -3197 C ATOM 1278 N LEU A 162 73.315 10.063 17.602 1.00 50.34 N ANISOU 1278 N LEU C 162 6449 7256 5423 -457 1918 -1694 N ATOM 1279 CA LEU A 162 72.207 10.171 18.554 1.00 52.65 C ANISOU 1279 CA LEU C 162 6286 8091 5628 -161 1548 -1472 C ATOM 1280 C LEU A 162 72.655 10.499 19.967 1.00 52.23 C ANISOU 1280 C LEU C 162 5897 8430 5516 386 1306 -1358 C ATOM 1281 O LEU A 162 73.802 10.181 20.308 1.00 62.49 O ANISOU 1281 O LEU C 162 8039 8700 7004 -362 1496 -2942 O ATOM 1282 CB LEU A 162 71.433 8.846 18.503 1.00 53.19 C ANISOU 1282 CB LEU C 162 6314 8196 5699 -499 1777 -1522 C ATOM 1283 CG LEU A 162 70.914 8.489 17.107 1.00 52.93 C ANISOU 1283 CG LEU C 162 6606 7838 5667 13 1777 -1363 C ATOM 1284 CD1 LEU A 162 70.038 7.257 17.187 1.00 55.07 C ANISOU 1284 CD1 LEU C 162 6561 7050 7311 156 2360 -995 C ATOM 1285 CD2 LEU A 162 70.204 9.707 16.541 1.00 57.05 C ANISOU 1285 CD2 LEU C 162 8865 8972 3838 -1552 778 -482 C ATOM 1286 N THR A 163 71.816 11.116 20.802 1.00 59.10 N ANISOU 1286 N THR C 163 6302 9840 6313 -767 1535 -340 N ATOM 1287 CA THR A 163 72.241 11.371 22.184 1.00 67.97 C ANISOU 1287 CA THR C 163 8737 10769 6321 -2093 2043 -691 C ATOM 1288 C THR A 163 71.942 10.166 23.078 1.00 72.03 C ANISOU 1288 C THR C 163 9650 11375 6344 -2327 1519 -773 C ATOM 1289 O THR A 163 70.982 9.439 22.824 1.00 63.46 O ANISOU 1289 O THR C 163 9754 9523 4834 -2098 377 -773 O ATOM 1290 CB THR A 163 71.573 12.606 22.814 1.00 67.87 C ANISOU 1290 CB THR C 163 8532 10536 6719 -1473 2303 -297 C ATOM 1291 OG1 THR A 163 70.209 12.297 23.157 1.00 77.41 O ANISOU 1291 OG1 THR C 163 9711 11701 8001 -1467 -319 417 O ATOM 1292 CG2 THR A 163 71.523 13.796 21.859 1.00 61.67 C ANISOU 1292 CG2 THR C 163 6295 9323 7815 -351 2422 -293 C ATOM 1293 N HIS A 164 72.744 9.954 24.109 1.00 73.18 N ANISOU 1293 N HIS C 164 8953 11950 6903 -2104 1660 -1261 N ATOM 1294 CA HIS A 164 72.536 8.891 25.083 1.00 79.94 C ANISOU 1294 CA HIS C 164 10826 12269 7277 -2713 673 -1193 C ATOM 1295 C HIS A 164 71.085 8.862 25.548 1.00 75.86 C ANISOU 1295 C HIS C 164 10789 12290 5744 -2880 480 -1278 C ATOM 1296 O HIS A 164 70.428 7.829 25.530 1.00 68.07 O ANISOU 1296 O HIS C 164 10732 12117 3012 -3617 -310 -48 O ATOM 1297 CB HIS A 164 73.441 9.097 26.288 1.00 86.94 C ANISOU 1297 CB HIS C 164 11525 12664 8842 -3047 658 -3009 C ATOM 1298 CG HIS A 164 73.977 7.858 26.930 1.00 98.83 C ANISOU 1298 CG HIS C 164 13596 13511 10445 -4228 -13 -3227 C ATOM 1299 ND1 HIS A 164 74.346 6.732 26.218 1.00104.21 N ANISOU 1299 ND1 HIS C 164 14138 14089 11368 -5006 -781 -2512 N ATOM 1300 CD2 HIS A 164 74.213 7.574 28.240 1.00102.90 C ANISOU 1300 CD2 HIS C 164 14181 14168 10747 -4985 -1232 -3005 C ATOM 1301 CE1 HIS A 164 74.788 5.805 27.060 1.00107.01 C ANISOU 1301 CE1 HIS C 164 14524 14378 11757 -5151 -1430 -2348 C ATOM 1302 NE2 HIS A 164 74.718 6.291 28.295 1.00106.55 N ANISOU 1302 NE2 HIS C 164 14544 14352 11590 -5250 -1668 -2462 N ATOM 1303 N ASP A 165 70.579 10.027 25.940 1.00 72.18 N ANISOU 1303 N ASP C 165 9561 12182 5684 -2138 1484 -1623 N ATOM 1304 CA ASP A 165 69.164 10.131 26.291 1.00 77.60 C ANISOU 1304 CA ASP C 165 11006 12333 6146 -1786 1999 -1092 C ATOM 1305 C ASP A 165 68.264 9.574 25.201 1.00 74.61 C ANISOU 1305 C ASP C 165 9901 12590 5858 -1162 1374 -630 C ATOM 1306 O ASP A 165 67.187 9.022 25.452 1.00 76.73 O ANISOU 1306 O ASP C 165 10896 11798 6461 -813 831 -553 O ATOM 1307 CB ASP A 165 68.835 11.601 26.559 1.00 85.81 C ANISOU 1307 CB ASP C 165 12889 12470 7243 -2487 3699 -1308 C ATOM 1308 CG ASP A 165 69.718 12.147 27.670 1.00 94.21 C ANISOU 1308 CG ASP C 165 14915 12585 8295 -2725 5300 -1274 C ATOM 1309 OD1 ASP A 165 70.888 11.710 27.749 1.00108.17 O ANISOU 1309 OD1 ASP C 165 16354 12710 12037 -2263 7768 -1380 O ATOM 1310 OD2 ASP A 165 69.237 12.992 28.455 1.00 97.35 O ANISOU 1310 OD2 ASP C 165 17132 13617 6241 -2539 4483 -704 O ATOM 1311 N THR A 166 68.689 9.708 23.941 1.00 74.67 N ANISOU 1311 N THR C 166 9546 12954 5873 -1010 1398 -554 N ATOM 1312 CA THR A 166 67.835 9.191 22.873 1.00 68.60 C ANISOU 1312 CA THR C 166 7758 12833 5476 -437 336 -156 C ATOM 1313 C THR A 166 68.046 7.697 22.653 1.00 68.94 C ANISOU 1313 C THR C 166 7970 12883 5341 -542 -156 716 C ATOM 1314 O THR A 166 67.068 6.988 22.416 1.00 68.20 O ANISOU 1314 O THR C 166 7559 12731 5624 -692 -530 1061 O ATOM 1315 CB THR A 166 68.043 9.895 21.516 1.00 72.37 C ANISOU 1315 CB THR C 166 9155 12702 5639 -1043 -61 -362 C ATOM 1316 OG1 THR A 166 67.909 11.316 21.665 1.00 75.94 O ANISOU 1316 OG1 THR C 166 8668 12928 7257 -920 327 -1882 O ATOM 1317 CG2 THR A 166 66.966 9.415 20.546 1.00 74.00 C ANISOU 1317 CG2 THR C 166 9650 13247 5218 -1212 624 39 C ATOM 1318 N ARG A 167 69.290 7.227 22.713 1.00 69.78 N ANISOU 1318 N ARG C 167 8682 12889 4941 -548 562 511 N ATOM 1319 CA ARG A 167 69.477 5.787 22.538 1.00 71.95 C ANISOU 1319 CA ARG C 167 8780 12745 5814 -629 917 -407 C ATOM 1320 C ARG A 167 68.765 5.094 23.705 1.00 74.23 C ANISOU 1320 C ARG C 167 8941 13769 5493 -1343 846 -439 C ATOM 1321 O ARG A 167 67.973 4.166 23.554 1.00 78.16 O ANISOU 1321 O ARG C 167 8228 14833 6636 -2496 226 -189 O ATOM 1322 CB ARG A 167 70.930 5.355 22.493 1.00 77.63 C ANISOU 1322 CB ARG C 167 9638 12639 7221 -665 1124 -961 C ATOM 1323 CG ARG A 167 71.970 6.339 22.027 1.00 81.73 C ANISOU 1323 CG ARG C 167 10758 12178 8116 -257 -90 -165 C ATOM 1324 CD ARG A 167 72.333 6.195 20.563 1.00 87.05 C ANISOU 1324 CD ARG C 167 12778 11970 8326 -590 -56 301 C ATOM 1325 NE ARG A 167 73.744 6.069 20.251 1.00 92.77 N ANISOU 1325 NE ARG C 167 14409 11696 9144 -662 -296 517 N ATOM 1326 CZ ARG A 167 74.587 6.864 19.622 1.00 95.37 C ANISOU 1326 CZ ARG C 167 15380 11275 9580 -374 -904 1145 C ATOM 1327 NH1 ARG A 167 74.251 8.044 19.121 1.00 94.39 N ANISOU 1327 NH1 ARG C 167 15117 11435 9312 -231 -1424 1589 N ATOM 1328 NH2 ARG A 167 75.863 6.505 19.464 1.00110.50 N ANISOU 1328 NH2 ARG C 167 19973 11216 10798 -1808 -3257 4175 N ATOM 1329 N VAL A 168 69.092 5.621 24.878 1.00 80.95 N ANISOU 1329 N VAL C 168 10812 14447 5497 -2185 1339 -777 N ATOM 1330 CA VAL A 168 68.484 5.194 26.118 1.00 84.04 C ANISOU 1330 CA VAL C 168 12024 14446 5461 -2415 1114 -475 C ATOM 1331 C VAL A 168 66.972 5.117 25.982 1.00 84.40 C ANISOU 1331 C VAL C 168 12875 13943 5251 -2397 603 -261 C ATOM 1332 O VAL A 168 66.404 4.046 26.164 1.00 89.82 O ANISOU 1332 O VAL C 168 12314 15343 6472 -1740 2248 -1764 O ATOM 1333 CB VAL A 168 68.820 6.162 27.269 1.00 88.21 C ANISOU 1333 CB VAL C 168 13524 14378 5615 -3379 1719 -807 C ATOM 1334 CG1 VAL A 168 67.715 6.123 28.315 1.00 86.04 C ANISOU 1334 CG1 VAL C 168 14085 12505 6102 -3940 1902 -833 C ATOM 1335 CG2 VAL A 168 70.177 5.806 27.856 1.00 86.16 C ANISOU 1335 CG2 VAL C 168 11934 14947 5855 -1949 1013 -643 C ATOM 1336 N ALA A 169 66.336 6.231 25.658 1.00 91.57 N ANISOU 1336 N ALA C 169 15364 13755 5673 -3339 -113 804 N ATOM 1337 CA ALA A 169 64.882 6.240 25.512 1.00 95.17 C ANISOU 1337 CA ALA C 169 16049 13584 6528 -3524 1372 390 C ATOM 1338 C ALA A 169 64.375 5.476 24.292 1.00102.07 C ANISOU 1338 C ALA C 169 17256 14134 7393 -4115 2423 545 C ATOM 1339 O ALA A 169 63.173 5.436 23.991 1.00106.85 O ANISOU 1339 O ALA C 169 19119 13265 8212 -5055 4172 -586 O ATOM 1340 CB ALA A 169 64.420 7.694 25.478 1.00103.83 C ANISOU 1340 CB ALA C 169 17666 14087 7697 -4586 2652 87 C ATOM 1341 N ASN A 170 65.271 4.832 23.534 1.00106.51 N ANISOU 1341 N ASN C 170 18134 14836 7500 -4499 2029 1062 N ATOM 1342 CA ASN A 170 64.775 4.060 22.387 1.00109.84 C ANISOU 1342 CA ASN C 170 18334 15718 7681 -5454 2226 978 C ATOM 1343 C ASN A 170 65.265 2.617 22.468 1.00112.59 C ANISOU 1343 C ASN C 170 18483 15901 8396 -5599 1805 941 C ATOM 1344 O ASN A 170 64.791 1.737 21.725 1.00116.92 O ANISOU 1344 O ASN C 170 21676 16275 6474 -7495 3171 1897 O ATOM 1345 CB ASN A 170 65.178 4.718 21.067 1.00107.00 C ANISOU 1345 CB ASN C 170 17223 15854 7580 -4994 2601 690 C ATOM 1346 CG ASN A 170 64.272 5.848 20.616 1.00104.44 C ANISOU 1346 CG ASN C 170 16237 15763 7682 -4573 2828 452 C ATOM 1347 OD1 ASN A 170 63.206 6.102 21.169 1.00109.05 O ANISOU 1347 OD1 ASN C 170 16961 15826 8648 -4927 1518 639 O ATOM 1348 ND2 ASN A 170 64.684 6.580 19.577 1.00 90.72 N ANISOU 1348 ND2 ASN C 170 11283 14971 8214 -2336 4491 -806 N ATOM 1349 N SER A 171 66.196 2.329 23.375 1.00110.23 N ANISOU 1349 N SER C 171 17178 15892 8812 -4576 354 679 N ATOM 1350 CA SER A 171 66.739 0.977 23.526 1.00111.31 C ANISOU 1350 CA SER C 171 17038 15580 9674 -4280 -170 887 C ATOM 1351 C SER A 171 65.658 -0.088 23.690 1.00111.01 C ANISOU 1351 C SER C 171 17047 15238 9894 -4199 -5 780 C ATOM 1352 O SER A 171 65.913 -1.252 23.354 1.00115.28 O ANISOU 1352 O SER C 171 17036 16296 10469 -5295 -2437 1977 O ATOM 1353 CB SER A 171 67.708 0.911 24.715 1.00111.07 C ANISOU 1353 CB SER C 171 16913 15240 10048 -3695 -673 693 C ATOM 1354 OG SER A 171 67.787 2.142 25.421 1.00113.97 O ANISOU 1354 OG SER C 171 18978 14524 9800 -4234 653 538 O ATOM 1355 N ARG A 172 64.489 0.288 24.190 1.00110.85 N ANISOU 1355 N ARG C 172 17451 14821 9847 -3968 200 169 N ATOM 1356 CA ARG A 172 63.306 -0.529 24.405 1.00111.98 C ANISOU 1356 CA ARG C 172 17665 14906 9976 -4058 -794 10 C ATOM 1357 C ARG A 172 62.848 -1.185 23.110 1.00111.03 C ANISOU 1357 C ARG C 172 16172 15559 10454 -3932 -939 -262 C ATOM 1358 O ARG A 172 62.494 -2.360 23.006 1.00112.06 O ANISOU 1358 O ARG C 172 16730 16836 9010 -5744 -1975 -11 O ATOM 1359 CB ARG A 172 62.166 0.298 25.003 1.00116.98 C ANISOU 1359 CB ARG C 172 19431 14785 10230 -3822 -1089 65 C ATOM 1360 CG ARG A 172 61.531 1.339 24.102 1.00128.53 C ANISOU 1360 CG ARG C 172 22686 15019 11132 -4938 -1604 -14 C ATOM 1361 CD ARG A 172 60.047 1.099 23.874 1.00133.23 C ANISOU 1361 CD ARG C 172 24043 14646 11932 -4849 -1006 -529 C ATOM 1362 NE ARG A 172 59.237 2.289 24.099 1.00140.27 N ANISOU 1362 NE ARG C 172 25830 14832 12636 -5439 -672 -487 N ATOM 1363 CZ ARG A 172 57.910 2.385 24.135 1.00142.46 C ANISOU 1363 CZ ARG C 172 26138 14766 13223 -5418 -605 -69 C ATOM 1364 NH1 ARG A 172 57.125 1.315 23.953 1.00146.19 N ANISOU 1364 NH1 ARG C 172 26094 15488 13962 -4749 -833 543 N ATOM 1365 NH2 ARG A 172 57.323 3.563 24.354 1.00148.11 N ANISOU 1365 NH2 ARG C 172 27294 15026 13955 -5942 -745 288 N ATOM 1366 N PHE A 173 62.858 -0.374 22.045 1.00 99.08 N ANISOU 1366 N PHE C 173 12166 15154 10327 -1652 -98 -625 N ATOM 1367 CA PHE A 173 62.554 -1.016 20.772 1.00 95.56 C ANISOU 1367 CA PHE C 173 11181 14684 10441 -1264 -294 -16 C ATOM 1368 C PHE A 173 63.698 -1.933 20.411 1.00 93.43 C ANISOU 1368 C PHE C 173 10204 14403 10892 -1050 -663 -317 C ATOM 1369 O PHE A 173 63.486 -3.024 19.877 1.00 90.44 O ANISOU 1369 O PHE C 173 8772 14217 11373 -1673 -2556 -482 O ATOM 1370 CB PHE A 173 62.308 0.047 19.707 1.00 90.93 C ANISOU 1370 CB PHE C 173 10884 13929 9734 -1337 138 461 C ATOM 1371 CG PHE A 173 61.305 1.069 20.235 1.00 92.38 C ANISOU 1371 CG PHE C 173 11175 14171 9755 -1241 -225 1018 C ATOM 1372 CD1 PHE A 173 59.949 0.897 20.036 1.00 91.14 C ANISOU 1372 CD1 PHE C 173 11094 14284 9251 -1076 -347 1420 C ATOM 1373 CD2 PHE A 173 61.756 2.177 20.923 1.00 91.66 C ANISOU 1373 CD2 PHE C 173 10907 13980 9941 -1040 -423 1644 C ATOM 1374 CE1 PHE A 173 59.047 1.826 20.518 1.00 91.11 C ANISOU 1374 CE1 PHE C 173 11004 14444 9172 -992 -551 1730 C ATOM 1375 CE2 PHE A 173 60.857 3.111 21.406 1.00 91.80 C ANISOU 1375 CE2 PHE C 173 10541 14096 10243 -794 -985 2187 C ATOM 1376 CZ PHE A 173 59.502 2.937 21.202 1.00 90.64 C ANISOU 1376 CZ PHE C 173 10223 14319 9898 -703 -1053 2344 C ATOM 1377 N PHE A 174 64.947 -1.562 20.698 1.00 98.63 N ANISOU 1377 N PHE C 174 10789 14856 11831 -833 -369 -1379 N ATOM 1378 CA PHE A 174 65.996 -2.533 20.311 1.00102.64 C ANISOU 1378 CA PHE C 174 12059 14291 12650 -629 -398 -2078 C ATOM 1379 C PHE A 174 66.129 -3.550 21.438 1.00108.34 C ANISOU 1379 C PHE C 174 12786 14844 13533 -651 -1222 -2243 C ATOM 1380 O PHE A 174 67.127 -3.604 22.143 1.00113.25 O ANISOU 1380 O PHE C 174 14713 14498 13819 212 -2451 -2631 O ATOM 1381 CB PHE A 174 67.288 -1.813 19.948 1.00100.89 C ANISOU 1381 CB PHE C 174 12146 13993 12196 -438 -292 -2674 C ATOM 1382 CG PHE A 174 67.299 -1.311 18.499 1.00101.23 C ANISOU 1382 CG PHE C 174 11869 14360 12232 -610 -257 -2760 C ATOM 1383 CD1 PHE A 174 66.498 -0.245 18.126 1.00101.15 C ANISOU 1383 CD1 PHE C 174 11722 14554 12156 -813 146 -2915 C ATOM 1384 CD2 PHE A 174 68.094 -1.921 17.541 1.00 99.50 C ANISOU 1384 CD2 PHE C 174 11610 14369 11828 -479 172 -2977 C ATOM 1385 CE1 PHE A 174 66.499 0.212 16.822 1.00100.80 C ANISOU 1385 CE1 PHE C 174 11514 14644 12141 -931 174 -2836 C ATOM 1386 CE2 PHE A 174 68.098 -1.481 16.232 1.00 98.42 C ANISOU 1386 CE2 PHE C 174 11506 14380 11508 -655 925 -3316 C ATOM 1387 CZ PHE A 174 67.282 -0.428 15.874 1.00100.40 C ANISOU 1387 CZ PHE C 174 11676 14579 11892 -1087 596 -3021 C ATOM 1388 N ASP A 175 65.077 -4.338 21.539 1.00112.09 N ANISOU 1388 N ASP C 175 12995 15173 14422 -436 -1786 -1485 N ATOM 1389 CA ASP A 175 64.400 -4.944 22.652 1.00115.08 C ANISOU 1389 CA ASP C 175 13761 15399 14564 -948 -2093 -893 C ATOM 1390 C ASP A 175 65.233 -4.640 23.915 1.00115.71 C ANISOU 1390 C ASP C 175 14276 15528 14161 -1845 -1488 -256 C ATOM 1391 O ASP A 175 66.067 -5.415 24.353 1.00101.68 O ANISOU 1391 O ASP C 175 8131 15542 14961 -499 -1721 -833 O ATOM 1392 CB ASP A 175 64.099 -6.441 22.556 1.00113.42 C ANISOU 1392 CB ASP C 175 13335 15222 14536 -254 -2220 -790 C ATOM 1393 CG ASP A 175 62.646 -6.761 22.919 1.00114.59 C ANISOU 1393 CG ASP C 175 14314 14779 14446 34 -1892 -751 C ATOM 1394 OD1 ASP A 175 61.870 -5.813 23.212 1.00117.13 O ANISOU 1394 OD1 ASP C 175 16380 14695 13429 52 333 -1017 O ATOM 1395 OD2 ASP A 175 62.254 -7.951 22.927 1.00114.39 O ANISOU 1395 OD2 ASP C 175 13894 14998 14569 1145 -918 -1667 O ATOM 1396 N ASN A 176 64.895 -3.445 24.383 1.00121.11 N ANISOU 1396 N ASN C 176 16259 15316 14442 -2523 -1645 359 N ATOM 1397 CA ASN A 176 65.299 -2.840 25.641 1.00119.04 C ANISOU 1397 CA ASN C 176 16189 14492 14550 -2736 -1505 839 C ATOM 1398 C ASN A 176 66.794 -2.989 25.886 1.00119.68 C ANISOU 1398 C ASN C 176 16495 14491 14488 -2749 -1624 469 C ATOM 1399 O ASN A 176 67.263 -3.141 27.011 1.00124.72 O ANISOU 1399 O ASN C 176 17735 14741 14911 -3286 -2318 -305 O ATOM 1400 CB ASN A 176 64.436 -3.476 26.744 1.00122.57 C ANISOU 1400 CB ASN C 176 17638 13976 14957 -3487 -2272 1753 C ATOM 1401 CG ASN A 176 63.043 -3.816 26.223 1.00119.83 C ANISOU 1401 CG ASN C 176 17236 13557 14738 -3318 -2834 2375 C ATOM 1402 OD1 ASN A 176 62.733 -4.974 25.937 1.00112.39 O ANISOU 1402 OD1 ASN C 176 17127 13114 12463 -3026 -3341 3384 O ATOM 1403 ND2 ASN A 176 62.190 -2.809 26.070 1.00118.58 N ANISOU 1403 ND2 ASN C 176 15982 13336 15738 -2785 -4764 2945 N ATOM 1404 N ASP A 177 67.531 -2.928 24.787 1.00121.16 N ANISOU 1404 N ASP C 177 16699 14395 14941 -2643 -2025 583 N ATOM 1405 CA ASP A 177 68.952 -3.224 24.703 1.00120.08 C ANISOU 1405 CA ASP C 177 16473 14274 14877 -2799 -2648 -20 C ATOM 1406 C ASP A 177 69.709 -2.052 24.090 1.00116.88 C ANISOU 1406 C ASP C 177 16061 14590 13758 -2498 -1936 -826 C ATOM 1407 O ASP A 177 69.847 -1.953 22.868 1.00116.90 O ANISOU 1407 O ASP C 177 15584 15979 12852 -4161 -1973 -6623 O ATOM 1408 CB ASP A 177 69.095 -4.519 23.907 1.00123.47 C ANISOU 1408 CB ASP C 177 16783 14388 15742 -4064 -3476 197 C ATOM 1409 CG ASP A 177 70.473 -4.799 23.336 1.00128.08 C ANISOU 1409 CG ASP C 177 17759 14285 16618 -4454 -4378 444 C ATOM 1410 OD1 ASP A 177 71.462 -4.302 23.923 1.00128.91 O ANISOU 1410 OD1 ASP C 177 17629 14208 17141 -3845 -5296 -103 O ATOM 1411 OD2 ASP A 177 70.563 -5.523 22.308 1.00134.42 O ANISOU 1411 OD2 ASP C 177 18686 14781 17606 -5619 -4369 1175 O ATOM 1412 N VAL A 178 70.194 -1.163 24.952 1.00118.66 N ANISOU 1412 N VAL C 178 16676 14823 13586 -3116 -1669 -593 N ATOM 1413 CA VAL A 178 70.951 0.025 24.606 1.00114.96 C ANISOU 1413 CA VAL C 178 16440 14173 13065 -2790 -1097 -961 C ATOM 1414 C VAL A 178 72.393 -0.300 24.211 1.00114.77 C ANISOU 1414 C VAL C 178 16742 13959 12908 -3083 -1201 -979 C ATOM 1415 O VAL A 178 73.331 0.109 24.901 1.00114.89 O ANISOU 1415 O VAL C 178 16482 13515 13656 -3279 -892 -779 O ATOM 1416 CB VAL A 178 70.991 1.020 25.788 1.00114.12 C ANISOU 1416 CB VAL C 178 16879 14133 12349 -2691 -1395 -955 C ATOM 1417 CG1 VAL A 178 70.574 2.417 25.360 1.00100.42 C ANISOU 1417 CG1 VAL C 178 16419 12787 8949 -1649 -3 -1912 C ATOM 1418 CG2 VAL A 178 70.101 0.509 26.927 1.00108.95 C ANISOU 1418 CG2 VAL C 178 14263 13668 13463 -2327 -635 -648 C ATOM 1419 N ASN A 179 72.566 -1.023 23.114 1.00116.58 N ANISOU 1419 N ASN C 179 17945 13795 12556 -3598 -1127 -1455 N ATOM 1420 CA ASN A 179 73.855 -1.403 22.556 1.00116.97 C ANISOU 1420 CA ASN C 179 19049 13285 12108 -3906 -966 -1844 C ATOM 1421 C ASN A 179 73.708 -1.709 21.061 1.00115.42 C ANISOU 1421 C ASN C 179 18661 12859 12334 -4366 -546 -1960 C ATOM 1422 O ASN A 179 74.683 -1.741 20.322 1.00111.17 O ANISOU 1422 O ASN C 179 18670 11973 11594 -4270 -82 -2598 O ATOM 1423 CB ASN A 179 74.444 -2.631 23.249 1.00126.19 C ANISOU 1423 CB ASN C 179 20612 14193 13140 -4450 -586 -3101 C ATOM 1424 CG ASN A 179 75.271 -2.318 24.480 1.00133.83 C ANISOU 1424 CG ASN C 179 21547 15588 13714 -4664 -1 -3782 C ATOM 1425 OD1 ASN A 179 76.188 -1.489 24.449 1.00141.47 O ANISOU 1425 OD1 ASN C 179 22131 16168 15453 -3717 104 -5270 O ATOM 1426 ND2 ASN A 179 74.960 -2.987 25.588 1.00140.96 N ANISOU 1426 ND2 ASN C 179 22307 17586 13667 -5567 -254 -4832 N ATOM 1427 N GLN A 180 72.456 -1.932 20.695 1.00113.09 N ANISOU 1427 N GLN C 180 18065 12522 12383 -4550 -539 -1364 N ATOM 1428 CA GLN A 180 72.039 -2.266 19.345 1.00111.28 C ANISOU 1428 CA GLN C 180 17368 12221 12694 -4603 -233 -1241 C ATOM 1429 C GLN A 180 71.397 -1.072 18.637 1.00107.47 C ANISOU 1429 C GLN C 180 16498 11752 12582 -4276 637 -1433 C ATOM 1430 O GLN A 180 71.497 -0.962 17.414 1.00110.04 O ANISOU 1430 O GLN C 180 17836 11203 12770 -6924 -34 -201 O ATOM 1431 CB GLN A 180 71.065 -3.451 19.373 1.00115.85 C ANISOU 1431 CB GLN C 180 17179 13290 13550 -5064 -396 -286 C ATOM 1432 CG GLN A 180 71.504 -4.601 18.473 1.00120.97 C ANISOU 1432 CG GLN C 180 17873 13992 14097 -4886 274 156 C ATOM 1433 CD GLN A 180 72.517 -4.155 17.424 1.00126.63 C ANISOU 1433 CD GLN C 180 19208 14437 14468 -4872 -191 735 C ATOM 1434 OE1 GLN A 180 72.143 -3.709 16.340 1.00134.88 O ANISOU 1434 OE1 GLN C 180 21173 16732 13344 -5194 390 1458 O ATOM 1435 NE2 GLN A 180 73.802 -4.261 17.750 1.00134.37 N ANISOU 1435 NE2 GLN C 180 20493 13494 17068 -4682 -570 1136 N ATOM 1436 N VAL A 181 70.762 -0.223 19.438 1.00 91.41 N ANISOU 1436 N VAL C 181 12209 11447 11077 -2514 -691 -1245 N ATOM 1437 CA VAL A 181 70.240 1.071 19.007 1.00 87.48 C ANISOU 1437 CA VAL C 181 12009 11197 10032 -2443 244 -1415 C ATOM 1438 C VAL A 181 71.256 1.743 18.087 1.00 80.41 C ANISOU 1438 C VAL C 181 10823 10634 9095 -1836 1155 -2706 C ATOM 1439 O VAL A 181 72.366 2.000 18.566 1.00 92.19 O ANISOU 1439 O VAL C 181 11677 11840 11511 -1460 997 -4631 O ATOM 1440 CB VAL A 181 69.944 1.997 20.203 1.00 90.28 C ANISOU 1440 CB VAL C 181 12256 11761 10287 -2070 945 -1371 C ATOM 1441 CG1 VAL A 181 69.055 3.165 19.779 1.00 79.58 C ANISOU 1441 CG1 VAL C 181 8542 12793 8903 -2166 3719 -2698 C ATOM 1442 CG2 VAL A 181 69.334 1.204 21.354 1.00 90.23 C ANISOU 1442 CG2 VAL C 181 13190 11625 9469 -2396 839 -1705 C ATOM 1443 N PRO A 182 70.919 2.007 16.838 1.00 78.75 N ANISOU 1443 N PRO C 182 10355 10446 9119 -2988 1354 -2686 N ATOM 1444 CA PRO A 182 71.909 2.497 15.859 1.00 76.52 C ANISOU 1444 CA PRO C 182 10676 9754 8644 -3288 1639 -2374 C ATOM 1445 C PRO A 182 72.618 3.728 16.396 1.00 71.68 C ANISOU 1445 C PRO C 182 10376 9002 7857 -3382 1082 -2873 C ATOM 1446 O PRO A 182 72.057 4.473 17.209 1.00 66.00 O ANISOU 1446 O PRO C 182 9654 8907 6513 -1321 1615 -2978 O ATOM 1447 CB PRO A 182 71.038 2.813 14.642 1.00 75.44 C ANISOU 1447 CB PRO C 182 10308 9585 8770 -2867 1719 -2322 C ATOM 1448 CG PRO A 182 69.863 1.898 14.774 1.00 76.20 C ANISOU 1448 CG PRO C 182 10118 9995 8838 -3110 1344 -2279 C ATOM 1449 CD PRO A 182 69.577 1.887 16.256 1.00 76.74 C ANISOU 1449 CD PRO C 182 10206 10234 8719 -3262 1277 -2719 C ATOM 1450 N LYS A 183 73.869 3.971 16.021 1.00 66.25 N ANISOU 1450 N LYS C 183 10340 8136 6695 -4050 1488 -2470 N ATOM 1451 CA LYS A 183 74.543 5.095 16.668 1.00 67.52 C ANISOU 1451 CA LYS C 183 10571 8502 6581 -3366 1692 -1915 C ATOM 1452 C LYS A 183 74.146 6.409 16.007 1.00 61.25 C ANISOU 1452 C LYS C 183 9080 8020 6172 -2590 2056 -1793 C ATOM 1453 O LYS A 183 74.211 7.467 16.630 1.00 62.32 O ANISOU 1453 O LYS C 183 8010 8614 7056 -1762 3204 -3628 O ATOM 1454 CB LYS A 183 76.058 4.927 16.621 1.00 75.36 C ANISOU 1454 CB LYS C 183 12471 8389 7774 -2993 2715 -2713 C ATOM 1455 CG LYS A 183 76.580 4.133 17.819 1.00 84.45 C ANISOU 1455 CG LYS C 183 14227 9329 8531 -2830 1521 -3164 C ATOM 1456 CD LYS A 183 75.465 3.333 18.472 1.00 95.52 C ANISOU 1456 CD LYS C 183 15282 11438 9573 -3046 265 -1703 C ATOM 1457 CE LYS A 183 75.523 3.352 19.991 1.00101.86 C ANISOU 1457 CE LYS C 183 16632 12453 9618 -3588 396 -1398 C ATOM 1458 NZ LYS A 183 74.211 2.963 20.593 1.00102.56 N ANISOU 1458 NZ LYS C 183 16349 13890 8727 -3036 990 -1168 N ATOM 1459 N TYR A 184 73.743 6.309 14.746 1.00 51.83 N ANISOU 1459 N TYR C 184 7385 6107 6202 -1451 1991 -1376 N ATOM 1460 CA TYR A 184 73.499 7.491 13.945 1.00 55.27 C ANISOU 1460 CA TYR C 184 8249 6086 6665 -1439 1539 -1697 C ATOM 1461 C TYR A 184 72.127 7.453 13.276 1.00 50.14 C ANISOU 1461 C TYR C 184 7486 5664 5900 -936 511 -893 C ATOM 1462 O TYR A 184 71.502 6.402 13.125 1.00 48.87 O ANISOU 1462 O TYR C 184 7286 5065 6217 -912 -386 -628 O ATOM 1463 CB TYR A 184 74.537 7.641 12.838 1.00 53.58 C ANISOU 1463 CB TYR C 184 6222 6312 7825 -223 1467 -2105 C ATOM 1464 CG TYR A 184 75.980 7.617 13.261 1.00 65.46 C ANISOU 1464 CG TYR C 184 7173 6790 10910 -60 1811 -3275 C ATOM 1465 CD1 TYR A 184 76.775 8.753 13.178 1.00 67.60 C ANISOU 1465 CD1 TYR C 184 6973 7049 11662 58 3033 -3556 C ATOM 1466 CD2 TYR A 184 76.561 6.443 13.732 1.00 73.31 C ANISOU 1466 CD2 TYR C 184 8066 7074 12715 -474 2087 -4017 C ATOM 1467 CE1 TYR A 184 78.104 8.727 13.563 1.00 72.07 C ANISOU 1467 CE1 TYR C 184 7801 7118 12467 126 3804 -3699 C ATOM 1468 CE2 TYR A 184 77.883 6.400 14.125 1.00 77.62 C ANISOU 1468 CE2 TYR C 184 8961 6918 13614 -526 2886 -4002 C ATOM 1469 CZ TYR A 184 78.645 7.545 14.035 1.00 77.23 C ANISOU 1469 CZ TYR C 184 8779 7214 13351 -254 4043 -4133 C ATOM 1470 OH TYR A 184 79.965 7.490 14.422 1.00 81.19 O ANISOU 1470 OH TYR C 184 9978 6232 14639 -89 4148 -3058 O ATOM 1471 N ALA A 185 71.687 8.644 12.865 1.00 44.28 N ANISOU 1471 N ALA C 185 6583 5134 5106 -446 559 -397 N ATOM 1472 CA ALA A 185 70.416 8.766 12.164 1.00 41.54 C ANISOU 1472 CA ALA C 185 6004 5031 4749 -416 508 -104 C ATOM 1473 C ALA A 185 70.514 9.851 11.101 1.00 39.24 C ANISOU 1473 C ALA C 185 5740 4871 4300 -717 912 133 C ATOM 1474 O ALA A 185 71.357 10.730 11.257 1.00 40.15 O ANISOU 1474 O ALA C 185 5793 5070 4394 -630 878 -475 O ATOM 1475 CB ALA A 185 69.281 9.101 13.115 1.00 40.34 C ANISOU 1475 CB ALA C 185 5188 5388 4751 -438 771 151 C ATOM 1476 N LEU A 186 69.654 9.735 10.106 1.00 37.19 N ANISOU 1476 N LEU C 186 5393 4789 3950 -862 1160 535 N ATOM 1477 CA LEU A 186 69.483 10.813 9.130 1.00 35.06 C ANISOU 1477 CA LEU C 186 4702 4519 4100 -214 1223 282 C ATOM 1478 C LEU A 186 68.278 11.643 9.579 1.00 33.86 C ANISOU 1478 C LEU C 186 4382 4655 3830 -287 401 524 C ATOM 1479 O LEU A 186 67.284 11.022 9.978 1.00 34.53 O ANISOU 1479 O LEU C 186 4199 5283 3639 -774 52 1064 O ATOM 1480 CB LEU A 186 69.264 10.291 7.720 1.00 36.12 C ANISOU 1480 CB LEU C 186 4452 5494 3779 94 711 865 C ATOM 1481 CG LEU A 186 70.499 10.188 6.830 1.00 39.23 C ANISOU 1481 CG LEU C 186 6353 4183 4371 259 794 461 C ATOM 1482 CD1 LEU A 186 71.721 9.911 7.673 1.00 42.75 C ANISOU 1482 CD1 LEU C 186 9437 3566 3240 -1441 -472 -47 C ATOM 1483 CD2 LEU A 186 70.307 9.142 5.729 1.00 40.18 C ANISOU 1483 CD2 LEU C 186 6145 4354 4767 -1365 226 1002 C ATOM 1484 N THR A 187 68.354 12.970 9.530 1.00 30.92 N ANISOU 1484 N THR C 187 4133 4155 3461 94 150 309 N ATOM 1485 CA THR A 187 67.195 13.763 9.950 1.00 32.43 C ANISOU 1485 CA THR C 187 4606 4346 3371 -190 -100 590 C ATOM 1486 C THR A 187 67.003 14.989 9.095 1.00 30.01 C ANISOU 1486 C THR C 187 4081 4157 3164 -36 197 666 C ATOM 1487 O THR A 187 67.978 15.637 8.683 1.00 30.48 O ANISOU 1487 O THR C 187 3846 4335 3400 -14 462 717 O ATOM 1488 CB THR A 187 67.378 14.191 11.421 1.00 33.44 C ANISOU 1488 CB THR C 187 4926 4319 3459 -409 73 284 C ATOM 1489 OG1 THR A 187 66.256 14.952 11.896 1.00 37.26 O ANISOU 1489 OG1 THR C 187 6156 4383 3620 301 1094 527 O ATOM 1490 CG2 THR A 187 68.616 15.086 11.585 1.00 33.76 C ANISOU 1490 CG2 THR C 187 5268 4475 3086 12 -123 -62 C ATOM 1491 N VAL A 188 65.769 15.379 8.801 1.00 28.57 N ANISOU 1491 N VAL C 188 3740 4203 2911 -94 603 608 N ATOM 1492 CA VAL A 188 65.620 16.687 8.164 1.00 29.31 C ANISOU 1492 CA VAL C 188 3735 4253 3147 34 387 510 C ATOM 1493 C VAL A 188 66.125 17.784 9.090 1.00 30.26 C ANISOU 1493 C VAL C 188 3591 4490 3416 -170 473 -521 C ATOM 1494 O VAL A 188 66.222 17.614 10.320 1.00 29.19 O ANISOU 1494 O VAL C 188 3485 4361 3245 -525 366 186 O ATOM 1495 CB VAL A 188 64.147 16.976 7.822 1.00 29.17 C ANISOU 1495 CB VAL C 188 4038 4367 2679 -104 1059 342 C ATOM 1496 CG1 VAL A 188 63.630 15.936 6.831 1.00 31.08 C ANISOU 1496 CG1 VAL C 188 3683 4932 3194 -158 1065 776 C ATOM 1497 CG2 VAL A 188 63.298 16.996 9.090 1.00 28.12 C ANISOU 1497 CG2 VAL C 188 3455 4019 3209 -169 1025 629 C ATOM 1498 N GLY A 189 66.448 18.933 8.499 1.00 28.38 N ANISOU 1498 N GLY C 189 3717 3841 3224 -117 155 384 N ATOM 1499 CA GLY A 189 66.927 20.045 9.300 1.00 28.02 C ANISOU 1499 CA GLY C 189 3469 4112 3066 46 -121 769 C ATOM 1500 C GLY A 189 65.841 20.974 9.801 1.00 27.71 C ANISOU 1500 C GLY C 189 3463 3891 3172 18 212 417 C ATOM 1501 O GLY A 189 64.668 20.823 9.425 1.00 27.45 O ANISOU 1501 O GLY C 189 3160 3989 3282 -145 31 50 O ATOM 1502 N VAL A 190 66.226 21.937 10.637 1.00 26.82 N ANISOU 1502 N VAL C 190 3465 3926 2798 112 107 420 N ATOM 1503 CA VAL A 190 65.221 22.878 11.142 1.00 26.93 C ANISOU 1503 CA VAL C 190 3389 4048 2796 131 90 577 C ATOM 1504 C VAL A 190 64.707 23.753 10.013 1.00 28.09 C ANISOU 1504 C VAL C 190 3785 3971 2918 -213 119 637 C ATOM 1505 O VAL A 190 63.527 24.091 9.936 1.00 30.94 O ANISOU 1505 O VAL C 190 4716 3911 3129 -189 60 682 O ATOM 1506 CB VAL A 190 65.778 23.747 12.284 1.00 26.99 C ANISOU 1506 CB VAL C 190 3112 3553 3590 -134 386 136 C ATOM 1507 CG1 VAL A 190 64.727 24.739 12.789 1.00 25.38 C ANISOU 1507 CG1 VAL C 190 2744 3342 3558 112 575 -44 C ATOM 1508 CG2 VAL A 190 66.281 22.889 13.444 1.00 27.32 C ANISOU 1508 CG2 VAL C 190 4403 2881 3095 133 365 484 C ATOM 1509 N GLY A 191 65.592 24.137 9.099 1.00 28.27 N ANISOU 1509 N GLY C 191 3208 4106 3427 -304 -227 355 N ATOM 1510 CA GLY A 191 65.257 24.909 7.904 1.00 28.37 C ANISOU 1510 CA GLY C 191 3342 3994 3444 -476 -138 303 C ATOM 1511 C GLY A 191 64.302 24.116 7.028 1.00 28.92 C ANISOU 1511 C GLY C 191 3516 4195 3278 -472 -45 463 C ATOM 1512 O GLY A 191 63.341 24.641 6.459 1.00 30.95 O ANISOU 1512 O GLY C 191 3779 4123 3859 -480 519 391 O ATOM 1513 N THR A 192 64.565 22.813 6.917 1.00 29.18 N ANISOU 1513 N THR C 192 3439 4502 3147 -591 -134 402 N ATOM 1514 CA THR A 192 63.669 21.938 6.161 1.00 29.81 C ANISOU 1514 CA THR C 192 3857 4395 3073 -556 226 626 C ATOM 1515 C THR A 192 62.248 22.035 6.706 1.00 29.87 C ANISOU 1515 C THR C 192 4123 4135 3090 -435 71 136 C ATOM 1516 O THR A 192 61.255 22.166 5.992 1.00 30.88 O ANISOU 1516 O THR C 192 3359 4959 3417 -200 564 -87 O ATOM 1517 CB THR A 192 64.127 20.473 6.261 1.00 30.46 C ANISOU 1517 CB THR C 192 3949 4135 3491 -437 1053 19 C ATOM 1518 OG1 THR A 192 65.556 20.420 6.176 1.00 30.94 O ANISOU 1518 OG1 THR C 192 4233 4289 3235 -315 469 522 O ATOM 1519 CG2 THR A 192 63.568 19.647 5.106 1.00 28.56 C ANISOU 1519 CG2 THR C 192 3804 4881 2167 -406 239 587 C ATOM 1520 N LEU A 193 62.146 21.962 8.041 1.00 29.30 N ANISOU 1520 N LEU C 193 3907 4130 3097 -445 -282 243 N ATOM 1521 CA LEU A 193 60.824 22.055 8.666 1.00 28.61 C ANISOU 1521 CA LEU C 193 3432 4212 3224 9 467 216 C ATOM 1522 C LEU A 193 60.246 23.445 8.467 1.00 28.75 C ANISOU 1522 C LEU C 193 3528 4125 3272 31 128 531 C ATOM 1523 O LEU A 193 59.071 23.562 8.094 1.00 29.30 O ANISOU 1523 O LEU C 193 4126 4214 2793 -10 282 293 O ATOM 1524 CB LEU A 193 60.972 21.743 10.133 1.00 31.34 C ANISOU 1524 CB LEU C 193 4114 4565 3228 132 -171 407 C ATOM 1525 CG LEU A 193 59.874 21.381 11.109 1.00 35.04 C ANISOU 1525 CG LEU C 193 5419 4216 3677 812 52 819 C ATOM 1526 CD1 LEU A 193 59.631 22.524 12.104 1.00 39.91 C ANISOU 1526 CD1 LEU C 193 4504 3781 6878 259 -509 2372 C ATOM 1527 CD2 LEU A 193 58.564 20.978 10.453 1.00 40.58 C ANISOU 1527 CD2 LEU C 193 7843 3165 4409 1560 41 377 C ATOM 1528 N LEU A 194 61.049 24.486 8.726 1.00 28.35 N ANISOU 1528 N LEU C 194 3406 4654 2710 -78 -153 487 N ATOM 1529 CA LEU A 194 60.489 25.837 8.657 1.00 29.18 C ANISOU 1529 CA LEU C 194 3512 4386 3188 42 788 217 C ATOM 1530 C LEU A 194 60.076 26.234 7.255 1.00 27.64 C ANISOU 1530 C LEU C 194 3308 3882 3311 13 459 277 C ATOM 1531 O LEU A 194 59.236 27.119 7.044 1.00 32.48 O ANISOU 1531 O LEU C 194 4441 4208 3691 -751 230 449 O ATOM 1532 CB LEU A 194 61.505 26.859 9.203 1.00 30.39 C ANISOU 1532 CB LEU C 194 3416 4337 3793 268 610 -13 C ATOM 1533 CG LEU A 194 61.663 26.807 10.732 1.00 32.67 C ANISOU 1533 CG LEU C 194 4476 4134 3803 244 1480 184 C ATOM 1534 CD1 LEU A 194 62.759 27.748 11.219 1.00 33.19 C ANISOU 1534 CD1 LEU C 194 3856 4679 4076 -249 1257 200 C ATOM 1535 CD2 LEU A 194 60.329 27.111 11.403 1.00 37.87 C ANISOU 1535 CD2 LEU C 194 5689 4563 4135 478 209 271 C ATOM 1536 N ASP A 195 60.653 25.614 6.238 1.00 30.12 N ANISOU 1536 N ASP C 195 4211 4072 3163 -662 590 131 N ATOM 1537 CA ASP A 195 60.236 25.921 4.882 1.00 29.64 C ANISOU 1537 CA ASP C 195 4302 3758 3203 98 -79 213 C ATOM 1538 C ASP A 195 58.834 25.398 4.589 1.00 29.57 C ANISOU 1538 C ASP C 195 4117 3778 3340 -45 -78 100 C ATOM 1539 O ASP A 195 58.261 25.763 3.549 1.00 32.41 O ANISOU 1539 O ASP C 195 4205 4517 3592 -211 318 -376 O ATOM 1540 CB ASP A 195 61.183 25.261 3.870 1.00 32.84 C ANISOU 1540 CB ASP C 195 4666 4408 3404 87 -719 714 C ATOM 1541 CG ASP A 195 62.487 25.994 3.713 1.00 36.78 C ANISOU 1541 CG ASP C 195 5311 4142 4521 658 -307 529 C ATOM 1542 OD1 ASP A 195 62.561 27.120 4.246 1.00 41.73 O ANISOU 1542 OD1 ASP C 195 4379 5412 6064 -338 -1138 -93 O ATOM 1543 OD2 ASP A 195 63.393 25.438 3.066 1.00 46.56 O ANISOU 1543 OD2 ASP C 195 7158 4576 5955 488 -1854 1342 O ATOM 1544 N ALA A 196 58.259 24.546 5.432 1.00 29.67 N ANISOU 1544 N ALA C 196 3714 4500 3058 -289 263 755 N ATOM 1545 CA ALA A 196 56.891 24.089 5.120 1.00 27.17 C ANISOU 1545 CA ALA C 196 3566 4341 2418 -493 286 664 C ATOM 1546 C ALA A 196 55.895 25.237 5.217 1.00 28.00 C ANISOU 1546 C ALA C 196 3307 4465 2866 -680 569 151 C ATOM 1547 O ALA A 196 56.111 26.221 5.925 1.00 28.87 O ANISOU 1547 O ALA C 196 3380 4911 2678 -817 407 523 O ATOM 1548 CB ALA A 196 56.478 22.984 6.057 1.00 26.85 C ANISOU 1548 CB ALA C 196 3786 3619 2796 -451 4 594 C ATOM 1549 N GLU A 197 54.790 25.146 4.506 1.00 27.17 N ANISOU 1549 N GLU C 197 3167 4506 2651 43 -131 398 N ATOM 1550 CA GLU A 197 53.760 26.163 4.475 1.00 30.24 C ANISOU 1550 CA GLU C 197 3681 4448 3362 63 432 377 C ATOM 1551 C GLU A 197 53.059 26.263 5.821 1.00 30.02 C ANISOU 1551 C GLU C 197 3932 4152 3320 -495 120 257 C ATOM 1552 O GLU A 197 52.690 27.351 6.269 1.00 29.71 O ANISOU 1552 O GLU C 197 3706 5116 2466 -914 330 -139 O ATOM 1553 CB GLU A 197 52.727 25.792 3.410 1.00 40.52 C ANISOU 1553 CB GLU C 197 6248 5074 4074 -980 1874 -674 C ATOM 1554 CG GLU A 197 51.847 26.933 2.949 1.00 60.69 C ANISOU 1554 CG GLU C 197 10960 5871 6230 -2159 2147 -1972 C ATOM 1555 CD GLU A 197 51.045 26.593 1.705 1.00 66.66 C ANISOU 1555 CD GLU C 197 12361 6294 6674 -1720 2370 -2598 C ATOM 1556 OE1 GLU A 197 51.678 26.269 0.668 1.00 68.95 O ANISOU 1556 OE1 GLU C 197 12681 6424 7091 -1696 3962 -2134 O ATOM 1557 OE2 GLU A 197 49.794 26.656 1.783 1.00 72.08 O ANISOU 1557 OE2 GLU C 197 12903 7065 7420 -834 2072 -2632 O ATOM 1558 N GLU A 198 52.847 25.126 6.462 1.00 29.40 N ANISOU 1558 N GLU C 198 4080 4111 2979 -884 400 26 N ATOM 1559 CA GLU A 198 52.198 25.049 7.773 1.00 29.14 C ANISOU 1559 CA GLU C 198 3686 4407 2976 -596 412 4 C ATOM 1560 C GLU A 198 52.896 23.969 8.587 1.00 30.64 C ANISOU 1560 C GLU C 198 3990 4706 2945 -952 421 17 C ATOM 1561 O GLU A 198 53.276 22.928 8.024 1.00 26.56 O ANISOU 1561 O GLU C 198 3260 4014 2819 -140 508 -1 O ATOM 1562 CB GLU A 198 50.710 24.759 7.610 1.00 29.18 C ANISOU 1562 CB GLU C 198 3211 4607 3268 -706 933 303 C ATOM 1563 CG GLU A 198 49.925 24.639 8.918 1.00 32.96 C ANISOU 1563 CG GLU C 198 3877 4954 3691 -308 357 332 C ATOM 1564 CD GLU A 198 48.438 24.517 8.634 1.00 36.62 C ANISOU 1564 CD GLU C 198 5000 4709 4204 -89 1011 746 C ATOM 1565 OE1 GLU A 198 48.075 23.818 7.664 1.00 36.61 O ANISOU 1565 OE1 GLU C 198 5321 4283 4307 -280 1223 248 O ATOM 1566 OE2 GLU A 198 47.601 25.109 9.352 1.00 43.85 O ANISOU 1566 OE2 GLU C 198 7564 4664 4432 -101 1557 743 O ATOM 1567 N VAL A 199 53.091 24.218 9.876 1.00 28.01 N ANISOU 1567 N VAL C 199 3735 3995 2911 -590 355 193 N ATOM 1568 CA VAL A 199 53.763 23.279 10.764 1.00 28.79 C ANISOU 1568 CA VAL C 199 4099 3913 2926 -422 35 243 C ATOM 1569 C VAL A 199 52.806 22.946 11.900 1.00 26.71 C ANISOU 1569 C VAL C 199 3439 3620 3092 -347 251 296 C ATOM 1570 O VAL A 199 52.318 23.884 12.558 1.00 28.14 O ANISOU 1570 O VAL C 199 3635 4215 2844 -635 380 363 O ATOM 1571 CB VAL A 199 55.061 23.862 11.342 1.00 26.90 C ANISOU 1571 CB VAL C 199 3876 3732 2611 -293 -478 289 C ATOM 1572 CG1 VAL A 199 55.695 22.918 12.349 1.00 26.66 C ANISOU 1572 CG1 VAL C 199 4317 4077 1737 -515 -252 492 C ATOM 1573 CG2 VAL A 199 56.046 24.140 10.224 1.00 26.84 C ANISOU 1573 CG2 VAL C 199 3784 4224 2189 -724 -423 415 C ATOM 1574 N MET A 200 52.545 21.667 12.113 1.00 25.82 N ANISOU 1574 N MET C 200 3405 3339 3067 -293 498 -199 N ATOM 1575 CA MET A 200 51.642 21.258 13.193 1.00 26.13 C ANISOU 1575 CA MET C 200 3086 3834 3009 -311 524 -191 C ATOM 1576 C MET A 200 52.392 20.325 14.133 1.00 26.51 C ANISOU 1576 C MET C 200 3359 3860 2853 -621 688 -45 C ATOM 1577 O MET A 200 52.815 19.231 13.731 1.00 26.60 O ANISOU 1577 O MET C 200 3277 3787 3044 -483 920 -67 O ATOM 1578 CB MET A 200 50.381 20.593 12.620 1.00 25.55 C ANISOU 1578 CB MET C 200 3154 3628 2926 -420 893 307 C ATOM 1579 CG MET A 200 49.436 20.006 13.667 1.00 27.01 C ANISOU 1579 CG MET C 200 3214 3595 3455 -318 604 244 C ATOM 1580 SD MET A 200 47.878 19.437 12.964 1.00 28.73 S ANISOU 1580 SD MET C 200 3551 3918 3448 -104 689 149 S ATOM 1581 CE MET A 200 48.409 18.000 12.016 1.00 26.69 C ANISOU 1581 CE MET C 200 2874 4794 2472 -335 27 342 C ATOM 1582 N ILE A 201 52.581 20.755 15.388 1.00 23.46 N ANISOU 1582 N ILE C 201 2655 3502 2756 -211 435 140 N ATOM 1583 CA ILE A 201 53.347 19.984 16.349 1.00 24.79 C ANISOU 1583 CA ILE C 201 3173 3587 2659 -135 141 166 C ATOM 1584 C ILE A 201 52.397 19.340 17.351 1.00 26.52 C ANISOU 1584 C ILE C 201 3302 3637 3138 -120 -129 255 C ATOM 1585 O ILE A 201 51.557 20.033 17.931 1.00 27.81 O ANISOU 1585 O ILE C 201 4090 3835 2643 -342 -290 292 O ATOM 1586 CB ILE A 201 54.357 20.866 17.097 1.00 27.24 C ANISOU 1586 CB ILE C 201 3374 3618 3356 163 152 -363 C ATOM 1587 CG1 ILE A 201 55.254 21.643 16.123 1.00 27.24 C ANISOU 1587 CG1 ILE C 201 3081 3946 3322 -139 251 -186 C ATOM 1588 CG2 ILE A 201 55.162 20.035 18.088 1.00 25.31 C ANISOU 1588 CG2 ILE C 201 3326 3157 3136 -130 215 74 C ATOM 1589 CD1 ILE A 201 56.170 20.699 15.350 1.00 28.28 C ANISOU 1589 CD1 ILE C 201 3584 4313 2850 -494 -85 -87 C ATOM 1590 N LEU A 202 52.550 18.041 17.509 1.00 26.31 N ANISOU 1590 N LEU C 202 3092 3731 3174 -22 64 -128 N ATOM 1591 CA LEU A 202 51.791 17.257 18.459 1.00 26.30 C ANISOU 1591 CA LEU C 202 3483 3728 2784 -398 -43 153 C ATOM 1592 C LEU A 202 52.523 17.294 19.804 1.00 27.46 C ANISOU 1592 C LEU C 202 3413 4048 2970 -16 191 179 C ATOM 1593 O LEU A 202 53.707 16.945 19.863 1.00 28.40 O ANISOU 1593 O LEU C 202 3715 3947 3129 -232 511 123 O ATOM 1594 CB LEU A 202 51.671 15.809 18.019 1.00 27.98 C ANISOU 1594 CB LEU C 202 3026 4205 3402 -8 200 67 C ATOM 1595 CG LEU A 202 50.561 15.329 17.089 1.00 32.57 C ANISOU 1595 CG LEU C 202 4884 4340 3151 -665 1223 -340 C ATOM 1596 CD1 LEU A 202 49.923 16.448 16.302 1.00 29.03 C ANISOU 1596 CD1 LEU C 202 4459 5402 1168 -774 316 322 C ATOM 1597 CD2 LEU A 202 51.085 14.237 16.174 1.00 28.96 C ANISOU 1597 CD2 LEU C 202 4928 4324 1753 -81 81 254 C ATOM 1598 N VAL A 203 51.805 17.686 20.845 1.00 27.08 N ANISOU 1598 N VAL C 203 3379 4070 2841 -319 158 136 N ATOM 1599 CA VAL A 203 52.445 17.775 22.156 1.00 28.32 C ANISOU 1599 CA VAL C 203 3361 4483 2917 -368 193 -54 C ATOM 1600 C VAL A 203 51.691 16.950 23.208 1.00 28.11 C ANISOU 1600 C VAL C 203 3351 4416 2913 -207 204 -341 C ATOM 1601 O VAL A 203 50.587 17.355 23.600 1.00 31.28 O ANISOU 1601 O VAL C 203 4296 4820 2771 -986 -232 601 O ATOM 1602 CB VAL A 203 52.541 19.247 22.598 1.00 31.03 C ANISOU 1602 CB VAL C 203 3660 5547 2583 -1005 156 -265 C ATOM 1603 CG1 VAL A 203 53.392 19.338 23.887 1.00 27.47 C ANISOU 1603 CG1 VAL C 203 3351 4595 2491 -504 -35 175 C ATOM 1604 CG2 VAL A 203 53.095 20.169 21.515 1.00 29.06 C ANISOU 1604 CG2 VAL C 203 3679 5007 2355 -1074 283 118 C ATOM 1605 N LEU A 204 52.274 15.827 23.641 1.00 30.58 N ANISOU 1605 N LEU C 204 3955 4885 2778 -1079 110 214 N ATOM 1606 CA LEU A 204 51.659 14.876 24.546 1.00 30.91 C ANISOU 1606 CA LEU C 204 3857 4859 3028 -978 77 43 C ATOM 1607 C LEU A 204 52.504 14.609 25.781 1.00 29.57 C ANISOU 1607 C LEU C 204 3398 4788 3048 -201 -283 88 C ATOM 1608 O LEU A 204 53.688 14.296 25.675 1.00 31.99 O ANISOU 1608 O LEU C 204 4527 4559 3069 -551 -246 384 O ATOM 1609 CB LEU A 204 51.435 13.530 23.838 1.00 31.23 C ANISOU 1609 CB LEU C 204 3744 4804 3316 -564 188 378 C ATOM 1610 CG LEU A 204 50.496 13.535 22.632 1.00 34.71 C ANISOU 1610 CG LEU C 204 4546 4360 4282 -557 1005 214 C ATOM 1611 CD1 LEU A 204 50.397 12.136 22.045 1.00 33.44 C ANISOU 1611 CD1 LEU C 204 3953 5118 3633 -175 495 933 C ATOM 1612 CD2 LEU A 204 49.115 14.081 23.005 1.00 31.49 C ANISOU 1612 CD2 LEU C 204 4245 4809 2909 -221 105 641 C ATOM 1613 N GLY A 205 51.916 14.697 26.982 1.00 29.39 N ANISOU 1613 N GLY C 205 3684 4477 3005 108 341 145 N ATOM 1614 CA GLY A 205 52.645 14.251 28.163 1.00 29.33 C ANISOU 1614 CA GLY C 205 3309 4893 2943 -186 184 46 C ATOM 1615 C GLY A 205 53.224 15.422 28.931 1.00 29.69 C ANISOU 1615 C GLY C 205 3654 4708 2919 -229 429 95 C ATOM 1616 O GLY A 205 53.645 16.416 28.359 1.00 28.46 O ANISOU 1616 O GLY C 205 3423 4190 3199 -544 655 -51 O ATOM 1617 N SER A 206 53.216 15.277 30.258 1.00 31.83 N ANISOU 1617 N SER C 206 4673 4502 2919 -549 548 -276 N ATOM 1618 CA SER A 206 53.785 16.326 31.102 1.00 29.80 C ANISOU 1618 CA SER C 206 4041 4962 2320 -526 -102 -270 C ATOM 1619 C SER A 206 55.281 16.450 30.872 1.00 31.69 C ANISOU 1619 C SER C 206 4450 4768 2821 -451 78 -368 C ATOM 1620 O SER A 206 55.855 17.492 31.195 1.00 28.29 O ANISOU 1620 O SER C 206 4255 4279 2215 -476 -394 268 O ATOM 1621 CB SER A 206 53.476 16.059 32.585 1.00 33.90 C ANISOU 1621 CB SER C 206 4494 6018 2369 -833 -305 -238 C ATOM 1622 OG SER A 206 54.172 14.877 32.971 1.00 38.87 O ANISOU 1622 OG SER C 206 5664 6409 2695 -1460 -1342 262 O ATOM 1623 N GLN A 207 55.947 15.441 30.310 1.00 30.40 N ANISOU 1623 N GLN C 207 3695 4607 3248 -457 63 -618 N ATOM 1624 CA GLN A 207 57.364 15.643 30.016 1.00 32.40 C ANISOU 1624 CA GLN C 207 4520 4248 3542 -300 14 -920 C ATOM 1625 C GLN A 207 57.595 16.707 28.941 1.00 29.27 C ANISOU 1625 C GLN C 207 4194 3487 3441 -283 30 -247 C ATOM 1626 O GLN A 207 58.739 17.175 28.802 1.00 29.03 O ANISOU 1626 O GLN C 207 4537 3459 3036 -42 551 326 O ATOM 1627 CB GLN A 207 58.022 14.315 29.620 1.00 36.95 C ANISOU 1627 CB GLN C 207 4455 5029 4553 -804 -1270 278 C ATOM 1628 CG GLN A 207 57.767 13.883 28.189 1.00 47.12 C ANISOU 1628 CG GLN C 207 5195 7212 5495 -2280 256 49 C ATOM 1629 CD GLN A 207 56.599 12.920 28.062 1.00 58.32 C ANISOU 1629 CD GLN C 207 5271 8711 8178 -2199 1161 -85 C ATOM 1630 OE1 GLN A 207 55.606 13.013 28.810 1.00 66.79 O ANISOU 1630 OE1 GLN C 207 6080 5957 13342 -1004 1966 -111 O ATOM 1631 NE2 GLN A 207 56.729 11.992 27.106 1.00 76.22 N ANISOU 1631 NE2 GLN C 207 4748 13694 10520 -4923 636 1575 N ATOM 1632 N LYS A 208 56.586 17.116 28.178 1.00 25.90 N ANISOU 1632 N LYS C 208 4036 3076 2728 -346 -118 256 N ATOM 1633 CA LYS A 208 56.710 18.149 27.161 1.00 26.11 C ANISOU 1633 CA LYS C 208 3765 3732 2423 -458 139 294 C ATOM 1634 C LYS A 208 56.277 19.523 27.648 1.00 26.21 C ANISOU 1634 C LYS C 208 3512 3888 2558 -387 -252 646 C ATOM 1635 O LYS A 208 56.216 20.515 26.922 1.00 26.03 O ANISOU 1635 O LYS C 208 3872 3305 2713 -291 -176 195 O ATOM 1636 CB LYS A 208 55.810 17.787 25.972 1.00 26.25 C ANISOU 1636 CB LYS C 208 3674 3411 2887 -397 148 -17 C ATOM 1637 CG LYS A 208 56.043 16.351 25.499 1.00 30.23 C ANISOU 1637 CG LYS C 208 4395 3646 3444 -621 1015 -299 C ATOM 1638 CD LYS A 208 57.469 16.154 25.007 1.00 31.45 C ANISOU 1638 CD LYS C 208 4882 3749 3319 -1187 -14 134 C ATOM 1639 CE LYS A 208 57.539 14.830 24.249 1.00 33.73 C ANISOU 1639 CE LYS C 208 4506 4101 4209 -1327 -214 329 C ATOM 1640 NZ LYS A 208 58.925 14.513 23.840 1.00 36.37 N ANISOU 1640 NZ LYS C 208 5786 3210 4825 -1811 65 -212 N ATOM 1641 N ALA A 209 55.922 19.612 28.914 1.00 27.52 N ANISOU 1641 N ALA C 209 3856 3895 2704 -341 -333 905 N ATOM 1642 CA ALA A 209 55.327 20.844 29.425 1.00 25.88 C ANISOU 1642 CA ALA C 209 3565 3497 2773 -123 -826 957 C ATOM 1643 C ALA A 209 56.281 22.023 29.334 1.00 25.14 C ANISOU 1643 C ALA C 209 3546 3492 2513 -82 -760 754 C ATOM 1644 O ALA A 209 55.852 23.138 28.991 1.00 26.85 O ANISOU 1644 O ALA C 209 3455 3812 2936 -140 -241 8 O ATOM 1645 CB ALA A 209 54.826 20.624 30.860 1.00 23.02 C ANISOU 1645 CB ALA C 209 2921 3511 2316 25 -299 546 C ATOM 1646 N LEU A 210 57.557 21.821 29.629 1.00 25.44 N ANISOU 1646 N LEU C 210 3524 3670 2471 -183 -458 358 N ATOM 1647 CA LEU A 210 58.486 22.969 29.529 1.00 25.96 C ANISOU 1647 CA LEU C 210 3513 3934 2415 -72 -197 183 C ATOM 1648 C LEU A 210 58.671 23.390 28.079 1.00 25.20 C ANISOU 1648 C LEU C 210 3328 3734 2514 20 -310 632 C ATOM 1649 O LEU A 210 58.814 24.575 27.764 1.00 31.16 O ANISOU 1649 O LEU C 210 4203 4560 3078 -900 -917 898 O ATOM 1650 CB LEU A 210 59.853 22.659 30.145 1.00 27.50 C ANISOU 1650 CB LEU C 210 3969 3660 2821 -64 138 434 C ATOM 1651 CG LEU A 210 59.906 22.689 31.671 1.00 30.14 C ANISOU 1651 CG LEU C 210 4555 3985 2914 -429 747 -23 C ATOM 1652 CD1 LEU A 210 61.201 22.071 32.182 1.00 40.51 C ANISOU 1652 CD1 LEU C 210 6486 4436 4470 -530 822 -963 C ATOM 1653 CD2 LEU A 210 59.760 24.107 32.196 1.00 33.37 C ANISOU 1653 CD2 LEU C 210 4280 4458 3940 -58 1358 352 C ATOM 1654 N ALA A 211 58.671 22.393 27.183 1.00 27.48 N ANISOU 1654 N ALA C 211 4486 3291 2663 -308 115 631 N ATOM 1655 CA ALA A 211 58.776 22.725 25.774 1.00 28.29 C ANISOU 1655 CA ALA C 211 3993 4123 2631 -618 294 169 C ATOM 1656 C ALA A 211 57.550 23.497 25.304 1.00 28.10 C ANISOU 1656 C ALA C 211 4031 3919 2728 -565 200 406 C ATOM 1657 O ALA A 211 57.698 24.436 24.509 1.00 28.25 O ANISOU 1657 O ALA C 211 3966 3542 3227 -506 8 452 O ATOM 1658 CB ALA A 211 58.968 21.443 24.985 1.00 25.95 C ANISOU 1658 CB ALA C 211 3715 3845 2298 -492 -138 300 C ATOM 1659 N LEU A 212 56.354 23.126 25.763 1.00 29.74 N ANISOU 1659 N LEU C 212 4595 4129 2575 -549 -229 649 N ATOM 1660 CA LEU A 212 55.122 23.790 25.359 1.00 25.23 C ANISOU 1660 CA LEU C 212 3555 4092 1940 -464 -338 834 C ATOM 1661 C LEU A 212 55.164 25.246 25.822 1.00 26.45 C ANISOU 1661 C LEU C 212 3253 4091 2706 -119 118 416 C ATOM 1662 O LEU A 212 54.752 26.155 25.106 1.00 26.73 O ANISOU 1662 O LEU C 212 3539 3928 2690 -461 108 723 O ATOM 1663 CB LEU A 212 53.883 23.179 25.979 1.00 26.14 C ANISOU 1663 CB LEU C 212 3254 5074 1604 -148 130 1069 C ATOM 1664 CG LEU A 212 52.625 22.984 25.164 1.00 31.40 C ANISOU 1664 CG LEU C 212 4836 4104 2990 228 -696 230 C ATOM 1665 CD1 LEU A 212 51.383 23.168 26.030 1.00 31.16 C ANISOU 1665 CD1 LEU C 212 5718 3975 2147 -356 505 747 C ATOM 1666 CD2 LEU A 212 52.526 23.877 23.931 1.00 29.99 C ANISOU 1666 CD2 LEU C 212 3747 2975 4675 428 -1429 -231 C ATOM 1667 N GLN A 213 55.653 25.374 27.050 1.00 28.60 N ANISOU 1667 N GLN C 213 3647 4297 2922 23 421 291 N ATOM 1668 CA GLN A 213 55.768 26.729 27.612 1.00 28.27 C ANISOU 1668 CA GLN C 213 3770 4308 2664 43 296 648 C ATOM 1669 C GLN A 213 56.749 27.576 26.796 1.00 27.90 C ANISOU 1669 C GLN C 213 3697 3508 3397 162 48 28 C ATOM 1670 O GLN A 213 56.470 28.755 26.539 1.00 26.94 O ANISOU 1670 O GLN C 213 3530 3710 2995 -146 559 542 O ATOM 1671 CB GLN A 213 56.169 26.673 29.098 1.00 29.86 C ANISOU 1671 CB GLN C 213 4273 4258 2815 304 573 427 C ATOM 1672 CG GLN A 213 55.846 27.980 29.826 1.00 39.30 C ANISOU 1672 CG GLN C 213 6207 5403 3322 -880 1789 -170 C ATOM 1673 CD GLN A 213 57.002 28.959 29.763 1.00 45.82 C ANISOU 1673 CD GLN C 213 5764 6136 5508 -1206 2816 22 C ATOM 1674 OE1 GLN A 213 58.106 28.530 29.416 1.00 53.98 O ANISOU 1674 OE1 GLN C 213 5710 6244 8557 -370 2661 187 O ATOM 1675 NE2 GLN A 213 56.804 30.237 30.040 1.00 57.17 N ANISOU 1675 NE2 GLN C 213 6683 8012 7026 -2886 1918 53 N ATOM 1676 N ALA A 214 57.877 26.970 26.426 1.00 28.99 N ANISOU 1676 N ALA C 214 4033 3798 3185 -353 -195 686 N ATOM 1677 CA ALA A 214 58.868 27.713 25.654 1.00 28.54 C ANISOU 1677 CA ALA C 214 3677 3693 3475 -175 -111 350 C ATOM 1678 C ALA A 214 58.297 28.059 24.287 1.00 28.15 C ANISOU 1678 C ALA C 214 3485 3684 3525 -42 -286 270 C ATOM 1679 O ALA A 214 58.608 29.149 23.775 1.00 32.38 O ANISOU 1679 O ALA C 214 3423 5591 3289 -771 170 210 O ATOM 1680 CB ALA A 214 60.164 26.946 25.455 1.00 28.84 C ANISOU 1680 CB ALA C 214 3188 3675 4096 -530 -1297 130 C ATOM 1681 N ALA A 215 57.488 27.175 23.707 1.00 26.92 N ANISOU 1681 N ALA C 215 3358 3711 3160 20 -495 438 N ATOM 1682 CA ALA A 215 56.898 27.445 22.393 1.00 30.50 C ANISOU 1682 CA ALA C 215 4225 3758 3604 -113 -91 36 C ATOM 1683 C ALA A 215 55.878 28.580 22.453 1.00 27.87 C ANISOU 1683 C ALA C 215 3067 3676 3846 215 -514 194 C ATOM 1684 O ALA A 215 55.857 29.451 21.584 1.00 28.10 O ANISOU 1684 O ALA C 215 3415 4015 3248 -44 -217 177 O ATOM 1685 CB ALA A 215 56.249 26.195 21.796 1.00 26.25 C ANISOU 1685 CB ALA C 215 4114 3604 2255 -51 -540 938 C ATOM 1686 N VAL A 216 55.018 28.579 23.470 1.00 26.01 N ANISOU 1686 N VAL C 216 2832 4068 2981 93 223 219 N ATOM 1687 CA VAL A 216 53.851 29.442 23.491 1.00 28.99 C ANISOU 1687 CA VAL C 216 3507 4112 3397 -225 178 765 C ATOM 1688 C VAL A 216 54.086 30.709 24.297 1.00 28.46 C ANISOU 1688 C VAL C 216 3112 4337 3362 -369 41 110 C ATOM 1689 O VAL A 216 53.719 31.808 23.830 1.00 31.65 O ANISOU 1689 O VAL C 216 3387 4551 4086 -556 -656 424 O ATOM 1690 CB VAL A 216 52.652 28.669 24.084 1.00 29.65 C ANISOU 1690 CB VAL C 216 3251 3832 4183 68 523 354 C ATOM 1691 CG1 VAL A 216 51.433 29.554 24.327 1.00 29.03 C ANISOU 1691 CG1 VAL C 216 3443 3719 3869 105 375 13 C ATOM 1692 CG2 VAL A 216 52.267 27.505 23.168 1.00 30.11 C ANISOU 1692 CG2 VAL C 216 3985 3878 3576 615 904 487 C ATOM 1693 N GLU A 217 54.667 30.645 25.491 1.00 29.52 N ANISOU 1693 N GLU C 217 3976 4112 3127 260 137 542 N ATOM 1694 CA GLU A 217 54.745 31.841 26.336 1.00 27.64 C ANISOU 1694 CA GLU C 217 3965 3921 2615 -127 -259 328 C ATOM 1695 C GLU A 217 56.157 32.399 26.376 1.00 27.57 C ANISOU 1695 C GLU C 217 3324 3921 3230 -513 -371 158 C ATOM 1696 O GLU A 217 56.344 33.567 26.691 1.00 30.82 O ANISOU 1696 O GLU C 217 3867 4616 3227 -699 388 516 O ATOM 1697 CB GLU A 217 54.382 31.593 27.806 1.00 28.51 C ANISOU 1697 CB GLU C 217 4447 3723 2661 -394 -510 230 C ATOM 1698 CG GLU A 217 52.917 31.513 28.134 1.00 31.72 C ANISOU 1698 CG GLU C 217 5028 3915 3109 -231 -796 545 C ATOM 1699 CD GLU A 217 52.666 30.984 29.532 1.00 30.22 C ANISOU 1699 CD GLU C 217 4414 4065 3004 153 -513 122 C ATOM 1700 OE1 GLU A 217 53.630 30.822 30.313 1.00 35.52 O ANISOU 1700 OE1 GLU C 217 5903 4209 3386 209 -68 -39 O ATOM 1701 OE2 GLU A 217 51.513 30.704 29.916 1.00 30.37 O ANISOU 1701 OE2 GLU C 217 4816 3827 2895 -71 -240 972 O ATOM 1702 N GLY A 218 57.159 31.580 26.091 1.00 27.03 N ANISOU 1702 N GLY C 218 3319 3806 3146 -253 182 24 N ATOM 1703 CA GLY A 218 58.513 32.111 26.211 1.00 27.96 C ANISOU 1703 CA GLY C 218 3346 4040 3238 -207 332 -278 C ATOM 1704 C GLY A 218 58.905 33.000 25.052 1.00 26.15 C ANISOU 1704 C GLY C 218 3303 3304 3330 261 346 -666 C ATOM 1705 O GLY A 218 58.149 33.226 24.123 1.00 26.74 O ANISOU 1705 O GLY C 218 3373 3412 3376 240 541 -709 O ATOM 1706 N CYS A 219 60.127 33.533 25.087 1.00 24.88 N ANISOU 1706 N CYS C 219 3568 2925 2958 352 743 37 N ATOM 1707 CA CYS A 219 60.579 34.342 23.984 1.00 30.38 C ANISOU 1707 CA CYS C 219 4496 3078 3969 623 -280 303 C ATOM 1708 C CYS A 219 61.360 33.490 22.975 1.00 30.85 C ANISOU 1708 C CYS C 219 4438 3599 3682 74 -540 392 C ATOM 1709 O CYS A 219 61.743 32.352 23.250 1.00 25.68 O ANISOU 1709 O CYS C 219 3123 3511 3124 661 -12 78 O ATOM 1710 CB CYS A 219 61.474 35.488 24.460 1.00 37.11 C ANISOU 1710 CB CYS C 219 3936 4930 5235 -330 -381 641 C ATOM 1711 SG CYS A 219 60.609 36.764 25.414 1.00 58.04 S ANISOU 1711 SG CYS C 219 7872 5748 8434 -1355 2190 1007 S ATOM 1712 N VAL A 220 61.597 34.077 21.814 1.00 27.88 N ANISOU 1712 N VAL C 220 3496 3703 3394 104 59 -12 N ATOM 1713 CA VAL A 220 62.350 33.384 20.771 1.00 26.75 C ANISOU 1713 CA VAL C 220 3323 3784 3057 282 28 -76 C ATOM 1714 C VAL A 220 63.806 33.162 21.176 1.00 26.58 C ANISOU 1714 C VAL C 220 3305 3766 3028 181 527 46 C ATOM 1715 O VAL A 220 64.559 34.077 21.528 1.00 26.98 O ANISOU 1715 O VAL C 220 3141 3674 3436 -52 435 -131 O ATOM 1716 CB VAL A 220 62.263 34.163 19.448 1.00 33.69 C ANISOU 1716 CB VAL C 220 5260 4232 3308 -763 -327 -237 C ATOM 1717 CG1 VAL A 220 63.159 33.488 18.400 1.00 29.53 C ANISOU 1717 CG1 VAL C 220 4246 4100 2875 -432 -540 -467 C ATOM 1718 CG2 VAL A 220 60.817 34.248 18.990 1.00 29.12 C ANISOU 1718 CG2 VAL C 220 4256 4208 2601 -760 -991 -56 C ATOM 1719 N ASN A 221 64.242 31.895 21.136 1.00 23.80 N ANISOU 1719 N ASN C 221 2734 3576 2733 519 250 357 N ATOM 1720 CA ASN A 221 65.651 31.653 21.411 1.00 26.01 C ANISOU 1720 CA ASN C 221 2969 3599 3315 539 773 400 C ATOM 1721 C ASN A 221 66.068 30.312 20.821 1.00 28.17 C ANISOU 1721 C ASN C 221 2942 3749 4012 85 133 543 C ATOM 1722 O ASN A 221 65.281 29.368 20.806 1.00 30.71 O ANISOU 1722 O ASN C 221 3047 3707 4914 270 773 475 O ATOM 1723 CB ASN A 221 65.947 31.709 22.909 1.00 33.22 C ANISOU 1723 CB ASN C 221 5329 3818 3475 153 881 -227 C ATOM 1724 CG ASN A 221 65.550 30.380 23.511 1.00 39.44 C ANISOU 1724 CG ASN C 221 6876 4170 3941 -916 -536 452 C ATOM 1725 OD1 ASN A 221 66.404 29.506 23.632 1.00 50.59 O ANISOU 1725 OD1 ASN C 221 9635 4632 4955 -1970 -966 36 O ATOM 1726 ND2 ASN A 221 64.274 30.273 23.845 1.00 39.14 N ANISOU 1726 ND2 ASN C 221 4934 5456 4482 -196 908 529 N ATOM 1727 N HIS A 222 67.298 30.232 20.318 1.00 24.93 N ANISOU 1727 N HIS C 222 3292 3123 3055 99 244 -201 N ATOM 1728 CA HIS A 222 67.693 29.022 19.607 1.00 28.03 C ANISOU 1728 CA HIS C 222 3672 3846 3130 -342 -116 313 C ATOM 1729 C HIS A 222 67.932 27.838 20.526 1.00 25.51 C ANISOU 1729 C HIS C 222 3150 3788 2756 -191 167 370 C ATOM 1730 O HIS A 222 68.107 26.716 20.069 1.00 26.47 O ANISOU 1730 O HIS C 222 3347 4108 2601 -357 606 -136 O ATOM 1731 CB HIS A 222 68.950 29.331 18.775 1.00 27.71 C ANISOU 1731 CB HIS C 222 3610 4005 2913 -335 -149 269 C ATOM 1732 CG HIS A 222 70.183 29.557 19.595 1.00 30.41 C ANISOU 1732 CG HIS C 222 4463 3639 3452 -122 171 392 C ATOM 1733 ND1 HIS A 222 71.421 29.377 19.040 1.00 30.51 N ANISOU 1733 ND1 HIS C 222 4026 3751 3813 -351 -41 647 N ATOM 1734 CD2 HIS A 222 70.412 29.957 20.888 1.00 28.37 C ANISOU 1734 CD2 HIS C 222 3804 3680 3294 164 -146 175 C ATOM 1735 CE1 HIS A 222 72.360 29.633 19.938 1.00 29.61 C ANISOU 1735 CE1 HIS C 222 3212 3860 4178 -174 -48 794 C ATOM 1736 NE2 HIS A 222 71.781 29.986 21.075 1.00 27.77 N ANISOU 1736 NE2 HIS C 222 3066 3834 3652 142 -437 335 N ATOM 1737 N MET A 223 67.987 28.043 21.846 1.00 25.07 N ANISOU 1737 N MET C 223 3191 3482 2852 -2 648 90 N ATOM 1738 CA MET A 223 68.269 26.885 22.697 1.00 27.84 C ANISOU 1738 CA MET C 223 3817 3836 2926 20 235 -63 C ATOM 1739 C MET A 223 67.020 25.997 22.815 1.00 28.01 C ANISOU 1739 C MET C 223 3332 3791 3519 -420 477 -313 C ATOM 1740 O MET A 223 67.136 24.780 23.010 1.00 32.61 O ANISOU 1740 O MET C 223 4043 4364 3982 -827 -476 -588 O ATOM 1741 CB MET A 223 68.770 27.285 24.082 1.00 31.81 C ANISOU 1741 CB MET C 223 3759 4994 3335 -137 569 -704 C ATOM 1742 CG MET A 223 70.180 27.807 24.232 1.00 35.49 C ANISOU 1742 CG MET C 223 4971 4284 4229 278 1229 -251 C ATOM 1743 SD MET A 223 71.524 26.643 23.909 1.00 45.43 S ANISOU 1743 SD MET C 223 7173 4720 5367 -457 4 786 S ATOM 1744 CE MET A 223 70.890 25.155 24.647 1.00 45.69 C ANISOU 1744 CE MET C 223 6965 6223 4174 -1548 947 -545 C ATOM 1745 N TRP A 224 65.831 26.579 22.709 1.00 26.46 N ANISOU 1745 N TRP C 224 3248 3792 3012 -210 580 -393 N ATOM 1746 CA TRP A 224 64.564 25.874 22.631 1.00 25.51 C ANISOU 1746 CA TRP C 224 2915 3982 2794 -399 599 -47 C ATOM 1747 C TRP A 224 64.059 26.039 21.203 1.00 23.92 C ANISOU 1747 C TRP C 224 2798 3541 2750 126 299 111 C ATOM 1748 O TRP A 224 63.325 26.995 20.922 1.00 28.18 O ANISOU 1748 O TRP C 224 4073 4026 2607 -664 -261 251 O ATOM 1749 CB TRP A 224 63.551 26.433 23.630 1.00 26.22 C ANISOU 1749 CB TRP C 224 3118 4195 2652 -420 353 18 C ATOM 1750 CG TRP A 224 63.971 26.145 25.057 1.00 27.79 C ANISOU 1750 CG TRP C 224 3388 4375 2797 -169 32 -98 C ATOM 1751 CD1 TRP A 224 64.879 26.846 25.792 1.00 28.37 C ANISOU 1751 CD1 TRP C 224 3671 4310 2800 -9 -75 -617 C ATOM 1752 CD2 TRP A 224 63.512 25.100 25.917 1.00 28.12 C ANISOU 1752 CD2 TRP C 224 3668 4114 2901 -141 -221 210 C ATOM 1753 NE1 TRP A 224 65.019 26.317 27.039 1.00 29.97 N ANISOU 1753 NE1 TRP C 224 3806 4833 2747 -261 -224 -395 N ATOM 1754 CE2 TRP A 224 64.184 25.230 27.146 1.00 30.42 C ANISOU 1754 CE2 TRP C 224 3885 4698 2975 -218 -329 -98 C ATOM 1755 CE3 TRP A 224 62.600 24.057 25.783 1.00 27.83 C ANISOU 1755 CE3 TRP C 224 3701 3809 3064 31 -475 414 C ATOM 1756 CZ2 TRP A 224 63.971 24.363 28.216 1.00 30.60 C ANISOU 1756 CZ2 TRP C 224 3923 4616 3087 -197 -442 -43 C ATOM 1757 CZ3 TRP A 224 62.380 23.189 26.838 1.00 28.39 C ANISOU 1757 CZ3 TRP C 224 3913 3697 3177 -26 -548 146 C ATOM 1758 CH2 TRP A 224 63.068 23.347 28.052 1.00 29.45 C ANISOU 1758 CH2 TRP C 224 3780 4361 3050 -619 -160 298 C ATOM 1759 N THR A 225 64.478 25.152 20.298 1.00 24.46 N ANISOU 1759 N THR C 225 2994 3587 2711 71 623 -144 N ATOM 1760 CA THR A 225 64.217 25.300 18.872 1.00 23.89 C ANISOU 1760 CA THR C 225 2936 3457 2683 -37 365 -176 C ATOM 1761 C THR A 225 62.745 25.567 18.595 1.00 23.19 C ANISOU 1761 C THR C 225 3060 3332 2421 -189 -249 -227 C ATOM 1762 O THR A 225 62.409 26.403 17.758 1.00 24.92 O ANISOU 1762 O THR C 225 3742 3616 2112 -581 -167 -160 O ATOM 1763 CB THR A 225 64.660 24.030 18.117 1.00 28.76 C ANISOU 1763 CB THR C 225 5097 3622 2209 -1100 151 -226 C ATOM 1764 OG1 THR A 225 66.026 23.772 18.442 1.00 26.14 O ANISOU 1764 OG1 THR C 225 3254 3870 2808 -573 134 514 O ATOM 1765 CG2 THR A 225 64.594 24.244 16.610 1.00 25.10 C ANISOU 1765 CG2 THR C 225 3289 3990 2260 -19 -1080 637 C ATOM 1766 N ILE A 226 61.871 24.865 19.295 1.00 23.82 N ANISOU 1766 N ILE C 226 3298 3556 2197 -70 -148 250 N ATOM 1767 CA ILE A 226 60.429 25.004 19.121 1.00 26.22 C ANISOU 1767 CA ILE C 226 3673 3367 2922 -125 -323 466 C ATOM 1768 C ILE A 226 59.967 26.446 19.301 1.00 27.08 C ANISOU 1768 C ILE C 226 3529 3616 3145 -236 -8 -107 C ATOM 1769 O ILE A 226 58.947 26.844 18.699 1.00 25.56 O ANISOU 1769 O ILE C 226 3398 3644 2671 -280 170 31 O ATOM 1770 CB ILE A 226 59.654 24.078 20.089 1.00 24.10 C ANISOU 1770 CB ILE C 226 3102 3689 2368 264 168 -148 C ATOM 1771 CG1 ILE A 226 58.190 23.870 19.670 1.00 26.09 C ANISOU 1771 CG1 ILE C 226 2996 3888 3031 95 447 -573 C ATOM 1772 CG2 ILE A 226 59.718 24.557 21.553 1.00 22.86 C ANISOU 1772 CG2 ILE C 226 2494 3551 2642 498 325 295 C ATOM 1773 CD1 ILE A 226 58.052 23.003 18.426 1.00 30.57 C ANISOU 1773 CD1 ILE C 226 3755 4324 3538 229 1015 -389 C ATOM 1774 N SER A 227 60.674 27.255 20.102 1.00 25.04 N ANISOU 1774 N SER C 227 3424 3454 2636 -15 -298 -68 N ATOM 1775 CA SER A 227 60.269 28.655 20.256 1.00 26.89 C ANISOU 1775 CA SER C 227 3845 3709 2662 -327 253 -370 C ATOM 1776 C SER A 227 60.373 29.420 18.936 1.00 27.33 C ANISOU 1776 C SER C 227 3780 3607 2999 -575 -69 -80 C ATOM 1777 O SER A 227 59.704 30.431 18.735 1.00 25.90 O ANISOU 1777 O SER C 227 3228 3565 3048 -395 43 -78 O ATOM 1778 CB SER A 227 61.107 29.376 21.315 1.00 28.65 C ANISOU 1778 CB SER C 227 3612 3899 3375 57 326 -525 C ATOM 1779 OG SER A 227 62.429 29.630 20.837 1.00 29.28 O ANISOU 1779 OG SER C 227 4302 3703 3122 -12 499 -34 O ATOM 1780 N CYS A 228 61.231 28.941 18.007 1.00 27.72 N ANISOU 1780 N CYS C 228 3531 3482 3517 -138 -413 144 N ATOM 1781 CA CYS A 228 61.324 29.775 16.802 1.00 30.52 C ANISOU 1781 CA CYS C 228 3796 4297 3502 -259 -491 167 C ATOM 1782 C CYS A 228 60.096 29.568 15.918 1.00 28.64 C ANISOU 1782 C CYS C 228 4034 3652 3198 -282 -635 375 C ATOM 1783 O CYS A 228 59.912 30.322 14.956 1.00 28.04 O ANISOU 1783 O CYS C 228 4053 4283 2318 -141 -620 895 O ATOM 1784 CB CYS A 228 62.690 29.546 16.139 1.00 35.97 C ANISOU 1784 CB CYS C 228 4947 4097 4625 374 -2151 -672 C ATOM 1785 SG CYS A 228 64.051 29.881 17.387 1.00 44.93 S ANISOU 1785 SG CYS C 228 6784 4787 5499 995 -101 253 S ATOM 1786 N LEU A 229 59.202 28.624 16.226 1.00 25.14 N ANISOU 1786 N LEU C 229 3768 3358 2425 -601 -289 556 N ATOM 1787 CA LEU A 229 57.947 28.549 15.465 1.00 26.01 C ANISOU 1787 CA LEU C 229 3763 3876 2245 -645 -166 307 C ATOM 1788 C LEU A 229 57.069 29.774 15.653 1.00 27.05 C ANISOU 1788 C LEU C 229 3811 3617 2851 -359 608 -10 C ATOM 1789 O LEU A 229 56.129 29.998 14.877 1.00 25.11 O ANISOU 1789 O LEU C 229 3310 3704 2526 -28 400 164 O ATOM 1790 CB LEU A 229 57.154 27.286 15.841 1.00 27.99 C ANISOU 1790 CB LEU C 229 3715 4359 2561 -462 -105 389 C ATOM 1791 CG LEU A 229 57.764 25.996 15.265 1.00 35.45 C ANISOU 1791 CG LEU C 229 4502 5677 3289 -1842 -283 498 C ATOM 1792 CD1 LEU A 229 56.963 24.783 15.687 1.00 35.34 C ANISOU 1792 CD1 LEU C 229 4276 6000 3152 -1493 117 -705 C ATOM 1793 CD2 LEU A 229 57.818 26.084 13.747 1.00 30.45 C ANISOU 1793 CD2 LEU C 229 3824 4477 3267 -1275 323 542 C ATOM 1794 N GLN A 230 57.351 30.594 16.659 1.00 26.40 N ANISOU 1794 N GLN C 230 3851 3533 2648 -560 549 -290 N ATOM 1795 CA GLN A 230 56.652 31.860 16.824 1.00 25.65 C ANISOU 1795 CA GLN C 230 3857 3443 2445 -411 8 347 C ATOM 1796 C GLN A 230 56.856 32.769 15.608 1.00 24.61 C ANISOU 1796 C GLN C 230 3239 3277 2836 167 82 -266 C ATOM 1797 O GLN A 230 56.048 33.655 15.336 1.00 26.95 O ANISOU 1797 O GLN C 230 3802 3453 2986 -187 192 -316 O ATOM 1798 CB GLN A 230 57.148 32.616 18.068 1.00 25.56 C ANISOU 1798 CB GLN C 230 4034 3023 2655 -236 224 432 C ATOM 1799 CG GLN A 230 56.774 31.950 19.382 1.00 25.03 C ANISOU 1799 CG GLN C 230 3973 3053 2486 296 372 499 C ATOM 1800 CD GLN A 230 57.274 32.720 20.590 1.00 27.22 C ANISOU 1800 CD GLN C 230 3859 3743 2742 -48 491 -185 C ATOM 1801 OE1 GLN A 230 57.399 33.951 20.530 1.00 28.77 O ANISOU 1801 OE1 GLN C 230 3961 3766 3204 -190 487 95 O ATOM 1802 NE2 GLN A 230 57.559 32.010 21.686 1.00 31.30 N ANISOU 1802 NE2 GLN C 230 4572 4527 2795 -375 440 -383 N ATOM 1803 N LEU A 231 57.967 32.547 14.901 1.00 25.39 N ANISOU 1803 N LEU C 231 3599 3562 2485 206 -28 -133 N ATOM 1804 CA LEU A 231 58.277 33.368 13.745 1.00 24.25 C ANISOU 1804 CA LEU C 231 3256 3484 2474 130 188 -459 C ATOM 1805 C LEU A 231 57.749 32.722 12.464 1.00 24.06 C ANISOU 1805 C LEU C 231 3218 3411 2514 113 235 -303 C ATOM 1806 O LEU A 231 57.841 33.298 11.372 1.00 31.82 O ANISOU 1806 O LEU C 231 4543 5218 2330 -1154 174 -216 O ATOM 1807 CB LEU A 231 59.789 33.571 13.605 1.00 25.21 C ANISOU 1807 CB LEU C 231 2684 3926 2969 149 149 -360 C ATOM 1808 CG LEU A 231 60.444 34.201 14.836 1.00 27.06 C ANISOU 1808 CG LEU C 231 3295 3610 3378 173 658 -285 C ATOM 1809 CD1 LEU A 231 61.938 34.351 14.581 1.00 28.51 C ANISOU 1809 CD1 LEU C 231 3502 4002 3326 534 145 -685 C ATOM 1810 CD2 LEU A 231 59.740 35.511 15.155 1.00 28.42 C ANISOU 1810 CD2 LEU C 231 3397 4006 3397 -320 521 -514 C ATOM 1811 N HIS A 232 57.193 31.525 12.598 1.00 26.95 N ANISOU 1811 N HIS C 232 3167 3463 3609 -99 451 265 N ATOM 1812 CA HIS A 232 56.722 30.857 11.377 1.00 26.73 C ANISOU 1812 CA HIS C 232 2986 3787 3384 -101 213 -20 C ATOM 1813 C HIS A 232 55.377 31.410 10.952 1.00 25.36 C ANISOU 1813 C HIS C 232 3199 3722 2714 -146 -298 93 C ATOM 1814 O HIS A 232 54.510 31.726 11.761 1.00 29.30 O ANISOU 1814 O HIS C 232 4631 3628 2874 -997 159 409 O ATOM 1815 CB HIS A 232 56.680 29.345 11.643 1.00 24.21 C ANISOU 1815 CB HIS C 232 3148 3584 2465 -189 147 217 C ATOM 1816 CG HIS A 232 56.434 28.577 10.381 1.00 24.58 C ANISOU 1816 CG HIS C 232 3459 3392 2489 -228 314 -9 C ATOM 1817 ND1 HIS A 232 55.156 28.362 9.914 1.00 24.87 N ANISOU 1817 ND1 HIS C 232 3275 3272 2904 -316 339 11 N ATOM 1818 CD2 HIS A 232 57.290 28.006 9.507 1.00 23.99 C ANISOU 1818 CD2 HIS C 232 3153 3477 2487 -108 361 69 C ATOM 1819 CE1 HIS A 232 55.232 27.670 8.781 1.00 27.11 C ANISOU 1819 CE1 HIS C 232 3390 3582 3326 73 781 245 C ATOM 1820 NE2 HIS A 232 56.509 27.442 8.514 1.00 27.56 N ANISOU 1820 NE2 HIS C 232 3913 3291 3266 -106 1117 149 N ATOM 1821 N PRO A 233 55.144 31.575 9.647 1.00 29.85 N ANISOU 1821 N PRO C 233 4389 4130 2825 -525 -831 -39 N ATOM 1822 CA PRO A 233 53.866 32.143 9.200 1.00 29.55 C ANISOU 1822 CA PRO C 233 4353 4227 2648 -629 20 -135 C ATOM 1823 C PRO A 233 52.653 31.338 9.651 1.00 30.17 C ANISOU 1823 C PRO C 233 4240 3997 3226 -655 269 54 C ATOM 1824 O PRO A 233 51.578 31.932 9.836 1.00 30.28 O ANISOU 1824 O PRO C 233 4342 3887 3276 -373 1171 -270 O ATOM 1825 CB PRO A 233 53.956 32.112 7.673 1.00 29.53 C ANISOU 1825 CB PRO C 233 4372 4156 2691 -1082 502 167 C ATOM 1826 CG PRO A 233 55.180 31.363 7.331 1.00 33.98 C ANISOU 1826 CG PRO C 233 5727 4093 3092 -287 649 102 C ATOM 1827 CD PRO A 233 56.062 31.281 8.541 1.00 31.71 C ANISOU 1827 CD PRO C 233 5181 4341 2525 -575 -100 46 C ATOM 1828 N LYS A 234 52.732 30.024 9.831 1.00 28.88 N ANISOU 1828 N LYS C 234 3639 4258 3076 -531 1301 -227 N ATOM 1829 CA LYS A 234 51.512 29.254 10.091 1.00 29.54 C ANISOU 1829 CA LYS C 234 3940 4172 3110 -404 1065 -86 C ATOM 1830 C LYS A 234 51.801 27.998 10.907 1.00 33.54 C ANISOU 1830 C LYS C 234 4515 4743 3485 -914 306 503 C ATOM 1831 O LYS A 234 51.971 26.896 10.360 1.00 27.61 O ANISOU 1831 O LYS C 234 2921 4179 3391 248 464 169 O ATOM 1832 CB LYS A 234 50.844 28.863 8.766 1.00 30.48 C ANISOU 1832 CB LYS C 234 3351 4769 3459 -536 1563 245 C ATOM 1833 CG LYS A 234 49.336 28.800 8.896 1.00 38.16 C ANISOU 1833 CG LYS C 234 4449 4908 5142 -7 2316 -28 C ATOM 1834 CD LYS A 234 48.707 28.136 7.683 1.00 47.81 C ANISOU 1834 CD LYS C 234 6546 5808 5814 -229 3168 -1844 C ATOM 1835 CE LYS A 234 49.015 28.967 6.450 1.00 54.11 C ANISOU 1835 CE LYS C 234 8746 6080 5734 -1419 2641 -2081 C ATOM 1836 NZ LYS A 234 47.723 29.431 5.859 1.00 66.62 N ANISOU 1836 NZ LYS C 234 10734 5787 8791 -2122 2186 -2864 N ATOM 1837 N ALA A 235 51.864 28.185 12.218 1.00 27.96 N ANISOU 1837 N ALA C 235 3557 3681 3387 -288 66 568 N ATOM 1838 CA ALA A 235 52.192 27.134 13.166 1.00 31.58 C ANISOU 1838 CA ALA C 235 3988 4098 3913 -355 -424 435 C ATOM 1839 C ALA A 235 51.041 26.834 14.127 1.00 29.07 C ANISOU 1839 C ALA C 235 3748 3818 3480 -355 -57 357 C ATOM 1840 O ALA A 235 50.262 27.683 14.604 1.00 31.00 O ANISOU 1840 O ALA C 235 3926 3599 4253 -14 747 353 O ATOM 1841 CB ALA A 235 53.447 27.523 13.944 1.00 30.40 C ANISOU 1841 CB ALA C 235 4795 3101 3656 -216 -579 613 C ATOM 1842 N ILE A 236 50.914 25.534 14.425 1.00 26.94 N ANISOU 1842 N ILE C 236 3158 3904 3176 100 507 -133 N ATOM 1843 CA ILE A 236 49.856 25.050 15.294 1.00 31.10 C ANISOU 1843 CA ILE C 236 3868 4157 3793 175 -244 -227 C ATOM 1844 C ILE A 236 50.418 24.052 16.293 1.00 29.56 C ANISOU 1844 C ILE C 236 3757 4065 3411 -181 121 1 C ATOM 1845 O ILE A 236 51.094 23.136 15.846 1.00 33.00 O ANISOU 1845 O ILE C 236 5284 4375 2879 -612 -69 189 O ATOM 1846 CB ILE A 236 48.755 24.352 14.474 1.00 31.23 C ANISOU 1846 CB ILE C 236 3621 4325 3921 596 -804 -478 C ATOM 1847 CG1 ILE A 236 48.340 25.156 13.249 1.00 35.13 C ANISOU 1847 CG1 ILE C 236 3770 5456 4123 385 -695 -1035 C ATOM 1848 CG2 ILE A 236 47.547 24.014 15.333 1.00 31.42 C ANISOU 1848 CG2 ILE C 236 2994 5127 3817 -118 -89 1014 C ATOM 1849 CD1 ILE A 236 47.261 24.525 12.385 1.00 55.06 C ANISOU 1849 CD1 ILE C 236 7612 6737 6571 -825 3180 -2168 C ATOM 1850 N MET A 237 50.136 24.251 17.563 1.00 29.36 N ANISOU 1850 N MET C 237 3617 4074 3464 -752 422 95 N ATOM 1851 CA MET A 237 50.452 23.306 18.614 1.00 30.49 C ANISOU 1851 CA MET C 237 3624 4555 3407 -270 224 -150 C ATOM 1852 C MET A 237 49.147 22.606 19.038 1.00 30.72 C ANISOU 1852 C MET C 237 3624 4444 3602 -190 392 -60 C ATOM 1853 O MET A 237 48.191 23.317 19.377 1.00 31.33 O ANISOU 1853 O MET C 237 3859 4527 3519 -259 548 85 O ATOM 1854 CB MET A 237 51.041 23.927 19.871 1.00 32.89 C ANISOU 1854 CB MET C 237 3613 4865 4018 -523 678 -645 C ATOM 1855 CG MET A 237 52.171 24.907 19.725 1.00 37.03 C ANISOU 1855 CG MET C 237 3307 5944 4817 -827 797 294 C ATOM 1856 SD MET A 237 53.611 24.235 18.921 1.00 48.54 S ANISOU 1856 SD MET C 237 5863 5740 6841 -99 -1040 349 S ATOM 1857 CE MET A 237 54.468 23.328 20.192 1.00 42.25 C ANISOU 1857 CE MET C 237 6070 5304 4680 934 -1908 1637 C ATOM 1858 N VAL A 238 49.172 21.286 18.993 1.00 29.35 N ANISOU 1858 N VAL C 238 3627 4330 3193 -186 196 -143 N ATOM 1859 CA VAL A 238 47.999 20.498 19.392 1.00 28.91 C ANISOU 1859 CA VAL C 238 3688 4254 3042 -176 227 13 C ATOM 1860 C VAL A 238 48.362 19.706 20.642 1.00 28.28 C ANISOU 1860 C VAL C 238 3595 4044 3107 -184 263 -10 C ATOM 1861 O VAL A 238 49.272 18.874 20.601 1.00 28.31 O ANISOU 1861 O VAL C 238 3533 4080 3146 -227 80 217 O ATOM 1862 CB VAL A 238 47.519 19.559 18.278 1.00 29.24 C ANISOU 1862 CB VAL C 238 3648 4347 3114 -173 238 -121 C ATOM 1863 CG1 VAL A 238 46.147 18.969 18.604 1.00 27.27 C ANISOU 1863 CG1 VAL C 238 3419 4035 2908 -480 56 -206 C ATOM 1864 CG2 VAL A 238 47.513 20.309 16.948 1.00 26.61 C ANISOU 1864 CG2 VAL C 238 3134 3775 3200 279 288 -355 C ATOM 1865 N CYS A 239 47.675 19.978 21.762 1.00 25.74 N ANISOU 1865 N CYS C 239 3053 3681 3047 -106 288 -148 N ATOM 1866 CA CYS A 239 48.253 19.382 22.965 1.00 29.29 C ANISOU 1866 CA CYS C 239 3473 4457 3199 307 101 -600 C ATOM 1867 C CYS A 239 47.222 18.712 23.854 1.00 28.69 C ANISOU 1867 C CYS C 239 4053 3961 2886 -135 87 142 C ATOM 1868 O CYS A 239 46.006 18.945 23.783 1.00 29.05 O ANISOU 1868 O CYS C 239 3648 3928 3461 -210 517 295 O ATOM 1869 CB CYS A 239 49.005 20.516 23.676 1.00 34.03 C ANISOU 1869 CB CYS C 239 4347 3865 4719 742 1239 -760 C ATOM 1870 SG CYS A 239 47.931 21.689 24.547 1.00 39.99 S ANISOU 1870 SG CYS C 239 5272 5296 4628 -462 850 -44 S ATOM 1871 N ASP A 240 47.736 17.825 24.734 1.00 26.15 N ANISOU 1871 N ASP C 240 3033 4251 2650 -398 564 161 N ATOM 1872 CA ASP A 240 46.831 17.182 25.678 1.00 29.09 C ANISOU 1872 CA ASP C 240 3413 4564 3075 -481 205 457 C ATOM 1873 C ASP A 240 46.900 17.889 27.024 1.00 28.66 C ANISOU 1873 C ASP C 240 3324 4458 3108 105 229 659 C ATOM 1874 O ASP A 240 47.671 18.833 27.193 1.00 28.38 O ANISOU 1874 O ASP C 240 3477 3970 3336 387 396 598 O ATOM 1875 CB ASP A 240 47.158 15.713 25.842 1.00 29.89 C ANISOU 1875 CB ASP C 240 3770 4689 2899 -685 -195 549 C ATOM 1876 CG ASP A 240 48.471 15.400 26.495 1.00 31.16 C ANISOU 1876 CG ASP C 240 4159 4670 3010 -564 -486 520 C ATOM 1877 OD1 ASP A 240 49.252 16.301 26.852 1.00 32.48 O ANISOU 1877 OD1 ASP C 240 4104 4798 3439 -167 -804 258 O ATOM 1878 OD2 ASP A 240 48.716 14.184 26.653 1.00 31.57 O ANISOU 1878 OD2 ASP C 240 4681 4817 2497 -942 -278 564 O ATOM 1879 N GLU A 241 46.091 17.444 27.973 1.00 29.71 N ANISOU 1879 N GLU C 241 3604 4350 3333 116 44 789 N ATOM 1880 CA GLU A 241 46.049 18.150 29.270 1.00 31.31 C ANISOU 1880 CA GLU C 241 4200 4568 3129 131 101 643 C ATOM 1881 C GLU A 241 47.348 18.100 30.054 1.00 29.43 C ANISOU 1881 C GLU C 241 3646 4509 3026 -128 -340 422 C ATOM 1882 O GLU A 241 47.839 19.142 30.523 1.00 29.66 O ANISOU 1882 O GLU C 241 4029 4344 2898 -75 59 731 O ATOM 1883 CB GLU A 241 44.888 17.577 30.101 1.00 31.59 C ANISOU 1883 CB GLU C 241 4093 5054 2857 382 334 599 C ATOM 1884 CG GLU A 241 44.860 18.056 31.545 1.00 39.18 C ANISOU 1884 CG GLU C 241 6070 5726 3091 -330 353 1361 C ATOM 1885 CD GLU A 241 43.697 17.379 32.259 1.00 49.17 C ANISOU 1885 CD GLU C 241 8485 5771 4425 -723 -2413 1325 C ATOM 1886 OE1 GLU A 241 42.550 17.778 31.975 1.00 58.40 O ANISOU 1886 OE1 GLU C 241 8545 5563 8081 -181 -2846 1624 O ATOM 1887 OE2 GLU A 241 43.923 16.451 33.072 1.00 68.54 O ANISOU 1887 OE2 GLU C 241 9711 9225 7105 -1444 -3487 -521 O ATOM 1888 N PRO A 242 47.982 16.947 30.278 1.00 30.69 N ANISOU 1888 N PRO C 242 4110 4639 2911 -380 -720 663 N ATOM 1889 CA PRO A 242 49.205 16.922 31.074 1.00 31.27 C ANISOU 1889 CA PRO C 242 4644 4100 3136 -448 -489 889 C ATOM 1890 C PRO A 242 50.318 17.789 30.492 1.00 29.98 C ANISOU 1890 C PRO C 242 4208 4477 2705 -484 -265 214 C ATOM 1891 O PRO A 242 51.189 18.231 31.265 1.00 31.45 O ANISOU 1891 O PRO C 242 4778 4586 2587 -409 303 684 O ATOM 1892 CB PRO A 242 49.662 15.469 31.029 1.00 33.73 C ANISOU 1892 CB PRO C 242 4340 4658 3819 -618 -690 612 C ATOM 1893 CG PRO A 242 48.547 14.678 30.428 1.00 34.64 C ANISOU 1893 CG PRO C 242 4523 4941 3700 -700 -610 174 C ATOM 1894 CD PRO A 242 47.554 15.615 29.835 1.00 34.24 C ANISOU 1894 CD PRO C 242 5007 5146 2856 -1301 125 244 C ATOM 1895 N SER A 243 50.326 18.033 29.185 1.00 29.23 N ANISOU 1895 N SER C 243 3971 4416 2718 -540 -182 61 N ATOM 1896 CA SER A 243 51.388 18.854 28.605 1.00 27.31 C ANISOU 1896 CA SER C 243 3917 4111 2349 -525 14 50 C ATOM 1897 C SER A 243 51.274 20.330 28.987 1.00 27.62 C ANISOU 1897 C SER C 243 3848 3712 2935 -250 285 29 C ATOM 1898 O SER A 243 52.209 21.107 28.769 1.00 26.17 O ANISOU 1898 O SER C 243 3898 3493 2554 -331 352 425 O ATOM 1899 CB SER A 243 51.366 18.713 27.074 1.00 29.73 C ANISOU 1899 CB SER C 243 4950 3969 2378 -585 1 256 C ATOM 1900 OG SER A 243 50.299 19.488 26.526 1.00 27.83 O ANISOU 1900 OG SER C 243 3599 4346 2629 -370 39 -250 O ATOM 1901 N THR A 244 50.130 20.740 29.542 1.00 26.75 N ANISOU 1901 N THR C 244 3617 3871 2676 -168 129 104 N ATOM 1902 CA THR A 244 49.893 22.156 29.808 1.00 27.91 C ANISOU 1902 CA THR C 244 4136 3994 2473 -596 -30 87 C ATOM 1903 C THR A 244 50.367 22.610 31.190 1.00 25.34 C ANISOU 1903 C THR C 244 3259 3619 2751 131 26 212 C ATOM 1904 O THR A 244 50.056 23.761 31.534 1.00 30.29 O ANISOU 1904 O THR C 244 4601 4276 2633 -678 -13 649 O ATOM 1905 CB THR A 244 48.398 22.541 29.727 1.00 28.25 C ANISOU 1905 CB THR C 244 4132 4062 2537 -640 618 -320 C ATOM 1906 OG1 THR A 244 47.683 21.814 30.745 1.00 31.66 O ANISOU 1906 OG1 THR C 244 4688 4038 3302 -486 317 809 O ATOM 1907 CG2 THR A 244 47.772 22.205 28.372 1.00 32.74 C ANISOU 1907 CG2 THR C 244 4748 4681 3012 -1123 1583 -177 C ATOM 1908 N MET A 245 51.069 21.784 31.947 1.00 27.73 N ANISOU 1908 N MET C 245 3833 3638 3063 254 323 -141 N ATOM 1909 CA MET A 245 51.425 22.007 33.347 1.00 29.15 C ANISOU 1909 CA MET C 245 3841 4124 3111 -106 489 -229 C ATOM 1910 C MET A 245 52.221 23.287 33.597 1.00 28.19 C ANISOU 1910 C MET C 245 3793 3985 2932 -127 329 146 C ATOM 1911 O MET A 245 52.104 23.911 34.667 1.00 28.07 O ANISOU 1911 O MET C 245 3395 4168 3100 -545 -121 637 O ATOM 1912 CB MET A 245 52.251 20.832 33.924 1.00 32.08 C ANISOU 1912 CB MET C 245 4907 4979 2302 -1388 557 16 C ATOM 1913 CG MET A 245 51.451 19.574 34.202 1.00 33.99 C ANISOU 1913 CG MET C 245 4894 4983 3038 -1511 528 382 C ATOM 1914 SD MET A 245 50.032 19.806 35.299 1.00 43.11 S ANISOU 1914 SD MET C 245 7059 5708 3614 -496 -528 370 S ATOM 1915 CE MET A 245 48.656 19.987 34.169 1.00 42.86 C ANISOU 1915 CE MET C 245 5039 5972 5272 -297 -1271 -500 C ATOM 1916 N GLU A 246 53.065 23.708 32.661 1.00 27.84 N ANISOU 1916 N GLU C 246 3908 3836 2832 -253 438 416 N ATOM 1917 CA GLU A 246 53.928 24.858 32.899 1.00 27.58 C ANISOU 1917 CA GLU C 246 3866 3777 2835 -124 306 269 C ATOM 1918 C GLU A 246 53.344 26.134 32.317 1.00 27.70 C ANISOU 1918 C GLU C 246 3831 3611 3081 5 87 364 C ATOM 1919 O GLU A 246 53.981 27.192 32.416 1.00 30.01 O ANISOU 1919 O GLU C 246 3882 4391 3127 -343 502 121 O ATOM 1920 CB GLU A 246 55.303 24.591 32.286 1.00 26.55 C ANISOU 1920 CB GLU C 246 3614 3741 2732 -456 483 478 C ATOM 1921 CG GLU A 246 55.998 23.390 32.924 1.00 29.45 C ANISOU 1921 CG GLU C 246 4390 3866 2933 -516 254 251 C ATOM 1922 CD GLU A 246 56.665 23.732 34.238 1.00 29.68 C ANISOU 1922 CD GLU C 246 3787 4147 3342 -285 257 -45 C ATOM 1923 OE1 GLU A 246 56.581 24.912 34.661 1.00 32.95 O ANISOU 1923 OE1 GLU C 246 4022 4907 3589 -275 356 926 O ATOM 1924 OE2 GLU A 246 57.275 22.830 34.855 1.00 32.32 O ANISOU 1924 OE2 GLU C 246 4831 3772 3677 228 -161 -223 O ATOM 1925 N LEU A 247 52.157 26.079 31.714 1.00 27.85 N ANISOU 1925 N LEU C 247 4243 3797 2543 -168 485 316 N ATOM 1926 CA LEU A 247 51.539 27.302 31.189 1.00 26.84 C ANISOU 1926 CA LEU C 247 4342 3880 1975 -95 222 389 C ATOM 1927 C LEU A 247 50.851 28.104 32.275 1.00 28.12 C ANISOU 1927 C LEU C 247 4599 4000 2084 -399 350 412 C ATOM 1928 O LEU A 247 50.442 27.499 33.271 1.00 27.40 O ANISOU 1928 O LEU C 247 4793 3795 1823 -571 446 390 O ATOM 1929 CB LEU A 247 50.490 26.975 30.112 1.00 26.12 C ANISOU 1929 CB LEU C 247 3883 3889 2151 -158 258 429 C ATOM 1930 CG LEU A 247 51.008 26.273 28.857 1.00 27.37 C ANISOU 1930 CG LEU C 247 4202 4010 2188 143 419 533 C ATOM 1931 CD1 LEU A 247 49.830 25.980 27.924 1.00 25.57 C ANISOU 1931 CD1 LEU C 247 2934 4540 2240 -178 83 230 C ATOM 1932 CD2 LEU A 247 52.066 27.132 28.195 1.00 24.81 C ANISOU 1932 CD2 LEU C 247 3837 3233 2357 45 816 662 C ATOM 1933 N LYS A 248 50.665 29.404 32.112 1.00 28.25 N ANISOU 1933 N LYS C 248 4041 4115 2577 -83 270 586 N ATOM 1934 CA LYS A 248 49.806 30.084 33.086 1.00 27.77 C ANISOU 1934 CA LYS C 248 3864 3955 2733 -359 -276 579 C ATOM 1935 C LYS A 248 48.343 29.725 32.831 1.00 27.06 C ANISOU 1935 C LYS C 248 3758 4145 2381 -282 -377 518 C ATOM 1936 O LYS A 248 47.950 29.490 31.684 1.00 27.94 O ANISOU 1936 O LYS C 248 3636 4469 2510 -630 -64 591 O ATOM 1937 CB LYS A 248 49.929 31.593 33.053 1.00 27.56 C ANISOU 1937 CB LYS C 248 3811 4018 2643 -336 130 12 C ATOM 1938 CG LYS A 248 51.291 32.147 33.462 1.00 30.94 C ANISOU 1938 CG LYS C 248 3946 4092 3718 324 -465 382 C ATOM 1939 CD LYS A 248 51.233 33.653 33.205 1.00 36.79 C ANISOU 1939 CD LYS C 248 3777 4469 5732 267 -268 248 C ATOM 1940 CE LYS A 248 52.587 34.306 33.453 1.00 41.56 C ANISOU 1940 CE LYS C 248 3895 5194 6701 316 1231 655 C ATOM 1941 NZ LYS A 248 52.408 35.465 34.388 1.00 64.44 N ANISOU 1941 NZ LYS C 248 7675 7829 8980 -1186 4287 57 N ATOM 1942 N VAL A 249 47.563 29.687 33.893 1.00 27.82 N ANISOU 1942 N VAL C 249 4064 3966 2541 -418 -418 653 N ATOM 1943 CA VAL A 249 46.128 29.434 33.803 1.00 29.14 C ANISOU 1943 CA VAL C 249 4339 3867 2865 -364 -622 687 C ATOM 1944 C VAL A 249 45.494 30.364 32.792 1.00 29.69 C ANISOU 1944 C VAL C 249 4243 4183 2856 -604 51 363 C ATOM 1945 O VAL A 249 44.638 29.986 31.988 1.00 29.65 O ANISOU 1945 O VAL C 249 4190 4321 2753 -180 -49 692 O ATOM 1946 CB VAL A 249 45.501 29.608 35.205 1.00 30.17 C ANISOU 1946 CB VAL C 249 4621 3819 3023 -532 -573 890 C ATOM 1947 CG1 VAL A 249 43.984 29.680 35.111 1.00 29.07 C ANISOU 1947 CG1 VAL C 249 5318 3551 2176 -649 -309 701 C ATOM 1948 CG2 VAL A 249 45.926 28.486 36.142 1.00 24.16 C ANISOU 1948 CG2 VAL C 249 3130 3405 2647 514 -231 679 C ATOM 1949 N LYS A 250 45.871 31.638 32.764 1.00 27.54 N ANISOU 1949 N LYS C 250 3970 4005 2488 39 -519 338 N ATOM 1950 CA LYS A 250 45.179 32.538 31.819 1.00 27.82 C ANISOU 1950 CA LYS C 250 4165 3806 2600 -394 167 308 C ATOM 1951 C LYS A 250 45.539 32.260 30.362 1.00 27.22 C ANISOU 1951 C LYS C 250 4222 3668 2452 -25 224 26 C ATOM 1952 O LYS A 250 44.768 32.554 29.422 1.00 28.24 O ANISOU 1952 O LYS C 250 3419 4438 2873 -240 412 -535 O ATOM 1953 CB LYS A 250 45.500 34.000 32.126 1.00 30.23 C ANISOU 1953 CB LYS C 250 4164 4250 3073 -540 123 477 C ATOM 1954 CG LYS A 250 46.996 34.308 31.972 1.00 31.70 C ANISOU 1954 CG LYS C 250 4092 4896 3057 -244 -261 487 C ATOM 1955 CD LYS A 250 47.162 35.822 32.125 1.00 35.06 C ANISOU 1955 CD LYS C 250 4216 5425 3681 -254 811 324 C ATOM 1956 CE LYS A 250 48.591 36.255 31.861 1.00 36.44 C ANISOU 1956 CE LYS C 250 4030 6135 3681 24 798 111 C ATOM 1957 NZ LYS A 250 48.730 37.722 32.082 1.00 41.29 N ANISOU 1957 NZ LYS C 250 4044 7263 4381 -820 -949 157 N ATOM 1958 N THR A 251 46.734 31.708 30.149 1.00 27.37 N ANISOU 1958 N THR C 251 3712 3797 2891 137 196 475 N ATOM 1959 CA THR A 251 47.146 31.363 28.794 1.00 31.40 C ANISOU 1959 CA THR C 251 4784 4275 2872 -274 472 537 C ATOM 1960 C THR A 251 46.284 30.223 28.272 1.00 29.52 C ANISOU 1960 C THR C 251 4861 3738 2619 -202 455 249 C ATOM 1961 O THR A 251 45.792 30.266 27.146 1.00 32.25 O ANISOU 1961 O THR C 251 5614 3891 2749 -72 548 83 O ATOM 1962 CB THR A 251 48.614 30.908 28.776 1.00 28.46 C ANISOU 1962 CB THR C 251 4228 4524 2061 80 99 797 C ATOM 1963 OG1 THR A 251 49.420 31.985 29.251 1.00 29.70 O ANISOU 1963 OG1 THR C 251 4389 4539 2356 -373 456 437 O ATOM 1964 CG2 THR A 251 49.053 30.575 27.348 1.00 31.07 C ANISOU 1964 CG2 THR C 251 5112 4743 1949 -1025 259 640 C ATOM 1965 N LEU A 252 46.121 29.205 29.124 1.00 29.85 N ANISOU 1965 N LEU C 252 4893 3879 2568 -589 377 794 N ATOM 1966 CA LEU A 252 45.311 28.047 28.739 1.00 34.76 C ANISOU 1966 CA LEU C 252 4921 5004 3281 -1060 667 206 C ATOM 1967 C LEU A 252 43.867 28.480 28.543 1.00 33.21 C ANISOU 1967 C LEU C 252 3835 5125 3657 -622 356 619 C ATOM 1968 O LEU A 252 43.173 28.085 27.598 1.00 35.21 O ANISOU 1968 O LEU C 252 4810 5168 3402 -383 402 545 O ATOM 1969 CB LEU A 252 45.498 26.930 29.773 1.00 36.74 C ANISOU 1969 CB LEU C 252 5077 5825 3058 -1259 574 306 C ATOM 1970 CG LEU A 252 44.892 25.566 29.441 1.00 39.19 C ANISOU 1970 CG LEU C 252 5216 5905 3768 -1667 697 -49 C ATOM 1971 CD1 LEU A 252 45.462 25.009 28.127 1.00 34.52 C ANISOU 1971 CD1 LEU C 252 4461 5526 3128 -1047 903 -630 C ATOM 1972 CD2 LEU A 252 45.055 24.589 30.607 1.00 35.04 C ANISOU 1972 CD2 LEU C 252 4735 5034 3545 -297 241 214 C ATOM 1973 N ARG A 253 43.343 29.345 29.407 1.00 36.36 N ANISOU 1973 N ARG C 253 5121 5135 3561 -1103 453 433 N ATOM 1974 CA ARG A 253 41.983 29.875 29.300 1.00 38.59 C ANISOU 1974 CA ARG C 253 6027 5184 3451 -732 264 695 C ATOM 1975 C ARG A 253 41.768 30.694 28.029 1.00 38.93 C ANISOU 1975 C ARG C 253 6532 4733 3528 -872 285 679 C ATOM 1976 O ARG A 253 40.722 30.615 27.370 1.00 43.82 O ANISOU 1976 O ARG C 253 8345 4533 3773 -354 382 699 O ATOM 1977 CB ARG A 253 41.659 30.705 30.570 1.00 39.74 C ANISOU 1977 CB ARG C 253 6022 5503 3574 -39 425 1090 C ATOM 1978 CG ARG A 253 40.285 31.338 30.487 1.00 54.89 C ANISOU 1978 CG ARG C 253 9916 5416 5523 -414 1567 1488 C ATOM 1979 CD ARG A 253 40.024 32.390 31.551 1.00 78.02 C ANISOU 1979 CD ARG C 253 15665 7538 6442 -2471 1999 2875 C ATOM 1980 NE ARG A 253 38.961 31.921 32.452 1.00 91.76 N ANISOU 1980 NE ARG C 253 18216 8596 8054 -2693 518 4537 N ATOM 1981 CZ ARG A 253 37.729 32.385 32.543 1.00 97.65 C ANISOU 1981 CZ ARG C 253 19916 8465 8723 -3233 -1149 4968 C ATOM 1982 NH1 ARG A 253 37.304 33.400 31.802 1.00111.61 N ANISOU 1982 NH1 ARG C 253 22556 9699 10151 -3763 -1219 3091 N ATOM 1983 NH2 ARG A 253 36.893 31.825 33.420 1.00109.51 N ANISOU 1983 NH2 ARG C 253 21238 10420 9950 -2615 -1744 6339 N ATOM 1984 N TYR A 254 42.752 31.509 27.644 1.00 37.12 N ANISOU 1984 N TYR C 254 6131 4846 3126 -1609 379 1414 N ATOM 1985 CA TYR A 254 42.709 32.301 26.422 1.00 35.87 C ANISOU 1985 CA TYR C 254 5615 4834 3181 -1309 945 472 C ATOM 1986 C TYR A 254 42.544 31.451 25.162 1.00 37.91 C ANISOU 1986 C TYR C 254 6403 4597 3404 -1551 1324 326 C ATOM 1987 O TYR A 254 41.708 31.699 24.269 1.00 40.95 O ANISOU 1987 O TYR C 254 6914 4843 3804 -1788 1812 35 O ATOM 1988 CB TYR A 254 43.991 33.137 26.302 1.00 36.39 C ANISOU 1988 CB TYR C 254 5681 4772 3376 -1304 537 241 C ATOM 1989 CG TYR A 254 44.133 33.835 24.957 1.00 38.96 C ANISOU 1989 CG TYR C 254 6344 4956 3504 -1260 251 145 C ATOM 1990 CD1 TYR A 254 43.335 34.936 24.641 1.00 39.58 C ANISOU 1990 CD1 TYR C 254 6319 5114 3605 -1409 243 101 C ATOM 1991 CD2 TYR A 254 45.060 33.412 24.002 1.00 38.99 C ANISOU 1991 CD2 TYR C 254 6008 5015 3791 -1020 -21 264 C ATOM 1992 CE1 TYR A 254 43.449 35.591 23.423 1.00 39.41 C ANISOU 1992 CE1 TYR C 254 5976 4999 3999 -1329 -150 339 C ATOM 1993 CE2 TYR A 254 45.185 34.056 22.782 1.00 38.40 C ANISOU 1993 CE2 TYR C 254 5911 4858 3822 -1107 9 202 C ATOM 1994 CZ TYR A 254 44.378 35.143 22.499 1.00 40.32 C ANISOU 1994 CZ TYR C 254 6003 4892 4425 -1207 -391 446 C ATOM 1995 OH TYR A 254 44.480 35.802 21.299 1.00 45.13 O ANISOU 1995 OH TYR C 254 8431 4773 3942 -2493 -374 763 O ATOM 1996 N PHE A 255 43.388 30.407 25.067 1.00 35.08 N ANISOU 1996 N PHE C 255 5750 4409 3169 -1228 493 761 N ATOM 1997 CA PHE A 255 43.325 29.576 23.868 1.00 35.31 C ANISOU 1997 CA PHE C 255 6118 3955 3345 -899 881 713 C ATOM 1998 C PHE A 255 42.103 28.669 23.912 1.00 37.20 C ANISOU 1998 C PHE C 255 6690 3719 3723 -226 1206 146 C ATOM 1999 O PHE A 255 41.553 28.321 22.863 1.00 43.90 O ANISOU 1999 O PHE C 255 7467 5107 4107 -410 1880 93 O ATOM 2000 CB PHE A 255 44.595 28.729 23.723 1.00 30.76 C ANISOU 2000 CB PHE C 255 5648 3871 2168 -513 606 429 C ATOM 2001 CG PHE A 255 45.783 29.586 23.311 1.00 32.15 C ANISOU 2001 CG PHE C 255 5329 4350 2537 -747 575 341 C ATOM 2002 CD1 PHE A 255 45.875 30.048 22.005 1.00 32.72 C ANISOU 2002 CD1 PHE C 255 5091 4551 2790 -971 383 146 C ATOM 2003 CD2 PHE A 255 46.786 29.923 24.201 1.00 33.72 C ANISOU 2003 CD2 PHE C 255 5637 4575 2600 -310 721 593 C ATOM 2004 CE1 PHE A 255 46.948 30.837 21.597 1.00 33.26 C ANISOU 2004 CE1 PHE C 255 5722 4267 2648 -363 397 298 C ATOM 2005 CE2 PHE A 255 47.856 30.705 23.806 1.00 33.15 C ANISOU 2005 CE2 PHE C 255 5674 4244 2679 -442 398 229 C ATOM 2006 CZ PHE A 255 47.957 31.161 22.500 1.00 33.28 C ANISOU 2006 CZ PHE C 255 5897 4050 2699 -507 396 102 C ATOM 2007 N ASN A 256 41.687 28.278 25.114 1.00 37.09 N ANISOU 2007 N ASN C 256 6241 3836 4015 42 1174 699 N ATOM 2008 CA ASN A 256 40.503 27.440 25.239 1.00 42.58 C ANISOU 2008 CA ASN C 256 6272 5204 4702 471 1442 342 C ATOM 2009 C ASN A 256 39.279 28.226 24.788 1.00 43.82 C ANISOU 2009 C ASN C 256 5694 5102 5854 798 1520 286 C ATOM 2010 O ASN A 256 38.367 27.589 24.256 1.00 49.55 O ANISOU 2010 O ASN C 256 5990 5059 7777 1151 2251 909 O ATOM 2011 CB ASN A 256 40.265 26.915 26.654 1.00 45.84 C ANISOU 2011 CB ASN C 256 7020 5227 5172 1072 563 854 C ATOM 2012 CG ASN A 256 40.803 25.501 26.798 1.00 51.15 C ANISOU 2012 CG ASN C 256 7453 6339 5643 319 -365 978 C ATOM 2013 OD1 ASN A 256 40.275 24.521 26.255 1.00 63.15 O ANISOU 2013 OD1 ASN C 256 7543 8146 8305 -609 370 -352 O ATOM 2014 ND2 ASN A 256 41.901 25.389 27.526 1.00 59.01 N ANISOU 2014 ND2 ASN C 256 10319 7443 4660 -2024 1467 -407 N ATOM 2015 N GLU A 257 39.288 29.547 24.989 1.00 43.26 N ANISOU 2015 N GLU C 257 6315 5509 4613 250 2117 -95 N ATOM 2016 CA GLU A 257 38.134 30.311 24.506 1.00 46.91 C ANISOU 2016 CA GLU C 257 6788 5798 5238 -98 2812 -601 C ATOM 2017 C GLU A 257 38.259 30.617 23.022 1.00 49.57 C ANISOU 2017 C GLU C 257 8194 5336 5303 -921 2507 -405 C ATOM 2018 O GLU A 257 37.323 30.505 22.218 1.00 49.09 O ANISOU 2018 O GLU C 257 8394 5604 4654 -481 2513 81 O ATOM 2019 CB GLU A 257 37.982 31.561 25.389 1.00 57.48 C ANISOU 2019 CB GLU C 257 9569 6628 5642 -1616 3645 -717 C ATOM 2020 CG GLU A 257 37.778 31.160 26.859 1.00 69.57 C ANISOU 2020 CG GLU C 257 11906 8594 5933 -2785 2731 806 C ATOM 2021 CD GLU A 257 37.596 32.336 27.790 1.00 79.02 C ANISOU 2021 CD GLU C 257 13844 9722 6456 -4129 2561 1566 C ATOM 2022 OE1 GLU A 257 37.914 33.468 27.351 1.00 96.05 O ANISOU 2022 OE1 GLU C 257 16292 11402 8801 -8311 1429 2019 O ATOM 2023 OE2 GLU A 257 37.134 32.171 28.949 1.00 89.60 O ANISOU 2023 OE2 GLU C 257 17551 9594 6899 -4298 1870 2295 O ATOM 2024 N LEU A 258 39.441 31.017 22.565 1.00 47.38 N ANISOU 2024 N LEU C 258 8517 4891 4593 -940 2611 -410 N ATOM 2025 CA LEU A 258 39.637 31.331 21.164 1.00 50.87 C ANISOU 2025 CA LEU C 258 9305 5186 4839 -1285 2010 -881 C ATOM 2026 C LEU A 258 39.396 30.154 20.229 1.00 50.46 C ANISOU 2026 C LEU C 258 9888 5220 4064 -1167 1960 -398 C ATOM 2027 O LEU A 258 39.106 30.312 19.039 1.00 56.43 O ANISOU 2027 O LEU C 258 11745 5327 4367 -475 2277 -1063 O ATOM 2028 CB LEU A 258 41.078 31.845 21.020 1.00 51.82 C ANISOU 2028 CB LEU C 258 9073 5350 5265 -1419 867 -1596 C ATOM 2029 CG LEU A 258 41.506 32.261 19.610 1.00 55.99 C ANISOU 2029 CG LEU C 258 10130 5524 5618 -1907 118 -1687 C ATOM 2030 CD1 LEU A 258 40.733 33.502 19.192 1.00 64.99 C ANISOU 2030 CD1 LEU C 258 12598 5423 6671 -2252 -809 -1670 C ATOM 2031 CD2 LEU A 258 43.003 32.524 19.526 1.00 50.86 C ANISOU 2031 CD2 LEU C 258 8474 5253 5598 -2781 244 -1079 C ATOM 2032 N GLU A 259 39.516 28.908 20.691 1.00 46.86 N ANISOU 2032 N GLU C 259 8842 4555 4407 -487 1357 1040 N ATOM 2033 CA GLU A 259 39.492 27.797 19.732 1.00 45.60 C ANISOU 2033 CA GLU C 259 8904 4446 3977 14 1545 864 C ATOM 2034 C GLU A 259 38.308 26.895 20.030 1.00 49.17 C ANISOU 2034 C GLU C 259 8743 5471 4468 -133 1080 653 C ATOM 2035 O GLU A 259 38.155 25.801 19.482 1.00 48.07 O ANISOU 2035 O GLU C 259 8710 5793 3760 -122 724 1091 O ATOM 2036 CB GLU A 259 40.844 27.065 19.803 1.00 46.80 C ANISOU 2036 CB GLU C 259 8304 4519 4958 -451 4472 -385 C ATOM 2037 CG GLU A 259 41.322 26.593 18.422 1.00 57.76 C ANISOU 2037 CG GLU C 259 11515 4176 6255 -917 2905 1180 C ATOM 2038 CD GLU A 259 42.185 27.625 17.729 1.00 55.12 C ANISOU 2038 CD GLU C 259 11185 3572 6186 -78 3406 341 C ATOM 2039 OE1 GLU A 259 41.842 28.048 16.628 1.00 65.96 O ANISOU 2039 OE1 GLU C 259 14529 6178 4355 450 2391 1987 O ATOM 2040 OE2 GLU A 259 43.196 28.092 18.279 1.00 69.79 O ANISOU 2040 OE2 GLU C 259 9600 4789 12129 -2508 6009 -1473 O ATOM 2041 N ALA A 260 37.448 27.374 20.948 1.00 44.52 N ANISOU 2041 N ALA C 260 7647 4863 4406 659 1995 297 N ATOM 2042 CA ALA A 260 36.330 26.561 21.408 1.00 46.86 C ANISOU 2042 CA ALA C 260 7440 5203 5160 694 2246 501 C ATOM 2043 C ALA A 260 35.486 25.968 20.285 1.00 49.08 C ANISOU 2043 C ALA C 260 7882 5158 5608 701 2566 260 C ATOM 2044 O ALA A 260 35.092 24.804 20.320 1.00 49.48 O ANISOU 2044 O ALA C 260 7474 4853 6474 1891 2292 -515 O ATOM 2045 CB ALA A 260 35.415 27.379 22.319 1.00 45.90 C ANISOU 2045 CB ALA C 260 7330 5013 5096 694 1846 434 C ATOM 2046 N GLU A 261 35.194 26.773 19.277 1.00 49.76 N ANISOU 2046 N GLU C 261 8015 5128 5762 1212 2289 43 N ATOM 2047 CA GLU A 261 34.278 26.329 18.224 1.00 58.83 C ANISOU 2047 CA GLU C 261 10236 5801 6317 766 3757 -241 C ATOM 2048 C GLU A 261 34.929 25.232 17.388 1.00 57.24 C ANISOU 2048 C GLU C 261 9715 5717 6317 1168 3269 162 C ATOM 2049 O GLU A 261 34.275 24.405 16.753 1.00 52.72 O ANISOU 2049 O GLU C 261 9668 4880 5484 1062 2959 9 O ATOM 2050 CB GLU A 261 33.872 27.503 17.339 1.00 65.59 C ANISOU 2050 CB GLU C 261 11761 5403 7757 725 3823 -1336 C ATOM 2051 CG GLU A 261 32.479 28.062 17.498 1.00 78.63 C ANISOU 2051 CG GLU C 261 14955 5645 9274 230 1777 93 C ATOM 2052 CD GLU A 261 31.493 27.322 18.382 1.00 90.73 C ANISOU 2052 CD GLU C 261 17714 6934 9826 -99 89 1602 C ATOM 2053 OE1 GLU A 261 30.714 26.466 17.892 1.00 93.00 O ANISOU 2053 OE1 GLU C 261 17444 7105 10786 2597 -995 2857 O ATOM 2054 OE2 GLU A 261 31.465 27.601 19.608 1.00105.06 O ANISOU 2054 OE2 GLU C 261 22097 7991 9831 -725 257 1875 O ATOM 2055 N ASN A 262 36.261 25.282 17.426 1.00 55.39 N ANISOU 2055 N ASN C 262 8542 6013 6493 1073 2350 -29 N ATOM 2056 CA ASN A 262 37.081 24.416 16.595 1.00 49.60 C ANISOU 2056 CA ASN C 262 7153 5570 6124 1345 2237 -416 C ATOM 2057 C ASN A 262 37.439 23.113 17.278 1.00 51.02 C ANISOU 2057 C ASN C 262 6661 6390 6334 1264 2201 -590 C ATOM 2058 O ASN A 262 38.119 22.277 16.677 1.00 50.52 O ANISOU 2058 O ASN C 262 5771 7727 5697 206 2684 -634 O ATOM 2059 CB ASN A 262 38.396 25.126 16.217 1.00 44.56 C ANISOU 2059 CB ASN C 262 6658 5448 4826 1299 2615 -1416 C ATOM 2060 CG ASN A 262 38.139 26.439 15.506 1.00 50.37 C ANISOU 2060 CG ASN C 262 7736 5882 5522 772 1870 -1257 C ATOM 2061 OD1 ASN A 262 37.332 26.481 14.579 1.00 60.86 O ANISOU 2061 OD1 ASN C 262 7865 6632 8626 255 2311 -3505 O ATOM 2062 ND2 ASN A 262 38.792 27.515 15.906 1.00 53.11 N ANISOU 2062 ND2 ASN C 262 7280 5719 7181 968 1356 -2464 N ATOM 2063 N ILE A 263 37.037 22.911 18.533 1.00 54.88 N ANISOU 2063 N ILE C 263 7854 6657 6339 921 1957 -511 N ATOM 2064 CA ILE A 263 37.523 21.636 19.087 1.00 58.84 C ANISOU 2064 CA ILE C 263 9072 7101 6182 199 1693 -315 C ATOM 2065 C ILE A 263 36.344 20.737 19.398 1.00 61.53 C ANISOU 2065 C ILE C 263 8805 8054 6522 -134 1228 -518 C ATOM 2066 O ILE A 263 36.410 19.786 20.169 1.00 73.30 O ANISOU 2066 O ILE C 263 11969 8937 6945 -1392 -1345 1505 O ATOM 2067 CB ILE A 263 38.387 21.883 20.318 1.00 60.11 C ANISOU 2067 CB ILE C 263 9075 7875 5889 -323 1516 -647 C ATOM 2068 CG1 ILE A 263 37.661 22.673 21.407 1.00 60.97 C ANISOU 2068 CG1 ILE C 263 8141 8593 6432 -189 1709 -123 C ATOM 2069 CG2 ILE A 263 39.668 22.613 19.961 1.00 53.81 C ANISOU 2069 CG2 ILE C 263 7700 7705 5041 -1213 2539 -212 C ATOM 2070 CD1 ILE A 263 38.514 23.866 21.809 1.00 73.31 C ANISOU 2070 CD1 ILE C 263 6995 13184 7674 -2081 804 -698 C ATOM 2071 N LYS A 264 35.219 21.049 18.763 1.00 68.81 N ANISOU 2071 N LYS C 264 9647 7885 8611 823 2206 -294 N ATOM 2072 CA LYS A 264 34.056 20.167 18.876 1.00 76.55 C ANISOU 2072 CA LYS C 264 9629 8575 10881 860 1904 544 C ATOM 2073 C LYS A 264 34.055 19.101 17.785 1.00 77.52 C ANISOU 2073 C LYS C 264 8825 8920 11709 1188 1942 1056 C ATOM 2074 O LYS A 264 34.454 19.296 16.639 1.00 75.36 O ANISOU 2074 O LYS C 264 8680 8512 11443 798 2272 1025 O ATOM 2075 CB LYS A 264 32.771 21.000 18.836 1.00 76.51 C ANISOU 2075 CB LYS C 264 8786 8559 11725 1096 2521 342 C ATOM 2076 CG LYS A 264 32.887 22.372 19.487 1.00 80.69 C ANISOU 2076 CG LYS C 264 9279 9173 12207 413 2836 -39 C ATOM 2077 CD LYS A 264 31.660 23.223 19.187 1.00 78.42 C ANISOU 2077 CD LYS C 264 8394 9101 12301 798 3041 -22 C ATOM 2078 CE LYS A 264 31.226 23.981 20.433 1.00 78.43 C ANISOU 2078 CE LYS C 264 8762 8938 12101 682 3169 -309 C ATOM 2079 NZ LYS A 264 32.381 24.255 21.333 1.00 84.34 N ANISOU 2079 NZ LYS C 264 9861 10332 11853 -92 2924 -2156 N ATOM 2080 N GLY A 265 33.587 17.905 18.141 1.00 83.82 N ANISOU 2080 N GLY C 265 9209 9687 12953 641 1313 1474 N ATOM 2081 CA GLY A 265 33.498 16.823 17.170 1.00 83.43 C ANISOU 2081 CA GLY C 265 8380 9797 13523 1086 1098 2205 C ATOM 2082 C GLY A 265 34.844 16.123 17.043 1.00 87.07 C ANISOU 2082 C GLY C 265 9740 9860 13482 955 155 2653 C ATOM 2083 O GLY A 265 34.930 14.907 17.224 1.00 86.51 O ANISOU 2083 O GLY C 265 9490 9550 13831 1140 650 2459 O ATOM 2084 N LEU A 266 35.848 16.938 16.740 1.00 87.12 N ANISOU 2084 N LEU C 266 10153 9542 13408 970 -584 2410 N ATOM 2085 CA LEU A 266 37.230 16.498 16.591 1.00 89.29 C ANISOU 2085 CA LEU C 266 11062 9587 13277 985 -987 2797 C ATOM 2086 C LEU A 266 37.479 15.849 15.236 1.00 94.29 C ANISOU 2086 C LEU C 266 12132 10436 13258 560 -957 2916 C ATOM 2087 O LEU A 266 36.851 14.906 14.762 1.00101.99 O ANISOU 2087 O LEU C 266 13306 11900 13546 462 432 1647 O ATOM 2088 CB LEU A 266 37.600 15.556 17.740 1.00 91.54 C ANISOU 2088 CB LEU C 266 12387 9172 13221 91 -931 3141 C ATOM 2089 CG LEU A 266 37.876 16.202 19.097 1.00 90.13 C ANISOU 2089 CG LEU C 266 12137 8943 13166 180 -1012 3032 C ATOM 2090 CD1 LEU A 266 38.633 17.501 18.915 1.00 80.49 C ANISOU 2090 CD1 LEU C 266 12358 8433 9792 236 -1914 3047 C ATOM 2091 CD2 LEU A 266 36.587 16.442 19.869 1.00 86.96 C ANISOU 2091 CD2 LEU C 266 10986 9425 12628 351 -1463 2828 C ATOM 2092 OXT LEU A 266 38.526 17.004 15.393 1.00 99.16 O ANISOU 2092 OXT LEU C 266 11642 11558 14475 367 -2546 3302 O TER 2093 LEU C 266 ATOM 1 N MET A 1 76.445 31.955 53.899 1.00 38.92 N ANISOU 1 N MET D 1 5098 6097 3592 -1489 447 362 N ATOM 2 CA MET A 1 76.304 30.569 53.476 1.00 39.64 C ANISOU 2 CA MET D 1 4671 6407 3983 -879 140 -405 C ATOM 3 C MET A 1 77.622 30.144 52.843 1.00 37.92 C ANISOU 3 C MET D 1 4914 5679 3813 -933 633 -168 C ATOM 4 O MET A 1 78.231 30.963 52.128 1.00 46.58 O ANISOU 4 O MET D 1 5309 7754 4636 -2033 -63 1256 O ATOM 5 CB MET A 1 75.170 30.373 52.463 1.00 40.12 C ANISOU 5 CB MET D 1 4934 6308 4004 -354 -109 -293 C ATOM 6 CG MET A 1 75.201 28.964 51.877 1.00 43.45 C ANISOU 6 CG MET D 1 5363 6642 4505 -613 -169 -839 C ATOM 7 SD MET A 1 73.954 28.700 50.575 1.00 40.76 S ANISOU 7 SD MET D 1 5716 5321 4449 -844 351 -81 S ATOM 8 CE MET A 1 72.508 28.701 51.688 1.00 40.89 C ANISOU 8 CE MET D 1 5132 5850 4556 -1337 -1383 -497 C ATOM 9 N ARG A 2 78.053 28.920 53.094 1.00 32.45 N ANISOU 9 N ARG D 2 4810 4307 3211 -795 419 -513 N ATOM 10 CA ARG A 2 79.266 28.444 52.429 1.00 31.91 C ANISOU 10 CA ARG D 2 5037 4272 2817 -1111 367 -36 C ATOM 11 C ARG A 2 78.844 27.436 51.367 1.00 31.66 C ANISOU 11 C ARG D 2 4806 4445 2778 -1169 640 -178 C ATOM 12 O ARG A 2 77.865 26.716 51.537 1.00 35.19 O ANISOU 12 O ARG D 2 5848 4297 3224 -928 50 -345 O ATOM 13 CB ARG A 2 80.246 27.845 53.431 1.00 30.78 C ANISOU 13 CB ARG D 2 5683 3264 2747 -322 224 278 C ATOM 14 CG ARG A 2 80.714 28.789 54.533 1.00 31.74 C ANISOU 14 CG ARG D 2 6052 3464 2546 -297 -63 449 C ATOM 15 CD ARG A 2 81.545 28.043 55.575 1.00 34.98 C ANISOU 15 CD ARG D 2 6719 3922 2652 -266 253 153 C ATOM 16 NE ARG A 2 82.791 27.557 54.972 1.00 34.41 N ANISOU 16 NE ARG D 2 6379 4594 2103 -53 429 -191 N ATOM 17 CZ ARG A 2 83.601 26.666 55.509 1.00 36.03 C ANISOU 17 CZ ARG D 2 5807 4903 2981 -919 503 344 C ATOM 18 NH1 ARG A 2 83.284 26.162 56.683 1.00 40.91 N ANISOU 18 NH1 ARG D 2 6260 5762 3522 -1418 799 915 N ATOM 19 NH2 ARG A 2 84.717 26.264 54.914 1.00 34.88 N ANISOU 19 NH2 ARG D 2 5784 4351 3119 -751 335 -382 N ATOM 20 N LEU A 3 79.572 27.408 50.259 1.00 31.74 N ANISOU 20 N LEU D 3 4926 4478 2657 -969 591 -365 N ATOM 21 CA LEU A 3 79.411 26.362 49.260 1.00 30.10 C ANISOU 21 CA LEU D 3 4287 4342 2806 -471 790 -760 C ATOM 22 C LEU A 3 80.775 25.669 49.137 1.00 29.83 C ANISOU 22 C LEU D 3 4583 3777 2975 -455 909 -446 C ATOM 23 O LEU A 3 81.734 26.382 48.837 1.00 32.73 O ANISOU 23 O LEU D 3 5431 3887 3119 -772 569 -246 O ATOM 24 CB LEU A 3 78.939 26.888 47.908 1.00 28.39 C ANISOU 24 CB LEU D 3 3943 4351 2491 -526 530 -177 C ATOM 25 CG LEU A 3 78.844 25.895 46.741 1.00 30.84 C ANISOU 25 CG LEU D 3 4457 4660 2600 -868 475 -330 C ATOM 26 CD1 LEU A 3 77.820 24.819 47.023 1.00 32.59 C ANISOU 26 CD1 LEU D 3 4263 4270 3850 -374 15 -436 C ATOM 27 CD2 LEU A 3 78.458 26.596 45.449 1.00 31.39 C ANISOU 27 CD2 LEU D 3 3956 5259 2710 -90 417 -825 C ATOM 28 N ILE A 4 80.816 24.370 49.391 1.00 29.63 N ANISOU 28 N ILE D 4 4344 3841 3072 -259 982 -342 N ATOM 29 CA ILE A 4 82.061 23.619 49.260 1.00 29.55 C ANISOU 29 CA ILE D 4 4606 3487 3133 -143 936 162 C ATOM 30 C ILE A 4 81.982 22.814 47.972 1.00 30.18 C ANISOU 30 C ILE D 4 4166 4260 3043 -442 1143 178 C ATOM 31 O ILE A 4 81.303 21.772 47.902 1.00 32.25 O ANISOU 31 O ILE D 4 4551 4378 3323 -649 453 454 O ATOM 32 CB ILE A 4 82.315 22.677 50.444 1.00 27.05 C ANISOU 32 CB ILE D 4 3924 3415 2937 -176 550 63 C ATOM 33 CG1 ILE A 4 82.020 23.270 51.823 1.00 29.47 C ANISOU 33 CG1 ILE D 4 4697 3441 3059 -175 216 596 C ATOM 34 CG2 ILE A 4 83.744 22.117 50.382 1.00 27.89 C ANISOU 34 CG2 ILE D 4 4136 3481 2980 -8 132 -560 C ATOM 35 CD1 ILE A 4 82.735 24.560 52.149 1.00 33.52 C ANISOU 35 CD1 ILE D 4 5050 4991 2694 -1287 715 -196 C ATOM 36 N PRO A 5 82.609 23.283 46.906 1.00 32.38 N ANISOU 36 N PRO D 5 4856 4317 3131 -679 830 285 N ATOM 37 CA PRO A 5 82.481 22.605 45.610 1.00 30.96 C ANISOU 37 CA PRO D 5 4547 3924 3290 -305 590 340 C ATOM 38 C PRO A 5 83.553 21.529 45.485 1.00 32.73 C ANISOU 38 C PRO D 5 4676 3912 3847 7 682 -203 C ATOM 39 O PRO A 5 84.740 21.850 45.333 1.00 41.35 O ANISOU 39 O PRO D 5 5900 4187 5623 717 832 -29 O ATOM 40 CB PRO A 5 82.707 23.724 44.601 1.00 31.19 C ANISOU 40 CB PRO D 5 4759 4059 3031 -415 332 559 C ATOM 41 CG PRO A 5 83.045 24.942 45.388 1.00 36.93 C ANISOU 41 CG PRO D 5 6032 5134 2865 -1639 480 549 C ATOM 42 CD PRO A 5 83.456 24.472 46.761 1.00 33.62 C ANISOU 42 CD PRO D 5 5289 4328 3157 -800 506 366 C ATOM 43 N LEU A 6 83.110 20.280 45.563 1.00 33.33 N ANISOU 43 N LEU D 6 4570 4819 3274 -481 776 -193 N ATOM 44 CA LEU A 6 84.017 19.163 45.389 1.00 33.33 C ANISOU 44 CA LEU D 6 4731 4654 3278 -246 525 613 C ATOM 45 C LEU A 6 83.683 18.384 44.126 1.00 31.09 C ANISOU 45 C LEU D 6 4147 4368 3297 279 673 476 C ATOM 46 O LEU A 6 82.727 18.604 43.402 1.00 32.27 O ANISOU 46 O LEU D 6 4119 4542 3601 99 1150 523 O ATOM 47 CB LEU A 6 83.967 18.269 46.651 1.00 30.93 C ANISOU 47 CB LEU D 6 3860 4785 3106 349 44 1093 C ATOM 48 CG LEU A 6 84.410 19.019 47.917 1.00 32.11 C ANISOU 48 CG LEU D 6 4765 4312 3124 71 328 1115 C ATOM 49 CD1 LEU A 6 83.987 18.277 49.177 1.00 35.25 C ANISOU 49 CD1 LEU D 6 5001 5247 3147 -439 1216 761 C ATOM 50 CD2 LEU A 6 85.913 19.285 47.911 1.00 35.77 C ANISOU 50 CD2 LEU D 6 4293 4843 4453 743 779 713 C ATOM 51 N THR A 7 84.523 17.382 43.828 1.00 31.68 N ANISOU 51 N THR D 7 4224 4112 3701 321 509 420 N ATOM 52 CA THR A 7 84.337 16.611 42.609 1.00 33.08 C ANISOU 52 CA THR D 7 4689 4514 3367 118 295 845 C ATOM 53 C THR A 7 83.460 15.390 42.806 1.00 31.24 C ANISOU 53 C THR D 7 3910 4252 3706 464 192 409 C ATOM 54 O THR A 7 82.467 15.290 42.081 1.00 35.37 O ANISOU 54 O THR D 7 6266 4839 2335 243 238 189 O ATOM 55 CB THR A 7 85.705 16.166 42.055 1.00 35.77 C ANISOU 55 CB THR D 7 5099 4124 4366 201 -284 440 C ATOM 56 OG1 THR A 7 86.547 17.322 41.999 1.00 47.75 O ANISOU 56 OG1 THR D 7 8771 4110 5264 -541 -867 1016 O ATOM 57 CG2 THR A 7 85.554 15.642 40.634 1.00 37.28 C ANISOU 57 CG2 THR D 7 4307 5762 4097 -525 -261 1003 C ATOM 58 N THR A 8 83.808 14.498 43.735 1.00 30.84 N ANISOU 58 N THR D 8 4104 4019 3596 438 215 699 N ATOM 59 CA THR A 8 83.120 13.224 43.872 1.00 31.16 C ANISOU 59 CA THR D 8 4406 3978 3457 355 94 571 C ATOM 60 C THR A 8 82.376 13.136 45.212 1.00 30.18 C ANISOU 60 C THR D 8 4125 4102 3240 241 452 507 C ATOM 61 O THR A 8 82.622 13.876 46.155 1.00 31.39 O ANISOU 61 O THR D 8 4238 4017 3672 414 -241 687 O ATOM 62 CB THR A 8 84.095 12.039 43.802 1.00 35.03 C ANISOU 62 CB THR D 8 4296 4909 4104 3 -51 1001 C ATOM 63 OG1 THR A 8 84.916 12.126 44.990 1.00 34.44 O ANISOU 63 OG1 THR D 8 4112 4849 4124 424 677 1479 O ATOM 64 CG2 THR A 8 85.048 12.109 42.617 1.00 37.97 C ANISOU 64 CG2 THR D 8 4096 6196 4135 368 -39 1312 C ATOM 65 N ALA A 9 81.439 12.185 45.245 1.00 32.06 N ANISOU 65 N ALA D 9 4160 4378 3641 -281 174 869 N ATOM 66 CA ALA A 9 80.738 11.845 46.471 1.00 31.04 C ANISOU 66 CA ALA D 9 4421 4042 3330 54 124 490 C ATOM 67 C ALA A 9 81.719 11.460 47.574 1.00 32.92 C ANISOU 67 C ALA D 9 3707 5331 3470 167 -40 180 C ATOM 68 O ALA A 9 81.519 11.789 48.748 1.00 32.03 O ANISOU 68 O ALA D 9 3626 5124 3421 -138 -7 107 O ATOM 69 CB ALA A 9 79.759 10.713 46.207 1.00 30.59 C ANISOU 69 CB ALA D 9 3188 4023 4410 94 -250 811 C ATOM 70 N GLU A 10 82.799 10.744 47.229 1.00 33.85 N ANISOU 70 N GLU D 10 3775 5271 3814 125 16 681 N ATOM 71 CA GLU A 10 83.701 10.326 48.302 1.00 39.43 C ANISOU 71 CA GLU D 10 3560 5969 5451 -195 889 8 C ATOM 72 C GLU A 10 84.347 11.564 48.914 1.00 37.01 C ANISOU 72 C GLU D 10 4141 5260 4661 -46 1227 292 C ATOM 73 O GLU A 10 84.487 11.601 50.136 1.00 32.98 O ANISOU 73 O GLU D 10 3149 4745 4635 151 1622 525 O ATOM 74 CB GLU A 10 84.807 9.384 47.871 1.00 42.67 C ANISOU 74 CB GLU D 10 4032 6783 5397 396 705 329 C ATOM 75 CG GLU A 10 84.956 9.074 46.412 1.00 55.83 C ANISOU 75 CG GLU D 10 6703 8353 6159 -877 -1108 26 C ATOM 76 CD GLU A 10 83.818 8.321 45.757 1.00 68.33 C ANISOU 76 CD GLU D 10 9689 9367 6907 -3509 778 -1069 C ATOM 77 OE1 GLU A 10 83.305 8.855 44.748 1.00 57.50 O ANISOU 77 OE1 GLU D 10 7455 8986 5406 -2363 -1163 -518 O ATOM 78 OE2 GLU A 10 83.460 7.219 46.241 1.00 89.46 O ANISOU 78 OE2 GLU D 10 12970 11278 9744 -5873 3114 -2031 O ATOM 79 N GLN A 11 84.718 12.526 48.077 1.00 33.27 N ANISOU 79 N GLN D 11 4292 4510 3841 620 787 482 N ATOM 80 CA GLN A 11 85.259 13.742 48.658 1.00 33.41 C ANISOU 80 CA GLN D 11 4958 4221 3514 370 560 1011 C ATOM 81 C GLN A 11 84.198 14.471 49.479 1.00 32.06 C ANISOU 81 C GLN D 11 5269 3696 3218 185 402 974 C ATOM 82 O GLN A 11 84.479 15.052 50.533 1.00 32.12 O ANISOU 82 O GLN D 11 4172 4714 3319 -288 990 514 O ATOM 83 CB GLN A 11 85.739 14.729 47.596 1.00 34.19 C ANISOU 83 CB GLN D 11 5234 4412 3344 568 454 1209 C ATOM 84 CG GLN A 11 87.024 14.393 46.864 1.00 37.54 C ANISOU 84 CG GLN D 11 5259 4933 4070 883 549 1570 C ATOM 85 CD GLN A 11 87.227 15.374 45.718 1.00 38.16 C ANISOU 85 CD GLN D 11 6373 4487 3639 963 681 1402 C ATOM 86 OE1 GLN A 11 86.366 15.477 44.850 1.00 42.48 O ANISOU 86 OE1 GLN D 11 6455 5597 4087 -229 922 138 O ATOM 87 NE2 GLN A 11 88.319 16.106 45.698 1.00 52.12 N ANISOU 87 NE2 GLN D 11 9658 4581 5564 324 2102 1353 N ATOM 88 N VAL A 12 82.960 14.495 48.997 1.00 32.02 N ANISOU 88 N VAL D 12 4669 3928 3568 125 474 777 N ATOM 89 CA VAL A 12 81.942 15.188 49.805 1.00 30.86 C ANISOU 89 CA VAL D 12 4315 4473 2937 105 733 602 C ATOM 90 C VAL A 12 81.804 14.542 51.172 1.00 31.72 C ANISOU 90 C VAL D 12 4118 4969 2964 -299 730 513 C ATOM 91 O VAL A 12 81.750 15.208 52.232 1.00 33.07 O ANISOU 91 O VAL D 12 5054 4690 2820 -1018 1080 -72 O ATOM 92 CB VAL A 12 80.599 15.168 49.063 1.00 30.93 C ANISOU 92 CB VAL D 12 4292 4529 2930 249 606 644 C ATOM 93 CG1 VAL A 12 79.426 15.531 49.976 1.00 26.77 C ANISOU 93 CG1 VAL D 12 2518 4821 2832 -406 1004 825 C ATOM 94 CG2 VAL A 12 80.684 16.117 47.864 1.00 27.85 C ANISOU 94 CG2 VAL D 12 4346 3318 2917 63 533 331 C ATOM 95 N GLY A 13 81.729 13.207 51.230 1.00 34.20 N ANISOU 95 N GLY D 13 4049 5732 3212 -520 779 305 N ATOM 96 CA GLY A 13 81.610 12.566 52.553 1.00 29.99 C ANISOU 96 CA GLY D 13 3565 4722 3108 -212 638 236 C ATOM 97 C GLY A 13 82.841 12.839 53.397 1.00 32.48 C ANISOU 97 C GLY D 13 4481 4605 3254 -5 535 274 C ATOM 98 O GLY A 13 82.755 13.028 54.617 1.00 29.43 O ANISOU 98 O GLY D 13 3679 4384 3119 -135 1000 386 O ATOM 99 N LYS A 14 84.048 12.880 52.806 1.00 34.10 N ANISOU 99 N LYS D 14 4805 4698 3454 70 236 279 N ATOM 100 CA LYS A 14 85.200 13.105 53.695 1.00 33.19 C ANISOU 100 CA LYS D 14 3933 4702 3977 -10 646 255 C ATOM 101 C LYS A 14 85.165 14.503 54.283 1.00 32.13 C ANISOU 101 C LYS D 14 3945 4509 3753 -74 844 197 C ATOM 102 O LYS A 14 85.524 14.739 55.436 1.00 30.73 O ANISOU 102 O LYS D 14 3695 4154 3826 518 707 190 O ATOM 103 CB LYS A 14 86.521 12.854 52.956 1.00 35.28 C ANISOU 103 CB LYS D 14 3443 5482 4479 324 1177 812 C ATOM 104 CG LYS A 14 86.770 11.358 52.795 1.00 44.78 C ANISOU 104 CG LYS D 14 3870 7448 5695 -306 234 716 C ATOM 105 CD LYS A 14 87.835 10.995 51.782 1.00 51.11 C ANISOU 105 CD LYS D 14 4335 7781 7302 381 -432 799 C ATOM 106 CE LYS A 14 88.213 9.518 51.873 1.00 59.42 C ANISOU 106 CE LYS D 14 4853 9178 8545 -1037 -1909 511 C ATOM 107 NZ LYS A 14 87.679 8.722 50.725 1.00 82.88 N ANISOU 107 NZ LYS D 14 9491 12124 9874 -4405 -260 -1517 N ATOM 108 N TRP A 15 84.727 15.453 53.475 1.00 32.83 N ANISOU 108 N TRP D 15 3964 4686 3826 16 920 319 N ATOM 109 CA TRP A 15 84.697 16.851 53.893 1.00 31.38 C ANISOU 109 CA TRP D 15 3957 4475 3492 36 838 671 C ATOM 110 C TRP A 15 83.686 17.019 55.019 1.00 30.90 C ANISOU 110 C TRP D 15 4466 4001 3273 -274 838 651 C ATOM 111 O TRP A 15 83.939 17.609 56.076 1.00 30.21 O ANISOU 111 O TRP D 15 3919 3861 3699 -145 576 482 O ATOM 112 CB TRP A 15 84.358 17.813 52.717 1.00 32.35 C ANISOU 112 CB TRP D 15 4518 4618 3156 -598 816 601 C ATOM 113 CG TRP A 15 84.709 19.238 53.109 1.00 32.69 C ANISOU 113 CG TRP D 15 4393 4590 3440 -423 1089 0 C ATOM 114 CD1 TRP A 15 85.858 19.908 52.794 1.00 33.69 C ANISOU 114 CD1 TRP D 15 4677 4557 3565 -529 1072 -65 C ATOM 115 CD2 TRP A 15 83.916 20.159 53.885 1.00 33.36 C ANISOU 115 CD2 TRP D 15 4267 4495 3913 -175 1017 -585 C ATOM 116 NE1 TRP A 15 85.837 21.183 53.320 1.00 35.12 N ANISOU 116 NE1 TRP D 15 4626 4609 4109 -443 1009 -286 N ATOM 117 CE2 TRP A 15 84.655 21.362 53.993 1.00 34.81 C ANISOU 117 CE2 TRP D 15 4363 4726 4137 -481 1105 -233 C ATOM 118 CE3 TRP A 15 82.656 20.099 54.499 1.00 29.62 C ANISOU 118 CE3 TRP D 15 3588 4554 3111 -87 1519 -713 C ATOM 119 CZ2 TRP A 15 84.189 22.480 54.684 1.00 32.81 C ANISOU 119 CZ2 TRP D 15 3755 4507 4204 -110 1598 -773 C ATOM 120 CZ3 TRP A 15 82.194 21.201 55.182 1.00 33.75 C ANISOU 120 CZ3 TRP D 15 4283 5014 3525 -980 862 188 C ATOM 121 CH2 TRP A 15 82.958 22.379 55.267 1.00 35.37 C ANISOU 121 CH2 TRP D 15 4813 4770 3856 -814 679 -158 C ATOM 122 N ALA A 16 82.492 16.496 54.754 1.00 30.94 N ANISOU 122 N ALA D 16 4454 4063 3239 -229 793 488 N ATOM 123 CA ALA A 16 81.406 16.585 55.740 1.00 29.29 C ANISOU 123 CA ALA D 16 3856 4129 3145 116 1164 397 C ATOM 124 C ALA A 16 81.781 15.895 57.040 1.00 29.05 C ANISOU 124 C ALA D 16 3699 4539 2798 -316 790 36 C ATOM 125 O ALA A 16 81.620 16.385 58.155 1.00 33.29 O ANISOU 125 O ALA D 16 4768 4944 2935 -1247 418 291 O ATOM 126 CB ALA A 16 80.164 15.961 55.125 1.00 26.10 C ANISOU 126 CB ALA D 16 2751 4510 2657 366 -21 59 C ATOM 127 N ALA A 17 82.324 14.680 56.910 1.00 30.90 N ANISOU 127 N ALA D 17 3685 4787 3270 -548 1021 78 N ATOM 128 CA ALA A 17 82.740 13.952 58.109 1.00 29.58 C ANISOU 128 CA ALA D 17 3656 4664 2920 9 781 291 C ATOM 129 C ALA A 17 83.835 14.722 58.828 1.00 30.77 C ANISOU 129 C ALA D 17 3429 4455 3808 304 1037 159 C ATOM 130 O ALA A 17 83.811 14.851 60.066 1.00 33.56 O ANISOU 130 O ALA D 17 5242 3549 3961 322 391 -19 O ATOM 131 CB ALA A 17 83.164 12.543 57.733 1.00 31.67 C ANISOU 131 CB ALA D 17 3817 5595 2621 -705 945 938 C ATOM 132 N ARG A 18 84.817 15.275 58.136 1.00 33.37 N ANISOU 132 N ARG D 18 4138 4690 3852 -305 976 359 N ATOM 133 CA ARG A 18 85.850 16.059 58.813 1.00 32.76 C ANISOU 133 CA ARG D 18 3847 4462 4140 76 1273 399 C ATOM 134 C ARG A 18 85.241 17.282 59.499 1.00 31.33 C ANISOU 134 C ARG D 18 4125 3797 3982 276 1024 85 C ATOM 135 O ARG A 18 85.689 17.656 60.608 1.00 36.95 O ANISOU 135 O ARG D 18 4887 4509 4643 82 1079 -703 O ATOM 136 CB ARG A 18 86.930 16.470 57.815 1.00 33.91 C ANISOU 136 CB ARG D 18 3988 4728 4170 240 1013 497 C ATOM 137 CG ARG A 18 88.153 17.122 58.452 1.00 37.46 C ANISOU 137 CG ARG D 18 4925 4534 4776 327 1308 593 C ATOM 138 CD ARG A 18 89.200 17.429 57.378 1.00 41.00 C ANISOU 138 CD ARG D 18 5949 4767 4862 140 1220 802 C ATOM 139 NE ARG A 18 88.750 18.512 56.497 1.00 45.31 N ANISOU 139 NE ARG D 18 6946 5829 4442 -324 1671 479 N ATOM 140 CZ ARG A 18 89.467 19.105 55.565 1.00 50.53 C ANISOU 140 CZ ARG D 18 7873 6006 5319 -150 2270 950 C ATOM 141 NH1 ARG A 18 90.721 18.723 55.358 1.00 60.56 N ANISOU 141 NH1 ARG D 18 8888 7188 6934 529 1145 1804 N ATOM 142 NH2 ARG A 18 88.931 20.074 54.841 1.00 58.04 N ANISOU 142 NH2 ARG D 18 9870 5866 6316 -870 4164 -161 N ATOM 143 N HIS A 19 84.239 17.916 58.890 1.00 30.93 N ANISOU 143 N HIS D 19 4001 3875 3875 385 985 358 N ATOM 144 CA HIS A 19 83.574 19.083 59.485 1.00 29.19 C ANISOU 144 CA HIS D 19 4131 3571 3390 299 962 56 C ATOM 145 C HIS A 19 82.913 18.686 60.803 1.00 30.19 C ANISOU 145 C HIS D 19 4403 3642 3426 10 894 90 C ATOM 146 O HIS A 19 83.037 19.304 61.867 1.00 36.06 O ANISOU 146 O HIS D 19 6311 3812 3577 -286 289 203 O ATOM 147 CB HIS A 19 82.545 19.689 58.519 1.00 28.79 C ANISOU 147 CB HIS D 19 4045 3511 3382 510 825 102 C ATOM 148 CG HIS A 19 82.020 21.012 58.979 1.00 30.50 C ANISOU 148 CG HIS D 19 4090 3803 3695 373 813 -201 C ATOM 149 ND1 HIS A 19 82.789 22.144 59.086 1.00 33.56 N ANISOU 149 ND1 HIS D 19 4787 3990 3973 -5 382 44 N ATOM 150 CD2 HIS A 19 80.776 21.397 59.378 1.00 31.72 C ANISOU 150 CD2 HIS D 19 3922 3984 4146 448 549 -610 C ATOM 151 CE1 HIS A 19 82.068 23.165 59.517 1.00 34.20 C ANISOU 151 CE1 HIS D 19 4915 4265 3813 -128 130 -220 C ATOM 152 NE2 HIS A 19 80.835 22.732 59.704 1.00 34.50 N ANISOU 152 NE2 HIS D 19 4320 4316 4472 92 236 -445 N ATOM 153 N ILE A 20 82.168 17.579 60.745 1.00 33.50 N ANISOU 153 N ILE D 20 4840 4222 3665 -726 1231 153 N ATOM 154 CA ILE A 20 81.490 17.058 61.946 1.00 32.34 C ANISOU 154 CA ILE D 20 4869 3846 3575 -275 1542 -52 C ATOM 155 C ILE A 20 82.521 16.807 63.034 1.00 33.02 C ANISOU 155 C ILE D 20 4689 4221 3637 -170 1282 -341 C ATOM 156 O ILE A 20 82.334 17.286 64.156 1.00 35.06 O ANISOU 156 O ILE D 20 5147 4395 3778 -369 1052 -545 O ATOM 157 CB ILE A 20 80.676 15.792 61.614 1.00 31.64 C ANISOU 157 CB ILE D 20 4972 3796 3253 -249 1104 99 C ATOM 158 CG1 ILE A 20 79.482 16.046 60.685 1.00 27.21 C ANISOU 158 CG1 ILE D 20 4083 3578 2679 -480 788 382 C ATOM 159 CG2 ILE A 20 80.237 15.101 62.895 1.00 30.74 C ANISOU 159 CG2 ILE D 20 4222 4101 3356 -234 1397 63 C ATOM 160 CD1 ILE A 20 78.812 14.811 60.124 1.00 27.95 C ANISOU 160 CD1 ILE D 20 3960 3676 2983 -143 98 227 C ATOM 161 N VAL A 21 83.589 16.098 62.699 1.00 33.86 N ANISOU 161 N VAL D 21 4471 4460 3934 -273 1515 -76 N ATOM 162 CA VAL A 21 84.639 15.789 63.670 1.00 34.17 C ANISOU 162 CA VAL D 21 4534 4381 4068 -123 1204 -318 C ATOM 163 C VAL A 21 85.230 17.050 64.290 1.00 36.10 C ANISOU 163 C VAL D 21 5749 4619 3350 -662 814 77 C ATOM 164 O VAL A 21 85.456 17.198 65.498 1.00 37.00 O ANISOU 164 O VAL D 21 6030 4317 3713 -347 2338 -810 O ATOM 165 CB VAL A 21 85.752 14.954 63.000 1.00 37.20 C ANISOU 165 CB VAL D 21 4646 4993 4495 100 1086 -325 C ATOM 166 CG1 VAL A 21 86.993 14.926 63.894 1.00 33.39 C ANISOU 166 CG1 VAL D 21 3606 5524 3557 -231 1759 143 C ATOM 167 CG2 VAL A 21 85.243 13.557 62.675 1.00 37.04 C ANISOU 167 CG2 VAL D 21 4146 5571 4354 -179 1433 -119 C ATOM 168 N ASN A 22 85.505 18.035 63.442 1.00 35.42 N ANISOU 168 N ASN D 22 5578 4810 3072 -833 684 -45 N ATOM 169 CA ASN A 22 86.088 19.270 63.954 1.00 36.23 C ANISOU 169 CA ASN D 22 5802 4366 3596 -598 428 13 C ATOM 170 C ASN A 22 85.095 20.015 64.828 1.00 35.13 C ANISOU 170 C ASN D 22 5692 4331 3324 -622 502 -178 C ATOM 171 O ASN A 22 85.467 20.605 65.846 1.00 37.68 O ANISOU 171 O ASN D 22 5612 5340 3365 -947 734 -548 O ATOM 172 CB ASN A 22 86.581 20.112 62.775 1.00 39.79 C ANISOU 172 CB ASN D 22 6436 4639 4041 -967 142 475 C ATOM 173 CG ASN A 22 87.796 19.518 62.081 1.00 45.83 C ANISOU 173 CG ASN D 22 7258 5374 4783 -947 -662 925 C ATOM 174 OD1 ASN A 22 88.198 20.047 61.045 1.00 54.80 O ANISOU 174 OD1 ASN D 22 8143 7299 5378 -1210 -963 2065 O ATOM 175 ND2 ASN A 22 88.405 18.455 62.591 1.00 45.89 N ANISOU 175 ND2 ASN D 22 7308 5443 4685 354 -589 472 N ATOM 176 N ARG A 23 83.806 20.017 64.496 1.00 35.83 N ANISOU 176 N ARG D 23 5833 4392 3389 -470 976 198 N ATOM 177 CA ARG A 23 82.866 20.667 65.410 1.00 33.81 C ANISOU 177 CA ARG D 23 5251 4775 2818 -351 1334 -299 C ATOM 178 C ARG A 23 82.815 19.930 66.736 1.00 34.96 C ANISOU 178 C ARG D 23 5254 5289 2741 -722 1197 -306 C ATOM 179 O ARG A 23 82.817 20.556 67.794 1.00 36.82 O ANISOU 179 O ARG D 23 5818 5426 2745 -279 1168 -752 O ATOM 180 CB ARG A 23 81.465 20.701 64.797 1.00 35.25 C ANISOU 180 CB ARG D 23 5146 4909 3337 -363 1235 -638 C ATOM 181 CG ARG A 23 81.456 21.701 63.657 1.00 30.89 C ANISOU 181 CG ARG D 23 4207 4471 3060 112 732 -412 C ATOM 182 CD ARG A 23 81.601 23.130 64.202 1.00 38.51 C ANISOU 182 CD ARG D 23 5582 5100 3950 -1057 249 -41 C ATOM 183 NE ARG A 23 81.213 24.042 63.112 1.00 40.05 N ANISOU 183 NE ARG D 23 4953 5583 4681 -1159 237 382 N ATOM 184 CZ ARG A 23 81.794 25.198 62.827 1.00 46.54 C ANISOU 184 CZ ARG D 23 6432 5918 5332 -1957 791 -23 C ATOM 185 NH1 ARG A 23 82.819 25.596 63.585 1.00 45.47 N ANISOU 185 NH1 ARG D 23 6255 5597 5424 -1602 1236 316 N ATOM 186 NH2 ARG A 23 81.346 25.923 61.806 1.00 39.35 N ANISOU 186 NH2 ARG D 23 5844 4406 4700 -1401 167 496 N ATOM 187 N ILE A 24 82.767 18.597 66.677 1.00 36.60 N ANISOU 187 N ILE D 24 5032 5082 3794 -531 1463 -307 N ATOM 188 CA ILE A 24 82.726 17.863 67.936 1.00 36.12 C ANISOU 188 CA ILE D 24 4944 4952 3828 -444 1575 -410 C ATOM 189 C ILE A 24 83.992 18.089 68.746 1.00 37.86 C ANISOU 189 C ILE D 24 5388 5292 3707 -139 1001 -707 C ATOM 190 O ILE A 24 83.992 18.310 69.961 1.00 43.09 O ANISOU 190 O ILE D 24 6870 5635 3868 -744 545 -885 O ATOM 191 CB ILE A 24 82.535 16.359 67.676 1.00 33.76 C ANISOU 191 CB ILE D 24 4106 5106 3616 84 1724 -768 C ATOM 192 CG1 ILE A 24 81.159 16.018 67.115 1.00 32.78 C ANISOU 192 CG1 ILE D 24 4389 4766 3300 68 1392 -388 C ATOM 193 CG2 ILE A 24 82.831 15.560 68.954 1.00 35.69 C ANISOU 193 CG2 ILE D 24 3904 6526 3130 -272 1273 -1019 C ATOM 194 CD1 ILE A 24 81.057 14.666 66.463 1.00 33.70 C ANISOU 194 CD1 ILE D 24 4440 4508 3855 -216 1429 -75 C ATOM 195 N ASN A 25 85.163 18.042 68.106 1.00 39.70 N ANISOU 195 N ASN D 25 5448 5176 4462 -73 823 -715 N ATOM 196 CA ASN A 25 86.379 18.138 68.920 1.00 38.29 C ANISOU 196 CA ASN D 25 4951 5480 4118 -75 1363 -477 C ATOM 197 C ASN A 25 86.539 19.549 69.456 1.00 38.36 C ANISOU 197 C ASN D 25 5064 5487 4025 -82 1665 -1018 C ATOM 198 O ASN A 25 87.076 19.791 70.547 1.00 45.52 O ANISOU 198 O ASN D 25 6670 6190 4436 -504 2035 -1597 O ATOM 199 CB ASN A 25 87.587 17.649 68.118 1.00 38.75 C ANISOU 199 CB ASN D 25 5514 5043 4167 -147 1240 -254 C ATOM 200 CG ASN A 25 87.628 16.141 67.939 1.00 37.94 C ANISOU 200 CG ASN D 25 4753 5011 4650 399 1590 199 C ATOM 201 OD1 ASN A 25 87.024 15.400 68.721 1.00 43.68 O ANISOU 201 OD1 ASN D 25 5939 5284 5373 -193 1400 577 O ATOM 202 ND2 ASN A 25 88.314 15.608 66.938 1.00 38.06 N ANISOU 202 ND2 ASN D 25 5159 4318 4983 639 1083 -371 N ATOM 203 N ALA A 26 86.058 20.573 68.754 1.00 39.03 N ANISOU 203 N ALA D 26 5387 5650 3794 -559 1731 -124 N ATOM 204 CA ALA A 26 86.243 21.922 69.307 1.00 39.56 C ANISOU 204 CA ALA D 26 5776 5022 4232 -740 1787 -16 C ATOM 205 C ALA A 26 85.276 22.195 70.448 1.00 39.68 C ANISOU 205 C ALA D 26 6338 4625 4112 -760 1116 -698 C ATOM 206 O ALA A 26 85.566 22.993 71.328 1.00 47.53 O ANISOU 206 O ALA D 26 9724 4861 3475 -1902 1068 -498 O ATOM 207 CB ALA A 26 86.042 22.970 68.223 1.00 36.18 C ANISOU 207 CB ALA D 26 5123 4342 4282 -55 1936 -723 C ATOM 208 N PHE A 27 84.122 21.535 70.410 1.00 38.35 N ANISOU 208 N PHE D 27 5942 4615 4013 -405 1029 -920 N ATOM 209 CA PHE A 27 83.073 21.715 71.405 1.00 40.04 C ANISOU 209 CA PHE D 27 6188 5010 4013 -384 1177 -579 C ATOM 210 C PHE A 27 83.410 21.026 72.723 1.00 41.26 C ANISOU 210 C PHE D 27 6808 4817 4051 -346 1448 -885 C ATOM 211 O PHE A 27 83.011 21.512 73.781 1.00 41.16 O ANISOU 211 O PHE D 27 7394 4144 4103 -954 1316 -139 O ATOM 212 CB PHE A 27 81.759 21.144 70.896 1.00 37.50 C ANISOU 212 CB PHE D 27 5627 5273 3349 184 623 -681 C ATOM 213 CG PHE A 27 80.515 21.295 71.751 1.00 36.10 C ANISOU 213 CG PHE D 27 4925 5379 3413 -351 584 -349 C ATOM 214 CD1 PHE A 27 79.703 22.400 71.581 1.00 36.57 C ANISOU 214 CD1 PHE D 27 4890 5474 3529 -493 506 -721 C ATOM 215 CD2 PHE A 27 80.166 20.344 72.694 1.00 37.55 C ANISOU 215 CD2 PHE D 27 5136 5593 3540 -1063 296 -375 C ATOM 216 CE1 PHE A 27 78.568 22.554 72.336 1.00 37.05 C ANISOU 216 CE1 PHE D 27 4493 5781 3805 -495 810 -343 C ATOM 217 CE2 PHE A 27 79.016 20.487 73.454 1.00 38.14 C ANISOU 217 CE2 PHE D 27 4737 5829 3926 -1438 374 177 C ATOM 218 CZ PHE A 27 78.203 21.591 73.264 1.00 39.50 C ANISOU 218 CZ PHE D 27 4809 6140 4058 -1157 437 -99 C ATOM 219 N LYS A 28 84.119 19.910 72.626 1.00 44.61 N ANISOU 219 N LYS D 28 6756 5747 4445 -570 1777 -641 N ATOM 220 CA LYS A 28 84.552 19.169 73.814 1.00 46.21 C ANISOU 220 CA LYS D 28 7387 5462 4708 -684 2205 -620 C ATOM 221 C LYS A 28 83.373 18.710 74.669 1.00 44.35 C ANISOU 221 C LYS D 28 7283 5607 3960 -986 1123 -833 C ATOM 222 O LYS A 28 83.204 19.185 75.795 1.00 49.03 O ANISOU 222 O LYS D 28 8259 6865 3505 -1735 1498 -1172 O ATOM 223 CB LYS A 28 85.499 20.029 74.661 1.00 52.78 C ANISOU 223 CB LYS D 28 8806 5571 5675 -713 2907 -1237 C ATOM 224 CG LYS A 28 86.841 20.264 73.999 1.00 62.04 C ANISOU 224 CG LYS D 28 10735 5380 7459 -1095 2638 -533 C ATOM 225 CD LYS A 28 87.259 21.730 74.005 1.00 83.37 C ANISOU 225 CD LYS D 28 14704 6945 10028 -3815 2545 -213 C ATOM 226 CE LYS A 28 87.868 22.145 72.670 1.00 92.61 C ANISOU 226 CE LYS D 28 16511 7514 11163 -4622 2424 933 C ATOM 227 NZ LYS A 28 87.783 23.605 72.383 1.00103.41 N ANISOU 227 NZ LYS D 28 18273 7587 13433 -5443 6133 -1423 N ATOM 228 N PRO A 29 82.573 17.796 74.130 1.00 39.46 N ANISOU 228 N PRO D 29 5785 5362 3845 -424 1002 -725 N ATOM 229 CA PRO A 29 81.321 17.391 74.768 1.00 37.54 C ANISOU 229 CA PRO D 29 5009 5543 3711 -230 939 -695 C ATOM 230 C PRO A 29 81.560 16.570 76.026 1.00 41.25 C ANISOU 230 C PRO D 29 6231 5831 3612 -708 1172 -774 C ATOM 231 O PRO A 29 82.567 15.867 76.104 1.00 43.73 O ANISOU 231 O PRO D 29 5745 6606 4264 -1134 1934 -461 O ATOM 232 CB PRO A 29 80.675 16.494 73.700 1.00 35.65 C ANISOU 232 CB PRO D 29 4574 5268 3702 -35 1111 -669 C ATOM 233 CG PRO A 29 81.853 15.922 72.970 1.00 36.41 C ANISOU 233 CG PRO D 29 5121 5152 3560 33 908 -576 C ATOM 234 CD PRO A 29 82.815 17.081 72.862 1.00 38.15 C ANISOU 234 CD PRO D 29 5260 5248 3985 -108 942 -559 C ATOM 235 N THR A 30 80.627 16.672 76.966 1.00 45.50 N ANISOU 235 N THR D 30 7490 6010 3786 -1299 469 -481 N ATOM 236 CA THR A 30 80.673 15.860 78.176 1.00 46.83 C ANISOU 236 CA THR D 30 7609 6480 3702 -1843 299 -454 C ATOM 237 C THR A 30 79.295 15.275 78.477 1.00 50.02 C ANISOU 237 C THR D 30 8268 6557 4179 -1744 797 -198 C ATOM 238 O THR A 30 78.312 15.600 77.806 1.00 52.51 O ANISOU 238 O THR D 30 8664 6438 4849 -1677 1162 -222 O ATOM 239 CB THR A 30 81.153 16.664 79.399 1.00 44.09 C ANISOU 239 CB THR D 30 6711 6582 3459 -1159 -332 -109 C ATOM 240 OG1 THR A 30 80.224 17.723 79.650 1.00 46.64 O ANISOU 240 OG1 THR D 30 6551 7076 4093 -953 237 201 O ATOM 241 CG2 THR A 30 82.496 17.320 79.122 1.00 42.08 C ANISOU 241 CG2 THR D 30 7296 6431 2261 -443 1449 -777 C ATOM 242 N ALA A 31 79.249 14.417 79.496 1.00 52.97 N ANISOU 242 N ALA D 31 8827 7004 4296 -1634 985 127 N ATOM 243 CA ALA A 31 78.018 13.757 79.912 1.00 53.78 C ANISOU 243 CA ALA D 31 9115 6975 4346 -1331 1698 68 C ATOM 244 C ALA A 31 76.894 14.769 80.120 1.00 54.14 C ANISOU 244 C ALA D 31 9096 7145 4330 -1356 1670 468 C ATOM 245 O ALA A 31 75.743 14.507 79.779 1.00 56.11 O ANISOU 245 O ALA D 31 9632 7247 4442 -738 -88 303 O ATOM 246 CB ALA A 31 78.235 12.955 81.191 1.00 55.18 C ANISOU 246 CB ALA D 31 9035 7432 4499 -1937 1730 -40 C ATOM 247 N ASP A 32 77.258 15.915 80.690 1.00 54.17 N ANISOU 247 N ASP D 32 8981 7218 4383 -1307 1864 231 N ATOM 248 CA ASP A 32 76.288 16.948 81.044 1.00 56.83 C ANISOU 248 CA ASP D 32 9268 7418 4908 -1227 1294 339 C ATOM 249 C ASP A 32 76.202 18.049 79.991 1.00 53.60 C ANISOU 249 C ASP D 32 8274 6953 5141 -1152 740 731 C ATOM 250 O ASP A 32 75.331 18.924 80.072 1.00 51.86 O ANISOU 250 O ASP D 32 8029 7728 3949 -1792 -388 384 O ATOM 251 CB ASP A 32 76.635 17.526 82.419 1.00 62.94 C ANISOU 251 CB ASP D 32 10524 8347 5042 -1065 743 143 C ATOM 252 CG ASP A 32 76.349 16.521 83.526 1.00 73.31 C ANISOU 252 CG ASP D 32 14176 8786 4892 -2321 1926 -630 C ATOM 253 OD1 ASP A 32 75.293 15.838 83.496 1.00 85.57 O ANISOU 253 OD1 ASP D 32 18137 8895 5480 -4880 594 -885 O ATOM 254 OD2 ASP A 32 77.181 16.386 84.457 1.00102.79 O ANISOU 254 OD2 ASP D 32 18775 12167 8113 -4367 5851 -3177 O ATOM 255 N ARG A 33 77.095 18.007 79.005 1.00 47.75 N ANISOU 255 N ARG D 33 7703 6550 3890 -716 804 -507 N ATOM 256 CA ARG A 33 77.043 18.959 77.900 1.00 44.00 C ANISOU 256 CA ARG D 33 6663 6144 3912 -801 287 -402 C ATOM 257 C ARG A 33 77.423 18.205 76.625 1.00 42.40 C ANISOU 257 C ARG D 33 6310 5814 3985 -788 346 -194 C ATOM 258 O ARG A 33 78.567 18.289 76.172 1.00 42.09 O ANISOU 258 O ARG D 33 6755 5625 3612 -979 834 113 O ATOM 259 CB ARG A 33 77.948 20.171 78.113 1.00 46.13 C ANISOU 259 CB ARG D 33 6191 6304 5030 -675 436 -1107 C ATOM 260 CG ARG A 33 77.492 21.379 77.310 1.00 48.91 C ANISOU 260 CG ARG D 33 5890 6223 6471 -488 610 -650 C ATOM 261 CD ARG A 33 78.575 22.454 77.237 1.00 50.23 C ANISOU 261 CD ARG D 33 5725 6018 7342 -54 992 -652 C ATOM 262 NE ARG A 33 79.856 21.845 76.931 1.00 54.48 N ANISOU 262 NE ARG D 33 6214 6723 7762 313 312 -655 N ATOM 263 CZ ARG A 33 80.760 22.177 76.028 1.00 51.40 C ANISOU 263 CZ ARG D 33 5936 6491 7104 380 692 -1028 C ATOM 264 NH1 ARG A 33 80.642 23.192 75.194 1.00 45.95 N ANISOU 264 NH1 ARG D 33 5864 5661 5935 -359 383 -2613 N ATOM 265 NH2 ARG A 33 81.850 21.415 75.987 1.00 51.57 N ANISOU 265 NH2 ARG D 33 6382 6499 6714 886 1086 -1189 N ATOM 266 N PRO A 34 76.446 17.466 76.113 1.00 38.08 N ANISOU 266 N PRO D 34 5036 5895 3539 -293 777 -377 N ATOM 267 CA PRO A 34 76.670 16.693 74.893 1.00 37.24 C ANISOU 267 CA PRO D 34 5165 5475 3510 -542 698 62 C ATOM 268 C PRO A 34 76.659 17.568 73.644 1.00 37.15 C ANISOU 268 C PRO D 34 4964 5495 3654 -911 572 154 C ATOM 269 O PRO A 34 76.032 18.622 73.641 1.00 34.83 O ANISOU 269 O PRO D 34 4961 4858 3415 -1190 232 197 O ATOM 270 CB PRO A 34 75.447 15.767 74.855 1.00 34.64 C ANISOU 270 CB PRO D 34 3958 5439 3767 -423 591 302 C ATOM 271 CG PRO A 34 74.372 16.541 75.557 1.00 34.98 C ANISOU 271 CG PRO D 34 4129 5589 3573 -786 -2 -77 C ATOM 272 CD PRO A 34 75.086 17.293 76.641 1.00 35.93 C ANISOU 272 CD PRO D 34 4820 5946 2885 -437 898 -291 C ATOM 273 N PHE A 35 77.324 17.121 72.590 1.00 33.50 N ANISOU 273 N PHE D 35 4323 4795 3610 -209 1093 92 N ATOM 274 CA PHE A 35 77.203 17.666 71.245 1.00 34.47 C ANISOU 274 CA PHE D 35 4715 4901 3480 -303 1108 -166 C ATOM 275 C PHE A 35 75.984 17.039 70.583 1.00 30.80 C ANISOU 275 C PHE D 35 3745 4708 3249 -133 283 80 C ATOM 276 O PHE A 35 75.861 15.808 70.522 1.00 34.69 O ANISOU 276 O PHE D 35 4370 5498 3313 -953 865 102 O ATOM 277 CB PHE A 35 78.444 17.360 70.426 1.00 31.19 C ANISOU 277 CB PHE D 35 4628 4378 2845 -147 1408 -659 C ATOM 278 CG PHE A 35 78.443 18.103 69.088 1.00 32.85 C ANISOU 278 CG PHE D 35 4726 4756 2998 -563 1396 -552 C ATOM 279 CD1 PHE A 35 78.957 19.382 69.015 1.00 34.09 C ANISOU 279 CD1 PHE D 35 4555 4989 3409 -659 1006 -231 C ATOM 280 CD2 PHE A 35 77.931 17.492 67.962 1.00 32.16 C ANISOU 280 CD2 PHE D 35 4104 5072 3044 -292 1803 -911 C ATOM 281 CE1 PHE A 35 78.960 20.074 67.819 1.00 36.47 C ANISOU 281 CE1 PHE D 35 5383 4816 3659 -970 1408 -344 C ATOM 282 CE2 PHE A 35 77.935 18.187 66.755 1.00 32.59 C ANISOU 282 CE2 PHE D 35 4209 5400 2773 -710 1003 -232 C ATOM 283 CZ PHE A 35 78.456 19.473 66.677 1.00 31.87 C ANISOU 283 CZ PHE D 35 4006 4644 3461 -139 1146 -158 C ATOM 284 N VAL A 36 75.072 17.860 70.084 1.00 31.61 N ANISOU 284 N VAL D 36 4174 4493 3343 -147 942 418 N ATOM 285 CA VAL A 36 73.825 17.338 69.533 1.00 31.43 C ANISOU 285 CA VAL D 36 4778 4483 2682 123 698 564 C ATOM 286 C VAL A 36 73.868 17.405 68.007 1.00 32.63 C ANISOU 286 C VAL D 36 5038 4700 2660 -862 252 757 C ATOM 287 O VAL A 36 74.035 18.502 67.451 1.00 32.32 O ANISOU 287 O VAL D 36 4713 5181 2386 -1089 704 -255 O ATOM 288 CB VAL A 36 72.596 18.073 70.095 1.00 31.27 C ANISOU 288 CB VAL D 36 4827 4559 2494 99 136 -277 C ATOM 289 CG1 VAL A 36 71.313 17.442 69.571 1.00 27.48 C ANISOU 289 CG1 VAL D 36 3380 4632 2430 -165 -163 -417 C ATOM 290 CG2 VAL A 36 72.619 18.061 71.638 1.00 28.93 C ANISOU 290 CG2 VAL D 36 3655 4842 2496 -270 474 -500 C ATOM 291 N LEU A 37 73.736 16.245 67.374 1.00 30.67 N ANISOU 291 N LEU D 37 4517 4144 2994 -623 685 483 N ATOM 292 CA LEU A 37 73.930 16.051 65.949 1.00 28.29 C ANISOU 292 CA LEU D 37 3603 4101 3043 -644 539 372 C ATOM 293 C LEU A 37 72.646 15.590 65.277 1.00 28.55 C ANISOU 293 C LEU D 37 3493 4173 3181 -461 441 330 C ATOM 294 O LEU A 37 72.166 14.524 65.670 1.00 29.10 O ANISOU 294 O LEU D 37 3783 3994 3281 -337 844 224 O ATOM 295 CB LEU A 37 74.936 14.944 65.686 1.00 32.82 C ANISOU 295 CB LEU D 37 3775 4139 4557 -272 387 425 C ATOM 296 CG LEU A 37 76.107 15.012 64.723 1.00 32.63 C ANISOU 296 CG LEU D 37 3723 5069 3608 -636 -25 474 C ATOM 297 CD1 LEU A 37 76.499 13.594 64.310 1.00 32.91 C ANISOU 297 CD1 LEU D 37 4935 4662 2905 -2002 -779 347 C ATOM 298 CD2 LEU A 37 75.884 15.872 63.493 1.00 28.13 C ANISOU 298 CD2 LEU D 37 4074 4126 2488 234 -64 -1156 C ATOM 299 N GLY A 38 72.139 16.321 64.296 1.00 29.00 N ANISOU 299 N GLY D 38 3598 4227 3192 -802 506 96 N ATOM 300 CA GLY A 38 70.967 15.879 63.547 1.00 27.79 C ANISOU 300 CA GLY D 38 3542 4232 2786 -519 8 203 C ATOM 301 C GLY A 38 71.422 15.142 62.285 1.00 28.30 C ANISOU 301 C GLY D 38 3406 4072 3273 -349 -292 388 C ATOM 302 O GLY A 38 72.412 15.541 61.656 1.00 26.56 O ANISOU 302 O GLY D 38 3348 4128 2614 -59 648 328 O ATOM 303 N LEU A 39 70.731 14.060 61.926 1.00 26.66 N ANISOU 303 N LEU D 39 3158 3916 3056 106 -40 -130 N ATOM 304 CA LEU A 39 71.220 13.160 60.893 1.00 26.08 C ANISOU 304 CA LEU D 39 2896 3741 3271 159 -45 -11 C ATOM 305 C LEU A 39 70.153 12.724 59.912 1.00 25.74 C ANISOU 305 C LEU D 39 3267 3450 3064 -333 27 177 C ATOM 306 O LEU A 39 68.992 12.558 60.273 1.00 27.38 O ANISOU 306 O LEU D 39 3133 3840 3430 335 36 -56 O ATOM 307 CB LEU A 39 71.791 11.891 61.558 1.00 28.35 C ANISOU 307 CB LEU D 39 3119 4457 3196 -71 160 283 C ATOM 308 CG LEU A 39 73.047 12.127 62.398 1.00 29.90 C ANISOU 308 CG LEU D 39 3207 4583 3570 -75 755 292 C ATOM 309 CD1 LEU A 39 73.548 10.816 63.012 1.00 28.57 C ANISOU 309 CD1 LEU D 39 3188 5131 2536 -340 361 570 C ATOM 310 CD2 LEU A 39 74.152 12.791 61.579 1.00 29.84 C ANISOU 310 CD2 LEU D 39 3316 4361 3659 -386 957 143 C ATOM 311 N PRO A 40 70.513 12.533 58.658 1.00 27.30 N ANISOU 311 N PRO D 40 3357 4166 2850 -156 495 260 N ATOM 312 CA PRO A 40 69.617 11.953 57.658 1.00 27.80 C ANISOU 312 CA PRO D 40 3695 4172 2697 -269 673 271 C ATOM 313 C PRO A 40 69.978 10.538 57.237 1.00 29.36 C ANISOU 313 C PRO D 40 3953 3855 3348 -565 426 409 C ATOM 314 O PRO A 40 71.013 9.990 57.640 1.00 28.16 O ANISOU 314 O PRO D 40 3646 3956 3097 -554 -80 202 O ATOM 315 CB PRO A 40 69.926 12.896 56.475 1.00 26.34 C ANISOU 315 CB PRO D 40 3850 3430 2729 -341 378 300 C ATOM 316 CG PRO A 40 71.408 13.067 56.584 1.00 26.74 C ANISOU 316 CG PRO D 40 3569 3895 2697 62 756 21 C ATOM 317 CD PRO A 40 71.793 12.930 58.046 1.00 26.74 C ANISOU 317 CD PRO D 40 3568 4218 2373 -160 163 111 C ATOM 318 N THR A 41 69.125 9.943 56.410 1.00 30.65 N ANISOU 318 N THR D 41 4076 4449 3119 -593 654 129 N ATOM 319 CA THR A 41 69.342 8.608 55.881 1.00 32.57 C ANISOU 319 CA THR D 41 4423 4492 3462 -721 316 55 C ATOM 320 C THR A 41 69.326 8.685 54.354 1.00 34.25 C ANISOU 320 C THR D 41 4493 5077 3445 -735 278 149 C ATOM 321 O THR A 41 69.215 9.782 53.793 1.00 39.20 O ANISOU 321 O THR D 41 4684 6525 3685 -983 561 213 O ATOM 322 CB THR A 41 68.312 7.558 56.340 1.00 33.71 C ANISOU 322 CB THR D 41 5253 4338 3216 -1003 374 -341 C ATOM 323 OG1 THR A 41 67.011 7.952 55.884 1.00 36.62 O ANISOU 323 OG1 THR D 41 6285 4357 3273 -747 1025 -314 O ATOM 324 CG2 THR A 41 68.185 7.452 57.847 1.00 31.31 C ANISOU 324 CG2 THR D 41 5179 3499 3219 550 189 -159 C ATOM 325 N GLY A 42 69.438 7.555 53.682 1.00 36.09 N ANISOU 325 N GLY D 42 4541 5612 3561 -598 114 26 N ATOM 326 CA GLY A 42 69.403 7.472 52.241 1.00 36.71 C ANISOU 326 CA GLY D 42 4990 5433 3523 -684 16 166 C ATOM 327 C GLY A 42 70.774 7.338 51.627 1.00 35.57 C ANISOU 327 C GLY D 42 4942 5088 3485 -742 147 -25 C ATOM 328 O GLY A 42 71.806 7.248 52.260 1.00 35.05 O ANISOU 328 O GLY D 42 5529 4786 3001 -940 306 113 O ATOM 329 N GLY A 43 70.830 7.315 50.298 1.00 34.07 N ANISOU 329 N GLY D 43 4938 4519 3487 -272 530 59 N ATOM 330 CA GLY A 43 72.094 7.138 49.594 1.00 33.79 C ANISOU 330 CA GLY D 43 4362 4499 3976 -767 424 439 C ATOM 331 C GLY A 43 72.996 8.352 49.732 1.00 31.78 C ANISOU 331 C GLY D 43 4012 4468 3594 -551 440 29 C ATOM 332 O GLY A 43 74.219 8.209 49.712 1.00 32.96 O ANISOU 332 O GLY D 43 4103 4546 3873 -467 797 284 O ATOM 333 N THR A 44 72.432 9.546 49.868 1.00 30.70 N ANISOU 333 N THR D 44 3928 4790 2946 -615 788 -67 N ATOM 334 CA THR A 44 73.251 10.759 49.895 1.00 31.56 C ANISOU 334 CA THR D 44 4083 4857 3050 -743 580 -30 C ATOM 335 C THR A 44 74.253 10.803 51.026 1.00 27.57 C ANISOU 335 C THR D 44 3397 4242 2838 -98 107 451 C ATOM 336 O THR A 44 75.431 11.086 50.762 1.00 29.25 O ANISOU 336 O THR D 44 2870 4461 3782 -108 348 1007 O ATOM 337 CB THR A 44 72.339 12.010 49.960 1.00 32.96 C ANISOU 337 CB THR D 44 4063 4366 4094 -645 1021 -659 C ATOM 338 OG1 THR A 44 71.660 12.137 48.698 1.00 40.12 O ANISOU 338 OG1 THR D 44 5055 5581 4609 -1401 1930 -1118 O ATOM 339 CG2 THR A 44 73.137 13.285 50.138 1.00 30.57 C ANISOU 339 CG2 THR D 44 4264 4209 3141 -760 433 432 C ATOM 340 N PRO A 45 73.920 10.592 52.297 1.00 27.52 N ANISOU 340 N PRO D 45 3448 4170 2840 -157 392 440 N ATOM 341 CA PRO A 45 74.978 10.611 53.308 1.00 28.21 C ANISOU 341 CA PRO D 45 3447 4269 3002 63 271 322 C ATOM 342 C PRO A 45 75.819 9.342 53.387 1.00 28.67 C ANISOU 342 C PRO D 45 3466 4244 3183 199 52 130 C ATOM 343 O PRO A 45 76.650 9.248 54.297 1.00 29.73 O ANISOU 343 O PRO D 45 3427 4747 3122 -639 856 110 O ATOM 344 CB PRO A 45 74.171 10.762 54.616 1.00 26.66 C ANISOU 344 CB PRO D 45 3291 3904 2934 -104 69 9 C ATOM 345 CG PRO A 45 72.842 10.123 54.323 1.00 26.85 C ANISOU 345 CG PRO D 45 3873 3958 2372 -165 -185 -94 C ATOM 346 CD PRO A 45 72.574 10.388 52.854 1.00 28.88 C ANISOU 346 CD PRO D 45 4611 3828 2536 -229 346 252 C ATOM 347 N MET A 46 75.709 8.328 52.544 1.00 31.24 N ANISOU 347 N MET D 46 3654 5111 3103 -530 326 104 N ATOM 348 CA MET A 46 76.523 7.114 52.723 1.00 32.62 C ANISOU 348 CA MET D 46 3597 4831 3968 -342 -49 882 C ATOM 349 C MET A 46 78.030 7.346 52.790 1.00 34.04 C ANISOU 349 C MET D 46 4307 4874 3754 -194 1028 833 C ATOM 350 O MET A 46 78.705 6.819 53.673 1.00 36.82 O ANISOU 350 O MET D 46 4296 5735 3957 -568 1120 309 O ATOM 351 CB MET A 46 76.304 6.084 51.602 1.00 32.57 C ANISOU 351 CB MET D 46 3155 5559 3662 142 294 281 C ATOM 352 CG MET A 46 74.932 5.437 51.623 1.00 39.33 C ANISOU 352 CG MET D 46 4828 5541 4573 142 -53 -347 C ATOM 353 SD MET A 46 74.805 4.304 53.022 1.00 54.33 S ANISOU 353 SD MET D 46 6699 6308 7636 -571 996 1817 S ATOM 354 CE MET A 46 75.814 2.944 52.450 1.00 56.96 C ANISOU 354 CE MET D 46 5802 8021 7819 43 2212 -1512 C ATOM 355 N THR A 47 78.612 8.126 51.874 1.00 32.40 N ANISOU 355 N THR D 47 3999 4720 3590 -566 433 774 N ATOM 356 CA THR A 47 80.067 8.281 51.975 1.00 31.89 C ANISOU 356 CA THR D 47 3595 4904 3620 -412 345 823 C ATOM 357 C THR A 47 80.437 9.086 53.211 1.00 32.90 C ANISOU 357 C THR D 47 4405 4460 3634 -205 58 935 C ATOM 358 O THR A 47 81.567 8.968 53.718 1.00 33.63 O ANISOU 358 O THR D 47 4046 4683 4048 -241 43 705 O ATOM 359 CB THR A 47 80.693 8.961 50.740 1.00 30.82 C ANISOU 359 CB THR D 47 4163 4178 3369 -198 1031 189 C ATOM 360 OG1 THR A 47 80.074 10.255 50.575 1.00 33.92 O ANISOU 360 OG1 THR D 47 4147 5056 3687 -660 646 709 O ATOM 361 CG2 THR A 47 80.495 8.164 49.449 1.00 31.26 C ANISOU 361 CG2 THR D 47 3715 4857 3305 -117 1007 160 C ATOM 362 N THR A 48 79.536 9.920 53.734 1.00 29.54 N ANISOU 362 N THR D 48 4228 3914 3080 -357 324 878 N ATOM 363 CA THR A 48 79.868 10.645 54.969 1.00 27.79 C ANISOU 363 CA THR D 48 3417 3989 3153 -39 813 442 C ATOM 364 C THR A 48 79.960 9.712 56.175 1.00 28.17 C ANISOU 364 C THR D 48 3178 4078 3446 -129 980 221 C ATOM 365 O THR A 48 80.889 9.810 56.973 1.00 30.90 O ANISOU 365 O THR D 48 4012 4516 3213 -461 995 -116 O ATOM 366 CB THR A 48 78.836 11.759 55.224 1.00 28.55 C ANISOU 366 CB THR D 48 3209 4227 3412 -173 1019 -331 C ATOM 367 OG1 THR A 48 78.883 12.700 54.145 1.00 29.67 O ANISOU 367 OG1 THR D 48 3288 4736 3250 -144 689 174 O ATOM 368 CG2 THR A 48 79.158 12.547 56.483 1.00 27.34 C ANISOU 368 CG2 THR D 48 3844 3330 3213 -240 602 305 C ATOM 369 N TYR A 49 79.019 8.795 56.345 1.00 29.41 N ANISOU 369 N TYR D 49 3728 4195 3251 -350 798 446 N ATOM 370 CA TYR A 49 79.006 7.807 57.420 1.00 29.62 C ANISOU 370 CA TYR D 49 3529 4508 3217 -357 716 488 C ATOM 371 C TYR A 49 80.240 6.913 57.313 1.00 31.06 C ANISOU 371 C TYR D 49 3479 4980 3342 -281 483 -129 C ATOM 372 O TYR A 49 80.946 6.644 58.290 1.00 32.01 O ANISOU 372 O TYR D 49 3581 5256 3326 -193 493 -166 O ATOM 373 CB TYR A 49 77.718 6.979 57.395 1.00 28.70 C ANISOU 373 CB TYR D 49 3729 4516 2661 -593 763 432 C ATOM 374 CG TYR A 49 76.513 7.782 57.837 1.00 28.86 C ANISOU 374 CG TYR D 49 3899 4225 2843 -562 643 535 C ATOM 375 CD1 TYR A 49 76.547 8.526 59.019 1.00 29.67 C ANISOU 375 CD1 TYR D 49 3644 4428 3202 -472 600 139 C ATOM 376 CD2 TYR A 49 75.339 7.809 57.093 1.00 28.94 C ANISOU 376 CD2 TYR D 49 4228 4131 2636 -369 435 627 C ATOM 377 CE1 TYR A 49 75.442 9.263 59.430 1.00 30.68 C ANISOU 377 CE1 TYR D 49 4273 3965 3417 -273 178 282 C ATOM 378 CE2 TYR A 49 74.218 8.547 57.490 1.00 29.44 C ANISOU 378 CE2 TYR D 49 4204 4244 2736 -319 475 638 C ATOM 379 CZ TYR A 49 74.292 9.269 58.659 1.00 30.49 C ANISOU 379 CZ TYR D 49 4441 3847 3297 -119 27 397 C ATOM 380 OH TYR A 49 73.213 10.005 59.082 1.00 29.81 O ANISOU 380 OH TYR D 49 4119 4185 3023 -249 372 598 O ATOM 381 N LYS A 50 80.522 6.464 56.085 1.00 30.55 N ANISOU 381 N LYS D 50 3676 4614 3316 -206 455 -43 N ATOM 382 CA LYS A 50 81.718 5.651 55.866 1.00 33.48 C ANISOU 382 CA LYS D 50 3763 4868 4090 -138 300 528 C ATOM 383 C LYS A 50 82.954 6.412 56.333 1.00 34.21 C ANISOU 383 C LYS D 50 3396 4891 4709 5 747 390 C ATOM 384 O LYS A 50 83.811 5.835 57.026 1.00 34.90 O ANISOU 384 O LYS D 50 3537 5537 4188 130 643 348 O ATOM 385 CB LYS A 50 81.830 5.245 54.398 1.00 36.30 C ANISOU 385 CB LYS D 50 3582 6026 4183 140 229 363 C ATOM 386 CG LYS A 50 83.213 4.748 54.011 1.00 44.99 C ANISOU 386 CG LYS D 50 4759 6862 5473 802 -824 439 C ATOM 387 CD LYS A 50 83.389 4.709 52.499 1.00 58.15 C ANISOU 387 CD LYS D 50 7857 8435 5801 -219 -2354 1304 C ATOM 388 CE LYS A 50 84.655 4.006 52.023 1.00 62.07 C ANISOU 388 CE LYS D 50 7631 9259 6695 -492 -3182 1119 C ATOM 389 NZ LYS A 50 84.404 2.844 51.129 1.00 67.58 N ANISOU 389 NZ LYS D 50 6656 10188 8835 -1236 -2240 -114 N ATOM 390 N ALA A 51 83.088 7.690 55.991 1.00 33.07 N ANISOU 390 N ALA D 51 3618 4766 4180 -56 576 739 N ATOM 391 CA ALA A 51 84.249 8.450 56.441 1.00 38.48 C ANISOU 391 CA ALA D 51 5429 4882 4308 -518 249 671 C ATOM 392 C ALA A 51 84.222 8.750 57.934 1.00 37.45 C ANISOU 392 C ALA D 51 5427 4726 4077 -234 819 774 C ATOM 393 O ALA A 51 85.259 8.744 58.620 1.00 39.04 O ANISOU 393 O ALA D 51 5435 4712 4686 -181 578 452 O ATOM 394 CB ALA A 51 84.344 9.764 55.669 1.00 38.64 C ANISOU 394 CB ALA D 51 6696 4148 3837 -483 1315 -169 C ATOM 395 N LEU A 52 83.039 9.036 58.490 1.00 35.68 N ANISOU 395 N LEU D 52 5046 4696 3814 -349 927 699 N ATOM 396 CA LEU A 52 82.971 9.247 59.935 1.00 33.57 C ANISOU 396 CA LEU D 52 4097 4791 3867 -151 930 194 C ATOM 397 C LEU A 52 83.448 7.994 60.672 1.00 36.49 C ANISOU 397 C LEU D 52 4286 5492 4087 -463 1111 -39 C ATOM 398 O LEU A 52 84.230 8.051 61.626 1.00 38.80 O ANISOU 398 O LEU D 52 4941 5301 4500 -245 1690 70 O ATOM 399 CB LEU A 52 81.546 9.577 60.363 1.00 35.41 C ANISOU 399 CB LEU D 52 4291 4751 4413 -274 184 39 C ATOM 400 CG LEU A 52 81.121 11.031 60.449 1.00 38.29 C ANISOU 400 CG LEU D 52 4407 4980 5163 -433 -340 505 C ATOM 401 CD1 LEU A 52 79.646 11.131 60.815 1.00 45.21 C ANISOU 401 CD1 LEU D 52 4596 5953 6630 -275 -507 2054 C ATOM 402 CD2 LEU A 52 82.002 11.783 61.447 1.00 41.23 C ANISOU 402 CD2 LEU D 52 5482 6511 3672 -1048 -925 517 C ATOM 403 N VAL A 53 82.963 6.833 60.233 1.00 34.15 N ANISOU 403 N VAL D 53 3484 5648 3844 -77 -36 542 N ATOM 404 CA VAL A 53 83.386 5.597 60.896 1.00 34.02 C ANISOU 404 CA VAL D 53 3492 5687 3746 6 -38 663 C ATOM 405 C VAL A 53 84.899 5.412 60.887 1.00 35.71 C ANISOU 405 C VAL D 53 3968 5688 3913 210 505 903 C ATOM 406 O VAL A 53 85.551 4.996 61.863 1.00 37.15 O ANISOU 406 O VAL D 53 5239 5205 3671 335 614 801 O ATOM 407 CB VAL A 53 82.674 4.431 60.194 1.00 34.43 C ANISOU 407 CB VAL D 53 3146 5744 4193 115 -316 640 C ATOM 408 CG1 VAL A 53 83.310 3.104 60.581 1.00 34.38 C ANISOU 408 CG1 VAL D 53 3037 5677 4350 336 -480 1600 C ATOM 409 CG2 VAL A 53 81.197 4.481 60.550 1.00 32.94 C ANISOU 409 CG2 VAL D 53 3012 5751 3754 300 394 532 C ATOM 410 N GLU A 54 85.480 5.752 59.737 1.00 36.62 N ANISOU 410 N GLU D 54 4243 5648 4023 367 921 994 N ATOM 411 CA GLU A 54 86.905 5.631 59.499 1.00 37.38 C ANISOU 411 CA GLU D 54 4634 5511 4059 340 472 836 C ATOM 412 C GLU A 54 87.690 6.496 60.489 1.00 38.61 C ANISOU 412 C GLU D 54 4553 5914 4205 351 560 489 C ATOM 413 O GLU A 54 88.666 6.057 61.113 1.00 41.06 O ANISOU 413 O GLU D 54 4916 6097 4589 -34 1338 407 O ATOM 414 CB GLU A 54 87.284 6.014 58.058 1.00 41.10 C ANISOU 414 CB GLU D 54 5125 6523 3967 353 -3 1093 C ATOM 415 CG GLU A 54 87.517 4.869 57.103 1.00 58.89 C ANISOU 415 CG GLU D 54 8324 8511 5542 -1348 -2116 1608 C ATOM 416 CD GLU A 54 87.465 5.269 55.638 1.00 65.60 C ANISOU 416 CD GLU D 54 9639 10092 5195 -2264 -2694 1559 C ATOM 417 OE1 GLU A 54 87.296 6.460 55.287 1.00 88.06 O ANISOU 417 OE1 GLU D 54 13342 12442 7675 -5923 49 1437 O ATOM 418 OE2 GLU A 54 87.598 4.373 54.769 1.00 87.65 O ANISOU 418 OE2 GLU D 54 14582 11984 6736 -3012 -5420 578 O ATOM 419 N MET A 55 87.238 7.739 60.608 1.00 39.25 N ANISOU 419 N MET D 55 4572 5933 4408 388 290 604 N ATOM 420 CA MET A 55 87.902 8.673 61.512 1.00 40.82 C ANISOU 420 CA MET D 55 5468 5886 4156 -399 382 995 C ATOM 421 C MET A 55 87.811 8.235 62.968 1.00 40.32 C ANISOU 421 C MET D 55 5277 5804 4237 -258 593 957 C ATOM 422 O MET A 55 88.705 8.443 63.806 1.00 41.77 O ANISOU 422 O MET D 55 5137 5985 4748 -205 1262 839 O ATOM 423 CB MET A 55 87.250 10.048 61.311 1.00 37.31 C ANISOU 423 CB MET D 55 5429 5474 3274 -54 447 305 C ATOM 424 CG MET A 55 87.510 10.582 59.904 1.00 37.55 C ANISOU 424 CG MET D 55 5293 5936 3040 76 223 264 C ATOM 425 SD MET A 55 86.814 12.232 59.687 1.00 42.14 S ANISOU 425 SD MET D 55 5526 5570 4915 -157 981 545 S ATOM 426 CE MET A 55 88.035 13.239 60.545 1.00 45.49 C ANISOU 426 CE MET D 55 6271 6996 4015 -1031 738 -217 C ATOM 427 N HIS A 56 86.668 7.618 63.283 1.00 40.28 N ANISOU 427 N HIS D 56 4606 5840 4861 -327 1653 1152 N ATOM 428 CA HIS A 56 86.428 7.096 64.631 1.00 36.50 C ANISOU 428 CA HIS D 56 4299 5254 4317 438 1371 679 C ATOM 429 C HIS A 56 87.423 5.982 64.897 1.00 37.39 C ANISOU 429 C HIS D 56 4325 5505 4376 325 1460 -163 C ATOM 430 O HIS A 56 88.109 5.844 65.910 1.00 42.59 O ANISOU 430 O HIS D 56 5264 6224 4696 -194 2341 -302 O ATOM 431 CB HIS A 56 84.997 6.560 64.765 1.00 35.48 C ANISOU 431 CB HIS D 56 4505 5119 3858 263 1363 337 C ATOM 432 CG HIS A 56 84.819 5.849 66.079 1.00 35.58 C ANISOU 432 CG HIS D 56 4589 4952 3976 201 1449 293 C ATOM 433 ND1 HIS A 56 85.033 6.461 67.298 1.00 35.66 N ANISOU 433 ND1 HIS D 56 4452 5245 3851 87 1267 567 N ATOM 434 CD2 HIS A 56 84.475 4.572 66.360 1.00 37.60 C ANISOU 434 CD2 HIS D 56 5221 4959 4106 -114 1382 360 C ATOM 435 CE1 HIS A 56 84.817 5.598 68.272 1.00 37.12 C ANISOU 435 CE1 HIS D 56 4915 5180 4010 -158 1590 277 C ATOM 436 NE2 HIS A 56 84.473 4.437 67.738 1.00 37.17 N ANISOU 436 NE2 HIS D 56 4672 5325 4126 -86 1582 188 N ATOM 437 N LYS A 57 87.508 5.107 63.884 1.00 41.30 N ANISOU 437 N LYS D 57 4464 6290 4937 -121 1128 -94 N ATOM 438 CA LYS A 57 88.415 3.964 64.058 1.00 43.41 C ANISOU 438 CA LYS D 57 4456 6226 5813 -116 1049 104 C ATOM 439 C LYS A 57 89.847 4.451 64.106 1.00 44.80 C ANISOU 439 C LYS D 57 4939 6334 5749 138 1462 5 C ATOM 440 O LYS A 57 90.706 3.848 64.752 1.00 50.05 O ANISOU 440 O LYS D 57 5462 6879 6674 355 2127 44 O ATOM 441 CB LYS A 57 88.140 2.927 62.962 1.00 44.48 C ANISOU 441 CB LYS D 57 4340 6575 5985 166 906 -158 C ATOM 442 CG LYS A 57 86.684 2.461 63.020 1.00 51.01 C ANISOU 442 CG LYS D 57 6070 6341 6971 -158 1498 -455 C ATOM 443 CD LYS A 57 86.447 1.300 62.075 1.00 56.88 C ANISOU 443 CD LYS D 57 6968 7301 7343 -997 1728 -1021 C ATOM 444 CE LYS A 57 85.539 0.264 62.725 1.00 64.05 C ANISOU 444 CE LYS D 57 8349 7361 8627 -1687 2644 -1279 C ATOM 445 NZ LYS A 57 85.108 -0.786 61.741 1.00 78.18 N ANISOU 445 NZ LYS D 57 13083 8827 7794 -4030 3470 -2024 N ATOM 446 N ALA A 58 90.165 5.571 63.471 1.00 42.30 N ANISOU 446 N ALA D 58 4369 5980 5724 145 968 -91 N ATOM 447 CA ALA A 58 91.540 6.043 63.489 1.00 42.20 C ANISOU 447 CA ALA D 58 3914 6116 6006 458 1348 -142 C ATOM 448 C ALA A 58 91.816 6.778 64.787 1.00 43.86 C ANISOU 448 C ALA D 58 5241 5672 5750 264 1375 67 C ATOM 449 O ALA A 58 92.901 7.327 64.982 1.00 47.11 O ANISOU 449 O ALA D 58 5609 5777 6512 631 1364 -245 O ATOM 450 CB ALA A 58 91.796 6.951 62.296 1.00 40.88 C ANISOU 450 CB ALA D 58 4030 5802 5701 512 1062 -162 C ATOM 451 N GLY A 59 90.831 6.799 65.673 1.00 42.92 N ANISOU 451 N GLY D 59 4849 5919 5541 87 1691 300 N ATOM 452 CA GLY A 59 90.978 7.470 66.947 1.00 41.52 C ANISOU 452 CA GLY D 59 5229 5218 5327 449 1947 220 C ATOM 453 C GLY A 59 90.867 8.977 66.836 1.00 42.22 C ANISOU 453 C GLY D 59 5145 5719 5179 358 1743 -268 C ATOM 454 O GLY A 59 91.421 9.676 67.705 1.00 50.77 O ANISOU 454 O GLY D 59 6546 7108 5637 -812 2419 -1105 O ATOM 455 N GLN A 60 90.180 9.527 65.823 1.00 40.36 N ANISOU 455 N GLN D 60 5158 5593 4585 343 1617 281 N ATOM 456 CA GLN A 60 90.145 10.992 65.736 1.00 42.17 C ANISOU 456 CA GLN D 60 5305 5372 5345 297 1772 391 C ATOM 457 C GLN A 60 88.899 11.604 66.365 1.00 42.03 C ANISOU 457 C GLN D 60 5129 5202 5637 118 1539 193 C ATOM 458 O GLN A 60 88.735 12.816 66.553 1.00 41.80 O ANISOU 458 O GLN D 60 5215 5402 5265 4 1695 -339 O ATOM 459 CB GLN A 60 90.246 11.418 64.274 1.00 43.43 C ANISOU 459 CB GLN D 60 4704 6522 5274 -49 1679 279 C ATOM 460 CG GLN A 60 91.475 10.908 63.533 1.00 49.81 C ANISOU 460 CG GLN D 60 5483 7271 6171 -728 312 1074 C ATOM 461 CD GLN A 60 91.329 11.080 62.032 1.00 56.33 C ANISOU 461 CD GLN D 60 6998 8291 6113 -1600 309 1365 C ATOM 462 OE1 GLN A 60 90.964 12.152 61.552 1.00 64.84 O ANISOU 462 OE1 GLN D 60 8153 10132 6352 -3034 1176 828 O ATOM 463 NE2 GLN A 60 91.587 10.052 61.238 1.00 65.00 N ANISOU 463 NE2 GLN D 60 7738 10357 6604 -1472 135 -715 N ATOM 464 N VAL A 61 87.945 10.740 66.726 1.00 40.33 N ANISOU 464 N VAL D 61 4988 4883 5451 458 1903 -213 N ATOM 465 CA VAL A 61 86.693 11.258 67.274 1.00 38.51 C ANISOU 465 CA VAL D 61 4772 5192 4668 108 1718 -6 C ATOM 466 C VAL A 61 86.003 10.188 68.109 1.00 38.79 C ANISOU 466 C VAL D 61 4662 5459 4616 53 1839 17 C ATOM 467 O VAL A 61 86.045 8.984 67.873 1.00 38.01 O ANISOU 467 O VAL D 61 5177 5154 4111 -178 1776 -439 O ATOM 468 CB VAL A 61 85.780 11.744 66.130 1.00 35.87 C ANISOU 468 CB VAL D 61 3459 5851 4319 38 1149 136 C ATOM 469 CG1 VAL A 61 85.293 10.573 65.284 1.00 34.05 C ANISOU 469 CG1 VAL D 61 3899 4739 4300 -57 1588 390 C ATOM 470 CG2 VAL A 61 84.560 12.525 66.615 1.00 38.36 C ANISOU 470 CG2 VAL D 61 4114 5000 5463 207 905 784 C ATOM 471 N SER A 62 85.318 10.646 69.145 1.00 37.71 N ANISOU 471 N SER D 62 5016 5335 3977 -210 1931 -311 N ATOM 472 CA SER A 62 84.507 9.751 69.955 1.00 37.37 C ANISOU 472 CA SER D 62 5117 5136 3946 -253 1835 -455 C ATOM 473 C SER A 62 83.059 10.237 69.983 1.00 36.60 C ANISOU 473 C SER D 62 4929 5187 3790 -330 1269 -663 C ATOM 474 O SER A 62 82.834 11.452 70.060 1.00 36.49 O ANISOU 474 O SER D 62 5074 5273 3517 -543 949 191 O ATOM 475 CB SER A 62 85.096 9.660 71.365 1.00 38.05 C ANISOU 475 CB SER D 62 5419 5105 3934 -500 1942 -461 C ATOM 476 OG SER A 62 84.268 8.811 72.137 1.00 39.31 O ANISOU 476 OG SER D 62 5994 5146 3794 -33 1566 -189 O ATOM 477 N PHE A 63 82.108 9.315 69.929 1.00 34.91 N ANISOU 477 N PHE D 63 4813 5129 3321 -286 441 -70 N ATOM 478 CA PHE A 63 80.700 9.680 69.997 1.00 36.39 C ANISOU 478 CA PHE D 63 4612 5181 4035 -376 400 135 C ATOM 479 C PHE A 63 80.093 9.387 71.368 1.00 36.50 C ANISOU 479 C PHE D 63 4735 4958 4175 -34 786 186 C ATOM 480 O PHE A 63 78.857 9.427 71.474 1.00 38.39 O ANISOU 480 O PHE D 63 5144 4391 5052 -390 1827 750 O ATOM 481 CB PHE A 63 79.935 8.942 68.891 1.00 36.21 C ANISOU 481 CB PHE D 63 4572 4909 4277 -185 524 46 C ATOM 482 CG PHE A 63 80.414 9.436 67.519 1.00 36.61 C ANISOU 482 CG PHE D 63 4825 4951 4133 -434 306 -78 C ATOM 483 CD1 PHE A 63 79.957 10.626 66.984 1.00 36.87 C ANISOU 483 CD1 PHE D 63 5009 5238 3761 -73 617 -241 C ATOM 484 CD2 PHE A 63 81.326 8.693 66.799 1.00 37.65 C ANISOU 484 CD2 PHE D 63 5038 4681 4585 -129 290 152 C ATOM 485 CE1 PHE A 63 80.388 11.120 65.762 1.00 33.38 C ANISOU 485 CE1 PHE D 63 4701 4616 3368 641 566 -647 C ATOM 486 CE2 PHE A 63 81.768 9.150 65.585 1.00 35.30 C ANISOU 486 CE2 PHE D 63 4691 4592 4131 692 760 -337 C ATOM 487 CZ PHE A 63 81.301 10.348 65.065 1.00 35.04 C ANISOU 487 CZ PHE D 63 4500 4689 4124 616 532 -552 C ATOM 488 N LYS A 64 80.909 9.112 72.374 1.00 38.20 N ANISOU 488 N LYS D 64 5030 5353 4130 -38 730 -177 N ATOM 489 CA LYS A 64 80.472 8.832 73.731 1.00 40.02 C ANISOU 489 CA LYS D 64 5502 5507 4198 300 823 -81 C ATOM 490 C LYS A 64 79.540 9.897 74.300 1.00 37.29 C ANISOU 490 C LYS D 64 5325 4801 4043 -159 918 157 C ATOM 491 O LYS A 64 78.582 9.595 75.003 1.00 38.94 O ANISOU 491 O LYS D 64 5244 5721 3830 -406 1042 819 O ATOM 492 CB LYS A 64 81.682 8.769 74.676 1.00 46.94 C ANISOU 492 CB LYS D 64 5209 7329 5298 -39 2426 -724 C ATOM 493 CG LYS A 64 81.831 7.497 75.481 1.00 63.62 C ANISOU 493 CG LYS D 64 6935 9358 7882 -2352 3791 -1694 C ATOM 494 CD LYS A 64 82.049 6.291 74.577 1.00 78.52 C ANISOU 494 CD LYS D 64 7690 11352 10791 -3655 2791 -1979 C ATOM 495 CE LYS A 64 82.658 5.110 75.315 1.00 84.39 C ANISOU 495 CE LYS D 64 7679 12216 12171 -4131 3197 -2918 C ATOM 496 NZ LYS A 64 81.839 3.869 75.142 1.00 86.17 N ANISOU 496 NZ LYS D 64 6178 12119 14443 -3347 2915 -3978 N ATOM 497 N HIS A 65 79.834 11.171 74.010 1.00 36.57 N ANISOU 497 N HIS D 65 5551 4340 4002 -26 1786 -468 N ATOM 498 CA HIS A 65 78.955 12.233 74.505 1.00 38.83 C ANISOU 498 CA HIS D 65 5328 5346 4082 -462 1852 -408 C ATOM 499 C HIS A 65 78.346 13.017 73.349 1.00 38.25 C ANISOU 499 C HIS D 65 5120 5684 3728 -1069 1583 -694 C ATOM 500 O HIS A 65 78.183 14.240 73.381 1.00 41.41 O ANISOU 500 O HIS D 65 5806 6432 3494 -2087 1577 86 O ATOM 501 CB HIS A 65 79.703 13.160 75.476 1.00 40.34 C ANISOU 501 CB HIS D 65 5878 5839 3610 -755 1960 -446 C ATOM 502 CG HIS A 65 80.219 12.329 76.628 1.00 40.80 C ANISOU 502 CG HIS D 65 5719 5801 3983 -378 2110 -308 C ATOM 503 ND1 HIS A 65 79.379 11.509 77.347 1.00 43.19 N ANISOU 503 ND1 HIS D 65 6066 5694 4649 -380 2888 -350 N ATOM 504 CD2 HIS A 65 81.442 12.168 77.161 1.00 40.00 C ANISOU 504 CD2 HIS D 65 5536 5771 3890 -317 1611 -476 C ATOM 505 CE1 HIS A 65 80.058 10.882 78.292 1.00 42.44 C ANISOU 505 CE1 HIS D 65 5471 5790 4863 -448 2721 -458 C ATOM 506 NE2 HIS A 65 81.319 11.265 78.201 1.00 41.61 N ANISOU 506 NE2 HIS D 65 5402 5891 4518 -294 2141 -579 N ATOM 507 N VAL A 66 77.999 12.291 72.290 1.00 37.49 N ANISOU 507 N VAL D 66 5759 5103 3382 -1048 1137 -45 N ATOM 508 CA VAL A 66 77.301 12.882 71.149 1.00 32.58 C ANISOU 508 CA VAL D 66 4729 4641 3010 -406 319 -29 C ATOM 509 C VAL A 66 75.868 12.356 71.196 1.00 33.64 C ANISOU 509 C VAL D 66 4180 4617 3983 -624 -195 260 C ATOM 510 O VAL A 66 75.648 11.153 71.330 1.00 33.70 O ANISOU 510 O VAL D 66 4237 4861 3709 -609 849 178 O ATOM 511 CB VAL A 66 77.971 12.580 69.801 1.00 30.79 C ANISOU 511 CB VAL D 66 3995 4534 3171 -53 257 -274 C ATOM 512 CG1 VAL A 66 77.093 13.076 68.664 1.00 28.54 C ANISOU 512 CG1 VAL D 66 3481 4398 2965 -354 114 -163 C ATOM 513 CG2 VAL A 66 79.342 13.235 69.744 1.00 30.17 C ANISOU 513 CG2 VAL D 66 4545 4483 2433 -485 1011 -15 C ATOM 514 N VAL A 67 74.915 13.266 71.113 1.00 31.87 N ANISOU 514 N VAL D 67 4128 4521 3461 -709 -113 361 N ATOM 515 CA VAL A 67 73.500 12.900 71.088 1.00 30.76 C ANISOU 515 CA VAL D 67 4351 4529 2807 -642 557 496 C ATOM 516 C VAL A 67 73.013 13.110 69.667 1.00 32.92 C ANISOU 516 C VAL D 67 5272 4611 2623 -1317 528 447 C ATOM 517 O VAL A 67 73.399 14.120 69.092 1.00 30.50 O ANISOU 517 O VAL D 67 4243 4471 2876 -943 593 329 O ATOM 518 CB VAL A 67 72.686 13.752 72.076 1.00 29.57 C ANISOU 518 CB VAL D 67 4338 4257 2639 -267 644 21 C ATOM 519 CG1 VAL A 67 71.193 13.729 71.798 1.00 30.25 C ANISOU 519 CG1 VAL D 67 3849 4230 3417 -556 1119 -73 C ATOM 520 CG2 VAL A 67 73.002 13.287 73.507 1.00 30.09 C ANISOU 520 CG2 VAL D 67 4433 4375 2624 -348 692 -66 C ATOM 521 N THR A 68 72.218 12.198 69.128 1.00 28.03 N ANISOU 521 N THR D 68 3537 4225 2890 -529 249 556 N ATOM 522 CA THR A 68 71.754 12.362 67.768 1.00 29.02 C ANISOU 522 CA THR D 68 3571 4427 3030 -384 231 247 C ATOM 523 C THR A 68 70.229 12.328 67.675 1.00 30.37 C ANISOU 523 C THR D 68 3931 4335 3271 -363 415 481 C ATOM 524 O THR A 68 69.584 11.646 68.472 1.00 30.55 O ANISOU 524 O THR D 68 3681 5014 2912 -8 120 888 O ATOM 525 CB THR A 68 72.292 11.263 66.823 1.00 29.30 C ANISOU 525 CB THR D 68 3836 4069 3229 -676 13 152 C ATOM 526 OG1 THR A 68 71.792 9.992 67.284 1.00 32.78 O ANISOU 526 OG1 THR D 68 4298 4521 3636 -1125 476 -23 O ATOM 527 CG2 THR A 68 73.806 11.174 66.823 1.00 29.46 C ANISOU 527 CG2 THR D 68 3888 4619 2685 -190 116 216 C ATOM 528 N PHE A 69 69.717 13.040 66.675 1.00 26.17 N ANISOU 528 N PHE D 69 3142 3973 2828 -405 -171 461 N ATOM 529 CA PHE A 69 68.323 13.106 66.283 1.00 28.36 C ANISOU 529 CA PHE D 69 4053 3805 2918 -327 39 377 C ATOM 530 C PHE A 69 68.226 12.831 64.789 1.00 28.95 C ANISOU 530 C PHE D 69 4260 3775 2963 -296 -115 416 C ATOM 531 O PHE A 69 68.874 13.555 63.999 1.00 28.25 O ANISOU 531 O PHE D 69 3897 3916 2922 -395 166 336 O ATOM 532 CB PHE A 69 67.727 14.479 66.590 1.00 27.11 C ANISOU 532 CB PHE D 69 3946 3445 2910 366 -37 248 C ATOM 533 CG PHE A 69 67.458 14.709 68.074 1.00 29.98 C ANISOU 533 CG PHE D 69 4332 4143 2916 -201 -101 390 C ATOM 534 CD1 PHE A 69 68.374 15.359 68.885 1.00 28.94 C ANISOU 534 CD1 PHE D 69 3373 4621 3001 -218 45 10 C ATOM 535 CD2 PHE A 69 66.270 14.266 68.652 1.00 29.05 C ANISOU 535 CD2 PHE D 69 3395 4491 3153 -163 -363 721 C ATOM 536 CE1 PHE A 69 68.105 15.545 70.243 1.00 32.19 C ANISOU 536 CE1 PHE D 69 4194 4791 3244 -637 -524 139 C ATOM 537 CE2 PHE A 69 65.998 14.446 70.010 1.00 29.75 C ANISOU 537 CE2 PHE D 69 3479 4711 3115 -454 -360 666 C ATOM 538 CZ PHE A 69 66.927 15.095 70.813 1.00 30.71 C ANISOU 538 CZ PHE D 69 3704 4962 3002 -824 566 495 C ATOM 539 N ASN A 70 67.453 11.828 64.389 1.00 30.06 N ANISOU 539 N ASN D 70 4586 4001 2834 -680 375 281 N ATOM 540 CA ASN A 70 67.291 11.573 62.950 1.00 29.07 C ANISOU 540 CA ASN D 70 4588 3587 2872 -24 68 333 C ATOM 541 C ASN A 70 66.086 12.323 62.394 1.00 29.49 C ANISOU 541 C ASN D 70 4517 3953 2734 -58 233 569 C ATOM 542 O ASN A 70 65.119 12.603 63.115 1.00 31.09 O ANISOU 542 O ASN D 70 3473 5192 3147 -294 65 920 O ATOM 543 CB ASN A 70 67.154 10.073 62.710 1.00 29.68 C ANISOU 543 CB ASN D 70 4644 4010 2622 -236 660 -339 C ATOM 544 CG ASN A 70 68.469 9.505 62.218 1.00 30.70 C ANISOU 544 CG ASN D 70 4485 4351 2830 -322 261 -659 C ATOM 545 OD1 ASN A 70 69.378 9.281 63.020 1.00 29.40 O ANISOU 545 OD1 ASN D 70 3944 4144 3082 -610 749 -266 O ATOM 546 ND2 ASN A 70 68.566 9.273 60.904 1.00 31.69 N ANISOU 546 ND2 ASN D 70 4365 4965 2709 -885 503 -33 N ATOM 547 N MET A 71 66.107 12.660 61.115 1.00 30.26 N ANISOU 547 N MET D 71 4718 4257 2522 -619 19 126 N ATOM 548 CA MET A 71 65.079 13.462 60.475 1.00 35.32 C ANISOU 548 CA MET D 71 5264 4956 3202 -786 731 -453 C ATOM 549 C MET A 71 63.731 12.756 60.356 1.00 33.84 C ANISOU 549 C MET D 71 4434 4942 3480 -273 159 -110 C ATOM 550 O MET A 71 62.687 13.414 60.419 1.00 34.08 O ANISOU 550 O MET D 71 4080 5334 3533 -667 -539 991 O ATOM 551 CB MET A 71 65.505 13.877 59.041 1.00 33.33 C ANISOU 551 CB MET D 71 4725 4761 3178 347 567 -368 C ATOM 552 CG MET A 71 66.673 14.833 58.968 1.00 39.27 C ANISOU 552 CG MET D 71 5876 5010 4034 -447 1789 -208 C ATOM 553 SD MET A 71 66.901 15.629 57.359 1.00 43.40 S ANISOU 553 SD MET D 71 6840 5791 3859 -207 1793 -100 S ATOM 554 CE MET A 71 66.177 14.387 56.280 1.00 41.95 C ANISOU 554 CE MET D 71 7854 4657 3430 -390 565 1391 C ATOM 555 N ASP A 72 63.746 11.430 60.142 1.00 27.73 N ANISOU 555 N ASP D 72 3999 3840 2697 424 -414 894 N ATOM 556 CA ASP A 72 62.478 10.785 59.844 1.00 33.08 C ANISOU 556 CA ASP D 72 4116 4226 4227 316 867 -224 C ATOM 557 C ASP A 72 62.485 9.273 60.054 1.00 34.95 C ANISOU 557 C ASP D 72 4227 4434 4617 -87 -49 -111 C ATOM 558 O ASP A 72 63.525 8.678 60.360 1.00 34.87 O ANISOU 558 O ASP D 72 4536 4410 4302 -599 1563 41 O ATOM 559 CB ASP A 72 62.118 11.126 58.397 1.00 44.06 C ANISOU 559 CB ASP D 72 8100 4460 4179 -904 1573 -158 C ATOM 560 CG ASP A 72 63.283 11.176 57.436 1.00 45.45 C ANISOU 560 CG ASP D 72 7717 5146 4405 -817 1610 227 C ATOM 561 OD1 ASP A 72 64.278 10.426 57.589 1.00 53.37 O ANISOU 561 OD1 ASP D 72 7062 6641 6577 -863 359 -146 O ATOM 562 OD2 ASP A 72 63.212 11.980 56.487 1.00 51.96 O ANISOU 562 OD2 ASP D 72 9349 5745 4650 -1909 1927 489 O ATOM 563 N GLU A 73 61.303 8.671 59.893 1.00 36.89 N ANISOU 563 N GLU D 73 5316 4442 4257 -233 830 -91 N ATOM 564 CA GLU A 73 61.056 7.237 59.991 1.00 39.23 C ANISOU 564 CA GLU D 73 6067 4619 4219 -758 722 -146 C ATOM 565 C GLU A 73 59.736 6.876 59.311 1.00 37.56 C ANISOU 565 C GLU D 73 5713 4623 3935 -492 333 21 C ATOM 566 O GLU A 73 58.780 7.660 59.269 1.00 40.77 O ANISOU 566 O GLU D 73 5444 5701 4344 -700 972 -594 O ATOM 567 CB GLU A 73 61.075 6.778 61.454 1.00 34.97 C ANISOU 567 CB GLU D 73 4785 4198 4304 107 553 228 C ATOM 568 CG GLU A 73 60.928 5.284 61.691 1.00 42.01 C ANISOU 568 CG GLU D 73 5410 5682 4869 -845 554 426 C ATOM 569 CD GLU A 73 62.003 4.411 61.046 1.00 41.86 C ANISOU 569 CD GLU D 73 5233 6069 4603 -1168 280 -224 C ATOM 570 OE1 GLU A 73 61.892 4.174 59.814 1.00 39.20 O ANISOU 570 OE1 GLU D 73 4960 5439 4493 -1399 763 -263 O ATOM 571 OE2 GLU A 73 62.927 3.977 61.806 1.00 38.00 O ANISOU 571 OE2 GLU D 73 4982 6112 3345 -1143 204 643 O ATOM 572 N TYR A 74 59.689 5.660 58.753 1.00 37.36 N ANISOU 572 N TYR D 74 5673 4875 3647 -565 541 -202 N ATOM 573 CA TYR A 74 58.449 5.155 58.184 1.00 41.28 C ANISOU 573 CA TYR D 74 5667 5053 4964 -481 541 -711 C ATOM 574 C TYR A 74 57.433 4.814 59.266 1.00 41.19 C ANISOU 574 C TYR D 74 5495 4709 5448 -293 751 -648 C ATOM 575 O TYR A 74 57.768 4.308 60.351 1.00 39.71 O ANISOU 575 O TYR D 74 5055 4567 5465 -126 667 -328 O ATOM 576 CB TYR A 74 58.674 3.889 57.369 1.00 41.08 C ANISOU 576 CB TYR D 74 5489 4886 5233 -454 679 -990 C ATOM 577 CG TYR A 74 59.331 4.115 56.032 1.00 43.17 C ANISOU 577 CG TYR D 74 6067 5477 4860 -1198 336 -1187 C ATOM 578 CD1 TYR A 74 58.772 4.924 55.059 1.00 45.76 C ANISOU 578 CD1 TYR D 74 6685 5643 5060 -1237 755 -1295 C ATOM 579 CD2 TYR A 74 60.543 3.494 55.755 1.00 43.30 C ANISOU 579 CD2 TYR D 74 5970 6098 4385 -1347 42 -628 C ATOM 580 CE1 TYR A 74 59.422 5.093 53.850 1.00 50.27 C ANISOU 580 CE1 TYR D 74 7361 6441 5297 -1381 916 -798 C ATOM 581 CE2 TYR A 74 61.195 3.658 54.553 1.00 46.74 C ANISOU 581 CE2 TYR D 74 6844 6625 4291 -1476 254 -474 C ATOM 582 CZ TYR A 74 60.626 4.469 53.592 1.00 50.91 C ANISOU 582 CZ TYR D 74 7258 7085 5001 -1429 845 -134 C ATOM 583 OH TYR A 74 61.274 4.636 52.383 1.00 55.75 O ANISOU 583 OH TYR D 74 8276 8611 4294 -813 895 -463 O ATOM 584 N VAL A 75 56.178 5.094 58.937 1.00 42.13 N ANISOU 584 N VAL D 75 4919 5224 5863 -261 738 -759 N ATOM 585 CA VAL A 75 55.088 4.761 59.857 1.00 47.19 C ANISOU 585 CA VAL D 75 5788 5097 7045 -33 166 -493 C ATOM 586 C VAL A 75 54.642 3.320 59.608 1.00 48.55 C ANISOU 586 C VAL D 75 6285 5224 6940 -454 735 -542 C ATOM 587 O VAL A 75 54.527 2.961 58.425 1.00 48.47 O ANISOU 587 O VAL D 75 5693 5860 6862 -1170 726 -226 O ATOM 588 CB VAL A 75 53.902 5.727 59.681 1.00 48.86 C ANISOU 588 CB VAL D 75 6013 5205 7348 131 647 -104 C ATOM 589 CG1 VAL A 75 52.641 5.138 60.307 1.00 53.29 C ANISOU 589 CG1 VAL D 75 6667 5126 8455 481 1334 91 C ATOM 590 CG2 VAL A 75 54.198 7.110 60.259 1.00 43.92 C ANISOU 590 CG2 VAL D 75 5319 5653 5715 67 1547 -167 C ATOM 591 N GLY A 76 54.418 2.528 60.642 1.00 50.75 N ANISOU 591 N GLY D 76 7221 5344 6717 -516 356 -120 N ATOM 592 CA GLY A 76 53.886 1.181 60.590 1.00 50.36 C ANISOU 592 CA GLY D 76 6827 5542 6765 -498 1207 -437 C ATOM 593 C GLY A 76 54.838 0.113 60.109 1.00 52.70 C ANISOU 593 C GLY D 76 6657 6001 7365 -559 1338 -104 C ATOM 594 O GLY A 76 54.509 -1.056 59.887 1.00 53.35 O ANISOU 594 O GLY D 76 6451 6305 7513 -727 1657 -39 O ATOM 595 N LEU A 77 56.099 0.473 59.910 1.00 51.62 N ANISOU 595 N LEU D 77 6184 6058 7372 -182 2057 -442 N ATOM 596 CA LEU A 77 57.093 -0.510 59.482 1.00 51.42 C ANISOU 596 CA LEU D 77 6268 6170 7100 -353 1735 -602 C ATOM 597 C LEU A 77 57.737 -1.044 60.747 1.00 48.97 C ANISOU 597 C LEU D 77 5514 6321 6772 -359 1217 -704 C ATOM 598 O LEU A 77 58.073 -0.200 61.592 1.00 53.77 O ANISOU 598 O LEU D 77 7868 6544 6016 -2227 1383 112 O ATOM 599 CB LEU A 77 58.088 0.181 58.577 1.00 52.44 C ANISOU 599 CB LEU D 77 7136 6167 6620 -351 1335 -752 C ATOM 600 CG LEU A 77 58.681 -0.529 57.372 1.00 54.52 C ANISOU 600 CG LEU D 77 7227 5709 7779 133 600 -1018 C ATOM 601 CD1 LEU A 77 60.204 -0.493 57.447 1.00 54.85 C ANISOU 601 CD1 LEU D 77 5875 7127 7838 795 1700 -2120 C ATOM 602 CD2 LEU A 77 58.191 -1.961 57.258 1.00 59.94 C ANISOU 602 CD2 LEU D 77 7100 6902 8774 -680 -44 781 C ATOM 603 N PRO A 78 57.910 -2.343 60.948 1.00 49.97 N ANISOU 603 N PRO D 78 5464 6640 6884 -337 1061 -178 N ATOM 604 CA PRO A 78 58.602 -2.789 62.174 1.00 51.66 C ANISOU 604 CA PRO D 78 5460 6928 7242 -311 1309 -262 C ATOM 605 C PRO A 78 60.029 -2.243 62.235 1.00 48.74 C ANISOU 605 C PRO D 78 5262 6812 6445 -642 1623 -73 C ATOM 606 O PRO A 78 60.739 -2.315 61.226 1.00 51.65 O ANISOU 606 O PRO D 78 6508 6970 6146 -1049 2070 410 O ATOM 607 CB PRO A 78 58.611 -4.308 62.039 1.00 54.45 C ANISOU 607 CB PRO D 78 6132 6946 7612 -961 1705 -379 C ATOM 608 CG PRO A 78 57.534 -4.627 61.058 1.00 52.18 C ANISOU 608 CG PRO D 78 5589 6980 7258 -538 1438 -211 C ATOM 609 CD PRO A 78 57.480 -3.467 60.104 1.00 49.69 C ANISOU 609 CD PRO D 78 5322 6615 6941 -498 978 73 C ATOM 610 N LYS A 79 60.465 -1.709 63.368 1.00 48.19 N ANISOU 610 N LYS D 79 5083 7123 6104 -876 2386 -94 N ATOM 611 CA LYS A 79 61.802 -1.150 63.510 1.00 54.40 C ANISOU 611 CA LYS D 79 7407 6964 6298 -1288 1942 -134 C ATOM 612 C LYS A 79 62.890 -2.088 62.999 1.00 53.90 C ANISOU 612 C LYS D 79 7398 6095 6984 -536 2690 4 C ATOM 613 O LYS A 79 63.850 -1.662 62.345 1.00 58.96 O ANISOU 613 O LYS D 79 8627 5807 7968 -892 2034 91 O ATOM 614 CB LYS A 79 62.085 -0.805 64.976 1.00 64.52 C ANISOU 614 CB LYS D 79 10277 7584 6653 -3394 1702 -620 C ATOM 615 CG LYS A 79 61.652 0.589 65.399 1.00 81.09 C ANISOU 615 CG LYS D 79 12443 9681 8687 -6045 205 -51 C ATOM 616 CD LYS A 79 62.386 1.040 66.663 1.00 94.67 C ANISOU 616 CD LYS D 79 16385 10464 9120 -7758 -149 -552 C ATOM 617 CE LYS A 79 62.071 2.490 67.015 1.00100.31 C ANISOU 617 CE LYS D 79 17239 10681 10196 -8238 -1562 180 C ATOM 618 NZ LYS A 79 63.257 3.318 67.404 1.00 99.23 N ANISOU 618 NZ LYS D 79 16487 9198 12017 -7898 -3093 3219 N ATOM 619 N GLU A 80 62.791 -3.384 63.274 1.00 55.66 N ANISOU 619 N GLU D 80 7175 6753 7220 -583 2365 620 N ATOM 620 CA GLU A 80 63.818 -4.311 62.803 1.00 59.52 C ANISOU 620 CA GLU D 80 7348 7740 7526 -424 2377 1678 C ATOM 621 C GLU A 80 63.667 -4.657 61.328 1.00 58.33 C ANISOU 621 C GLU D 80 7538 6988 7636 -723 2023 1750 C ATOM 622 O GLU A 80 64.462 -5.452 60.810 1.00 60.27 O ANISOU 622 O GLU D 80 7470 6869 8561 -1035 1553 1201 O ATOM 623 CB GLU A 80 63.845 -5.622 63.605 1.00 68.18 C ANISOU 623 CB GLU D 80 7326 10033 8545 -363 3156 1880 C ATOM 624 CG GLU A 80 65.156 -5.827 64.355 1.00 79.36 C ANISOU 624 CG GLU D 80 8602 11058 10492 -46 4197 1108 C ATOM 625 CD GLU A 80 66.103 -6.877 63.814 1.00 85.38 C ANISOU 625 CD GLU D 80 8638 11323 12480 946 4294 1367 C ATOM 626 OE1 GLU A 80 66.420 -7.862 64.536 1.00 99.94 O ANISOU 626 OE1 GLU D 80 8592 11873 17506 -1411 5570 441 O ATOM 627 OE2 GLU A 80 66.561 -6.732 62.653 1.00102.82 O ANISOU 627 OE2 GLU D 80 12178 12381 14509 1275 2104 3815 O ATOM 628 N HIS A 81 62.697 -4.110 60.603 1.00 57.52 N ANISOU 628 N HIS D 81 7404 6948 7504 -1180 1928 1251 N ATOM 629 CA HIS A 81 62.759 -4.310 59.146 1.00 55.43 C ANISOU 629 CA HIS D 81 5668 7555 7838 -647 972 401 C ATOM 630 C HIS A 81 64.071 -3.708 58.659 1.00 51.01 C ANISOU 630 C HIS D 81 5461 7634 6288 -559 567 149 C ATOM 631 O HIS A 81 64.505 -2.633 59.083 1.00 45.52 O ANISOU 631 O HIS D 81 5018 7368 4909 -184 648 374 O ATOM 632 CB HIS A 81 61.544 -3.688 58.463 1.00 57.02 C ANISOU 632 CB HIS D 81 6080 7270 8314 -800 939 -523 C ATOM 633 CG HIS A 81 61.511 -3.870 56.978 1.00 60.06 C ANISOU 633 CG HIS D 81 6354 8163 8302 -1518 1174 -661 C ATOM 634 ND1 HIS A 81 60.625 -4.734 56.362 1.00 61.95 N ANISOU 634 ND1 HIS D 81 6815 8307 8417 -1426 1148 -885 N ATOM 635 CD2 HIS A 81 62.221 -3.345 55.962 1.00 60.36 C ANISOU 635 CD2 HIS D 81 6050 8619 8265 -1854 520 -442 C ATOM 636 CE1 HIS A 81 60.802 -4.716 55.048 1.00 62.89 C ANISOU 636 CE1 HIS D 81 6559 8713 8624 -1590 -243 -604 C ATOM 637 NE2 HIS A 81 61.782 -3.866 54.773 1.00 62.21 N ANISOU 637 NE2 HIS D 81 6300 8795 8540 -1619 -512 -427 N ATOM 638 N PRO A 82 64.786 -4.347 57.748 1.00 54.15 N ANISOU 638 N PRO D 82 6012 8050 6511 -1228 -93 49 N ATOM 639 CA PRO A 82 66.101 -3.848 57.352 1.00 54.66 C ANISOU 639 CA PRO D 82 6053 8363 6353 -1964 -1118 871 C ATOM 640 C PRO A 82 66.078 -2.502 56.626 1.00 58.22 C ANISOU 640 C PRO D 82 6080 9549 6492 -2448 -1232 928 C ATOM 641 O PRO A 82 67.128 -1.848 56.538 1.00 65.27 O ANISOU 641 O PRO D 82 6657 9514 8628 -3346 -253 386 O ATOM 642 CB PRO A 82 66.593 -4.914 56.366 1.00 57.60 C ANISOU 642 CB PRO D 82 6202 8897 6785 -2495 -1300 694 C ATOM 643 CG PRO A 82 65.749 -6.113 56.631 1.00 61.64 C ANISOU 643 CG PRO D 82 7485 8655 7281 -2687 -1574 473 C ATOM 644 CD PRO A 82 64.400 -5.575 57.047 1.00 61.44 C ANISOU 644 CD PRO D 82 7545 8452 7347 -2048 -486 -22 C ATOM 645 N GLU A 83 64.930 -2.098 56.111 1.00 60.08 N ANISOU 645 N GLU D 83 6911 10136 5779 -2649 -491 346 N ATOM 646 CA GLU A 83 64.724 -0.850 55.397 1.00 58.75 C ANISOU 646 CA GLU D 83 7323 9833 5165 -2875 -527 401 C ATOM 647 C GLU A 83 64.153 0.245 56.283 1.00 49.36 C ANISOU 647 C GLU D 83 6323 7416 5015 -1136 126 106 C ATOM 648 O GLU A 83 63.954 1.388 55.854 1.00 47.67 O ANISOU 648 O GLU D 83 6268 7574 4270 -680 229 332 O ATOM 649 CB GLU A 83 63.800 -1.055 54.194 1.00 72.69 C ANISOU 649 CB GLU D 83 9982 12292 5346 -5237 740 -929 C ATOM 650 CG GLU A 83 64.490 -1.708 53.004 1.00 77.05 C ANISOU 650 CG GLU D 83 10408 13710 5159 -4911 703 -1110 C ATOM 651 CD GLU A 83 65.946 -1.308 52.861 1.00 80.81 C ANISOU 651 CD GLU D 83 10734 13895 6074 -4907 -9 -221 C ATOM 652 OE1 GLU A 83 66.273 -0.103 52.803 1.00 89.49 O ANISOU 652 OE1 GLU D 83 13427 14399 6175 -6529 -398 -45 O ATOM 653 OE2 GLU A 83 66.803 -2.223 52.797 1.00 90.04 O ANISOU 653 OE2 GLU D 83 11351 16138 6721 -3189 509 -996 O ATOM 654 N SER A 84 63.876 -0.014 57.550 1.00 40.77 N ANISOU 654 N SER D 84 4873 5560 5057 -332 490 -137 N ATOM 655 CA SER A 84 63.514 1.086 58.443 1.00 39.95 C ANISOU 655 CA SER D 84 4506 6067 4608 -437 974 -437 C ATOM 656 C SER A 84 64.681 2.055 58.537 1.00 40.12 C ANISOU 656 C SER D 84 4629 6113 4502 -706 506 137 C ATOM 657 O SER A 84 65.822 1.686 58.225 1.00 39.83 O ANISOU 657 O SER D 84 4325 5873 4937 -1163 135 309 O ATOM 658 CB SER A 84 63.173 0.550 59.831 1.00 36.56 C ANISOU 658 CB SER D 84 3963 5194 4736 -166 963 -458 C ATOM 659 OG SER A 84 64.336 0.059 60.479 1.00 34.84 O ANISOU 659 OG SER D 84 4221 4760 4256 -13 543 -616 O ATOM 660 N TYR A 85 64.413 3.288 58.967 1.00 36.91 N ANISOU 660 N TYR D 85 4557 5925 3540 -512 460 563 N ATOM 661 CA TYR A 85 65.549 4.212 59.084 1.00 38.87 C ANISOU 661 CA TYR D 85 4545 6043 4179 -825 976 304 C ATOM 662 C TYR A 85 66.370 3.859 60.320 1.00 36.56 C ANISOU 662 C TYR D 85 4016 5694 4181 -729 923 584 C ATOM 663 O TYR A 85 67.591 4.052 60.329 1.00 35.47 O ANISOU 663 O TYR D 85 4698 5285 3494 -1150 601 460 O ATOM 664 CB TYR A 85 65.063 5.668 59.063 1.00 41.00 C ANISOU 664 CB TYR D 85 4519 6535 4525 -762 1324 -738 C ATOM 665 CG TYR A 85 64.578 6.111 57.687 1.00 45.44 C ANISOU 665 CG TYR D 85 5347 7087 4830 -1091 1841 -806 C ATOM 666 CD1 TYR A 85 64.691 5.241 56.603 1.00 45.44 C ANISOU 666 CD1 TYR D 85 5931 6893 4440 -1465 2026 -799 C ATOM 667 CD2 TYR A 85 64.024 7.352 57.450 1.00 45.14 C ANISOU 667 CD2 TYR D 85 5301 7010 4841 -551 1953 211 C ATOM 668 CE1 TYR A 85 64.268 5.604 55.351 1.00 45.55 C ANISOU 668 CE1 TYR D 85 5920 6908 4481 -1493 2272 -227 C ATOM 669 CE2 TYR A 85 63.585 7.737 56.202 1.00 45.60 C ANISOU 669 CE2 TYR D 85 5642 6929 4757 -819 2032 397 C ATOM 670 CZ TYR A 85 63.714 6.854 55.166 1.00 46.45 C ANISOU 670 CZ TYR D 85 5882 6851 4915 -1443 2206 28 C ATOM 671 OH TYR A 85 63.293 7.192 53.906 1.00 44.32 O ANISOU 671 OH TYR D 85 5391 6372 5076 -1046 2153 -207 O ATOM 672 N TYR A 86 65.731 3.335 61.370 1.00 34.54 N ANISOU 672 N TYR D 86 3497 5354 4274 -575 813 547 N ATOM 673 CA TYR A 86 66.435 2.742 62.493 1.00 33.41 C ANISOU 673 CA TYR D 86 4260 4623 3814 -451 688 435 C ATOM 674 C TYR A 86 67.509 1.790 61.957 1.00 31.85 C ANISOU 674 C TYR D 86 3948 4639 3515 -459 1061 145 C ATOM 675 O TYR A 86 68.697 1.852 62.322 1.00 35.51 O ANISOU 675 O TYR D 86 3996 5070 4426 -291 1607 -120 O ATOM 676 CB TYR A 86 65.428 2.009 63.372 1.00 36.45 C ANISOU 676 CB TYR D 86 5065 4979 3806 -845 382 679 C ATOM 677 CG TYR A 86 66.027 1.018 64.350 1.00 37.16 C ANISOU 677 CG TYR D 86 5383 4560 4175 -1000 727 667 C ATOM 678 CD1 TYR A 86 66.415 1.471 65.609 1.00 37.49 C ANISOU 678 CD1 TYR D 86 5644 4405 4197 -694 821 588 C ATOM 679 CD2 TYR A 86 66.199 -0.337 64.071 1.00 37.27 C ANISOU 679 CD2 TYR D 86 4696 4538 4927 -73 415 567 C ATOM 680 CE1 TYR A 86 66.964 0.622 66.554 1.00 39.99 C ANISOU 680 CE1 TYR D 86 5869 5350 3974 -1235 886 920 C ATOM 681 CE2 TYR A 86 66.750 -1.194 65.002 1.00 37.76 C ANISOU 681 CE2 TYR D 86 4554 4612 5179 237 399 437 C ATOM 682 CZ TYR A 86 67.127 -0.708 66.239 1.00 41.68 C ANISOU 682 CZ TYR D 86 5611 5481 4744 -869 767 708 C ATOM 683 OH TYR A 86 67.675 -1.557 67.177 1.00 41.02 O ANISOU 683 OH TYR D 86 4878 5730 4978 98 398 544 O ATOM 684 N SER A 87 67.088 0.874 61.079 1.00 34.05 N ANISOU 684 N SER D 87 4519 4337 4081 -1045 546 605 N ATOM 685 CA SER A 87 67.985 -0.177 60.603 1.00 35.21 C ANISOU 685 CA SER D 87 4647 4861 3871 -770 492 380 C ATOM 686 C SER A 87 69.118 0.394 59.758 1.00 33.45 C ANISOU 686 C SER D 87 4273 4825 3612 -579 739 247 C ATOM 687 O SER A 87 70.259 -0.026 59.951 1.00 33.44 O ANISOU 687 O SER D 87 3240 5338 4128 -807 228 544 O ATOM 688 CB SER A 87 67.239 -1.246 59.802 1.00 36.43 C ANISOU 688 CB SER D 87 4146 4853 4842 -654 427 102 C ATOM 689 OG SER A 87 66.463 -2.034 60.698 1.00 40.72 O ANISOU 689 OG SER D 87 5011 5327 5135 -1476 -398 470 O ATOM 690 N PHE A 88 68.766 1.309 58.856 1.00 33.41 N ANISOU 690 N PHE D 88 3834 4886 3972 -1075 640 82 N ATOM 691 CA PHE A 88 69.768 2.013 58.077 1.00 30.53 C ANISOU 691 CA PHE D 88 3381 4744 3476 -631 655 -81 C ATOM 692 C PHE A 88 70.799 2.603 59.032 1.00 27.74 C ANISOU 692 C PHE D 88 2666 4843 3031 -313 829 50 C ATOM 693 O PHE A 88 71.995 2.482 58.775 1.00 30.41 O ANISOU 693 O PHE D 88 3926 4671 2959 -249 399 384 O ATOM 694 CB PHE A 88 69.138 3.139 57.251 1.00 28.25 C ANISOU 694 CB PHE D 88 3563 3873 3299 -85 756 -130 C ATOM 695 CG PHE A 88 70.139 4.021 56.500 1.00 30.86 C ANISOU 695 CG PHE D 88 3418 4455 3853 -457 419 466 C ATOM 696 CD1 PHE A 88 70.825 5.133 57.009 1.00 31.31 C ANISOU 696 CD1 PHE D 88 4064 4487 3345 -831 875 514 C ATOM 697 CD2 PHE A 88 70.391 3.674 55.176 1.00 32.13 C ANISOU 697 CD2 PHE D 88 3623 4395 4192 -326 -162 629 C ATOM 698 CE1 PHE A 88 71.740 5.836 56.257 1.00 36.09 C ANISOU 698 CE1 PHE D 88 4567 5131 4015 -1525 -609 1295 C ATOM 699 CE2 PHE A 88 71.289 4.385 54.414 1.00 31.90 C ANISOU 699 CE2 PHE D 88 3708 4616 3796 -736 341 500 C ATOM 700 CZ PHE A 88 71.967 5.469 54.931 1.00 33.19 C ANISOU 700 CZ PHE D 88 3783 5050 3779 -1242 -189 845 C ATOM 701 N MET A 89 70.384 3.369 60.042 1.00 29.41 N ANISOU 701 N MET D 89 2935 4876 3362 -421 500 79 N ATOM 702 CA MET A 89 71.308 4.150 60.870 1.00 29.82 C ANISOU 702 CA MET D 89 2897 4849 3585 -631 451 92 C ATOM 703 C MET A 89 72.245 3.257 61.680 1.00 28.85 C ANISOU 703 C MET D 89 3158 4680 3123 -736 546 107 C ATOM 704 O MET A 89 73.430 3.574 61.848 1.00 29.56 O ANISOU 704 O MET D 89 3066 4752 3415 -354 467 598 O ATOM 705 CB MET A 89 70.554 5.099 61.819 1.00 30.13 C ANISOU 705 CB MET D 89 3193 4668 3586 -720 301 308 C ATOM 706 CG MET A 89 69.907 6.268 61.070 1.00 30.03 C ANISOU 706 CG MET D 89 2944 4561 3905 -524 144 731 C ATOM 707 SD MET A 89 71.152 7.279 60.229 1.00 31.40 S ANISOU 707 SD MET D 89 4243 4373 3316 -908 432 245 S ATOM 708 CE MET A 89 72.257 7.656 61.581 1.00 30.87 C ANISOU 708 CE MET D 89 4601 4671 2457 -598 -366 517 C ATOM 709 N HIS A 90 71.721 2.138 62.199 1.00 30.25 N ANISOU 709 N HIS D 90 3395 4865 3233 -852 488 354 N ATOM 710 CA HIS A 90 72.598 1.225 62.937 1.00 31.13 C ANISOU 710 CA HIS D 90 3569 5055 3205 -723 689 800 C ATOM 711 C HIS A 90 73.603 0.570 62.003 1.00 30.39 C ANISOU 711 C HIS D 90 3538 4858 3150 -617 691 477 C ATOM 712 O HIS A 90 74.817 0.552 62.201 1.00 32.67 O ANISOU 712 O HIS D 90 3926 4798 3690 -483 810 703 O ATOM 713 CB HIS A 90 71.739 0.185 63.689 1.00 31.72 C ANISOU 713 CB HIS D 90 3515 5022 3515 -1054 337 785 C ATOM 714 CG HIS A 90 71.117 0.838 64.895 1.00 32.17 C ANISOU 714 CG HIS D 90 4100 4569 3556 -480 217 674 C ATOM 715 ND1 HIS A 90 71.804 1.063 66.071 1.00 29.81 N ANISOU 715 ND1 HIS D 90 3433 4288 3604 -380 177 698 N ATOM 716 CD2 HIS A 90 69.878 1.342 65.112 1.00 33.01 C ANISOU 716 CD2 HIS D 90 4532 4539 3470 -153 107 233 C ATOM 717 CE1 HIS A 90 71.010 1.662 66.951 1.00 28.80 C ANISOU 717 CE1 HIS D 90 3279 3942 3724 65 245 308 C ATOM 718 NE2 HIS A 90 69.830 1.840 66.396 1.00 30.26 N ANISOU 718 NE2 HIS D 90 3720 4212 3567 -19 255 -218 N ATOM 719 N ARG A 91 73.111 -0.002 60.913 1.00 33.11 N ANISOU 719 N ARG D 91 4353 4960 3268 -1110 444 493 N ATOM 720 CA ARG A 91 73.963 -0.707 59.946 1.00 36.54 C ANISOU 720 CA ARG D 91 4700 5273 3912 -1226 -152 447 C ATOM 721 C ARG A 91 75.040 0.165 59.331 1.00 36.40 C ANISOU 721 C ARG D 91 4322 5316 4192 -652 20 690 C ATOM 722 O ARG A 91 76.147 -0.321 59.098 1.00 35.21 O ANISOU 722 O ARG D 91 3853 6253 3272 -721 142 1023 O ATOM 723 CB ARG A 91 73.058 -1.265 58.851 1.00 43.09 C ANISOU 723 CB ARG D 91 6615 5891 3866 -2657 -136 202 C ATOM 724 CG ARG A 91 73.709 -1.716 57.573 1.00 43.92 C ANISOU 724 CG ARG D 91 6204 5813 4670 -1722 -732 -351 C ATOM 725 CD ARG A 91 72.656 -2.386 56.689 1.00 46.77 C ANISOU 725 CD ARG D 91 5724 6840 5208 -1314 -893 -1308 C ATOM 726 NE ARG A 91 71.659 -1.480 56.141 1.00 47.83 N ANISOU 726 NE ARG D 91 5608 7281 5286 -1124 -1010 -968 N ATOM 727 CZ ARG A 91 70.338 -1.498 56.244 1.00 48.30 C ANISOU 727 CZ ARG D 91 5533 7333 5485 -1133 -564 -607 C ATOM 728 NH1 ARG A 91 69.688 -2.430 56.931 1.00 47.57 N ANISOU 728 NH1 ARG D 91 4548 7368 6160 -1242 -543 -593 N ATOM 729 NH2 ARG A 91 69.664 -0.530 55.627 1.00 47.84 N ANISOU 729 NH2 ARG D 91 6123 6762 5292 -1219 -18 -561 N ATOM 730 N ASN A 92 74.759 1.431 59.044 1.00 32.32 N ANISOU 730 N ASN D 92 4072 4467 3741 -99 -65 946 N ATOM 731 CA ASN A 92 75.721 2.327 58.396 1.00 30.99 C ANISOU 731 CA ASN D 92 4345 4296 3134 -55 -210 654 C ATOM 732 C ASN A 92 76.517 3.182 59.369 1.00 31.42 C ANISOU 732 C ASN D 92 3701 4645 3593 -93 -208 329 C ATOM 733 O ASN A 92 77.545 3.778 59.015 1.00 32.32 O ANISOU 733 O ASN D 92 4081 4476 3724 -48 596 108 O ATOM 734 CB ASN A 92 74.992 3.232 57.375 1.00 35.51 C ANISOU 734 CB ASN D 92 5302 5141 3048 -289 344 650 C ATOM 735 CG ASN A 92 74.515 2.392 56.206 1.00 38.19 C ANISOU 735 CG ASN D 92 5988 5080 3443 157 113 269 C ATOM 736 OD1 ASN A 92 75.343 1.846 55.472 1.00 43.56 O ANISOU 736 OD1 ASN D 92 7035 5406 4112 539 -878 -301 O ATOM 737 ND2 ASN A 92 73.219 2.245 56.010 1.00 37.21 N ANISOU 737 ND2 ASN D 92 6000 4543 3596 -327 826 925 N ATOM 738 N PHE A 93 76.105 3.276 60.629 1.00 31.32 N ANISOU 738 N PHE D 93 3640 5181 3080 -457 518 137 N ATOM 739 CA PHE A 93 76.872 4.165 61.516 1.00 28.57 C ANISOU 739 CA PHE D 93 3360 4444 3050 -53 634 424 C ATOM 740 C PHE A 93 76.923 3.683 62.955 1.00 29.40 C ANISOU 740 C PHE D 93 3412 4803 2958 61 460 346 C ATOM 741 O PHE A 93 77.996 3.427 63.502 1.00 31.72 O ANISOU 741 O PHE D 93 4734 4118 3201 -208 1108 177 O ATOM 742 CB PHE A 93 76.219 5.546 61.434 1.00 30.39 C ANISOU 742 CB PHE D 93 3405 4753 3391 -284 565 244 C ATOM 743 CG PHE A 93 76.892 6.637 62.243 1.00 31.25 C ANISOU 743 CG PHE D 93 3730 4660 3483 -377 581 243 C ATOM 744 CD1 PHE A 93 78.266 6.819 62.157 1.00 29.95 C ANISOU 744 CD1 PHE D 93 3466 4815 3097 -206 1137 161 C ATOM 745 CD2 PHE A 93 76.135 7.462 63.070 1.00 30.73 C ANISOU 745 CD2 PHE D 93 3209 4834 3633 -91 802 -453 C ATOM 746 CE1 PHE A 93 78.876 7.820 62.884 1.00 31.44 C ANISOU 746 CE1 PHE D 93 3859 4705 3380 -265 1086 121 C ATOM 747 CE2 PHE A 93 76.740 8.465 63.802 1.00 31.69 C ANISOU 747 CE2 PHE D 93 3531 4731 3780 -329 747 -274 C ATOM 748 CZ PHE A 93 78.111 8.633 63.704 1.00 30.27 C ANISOU 748 CZ PHE D 93 3337 4728 3437 -361 1314 -233 C ATOM 749 N PHE A 94 75.770 3.566 63.620 1.00 30.65 N ANISOU 749 N PHE D 94 3692 4745 3207 -184 587 693 N ATOM 750 CA PHE A 94 75.833 3.315 65.058 1.00 30.56 C ANISOU 750 CA PHE D 94 3572 4889 3150 -114 485 514 C ATOM 751 C PHE A 94 76.497 1.968 65.344 1.00 30.65 C ANISOU 751 C PHE D 94 3623 4807 3218 -236 584 160 C ATOM 752 O PHE A 94 77.223 1.869 66.345 1.00 33.71 O ANISOU 752 O PHE D 94 4416 4812 3580 -311 1262 241 O ATOM 753 CB PHE A 94 74.459 3.363 65.716 1.00 30.31 C ANISOU 753 CB PHE D 94 3761 4790 2966 -302 103 374 C ATOM 754 CG PHE A 94 73.664 4.642 65.546 1.00 30.45 C ANISOU 754 CG PHE D 94 3625 4942 3003 -409 -384 421 C ATOM 755 CD1 PHE A 94 74.269 5.883 65.689 1.00 33.40 C ANISOU 755 CD1 PHE D 94 4161 5402 3128 -855 168 -429 C ATOM 756 CD2 PHE A 94 72.307 4.581 65.247 1.00 30.80 C ANISOU 756 CD2 PHE D 94 3484 5250 2967 -482 9 -58 C ATOM 757 CE1 PHE A 94 73.522 7.048 65.535 1.00 33.70 C ANISOU 757 CE1 PHE D 94 4110 5756 2937 -1099 -5 -243 C ATOM 758 CE2 PHE A 94 71.554 5.742 65.096 1.00 31.73 C ANISOU 758 CE2 PHE D 94 3582 5591 2883 -645 582 43 C ATOM 759 CZ PHE A 94 72.168 6.976 65.249 1.00 31.82 C ANISOU 759 CZ PHE D 94 3680 5899 2510 -850 -114 199 C ATOM 760 N ASP A 95 76.337 0.940 64.528 1.00 34.08 N ANISOU 760 N ASP D 95 4049 5597 3304 -634 -44 629 N ATOM 761 CA ASP A 95 76.985 -0.346 64.757 1.00 34.35 C ANISOU 761 CA ASP D 95 4079 5311 3660 -767 150 542 C ATOM 762 C ASP A 95 78.501 -0.225 64.822 1.00 36.57 C ANISOU 762 C ASP D 95 4287 5317 4292 -783 779 50 C ATOM 763 O ASP A 95 79.145 -1.146 65.326 1.00 39.69 O ANISOU 763 O ASP D 95 4476 5756 4849 -983 1093 -549 O ATOM 764 CB ASP A 95 76.686 -1.347 63.639 1.00 35.67 C ANISOU 764 CB ASP D 95 3774 5708 4073 -1030 780 -226 C ATOM 765 CG ASP A 95 75.298 -1.941 63.667 1.00 34.99 C ANISOU 765 CG ASP D 95 3899 5693 3703 -1159 304 312 C ATOM 766 OD1 ASP A 95 74.514 -1.664 64.596 1.00 35.39 O ANISOU 766 OD1 ASP D 95 4277 6282 2888 -1864 648 822 O ATOM 767 OD2 ASP A 95 74.979 -2.710 62.734 1.00 33.74 O ANISOU 767 OD2 ASP D 95 4027 5208 3586 -667 131 421 O ATOM 768 N HIS A 96 79.083 0.854 64.317 1.00 36.46 N ANISOU 768 N HIS D 96 4684 5293 3875 -526 734 493 N ATOM 769 CA HIS A 96 80.531 0.956 64.221 1.00 35.36 C ANISOU 769 CA HIS D 96 4348 5461 3624 -367 1275 209 C ATOM 770 C HIS A 96 81.151 2.019 65.101 1.00 35.19 C ANISOU 770 C HIS D 96 4029 5694 3647 -425 1626 -52 C ATOM 771 O HIS A 96 82.378 2.180 65.025 1.00 39.30 O ANISOU 771 O HIS D 96 4650 5773 4509 -187 730 -354 O ATOM 772 CB HIS A 96 80.916 1.269 62.754 1.00 33.49 C ANISOU 772 CB HIS D 96 4456 4624 3644 -211 1455 117 C ATOM 773 CG HIS A 96 80.147 0.337 61.855 1.00 38.62 C ANISOU 773 CG HIS D 96 4939 5649 4085 -462 1172 -559 C ATOM 774 ND1 HIS A 96 80.465 -0.995 61.710 1.00 40.50 N ANISOU 774 ND1 HIS D 96 4989 6057 4344 -654 1265 -701 N ATOM 775 CD2 HIS A 96 79.060 0.552 61.078 1.00 40.14 C ANISOU 775 CD2 HIS D 96 5023 6117 4113 -720 1221 -1071 C ATOM 776 CE1 HIS A 96 79.626 -1.573 60.881 1.00 39.67 C ANISOU 776 CE1 HIS D 96 4932 6129 4012 -470 882 -603 C ATOM 777 NE2 HIS A 96 78.760 -0.650 60.478 1.00 37.90 N ANISOU 777 NE2 HIS D 96 4805 5639 3956 -144 387 -484 N ATOM 778 N VAL A 97 80.360 2.732 65.896 1.00 34.62 N ANISOU 778 N VAL D 97 4461 5321 3373 -477 1494 54 N ATOM 779 CA VAL A 97 80.965 3.774 66.730 1.00 36.46 C ANISOU 779 CA VAL D 97 4874 5289 3692 -460 1178 36 C ATOM 780 C VAL A 97 80.566 3.612 68.193 1.00 35.96 C ANISOU 780 C VAL D 97 4654 5581 3426 -439 1679 -336 C ATOM 781 O VAL A 97 79.814 2.696 68.532 1.00 39.41 O ANISOU 781 O VAL D 97 5804 5797 3372 -914 25 271 O ATOM 782 CB VAL A 97 80.602 5.175 66.210 1.00 35.14 C ANISOU 782 CB VAL D 97 5139 5045 3167 -785 1099 236 C ATOM 783 CG1 VAL A 97 81.091 5.354 64.775 1.00 33.93 C ANISOU 783 CG1 VAL D 97 5390 4646 2856 -222 961 -318 C ATOM 784 CG2 VAL A 97 79.103 5.419 66.303 1.00 34.92 C ANISOU 784 CG2 VAL D 97 4327 5855 3086 -666 223 72 C ATOM 785 N ASP A 98 81.081 4.482 69.059 1.00 36.74 N ANISOU 785 N ASP D 98 4927 5302 3730 -197 1333 -352 N ATOM 786 CA ASP A 98 80.935 4.279 70.499 1.00 34.71 C ANISOU 786 CA ASP D 98 4702 4779 3708 -54 1044 -383 C ATOM 787 C ASP A 98 79.811 5.106 71.119 1.00 35.19 C ANISOU 787 C ASP D 98 4413 4907 4051 -182 914 -851 C ATOM 788 O ASP A 98 79.925 5.526 72.273 1.00 35.65 O ANISOU 788 O ASP D 98 4240 5630 3677 -138 1218 -561 O ATOM 789 CB ASP A 98 82.244 4.592 71.238 1.00 34.30 C ANISOU 789 CB ASP D 98 4389 4744 3901 -267 1045 -509 C ATOM 790 CG ASP A 98 82.726 6.013 70.982 1.00 42.85 C ANISOU 790 CG ASP D 98 6236 5461 4584 -1451 1620 -797 C ATOM 791 OD1 ASP A 98 82.182 6.681 70.068 1.00 41.13 O ANISOU 791 OD1 ASP D 98 5685 5525 4418 -1274 1366 -182 O ATOM 792 OD2 ASP A 98 83.655 6.455 71.695 1.00 40.73 O ANISOU 792 OD2 ASP D 98 6312 4815 4350 -870 814 -248 O ATOM 793 N ILE A 99 78.735 5.319 70.363 1.00 33.19 N ANISOU 793 N ILE D 99 4298 4713 3599 -396 1533 -192 N ATOM 794 CA ILE A 99 77.620 6.055 70.939 1.00 33.90 C ANISOU 794 CA ILE D 99 4695 4378 3809 -187 1492 28 C ATOM 795 C ILE A 99 76.672 5.159 71.747 1.00 36.58 C ANISOU 795 C ILE D 99 5231 4990 3677 -1364 534 289 C ATOM 796 O ILE A 99 76.239 4.077 71.352 1.00 35.36 O ANISOU 796 O ILE D 99 4707 4851 3876 -930 742 -274 O ATOM 797 CB ILE A 99 76.825 6.741 69.821 1.00 35.18 C ANISOU 797 CB ILE D 99 3998 5274 4095 -492 1345 -288 C ATOM 798 CG1 ILE A 99 75.778 7.755 70.297 1.00 34.23 C ANISOU 798 CG1 ILE D 99 4305 4669 4033 -422 1095 -6 C ATOM 799 CG2 ILE A 99 76.168 5.676 68.943 1.00 37.02 C ANISOU 799 CG2 ILE D 99 5269 6154 2643 -704 911 -99 C ATOM 800 CD1 ILE A 99 75.155 8.520 69.127 1.00 34.84 C ANISOU 800 CD1 ILE D 99 4107 4388 4744 -137 1473 605 C ATOM 801 N PRO A 100 76.300 5.630 72.939 1.00 36.88 N ANISOU 801 N PRO D 100 5587 5329 3097 -1531 930 -61 N ATOM 802 CA PRO A 100 75.365 4.899 73.779 1.00 35.29 C ANISOU 802 CA PRO D 100 4840 5035 3535 -1196 356 54 C ATOM 803 C PRO A 100 73.919 4.978 73.307 1.00 36.36 C ANISOU 803 C PRO D 100 4851 5250 3715 -1543 965 -480 C ATOM 804 O PRO A 100 73.477 5.996 72.781 1.00 39.45 O ANISOU 804 O PRO D 100 5703 5877 3407 -1736 1727 -330 O ATOM 805 CB PRO A 100 75.459 5.593 75.149 1.00 33.85 C ANISOU 805 CB PRO D 100 4530 5161 3171 -1211 970 -90 C ATOM 806 CG PRO A 100 76.152 6.886 74.909 1.00 37.64 C ANISOU 806 CG PRO D 100 5633 5438 3229 -1814 917 -195 C ATOM 807 CD PRO A 100 76.770 6.882 73.532 1.00 36.80 C ANISOU 807 CD PRO D 100 5032 5463 3487 -1619 913 121 C ATOM 808 N ALA A 101 73.157 3.904 73.519 1.00 30.99 N ANISOU 808 N ALA D 101 3433 5040 3303 -898 -430 305 N ATOM 809 CA ALA A 101 71.758 3.852 73.125 1.00 33.72 C ANISOU 809 CA ALA D 101 4081 5089 3640 -619 200 736 C ATOM 810 C ALA A 101 70.984 5.041 73.667 1.00 30.88 C ANISOU 810 C ALA D 101 3919 4368 3448 -629 404 347 C ATOM 811 O ALA A 101 70.103 5.599 73.015 1.00 32.77 O ANISOU 811 O ALA D 101 4178 4764 3512 -566 682 392 O ATOM 812 CB ALA A 101 71.117 2.558 73.613 1.00 33.55 C ANISOU 812 CB ALA D 101 3964 5017 3766 -861 593 -5 C ATOM 813 N GLU A 102 71.293 5.454 74.898 1.00 30.35 N ANISOU 813 N GLU D 102 4106 4392 3032 -846 605 806 N ATOM 814 CA GLU A 102 70.444 6.514 75.438 1.00 32.82 C ANISOU 814 CA GLU D 102 4063 5216 3191 -999 506 481 C ATOM 815 C GLU A 102 70.676 7.819 74.695 1.00 31.46 C ANISOU 815 C GLU D 102 3864 4733 3355 -396 864 489 C ATOM 816 O GLU A 102 69.852 8.725 74.802 1.00 34.82 O ANISOU 816 O GLU D 102 3726 5192 4311 -1043 -26 703 O ATOM 817 CB GLU A 102 70.713 6.698 76.928 1.00 35.90 C ANISOU 817 CB GLU D 102 4640 5930 3070 -1466 471 632 C ATOM 818 CG GLU A 102 72.205 6.905 77.174 1.00 42.27 C ANISOU 818 CG GLU D 102 6742 5952 3365 -1389 507 -204 C ATOM 819 CD GLU A 102 72.526 6.693 78.646 1.00 50.47 C ANISOU 819 CD GLU D 102 7995 7533 3648 -1747 1074 -687 C ATOM 820 OE1 GLU A 102 73.196 5.681 78.982 1.00 57.34 O ANISOU 820 OE1 GLU D 102 8278 9155 4353 -1924 1846 -96 O ATOM 821 OE2 GLU A 102 72.092 7.553 79.456 1.00 60.07 O ANISOU 821 OE2 GLU D 102 8655 10831 3336 -3672 902 -1579 O ATOM 822 N ASN A 103 71.771 7.930 73.950 1.00 32.64 N ANISOU 822 N ASN D 103 4396 4734 3272 -404 598 409 N ATOM 823 CA ASN A 103 72.058 9.149 73.203 1.00 33.57 C ANISOU 823 CA ASN D 103 5275 4740 2740 -1027 431 227 C ATOM 824 C ASN A 103 71.416 9.177 71.824 1.00 31.50 C ANISOU 824 C ASN D 103 4370 4610 2987 -737 366 81 C ATOM 825 O ASN A 103 71.489 10.200 71.130 1.00 32.15 O ANISOU 825 O ASN D 103 4006 4785 3422 -525 691 -130 O ATOM 826 CB ASN A 103 73.578 9.301 73.057 1.00 34.34 C ANISOU 826 CB ASN D 103 5232 4745 3072 -912 1374 133 C ATOM 827 CG ASN A 103 74.240 9.822 74.316 1.00 36.60 C ANISOU 827 CG ASN D 103 5288 5096 3522 -883 519 -207 C ATOM 828 OD1 ASN A 103 73.607 9.864 75.378 1.00 35.71 O ANISOU 828 OD1 ASN D 103 5044 5400 3123 -644 1347 -82 O ATOM 829 ND2 ASN A 103 75.501 10.217 74.253 1.00 35.38 N ANISOU 829 ND2 ASN D 103 5136 5176 3130 -685 1303 -224 N ATOM 830 N ILE A 104 70.785 8.096 71.363 1.00 32.91 N ANISOU 830 N ILE D 104 4556 4661 3286 -737 274 -56 N ATOM 831 CA ILE A 104 70.265 7.996 69.997 1.00 31.09 C ANISOU 831 CA ILE D 104 4505 4217 3091 -847 319 231 C ATOM 832 C ILE A 104 68.777 8.280 69.979 1.00 31.25 C ANISOU 832 C ILE D 104 4575 3985 3313 -949 706 460 C ATOM 833 O ILE A 104 67.997 7.670 70.715 1.00 32.27 O ANISOU 833 O ILE D 104 4783 4728 2752 -686 460 863 O ATOM 834 CB ILE A 104 70.516 6.613 69.370 1.00 31.31 C ANISOU 834 CB ILE D 104 4726 4326 2846 -1181 253 675 C ATOM 835 CG1 ILE A 104 72.010 6.285 69.261 1.00 31.28 C ANISOU 835 CG1 ILE D 104 4403 4559 2921 -1144 164 242 C ATOM 836 CG2 ILE A 104 69.826 6.459 68.015 1.00 29.67 C ANISOU 836 CG2 ILE D 104 4248 4267 2758 -881 104 781 C ATOM 837 CD1 ILE A 104 72.285 4.833 68.950 1.00 32.42 C ANISOU 837 CD1 ILE D 104 4680 4730 2907 -1500 -179 876 C ATOM 838 N ASN A 105 68.367 9.223 69.142 1.00 30.46 N ANISOU 838 N ASN D 105 4248 4407 2918 -945 333 590 N ATOM 839 CA ASN A 105 66.947 9.519 69.074 1.00 32.34 C ANISOU 839 CA ASN D 105 4321 4452 3516 -907 626 520 C ATOM 840 C ASN A 105 66.481 9.370 67.629 1.00 33.61 C ANISOU 840 C ASN D 105 4711 4436 3624 -724 491 392 C ATOM 841 O ASN A 105 67.017 9.933 66.678 1.00 30.80 O ANISOU 841 O ASN D 105 4042 4434 3227 -644 -297 398 O ATOM 842 CB ASN A 105 66.677 10.930 69.573 1.00 32.61 C ANISOU 842 CB ASN D 105 4246 4368 3777 -697 574 342 C ATOM 843 CG ASN A 105 67.033 11.124 71.024 1.00 35.09 C ANISOU 843 CG ASN D 105 4708 5076 3550 -880 272 688 C ATOM 844 OD1 ASN A 105 66.190 10.822 71.874 1.00 39.39 O ANISOU 844 OD1 ASN D 105 5905 5078 3981 -569 731 944 O ATOM 845 ND2 ASN A 105 68.237 11.606 71.326 1.00 29.24 N ANISOU 845 ND2 ASN D 105 3888 5167 2057 -734 610 859 N ATOM 846 N LEU A 106 65.440 8.553 67.509 1.00 31.95 N ANISOU 846 N LEU D 106 3952 4279 3909 -177 439 403 N ATOM 847 CA LEU A 106 64.807 8.234 66.242 1.00 34.22 C ANISOU 847 CA LEU D 106 4400 4562 4040 -423 543 158 C ATOM 848 C LEU A 106 63.300 8.318 66.447 1.00 34.71 C ANISOU 848 C LEU D 106 4913 4364 3913 -388 534 20 C ATOM 849 O LEU A 106 62.843 7.969 67.533 1.00 36.23 O ANISOU 849 O LEU D 106 4968 4770 4027 -138 604 233 O ATOM 850 CB LEU A 106 65.182 6.845 65.739 1.00 36.38 C ANISOU 850 CB LEU D 106 4510 4684 4630 -584 565 -435 C ATOM 851 CG LEU A 106 66.521 6.691 65.009 1.00 35.72 C ANISOU 851 CG LEU D 106 3771 5352 4451 -70 829 -681 C ATOM 852 CD1 LEU A 106 67.218 5.432 65.519 1.00 42.00 C ANISOU 852 CD1 LEU D 106 3910 6757 5290 -647 1129 138 C ATOM 853 CD2 LEU A 106 66.360 6.642 63.500 1.00 35.07 C ANISOU 853 CD2 LEU D 106 4779 4133 4415 -597 761 -603 C ATOM 854 N LEU A 107 62.536 8.765 65.467 1.00 34.53 N ANISOU 854 N LEU D 107 4691 4414 4014 -459 540 -33 N ATOM 855 CA LEU A 107 61.086 8.773 65.589 1.00 35.05 C ANISOU 855 CA LEU D 107 4619 4356 4344 -516 1190 479 C ATOM 856 C LEU A 107 60.525 7.358 65.641 1.00 37.46 C ANISOU 856 C LEU D 107 4938 4618 4678 -787 937 911 C ATOM 857 O LEU A 107 60.955 6.459 64.903 1.00 38.05 O ANISOU 857 O LEU D 107 5313 4559 4585 -800 755 183 O ATOM 858 CB LEU A 107 60.517 9.587 64.413 1.00 34.30 C ANISOU 858 CB LEU D 107 4586 4483 3964 -534 928 451 C ATOM 859 CG LEU A 107 60.567 11.101 64.690 1.00 34.06 C ANISOU 859 CG LEU D 107 4502 4681 3757 -547 836 807 C ATOM 860 CD1 LEU A 107 60.498 11.900 63.388 1.00 29.82 C ANISOU 860 CD1 LEU D 107 3380 4872 3080 -19 332 269 C ATOM 861 CD2 LEU A 107 59.469 11.492 65.662 1.00 33.01 C ANISOU 861 CD2 LEU D 107 5034 4156 3351 -512 683 489 C ATOM 862 N ASN A 108 59.555 7.132 66.542 1.00 39.13 N ANISOU 862 N ASN D 108 5989 4292 4588 -435 1104 684 N ATOM 863 CA ASN A 108 58.918 5.820 66.642 1.00 39.84 C ANISOU 863 CA ASN D 108 6362 4176 4599 -440 1482 556 C ATOM 864 C ASN A 108 57.750 5.725 65.669 1.00 40.69 C ANISOU 864 C ASN D 108 6208 4324 4928 -519 1857 483 C ATOM 865 O ASN A 108 56.631 6.171 65.936 1.00 43.29 O ANISOU 865 O ASN D 108 6790 3902 5756 -377 1638 598 O ATOM 866 CB ASN A 108 58.458 5.546 68.074 1.00 40.41 C ANISOU 866 CB ASN D 108 6331 4262 4760 21 1660 794 C ATOM 867 CG ASN A 108 57.912 4.148 68.264 1.00 38.84 C ANISOU 867 CG ASN D 108 5505 4307 4946 398 2042 806 C ATOM 868 OD1 ASN A 108 57.802 3.342 67.329 1.00 53.94 O ANISOU 868 OD1 ASN D 108 10729 5477 4290 -2612 3158 -571 O ATOM 869 ND2 ASN A 108 57.550 3.853 69.519 1.00 46.61 N ANISOU 869 ND2 ASN D 108 7358 5603 4750 -825 2625 612 N ATOM 870 N GLY A 109 57.993 5.129 64.504 1.00 40.85 N ANISOU 870 N GLY D 109 6270 4240 5010 -754 1842 113 N ATOM 871 CA GLY A 109 56.963 5.021 63.482 1.00 39.63 C ANISOU 871 CA GLY D 109 5024 4631 5402 78 1429 -31 C ATOM 872 C GLY A 109 55.855 4.065 63.878 1.00 42.22 C ANISOU 872 C GLY D 109 5622 4535 5887 -177 1869 -417 C ATOM 873 O GLY A 109 54.824 3.967 63.217 1.00 38.25 O ANISOU 873 O GLY D 109 4210 4790 5534 -176 293 -952 O ATOM 874 N ASN A 110 56.068 3.354 64.982 1.00 44.46 N ANISOU 874 N ASN D 110 5804 4980 6109 -380 1982 -24 N ATOM 875 CA ASN A 110 55.073 2.423 65.482 1.00 48.58 C ANISOU 875 CA ASN D 110 6429 5414 6615 -1018 1249 443 C ATOM 876 C ASN A 110 54.385 2.975 66.715 1.00 50.82 C ANISOU 876 C ASN D 110 6823 5772 6715 -709 1144 566 C ATOM 877 O ASN A 110 53.615 2.253 67.349 1.00 48.88 O ANISOU 877 O ASN D 110 7062 4473 7037 13 812 -66 O ATOM 878 CB ASN A 110 55.733 1.057 65.756 1.00 50.36 C ANISOU 878 CB ASN D 110 6487 5502 7146 -1451 1298 21 C ATOM 879 CG ASN A 110 56.157 0.387 64.456 1.00 50.62 C ANISOU 879 CG ASN D 110 6301 5774 7159 -1249 1332 -411 C ATOM 880 OD1 ASN A 110 55.313 0.108 63.598 1.00 52.61 O ANISOU 880 OD1 ASN D 110 6575 6222 7194 -811 1545 -529 O ATOM 881 ND2 ASN A 110 57.444 0.117 64.266 1.00 48.08 N ANISOU 881 ND2 ASN D 110 6147 5904 6217 -1209 1853 -182 N ATOM 882 N ALA A 111 54.623 4.234 67.086 1.00 46.92 N ANISOU 882 N ALA D 111 5573 5931 6322 -309 1461 920 N ATOM 883 CA ALA A 111 53.949 4.751 68.282 1.00 48.47 C ANISOU 883 CA ALA D 111 5790 6212 6414 129 1455 1048 C ATOM 884 C ALA A 111 52.430 4.670 68.112 1.00 52.94 C ANISOU 884 C ALA D 111 6797 6316 7001 455 1192 819 C ATOM 885 O ALA A 111 51.865 4.841 67.027 1.00 54.44 O ANISOU 885 O ALA D 111 7637 5640 7410 41 1768 691 O ATOM 886 CB ALA A 111 54.375 6.169 68.622 1.00 45.03 C ANISOU 886 CB ALA D 111 3698 5647 7765 1271 726 1998 C ATOM 887 N PRO A 112 51.763 4.383 69.229 1.00 55.19 N ANISOU 887 N PRO D 112 7572 6396 7003 848 638 742 N ATOM 888 CA PRO A 112 50.300 4.251 69.219 1.00 54.22 C ANISOU 888 CA PRO D 112 6868 6455 7279 743 569 625 C ATOM 889 C PRO A 112 49.647 5.617 69.025 1.00 59.71 C ANISOU 889 C PRO D 112 7025 6982 8682 359 1164 -242 C ATOM 890 O PRO A 112 48.690 5.740 68.253 1.00 77.93 O ANISOU 890 O PRO D 112 8031 7763 13817 567 2677 -2149 O ATOM 891 CB PRO A 112 49.988 3.662 70.596 1.00 57.18 C ANISOU 891 CB PRO D 112 7833 6256 7639 966 1000 896 C ATOM 892 CG PRO A 112 51.090 4.203 71.454 1.00 54.16 C ANISOU 892 CG PRO D 112 7183 6144 7253 1389 1098 1162 C ATOM 893 CD PRO A 112 52.316 4.171 70.576 1.00 53.80 C ANISOU 893 CD PRO D 112 6856 6468 7117 1172 1100 1377 C ATOM 894 N ASP A 113 50.157 6.651 69.688 1.00 58.97 N ANISOU 894 N ASP D 113 7871 6976 7558 -703 978 1015 N ATOM 895 CA ASP A 113 49.648 8.004 69.486 1.00 54.23 C ANISOU 895 CA ASP D 113 7651 6420 6535 -174 564 1816 C ATOM 896 C ASP A 113 50.654 8.848 68.700 1.00 52.93 C ANISOU 896 C ASP D 113 7586 6363 6163 180 639 1741 C ATOM 897 O ASP A 113 51.535 9.467 69.301 1.00 44.98 O ANISOU 897 O ASP D 113 5320 6095 5676 1212 693 1948 O ATOM 898 CB ASP A 113 49.353 8.678 70.823 1.00 54.08 C ANISOU 898 CB ASP D 113 7975 6588 5985 -110 988 1859 C ATOM 899 CG ASP A 113 48.660 10.016 70.670 1.00 58.32 C ANISOU 899 CG ASP D 113 7835 7247 7078 -138 293 1121 C ATOM 900 OD1 ASP A 113 48.618 10.566 69.556 1.00 53.98 O ANISOU 900 OD1 ASP D 113 5905 7266 7339 387 -41 1707 O ATOM 901 OD2 ASP A 113 48.138 10.528 71.682 1.00 61.72 O ANISOU 901 OD2 ASP D 113 8558 8578 6314 -863 -16 -699 O ATOM 902 N ILE A 114 50.495 8.854 67.382 1.00 51.56 N ANISOU 902 N ILE D 114 6967 6312 6311 -162 1211 1397 N ATOM 903 CA ILE A 114 51.394 9.560 66.478 1.00 52.94 C ANISOU 903 CA ILE D 114 7380 6739 5997 -693 1291 1417 C ATOM 904 C ILE A 114 51.592 11.025 66.824 1.00 49.80 C ANISOU 904 C ILE D 114 7019 5918 5983 -7 1190 1105 C ATOM 905 O ILE A 114 52.736 11.496 66.890 1.00 49.57 O ANISOU 905 O ILE D 114 6631 5887 6317 133 1737 1794 O ATOM 906 CB ILE A 114 50.870 9.462 65.030 1.00 55.04 C ANISOU 906 CB ILE D 114 7595 7188 6129 -1136 1136 1055 C ATOM 907 CG1 ILE A 114 50.931 8.033 64.480 1.00 59.43 C ANISOU 907 CG1 ILE D 114 8000 7943 6638 -2048 1462 914 C ATOM 908 CG2 ILE A 114 51.607 10.433 64.121 1.00 45.34 C ANISOU 908 CG2 ILE D 114 6371 5895 4960 -544 270 324 C ATOM 909 CD1 ILE A 114 52.307 7.421 64.711 1.00 67.13 C ANISOU 909 CD1 ILE D 114 7512 7919 10077 -1945 751 1921 C ATOM 910 N ASP A 115 50.527 11.795 67.047 1.00 48.77 N ANISOU 910 N ASP D 115 7171 5406 5955 66 1323 1323 N ATOM 911 CA ASP A 115 50.789 13.204 67.348 1.00 48.39 C ANISOU 911 CA ASP D 115 7228 5264 5896 282 442 1777 C ATOM 912 C ASP A 115 51.592 13.367 68.627 1.00 47.13 C ANISOU 912 C ASP D 115 6772 5891 5245 168 83 1979 C ATOM 913 O ASP A 115 52.385 14.300 68.724 1.00 40.86 O ANISOU 913 O ASP D 115 4896 6366 4264 -85 440 1617 O ATOM 914 CB ASP A 115 49.486 13.999 67.449 1.00 54.10 C ANISOU 914 CB ASP D 115 7425 5973 7156 638 193 1521 C ATOM 915 CG ASP A 115 48.837 14.077 66.075 1.00 57.98 C ANISOU 915 CG ASP D 115 7268 7039 7724 782 726 1041 C ATOM 916 OD1 ASP A 115 49.383 13.478 65.121 1.00 63.54 O ANISOU 916 OD1 ASP D 115 8889 7752 7500 -32 -83 573 O ATOM 917 OD2 ASP A 115 47.783 14.732 65.959 1.00 72.11 O ANISOU 917 OD2 ASP D 115 8323 7947 11127 1838 1191 119 O ATOM 918 N ALA A 116 51.369 12.458 69.562 1.00 45.03 N ANISOU 918 N ALA D 116 6608 5130 5370 362 -231 2216 N ATOM 919 CA ALA A 116 52.109 12.493 70.819 1.00 46.84 C ANISOU 919 CA ALA D 116 7112 5580 5106 -215 11 2295 C ATOM 920 C ALA A 116 53.598 12.213 70.618 1.00 42.63 C ANISOU 920 C ALA D 116 6829 5093 4274 -485 416 1882 C ATOM 921 O ALA A 116 54.466 12.897 71.192 1.00 43.65 O ANISOU 921 O ALA D 116 6664 5785 4135 -790 1404 1188 O ATOM 922 CB ALA A 116 51.486 11.491 71.772 1.00 45.03 C ANISOU 922 CB ALA D 116 5193 5521 6397 378 640 2551 C ATOM 923 N GLU A 117 53.885 11.204 69.805 1.00 40.19 N ANISOU 923 N GLU D 117 5901 5384 3985 -321 1107 1559 N ATOM 924 CA GLU A 117 55.256 10.851 69.421 1.00 42.41 C ANISOU 924 CA GLU D 117 6550 5019 4547 -371 582 1690 C ATOM 925 C GLU A 117 55.959 12.091 68.872 1.00 40.28 C ANISOU 925 C GLU D 117 6191 4878 4236 -462 829 1007 C ATOM 926 O GLU A 117 57.079 12.423 69.288 1.00 37.84 O ANISOU 926 O GLU D 117 5358 4923 4096 -54 799 1325 O ATOM 927 CB GLU A 117 55.223 9.710 68.413 1.00 41.10 C ANISOU 927 CB GLU D 117 6379 4044 5193 -218 420 1696 C ATOM 928 CG GLU A 117 56.509 9.224 67.777 1.00 39.62 C ANISOU 928 CG GLU D 117 5565 4581 4906 -77 1126 1712 C ATOM 929 CD GLU A 117 57.524 8.775 68.811 1.00 43.56 C ANISOU 929 CD GLU D 117 6478 4914 5158 -169 1533 1396 C ATOM 930 OE1 GLU A 117 57.087 8.360 69.911 1.00 40.98 O ANISOU 930 OE1 GLU D 117 5095 5747 4727 12 796 1432 O ATOM 931 OE2 GLU A 117 58.741 8.851 68.519 1.00 41.60 O ANISOU 931 OE2 GLU D 117 5582 5443 4780 120 1472 1403 O ATOM 932 N CYS A 118 55.292 12.781 67.944 1.00 36.59 N ANISOU 932 N CYS D 118 5340 4757 3805 -197 141 868 N ATOM 933 CA CYS A 118 55.891 13.933 67.277 1.00 35.42 C ANISOU 933 CA CYS D 118 4597 4601 4259 145 389 845 C ATOM 934 C CYS A 118 56.125 15.064 68.266 1.00 35.22 C ANISOU 934 C CYS D 118 4292 4824 4266 153 357 926 C ATOM 935 O CYS A 118 57.185 15.692 68.270 1.00 36.37 O ANISOU 935 O CYS D 118 5254 4837 3727 -302 589 909 O ATOM 936 CB CYS A 118 55.010 14.369 66.101 1.00 38.72 C ANISOU 936 CB CYS D 118 6019 4186 4508 272 977 881 C ATOM 937 SG CYS A 118 54.984 13.110 64.776 1.00 42.29 S ANISOU 937 SG CYS D 118 6457 5128 4485 -445 1404 310 S ATOM 938 N ARG A 119 55.164 15.335 69.130 1.00 39.08 N ANISOU 938 N ARG D 119 3719 5677 5451 379 14 1271 N ATOM 939 CA ARG A 119 55.343 16.293 70.217 1.00 44.31 C ANISOU 939 CA ARG D 119 4903 5728 6206 455 -1119 1422 C ATOM 940 C ARG A 119 56.502 16.005 71.161 1.00 43.76 C ANISOU 940 C ARG D 119 5164 6305 5159 166 -1336 1150 C ATOM 941 O ARG A 119 57.273 16.869 71.603 1.00 41.45 O ANISOU 941 O ARG D 119 5564 6327 3860 16 -1556 1553 O ATOM 942 CB ARG A 119 54.022 16.301 71.012 1.00 52.18 C ANISOU 942 CB ARG D 119 6079 6237 7511 557 -1925 2009 C ATOM 943 CG ARG A 119 53.681 17.637 71.645 1.00 62.59 C ANISOU 943 CG ARG D 119 7520 7269 8992 -116 -3727 3064 C ATOM 944 CD ARG A 119 52.344 17.567 72.401 1.00 70.06 C ANISOU 944 CD ARG D 119 8623 7363 10634 217 -4665 3157 C ATOM 945 NE ARG A 119 51.329 16.935 71.552 1.00 77.92 N ANISOU 945 NE ARG D 119 10834 7176 11594 33 -3455 2858 N ATOM 946 CZ ARG A 119 50.553 15.907 71.864 1.00 81.38 C ANISOU 946 CZ ARG D 119 11888 7786 11248 -990 -3153 2568 C ATOM 947 NH1 ARG A 119 50.632 15.331 73.065 1.00 79.87 N ANISOU 947 NH1 ARG D 119 11090 9685 9573 -1384 -5734 3721 N ATOM 948 NH2 ARG A 119 49.678 15.452 70.965 1.00 78.89 N ANISOU 948 NH2 ARG D 119 10717 8579 10677 -1734 -5670 2193 N ATOM 949 N GLN A 120 56.666 14.737 71.532 1.00 43.70 N ANISOU 949 N GLN D 120 5581 6454 4567 -50 -1033 1137 N ATOM 950 CA GLN A 120 57.744 14.350 72.442 1.00 43.77 C ANISOU 950 CA GLN D 120 6264 6209 4159 -91 -698 1472 C ATOM 951 C GLN A 120 59.125 14.522 71.822 1.00 42.63 C ANISOU 951 C GLN D 120 6254 5980 3964 -171 -1138 1024 C ATOM 952 O GLN A 120 60.086 14.937 72.481 1.00 40.35 O ANISOU 952 O GLN D 120 5549 6318 3463 -59 -564 1020 O ATOM 953 CB GLN A 120 57.534 12.889 72.872 1.00 51.15 C ANISOU 953 CB GLN D 120 8110 6639 4685 -934 797 1022 C ATOM 954 CG GLN A 120 56.276 12.702 73.695 1.00 60.59 C ANISOU 954 CG GLN D 120 10526 6828 5666 -1654 -68 1791 C ATOM 955 CD GLN A 120 55.879 11.251 73.877 1.00 66.38 C ANISOU 955 CD GLN D 120 11134 7736 6353 -2259 807 2050 C ATOM 956 OE1 GLN A 120 56.685 10.338 73.674 1.00 80.51 O ANISOU 956 OE1 GLN D 120 11531 10907 8151 -3681 -1848 4294 O ATOM 957 NE2 GLN A 120 54.618 11.042 74.260 1.00 65.48 N ANISOU 957 NE2 GLN D 120 12268 6515 6094 -1355 4376 647 N ATOM 958 N TYR A 121 59.219 14.192 70.527 1.00 39.41 N ANISOU 958 N TYR D 121 5523 5545 3904 -557 -941 999 N ATOM 959 CA TYR A 121 60.480 14.384 69.814 1.00 37.24 C ANISOU 959 CA TYR D 121 4934 5576 3642 -351 -578 889 C ATOM 960 C TYR A 121 60.942 15.837 69.912 1.00 35.57 C ANISOU 960 C TYR D 121 4686 5266 3564 -56 -151 609 C ATOM 961 O TYR A 121 62.090 16.115 70.266 1.00 39.31 O ANISOU 961 O TYR D 121 5066 5420 4451 -17 279 342 O ATOM 962 CB TYR A 121 60.317 13.968 68.356 1.00 32.78 C ANISOU 962 CB TYR D 121 4529 4380 3547 235 -18 741 C ATOM 963 CG TYR A 121 61.547 13.454 67.648 1.00 32.72 C ANISOU 963 CG TYR D 121 4195 4876 3362 79 -13 842 C ATOM 964 CD1 TYR A 121 62.193 12.312 68.118 1.00 32.38 C ANISOU 964 CD1 TYR D 121 4294 4542 3467 -45 155 697 C ATOM 965 CD2 TYR A 121 62.053 14.111 66.522 1.00 29.32 C ANISOU 965 CD2 TYR D 121 4353 3681 3105 719 514 215 C ATOM 966 CE1 TYR A 121 63.316 11.824 67.491 1.00 29.55 C ANISOU 966 CE1 TYR D 121 4346 3796 3086 310 491 52 C ATOM 967 CE2 TYR A 121 63.174 13.629 65.884 1.00 26.68 C ANISOU 967 CE2 TYR D 121 4082 3327 2727 406 295 -193 C ATOM 968 CZ TYR A 121 63.789 12.500 66.376 1.00 29.38 C ANISOU 968 CZ TYR D 121 4160 3638 3366 350 482 232 C ATOM 969 OH TYR A 121 64.914 11.989 65.756 1.00 30.92 O ANISOU 969 OH TYR D 121 3871 4298 3580 135 349 502 O ATOM 970 N GLU A 122 60.055 16.779 69.598 1.00 34.29 N ANISOU 970 N GLU D 122 4451 5144 3434 344 -834 1356 N ATOM 971 CA GLU A 122 60.395 18.199 69.697 1.00 37.50 C ANISOU 971 CA GLU D 122 4800 5818 3630 -156 498 -49 C ATOM 972 C GLU A 122 60.738 18.540 71.144 1.00 36.58 C ANISOU 972 C GLU D 122 4713 5633 3554 185 412 101 C ATOM 973 O GLU A 122 61.650 19.311 71.443 1.00 38.91 O ANISOU 973 O GLU D 122 4594 6036 4155 -416 -691 -119 O ATOM 974 CB GLU A 122 59.258 19.113 69.241 1.00 37.54 C ANISOU 974 CB GLU D 122 4948 5625 3692 -122 635 -69 C ATOM 975 CG GLU A 122 58.931 18.991 67.756 1.00 35.43 C ANISOU 975 CG GLU D 122 4337 5596 3529 370 210 271 C ATOM 976 CD GLU A 122 59.884 19.757 66.866 1.00 39.13 C ANISOU 976 CD GLU D 122 5390 5602 3876 -300 368 243 C ATOM 977 OE1 GLU A 122 60.689 20.554 67.392 1.00 40.51 O ANISOU 977 OE1 GLU D 122 5324 5966 4101 -741 -1057 413 O ATOM 978 OE2 GLU A 122 59.802 19.529 65.630 1.00 37.69 O ANISOU 978 OE2 GLU D 122 5819 4757 3746 -47 903 257 O ATOM 979 N GLU A 123 59.957 17.934 72.051 1.00 41.44 N ANISOU 979 N GLU D 123 5037 6678 4029 -410 -421 951 N ATOM 980 CA GLU A 123 60.283 18.240 73.452 1.00 45.19 C ANISOU 980 CA GLU D 123 6449 6777 3942 -681 -248 1030 C ATOM 981 C GLU A 123 61.659 17.719 73.835 1.00 44.81 C ANISOU 981 C GLU D 123 5963 7095 3967 -1105 -108 473 C ATOM 982 O GLU A 123 62.417 18.368 74.561 1.00 42.83 O ANISOU 982 O GLU D 123 6460 6124 3688 -484 -1306 1300 O ATOM 983 CB GLU A 123 59.193 17.657 74.356 1.00 52.97 C ANISOU 983 CB GLU D 123 7888 7594 4642 -1002 -1478 1840 C ATOM 984 CG GLU A 123 58.176 18.723 74.728 1.00 62.88 C ANISOU 984 CG GLU D 123 8488 7466 7937 376 -1773 1479 C ATOM 985 CD GLU A 123 56.781 18.461 74.207 1.00 75.26 C ANISOU 985 CD GLU D 123 10105 7469 11021 -13 -239 782 C ATOM 986 OE1 GLU A 123 56.108 17.541 74.722 1.00 94.72 O ANISOU 986 OE1 GLU D 123 15817 7792 12381 -1954 62 894 O ATOM 987 OE2 GLU A 123 56.349 19.187 73.273 1.00108.70 O ANISOU 987 OE2 GLU D 123 15891 10579 14830 -1925 4492 -3558 O ATOM 988 N LYS A 124 62.005 16.521 73.347 1.00 43.43 N ANISOU 988 N LYS D 124 6342 6311 3849 -1081 -739 1307 N ATOM 989 CA LYS A 124 63.329 15.991 73.689 1.00 43.60 C ANISOU 989 CA LYS D 124 5986 6783 3799 -1212 -366 1516 C ATOM 990 C LYS A 124 64.434 16.894 73.146 1.00 41.43 C ANISOU 990 C LYS D 124 6080 6378 3283 -809 740 844 C ATOM 991 O LYS A 124 65.424 17.145 73.834 1.00 39.70 O ANISOU 991 O LYS D 124 5588 6905 2593 -416 174 717 O ATOM 992 CB LYS A 124 63.484 14.556 73.177 1.00 48.70 C ANISOU 992 CB LYS D 124 6154 7889 4462 -1797 -661 2218 C ATOM 993 CG LYS A 124 63.753 13.514 74.245 1.00 63.43 C ANISOU 993 CG LYS D 124 7294 10431 6376 -3061 617 2158 C ATOM 994 CD LYS A 124 64.707 12.429 73.767 1.00 65.56 C ANISOU 994 CD LYS D 124 7032 11017 6862 -1995 1436 1559 C ATOM 995 CE LYS A 124 65.681 12.030 74.868 1.00 69.50 C ANISOU 995 CE LYS D 124 8209 12180 6018 -2846 2079 1601 C ATOM 996 NZ LYS A 124 66.557 10.880 74.477 1.00 75.15 N ANISOU 996 NZ LYS D 124 7038 17031 4484 -4576 3724 -1262 N ATOM 997 N ILE A 125 64.295 17.402 71.920 1.00 38.54 N ANISOU 997 N ILE D 125 4878 6076 3689 -691 1108 567 N ATOM 998 CA ILE A 125 65.333 18.307 71.400 1.00 34.53 C ANISOU 998 CA ILE D 125 3711 6172 3237 -519 393 769 C ATOM 999 C ILE A 125 65.492 19.502 72.341 1.00 38.08 C ANISOU 999 C ILE D 125 4373 6461 3635 -657 3 649 C ATOM 1000 O ILE A 125 66.595 19.861 72.776 1.00 40.44 O ANISOU 1000 O ILE D 125 5635 6242 3488 -613 -524 843 O ATOM 1001 CB ILE A 125 65.001 18.781 69.978 1.00 38.18 C ANISOU 1001 CB ILE D 125 4638 6414 3453 -940 800 561 C ATOM 1002 CG1 ILE A 125 65.054 17.669 68.936 1.00 37.72 C ANISOU 1002 CG1 ILE D 125 4797 6191 3344 -1317 1369 -151 C ATOM 1003 CG2 ILE A 125 65.921 19.932 69.587 1.00 31.39 C ANISOU 1003 CG2 ILE D 125 3778 5944 2204 -412 106 304 C ATOM 1004 CD1 ILE A 125 64.194 17.890 67.714 1.00 33.33 C ANISOU 1004 CD1 ILE D 125 3304 5887 3474 -140 1071 460 C ATOM 1005 N ARG A 126 64.339 20.104 72.675 1.00 39.91 N ANISOU 1005 N ARG D 126 5093 6528 3541 -592 -799 1236 N ATOM 1006 CA ARG A 126 64.367 21.266 73.569 1.00 41.68 C ANISOU 1006 CA ARG D 126 4615 6590 4630 -591 -504 396 C ATOM 1007 C ARG A 126 64.905 20.855 74.929 1.00 42.83 C ANISOU 1007 C ARG D 126 6096 6161 4016 -833 -706 654 C ATOM 1008 O ARG A 126 65.461 21.691 75.641 1.00 50.68 O ANISOU 1008 O ARG D 126 8113 7268 3876 -1592 -1649 650 O ATOM 1009 CB ARG A 126 62.996 21.935 73.703 1.00 49.83 C ANISOU 1009 CB ARG D 126 4423 7446 7066 -493 -945 639 C ATOM 1010 CG ARG A 126 62.472 22.446 72.367 1.00 61.30 C ANISOU 1010 CG ARG D 126 5305 8610 9378 -150 1073 -467 C ATOM 1011 CD ARG A 126 61.081 23.054 72.435 1.00 70.98 C ANISOU 1011 CD ARG D 126 6066 8802 12102 403 337 -1383 C ATOM 1012 NE ARG A 126 60.320 22.926 71.185 1.00 75.78 N ANISOU 1012 NE ARG D 126 6410 9126 13256 732 279 -2434 N ATOM 1013 CZ ARG A 126 59.103 22.386 71.127 1.00 80.52 C ANISOU 1013 CZ ARG D 126 7729 9012 13852 270 -308 -2303 C ATOM 1014 NH1 ARG A 126 58.519 21.931 72.236 1.00 75.26 N ANISOU 1014 NH1 ARG D 126 3984 10070 14544 614 -1937 -1211 N ATOM 1015 NH2 ARG A 126 58.455 22.293 69.967 1.00 84.71 N ANISOU 1015 NH2 ARG D 126 8443 9133 14609 154 -560 -3265 N ATOM 1016 N SER A 127 64.784 19.592 75.343 1.00 45.17 N ANISOU 1016 N SER D 127 6405 6105 4654 -537 272 666 N ATOM 1017 CA SER A 127 65.329 19.291 76.685 1.00 45.18 C ANISOU 1017 CA SER D 127 6382 6517 4269 -264 -284 650 C ATOM 1018 C SER A 127 66.838 19.477 76.665 1.00 44.06 C ANISOU 1018 C SER D 127 5846 6620 4274 -268 -1001 7 C ATOM 1019 O SER A 127 67.418 19.858 77.673 1.00 51.05 O ANISOU 1019 O SER D 127 9415 6449 3533 -269 -623 590 O ATOM 1020 CB SER A 127 64.968 17.887 77.155 1.00 46.96 C ANISOU 1020 CB SER D 127 6559 6827 4457 -337 566 241 C ATOM 1021 OG SER A 127 65.638 16.919 76.343 1.00 47.73 O ANISOU 1021 OG SER D 127 5686 6576 5873 44 856 1070 O ATOM 1022 N TYR A 128 67.499 19.230 75.537 1.00 41.48 N ANISOU 1022 N TYR D 128 5253 6118 4389 -622 -1232 -208 N ATOM 1023 CA TYR A 128 68.937 19.425 75.480 1.00 41.75 C ANISOU 1023 CA TYR D 128 5167 6292 4404 -421 -748 -126 C ATOM 1024 C TYR A 128 69.252 20.873 75.136 1.00 43.28 C ANISOU 1024 C TYR D 128 5150 5889 5406 -311 -543 -473 C ATOM 1025 O TYR A 128 70.350 21.341 75.414 1.00 50.69 O ANISOU 1025 O TYR D 128 6660 5912 6687 -290 -152 -716 O ATOM 1026 CB TYR A 128 69.602 18.553 74.421 1.00 40.32 C ANISOU 1026 CB TYR D 128 5256 6154 3908 -642 -520 476 C ATOM 1027 CG TYR A 128 69.676 17.081 74.759 1.00 38.84 C ANISOU 1027 CG TYR D 128 5027 5838 3892 -375 -576 486 C ATOM 1028 CD1 TYR A 128 70.660 16.593 75.607 1.00 40.46 C ANISOU 1028 CD1 TYR D 128 5413 5790 4169 -563 -303 184 C ATOM 1029 CD2 TYR A 128 68.745 16.194 74.212 1.00 36.34 C ANISOU 1029 CD2 TYR D 128 4779 5615 3412 -143 -577 724 C ATOM 1030 CE1 TYR A 128 70.730 15.251 75.918 1.00 41.77 C ANISOU 1030 CE1 TYR D 128 6297 5884 3690 -902 535 585 C ATOM 1031 CE2 TYR A 128 68.820 14.850 74.526 1.00 39.91 C ANISOU 1031 CE2 TYR D 128 4938 5837 4389 -371 -305 415 C ATOM 1032 CZ TYR A 128 69.807 14.392 75.374 1.00 41.74 C ANISOU 1032 CZ TYR D 128 6221 6101 3537 -1268 787 509 C ATOM 1033 OH TYR A 128 69.848 13.043 75.657 1.00 42.11 O ANISOU 1033 OH TYR D 128 6000 5514 4487 -746 719 1670 O ATOM 1034 N GLY A 129 68.295 21.561 74.511 1.00 42.11 N ANISOU 1034 N GLY D 129 5664 6058 4278 -85 -183 498 N ATOM 1035 CA GLY A 129 68.534 22.973 74.242 1.00 40.48 C ANISOU 1035 CA GLY D 129 6175 6021 3184 -368 176 -100 C ATOM 1036 C GLY A 129 68.568 23.221 72.753 1.00 37.91 C ANISOU 1036 C GLY D 129 5236 6069 3100 293 -58 -536 C ATOM 1037 O GLY A 129 67.747 23.963 72.231 1.00 40.86 O ANISOU 1037 O GLY D 129 5364 6091 4071 -64 550 -542 O ATOM 1038 N LYS A 130 69.502 22.606 72.027 1.00 41.09 N ANISOU 1038 N LYS D 130 5571 6204 3836 -158 -867 -467 N ATOM 1039 CA LYS A 130 69.496 22.867 70.593 1.00 39.33 C ANISOU 1039 CA LYS D 130 5076 5865 4003 -166 -797 221 C ATOM 1040 C LYS A 130 70.343 21.826 69.872 1.00 34.07 C ANISOU 1040 C LYS D 130 4613 4869 3463 492 -65 -221 C ATOM 1041 O LYS A 130 71.207 21.237 70.519 1.00 37.69 O ANISOU 1041 O LYS D 130 4983 5663 3676 -107 1081 345 O ATOM 1042 CB LYS A 130 70.071 24.243 70.274 1.00 48.04 C ANISOU 1042 CB LYS D 130 6199 6826 5226 -1318 -1696 846 C ATOM 1043 CG LYS A 130 71.563 24.281 70.619 1.00 56.92 C ANISOU 1043 CG LYS D 130 8814 5910 6904 -696 -2458 1845 C ATOM 1044 CD LYS A 130 72.134 25.629 70.188 1.00 64.23 C ANISOU 1044 CD LYS D 130 10079 6950 7377 -1460 -1556 2019 C ATOM 1045 CE LYS A 130 70.992 26.560 69.794 1.00 66.12 C ANISOU 1045 CE LYS D 130 10805 8179 6139 -1726 -125 739 C ATOM 1046 NZ LYS A 130 70.686 26.498 68.336 1.00 77.00 N ANISOU 1046 NZ LYS D 130 14511 8537 6209 -992 -1736 -441 N ATOM 1047 N ILE A 131 70.051 21.673 68.598 1.00 31.02 N ANISOU 1047 N ILE D 131 3861 4582 3345 -482 133 -47 N ATOM 1048 CA ILE A 131 70.903 20.827 67.760 1.00 31.31 C ANISOU 1048 CA ILE D 131 4012 4209 3678 -423 -81 -152 C ATOM 1049 C ILE A 131 72.088 21.677 67.340 1.00 30.73 C ANISOU 1049 C ILE D 131 3753 4269 3654 -517 150 -164 C ATOM 1050 O ILE A 131 71.882 22.773 66.810 1.00 34.14 O ANISOU 1050 O ILE D 131 3854 5108 4008 -791 188 99 O ATOM 1051 CB ILE A 131 70.082 20.271 66.580 1.00 33.63 C ANISOU 1051 CB ILE D 131 5058 4285 3436 -1033 -124 -9 C ATOM 1052 CG1 ILE A 131 68.965 19.342 67.078 1.00 31.40 C ANISOU 1052 CG1 ILE D 131 4514 4086 3331 -270 -208 42 C ATOM 1053 CG2 ILE A 131 70.971 19.591 65.553 1.00 25.43 C ANISOU 1053 CG2 ILE D 131 4033 3240 2391 138 1295 -502 C ATOM 1054 CD1 ILE A 131 67.942 18.921 66.074 1.00 29.42 C ANISOU 1054 CD1 ILE D 131 4061 4050 3066 284 -38 314 C ATOM 1055 N HIS A 132 73.326 21.250 67.579 1.00 28.52 N ANISOU 1055 N HIS D 132 4089 4323 2422 -235 -296 -275 N ATOM 1056 CA HIS A 132 74.471 22.072 67.199 1.00 30.32 C ANISOU 1056 CA HIS D 132 4157 4435 2930 -299 71 -4 C ATOM 1057 C HIS A 132 74.781 22.024 65.712 1.00 31.66 C ANISOU 1057 C HIS D 132 4407 4647 2975 -666 86 210 C ATOM 1058 O HIS A 132 75.246 23.026 65.150 1.00 33.63 O ANISOU 1058 O HIS D 132 5439 4291 3048 -711 1019 -321 O ATOM 1059 CB HIS A 132 75.704 21.612 67.987 1.00 30.62 C ANISOU 1059 CB HIS D 132 4246 4205 3184 -277 46 -46 C ATOM 1060 CG HIS A 132 75.443 21.742 69.465 1.00 32.30 C ANISOU 1060 CG HIS D 132 4720 4451 3103 -214 79 -368 C ATOM 1061 ND1 HIS A 132 75.454 22.955 70.118 1.00 37.74 N ANISOU 1061 ND1 HIS D 132 5939 5256 3143 -1222 -185 -328 N ATOM 1062 CD2 HIS A 132 75.168 20.816 70.394 1.00 30.12 C ANISOU 1062 CD2 HIS D 132 4730 4248 2467 -1 741 -1297 C ATOM 1063 CE1 HIS A 132 75.193 22.767 71.403 1.00 40.61 C ANISOU 1063 CE1 HIS D 132 6737 5694 3000 -1929 -57 -571 C ATOM 1064 NE2 HIS A 132 75.014 21.468 71.588 1.00 40.22 N ANISOU 1064 NE2 HIS D 132 6345 5845 3092 -1717 -282 -259 N ATOM 1065 N LEU A 133 74.534 20.863 65.110 1.00 31.59 N ANISOU 1065 N LEU D 133 4605 4354 3043 -380 -89 -26 N ATOM 1066 CA LEU A 133 74.798 20.657 63.695 1.00 28.37 C ANISOU 1066 CA LEU D 133 3938 3870 2972 -91 196 10 C ATOM 1067 C LEU A 133 73.773 19.688 63.121 1.00 28.98 C ANISOU 1067 C LEU D 133 3357 4254 3399 -330 353 -398 C ATOM 1068 O LEU A 133 73.707 18.544 63.595 1.00 32.62 O ANISOU 1068 O LEU D 133 4510 4525 3358 -792 898 -113 O ATOM 1069 CB LEU A 133 76.196 20.107 63.482 1.00 29.90 C ANISOU 1069 CB LEU D 133 3627 4260 3473 -104 292 -72 C ATOM 1070 CG LEU A 133 76.599 19.724 62.056 1.00 30.77 C ANISOU 1070 CG LEU D 133 3544 4725 3421 360 627 493 C ATOM 1071 CD1 LEU A 133 76.463 20.885 61.089 1.00 30.36 C ANISOU 1071 CD1 LEU D 133 3154 5025 3356 -426 420 -419 C ATOM 1072 CD2 LEU A 133 78.044 19.209 62.073 1.00 30.54 C ANISOU 1072 CD2 LEU D 133 3610 4669 3327 357 529 -212 C ATOM 1073 N PHE A 134 72.996 20.159 62.148 1.00 30.24 N ANISOU 1073 N PHE D 134 4088 4159 3241 -390 666 -253 N ATOM 1074 CA PHE A 134 72.007 19.298 61.511 1.00 27.13 C ANISOU 1074 CA PHE D 134 3676 3832 2800 -121 279 137 C ATOM 1075 C PHE A 134 72.484 19.036 60.080 1.00 27.18 C ANISOU 1075 C PHE D 134 3808 3450 3069 -186 63 527 C ATOM 1076 O PHE A 134 72.575 19.964 59.281 1.00 27.06 O ANISOU 1076 O PHE D 134 3762 3739 2780 -314 182 84 O ATOM 1077 CB PHE A 134 70.610 19.917 61.504 1.00 26.18 C ANISOU 1077 CB PHE D 134 3256 3825 2867 -375 109 415 C ATOM 1078 CG PHE A 134 69.471 18.918 61.598 1.00 28.15 C ANISOU 1078 CG PHE D 134 3764 3739 3192 -258 -66 289 C ATOM 1079 CD1 PHE A 134 69.453 17.776 60.806 1.00 27.28 C ANISOU 1079 CD1 PHE D 134 3910 3496 2959 7 63 -133 C ATOM 1080 CD2 PHE A 134 68.412 19.122 62.490 1.00 26.16 C ANISOU 1080 CD2 PHE D 134 3356 3681 2900 -3 414 148 C ATOM 1081 CE1 PHE A 134 68.413 16.876 60.911 1.00 29.02 C ANISOU 1081 CE1 PHE D 134 4191 3644 3192 -273 60 88 C ATOM 1082 CE2 PHE A 134 67.371 18.210 62.609 1.00 28.76 C ANISOU 1082 CE2 PHE D 134 4500 3692 2734 -148 175 169 C ATOM 1083 CZ PHE A 134 67.375 17.072 61.818 1.00 30.25 C ANISOU 1083 CZ PHE D 134 4737 3547 3210 -171 -64 52 C ATOM 1084 N MET A 135 72.797 17.800 59.758 1.00 26.32 N ANISOU 1084 N MET D 135 3595 3693 2714 -5 367 190 N ATOM 1085 CA MET A 135 73.195 17.360 58.446 1.00 25.09 C ANISOU 1085 CA MET D 135 3269 3703 2560 -166 605 448 C ATOM 1086 C MET A 135 71.981 16.826 57.706 1.00 25.40 C ANISOU 1086 C MET D 135 3207 3842 2601 -266 460 287 C ATOM 1087 O MET A 135 71.172 16.078 58.254 1.00 25.93 O ANISOU 1087 O MET D 135 3696 3701 2456 163 571 289 O ATOM 1088 CB MET A 135 74.263 16.255 58.534 1.00 25.32 C ANISOU 1088 CB MET D 135 3207 4013 2401 -318 701 302 C ATOM 1089 CG MET A 135 74.741 15.900 57.119 1.00 28.15 C ANISOU 1089 CG MET D 135 3367 4549 2781 -814 4 125 C ATOM 1090 SD MET A 135 76.200 14.833 57.174 1.00 31.02 S ANISOU 1090 SD MET D 135 3750 4653 3384 -375 -86 334 S ATOM 1091 CE MET A 135 75.411 13.280 57.665 1.00 28.43 C ANISOU 1091 CE MET D 135 3016 4068 3717 -83 256 -533 C ATOM 1092 N GLY A 136 71.800 17.189 56.436 1.00 24.78 N ANISOU 1092 N GLY D 136 3188 3786 2439 -503 167 240 N ATOM 1093 CA GLY A 136 70.653 16.670 55.688 1.00 27.87 C ANISOU 1093 CA GLY D 136 3717 4095 2776 -678 220 -175 C ATOM 1094 C GLY A 136 70.978 16.602 54.205 1.00 26.53 C ANISOU 1094 C GLY D 136 3610 3703 2768 -44 526 -170 C ATOM 1095 O GLY A 136 72.086 16.946 53.769 1.00 27.86 O ANISOU 1095 O GLY D 136 3389 3779 3417 81 -146 -182 O ATOM 1096 N GLY A 137 70.013 16.157 53.415 1.00 29.09 N ANISOU 1096 N GLY D 137 4509 3712 2831 -273 435 -262 N ATOM 1097 CA GLY A 137 70.097 16.247 51.954 1.00 28.89 C ANISOU 1097 CA GLY D 137 4062 4089 2827 -596 602 -311 C ATOM 1098 C GLY A 137 68.996 17.183 51.440 1.00 28.78 C ANISOU 1098 C GLY D 137 3846 4271 2819 -450 276 -211 C ATOM 1099 O GLY A 137 68.383 17.908 52.231 1.00 29.61 O ANISOU 1099 O GLY D 137 4311 4132 2806 -454 18 -10 O ATOM 1100 N VAL A 138 68.743 17.165 50.128 1.00 26.82 N ANISOU 1100 N VAL D 138 3435 3959 2794 -174 231 -77 N ATOM 1101 CA VAL A 138 67.695 18.048 49.602 1.00 24.45 C ANISOU 1101 CA VAL D 138 3353 3292 2644 -155 53 295 C ATOM 1102 C VAL A 138 66.974 17.335 48.465 1.00 24.17 C ANISOU 1102 C VAL D 138 3323 3399 2464 47 -81 329 C ATOM 1103 O VAL A 138 67.592 16.580 47.708 1.00 26.46 O ANISOU 1103 O VAL D 138 3429 3798 2826 -189 -351 516 O ATOM 1104 CB VAL A 138 68.310 19.399 49.182 1.00 25.77 C ANISOU 1104 CB VAL D 138 3325 3426 3039 -172 -199 611 C ATOM 1105 CG1 VAL A 138 69.375 19.185 48.110 1.00 28.40 C ANISOU 1105 CG1 VAL D 138 4717 3466 2609 121 -305 480 C ATOM 1106 CG2 VAL A 138 67.265 20.390 48.690 1.00 26.22 C ANISOU 1106 CG2 VAL D 138 3531 4230 2201 -424 148 240 C ATOM 1107 N GLY A 139 65.660 17.547 48.365 1.00 24.37 N ANISOU 1107 N GLY D 139 3893 2966 2402 32 106 679 N ATOM 1108 CA GLY A 139 64.898 16.901 47.307 1.00 26.69 C ANISOU 1108 CA GLY D 139 4036 3470 2635 13 248 245 C ATOM 1109 C GLY A 139 65.204 17.577 45.975 1.00 27.30 C ANISOU 1109 C GLY D 139 4457 3318 2597 -329 173 122 C ATOM 1110 O GLY A 139 65.765 18.685 45.915 1.00 28.89 O ANISOU 1110 O GLY D 139 4748 3244 2984 -395 -207 425 O ATOM 1111 N ASN A 140 64.839 16.917 44.868 1.00 25.69 N ANISOU 1111 N ASN D 140 3631 3502 2629 48 -42 124 N ATOM 1112 CA ASN A 140 65.023 17.480 43.547 1.00 27.00 C ANISOU 1112 CA ASN D 140 3575 4061 2622 -548 93 -99 C ATOM 1113 C ASN A 140 64.258 18.803 43.429 1.00 28.54 C ANISOU 1113 C ASN D 140 3580 3849 3413 -564 68 141 C ATOM 1114 O ASN A 140 64.665 19.695 42.665 1.00 26.79 O ANISOU 1114 O ASN D 140 3564 3855 2759 -580 23 -128 O ATOM 1115 CB ASN A 140 64.530 16.518 42.466 1.00 24.74 C ANISOU 1115 CB ASN D 140 3986 2859 2555 -398 -275 507 C ATOM 1116 CG ASN A 140 65.354 15.256 42.346 1.00 27.52 C ANISOU 1116 CG ASN D 140 4084 3268 3104 -302 -543 -183 C ATOM 1117 OD1 ASN A 140 66.358 15.041 43.046 1.00 28.78 O ANISOU 1117 OD1 ASN D 140 4295 4160 2480 -141 170 318 O ATOM 1118 ND2 ASN A 140 64.941 14.366 41.449 1.00 32.68 N ANISOU 1118 ND2 ASN D 140 4801 4318 3298 -1401 -449 -329 N ATOM 1119 N ASP A 141 63.158 18.917 44.159 1.00 25.43 N ANISOU 1119 N ASP D 141 3624 3714 2323 -341 347 -354 N ATOM 1120 CA ASP A 141 62.401 20.168 44.081 1.00 26.26 C ANISOU 1120 CA ASP D 141 3642 3814 2522 -331 355 -36 C ATOM 1121 C ASP A 141 62.752 21.106 45.226 1.00 26.49 C ANISOU 1121 C ASP D 141 3569 3491 3006 -170 94 -156 C ATOM 1122 O ASP A 141 61.971 22.022 45.527 1.00 25.75 O ANISOU 1122 O ASP D 141 3565 3223 2995 -391 112 560 O ATOM 1123 CB ASP A 141 60.892 19.892 44.081 1.00 26.72 C ANISOU 1123 CB ASP D 141 3547 3842 2765 -309 -249 -384 C ATOM 1124 CG ASP A 141 60.480 19.174 45.355 1.00 26.06 C ANISOU 1124 CG ASP D 141 3097 3817 2989 461 -314 22 C ATOM 1125 OD1 ASP A 141 59.292 18.804 45.488 1.00 34.78 O ANISOU 1125 OD1 ASP D 141 5599 3472 4144 141 402 -150 O ATOM 1126 OD2 ASP A 141 61.319 18.943 46.246 1.00 30.28 O ANISOU 1126 OD2 ASP D 141 4384 3992 3130 256 314 -130 O ATOM 1127 N GLY A 142 63.884 20.884 45.884 1.00 26.48 N ANISOU 1127 N GLY D 142 3962 3312 2788 -208 434 86 N ATOM 1128 CA GLY A 142 64.356 21.778 46.946 1.00 25.59 C ANISOU 1128 CA GLY D 142 3756 3176 2790 -148 467 139 C ATOM 1129 C GLY A 142 63.772 21.490 48.305 1.00 25.67 C ANISOU 1129 C GLY D 142 3392 3211 3151 224 -423 428 C ATOM 1130 O GLY A 142 64.122 22.173 49.297 1.00 27.27 O ANISOU 1130 O GLY D 142 3583 3831 2948 -36 154 66 O ATOM 1131 N HIS A 143 62.878 20.503 48.453 1.00 26.81 N ANISOU 1131 N HIS D 143 3542 3427 3216 -44 -50 594 N ATOM 1132 CA HIS A 143 62.251 20.247 49.767 1.00 27.70 C ANISOU 1132 CA HIS D 143 3694 3720 3113 -107 -43 623 C ATOM 1133 C HIS A 143 63.215 19.599 50.751 1.00 28.72 C ANISOU 1133 C HIS D 143 3819 4031 3063 -16 -117 490 C ATOM 1134 O HIS A 143 64.259 19.058 50.376 1.00 28.56 O ANISOU 1134 O HIS D 143 3322 4544 2984 -223 -216 252 O ATOM 1135 CB HIS A 143 61.018 19.345 49.633 1.00 28.55 C ANISOU 1135 CB HIS D 143 4574 3745 2530 -324 194 700 C ATOM 1136 CG HIS A 143 61.294 17.889 49.413 1.00 35.65 C ANISOU 1136 CG HIS D 143 5284 4866 3394 -1553 -40 960 C ATOM 1137 ND1 HIS A 143 61.371 17.338 48.147 1.00 33.00 N ANISOU 1137 ND1 HIS D 143 4485 4459 3595 -302 -143 483 N ATOM 1138 CD2 HIS A 143 61.489 16.844 50.272 1.00 39.21 C ANISOU 1138 CD2 HIS D 143 5260 5829 3811 -1714 220 735 C ATOM 1139 CE1 HIS A 143 61.608 16.043 48.205 1.00 33.43 C ANISOU 1139 CE1 HIS D 143 4082 4472 4145 252 -361 928 C ATOM 1140 NE2 HIS A 143 61.692 15.717 49.490 1.00 38.04 N ANISOU 1140 NE2 HIS D 143 4721 5393 4340 -876 -18 943 N ATOM 1141 N ILE A 144 62.824 19.614 52.025 1.00 27.69 N ANISOU 1141 N ILE D 144 4000 3529 2989 -166 -216 269 N ATOM 1142 CA ILE A 144 63.664 19.049 53.084 1.00 30.21 C ANISOU 1142 CA ILE D 144 4441 3961 3078 -20 -40 137 C ATOM 1143 C ILE A 144 62.953 17.929 53.822 1.00 30.24 C ANISOU 1143 C ILE D 144 4207 4313 2970 29 -24 347 C ATOM 1144 O ILE A 144 61.764 18.069 54.162 1.00 28.53 O ANISOU 1144 O ILE D 144 3824 4341 2677 -185 -149 407 O ATOM 1145 CB ILE A 144 64.084 20.199 54.009 1.00 35.87 C ANISOU 1145 CB ILE D 144 5317 5273 3038 -1017 499 -391 C ATOM 1146 CG1 ILE A 144 65.152 21.071 53.324 1.00 39.81 C ANISOU 1146 CG1 ILE D 144 6210 5401 3515 -2039 1688 -660 C ATOM 1147 CG2 ILE A 144 64.514 19.683 55.379 1.00 38.08 C ANISOU 1147 CG2 ILE D 144 5980 5485 3002 -1448 680 -144 C ATOM 1148 CD1 ILE A 144 65.474 22.346 54.052 1.00 44.89 C ANISOU 1148 CD1 ILE D 144 5198 7047 4812 -2738 1919 -773 C ATOM 1149 N ALA A 145 63.676 16.827 54.047 1.00 30.04 N ANISOU 1149 N ALA D 145 4019 4709 2687 51 -574 734 N ATOM 1150 CA ALA A 145 63.110 15.665 54.730 1.00 33.88 C ANISOU 1150 CA ALA D 145 4272 4899 3700 -516 -314 528 C ATOM 1151 C ALA A 145 61.809 15.276 54.052 1.00 32.88 C ANISOU 1151 C ALA D 145 3871 4994 3626 -722 282 533 C ATOM 1152 O ALA A 145 61.796 15.193 52.813 1.00 37.05 O ANISOU 1152 O ALA D 145 5636 4738 3703 -722 -285 559 O ATOM 1153 CB ALA A 145 62.897 15.957 56.209 1.00 31.60 C ANISOU 1153 CB ALA D 145 4304 4341 3363 -118 479 935 C ATOM 1154 N PHE A 146 60.724 15.058 54.792 1.00 32.14 N ANISOU 1154 N PHE D 146 4142 4992 3078 -336 1125 474 N ATOM 1155 CA PHE A 146 59.466 14.764 54.107 1.00 32.43 C ANISOU 1155 CA PHE D 146 4183 5097 3041 -475 853 228 C ATOM 1156 C PHE A 146 58.575 16.005 54.070 1.00 31.27 C ANISOU 1156 C PHE D 146 4169 4422 3293 -471 846 212 C ATOM 1157 O PHE A 146 57.378 15.897 53.756 1.00 35.15 O ANISOU 1157 O PHE D 146 4625 4822 3907 -252 620 -501 O ATOM 1158 CB PHE A 146 58.657 13.620 54.725 1.00 32.34 C ANISOU 1158 CB PHE D 146 4126 5133 3028 -936 384 31 C ATOM 1159 CG PHE A 146 59.282 12.271 54.399 1.00 36.84 C ANISOU 1159 CG PHE D 146 4333 5777 3886 -1021 -100 160 C ATOM 1160 CD1 PHE A 146 59.098 11.699 53.155 1.00 42.68 C ANISOU 1160 CD1 PHE D 146 4466 7257 4494 -1295 -187 -795 C ATOM 1161 CD2 PHE A 146 60.039 11.610 55.346 1.00 34.07 C ANISOU 1161 CD2 PHE D 146 3601 5135 4210 121 -789 -10 C ATOM 1162 CE1 PHE A 146 59.669 10.474 52.864 1.00 45.34 C ANISOU 1162 CE1 PHE D 146 4476 7702 5049 -1527 -157 -1240 C ATOM 1163 CE2 PHE A 146 60.612 10.389 55.074 1.00 35.10 C ANISOU 1163 CE2 PHE D 146 3813 5445 4079 116 -1337 176 C ATOM 1164 CZ PHE A 146 60.417 9.828 53.829 1.00 39.62 C ANISOU 1164 CZ PHE D 146 4236 6578 4238 -695 -785 -513 C ATOM 1165 N ASN A 147 59.138 17.166 54.377 1.00 31.88 N ANISOU 1165 N ASN D 147 4445 4628 3040 -483 137 78 N ATOM 1166 CA ASN A 147 58.319 18.367 54.211 1.00 31.70 C ANISOU 1166 CA ASN D 147 4438 4565 3042 -688 276 -26 C ATOM 1167 C ASN A 147 58.013 18.638 52.745 1.00 34.38 C ANISOU 1167 C ASN D 147 4673 5296 3095 -405 194 -487 C ATOM 1168 O ASN A 147 58.782 18.355 51.818 1.00 40.03 O ANISOU 1168 O ASN D 147 6438 5686 3087 254 632 390 O ATOM 1169 CB ASN A 147 59.066 19.566 54.801 1.00 30.43 C ANISOU 1169 CB ASN D 147 4384 4252 2927 -123 -373 45 C ATOM 1170 CG ASN A 147 59.277 19.362 56.290 1.00 30.24 C ANISOU 1170 CG ASN D 147 4651 3873 2967 1 -136 262 C ATOM 1171 OD1 ASN A 147 58.360 19.713 57.045 1.00 32.49 O ANISOU 1171 OD1 ASN D 147 4299 4953 3093 -219 -486 341 O ATOM 1172 ND2 ASN A 147 60.426 18.814 56.670 1.00 30.25 N ANISOU 1172 ND2 ASN D 147 4554 3366 3574 -380 304 317 N ATOM 1173 N GLU A 148 56.853 19.229 52.445 1.00 36.52 N ANISOU 1173 N GLU D 148 4784 5165 3926 -576 621 -647 N ATOM 1174 CA GLU A 148 56.567 19.477 51.044 1.00 37.62 C ANISOU 1174 CA GLU D 148 4800 5496 3996 -506 795 -628 C ATOM 1175 C GLU A 148 56.974 20.874 50.623 1.00 35.13 C ANISOU 1175 C GLU D 148 4193 5501 3653 -282 383 -550 C ATOM 1176 O GLU A 148 57.223 21.711 51.482 1.00 36.10 O ANISOU 1176 O GLU D 148 4942 5346 3428 -441 92 -134 O ATOM 1177 CB GLU A 148 55.074 19.193 50.824 1.00 44.63 C ANISOU 1177 CB GLU D 148 6139 5477 5341 -679 1299 -1418 C ATOM 1178 CG GLU A 148 55.031 17.841 50.092 1.00 62.51 C ANISOU 1178 CG GLU D 148 10150 6335 7266 -2672 -1198 -738 C ATOM 1179 CD GLU A 148 53.640 17.265 49.960 1.00 62.28 C ANISOU 1179 CD GLU D 148 10737 6366 6563 -2751 -91 -994 C ATOM 1180 OE1 GLU A 148 53.092 17.463 48.849 1.00 58.46 O ANISOU 1180 OE1 GLU D 148 8529 7728 5956 -589 -931 32 O ATOM 1181 OE2 GLU A 148 53.182 16.659 50.958 1.00 53.92 O ANISOU 1181 OE2 GLU D 148 7807 6685 5995 -228 -852 -345 O ATOM 1182 N PRO A 149 57.043 21.105 49.324 1.00 32.87 N ANISOU 1182 N PRO D 149 3807 5083 3601 -97 -179 -132 N ATOM 1183 CA PRO A 149 57.231 22.461 48.824 1.00 32.24 C ANISOU 1183 CA PRO D 149 4390 4418 3444 -319 -805 463 C ATOM 1184 C PRO A 149 56.128 23.346 49.408 1.00 31.02 C ANISOU 1184 C PRO D 149 3812 4107 3866 -8 -140 -98 C ATOM 1185 O PRO A 149 55.002 22.884 49.584 1.00 30.07 O ANISOU 1185 O PRO D 149 3975 4089 3359 -109 69 11 O ATOM 1186 CB PRO A 149 57.028 22.284 47.330 1.00 31.62 C ANISOU 1186 CB PRO D 149 4043 4309 3661 -329 -144 -207 C ATOM 1187 CG PRO A 149 57.421 20.868 47.046 1.00 34.44 C ANISOU 1187 CG PRO D 149 4321 5187 3579 -832 -344 -382 C ATOM 1188 CD PRO A 149 56.914 20.110 48.246 1.00 35.77 C ANISOU 1188 CD PRO D 149 4150 5686 3756 -783 18 -291 C ATOM 1189 N ALA A 150 56.453 24.588 49.718 1.00 31.18 N ANISOU 1189 N ALA D 150 3700 4110 4039 -107 -144 333 N ATOM 1190 CA ALA A 150 55.595 25.610 50.323 1.00 28.85 C ANISOU 1190 CA ALA D 150 3788 3648 3525 217 -129 -142 C ATOM 1191 C ALA A 150 55.246 25.215 51.750 1.00 30.57 C ANISOU 1191 C ALA D 150 4376 3691 3548 371 -19 -112 C ATOM 1192 O ALA A 150 54.261 25.716 52.290 1.00 31.66 O ANISOU 1192 O ALA D 150 4014 4233 3783 29 -88 363 O ATOM 1193 CB ALA A 150 54.331 25.885 49.524 1.00 31.71 C ANISOU 1193 CB ALA D 150 3074 4424 4551 -839 652 -1116 C ATOM 1194 N SER A 151 56.048 24.335 52.358 1.00 29.94 N ANISOU 1194 N SER D 151 3870 4227 3279 -100 -355 23 N ATOM 1195 CA SER A 151 55.896 24.104 53.780 1.00 28.79 C ANISOU 1195 CA SER D 151 3667 3912 3359 -130 -366 214 C ATOM 1196 C SER A 151 56.159 25.421 54.517 1.00 27.85 C ANISOU 1196 C SER D 151 3270 4162 3148 -5 -137 69 C ATOM 1197 O SER A 151 56.996 26.178 54.023 1.00 28.87 O ANISOU 1197 O SER D 151 3544 4607 2820 -650 -615 285 O ATOM 1198 CB SER A 151 56.902 23.099 54.349 1.00 29.68 C ANISOU 1198 CB SER D 151 3367 4612 3298 -169 -518 533 C ATOM 1199 OG SER A 151 56.573 21.755 54.026 1.00 34.72 O ANISOU 1199 OG SER D 151 3690 4948 4553 -486 -1143 1135 O ATOM 1200 N SER A 152 55.501 25.626 55.645 1.00 29.45 N ANISOU 1200 N SER D 152 3378 3942 3869 9 -659 386 N ATOM 1201 CA SER A 152 55.861 26.691 56.572 1.00 29.19 C ANISOU 1201 CA SER D 152 3469 4067 3556 16 -643 433 C ATOM 1202 C SER A 152 57.311 26.555 57.012 1.00 29.48 C ANISOU 1202 C SER D 152 3728 3893 3582 34 -663 526 C ATOM 1203 O SER A 152 57.800 25.446 57.299 1.00 29.07 O ANISOU 1203 O SER D 152 3750 3599 3698 168 -539 744 O ATOM 1204 CB SER A 152 54.953 26.667 57.811 1.00 24.29 C ANISOU 1204 CB SER D 152 2261 4031 2936 151 489 373 C ATOM 1205 OG SER A 152 55.484 27.581 58.771 1.00 30.65 O ANISOU 1205 OG SER D 152 4423 4323 2899 148 -104 292 O ATOM 1206 N LEU A 153 58.030 27.678 57.102 1.00 29.06 N ANISOU 1206 N LEU D 153 4048 4037 2954 -219 -370 477 N ATOM 1207 CA LEU A 153 59.421 27.631 57.560 1.00 29.26 C ANISOU 1207 CA LEU D 153 3685 3994 3440 -261 -742 284 C ATOM 1208 C LEU A 153 59.445 27.405 59.063 1.00 29.11 C ANISOU 1208 C LEU D 153 3316 4253 3491 209 -558 101 C ATOM 1209 O LEU A 153 60.504 27.208 59.664 1.00 34.08 O ANISOU 1209 O LEU D 153 4357 4097 4497 304 441 284 O ATOM 1210 CB LEU A 153 60.149 28.918 57.227 1.00 33.10 C ANISOU 1210 CB LEU D 153 3749 4053 4775 -216 131 228 C ATOM 1211 CG LEU A 153 60.999 28.988 55.952 1.00 40.02 C ANISOU 1211 CG LEU D 153 5950 5263 3992 -2329 133 679 C ATOM 1212 CD1 LEU A 153 60.540 28.019 54.880 1.00 36.67 C ANISOU 1212 CD1 LEU D 153 6870 4004 3059 -1329 1626 -51 C ATOM 1213 CD2 LEU A 153 61.026 30.409 55.395 1.00 35.55 C ANISOU 1213 CD2 LEU D 153 2763 5853 4889 200 331 967 C ATOM 1214 N ALA A 154 58.275 27.452 59.693 1.00 28.86 N ANISOU 1214 N ALA D 154 3772 3811 3384 -100 -231 365 N ATOM 1215 CA ALA A 154 58.219 27.133 61.118 1.00 30.37 C ANISOU 1215 CA ALA D 154 3746 4496 3297 -369 -386 198 C ATOM 1216 C ALA A 154 57.555 25.787 61.335 1.00 31.22 C ANISOU 1216 C ALA D 154 4347 4666 2850 -661 -348 317 C ATOM 1217 O ALA A 154 57.109 25.499 62.451 1.00 34.75 O ANISOU 1217 O ALA D 154 5023 4855 3323 -392 -1059 947 O ATOM 1218 CB ALA A 154 57.458 28.214 61.876 1.00 34.29 C ANISOU 1218 CB ALA D 154 4068 5230 3729 -356 -793 160 C ATOM 1219 N SER A 155 57.441 24.937 60.301 1.00 27.85 N ANISOU 1219 N SER D 155 3657 4121 2802 -121 7 9 N ATOM 1220 CA SER A 155 56.682 23.697 60.552 1.00 29.11 C ANISOU 1220 CA SER D 155 3680 4341 3039 -299 -34 162 C ATOM 1221 C SER A 155 57.458 22.813 61.514 1.00 31.02 C ANISOU 1221 C SER D 155 3935 4240 3611 -131 316 360 C ATOM 1222 O SER A 155 58.663 22.985 61.698 1.00 29.07 O ANISOU 1222 O SER D 155 4093 3993 2960 -410 506 489 O ATOM 1223 CB SER A 155 56.392 23.046 59.200 1.00 28.66 C ANISOU 1223 CB SER D 155 3994 4035 2860 -630 -380 718 C ATOM 1224 OG SER A 155 57.647 22.914 58.517 1.00 30.95 O ANISOU 1224 OG SER D 155 3936 4581 3242 -12 18 839 O ATOM 1225 N ARG A 156 56.808 21.854 62.166 1.00 27.27 N ANISOU 1225 N ARG D 156 3264 3955 3142 464 -1 470 N ATOM 1226 CA ARG A 156 57.396 21.015 63.201 1.00 28.27 C ANISOU 1226 CA ARG D 156 3079 4309 3353 470 18 544 C ATOM 1227 C ARG A 156 57.199 19.529 62.905 1.00 27.82 C ANISOU 1227 C ARG D 156 2907 3931 3731 789 -28 347 C ATOM 1228 O ARG A 156 56.512 19.194 61.934 1.00 31.42 O ANISOU 1228 O ARG D 156 4483 3701 3754 -136 705 427 O ATOM 1229 CB ARG A 156 56.749 21.343 64.554 1.00 30.35 C ANISOU 1229 CB ARG D 156 4010 4532 2991 289 -109 187 C ATOM 1230 CG ARG A 156 57.064 22.766 65.036 1.00 32.56 C ANISOU 1230 CG ARG D 156 4808 4586 2978 -232 -361 625 C ATOM 1231 CD ARG A 156 58.484 22.728 65.602 1.00 36.21 C ANISOU 1231 CD ARG D 156 5806 4472 3480 -146 -508 297 C ATOM 1232 NE ARG A 156 59.138 24.023 65.540 1.00 40.57 N ANISOU 1232 NE ARG D 156 6347 4722 4348 -532 -933 182 N ATOM 1233 CZ ARG A 156 60.391 24.234 65.928 1.00 40.13 C ANISOU 1233 CZ ARG D 156 5796 4720 4733 -761 -573 57 C ATOM 1234 NH1 ARG A 156 61.125 23.236 66.403 1.00 37.87 N ANISOU 1234 NH1 ARG D 156 5173 5635 3582 -493 -1594 379 N ATOM 1235 NH2 ARG A 156 60.870 25.463 65.824 1.00 40.93 N ANISOU 1235 NH2 ARG D 156 6082 4379 5092 -499 -635 1412 N ATOM 1236 N THR A 157 57.788 18.668 63.746 1.00 30.93 N ANISOU 1236 N THR D 157 3402 4458 3890 186 411 340 N ATOM 1237 CA THR A 157 57.772 17.225 63.558 1.00 31.02 C ANISOU 1237 CA THR D 157 3752 4415 3620 -155 491 575 C ATOM 1238 C THR A 157 56.343 16.734 63.414 1.00 30.19 C ANISOU 1238 C THR D 157 3483 4497 3492 48 735 555 C ATOM 1239 O THR A 157 55.489 17.150 64.209 1.00 35.36 O ANISOU 1239 O THR D 157 4388 4808 4240 93 111 919 O ATOM 1240 CB THR A 157 58.450 16.494 64.733 1.00 30.76 C ANISOU 1240 CB THR D 157 3447 4291 3950 77 433 279 C ATOM 1241 OG1 THR A 157 59.805 16.950 64.815 1.00 35.13 O ANISOU 1241 OG1 THR D 157 6169 4069 3109 -194 326 -108 O ATOM 1242 CG2 THR A 157 58.470 14.997 64.498 1.00 28.06 C ANISOU 1242 CG2 THR D 157 3457 4294 2910 150 280 74 C ATOM 1243 N ARG A 158 56.066 15.898 62.421 1.00 30.88 N ANISOU 1243 N ARG D 158 3677 4516 3538 -184 889 460 N ATOM 1244 CA ARG A 158 54.680 15.537 62.143 1.00 31.76 C ANISOU 1244 CA ARG D 158 3594 4736 3736 29 1033 278 C ATOM 1245 C ARG A 158 54.604 14.378 61.154 1.00 32.73 C ANISOU 1245 C ARG D 158 3919 4475 4043 -104 855 287 C ATOM 1246 O ARG A 158 55.586 14.038 60.514 1.00 34.08 O ANISOU 1246 O ARG D 158 4434 4672 3844 -90 510 247 O ATOM 1247 CB ARG A 158 53.903 16.733 61.580 1.00 34.38 C ANISOU 1247 CB ARG D 158 3660 5187 4217 9 1226 540 C ATOM 1248 CG ARG A 158 54.235 17.113 60.139 1.00 36.00 C ANISOU 1248 CG ARG D 158 4251 5275 4153 -123 1535 379 C ATOM 1249 CD ARG A 158 53.854 18.559 59.853 1.00 34.46 C ANISOU 1249 CD ARG D 158 4145 5227 3722 -368 735 1012 C ATOM 1250 NE ARG A 158 54.094 19.003 58.466 1.00 33.95 N ANISOU 1250 NE ARG D 158 4630 4450 3821 -159 1221 798 N ATOM 1251 CZ ARG A 158 55.292 19.428 58.055 1.00 36.78 C ANISOU 1251 CZ ARG D 158 6016 4217 3740 -394 521 541 C ATOM 1252 NH1 ARG A 158 56.288 19.432 58.946 1.00 31.31 N ANISOU 1252 NH1 ARG D 158 3855 4426 3616 -117 9 704 N ATOM 1253 NH2 ARG A 158 55.491 19.824 56.818 1.00 31.35 N ANISOU 1253 NH2 ARG D 158 3919 4507 3486 432 -249 696 N ATOM 1254 N ILE A 159 53.425 13.789 61.031 1.00 35.47 N ANISOU 1254 N ILE D 159 4542 4492 4441 -50 1111 179 N ATOM 1255 CA ILE A 159 53.211 12.708 60.090 1.00 35.07 C ANISOU 1255 CA ILE D 159 4407 4135 4782 416 896 -14 C ATOM 1256 C ILE A 159 52.890 13.314 58.718 1.00 37.45 C ANISOU 1256 C ILE D 159 4806 4741 4684 -268 875 -130 C ATOM 1257 O ILE A 159 52.234 14.357 58.659 1.00 39.31 O ANISOU 1257 O ILE D 159 4878 5013 5044 341 1309 -5 O ATOM 1258 CB ILE A 159 52.059 11.774 60.481 1.00 39.65 C ANISOU 1258 CB ILE D 159 5410 4542 5112 -294 284 485 C ATOM 1259 CG1 ILE A 159 52.016 10.505 59.623 1.00 41.71 C ANISOU 1259 CG1 ILE D 159 5362 5294 5191 -823 877 -95 C ATOM 1260 CG2 ILE A 159 50.729 12.513 60.431 1.00 38.23 C ANISOU 1260 CG2 ILE D 159 5699 3317 5509 -405 418 757 C ATOM 1261 CD1 ILE A 159 51.108 9.432 60.187 1.00 40.62 C ANISOU 1261 CD1 ILE D 159 5716 4824 4893 -491 821 -362 C ATOM 1262 N LYS A 160 53.359 12.643 57.685 1.00 40.97 N ANISOU 1262 N LYS D 160 5651 5057 4861 -739 423 378 N ATOM 1263 CA LYS A 160 53.199 12.991 56.298 1.00 43.00 C ANISOU 1263 CA LYS D 160 6809 4735 4795 -446 519 202 C ATOM 1264 C LYS A 160 52.780 11.766 55.468 1.00 44.52 C ANISOU 1264 C LYS D 160 6225 5368 5323 -675 1661 -868 C ATOM 1265 O LYS A 160 53.200 10.645 55.768 1.00 46.37 O ANISOU 1265 O LYS D 160 6438 5703 5476 -894 1992 -589 O ATOM 1266 CB LYS A 160 54.492 13.543 55.671 1.00 40.85 C ANISOU 1266 CB LYS D 160 5643 4962 4918 -153 508 397 C ATOM 1267 CG LYS A 160 54.986 14.883 56.176 1.00 43.72 C ANISOU 1267 CG LYS D 160 6473 4746 5394 -387 258 512 C ATOM 1268 CD LYS A 160 53.840 15.868 56.332 1.00 47.22 C ANISOU 1268 CD LYS D 160 5920 5840 6181 -889 443 211 C ATOM 1269 CE LYS A 160 53.746 16.801 55.145 1.00 51.24 C ANISOU 1269 CE LYS D 160 6579 6643 6247 -1400 612 143 C ATOM 1270 NZ LYS A 160 53.430 16.158 53.843 1.00 52.76 N ANISOU 1270 NZ LYS D 160 8506 5514 6026 -562 306 357 N ATOM 1271 N THR A 161 51.984 12.065 54.439 1.00 46.07 N ANISOU 1271 N THR D 161 6196 5573 5734 95 1582 -914 N ATOM 1272 CA THR A 161 51.605 11.104 53.414 1.00 50.03 C ANISOU 1272 CA THR D 161 6913 6464 5630 -308 1964 -1436 C ATOM 1273 C THR A 161 52.603 11.124 52.270 1.00 49.72 C ANISOU 1273 C THR D 161 6611 6875 5404 41 1749 -1746 C ATOM 1274 O THR A 161 52.721 12.122 51.568 1.00 51.50 O ANISOU 1274 O THR D 161 5747 7772 6050 61 770 -337 O ATOM 1275 CB THR A 161 50.213 11.432 52.855 1.00 50.46 C ANISOU 1275 CB THR D 161 6768 6590 5816 -161 1539 -1616 C ATOM 1276 OG1 THR A 161 49.292 11.480 53.955 1.00 55.20 O ANISOU 1276 OG1 THR D 161 6600 7971 6401 191 1818 -728 O ATOM 1277 CG2 THR A 161 49.737 10.343 51.907 1.00 52.69 C ANISOU 1277 CG2 THR D 161 4577 8539 6904 -166 2426 -3197 C ATOM 1278 N LEU A 162 53.361 10.063 52.061 1.00 50.34 N ANISOU 1278 N LEU D 162 6449 7256 5423 -457 1918 -1694 N ATOM 1279 CA LEU A 162 54.469 10.171 51.109 1.00 52.65 C ANISOU 1279 CA LEU D 162 6286 8091 5628 -161 1548 -1472 C ATOM 1280 C LEU A 162 54.021 10.499 49.696 1.00 52.23 C ANISOU 1280 C LEU D 162 5897 8430 5516 386 1306 -1358 C ATOM 1281 O LEU A 162 52.874 10.181 49.355 1.00 62.49 O ANISOU 1281 O LEU D 162 8039 8700 7004 -362 1496 -2942 O ATOM 1282 CB LEU A 162 55.243 8.846 51.160 1.00 53.19 C ANISOU 1282 CB LEU D 162 6314 8196 5699 -499 1777 -1522 C ATOM 1283 CG LEU A 162 55.762 8.489 52.556 1.00 52.93 C ANISOU 1283 CG LEU D 162 6606 7838 5667 13 1777 -1363 C ATOM 1284 CD1 LEU A 162 56.638 7.257 52.476 1.00 55.07 C ANISOU 1284 CD1 LEU D 162 6561 7050 7311 156 2360 -995 C ATOM 1285 CD2 LEU A 162 56.472 9.707 53.122 1.00 57.05 C ANISOU 1285 CD2 LEU D 162 8865 8972 3838 -1552 778 -482 C ATOM 1286 N THR A 163 54.860 11.116 48.861 1.00 59.10 N ANISOU 1286 N THR D 163 6302 9840 6313 -767 1535 -340 N ATOM 1287 CA THR A 163 54.435 11.371 47.479 1.00 67.97 C ANISOU 1287 CA THR D 163 8737 10769 6321 -2093 2043 -691 C ATOM 1288 C THR A 163 54.734 10.166 46.585 1.00 72.03 C ANISOU 1288 C THR D 163 9650 11375 6344 -2327 1519 -773 C ATOM 1289 O THR A 163 55.694 9.439 46.839 1.00 63.46 O ANISOU 1289 O THR D 163 9754 9523 4834 -2098 377 -773 O ATOM 1290 CB THR A 163 55.103 12.606 46.849 1.00 67.87 C ANISOU 1290 CB THR D 163 8532 10536 6719 -1473 2303 -297 C ATOM 1291 OG1 THR A 163 56.467 12.297 46.506 1.00 77.41 O ANISOU 1291 OG1 THR D 163 9711 11701 8001 -1467 -319 417 O ATOM 1292 CG2 THR A 163 55.153 13.796 47.804 1.00 61.67 C ANISOU 1292 CG2 THR D 163 6295 9323 7815 -351 2422 -293 C ATOM 1293 N HIS A 164 53.932 9.954 45.554 1.00 73.18 N ANISOU 1293 N HIS D 164 8953 11950 6903 -2104 1660 -1261 N ATOM 1294 CA HIS A 164 54.140 8.891 44.580 1.00 79.94 C ANISOU 1294 CA HIS D 164 10826 12269 7277 -2713 673 -1193 C ATOM 1295 C HIS A 164 55.591 8.862 44.115 1.00 75.86 C ANISOU 1295 C HIS D 164 10789 12290 5744 -2880 480 -1278 C ATOM 1296 O HIS A 164 56.248 7.829 44.133 1.00 68.07 O ANISOU 1296 O HIS D 164 10732 12117 3012 -3617 -310 -48 O ATOM 1297 CB HIS A 164 53.235 9.097 43.375 1.00 86.94 C ANISOU 1297 CB HIS D 164 11525 12664 8842 -3047 658 -3009 C ATOM 1298 CG HIS A 164 52.699 7.858 42.733 1.00 98.83 C ANISOU 1298 CG HIS D 164 13596 13511 10445 -4228 -13 -3227 C ATOM 1299 ND1 HIS A 164 52.330 6.732 43.445 1.00104.21 N ANISOU 1299 ND1 HIS D 164 14138 14089 11368 -5006 -781 -2512 N ATOM 1300 CD2 HIS A 164 52.463 7.574 41.423 1.00102.90 C ANISOU 1300 CD2 HIS D 164 14181 14168 10747 -4985 -1232 -3005 C ATOM 1301 CE1 HIS A 164 51.888 5.805 42.603 1.00107.01 C ANISOU 1301 CE1 HIS D 164 14524 14378 11757 -5151 -1430 -2348 C ATOM 1302 NE2 HIS A 164 51.958 6.291 41.368 1.00106.55 N ANISOU 1302 NE2 HIS D 164 14544 14352 11590 -5250 -1668 -2462 N ATOM 1303 N ASP A 165 56.097 10.027 43.723 1.00 72.18 N ANISOU 1303 N ASP D 165 9561 12182 5684 -2138 1484 -1623 N ATOM 1304 CA ASP A 165 57.512 10.131 43.372 1.00 77.60 C ANISOU 1304 CA ASP D 165 11006 12333 6146 -1786 1999 -1092 C ATOM 1305 C ASP A 165 58.412 9.574 44.462 1.00 74.61 C ANISOU 1305 C ASP D 165 9901 12590 5858 -1162 1374 -630 C ATOM 1306 O ASP A 165 59.489 9.022 44.211 1.00 76.73 O ANISOU 1306 O ASP D 165 10896 11798 6461 -813 831 -553 O ATOM 1307 CB ASP A 165 57.841 11.601 43.104 1.00 85.81 C ANISOU 1307 CB ASP D 165 12889 12470 7243 -2487 3699 -1308 C ATOM 1308 CG ASP A 165 56.958 12.147 41.993 1.00 94.21 C ANISOU 1308 CG ASP D 165 14915 12585 8295 -2725 5300 -1274 C ATOM 1309 OD1 ASP A 165 55.788 11.710 41.914 1.00108.17 O ANISOU 1309 OD1 ASP D 165 16354 12710 12037 -2263 7768 -1380 O ATOM 1310 OD2 ASP A 165 57.439 12.992 41.208 1.00 97.35 O ANISOU 1310 OD2 ASP D 165 17132 13617 6241 -2539 4483 -704 O ATOM 1311 N THR A 166 57.987 9.708 45.722 1.00 74.67 N ANISOU 1311 N THR D 166 9546 12954 5873 -1010 1398 -554 N ATOM 1312 CA THR A 166 58.841 9.191 46.790 1.00 68.60 C ANISOU 1312 CA THR D 166 7758 12833 5476 -437 336 -156 C ATOM 1313 C THR A 166 58.630 7.697 47.010 1.00 68.94 C ANISOU 1313 C THR D 166 7970 12883 5341 -542 -156 716 C ATOM 1314 O THR A 166 59.608 6.988 47.247 1.00 68.20 O ANISOU 1314 O THR D 166 7559 12731 5624 -692 -530 1061 O ATOM 1315 CB THR A 166 58.633 9.895 48.147 1.00 72.37 C ANISOU 1315 CB THR D 166 9155 12702 5639 -1043 -61 -362 C ATOM 1316 OG1 THR A 166 58.767 11.316 47.998 1.00 75.94 O ANISOU 1316 OG1 THR D 166 8668 12928 7257 -920 327 -1882 O ATOM 1317 CG2 THR A 166 59.710 9.415 49.117 1.00 74.00 C ANISOU 1317 CG2 THR D 166 9650 13247 5218 -1212 624 39 C ATOM 1318 N ARG A 167 57.386 7.227 46.950 1.00 69.78 N ANISOU 1318 N ARG D 167 8682 12889 4941 -548 562 511 N ATOM 1319 CA ARG A 167 57.199 5.787 47.125 1.00 71.95 C ANISOU 1319 CA ARG D 167 8780 12745 5814 -629 917 -407 C ATOM 1320 C ARG A 167 57.911 5.094 45.958 1.00 74.23 C ANISOU 1320 C ARG D 167 8941 13769 5493 -1343 846 -439 C ATOM 1321 O ARG A 167 58.703 4.166 46.109 1.00 78.16 O ANISOU 1321 O ARG D 167 8228 14833 6636 -2496 226 -189 O ATOM 1322 CB ARG A 167 55.746 5.355 47.170 1.00 77.63 C ANISOU 1322 CB ARG D 167 9638 12639 7221 -665 1124 -961 C ATOM 1323 CG ARG A 167 54.706 6.339 47.636 1.00 81.73 C ANISOU 1323 CG ARG D 167 10758 12178 8116 -257 -90 -165 C ATOM 1324 CD ARG A 167 54.343 6.195 49.100 1.00 87.05 C ANISOU 1324 CD ARG D 167 12778 11970 8326 -590 -56 301 C ATOM 1325 NE ARG A 167 52.932 6.069 49.412 1.00 92.77 N ANISOU 1325 NE ARG D 167 14409 11696 9144 -662 -296 517 N ATOM 1326 CZ ARG A 167 52.089 6.864 50.041 1.00 95.37 C ANISOU 1326 CZ ARG D 167 15380 11275 9580 -374 -904 1145 C ATOM 1327 NH1 ARG A 167 52.425 8.044 50.542 1.00 94.39 N ANISOU 1327 NH1 ARG D 167 15117 11435 9312 -231 -1424 1589 N ATOM 1328 NH2 ARG A 167 50.813 6.505 50.199 1.00110.50 N ANISOU 1328 NH2 ARG D 167 19973 11216 10798 -1808 -3257 4175 N ATOM 1329 N VAL A 168 57.584 5.621 44.785 1.00 80.95 N ANISOU 1329 N VAL D 168 10812 14447 5497 -2185 1339 -777 N ATOM 1330 CA VAL A 168 58.192 5.194 43.545 1.00 84.04 C ANISOU 1330 CA VAL D 168 12024 14446 5461 -2415 1114 -475 C ATOM 1331 C VAL A 168 59.704 5.117 43.681 1.00 84.40 C ANISOU 1331 C VAL D 168 12875 13943 5251 -2397 603 -261 C ATOM 1332 O VAL A 168 60.272 4.046 43.499 1.00 89.82 O ANISOU 1332 O VAL D 168 12314 15343 6472 -1740 2248 -1764 O ATOM 1333 CB VAL A 168 57.856 6.162 42.394 1.00 88.21 C ANISOU 1333 CB VAL D 168 13524 14378 5615 -3379 1719 -807 C ATOM 1334 CG1 VAL A 168 58.961 6.123 41.348 1.00 86.04 C ANISOU 1334 CG1 VAL D 168 14085 12505 6102 -3940 1902 -833 C ATOM 1335 CG2 VAL A 168 56.499 5.806 41.807 1.00 86.16 C ANISOU 1335 CG2 VAL D 168 11934 14947 5855 -1949 1013 -643 C ATOM 1336 N ALA A 169 60.340 6.231 44.005 1.00 91.57 N ANISOU 1336 N ALA D 169 15364 13755 5673 -3339 -113 804 N ATOM 1337 CA ALA A 169 61.794 6.240 44.151 1.00 95.17 C ANISOU 1337 CA ALA D 169 16049 13584 6528 -3524 1372 390 C ATOM 1338 C ALA A 169 62.301 5.476 45.371 1.00102.07 C ANISOU 1338 C ALA D 169 17256 14134 7393 -4115 2423 545 C ATOM 1339 O ALA A 169 63.503 5.436 45.672 1.00106.85 O ANISOU 1339 O ALA D 169 19119 13265 8212 -5055 4172 -586 O ATOM 1340 CB ALA A 169 62.256 7.694 44.185 1.00103.83 C ANISOU 1340 CB ALA D 169 17666 14087 7697 -4586 2652 87 C ATOM 1341 N ASN A 170 61.405 4.832 46.129 1.00106.51 N ANISOU 1341 N ASN D 170 18134 14836 7500 -4499 2029 1062 N ATOM 1342 CA ASN A 170 61.901 4.060 47.276 1.00109.84 C ANISOU 1342 CA ASN D 170 18334 15718 7681 -5454 2226 978 C ATOM 1343 C ASN A 170 61.411 2.617 47.195 1.00112.59 C ANISOU 1343 C ASN D 170 18483 15901 8396 -5599 1805 941 C ATOM 1344 O ASN A 170 61.885 1.737 47.938 1.00116.92 O ANISOU 1344 O ASN D 170 21676 16275 6474 -7495 3171 1897 O ATOM 1345 CB ASN A 170 61.498 4.718 48.596 1.00107.00 C ANISOU 1345 CB ASN D 170 17223 15854 7580 -4994 2601 690 C ATOM 1346 CG ASN A 170 62.404 5.848 49.047 1.00104.44 C ANISOU 1346 CG ASN D 170 16237 15763 7682 -4573 2828 452 C ATOM 1347 OD1 ASN A 170 63.470 6.102 48.494 1.00109.05 O ANISOU 1347 OD1 ASN D 170 16961 15826 8648 -4927 1518 639 O ATOM 1348 ND2 ASN A 170 61.992 6.580 50.086 1.00 90.72 N ANISOU 1348 ND2 ASN D 170 11283 14971 8214 -2336 4491 -806 N ATOM 1349 N SER A 171 60.480 2.329 46.288 1.00110.23 N ANISOU 1349 N SER D 171 17178 15892 8812 -4576 354 679 N ATOM 1350 CA SER A 171 59.937 0.977 46.137 1.00111.31 C ANISOU 1350 CA SER D 171 17038 15580 9674 -4280 -170 887 C ATOM 1351 C SER A 171 61.018 -0.088 45.973 1.00111.01 C ANISOU 1351 C SER D 171 17047 15238 9894 -4199 -5 780 C ATOM 1352 O SER A 171 60.763 -1.252 46.309 1.00115.28 O ANISOU 1352 O SER D 171 17036 16296 10469 -5295 -2437 1977 O ATOM 1353 CB SER A 171 58.968 0.911 44.948 1.00111.07 C ANISOU 1353 CB SER D 171 16913 15240 10048 -3695 -673 693 C ATOM 1354 OG SER A 171 58.889 2.142 44.242 1.00113.97 O ANISOU 1354 OG SER D 171 18978 14524 9800 -4234 653 538 O ATOM 1355 N ARG A 172 62.187 0.288 45.473 1.00110.85 N ANISOU 1355 N ARG D 172 17451 14821 9847 -3968 200 169 N ATOM 1356 CA ARG A 172 63.370 -0.529 45.258 1.00111.98 C ANISOU 1356 CA ARG D 172 17665 14906 9976 -4058 -794 10 C ATOM 1357 C ARG A 172 63.828 -1.185 46.553 1.00111.03 C ANISOU 1357 C ARG D 172 16172 15559 10454 -3932 -939 -262 C ATOM 1358 O ARG A 172 64.182 -2.360 46.657 1.00112.06 O ANISOU 1358 O ARG D 172 16730 16836 9010 -5744 -1975 -11 O ATOM 1359 CB ARG A 172 64.510 0.298 44.660 1.00116.98 C ANISOU 1359 CB ARG D 172 19431 14785 10230 -3822 -1089 65 C ATOM 1360 CG ARG A 172 65.145 1.339 45.561 1.00128.53 C ANISOU 1360 CG ARG D 172 22686 15019 11132 -4938 -1604 -14 C ATOM 1361 CD ARG A 172 66.629 1.099 45.789 1.00133.23 C ANISOU 1361 CD ARG D 172 24043 14646 11932 -4849 -1006 -529 C ATOM 1362 NE ARG A 172 67.439 2.289 45.564 1.00140.27 N ANISOU 1362 NE ARG D 172 25830 14832 12636 -5439 -672 -487 N ATOM 1363 CZ ARG A 172 68.766 2.385 45.528 1.00142.46 C ANISOU 1363 CZ ARG D 172 26138 14766 13223 -5418 -605 -69 C ATOM 1364 NH1 ARG A 172 69.551 1.315 45.710 1.00146.19 N ANISOU 1364 NH1 ARG D 172 26094 15488 13962 -4749 -833 543 N ATOM 1365 NH2 ARG A 172 69.353 3.563 45.309 1.00148.11 N ANISOU 1365 NH2 ARG D 172 27294 15026 13955 -5942 -745 288 N ATOM 1366 N PHE A 173 63.818 -0.374 47.618 1.00 99.08 N ANISOU 1366 N PHE D 173 12166 15154 10327 -1652 -98 -625 N ATOM 1367 CA PHE A 173 64.122 -1.016 48.891 1.00 95.56 C ANISOU 1367 CA PHE D 173 11181 14684 10441 -1264 -294 -16 C ATOM 1368 C PHE A 173 62.978 -1.933 49.252 1.00 93.43 C ANISOU 1368 C PHE D 173 10204 14403 10892 -1050 -663 -317 C ATOM 1369 O PHE A 173 63.190 -3.024 49.786 1.00 90.44 O ANISOU 1369 O PHE D 173 8772 14217 11373 -1673 -2556 -482 O ATOM 1370 CB PHE A 173 64.368 0.047 49.956 1.00 90.93 C ANISOU 1370 CB PHE D 173 10884 13929 9734 -1337 138 461 C ATOM 1371 CG PHE A 173 65.371 1.069 49.428 1.00 92.38 C ANISOU 1371 CG PHE D 173 11175 14171 9755 -1241 -225 1018 C ATOM 1372 CD1 PHE A 173 66.727 0.897 49.627 1.00 91.14 C ANISOU 1372 CD1 PHE D 173 11094 14284 9251 -1076 -347 1420 C ATOM 1373 CD2 PHE A 173 64.920 2.177 48.740 1.00 91.66 C ANISOU 1373 CD2 PHE D 173 10907 13980 9941 -1040 -423 1644 C ATOM 1374 CE1 PHE A 173 67.629 1.826 49.145 1.00 91.11 C ANISOU 1374 CE1 PHE D 173 11004 14444 9172 -992 -551 1730 C ATOM 1375 CE2 PHE A 173 65.819 3.111 48.257 1.00 91.80 C ANISOU 1375 CE2 PHE D 173 10541 14096 10243 -794 -985 2187 C ATOM 1376 CZ PHE A 173 67.174 2.937 48.461 1.00 90.64 C ANISOU 1376 CZ PHE D 173 10223 14319 9898 -703 -1053 2344 C ATOM 1377 N PHE A 174 61.729 -1.562 48.965 1.00 98.63 N ANISOU 1377 N PHE D 174 10789 14856 11831 -833 -369 -1379 N ATOM 1378 CA PHE A 174 60.680 -2.533 49.352 1.00102.64 C ANISOU 1378 CA PHE D 174 12059 14291 12650 -629 -398 -2078 C ATOM 1379 C PHE A 174 60.547 -3.550 48.225 1.00108.34 C ANISOU 1379 C PHE D 174 12786 14844 13533 -651 -1222 -2243 C ATOM 1380 O PHE A 174 59.549 -3.604 47.520 1.00113.25 O ANISOU 1380 O PHE D 174 14713 14498 13819 212 -2451 -2631 O ATOM 1381 CB PHE A 174 59.388 -1.813 49.715 1.00100.89 C ANISOU 1381 CB PHE D 174 12146 13993 12196 -438 -292 -2674 C ATOM 1382 CG PHE A 174 59.377 -1.311 51.164 1.00101.23 C ANISOU 1382 CG PHE D 174 11869 14360 12232 -610 -257 -2760 C ATOM 1383 CD1 PHE A 174 60.178 -0.245 51.537 1.00101.15 C ANISOU 1383 CD1 PHE D 174 11722 14554 12156 -813 146 -2915 C ATOM 1384 CD2 PHE A 174 58.582 -1.921 52.122 1.00 99.50 C ANISOU 1384 CD2 PHE D 174 11610 14369 11828 -479 172 -2977 C ATOM 1385 CE1 PHE A 174 60.177 0.212 52.841 1.00100.80 C ANISOU 1385 CE1 PHE D 174 11514 14644 12141 -931 174 -2836 C ATOM 1386 CE2 PHE A 174 58.578 -1.481 53.431 1.00 98.42 C ANISOU 1386 CE2 PHE D 174 11506 14380 11508 -655 925 -3316 C ATOM 1387 CZ PHE A 174 59.394 -0.428 53.789 1.00100.40 C ANISOU 1387 CZ PHE D 174 11676 14579 11892 -1087 596 -3021 C ATOM 1388 N ASP A 175 61.599 -4.338 48.124 1.00112.09 N ANISOU 1388 N ASP D 175 12995 15173 14422 -436 -1786 -1485 N ATOM 1389 CA ASP A 175 62.276 -4.944 47.011 1.00115.08 C ANISOU 1389 CA ASP D 175 13761 15399 14564 -948 -2093 -893 C ATOM 1390 C ASP A 175 61.443 -4.640 45.748 1.00115.71 C ANISOU 1390 C ASP D 175 14276 15528 14161 -1845 -1488 -256 C ATOM 1391 O ASP A 175 60.609 -5.415 45.310 1.00101.68 O ANISOU 1391 O ASP D 175 8131 15542 14961 -499 -1721 -833 O ATOM 1392 CB ASP A 175 62.577 -6.441 47.107 1.00113.42 C ANISOU 1392 CB ASP D 175 13335 15222 14536 -254 -2220 -790 C ATOM 1393 CG ASP A 175 64.030 -6.761 46.744 1.00114.59 C ANISOU 1393 CG ASP D 175 14314 14779 14446 34 -1892 -751 C ATOM 1394 OD1 ASP A 175 64.806 -5.813 46.451 1.00117.13 O ANISOU 1394 OD1 ASP D 175 16380 14695 13429 52 333 -1017 O ATOM 1395 OD2 ASP A 175 64.422 -7.951 46.736 1.00114.39 O ANISOU 1395 OD2 ASP D 175 13894 14998 14569 1145 -918 -1667 O ATOM 1396 N ASN A 176 61.781 -3.445 45.280 1.00121.11 N ANISOU 1396 N ASN D 176 16259 15316 14442 -2523 -1645 359 N ATOM 1397 CA ASN A 176 61.377 -2.840 44.022 1.00119.04 C ANISOU 1397 CA ASN D 176 16189 14492 14550 -2736 -1505 839 C ATOM 1398 C ASN A 176 59.882 -2.989 43.777 1.00119.68 C ANISOU 1398 C ASN D 176 16495 14491 14488 -2749 -1624 469 C ATOM 1399 O ASN A 176 59.413 -3.141 42.652 1.00124.72 O ANISOU 1399 O ASN D 176 17735 14741 14911 -3286 -2318 -305 O ATOM 1400 CB ASN A 176 62.240 -3.476 42.919 1.00122.57 C ANISOU 1400 CB ASN D 176 17638 13976 14957 -3487 -2272 1753 C ATOM 1401 CG ASN A 176 63.633 -3.816 43.440 1.00119.83 C ANISOU 1401 CG ASN D 176 17236 13557 14738 -3318 -2834 2375 C ATOM 1402 OD1 ASN A 176 63.943 -4.974 43.726 1.00112.39 O ANISOU 1402 OD1 ASN D 176 17127 13114 12463 -3026 -3341 3384 O ATOM 1403 ND2 ASN A 176 64.486 -2.809 43.593 1.00118.58 N ANISOU 1403 ND2 ASN D 176 15982 13336 15738 -2785 -4764 2945 N ATOM 1404 N ASP A 177 59.145 -2.928 44.876 1.00121.16 N ANISOU 1404 N ASP D 177 16699 14395 14941 -2643 -2025 583 N ATOM 1405 CA ASP A 177 57.724 -3.224 44.960 1.00120.08 C ANISOU 1405 CA ASP D 177 16473 14274 14877 -2799 -2648 -20 C ATOM 1406 C ASP A 177 56.967 -2.052 45.573 1.00116.88 C ANISOU 1406 C ASP D 177 16061 14590 13758 -2498 -1936 -826 C ATOM 1407 O ASP A 177 56.829 -1.953 46.795 1.00116.90 O ANISOU 1407 O ASP D 177 15584 15979 12852 -4161 -1973 -6623 O ATOM 1408 CB ASP A 177 57.581 -4.519 45.756 1.00123.47 C ANISOU 1408 CB ASP D 177 16783 14388 15742 -4064 -3476 197 C ATOM 1409 CG ASP A 177 56.203 -4.799 46.327 1.00128.08 C ANISOU 1409 CG ASP D 177 17759 14285 16618 -4454 -4378 444 C ATOM 1410 OD1 ASP A 177 55.214 -4.302 45.740 1.00128.91 O ANISOU 1410 OD1 ASP D 177 17629 14208 17141 -3845 -5296 -103 O ATOM 1411 OD2 ASP A 177 56.113 -5.523 47.355 1.00134.42 O ANISOU 1411 OD2 ASP D 177 18686 14781 17606 -5619 -4369 1175 O ATOM 1412 N VAL A 178 56.482 -1.163 44.711 1.00118.66 N ANISOU 1412 N VAL D 178 16676 14823 13586 -3116 -1669 -593 N ATOM 1413 CA VAL A 178 55.725 0.025 45.057 1.00114.96 C ANISOU 1413 CA VAL D 178 16440 14173 13065 -2790 -1097 -961 C ATOM 1414 C VAL A 178 54.283 -0.300 45.452 1.00114.77 C ANISOU 1414 C VAL D 178 16742 13959 12908 -3083 -1201 -979 C ATOM 1415 O VAL A 178 53.345 0.109 44.762 1.00114.89 O ANISOU 1415 O VAL D 178 16482 13515 13656 -3279 -892 -779 O ATOM 1416 CB VAL A 178 55.685 1.020 43.875 1.00114.12 C ANISOU 1416 CB VAL D 178 16879 14133 12349 -2691 -1395 -955 C ATOM 1417 CG1 VAL A 178 56.102 2.417 44.303 1.00100.42 C ANISOU 1417 CG1 VAL D 178 16419 12787 8949 -1649 -3 -1912 C ATOM 1418 CG2 VAL A 178 56.575 0.509 42.736 1.00108.95 C ANISOU 1418 CG2 VAL D 178 14263 13668 13463 -2327 -635 -648 C ATOM 1419 N ASN A 179 54.110 -1.023 46.549 1.00116.58 N ANISOU 1419 N ASN D 179 17945 13795 12556 -3598 -1127 -1455 N ATOM 1420 CA ASN A 179 52.821 -1.403 47.107 1.00116.97 C ANISOU 1420 CA ASN D 179 19049 13285 12108 -3906 -966 -1844 C ATOM 1421 C ASN A 179 52.968 -1.709 48.602 1.00115.42 C ANISOU 1421 C ASN D 179 18661 12859 12334 -4366 -546 -1960 C ATOM 1422 O ASN A 179 51.993 -1.741 49.341 1.00111.17 O ANISOU 1422 O ASN D 179 18670 11973 11594 -4270 -82 -2598 O ATOM 1423 CB ASN A 179 52.232 -2.631 46.414 1.00126.19 C ANISOU 1423 CB ASN D 179 20612 14193 13140 -4450 -586 -3101 C ATOM 1424 CG ASN A 179 51.405 -2.318 45.183 1.00133.83 C ANISOU 1424 CG ASN D 179 21547 15588 13714 -4664 -1 -3782 C ATOM 1425 OD1 ASN A 179 50.488 -1.489 45.214 1.00141.47 O ANISOU 1425 OD1 ASN D 179 22131 16168 15453 -3717 104 -5270 O ATOM 1426 ND2 ASN A 179 51.716 -2.987 44.075 1.00140.96 N ANISOU 1426 ND2 ASN D 179 22307 17586 13667 -5567 -254 -4832 N ATOM 1427 N GLN A 180 54.220 -1.932 48.968 1.00113.09 N ANISOU 1427 N GLN D 180 18065 12522 12383 -4550 -539 -1364 N ATOM 1428 CA GLN A 180 54.637 -2.266 50.318 1.00111.28 C ANISOU 1428 CA GLN D 180 17368 12221 12694 -4603 -233 -1241 C ATOM 1429 C GLN A 180 55.279 -1.072 51.026 1.00107.47 C ANISOU 1429 C GLN D 180 16498 11752 12582 -4276 637 -1433 C ATOM 1430 O GLN A 180 55.179 -0.962 52.249 1.00110.04 O ANISOU 1430 O GLN D 180 17836 11203 12770 -6924 -34 -201 O ATOM 1431 CB GLN A 180 55.611 -3.451 50.290 1.00115.85 C ANISOU 1431 CB GLN D 180 17179 13290 13550 -5064 -396 -286 C ATOM 1432 CG GLN A 180 55.172 -4.601 51.190 1.00120.97 C ANISOU 1432 CG GLN D 180 17873 13992 14097 -4886 274 156 C ATOM 1433 CD GLN A 180 54.159 -4.155 52.239 1.00126.63 C ANISOU 1433 CD GLN D 180 19208 14437 14468 -4872 -191 735 C ATOM 1434 OE1 GLN A 180 54.533 -3.709 53.323 1.00134.88 O ANISOU 1434 OE1 GLN D 180 21173 16732 13344 -5194 390 1458 O ATOM 1435 NE2 GLN A 180 52.874 -4.261 51.913 1.00134.37 N ANISOU 1435 NE2 GLN D 180 20493 13494 17068 -4682 -570 1136 N ATOM 1436 N VAL A 181 55.914 -0.223 50.225 1.00 91.41 N ANISOU 1436 N VAL D 181 12209 11447 11077 -2514 -691 -1245 N ATOM 1437 CA VAL A 181 56.436 1.071 50.656 1.00 87.48 C ANISOU 1437 CA VAL D 181 12009 11197 10032 -2443 244 -1415 C ATOM 1438 C VAL A 181 55.420 1.743 51.576 1.00 80.41 C ANISOU 1438 C VAL D 181 10823 10634 9095 -1836 1155 -2706 C ATOM 1439 O VAL A 181 54.310 2.000 51.097 1.00 92.19 O ANISOU 1439 O VAL D 181 11677 11840 11511 -1460 997 -4631 O ATOM 1440 CB VAL A 181 56.732 1.997 49.460 1.00 90.28 C ANISOU 1440 CB VAL D 181 12256 11761 10287 -2070 945 -1371 C ATOM 1441 CG1 VAL A 181 57.621 3.165 49.884 1.00 79.58 C ANISOU 1441 CG1 VAL D 181 8542 12793 8903 -2166 3719 -2698 C ATOM 1442 CG2 VAL A 181 57.342 1.204 48.309 1.00 90.23 C ANISOU 1442 CG2 VAL D 181 13190 11625 9469 -2396 839 -1705 C ATOM 1443 N PRO A 182 55.757 2.007 52.825 1.00 78.75 N ANISOU 1443 N PRO D 182 10355 10446 9119 -2988 1354 -2686 N ATOM 1444 CA PRO A 182 54.767 2.497 53.804 1.00 76.52 C ANISOU 1444 CA PRO D 182 10676 9754 8644 -3288 1639 -2374 C ATOM 1445 C PRO A 182 54.058 3.728 53.267 1.00 71.68 C ANISOU 1445 C PRO D 182 10376 9002 7857 -3382 1082 -2873 C ATOM 1446 O PRO A 182 54.619 4.473 52.454 1.00 66.00 O ANISOU 1446 O PRO D 182 9654 8907 6513 -1321 1615 -2978 O ATOM 1447 CB PRO A 182 55.638 2.813 55.021 1.00 75.44 C ANISOU 1447 CB PRO D 182 10308 9585 8770 -2867 1719 -2322 C ATOM 1448 CG PRO A 182 56.813 1.898 54.889 1.00 76.20 C ANISOU 1448 CG PRO D 182 10118 9995 8838 -3110 1344 -2279 C ATOM 1449 CD PRO A 182 57.099 1.887 53.407 1.00 76.74 C ANISOU 1449 CD PRO D 182 10206 10234 8719 -3262 1277 -2719 C ATOM 1450 N LYS A 183 52.807 3.971 53.642 1.00 66.25 N ANISOU 1450 N LYS D 183 10340 8136 6695 -4050 1488 -2470 N ATOM 1451 CA LYS A 183 52.133 5.095 52.995 1.00 67.52 C ANISOU 1451 CA LYS D 183 10571 8502 6581 -3366 1692 -1915 C ATOM 1452 C LYS A 183 52.530 6.409 53.656 1.00 61.25 C ANISOU 1452 C LYS D 183 9080 8020 6172 -2590 2056 -1793 C ATOM 1453 O LYS A 183 52.465 7.467 53.033 1.00 62.32 O ANISOU 1453 O LYS D 183 8010 8614 7056 -1762 3204 -3628 O ATOM 1454 CB LYS A 183 50.618 4.927 53.042 1.00 75.36 C ANISOU 1454 CB LYS D 183 12471 8389 7774 -2993 2715 -2713 C ATOM 1455 CG LYS A 183 50.096 4.133 51.844 1.00 84.45 C ANISOU 1455 CG LYS D 183 14227 9329 8531 -2830 1521 -3164 C ATOM 1456 CD LYS A 183 51.211 3.333 51.191 1.00 95.52 C ANISOU 1456 CD LYS D 183 15282 11438 9573 -3046 265 -1703 C ATOM 1457 CE LYS A 183 51.153 3.352 49.672 1.00101.86 C ANISOU 1457 CE LYS D 183 16632 12453 9618 -3588 396 -1398 C ATOM 1458 NZ LYS A 183 52.465 2.963 49.070 1.00102.56 N ANISOU 1458 NZ LYS D 183 16349 13890 8727 -3036 990 -1168 N ATOM 1459 N TYR A 184 52.933 6.309 54.917 1.00 51.83 N ANISOU 1459 N TYR D 184 7385 6107 6202 -1451 1991 -1376 N ATOM 1460 CA TYR A 184 53.177 7.491 55.718 1.00 55.27 C ANISOU 1460 CA TYR D 184 8249 6086 6665 -1439 1539 -1697 C ATOM 1461 C TYR A 184 54.549 7.453 56.387 1.00 50.14 C ANISOU 1461 C TYR D 184 7486 5664 5900 -936 511 -893 C ATOM 1462 O TYR A 184 55.174 6.402 56.538 1.00 48.87 O ANISOU 1462 O TYR D 184 7286 5065 6217 -912 -386 -628 O ATOM 1463 CB TYR A 184 52.139 7.641 56.825 1.00 53.58 C ANISOU 1463 CB TYR D 184 6222 6312 7825 -223 1467 -2105 C ATOM 1464 CG TYR A 184 50.696 7.617 56.402 1.00 65.46 C ANISOU 1464 CG TYR D 184 7173 6790 10910 -60 1811 -3275 C ATOM 1465 CD1 TYR A 184 49.901 8.753 56.485 1.00 67.60 C ANISOU 1465 CD1 TYR D 184 6973 7049 11662 58 3033 -3556 C ATOM 1466 CD2 TYR A 184 50.115 6.443 55.931 1.00 73.31 C ANISOU 1466 CD2 TYR D 184 8066 7074 12715 -474 2087 -4017 C ATOM 1467 CE1 TYR A 184 48.572 8.727 56.100 1.00 72.07 C ANISOU 1467 CE1 TYR D 184 7801 7118 12467 126 3804 -3699 C ATOM 1468 CE2 TYR A 184 48.793 6.400 55.538 1.00 77.62 C ANISOU 1468 CE2 TYR D 184 8961 6918 13614 -526 2886 -4002 C ATOM 1469 CZ TYR A 184 48.031 7.545 55.628 1.00 77.23 C ANISOU 1469 CZ TYR D 184 8779 7214 13351 -254 4043 -4133 C ATOM 1470 OH TYR A 184 46.711 7.490 55.241 1.00 81.19 O ANISOU 1470 OH TYR D 184 9978 6232 14639 -89 4148 -3058 O ATOM 1471 N ALA A 185 54.989 8.644 56.798 1.00 44.28 N ANISOU 1471 N ALA D 185 6583 5134 5106 -446 559 -397 N ATOM 1472 CA ALA A 185 56.260 8.766 57.499 1.00 41.54 C ANISOU 1472 CA ALA D 185 6004 5031 4749 -416 508 -104 C ATOM 1473 C ALA A 185 56.162 9.851 58.562 1.00 39.24 C ANISOU 1473 C ALA D 185 5740 4871 4300 -717 912 133 C ATOM 1474 O ALA A 185 55.319 10.730 58.406 1.00 40.15 O ANISOU 1474 O ALA D 185 5793 5070 4394 -630 878 -475 O ATOM 1475 CB ALA A 185 57.395 9.101 56.548 1.00 40.34 C ANISOU 1475 CB ALA D 185 5188 5388 4751 -438 771 151 C ATOM 1476 N LEU A 186 57.022 9.735 59.557 1.00 37.19 N ANISOU 1476 N LEU D 186 5393 4789 3950 -862 1160 535 N ATOM 1477 CA LEU A 186 57.193 10.813 60.533 1.00 35.06 C ANISOU 1477 CA LEU D 186 4702 4519 4100 -214 1223 282 C ATOM 1478 C LEU A 186 58.398 11.643 60.084 1.00 33.86 C ANISOU 1478 C LEU D 186 4382 4655 3830 -287 401 524 C ATOM 1479 O LEU A 186 59.392 11.022 59.685 1.00 34.53 O ANISOU 1479 O LEU D 186 4199 5283 3639 -774 52 1064 O ATOM 1480 CB LEU A 186 57.412 10.291 61.943 1.00 36.12 C ANISOU 1480 CB LEU D 186 4452 5494 3779 94 711 865 C ATOM 1481 CG LEU A 186 56.177 10.188 62.833 1.00 39.23 C ANISOU 1481 CG LEU D 186 6353 4183 4371 259 794 461 C ATOM 1482 CD1 LEU A 186 54.955 9.911 61.990 1.00 42.75 C ANISOU 1482 CD1 LEU D 186 9437 3566 3240 -1441 -472 -47 C ATOM 1483 CD2 LEU A 186 56.369 9.142 63.934 1.00 40.18 C ANISOU 1483 CD2 LEU D 186 6145 4354 4767 -1365 226 1002 C ATOM 1484 N THR A 187 58.322 12.970 60.133 1.00 30.92 N ANISOU 1484 N THR D 187 4133 4155 3461 94 150 309 N ATOM 1485 CA THR A 187 59.481 13.763 59.713 1.00 32.43 C ANISOU 1485 CA THR D 187 4606 4346 3371 -190 -100 590 C ATOM 1486 C THR A 187 59.673 14.989 60.568 1.00 30.01 C ANISOU 1486 C THR D 187 4081 4157 3164 -36 197 666 C ATOM 1487 O THR A 187 58.698 15.637 60.980 1.00 30.48 O ANISOU 1487 O THR D 187 3846 4335 3400 -14 462 717 O ATOM 1488 CB THR A 187 59.298 14.191 58.242 1.00 33.44 C ANISOU 1488 CB THR D 187 4926 4319 3459 -409 73 284 C ATOM 1489 OG1 THR A 187 60.420 14.952 57.767 1.00 37.26 O ANISOU 1489 OG1 THR D 187 6156 4383 3620 301 1094 527 O ATOM 1490 CG2 THR A 187 58.060 15.086 58.078 1.00 33.76 C ANISOU 1490 CG2 THR D 187 5268 4475 3086 12 -123 -62 C ATOM 1491 N VAL A 188 60.907 15.379 60.862 1.00 28.57 N ANISOU 1491 N VAL D 188 3740 4203 2911 -94 603 608 N ATOM 1492 CA VAL A 188 61.056 16.687 61.499 1.00 29.31 C ANISOU 1492 CA VAL D 188 3735 4253 3147 34 387 510 C ATOM 1493 C VAL A 188 60.551 17.784 60.573 1.00 30.26 C ANISOU 1493 C VAL D 188 3591 4490 3416 -170 473 -521 C ATOM 1494 O VAL A 188 60.454 17.614 59.343 1.00 29.19 O ANISOU 1494 O VAL D 188 3485 4361 3245 -525 366 186 O ATOM 1495 CB VAL A 188 62.529 16.976 61.841 1.00 29.17 C ANISOU 1495 CB VAL D 188 4038 4367 2679 -104 1059 342 C ATOM 1496 CG1 VAL A 188 63.046 15.936 62.832 1.00 31.08 C ANISOU 1496 CG1 VAL D 188 3683 4932 3194 -158 1065 776 C ATOM 1497 CG2 VAL A 188 63.378 16.996 60.573 1.00 28.12 C ANISOU 1497 CG2 VAL D 188 3455 4019 3209 -169 1025 629 C ATOM 1498 N GLY A 189 60.228 18.933 61.164 1.00 28.38 N ANISOU 1498 N GLY D 189 3717 3841 3224 -117 155 384 N ATOM 1499 CA GLY A 189 59.749 20.045 60.363 1.00 28.02 C ANISOU 1499 CA GLY D 189 3469 4112 3066 46 -121 769 C ATOM 1500 C GLY A 189 60.835 20.974 59.862 1.00 27.71 C ANISOU 1500 C GLY D 189 3463 3891 3172 18 212 417 C ATOM 1501 O GLY A 189 62.008 20.823 60.238 1.00 27.45 O ANISOU 1501 O GLY D 189 3160 3989 3282 -145 31 50 O ATOM 1502 N VAL A 190 60.450 21.937 59.026 1.00 26.82 N ANISOU 1502 N VAL D 190 3465 3926 2798 112 107 420 N ATOM 1503 CA VAL A 190 61.455 22.878 58.521 1.00 26.93 C ANISOU 1503 CA VAL D 190 3389 4048 2796 131 90 577 C ATOM 1504 C VAL A 190 61.969 23.753 59.650 1.00 28.09 C ANISOU 1504 C VAL D 190 3785 3971 2918 -213 119 637 C ATOM 1505 O VAL A 190 63.149 24.091 59.727 1.00 30.94 O ANISOU 1505 O VAL D 190 4716 3911 3129 -189 60 682 O ATOM 1506 CB VAL A 190 60.898 23.747 57.379 1.00 26.99 C ANISOU 1506 CB VAL D 190 3112 3553 3590 -134 386 136 C ATOM 1507 CG1 VAL A 190 61.949 24.739 56.874 1.00 25.38 C ANISOU 1507 CG1 VAL D 190 2744 3342 3558 112 575 -44 C ATOM 1508 CG2 VAL A 190 60.395 22.889 56.219 1.00 27.32 C ANISOU 1508 CG2 VAL D 190 4403 2881 3095 133 365 484 C ATOM 1509 N GLY A 191 61.084 24.137 60.564 1.00 28.27 N ANISOU 1509 N GLY D 191 3208 4106 3427 -304 -227 355 N ATOM 1510 CA GLY A 191 61.419 24.909 61.759 1.00 28.37 C ANISOU 1510 CA GLY D 191 3342 3994 3444 -476 -138 303 C ATOM 1511 C GLY A 191 62.374 24.116 62.635 1.00 28.92 C ANISOU 1511 C GLY D 191 3516 4195 3278 -472 -45 463 C ATOM 1512 O GLY A 191 63.335 24.641 63.204 1.00 30.95 O ANISOU 1512 O GLY D 191 3779 4123 3859 -480 519 391 O ATOM 1513 N THR A 192 62.111 22.813 62.746 1.00 29.18 N ANISOU 1513 N THR D 192 3439 4502 3147 -591 -134 402 N ATOM 1514 CA THR A 192 63.007 21.938 63.502 1.00 29.81 C ANISOU 1514 CA THR D 192 3857 4395 3073 -556 226 626 C ATOM 1515 C THR A 192 64.428 22.035 62.957 1.00 29.87 C ANISOU 1515 C THR D 192 4123 4135 3090 -435 71 136 C ATOM 1516 O THR A 192 65.421 22.166 63.671 1.00 30.88 O ANISOU 1516 O THR D 192 3359 4959 3417 -200 564 -87 O ATOM 1517 CB THR A 192 62.549 20.473 63.402 1.00 30.46 C ANISOU 1517 CB THR D 192 3949 4135 3491 -437 1053 19 C ATOM 1518 OG1 THR A 192 61.120 20.420 63.487 1.00 30.94 O ANISOU 1518 OG1 THR D 192 4233 4289 3235 -315 469 522 O ATOM 1519 CG2 THR A 192 63.108 19.647 64.557 1.00 28.56 C ANISOU 1519 CG2 THR D 192 3804 4881 2167 -406 239 587 C ATOM 1520 N LEU A 193 64.530 21.962 61.622 1.00 29.30 N ANISOU 1520 N LEU D 193 3907 4130 3097 -445 -282 243 N ATOM 1521 CA LEU A 193 65.852 22.055 60.997 1.00 28.61 C ANISOU 1521 CA LEU D 193 3432 4212 3224 9 467 216 C ATOM 1522 C LEU A 193 66.430 23.445 61.196 1.00 28.75 C ANISOU 1522 C LEU D 193 3528 4125 3272 31 128 531 C ATOM 1523 O LEU A 193 67.605 23.562 61.569 1.00 29.30 O ANISOU 1523 O LEU D 193 4126 4214 2793 -10 282 293 O ATOM 1524 CB LEU A 193 65.704 21.743 59.530 1.00 31.34 C ANISOU 1524 CB LEU D 193 4114 4565 3228 132 -171 407 C ATOM 1525 CG LEU A 193 66.802 21.381 58.554 1.00 35.04 C ANISOU 1525 CG LEU D 193 5419 4216 3677 812 52 819 C ATOM 1526 CD1 LEU A 193 67.045 22.524 57.559 1.00 39.91 C ANISOU 1526 CD1 LEU D 193 4504 3781 6878 259 -509 2372 C ATOM 1527 CD2 LEU A 193 68.112 20.978 59.210 1.00 40.58 C ANISOU 1527 CD2 LEU D 193 7843 3165 4409 1560 41 377 C ATOM 1528 N LEU A 194 65.627 24.486 60.937 1.00 28.35 N ANISOU 1528 N LEU D 194 3406 4654 2710 -78 -153 487 N ATOM 1529 CA LEU A 194 66.187 25.837 61.006 1.00 29.18 C ANISOU 1529 CA LEU D 194 3512 4386 3188 42 788 217 C ATOM 1530 C LEU A 194 66.600 26.234 62.408 1.00 27.64 C ANISOU 1530 C LEU D 194 3308 3882 3311 13 459 277 C ATOM 1531 O LEU A 194 67.440 27.119 62.619 1.00 32.48 O ANISOU 1531 O LEU D 194 4441 4208 3691 -751 230 449 O ATOM 1532 CB LEU A 194 65.171 26.859 60.460 1.00 30.39 C ANISOU 1532 CB LEU D 194 3416 4337 3793 268 610 -13 C ATOM 1533 CG LEU A 194 65.013 26.807 58.931 1.00 32.67 C ANISOU 1533 CG LEU D 194 4476 4134 3803 244 1480 184 C ATOM 1534 CD1 LEU A 194 63.917 27.748 58.444 1.00 33.19 C ANISOU 1534 CD1 LEU D 194 3856 4679 4076 -249 1257 200 C ATOM 1535 CD2 LEU A 194 66.347 27.111 58.260 1.00 37.87 C ANISOU 1535 CD2 LEU D 194 5689 4563 4135 478 209 271 C ATOM 1536 N ASP A 195 66.023 25.614 63.425 1.00 30.12 N ANISOU 1536 N ASP D 195 4211 4072 3163 -662 590 131 N ATOM 1537 CA ASP A 195 66.440 25.921 64.781 1.00 29.64 C ANISOU 1537 CA ASP D 195 4302 3758 3203 98 -79 213 C ATOM 1538 C ASP A 195 67.842 25.398 65.074 1.00 29.57 C ANISOU 1538 C ASP D 195 4117 3778 3340 -45 -78 100 C ATOM 1539 O ASP A 195 68.415 25.763 66.114 1.00 32.41 O ANISOU 1539 O ASP D 195 4205 4517 3592 -211 318 -376 O ATOM 1540 CB ASP A 195 65.493 25.261 65.793 1.00 32.84 C ANISOU 1540 CB ASP D 195 4666 4408 3404 87 -719 714 C ATOM 1541 CG ASP A 195 64.189 25.994 65.950 1.00 36.78 C ANISOU 1541 CG ASP D 195 5311 4142 4521 658 -307 529 C ATOM 1542 OD1 ASP A 195 64.115 27.120 65.417 1.00 41.73 O ANISOU 1542 OD1 ASP D 195 4379 5412 6064 -338 -1138 -93 O ATOM 1543 OD2 ASP A 195 63.283 25.438 66.597 1.00 46.56 O ANISOU 1543 OD2 ASP D 195 7158 4576 5955 488 -1854 1342 O ATOM 1544 N ALA A 196 68.417 24.546 64.231 1.00 29.67 N ANISOU 1544 N ALA D 196 3714 4500 3058 -289 263 755 N ATOM 1545 CA ALA A 196 69.785 24.089 64.543 1.00 27.17 C ANISOU 1545 CA ALA D 196 3566 4341 2418 -493 286 664 C ATOM 1546 C ALA A 196 70.781 25.237 64.446 1.00 28.00 C ANISOU 1546 C ALA D 196 3307 4465 2866 -680 569 151 C ATOM 1547 O ALA A 196 70.565 26.221 63.738 1.00 28.87 O ANISOU 1547 O ALA D 196 3380 4911 2678 -817 407 523 O ATOM 1548 CB ALA A 196 70.198 22.984 63.606 1.00 26.85 C ANISOU 1548 CB ALA D 196 3786 3619 2796 -451 4 594 C ATOM 1549 N GLU A 197 71.886 25.146 65.157 1.00 27.17 N ANISOU 1549 N GLU D 197 3167 4506 2651 43 -131 398 N ATOM 1550 CA GLU A 197 72.916 26.163 65.188 1.00 30.24 C ANISOU 1550 CA GLU D 197 3681 4448 3362 63 432 377 C ATOM 1551 C GLU A 197 73.617 26.263 63.842 1.00 30.02 C ANISOU 1551 C GLU D 197 3932 4152 3320 -495 120 257 C ATOM 1552 O GLU A 197 73.986 27.351 63.394 1.00 29.71 O ANISOU 1552 O GLU D 197 3706 5116 2466 -914 330 -139 O ATOM 1553 CB GLU A 197 73.949 25.792 66.253 1.00 40.52 C ANISOU 1553 CB GLU D 197 6248 5074 4074 -980 1874 -674 C ATOM 1554 CG GLU A 197 74.829 26.933 66.714 1.00 60.69 C ANISOU 1554 CG GLU D 197 10960 5871 6230 -2159 2147 -1972 C ATOM 1555 CD GLU A 197 75.631 26.593 67.958 1.00 66.66 C ANISOU 1555 CD GLU D 197 12361 6294 6674 -1720 2370 -2598 C ATOM 1556 OE1 GLU A 197 74.998 26.269 68.995 1.00 68.95 O ANISOU 1556 OE1 GLU D 197 12681 6424 7091 -1696 3962 -2134 O ATOM 1557 OE2 GLU A 197 76.882 26.656 67.880 1.00 72.08 O ANISOU 1557 OE2 GLU D 197 12903 7065 7420 -834 2072 -2632 O ATOM 1558 N GLU A 198 73.829 25.126 63.201 1.00 29.40 N ANISOU 1558 N GLU D 198 4080 4111 2979 -884 400 26 N ATOM 1559 CA GLU A 198 74.478 25.049 61.890 1.00 29.14 C ANISOU 1559 CA GLU D 198 3686 4407 2976 -596 412 4 C ATOM 1560 C GLU A 198 73.780 23.969 61.076 1.00 30.64 C ANISOU 1560 C GLU D 198 3990 4706 2945 -952 421 17 C ATOM 1561 O GLU A 198 73.400 22.928 61.639 1.00 26.56 O ANISOU 1561 O GLU D 198 3260 4014 2819 -140 508 -1 O ATOM 1562 CB GLU A 198 75.966 24.759 62.053 1.00 29.18 C ANISOU 1562 CB GLU D 198 3211 4607 3268 -706 933 303 C ATOM 1563 CG GLU A 198 76.751 24.639 60.745 1.00 32.96 C ANISOU 1563 CG GLU D 198 3877 4954 3691 -308 357 332 C ATOM 1564 CD GLU A 198 78.238 24.517 61.029 1.00 36.62 C ANISOU 1564 CD GLU D 198 5000 4709 4204 -89 1011 746 C ATOM 1565 OE1 GLU A 198 78.601 23.818 61.999 1.00 36.61 O ANISOU 1565 OE1 GLU D 198 5321 4283 4307 -280 1223 248 O ATOM 1566 OE2 GLU A 198 79.075 25.109 60.311 1.00 43.85 O ANISOU 1566 OE2 GLU D 198 7564 4664 4432 -101 1557 743 O ATOM 1567 N VAL A 199 73.585 24.218 59.787 1.00 28.01 N ANISOU 1567 N VAL D 199 3735 3995 2911 -590 355 193 N ATOM 1568 CA VAL A 199 72.913 23.279 58.899 1.00 28.79 C ANISOU 1568 CA VAL D 199 4099 3913 2926 -422 35 243 C ATOM 1569 C VAL A 199 73.870 22.946 57.763 1.00 26.71 C ANISOU 1569 C VAL D 199 3439 3620 3092 -347 251 296 C ATOM 1570 O VAL A 199 74.358 23.884 57.105 1.00 28.14 O ANISOU 1570 O VAL D 199 3635 4215 2844 -635 380 363 O ATOM 1571 CB VAL A 199 71.615 23.862 58.321 1.00 26.90 C ANISOU 1571 CB VAL D 199 3876 3732 2611 -293 -478 289 C ATOM 1572 CG1 VAL A 199 70.981 22.918 57.314 1.00 26.66 C ANISOU 1572 CG1 VAL D 199 4317 4077 1737 -515 -252 492 C ATOM 1573 CG2 VAL A 199 70.630 24.140 59.439 1.00 26.84 C ANISOU 1573 CG2 VAL D 199 3784 4224 2189 -724 -423 415 C ATOM 1574 N MET A 200 74.131 21.667 57.550 1.00 25.82 N ANISOU 1574 N MET D 200 3405 3339 3067 -293 498 -199 N ATOM 1575 CA MET A 200 75.034 21.258 56.470 1.00 26.13 C ANISOU 1575 CA MET D 200 3086 3834 3009 -311 524 -191 C ATOM 1576 C MET A 200 74.284 20.325 55.530 1.00 26.51 C ANISOU 1576 C MET D 200 3359 3860 2853 -621 688 -45 C ATOM 1577 O MET A 200 73.861 19.231 55.932 1.00 26.60 O ANISOU 1577 O MET D 200 3277 3787 3044 -483 920 -67 O ATOM 1578 CB MET A 200 76.295 20.593 57.043 1.00 25.55 C ANISOU 1578 CB MET D 200 3154 3628 2926 -420 893 307 C ATOM 1579 CG MET A 200 77.240 20.006 55.996 1.00 27.01 C ANISOU 1579 CG MET D 200 3214 3595 3455 -318 604 244 C ATOM 1580 SD MET A 200 78.798 19.437 56.699 1.00 28.73 S ANISOU 1580 SD MET D 200 3551 3918 3448 -104 689 149 S ATOM 1581 CE MET A 200 78.267 18.000 57.647 1.00 26.69 C ANISOU 1581 CE MET D 200 2874 4794 2472 -335 27 342 C ATOM 1582 N ILE A 201 74.095 20.755 54.275 1.00 23.46 N ANISOU 1582 N ILE D 201 2655 3502 2756 -211 435 140 N ATOM 1583 CA ILE A 201 73.329 19.984 53.314 1.00 24.79 C ANISOU 1583 CA ILE D 201 3173 3587 2659 -135 141 166 C ATOM 1584 C ILE A 201 74.279 19.340 52.312 1.00 26.52 C ANISOU 1584 C ILE D 201 3302 3637 3138 -120 -129 255 C ATOM 1585 O ILE A 201 75.119 20.033 51.732 1.00 27.81 O ANISOU 1585 O ILE D 201 4090 3835 2643 -342 -290 292 O ATOM 1586 CB ILE A 201 72.319 20.866 52.566 1.00 27.24 C ANISOU 1586 CB ILE D 201 3374 3618 3356 163 152 -363 C ATOM 1587 CG1 ILE A 201 71.422 21.643 53.540 1.00 27.24 C ANISOU 1587 CG1 ILE D 201 3081 3946 3322 -139 251 -186 C ATOM 1588 CG2 ILE A 201 71.514 20.035 51.575 1.00 25.31 C ANISOU 1588 CG2 ILE D 201 3326 3157 3136 -130 215 74 C ATOM 1589 CD1 ILE A 201 70.506 20.699 54.313 1.00 28.28 C ANISOU 1589 CD1 ILE D 201 3584 4313 2850 -494 -85 -87 C ATOM 1590 N LEU A 202 74.126 18.041 52.154 1.00 26.31 N ANISOU 1590 N LEU D 202 3092 3731 3174 -22 64 -128 N ATOM 1591 CA LEU A 202 74.885 17.257 51.204 1.00 26.30 C ANISOU 1591 CA LEU D 202 3483 3728 2784 -398 -43 153 C ATOM 1592 C LEU A 202 74.153 17.294 49.859 1.00 27.46 C ANISOU 1592 C LEU D 202 3413 4048 2970 -16 191 179 C ATOM 1593 O LEU A 202 72.969 16.945 49.800 1.00 28.40 O ANISOU 1593 O LEU D 202 3715 3947 3129 -232 511 123 O ATOM 1594 CB LEU A 202 75.005 15.809 51.644 1.00 27.98 C ANISOU 1594 CB LEU D 202 3026 4205 3402 -8 200 67 C ATOM 1595 CG LEU A 202 76.115 15.329 52.574 1.00 32.57 C ANISOU 1595 CG LEU D 202 4884 4340 3151 -665 1223 -340 C ATOM 1596 CD1 LEU A 202 76.753 16.448 53.361 1.00 29.03 C ANISOU 1596 CD1 LEU D 202 4459 5402 1168 -774 316 322 C ATOM 1597 CD2 LEU A 202 75.591 14.237 53.489 1.00 28.96 C ANISOU 1597 CD2 LEU D 202 4928 4324 1753 -81 81 254 C ATOM 1598 N VAL A 203 74.871 17.686 48.818 1.00 27.08 N ANISOU 1598 N VAL D 203 3379 4070 2841 -319 158 136 N ATOM 1599 CA VAL A 203 74.231 17.775 47.507 1.00 28.32 C ANISOU 1599 CA VAL D 203 3361 4483 2917 -368 193 -54 C ATOM 1600 C VAL A 203 74.985 16.950 46.455 1.00 28.11 C ANISOU 1600 C VAL D 203 3351 4416 2913 -207 204 -341 C ATOM 1601 O VAL A 203 76.089 17.355 46.063 1.00 31.28 O ANISOU 1601 O VAL D 203 4296 4820 2771 -986 -232 601 O ATOM 1602 CB VAL A 203 74.135 19.247 47.065 1.00 31.03 C ANISOU 1602 CB VAL D 203 3660 5547 2583 -1005 156 -265 C ATOM 1603 CG1 VAL A 203 73.284 19.338 45.776 1.00 27.47 C ANISOU 1603 CG1 VAL D 203 3351 4595 2491 -504 -35 175 C ATOM 1604 CG2 VAL A 203 73.581 20.169 48.148 1.00 29.06 C ANISOU 1604 CG2 VAL D 203 3679 5007 2355 -1074 283 118 C ATOM 1605 N LEU A 204 74.402 15.827 46.022 1.00 30.58 N ANISOU 1605 N LEU D 204 3955 4885 2778 -1079 110 214 N ATOM 1606 CA LEU A 204 75.017 14.876 45.117 1.00 30.91 C ANISOU 1606 CA LEU D 204 3857 4859 3028 -978 77 43 C ATOM 1607 C LEU A 204 74.172 14.609 43.882 1.00 29.57 C ANISOU 1607 C LEU D 204 3398 4788 3048 -201 -283 88 C ATOM 1608 O LEU A 204 72.988 14.296 43.988 1.00 31.99 O ANISOU 1608 O LEU D 204 4527 4559 3069 -551 -246 384 O ATOM 1609 CB LEU A 204 75.241 13.530 45.825 1.00 31.23 C ANISOU 1609 CB LEU D 204 3744 4804 3316 -564 188 378 C ATOM 1610 CG LEU A 204 76.180 13.535 47.031 1.00 34.71 C ANISOU 1610 CG LEU D 204 4546 4360 4282 -557 1005 214 C ATOM 1611 CD1 LEU A 204 76.279 12.136 47.618 1.00 33.44 C ANISOU 1611 CD1 LEU D 204 3953 5118 3633 -175 495 933 C ATOM 1612 CD2 LEU A 204 77.561 14.081 46.658 1.00 31.49 C ANISOU 1612 CD2 LEU D 204 4245 4809 2909 -221 105 641 C ATOM 1613 N GLY A 205 74.760 14.697 42.681 1.00 29.39 N ANISOU 1613 N GLY D 205 3684 4477 3005 108 341 145 N ATOM 1614 CA GLY A 205 74.031 14.251 41.500 1.00 29.33 C ANISOU 1614 CA GLY D 205 3309 4893 2943 -186 184 46 C ATOM 1615 C GLY A 205 73.452 15.422 40.732 1.00 29.69 C ANISOU 1615 C GLY D 205 3654 4708 2919 -229 429 95 C ATOM 1616 O GLY A 205 73.031 16.416 41.304 1.00 28.46 O ANISOU 1616 O GLY D 205 3423 4190 3199 -544 655 -51 O ATOM 1617 N SER A 206 73.460 15.277 39.405 1.00 31.83 N ANISOU 1617 N SER D 206 4673 4502 2919 -549 548 -276 N ATOM 1618 CA SER A 206 72.891 16.326 38.561 1.00 29.80 C ANISOU 1618 CA SER D 206 4041 4962 2320 -526 -102 -270 C ATOM 1619 C SER A 206 71.395 16.450 38.791 1.00 31.69 C ANISOU 1619 C SER D 206 4450 4768 2821 -451 78 -368 C ATOM 1620 O SER A 206 70.821 17.492 38.468 1.00 28.29 O ANISOU 1620 O SER D 206 4255 4279 2215 -476 -394 268 O ATOM 1621 CB SER A 206 73.200 16.059 37.078 1.00 33.90 C ANISOU 1621 CB SER D 206 4494 6018 2369 -833 -305 -238 C ATOM 1622 OG SER A 206 72.504 14.877 36.692 1.00 38.87 O ANISOU 1622 OG SER D 206 5664 6409 2695 -1460 -1342 262 O ATOM 1623 N GLN A 207 70.729 15.441 39.353 1.00 30.40 N ANISOU 1623 N GLN D 207 3695 4607 3248 -457 63 -618 N ATOM 1624 CA GLN A 207 69.312 15.643 39.647 1.00 32.40 C ANISOU 1624 CA GLN D 207 4520 4248 3542 -300 14 -920 C ATOM 1625 C GLN A 207 69.081 16.707 40.722 1.00 29.27 C ANISOU 1625 C GLN D 207 4194 3487 3441 -283 30 -247 C ATOM 1626 O GLN A 207 67.937 17.175 40.861 1.00 29.03 O ANISOU 1626 O GLN D 207 4537 3459 3036 -42 551 326 O ATOM 1627 CB GLN A 207 68.654 14.315 40.043 1.00 36.95 C ANISOU 1627 CB GLN D 207 4455 5029 4553 -804 -1270 278 C ATOM 1628 CG GLN A 207 68.909 13.883 41.474 1.00 47.12 C ANISOU 1628 CG GLN D 207 5195 7212 5495 -2280 256 49 C ATOM 1629 CD GLN A 207 70.077 12.920 41.601 1.00 58.32 C ANISOU 1629 CD GLN D 207 5271 8711 8178 -2199 1161 -85 C ATOM 1630 OE1 GLN A 207 71.070 13.013 40.853 1.00 66.79 O ANISOU 1630 OE1 GLN D 207 6080 5957 13342 -1004 1966 -111 O ATOM 1631 NE2 GLN A 207 69.947 11.992 42.557 1.00 76.22 N ANISOU 1631 NE2 GLN D 207 4748 13694 10520 -4923 636 1575 N ATOM 1632 N LYS A 208 70.090 17.116 41.485 1.00 25.90 N ANISOU 1632 N LYS D 208 4036 3076 2728 -346 -118 256 N ATOM 1633 CA LYS A 208 69.966 18.149 42.502 1.00 26.11 C ANISOU 1633 CA LYS D 208 3765 3732 2423 -458 139 294 C ATOM 1634 C LYS A 208 70.399 19.523 42.015 1.00 26.21 C ANISOU 1634 C LYS D 208 3512 3888 2558 -387 -252 646 C ATOM 1635 O LYS A 208 70.460 20.515 42.741 1.00 26.03 O ANISOU 1635 O LYS D 208 3872 3305 2713 -291 -176 195 O ATOM 1636 CB LYS A 208 70.866 17.787 43.691 1.00 26.25 C ANISOU 1636 CB LYS D 208 3674 3411 2887 -397 148 -17 C ATOM 1637 CG LYS A 208 70.633 16.351 44.164 1.00 30.23 C ANISOU 1637 CG LYS D 208 4395 3646 3444 -621 1015 -299 C ATOM 1638 CD LYS A 208 69.207 16.154 44.656 1.00 31.45 C ANISOU 1638 CD LYS D 208 4882 3749 3319 -1187 -14 134 C ATOM 1639 CE LYS A 208 69.137 14.830 45.414 1.00 33.73 C ANISOU 1639 CE LYS D 208 4506 4101 4209 -1327 -214 329 C ATOM 1640 NZ LYS A 208 67.751 14.513 45.823 1.00 36.37 N ANISOU 1640 NZ LYS D 208 5786 3210 4825 -1811 65 -212 N ATOM 1641 N ALA A 209 70.754 19.612 40.749 1.00 27.52 N ANISOU 1641 N ALA D 209 3856 3895 2704 -341 -333 905 N ATOM 1642 CA ALA A 209 71.349 20.844 40.238 1.00 25.88 C ANISOU 1642 CA ALA D 209 3565 3497 2773 -123 -826 957 C ATOM 1643 C ALA A 209 70.395 22.023 40.329 1.00 25.14 C ANISOU 1643 C ALA D 209 3546 3492 2513 -82 -760 754 C ATOM 1644 O ALA A 209 70.824 23.138 40.672 1.00 26.85 O ANISOU 1644 O ALA D 209 3455 3812 2936 -140 -241 8 O ATOM 1645 CB ALA A 209 71.850 20.624 38.803 1.00 23.02 C ANISOU 1645 CB ALA D 209 2921 3511 2316 25 -299 546 C ATOM 1646 N LEU A 210 69.119 21.821 40.034 1.00 25.44 N ANISOU 1646 N LEU D 210 3524 3670 2471 -183 -458 358 N ATOM 1647 CA LEU A 210 68.190 22.969 40.134 1.00 25.96 C ANISOU 1647 CA LEU D 210 3513 3934 2415 -72 -197 183 C ATOM 1648 C LEU A 210 68.005 23.390 41.584 1.00 25.20 C ANISOU 1648 C LEU D 210 3328 3734 2514 20 -310 632 C ATOM 1649 O LEU A 210 67.862 24.575 41.899 1.00 31.16 O ANISOU 1649 O LEU D 210 4203 4560 3078 -900 -917 898 O ATOM 1650 CB LEU A 210 66.823 22.659 39.518 1.00 27.50 C ANISOU 1650 CB LEU D 210 3969 3660 2821 -64 138 434 C ATOM 1651 CG LEU A 210 66.770 22.689 37.992 1.00 30.14 C ANISOU 1651 CG LEU D 210 4555 3985 2914 -429 747 -23 C ATOM 1652 CD1 LEU A 210 65.475 22.071 37.481 1.00 40.51 C ANISOU 1652 CD1 LEU D 210 6486 4436 4470 -530 822 -963 C ATOM 1653 CD2 LEU A 210 66.916 24.107 37.467 1.00 33.37 C ANISOU 1653 CD2 LEU D 210 4280 4458 3940 -58 1358 352 C ATOM 1654 N ALA A 211 68.005 22.393 42.480 1.00 27.48 N ANISOU 1654 N ALA D 211 4486 3291 2663 -308 115 631 N ATOM 1655 CA ALA A 211 67.900 22.725 43.889 1.00 28.29 C ANISOU 1655 CA ALA D 211 3993 4123 2631 -618 294 169 C ATOM 1656 C ALA A 211 69.126 23.497 44.359 1.00 28.10 C ANISOU 1656 C ALA D 211 4031 3919 2728 -565 200 406 C ATOM 1657 O ALA A 211 68.978 24.436 45.154 1.00 28.25 O ANISOU 1657 O ALA D 211 3966 3542 3227 -506 8 452 O ATOM 1658 CB ALA A 211 67.708 21.443 44.678 1.00 25.95 C ANISOU 1658 CB ALA D 211 3715 3845 2298 -492 -138 300 C ATOM 1659 N LEU A 212 70.322 23.126 43.900 1.00 29.74 N ANISOU 1659 N LEU D 212 4595 4129 2575 -549 -229 649 N ATOM 1660 CA LEU A 212 71.554 23.790 44.304 1.00 25.23 C ANISOU 1660 CA LEU D 212 3555 4092 1940 -464 -338 834 C ATOM 1661 C LEU A 212 71.512 25.246 43.841 1.00 26.45 C ANISOU 1661 C LEU D 212 3253 4091 2706 -119 118 416 C ATOM 1662 O LEU A 212 71.924 26.155 44.557 1.00 26.73 O ANISOU 1662 O LEU D 212 3539 3928 2690 -461 108 723 O ATOM 1663 CB LEU A 212 72.793 23.179 43.684 1.00 26.14 C ANISOU 1663 CB LEU D 212 3254 5074 1604 -148 130 1069 C ATOM 1664 CG LEU A 212 74.051 22.984 44.499 1.00 31.40 C ANISOU 1664 CG LEU D 212 4836 4104 2990 228 -696 230 C ATOM 1665 CD1 LEU A 212 75.293 23.168 43.633 1.00 31.16 C ANISOU 1665 CD1 LEU D 212 5718 3975 2147 -356 505 747 C ATOM 1666 CD2 LEU A 212 74.150 23.877 45.732 1.00 29.99 C ANISOU 1666 CD2 LEU D 212 3747 2975 4675 428 -1429 -231 C ATOM 1667 N GLN A 213 71.023 25.374 42.613 1.00 28.60 N ANISOU 1667 N GLN D 213 3647 4297 2922 23 421 291 N ATOM 1668 CA GLN A 213 70.908 26.729 42.051 1.00 28.27 C ANISOU 1668 CA GLN D 213 3770 4308 2664 43 296 648 C ATOM 1669 C GLN A 213 69.927 27.576 42.867 1.00 27.90 C ANISOU 1669 C GLN D 213 3697 3508 3397 162 48 28 C ATOM 1670 O GLN A 213 70.206 28.755 43.124 1.00 26.94 O ANISOU 1670 O GLN D 213 3530 3710 2995 -146 559 542 O ATOM 1671 CB GLN A 213 70.507 26.673 40.565 1.00 29.86 C ANISOU 1671 CB GLN D 213 4273 4258 2815 304 573 427 C ATOM 1672 CG GLN A 213 70.830 27.980 39.837 1.00 39.30 C ANISOU 1672 CG GLN D 213 6207 5403 3322 -880 1789 -170 C ATOM 1673 CD GLN A 213 69.674 28.959 39.900 1.00 45.82 C ANISOU 1673 CD GLN D 213 5764 6136 5508 -1206 2816 22 C ATOM 1674 OE1 GLN A 213 68.570 28.530 40.247 1.00 53.98 O ANISOU 1674 OE1 GLN D 213 5710 6244 8557 -370 2661 187 O ATOM 1675 NE2 GLN A 213 69.872 30.237 39.623 1.00 57.17 N ANISOU 1675 NE2 GLN D 213 6683 8012 7026 -2886 1918 53 N ATOM 1676 N ALA A 214 68.799 26.970 43.237 1.00 28.99 N ANISOU 1676 N ALA D 214 4033 3798 3185 -353 -195 686 N ATOM 1677 CA ALA A 214 67.808 27.713 44.009 1.00 28.54 C ANISOU 1677 CA ALA D 214 3677 3693 3475 -175 -111 350 C ATOM 1678 C ALA A 214 68.379 28.059 45.376 1.00 28.15 C ANISOU 1678 C ALA D 214 3485 3684 3525 -42 -286 270 C ATOM 1679 O ALA A 214 68.068 29.149 45.888 1.00 32.38 O ANISOU 1679 O ALA D 214 3423 5591 3289 -771 170 210 O ATOM 1680 CB ALA A 214 66.512 26.946 44.208 1.00 28.84 C ANISOU 1680 CB ALA D 214 3188 3675 4096 -530 -1297 130 C ATOM 1681 N ALA A 215 69.188 27.175 45.956 1.00 26.92 N ANISOU 1681 N ALA D 215 3358 3711 3160 20 -495 438 N ATOM 1682 CA ALA A 215 69.778 27.445 47.270 1.00 30.50 C ANISOU 1682 CA ALA D 215 4225 3758 3604 -113 -91 36 C ATOM 1683 C ALA A 215 70.798 28.580 47.210 1.00 27.87 C ANISOU 1683 C ALA D 215 3067 3676 3846 215 -514 194 C ATOM 1684 O ALA A 215 70.819 29.451 48.079 1.00 28.10 O ANISOU 1684 O ALA D 215 3415 4015 3248 -44 -217 177 O ATOM 1685 CB ALA A 215 70.427 26.195 47.867 1.00 26.25 C ANISOU 1685 CB ALA D 215 4114 3604 2255 -51 -540 938 C ATOM 1686 N VAL A 216 71.658 28.579 46.193 1.00 26.01 N ANISOU 1686 N VAL D 216 2832 4068 2981 93 223 219 N ATOM 1687 CA VAL A 216 72.825 29.442 46.172 1.00 28.99 C ANISOU 1687 CA VAL D 216 3507 4112 3397 -225 178 765 C ATOM 1688 C VAL A 216 72.590 30.709 45.366 1.00 28.46 C ANISOU 1688 C VAL D 216 3112 4337 3362 -369 41 110 C ATOM 1689 O VAL A 216 72.957 31.808 45.833 1.00 31.65 O ANISOU 1689 O VAL D 216 3387 4551 4086 -556 -656 424 O ATOM 1690 CB VAL A 216 74.024 28.669 45.579 1.00 29.65 C ANISOU 1690 CB VAL D 216 3251 3832 4183 68 523 354 C ATOM 1691 CG1 VAL A 216 75.243 29.554 45.336 1.00 29.03 C ANISOU 1691 CG1 VAL D 216 3443 3719 3869 105 375 13 C ATOM 1692 CG2 VAL A 216 74.409 27.505 46.495 1.00 30.11 C ANISOU 1692 CG2 VAL D 216 3985 3878 3576 615 904 487 C ATOM 1693 N GLU A 217 72.009 30.645 44.172 1.00 29.52 N ANISOU 1693 N GLU D 217 3976 4112 3127 260 137 542 N ATOM 1694 CA GLU A 217 71.931 31.841 43.327 1.00 27.64 C ANISOU 1694 CA GLU D 217 3965 3921 2615 -127 -259 328 C ATOM 1695 C GLU A 217 70.519 32.399 43.287 1.00 27.57 C ANISOU 1695 C GLU D 217 3324 3921 3230 -513 -371 158 C ATOM 1696 O GLU A 217 70.332 33.567 42.972 1.00 30.82 O ANISOU 1696 O GLU D 217 3867 4616 3227 -699 388 516 O ATOM 1697 CB GLU A 217 72.294 31.593 41.857 1.00 28.51 C ANISOU 1697 CB GLU D 217 4447 3723 2661 -394 -510 230 C ATOM 1698 CG GLU A 217 73.759 31.513 41.529 1.00 31.72 C ANISOU 1698 CG GLU D 217 5028 3915 3109 -231 -796 545 C ATOM 1699 CD GLU A 217 74.010 30.984 40.131 1.00 30.22 C ANISOU 1699 CD GLU D 217 4414 4065 3004 153 -513 122 C ATOM 1700 OE1 GLU A 217 73.046 30.822 39.350 1.00 35.52 O ANISOU 1700 OE1 GLU D 217 5903 4209 3386 209 -68 -39 O ATOM 1701 OE2 GLU A 217 75.163 30.704 39.747 1.00 30.37 O ANISOU 1701 OE2 GLU D 217 4816 3827 2895 -71 -240 972 O ATOM 1702 N GLY A 218 69.517 31.580 43.572 1.00 27.03 N ANISOU 1702 N GLY D 218 3319 3806 3146 -253 182 24 N ATOM 1703 CA GLY A 218 68.163 32.111 43.452 1.00 27.96 C ANISOU 1703 CA GLY D 218 3346 4040 3238 -207 332 -278 C ATOM 1704 C GLY A 218 67.771 33.000 44.611 1.00 26.15 C ANISOU 1704 C GLY D 218 3303 3304 3330 261 346 -666 C ATOM 1705 O GLY A 218 68.527 33.226 45.540 1.00 26.74 O ANISOU 1705 O GLY D 218 3373 3412 3376 240 541 -709 O ATOM 1706 N CYS A 219 66.549 33.533 44.576 1.00 24.88 N ANISOU 1706 N CYS D 219 3568 2925 2958 352 743 37 N ATOM 1707 CA CYS A 219 66.097 34.342 45.679 1.00 30.38 C ANISOU 1707 CA CYS D 219 4496 3078 3969 623 -280 303 C ATOM 1708 C CYS A 219 65.316 33.490 46.688 1.00 30.85 C ANISOU 1708 C CYS D 219 4438 3599 3682 74 -540 392 C ATOM 1709 O CYS A 219 64.933 32.352 46.413 1.00 25.68 O ANISOU 1709 O CYS D 219 3123 3511 3124 661 -12 78 O ATOM 1710 CB CYS A 219 65.202 35.488 45.203 1.00 37.11 C ANISOU 1710 CB CYS D 219 3936 4930 5235 -330 -381 641 C ATOM 1711 SG CYS A 219 66.067 36.764 44.249 1.00 58.04 S ANISOU 1711 SG CYS D 219 7872 5748 8434 -1355 2190 1007 S ATOM 1712 N VAL A 220 65.079 34.077 47.849 1.00 27.88 N ANISOU 1712 N VAL D 220 3496 3703 3394 104 59 -12 N ATOM 1713 CA VAL A 220 64.326 33.384 48.892 1.00 26.75 C ANISOU 1713 CA VAL D 220 3323 3784 3057 282 28 -76 C ATOM 1714 C VAL A 220 62.870 33.162 48.487 1.00 26.58 C ANISOU 1714 C VAL D 220 3305 3766 3028 181 527 46 C ATOM 1715 O VAL A 220 62.117 34.077 48.135 1.00 26.98 O ANISOU 1715 O VAL D 220 3141 3674 3436 -52 435 -131 O ATOM 1716 CB VAL A 220 64.413 34.163 50.215 1.00 33.69 C ANISOU 1716 CB VAL D 220 5260 4232 3308 -763 -327 -237 C ATOM 1717 CG1 VAL A 220 63.517 33.488 51.263 1.00 29.53 C ANISOU 1717 CG1 VAL D 220 4246 4100 2875 -432 -540 -467 C ATOM 1718 CG2 VAL A 220 65.859 34.248 50.673 1.00 29.12 C ANISOU 1718 CG2 VAL D 220 4256 4208 2601 -760 -991 -56 C ATOM 1719 N ASN A 221 62.434 31.895 48.527 1.00 23.80 N ANISOU 1719 N ASN D 221 2734 3576 2733 519 250 357 N ATOM 1720 CA ASN A 221 61.025 31.653 48.252 1.00 26.01 C ANISOU 1720 CA ASN D 221 2969 3599 3315 539 773 400 C ATOM 1721 C ASN A 221 60.608 30.312 48.842 1.00 28.17 C ANISOU 1721 C ASN D 221 2942 3749 4012 85 133 543 C ATOM 1722 O ASN A 221 61.395 29.368 48.857 1.00 30.71 O ANISOU 1722 O ASN D 221 3047 3707 4914 270 773 475 O ATOM 1723 CB ASN A 221 60.729 31.709 46.754 1.00 33.22 C ANISOU 1723 CB ASN D 221 5329 3818 3475 153 881 -227 C ATOM 1724 CG ASN A 221 61.126 30.380 46.152 1.00 39.44 C ANISOU 1724 CG ASN D 221 6876 4170 3941 -916 -536 452 C ATOM 1725 OD1 ASN A 221 60.272 29.506 46.031 1.00 50.59 O ANISOU 1725 OD1 ASN D 221 9635 4632 4955 -1970 -966 36 O ATOM 1726 ND2 ASN A 221 62.402 30.273 45.818 1.00 39.14 N ANISOU 1726 ND2 ASN D 221 4934 5456 4482 -196 908 529 N ATOM 1727 N HIS A 222 59.378 30.232 49.345 1.00 24.93 N ANISOU 1727 N HIS D 222 3292 3123 3055 99 244 -201 N ATOM 1728 CA HIS A 222 58.983 29.022 50.056 1.00 28.03 C ANISOU 1728 CA HIS D 222 3672 3846 3130 -342 -116 313 C ATOM 1729 C HIS A 222 58.744 27.838 49.137 1.00 25.51 C ANISOU 1729 C HIS D 222 3150 3788 2756 -191 167 370 C ATOM 1730 O HIS A 222 58.569 26.716 49.594 1.00 26.47 O ANISOU 1730 O HIS D 222 3347 4108 2601 -357 606 -136 O ATOM 1731 CB HIS A 222 57.726 29.331 50.888 1.00 27.71 C ANISOU 1731 CB HIS D 222 3610 4005 2913 -335 -149 269 C ATOM 1732 CG HIS A 222 56.493 29.557 50.068 1.00 30.41 C ANISOU 1732 CG HIS D 222 4463 3639 3452 -122 171 392 C ATOM 1733 ND1 HIS A 222 55.255 29.377 50.623 1.00 30.51 N ANISOU 1733 ND1 HIS D 222 4026 3751 3813 -351 -41 647 N ATOM 1734 CD2 HIS A 222 56.264 29.957 48.775 1.00 28.37 C ANISOU 1734 CD2 HIS D 222 3804 3680 3294 164 -146 175 C ATOM 1735 CE1 HIS A 222 54.316 29.633 49.725 1.00 29.61 C ANISOU 1735 CE1 HIS D 222 3212 3860 4178 -174 -48 794 C ATOM 1736 NE2 HIS A 222 54.895 29.986 48.588 1.00 27.77 N ANISOU 1736 NE2 HIS D 222 3066 3834 3652 142 -437 335 N ATOM 1737 N MET A 223 58.689 28.043 47.817 1.00 25.07 N ANISOU 1737 N MET D 223 3191 3482 2852 -2 648 90 N ATOM 1738 CA MET A 223 58.407 26.885 46.966 1.00 27.84 C ANISOU 1738 CA MET D 223 3817 3836 2926 20 235 -63 C ATOM 1739 C MET A 223 59.656 25.997 46.848 1.00 28.01 C ANISOU 1739 C MET D 223 3332 3791 3519 -420 477 -313 C ATOM 1740 O MET A 223 59.540 24.780 46.653 1.00 32.61 O ANISOU 1740 O MET D 223 4043 4364 3982 -827 -476 -588 O ATOM 1741 CB MET A 223 57.906 27.285 45.581 1.00 31.81 C ANISOU 1741 CB MET D 223 3759 4994 3335 -137 569 -704 C ATOM 1742 CG MET A 223 56.496 27.807 45.431 1.00 35.49 C ANISOU 1742 CG MET D 223 4971 4284 4229 278 1229 -251 C ATOM 1743 SD MET A 223 55.152 26.643 45.754 1.00 45.43 S ANISOU 1743 SD MET D 223 7173 4720 5367 -457 4 786 S ATOM 1744 CE MET A 223 55.786 25.155 45.016 1.00 45.69 C ANISOU 1744 CE MET D 223 6965 6223 4174 -1548 947 -545 C ATOM 1745 N TRP A 224 60.845 26.579 46.954 1.00 26.46 N ANISOU 1745 N TRP D 224 3248 3792 3012 -210 580 -393 N ATOM 1746 CA TRP A 224 62.112 25.874 47.032 1.00 25.51 C ANISOU 1746 CA TRP D 224 2915 3982 2794 -399 599 -47 C ATOM 1747 C TRP A 224 62.617 26.039 48.460 1.00 23.92 C ANISOU 1747 C TRP D 224 2798 3541 2750 126 299 111 C ATOM 1748 O TRP A 224 63.351 26.995 48.741 1.00 28.18 O ANISOU 1748 O TRP D 224 4073 4026 2607 -664 -261 251 O ATOM 1749 CB TRP A 224 63.125 26.433 46.033 1.00 26.22 C ANISOU 1749 CB TRP D 224 3118 4195 2652 -420 353 18 C ATOM 1750 CG TRP A 224 62.705 26.145 44.606 1.00 27.79 C ANISOU 1750 CG TRP D 224 3388 4375 2797 -169 32 -98 C ATOM 1751 CD1 TRP A 224 61.797 26.846 43.871 1.00 28.37 C ANISOU 1751 CD1 TRP D 224 3671 4310 2800 -9 -75 -617 C ATOM 1752 CD2 TRP A 224 63.164 25.100 43.746 1.00 28.12 C ANISOU 1752 CD2 TRP D 224 3668 4114 2901 -141 -221 210 C ATOM 1753 NE1 TRP A 224 61.657 26.317 42.624 1.00 29.97 N ANISOU 1753 NE1 TRP D 224 3806 4833 2747 -261 -224 -395 N ATOM 1754 CE2 TRP A 224 62.492 25.230 42.517 1.00 30.42 C ANISOU 1754 CE2 TRP D 224 3885 4698 2975 -218 -329 -98 C ATOM 1755 CE3 TRP A 224 64.076 24.057 43.880 1.00 27.83 C ANISOU 1755 CE3 TRP D 224 3701 3809 3064 31 -475 414 C ATOM 1756 CZ2 TRP A 224 62.705 24.363 41.447 1.00 30.60 C ANISOU 1756 CZ2 TRP D 224 3923 4616 3087 -197 -442 -43 C ATOM 1757 CZ3 TRP A 224 64.296 23.189 42.825 1.00 28.39 C ANISOU 1757 CZ3 TRP D 224 3913 3697 3177 -26 -548 146 C ATOM 1758 CH2 TRP A 224 63.608 23.347 41.611 1.00 29.45 C ANISOU 1758 CH2 TRP D 224 3780 4361 3050 -619 -160 298 C ATOM 1759 N THR A 225 62.198 25.152 49.365 1.00 24.46 N ANISOU 1759 N THR D 225 2994 3587 2711 71 623 -144 N ATOM 1760 CA THR A 225 62.459 25.300 50.791 1.00 23.89 C ANISOU 1760 CA THR D 225 2936 3457 2683 -37 365 -176 C ATOM 1761 C THR A 225 63.931 25.567 51.068 1.00 23.19 C ANISOU 1761 C THR D 225 3060 3332 2421 -189 -249 -227 C ATOM 1762 O THR A 225 64.267 26.403 51.905 1.00 24.92 O ANISOU 1762 O THR D 225 3742 3616 2112 -581 -167 -160 O ATOM 1763 CB THR A 225 62.016 24.030 51.546 1.00 28.76 C ANISOU 1763 CB THR D 225 5097 3622 2209 -1100 151 -226 C ATOM 1764 OG1 THR A 225 60.650 23.772 51.221 1.00 26.14 O ANISOU 1764 OG1 THR D 225 3254 3870 2808 -573 134 514 O ATOM 1765 CG2 THR A 225 62.082 24.244 53.053 1.00 25.10 C ANISOU 1765 CG2 THR D 225 3289 3990 2260 -19 -1080 637 C ATOM 1766 N ILE A 226 64.805 24.865 50.368 1.00 23.82 N ANISOU 1766 N ILE D 226 3298 3556 2197 -70 -148 250 N ATOM 1767 CA ILE A 226 66.247 25.004 50.542 1.00 26.22 C ANISOU 1767 CA ILE D 226 3673 3367 2922 -125 -323 466 C ATOM 1768 C ILE A 226 66.709 26.446 50.362 1.00 27.08 C ANISOU 1768 C ILE D 226 3529 3616 3145 -236 -8 -107 C ATOM 1769 O ILE A 226 67.729 26.844 50.964 1.00 25.56 O ANISOU 1769 O ILE D 226 3398 3644 2671 -280 170 31 O ATOM 1770 CB ILE A 226 67.022 24.078 49.574 1.00 24.10 C ANISOU 1770 CB ILE D 226 3102 3689 2368 264 168 -148 C ATOM 1771 CG1 ILE A 226 68.486 23.870 49.993 1.00 26.09 C ANISOU 1771 CG1 ILE D 226 2996 3888 3031 95 447 -573 C ATOM 1772 CG2 ILE A 226 66.958 24.557 48.110 1.00 22.86 C ANISOU 1772 CG2 ILE D 226 2494 3551 2642 498 325 295 C ATOM 1773 CD1 ILE A 226 68.624 23.003 51.237 1.00 30.57 C ANISOU 1773 CD1 ILE D 226 3755 4324 3538 229 1015 -389 C ATOM 1774 N SER A 227 66.002 27.255 49.561 1.00 25.04 N ANISOU 1774 N SER D 227 3424 3454 2636 -15 -298 -68 N ATOM 1775 CA SER A 227 66.407 28.655 49.407 1.00 26.89 C ANISOU 1775 CA SER D 227 3845 3709 2662 -327 253 -370 C ATOM 1776 C SER A 227 66.303 29.420 50.727 1.00 27.33 C ANISOU 1776 C SER D 227 3780 3607 2999 -575 -69 -80 C ATOM 1777 O SER A 227 66.972 30.431 50.928 1.00 25.90 O ANISOU 1777 O SER D 227 3228 3565 3048 -395 43 -78 O ATOM 1778 CB SER A 227 65.569 29.376 48.348 1.00 28.65 C ANISOU 1778 CB SER D 227 3612 3899 3375 57 326 -525 C ATOM 1779 OG SER A 227 64.247 29.630 48.826 1.00 29.28 O ANISOU 1779 OG SER D 227 4302 3703 3122 -12 499 -34 O ATOM 1780 N CYS A 228 65.445 28.941 51.656 1.00 27.72 N ANISOU 1780 N CYS D 228 3531 3482 3517 -138 -413 144 N ATOM 1781 CA CYS A 228 65.352 29.775 52.861 1.00 30.52 C ANISOU 1781 CA CYS D 228 3796 4297 3502 -259 -491 167 C ATOM 1782 C CYS A 228 66.580 29.568 53.745 1.00 28.64 C ANISOU 1782 C CYS D 228 4034 3652 3198 -282 -635 375 C ATOM 1783 O CYS A 228 66.764 30.322 54.707 1.00 28.04 O ANISOU 1783 O CYS D 228 4053 4283 2318 -141 -620 895 O ATOM 1784 CB CYS A 228 63.986 29.546 53.524 1.00 35.97 C ANISOU 1784 CB CYS D 228 4947 4097 4625 374 -2151 -672 C ATOM 1785 SG CYS A 228 62.625 29.881 52.276 1.00 44.93 S ANISOU 1785 SG CYS D 228 6784 4787 5499 995 -101 253 S ATOM 1786 N LEU A 229 67.474 28.624 53.437 1.00 25.14 N ANISOU 1786 N LEU D 229 3768 3358 2425 -601 -289 556 N ATOM 1787 CA LEU A 229 68.729 28.549 54.198 1.00 26.01 C ANISOU 1787 CA LEU D 229 3763 3876 2245 -645 -166 307 C ATOM 1788 C LEU A 229 69.607 29.774 54.010 1.00 27.05 C ANISOU 1788 C LEU D 229 3811 3617 2851 -359 608 -10 C ATOM 1789 O LEU A 229 70.547 29.998 54.786 1.00 25.11 O ANISOU 1789 O LEU D 229 3310 3704 2526 -28 400 164 O ATOM 1790 CB LEU A 229 69.522 27.286 53.822 1.00 27.99 C ANISOU 1790 CB LEU D 229 3715 4359 2561 -462 -105 389 C ATOM 1791 CG LEU A 229 68.912 25.996 54.398 1.00 35.45 C ANISOU 1791 CG LEU D 229 4502 5677 3289 -1842 -283 498 C ATOM 1792 CD1 LEU A 229 69.713 24.783 53.976 1.00 35.34 C ANISOU 1792 CD1 LEU D 229 4276 6000 3152 -1493 117 -705 C ATOM 1793 CD2 LEU A 229 68.858 26.084 55.916 1.00 30.45 C ANISOU 1793 CD2 LEU D 229 3824 4477 3267 -1275 323 542 C ATOM 1794 N GLN A 230 69.325 30.594 53.004 1.00 26.40 N ANISOU 1794 N GLN D 230 3851 3533 2648 -560 549 -290 N ATOM 1795 CA GLN A 230 70.024 31.860 52.839 1.00 25.65 C ANISOU 1795 CA GLN D 230 3857 3443 2445 -411 8 347 C ATOM 1796 C GLN A 230 69.820 32.769 54.055 1.00 24.61 C ANISOU 1796 C GLN D 230 3239 3277 2836 167 82 -266 C ATOM 1797 O GLN A 230 70.628 33.655 54.327 1.00 26.95 O ANISOU 1797 O GLN D 230 3802 3453 2986 -187 192 -316 O ATOM 1798 CB GLN A 230 69.528 32.616 51.595 1.00 25.56 C ANISOU 1798 CB GLN D 230 4034 3023 2655 -236 224 432 C ATOM 1799 CG GLN A 230 69.902 31.950 50.281 1.00 25.03 C ANISOU 1799 CG GLN D 230 3973 3053 2486 296 372 499 C ATOM 1800 CD GLN A 230 69.402 32.720 49.073 1.00 27.22 C ANISOU 1800 CD GLN D 230 3859 3743 2742 -48 491 -185 C ATOM 1801 OE1 GLN A 230 69.277 33.951 49.133 1.00 28.77 O ANISOU 1801 OE1 GLN D 230 3961 3766 3204 -190 487 95 O ATOM 1802 NE2 GLN A 230 69.117 32.010 47.977 1.00 31.30 N ANISOU 1802 NE2 GLN D 230 4572 4527 2795 -375 440 -383 N ATOM 1803 N LEU A 231 68.709 32.547 54.762 1.00 25.39 N ANISOU 1803 N LEU D 231 3599 3562 2485 206 -28 -133 N ATOM 1804 CA LEU A 231 68.399 33.368 55.918 1.00 24.25 C ANISOU 1804 CA LEU D 231 3256 3484 2474 130 188 -459 C ATOM 1805 C LEU A 231 68.927 32.722 57.199 1.00 24.06 C ANISOU 1805 C LEU D 231 3218 3411 2514 113 235 -303 C ATOM 1806 O LEU A 231 68.835 33.298 58.291 1.00 31.82 O ANISOU 1806 O LEU D 231 4543 5218 2330 -1154 174 -216 O ATOM 1807 CB LEU A 231 66.887 33.571 56.058 1.00 25.21 C ANISOU 1807 CB LEU D 231 2684 3926 2969 149 149 -360 C ATOM 1808 CG LEU A 231 66.232 34.201 54.827 1.00 27.06 C ANISOU 1808 CG LEU D 231 3295 3610 3378 173 658 -285 C ATOM 1809 CD1 LEU A 231 64.738 34.351 55.082 1.00 28.51 C ANISOU 1809 CD1 LEU D 231 3502 4002 3326 534 145 -685 C ATOM 1810 CD2 LEU A 231 66.936 35.511 54.508 1.00 28.42 C ANISOU 1810 CD2 LEU D 231 3397 4006 3397 -320 521 -514 C ATOM 1811 N HIS A 232 69.483 31.525 57.065 1.00 26.95 N ANISOU 1811 N HIS D 232 3167 3463 3609 -99 451 265 N ATOM 1812 CA HIS A 232 69.954 30.857 58.286 1.00 26.73 C ANISOU 1812 CA HIS D 232 2986 3787 3384 -101 213 -20 C ATOM 1813 C HIS A 232 71.299 31.410 58.711 1.00 25.36 C ANISOU 1813 C HIS D 232 3199 3722 2714 -146 -298 93 C ATOM 1814 O HIS A 232 72.166 31.726 57.902 1.00 29.30 O ANISOU 1814 O HIS D 232 4631 3628 2874 -997 159 409 O ATOM 1815 CB HIS A 232 69.996 29.345 58.020 1.00 24.21 C ANISOU 1815 CB HIS D 232 3148 3584 2465 -189 147 217 C ATOM 1816 CG HIS A 232 70.242 28.577 59.282 1.00 24.58 C ANISOU 1816 CG HIS D 232 3459 3392 2489 -228 314 -9 C ATOM 1817 ND1 HIS A 232 71.520 28.362 59.749 1.00 24.87 N ANISOU 1817 ND1 HIS D 232 3275 3272 2904 -316 339 11 N ATOM 1818 CD2 HIS A 232 69.386 28.006 60.156 1.00 23.99 C ANISOU 1818 CD2 HIS D 232 3153 3477 2487 -108 361 69 C ATOM 1819 CE1 HIS A 232 71.444 27.670 60.882 1.00 27.11 C ANISOU 1819 CE1 HIS D 232 3390 3582 3326 73 781 245 C ATOM 1820 NE2 HIS A 232 70.167 27.442 61.149 1.00 27.56 N ANISOU 1820 NE2 HIS D 232 3913 3291 3266 -106 1117 149 N ATOM 1821 N PRO A 233 71.532 31.575 60.016 1.00 29.85 N ANISOU 1821 N PRO D 233 4389 4130 2825 -525 -831 -39 N ATOM 1822 CA PRO A 233 72.810 32.143 60.463 1.00 29.55 C ANISOU 1822 CA PRO D 233 4353 4227 2648 -629 20 -135 C ATOM 1823 C PRO A 233 74.023 31.338 60.012 1.00 30.17 C ANISOU 1823 C PRO D 233 4240 3997 3226 -655 269 54 C ATOM 1824 O PRO A 233 75.098 31.932 59.827 1.00 30.28 O ANISOU 1824 O PRO D 233 4342 3887 3276 -373 1171 -270 O ATOM 1825 CB PRO A 233 72.720 32.112 61.990 1.00 29.53 C ANISOU 1825 CB PRO D 233 4372 4156 2691 -1082 502 167 C ATOM 1826 CG PRO A 233 71.496 31.363 62.332 1.00 33.98 C ANISOU 1826 CG PRO D 233 5727 4093 3092 -287 649 102 C ATOM 1827 CD PRO A 233 70.614 31.281 61.122 1.00 31.71 C ANISOU 1827 CD PRO D 233 5181 4341 2525 -575 -100 46 C ATOM 1828 N LYS A 234 73.944 30.024 59.832 1.00 28.88 N ANISOU 1828 N LYS D 234 3639 4258 3076 -531 1301 -227 N ATOM 1829 CA LYS A 234 75.164 29.254 59.572 1.00 29.54 C ANISOU 1829 CA LYS D 234 3940 4172 3110 -404 1065 -86 C ATOM 1830 C LYS A 234 74.875 27.998 58.756 1.00 33.54 C ANISOU 1830 C LYS D 234 4515 4743 3485 -914 306 503 C ATOM 1831 O LYS A 234 74.705 26.896 59.303 1.00 27.61 O ANISOU 1831 O LYS D 234 2921 4179 3391 248 464 169 O ATOM 1832 CB LYS A 234 75.832 28.863 60.897 1.00 30.48 C ANISOU 1832 CB LYS D 234 3351 4769 3459 -536 1563 245 C ATOM 1833 CG LYS A 234 77.340 28.800 60.767 1.00 38.16 C ANISOU 1833 CG LYS D 234 4449 4908 5142 -7 2316 -28 C ATOM 1834 CD LYS A 234 77.969 28.136 61.980 1.00 47.81 C ANISOU 1834 CD LYS D 234 6546 5808 5814 -229 3168 -1844 C ATOM 1835 CE LYS A 234 77.661 28.967 63.213 1.00 54.11 C ANISOU 1835 CE LYS D 234 8746 6080 5734 -1419 2641 -2081 C ATOM 1836 NZ LYS A 234 78.953 29.431 63.804 1.00 66.62 N ANISOU 1836 NZ LYS D 234 10734 5787 8791 -2122 2186 -2864 N ATOM 1837 N ALA A 235 74.812 28.185 57.445 1.00 27.96 N ANISOU 1837 N ALA D 235 3557 3681 3387 -288 66 568 N ATOM 1838 CA ALA A 235 74.484 27.134 56.497 1.00 31.58 C ANISOU 1838 CA ALA D 235 3988 4098 3913 -355 -424 435 C ATOM 1839 C ALA A 235 75.635 26.834 55.536 1.00 29.07 C ANISOU 1839 C ALA D 235 3748 3818 3480 -355 -57 357 C ATOM 1840 O ALA A 235 76.414 27.683 55.059 1.00 31.00 O ANISOU 1840 O ALA D 235 3926 3599 4253 -14 747 353 O ATOM 1841 CB ALA A 235 73.229 27.523 55.719 1.00 30.40 C ANISOU 1841 CB ALA D 235 4795 3101 3656 -216 -579 613 C ATOM 1842 N ILE A 236 75.762 25.534 55.238 1.00 26.94 N ANISOU 1842 N ILE D 236 3158 3904 3176 100 507 -133 N ATOM 1843 CA ILE A 236 76.820 25.050 54.369 1.00 31.10 C ANISOU 1843 CA ILE D 236 3868 4157 3793 175 -244 -227 C ATOM 1844 C ILE A 236 76.258 24.052 53.370 1.00 29.56 C ANISOU 1844 C ILE D 236 3757 4065 3411 -181 121 1 C ATOM 1845 O ILE A 236 75.582 23.136 53.817 1.00 33.00 O ANISOU 1845 O ILE D 236 5284 4375 2879 -612 -69 189 O ATOM 1846 CB ILE A 236 77.921 24.352 55.189 1.00 31.23 C ANISOU 1846 CB ILE D 236 3621 4325 3921 596 -804 -478 C ATOM 1847 CG1 ILE A 236 78.336 25.156 56.414 1.00 35.13 C ANISOU 1847 CG1 ILE D 236 3770 5456 4123 385 -695 -1035 C ATOM 1848 CG2 ILE A 236 79.129 24.014 54.330 1.00 31.42 C ANISOU 1848 CG2 ILE D 236 2994 5127 3817 -118 -89 1014 C ATOM 1849 CD1 ILE A 236 79.415 24.525 57.278 1.00 55.06 C ANISOU 1849 CD1 ILE D 236 7612 6737 6571 -825 3180 -2168 C ATOM 1850 N MET A 237 76.540 24.251 52.100 1.00 29.36 N ANISOU 1850 N MET D 237 3617 4074 3464 -752 422 95 N ATOM 1851 CA MET A 237 76.224 23.306 51.049 1.00 30.49 C ANISOU 1851 CA MET D 237 3624 4555 3407 -270 224 -150 C ATOM 1852 C MET A 237 77.529 22.606 50.625 1.00 30.72 C ANISOU 1852 C MET D 237 3624 4444 3602 -190 392 -60 C ATOM 1853 O MET A 237 78.485 23.317 50.286 1.00 31.33 O ANISOU 1853 O MET D 237 3859 4527 3519 -259 548 85 O ATOM 1854 CB MET A 237 75.635 23.927 49.792 1.00 32.89 C ANISOU 1854 CB MET D 237 3613 4865 4018 -523 678 -645 C ATOM 1855 CG MET A 237 74.505 24.907 49.938 1.00 37.03 C ANISOU 1855 CG MET D 237 3307 5944 4817 -827 797 294 C ATOM 1856 SD MET A 237 73.065 24.235 50.742 1.00 48.54 S ANISOU 1856 SD MET D 237 5863 5740 6841 -99 -1040 349 S ATOM 1857 CE MET A 237 72.208 23.328 49.471 1.00 42.25 C ANISOU 1857 CE MET D 237 6070 5304 4680 934 -1908 1637 C ATOM 1858 N VAL A 238 77.504 21.286 50.670 1.00 29.35 N ANISOU 1858 N VAL D 238 3627 4330 3193 -186 196 -143 N ATOM 1859 CA VAL A 238 78.677 20.498 50.271 1.00 28.91 C ANISOU 1859 CA VAL D 238 3688 4254 3042 -176 227 13 C ATOM 1860 C VAL A 238 78.314 19.706 49.021 1.00 28.28 C ANISOU 1860 C VAL D 238 3595 4044 3107 -184 263 -10 C ATOM 1861 O VAL A 238 77.404 18.874 49.062 1.00 28.31 O ANISOU 1861 O VAL D 238 3533 4080 3146 -227 80 217 O ATOM 1862 CB VAL A 238 79.157 19.559 51.385 1.00 29.24 C ANISOU 1862 CB VAL D 238 3648 4347 3114 -173 238 -121 C ATOM 1863 CG1 VAL A 238 80.529 18.969 51.059 1.00 27.27 C ANISOU 1863 CG1 VAL D 238 3419 4035 2908 -480 56 -206 C ATOM 1864 CG2 VAL A 238 79.163 20.309 52.715 1.00 26.61 C ANISOU 1864 CG2 VAL D 238 3134 3775 3200 279 288 -355 C ATOM 1865 N CYS A 239 79.001 19.978 47.901 1.00 25.74 N ANISOU 1865 N CYS D 239 3053 3681 3047 -106 288 -148 N ATOM 1866 CA CYS A 239 78.423 19.382 46.698 1.00 29.29 C ANISOU 1866 CA CYS D 239 3473 4457 3199 307 101 -600 C ATOM 1867 C CYS A 239 79.454 18.712 45.809 1.00 28.69 C ANISOU 1867 C CYS D 239 4053 3961 2886 -135 87 142 C ATOM 1868 O CYS A 239 80.670 18.945 45.880 1.00 29.05 O ANISOU 1868 O CYS D 239 3648 3928 3461 -210 517 295 O ATOM 1869 CB CYS A 239 77.671 20.516 45.987 1.00 34.03 C ANISOU 1869 CB CYS D 239 4347 3865 4719 742 1239 -760 C ATOM 1870 SG CYS A 239 78.745 21.689 45.116 1.00 39.99 S ANISOU 1870 SG CYS D 239 5272 5296 4628 -462 850 -44 S ATOM 1871 N ASP A 240 78.940 17.825 44.929 1.00 26.15 N ANISOU 1871 N ASP D 240 3033 4251 2650 -398 564 161 N ATOM 1872 CA ASP A 240 79.845 17.182 43.985 1.00 29.09 C ANISOU 1872 CA ASP D 240 3413 4564 3075 -481 205 457 C ATOM 1873 C ASP A 240 79.776 17.889 42.639 1.00 28.66 C ANISOU 1873 C ASP D 240 3324 4458 3108 105 229 659 C ATOM 1874 O ASP A 240 79.005 18.833 42.470 1.00 28.38 O ANISOU 1874 O ASP D 240 3477 3970 3336 387 396 598 O ATOM 1875 CB ASP A 240 79.518 15.713 43.821 1.00 29.89 C ANISOU 1875 CB ASP D 240 3770 4689 2899 -685 -195 549 C ATOM 1876 CG ASP A 240 78.205 15.400 43.168 1.00 31.16 C ANISOU 1876 CG ASP D 240 4159 4670 3010 -564 -486 520 C ATOM 1877 OD1 ASP A 240 77.424 16.301 42.811 1.00 32.48 O ANISOU 1877 OD1 ASP D 240 4104 4798 3439 -167 -804 258 O ATOM 1878 OD2 ASP A 240 77.960 14.184 43.010 1.00 31.57 O ANISOU 1878 OD2 ASP D 240 4681 4817 2497 -942 -278 564 O ATOM 1879 N GLU A 241 80.585 17.444 41.690 1.00 29.71 N ANISOU 1879 N GLU D 241 3604 4350 3333 116 44 789 N ATOM 1880 CA GLU A 241 80.627 18.150 40.393 1.00 31.31 C ANISOU 1880 CA GLU D 241 4200 4568 3129 131 101 643 C ATOM 1881 C GLU A 241 79.328 18.100 39.609 1.00 29.43 C ANISOU 1881 C GLU D 241 3646 4509 3026 -128 -340 422 C ATOM 1882 O GLU A 241 78.837 19.142 39.140 1.00 29.66 O ANISOU 1882 O GLU D 241 4029 4344 2898 -75 59 731 O ATOM 1883 CB GLU A 241 81.788 17.577 39.562 1.00 31.59 C ANISOU 1883 CB GLU D 241 4093 5054 2857 382 334 599 C ATOM 1884 CG GLU A 241 81.816 18.056 38.118 1.00 39.18 C ANISOU 1884 CG GLU D 241 6070 5726 3091 -330 353 1361 C ATOM 1885 CD GLU A 241 82.979 17.379 37.404 1.00 49.17 C ANISOU 1885 CD GLU D 241 8485 5771 4425 -723 -2413 1325 C ATOM 1886 OE1 GLU A 241 84.126 17.778 37.688 1.00 58.40 O ANISOU 1886 OE1 GLU D 241 8545 5563 8081 -181 -2846 1624 O ATOM 1887 OE2 GLU A 241 82.753 16.451 36.591 1.00 68.54 O ANISOU 1887 OE2 GLU D 241 9711 9225 7105 -1444 -3487 -521 O ATOM 1888 N PRO A 242 78.694 16.947 39.385 1.00 30.69 N ANISOU 1888 N PRO D 242 4110 4639 2911 -380 -720 663 N ATOM 1889 CA PRO A 242 77.471 16.922 38.589 1.00 31.27 C ANISOU 1889 CA PRO D 242 4644 4100 3136 -448 -489 889 C ATOM 1890 C PRO A 242 76.358 17.789 39.171 1.00 29.98 C ANISOU 1890 C PRO D 242 4208 4477 2705 -484 -265 214 C ATOM 1891 O PRO A 242 75.487 18.231 38.398 1.00 31.45 O ANISOU 1891 O PRO D 242 4778 4586 2587 -409 303 684 O ATOM 1892 CB PRO A 242 77.014 15.469 38.634 1.00 33.73 C ANISOU 1892 CB PRO D 242 4340 4658 3819 -618 -690 612 C ATOM 1893 CG PRO A 242 78.129 14.678 39.235 1.00 34.64 C ANISOU 1893 CG PRO D 242 4523 4941 3700 -700 -610 174 C ATOM 1894 CD PRO A 242 79.122 15.615 39.828 1.00 34.24 C ANISOU 1894 CD PRO D 242 5007 5146 2856 -1301 125 244 C ATOM 1895 N SER A 243 76.350 18.033 40.478 1.00 29.23 N ANISOU 1895 N SER D 243 3971 4416 2718 -540 -182 61 N ATOM 1896 CA SER A 243 75.288 18.854 41.058 1.00 27.31 C ANISOU 1896 CA SER D 243 3917 4111 2349 -525 14 50 C ATOM 1897 C SER A 243 75.402 20.330 40.676 1.00 27.62 C ANISOU 1897 C SER D 243 3848 3712 2935 -250 285 29 C ATOM 1898 O SER A 243 74.467 21.107 40.894 1.00 26.17 O ANISOU 1898 O SER D 243 3898 3493 2554 -331 352 425 O ATOM 1899 CB SER A 243 75.310 18.713 42.589 1.00 29.73 C ANISOU 1899 CB SER D 243 4950 3969 2378 -585 1 256 C ATOM 1900 OG SER A 243 76.377 19.488 43.137 1.00 27.83 O ANISOU 1900 OG SER D 243 3599 4346 2629 -370 39 -250 O ATOM 1901 N THR A 244 76.546 20.740 40.121 1.00 26.75 N ANISOU 1901 N THR D 244 3617 3871 2676 -168 129 104 N ATOM 1902 CA THR A 244 76.783 22.156 39.855 1.00 27.91 C ANISOU 1902 CA THR D 244 4136 3994 2473 -596 -30 87 C ATOM 1903 C THR A 244 76.309 22.610 38.473 1.00 25.34 C ANISOU 1903 C THR D 244 3259 3619 2751 131 26 212 C ATOM 1904 O THR A 244 76.620 23.761 38.129 1.00 30.29 O ANISOU 1904 O THR D 244 4601 4276 2633 -678 -13 649 O ATOM 1905 CB THR A 244 78.278 22.541 39.936 1.00 28.25 C ANISOU 1905 CB THR D 244 4132 4062 2537 -640 618 -320 C ATOM 1906 OG1 THR A 244 78.993 21.814 38.918 1.00 31.66 O ANISOU 1906 OG1 THR D 244 4688 4038 3302 -486 317 809 O ATOM 1907 CG2 THR A 244 78.904 22.205 41.291 1.00 32.74 C ANISOU 1907 CG2 THR D 244 4748 4681 3012 -1123 1583 -177 C ATOM 1908 N MET A 245 75.607 21.784 37.716 1.00 27.73 N ANISOU 1908 N MET D 245 3833 3638 3063 254 323 -141 N ATOM 1909 CA MET A 245 75.251 22.007 36.316 1.00 29.15 C ANISOU 1909 CA MET D 245 3841 4124 3111 -106 489 -229 C ATOM 1910 C MET A 245 74.455 23.287 36.066 1.00 28.19 C ANISOU 1910 C MET D 245 3793 3985 2932 -127 329 146 C ATOM 1911 O MET A 245 74.572 23.911 34.996 1.00 28.07 O ANISOU 1911 O MET D 245 3395 4168 3100 -545 -121 637 O ATOM 1912 CB MET A 245 74.425 20.832 35.739 1.00 32.08 C ANISOU 1912 CB MET D 245 4907 4979 2302 -1388 557 16 C ATOM 1913 CG MET A 245 75.225 19.574 35.461 1.00 33.99 C ANISOU 1913 CG MET D 245 4894 4983 3038 -1511 528 382 C ATOM 1914 SD MET A 245 76.644 19.806 34.364 1.00 43.11 S ANISOU 1914 SD MET D 245 7059 5708 3614 -496 -528 370 S ATOM 1915 CE MET A 245 78.020 19.987 35.494 1.00 42.86 C ANISOU 1915 CE MET D 245 5039 5972 5272 -297 -1271 -500 C ATOM 1916 N GLU A 246 73.611 23.708 37.002 1.00 27.84 N ANISOU 1916 N GLU D 246 3908 3836 2832 -253 438 416 N ATOM 1917 CA GLU A 246 72.748 24.858 36.764 1.00 27.58 C ANISOU 1917 CA GLU D 246 3866 3777 2835 -124 306 269 C ATOM 1918 C GLU A 246 73.332 26.134 37.346 1.00 27.70 C ANISOU 1918 C GLU D 246 3831 3611 3081 5 87 364 C ATOM 1919 O GLU A 246 72.695 27.192 37.247 1.00 30.01 O ANISOU 1919 O GLU D 246 3882 4391 3127 -343 502 121 O ATOM 1920 CB GLU A 246 71.373 24.591 37.377 1.00 26.55 C ANISOU 1920 CB GLU D 246 3614 3741 2732 -456 483 478 C ATOM 1921 CG GLU A 246 70.678 23.390 36.739 1.00 29.45 C ANISOU 1921 CG GLU D 246 4390 3866 2933 -516 254 251 C ATOM 1922 CD GLU A 246 70.011 23.732 35.425 1.00 29.68 C ANISOU 1922 CD GLU D 246 3787 4147 3342 -285 257 -45 C ATOM 1923 OE1 GLU A 246 70.095 24.912 35.002 1.00 32.95 O ANISOU 1923 OE1 GLU D 246 4022 4907 3589 -275 356 926 O ATOM 1924 OE2 GLU A 246 69.401 22.830 34.808 1.00 32.32 O ANISOU 1924 OE2 GLU D 246 4831 3772 3677 228 -161 -223 O ATOM 1925 N LEU A 247 74.519 26.079 37.949 1.00 27.85 N ANISOU 1925 N LEU D 247 4243 3797 2543 -168 485 316 N ATOM 1926 CA LEU A 247 75.137 27.302 38.474 1.00 26.84 C ANISOU 1926 CA LEU D 247 4342 3880 1975 -95 222 389 C ATOM 1927 C LEU A 247 75.825 28.104 37.388 1.00 28.12 C ANISOU 1927 C LEU D 247 4599 4000 2084 -399 350 412 C ATOM 1928 O LEU A 247 76.234 27.499 36.392 1.00 27.40 O ANISOU 1928 O LEU D 247 4793 3795 1823 -571 446 390 O ATOM 1929 CB LEU A 247 76.186 26.975 39.551 1.00 26.12 C ANISOU 1929 CB LEU D 247 3883 3889 2151 -158 258 429 C ATOM 1930 CG LEU A 247 75.668 26.273 40.806 1.00 27.37 C ANISOU 1930 CG LEU D 247 4202 4010 2188 143 419 533 C ATOM 1931 CD1 LEU A 247 76.846 25.980 41.739 1.00 25.57 C ANISOU 1931 CD1 LEU D 247 2934 4540 2240 -178 83 230 C ATOM 1932 CD2 LEU A 247 74.610 27.132 41.468 1.00 24.81 C ANISOU 1932 CD2 LEU D 247 3837 3233 2357 45 816 662 C ATOM 1933 N LYS A 248 76.011 29.404 37.551 1.00 28.25 N ANISOU 1933 N LYS D 248 4041 4115 2577 -83 270 586 N ATOM 1934 CA LYS A 248 76.870 30.084 36.577 1.00 27.77 C ANISOU 1934 CA LYS D 248 3864 3955 2733 -359 -276 579 C ATOM 1935 C LYS A 248 78.333 29.725 36.832 1.00 27.06 C ANISOU 1935 C LYS D 248 3758 4145 2381 -282 -377 518 C ATOM 1936 O LYS A 248 78.726 29.490 37.979 1.00 27.94 O ANISOU 1936 O LYS D 248 3636 4469 2510 -630 -64 591 O ATOM 1937 CB LYS A 248 76.747 31.593 36.610 1.00 27.56 C ANISOU 1937 CB LYS D 248 3811 4018 2643 -336 130 12 C ATOM 1938 CG LYS A 248 75.385 32.147 36.201 1.00 30.94 C ANISOU 1938 CG LYS D 248 3946 4092 3718 324 -465 382 C ATOM 1939 CD LYS A 248 75.443 33.653 36.458 1.00 36.79 C ANISOU 1939 CD LYS D 248 3777 4469 5732 267 -268 248 C ATOM 1940 CE LYS A 248 74.089 34.306 36.210 1.00 41.56 C ANISOU 1940 CE LYS D 248 3895 5194 6701 316 1231 655 C ATOM 1941 NZ LYS A 248 74.268 35.465 35.275 1.00 64.44 N ANISOU 1941 NZ LYS D 248 7675 7829 8980 -1186 4287 57 N ATOM 1942 N VAL A 249 79.113 29.687 35.770 1.00 27.82 N ANISOU 1942 N VAL D 249 4064 3966 2541 -418 -418 653 N ATOM 1943 CA VAL A 249 80.548 29.434 35.860 1.00 29.14 C ANISOU 1943 CA VAL D 249 4339 3867 2865 -364 -622 687 C ATOM 1944 C VAL A 249 81.182 30.364 36.871 1.00 29.69 C ANISOU 1944 C VAL D 249 4243 4183 2856 -604 51 363 C ATOM 1945 O VAL A 249 82.038 29.986 37.675 1.00 29.65 O ANISOU 1945 O VAL D 249 4190 4321 2753 -180 -49 692 O ATOM 1946 CB VAL A 249 81.175 29.608 34.458 1.00 30.17 C ANISOU 1946 CB VAL D 249 4621 3819 3023 -532 -573 890 C ATOM 1947 CG1 VAL A 249 82.692 29.680 34.552 1.00 29.07 C ANISOU 1947 CG1 VAL D 249 5318 3551 2176 -649 -309 701 C ATOM 1948 CG2 VAL A 249 80.750 28.486 33.521 1.00 24.16 C ANISOU 1948 CG2 VAL D 249 3130 3405 2647 514 -231 679 C ATOM 1949 N LYS A 250 80.805 31.638 36.899 1.00 27.54 N ANISOU 1949 N LYS D 250 3970 4005 2488 39 -519 338 N ATOM 1950 CA LYS A 250 81.497 32.538 37.844 1.00 27.82 C ANISOU 1950 CA LYS D 250 4165 3806 2600 -394 167 308 C ATOM 1951 C LYS A 250 81.137 32.260 39.301 1.00 27.22 C ANISOU 1951 C LYS D 250 4222 3668 2452 -25 224 26 C ATOM 1952 O LYS A 250 81.908 32.554 40.241 1.00 28.24 O ANISOU 1952 O LYS D 250 3419 4438 2873 -240 412 -535 O ATOM 1953 CB LYS A 250 81.176 34.000 37.537 1.00 30.23 C ANISOU 1953 CB LYS D 250 4164 4250 3073 -540 123 477 C ATOM 1954 CG LYS A 250 79.680 34.308 37.691 1.00 31.70 C ANISOU 1954 CG LYS D 250 4092 4896 3057 -244 -261 487 C ATOM 1955 CD LYS A 250 79.514 35.822 37.538 1.00 35.06 C ANISOU 1955 CD LYS D 250 4216 5425 3681 -254 811 324 C ATOM 1956 CE LYS A 250 78.085 36.255 37.802 1.00 36.44 C ANISOU 1956 CE LYS D 250 4030 6135 3681 24 798 111 C ATOM 1957 NZ LYS A 250 77.946 37.722 37.581 1.00 41.29 N ANISOU 1957 NZ LYS D 250 4044 7263 4381 -820 -949 157 N ATOM 1958 N THR A 251 79.942 31.708 39.514 1.00 27.37 N ANISOU 1958 N THR D 251 3712 3797 2891 137 196 475 N ATOM 1959 CA THR A 251 79.530 31.363 40.869 1.00 31.40 C ANISOU 1959 CA THR D 251 4784 4275 2872 -274 472 537 C ATOM 1960 C THR A 251 80.392 30.223 41.391 1.00 29.52 C ANISOU 1960 C THR D 251 4861 3738 2619 -202 455 249 C ATOM 1961 O THR A 251 80.884 30.266 42.517 1.00 32.25 O ANISOU 1961 O THR D 251 5614 3891 2749 -72 548 83 O ATOM 1962 CB THR A 251 78.062 30.908 40.887 1.00 28.46 C ANISOU 1962 CB THR D 251 4228 4524 2061 80 99 797 C ATOM 1963 OG1 THR A 251 77.256 31.985 40.412 1.00 29.70 O ANISOU 1963 OG1 THR D 251 4389 4539 2356 -373 456 437 O ATOM 1964 CG2 THR A 251 77.623 30.575 42.315 1.00 31.07 C ANISOU 1964 CG2 THR D 251 5112 4743 1949 -1025 259 640 C ATOM 1965 N LEU A 252 80.555 29.205 40.539 1.00 29.85 N ANISOU 1965 N LEU D 252 4893 3879 2568 -589 377 794 N ATOM 1966 CA LEU A 252 81.365 28.047 40.924 1.00 34.76 C ANISOU 1966 CA LEU D 252 4921 5004 3281 -1060 667 206 C ATOM 1967 C LEU A 252 82.809 28.480 41.120 1.00 33.21 C ANISOU 1967 C LEU D 252 3835 5125 3657 -622 356 619 C ATOM 1968 O LEU A 252 83.503 28.085 42.065 1.00 35.21 O ANISOU 1968 O LEU D 252 4810 5168 3402 -383 402 545 O ATOM 1969 CB LEU A 252 81.178 26.930 39.890 1.00 36.74 C ANISOU 1969 CB LEU D 252 5077 5825 3058 -1259 574 306 C ATOM 1970 CG LEU A 252 81.784 25.566 40.222 1.00 39.19 C ANISOU 1970 CG LEU D 252 5216 5905 3768 -1667 697 -49 C ATOM 1971 CD1 LEU A 252 81.214 25.009 41.536 1.00 34.52 C ANISOU 1971 CD1 LEU D 252 4461 5526 3128 -1047 903 -630 C ATOM 1972 CD2 LEU A 252 81.621 24.589 39.056 1.00 35.04 C ANISOU 1972 CD2 LEU D 252 4735 5034 3545 -297 241 214 C ATOM 1973 N ARG A 253 83.333 29.345 40.256 1.00 36.36 N ANISOU 1973 N ARG D 253 5121 5135 3561 -1103 453 433 N ATOM 1974 CA ARG A 253 84.693 29.875 40.363 1.00 38.59 C ANISOU 1974 CA ARG D 253 6027 5184 3451 -732 264 695 C ATOM 1975 C ARG A 253 84.908 30.694 41.634 1.00 38.93 C ANISOU 1975 C ARG D 253 6532 4733 3528 -872 285 679 C ATOM 1976 O ARG A 253 85.954 30.615 42.293 1.00 43.82 O ANISOU 1976 O ARG D 253 8345 4533 3773 -354 382 699 O ATOM 1977 CB ARG A 253 85.017 30.705 39.093 1.00 39.74 C ANISOU 1977 CB ARG D 253 6022 5503 3574 -39 425 1090 C ATOM 1978 CG ARG A 253 86.391 31.338 39.176 1.00 54.89 C ANISOU 1978 CG ARG D 253 9916 5416 5523 -414 1567 1488 C ATOM 1979 CD ARG A 253 86.652 32.390 38.112 1.00 78.02 C ANISOU 1979 CD ARG D 253 15665 7538 6442 -2471 1999 2875 C ATOM 1980 NE ARG A 253 87.715 31.921 37.211 1.00 91.76 N ANISOU 1980 NE ARG D 253 18216 8596 8054 -2693 518 4537 N ATOM 1981 CZ ARG A 253 88.947 32.385 37.120 1.00 97.65 C ANISOU 1981 CZ ARG D 253 19916 8465 8723 -3233 -1149 4968 C ATOM 1982 NH1 ARG A 253 89.372 33.400 37.861 1.00111.61 N ANISOU 1982 NH1 ARG D 253 22556 9699 10151 -3763 -1219 3091 N ATOM 1983 NH2 ARG A 253 89.783 31.825 36.243 1.00109.51 N ANISOU 1983 NH2 ARG D 253 21238 10420 9950 -2615 -1744 6339 N ATOM 1984 N TYR A 254 83.924 31.509 42.019 1.00 37.12 N ANISOU 1984 N TYR D 254 6131 4846 3126 -1609 379 1414 N ATOM 1985 CA TYR A 254 83.967 32.301 43.241 1.00 35.87 C ANISOU 1985 CA TYR D 254 5615 4834 3181 -1309 945 472 C ATOM 1986 C TYR A 254 84.132 31.451 44.501 1.00 37.91 C ANISOU 1986 C TYR D 254 6403 4597 3404 -1551 1324 326 C ATOM 1987 O TYR A 254 84.968 31.699 45.394 1.00 40.95 O ANISOU 1987 O TYR D 254 6914 4843 3804 -1788 1812 35 O ATOM 1988 CB TYR A 254 82.685 33.137 43.361 1.00 36.39 C ANISOU 1988 CB TYR D 254 5681 4772 3376 -1304 537 241 C ATOM 1989 CG TYR A 254 82.543 33.835 44.706 1.00 38.96 C ANISOU 1989 CG TYR D 254 6344 4956 3504 -1260 251 145 C ATOM 1990 CD1 TYR A 254 83.341 34.936 45.022 1.00 39.58 C ANISOU 1990 CD1 TYR D 254 6319 5114 3605 -1409 243 101 C ATOM 1991 CD2 TYR A 254 81.616 33.412 45.661 1.00 38.99 C ANISOU 1991 CD2 TYR D 254 6008 5015 3791 -1020 -21 264 C ATOM 1992 CE1 TYR A 254 83.227 35.591 46.240 1.00 39.41 C ANISOU 1992 CE1 TYR D 254 5976 4999 3999 -1329 -150 339 C ATOM 1993 CE2 TYR A 254 81.491 34.056 46.881 1.00 38.40 C ANISOU 1993 CE2 TYR D 254 5911 4858 3822 -1107 9 202 C ATOM 1994 CZ TYR A 254 82.298 35.143 47.164 1.00 40.32 C ANISOU 1994 CZ TYR D 254 6003 4892 4425 -1207 -391 446 C ATOM 1995 OH TYR A 254 82.196 35.802 48.364 1.00 45.13 O ANISOU 1995 OH TYR D 254 8431 4773 3942 -2493 -374 763 O ATOM 1996 N PHE A 255 83.288 30.407 44.596 1.00 35.08 N ANISOU 1996 N PHE D 255 5750 4409 3169 -1228 493 761 N ATOM 1997 CA PHE A 255 83.351 29.576 45.795 1.00 35.31 C ANISOU 1997 CA PHE D 255 6118 3955 3345 -899 881 713 C ATOM 1998 C PHE A 255 84.573 28.669 45.751 1.00 37.20 C ANISOU 1998 C PHE D 255 6690 3719 3723 -226 1206 146 C ATOM 1999 O PHE A 255 85.123 28.321 46.800 1.00 43.90 O ANISOU 1999 O PHE D 255 7467 5107 4107 -410 1880 93 O ATOM 2000 CB PHE A 255 82.081 28.729 45.940 1.00 30.76 C ANISOU 2000 CB PHE D 255 5648 3871 2168 -513 606 429 C ATOM 2001 CG PHE A 255 80.893 29.586 46.352 1.00 32.15 C ANISOU 2001 CG PHE D 255 5329 4350 2537 -747 575 341 C ATOM 2002 CD1 PHE A 255 80.801 30.048 47.658 1.00 32.72 C ANISOU 2002 CD1 PHE D 255 5091 4551 2790 -971 383 146 C ATOM 2003 CD2 PHE A 255 79.890 29.923 45.462 1.00 33.72 C ANISOU 2003 CD2 PHE D 255 5637 4575 2600 -310 721 593 C ATOM 2004 CE1 PHE A 255 79.728 30.837 48.066 1.00 33.26 C ANISOU 2004 CE1 PHE D 255 5722 4267 2648 -363 397 298 C ATOM 2005 CE2 PHE A 255 78.820 30.705 45.857 1.00 33.15 C ANISOU 2005 CE2 PHE D 255 5674 4244 2679 -442 398 229 C ATOM 2006 CZ PHE A 255 78.719 31.161 47.163 1.00 33.28 C ANISOU 2006 CZ PHE D 255 5897 4050 2699 -507 396 102 C ATOM 2007 N ASN A 256 84.989 28.278 44.549 1.00 37.09 N ANISOU 2007 N ASN D 256 6241 3836 4015 42 1174 699 N ATOM 2008 CA ASN A 256 86.173 27.440 44.424 1.00 42.58 C ANISOU 2008 CA ASN D 256 6272 5204 4702 471 1442 342 C ATOM 2009 C ASN A 256 87.397 28.226 44.875 1.00 43.82 C ANISOU 2009 C ASN D 256 5694 5102 5854 798 1520 286 C ATOM 2010 O ASN A 256 88.309 27.589 45.407 1.00 49.55 O ANISOU 2010 O ASN D 256 5990 5059 7777 1151 2251 909 O ATOM 2011 CB ASN A 256 86.411 26.915 43.009 1.00 45.84 C ANISOU 2011 CB ASN D 256 7020 5227 5172 1072 563 854 C ATOM 2012 CG ASN A 256 85.873 25.501 42.865 1.00 51.15 C ANISOU 2012 CG ASN D 256 7453 6339 5643 319 -365 978 C ATOM 2013 OD1 ASN A 256 86.401 24.521 43.408 1.00 63.15 O ANISOU 2013 OD1 ASN D 256 7543 8146 8305 -609 370 -352 O ATOM 2014 ND2 ASN A 256 84.775 25.389 42.137 1.00 59.01 N ANISOU 2014 ND2 ASN D 256 10319 7443 4660 -2024 1467 -407 N ATOM 2015 N GLU A 257 87.388 29.547 44.674 1.00 43.26 N ANISOU 2015 N GLU D 257 6315 5509 4613 250 2117 -95 N ATOM 2016 CA GLU A 257 88.542 30.311 45.157 1.00 46.91 C ANISOU 2016 CA GLU D 257 6788 5798 5238 -98 2812 -601 C ATOM 2017 C GLU A 257 88.417 30.617 46.641 1.00 49.57 C ANISOU 2017 C GLU D 257 8194 5336 5303 -921 2507 -405 C ATOM 2018 O GLU A 257 89.353 30.505 47.445 1.00 49.09 O ANISOU 2018 O GLU D 257 8394 5604 4654 -481 2513 81 O ATOM 2019 CB GLU A 257 88.694 31.561 44.274 1.00 57.48 C ANISOU 2019 CB GLU D 257 9569 6628 5642 -1616 3645 -717 C ATOM 2020 CG GLU A 257 88.898 31.160 42.804 1.00 69.57 C ANISOU 2020 CG GLU D 257 11906 8594 5933 -2785 2731 806 C ATOM 2021 CD GLU A 257 89.080 32.336 41.873 1.00 79.02 C ANISOU 2021 CD GLU D 257 13844 9722 6456 -4129 2561 1566 C ATOM 2022 OE1 GLU A 257 88.762 33.468 42.312 1.00 96.05 O ANISOU 2022 OE1 GLU D 257 16292 11402 8801 -8311 1429 2019 O ATOM 2023 OE2 GLU A 257 89.542 32.171 40.714 1.00 89.60 O ANISOU 2023 OE2 GLU D 257 17551 9594 6899 -4298 1870 2295 O ATOM 2024 N LEU A 258 87.235 31.017 47.098 1.00 47.38 N ANISOU 2024 N LEU D 258 8517 4891 4593 -940 2611 -410 N ATOM 2025 CA LEU A 258 87.039 31.331 48.499 1.00 50.87 C ANISOU 2025 CA LEU D 258 9305 5186 4839 -1285 2010 -881 C ATOM 2026 C LEU A 258 87.280 30.154 49.434 1.00 50.46 C ANISOU 2026 C LEU D 258 9888 5220 4064 -1167 1960 -398 C ATOM 2027 O LEU A 258 87.570 30.312 50.624 1.00 56.43 O ANISOU 2027 O LEU D 258 11745 5327 4367 -475 2277 -1063 O ATOM 2028 CB LEU A 258 85.598 31.845 48.643 1.00 51.82 C ANISOU 2028 CB LEU D 258 9073 5350 5265 -1419 867 -1596 C ATOM 2029 CG LEU A 258 85.170 32.261 50.053 1.00 55.99 C ANISOU 2029 CG LEU D 258 10130 5524 5618 -1907 118 -1687 C ATOM 2030 CD1 LEU A 258 85.943 33.502 50.471 1.00 64.99 C ANISOU 2030 CD1 LEU D 258 12598 5423 6671 -2252 -809 -1670 C ATOM 2031 CD2 LEU A 258 83.673 32.524 50.137 1.00 50.86 C ANISOU 2031 CD2 LEU D 258 8474 5253 5598 -2781 244 -1079 C ATOM 2032 N GLU A 259 87.160 28.908 48.972 1.00 46.86 N ANISOU 2032 N GLU D 259 8842 4555 4407 -487 1357 1040 N ATOM 2033 CA GLU A 259 87.184 27.797 49.931 1.00 45.60 C ANISOU 2033 CA GLU D 259 8904 4446 3977 14 1545 864 C ATOM 2034 C GLU A 259 88.368 26.895 49.633 1.00 49.17 C ANISOU 2034 C GLU D 259 8743 5471 4468 -133 1080 653 C ATOM 2035 O GLU A 259 88.521 25.801 50.181 1.00 48.07 O ANISOU 2035 O GLU D 259 8710 5793 3760 -122 724 1091 O ATOM 2036 CB GLU A 259 85.832 27.065 49.860 1.00 46.80 C ANISOU 2036 CB GLU D 259 8304 4519 4958 -451 4472 -385 C ATOM 2037 CG GLU A 259 85.354 26.593 51.241 1.00 57.76 C ANISOU 2037 CG GLU D 259 11515 4176 6255 -917 2905 1180 C ATOM 2038 CD GLU A 259 84.491 27.625 51.934 1.00 55.12 C ANISOU 2038 CD GLU D 259 11185 3572 6186 -78 3406 341 C ATOM 2039 OE1 GLU A 259 84.834 28.048 53.035 1.00 65.96 O ANISOU 2039 OE1 GLU D 259 14529 6178 4355 450 2391 1987 O ATOM 2040 OE2 GLU A 259 83.480 28.092 51.384 1.00 69.79 O ANISOU 2040 OE2 GLU D 259 9600 4789 12129 -2508 6009 -1473 O ATOM 2041 N ALA A 260 89.228 27.374 48.715 1.00 44.52 N ANISOU 2041 N ALA D 260 7647 4863 4406 659 1995 297 N ATOM 2042 CA ALA A 260 90.346 26.561 48.255 1.00 46.86 C ANISOU 2042 CA ALA D 260 7440 5203 5160 694 2246 501 C ATOM 2043 C ALA A 260 91.190 25.968 49.378 1.00 49.08 C ANISOU 2043 C ALA D 260 7882 5158 5608 701 2566 260 C ATOM 2044 O ALA A 260 91.584 24.804 49.343 1.00 49.48 O ANISOU 2044 O ALA D 260 7474 4853 6474 1891 2292 -515 O ATOM 2045 CB ALA A 260 91.261 27.379 47.344 1.00 45.90 C ANISOU 2045 CB ALA D 260 7330 5013 5096 694 1846 434 C ATOM 2046 N GLU A 261 91.482 26.773 50.386 1.00 49.76 N ANISOU 2046 N GLU D 261 8015 5128 5762 1212 2289 43 N ATOM 2047 CA GLU A 261 92.398 26.329 51.439 1.00 58.83 C ANISOU 2047 CA GLU D 261 10236 5801 6317 766 3757 -241 C ATOM 2048 C GLU A 261 91.747 25.232 52.275 1.00 57.24 C ANISOU 2048 C GLU D 261 9715 5717 6317 1168 3269 162 C ATOM 2049 O GLU A 261 92.401 24.405 52.910 1.00 52.72 O ANISOU 2049 O GLU D 261 9668 4880 5484 1062 2959 9 O ATOM 2050 CB GLU A 261 92.804 27.503 52.324 1.00 65.59 C ANISOU 2050 CB GLU D 261 11761 5403 7757 725 3823 -1336 C ATOM 2051 CG GLU A 261 94.197 28.062 52.165 1.00 78.63 C ANISOU 2051 CG GLU D 261 14955 5645 9274 230 1777 93 C ATOM 2052 CD GLU A 261 95.183 27.322 51.281 1.00 90.73 C ANISOU 2052 CD GLU D 261 17714 6934 9826 -99 89 1602 C ATOM 2053 OE1 GLU A 261 95.962 26.466 51.771 1.00 93.00 O ANISOU 2053 OE1 GLU D 261 17444 7105 10786 2597 -995 2857 O ATOM 2054 OE2 GLU A 261 95.211 27.601 50.055 1.00105.06 O ANISOU 2054 OE2 GLU D 261 22097 7991 9831 -725 257 1875 O ATOM 2055 N ASN A 262 90.415 25.282 52.237 1.00 55.39 N ANISOU 2055 N ASN D 262 8542 6013 6493 1073 2350 -29 N ATOM 2056 CA ASN A 262 89.595 24.416 53.068 1.00 49.60 C ANISOU 2056 CA ASN D 262 7153 5570 6124 1345 2237 -416 C ATOM 2057 C ASN A 262 89.237 23.113 52.385 1.00 51.02 C ANISOU 2057 C ASN D 262 6661 6390 6334 1264 2201 -590 C ATOM 2058 O ASN A 262 88.557 22.277 52.986 1.00 50.52 O ANISOU 2058 O ASN D 262 5771 7727 5697 206 2684 -634 O ATOM 2059 CB ASN A 262 88.280 25.126 53.446 1.00 44.56 C ANISOU 2059 CB ASN D 262 6658 5448 4826 1299 2615 -1416 C ATOM 2060 CG ASN A 262 88.537 26.439 54.157 1.00 50.37 C ANISOU 2060 CG ASN D 262 7736 5882 5522 772 1870 -1257 C ATOM 2061 OD1 ASN A 262 89.344 26.481 55.084 1.00 60.86 O ANISOU 2061 OD1 ASN D 262 7865 6632 8626 255 2311 -3505 O ATOM 2062 ND2 ASN A 262 87.884 27.515 53.757 1.00 53.11 N ANISOU 2062 ND2 ASN D 262 7280 5719 7181 968 1356 -2464 N ATOM 2063 N ILE A 263 89.639 22.911 51.130 1.00 54.88 N ANISOU 2063 N ILE D 263 7854 6657 6339 921 1957 -511 N ATOM 2064 CA ILE A 263 89.153 21.636 50.576 1.00 58.84 C ANISOU 2064 CA ILE D 263 9072 7101 6182 199 1693 -315 C ATOM 2065 C ILE A 263 90.332 20.737 50.265 1.00 61.53 C ANISOU 2065 C ILE D 263 8805 8054 6522 -134 1228 -518 C ATOM 2066 O ILE A 263 90.266 19.786 49.494 1.00 73.30 O ANISOU 2066 O ILE D 263 11969 8937 6945 -1392 -1345 1505 O ATOM 2067 CB ILE A 263 88.289 21.883 49.345 1.00 60.11 C ANISOU 2067 CB ILE D 263 9075 7875 5889 -323 1516 -647 C ATOM 2068 CG1 ILE A 263 89.015 22.673 48.256 1.00 60.97 C ANISOU 2068 CG1 ILE D 263 8141 8593 6432 -189 1709 -123 C ATOM 2069 CG2 ILE A 263 87.008 22.613 49.702 1.00 53.81 C ANISOU 2069 CG2 ILE D 263 7700 7705 5041 -1213 2539 -212 C ATOM 2070 CD1 ILE A 263 88.162 23.866 47.854 1.00 73.31 C ANISOU 2070 CD1 ILE D 263 6995 13184 7674 -2081 804 -698 C ATOM 2071 N LYS A 264 91.457 21.049 50.900 1.00 68.81 N ANISOU 2071 N LYS D 264 9647 7885 8611 823 2206 -294 N ATOM 2072 CA LYS A 264 92.620 20.167 50.787 1.00 76.55 C ANISOU 2072 CA LYS D 264 9629 8575 10881 860 1904 544 C ATOM 2073 C LYS A 264 92.621 19.101 51.878 1.00 77.52 C ANISOU 2073 C LYS D 264 8825 8920 11709 1188 1942 1056 C ATOM 2074 O LYS A 264 92.222 19.296 53.024 1.00 75.36 O ANISOU 2074 O LYS D 264 8680 8512 11443 798 2272 1025 O ATOM 2075 CB LYS A 264 93.905 21.000 50.827 1.00 76.51 C ANISOU 2075 CB LYS D 264 8786 8559 11725 1096 2521 342 C ATOM 2076 CG LYS A 264 93.789 22.372 50.176 1.00 80.69 C ANISOU 2076 CG LYS D 264 9279 9173 12207 413 2836 -39 C ATOM 2077 CD LYS A 264 95.016 23.223 50.476 1.00 78.42 C ANISOU 2077 CD LYS D 264 8394 9101 12301 798 3041 -22 C ATOM 2078 CE LYS A 264 95.450 23.981 49.230 1.00 78.43 C ANISOU 2078 CE LYS D 264 8762 8938 12101 682 3169 -309 C ATOM 2079 NZ LYS A 264 94.295 24.255 48.330 1.00 84.34 N ANISOU 2079 NZ LYS D 264 9861 10332 11853 -92 2924 -2156 N ATOM 2080 N GLY A 265 93.089 17.905 51.522 1.00 83.82 N ANISOU 2080 N GLY D 265 9209 9687 12953 641 1313 1474 N ATOM 2081 CA GLY A 265 93.178 16.823 52.493 1.00 83.43 C ANISOU 2081 CA GLY D 265 8380 9797 13523 1086 1098 2205 C ATOM 2082 C GLY A 265 91.832 16.123 52.620 1.00 87.07 C ANISOU 2082 C GLY D 265 9740 9860 13482 955 155 2653 C ATOM 2083 O GLY A 265 91.746 14.907 52.439 1.00 86.51 O ANISOU 2083 O GLY D 265 9490 9550 13831 1140 650 2459 O ATOM 2084 N LEU A 266 90.828 16.938 52.923 1.00 87.12 N ANISOU 2084 N LEU D 266 10153 9542 13408 970 -584 2410 N ATOM 2085 CA LEU A 266 89.446 16.498 53.072 1.00 89.29 C ANISOU 2085 CA LEU D 266 11062 9587 13277 985 -987 2797 C ATOM 2086 C LEU A 266 89.197 15.849 54.427 1.00 94.29 C ANISOU 2086 C LEU D 266 12132 10436 13258 560 -957 2916 C ATOM 2087 O LEU A 266 89.825 14.906 54.901 1.00101.99 O ANISOU 2087 O LEU D 266 13306 11900 13546 462 432 1647 O ATOM 2088 CB LEU A 266 89.076 15.556 51.923 1.00 91.54 C ANISOU 2088 CB LEU D 266 12387 9172 13221 91 -931 3141 C ATOM 2089 CG LEU A 266 88.800 16.202 50.566 1.00 90.13 C ANISOU 2089 CG LEU D 266 12137 8943 13166 180 -1012 3032 C ATOM 2090 CD1 LEU A 266 88.043 17.501 50.748 1.00 80.49 C ANISOU 2090 CD1 LEU D 266 12358 8433 9792 236 -1914 3047 C ATOM 2091 CD2 LEU A 266 90.089 16.442 49.794 1.00 86.96 C ANISOU 2091 CD2 LEU D 266 10986 9425 12628 351 -1463 2828 C ATOM 2092 OXT LEU A 266 88.150 17.004 54.270 1.00 99.16 O ANISOU 2092 OXT LEU D 266 11642 11558 14475 367 -2546 3302 O TER 2093 LEU D 266 ATOM 1 N MET A 1 52.790 27.524 53.899 1.00 38.92 N ANISOU 1 N MET E 1 5098 6097 3592 -1489 447 362 N ATOM 2 CA MET A 1 51.659 28.339 53.476 1.00 39.64 C ANISOU 2 CA MET E 1 4671 6407 3983 -879 140 -405 C ATOM 3 C MET A 1 50.633 27.410 52.843 1.00 37.92 C ANISOU 3 C MET E 1 4914 5679 3813 -933 633 -168 C ATOM 4 O MET A 1 51.037 26.473 52.128 1.00 46.58 O ANISOU 4 O MET E 1 5309 7754 4636 -2033 -63 1256 O ATOM 5 CB MET A 1 52.057 29.419 52.463 1.00 40.12 C ANISOU 5 CB MET E 1 4934 6308 4004 -354 -109 -293 C ATOM 6 CG MET A 1 50.821 30.097 51.877 1.00 43.45 C ANISOU 6 CG MET E 1 5363 6642 4505 -613 -169 -839 C ATOM 7 SD MET A 1 51.216 31.308 50.575 1.00 40.76 S ANISOU 7 SD MET E 1 5716 5321 4449 -844 351 -81 S ATOM 8 CE MET A 1 51.940 32.560 51.688 1.00 40.89 C ANISOU 8 CE MET E 1 5132 5850 4556 -1337 -1383 -497 C ATOM 9 N ARG A 2 49.357 27.649 53.094 1.00 32.45 N ANISOU 9 N ARG E 2 4810 4307 3211 -795 419 -513 N ATOM 10 CA ARG A 2 48.338 26.836 52.429 1.00 31.91 C ANISOU 10 CA ARG E 2 5037 4272 2817 -1111 367 -36 C ATOM 11 C ARG A 2 47.676 27.706 51.367 1.00 31.66 C ANISOU 11 C ARG E 2 4806 4445 2778 -1169 640 -178 C ATOM 12 O ARG A 2 47.542 28.914 51.537 1.00 35.19 O ANISOU 12 O ARG E 2 5848 4297 3224 -928 50 -345 O ATOM 13 CB ARG A 2 47.330 26.287 53.431 1.00 30.78 C ANISOU 13 CB ARG E 2 5683 3264 2747 -322 224 278 C ATOM 14 CG ARG A 2 47.913 25.410 54.533 1.00 31.74 C ANISOU 14 CG ARG E 2 6052 3464 2546 -297 -63 449 C ATOM 15 CD ARG A 2 46.851 25.063 55.575 1.00 34.98 C ANISOU 15 CD ARG E 2 6719 3922 2652 -266 253 153 C ATOM 16 NE ARG A 2 45.807 24.227 54.972 1.00 34.41 N ANISOU 16 NE ARG E 2 6379 4594 2103 -53 429 -191 N ATOM 17 CZ ARG A 2 44.631 23.971 55.509 1.00 36.03 C ANISOU 17 CZ ARG E 2 5807 4903 2981 -919 503 344 C ATOM 18 NH1 ARG A 2 44.353 24.498 56.683 1.00 40.91 N ANISOU 18 NH1 ARG E 2 6260 5762 3522 -1418 799 915 N ATOM 19 NH2 ARG A 2 43.725 23.206 54.914 1.00 34.88 N ANISOU 19 NH2 ARG E 2 5784 4351 3119 -751 335 -382 N ATOM 20 N LEU A 3 47.288 27.089 50.259 1.00 31.74 N ANISOU 20 N LEU E 3 4926 4478 2657 -969 591 -365 N ATOM 21 CA LEU A 3 46.463 27.752 49.260 1.00 30.10 C ANISOU 21 CA LEU E 3 4287 4342 2806 -471 790 -760 C ATOM 22 C LEU A 3 45.181 26.917 49.137 1.00 29.83 C ANISOU 22 C LEU E 3 4583 3777 2975 -455 909 -446 C ATOM 23 O LEU A 3 45.318 25.730 48.837 1.00 32.73 O ANISOU 23 O LEU E 3 5431 3887 3119 -772 569 -246 O ATOM 24 CB LEU A 3 47.154 27.897 47.908 1.00 28.39 C ANISOU 24 CB LEU E 3 3943 4351 2491 -526 530 -177 C ATOM 25 CG LEU A 3 46.342 28.476 46.741 1.00 30.84 C ANISOU 25 CG LEU E 3 4457 4660 2600 -868 475 -330 C ATOM 26 CD1 LEU A 3 45.922 29.901 47.023 1.00 32.59 C ANISOU 26 CD1 LEU E 3 4263 4270 3850 -374 15 -436 C ATOM 27 CD2 LEU A 3 47.142 28.460 45.449 1.00 31.39 C ANISOU 27 CD2 LEU E 3 3956 5259 2710 -90 417 -825 C ATOM 28 N ILE A 4 44.035 27.531 49.391 1.00 29.63 N ANISOU 28 N ILE E 4 4344 3841 3072 -259 982 -342 N ATOM 29 CA ILE A 4 42.762 26.828 49.260 1.00 29.55 C ANISOU 29 CA ILE E 4 4606 3487 3133 -143 936 162 C ATOM 30 C ILE A 4 42.104 27.299 47.972 1.00 30.18 C ANISOU 30 C ILE E 4 4166 4260 3043 -442 1143 178 C ATOM 31 O ILE A 4 41.541 28.408 47.902 1.00 32.25 O ANISOU 31 O ILE E 4 4551 4378 3323 -649 453 454 O ATOM 32 CB ILE A 4 41.819 27.079 50.444 1.00 27.05 C ANISOU 32 CB ILE E 4 3924 3415 2937 -176 550 63 C ATOM 33 CG1 ILE A 4 42.480 27.038 51.823 1.00 29.47 C ANISOU 33 CG1 ILE E 4 4697 3441 3059 -175 216 596 C ATOM 34 CG2 ILE A 4 40.620 26.122 50.382 1.00 27.89 C ANISOU 34 CG2 ILE E 4 4136 3481 2980 -8 132 -560 C ATOM 35 CD1 ILE A 4 43.240 25.774 52.149 1.00 33.52 C ANISOU 35 CD1 ILE E 4 5050 4991 2694 -1287 715 -196 C ATOM 36 N PRO A 5 42.197 26.522 46.906 1.00 32.38 N ANISOU 36 N PRO E 5 4856 4317 3131 -679 830 285 N ATOM 37 CA PRO A 5 41.674 26.971 45.610 1.00 30.96 C ANISOU 37 CA PRO E 5 4547 3924 3290 -305 590 340 C ATOM 38 C PRO A 5 40.206 26.581 45.485 1.00 32.73 C ANISOU 38 C PRO E 5 4676 3912 3847 7 682 -203 C ATOM 39 O PRO A 5 39.891 25.393 45.333 1.00 41.35 O ANISOU 39 O PRO E 5 5900 4187 5623 717 832 -29 O ATOM 40 CB PRO A 5 42.530 26.216 44.601 1.00 31.19 C ANISOU 40 CB PRO E 5 4759 4059 3031 -415 332 559 C ATOM 41 CG PRO A 5 43.416 25.315 45.388 1.00 36.93 C ANISOU 41 CG PRO E 5 6032 5134 2865 -1639 480 549 C ATOM 42 CD PRO A 5 42.803 25.194 46.761 1.00 33.62 C ANISOU 42 CD PRO E 5 5289 4328 3157 -800 506 366 C ATOM 43 N LEU A 6 39.346 27.589 45.563 1.00 33.33 N ANISOU 43 N LEU E 6 4570 4819 3274 -481 776 -193 N ATOM 44 CA LEU A 6 37.925 27.362 45.389 1.00 33.33 C ANISOU 44 CA LEU E 6 4731 4654 3278 -246 525 613 C ATOM 45 C LEU A 6 37.418 28.041 44.126 1.00 31.09 C ANISOU 45 C LEU E 6 4147 4368 3297 279 673 476 C ATOM 46 O LEU A 6 38.086 28.759 43.402 1.00 32.27 O ANISOU 46 O LEU E 6 4119 4542 3601 99 1150 523 O ATOM 47 CB LEU A 6 37.176 27.852 46.651 1.00 30.93 C ANISOU 47 CB LEU E 6 3860 4785 3106 349 44 1093 C ATOM 48 CG LEU A 6 37.604 27.094 47.917 1.00 32.11 C ANISOU 48 CG LEU E 6 4765 4312 3124 71 328 1115 C ATOM 49 CD1 LEU A 6 37.173 27.831 49.177 1.00 35.25 C ANISOU 49 CD1 LEU E 6 5001 5247 3147 -439 1216 761 C ATOM 50 CD2 LEU A 6 37.083 25.659 47.911 1.00 35.77 C ANISOU 50 CD2 LEU E 6 4293 4843 4453 743 779 713 C ATOM 51 N THR A 7 36.130 27.815 43.828 1.00 31.68 N ANISOU 51 N THR E 7 4224 4112 3701 321 509 420 N ATOM 52 CA THR A 7 35.555 28.361 42.609 1.00 33.08 C ANISOU 52 CA THR E 7 4689 4514 3367 118 295 845 C ATOM 53 C THR A 7 34.936 29.731 42.806 1.00 31.24 C ANISOU 53 C THR E 7 3910 4252 3706 464 192 409 C ATOM 54 O THR A 7 35.346 30.641 42.081 1.00 35.37 O ANISOU 54 O THR E 7 6266 4839 2335 243 238 189 O ATOM 55 CB THR A 7 34.486 27.399 42.055 1.00 35.77 C ANISOU 55 CB THR E 7 5099 4124 4366 201 -284 440 C ATOM 56 OG1 THR A 7 35.066 26.092 41.999 1.00 47.75 O ANISOU 56 OG1 THR E 7 8771 4110 5264 -541 -867 1016 O ATOM 57 CG2 THR A 7 34.107 27.792 40.634 1.00 37.28 C ANISOU 57 CG2 THR E 7 4307 5762 4097 -525 -261 1003 C ATOM 58 N THR A 8 33.990 29.876 43.735 1.00 30.84 N ANISOU 58 N THR E 8 4104 4019 3596 438 215 699 N ATOM 59 CA THR A 8 33.230 31.109 43.872 1.00 31.16 C ANISOU 59 CA THR E 8 4406 3978 3457 355 94 571 C ATOM 60 C THR A 8 33.526 31.797 45.212 1.00 30.18 C ANISOU 60 C THR E 8 4125 4102 3240 241 452 507 C ATOM 61 O THR A 8 34.044 31.214 46.155 1.00 31.39 O ANISOU 61 O THR E 8 4238 4017 3672 414 -241 687 O ATOM 62 CB THR A 8 31.717 30.857 43.802 1.00 35.03 C ANISOU 62 CB THR E 8 4296 4909 4104 3 -51 1001 C ATOM 63 OG1 THR A 8 31.381 30.102 44.990 1.00 34.44 O ANISOU 63 OG1 THR E 8 4112 4849 4124 424 677 1479 O ATOM 64 CG2 THR A 8 31.301 29.996 42.617 1.00 37.97 C ANISOU 64 CG2 THR E 8 4096 6196 4135 368 -39 1312 C ATOM 65 N ALA A 9 33.171 33.084 45.245 1.00 32.06 N ANISOU 65 N ALA E 9 4160 4378 3641 -281 174 869 N ATOM 66 CA ALA A 9 33.227 33.861 46.471 1.00 31.04 C ANISOU 66 CA ALA E 9 4421 4042 3330 54 124 490 C ATOM 67 C ALA A 9 32.403 33.204 47.574 1.00 32.92 C ANISOU 67 C ALA E 9 3707 5331 3470 167 -40 180 C ATOM 68 O ALA A 9 32.788 33.213 48.748 1.00 32.03 O ANISOU 68 O ALA E 9 3626 5124 3421 -138 -7 107 O ATOM 69 CB ALA A 9 32.736 35.275 46.207 1.00 30.59 C ANISOU 69 CB ALA E 9 3188 4023 4410 94 -250 811 C ATOM 70 N GLU A 10 31.243 32.627 47.229 1.00 33.85 N ANISOU 70 N GLU E 10 3775 5271 3814 125 16 681 N ATOM 71 CA GLU A 10 30.430 32.055 48.302 1.00 39.43 C ANISOU 71 CA GLU E 10 3560 5969 5451 -195 889 8 C ATOM 72 C GLU A 10 31.179 30.876 48.914 1.00 37.01 C ANISOU 72 C GLU E 10 4141 5260 4661 -46 1227 292 C ATOM 73 O GLU A 10 31.141 30.736 50.136 1.00 32.98 O ANISOU 73 O GLU E 10 3149 4745 4635 151 1622 525 O ATOM 74 CB GLU A 10 29.061 31.568 47.871 1.00 42.67 C ANISOU 74 CB GLU E 10 4032 6783 5397 396 705 329 C ATOM 75 CG GLU A 10 28.718 31.594 46.412 1.00 55.83 C ANISOU 75 CG GLU E 10 6703 8353 6159 -877 -1108 26 C ATOM 76 CD GLU A 10 28.635 32.956 45.757 1.00 68.33 C ANISOU 76 CD GLU E 10 9689 9367 6907 -3509 778 -1069 C ATOM 77 OE1 GLU A 10 29.354 33.133 44.748 1.00 57.50 O ANISOU 77 OE1 GLU E 10 7455 8986 5406 -2363 -1163 -518 O ATOM 78 OE2 GLU A 10 27.860 33.817 46.241 1.00 89.46 O ANISOU 78 OE2 GLU E 10 12970 11278 9744 -5873 3114 -2031 O ATOM 79 N GLN A 11 31.827 30.074 48.077 1.00 33.27 N ANISOU 79 N GLN E 11 4292 4510 3841 620 787 482 N ATOM 80 CA GLN A 11 32.609 28.997 48.658 1.00 33.41 C ANISOU 80 CA GLN E 11 4958 4221 3514 370 560 1011 C ATOM 81 C GLN A 11 33.771 29.552 49.479 1.00 32.06 C ANISOU 81 C GLN E 11 5269 3696 3218 185 402 974 C ATOM 82 O GLN A 11 34.134 29.018 50.533 1.00 32.12 O ANISOU 82 O GLN E 11 4172 4714 3319 -288 990 514 O ATOM 83 CB GLN A 11 33.224 28.088 47.596 1.00 34.19 C ANISOU 83 CB GLN E 11 5234 4412 3344 568 454 1209 C ATOM 84 CG GLN A 11 32.291 27.143 46.864 1.00 37.54 C ANISOU 84 CG GLN E 11 5259 4933 4070 883 549 1570 C ATOM 85 CD GLN A 11 33.039 26.477 45.718 1.00 38.16 C ANISOU 85 CD GLN E 11 6373 4487 3639 963 681 1402 C ATOM 86 OE1 GLN A 11 33.558 27.171 44.850 1.00 42.48 O ANISOU 86 OE1 GLN E 11 6455 5597 4087 -229 922 138 O ATOM 87 NE2 GLN A 11 33.127 25.165 45.698 1.00 52.12 N ANISOU 87 NE2 GLN E 11 9658 4581 5564 324 2102 1353 N ATOM 88 N VAL A 12 34.411 30.612 48.997 1.00 32.02 N ANISOU 88 N VAL E 12 4669 3928 3568 125 474 777 N ATOM 89 CA VAL A 12 35.520 31.147 49.805 1.00 30.86 C ANISOU 89 CA VAL E 12 4315 4473 2937 105 733 602 C ATOM 90 C VAL A 12 35.030 31.589 51.172 1.00 31.72 C ANISOU 90 C VAL E 12 4118 4969 2964 -299 730 513 C ATOM 91 O VAL A 12 35.634 31.303 52.232 1.00 33.07 O ANISOU 91 O VAL E 12 5054 4690 2820 -1018 1080 -72 O ATOM 92 CB VAL A 12 36.175 32.320 49.063 1.00 30.93 C ANISOU 92 CB VAL E 12 4292 4529 2930 249 606 644 C ATOM 93 CG1 VAL A 12 37.075 33.154 49.976 1.00 26.77 C ANISOU 93 CG1 VAL E 12 2518 4821 2832 -406 1004 825 C ATOM 94 CG2 VAL A 12 36.954 31.772 47.864 1.00 27.85 C ANISOU 94 CG2 VAL E 12 4346 3318 2917 63 533 331 C ATOM 95 N GLY A 13 33.911 32.322 51.230 1.00 34.20 N ANISOU 95 N GLY E 13 4049 5732 3212 -520 779 305 N ATOM 96 CA GLY A 13 33.415 32.745 52.553 1.00 29.99 C ANISOU 96 CA GLY E 13 3565 4722 3108 -212 638 236 C ATOM 97 C GLY A 13 33.036 31.543 53.397 1.00 32.48 C ANISOU 97 C GLY E 13 4481 4605 3254 -5 535 274 C ATOM 98 O GLY A 13 33.243 31.523 54.617 1.00 29.43 O ANISOU 98 O GLY E 13 3679 4384 3119 -135 1000 386 O ATOM 99 N LYS A 14 32.468 30.477 52.806 1.00 34.10 N ANISOU 99 N LYS E 14 4805 4698 3454 70 236 279 N ATOM 100 CA LYS A 14 32.087 29.367 53.695 1.00 33.19 C ANISOU 100 CA LYS E 14 3933 4702 3977 -10 646 255 C ATOM 101 C LYS A 14 33.315 28.698 54.283 1.00 32.13 C ANISOU 101 C LYS E 14 3945 4509 3753 -74 844 197 C ATOM 102 O LYS A 14 33.340 28.269 55.436 1.00 30.73 O ANISOU 102 O LYS E 14 3695 4154 3826 518 707 190 O ATOM 103 CB LYS A 14 31.209 28.348 52.956 1.00 35.28 C ANISOU 103 CB LYS E 14 3443 5482 4479 324 1177 812 C ATOM 104 CG LYS A 14 29.789 28.881 52.795 1.00 44.78 C ANISOU 104 CG LYS E 14 3870 7448 5695 -306 234 716 C ATOM 105 CD LYS A 14 28.942 28.140 51.782 1.00 51.11 C ANISOU 105 CD LYS E 14 4335 7781 7302 381 -432 799 C ATOM 106 CE LYS A 14 27.474 28.551 51.873 1.00 59.42 C ANISOU 106 CE LYS E 14 4853 9178 8545 -1037 -1909 511 C ATOM 107 NZ LYS A 14 27.052 29.411 50.725 1.00 82.88 N ANISOU 107 NZ LYS E 14 9491 12124 9874 -4405 -260 -1517 N ATOM 108 N TRP A 15 34.357 28.602 53.475 1.00 32.83 N ANISOU 108 N TRP E 15 3964 4686 3826 16 920 319 N ATOM 109 CA TRP A 15 35.583 27.929 53.893 1.00 31.38 C ANISOU 109 CA TRP E 15 3957 4475 3492 36 838 671 C ATOM 110 C TRP A 15 36.234 28.721 55.019 1.00 30.90 C ANISOU 110 C TRP E 15 4466 4001 3273 -274 838 651 C ATOM 111 O TRP A 15 36.618 28.207 56.076 1.00 30.21 O ANISOU 111 O TRP E 15 3919 3861 3699 -145 576 482 O ATOM 112 CB TRP A 15 36.585 27.742 52.717 1.00 32.35 C ANISOU 112 CB TRP E 15 4518 4618 3156 -598 816 601 C ATOM 113 CG TRP A 15 37.644 26.726 53.109 1.00 32.69 C ANISOU 113 CG TRP E 15 4393 4590 3440 -423 1089 0 C ATOM 114 CD1 TRP A 15 37.650 25.395 52.794 1.00 33.69 C ANISOU 114 CD1 TRP E 15 4677 4557 3565 -529 1072 -65 C ATOM 115 CD2 TRP A 15 38.838 26.952 53.885 1.00 33.36 C ANISOU 115 CD2 TRP E 15 4267 4495 3913 -175 1017 -585 C ATOM 116 NE1 TRP A 15 38.764 24.776 53.320 1.00 35.12 N ANISOU 116 NE1 TRP E 15 4626 4609 4109 -443 1009 -286 N ATOM 117 CE2 TRP A 15 39.510 25.710 53.993 1.00 34.81 C ANISOU 117 CE2 TRP E 15 4363 4726 4137 -481 1105 -233 C ATOM 118 CE3 TRP A 15 39.416 28.073 54.499 1.00 29.62 C ANISOU 118 CE3 TRP E 15 3588 4554 3111 -87 1519 -713 C ATOM 119 CZ2 TRP A 15 40.712 25.555 54.684 1.00 32.81 C ANISOU 119 CZ2 TRP E 15 3755 4507 4204 -110 1598 -773 C ATOM 120 CZ3 TRP A 15 40.602 27.922 55.182 1.00 33.75 C ANISOU 120 CZ3 TRP E 15 4283 5014 3525 -980 862 188 C ATOM 121 CH2 TRP A 15 41.240 26.671 55.267 1.00 35.37 C ANISOU 121 CH2 TRP E 15 4813 4770 3856 -814 679 -158 C ATOM 122 N ALA A 16 36.378 30.016 54.754 1.00 30.94 N ANISOU 122 N ALA E 16 4454 4063 3239 -229 793 488 N ATOM 123 CA ALA A 16 36.998 30.912 55.740 1.00 29.29 C ANISOU 123 CA ALA E 16 3856 4129 3145 116 1164 397 C ATOM 124 C ALA A 16 36.213 30.933 57.040 1.00 29.05 C ANISOU 124 C ALA E 16 3699 4539 2798 -316 790 36 C ATOM 125 O ALA A 16 36.718 30.827 58.155 1.00 33.29 O ANISOU 125 O ALA E 16 4768 4944 2935 -1247 418 291 O ATOM 126 CB ALA A 16 37.079 32.300 55.125 1.00 26.10 C ANISOU 126 CB ALA E 16 2751 4510 2657 366 -21 59 C ATOM 127 N ALA A 17 34.889 31.070 56.910 1.00 30.90 N ANISOU 127 N ALA E 17 3685 4787 3270 -548 1021 78 N ATOM 128 CA ALA A 17 34.051 31.074 58.109 1.00 29.58 C ANISOU 128 CA ALA E 17 3656 4664 2920 9 781 291 C ATOM 129 C ALA A 17 34.170 29.741 58.828 1.00 30.77 C ANISOU 129 C ALA E 17 3429 4455 3808 304 1037 159 C ATOM 130 O ALA A 17 34.294 29.697 60.066 1.00 33.56 O ANISOU 130 O ALA E 17 5242 3549 3961 322 391 -19 O ATOM 131 CB ALA A 17 32.619 31.411 57.733 1.00 31.67 C ANISOU 131 CB ALA E 17 3817 5595 2621 -705 945 938 C ATOM 132 N ARG A 18 34.158 28.614 58.136 1.00 33.37 N ANISOU 132 N ARG E 18 4138 4690 3852 -305 976 359 N ATOM 133 CA ARG A 18 34.321 27.327 58.813 1.00 32.76 C ANISOU 133 CA ARG E 18 3847 4462 4140 76 1273 399 C ATOM 134 C ARG A 18 35.684 27.243 59.499 1.00 31.33 C ANISOU 134 C ARG E 18 4125 3797 3982 276 1024 85 C ATOM 135 O ARG A 18 35.784 26.668 60.608 1.00 36.95 O ANISOU 135 O ARG E 18 4887 4509 4643 82 1079 -703 O ATOM 136 CB ARG A 18 34.136 26.186 57.815 1.00 33.91 C ANISOU 136 CB ARG E 18 3988 4728 4170 240 1013 497 C ATOM 137 CG ARG A 18 34.090 24.801 58.452 1.00 37.46 C ANISOU 137 CG ARG E 18 4925 4534 4776 327 1308 593 C ATOM 138 CD ARG A 18 33.832 23.741 57.378 1.00 41.00 C ANISOU 138 CD ARG E 18 5949 4767 4862 140 1220 802 C ATOM 139 NE ARG A 18 34.995 23.589 56.497 1.00 45.31 N ANISOU 139 NE ARG E 18 6946 5829 4442 -324 1671 479 N ATOM 140 CZ ARG A 18 35.150 22.671 55.565 1.00 50.53 C ANISOU 140 CZ ARG E 18 7873 6006 5319 -150 2270 950 C ATOM 141 NH1 ARG A 18 34.192 21.776 55.358 1.00 60.56 N ANISOU 141 NH1 ARG E 18 8888 7188 6934 529 1145 1804 N ATOM 142 NH2 ARG A 18 36.257 22.651 54.841 1.00 58.04 N ANISOU 142 NH2 ARG E 18 9870 5866 6316 -870 4164 -161 N ATOM 143 N HIS A 19 36.734 27.794 58.890 1.00 30.93 N ANISOU 143 N HIS E 19 4001 3875 3875 385 985 358 N ATOM 144 CA HIS A 19 38.077 27.786 59.485 1.00 29.19 C ANISOU 144 CA HIS E 19 4131 3571 3390 299 962 56 C ATOM 145 C HIS A 19 38.064 28.557 60.803 1.00 30.19 C ANISOU 145 C HIS E 19 4403 3642 3426 10 894 90 C ATOM 146 O HIS A 19 38.537 28.141 61.867 1.00 36.06 O ANISOU 146 O HIS E 19 6311 3812 3577 -286 289 203 O ATOM 147 CB HIS A 19 39.117 28.374 58.519 1.00 28.79 C ANISOU 147 CB HIS E 19 4045 3511 3382 510 825 102 C ATOM 148 CG HIS A 19 40.525 28.167 58.979 1.00 30.50 C ANISOU 148 CG HIS E 19 4090 3803 3695 373 813 -201 C ATOM 149 ND1 HIS A 19 41.121 26.935 59.086 1.00 33.56 N ANISOU 149 ND1 HIS E 19 4787 3990 3973 -5 382 44 N ATOM 150 CD2 HIS A 19 41.480 29.052 59.378 1.00 31.72 C ANISOU 150 CD2 HIS E 19 3922 3984 4146 448 549 -610 C ATOM 151 CE1 HIS A 19 42.365 27.049 59.517 1.00 34.20 C ANISOU 151 CE1 HIS E 19 4915 4265 3813 -128 130 -220 C ATOM 152 NE2 HIS A 19 42.607 28.334 59.704 1.00 34.50 N ANISOU 152 NE2 HIS E 19 4320 4316 4472 92 236 -445 N ATOM 153 N ILE A 20 37.478 29.755 60.745 1.00 33.50 N ANISOU 153 N ILE E 20 4840 4222 3665 -726 1231 153 N ATOM 154 CA ILE A 20 37.366 30.603 61.946 1.00 32.34 C ANISOU 154 CA ILE E 20 4869 3846 3575 -275 1542 -52 C ATOM 155 C ILE A 20 36.633 29.836 63.034 1.00 33.02 C ANISOU 155 C ILE E 20 4689 4221 3637 -170 1282 -341 C ATOM 156 O ILE A 20 37.141 29.758 64.156 1.00 35.06 O ANISOU 156 O ILE E 20 5147 4395 3778 -369 1052 -545 O ATOM 157 CB ILE A 20 36.676 31.941 61.614 1.00 31.64 C ANISOU 157 CB ILE E 20 4972 3796 3253 -249 1104 99 C ATOM 158 CG1 ILE A 20 37.493 32.848 60.685 1.00 27.21 C ANISOU 158 CG1 ILE E 20 4083 3578 2679 -480 788 382 C ATOM 159 CG2 ILE A 20 36.297 32.667 62.895 1.00 30.74 C ANISOU 159 CG2 ILE E 20 4222 4101 3356 -234 1397 63 C ATOM 160 CD1 ILE A 20 36.759 34.046 60.124 1.00 27.95 C ANISOU 160 CD1 ILE E 20 3960 3676 2983 -143 98 227 C ATOM 161 N VAL A 21 35.485 29.265 62.699 1.00 33.86 N ANISOU 161 N VAL E 21 4471 4460 3934 -273 1515 -76 N ATOM 162 CA VAL A 21 34.692 28.511 63.670 1.00 34.17 C ANISOU 162 CA VAL E 21 4534 4381 4068 -123 1204 -318 C ATOM 163 C VAL A 21 35.489 27.368 64.290 1.00 36.10 C ANISOU 163 C VAL E 21 5749 4619 3350 -662 814 77 C ATOM 164 O VAL A 21 35.504 27.099 65.498 1.00 37.00 O ANISOU 164 O VAL E 21 6030 4317 3713 -347 2338 -810 O ATOM 165 CB VAL A 21 33.412 27.964 63.000 1.00 37.20 C ANISOU 165 CB VAL E 21 4646 4993 4495 100 1086 -325 C ATOM 166 CG1 VAL A 21 32.768 26.903 63.894 1.00 33.39 C ANISOU 166 CG1 VAL E 21 3606 5524 3557 -231 1759 143 C ATOM 167 CG2 VAL A 21 32.457 29.104 62.675 1.00 37.04 C ANISOU 167 CG2 VAL E 21 4146 5571 4354 -179 1433 -119 C ATOM 168 N ASN A 22 36.204 26.638 63.442 1.00 35.42 N ANISOU 168 N ASN E 22 5578 4810 3072 -833 684 -45 N ATOM 169 CA ASN A 22 36.982 25.515 63.954 1.00 36.23 C ANISOU 169 CA ASN E 22 5802 4366 3596 -598 428 13 C ATOM 170 C ASN A 22 38.124 26.003 64.828 1.00 35.13 C ANISOU 170 C ASN E 22 5692 4331 3324 -622 502 -178 C ATOM 171 O ASN A 22 38.449 25.385 65.846 1.00 37.68 O ANISOU 171 O ASN E 22 5612 5340 3365 -947 734 -548 O ATOM 172 CB ASN A 22 37.465 24.667 62.775 1.00 39.79 C ANISOU 172 CB ASN E 22 6436 4639 4041 -967 142 475 C ATOM 173 CG ASN A 22 36.343 23.912 62.081 1.00 45.83 C ANISOU 173 CG ASN E 22 7258 5374 4783 -947 -662 925 C ATOM 174 OD1 ASN A 22 36.600 23.299 61.045 1.00 54.80 O ANISOU 174 OD1 ASN E 22 8143 7299 5378 -1210 -963 2065 O ATOM 175 ND2 ASN A 22 35.118 23.916 62.591 1.00 45.89 N ANISOU 175 ND2 ASN E 22 7308 5443 4685 354 -589 472 N ATOM 176 N ARG A 23 38.770 27.118 64.496 1.00 35.83 N ANISOU 176 N ARG E 23 5833 4392 3389 -470 976 198 N ATOM 177 CA ARG A 23 39.803 27.607 65.410 1.00 33.81 C ANISOU 177 CA ARG E 23 5251 4775 2818 -351 1334 -299 C ATOM 178 C ARG A 23 39.190 28.020 66.736 1.00 34.96 C ANISOU 178 C ARG E 23 5254 5289 2741 -722 1197 -306 C ATOM 179 O ARG A 23 39.732 27.705 67.794 1.00 36.82 O ANISOU 179 O ARG E 23 5818 5426 2745 -279 1168 -752 O ATOM 180 CB ARG A 23 40.533 28.803 64.797 1.00 35.25 C ANISOU 180 CB ARG E 23 5146 4909 3337 -363 1235 -638 C ATOM 181 CG ARG A 23 41.404 28.311 63.657 1.00 30.89 C ANISOU 181 CG ARG E 23 4207 4471 3060 112 732 -412 C ATOM 182 CD ARG A 23 42.569 27.471 64.202 1.00 38.51 C ANISOU 182 CD ARG E 23 5582 5100 3950 -1057 249 -41 C ATOM 183 NE ARG A 23 43.552 27.351 63.112 1.00 40.05 N ANISOU 183 NE ARG E 23 4953 5583 4681 -1159 237 382 N ATOM 184 CZ ARG A 23 44.263 26.270 62.827 1.00 46.54 C ANISOU 184 CZ ARG E 23 6432 5918 5332 -1957 791 -23 C ATOM 185 NH1 ARG A 23 44.095 25.183 63.585 1.00 45.47 N ANISOU 185 NH1 ARG E 23 6255 5597 5424 -1602 1236 316 N ATOM 186 NH2 ARG A 23 45.115 26.295 61.806 1.00 39.35 N ANISOU 186 NH2 ARG E 23 5844 4406 4700 -1401 167 496 N ATOM 187 N ILE A 24 38.060 28.728 66.677 1.00 36.60 N ANISOU 187 N ILE E 24 5032 5082 3794 -531 1463 -307 N ATOM 188 CA ILE A 24 37.445 29.130 67.936 1.00 36.12 C ANISOU 188 CA ILE E 24 4944 4952 3828 -444 1575 -410 C ATOM 189 C ILE A 24 37.008 27.921 68.746 1.00 37.86 C ANISOU 189 C ILE E 24 5388 5292 3707 -139 1001 -707 C ATOM 190 O ILE A 24 37.199 27.810 69.961 1.00 43.09 O ANISOU 190 O ILE E 24 6870 5635 3868 -744 545 -885 O ATOM 191 CB ILE A 24 36.238 30.048 67.676 1.00 33.76 C ANISOU 191 CB ILE E 24 4106 5106 3616 84 1724 -768 C ATOM 192 CG1 ILE A 24 36.631 31.410 67.115 1.00 32.78 C ANISOU 192 CG1 ILE E 24 4389 4766 3300 68 1392 -388 C ATOM 193 CG2 ILE A 24 35.398 30.191 68.954 1.00 35.69 C ANISOU 193 CG2 ILE E 24 3904 6526 3130 -272 1273 -1019 C ATOM 194 CD1 ILE A 24 35.511 32.174 66.463 1.00 33.70 C ANISOU 194 CD1 ILE E 24 4440 4508 3855 -216 1429 -75 C ATOM 195 N ASN A 25 36.381 26.930 68.106 1.00 39.70 N ANISOU 195 N ASN E 25 5448 5176 4462 -73 823 -715 N ATOM 196 CA ASN A 25 35.856 25.829 68.920 1.00 38.29 C ANISOU 196 CA ASN E 25 4951 5480 4118 -75 1363 -477 C ATOM 197 C ASN A 25 36.998 24.985 69.456 1.00 38.36 C ANISOU 197 C ASN E 25 5064 5487 4025 -82 1665 -1018 C ATOM 198 O ASN A 25 36.940 24.399 70.547 1.00 45.52 O ANISOU 198 O ASN E 25 6670 6190 4436 -504 2035 -1597 O ATOM 199 CB ASN A 25 34.829 25.028 68.118 1.00 38.75 C ANISOU 199 CB ASN E 25 5514 5043 4167 -147 1240 -254 C ATOM 200 CG ASN A 25 33.502 25.746 67.939 1.00 37.94 C ANISOU 200 CG ASN E 25 4753 5011 4650 399 1590 199 C ATOM 201 OD1 ASN A 25 33.163 26.640 68.721 1.00 43.68 O ANISOU 201 OD1 ASN E 25 5939 5284 5373 -193 1400 577 O ATOM 202 ND2 ASN A 25 32.698 25.418 66.938 1.00 38.06 N ANISOU 202 ND2 ASN E 25 5159 4318 4983 639 1083 -371 N ATOM 203 N ALA A 26 38.126 24.890 68.754 1.00 39.03 N ANISOU 203 N ALA E 26 5387 5650 3794 -559 1731 -124 N ATOM 204 CA ALA A 26 39.201 24.055 69.307 1.00 39.56 C ANISOU 204 CA ALA E 26 5776 5022 4232 -740 1787 -16 C ATOM 205 C ALA A 26 39.921 24.756 70.448 1.00 39.68 C ANISOU 205 C ALA E 26 6338 4625 4112 -760 1116 -698 C ATOM 206 O ALA A 26 40.468 24.106 71.328 1.00 47.53 O ANISOU 206 O ALA E 26 9724 4861 3475 -1902 1068 -498 O ATOM 207 CB ALA A 26 40.210 23.705 68.223 1.00 36.18 C ANISOU 207 CB ALA E 26 5123 4342 4282 -55 1936 -723 C ATOM 208 N PHE A 27 39.927 26.085 70.410 1.00 38.35 N ANISOU 208 N PHE E 27 5942 4615 4013 -405 1029 -920 N ATOM 209 CA PHE A 27 40.607 26.904 71.405 1.00 40.04 C ANISOU 209 CA PHE E 27 6188 5010 4013 -384 1177 -579 C ATOM 210 C PHE A 27 39.842 26.957 72.723 1.00 41.26 C ANISOU 210 C PHE E 27 6808 4817 4051 -346 1448 -885 C ATOM 211 O PHE A 27 40.462 27.059 73.781 1.00 41.16 O ANISOU 211 O PHE E 27 7394 4144 4103 -954 1316 -139 O ATOM 212 CB PHE A 27 40.770 28.327 70.896 1.00 37.50 C ANISOU 212 CB PHE E 27 5627 5273 3349 184 623 -681 C ATOM 213 CG PHE A 27 41.522 29.329 71.751 1.00 36.10 C ANISOU 213 CG PHE E 27 4925 5379 3413 -351 584 -349 C ATOM 214 CD1 PHE A 27 42.885 29.480 71.581 1.00 36.57 C ANISOU 214 CD1 PHE E 27 4890 5474 3529 -493 506 -721 C ATOM 215 CD2 PHE A 27 40.873 30.107 72.694 1.00 37.55 C ANISOU 215 CD2 PHE E 27 5136 5593 3540 -1063 296 -375 C ATOM 216 CE1 PHE A 27 43.586 30.386 72.336 1.00 37.05 C ANISOU 216 CE1 PHE E 27 4493 5781 3805 -495 810 -343 C ATOM 217 CE2 PHE A 27 41.572 31.031 73.454 1.00 38.14 C ANISOU 217 CE2 PHE E 27 4737 5829 3926 -1438 374 177 C ATOM 218 CZ PHE A 27 42.935 31.183 73.264 1.00 39.50 C ANISOU 218 CZ PHE E 27 4809 6140 4058 -1157 437 -99 C ATOM 219 N LYS A 28 38.521 26.900 72.626 1.00 44.61 N ANISOU 219 N LYS E 28 6756 5747 4445 -570 1777 -641 N ATOM 220 CA LYS A 28 37.663 26.896 73.814 1.00 46.21 C ANISOU 220 CA LYS E 28 7387 5462 4708 -684 2205 -620 C ATOM 221 C LYS A 28 37.855 28.146 74.669 1.00 44.35 C ANISOU 221 C LYS E 28 7283 5607 3960 -986 1123 -833 C ATOM 222 O LYS A 28 38.351 28.055 75.795 1.00 49.03 O ANISOU 222 O LYS E 28 8259 6865 3505 -1735 1498 -1172 O ATOM 223 CB LYS A 28 37.934 25.646 74.661 1.00 52.78 C ANISOU 223 CB LYS E 28 8806 5571 5675 -713 2907 -1237 C ATOM 224 CG LYS A 28 37.467 24.366 73.999 1.00 62.04 C ANISOU 224 CG LYS E 28 10735 5380 7459 -1095 2638 -533 C ATOM 225 CD LYS A 28 38.527 23.271 74.005 1.00 83.37 C ANISOU 225 CD LYS E 28 14704 6945 10028 -3815 2545 -213 C ATOM 226 CE LYS A 28 38.582 22.536 72.670 1.00 92.61 C ANISOU 226 CE LYS E 28 16511 7514 11163 -4622 2424 933 C ATOM 227 NZ LYS A 28 39.889 21.880 72.383 1.00103.41 N ANISOU 227 NZ LYS E 28 18273 7587 13433 -5443 6133 -1423 N ATOM 228 N PRO A 29 37.463 29.296 74.130 1.00 39.46 N ANISOU 228 N PRO E 29 5785 5362 3845 -424 1002 -725 N ATOM 229 CA PRO A 29 37.738 30.583 74.768 1.00 37.54 C ANISOU 229 CA PRO E 29 5009 5543 3711 -230 939 -695 C ATOM 230 C PRO A 29 36.908 30.787 76.026 1.00 41.25 C ANISOU 230 C PRO E 29 6231 5831 3612 -708 1172 -774 C ATOM 231 O PRO A 29 35.796 30.266 76.104 1.00 43.73 O ANISOU 231 O PRO E 29 5745 6606 4264 -1134 1934 -461 O ATOM 232 CB PRO A 29 37.285 31.591 73.700 1.00 35.65 C ANISOU 232 CB PRO E 29 4574 5268 3702 -35 1111 -669 C ATOM 233 CG PRO A 29 36.200 30.857 72.970 1.00 36.41 C ANISOU 233 CG PRO E 29 5121 5152 3560 33 908 -576 C ATOM 234 CD PRO A 29 36.723 29.444 72.862 1.00 38.15 C ANISOU 234 CD PRO E 29 5260 5248 3985 -108 942 -559 C ATOM 235 N THR A 30 37.463 31.544 76.966 1.00 45.50 N ANISOU 235 N THR E 30 7490 6010 3786 -1299 469 -481 N ATOM 236 CA THR A 30 36.737 31.910 78.176 1.00 46.83 C ANISOU 236 CA THR E 30 7609 6480 3702 -1843 299 -454 C ATOM 237 C THR A 30 36.919 33.396 78.477 1.00 50.02 C ANISOU 237 C THR E 30 8268 6557 4179 -1744 797 -198 C ATOM 238 O THR A 30 37.692 34.085 77.806 1.00 52.51 O ANISOU 238 O THR E 30 8664 6438 4849 -1677 1162 -222 O ATOM 239 CB THR A 30 37.193 31.092 79.399 1.00 44.09 C ANISOU 239 CB THR E 30 6711 6582 3459 -1159 -332 -109 C ATOM 240 OG1 THR A 30 38.575 31.367 79.650 1.00 46.64 O ANISOU 240 OG1 THR E 30 6551 7076 4093 -953 237 201 O ATOM 241 CG2 THR A 30 37.090 29.601 79.122 1.00 42.08 C ANISOU 241 CG2 THR E 30 7296 6431 2261 -443 1449 -777 C ATOM 242 N ALA A 31 36.199 33.865 79.496 1.00 52.97 N ANISOU 242 N ALA E 31 8827 7004 4296 -1634 985 127 N ATOM 243 CA ALA A 31 36.243 35.260 79.912 1.00 53.78 C ANISOU 243 CA ALA E 31 9115 6975 4346 -1331 1698 68 C ATOM 244 C ALA A 31 37.681 35.728 80.120 1.00 54.14 C ANISOU 244 C ALA E 31 9096 7145 4330 -1356 1670 468 C ATOM 245 O ALA A 31 38.030 36.856 79.779 1.00 56.11 O ANISOU 245 O ALA E 31 9632 7247 4442 -738 -88 303 O ATOM 246 CB ALA A 31 35.440 35.474 81.191 1.00 55.18 C ANISOU 246 CB ALA E 31 9035 7432 4499 -1937 1730 -40 C ATOM 247 N ASP A 32 38.492 34.840 80.690 1.00 54.17 N ANISOU 247 N ASP E 32 8981 7218 4383 -1307 1864 231 N ATOM 248 CA ASP A 32 39.871 35.163 81.044 1.00 56.83 C ANISOU 248 CA ASP E 32 9268 7418 4908 -1227 1294 339 C ATOM 249 C ASP A 32 40.868 34.687 79.991 1.00 53.60 C ANISOU 249 C ASP E 32 8274 6953 5141 -1152 740 731 C ATOM 250 O ASP A 32 42.061 35.004 80.072 1.00 51.86 O ANISOU 250 O ASP E 32 8029 7728 3949 -1792 -388 384 O ATOM 251 CB ASP A 32 40.199 34.574 82.419 1.00 62.94 C ANISOU 251 CB ASP E 32 10524 8347 5042 -1065 743 143 C ATOM 252 CG ASP A 32 39.471 35.324 83.526 1.00 73.31 C ANISOU 252 CG ASP E 32 14176 8786 4892 -2321 1926 -630 C ATOM 253 OD1 ASP A 32 39.408 36.580 83.496 1.00 85.57 O ANISOU 253 OD1 ASP E 32 18137 8895 5480 -4880 594 -885 O ATOM 254 OD2 ASP A 32 38.938 34.671 84.457 1.00102.79 O ANISOU 254 OD2 ASP E 32 18775 12167 8113 -4367 5851 -3177 O ATOM 255 N ARG A 33 40.385 33.935 79.005 1.00 47.75 N ANISOU 255 N ARG E 33 7703 6550 3890 -716 804 -507 N ATOM 256 CA ARG A 33 41.235 33.504 77.900 1.00 44.00 C ANISOU 256 CA ARG E 33 6663 6144 3912 -801 287 -402 C ATOM 257 C ARG A 33 40.393 33.552 76.625 1.00 42.40 C ANISOU 257 C ARG E 33 6310 5814 3985 -788 346 -194 C ATOM 258 O ARG A 33 39.893 32.519 76.172 1.00 42.09 O ANISOU 258 O ARG E 33 6755 5625 3612 -979 834 113 O ATOM 259 CB ARG A 33 41.832 32.114 78.113 1.00 46.13 C ANISOU 259 CB ARG E 33 6191 6304 5030 -675 436 -1107 C ATOM 260 CG ARG A 33 43.107 31.905 77.310 1.00 48.91 C ANISOU 260 CG ARG E 33 5890 6223 6471 -488 610 -650 C ATOM 261 CD ARG A 33 43.496 30.430 77.237 1.00 50.23 C ANISOU 261 CD ARG E 33 5725 6018 7342 -54 992 -652 C ATOM 262 NE ARG A 33 42.328 29.625 76.931 1.00 54.48 N ANISOU 262 NE ARG E 33 6214 6723 7762 313 312 -655 N ATOM 263 CZ ARG A 33 42.164 28.676 76.028 1.00 51.40 C ANISOU 263 CZ ARG E 33 5936 6491 7104 380 692 -1028 C ATOM 264 NH1 ARG A 33 43.102 28.271 75.194 1.00 45.95 N ANISOU 264 NH1 ARG E 33 5864 5661 5935 -359 383 -2613 N ATOM 265 NH2 ARG A 33 40.959 28.113 75.987 1.00 51.57 N ANISOU 265 NH2 ARG E 33 6382 6499 6714 886 1086 -1189 N ATOM 266 N PRO A 34 40.241 34.767 76.113 1.00 38.08 N ANISOU 266 N PRO E 34 5036 5895 3539 -293 777 -377 N ATOM 267 CA PRO A 34 39.460 34.960 74.893 1.00 37.24 C ANISOU 267 CA PRO E 34 5165 5475 3510 -542 698 62 C ATOM 268 C PRO A 34 40.223 34.532 73.644 1.00 37.15 C ANISOU 268 C PRO E 34 4964 5495 3654 -911 572 154 C ATOM 269 O PRO A 34 41.449 34.548 73.641 1.00 34.83 O ANISOU 269 O PRO E 34 4961 4858 3415 -1190 232 197 O ATOM 270 CB PRO A 34 39.269 36.482 74.855 1.00 34.64 C ANISOU 270 CB PRO E 34 3958 5439 3767 -423 591 302 C ATOM 271 CG PRO A 34 40.477 37.026 75.557 1.00 34.98 C ANISOU 271 CG PRO E 34 4129 5589 3573 -786 -2 -77 C ATOM 272 CD PRO A 34 40.771 36.032 76.641 1.00 35.93 C ANISOU 272 CD PRO E 34 4820 5946 2885 -437 898 -291 C ATOM 273 N PHE A 35 39.503 34.180 72.590 1.00 33.50 N ANISOU 273 N PHE E 35 4323 4795 3610 -209 1093 92 N ATOM 274 CA PHE A 35 40.036 34.012 71.245 1.00 34.47 C ANISOU 274 CA PHE E 35 4715 4901 3480 -303 1108 -166 C ATOM 275 C PHE A 35 40.102 35.381 70.583 1.00 30.80 C ANISOU 275 C PHE E 35 3745 4708 3249 -133 283 80 C ATOM 276 O PHE A 35 39.097 36.103 70.522 1.00 34.69 O ANISOU 276 O PHE E 35 4370 5498 3313 -953 865 102 O ATOM 277 CB PHE A 35 39.150 33.090 70.426 1.00 31.19 C ANISOU 277 CB PHE E 35 4628 4378 2845 -147 1408 -659 C ATOM 278 CG PHE A 35 39.794 32.720 69.088 1.00 32.85 C ANISOU 278 CG PHE E 35 4726 4756 2998 -563 1396 -552 C ATOM 279 CD1 PHE A 35 40.645 31.635 69.015 1.00 34.09 C ANISOU 279 CD1 PHE E 35 4555 4989 3409 -659 1006 -231 C ATOM 280 CD2 PHE A 35 39.521 33.469 67.962 1.00 32.16 C ANISOU 280 CD2 PHE E 35 4104 5072 3044 -292 1803 -911 C ATOM 281 CE1 PHE A 35 41.243 31.286 67.819 1.00 36.47 C ANISOU 281 CE1 PHE E 35 5383 4816 3659 -970 1408 -344 C ATOM 282 CE2 PHE A 35 40.121 33.117 66.755 1.00 32.59 C ANISOU 282 CE2 PHE E 35 4209 5400 2773 -710 1003 -232 C ATOM 283 CZ PHE A 35 40.974 32.023 66.677 1.00 31.87 C ANISOU 283 CZ PHE E 35 4006 4644 3461 -139 1146 -158 C ATOM 284 N VAL A 36 41.269 35.760 70.084 1.00 31.61 N ANISOU 284 N VAL E 36 4174 4493 3343 -147 942 418 N ATOM 285 CA VAL A 36 41.441 37.101 69.533 1.00 31.43 C ANISOU 285 CA VAL E 36 4778 4483 2682 123 698 564 C ATOM 286 C VAL A 36 41.477 37.031 68.007 1.00 32.63 C ANISOU 286 C VAL E 36 5038 4700 2660 -862 252 757 C ATOM 287 O VAL A 36 42.344 36.337 67.451 1.00 32.32 O ANISOU 287 O VAL E 36 4713 5181 2386 -1089 704 -255 O ATOM 288 CB VAL A 36 42.691 37.798 70.095 1.00 31.27 C ANISOU 288 CB VAL E 36 4827 4559 2494 99 136 -277 C ATOM 289 CG1 VAL A 36 42.787 39.225 69.571 1.00 27.48 C ANISOU 289 CG1 VAL E 36 3380 4632 2430 -165 -163 -417 C ATOM 290 CG2 VAL A 36 42.670 37.784 71.638 1.00 28.93 C ANISOU 290 CG2 VAL E 36 3655 4842 2496 -270 474 -500 C ATOM 291 N LEU A 37 40.539 37.725 67.374 1.00 30.67 N ANISOU 291 N LEU E 37 4517 4144 2994 -623 685 483 N ATOM 292 CA LEU A 37 40.274 37.654 65.949 1.00 28.29 C ANISOU 292 CA LEU E 37 3603 4101 3043 -644 539 372 C ATOM 293 C LEU A 37 40.516 38.996 65.277 1.00 28.55 C ANISOU 293 C LEU E 37 3493 4173 3181 -461 441 330 C ATOM 294 O LEU A 37 39.833 39.945 65.670 1.00 29.10 O ANISOU 294 O LEU E 37 3783 3994 3281 -337 844 224 O ATOM 295 CB LEU A 37 38.812 37.336 65.686 1.00 32.82 C ANISOU 295 CB LEU E 37 3775 4139 4557 -272 387 425 C ATOM 296 CG LEU A 37 38.285 36.288 64.723 1.00 32.63 C ANISOU 296 CG LEU E 37 3723 5069 3608 -636 -25 474 C ATOM 297 CD1 LEU A 37 36.861 36.658 64.310 1.00 32.91 C ANISOU 297 CD1 LEU E 37 4935 4662 2905 -2002 -779 347 C ATOM 298 CD2 LEU A 37 39.141 36.051 63.493 1.00 28.13 C ANISOU 298 CD2 LEU E 37 4074 4126 2488 234 -64 -1156 C ATOM 299 N GLY A 38 41.403 39.070 64.296 1.00 29.00 N ANISOU 299 N GLY E 38 3598 4227 3192 -802 506 96 N ATOM 300 CA GLY A 38 41.606 40.306 63.547 1.00 27.79 C ANISOU 300 CA GLY E 38 3542 4232 2786 -519 8 203 C ATOM 301 C GLY A 38 40.740 40.280 62.285 1.00 28.30 C ANISOU 301 C GLY E 38 3406 4072 3273 -349 -292 388 C ATOM 302 O GLY A 38 40.591 39.224 61.656 1.00 26.56 O ANISOU 302 O GLY E 38 3348 4128 2614 -59 648 328 O ATOM 303 N LEU A 39 40.149 41.420 61.926 1.00 26.66 N ANISOU 303 N LEU E 39 3158 3916 3056 106 -40 -130 N ATOM 304 CA LEU A 39 39.125 41.446 60.893 1.00 26.08 C ANISOU 304 CA LEU E 39 2896 3741 3271 159 -45 -11 C ATOM 305 C LEU A 39 39.281 42.588 59.912 1.00 25.74 C ANISOU 305 C LEU E 39 3267 3450 3064 -333 27 177 C ATOM 306 O LEU A 39 39.718 43.677 60.273 1.00 27.38 O ANISOU 306 O LEU E 39 3133 3840 3430 335 36 -56 O ATOM 307 CB LEU A 39 37.740 41.586 61.558 1.00 28.35 C ANISOU 307 CB LEU E 39 3119 4457 3196 -71 160 283 C ATOM 308 CG LEU A 39 37.317 40.380 62.398 1.00 29.90 C ANISOU 308 CG LEU E 39 3207 4583 3570 -75 755 292 C ATOM 309 CD1 LEU A 39 35.931 40.602 63.012 1.00 28.57 C ANISOU 309 CD1 LEU E 39 3188 5131 2536 -340 361 570 C ATOM 310 CD2 LEU A 39 37.339 39.092 61.579 1.00 29.84 C ANISOU 310 CD2 LEU E 39 3316 4361 3659 -386 957 143 C ATOM 311 N PRO A 40 38.935 42.372 58.658 1.00 27.30 N ANISOU 311 N PRO E 40 3357 4166 2850 -156 495 260 N ATOM 312 CA PRO A 40 38.881 43.438 57.658 1.00 27.80 C ANISOU 312 CA PRO E 40 3695 4172 2697 -269 673 271 C ATOM 313 C PRO A 40 37.475 43.833 57.237 1.00 29.36 C ANISOU 313 C PRO E 40 3953 3855 3348 -565 426 409 C ATOM 314 O PRO A 40 36.483 43.211 57.640 1.00 28.16 O ANISOU 314 O PRO E 40 3646 3956 3097 -554 -80 202 O ATOM 315 CB PRO A 40 39.543 42.699 56.475 1.00 26.34 C ANISOU 315 CB PRO E 40 3850 3430 2729 -341 378 300 C ATOM 316 CG PRO A 40 38.950 41.330 56.584 1.00 26.74 C ANISOU 316 CG PRO E 40 3569 3895 2697 62 756 21 C ATOM 317 CD PRO A 40 38.639 41.065 58.046 1.00 26.74 C ANISOU 317 CD PRO E 40 3568 4218 2373 -160 163 111 C ATOM 318 N THR A 41 37.386 44.869 56.410 1.00 30.65 N ANISOU 318 N THR E 41 4076 4449 3119 -593 654 129 N ATOM 319 CA THR A 41 36.122 45.349 55.881 1.00 32.57 C ANISOU 319 CA THR E 41 4423 4492 3462 -721 316 55 C ATOM 320 C THR A 41 36.196 45.324 54.354 1.00 34.25 C ANISOU 320 C THR E 41 4493 5077 3445 -735 278 149 C ATOM 321 O THR A 41 37.202 44.872 53.793 1.00 39.20 O ANISOU 321 O THR E 41 4684 6525 3685 -983 561 213 O ATOM 322 CB THR A 41 35.727 46.766 56.340 1.00 33.71 C ANISOU 322 CB THR E 41 5253 4338 3216 -1003 374 -341 C ATOM 323 OG1 THR A 41 36.719 47.696 55.884 1.00 36.62 O ANISOU 323 OG1 THR E 41 6285 4357 3273 -747 1025 -314 O ATOM 324 CG2 THR A 41 35.699 46.929 57.847 1.00 31.31 C ANISOU 324 CG2 THR E 41 5179 3499 3219 550 189 -159 C ATOM 325 N GLY A 42 35.162 45.792 53.682 1.00 36.09 N ANISOU 325 N GLY E 42 4541 5612 3561 -598 114 26 N ATOM 326 CA GLY A 42 35.107 45.864 52.241 1.00 36.71 C ANISOU 326 CA GLY E 42 4990 5433 3523 -684 16 166 C ATOM 327 C GLY A 42 34.306 44.743 51.627 1.00 35.57 C ANISOU 327 C GLY E 42 4942 5088 3485 -742 147 -25 C ATOM 328 O GLY A 42 33.712 43.895 52.260 1.00 35.05 O ANISOU 328 O GLY E 42 5529 4786 3001 -940 306 113 O ATOM 329 N GLY A 43 34.258 44.707 50.298 1.00 34.07 N ANISOU 329 N GLY E 43 4938 4519 3487 -272 530 59 N ATOM 330 CA GLY A 43 33.473 43.700 49.594 1.00 33.79 C ANISOU 330 CA GLY E 43 4362 4499 3976 -767 424 439 C ATOM 331 C GLY A 43 34.073 42.312 49.732 1.00 31.78 C ANISOU 331 C GLY E 43 4012 4468 3594 -551 440 29 C ATOM 332 O GLY A 43 33.338 41.325 49.712 1.00 32.96 O ANISOU 332 O GLY E 43 4103 4546 3873 -467 797 284 O ATOM 333 N THR A 44 35.389 42.204 49.868 1.00 30.70 N ANISOU 333 N THR E 44 3928 4790 2946 -615 788 -67 N ATOM 334 CA THR A 44 36.030 40.888 49.895 1.00 31.56 C ANISOU 334 CA THR E 44 4083 4857 3050 -743 580 -30 C ATOM 335 C THR A 44 35.567 39.998 51.026 1.00 27.57 C ANISOU 335 C THR E 44 3397 4242 2838 -98 107 451 C ATOM 336 O THR A 44 35.223 38.837 50.762 1.00 29.25 O ANISOU 336 O THR E 44 2870 4461 3782 -108 348 1007 O ATOM 337 CB THR A 44 37.569 41.052 49.960 1.00 32.96 C ANISOU 337 CB THR E 44 4063 4366 4094 -645 1021 -659 C ATOM 338 OG1 THR A 44 38.019 41.577 48.698 1.00 40.12 O ANISOU 338 OG1 THR E 44 5055 5581 4609 -1401 1930 -1118 O ATOM 339 CG2 THR A 44 38.275 39.724 50.138 1.00 30.57 C ANISOU 339 CG2 THR E 44 4264 4209 3141 -760 433 432 C ATOM 340 N PRO A 45 35.551 40.392 52.297 1.00 27.52 N ANISOU 340 N PRO E 45 3448 4170 2840 -157 392 440 N ATOM 341 CA PRO A 45 35.038 39.466 53.308 1.00 28.21 C ANISOU 341 CA PRO E 45 3447 4269 3002 63 271 322 C ATOM 342 C PRO A 45 33.519 39.372 53.387 1.00 28.67 C ANISOU 342 C PRO E 45 3466 4244 3183 199 52 130 C ATOM 343 O PRO A 45 33.022 38.700 54.297 1.00 29.73 O ANISOU 343 O PRO E 45 3427 4747 3122 -639 856 110 O ATOM 344 CB PRO A 45 35.573 40.090 54.616 1.00 26.66 C ANISOU 344 CB PRO E 45 3291 3904 2934 -104 69 9 C ATOM 345 CG PRO A 45 35.684 41.560 54.323 1.00 26.85 C ANISOU 345 CG PRO E 45 3873 3958 2372 -165 -185 -94 C ATOM 346 CD PRO A 45 36.047 41.660 52.854 1.00 28.88 C ANISOU 346 CD PRO E 45 4611 3828 2536 -229 346 252 C ATOM 347 N MET A 46 32.696 39.975 52.544 1.00 31.24 N ANISOU 347 N MET E 46 3654 5111 3103 -530 326 104 N ATOM 348 CA MET A 46 31.237 39.877 52.723 1.00 32.62 C ANISOU 348 CA MET E 46 3597 4831 3968 -342 -49 882 C ATOM 349 C MET A 46 30.685 38.456 52.790 1.00 34.04 C ANISOU 349 C MET E 46 4307 4874 3754 -194 1028 833 C ATOM 350 O MET A 46 29.891 38.134 53.673 1.00 36.82 O ANISOU 350 O MET E 46 4296 5735 3957 -568 1120 309 O ATOM 351 CB MET A 46 30.455 40.581 51.602 1.00 32.57 C ANISOU 351 CB MET E 46 3155 5559 3662 142 294 281 C ATOM 352 CG MET A 46 30.581 42.093 51.623 1.00 39.33 C ANISOU 352 CG MET E 46 4828 5541 4573 142 -53 -347 C ATOM 353 SD MET A 46 29.663 42.769 53.022 1.00 54.33 S ANISOU 353 SD MET E 46 6699 6308 7636 -571 996 1817 S ATOM 354 CE MET A 46 27.981 42.576 52.450 1.00 56.96 C ANISOU 354 CE MET E 46 5802 8021 7819 43 2212 -1512 C ATOM 355 N THR A 47 31.069 37.562 51.874 1.00 32.40 N ANISOU 355 N THR E 47 3999 4720 3590 -566 433 774 N ATOM 356 CA THR A 47 30.476 36.224 51.975 1.00 31.89 C ANISOU 356 CA THR E 47 3595 4904 3620 -412 345 823 C ATOM 357 C THR A 47 30.988 35.501 53.211 1.00 32.90 C ANISOU 357 C THR E 47 4405 4460 3634 -205 58 935 C ATOM 358 O THR A 47 30.321 34.582 53.718 1.00 33.63 O ANISOU 358 O THR E 47 4046 4683 4048 -241 43 705 O ATOM 359 CB THR A 47 30.752 35.342 50.740 1.00 30.82 C ANISOU 359 CB THR E 47 4163 4178 3369 -198 1031 189 C ATOM 360 OG1 THR A 47 32.182 35.231 50.575 1.00 33.92 O ANISOU 360 OG1 THR E 47 4147 5056 3687 -660 646 709 O ATOM 361 CG2 THR A 47 30.161 35.912 49.449 1.00 31.26 C ANISOU 361 CG2 THR E 47 3715 4857 3305 -117 1007 160 C ATOM 362 N THR A 48 32.161 35.865 53.734 1.00 29.54 N ANISOU 362 N THR E 48 4228 3914 3080 -357 324 878 N ATOM 363 CA THR A 48 32.623 35.214 54.969 1.00 27.79 C ANISOU 363 CA THR E 48 3417 3989 3153 -39 813 442 C ATOM 364 C THR A 48 31.769 35.601 56.175 1.00 28.17 C ANISOU 364 C THR E 48 3178 4078 3446 -129 980 221 C ATOM 365 O THR A 48 31.389 34.748 56.973 1.00 30.90 O ANISOU 365 O THR E 48 4012 4516 3213 -461 995 -116 O ATOM 366 CB THR A 48 34.104 35.551 55.224 1.00 28.55 C ANISOU 366 CB THR E 48 3209 4227 3412 -173 1019 -331 C ATOM 367 OG1 THR A 48 34.895 35.040 54.145 1.00 29.67 O ANISOU 367 OG1 THR E 48 3288 4736 3250 -144 689 174 O ATOM 368 CG2 THR A 48 34.625 34.878 56.483 1.00 27.34 C ANISOU 368 CG2 THR E 48 3844 3330 3213 -240 602 305 C ATOM 369 N TYR A 49 31.445 36.875 56.345 1.00 29.41 N ANISOU 369 N TYR E 49 3728 4195 3251 -350 798 446 N ATOM 370 CA TYR A 49 30.596 37.380 57.420 1.00 29.62 C ANISOU 370 CA TYR E 49 3529 4508 3217 -357 716 488 C ATOM 371 C TYR A 49 29.205 36.758 57.313 1.00 31.06 C ANISOU 371 C TYR E 49 3479 4980 3342 -281 483 -129 C ATOM 372 O TYR A 49 28.619 36.281 58.290 1.00 32.01 O ANISOU 372 O TYR E 49 3581 5256 3326 -193 493 -166 O ATOM 373 CB TYR A 49 30.523 38.909 57.395 1.00 28.70 C ANISOU 373 CB TYR E 49 3729 4516 2661 -593 763 432 C ATOM 374 CG TYR A 49 31.821 39.551 57.837 1.00 28.86 C ANISOU 374 CG TYR E 49 3899 4225 2843 -562 643 535 C ATOM 375 CD1 TYR A 49 32.448 39.150 59.019 1.00 29.67 C ANISOU 375 CD1 TYR E 49 3644 4428 3202 -472 600 139 C ATOM 376 CD2 TYR A 49 32.431 40.555 57.093 1.00 28.94 C ANISOU 376 CD2 TYR E 49 4228 4131 2636 -369 435 627 C ATOM 377 CE1 TYR A 49 33.639 39.738 59.430 1.00 30.68 C ANISOU 377 CE1 TYR E 49 4273 3965 3417 -273 178 282 C ATOM 378 CE2 TYR A 49 33.631 41.156 57.490 1.00 29.44 C ANISOU 378 CE2 TYR E 49 4204 4244 2736 -319 475 638 C ATOM 379 CZ TYR A 49 34.219 40.731 58.659 1.00 30.49 C ANISOU 379 CZ TYR E 49 4441 3847 3297 -119 27 397 C ATOM 380 OH TYR A 49 35.396 41.298 59.082 1.00 29.81 O ANISOU 380 OH TYR E 49 4119 4185 3023 -249 372 598 O ATOM 381 N LYS A 50 28.675 36.738 56.085 1.00 30.55 N ANISOU 381 N LYS E 50 3676 4614 3316 -206 455 -43 N ATOM 382 CA LYS A 50 27.373 36.109 55.866 1.00 33.48 C ANISOU 382 CA LYS E 50 3763 4868 4090 -138 300 528 C ATOM 383 C LYS A 50 27.414 34.658 56.333 1.00 34.21 C ANISOU 383 C LYS E 50 3396 4891 4709 5 747 390 C ATOM 384 O LYS A 50 26.486 34.205 57.026 1.00 34.90 O ANISOU 384 O LYS E 50 3537 5537 4188 130 643 348 O ATOM 385 CB LYS A 50 26.965 36.215 54.398 1.00 36.30 C ANISOU 385 CB LYS E 50 3582 6026 4183 140 229 363 C ATOM 386 CG LYS A 50 25.843 35.266 54.011 1.00 44.99 C ANISOU 386 CG LYS E 50 4759 6862 5473 802 -824 439 C ATOM 387 CD LYS A 50 25.722 35.133 52.499 1.00 58.15 C ANISOU 387 CD LYS E 50 7857 8435 5801 -219 -2354 1304 C ATOM 388 CE LYS A 50 24.480 34.388 52.023 1.00 62.07 C ANISOU 388 CE LYS E 50 7631 9259 6695 -492 -3182 1119 C ATOM 389 NZ LYS A 50 23.599 35.187 51.129 1.00 67.58 N ANISOU 389 NZ LYS E 50 6656 10188 8835 -1236 -2240 -114 N ATOM 390 N ALA A 51 28.454 33.903 55.991 1.00 33.07 N ANISOU 390 N ALA E 51 3618 4766 4180 -56 576 739 N ATOM 391 CA ALA A 51 28.531 32.518 56.441 1.00 38.48 C ANISOU 391 CA ALA E 51 5429 4882 4308 -518 249 671 C ATOM 392 C ALA A 51 28.805 32.391 57.934 1.00 37.45 C ANISOU 392 C ALA E 51 5427 4726 4077 -234 819 774 C ATOM 393 O ALA A 51 28.281 31.496 58.620 1.00 39.04 O ANISOU 393 O ALA E 51 5435 4712 4686 -181 578 452 O ATOM 394 CB ALA A 51 29.622 31.778 55.669 1.00 38.64 C ANISOU 394 CB ALA E 51 6696 4148 3837 -483 1315 -169 C ATOM 395 N LEU A 52 29.644 33.273 58.490 1.00 35.68 N ANISOU 395 N LEU E 52 5046 4696 3814 -349 927 699 N ATOM 396 CA LEU A 52 29.860 33.226 59.935 1.00 33.57 C ANISOU 396 CA LEU E 52 4097 4791 3867 -151 930 194 C ATOM 397 C LEU A 52 28.537 33.440 60.672 1.00 36.49 C ANISOU 397 C LEU E 52 4286 5492 4087 -463 1111 -39 C ATOM 398 O LEU A 52 28.195 32.734 61.626 1.00 38.80 O ANISOU 398 O LEU E 52 4941 5301 4500 -245 1690 70 O ATOM 399 CB LEU A 52 30.859 34.295 60.363 1.00 35.41 C ANISOU 399 CB LEU E 52 4291 4751 4413 -274 184 39 C ATOM 400 CG LEU A 52 32.331 33.936 60.449 1.00 38.29 C ANISOU 400 CG LEU E 52 4407 4980 5163 -433 -340 505 C ATOM 401 CD1 LEU A 52 33.155 35.164 60.815 1.00 45.21 C ANISOU 401 CD1 LEU E 52 4596 5953 6630 -275 -507 2054 C ATOM 402 CD2 LEU A 52 32.541 32.797 61.447 1.00 41.23 C ANISOU 402 CD2 LEU E 52 5482 6511 3672 -1048 -925 517 C ATOM 403 N VAL A 53 27.774 34.440 60.233 1.00 34.15 N ANISOU 403 N VAL E 53 3484 5648 3844 -77 -36 542 N ATOM 404 CA VAL A 53 26.492 34.692 60.896 1.00 34.02 C ANISOU 404 CA VAL E 53 3492 5687 3746 6 -38 663 C ATOM 405 C VAL A 53 25.575 33.474 60.887 1.00 35.71 C ANISOU 405 C VAL E 53 3968 5688 3913 210 505 903 C ATOM 406 O VAL A 53 24.889 33.117 61.863 1.00 37.15 O ANISOU 406 O VAL E 53 5239 5205 3671 335 614 801 O ATOM 407 CB VAL A 53 25.838 35.891 60.194 1.00 34.43 C ANISOU 407 CB VAL E 53 3146 5744 4193 115 -316 640 C ATOM 408 CG1 VAL A 53 24.371 36.004 60.581 1.00 34.38 C ANISOU 408 CG1 VAL E 53 3037 5677 4350 336 -480 1600 C ATOM 409 CG2 VAL A 53 26.620 37.146 60.550 1.00 32.94 C ANISOU 409 CG2 VAL E 53 3012 5751 3754 300 394 532 C ATOM 410 N GLU A 54 25.579 32.801 59.737 1.00 36.62 N ANISOU 410 N GLU E 54 4243 5648 4023 367 921 994 N ATOM 411 CA GLU A 54 24.762 31.627 59.499 1.00 37.38 C ANISOU 411 CA GLU E 54 4634 5511 4059 340 472 836 C ATOM 412 C GLU A 54 25.119 30.515 60.489 1.00 38.61 C ANISOU 412 C GLU E 54 4553 5914 4205 351 560 489 C ATOM 413 O GLU A 54 24.251 29.889 61.113 1.00 41.06 O ANISOU 413 O GLU E 54 4916 6097 4589 -34 1338 407 O ATOM 414 CB GLU A 54 24.904 31.108 58.058 1.00 41.10 C ANISOU 414 CB GLU E 54 5125 6523 3967 353 -3 1093 C ATOM 415 CG GLU A 54 23.796 31.478 57.103 1.00 58.89 C ANISOU 415 CG GLU E 54 8324 8511 5542 -1348 -2116 1608 C ATOM 416 CD GLU A 54 24.169 31.323 55.638 1.00 65.60 C ANISOU 416 CD GLU E 54 9639 10092 5195 -2264 -2694 1559 C ATOM 417 OE1 GLU A 54 25.285 30.874 55.287 1.00 88.06 O ANISOU 417 OE1 GLU E 54 13342 12442 7675 -5923 49 1437 O ATOM 418 OE2 GLU A 54 23.326 31.656 54.769 1.00 87.65 O ANISOU 418 OE2 GLU E 54 14582 11984 6736 -3012 -5420 578 O ATOM 419 N MET A 55 26.421 30.285 60.608 1.00 39.25 N ANISOU 419 N MET E 55 4572 5933 4408 388 290 604 N ATOM 420 CA MET A 55 26.898 29.243 61.512 1.00 40.82 C ANISOU 420 CA MET E 55 5468 5886 4156 -399 382 995 C ATOM 421 C MET A 55 26.564 29.541 62.968 1.00 40.32 C ANISOU 421 C MET E 55 5277 5804 4237 -258 593 957 C ATOM 422 O MET A 55 26.297 28.662 63.806 1.00 41.77 O ANISOU 422 O MET E 55 5137 5985 4748 -205 1262 839 O ATOM 423 CB MET A 55 28.415 29.120 61.311 1.00 37.31 C ANISOU 423 CB MET E 55 5429 5474 3274 -54 447 305 C ATOM 424 CG MET A 55 28.747 28.628 59.904 1.00 37.55 C ANISOU 424 CG MET E 55 5293 5936 3040 76 223 264 C ATOM 425 SD MET A 55 30.524 28.406 59.687 1.00 42.14 S ANISOU 425 SD MET E 55 5526 5570 4915 -157 981 545 S ATOM 426 CE MET A 55 30.786 26.845 60.545 1.00 45.49 C ANISOU 426 CE MET E 55 6271 6996 4015 -1031 738 -217 C ATOM 427 N HIS A 56 26.601 30.839 63.283 1.00 40.28 N ANISOU 427 N HIS E 56 4606 5840 4861 -327 1653 1152 N ATOM 428 CA HIS A 56 26.269 31.308 64.631 1.00 36.50 C ANISOU 428 CA HIS E 56 4299 5254 4317 438 1371 679 C ATOM 429 C HIS A 56 24.807 31.003 64.897 1.00 37.39 C ANISOU 429 C HIS E 56 4325 5505 4376 325 1460 -163 C ATOM 430 O HIS A 56 24.345 30.478 65.910 1.00 42.59 O ANISOU 430 O HIS E 56 5264 6224 4696 -194 2341 -302 O ATOM 431 CB HIS A 56 26.521 32.815 64.765 1.00 35.48 C ANISOU 431 CB HIS E 56 4505 5119 3858 263 1363 337 C ATOM 432 CG HIS A 56 25.994 33.325 66.079 1.00 35.58 C ANISOU 432 CG HIS E 56 4589 4952 3976 201 1449 293 C ATOM 433 ND1 HIS A 56 26.417 32.833 67.298 1.00 35.66 N ANISOU 433 ND1 HIS E 56 4452 5245 3851 87 1267 567 N ATOM 434 CD2 HIS A 56 25.060 34.261 66.360 1.00 37.60 C ANISOU 434 CD2 HIS E 56 5221 4959 4106 -114 1382 360 C ATOM 435 CE1 HIS A 56 25.778 33.452 68.272 1.00 37.12 C ANISOU 435 CE1 HIS E 56 4915 5180 4010 -158 1590 277 C ATOM 436 NE2 HIS A 56 24.944 34.330 67.738 1.00 37.17 N ANISOU 436 NE2 HIS E 56 4672 5325 4126 -86 1582 188 N ATOM 437 N LYS A 57 24.007 31.367 63.884 1.00 41.30 N ANISOU 437 N LYS E 57 4464 6290 4937 -121 1128 -94 N ATOM 438 CA LYS A 57 22.563 31.153 64.058 1.00 43.41 C ANISOU 438 CA LYS E 57 4456 6226 5813 -116 1049 104 C ATOM 439 C LYS A 57 22.269 29.669 64.106 1.00 44.80 C ANISOU 439 C LYS E 57 4939 6334 5749 138 1462 5 C ATOM 440 O LYS A 57 21.318 29.227 64.752 1.00 50.05 O ANISOU 440 O LYS E 57 5462 6879 6674 355 2127 44 O ATOM 441 CB LYS A 57 21.803 31.910 62.962 1.00 44.48 C ANISOU 441 CB LYS E 57 4340 6575 5985 166 906 -158 C ATOM 442 CG LYS A 57 22.127 33.404 63.020 1.00 51.01 C ANISOU 442 CG LYS E 57 6070 6341 6971 -158 1498 -455 C ATOM 443 CD LYS A 57 21.240 34.189 62.075 1.00 56.88 C ANISOU 443 CD LYS E 57 6968 7301 7343 -997 1728 -1021 C ATOM 444 CE LYS A 57 20.797 35.494 62.725 1.00 64.05 C ANISOU 444 CE LYS E 57 8349 7361 8627 -1687 2644 -1279 C ATOM 445 NZ LYS A 57 20.103 36.392 61.741 1.00 78.18 N ANISOU 445 NZ LYS E 57 13083 8827 7794 -4030 3470 -2024 N ATOM 446 N ALA A 58 23.080 28.834 63.471 1.00 42.30 N ANISOU 446 N ALA E 58 4369 5980 5724 145 968 -91 N ATOM 447 CA ALA A 58 22.801 27.407 63.489 1.00 42.20 C ANISOU 447 CA ALA E 58 3914 6116 6006 458 1348 -142 C ATOM 448 C ALA A 58 23.300 26.801 64.787 1.00 43.86 C ANISOU 448 C ALA E 58 5241 5672 5750 264 1375 67 C ATOM 449 O ALA A 58 23.233 25.587 64.982 1.00 47.11 O ANISOU 449 O ALA E 58 5609 5777 6512 631 1364 -245 O ATOM 450 CB ALA A 58 23.460 26.731 62.296 1.00 40.88 C ANISOU 450 CB ALA E 58 4030 5802 5701 512 1062 -162 C ATOM 451 N GLY A 59 23.811 27.643 65.673 1.00 42.92 N ANISOU 451 N GLY E 59 4849 5919 5541 87 1691 300 N ATOM 452 CA GLY A 59 24.318 27.181 66.947 1.00 41.52 C ANISOU 452 CA GLY E 59 5229 5218 5327 449 1947 220 C ATOM 453 C GLY A 59 25.679 26.523 66.836 1.00 42.22 C ANISOU 453 C GLY E 59 5145 5719 5179 358 1743 -268 C ATOM 454 O GLY A 59 26.007 25.694 67.705 1.00 50.77 O ANISOU 454 O GLY E 59 6546 7108 5637 -812 2419 -1105 O ATOM 455 N GLN A 60 26.499 26.843 65.823 1.00 40.36 N ANISOU 455 N GLN E 60 5158 5593 4585 343 1617 281 N ATOM 456 CA GLN A 60 27.785 26.141 65.736 1.00 42.17 C ANISOU 456 CA GLN E 60 5305 5372 5345 297 1772 391 C ATOM 457 C GLN A 60 28.938 26.914 66.365 1.00 42.03 C ANISOU 457 C GLN E 60 5129 5202 5637 118 1539 193 C ATOM 458 O GLN A 60 30.069 26.450 66.553 1.00 41.80 O ANISOU 458 O GLN E 60 5215 5402 5265 4 1695 -339 O ATOM 459 CB GLN A 60 28.103 25.840 64.274 1.00 43.43 C ANISOU 459 CB GLN E 60 4704 6522 5274 -49 1679 279 C ATOM 460 CG GLN A 60 27.047 25.031 63.533 1.00 49.81 C ANISOU 460 CG GLN E 60 5483 7271 6171 -728 312 1074 C ATOM 461 CD GLN A 60 27.269 25.072 62.032 1.00 56.33 C ANISOU 461 CD GLN E 60 6998 8291 6113 -1600 309 1365 C ATOM 462 OE1 GLN A 60 28.380 24.852 61.552 1.00 64.84 O ANISOU 462 OE1 GLN E 60 8153 10132 6352 -3034 1176 828 O ATOM 463 NE2 GLN A 60 26.250 25.362 61.238 1.00 65.00 N ANISOU 463 NE2 GLN E 60 7738 10357 6604 -1472 135 -715 N ATOM 464 N VAL A 61 28.667 28.172 66.726 1.00 40.33 N ANISOU 464 N VAL E 61 4988 4883 5451 458 1903 -213 N ATOM 465 CA VAL A 61 29.741 28.997 67.274 1.00 38.51 C ANISOU 465 CA VAL E 61 4772 5192 4668 108 1718 -6 C ATOM 466 C VAL A 61 29.160 30.130 68.109 1.00 38.79 C ANISOU 466 C VAL E 61 4662 5459 4616 53 1839 17 C ATOM 467 O VAL A 61 28.096 30.695 67.873 1.00 38.01 O ANISOU 467 O VAL E 61 5177 5154 4111 -178 1776 -439 O ATOM 468 CB VAL A 61 30.619 29.545 66.130 1.00 35.87 C ANISOU 468 CB VAL E 61 3459 5851 4319 38 1149 136 C ATOM 469 CG1 VAL A 61 29.848 30.552 65.284 1.00 34.05 C ANISOU 469 CG1 VAL E 61 3899 4739 4300 -57 1588 390 C ATOM 470 CG2 VAL A 61 31.905 30.211 66.615 1.00 38.36 C ANISOU 470 CG2 VAL E 61 4114 5000 5463 207 905 784 C ATOM 471 N SER A 62 29.899 30.494 69.145 1.00 37.71 N ANISOU 471 N SER E 62 5016 5335 3977 -210 1931 -311 N ATOM 472 CA SER A 62 29.529 31.644 69.955 1.00 37.37 C ANISOU 472 CA SER E 62 5117 5136 3946 -253 1835 -455 C ATOM 473 C SER A 62 30.674 32.655 69.983 1.00 36.60 C ANISOU 473 C SER E 62 4929 5187 3790 -330 1269 -663 C ATOM 474 O SER A 62 31.839 32.242 70.060 1.00 36.49 O ANISOU 474 O SER E 62 5074 5273 3517 -543 949 191 O ATOM 475 CB SER A 62 29.156 31.179 71.365 1.00 38.05 C ANISOU 475 CB SER E 62 5419 5105 3934 -500 1942 -461 C ATOM 476 OG SER A 62 28.835 32.321 72.137 1.00 39.31 O ANISOU 476 OG SER E 62 5994 5146 3794 -33 1566 -189 O ATOM 477 N PHE A 63 30.351 33.939 69.929 1.00 34.91 N ANISOU 477 N PHE E 63 4813 5129 3321 -286 441 -70 N ATOM 478 CA PHE A 63 31.371 34.976 69.997 1.00 36.39 C ANISOU 478 CA PHE E 63 4612 5181 4035 -376 400 135 C ATOM 479 C PHE A 63 31.421 35.649 71.368 1.00 36.50 C ANISOU 479 C PHE E 63 4735 4958 4175 -34 786 186 C ATOM 480 O PHE A 63 32.073 36.699 71.474 1.00 38.39 O ANISOU 480 O PHE E 63 5144 4391 5052 -390 1827 750 O ATOM 481 CB PHE A 63 31.115 36.008 68.891 1.00 36.21 C ANISOU 481 CB PHE E 63 4572 4909 4277 -185 524 46 C ATOM 482 CG PHE A 63 31.303 35.346 67.519 1.00 36.61 C ANISOU 482 CG PHE E 63 4825 4951 4133 -434 306 -78 C ATOM 483 CD1 PHE A 63 32.562 35.147 66.984 1.00 36.87 C ANISOU 483 CD1 PHE E 63 5009 5238 3761 -73 617 -241 C ATOM 484 CD2 PHE A 63 30.203 34.928 66.799 1.00 37.65 C ANISOU 484 CD2 PHE E 63 5038 4681 4585 -129 290 152 C ATOM 485 CE1 PHE A 63 32.774 34.527 65.762 1.00 33.38 C ANISOU 485 CE1 PHE E 63 4701 4616 3368 641 566 -647 C ATOM 486 CE2 PHE A 63 30.378 34.316 65.585 1.00 35.30 C ANISOU 486 CE2 PHE E 63 4691 4592 4131 692 760 -337 C ATOM 487 CZ PHE A 63 31.649 34.122 65.065 1.00 35.04 C ANISOU 487 CZ PHE E 63 4500 4689 4124 616 532 -552 C ATOM 488 N LYS A 64 30.775 35.079 72.374 1.00 38.20 N ANISOU 488 N LYS E 64 5030 5353 4130 -38 730 -177 N ATOM 489 CA LYS A 64 30.751 35.598 73.731 1.00 40.02 C ANISOU 489 CA LYS E 64 5502 5507 4198 300 823 -81 C ATOM 490 C LYS A 64 32.139 35.872 74.300 1.00 37.29 C ANISOU 490 C LYS E 64 5325 4801 4043 -159 918 157 C ATOM 491 O LYS A 64 32.356 36.853 75.003 1.00 38.94 O ANISOU 491 O LYS E 64 5244 5721 3830 -406 1042 819 O ATOM 492 CB LYS A 64 30.091 34.582 74.676 1.00 46.94 C ANISOU 492 CB LYS E 64 5209 7329 5298 -39 2426 -724 C ATOM 493 CG LYS A 64 28.915 35.088 75.481 1.00 63.62 C ANISOU 493 CG LYS E 64 6935 9358 7882 -2352 3791 -1694 C ATOM 494 CD LYS A 64 27.762 35.503 74.577 1.00 78.52 C ANISOU 494 CD LYS E 64 7690 11352 10791 -3655 2791 -1979 C ATOM 495 CE LYS A 64 26.434 35.566 75.315 1.00 84.39 C ANISOU 495 CE LYS E 64 7679 12216 12171 -4131 3197 -2918 C ATOM 496 NZ LYS A 64 25.769 36.896 75.142 1.00 86.17 N ANISOU 496 NZ LYS E 64 6178 12119 14443 -3347 2915 -3978 N ATOM 497 N HIS A 65 33.095 34.981 74.010 1.00 36.57 N ANISOU 497 N HIS E 65 5551 4340 4002 -26 1786 -468 N ATOM 498 CA HIS A 65 34.455 35.211 74.505 1.00 38.83 C ANISOU 498 CA HIS E 65 5328 5346 4082 -462 1852 -408 C ATOM 499 C HIS A 65 35.438 35.346 73.349 1.00 38.25 C ANISOU 499 C HIS E 65 5120 5684 3728 -1069 1583 -694 C ATOM 500 O HIS A 65 36.579 34.876 73.381 1.00 41.41 O ANISOU 500 O HIS E 65 5806 6432 3494 -2087 1577 86 O ATOM 501 CB HIS A 65 34.884 34.100 75.476 1.00 40.34 C ANISOU 501 CB HIS E 65 5878 5839 3610 -755 1960 -446 C ATOM 502 CG HIS A 65 33.906 34.068 76.628 1.00 40.80 C ANISOU 502 CG HIS E 65 5719 5801 3983 -378 2110 -308 C ATOM 503 ND1 HIS A 65 33.616 35.206 77.347 1.00 43.19 N ANISOU 503 ND1 HIS E 65 6066 5694 4649 -380 2888 -350 N ATOM 504 CD2 HIS A 65 33.155 33.090 77.161 1.00 40.00 C ANISOU 504 CD2 HIS E 65 5536 5771 3890 -317 1611 -476 C ATOM 505 CE1 HIS A 65 32.733 34.931 78.292 1.00 42.44 C ANISOU 505 CE1 HIS E 65 5471 5790 4863 -448 2721 -458 C ATOM 506 NE2 HIS A 65 32.434 33.648 78.201 1.00 41.61 N ANISOU 506 NE2 HIS E 65 5402 5891 4518 -294 2141 -579 N ATOM 507 N VAL A 66 34.983 36.010 72.290 1.00 37.49 N ANISOU 507 N VAL E 66 5759 5103 3382 -1048 1137 -45 N ATOM 508 CA VAL A 66 35.844 36.319 71.149 1.00 32.58 C ANISOU 508 CA VAL E 66 4729 4641 3010 -406 319 -29 C ATOM 509 C VAL A 66 36.105 37.823 71.196 1.00 33.64 C ANISOU 509 C VAL E 66 4180 4617 3983 -624 -195 260 C ATOM 510 O VAL A 66 35.173 38.615 71.330 1.00 33.70 O ANISOU 510 O VAL E 66 4237 4861 3709 -609 849 178 O ATOM 511 CB VAL A 66 35.247 35.890 69.801 1.00 30.79 C ANISOU 511 CB VAL E 66 3995 4534 3171 -53 257 -274 C ATOM 512 CG1 VAL A 66 36.116 36.402 68.664 1.00 28.54 C ANISOU 512 CG1 VAL E 66 3481 4398 2965 -354 114 -163 C ATOM 513 CG2 VAL A 66 35.129 34.375 69.744 1.00 30.17 C ANISOU 513 CG2 VAL E 66 4545 4483 2433 -485 1011 -15 C ATOM 514 N VAL A 67 37.369 38.193 71.113 1.00 31.87 N ANISOU 514 N VAL E 67 4128 4521 3461 -709 -113 361 N ATOM 515 CA VAL A 67 37.760 39.602 71.088 1.00 30.76 C ANISOU 515 CA VAL E 67 4351 4529 2807 -642 557 496 C ATOM 516 C VAL A 67 38.185 39.919 69.667 1.00 32.92 C ANISOU 516 C VAL E 67 5272 4611 2623 -1317 528 447 C ATOM 517 O VAL A 67 38.867 39.079 69.092 1.00 30.50 O ANISOU 517 O VAL E 67 4243 4471 2876 -943 593 329 O ATOM 518 CB VAL A 67 38.905 39.881 72.076 1.00 29.57 C ANISOU 518 CB VAL E 67 4338 4257 2639 -267 644 21 C ATOM 519 CG1 VAL A 67 39.631 41.185 71.798 1.00 30.25 C ANISOU 519 CG1 VAL E 67 3849 4230 3417 -556 1119 -73 C ATOM 520 CG2 VAL A 67 38.344 39.840 73.507 1.00 30.09 C ANISOU 520 CG2 VAL E 67 4433 4375 2624 -348 692 -66 C ATOM 521 N THR A 68 37.793 41.063 69.128 1.00 28.03 N ANISOU 521 N THR E 68 3537 4225 2890 -529 249 556 N ATOM 522 CA THR A 68 38.167 41.383 67.768 1.00 29.02 C ANISOU 522 CA THR E 68 3571 4427 3030 -384 231 247 C ATOM 523 C THR A 68 38.900 42.721 67.675 1.00 30.37 C ANISOU 523 C THR E 68 3931 4335 3271 -363 415 481 C ATOM 524 O THR A 68 38.632 43.620 68.472 1.00 30.55 O ANISOU 524 O THR E 68 3681 5014 2912 -8 120 888 O ATOM 525 CB THR A 68 36.946 41.466 66.823 1.00 29.30 C ANISOU 525 CB THR E 68 3836 4069 3229 -676 13 152 C ATOM 526 OG1 THR A 68 36.095 42.535 67.284 1.00 32.78 O ANISOU 526 OG1 THR E 68 4298 4521 3636 -1125 476 -23 O ATOM 527 CG2 THR A 68 36.112 40.200 66.823 1.00 29.46 C ANISOU 527 CG2 THR E 68 3888 4619 2685 -190 116 216 C ATOM 528 N PHE A 69 39.773 42.808 66.675 1.00 26.17 N ANISOU 528 N PHE E 69 3142 3973 2828 -405 -171 461 N ATOM 529 CA PHE A 69 40.527 43.982 66.283 1.00 28.36 C ANISOU 529 CA PHE E 69 4053 3805 2918 -327 39 377 C ATOM 530 C PHE A 69 40.337 44.204 64.789 1.00 28.95 C ANISOU 530 C PHE E 69 4260 3775 2963 -296 -115 416 C ATOM 531 O PHE A 69 40.640 43.280 63.999 1.00 28.25 O ANISOU 531 O PHE E 69 3897 3916 2922 -395 166 336 O ATOM 532 CB PHE A 69 42.014 43.812 66.590 1.00 27.11 C ANISOU 532 CB PHE E 69 3946 3445 2910 366 -37 248 C ATOM 533 CG PHE A 69 42.348 43.930 68.074 1.00 29.98 C ANISOU 533 CG PHE E 69 4332 4143 2916 -201 -101 390 C ATOM 534 CD1 PHE A 69 42.452 42.812 68.885 1.00 28.94 C ANISOU 534 CD1 PHE E 69 3373 4621 3001 -218 45 10 C ATOM 535 CD2 PHE A 69 42.558 45.180 68.652 1.00 29.05 C ANISOU 535 CD2 PHE E 69 3395 4491 3153 -163 -363 721 C ATOM 536 CE1 PHE A 69 42.748 42.951 70.243 1.00 32.19 C ANISOU 536 CE1 PHE E 69 4194 4791 3244 -637 -524 139 C ATOM 537 CE2 PHE A 69 42.850 45.326 70.010 1.00 29.75 C ANISOU 537 CE2 PHE E 69 3479 4711 3115 -454 -360 666 C ATOM 538 CZ PHE A 69 42.947 44.197 70.813 1.00 30.71 C ANISOU 538 CZ PHE E 69 3704 4962 3002 -824 566 495 C ATOM 539 N ASN A 70 39.855 45.374 64.389 1.00 30.06 N ANISOU 539 N ASN E 70 4586 4001 2834 -680 375 281 N ATOM 540 CA ASN A 70 39.715 45.642 62.950 1.00 29.07 C ANISOU 540 CA ASN E 70 4588 3587 2872 -24 68 333 C ATOM 541 C ASN A 70 40.967 46.311 62.394 1.00 29.49 C ANISOU 541 C ASN E 70 4517 3953 2734 -58 233 569 C ATOM 542 O ASN A 70 41.693 47.008 63.115 1.00 31.09 O ANISOU 542 O ASN E 70 3473 5192 3147 -294 65 920 O ATOM 543 CB ASN A 70 38.484 46.511 62.710 1.00 29.68 C ANISOU 543 CB ASN E 70 4644 4010 2622 -236 660 -339 C ATOM 544 CG ASN A 70 37.335 45.656 62.218 1.00 30.70 C ANISOU 544 CG ASN E 70 4485 4351 2830 -322 261 -659 C ATOM 545 OD1 ASN A 70 36.687 44.981 63.020 1.00 29.40 O ANISOU 545 OD1 ASN E 70 3944 4144 3082 -610 749 -266 O ATOM 546 ND2 ASN A 70 37.086 45.688 60.904 1.00 31.69 N ANISOU 546 ND2 ASN E 70 4365 4965 2709 -885 503 -33 N ATOM 547 N MET A 71 41.248 46.124 61.115 1.00 30.26 N ANISOU 547 N MET E 71 4718 4257 2522 -619 19 126 N ATOM 548 CA MET A 71 42.457 46.614 60.475 1.00 35.32 C ANISOU 548 CA MET E 71 5264 4956 3202 -786 731 -453 C ATOM 549 C MET A 71 42.520 48.134 60.356 1.00 33.84 C ANISOU 549 C MET E 71 4434 4942 3480 -273 159 -110 C ATOM 550 O MET A 71 43.611 48.709 60.419 1.00 34.08 O ANISOU 550 O MET E 71 4080 5334 3533 -667 -539 991 O ATOM 551 CB MET A 71 42.603 46.037 59.041 1.00 33.33 C ANISOU 551 CB MET E 71 4725 4761 3178 347 567 -368 C ATOM 552 CG MET A 71 42.847 44.548 58.968 1.00 39.27 C ANISOU 552 CG MET E 71 5876 5010 4034 -447 1789 -208 C ATOM 553 SD MET A 71 43.422 43.952 57.359 1.00 43.40 S ANISOU 553 SD MET E 71 6840 5791 3859 -207 1793 -100 S ATOM 554 CE MET A 71 42.709 45.200 56.280 1.00 41.95 C ANISOU 554 CE MET E 71 7854 4657 3430 -390 565 1391 C ATOM 555 N ASP A 72 41.364 48.784 60.142 1.00 27.73 N ANISOU 555 N ASP E 72 3999 3840 2697 424 -414 894 N ATOM 556 CA ASP A 72 41.439 50.205 59.844 1.00 33.08 C ANISOU 556 CA ASP E 72 4116 4226 4227 316 867 -224 C ATOM 557 C ASP A 72 40.126 50.955 60.054 1.00 34.95 C ANISOU 557 C ASP E 72 4227 4434 4617 -87 -49 -111 C ATOM 558 O ASP A 72 39.091 50.351 60.360 1.00 34.87 O ANISOU 558 O ASP E 72 4536 4410 4302 -599 1563 41 O ATOM 559 CB ASP A 72 41.915 50.346 58.397 1.00 44.06 C ANISOU 559 CB ASP E 72 8100 4460 4179 -904 1573 -158 C ATOM 560 CG ASP A 72 41.375 49.312 57.436 1.00 45.45 C ANISOU 560 CG ASP E 72 7717 5146 4405 -817 1610 227 C ATOM 561 OD1 ASP A 72 40.228 48.825 57.589 1.00 53.37 O ANISOU 561 OD1 ASP E 72 7062 6641 6577 -863 359 -146 O ATOM 562 OD2 ASP A 72 42.107 48.972 56.487 1.00 51.96 O ANISOU 562 OD2 ASP E 72 9349 5745 4650 -1909 1927 489 O ATOM 563 N GLU A 73 40.196 52.279 59.893 1.00 36.89 N ANISOU 563 N GLU E 73 5316 4442 4257 -233 830 -91 N ATOM 564 CA GLU A 73 39.077 53.210 59.991 1.00 39.23 C ANISOU 564 CA GLU E 73 6067 4619 4219 -758 722 -146 C ATOM 565 C GLU A 73 39.425 54.534 59.311 1.00 37.56 C ANISOU 565 C GLU E 73 5713 4623 3935 -492 333 21 C ATOM 566 O GLU A 73 40.582 54.970 59.269 1.00 40.77 O ANISOU 566 O GLU E 73 5444 5701 4344 -700 972 -594 O ATOM 567 CB GLU A 73 38.670 53.423 61.454 1.00 34.97 C ANISOU 567 CB GLU E 73 4785 4198 4304 107 553 228 C ATOM 568 CG GLU A 73 37.450 54.298 61.691 1.00 42.01 C ANISOU 568 CG GLU E 73 5410 5682 4869 -845 554 426 C ATOM 569 CD GLU A 73 36.157 53.803 61.046 1.00 41.86 C ANISOU 569 CD GLU E 73 5233 6069 4603 -1168 280 -224 C ATOM 570 OE1 GLU A 73 36.007 54.017 59.814 1.00 39.20 O ANISOU 570 OE1 GLU E 73 4960 5439 4493 -1399 763 -263 O ATOM 571 OE2 GLU A 73 35.319 53.220 61.806 1.00 38.00 O ANISOU 571 OE2 GLU E 73 4982 6112 3345 -1143 204 643 O ATOM 572 N TYR A 74 38.395 55.183 58.753 1.00 37.36 N ANISOU 572 N TYR E 74 5673 4875 3647 -565 541 -202 N ATOM 573 CA TYR A 74 38.578 56.509 58.184 1.00 41.28 C ANISOU 573 CA TYR E 74 5667 5053 4964 -481 541 -711 C ATOM 574 C TYR A 74 38.790 57.559 59.266 1.00 41.19 C ANISOU 574 C TYR E 74 5495 4709 5448 -293 751 -648 C ATOM 575 O TYR A 74 38.185 57.522 60.351 1.00 39.71 O ANISOU 575 O TYR E 74 5055 4567 5465 -126 667 -328 O ATOM 576 CB TYR A 74 37.369 56.947 57.369 1.00 41.08 C ANISOU 576 CB TYR E 74 5489 4886 5233 -454 679 -990 C ATOM 577 CG TYR A 74 37.236 56.265 56.032 1.00 43.17 C ANISOU 577 CG TYR E 74 6067 5477 4860 -1198 336 -1187 C ATOM 578 CD1 TYR A 74 38.216 56.345 55.059 1.00 45.76 C ANISOU 578 CD1 TYR E 74 6685 5643 5060 -1237 755 -1295 C ATOM 579 CD2 TYR A 74 36.092 55.526 55.755 1.00 43.30 C ANISOU 579 CD2 TYR E 74 5970 6098 4385 -1347 42 -628 C ATOM 580 CE1 TYR A 74 38.038 55.697 53.850 1.00 50.27 C ANISOU 580 CE1 TYR E 74 7361 6441 5297 -1381 916 -798 C ATOM 581 CE2 TYR A 74 35.908 54.879 54.553 1.00 46.74 C ANISOU 581 CE2 TYR E 74 6844 6625 4291 -1476 254 -474 C ATOM 582 CZ TYR A 74 36.895 54.967 53.592 1.00 50.91 C ANISOU 582 CZ TYR E 74 7258 7085 5001 -1429 845 -134 C ATOM 583 OH TYR A 74 36.716 54.322 52.383 1.00 55.75 O ANISOU 583 OH TYR E 74 8276 8611 4294 -813 895 -463 O ATOM 584 N VAL A 75 39.660 58.506 58.937 1.00 42.13 N ANISOU 584 N VAL E 75 4919 5224 5863 -261 738 -759 N ATOM 585 CA VAL A 75 39.917 59.617 59.857 1.00 47.19 C ANISOU 585 CA VAL E 75 5788 5097 7045 -33 166 -493 C ATOM 586 C VAL A 75 38.892 60.723 59.608 1.00 48.55 C ANISOU 586 C VAL E 75 6285 5224 6940 -454 735 -542 C ATOM 587 O VAL A 75 38.639 61.002 58.425 1.00 48.47 O ANISOU 587 O VAL E 75 5693 5860 6862 -1170 726 -226 O ATOM 588 CB VAL A 75 41.347 60.161 59.681 1.00 48.86 C ANISOU 588 CB VAL E 75 6013 5205 7348 131 647 -104 C ATOM 589 CG1 VAL A 75 41.467 61.547 60.307 1.00 53.29 C ANISOU 589 CG1 VAL E 75 6667 5126 8455 481 1334 91 C ATOM 590 CG2 VAL A 75 42.397 59.213 60.259 1.00 43.92 C ANISOU 590 CG2 VAL E 75 5319 5653 5715 67 1547 -167 C ATOM 591 N GLY A 76 38.318 61.313 60.642 1.00 50.75 N ANISOU 591 N GLY E 76 7221 5344 6717 -516 356 -120 N ATOM 592 CA GLY A 76 37.418 62.447 60.590 1.00 50.36 C ANISOU 592 CA GLY E 76 6827 5542 6765 -498 1207 -437 C ATOM 593 C GLY A 76 36.017 62.157 60.109 1.00 52.70 C ANISOU 593 C GLY E 76 6657 6001 7365 -559 1338 -104 C ATOM 594 O GLY A 76 35.169 63.027 59.887 1.00 53.35 O ANISOU 594 O GLY E 76 6451 6305 7513 -727 1657 -39 O ATOM 595 N LEU A 77 35.698 60.885 59.910 1.00 51.62 N ANISOU 595 N LEU E 77 6184 6058 7372 -182 2057 -442 N ATOM 596 CA LEU A 77 34.350 60.516 59.482 1.00 51.42 C ANISOU 596 CA LEU E 77 6268 6170 7100 -353 1735 -602 C ATOM 597 C LEU A 77 33.565 60.225 60.747 1.00 48.97 C ANISOU 597 C LEU E 77 5514 6321 6772 -359 1217 -704 C ATOM 598 O LEU A 77 34.128 59.512 61.592 1.00 53.77 O ANISOU 598 O LEU E 77 7868 6544 6016 -2227 1383 112 O ATOM 599 CB LEU A 77 34.451 59.308 58.577 1.00 52.44 C ANISOU 599 CB LEU E 77 7136 6167 6620 -351 1335 -752 C ATOM 600 CG LEU A 77 33.539 59.150 57.372 1.00 54.52 C ANISOU 600 CG LEU E 77 7227 5709 7779 133 600 -1018 C ATOM 601 CD1 LEU A 77 32.809 57.813 57.447 1.00 54.85 C ANISOU 601 CD1 LEU E 77 5875 7127 7838 795 1700 -2120 C ATOM 602 CD2 LEU A 77 32.544 60.290 57.258 1.00 59.94 C ANISOU 602 CD2 LEU E 77 7100 6902 8774 -680 -44 781 C ATOM 603 N PRO A 78 32.354 60.725 60.948 1.00 49.97 N ANISOU 603 N PRO E 78 5464 6640 6884 -337 1061 -178 N ATOM 604 CA PRO A 78 31.622 60.348 62.174 1.00 51.66 C ANISOU 604 CA PRO E 78 5460 6928 7242 -311 1309 -262 C ATOM 605 C PRO A 78 31.381 58.839 62.235 1.00 48.74 C ANISOU 605 C PRO E 78 5262 6812 6445 -642 1623 -73 C ATOM 606 O PRO A 78 30.964 58.261 61.226 1.00 51.65 O ANISOU 606 O PRO E 78 6508 6970 6146 -1049 2070 410 O ATOM 607 CB PRO A 78 30.302 61.100 62.039 1.00 54.45 C ANISOU 607 CB PRO E 78 6132 6946 7612 -961 1705 -379 C ATOM 608 CG PRO A 78 30.564 62.192 61.058 1.00 52.18 C ANISOU 608 CG PRO E 78 5589 6980 7258 -538 1438 -211 C ATOM 609 CD PRO A 78 31.595 61.659 60.104 1.00 49.69 C ANISOU 609 CD PRO E 78 5322 6615 6941 -498 978 73 C ATOM 610 N LYS A 79 31.625 58.195 63.368 1.00 48.19 N ANISOU 610 N LYS E 79 5083 7123 6104 -876 2386 -94 N ATOM 611 CA LYS A 79 31.441 56.757 63.510 1.00 54.40 C ANISOU 611 CA LYS E 79 7407 6964 6298 -1288 1942 -134 C ATOM 612 C LYS A 79 30.085 56.284 62.999 1.00 53.90 C ANISOU 612 C LYS E 79 7398 6095 6984 -536 2690 4 C ATOM 613 O LYS A 79 29.974 55.240 62.345 1.00 58.96 O ANISOU 613 O LYS E 79 8627 5807 7968 -892 2034 91 O ATOM 614 CB LYS A 79 31.598 56.340 64.976 1.00 64.52 C ANISOU 614 CB LYS E 79 10277 7584 6653 -3394 1702 -620 C ATOM 615 CG LYS A 79 33.022 56.018 65.399 1.00 81.09 C ANISOU 615 CG LYS E 79 12443 9681 8687 -6045 205 -51 C ATOM 616 CD LYS A 79 33.046 55.157 66.663 1.00 94.67 C ANISOU 616 CD LYS E 79 16385 10464 9120 -7758 -149 -552 C ATOM 617 CE LYS A 79 34.459 54.704 67.015 1.00100.31 C ANISOU 617 CE LYS E 79 17239 10681 10196 -8238 -1562 180 C ATOM 618 NZ LYS A 79 34.583 53.263 67.404 1.00 99.23 N ANISOU 618 NZ LYS E 79 16487 9198 12017 -7898 -3093 3219 N ATOM 619 N GLU A 80 29.012 57.018 63.274 1.00 55.66 N ANISOU 619 N GLU E 80 7175 6753 7220 -583 2365 620 N ATOM 620 CA GLU A 80 27.696 56.592 62.803 1.00 59.52 C ANISOU 620 CA GLU E 80 7348 7740 7526 -424 2377 1678 C ATOM 621 C GLU A 80 27.472 56.896 61.328 1.00 58.33 C ANISOU 621 C GLU E 80 7538 6988 7636 -723 2023 1750 C ATOM 622 O GLU A 80 26.386 56.605 60.810 1.00 60.27 O ANISOU 622 O GLU E 80 7470 6869 8561 -1035 1553 1201 O ATOM 623 CB GLU A 80 26.547 57.224 63.605 1.00 68.18 C ANISOU 623 CB GLU E 80 7326 10033 8545 -363 3156 1880 C ATOM 624 CG GLU A 80 25.714 56.191 64.355 1.00 79.36 C ANISOU 624 CG GLU E 80 8602 11058 10492 -46 4197 1108 C ATOM 625 CD GLU A 80 24.331 55.896 63.814 1.00 85.38 C ANISOU 625 CD GLU E 80 8638 11323 12480 946 4294 1367 C ATOM 626 OE1 GLU A 80 23.319 56.114 64.536 1.00 99.94 O ANISOU 626 OE1 GLU E 80 8592 11873 17506 -1411 5570 441 O ATOM 627 OE2 GLU A 80 24.227 55.427 62.653 1.00102.82 O ANISOU 627 OE2 GLU E 80 12178 12381 14509 1275 2104 3815 O ATOM 628 N HIS A 81 28.430 57.462 60.603 1.00 57.52 N ANISOU 628 N HIS E 81 7404 6948 7504 -1180 1928 1251 N ATOM 629 CA HIS A 81 28.226 57.509 59.146 1.00 55.43 C ANISOU 629 CA HIS E 81 5668 7555 7838 -647 972 401 C ATOM 630 C HIS A 81 28.091 56.072 58.659 1.00 51.01 C ANISOU 630 C HIS E 81 5461 7634 6288 -559 567 149 C ATOM 631 O HIS A 81 28.805 55.158 59.083 1.00 45.52 O ANISOU 631 O HIS E 81 5018 7368 4909 -184 648 374 O ATOM 632 CB HIS A 81 29.372 58.250 58.463 1.00 57.02 C ANISOU 632 CB HIS E 81 6080 7270 8314 -800 939 -523 C ATOM 633 CG HIS A 81 29.231 58.370 56.978 1.00 60.06 C ANISOU 633 CG HIS E 81 6354 8163 8302 -1518 1174 -661 C ATOM 634 ND1 HIS A 81 28.926 59.569 56.362 1.00 61.95 N ANISOU 634 ND1 HIS E 81 6815 8307 8417 -1426 1148 -885 N ATOM 635 CD2 HIS A 81 29.331 57.492 55.962 1.00 60.36 C ANISOU 635 CD2 HIS E 81 6050 8619 8265 -1854 520 -442 C ATOM 636 CE1 HIS A 81 28.853 59.406 55.048 1.00 62.89 C ANISOU 636 CE1 HIS E 81 6559 8713 8624 -1590 -243 -604 C ATOM 637 NE2 HIS A 81 29.099 58.133 54.773 1.00 62.21 N ANISOU 637 NE2 HIS E 81 6300 8795 8540 -1619 -512 -427 N ATOM 638 N PRO A 82 27.181 55.772 57.748 1.00 54.15 N ANISOU 638 N PRO E 82 6012 8050 6511 -1228 -93 49 N ATOM 639 CA PRO A 82 26.955 54.384 57.352 1.00 54.66 C ANISOU 639 CA PRO E 82 6053 8363 6353 -1964 -1118 871 C ATOM 640 C PRO A 82 28.132 53.730 56.626 1.00 58.22 C ANISOU 640 C PRO E 82 6080 9549 6492 -2448 -1232 928 C ATOM 641 O PRO A 82 28.174 52.494 56.538 1.00 65.27 O ANISOU 641 O PRO E 82 6657 9514 8628 -3346 -253 386 O ATOM 642 CB PRO A 82 25.786 54.490 56.366 1.00 57.60 C ANISOU 642 CB PRO E 82 6202 8897 6785 -2495 -1300 694 C ATOM 643 CG PRO A 82 25.169 55.821 56.631 1.00 61.64 C ANISOU 643 CG PRO E 82 7485 8655 7281 -2687 -1574 473 C ATOM 644 CD PRO A 82 26.310 56.720 57.047 1.00 61.44 C ANISOU 644 CD PRO E 82 7545 8452 7347 -2048 -486 -22 C ATOM 645 N GLU A 83 29.056 54.523 56.111 1.00 60.08 N ANISOU 645 N GLU E 83 6911 10136 5779 -2649 -491 346 N ATOM 646 CA GLU A 83 30.240 54.077 55.397 1.00 58.75 C ANISOU 646 CA GLU E 83 7323 9833 5165 -2875 -527 401 C ATOM 647 C GLU A 83 31.474 54.024 56.283 1.00 49.36 C ANISOU 647 C GLU E 83 6323 7416 5015 -1136 126 106 C ATOM 648 O GLU A 83 32.563 53.625 55.854 1.00 47.67 O ANISOU 648 O GLU E 83 6268 7574 4270 -680 229 332 O ATOM 649 CB GLU A 83 30.524 54.980 54.194 1.00 72.69 C ANISOU 649 CB GLU E 83 9982 12292 5346 -5237 740 -929 C ATOM 650 CG GLU A 83 29.614 54.709 53.004 1.00 77.05 C ANISOU 650 CG GLU E 83 10408 13710 5159 -4911 703 -1110 C ATOM 651 CD GLU A 83 29.232 53.248 52.861 1.00 80.81 C ANISOU 651 CD GLU E 83 10734 13895 6074 -4907 -9 -221 C ATOM 652 OE1 GLU A 83 30.112 52.362 52.803 1.00 89.49 O ANISOU 652 OE1 GLU E 83 13427 14399 6175 -6529 -398 -45 O ATOM 653 OE2 GLU A 83 28.011 52.963 52.797 1.00 90.04 O ANISOU 653 OE2 GLU E 83 11351 16138 6721 -3189 509 -996 O ATOM 654 N SER A 84 31.388 54.393 57.550 1.00 40.77 N ANISOU 654 N SER E 84 4873 5560 5057 -332 490 -137 N ATOM 655 CA SER A 84 32.521 54.157 58.443 1.00 39.95 C ANISOU 655 CA SER E 84 4506 6067 4608 -437 974 -437 C ATOM 656 C SER A 84 32.777 52.662 58.537 1.00 40.12 C ANISOU 656 C SER E 84 4629 6113 4502 -706 506 137 C ATOM 657 O SER A 84 31.887 51.858 58.225 1.00 39.83 O ANISOU 657 O SER E 84 4325 5873 4937 -1163 135 309 O ATOM 658 CB SER A 84 32.228 54.720 59.831 1.00 36.56 C ANISOU 658 CB SER E 84 3963 5194 4736 -166 963 -458 C ATOM 659 OG SER A 84 31.221 53.959 60.479 1.00 34.84 O ANISOU 659 OG SER E 84 4221 4760 4256 -13 543 -616 O ATOM 660 N TYR A 85 33.979 52.277 58.967 1.00 36.91 N ANISOU 660 N TYR E 85 4557 5925 3540 -512 460 563 N ATOM 661 CA TYR A 85 34.211 50.832 59.084 1.00 38.87 C ANISOU 661 CA TYR E 85 4545 6043 4179 -825 976 304 C ATOM 662 C TYR A 85 33.495 50.297 60.320 1.00 36.56 C ANISOU 662 C TYR E 85 4016 5694 4181 -729 923 584 C ATOM 663 O TYR A 85 33.052 49.143 60.329 1.00 35.47 O ANISOU 663 O TYR E 85 4698 5285 3494 -1150 601 460 O ATOM 664 CB TYR A 85 35.715 50.525 59.063 1.00 41.00 C ANISOU 664 CB TYR E 85 4519 6535 4525 -762 1324 -738 C ATOM 665 CG TYR A 85 36.341 50.723 57.687 1.00 45.44 C ANISOU 665 CG TYR E 85 5347 7087 4830 -1091 1841 -806 C ATOM 666 CD1 TYR A 85 35.531 51.060 56.603 1.00 45.44 C ANISOU 666 CD1 TYR E 85 5931 6893 4440 -1465 2026 -799 C ATOM 667 CD2 TYR A 85 37.693 50.582 57.450 1.00 45.14 C ANISOU 667 CD2 TYR E 85 5301 7010 4841 -551 1953 211 C ATOM 668 CE1 TYR A 85 36.057 51.245 55.351 1.00 45.55 C ANISOU 668 CE1 TYR E 85 5920 6908 4481 -1493 2272 -227 C ATOM 669 CE2 TYR A 85 38.246 50.770 56.202 1.00 45.60 C ANISOU 669 CE2 TYR E 85 5642 6929 4757 -819 2032 397 C ATOM 670 CZ TYR A 85 37.417 51.100 55.166 1.00 46.45 C ANISOU 670 CZ TYR E 85 5882 6851 4915 -1443 2206 28 C ATOM 671 OH TYR A 85 37.920 51.295 53.906 1.00 44.32 O ANISOU 671 OH TYR E 85 5391 6372 5076 -1046 2153 -207 O ATOM 672 N TYR A 86 33.361 51.112 61.370 1.00 34.54 N ANISOU 672 N TYR E 86 3497 5354 4274 -575 813 547 N ATOM 673 CA TYR A 86 32.495 50.799 62.493 1.00 33.41 C ANISOU 673 CA TYR E 86 4260 4623 3814 -451 688 435 C ATOM 674 C TYR A 86 31.134 50.345 61.957 1.00 31.85 C ANISOU 674 C TYR E 86 3948 4639 3515 -459 1061 145 C ATOM 675 O TYR A 86 30.593 49.285 62.322 1.00 35.51 O ANISOU 675 O TYR E 86 3996 5070 4426 -291 1607 -120 O ATOM 676 CB TYR A 86 32.364 52.038 63.372 1.00 36.45 C ANISOU 676 CB TYR E 86 5065 4979 3806 -845 382 679 C ATOM 677 CG TYR A 86 31.206 52.015 64.350 1.00 37.16 C ANISOU 677 CG TYR E 86 5383 4560 4175 -1000 727 667 C ATOM 678 CD1 TYR A 86 31.404 51.452 65.609 1.00 37.49 C ANISOU 678 CD1 TYR E 86 5644 4405 4197 -694 821 588 C ATOM 679 CD2 TYR A 86 29.946 52.543 64.071 1.00 37.27 C ANISOU 679 CD2 TYR E 86 4696 4538 4927 -73 415 567 C ATOM 680 CE1 TYR A 86 30.395 51.401 66.554 1.00 39.99 C ANISOU 680 CE1 TYR E 86 5869 5350 3974 -1235 886 920 C ATOM 681 CE2 TYR A 86 28.929 52.494 65.002 1.00 37.76 C ANISOU 681 CE2 TYR E 86 4554 4612 5179 237 399 437 C ATOM 682 CZ TYR A 86 29.161 51.925 66.239 1.00 41.68 C ANISOU 682 CZ TYR E 86 5611 5481 4744 -869 767 708 C ATOM 683 OH TYR A 86 28.152 51.875 67.177 1.00 41.02 O ANISOU 683 OH TYR E 86 4878 5730 4978 98 398 544 O ATOM 684 N SER A 87 30.551 51.168 61.079 1.00 34.05 N ANISOU 684 N SER E 87 4519 4337 4081 -1045 546 605 N ATOM 685 CA SER A 87 29.192 50.916 60.603 1.00 35.21 C ANISOU 685 CA SER E 87 4647 4861 3871 -770 492 380 C ATOM 686 C SER A 87 29.120 49.650 59.758 1.00 33.45 C ANISOU 686 C SER E 87 4273 4825 3612 -579 739 247 C ATOM 687 O SER A 87 28.186 48.871 59.951 1.00 33.44 O ANISOU 687 O SER E 87 3240 5338 4128 -807 228 544 O ATOM 688 CB SER A 87 28.639 52.097 59.802 1.00 36.43 C ANISOU 688 CB SER E 87 4146 4853 4842 -654 427 102 C ATOM 689 OG SER A 87 28.345 53.163 60.698 1.00 40.72 O ANISOU 689 OG SER E 87 5011 5327 5135 -1476 -398 470 O ATOM 690 N PHE A 88 30.089 49.497 58.856 1.00 33.41 N ANISOU 690 N PHE E 88 3834 4886 3972 -1075 640 82 N ATOM 691 CA PHE A 88 30.197 48.277 58.077 1.00 30.53 C ANISOU 691 CA PHE E 88 3381 4744 3476 -631 655 -81 C ATOM 692 C PHE A 88 30.193 47.089 59.032 1.00 27.74 C ANISOU 692 C PHE E 88 2666 4843 3031 -313 829 50 C ATOM 693 O PHE A 88 29.490 46.114 58.775 1.00 30.41 O ANISOU 693 O PHE E 88 3926 4671 2959 -249 399 384 O ATOM 694 CB PHE A 88 31.487 48.260 57.251 1.00 28.25 C ANISOU 694 CB PHE E 88 3563 3873 3299 -85 756 -130 C ATOM 695 CG PHE A 88 31.751 46.952 56.500 1.00 30.86 C ANISOU 695 CG PHE E 88 3418 4455 3853 -457 419 466 C ATOM 696 CD1 PHE A 88 32.371 45.802 57.009 1.00 31.31 C ANISOU 696 CD1 PHE E 88 4064 4487 3345 -831 875 514 C ATOM 697 CD2 PHE A 88 31.324 46.907 55.176 1.00 32.13 C ANISOU 697 CD2 PHE E 88 3623 4395 4192 -326 -162 629 C ATOM 698 CE1 PHE A 88 32.522 44.658 56.257 1.00 36.09 C ANISOU 698 CE1 PHE E 88 4567 5131 4015 -1525 -609 1295 C ATOM 699 CE2 PHE A 88 31.491 45.774 54.414 1.00 31.90 C ANISOU 699 CE2 PHE E 88 3708 4616 3796 -736 341 500 C ATOM 700 CZ PHE A 88 32.091 44.645 54.931 1.00 33.19 C ANISOU 700 CZ PHE E 88 3783 5050 3779 -1242 -189 845 C ATOM 701 N MET A 89 31.064 47.066 60.042 1.00 29.41 N ANISOU 701 N MET E 89 2935 4876 3362 -421 500 79 N ATOM 702 CA MET A 89 31.278 45.875 60.870 1.00 29.82 C ANISOU 702 CA MET E 89 2897 4849 3585 -631 451 92 C ATOM 703 C MET A 89 30.036 45.510 61.680 1.00 28.85 C ANISOU 703 C MET E 89 3158 4680 3123 -736 546 107 C ATOM 704 O MET A 89 29.718 44.325 61.848 1.00 29.56 O ANISOU 704 O MET E 89 3066 4752 3415 -354 467 598 O ATOM 705 CB MET A 89 32.477 46.053 61.819 1.00 30.13 C ANISOU 705 CB MET E 89 3193 4668 3586 -720 301 308 C ATOM 706 CG MET A 89 33.813 46.029 61.070 1.00 30.03 C ANISOU 706 CG MET E 89 2944 4561 3905 -524 144 731 C ATOM 707 SD MET A 89 34.066 44.446 60.229 1.00 31.40 S ANISOU 707 SD MET E 89 4243 4373 3316 -908 432 245 S ATOM 708 CE MET A 89 33.840 43.300 61.581 1.00 30.87 C ANISOU 708 CE MET E 89 4601 4671 2457 -598 -366 517 C ATOM 709 N HIS A 90 29.329 46.524 62.199 1.00 30.25 N ANISOU 709 N HIS E 90 3395 4865 3233 -852 488 354 N ATOM 710 CA HIS A 90 28.100 46.220 62.937 1.00 31.13 C ANISOU 710 CA HIS E 90 3569 5055 3205 -723 689 800 C ATOM 711 C HIS A 90 27.030 45.678 62.003 1.00 30.39 C ANISOU 711 C HIS E 90 3538 4858 3150 -617 691 477 C ATOM 712 O HIS A 90 26.407 44.635 62.201 1.00 32.67 O ANISOU 712 O HIS E 90 3926 4798 3690 -483 810 703 O ATOM 713 CB HIS A 90 27.629 47.484 63.689 1.00 31.72 C ANISOU 713 CB HIS E 90 3515 5022 3515 -1054 337 785 C ATOM 714 CG HIS A 90 28.505 47.697 64.895 1.00 32.17 C ANISOU 714 CG HIS E 90 4100 4569 3556 -480 217 674 C ATOM 715 ND1 HIS A 90 28.357 46.989 66.071 1.00 29.81 N ANISOU 715 ND1 HIS E 90 3433 4288 3604 -380 177 698 N ATOM 716 CD2 HIS A 90 29.561 48.518 65.112 1.00 33.01 C ANISOU 716 CD2 HIS E 90 4532 4539 3470 -153 107 233 C ATOM 717 CE1 HIS A 90 29.272 47.377 66.951 1.00 28.80 C ANISOU 717 CE1 HIS E 90 3279 3942 3724 65 245 308 C ATOM 718 NE2 HIS A 90 30.017 48.310 66.396 1.00 30.26 N ANISOU 718 NE2 HIS E 90 3720 4212 3567 -19 255 -218 N ATOM 719 N ARG A 91 26.781 46.390 60.913 1.00 33.11 N ANISOU 719 N ARG E 91 4353 4960 3268 -1110 444 493 N ATOM 720 CA ARG A 91 25.744 46.004 59.946 1.00 36.54 C ANISOU 720 CA ARG E 91 4700 5273 3912 -1226 -152 447 C ATOM 721 C ARG A 91 25.961 44.636 59.331 1.00 36.40 C ANISOU 721 C ARG E 91 4322 5316 4192 -652 20 690 C ATOM 722 O ARG A 91 24.987 43.920 59.098 1.00 35.21 O ANISOU 722 O ARG E 91 3853 6253 3272 -721 142 1023 O ATOM 723 CB ARG A 91 25.714 47.067 58.851 1.00 43.09 C ANISOU 723 CB ARG E 91 6615 5891 3866 -2657 -136 202 C ATOM 724 CG ARG A 91 24.997 46.729 57.573 1.00 43.92 C ANISOU 724 CG ARG E 91 6204 5813 4670 -1722 -732 -351 C ATOM 725 CD ARG A 91 24.944 47.976 56.689 1.00 46.77 C ANISOU 725 CD ARG E 91 5724 6840 5208 -1314 -893 -1308 C ATOM 726 NE ARG A 91 26.227 48.386 56.141 1.00 47.83 N ANISOU 726 NE ARG E 91 5608 7281 5286 -1124 -1010 -968 N ATOM 727 CZ ARG A 91 26.872 49.539 56.244 1.00 48.30 C ANISOU 727 CZ ARG E 91 5533 7333 5485 -1133 -564 -607 C ATOM 728 NH1 ARG A 91 26.390 50.568 56.931 1.00 47.57 N ANISOU 728 NH1 ARG E 91 4548 7368 6160 -1242 -543 -593 N ATOM 729 NH2 ARG A 91 28.047 49.639 55.627 1.00 47.84 N ANISOU 729 NH2 ARG E 91 6123 6762 5292 -1219 -18 -561 N ATOM 730 N ASN A 92 27.198 44.246 59.044 1.00 32.32 N ANISOU 730 N ASN E 92 4072 4467 3741 -99 -65 946 N ATOM 731 CA ASN A 92 27.493 42.965 58.396 1.00 30.99 C ANISOU 731 CA ASN E 92 4345 4296 3134 -55 -210 654 C ATOM 732 C ASN A 92 27.835 41.848 59.369 1.00 31.42 C ANISOU 732 C ASN E 92 3701 4645 3593 -93 -208 329 C ATOM 733 O ASN A 92 27.837 40.660 59.015 1.00 32.32 O ANISOU 733 O ASN E 92 4081 4476 3724 -48 596 108 O ATOM 734 CB ASN A 92 28.641 43.144 57.375 1.00 35.51 C ANISOU 734 CB ASN E 92 5302 5141 3048 -289 344 650 C ATOM 735 CG ASN A 92 28.152 43.977 56.206 1.00 38.19 C ANISOU 735 CG ASN E 92 5988 5080 3443 157 113 269 C ATOM 736 OD1 ASN A 92 27.265 43.533 55.472 1.00 43.56 O ANISOU 736 OD1 ASN E 92 7035 5406 4112 539 -878 -301 O ATOM 737 ND2 ASN A 92 28.673 45.173 56.010 1.00 37.21 N ANISOU 737 ND2 ASN E 92 6000 4543 3596 -327 826 925 N ATOM 738 N PHE A 93 28.123 42.158 60.629 1.00 31.32 N ANISOU 738 N PHE E 93 3640 5181 3080 -457 518 137 N ATOM 739 CA PHE A 93 28.509 41.049 61.516 1.00 28.57 C ANISOU 739 CA PHE E 93 3360 4444 3050 -53 634 424 C ATOM 740 C PHE A 93 28.066 41.246 62.955 1.00 29.40 C ANISOU 740 C PHE E 93 3412 4803 2958 61 460 346 C ATOM 741 O PHE A 93 27.308 40.444 63.502 1.00 31.72 O ANISOU 741 O PHE E 93 4734 4118 3201 -208 1108 177 O ATOM 742 CB PHE A 93 30.032 40.924 61.434 1.00 30.39 C ANISOU 742 CB PHE E 93 3405 4753 3391 -284 565 244 C ATOM 743 CG PHE A 93 30.640 39.796 62.243 1.00 31.25 C ANISOU 743 CG PHE E 93 3730 4660 3483 -377 581 243 C ATOM 744 CD1 PHE A 93 30.110 38.515 62.157 1.00 29.95 C ANISOU 744 CD1 PHE E 93 3466 4815 3097 -206 1137 161 C ATOM 745 CD2 PHE A 93 31.733 40.039 63.070 1.00 30.73 C ANISOU 745 CD2 PHE E 93 3209 4834 3633 -91 802 -453 C ATOM 746 CE1 PHE A 93 30.672 37.486 62.884 1.00 31.44 C ANISOU 746 CE1 PHE E 93 3859 4705 3380 -265 1086 121 C ATOM 747 CE2 PHE A 93 32.299 39.013 63.802 1.00 31.69 C ANISOU 747 CE2 PHE E 93 3531 4731 3780 -329 747 -274 C ATOM 748 CZ PHE A 93 31.759 37.742 63.704 1.00 30.27 C ANISOU 748 CZ PHE E 93 3337 4728 3437 -361 1314 -233 C ATOM 749 N PHE A 94 28.541 42.303 63.620 1.00 30.65 N ANISOU 749 N PHE E 94 3692 4745 3207 -184 587 693 N ATOM 750 CA PHE A 94 28.293 42.374 65.058 1.00 30.56 C ANISOU 750 CA PHE E 94 3572 4889 3150 -114 485 514 C ATOM 751 C PHE A 94 26.794 42.472 65.344 1.00 30.65 C ANISOU 751 C PHE E 94 3623 4807 3218 -236 584 160 C ATOM 752 O PHE A 94 26.345 41.893 66.345 1.00 33.71 O ANISOU 752 O PHE E 94 4416 4812 3580 -311 1262 241 O ATOM 753 CB PHE A 94 29.021 43.540 65.716 1.00 30.31 C ANISOU 753 CB PHE E 94 3761 4790 2966 -302 103 374 C ATOM 754 CG PHE A 94 30.526 43.589 65.546 1.00 30.45 C ANISOU 754 CG PHE E 94 3625 4942 3003 -409 -384 421 C ATOM 755 CD1 PHE A 94 31.298 42.444 65.689 1.00 33.40 C ANISOU 755 CD1 PHE E 94 4161 5402 3128 -855 168 -429 C ATOM 756 CD2 PHE A 94 31.152 44.794 65.247 1.00 30.80 C ANISOU 756 CD2 PHE E 94 3484 5250 2967 -482 9 -58 C ATOM 757 CE1 PHE A 94 32.681 42.509 65.535 1.00 33.70 C ANISOU 757 CE1 PHE E 94 4110 5756 2937 -1099 -5 -243 C ATOM 758 CE2 PHE A 94 32.534 44.866 65.096 1.00 31.73 C ANISOU 758 CE2 PHE E 94 3582 5591 2883 -645 582 43 C ATOM 759 CZ PHE A 94 33.295 43.717 65.249 1.00 31.82 C ANISOU 759 CZ PHE E 94 3680 5899 2510 -850 -114 199 C ATOM 760 N ASP A 95 25.984 43.125 64.528 1.00 34.08 N ANISOU 760 N ASP E 95 4049 5597 3304 -634 -44 629 N ATOM 761 CA ASP A 95 24.546 43.207 64.757 1.00 34.35 C ANISOU 761 CA ASP E 95 4079 5311 3660 -767 150 542 C ATOM 762 C ASP A 95 23.893 41.833 64.822 1.00 36.57 C ANISOU 762 C ASP E 95 4287 5317 4292 -783 779 50 C ATOM 763 O ASP A 95 22.773 41.736 65.326 1.00 39.69 O ANISOU 763 O ASP E 95 4476 5756 4849 -983 1093 -549 O ATOM 764 CB ASP A 95 23.828 43.966 63.639 1.00 35.67 C ANISOU 764 CB ASP E 95 3774 5708 4073 -1030 780 -226 C ATOM 765 CG ASP A 95 24.008 45.465 63.667 1.00 34.99 C ANISOU 765 CG ASP E 95 3899 5693 3703 -1159 304 312 C ATOM 766 OD1 ASP A 95 24.640 46.006 64.596 1.00 35.39 O ANISOU 766 OD1 ASP E 95 4277 6282 2888 -1864 648 822 O ATOM 767 OD2 ASP A 95 23.502 46.126 62.734 1.00 33.74 O ANISOU 767 OD2 ASP E 95 4027 5208 3586 -667 131 421 O ATOM 768 N HIS A 96 24.536 40.790 64.317 1.00 36.46 N ANISOU 768 N HIS E 96 4684 5293 3875 -526 734 493 N ATOM 769 CA HIS A 96 23.900 39.485 64.221 1.00 35.36 C ANISOU 769 CA HIS E 96 4348 5461 3624 -367 1275 209 C ATOM 770 C HIS A 96 24.511 38.416 65.101 1.00 35.19 C ANISOU 770 C HIS E 96 4029 5694 3647 -425 1626 -52 C ATOM 771 O HIS A 96 24.037 37.273 65.025 1.00 39.30 O ANISOU 771 O HIS E 96 4650 5773 4509 -187 730 -354 O ATOM 772 CB HIS A 96 23.979 38.995 62.754 1.00 33.49 C ANISOU 772 CB HIS E 96 4456 4624 3644 -211 1455 117 C ATOM 773 CG HIS A 96 23.556 40.127 61.855 1.00 38.62 C ANISOU 773 CG HIS E 96 4939 5649 4085 -462 1172 -559 C ATOM 774 ND1 HIS A 96 22.244 40.517 61.710 1.00 40.50 N ANISOU 774 ND1 HIS E 96 4989 6057 4344 -654 1265 -701 N ATOM 775 CD2 HIS A 96 24.286 40.961 61.078 1.00 40.14 C ANISOU 775 CD2 HIS E 96 5023 6117 4113 -720 1221 -1071 C ATOM 776 CE1 HIS A 96 22.163 41.533 60.881 1.00 39.67 C ANISOU 776 CE1 HIS E 96 4932 6129 4012 -470 882 -603 C ATOM 777 NE2 HIS A 96 23.395 41.822 60.478 1.00 37.90 N ANISOU 777 NE2 HIS E 96 4805 5639 3956 -144 387 -484 N ATOM 778 N VAL A 97 25.524 38.745 65.896 1.00 34.62 N ANISOU 778 N VAL E 97 4461 5321 3373 -477 1494 54 N ATOM 779 CA VAL A 97 26.124 37.700 66.730 1.00 36.46 C ANISOU 779 CA VAL E 97 4874 5289 3692 -460 1178 36 C ATOM 780 C VAL A 97 26.183 38.127 68.193 1.00 35.96 C ANISOU 780 C VAL E 97 4654 5581 3426 -439 1679 -336 C ATOM 781 O VAL A 97 25.766 39.236 68.532 1.00 39.41 O ANISOU 781 O VAL E 97 5804 5797 3372 -914 25 271 O ATOM 782 CB VAL A 97 27.519 37.314 66.210 1.00 35.14 C ANISOU 782 CB VAL E 97 5139 5045 3167 -785 1099 236 C ATOM 783 CG1 VAL A 97 27.429 36.801 64.775 1.00 33.93 C ANISOU 783 CG1 VAL E 97 5390 4646 2856 -222 961 -318 C ATOM 784 CG2 VAL A 97 28.480 38.490 66.303 1.00 34.92 C ANISOU 784 CG2 VAL E 97 4327 5855 3086 -666 223 72 C ATOM 785 N ASP A 98 26.679 37.245 69.059 1.00 36.74 N ANISOU 785 N ASP E 98 4927 5302 3730 -197 1333 -352 N ATOM 786 CA ASP A 98 26.576 37.473 70.499 1.00 34.71 C ANISOU 786 CA ASP E 98 4702 4779 3708 -54 1044 -383 C ATOM 787 C ASP A 98 27.854 38.033 71.119 1.00 35.19 C ANISOU 787 C ASP E 98 4413 4907 4051 -182 914 -851 C ATOM 788 O ASP A 98 28.161 37.725 72.273 1.00 35.65 O ANISOU 788 O ASP E 98 4240 5630 3677 -138 1218 -561 O ATOM 789 CB ASP A 98 26.193 36.183 71.238 1.00 34.30 C ANISOU 789 CB ASP E 98 4389 4744 3901 -267 1045 -509 C ATOM 790 CG ASP A 98 27.182 35.055 70.982 1.00 42.85 C ANISOU 790 CG ASP E 98 6236 5461 4584 -1451 1620 -797 C ATOM 791 OD1 ASP A 98 28.033 35.192 70.068 1.00 41.13 O ANISOU 791 OD1 ASP E 98 5685 5525 4418 -1274 1366 -182 O ATOM 792 OD2 ASP A 98 27.101 34.030 71.695 1.00 40.73 O ANISOU 792 OD2 ASP E 98 6312 4815 4350 -870 814 -248 O ATOM 793 N ILE A 99 28.577 38.858 70.363 1.00 33.19 N ANISOU 793 N ILE E 99 4298 4713 3599 -396 1533 -192 N ATOM 794 CA ILE A 99 29.772 39.456 70.939 1.00 33.90 C ANISOU 794 CA ILE E 99 4695 4378 3809 -187 1492 28 C ATOM 795 C ILE A 99 29.470 40.725 71.747 1.00 36.58 C ANISOU 795 C ILE E 99 5231 4990 3677 -1364 534 289 C ATOM 796 O ILE A 99 28.749 41.641 71.352 1.00 35.36 O ANISOU 796 O ILE E 99 4707 4851 3876 -930 742 -274 O ATOM 797 CB ILE A 99 30.763 39.802 69.821 1.00 35.18 C ANISOU 797 CB ILE E 99 3998 5274 4095 -492 1345 -288 C ATOM 798 CG1 ILE A 99 32.165 40.202 70.297 1.00 34.23 C ANISOU 798 CG1 ILE E 99 4305 4669 4033 -422 1095 -6 C ATOM 799 CG2 ILE A 99 30.169 40.903 68.943 1.00 37.02 C ANISOU 799 CG2 ILE E 99 5269 6154 2643 -704 911 -99 C ATOM 800 CD1 ILE A 99 33.139 40.359 69.127 1.00 34.84 C ANISOU 800 CD1 ILE E 99 4107 4388 4744 -137 1473 605 C ATOM 801 N PRO A 100 30.064 40.812 72.939 1.00 36.88 N ANISOU 801 N PRO E 100 5587 5329 3097 -1531 930 -61 N ATOM 802 CA PRO A 100 29.898 41.987 73.779 1.00 35.29 C ANISOU 802 CA PRO E 100 4840 5035 3535 -1196 356 54 C ATOM 803 C PRO A 100 30.690 43.200 73.307 1.00 36.36 C ANISOU 803 C PRO E 100 4851 5250 3715 -1543 965 -480 C ATOM 804 O PRO A 100 31.792 43.074 72.781 1.00 39.45 O ANISOU 804 O PRO E 100 5703 5877 3407 -1736 1727 -330 O ATOM 805 CB PRO A 100 30.452 41.559 75.149 1.00 33.85 C ANISOU 805 CB PRO E 100 4530 5161 3171 -1211 970 -90 C ATOM 806 CG PRO A 100 31.225 40.312 74.909 1.00 37.64 C ANISOU 806 CG PRO E 100 5633 5438 3229 -1814 917 -195 C ATOM 807 CD PRO A 100 30.913 39.779 73.532 1.00 36.80 C ANISOU 807 CD PRO E 100 5032 5463 3487 -1619 913 121 C ATOM 808 N ALA A 101 30.140 44.397 73.519 1.00 30.99 N ANISOU 808 N ALA E 101 3433 5040 3303 -898 -430 305 N ATOM 809 CA ALA A 101 30.795 45.634 73.125 1.00 33.72 C ANISOU 809 CA ALA E 101 4081 5089 3640 -619 200 736 C ATOM 810 C ALA A 101 32.212 45.710 73.667 1.00 30.88 C ANISOU 810 C ALA E 101 3919 4368 3448 -629 404 347 C ATOM 811 O ALA A 101 33.135 46.194 73.015 1.00 32.77 O ANISOU 811 O ALA E 101 4178 4764 3512 -566 682 392 O ATOM 812 CB ALA A 101 29.995 46.836 73.613 1.00 33.55 C ANISOU 812 CB ALA E 101 3964 5017 3766 -861 593 -5 C ATOM 813 N GLU A 102 32.415 45.236 74.898 1.00 30.35 N ANISOU 813 N GLU E 102 4106 4392 3032 -846 605 806 N ATOM 814 CA GLU A 102 33.757 45.441 75.438 1.00 32.82 C ANISOU 814 CA GLU E 102 4063 5216 3191 -999 506 481 C ATOM 815 C GLU A 102 34.772 44.588 74.695 1.00 31.46 C ANISOU 815 C GLU E 102 3864 4733 3355 -396 864 489 C ATOM 816 O GLU A 102 35.968 44.848 74.802 1.00 34.82 O ANISOU 816 O GLU E 102 3726 5192 4311 -1043 -26 703 O ATOM 817 CB GLU A 102 33.782 45.116 76.928 1.00 35.90 C ANISOU 817 CB GLU E 102 4640 5930 3070 -1466 471 632 C ATOM 818 CG GLU A 102 33.216 43.721 77.174 1.00 42.27 C ANISOU 818 CG GLU E 102 6742 5952 3365 -1389 507 -204 C ATOM 819 CD GLU A 102 32.871 43.549 78.646 1.00 50.47 C ANISOU 819 CD GLU E 102 7995 7533 3648 -1747 1074 -687 C ATOM 820 OE1 GLU A 102 31.660 43.475 78.982 1.00 57.34 O ANISOU 820 OE1 GLU E 102 8278 9155 4353 -1924 1846 -96 O ATOM 821 OE2 GLU A 102 33.833 43.495 79.456 1.00 60.07 O ANISOU 821 OE2 GLU E 102 8655 10831 3336 -3672 902 -1579 O ATOM 822 N ASN A 103 34.320 43.584 73.950 1.00 32.64 N ANISOU 822 N ASN E 103 4396 4734 3272 -404 598 409 N ATOM 823 CA ASN A 103 35.232 42.726 73.203 1.00 33.57 C ANISOU 823 CA ASN E 103 5275 4740 2740 -1027 431 227 C ATOM 824 C ASN A 103 35.578 43.268 71.824 1.00 31.50 C ANISOU 824 C ASN E 103 4370 4610 2987 -737 366 81 C ATOM 825 O ASN A 103 36.427 42.693 71.130 1.00 32.15 O ANISOU 825 O ASN E 103 4006 4785 3422 -525 691 -130 O ATOM 826 CB ASN A 103 34.604 41.334 73.057 1.00 34.34 C ANISOU 826 CB ASN E 103 5232 4745 3072 -912 1374 133 C ATOM 827 CG ASN A 103 34.724 40.500 74.316 1.00 36.60 C ANISOU 827 CG ASN E 103 5288 5096 3522 -883 519 -207 C ATOM 828 OD1 ASN A 103 35.077 41.027 75.378 1.00 35.71 O ANISOU 828 OD1 ASN E 103 5044 5400 3123 -644 1347 -82 O ATOM 829 ND2 ASN A 103 34.436 39.210 74.253 1.00 35.38 N ANISOU 829 ND2 ASN E 103 5136 5176 3130 -685 1303 -224 N ATOM 830 N ILE A 104 34.957 44.355 71.363 1.00 32.91 N ANISOU 830 N ILE E 104 4556 4661 3286 -737 274 -56 N ATOM 831 CA ILE A 104 35.130 44.855 69.997 1.00 31.09 C ANISOU 831 CA ILE E 104 4505 4217 3091 -847 319 231 C ATOM 832 C ILE A 104 36.120 46.002 69.979 1.00 31.25 C ANISOU 832 C ILE E 104 4575 3985 3313 -949 706 460 C ATOM 833 O ILE A 104 35.982 46.982 70.715 1.00 32.27 O ANISOU 833 O ILE E 104 4783 4728 2752 -686 460 863 O ATOM 834 CB ILE A 104 33.807 45.329 69.370 1.00 31.31 C ANISOU 834 CB ILE E 104 4726 4326 2846 -1181 253 675 C ATOM 835 CG1 ILE A 104 32.776 44.200 69.261 1.00 31.28 C ANISOU 835 CG1 ILE E 104 4403 4559 2921 -1144 164 242 C ATOM 836 CG2 ILE A 104 34.019 46.004 68.015 1.00 29.67 C ANISOU 836 CG2 ILE E 104 4248 4267 2758 -881 104 781 C ATOM 837 CD1 ILE A 104 31.381 44.688 68.950 1.00 32.42 C ANISOU 837 CD1 ILE E 104 4680 4730 2907 -1500 -179 876 C ATOM 838 N ASN A 105 37.142 45.885 69.142 1.00 30.46 N ANISOU 838 N ASN E 105 4248 4407 2918 -945 333 590 N ATOM 839 CA ASN A 105 38.108 46.967 69.074 1.00 32.34 C ANISOU 839 CA ASN E 105 4321 4452 3516 -907 626 520 C ATOM 840 C ASN A 105 38.212 47.446 67.629 1.00 33.61 C ANISOU 840 C ASN E 105 4711 4436 3624 -724 491 392 C ATOM 841 O ASN A 105 38.432 46.700 66.678 1.00 30.80 O ANISOU 841 O ASN E 105 4042 4434 3227 -644 -297 398 O ATOM 842 CB ASN A 105 39.465 46.496 69.573 1.00 32.61 C ANISOU 842 CB ASN E 105 4246 4368 3777 -697 574 342 C ATOM 843 CG ASN A 105 39.455 46.091 71.024 1.00 35.09 C ANISOU 843 CG ASN E 105 4708 5076 3550 -880 272 688 C ATOM 844 OD1 ASN A 105 39.615 46.972 71.874 1.00 39.39 O ANISOU 844 OD1 ASN E 105 5905 5078 3981 -569 731 944 O ATOM 845 ND2 ASN A 105 39.271 44.807 71.326 1.00 29.24 N ANISOU 845 ND2 ASN E 105 3888 5167 2057 -734 610 859 N ATOM 846 N LEU A 106 38.025 48.756 67.509 1.00 31.95 N ANISOU 846 N LEU E 106 3952 4279 3909 -177 439 403 N ATOM 847 CA LEU A 106 38.065 49.463 66.242 1.00 34.22 C ANISOU 847 CA LEU E 106 4400 4562 4040 -423 543 158 C ATOM 848 C LEU A 106 38.892 50.726 66.447 1.00 34.71 C ANISOU 848 C LEU E 106 4913 4364 3913 -388 534 20 C ATOM 849 O LEU A 106 38.818 51.296 67.533 1.00 36.23 O ANISOU 849 O LEU E 106 4968 4770 4027 -138 604 233 O ATOM 850 CB LEU A 106 36.675 49.833 65.739 1.00 36.38 C ANISOU 850 CB LEU E 106 4510 4684 4630 -584 565 -435 C ATOM 851 CG LEU A 106 35.872 48.750 65.009 1.00 35.72 C ANISOU 851 CG LEU E 106 3771 5352 4451 -70 829 -681 C ATOM 852 CD1 LEU A 106 34.433 48.776 65.519 1.00 42.00 C ANISOU 852 CD1 LEU E 106 3910 6757 5290 -647 1129 138 C ATOM 853 CD2 LEU A 106 35.910 48.914 63.500 1.00 35.07 C ANISOU 853 CD2 LEU E 106 4779 4133 4415 -597 761 -603 C ATOM 854 N LEU A 107 39.661 51.164 65.467 1.00 34.53 N ANISOU 854 N LEU E 107 4691 4414 4014 -459 540 -33 N ATOM 855 CA LEU A 107 40.393 52.416 65.589 1.00 35.05 C ANISOU 855 CA LEU E 107 4619 4356 4344 -516 1190 479 C ATOM 856 C LEU A 107 39.448 53.609 65.641 1.00 37.46 C ANISOU 856 C LEU E 107 4938 4618 4678 -787 937 911 C ATOM 857 O LEU A 107 38.454 53.687 64.903 1.00 38.05 O ANISOU 857 O LEU E 107 5313 4559 4585 -800 755 183 O ATOM 858 CB LEU A 107 41.382 52.502 64.413 1.00 34.30 C ANISOU 858 CB LEU E 107 4586 4483 3964 -534 928 451 C ATOM 859 CG LEU A 107 42.668 51.702 64.690 1.00 34.06 C ANISOU 859 CG LEU E 107 4502 4681 3757 -547 836 807 C ATOM 860 CD1 LEU A 107 43.395 51.362 63.388 1.00 29.82 C ANISOU 860 CD1 LEU E 107 3380 4872 3080 -19 332 269 C ATOM 861 CD2 LEU A 107 43.556 52.457 65.662 1.00 33.01 C ANISOU 861 CD2 LEU E 107 5034 4156 3351 -512 683 489 C ATOM 862 N ASN A 108 39.737 54.562 66.542 1.00 39.13 N ANISOU 862 N ASN E 108 5989 4292 4588 -435 1104 684 N ATOM 863 CA ASN A 108 38.919 55.770 66.642 1.00 39.84 C ANISOU 863 CA ASN E 108 6362 4176 4599 -440 1482 556 C ATOM 864 C ASN A 108 39.421 56.829 65.669 1.00 40.69 C ANISOU 864 C ASN E 108 6208 4324 4928 -519 1857 483 C ATOM 865 O ASN A 108 40.367 57.575 65.936 1.00 43.29 O ANISOU 865 O ASN E 108 6790 3902 5756 -377 1638 598 O ATOM 866 CB ASN A 108 38.912 56.305 68.074 1.00 40.41 C ANISOU 866 CB ASN E 108 6331 4262 4760 21 1660 794 C ATOM 867 CG ASN A 108 37.974 57.477 68.264 1.00 38.84 C ANISOU 867 CG ASN E 108 5505 4307 4946 398 2042 806 C ATOM 868 OD1 ASN A 108 37.331 57.976 67.329 1.00 53.94 O ANISOU 868 OD1 ASN E 108 10729 5477 4290 -2612 3158 -571 O ATOM 869 ND2 ASN A 108 37.900 57.938 69.519 1.00 46.61 N ANISOU 869 ND2 ASN E 108 7358 5603 4750 -825 2625 612 N ATOM 870 N GLY A 109 38.783 56.917 64.504 1.00 40.85 N ANISOU 870 N GLY E 109 6270 4240 5010 -754 1842 113 N ATOM 871 CA GLY A 109 39.205 57.863 63.482 1.00 39.63 C ANISOU 871 CA GLY E 109 5024 4631 5402 78 1429 -31 C ATOM 872 C GLY A 109 38.931 59.300 63.878 1.00 42.22 C ANISOU 872 C GLY E 109 5622 4535 5887 -177 1869 -417 C ATOM 873 O GLY A 109 39.361 60.242 63.217 1.00 38.25 O ANISOU 873 O GLY E 109 4210 4790 5534 -176 293 -952 O ATOM 874 N ASN A 110 38.209 59.471 64.982 1.00 44.46 N ANISOU 874 N ASN E 110 5804 4980 6109 -380 1982 -24 N ATOM 875 CA ASN A 110 37.900 60.799 65.482 1.00 48.58 C ANISOU 875 CA ASN E 110 6429 5414 6615 -1018 1249 443 C ATOM 876 C ASN A 110 38.722 61.118 66.715 1.00 50.82 C ANISOU 876 C ASN E 110 6823 5772 6715 -709 1144 566 C ATOM 877 O ASN A 110 38.482 62.146 67.349 1.00 48.88 O ANISOU 877 O ASN E 110 7062 4473 7037 13 812 -66 O ATOM 878 CB ASN A 110 36.387 60.910 65.756 1.00 50.36 C ANISOU 878 CB ASN E 110 6487 5502 7146 -1451 1298 21 C ATOM 879 CG ASN A 110 35.595 60.878 64.456 1.00 50.62 C ANISOU 879 CG ASN E 110 6301 5774 7159 -1249 1332 -411 C ATOM 880 OD1 ASN A 110 35.775 61.748 63.598 1.00 52.61 O ANISOU 880 OD1 ASN E 110 6575 6222 7194 -811 1545 -529 O ATOM 881 ND2 ASN A 110 34.717 59.898 64.266 1.00 48.08 N ANISOU 881 ND2 ASN E 110 6147 5904 6217 -1209 1853 -182 N ATOM 882 N ALA A 111 39.693 60.283 67.086 1.00 46.92 N ANISOU 882 N ALA E 111 5573 5931 6322 -309 1461 920 N ATOM 883 CA ALA A 111 40.478 60.608 68.282 1.00 48.47 C ANISOU 883 CA ALA E 111 5790 6212 6414 129 1455 1048 C ATOM 884 C ALA A 111 41.167 61.964 68.112 1.00 52.94 C ANISOU 884 C ALA E 111 6797 6316 7001 455 1192 819 C ATOM 885 O ALA A 111 41.598 62.368 67.027 1.00 54.44 O ANISOU 885 O ALA E 111 7637 5640 7410 41 1768 691 O ATOM 886 CB ALA A 111 41.493 59.530 68.622 1.00 45.03 C ANISOU 886 CB ALA E 111 3698 5647 7765 1271 726 1998 C ATOM 887 N PRO A 112 41.252 62.685 69.229 1.00 55.19 N ANISOU 887 N PRO E 112 7572 6396 7003 848 638 742 N ATOM 888 CA PRO A 112 41.869 64.018 69.219 1.00 54.22 C ANISOU 888 CA PRO E 112 6868 6455 7279 743 569 625 C ATOM 889 C PRO A 112 43.379 63.900 69.025 1.00 59.71 C ANISOU 889 C PRO E 112 7025 6982 8682 359 1164 -242 C ATOM 890 O PRO A 112 43.964 64.668 68.253 1.00 77.93 O ANISOU 890 O PRO E 112 8031 7763 13817 567 2677 -2149 O ATOM 891 CB PRO A 112 41.515 64.583 70.596 1.00 57.18 C ANISOU 891 CB PRO E 112 7833 6256 7639 966 1000 896 C ATOM 892 CG PRO A 112 41.433 63.358 71.454 1.00 54.16 C ANISOU 892 CG PRO E 112 7183 6144 7253 1389 1098 1162 C ATOM 893 CD PRO A 112 40.792 62.312 70.576 1.00 53.80 C ANISOU 893 CD PRO E 112 6856 6468 7117 1172 1100 1377 C ATOM 894 N ASP A 113 44.020 62.942 69.688 1.00 58.97 N ANISOU 894 N ASP E 113 7871 6976 7558 -703 978 1015 N ATOM 895 CA ASP A 113 45.446 62.706 69.486 1.00 54.23 C ANISOU 895 CA ASP E 113 7651 6420 6535 -174 564 1816 C ATOM 896 C ASP A 113 45.674 61.413 68.700 1.00 52.93 C ANISOU 896 C ASP E 113 7586 6363 6163 180 639 1741 C ATOM 897 O ASP A 113 45.769 60.341 69.301 1.00 44.98 O ANISOU 897 O ASP E 113 5320 6095 5676 1212 693 1948 O ATOM 898 CB ASP A 113 46.177 62.625 70.823 1.00 54.08 C ANISOU 898 CB ASP E 113 7975 6588 5985 -110 988 1859 C ATOM 899 CG ASP A 113 47.682 62.556 70.670 1.00 58.32 C ANISOU 899 CG ASP E 113 7835 7247 7078 -138 293 1121 C ATOM 900 OD1 ASP A 113 48.179 62.317 69.556 1.00 53.98 O ANISOU 900 OD1 ASP E 113 5905 7266 7339 387 -41 1707 O ATOM 901 OD2 ASP A 113 48.387 62.752 71.682 1.00 61.72 O ANISOU 901 OD2 ASP E 113 8558 8578 6314 -863 -16 -699 O ATOM 902 N ILE A 114 45.758 61.548 67.382 1.00 51.56 N ANISOU 902 N ILE E 114 6967 6312 6311 -162 1211 1397 N ATOM 903 CA ILE A 114 45.920 60.416 66.478 1.00 52.94 C ANISOU 903 CA ILE E 114 7380 6739 5997 -693 1291 1417 C ATOM 904 C ILE A 114 47.090 59.512 66.824 1.00 49.80 C ANISOU 904 C ILE E 114 7019 5918 5983 -7 1190 1105 C ATOM 905 O ILE A 114 46.926 58.286 66.890 1.00 49.57 O ANISOU 905 O ILE E 114 6631 5887 6317 133 1737 1794 O ATOM 906 CB ILE A 114 46.097 60.919 65.030 1.00 55.04 C ANISOU 906 CB ILE E 114 7595 7188 6129 -1136 1136 1055 C ATOM 907 CG1 ILE A 114 44.829 61.581 64.480 1.00 59.43 C ANISOU 907 CG1 ILE E 114 8000 7943 6638 -2048 1462 914 C ATOM 908 CG2 ILE A 114 46.570 59.795 64.121 1.00 45.34 C ANISOU 908 CG2 ILE E 114 6371 5895 4960 -544 270 324 C ATOM 909 CD1 ILE A 114 43.611 60.695 64.711 1.00 67.13 C ANISOU 909 CD1 ILE E 114 7512 7919 10077 -1945 751 1921 C ATOM 910 N ASP A 115 48.289 60.050 67.047 1.00 48.77 N ANISOU 910 N ASP E 115 7171 5406 5955 66 1323 1323 N ATOM 911 CA ASP A 115 49.379 59.118 67.348 1.00 48.39 C ANISOU 911 CA ASP E 115 7228 5264 5896 282 442 1777 C ATOM 912 C ASP A 115 49.118 58.341 68.627 1.00 47.13 C ANISOU 912 C ASP E 115 6772 5891 5245 168 83 1979 C ATOM 913 O ASP A 115 49.530 57.188 68.724 1.00 40.86 O ANISOU 913 O ASP E 115 4896 6366 4264 -85 440 1617 O ATOM 914 CB ASP A 115 50.718 59.849 67.449 1.00 54.10 C ANISOU 914 CB ASP E 115 7425 5973 7156 638 193 1521 C ATOM 915 CG ASP A 115 51.110 60.372 66.075 1.00 57.98 C ANISOU 915 CG ASP E 115 7268 7039 7724 782 726 1041 C ATOM 916 OD1 ASP A 115 50.319 60.199 65.121 1.00 63.54 O ANISOU 916 OD1 ASP E 115 8889 7752 7500 -32 -83 573 O ATOM 917 OD2 ASP A 115 52.205 60.957 65.959 1.00 72.11 O ANISOU 917 OD2 ASP E 115 8323 7947 11127 1838 1191 119 O ATOM 918 N ALA A 116 48.442 58.989 69.562 1.00 45.03 N ANISOU 918 N ALA E 116 6608 5130 5370 362 -231 2216 N ATOM 919 CA ALA A 116 48.103 58.330 70.819 1.00 46.84 C ANISOU 919 CA ALA E 116 7112 5580 5106 -215 11 2295 C ATOM 920 C ALA A 116 47.116 57.181 70.618 1.00 42.63 C ANISOU 920 C ALA E 116 6829 5093 4274 -485 416 1882 C ATOM 921 O ALA A 116 47.274 56.087 71.192 1.00 43.65 O ANISOU 921 O ALA E 116 6664 5785 4135 -790 1404 1188 O ATOM 922 CB ALA A 116 47.547 59.371 71.772 1.00 45.03 C ANISOU 922 CB ALA E 116 5193 5521 6397 378 640 2551 C ATOM 923 N GLU A 117 46.099 57.437 69.805 1.00 40.19 N ANISOU 923 N GLU E 117 5901 5384 3985 -321 1107 1559 N ATOM 924 CA GLU A 117 45.107 56.426 69.421 1.00 42.41 C ANISOU 924 CA GLU E 117 6550 5019 4547 -371 582 1690 C ATOM 925 C GLU A 117 45.829 55.197 68.872 1.00 40.28 C ANISOU 925 C GLU E 117 6191 4878 4236 -462 829 1007 C ATOM 926 O GLU A 117 45.557 54.061 69.288 1.00 37.84 O ANISOU 926 O GLU E 117 5358 4923 4096 -54 799 1325 O ATOM 927 CB GLU A 117 44.135 57.025 68.413 1.00 41.10 C ANISOU 927 CB GLU E 117 6379 4044 5193 -218 420 1696 C ATOM 928 CG GLU A 117 43.072 56.154 67.777 1.00 39.62 C ANISOU 928 CG GLU E 117 5565 4581 4906 -77 1126 1712 C ATOM 929 CD GLU A 117 42.175 55.500 68.811 1.00 43.56 C ANISOU 929 CD GLU E 117 6478 4914 5158 -169 1533 1396 C ATOM 930 OE1 GLU A 117 42.035 56.086 69.911 1.00 40.98 O ANISOU 930 OE1 GLU E 117 5095 5747 4727 12 796 1432 O ATOM 931 OE2 GLU A 117 41.633 54.408 68.519 1.00 41.60 O ANISOU 931 OE2 GLU E 117 5582 5443 4780 120 1472 1403 O ATOM 932 N CYS A 118 46.761 55.430 67.944 1.00 36.59 N ANISOU 932 N CYS E 118 5340 4757 3805 -197 141 868 N ATOM 933 CA CYS A 118 47.459 54.335 67.277 1.00 35.42 C ANISOU 933 CA CYS E 118 4597 4601 4259 145 389 845 C ATOM 934 C CYS A 118 48.321 53.567 68.266 1.00 35.22 C ANISOU 934 C CYS E 118 4292 4824 4266 153 357 926 C ATOM 935 O CYS A 118 48.335 52.335 68.270 1.00 36.37 O ANISOU 935 O CYS E 118 5254 4837 3727 -302 589 909 O ATOM 936 CB CYS A 118 48.277 54.880 66.101 1.00 38.72 C ANISOU 936 CB CYS E 118 6019 4186 4508 272 977 881 C ATOM 937 SG CYS A 118 47.200 55.532 64.776 1.00 42.29 S ANISOU 937 SG CYS E 118 6457 5128 4485 -445 1404 310 S ATOM 938 N ARG A 119 49.037 54.264 69.130 1.00 39.08 N ANISOU 938 N ARG E 119 3719 5677 5451 379 14 1271 N ATOM 939 CA ARG A 119 49.777 53.630 70.217 1.00 44.31 C ANISOU 939 CA ARG E 119 4903 5728 6206 455 -1119 1422 C ATOM 940 C ARG A 119 48.948 52.770 71.161 1.00 43.76 C ANISOU 940 C ARG E 119 5164 6305 5159 166 -1336 1150 C ATOM 941 O ARG A 119 49.310 51.670 71.603 1.00 41.45 O ANISOU 941 O ARG E 119 5564 6327 3860 16 -1556 1553 O ATOM 942 CB ARG A 119 50.444 54.770 71.012 1.00 52.18 C ANISOU 942 CB ARG E 119 6079 6237 7511 557 -1925 2009 C ATOM 943 CG ARG A 119 51.771 54.397 71.645 1.00 62.59 C ANISOU 943 CG ARG E 119 7520 7269 8992 -116 -3727 3064 C ATOM 944 CD ARG A 119 52.380 55.590 72.401 1.00 70.06 C ANISOU 944 CD ARG E 119 8623 7363 10634 217 -4665 3157 C ATOM 945 NE ARG A 119 52.340 56.785 71.552 1.00 77.92 N ANISOU 945 NE ARG E 119 10834 7176 11594 33 -3455 2858 N ATOM 946 CZ ARG A 119 51.837 57.971 71.864 1.00 81.38 C ANISOU 946 CZ ARG E 119 11888 7786 11248 -990 -3153 2568 C ATOM 947 NH1 ARG A 119 51.299 58.190 73.065 1.00 79.87 N ANISOU 947 NH1 ARG E 119 11090 9685 9573 -1384 -5734 3721 N ATOM 948 NH2 ARG A 119 51.881 58.956 70.965 1.00 78.89 N ANISOU 948 NH2 ARG E 119 10717 8579 10677 -1734 -5670 2193 N ATOM 949 N GLN A 120 47.768 53.262 71.532 1.00 43.70 N ANISOU 949 N GLN E 120 5581 6454 4567 -50 -1033 1137 N ATOM 950 CA GLN A 120 46.893 52.522 72.442 1.00 43.77 C ANISOU 950 CA GLN E 120 6264 6209 4159 -91 -698 1472 C ATOM 951 C GLN A 120 46.352 51.240 71.822 1.00 42.63 C ANISOU 951 C GLN E 120 6254 5980 3964 -171 -1138 1024 C ATOM 952 O GLN A 120 46.231 50.200 72.481 1.00 40.35 O ANISOU 952 O GLN E 120 5549 6318 3463 -59 -564 1020 O ATOM 953 CB GLN A 120 45.733 53.434 72.872 1.00 51.15 C ANISOU 953 CB GLN E 120 8110 6639 4685 -934 797 1022 C ATOM 954 CG GLN A 120 46.200 54.617 73.695 1.00 60.59 C ANISOU 954 CG GLN E 120 10526 6828 5666 -1654 -68 1791 C ATOM 955 CD GLN A 120 45.142 55.687 73.877 1.00 66.38 C ANISOU 955 CD GLN E 120 11134 7736 6353 -2259 807 2050 C ATOM 956 OE1 GLN A 120 43.949 55.445 73.674 1.00 80.51 O ANISOU 956 OE1 GLN E 120 11531 10907 8151 -3681 -1848 4294 O ATOM 957 NE2 GLN A 120 45.592 56.883 74.260 1.00 65.48 N ANISOU 957 NE2 GLN E 120 12268 6515 6094 -1355 4376 647 N ATOM 958 N TYR A 121 46.019 51.324 70.527 1.00 39.41 N ANISOU 958 N TYR E 121 5523 5545 3904 -557 -941 999 N ATOM 959 CA TYR A 121 45.555 50.135 69.814 1.00 37.24 C ANISOU 959 CA TYR E 121 4934 5576 3642 -351 -578 889 C ATOM 960 C TYR A 121 46.582 49.009 69.912 1.00 35.57 C ANISOU 960 C TYR E 121 4686 5266 3564 -56 -151 609 C ATOM 961 O TYR A 121 46.249 47.876 70.266 1.00 39.31 O ANISOU 961 O TYR E 121 5066 5420 4451 -17 279 342 O ATOM 962 CB TYR A 121 45.276 50.485 68.356 1.00 32.78 C ANISOU 962 CB TYR E 121 4529 4380 3547 235 -18 741 C ATOM 963 CG TYR A 121 44.216 49.676 67.648 1.00 32.72 C ANISOU 963 CG TYR E 121 4195 4876 3362 79 -13 842 C ATOM 964 CD1 TYR A 121 42.904 49.688 68.118 1.00 32.38 C ANISOU 964 CD1 TYR E 121 4294 4542 3467 -45 155 697 C ATOM 965 CD2 TYR A 121 44.532 48.910 66.522 1.00 29.32 C ANISOU 965 CD2 TYR E 121 4353 3681 3105 719 514 215 C ATOM 966 CE1 TYR A 121 41.920 48.959 67.491 1.00 29.55 C ANISOU 966 CE1 TYR E 121 4346 3796 3086 310 491 52 C ATOM 967 CE2 TYR A 121 43.554 48.180 65.884 1.00 26.68 C ANISOU 967 CE2 TYR E 121 4082 3327 2727 406 295 -193 C ATOM 968 CZ TYR A 121 42.269 48.212 66.376 1.00 29.38 C ANISOU 968 CZ TYR E 121 4160 3638 3366 350 482 232 C ATOM 969 OH TYR A 121 41.264 47.493 65.756 1.00 30.92 O ANISOU 969 OH TYR E 121 3871 4298 3580 135 349 502 O ATOM 970 N GLU A 122 47.842 49.306 69.598 1.00 34.29 N ANISOU 970 N GLU E 122 4451 5144 3434 344 -834 1356 N ATOM 971 CA GLU A 122 48.901 48.302 69.697 1.00 37.50 C ANISOU 971 CA GLU E 122 4800 5818 3630 -156 498 -49 C ATOM 972 C GLU A 122 49.025 47.834 71.144 1.00 36.58 C ANISOU 972 C GLU E 122 4713 5633 3554 185 412 101 C ATOM 973 O GLU A 122 49.237 46.659 71.443 1.00 38.91 O ANISOU 973 O GLU E 122 4594 6036 4155 -416 -691 -119 O ATOM 974 CB GLU A 122 50.261 48.829 69.241 1.00 37.54 C ANISOU 974 CB GLU E 122 4948 5625 3692 -122 635 -69 C ATOM 975 CG GLU A 122 50.319 49.173 67.756 1.00 35.43 C ANISOU 975 CG GLU E 122 4337 5596 3529 370 210 271 C ATOM 976 CD GLU A 122 50.506 47.965 66.866 1.00 39.13 C ANISOU 976 CD GLU E 122 5390 5602 3876 -300 368 243 C ATOM 977 OE1 GLU A 122 50.794 46.869 67.392 1.00 40.51 O ANISOU 977 OE1 GLU E 122 5324 5966 4101 -741 -1057 413 O ATOM 978 OE2 GLU A 122 50.349 48.150 65.630 1.00 37.69 O ANISOU 978 OE2 GLU E 122 5819 4757 3746 -47 903 257 O ATOM 979 N GLU A 123 48.891 48.813 72.051 1.00 41.44 N ANISOU 979 N GLU E 123 5037 6678 4029 -410 -421 951 N ATOM 980 CA GLU A 123 48.993 48.378 73.452 1.00 45.19 C ANISOU 980 CA GLU E 123 6449 6777 3942 -681 -248 1030 C ATOM 981 C GLU A 123 47.854 47.447 73.835 1.00 44.81 C ANISOU 981 C GLU E 123 5963 7095 3967 -1105 -108 473 C ATOM 982 O GLU A 123 48.037 46.466 74.561 1.00 42.83 O ANISOU 982 O GLU E 123 6460 6124 3688 -484 -1306 1300 O ATOM 983 CB GLU A 123 49.033 49.613 74.356 1.00 52.97 C ANISOU 983 CB GLU E 123 7888 7594 4642 -1002 -1478 1840 C ATOM 984 CG GLU A 123 50.465 49.961 74.728 1.00 62.88 C ANISOU 984 CG GLU E 123 8488 7466 7937 376 -1773 1479 C ATOM 985 CD GLU A 123 50.935 51.300 74.207 1.00 75.26 C ANISOU 985 CD GLU E 123 10105 7469 11021 -13 -239 782 C ATOM 986 OE1 GLU A 123 50.475 52.343 74.722 1.00 94.72 O ANISOU 986 OE1 GLU E 123 15817 7792 12381 -1954 62 894 O ATOM 987 OE2 GLU A 123 51.780 51.311 73.273 1.00108.70 O ANISOU 987 OE2 GLU E 123 15891 10579 14830 -1925 4492 -3558 O ATOM 988 N LYS A 124 46.643 47.746 73.347 1.00 43.43 N ANISOU 988 N LYS E 124 6342 6311 3849 -1081 -739 1307 N ATOM 989 CA LYS A 124 45.522 46.865 73.689 1.00 43.60 C ANISOU 989 CA LYS E 124 5986 6783 3799 -1212 -366 1516 C ATOM 990 C LYS A 124 45.752 45.456 73.146 1.00 41.43 C ANISOU 990 C LYS E 124 6080 6378 3283 -809 740 844 C ATOM 991 O LYS A 124 45.474 44.473 73.834 1.00 39.70 O ANISOU 991 O LYS E 124 5588 6905 2593 -416 174 717 O ATOM 992 CB LYS A 124 44.202 47.448 73.177 1.00 48.70 C ANISOU 992 CB LYS E 124 6154 7889 4462 -1797 -661 2218 C ATOM 993 CG LYS A 124 43.165 47.736 74.245 1.00 63.43 C ANISOU 993 CG LYS E 124 7294 10431 6376 -3061 617 2158 C ATOM 994 CD LYS A 124 41.748 47.452 73.767 1.00 65.56 C ANISOU 994 CD LYS E 124 7032 11017 6862 -1995 1436 1559 C ATOM 995 CE LYS A 124 40.916 46.808 74.868 1.00 69.50 C ANISOU 995 CE LYS E 124 8209 12180 6018 -2846 2079 1601 C ATOM 996 NZ LYS A 124 39.482 46.625 74.477 1.00 75.15 N ANISOU 996 NZ LYS E 124 7038 17031 4484 -4576 3724 -1262 N ATOM 997 N ILE A 125 46.261 45.323 71.920 1.00 38.54 N ANISOU 997 N ILE E 125 4878 6076 3689 -691 1108 567 N ATOM 998 CA ILE A 125 46.526 43.971 71.400 1.00 34.53 C ANISOU 998 CA ILE E 125 3711 6172 3237 -519 393 769 C ATOM 999 C ILE A 125 47.481 43.236 72.341 1.00 38.08 C ANISOU 999 C ILE E 125 4373 6461 3635 -657 3 649 C ATOM 1000 O ILE A 125 47.241 42.101 72.776 1.00 40.44 O ANISOU 1000 O ILE E 125 5635 6242 3488 -613 -524 843 O ATOM 1001 CB ILE A 125 47.102 44.022 69.978 1.00 38.18 C ANISOU 1001 CB ILE E 125 4638 6414 3453 -940 800 561 C ATOM 1002 CG1 ILE A 125 46.113 44.532 68.936 1.00 37.72 C ANISOU 1002 CG1 ILE E 125 4797 6191 3344 -1317 1369 -151 C ATOM 1003 CG2 ILE A 125 47.639 42.650 69.587 1.00 31.39 C ANISOU 1003 CG2 ILE E 125 3778 5944 2204 -412 106 304 C ATOM 1004 CD1 ILE A 125 46.734 45.166 67.714 1.00 33.33 C ANISOU 1004 CD1 ILE E 125 3304 5887 3474 -140 1071 460 C ATOM 1005 N ARG A 126 48.579 43.934 72.675 1.00 39.91 N ANISOU 1005 N ARG E 126 5093 6528 3541 -592 -799 1236 N ATOM 1006 CA ARG A 126 49.571 43.328 73.569 1.00 41.68 C ANISOU 1006 CA ARG E 126 4615 6590 4630 -591 -504 396 C ATOM 1007 C ARG A 126 48.947 43.068 74.929 1.00 42.83 C ANISOU 1007 C ARG E 126 6096 6161 4016 -833 -706 654 C ATOM 1008 O ARG A 126 49.392 42.168 75.641 1.00 50.68 O ANISOU 1008 O ARG E 126 8113 7268 3876 -1592 -1649 650 O ATOM 1009 CB ARG A 126 50.836 44.181 73.703 1.00 49.83 C ANISOU 1009 CB ARG E 126 4423 7446 7066 -493 -945 639 C ATOM 1010 CG ARG A 126 51.541 44.379 72.367 1.00 61.30 C ANISOU 1010 CG ARG E 126 5305 8610 9378 -150 1073 -467 C ATOM 1011 CD ARG A 126 52.763 45.280 72.435 1.00 70.98 C ANISOU 1011 CD ARG E 126 6066 8802 12102 403 337 -1383 C ATOM 1012 NE ARG A 126 53.032 46.003 71.185 1.00 75.78 N ANISOU 1012 NE ARG E 126 6410 9126 13256 732 279 -2434 N ATOM 1013 CZ ARG A 126 53.173 47.327 71.127 1.00 80.52 C ANISOU 1013 CZ ARG E 126 7729 9012 13852 270 -308 -2303 C ATOM 1014 NH1 ARG A 126 53.071 48.060 72.236 1.00 75.26 N ANISOU 1014 NH1 ARG E 126 3984 10070 14544 614 -1937 -1211 N ATOM 1015 NH2 ARG A 126 53.417 47.935 69.967 1.00 84.71 N ANISOU 1015 NH2 ARG E 126 8443 9133 14609 154 -560 -3265 N ATOM 1016 N SER A 127 47.913 43.804 75.343 1.00 45.17 N ANISOU 1016 N SER E 127 6405 6105 4654 -537 272 666 N ATOM 1017 CA SER A 127 47.380 43.483 76.685 1.00 45.18 C ANISOU 1017 CA SER E 127 6382 6517 4269 -264 -284 650 C ATOM 1018 C SER A 127 46.787 42.083 76.665 1.00 44.06 C ANISOU 1018 C SER E 127 5846 6620 4274 -268 -1001 7 C ATOM 1019 O SER A 127 46.827 41.390 77.673 1.00 51.05 O ANISOU 1019 O SER E 127 9415 6449 3533 -269 -623 590 O ATOM 1020 CB SER A 127 46.344 44.497 77.155 1.00 46.96 C ANISOU 1020 CB SER E 127 6559 6827 4457 -337 566 241 C ATOM 1021 OG SER A 127 45.171 44.401 76.343 1.00 47.73 O ANISOU 1021 OG SER E 127 5686 6576 5873 44 856 1070 O ATOM 1022 N TYR A 128 46.242 41.634 75.537 1.00 41.48 N ANISOU 1022 N TYR E 128 5253 6118 4389 -622 -1232 -208 N ATOM 1023 CA TYR A 128 45.692 40.291 75.480 1.00 41.75 C ANISOU 1023 CA TYR E 128 5167 6292 4404 -421 -748 -126 C ATOM 1024 C TYR A 128 46.789 39.294 75.136 1.00 43.28 C ANISOU 1024 C TYR E 128 5150 5889 5406 -311 -543 -473 C ATOM 1025 O TYR A 128 46.645 38.109 75.414 1.00 50.69 O ANISOU 1025 O TYR E 128 6660 5912 6687 -290 -152 -716 O ATOM 1026 CB TYR A 128 44.604 40.151 74.421 1.00 40.32 C ANISOU 1026 CB TYR E 128 5256 6154 3908 -642 -520 476 C ATOM 1027 CG TYR A 128 43.293 40.823 74.759 1.00 38.84 C ANISOU 1027 CG TYR E 128 5027 5838 3892 -375 -576 486 C ATOM 1028 CD1 TYR A 128 42.378 40.215 75.607 1.00 40.46 C ANISOU 1028 CD1 TYR E 128 5413 5790 4169 -563 -303 184 C ATOM 1029 CD2 TYR A 128 42.990 42.073 74.212 1.00 36.34 C ANISOU 1029 CD2 TYR E 128 4779 5615 3412 -143 -577 724 C ATOM 1030 CE1 TYR A 128 41.181 40.825 75.918 1.00 41.77 C ANISOU 1030 CE1 TYR E 128 6297 5884 3690 -902 535 585 C ATOM 1031 CE2 TYR A 128 41.789 42.680 74.526 1.00 39.91 C ANISOU 1031 CE2 TYR E 128 4938 5837 4389 -371 -305 415 C ATOM 1032 CZ TYR A 128 40.898 42.054 75.374 1.00 41.74 C ANISOU 1032 CZ TYR E 128 6221 6101 3537 -1268 787 509 C ATOM 1033 OH TYR A 128 39.709 42.693 75.657 1.00 42.11 O ANISOU 1033 OH TYR E 128 6000 5514 4487 -746 719 1670 O ATOM 1034 N GLY A 129 47.863 39.779 74.511 1.00 42.11 N ANISOU 1034 N GLY E 129 5664 6058 4278 -85 -183 498 N ATOM 1035 CA GLY A 129 48.966 38.866 74.242 1.00 40.48 C ANISOU 1035 CA GLY E 129 6175 6021 3184 -368 176 -100 C ATOM 1036 C GLY A 129 49.164 38.713 72.753 1.00 37.91 C ANISOU 1036 C GLY E 129 5236 6069 3100 293 -58 -536 C ATOM 1037 O GLY A 129 50.217 39.052 72.231 1.00 40.86 O ANISOU 1037 O GLY E 129 5364 6091 4071 -64 550 -542 O ATOM 1038 N LYS A 130 48.164 38.211 72.027 1.00 41.09 N ANISOU 1038 N LYS E 130 5571 6204 3836 -158 -867 -467 N ATOM 1039 CA LYS A 130 48.394 38.086 70.593 1.00 39.33 C ANISOU 1039 CA LYS E 130 5076 5865 4003 -166 -797 221 C ATOM 1040 C LYS A 130 47.069 37.873 69.872 1.00 34.07 C ANISOU 1040 C LYS E 130 4613 4869 3463 492 -65 -221 C ATOM 1041 O LYS A 130 46.126 37.419 70.519 1.00 37.69 O ANISOU 1041 O LYS E 130 4983 5663 3676 -107 1081 345 O ATOM 1042 CB LYS A 130 49.298 36.900 70.274 1.00 48.04 C ANISOU 1042 CB LYS E 130 6199 6826 5226 -1318 -1696 846 C ATOM 1043 CG LYS A 130 48.585 35.589 70.619 1.00 56.92 C ANISOU 1043 CG LYS E 130 8814 5910 6904 -696 -2458 1845 C ATOM 1044 CD LYS A 130 49.466 34.420 70.188 1.00 64.23 C ANISOU 1044 CD LYS E 130 10079 6950 7377 -1460 -1556 2019 C ATOM 1045 CE LYS A 130 50.844 34.944 69.794 1.00 66.12 C ANISOU 1045 CE LYS E 130 10805 8179 6139 -1726 -125 739 C ATOM 1046 NZ LYS A 130 50.943 35.240 68.336 1.00 77.00 N ANISOU 1046 NZ LYS E 130 14511 8537 6209 -992 -1736 -441 N ATOM 1047 N ILE A 131 47.082 38.202 68.598 1.00 31.02 N ANISOU 1047 N ILE E 131 3861 4582 3345 -482 133 -47 N ATOM 1048 CA ILE A 131 45.923 37.888 67.760 1.00 31.31 C ANISOU 1048 CA ILE E 131 4012 4209 3678 -423 -81 -152 C ATOM 1049 C ILE A 131 46.067 36.436 67.340 1.00 30.73 C ANISOU 1049 C ILE E 131 3753 4269 3654 -517 150 -164 C ATOM 1050 O ILE A 131 47.119 36.066 66.810 1.00 34.14 O ANISOU 1050 O ILE E 131 3854 5108 4008 -791 188 99 O ATOM 1051 CB ILE A 131 45.852 38.877 66.580 1.00 33.63 C ANISOU 1051 CB ILE E 131 5058 4285 3436 -1033 -124 -9 C ATOM 1052 CG1 ILE A 131 45.606 40.308 67.078 1.00 31.40 C ANISOU 1052 CG1 ILE E 131 4514 4086 3331 -270 -208 42 C ATOM 1053 CG2 ILE A 131 44.819 38.446 65.553 1.00 25.43 C ANISOU 1053 CG2 ILE E 131 4033 3240 2391 138 1295 -502 C ATOM 1054 CD1 ILE A 131 45.753 41.405 66.074 1.00 29.42 C ANISOU 1054 CD1 ILE E 131 4061 4050 3066 284 -38 314 C ATOM 1055 N HIS A 132 45.078 35.578 67.579 1.00 28.52 N ANISOU 1055 N HIS E 132 4089 4323 2422 -235 -296 -275 N ATOM 1056 CA HIS A 132 45.218 34.175 67.199 1.00 30.32 C ANISOU 1056 CA HIS E 132 4157 4435 2930 -299 71 -4 C ATOM 1057 C HIS A 132 45.021 33.930 65.712 1.00 31.66 C ANISOU 1057 C HIS E 132 4407 4647 2975 -666 86 210 C ATOM 1058 O HIS A 132 45.656 33.027 65.150 1.00 33.63 O ANISOU 1058 O HIS E 132 5439 4291 3048 -711 1019 -321 O ATOM 1059 CB HIS A 132 44.203 33.337 67.987 1.00 30.62 C ANISOU 1059 CB HIS E 132 4246 4205 3184 -277 46 -46 C ATOM 1060 CG HIS A 132 44.446 33.498 69.465 1.00 32.30 C ANISOU 1060 CG HIS E 132 4720 4451 3103 -214 79 -368 C ATOM 1061 ND1 HIS A 132 45.491 32.882 70.118 1.00 37.74 N ANISOU 1061 ND1 HIS E 132 5939 5256 3143 -1222 -185 -328 N ATOM 1062 CD2 HIS A 132 43.781 34.199 70.394 1.00 30.12 C ANISOU 1062 CD2 HIS E 132 4730 4248 2467 -1 741 -1297 C ATOM 1063 CE1 HIS A 132 45.458 33.202 71.403 1.00 40.61 C ANISOU 1063 CE1 HIS E 132 6737 5694 3000 -1929 -57 -571 C ATOM 1064 NE2 HIS A 132 44.423 34.006 71.588 1.00 40.22 N ANISOU 1064 NE2 HIS E 132 6345 5845 3092 -1717 -282 -259 N ATOM 1065 N LEU A 133 44.139 34.725 65.110 1.00 31.59 N ANISOU 1065 N LEU E 133 4605 4354 3043 -380 -89 -26 N ATOM 1066 CA LEU A 133 43.828 34.599 63.695 1.00 28.37 C ANISOU 1066 CA LEU E 133 3938 3870 2972 -91 196 10 C ATOM 1067 C LEU A 133 43.502 35.971 63.121 1.00 28.98 C ANISOU 1067 C LEU E 133 3357 4254 3399 -330 353 -398 C ATOM 1068 O LEU A 133 42.544 36.600 63.595 1.00 32.62 O ANISOU 1068 O LEU E 133 4510 4525 3358 -792 898 -113 O ATOM 1069 CB LEU A 133 42.653 33.664 63.482 1.00 29.90 C ANISOU 1069 CB LEU E 133 3627 4260 3473 -104 292 -72 C ATOM 1070 CG LEU A 133 42.120 33.506 62.056 1.00 30.77 C ANISOU 1070 CG LEU E 133 3544 4725 3421 360 627 493 C ATOM 1071 CD1 LEU A 133 43.193 33.043 61.089 1.00 30.36 C ANISOU 1071 CD1 LEU E 133 3154 5025 3356 -426 420 -419 C ATOM 1072 CD2 LEU A 133 40.951 32.512 62.073 1.00 30.54 C ANISOU 1072 CD2 LEU E 133 3610 4669 3327 357 529 -212 C ATOM 1073 N PHE A 134 44.298 36.409 62.148 1.00 30.24 N ANISOU 1073 N PHE E 134 4088 4159 3241 -390 666 -253 N ATOM 1074 CA PHE A 134 44.047 37.696 61.511 1.00 27.13 C ANISOU 1074 CA PHE E 134 3676 3832 2800 -121 279 137 C ATOM 1075 C PHE A 134 43.582 37.414 60.080 1.00 27.18 C ANISOU 1075 C PHE E 134 3808 3450 3069 -186 63 527 C ATOM 1076 O PHE A 134 44.340 36.871 59.281 1.00 27.06 O ANISOU 1076 O PHE E 134 3762 3739 2780 -314 182 84 O ATOM 1077 CB PHE A 134 45.282 38.596 61.504 1.00 26.18 C ANISOU 1077 CB PHE E 134 3256 3825 2867 -375 109 415 C ATOM 1078 CG PHE A 134 44.986 40.082 61.598 1.00 28.15 C ANISOU 1078 CG PHE E 134 3764 3739 3192 -258 -66 289 C ATOM 1079 CD1 PHE A 134 44.006 40.669 60.806 1.00 27.28 C ANISOU 1079 CD1 PHE E 134 3910 3496 2959 7 63 -133 C ATOM 1080 CD2 PHE A 134 45.692 40.897 62.490 1.00 26.16 C ANISOU 1080 CD2 PHE E 134 3356 3681 2900 -3 414 148 C ATOM 1081 CE1 PHE A 134 43.746 42.019 60.911 1.00 29.02 C ANISOU 1081 CE1 PHE E 134 4191 3644 3192 -273 60 88 C ATOM 1082 CE2 PHE A 134 45.423 42.254 62.609 1.00 28.76 C ANISOU 1082 CE2 PHE E 134 4500 3692 2734 -148 175 169 C ATOM 1083 CZ PHE A 134 44.435 42.820 61.818 1.00 30.25 C ANISOU 1083 CZ PHE E 134 4737 3547 3210 -171 -64 52 C ATOM 1084 N MET A 135 42.355 37.761 59.758 1.00 26.32 N ANISOU 1084 N MET E 135 3595 3693 2714 -5 367 190 N ATOM 1085 CA MET A 135 41.775 37.636 58.446 1.00 25.09 C ANISOU 1085 CA MET E 135 3269 3703 2560 -166 605 448 C ATOM 1086 C MET A 135 41.919 38.954 57.706 1.00 25.40 C ANISOU 1086 C MET E 135 3207 3842 2601 -266 460 287 C ATOM 1087 O MET A 135 41.676 40.029 58.254 1.00 25.93 O ANISOU 1087 O MET E 135 3696 3701 2456 163 571 289 O ATOM 1088 CB MET A 135 40.284 37.263 58.534 1.00 25.32 C ANISOU 1088 CB MET E 135 3207 4013 2401 -318 701 302 C ATOM 1089 CG MET A 135 39.737 37.027 57.119 1.00 28.15 C ANISOU 1089 CG MET E 135 3367 4549 2781 -814 4 125 C ATOM 1090 SD MET A 135 38.084 36.297 57.174 1.00 31.02 S ANISOU 1090 SD MET E 135 3750 4653 3384 -375 -86 334 S ATOM 1091 CE MET A 135 37.133 37.757 57.665 1.00 28.43 C ANISOU 1091 CE MET E 135 3016 4068 3717 -83 256 -533 C ATOM 1092 N GLY A 136 42.324 38.930 56.436 1.00 24.78 N ANISOU 1092 N GLY E 136 3188 3786 2439 -503 167 240 N ATOM 1093 CA GLY A 136 42.448 40.183 55.688 1.00 27.87 C ANISOU 1093 CA GLY E 136 3717 4095 2776 -678 220 -175 C ATOM 1094 C GLY A 136 42.227 39.935 54.205 1.00 26.53 C ANISOU 1094 C GLY E 136 3610 3703 2768 -44 526 -170 C ATOM 1095 O GLY A 136 41.971 38.803 53.769 1.00 27.86 O ANISOU 1095 O GLY E 136 3389 3779 3417 81 -146 -182 O ATOM 1096 N GLY A 137 42.324 40.993 53.415 1.00 29.09 N ANISOU 1096 N GLY E 137 4509 3712 2831 -273 435 -262 N ATOM 1097 CA GLY A 137 42.360 40.875 51.954 1.00 28.89 C ANISOU 1097 CA GLY E 137 4062 4089 2827 -596 602 -311 C ATOM 1098 C GLY A 137 43.721 41.361 51.440 1.00 28.78 C ANISOU 1098 C GLY E 137 3846 4271 2819 -450 276 -211 C ATOM 1099 O GLY A 137 44.655 41.529 52.231 1.00 29.61 O ANISOU 1099 O GLY E 137 4311 4132 2806 -454 18 -10 O ATOM 1100 N VAL A 138 43.832 41.589 50.128 1.00 26.82 N ANISOU 1100 N VAL E 138 3435 3959 2794 -174 231 -77 N ATOM 1101 CA VAL A 138 45.120 42.055 49.602 1.00 24.45 C ANISOU 1101 CA VAL E 138 3353 3292 2644 -155 53 295 C ATOM 1102 C VAL A 138 44.863 43.036 48.465 1.00 24.17 C ANISOU 1102 C VAL E 138 3323 3399 2464 47 -81 329 C ATOM 1103 O VAL A 138 43.901 42.878 47.708 1.00 26.46 O ANISOU 1103 O VAL E 138 3429 3798 2826 -189 -351 516 O ATOM 1104 CB VAL A 138 45.983 40.847 49.182 1.00 25.77 C ANISOU 1104 CB VAL E 138 3325 3426 3039 -172 -199 611 C ATOM 1105 CG1 VAL A 138 45.265 40.032 48.110 1.00 28.40 C ANISOU 1105 CG1 VAL E 138 4717 3466 2609 121 -305 480 C ATOM 1106 CG2 VAL A 138 47.364 41.256 48.690 1.00 26.22 C ANISOU 1106 CG2 VAL E 138 3531 4230 2201 -424 148 240 C ATOM 1107 N GLY A 139 45.704 44.068 48.365 1.00 24.37 N ANISOU 1107 N GLY E 139 3893 2966 2402 32 106 679 N ATOM 1108 CA GLY A 139 45.526 45.051 47.307 1.00 26.69 C ANISOU 1108 CA GLY E 139 4036 3470 2635 13 248 245 C ATOM 1109 C GLY A 139 45.958 44.448 45.975 1.00 27.30 C ANISOU 1109 C GLY E 139 4457 3318 2597 -329 173 122 C ATOM 1110 O GLY A 139 46.637 43.408 45.915 1.00 28.89 O ANISOU 1110 O GLY E 139 4748 3244 2984 -395 -207 425 O ATOM 1111 N ASN A 140 45.569 45.094 44.868 1.00 25.69 N ANISOU 1111 N ASN E 140 3631 3502 2629 48 -42 124 N ATOM 1112 CA ASN A 140 45.964 44.653 43.547 1.00 27.00 C ANISOU 1112 CA ASN E 140 3575 4061 2622 -548 93 -99 C ATOM 1113 C ASN A 140 47.493 44.654 43.429 1.00 28.54 C ANISOU 1113 C ASN E 140 3580 3849 3413 -564 68 141 C ATOM 1114 O ASN A 140 48.062 43.856 42.665 1.00 26.79 O ANISOU 1114 O ASN E 140 3564 3855 2759 -580 23 -128 O ATOM 1115 CB ASN A 140 45.378 45.561 42.466 1.00 24.74 C ANISOU 1115 CB ASN E 140 3986 2859 2555 -398 -275 507 C ATOM 1116 CG ASN A 140 43.873 45.478 42.346 1.00 27.52 C ANISOU 1116 CG ASN E 140 4084 3268 3104 -302 -543 -183 C ATOM 1117 OD1 ASN A 140 43.185 44.716 43.046 1.00 28.78 O ANISOU 1117 OD1 ASN E 140 4295 4160 2480 -141 170 318 O ATOM 1118 ND2 ASN A 140 43.309 46.281 41.449 1.00 32.68 N ANISOU 1118 ND2 ASN E 140 4801 4318 3298 -1401 -449 -329 N ATOM 1119 N ASP A 141 48.142 45.550 44.159 1.00 25.43 N ANISOU 1119 N ASP E 141 3624 3714 2323 -341 347 -354 N ATOM 1120 CA ASP A 141 49.604 45.580 44.081 1.00 26.26 C ANISOU 1120 CA ASP E 141 3642 3814 2522 -331 355 -36 C ATOM 1121 C ASP A 141 50.240 44.807 45.226 1.00 26.49 C ANISOU 1121 C ASP E 141 3569 3491 3006 -170 94 -156 C ATOM 1122 O ASP A 141 51.424 45.025 45.527 1.00 25.75 O ANISOU 1122 O ASP E 141 3565 3223 2995 -391 112 560 O ATOM 1123 CB ASP A 141 50.119 47.025 44.081 1.00 26.72 C ANISOU 1123 CB ASP E 141 3547 3842 2765 -309 -249 -384 C ATOM 1124 CG ASP A 141 49.703 47.741 45.355 1.00 26.06 C ANISOU 1124 CG ASP E 141 3097 3817 2989 461 -314 22 C ATOM 1125 OD1 ASP A 141 49.977 48.954 45.488 1.00 34.78 O ANISOU 1125 OD1 ASP E 141 5599 3472 4144 141 402 -150 O ATOM 1126 OD2 ASP A 141 49.084 47.129 46.246 1.00 30.28 O ANISOU 1126 OD2 ASP E 141 4384 3992 3130 256 314 -130 O ATOM 1127 N GLY A 142 49.482 43.937 45.884 1.00 26.48 N ANISOU 1127 N GLY E 142 3962 3312 2788 -208 434 86 N ATOM 1128 CA GLY A 142 50.020 43.082 46.946 1.00 25.59 C ANISOU 1128 CA GLY E 142 3756 3176 2790 -148 467 139 C ATOM 1129 C GLY A 142 50.063 43.731 48.305 1.00 25.67 C ANISOU 1129 C GLY E 142 3392 3211 3151 224 -423 428 C ATOM 1130 O GLY A 142 50.480 43.087 49.297 1.00 27.27 O ANISOU 1130 O GLY E 142 3583 3831 2948 -36 154 66 O ATOM 1131 N HIS A 143 49.655 44.999 48.453 1.00 26.81 N ANISOU 1131 N HIS E 143 3542 3427 3216 -44 -50 594 N ATOM 1132 CA HIS A 143 49.747 45.670 49.767 1.00 27.70 C ANISOU 1132 CA HIS E 143 3694 3720 3113 -107 -43 623 C ATOM 1133 C HIS A 143 48.704 45.159 50.751 1.00 28.72 C ANISOU 1133 C HIS E 143 3819 4031 3063 -16 -117 490 C ATOM 1134 O HIS A 143 47.713 44.526 50.376 1.00 28.56 O ANISOU 1134 O HIS E 143 3322 4544 2984 -223 -216 252 O ATOM 1135 CB HIS A 143 49.582 47.189 49.633 1.00 28.55 C ANISOU 1135 CB HIS E 143 4574 3745 2530 -324 194 700 C ATOM 1136 CG HIS A 143 48.183 47.678 49.413 1.00 35.65 C ANISOU 1136 CG HIS E 143 5284 4866 3394 -1553 -40 960 C ATOM 1137 ND1 HIS A 143 47.668 47.887 48.147 1.00 33.00 N ANISOU 1137 ND1 HIS E 143 4485 4459 3595 -302 -143 483 N ATOM 1138 CD2 HIS A 143 47.181 48.031 50.272 1.00 39.21 C ANISOU 1138 CD2 HIS E 143 5260 5829 3811 -1714 220 735 C ATOM 1139 CE1 HIS A 143 46.428 48.329 48.205 1.00 33.43 C ANISOU 1139 CE1 HIS E 143 4082 4472 4145 252 -361 928 C ATOM 1140 NE2 HIS A 143 46.103 48.419 49.490 1.00 38.04 N ANISOU 1140 NE2 HIS E 143 4721 5393 4340 -876 -18 943 N ATOM 1141 N ILE A 144 48.912 45.491 52.025 1.00 27.69 N ANISOU 1141 N ILE E 144 4000 3529 2989 -166 -216 269 N ATOM 1142 CA ILE A 144 48.003 45.046 53.084 1.00 30.21 C ANISOU 1142 CA ILE E 144 4441 3961 3078 -20 -40 137 C ATOM 1143 C ILE A 144 47.388 46.221 53.822 1.00 30.24 C ANISOU 1143 C ILE E 144 4207 4313 2970 29 -24 347 C ATOM 1144 O ILE A 144 48.104 47.181 54.162 1.00 28.53 O ANISOU 1144 O ILE E 144 3824 4341 2677 -185 -149 407 O ATOM 1145 CB ILE A 144 48.789 44.107 54.009 1.00 35.87 C ANISOU 1145 CB ILE E 144 5317 5273 3038 -1017 499 -391 C ATOM 1146 CG1 ILE A 144 49.010 42.746 53.324 1.00 39.81 C ANISOU 1146 CG1 ILE E 144 6210 5401 3515 -2039 1688 -660 C ATOM 1147 CG2 ILE A 144 48.127 43.992 55.379 1.00 38.08 C ANISOU 1147 CG2 ILE E 144 5980 5485 3002 -1448 680 -144 C ATOM 1148 CD1 ILE A 144 49.953 41.830 54.052 1.00 44.89 C ANISOU 1148 CD1 ILE E 144 5198 7047 4812 -2738 1919 -773 C ATOM 1149 N ALA A 145 46.073 46.146 54.047 1.00 30.04 N ANISOU 1149 N ALA E 145 4019 4709 2687 51 -574 734 N ATOM 1150 CA ALA A 145 45.349 47.217 54.730 1.00 33.88 C ANISOU 1150 CA ALA E 145 4272 4899 3700 -516 -314 528 C ATOM 1151 C ALA A 145 45.663 48.538 54.052 1.00 32.88 C ANISOU 1151 C ALA E 145 3871 4994 3626 -722 282 533 C ATOM 1152 O ALA A 145 45.597 48.591 52.813 1.00 37.05 O ANISOU 1152 O ALA E 145 5636 4738 3703 -722 -285 559 O ATOM 1153 CB ALA A 145 45.709 47.256 56.209 1.00 31.60 C ANISOU 1153 CB ALA E 145 4304 4341 3363 -118 479 935 C ATOM 1154 N PHE A 146 46.017 49.587 54.792 1.00 32.14 N ANISOU 1154 N PHE E 146 4142 4992 3078 -336 1125 474 N ATOM 1155 CA PHE A 146 46.391 50.823 54.107 1.00 32.43 C ANISOU 1155 CA PHE E 146 4183 5097 3041 -475 853 228 C ATOM 1156 C PHE A 146 47.911 50.975 54.070 1.00 31.27 C ANISOU 1156 C PHE E 146 4169 4422 3293 -471 846 212 C ATOM 1157 O PHE A 146 48.416 52.065 53.756 1.00 35.15 O ANISOU 1157 O PHE E 146 4625 4822 3907 -252 620 -501 O ATOM 1158 CB PHE A 146 45.805 52.096 54.725 1.00 32.34 C ANISOU 1158 CB PHE E 146 4126 5133 3028 -936 384 31 C ATOM 1159 CG PHE A 146 44.324 52.229 54.399 1.00 36.84 C ANISOU 1159 CG PHE E 146 4333 5777 3886 -1021 -100 160 C ATOM 1160 CD1 PHE A 146 43.921 52.675 53.155 1.00 42.68 C ANISOU 1160 CD1 PHE E 146 4466 7257 4494 -1295 -187 -795 C ATOM 1161 CD2 PHE A 146 43.373 51.904 55.346 1.00 34.07 C ANISOU 1161 CD2 PHE E 146 3601 5135 4210 121 -789 -10 C ATOM 1162 CE1 PHE A 146 42.574 52.793 52.864 1.00 45.34 C ANISOU 1162 CE1 PHE E 146 4476 7702 5049 -1527 -157 -1240 C ATOM 1163 CE2 PHE A 146 42.029 52.019 55.074 1.00 35.10 C ANISOU 1163 CE2 PHE E 146 3813 5445 4079 116 -1337 176 C ATOM 1164 CZ PHE A 146 41.641 52.468 53.829 1.00 39.62 C ANISOU 1164 CZ PHE E 146 4236 6578 4238 -695 -785 -513 C ATOM 1165 N ASN A 147 48.635 49.907 54.377 1.00 31.88 N ANISOU 1165 N ASN E 147 4445 4628 3040 -483 137 78 N ATOM 1166 CA ASN A 147 50.085 50.015 54.211 1.00 31.70 C ANISOU 1166 CA ASN E 147 4438 4565 3042 -688 276 -26 C ATOM 1167 C ASN A 147 50.473 50.145 52.745 1.00 34.38 C ANISOU 1167 C ASN E 147 4673 5296 3095 -405 194 -487 C ATOM 1168 O ASN A 147 49.843 49.620 51.818 1.00 40.03 O ANISOU 1168 O ASN E 147 6438 5686 3087 254 632 390 O ATOM 1169 CB ASN A 147 50.750 48.769 54.801 1.00 30.43 C ANISOU 1169 CB ASN E 147 4384 4252 2927 -123 -373 45 C ATOM 1170 CG ASN A 147 50.467 48.688 56.290 1.00 30.24 C ANISOU 1170 CG ASN E 147 4651 3873 2967 1 -136 262 C ATOM 1171 OD1 ASN A 147 51.230 49.307 57.045 1.00 32.49 O ANISOU 1171 OD1 ASN E 147 4299 4953 3093 -219 -486 341 O ATOM 1172 ND2 ASN A 147 49.418 47.967 56.670 1.00 30.25 N ANISOU 1172 ND2 ASN E 147 4554 3366 3574 -380 304 317 N ATOM 1173 N GLU A 148 51.564 50.854 52.445 1.00 36.52 N ANISOU 1173 N GLU E 148 4784 5165 3926 -576 621 -647 N ATOM 1174 CA GLU A 148 51.922 50.978 51.044 1.00 37.62 C ANISOU 1174 CA GLU E 148 4800 5496 3996 -506 795 -628 C ATOM 1175 C GLU A 148 52.928 49.927 50.623 1.00 35.13 C ANISOU 1175 C GLU E 148 4193 5501 3653 -282 383 -550 C ATOM 1176 O GLU A 148 53.529 49.292 51.482 1.00 36.10 O ANISOU 1176 O GLU E 148 4942 5346 3428 -441 92 -134 O ATOM 1177 CB GLU A 148 52.423 52.413 50.824 1.00 44.63 C ANISOU 1177 CB GLU E 148 6139 5477 5341 -679 1299 -1418 C ATOM 1178 CG GLU A 148 51.273 53.126 50.092 1.00 62.51 C ANISOU 1178 CG GLU E 148 10150 6335 7266 -2672 -1198 -738 C ATOM 1179 CD GLU A 148 51.470 54.618 49.960 1.00 62.28 C ANISOU 1179 CD GLU E 148 10737 6366 6563 -2751 -91 -994 C ATOM 1180 OE1 GLU A 148 51.915 54.994 48.849 1.00 58.46 O ANISOU 1180 OE1 GLU E 148 8529 7728 5956 -589 -931 32 O ATOM 1181 OE2 GLU A 148 51.174 55.318 50.958 1.00 53.92 O ANISOU 1181 OE2 GLU E 148 7807 6685 5995 -228 -852 -345 O ATOM 1182 N PRO A 149 53.094 49.751 49.324 1.00 32.87 N ANISOU 1182 N PRO E 149 3807 5083 3601 -97 -179 -132 N ATOM 1183 CA PRO A 149 54.174 48.911 48.824 1.00 32.24 C ANISOU 1183 CA PRO E 149 4390 4418 3444 -319 -805 463 C ATOM 1184 C PRO A 149 55.492 49.423 49.408 1.00 31.02 C ANISOU 1184 C PRO E 149 3812 4107 3866 -8 -140 -98 C ATOM 1185 O PRO A 149 55.655 50.630 49.584 1.00 30.07 O ANISOU 1185 O PRO E 149 3975 4089 3359 -109 69 11 O ATOM 1186 CB PRO A 149 54.123 49.175 47.330 1.00 31.62 C ANISOU 1186 CB PRO E 149 4043 4309 3661 -329 -144 -207 C ATOM 1187 CG PRO A 149 52.700 49.543 47.046 1.00 34.44 C ANISOU 1187 CG PRO E 149 4321 5187 3579 -832 -344 -382 C ATOM 1188 CD PRO A 149 52.297 50.361 48.246 1.00 35.77 C ANISOU 1188 CD PRO E 149 4150 5686 3756 -783 18 -291 C ATOM 1189 N ALA A 150 56.405 48.521 49.718 1.00 31.18 N ANISOU 1189 N ALA E 150 3700 4110 4039 -107 -144 333 N ATOM 1190 CA ALA A 150 57.719 48.753 50.323 1.00 28.85 C ANISOU 1190 CA ALA E 150 3788 3648 3525 217 -129 -142 C ATOM 1191 C ALA A 150 57.552 49.253 51.750 1.00 30.57 C ANISOU 1191 C ALA E 150 4376 3691 3548 371 -19 -112 C ATOM 1192 O ALA A 150 58.478 49.855 52.290 1.00 31.66 O ANISOU 1192 O ALA E 150 4014 4233 3783 29 -88 363 O ATOM 1193 CB ALA A 150 58.589 49.710 49.524 1.00 31.71 C ANISOU 1193 CB ALA E 150 3074 4424 4551 -839 652 -1116 C ATOM 1194 N SER A 151 56.389 48.998 52.358 1.00 29.94 N ANISOU 1194 N SER E 151 3870 4227 3279 -100 -355 23 N ATOM 1195 CA SER A 151 56.265 49.245 53.780 1.00 28.79 C ANISOU 1195 CA SER E 151 3667 3912 3359 -130 -366 214 C ATOM 1196 C SER A 151 57.274 48.359 54.517 1.00 27.85 C ANISOU 1196 C SER E 151 3270 4162 3148 -5 -137 69 C ATOM 1197 O SER A 151 57.511 47.255 54.023 1.00 28.87 O ANISOU 1197 O SER E 151 3544 4607 2820 -650 -615 285 O ATOM 1198 CB SER A 151 54.891 48.877 54.349 1.00 29.68 C ANISOU 1198 CB SER E 151 3367 4612 3298 -169 -518 533 C ATOM 1199 OG SER A 151 53.892 49.833 54.026 1.00 34.72 O ANISOU 1199 OG SER E 151 3690 4948 4553 -486 -1143 1135 O ATOM 1200 N SER A 152 57.780 48.826 55.645 1.00 29.45 N ANISOU 1200 N SER E 152 3378 3942 3869 9 -659 386 N ATOM 1201 CA SER A 152 58.523 47.982 56.572 1.00 29.19 C ANISOU 1201 CA SER E 152 3469 4067 3556 16 -643 433 C ATOM 1202 C SER A 152 57.680 46.794 57.012 1.00 29.48 C ANISOU 1202 C SER E 152 3728 3893 3582 34 -663 526 C ATOM 1203 O SER A 152 56.475 46.925 57.299 1.00 29.07 O ANISOU 1203 O SER E 152 3750 3599 3698 168 -539 744 O ATOM 1204 CB SER A 152 58.956 48.780 57.811 1.00 24.29 C ANISOU 1204 CB SER E 152 2261 4031 2936 151 489 373 C ATOM 1205 OG SER A 152 59.482 47.864 58.771 1.00 30.65 O ANISOU 1205 OG SER E 152 4423 4323 2899 148 -104 292 O ATOM 1206 N LEU A 153 58.293 45.610 57.102 1.00 29.06 N ANISOU 1206 N LEU E 153 4048 4037 2954 -219 -370 477 N ATOM 1207 CA LEU A 153 57.557 44.429 57.560 1.00 29.26 C ANISOU 1207 CA LEU E 153 3685 3994 3440 -261 -742 284 C ATOM 1208 C LEU A 153 57.349 44.521 59.063 1.00 29.11 C ANISOU 1208 C LEU E 153 3316 4253 3491 209 -558 101 C ATOM 1209 O LEU A 153 56.649 43.703 59.664 1.00 34.08 O ANISOU 1209 O LEU E 153 4357 4097 4497 304 441 284 O ATOM 1210 CB LEU A 153 58.307 43.155 57.227 1.00 33.10 C ANISOU 1210 CB LEU E 153 3749 4053 4775 -216 131 228 C ATOM 1211 CG LEU A 153 57.943 42.384 55.952 1.00 40.02 C ANISOU 1211 CG LEU E 153 5950 5263 3992 -2329 133 679 C ATOM 1212 CD1 LEU A 153 57.333 43.266 54.880 1.00 36.67 C ANISOU 1212 CD1 LEU E 153 6870 4004 3059 -1329 1626 -51 C ATOM 1213 CD2 LEU A 153 59.160 41.650 55.395 1.00 35.55 C ANISOU 1213 CD2 LEU E 153 2763 5853 4889 200 331 967 C ATOM 1214 N ALA A 154 57.975 45.511 59.693 1.00 28.86 N ANISOU 1214 N ALA E 154 3772 3811 3384 -100 -231 365 N ATOM 1215 CA ALA A 154 57.726 45.719 61.118 1.00 30.37 C ANISOU 1215 CA ALA E 154 3746 4496 3297 -369 -386 198 C ATOM 1216 C ALA A 154 56.893 46.967 61.335 1.00 31.22 C ANISOU 1216 C ALA E 154 4347 4666 2850 -661 -348 317 C ATOM 1217 O ALA A 154 56.866 47.497 62.451 1.00 34.75 O ANISOU 1217 O ALA E 154 5023 4855 3323 -392 -1059 947 O ATOM 1218 CB ALA A 154 59.043 45.838 61.876 1.00 34.29 C ANISOU 1218 CB ALA E 154 4068 5230 3729 -356 -793 160 C ATOM 1219 N SER A 155 56.214 47.491 60.301 1.00 27.85 N ANISOU 1219 N SER E 155 3657 4121 2802 -121 7 9 N ATOM 1220 CA SER A 155 55.519 48.768 60.552 1.00 29.11 C ANISOU 1220 CA SER E 155 3680 4341 3039 -299 -34 162 C ATOM 1221 C SER A 155 54.366 48.538 61.514 1.00 31.02 C ANISOU 1221 C SER E 155 3935 4240 3611 -131 316 360 C ATOM 1222 O SER A 155 53.912 47.408 61.698 1.00 29.07 O ANISOU 1222 O SER E 155 4093 3993 2960 -410 506 489 O ATOM 1223 CB SER A 155 55.100 49.345 59.200 1.00 28.66 C ANISOU 1223 CB SER E 155 3994 4035 2860 -630 -380 718 C ATOM 1224 OG SER A 155 54.359 48.324 58.517 1.00 30.95 O ANISOU 1224 OG SER E 155 3936 4581 3242 -12 18 839 O ATOM 1225 N ARG A 156 53.860 49.580 62.166 1.00 27.27 N ANISOU 1225 N ARG E 156 3264 3955 3142 464 -1 470 N ATOM 1226 CA ARG A 156 52.840 49.491 63.201 1.00 28.27 C ANISOU 1226 CA ARG E 156 3079 4309 3353 470 18 544 C ATOM 1227 C ARG A 156 51.651 50.404 62.905 1.00 27.82 C ANISOU 1227 C ARG E 156 2907 3931 3731 789 -28 347 C ATOM 1228 O ARG A 156 51.705 51.167 61.934 1.00 31.42 O ANISOU 1228 O ARG E 156 4483 3701 3754 -136 705 427 O ATOM 1229 CB ARG A 156 53.447 49.887 64.554 1.00 30.35 C ANISOU 1229 CB ARG E 156 4010 4532 2991 289 -109 187 C ATOM 1230 CG ARG A 156 54.522 48.903 65.036 1.00 32.56 C ANISOU 1230 CG ARG E 156 4808 4586 2978 -232 -361 625 C ATOM 1231 CD ARG A 156 53.779 47.692 65.602 1.00 36.21 C ANISOU 1231 CD ARG E 156 5806 4472 3480 -146 -508 297 C ATOM 1232 NE ARG A 156 54.573 46.478 65.540 1.00 40.57 N ANISOU 1232 NE ARG E 156 6347 4722 4348 -532 -933 182 N ATOM 1233 CZ ARG A 156 54.130 45.287 65.928 1.00 40.13 C ANISOU 1233 CZ ARG E 156 5796 4720 4733 -761 -573 57 C ATOM 1234 NH1 ARG A 156 52.899 45.151 66.403 1.00 37.87 N ANISOU 1234 NH1 ARG E 156 5173 5635 3582 -493 -1594 379 N ATOM 1235 NH2 ARG A 156 54.955 44.258 65.824 1.00 40.93 N ANISOU 1235 NH2 ARG E 156 6082 4379 5092 -499 -635 1412 N ATOM 1236 N THR A 157 50.611 50.325 63.746 1.00 30.93 N ANISOU 1236 N THR E 157 3402 4458 3890 186 411 340 N ATOM 1237 CA THR A 157 49.369 51.060 63.558 1.00 31.02 C ANISOU 1237 CA THR E 157 3752 4415 3620 -155 491 575 C ATOM 1238 C THR A 157 49.659 52.543 63.414 1.00 30.19 C ANISOU 1238 C THR E 157 3483 4497 3492 48 735 555 C ATOM 1239 O THR A 157 50.446 53.075 64.209 1.00 35.36 O ANISOU 1239 O THR E 157 4388 4808 4240 93 111 919 O ATOM 1240 CB THR A 157 48.397 50.839 64.733 1.00 30.76 C ANISOU 1240 CB THR E 157 3447 4291 3950 77 433 279 C ATOM 1241 OG1 THR A 157 48.115 49.437 64.815 1.00 35.13 O ANISOU 1241 OG1 THR E 157 6169 4069 3109 -194 326 -108 O ATOM 1242 CG2 THR A 157 47.091 51.570 64.498 1.00 28.06 C ANISOU 1242 CG2 THR E 157 3457 4294 2910 150 280 74 C ATOM 1243 N ARG A 158 49.073 53.201 62.421 1.00 30.88 N ANISOU 1243 N ARG E 158 3677 4516 3538 -184 889 460 N ATOM 1244 CA ARG A 158 49.453 54.582 62.143 1.00 31.76 C ANISOU 1244 CA ARG E 158 3594 4736 3736 29 1033 278 C ATOM 1245 C ARG A 158 48.488 55.227 61.154 1.00 32.73 C ANISOU 1245 C ARG E 158 3919 4475 4043 -104 855 287 C ATOM 1246 O ARG A 158 47.702 54.547 60.514 1.00 34.08 O ANISOU 1246 O ARG E 158 4434 4672 3844 -90 510 247 O ATOM 1247 CB ARG A 158 50.878 54.657 61.580 1.00 34.38 C ANISOU 1247 CB ARG E 158 3660 5187 4217 9 1226 540 C ATOM 1248 CG ARG A 158 51.041 54.179 60.139 1.00 36.00 C ANISOU 1248 CG ARG E 158 4251 5275 4153 -123 1535 379 C ATOM 1249 CD ARG A 158 52.484 53.786 59.853 1.00 34.46 C ANISOU 1249 CD ARG E 158 4145 5227 3722 -368 735 1012 C ATOM 1250 NE ARG A 158 52.748 53.356 58.466 1.00 33.95 N ANISOU 1250 NE ARG E 158 4630 4450 3821 -159 1221 798 N ATOM 1251 CZ ARG A 158 52.517 52.107 58.055 1.00 36.78 C ANISOU 1251 CZ ARG E 158 6016 4217 3740 -394 521 541 C ATOM 1252 NH1 ARG A 158 52.023 51.242 58.946 1.00 31.31 N ANISOU 1252 NH1 ARG E 158 3855 4426 3616 -117 9 704 N ATOM 1253 NH2 ARG A 158 52.760 51.736 56.818 1.00 31.35 N ANISOU 1253 NH2 ARG E 158 3919 4507 3486 432 -249 696 N ATOM 1254 N ILE A 159 48.567 56.543 61.031 1.00 35.47 N ANISOU 1254 N ILE E 159 4542 4492 4441 -50 1111 179 N ATOM 1255 CA ILE A 159 47.738 57.268 60.090 1.00 35.07 C ANISOU 1255 CA ILE E 159 4407 4135 4782 416 896 -14 C ATOM 1256 C ILE A 159 48.423 57.244 58.718 1.00 37.45 C ANISOU 1256 C ILE E 159 4806 4741 4684 -268 875 -130 C ATOM 1257 O ILE A 159 49.654 57.290 58.659 1.00 39.31 O ANISOU 1257 O ILE E 159 4878 5013 5044 341 1309 -5 O ATOM 1258 CB ILE A 159 47.505 58.733 60.481 1.00 39.65 C ANISOU 1258 CB ILE E 159 5410 4542 5112 -294 284 485 C ATOM 1259 CG1 ILE A 159 46.428 59.405 59.623 1.00 41.71 C ANISOU 1259 CG1 ILE E 159 5362 5294 5191 -823 877 -95 C ATOM 1260 CG2 ILE A 159 48.810 59.515 60.431 1.00 38.23 C ANISOU 1260 CG2 ILE E 159 5699 3317 5509 -405 418 757 C ATOM 1261 CD1 ILE A 159 45.952 60.728 60.187 1.00 40.62 C ANISOU 1261 CD1 ILE E 159 5716 4824 4893 -491 821 -362 C ATOM 1262 N LYS A 160 47.608 57.173 57.685 1.00 40.97 N ANISOU 1262 N LYS E 160 5651 5057 4861 -739 423 378 N ATOM 1263 CA LYS A 160 47.989 57.138 56.298 1.00 43.00 C ANISOU 1263 CA LYS E 160 6809 4735 4795 -446 519 202 C ATOM 1264 C LYS A 160 47.138 58.113 55.468 1.00 44.52 C ANISOU 1264 C LYS E 160 6225 5368 5323 -675 1661 -868 C ATOM 1265 O LYS A 160 45.957 58.309 55.768 1.00 46.37 O ANISOU 1265 O LYS E 160 6438 5703 5476 -894 1992 -589 O ATOM 1266 CB LYS A 160 47.821 55.742 55.671 1.00 40.85 C ANISOU 1266 CB LYS E 160 5643 4962 4918 -153 508 397 C ATOM 1267 CG LYS A 160 48.734 54.644 56.176 1.00 43.72 C ANISOU 1267 CG LYS E 160 6473 4746 5394 -387 258 512 C ATOM 1268 CD LYS A 160 50.160 55.144 56.332 1.00 47.22 C ANISOU 1268 CD LYS E 160 5920 5840 6181 -889 443 211 C ATOM 1269 CE LYS A 160 51.015 54.759 55.145 1.00 51.24 C ANISOU 1269 CE LYS E 160 6579 6643 6247 -1400 612 143 C ATOM 1270 NZ LYS A 160 50.616 55.354 53.843 1.00 52.76 N ANISOU 1270 NZ LYS E 160 8506 5514 6026 -562 306 357 N ATOM 1271 N THR A 161 47.795 58.653 54.439 1.00 46.07 N ANISOU 1271 N THR E 161 6196 5573 5734 95 1582 -914 N ATOM 1272 CA THR A 161 47.152 59.461 53.414 1.00 50.03 C ANISOU 1272 CA THR E 161 6913 6464 5630 -308 1964 -1436 C ATOM 1273 C THR A 161 46.670 58.587 52.270 1.00 49.72 C ANISOU 1273 C THR E 161 6611 6875 5404 41 1749 -1746 C ATOM 1274 O THR A 161 47.476 57.986 51.568 1.00 51.50 O ANISOU 1274 O THR E 161 5747 7772 6050 61 770 -337 O ATOM 1275 CB THR A 161 48.132 60.503 52.855 1.00 50.46 C ANISOU 1275 CB THR E 161 6768 6590 5816 -161 1539 -1616 C ATOM 1276 OG1 THR A 161 48.634 61.276 53.955 1.00 55.20 O ANISOU 1276 OG1 THR E 161 6600 7971 6401 191 1818 -728 O ATOM 1277 CG2 THR A 161 47.427 61.459 51.907 1.00 52.69 C ANISOU 1277 CG2 THR E 161 4577 8539 6904 -166 2426 -3197 C ATOM 1278 N LEU A 162 45.372 58.461 52.061 1.00 50.34 N ANISOU 1278 N LEU E 162 6449 7256 5423 -457 1918 -1694 N ATOM 1279 CA LEU A 162 44.912 57.447 51.109 1.00 52.65 C ANISOU 1279 CA LEU E 162 6286 8091 5628 -161 1548 -1472 C ATOM 1280 C LEU A 162 45.420 57.672 49.696 1.00 52.23 C ANISOU 1280 C LEU E 162 5897 8430 5516 386 1306 -1358 C ATOM 1281 O LEU A 162 45.718 58.824 49.355 1.00 62.49 O ANISOU 1281 O LEU E 162 8039 8700 7004 -362 1496 -2942 O ATOM 1282 CB LEU A 162 43.378 57.440 51.160 1.00 53.19 C ANISOU 1282 CB LEU E 162 6314 8196 5699 -499 1777 -1522 C ATOM 1283 CG LEU A 162 42.809 57.169 52.556 1.00 52.93 C ANISOU 1283 CG LEU E 162 6606 7838 5667 13 1777 -1363 C ATOM 1284 CD1 LEU A 162 41.304 57.026 52.476 1.00 55.07 C ANISOU 1284 CD1 LEU E 162 6561 7050 7311 156 2360 -995 C ATOM 1285 CD2 LEU A 162 43.508 55.945 53.122 1.00 57.05 C ANISOU 1285 CD2 LEU E 162 8865 8972 3838 -1552 778 -482 C ATOM 1286 N THR A 163 45.535 56.636 48.861 1.00 59.10 N ANISOU 1286 N THR E 163 6302 9840 6313 -767 1535 -340 N ATOM 1287 CA THR A 163 45.968 56.877 47.479 1.00 67.97 C ANISOU 1287 CA THR E 163 8737 10769 6321 -2093 2043 -691 C ATOM 1288 C THR A 163 44.775 57.221 46.585 1.00 72.03 C ANISOU 1288 C THR E 163 9650 11375 6344 -2327 1519 -773 C ATOM 1289 O THR A 163 43.665 56.753 46.839 1.00 63.46 O ANISOU 1289 O THR E 163 9754 9523 4834 -2098 377 -773 O ATOM 1290 CB THR A 163 46.704 55.681 46.849 1.00 67.87 C ANISOU 1290 CB THR E 163 8532 10536 6719 -1473 2303 -297 C ATOM 1291 OG1 THR A 163 45.754 54.654 46.506 1.00 77.41 O ANISOU 1291 OG1 THR E 163 9711 11701 8001 -1467 -319 417 O ATOM 1292 CG2 THR A 163 47.709 55.043 47.804 1.00 61.67 C ANISOU 1292 CG2 THR E 163 6295 9323 7815 -351 2422 -293 C ATOM 1293 N HIS A 164 44.992 58.021 45.554 1.00 73.18 N ANISOU 1293 N HIS E 164 8953 11950 6903 -2104 1660 -1261 N ATOM 1294 CA HIS A 164 43.968 58.373 44.580 1.00 79.94 C ANISOU 1294 CA HIS E 164 10826 12269 7277 -2713 673 -1193 C ATOM 1295 C HIS A 164 43.217 57.131 44.115 1.00 75.86 C ANISOU 1295 C HIS E 164 10789 12290 5744 -2880 480 -1278 C ATOM 1296 O HIS A 164 41.994 57.078 44.133 1.00 68.07 O ANISOU 1296 O HIS E 164 10732 12117 3012 -3617 -310 -48 O ATOM 1297 CB HIS A 164 44.599 59.053 43.375 1.00 86.94 C ANISOU 1297 CB HIS E 164 11525 12664 8842 -3047 658 -3009 C ATOM 1298 CG HIS A 164 43.794 60.137 42.733 1.00 98.83 C ANISOU 1298 CG HIS E 164 13596 13511 10445 -4228 -13 -3227 C ATOM 1299 ND1 HIS A 164 43.003 61.020 43.445 1.00104.21 N ANISOU 1299 ND1 HIS E 164 14138 14089 11368 -5006 -781 -2512 N ATOM 1300 CD2 HIS A 164 43.666 60.483 41.423 1.00102.90 C ANISOU 1300 CD2 HIS E 164 14181 14168 10747 -4985 -1232 -3005 C ATOM 1301 CE1 HIS A 164 42.421 61.866 42.603 1.00107.01 C ANISOU 1301 CE1 HIS E 164 14524 14378 11757 -5151 -1430 -2348 C ATOM 1302 NE2 HIS A 164 42.807 61.562 41.368 1.00106.55 N ANISOU 1302 NE2 HIS E 164 14544 14352 11590 -5250 -1668 -2462 N ATOM 1303 N ASP A 165 43.973 56.110 43.723 1.00 72.18 N ANISOU 1303 N ASP E 165 9561 12182 5684 -2138 1484 -1623 N ATOM 1304 CA ASP A 165 43.356 54.832 43.372 1.00 77.60 C ANISOU 1304 CA ASP E 165 11006 12333 6146 -1786 1999 -1092 C ATOM 1305 C ASP A 165 42.423 54.331 44.462 1.00 74.61 C ANISOU 1305 C ASP E 165 9901 12590 5858 -1162 1374 -630 C ATOM 1306 O ASP A 165 41.407 53.675 44.211 1.00 76.73 O ANISOU 1306 O ASP E 165 10896 11798 6461 -813 831 -553 O ATOM 1307 CB ASP A 165 44.464 53.812 43.104 1.00 85.81 C ANISOU 1307 CB ASP E 165 12889 12470 7243 -2487 3699 -1308 C ATOM 1308 CG ASP A 165 45.379 54.304 41.993 1.00 94.21 C ANISOU 1308 CG ASP E 165 14915 12585 8295 -2725 5300 -1274 C ATOM 1309 OD1 ASP A 165 45.585 55.536 41.914 1.00108.17 O ANISOU 1309 OD1 ASP E 165 16354 12710 12037 -2263 7768 -1380 O ATOM 1310 OD2 ASP A 165 45.870 53.465 41.208 1.00 97.35 O ANISOU 1310 OD2 ASP E 165 17132 13617 6241 -2539 4483 -704 O ATOM 1311 N THR A 166 42.752 54.632 45.722 1.00 74.67 N ANISOU 1311 N THR E 166 9546 12954 5873 -1010 1398 -554 N ATOM 1312 CA THR A 166 41.877 54.151 46.790 1.00 68.60 C ANISOU 1312 CA THR E 166 7758 12833 5476 -437 336 -156 C ATOM 1313 C THR A 166 40.689 55.081 47.010 1.00 68.94 C ANISOU 1313 C THR E 166 7970 12883 5341 -542 -156 716 C ATOM 1314 O THR A 166 39.586 54.589 47.247 1.00 68.20 O ANISOU 1314 O THR E 166 7559 12731 5624 -692 -530 1061 O ATOM 1315 CB THR A 166 42.591 53.979 48.147 1.00 72.37 C ANISOU 1315 CB THR E 166 9155 12702 5639 -1043 -61 -362 C ATOM 1316 OG1 THR A 166 43.754 53.153 47.998 1.00 75.94 O ANISOU 1316 OG1 THR E 166 8668 12928 7257 -920 327 -1882 O ATOM 1317 CG2 THR A 166 41.637 53.287 49.117 1.00 74.00 C ANISOU 1317 CG2 THR E 166 9650 13247 5218 -1212 624 39 C ATOM 1318 N ARG A 167 40.904 56.393 46.950 1.00 69.78 N ANISOU 1318 N ARG E 167 8682 12889 4941 -548 562 511 N ATOM 1319 CA ARG A 167 39.750 57.275 47.125 1.00 71.95 C ANISOU 1319 CA ARG E 167 8780 12745 5814 -629 917 -407 C ATOM 1320 C ARG A 167 38.794 57.005 45.958 1.00 74.23 C ANISOU 1320 C ARG E 167 8941 13769 5493 -1343 846 -439 C ATOM 1321 O ARG A 167 37.594 56.783 46.109 1.00 78.16 O ANISOU 1321 O ARG E 167 8228 14833 6636 -2496 226 -189 O ATOM 1322 CB ARG A 167 40.103 58.750 47.170 1.00 77.63 C ANISOU 1322 CB ARG E 167 9638 12639 7221 -665 1124 -961 C ATOM 1323 CG ARG A 167 41.475 59.158 47.636 1.00 81.73 C ANISOU 1323 CG ARG E 167 10758 12178 8116 -257 -90 -165 C ATOM 1324 CD ARG A 167 41.532 59.545 49.100 1.00 87.05 C ANISOU 1324 CD ARG E 167 12778 11970 8326 -590 -56 301 C ATOM 1325 NE ARG A 167 42.128 60.830 49.412 1.00 92.77 N ANISOU 1325 NE ARG E 167 14409 11696 9144 -662 -296 517 N ATOM 1326 CZ ARG A 167 43.238 61.162 50.041 1.00 95.37 C ANISOU 1326 CZ ARG E 167 15380 11275 9580 -374 -904 1145 C ATOM 1327 NH1 ARG A 167 44.092 60.281 50.542 1.00 94.39 N ANISOU 1327 NH1 ARG E 167 15117 11435 9312 -231 -1424 1589 N ATOM 1328 NH2 ARG A 167 43.565 62.447 50.199 1.00110.50 N ANISOU 1328 NH2 ARG E 167 19973 11216 10798 -1808 -3257 4175 N ATOM 1329 N VAL A 168 39.414 57.025 44.785 1.00 80.95 N ANISOU 1329 N VAL E 168 10812 14447 5497 -2185 1339 -777 N ATOM 1330 CA VAL A 168 38.740 56.712 43.545 1.00 84.04 C ANISOU 1330 CA VAL E 168 12024 14446 5461 -2415 1114 -475 C ATOM 1331 C VAL A 168 37.918 55.441 43.681 1.00 84.40 C ANISOU 1331 C VAL E 168 12875 13943 5251 -2397 603 -261 C ATOM 1332 O VAL A 168 36.706 55.485 43.499 1.00 89.82 O ANISOU 1332 O VAL E 168 12314 15343 6472 -1740 2248 -1764 O ATOM 1333 CB VAL A 168 39.746 56.519 42.394 1.00 88.21 C ANISOU 1333 CB VAL E 168 13524 14378 5615 -3379 1719 -807 C ATOM 1334 CG1 VAL A 168 39.160 55.582 41.348 1.00 86.04 C ANISOU 1334 CG1 VAL E 168 14085 12505 6102 -3940 1902 -833 C ATOM 1335 CG2 VAL A 168 40.117 57.872 41.807 1.00 86.16 C ANISOU 1335 CG2 VAL E 168 11934 14947 5855 -1949 1013 -643 C ATOM 1336 N ALA A 169 38.564 54.333 44.005 1.00 91.57 N ANISOU 1336 N ALA E 169 15364 13755 5673 -3339 -113 804 N ATOM 1337 CA ALA A 169 37.845 53.069 44.151 1.00 95.17 C ANISOU 1337 CA ALA E 169 16049 13584 6528 -3524 1372 390 C ATOM 1338 C ALA A 169 36.930 53.012 45.371 1.00102.07 C ANISOU 1338 C ALA E 169 17256 14134 7393 -4115 2423 545 C ATOM 1339 O ALA A 169 36.294 51.992 45.672 1.00106.85 O ANISOU 1339 O ALA E 169 19119 13265 8212 -5055 4172 -586 O ATOM 1340 CB ALA A 169 38.873 51.943 44.185 1.00103.83 C ANISOU 1340 CB ALA E 169 17666 14087 7697 -4586 2652 87 C ATOM 1341 N ASN A 170 36.820 54.110 46.129 1.00106.51 N ANISOU 1341 N ASN E 170 18134 14836 7500 -4499 2029 1062 N ATOM 1342 CA ASN A 170 35.904 54.067 47.276 1.00109.84 C ANISOU 1342 CA ASN E 170 18334 15718 7681 -5454 2226 978 C ATOM 1343 C ASN A 170 34.899 55.213 47.195 1.00112.59 C ANISOU 1343 C ASN E 170 18483 15901 8396 -5599 1805 941 C ATOM 1344 O ASN A 170 33.900 55.242 47.938 1.00116.92 O ANISOU 1344 O ASN E 170 21676 16275 6474 -7495 3171 1897 O ATOM 1345 CB ASN A 170 36.675 54.087 48.596 1.00107.00 C ANISOU 1345 CB ASN E 170 17223 15854 7580 -4994 2601 690 C ATOM 1346 CG ASN A 170 37.200 52.737 49.047 1.00104.44 C ANISOU 1346 CG ASN E 170 16237 15763 7682 -4573 2828 452 C ATOM 1347 OD1 ASN A 170 36.887 51.687 48.494 1.00109.05 O ANISOU 1347 OD1 ASN E 170 16961 15826 8648 -4927 1518 639 O ATOM 1348 ND2 ASN A 170 38.041 52.728 50.086 1.00 90.72 N ANISOU 1348 ND2 ASN E 170 11283 14971 8214 -2336 4491 -806 N ATOM 1349 N SER A 171 35.115 56.163 46.288 1.00110.23 N ANISOU 1349 N SER E 171 17178 15892 8812 -4576 354 679 N ATOM 1350 CA SER A 171 34.216 57.309 46.137 1.00111.31 C ANISOU 1350 CA SER E 171 17038 15580 9674 -4280 -170 887 C ATOM 1351 C SER A 171 32.753 56.905 45.973 1.00111.01 C ANISOU 1351 C SER E 171 17047 15238 9894 -4199 -5 780 C ATOM 1352 O SER A 171 31.872 57.708 46.309 1.00115.28 O ANISOU 1352 O SER E 171 17036 16296 10469 -5295 -2437 1977 O ATOM 1353 CB SER A 171 34.643 58.181 44.948 1.00111.07 C ANISOU 1353 CB SER E 171 16913 15240 10048 -3695 -673 693 C ATOM 1354 OG SER A 171 35.748 57.634 44.242 1.00113.97 O ANISOU 1354 OG SER E 171 18978 14524 9800 -4234 653 538 O ATOM 1355 N ARG A 172 32.494 55.705 45.473 1.00110.85 N ANISOU 1355 N ARG E 172 17451 14821 9847 -3968 200 169 N ATOM 1356 CA ARG A 172 31.195 55.089 45.258 1.00111.98 C ANISOU 1356 CA ARG E 172 17665 14906 9976 -4058 -794 10 C ATOM 1357 C ARG A 172 30.398 55.020 46.553 1.00111.03 C ANISOU 1357 C ARG E 172 16172 15559 10454 -3932 -939 -262 C ATOM 1358 O ARG A 172 29.203 55.302 46.657 1.00112.06 O ANISOU 1358 O ARG E 172 16730 16836 9010 -5744 -1975 -11 O ATOM 1359 CB ARG A 172 31.341 53.688 44.660 1.00116.98 C ANISOU 1359 CB ARG E 172 19431 14785 10230 -3822 -1089 65 C ATOM 1360 CG ARG A 172 31.925 52.618 45.561 1.00128.53 C ANISOU 1360 CG ARG E 172 22686 15019 11132 -4938 -1604 -14 C ATOM 1361 CD ARG A 172 30.975 51.453 45.789 1.00133.23 C ANISOU 1361 CD ARG E 172 24043 14646 11932 -4849 -1006 -529 C ATOM 1362 NE ARG A 172 31.601 50.156 45.564 1.00140.27 N ANISOU 1362 NE ARG E 172 25830 14832 12636 -5439 -672 -487 N ATOM 1363 CZ ARG A 172 31.021 48.959 45.528 1.00142.46 C ANISOU 1363 CZ ARG E 172 26138 14766 13223 -5418 -605 -69 C ATOM 1364 NH1 ARG A 172 29.701 48.814 45.710 1.00146.19 N ANISOU 1364 NH1 ARG E 172 26094 15488 13962 -4749 -833 543 N ATOM 1365 NH2 ARG A 172 31.747 47.862 45.309 1.00148.11 N ANISOU 1365 NH2 ARG E 172 27294 15026 13955 -5942 -745 288 N ATOM 1366 N PHE A 173 31.105 54.624 47.618 1.00 99.08 N ANISOU 1366 N PHE E 173 12166 15154 10327 -1652 -98 -625 N ATOM 1367 CA PHE A 173 30.397 54.681 48.891 1.00 95.56 C ANISOU 1367 CA PHE E 173 11181 14684 10441 -1264 -294 -16 C ATOM 1368 C PHE A 173 30.175 56.131 49.252 1.00 93.43 C ANISOU 1368 C PHE E 173 10204 14403 10892 -1050 -663 -317 C ATOM 1369 O PHE A 173 29.124 56.492 49.786 1.00 90.44 O ANISOU 1369 O PHE E 173 8772 14217 11373 -1673 -2556 -482 O ATOM 1370 CB PHE A 173 31.195 53.937 49.956 1.00 90.93 C ANISOU 1370 CB PHE E 173 10884 13929 9734 -1337 138 461 C ATOM 1371 CG PHE A 173 31.578 52.557 49.428 1.00 92.38 C ANISOU 1371 CG PHE E 173 11175 14171 9755 -1241 -225 1018 C ATOM 1372 CD1 PHE A 173 30.751 51.469 49.627 1.00 91.14 C ANISOU 1372 CD1 PHE E 173 11094 14284 9251 -1076 -347 1420 C ATOM 1373 CD2 PHE A 173 32.763 52.394 48.740 1.00 91.66 C ANISOU 1373 CD2 PHE E 173 10907 13980 9941 -1040 -423 1644 C ATOM 1374 CE1 PHE A 173 31.105 50.223 49.145 1.00 91.11 C ANISOU 1374 CE1 PHE E 173 11004 14444 9172 -992 -551 1730 C ATOM 1375 CE2 PHE A 173 33.123 51.148 48.257 1.00 91.80 C ANISOU 1375 CE2 PHE E 173 10541 14096 10243 -794 -985 2187 C ATOM 1376 CZ PHE A 173 32.295 50.062 48.461 1.00 90.64 C ANISOU 1376 CZ PHE E 173 10223 14319 9898 -703 -1053 2344 C ATOM 1377 N PHE A 174 31.121 57.027 48.965 1.00 98.63 N ANISOU 1377 N PHE E 174 10789 14856 11831 -833 -369 -1379 N ATOM 1378 CA PHE A 174 30.804 58.421 49.352 1.00102.64 C ANISOU 1378 CA PHE E 174 12059 14291 12650 -629 -398 -2078 C ATOM 1379 C PHE A 174 29.990 59.045 48.225 1.00108.34 C ANISOU 1379 C PHE E 174 12786 14844 13533 -651 -1222 -2243 C ATOM 1380 O PHE A 174 30.442 59.936 47.520 1.00113.25 O ANISOU 1380 O PHE E 174 14713 14498 13819 212 -2451 -2631 O ATOM 1381 CB PHE A 174 32.074 59.179 49.715 1.00100.89 C ANISOU 1381 CB PHE E 174 12146 13993 12196 -438 -292 -2674 C ATOM 1382 CG PHE A 174 32.514 58.938 51.164 1.00101.23 C ANISOU 1382 CG PHE E 174 11869 14360 12232 -610 -257 -2760 C ATOM 1383 CD1 PHE A 174 33.037 57.711 51.537 1.00101.15 C ANISOU 1383 CD1 PHE E 174 11722 14554 12156 -813 146 -2915 C ATOM 1384 CD2 PHE A 174 32.383 59.932 52.122 1.00 99.50 C ANISOU 1384 CD2 PHE E 174 11610 14369 11828 -479 172 -2977 C ATOM 1385 CE1 PHE A 174 33.433 57.484 52.841 1.00100.80 C ANISOU 1385 CE1 PHE E 174 11514 14644 12141 -931 174 -2836 C ATOM 1386 CE2 PHE A 174 32.766 59.715 53.431 1.00 98.42 C ANISOU 1386 CE2 PHE E 174 11506 14380 11508 -655 925 -3316 C ATOM 1387 CZ PHE A 174 33.270 58.482 53.789 1.00100.40 C ANISOU 1387 CZ PHE E 174 11676 14579 11892 -1087 596 -3021 C ATOM 1388 N ASP A 175 28.782 58.527 48.124 1.00112.09 N ANISOU 1388 N ASP E 175 12995 15173 14422 -436 -1786 -1485 N ATOM 1389 CA ASP A 175 27.918 58.244 47.011 1.00115.08 C ANISOU 1389 CA ASP E 175 13761 15399 14564 -948 -2093 -893 C ATOM 1390 C ASP A 175 28.598 58.814 45.748 1.00115.71 C ANISOU 1390 C ASP E 175 14276 15528 14161 -1845 -1488 -256 C ATOM 1391 O ASP A 175 28.344 59.923 45.310 1.00101.68 O ANISOU 1391 O ASP E 175 8131 15542 14961 -499 -1721 -833 O ATOM 1392 CB ASP A 175 26.472 58.732 47.107 1.00113.42 C ANISOU 1392 CB ASP E 175 13335 15222 14536 -254 -2220 -790 C ATOM 1393 CG ASP A 175 25.468 57.633 46.744 1.00114.59 C ANISOU 1393 CG ASP E 175 14314 14779 14446 34 -1892 -751 C ATOM 1394 OD1 ASP A 175 25.901 56.487 46.451 1.00117.13 O ANISOU 1394 OD1 ASP E 175 16380 14695 13429 52 333 -1017 O ATOM 1395 OD2 ASP A 175 24.241 57.889 46.736 1.00114.39 O ANISOU 1395 OD2 ASP E 175 13894 14998 14569 1145 -918 -1667 O ATOM 1396 N ASN A 176 29.464 57.923 45.280 1.00121.11 N ANISOU 1396 N ASN E 176 16259 15316 14442 -2523 -1645 359 N ATOM 1397 CA ASN A 176 30.190 57.971 44.022 1.00119.04 C ANISOU 1397 CA ASN E 176 16189 14492 14550 -2736 -1505 839 C ATOM 1398 C ASN A 176 30.808 59.340 43.777 1.00119.68 C ANISOU 1398 C ASN E 176 16495 14491 14488 -2749 -1624 469 C ATOM 1399 O ASN A 176 30.911 59.822 42.652 1.00124.72 O ANISOU 1399 O ASN E 176 17735 14741 14911 -3286 -2318 -305 O ATOM 1400 CB ASN A 176 29.208 57.541 42.919 1.00122.57 C ANISOU 1400 CB ASN E 176 17638 13976 14957 -3487 -2272 1753 C ATOM 1401 CG ASN A 176 28.217 56.505 43.440 1.00119.83 C ANISOU 1401 CG ASN E 176 17236 13557 14738 -3318 -2834 2375 C ATOM 1402 OD1 ASN A 176 27.059 56.815 43.726 1.00112.39 O ANISOU 1402 OD1 ASN E 176 17127 13114 12463 -3026 -3341 3384 O ATOM 1403 ND2 ASN A 176 28.662 55.263 43.593 1.00118.58 N ANISOU 1403 ND2 ASN E 176 15982 13336 15738 -2785 -4764 2945 N ATOM 1404 N ASP A 177 31.230 59.947 44.876 1.00121.16 N ANISOU 1404 N ASP E 177 16699 14395 14941 -2643 -2025 583 N ATOM 1405 CA ASP A 177 31.684 61.326 44.960 1.00120.08 C ANISOU 1405 CA ASP E 177 16473 14274 14877 -2799 -2648 -20 C ATOM 1406 C ASP A 177 33.077 61.396 45.573 1.00116.88 C ANISOU 1406 C ASP E 177 16061 14590 13758 -2498 -1936 -826 C ATOM 1407 O ASP A 177 33.232 61.466 46.795 1.00116.90 O ANISOU 1407 O ASP E 177 15584 15979 12852 -4161 -1973 -6623 O ATOM 1408 CB ASP A 177 30.634 62.097 45.756 1.00123.47 C ANISOU 1408 CB ASP E 177 16783 14388 15742 -4064 -3476 197 C ATOM 1409 CG ASP A 177 31.080 63.431 46.327 1.00128.08 C ANISOU 1409 CG ASP E 177 17759 14285 16618 -4454 -4378 444 C ATOM 1410 OD1 ASP A 177 32.005 64.039 45.740 1.00128.91 O ANISOU 1410 OD1 ASP E 177 17629 14208 17141 -3845 -5296 -103 O ATOM 1411 OD2 ASP A 177 30.499 63.871 47.355 1.00134.42 O ANISOU 1411 OD2 ASP E 177 18686 14781 17606 -5619 -4369 1175 O ATOM 1412 N VAL A 178 34.090 61.371 44.711 1.00118.66 N ANISOU 1412 N VAL E 178 16676 14823 13586 -3116 -1669 -593 N ATOM 1413 CA VAL A 178 35.497 61.433 45.057 1.00114.96 C ANISOU 1413 CA VAL E 178 16440 14173 13065 -2790 -1097 -961 C ATOM 1414 C VAL A 178 35.937 62.844 45.452 1.00114.77 C ANISOU 1414 C VAL E 178 16742 13959 12908 -3083 -1201 -979 C ATOM 1415 O VAL A 178 36.760 63.452 44.762 1.00114.89 O ANISOU 1415 O VAL E 178 16482 13515 13656 -3279 -892 -779 O ATOM 1416 CB VAL A 178 36.379 60.970 43.875 1.00114.12 C ANISOU 1416 CB VAL E 178 16879 14133 12349 -2691 -1395 -955 C ATOM 1417 CG1 VAL A 178 37.380 59.910 44.303 1.00100.42 C ANISOU 1417 CG1 VAL E 178 16419 12787 8949 -1649 -3 -1912 C ATOM 1418 CG2 VAL A 178 35.491 60.455 42.736 1.00108.95 C ANISOU 1418 CG2 VAL E 178 14263 13668 13463 -2327 -635 -648 C ATOM 1419 N ASN A 179 35.397 63.355 46.549 1.00116.58 N ANISOU 1419 N ASN E 179 17945 13795 12556 -3598 -1127 -1455 N ATOM 1420 CA ASN A 179 35.713 64.662 47.107 1.00116.97 C ANISOU 1420 CA ASN E 179 19049 13285 12108 -3906 -966 -1844 C ATOM 1421 C ASN A 179 35.374 64.687 48.602 1.00115.42 C ANISOU 1421 C ASN E 179 18661 12859 12334 -4366 -546 -1960 C ATOM 1422 O ASN A 179 35.834 65.548 49.341 1.00111.17 O ANISOU 1422 O ASN E 179 18670 11973 11594 -4270 -82 -2598 O ATOM 1423 CB ASN A 179 34.943 65.786 46.414 1.00126.19 C ANISOU 1423 CB ASN E 179 20612 14193 13140 -4450 -586 -3101 C ATOM 1424 CG ASN A 179 35.628 66.346 45.183 1.00133.83 C ANISOU 1424 CG ASN E 179 21547 15588 13714 -4664 -1 -3782 C ATOM 1425 OD1 ASN A 179 36.804 66.725 45.214 1.00141.47 O ANISOU 1425 OD1 ASN E 179 22131 16168 15453 -3717 104 -5270 O ATOM 1426 ND2 ASN A 179 34.893 66.411 44.075 1.00140.96 N ANISOU 1426 ND2 ASN E 179 22307 17586 13667 -5567 -254 -4832 N ATOM 1427 N GLN A 180 34.555 63.715 48.968 1.00113.09 N ANISOU 1427 N GLN E 180 18065 12522 12383 -4550 -539 -1364 N ATOM 1428 CA GLN A 180 34.057 63.521 50.318 1.00111.28 C ANISOU 1428 CA GLN E 180 17368 12221 12694 -4603 -233 -1241 C ATOM 1429 C GLN A 180 34.770 62.368 51.026 1.00107.47 C ANISOU 1429 C GLN E 180 16498 11752 12582 -4276 637 -1433 C ATOM 1430 O GLN A 180 34.915 62.399 52.249 1.00110.04 O ANISOU 1430 O GLN E 180 17836 11203 12770 -6924 -34 -201 O ATOM 1431 CB GLN A 180 32.544 63.269 50.290 1.00115.85 C ANISOU 1431 CB GLN E 180 17179 13290 13550 -5064 -396 -286 C ATOM 1432 CG GLN A 180 31.767 64.225 51.190 1.00120.97 C ANISOU 1432 CG GLN E 180 17873 13992 14097 -4886 274 156 C ATOM 1433 CD GLN A 180 32.660 64.879 52.239 1.00126.63 C ANISOU 1433 CD GLN E 180 19208 14437 14468 -4872 -191 735 C ATOM 1434 OE1 GLN A 180 32.859 64.332 53.323 1.00134.88 O ANISOU 1434 OE1 GLN E 180 21173 16732 13344 -5194 390 1458 O ATOM 1435 NE2 GLN A 180 33.211 66.045 51.913 1.00134.37 N ANISOU 1435 NE2 GLN E 180 20493 13494 17068 -4682 -570 1136 N ATOM 1436 N VAL A 181 35.188 61.393 50.225 1.00 91.41 N ANISOU 1436 N VAL E 181 12209 11447 11077 -2514 -691 -1245 N ATOM 1437 CA VAL A 181 36.047 60.294 50.656 1.00 87.48 C ANISOU 1437 CA VAL E 181 12009 11197 10032 -2443 244 -1415 C ATOM 1438 C VAL A 181 37.138 60.838 51.576 1.00 80.41 C ANISOU 1438 C VAL E 181 10823 10634 9095 -1836 1155 -2706 C ATOM 1439 O VAL A 181 37.915 61.671 51.097 1.00 92.19 O ANISOU 1439 O VAL E 181 11677 11840 11511 -1460 997 -4631 O ATOM 1440 CB VAL A 181 36.701 59.575 49.460 1.00 90.28 C ANISOU 1440 CB VAL E 181 12256 11761 10287 -2070 945 -1371 C ATOM 1441 CG1 VAL A 181 37.268 58.221 49.884 1.00 79.58 C ANISOU 1441 CG1 VAL E 181 8542 12793 8903 -2166 3719 -2698 C ATOM 1442 CG2 VAL A 181 35.710 59.443 48.309 1.00 90.23 C ANISOU 1442 CG2 VAL E 181 13190 11625 9469 -2396 839 -1705 C ATOM 1443 N PRO A 182 37.197 60.414 52.825 1.00 78.75 N ANISOU 1443 N PRO E 182 10355 10446 9119 -2988 1354 -2686 N ATOM 1444 CA PRO A 182 38.117 61.026 53.804 1.00 76.52 C ANISOU 1444 CA PRO E 182 10676 9754 8644 -3288 1639 -2374 C ATOM 1445 C PRO A 182 39.538 61.025 53.267 1.00 71.68 C ANISOU 1445 C PRO E 182 10376 9002 7857 -3382 1082 -2873 C ATOM 1446 O PRO A 182 39.902 60.167 52.454 1.00 66.00 O ANISOU 1446 O PRO E 182 9654 8907 6513 -1321 1615 -2978 O ATOM 1447 CB PRO A 182 37.955 60.114 55.021 1.00 75.44 C ANISOU 1447 CB PRO E 182 10308 9585 8770 -2867 1719 -2322 C ATOM 1448 CG PRO A 182 36.575 59.554 54.889 1.00 76.20 C ANISOU 1448 CG PRO E 182 10118 9995 8838 -3110 1344 -2279 C ATOM 1449 CD PRO A 182 36.423 59.312 53.407 1.00 76.74 C ANISOU 1449 CD PRO E 182 10206 10234 8719 -3262 1277 -2719 C ATOM 1450 N LYS A 183 40.374 61.987 53.642 1.00 66.25 N ANISOU 1450 N LYS E 183 10340 8136 6695 -4050 1488 -2470 N ATOM 1451 CA LYS A 183 41.684 62.008 52.995 1.00 67.52 C ANISOU 1451 CA LYS E 183 10571 8502 6581 -3366 1692 -1915 C ATOM 1452 C LYS A 183 42.624 61.008 53.656 1.00 61.25 C ANISOU 1452 C LYS E 183 9080 8020 6172 -2590 2056 -1793 C ATOM 1453 O LYS A 183 43.572 60.535 53.033 1.00 62.32 O ANISOU 1453 O LYS E 183 8010 8614 7056 -1762 3204 -3628 O ATOM 1454 CB LYS A 183 42.296 63.405 53.042 1.00 75.36 C ANISOU 1454 CB LYS E 183 12471 8389 7774 -2993 2715 -2713 C ATOM 1455 CG LYS A 183 41.869 64.254 51.844 1.00 84.45 C ANISOU 1455 CG LYS E 183 14227 9329 8531 -2830 1521 -3164 C ATOM 1456 CD LYS A 183 40.619 63.688 51.191 1.00 95.52 C ANISOU 1456 CD LYS E 183 15282 11438 9573 -3046 265 -1703 C ATOM 1457 CE LYS A 183 40.664 63.729 49.672 1.00101.86 C ANISOU 1457 CE LYS E 183 16632 12453 9618 -3588 396 -1398 C ATOM 1458 NZ LYS A 183 39.671 62.787 49.070 1.00102.56 N ANISOU 1458 NZ LYS E 183 16349 13890 8727 -3036 990 -1168 N ATOM 1459 N TYR A 184 42.335 60.709 54.917 1.00 51.83 N ANISOU 1459 N TYR E 184 7385 6107 6202 -1451 1991 -1376 N ATOM 1460 CA TYR A 184 43.237 59.906 55.718 1.00 55.27 C ANISOU 1460 CA TYR E 184 8249 6086 6665 -1439 1539 -1697 C ATOM 1461 C TYR A 184 42.518 58.737 56.387 1.00 50.14 C ANISOU 1461 C TYR E 184 7486 5664 5900 -936 511 -893 C ATOM 1462 O TYR A 184 41.295 58.722 56.538 1.00 48.87 O ANISOU 1462 O TYR E 184 7286 5065 6217 -912 -386 -628 O ATOM 1463 CB TYR A 184 43.886 60.730 56.825 1.00 53.58 C ANISOU 1463 CB TYR E 184 6222 6312 7825 -223 1467 -2105 C ATOM 1464 CG TYR A 184 44.586 61.992 56.402 1.00 65.46 C ANISOU 1464 CG TYR E 184 7173 6790 10910 -60 1811 -3275 C ATOM 1465 CD1 TYR A 184 45.968 62.113 56.485 1.00 67.60 C ANISOU 1465 CD1 TYR E 184 6973 7049 11662 58 3033 -3556 C ATOM 1466 CD2 TYR A 184 43.860 63.082 55.931 1.00 73.31 C ANISOU 1466 CD2 TYR E 184 8066 7074 12715 -474 2087 -4017 C ATOM 1467 CE1 TYR A 184 46.610 63.277 56.100 1.00 72.07 C ANISOU 1467 CE1 TYR E 184 7801 7118 12467 126 3804 -3699 C ATOM 1468 CE2 TYR A 184 44.484 64.249 55.538 1.00 77.62 C ANISOU 1468 CE2 TYR E 184 8961 6918 13614 -526 2886 -4002 C ATOM 1469 CZ TYR A 184 45.857 64.336 55.628 1.00 77.23 C ANISOU 1469 CZ TYR E 184 8779 7214 13351 -254 4043 -4133 C ATOM 1470 OH TYR A 184 46.469 65.507 55.241 1.00 81.19 O ANISOU 1470 OH TYR E 184 9978 6232 14639 -89 4148 -3058 O ATOM 1471 N ALA A 185 43.329 57.761 56.798 1.00 44.28 N ANISOU 1471 N ALA E 185 6583 5134 5106 -446 559 -397 N ATOM 1472 CA ALA A 185 42.799 56.599 57.499 1.00 41.54 C ANISOU 1472 CA ALA E 185 6004 5031 4749 -416 508 -104 C ATOM 1473 C ALA A 185 43.788 56.142 58.562 1.00 39.24 C ANISOU 1473 C ALA E 185 5740 4871 4300 -717 912 133 C ATOM 1474 O ALA A 185 44.971 56.432 58.406 1.00 40.15 O ANISOU 1474 O ALA E 185 5793 5070 4394 -630 878 -475 O ATOM 1475 CB ALA A 185 42.522 55.449 56.548 1.00 40.34 C ANISOU 1475 CB ALA E 185 5188 5388 4751 -438 771 151 C ATOM 1476 N LEU A 186 43.258 55.455 59.557 1.00 37.19 N ANISOU 1476 N LEU E 186 5393 4789 3950 -862 1160 535 N ATOM 1477 CA LEU A 186 44.106 54.767 60.533 1.00 35.06 C ANISOU 1477 CA LEU E 186 4702 4519 4100 -214 1223 282 C ATOM 1478 C LEU A 186 44.222 53.309 60.084 1.00 33.86 C ANISOU 1478 C LEU E 186 4382 4655 3830 -287 401 524 C ATOM 1479 O LEU A 186 43.187 52.759 59.685 1.00 34.53 O ANISOU 1479 O LEU E 186 4199 5283 3639 -774 52 1064 O ATOM 1480 CB LEU A 186 43.544 54.839 61.943 1.00 36.12 C ANISOU 1480 CB LEU E 186 4452 5494 3779 94 711 865 C ATOM 1481 CG LEU A 186 44.073 55.960 62.833 1.00 39.23 C ANISOU 1481 CG LEU E 186 6353 4183 4371 259 794 461 C ATOM 1482 CD1 LEU A 186 44.444 57.157 61.990 1.00 42.75 C ANISOU 1482 CD1 LEU E 186 9437 3566 3240 -1441 -472 -47 C ATOM 1483 CD2 LEU A 186 43.071 56.317 63.934 1.00 40.18 C ANISOU 1483 CD2 LEU E 186 6145 4354 4767 -1365 226 1002 C ATOM 1484 N THR A 187 45.409 52.711 60.133 1.00 30.92 N ANISOU 1484 N THR E 187 4133 4155 3461 94 150 309 N ATOM 1485 CA THR A 187 45.516 51.311 59.713 1.00 32.43 C ANISOU 1485 CA THR E 187 4606 4346 3371 -190 -100 590 C ATOM 1486 C THR A 187 46.483 50.532 60.568 1.00 30.01 C ANISOU 1486 C THR E 187 4081 4157 3164 -36 197 666 C ATOM 1487 O THR A 187 47.531 51.052 60.980 1.00 30.48 O ANISOU 1487 O THR E 187 3846 4335 3400 -14 462 717 O ATOM 1488 CB THR A 187 45.979 51.255 58.242 1.00 33.44 C ANISOU 1488 CB THR E 187 4926 4319 3459 -409 73 284 C ATOM 1489 OG1 THR A 187 46.077 49.903 57.767 1.00 37.26 O ANISOU 1489 OG1 THR E 187 6156 4383 3620 301 1094 527 O ATOM 1490 CG2 THR A 187 47.373 51.880 58.078 1.00 33.76 C ANISOU 1490 CG2 THR E 187 5268 4475 3086 12 -123 -62 C ATOM 1491 N VAL A 188 46.203 49.268 60.862 1.00 28.57 N ANISOU 1491 N VAL E 188 3740 4203 2911 -94 603 608 N ATOM 1492 CA VAL A 188 47.261 48.485 61.499 1.00 29.31 C ANISOU 1492 CA VAL E 188 3735 4253 3147 34 387 510 C ATOM 1493 C VAL A 188 48.464 48.374 60.573 1.00 30.26 C ANISOU 1493 C VAL E 188 3591 4490 3416 -170 473 -521 C ATOM 1494 O VAL A 188 48.365 48.543 59.343 1.00 29.19 O ANISOU 1494 O VAL E 188 3485 4361 3245 -525 366 186 O ATOM 1495 CB VAL A 188 46.775 47.065 61.841 1.00 29.17 C ANISOU 1495 CB VAL E 188 4038 4367 2679 -104 1059 342 C ATOM 1496 CG1 VAL A 188 45.616 47.137 62.832 1.00 31.08 C ANISOU 1496 CG1 VAL E 188 3683 4932 3194 -158 1065 776 C ATOM 1497 CG2 VAL A 188 46.368 46.320 60.573 1.00 28.12 C ANISOU 1497 CG2 VAL E 188 3455 4019 3209 -169 1025 629 C ATOM 1498 N GLY A 189 49.620 48.079 61.164 1.00 28.38 N ANISOU 1498 N GLY E 189 3717 3841 3224 -117 155 384 N ATOM 1499 CA GLY A 189 50.823 47.938 60.363 1.00 28.02 C ANISOU 1499 CA GLY E 189 3469 4112 3066 46 -121 769 C ATOM 1500 C GLY A 189 51.085 46.533 59.862 1.00 27.71 C ANISOU 1500 C GLY E 189 3463 3891 3172 18 212 417 C ATOM 1501 O GLY A 189 50.367 45.593 60.238 1.00 27.45 O ANISOU 1501 O GLY E 189 3160 3989 3282 -145 31 50 O ATOM 1502 N VAL A 190 52.111 46.385 59.026 1.00 26.82 N ANISOU 1502 N VAL E 190 3465 3926 2798 112 107 420 N ATOM 1503 CA VAL A 190 52.423 45.044 58.521 1.00 26.93 C ANISOU 1503 CA VAL E 190 3389 4048 2796 131 90 577 C ATOM 1504 C VAL A 190 52.924 44.162 59.650 1.00 28.09 C ANISOU 1504 C VAL E 190 3785 3971 2918 -213 119 637 C ATOM 1505 O VAL A 190 52.627 42.971 59.727 1.00 30.94 O ANISOU 1505 O VAL E 190 4716 3911 3129 -189 60 682 O ATOM 1506 CB VAL A 190 53.455 45.092 57.379 1.00 26.99 C ANISOU 1506 CB VAL E 190 3112 3553 3590 -134 386 136 C ATOM 1507 CG1 VAL A 190 53.788 43.686 56.874 1.00 25.38 C ANISOU 1507 CG1 VAL E 190 2744 3342 3558 112 575 -44 C ATOM 1508 CG2 VAL A 190 52.963 45.956 56.219 1.00 27.32 C ANISOU 1508 CG2 VAL E 190 4403 2881 3095 133 365 484 C ATOM 1509 N GLY A 191 53.699 44.736 60.564 1.00 28.27 N ANISOU 1509 N GLY E 191 3208 4106 3427 -304 -227 355 N ATOM 1510 CA GLY A 191 54.200 44.060 61.759 1.00 28.37 C ANISOU 1510 CA GLY E 191 3342 3994 3444 -476 -138 303 C ATOM 1511 C GLY A 191 53.036 43.629 62.635 1.00 28.92 C ANISOU 1511 C GLY E 191 3516 4195 3278 -472 -45 463 C ATOM 1512 O GLY A 191 53.010 42.535 63.204 1.00 30.95 O ANISOU 1512 O GLY E 191 3779 4123 3859 -480 519 391 O ATOM 1513 N THR A 192 52.039 44.508 62.746 1.00 29.18 N ANISOU 1513 N THR E 192 3439 4502 3147 -591 -134 402 N ATOM 1514 CA THR A 192 50.833 44.170 63.502 1.00 29.81 C ANISOU 1514 CA THR E 192 3857 4395 3073 -556 226 626 C ATOM 1515 C THR A 192 50.207 42.891 62.957 1.00 29.87 C ANISOU 1515 C THR E 192 4123 4135 3090 -435 71 136 C ATOM 1516 O THR A 192 49.824 41.965 63.671 1.00 30.88 O ANISOU 1516 O THR E 192 3359 4959 3417 -200 564 -87 O ATOM 1517 CB THR A 192 49.793 45.299 63.402 1.00 30.46 C ANISOU 1517 CB THR E 192 3949 4135 3491 -437 1053 19 C ATOM 1518 OG1 THR A 192 50.462 46.563 63.487 1.00 30.94 O ANISOU 1518 OG1 THR E 192 4233 4289 3235 -315 469 522 O ATOM 1519 CG2 THR A 192 48.799 45.228 64.557 1.00 28.56 C ANISOU 1519 CG2 THR E 192 3804 4881 2167 -406 239 587 C ATOM 1520 N LEU A 193 50.093 42.839 61.622 1.00 29.30 N ANISOU 1520 N LEU E 193 3907 4130 3097 -445 -282 243 N ATOM 1521 CA LEU A 193 49.512 41.648 60.997 1.00 28.61 C ANISOU 1521 CA LEU E 193 3432 4212 3224 9 467 216 C ATOM 1522 C LEU A 193 50.427 40.452 61.196 1.00 28.75 C ANISOU 1522 C LEU E 193 3528 4125 3272 31 128 531 C ATOM 1523 O LEU A 193 49.941 39.376 61.569 1.00 29.30 O ANISOU 1523 O LEU E 193 4126 4214 2793 -10 282 293 O ATOM 1524 CB LEU A 193 49.316 41.932 59.530 1.00 31.34 C ANISOU 1524 CB LEU E 193 4114 4565 3228 132 -171 407 C ATOM 1525 CG LEU A 193 48.453 41.162 58.554 1.00 35.04 C ANISOU 1525 CG LEU E 193 5419 4216 3677 812 52 819 C ATOM 1526 CD1 LEU A 193 49.322 40.380 57.559 1.00 39.91 C ANISOU 1526 CD1 LEU E 193 4504 3781 6878 259 -509 2372 C ATOM 1527 CD2 LEU A 193 47.450 40.229 59.210 1.00 40.58 C ANISOU 1527 CD2 LEU E 193 7843 3165 4409 1560 41 377 C ATOM 1528 N LEU A 194 51.730 40.627 60.937 1.00 28.35 N ANISOU 1528 N LEU E 194 3406 4654 2710 -78 -153 487 N ATOM 1529 CA LEU A 194 52.620 39.466 61.006 1.00 29.18 C ANISOU 1529 CA LEU E 194 3512 4386 3188 42 788 217 C ATOM 1530 C LEU A 194 52.757 38.910 62.408 1.00 27.64 C ANISOU 1530 C LEU E 194 3308 3882 3311 13 459 277 C ATOM 1531 O LEU A 194 53.104 37.740 62.619 1.00 32.48 O ANISOU 1531 O LEU E 194 4441 4208 3691 -751 230 449 O ATOM 1532 CB LEU A 194 54.013 39.835 60.460 1.00 30.39 C ANISOU 1532 CB LEU E 194 3416 4337 3793 268 610 -13 C ATOM 1533 CG LEU A 194 54.047 39.998 58.931 1.00 32.67 C ANISOU 1533 CG LEU E 194 4476 4134 3803 244 1480 184 C ATOM 1534 CD1 LEU A 194 55.410 40.477 58.444 1.00 33.19 C ANISOU 1534 CD1 LEU E 194 3856 4679 4076 -249 1257 200 C ATOM 1535 CD2 LEU A 194 53.643 38.691 58.260 1.00 37.87 C ANISOU 1535 CD2 LEU E 194 5689 4563 4135 478 209 271 C ATOM 1536 N ASP A 195 52.509 39.720 63.425 1.00 30.12 N ANISOU 1536 N ASP E 195 4211 4072 3163 -662 590 131 N ATOM 1537 CA ASP A 195 52.566 39.205 64.781 1.00 29.64 C ANISOU 1537 CA ASP E 195 4302 3758 3203 98 -79 213 C ATOM 1538 C ASP A 195 51.412 38.253 65.074 1.00 29.57 C ANISOU 1538 C ASP E 195 4117 3778 3340 -45 -78 100 C ATOM 1539 O ASP A 195 51.442 37.574 66.114 1.00 32.41 O ANISOU 1539 O ASP E 195 4205 4517 3592 -211 318 -376 O ATOM 1540 CB ASP A 195 52.468 40.356 65.793 1.00 32.84 C ANISOU 1540 CB ASP E 195 4666 4408 3404 87 -719 714 C ATOM 1541 CG ASP A 195 53.755 41.118 65.950 1.00 36.78 C ANISOU 1541 CG ASP E 195 5311 4142 4521 658 -307 529 C ATOM 1542 OD1 ASP A 195 54.767 40.619 65.417 1.00 41.73 O ANISOU 1542 OD1 ASP E 195 4379 5412 6064 -338 -1138 -93 O ATOM 1543 OD2 ASP A 195 53.726 42.181 66.597 1.00 46.56 O ANISOU 1543 OD2 ASP E 195 7158 4576 5955 488 -1854 1342 O ATOM 1544 N ALA A 196 50.387 38.181 64.231 1.00 29.67 N ANISOU 1544 N ALA E 196 3714 4500 3058 -289 263 755 N ATOM 1545 CA ALA A 196 49.307 37.225 64.543 1.00 27.17 C ANISOU 1545 CA ALA E 196 3566 4341 2418 -493 286 664 C ATOM 1546 C ALA A 196 49.803 35.788 64.446 1.00 28.00 C ANISOU 1546 C ALA E 196 3307 4465 2866 -680 569 151 C ATOM 1547 O ALA A 196 50.764 35.483 63.738 1.00 28.87 O ANISOU 1547 O ALA E 196 3380 4911 2678 -817 407 523 O ATOM 1548 CB ALA A 196 48.144 37.419 63.606 1.00 26.85 C ANISOU 1548 CB ALA E 196 3786 3619 2796 -451 4 594 C ATOM 1549 N GLU A 197 49.172 34.877 65.157 1.00 27.17 N ANISOU 1549 N GLU E 197 3167 4506 2651 43 -131 398 N ATOM 1550 CA GLU A 197 49.538 33.476 65.188 1.00 30.24 C ANISOU 1550 CA GLU E 197 3681 4448 3362 63 432 377 C ATOM 1551 C GLU A 197 49.274 32.819 63.842 1.00 30.02 C ANISOU 1551 C GLU E 197 3932 4152 3320 -495 120 257 C ATOM 1552 O GLU A 197 50.032 31.955 63.394 1.00 29.71 O ANISOU 1552 O GLU E 197 3706 5116 2466 -914 330 -139 O ATOM 1553 CB GLU A 197 48.700 32.767 66.253 1.00 40.52 C ANISOU 1553 CB GLU E 197 6248 5074 4074 -980 1874 -674 C ATOM 1554 CG GLU A 197 49.248 31.434 66.714 1.00 60.69 C ANISOU 1554 CG GLU E 197 10960 5871 6230 -2159 2147 -1972 C ATOM 1555 CD GLU A 197 48.553 30.910 67.958 1.00 66.66 C ANISOU 1555 CD GLU E 197 12361 6294 6674 -1720 2370 -2598 C ATOM 1556 OE1 GLU A 197 48.589 31.620 68.995 1.00 68.95 O ANISOU 1556 OE1 GLU E 197 12681 6424 7091 -1696 3962 -2134 O ATOM 1557 OE2 GLU A 197 47.982 29.795 67.880 1.00 72.08 O ANISOU 1557 OE2 GLU E 197 12903 7065 7420 -834 2072 -2632 O ATOM 1558 N GLU A 198 48.183 33.204 63.201 1.00 29.40 N ANISOU 1558 N GLU E 198 4080 4111 2979 -884 400 26 N ATOM 1559 CA GLU A 198 47.792 32.680 61.890 1.00 29.14 C ANISOU 1559 CA GLU E 198 3686 4407 2976 -596 412 4 C ATOM 1560 C GLU A 198 47.206 33.825 61.076 1.00 30.64 C ANISOU 1560 C GLU E 198 3990 4706 2945 -952 421 17 C ATOM 1561 O GLU A 198 46.494 34.674 61.639 1.00 26.56 O ANISOU 1561 O GLU E 198 3260 4014 2819 -140 508 -1 O ATOM 1562 CB GLU A 198 46.797 31.537 62.053 1.00 29.18 C ANISOU 1562 CB GLU E 198 3211 4607 3268 -706 933 303 C ATOM 1563 CG GLU A 198 46.301 30.917 60.745 1.00 32.96 C ANISOU 1563 CG GLU E 198 3877 4954 3691 -308 357 332 C ATOM 1564 CD GLU A 198 45.451 29.690 61.029 1.00 36.62 C ANISOU 1564 CD GLU E 198 5000 4709 4204 -89 1011 746 C ATOM 1565 OE1 GLU A 198 44.664 29.725 61.999 1.00 36.61 O ANISOU 1565 OE1 GLU E 198 5321 4283 4307 -280 1223 248 O ATOM 1566 OE2 GLU A 198 45.545 28.669 60.311 1.00 43.85 O ANISOU 1566 OE2 GLU E 198 7564 4664 4432 -101 1557 743 O ATOM 1567 N VAL A 199 47.519 33.869 59.787 1.00 28.01 N ANISOU 1567 N VAL E 199 3735 3995 2911 -590 355 193 N ATOM 1568 CA VAL A 199 47.042 34.921 58.899 1.00 28.79 C ANISOU 1568 CA VAL E 199 4099 3913 2926 -422 35 243 C ATOM 1569 C VAL A 199 46.275 34.258 57.763 1.00 26.71 C ANISOU 1569 C VAL E 199 3439 3620 3092 -347 251 296 C ATOM 1570 O VAL A 199 46.843 33.367 57.105 1.00 28.14 O ANISOU 1570 O VAL E 199 3635 4215 2844 -635 380 363 O ATOM 1571 CB VAL A 199 48.195 35.753 58.321 1.00 26.90 C ANISOU 1571 CB VAL E 199 3876 3732 2611 -293 -478 289 C ATOM 1572 CG1 VAL A 199 47.695 36.774 57.314 1.00 26.66 C ANISOU 1572 CG1 VAL E 199 4317 4077 1737 -515 -252 492 C ATOM 1573 CG2 VAL A 199 48.929 36.467 59.439 1.00 26.84 C ANISOU 1573 CG2 VAL E 199 3784 4224 2189 -724 -423 415 C ATOM 1574 N MET A 200 45.037 34.672 57.550 1.00 25.82 N ANISOU 1574 N MET E 200 3405 3339 3067 -293 498 -199 N ATOM 1575 CA MET A 200 44.231 34.094 56.470 1.00 26.13 C ANISOU 1575 CA MET E 200 3086 3834 3009 -311 524 -191 C ATOM 1576 C MET A 200 43.798 35.210 55.530 1.00 26.51 C ANISOU 1576 C MET E 200 3359 3860 2853 -621 688 -45 C ATOM 1577 O MET A 200 43.062 36.124 55.932 1.00 26.60 O ANISOU 1577 O MET E 200 3277 3787 3044 -483 920 -67 O ATOM 1578 CB MET A 200 43.025 33.335 57.043 1.00 25.55 C ANISOU 1578 CB MET E 200 3154 3628 2926 -420 893 307 C ATOM 1579 CG MET A 200 42.044 32.810 55.996 1.00 27.01 C ANISOU 1579 CG MET E 200 3214 3595 3455 -318 604 244 C ATOM 1580 SD MET A 200 40.772 31.745 56.699 1.00 28.73 S ANISOU 1580 SD MET E 200 3551 3918 3448 -104 689 149 S ATOM 1581 CE MET A 200 39.793 32.923 57.647 1.00 26.69 C ANISOU 1581 CE MET E 200 2874 4794 2472 -335 27 342 C ATOM 1582 N ILE A 201 44.265 35.159 54.275 1.00 23.46 N ANISOU 1582 N ILE E 201 2655 3502 2756 -211 435 140 N ATOM 1583 CA ILE A 201 43.980 36.208 53.314 1.00 24.79 C ANISOU 1583 CA ILE E 201 3173 3587 2659 -135 141 166 C ATOM 1584 C ILE A 201 42.947 35.707 52.312 1.00 26.52 C ANISOU 1584 C ILE E 201 3302 3637 3138 -120 -129 255 C ATOM 1585 O ILE A 201 43.128 34.633 51.732 1.00 27.81 O ANISOU 1585 O ILE E 201 4090 3835 2643 -342 -290 292 O ATOM 1586 CB ILE A 201 45.249 36.641 52.566 1.00 27.24 C ANISOU 1586 CB ILE E 201 3374 3618 3356 163 152 -363 C ATOM 1587 CG1 ILE A 201 46.370 37.030 53.540 1.00 27.24 C ANISOU 1587 CG1 ILE E 201 3081 3946 3322 -139 251 -186 C ATOM 1588 CG2 ILE A 201 44.932 37.754 51.575 1.00 25.31 C ANISOU 1588 CG2 ILE E 201 3326 3157 3136 -130 215 74 C ATOM 1589 CD1 ILE A 201 46.011 38.295 54.313 1.00 28.28 C ANISOU 1589 CD1 ILE E 201 3584 4313 2850 -494 -85 -87 C ATOM 1590 N LEU A 202 41.899 36.489 52.154 1.00 26.31 N ANISOU 1590 N LEU E 202 3092 3731 3174 -22 64 -128 N ATOM 1591 CA LEU A 202 40.841 36.224 51.204 1.00 26.30 C ANISOU 1591 CA LEU E 202 3483 3728 2784 -398 -43 153 C ATOM 1592 C LEU A 202 41.238 36.839 49.859 1.00 27.46 C ANISOU 1592 C LEU E 202 3413 4048 2970 -16 191 179 C ATOM 1593 O LEU A 202 41.528 38.039 49.800 1.00 28.40 O ANISOU 1593 O LEU E 202 3715 3947 3129 -232 511 123 O ATOM 1594 CB LEU A 202 39.527 36.844 51.644 1.00 27.98 C ANISOU 1594 CB LEU E 202 3026 4205 3402 -8 200 67 C ATOM 1595 CG LEU A 202 38.556 36.122 52.574 1.00 32.57 C ANISOU 1595 CG LEU E 202 4884 4340 3151 -665 1223 -340 C ATOM 1596 CD1 LEU A 202 39.206 35.010 53.361 1.00 29.03 C ANISOU 1596 CD1 LEU E 202 4459 5402 1168 -774 316 322 C ATOM 1597 CD2 LEU A 202 37.872 37.123 53.489 1.00 28.96 C ANISOU 1597 CD2 LEU E 202 4928 4324 1753 -81 81 254 C ATOM 1598 N VAL A 203 41.219 36.022 48.818 1.00 27.08 N ANISOU 1598 N VAL E 203 3379 4070 2841 -319 158 136 N ATOM 1599 CA VAL A 203 41.616 36.531 47.507 1.00 28.32 C ANISOU 1599 CA VAL E 203 3361 4483 2917 -368 193 -54 C ATOM 1600 C VAL A 203 40.525 36.291 46.455 1.00 28.11 C ANISOU 1600 C VAL E 203 3351 4416 2913 -207 204 -341 C ATOM 1601 O VAL A 203 40.323 35.132 46.063 1.00 31.28 O ANISOU 1601 O VAL E 203 4296 4820 2771 -986 -232 601 O ATOM 1602 CB VAL A 203 42.939 35.878 47.065 1.00 31.03 C ANISOU 1602 CB VAL E 203 3660 5547 2583 -1005 156 -265 C ATOM 1603 CG1 VAL A 203 43.443 36.570 45.776 1.00 27.47 C ANISOU 1603 CG1 VAL E 203 3351 4595 2491 -504 -35 175 C ATOM 1604 CG2 VAL A 203 44.014 35.897 48.148 1.00 29.06 C ANISOU 1604 CG2 VAL E 203 3679 5007 2355 -1074 283 118 C ATOM 1605 N LEU A 204 39.843 37.357 46.022 1.00 30.58 N ANISOU 1605 N LEU E 204 3955 4885 2778 -1079 110 214 N ATOM 1606 CA LEU A 204 38.713 37.300 45.117 1.00 30.91 C ANISOU 1606 CA LEU E 204 3857 4859 3028 -978 77 43 C ATOM 1607 C LEU A 204 38.904 38.165 43.882 1.00 29.57 C ANISOU 1607 C LEU E 204 3398 4788 3048 -201 -283 88 C ATOM 1608 O LEU A 204 39.225 39.347 43.988 1.00 31.99 O ANISOU 1608 O LEU E 204 4527 4559 3069 -551 -246 384 O ATOM 1609 CB LEU A 204 37.435 37.779 45.825 1.00 31.23 C ANISOU 1609 CB LEU E 204 3744 4804 3316 -564 188 378 C ATOM 1610 CG LEU A 204 36.970 36.963 47.031 1.00 34.71 C ANISOU 1610 CG LEU E 204 4546 4360 4282 -557 1005 214 C ATOM 1611 CD1 LEU A 204 35.708 37.577 47.618 1.00 33.44 C ANISOU 1611 CD1 LEU E 204 3953 5118 3633 -175 495 933 C ATOM 1612 CD2 LEU A 204 36.752 35.494 46.658 1.00 31.49 C ANISOU 1612 CD2 LEU E 204 4245 4809 2909 -221 105 641 C ATOM 1613 N GLY A 205 38.686 37.612 42.681 1.00 29.39 N ANISOU 1613 N GLY E 205 3684 4477 3005 108 341 145 N ATOM 1614 CA GLY A 205 38.664 38.466 41.500 1.00 29.33 C ANISOU 1614 CA GLY E 205 3309 4893 2943 -186 184 46 C ATOM 1615 C GLY A 205 39.968 38.382 40.732 1.00 29.69 C ANISOU 1615 C GLY E 205 3654 4708 2919 -229 429 95 C ATOM 1616 O GLY A 205 41.039 38.250 41.304 1.00 28.46 O ANISOU 1616 O GLY E 205 3423 4190 3199 -544 655 -51 O ATOM 1617 N SER A 206 39.838 38.448 39.405 1.00 31.83 N ANISOU 1617 N SER E 206 4673 4502 2919 -549 548 -276 N ATOM 1618 CA SER A 206 41.031 38.416 38.561 1.00 29.80 C ANISOU 1618 CA SER E 206 4041 4962 2320 -526 -102 -270 C ATOM 1619 C SER A 206 41.887 39.650 38.791 1.00 31.69 C ANISOU 1619 C SER E 206 4450 4768 2821 -451 78 -368 C ATOM 1620 O SER A 206 43.076 39.626 38.468 1.00 28.29 O ANISOU 1620 O SER E 206 4255 4279 2215 -476 -394 268 O ATOM 1621 CB SER A 206 40.646 38.282 37.078 1.00 33.90 C ANISOU 1621 CB SER E 206 4494 6018 2369 -833 -305 -238 C ATOM 1622 OG SER A 206 39.970 39.476 36.692 1.00 38.87 O ANISOU 1622 OG SER E 206 5664 6409 2695 -1460 -1342 262 O ATOM 1623 N GLN A 207 41.346 40.731 39.353 1.00 30.40 N ANISOU 1623 N GLN E 207 3695 4607 3248 -457 63 -618 N ATOM 1624 CA GLN A 207 42.229 41.857 39.647 1.00 32.40 C ANISOU 1624 CA GLN E 207 4520 4248 3542 -300 14 -920 C ATOM 1625 C GLN A 207 43.266 41.525 40.722 1.00 29.27 C ANISOU 1625 C GLN E 207 4194 3487 3441 -283 30 -247 C ATOM 1626 O GLN A 207 44.244 42.282 40.861 1.00 29.03 O ANISOU 1626 O GLN E 207 4537 3459 3036 -42 551 326 O ATOM 1627 CB GLN A 207 41.408 43.091 40.043 1.00 36.95 C ANISOU 1627 CB GLN E 207 4455 5029 4553 -804 -1270 278 C ATOM 1628 CG GLN A 207 40.906 43.086 41.474 1.00 47.12 C ANISOU 1628 CG GLN E 207 5195 7212 5495 -2280 256 49 C ATOM 1629 CD GLN A 207 39.489 42.556 41.601 1.00 58.32 C ANISOU 1629 CD GLN E 207 5271 8711 8178 -2199 1161 -85 C ATOM 1630 OE1 GLN A 207 39.073 41.650 40.853 1.00 66.79 O ANISOU 1630 OE1 GLN E 207 6080 5957 13342 -1004 1966 -111 O ATOM 1631 NE2 GLN A 207 38.750 43.133 42.557 1.00 76.22 N ANISOU 1631 NE2 GLN E 207 4748 13694 10520 -4923 636 1575 N ATOM 1632 N LYS A 208 43.116 40.447 41.485 1.00 25.90 N ANISOU 1632 N LYS E 208 4036 3076 2728 -346 -118 256 N ATOM 1633 CA LYS A 208 44.073 40.038 42.502 1.00 26.11 C ANISOU 1633 CA LYS E 208 3765 3732 2423 -458 139 294 C ATOM 1634 C LYS A 208 45.046 38.976 42.015 1.00 26.21 C ANISOU 1634 C LYS E 208 3512 3888 2558 -387 -252 646 C ATOM 1635 O LYS A 208 45.874 38.427 42.741 1.00 26.03 O ANISOU 1635 O LYS E 208 3872 3305 2713 -291 -176 195 O ATOM 1636 CB LYS A 208 43.309 39.439 43.691 1.00 26.25 C ANISOU 1636 CB LYS E 208 3674 3411 2887 -397 148 -17 C ATOM 1637 CG LYS A 208 42.182 40.359 44.164 1.00 30.23 C ANISOU 1637 CG LYS E 208 4395 3646 3444 -621 1015 -299 C ATOM 1638 CD LYS A 208 42.724 41.693 44.656 1.00 31.45 C ANISOU 1638 CD LYS E 208 4882 3749 3319 -1187 -14 134 C ATOM 1639 CE LYS A 208 41.613 42.415 45.414 1.00 33.73 C ANISOU 1639 CE LYS E 208 4506 4101 4209 -1327 -214 329 C ATOM 1640 NZ LYS A 208 42.031 43.774 45.823 1.00 36.37 N ANISOU 1640 NZ LYS E 208 5786 3210 4825 -1811 65 -212 N ATOM 1641 N ALA A 209 44.946 38.624 40.749 1.00 27.52 N ANISOU 1641 N ALA E 209 3856 3895 2704 -341 -333 905 N ATOM 1642 CA ALA A 209 45.715 37.492 40.238 1.00 25.88 C ANISOU 1642 CA ALA E 209 3565 3497 2773 -123 -826 957 C ATOM 1643 C ALA A 209 47.213 37.729 40.329 1.00 25.14 C ANISOU 1643 C ALA E 209 3546 3492 2513 -82 -760 754 C ATOM 1644 O ALA A 209 47.964 36.800 40.672 1.00 26.85 O ANISOU 1644 O ALA E 209 3455 3812 2936 -140 -241 8 O ATOM 1645 CB ALA A 209 45.274 37.169 38.803 1.00 23.02 C ANISOU 1645 CB ALA E 209 2921 3511 2316 25 -299 546 C ATOM 1646 N LEU A 210 47.676 38.935 40.034 1.00 25.44 N ANISOU 1646 N LEU E 210 3524 3670 2471 -183 -458 358 N ATOM 1647 CA LEU A 210 49.135 39.166 40.134 1.00 25.96 C ANISOU 1647 CA LEU E 210 3513 3934 2415 -72 -197 183 C ATOM 1648 C LEU A 210 49.592 39.115 41.584 1.00 25.20 C ANISOU 1648 C LEU E 210 3328 3734 2514 20 -310 632 C ATOM 1649 O LEU A 210 50.690 38.647 41.899 1.00 31.16 O ANISOU 1649 O LEU E 210 4203 4560 3078 -900 -917 898 O ATOM 1650 CB LEU A 210 49.550 40.505 39.518 1.00 27.50 C ANISOU 1650 CB LEU E 210 3969 3660 2821 -64 138 434 C ATOM 1651 CG LEU A 210 49.602 40.536 37.992 1.00 30.14 C ANISOU 1651 CG LEU E 210 4555 3985 2914 -429 747 -23 C ATOM 1652 CD1 LEU A 210 49.715 41.966 37.481 1.00 40.51 C ANISOU 1652 CD1 LEU E 210 6486 4436 4470 -530 822 -963 C ATOM 1653 CD2 LEU A 210 50.757 39.700 37.467 1.00 33.37 C ANISOU 1653 CD2 LEU E 210 4280 4458 3940 -58 1358 352 C ATOM 1654 N ALA A 211 48.728 39.614 42.480 1.00 27.48 N ANISOU 1654 N ALA E 211 4486 3291 2663 -308 115 631 N ATOM 1655 CA ALA A 211 49.068 39.539 43.889 1.00 28.29 C ANISOU 1655 CA ALA E 211 3993 4123 2631 -618 294 169 C ATOM 1656 C ALA A 211 49.124 38.091 44.359 1.00 28.10 C ANISOU 1656 C ALA E 211 4031 3919 2728 -565 200 406 C ATOM 1657 O ALA A 211 50.011 37.750 45.154 1.00 28.25 O ANISOU 1657 O ALA E 211 3966 3542 3227 -506 8 452 O ATOM 1658 CB ALA A 211 48.054 40.346 44.678 1.00 25.95 C ANISOU 1658 CB ALA E 211 3715 3845 2298 -492 -138 300 C ATOM 1659 N LEU A 212 48.205 37.241 43.900 1.00 29.74 N ANISOU 1659 N LEU E 212 4595 4129 2575 -549 -229 649 N ATOM 1660 CA LEU A 212 48.164 35.842 44.304 1.00 25.23 C ANISOU 1660 CA LEU E 212 3555 4092 1940 -464 -338 834 C ATOM 1661 C LEU A 212 49.446 35.150 43.841 1.00 26.45 C ANISOU 1661 C LEU E 212 3253 4091 2706 -119 118 416 C ATOM 1662 O LEU A 212 50.027 34.339 44.557 1.00 26.73 O ANISOU 1662 O LEU E 212 3539 3928 2690 -461 108 723 O ATOM 1663 CB LEU A 212 47.015 35.075 43.684 1.00 26.14 C ANISOU 1663 CB LEU E 212 3254 5074 1604 -148 130 1069 C ATOM 1664 CG LEU A 212 46.217 34.083 44.499 1.00 31.40 C ANISOU 1664 CG LEU E 212 4836 4104 2990 228 -696 230 C ATOM 1665 CD1 LEU A 212 45.755 32.915 43.633 1.00 31.16 C ANISOU 1665 CD1 LEU E 212 5718 3975 2147 -356 505 747 C ATOM 1666 CD2 LEU A 212 46.941 33.550 45.732 1.00 29.99 C ANISOU 1666 CD2 LEU E 212 3747 2975 4675 428 -1429 -231 C ATOM 1667 N GLN A 213 49.801 35.510 42.613 1.00 28.60 N ANISOU 1667 N GLN E 213 3647 4297 2922 23 421 291 N ATOM 1668 CA GLN A 213 51.032 34.932 42.051 1.00 28.27 C ANISOU 1668 CA GLN E 213 3770 4308 2664 43 296 648 C ATOM 1669 C GLN A 213 52.256 35.358 42.867 1.00 27.90 C ANISOU 1669 C GLN E 213 3697 3508 3397 162 48 28 C ATOM 1670 O GLN A 213 53.138 34.527 43.124 1.00 26.94 O ANISOU 1670 O GLN E 213 3530 3710 2995 -146 559 542 O ATOM 1671 CB GLN A 213 51.184 35.307 40.565 1.00 29.86 C ANISOU 1671 CB GLN E 213 4273 4258 2815 304 573 427 C ATOM 1672 CG GLN A 213 52.154 34.374 39.837 1.00 39.30 C ANISOU 1672 CG GLN E 213 6207 5403 3322 -880 1789 -170 C ATOM 1673 CD GLN A 213 53.580 34.886 39.900 1.00 45.82 C ANISOU 1673 CD GLN E 213 5764 6136 5508 -1206 2816 22 C ATOM 1674 OE1 GLN A 213 53.761 36.056 40.247 1.00 53.98 O ANISOU 1674 OE1 GLN E 213 5710 6244 8557 -370 2661 187 O ATOM 1675 NE2 GLN A 213 54.588 34.075 39.623 1.00 57.17 N ANISOU 1675 NE2 GLN E 213 6683 8012 7026 -2886 1918 53 N ATOM 1676 N ALA A 214 52.295 36.638 43.237 1.00 28.99 N ANISOU 1676 N ALA E 214 4033 3798 3185 -353 -195 686 N ATOM 1677 CA ALA A 214 53.434 37.125 44.009 1.00 28.54 C ANISOU 1677 CA ALA E 214 3677 3693 3475 -175 -111 350 C ATOM 1678 C ALA A 214 53.448 36.457 45.376 1.00 28.15 C ANISOU 1678 C ALA E 214 3485 3684 3525 -42 -286 270 C ATOM 1679 O ALA A 214 54.548 36.181 45.888 1.00 32.38 O ANISOU 1679 O ALA E 214 3423 5591 3289 -771 170 210 O ATOM 1680 CB ALA A 214 53.418 38.630 44.208 1.00 28.84 C ANISOU 1680 CB ALA E 214 3188 3675 4096 -530 -1297 130 C ATOM 1681 N ALA A 215 52.278 36.199 45.956 1.00 26.92 N ANISOU 1681 N ALA E 215 3358 3711 3160 20 -495 438 N ATOM 1682 CA ALA A 215 52.217 35.553 47.270 1.00 30.50 C ANISOU 1682 CA ALA E 215 4225 3758 3604 -113 -91 36 C ATOM 1683 C ALA A 215 52.690 34.102 47.210 1.00 27.87 C ANISOU 1683 C ALA E 215 3067 3676 3846 215 -514 194 C ATOM 1684 O ALA A 215 53.434 33.648 48.079 1.00 28.10 O ANISOU 1684 O ALA E 215 3415 4015 3248 -44 -217 177 O ATOM 1685 CB ALA A 215 50.810 35.616 47.867 1.00 26.25 C ANISOU 1685 CB ALA E 215 4114 3604 2255 -51 -540 938 C ATOM 1686 N VAL A 216 52.259 33.357 46.193 1.00 26.01 N ANISOU 1686 N VAL E 216 2832 4068 2981 93 223 219 N ATOM 1687 CA VAL A 216 52.423 31.915 46.172 1.00 28.99 C ANISOU 1687 CA VAL E 216 3507 4112 3397 -225 178 765 C ATOM 1688 C VAL A 216 53.638 31.485 45.366 1.00 28.46 C ANISOU 1688 C VAL E 216 3112 4337 3362 -369 41 110 C ATOM 1689 O VAL A 216 54.406 30.618 45.833 1.00 31.65 O ANISOU 1689 O VAL E 216 3387 4551 4086 -556 -656 424 O ATOM 1690 CB VAL A 216 51.154 31.263 45.579 1.00 29.65 C ANISOU 1690 CB VAL E 216 3251 3832 4183 68 523 354 C ATOM 1691 CG1 VAL A 216 51.311 29.765 45.336 1.00 29.03 C ANISOU 1691 CG1 VAL E 216 3443 3719 3869 105 375 13 C ATOM 1692 CG2 VAL A 216 49.954 31.512 46.495 1.00 30.11 C ANISOU 1692 CG2 VAL E 216 3985 3878 3576 615 904 487 C ATOM 1693 N GLU A 217 53.873 32.021 44.172 1.00 29.52 N ANISOU 1693 N GLU E 217 3976 4112 3127 260 137 542 N ATOM 1694 CA GLU A 217 54.948 31.490 43.327 1.00 27.64 C ANISOU 1694 CA GLU E 217 3965 3921 2615 -127 -259 328 C ATOM 1695 C GLU A 217 56.137 32.434 43.287 1.00 27.57 C ANISOU 1695 C GLU E 217 3324 3921 3230 -513 -371 158 C ATOM 1696 O GLU A 217 57.242 32.012 42.972 1.00 30.82 O ANISOU 1696 O GLU E 217 3867 4616 3227 -699 388 516 O ATOM 1697 CB GLU A 217 54.551 31.300 41.857 1.00 28.51 C ANISOU 1697 CB GLU E 217 4447 3723 2661 -394 -510 230 C ATOM 1698 CG GLU A 217 53.750 30.071 41.529 1.00 31.72 C ANISOU 1698 CG GLU E 217 5028 3915 3109 -231 -796 545 C ATOM 1699 CD GLU A 217 53.166 30.118 40.131 1.00 30.22 C ANISOU 1699 CD GLU E 217 4414 4065 3004 153 -513 122 C ATOM 1700 OE1 GLU A 217 53.508 31.034 39.350 1.00 35.52 O ANISOU 1700 OE1 GLU E 217 5903 4209 3386 209 -68 -39 O ATOM 1701 OE2 GLU A 217 52.347 29.259 39.747 1.00 30.37 O ANISOU 1701 OE2 GLU E 217 4816 3827 2895 -71 -240 972 O ATOM 1702 N GLY A 218 55.928 33.711 43.572 1.00 27.03 N ANISOU 1702 N GLY E 218 3319 3806 3146 -253 182 24 N ATOM 1703 CA GLY A 218 57.065 34.618 43.452 1.00 27.96 C ANISOU 1703 CA GLY E 218 3346 4040 3238 -207 332 -278 C ATOM 1704 C GLY A 218 58.031 34.513 44.611 1.00 26.15 C ANISOU 1704 C GLY E 218 3303 3304 3330 261 346 -666 C ATOM 1705 O GLY A 218 57.849 33.745 45.540 1.00 26.74 O ANISOU 1705 O GLY E 218 3373 3412 3376 240 541 -709 O ATOM 1706 N CYS A 219 59.104 35.305 44.576 1.00 24.88 N ANISOU 1706 N CYS E 219 3568 2925 2958 352 743 37 N ATOM 1707 CA CYS A 219 60.030 35.292 45.679 1.00 30.38 C ANISOU 1707 CA CYS E 219 4496 3078 3969 623 -280 303 C ATOM 1708 C CYS A 219 59.683 36.395 46.688 1.00 30.85 C ANISOU 1708 C CYS E 219 4438 3599 3682 74 -540 392 C ATOM 1709 O CYS A 219 58.889 37.295 46.413 1.00 25.68 O ANISOU 1709 O CYS E 219 3123 3511 3124 661 -12 78 O ATOM 1710 CB CYS A 219 61.471 35.494 45.203 1.00 37.11 C ANISOU 1710 CB CYS E 219 3936 4930 5235 -330 -381 641 C ATOM 1711 SG CYS A 219 62.143 34.107 44.249 1.00 58.04 S ANISOU 1711 SG CYS E 219 7872 5748 8434 -1355 2190 1007 S ATOM 1712 N VAL A 220 60.310 36.306 47.849 1.00 27.88 N ANISOU 1712 N VAL E 220 3496 3703 3394 104 59 -12 N ATOM 1713 CA VAL A 220 60.086 37.305 48.892 1.00 26.75 C ANISOU 1713 CA VAL E 220 3323 3784 3057 282 28 -76 C ATOM 1714 C VAL A 220 60.622 38.677 48.487 1.00 26.58 C ANISOU 1714 C VAL E 220 3305 3766 3028 181 527 46 C ATOM 1715 O VAL A 220 61.791 38.871 48.135 1.00 26.98 O ANISOU 1715 O VAL E 220 3141 3674 3436 -52 435 -131 O ATOM 1716 CB VAL A 220 60.718 36.840 50.215 1.00 33.69 C ANISOU 1716 CB VAL E 220 5260 4232 3308 -763 -327 -237 C ATOM 1717 CG1 VAL A 220 60.581 37.953 51.263 1.00 29.53 C ANISOU 1717 CG1 VAL E 220 4246 4100 2875 -432 -540 -467 C ATOM 1718 CG2 VAL A 220 60.068 35.545 50.673 1.00 29.12 C ANISOU 1718 CG2 VAL E 220 4256 4208 2601 -760 -991 -56 C ATOM 1719 N ASN A 221 59.743 39.688 48.527 1.00 23.80 N ANISOU 1719 N ASN E 221 2734 3576 2733 519 250 357 N ATOM 1720 CA ASN A 221 60.238 41.029 48.252 1.00 26.01 C ANISOU 1720 CA ASN E 221 2969 3599 3315 539 773 400 C ATOM 1721 C ASN A 221 59.285 42.061 48.842 1.00 28.17 C ANISOU 1721 C ASN E 221 2942 3749 4012 85 133 543 C ATOM 1722 O ASN A 221 58.074 41.851 48.857 1.00 30.71 O ANISOU 1722 O ASN E 221 3047 3707 4914 270 773 475 O ATOM 1723 CB ASN A 221 60.434 41.257 46.754 1.00 33.22 C ANISOU 1723 CB ASN E 221 5329 3818 3475 153 881 -227 C ATOM 1724 CG ASN A 221 59.085 41.578 46.152 1.00 39.44 C ANISOU 1724 CG ASN E 221 6876 4170 3941 -916 -536 452 C ATOM 1725 OD1 ASN A 221 58.755 42.754 46.031 1.00 50.59 O ANISOU 1725 OD1 ASN E 221 9635 4632 4955 -1970 -966 36 O ATOM 1726 ND2 ASN A 221 58.354 40.526 45.818 1.00 39.14 N ANISOU 1726 ND2 ASN E 221 4934 5456 4482 -196 908 529 N ATOM 1727 N HIS A 222 59.831 43.166 49.345 1.00 24.93 N ANISOU 1727 N HIS E 222 3292 3123 3055 99 244 -201 N ATOM 1728 CA HIS A 222 58.980 44.113 50.056 1.00 28.03 C ANISOU 1728 CA HIS E 222 3672 3846 3130 -342 -116 313 C ATOM 1729 C HIS A 222 58.075 44.912 49.137 1.00 25.51 C ANISOU 1729 C HIS E 222 3150 3788 2756 -191 167 370 C ATOM 1730 O HIS A 222 57.190 45.624 49.594 1.00 26.47 O ANISOU 1730 O HIS E 222 3347 4108 2601 -357 606 -136 O ATOM 1731 CB HIS A 222 59.876 45.047 50.888 1.00 27.71 C ANISOU 1731 CB HIS E 222 3610 4005 2913 -335 -149 269 C ATOM 1732 CG HIS A 222 60.689 46.002 50.068 1.00 30.41 C ANISOU 1732 CG HIS E 222 4463 3639 3452 -122 171 392 C ATOM 1733 ND1 HIS A 222 61.152 47.164 50.623 1.00 30.51 N ANISOU 1733 ND1 HIS E 222 4026 3751 3813 -351 -41 647 N ATOM 1734 CD2 HIS A 222 61.150 46.000 48.775 1.00 28.37 C ANISOU 1734 CD2 HIS E 222 3804 3680 3294 164 -146 175 C ATOM 1735 CE1 HIS A 222 61.843 47.849 49.725 1.00 29.61 C ANISOU 1735 CE1 HIS E 222 3212 3860 4178 -174 -48 794 C ATOM 1736 NE2 HIS A 222 61.859 47.171 48.588 1.00 27.77 N ANISOU 1736 NE2 HIS E 222 3066 3834 3652 142 -437 335 N ATOM 1737 N MET A 223 58.280 44.857 47.817 1.00 25.07 N ANISOU 1737 N MET E 223 3191 3482 2852 -2 648 90 N ATOM 1738 CA MET A 223 57.417 45.680 46.966 1.00 27.84 C ANISOU 1738 CA MET E 223 3817 3836 2926 20 235 -63 C ATOM 1739 C MET A 223 56.024 45.042 46.848 1.00 28.01 C ANISOU 1739 C MET E 223 3332 3791 3519 -420 477 -313 C ATOM 1740 O MET A 223 55.028 45.752 46.653 1.00 32.61 O ANISOU 1740 O MET E 223 4043 4364 3982 -827 -476 -588 O ATOM 1741 CB MET A 223 58.015 45.914 45.581 1.00 31.81 C ANISOU 1741 CB MET E 223 3759 4994 3335 -137 569 -704 C ATOM 1742 CG MET A 223 59.172 46.874 45.431 1.00 35.49 C ANISOU 1742 CG MET E 223 4971 4284 4229 278 1229 -251 C ATOM 1743 SD MET A 223 58.835 48.620 45.754 1.00 45.43 S ANISOU 1743 SD MET E 223 7173 4720 5367 -457 4 786 S ATOM 1744 CE MET A 223 57.230 48.815 45.016 1.00 45.69 C ANISOU 1744 CE MET E 223 6965 6223 4174 -1548 947 -545 C ATOM 1745 N TRP A 224 55.934 43.722 46.954 1.00 26.46 N ANISOU 1745 N TRP E 224 3248 3792 3012 -210 580 -393 N ATOM 1746 CA TRP A 224 54.690 42.977 47.032 1.00 25.51 C ANISOU 1746 CA TRP E 224 2915 3982 2794 -399 599 -47 C ATOM 1747 C TRP A 224 54.580 42.457 48.460 1.00 23.92 C ANISOU 1747 C TRP E 224 2798 3541 2750 126 299 111 C ATOM 1748 O TRP A 224 55.041 41.344 48.741 1.00 28.18 O ANISOU 1748 O TRP E 224 4073 4026 2607 -664 -261 251 O ATOM 1749 CB TRP A 224 54.667 41.820 46.033 1.00 26.22 C ANISOU 1749 CB TRP E 224 3118 4195 2652 -420 353 18 C ATOM 1750 CG TRP A 224 54.628 42.328 44.606 1.00 27.79 C ANISOU 1750 CG TRP E 224 3388 4375 2797 -169 32 -98 C ATOM 1751 CD1 TRP A 224 55.689 42.764 43.871 1.00 28.37 C ANISOU 1751 CD1 TRP E 224 3671 4310 2800 -9 -75 -617 C ATOM 1752 CD2 TRP A 224 53.493 42.453 43.746 1.00 28.12 C ANISOU 1752 CD2 TRP E 224 3668 4114 2901 -141 -221 210 C ATOM 1753 NE1 TRP A 224 55.301 43.150 42.624 1.00 29.97 N ANISOU 1753 NE1 TRP E 224 3806 4833 2747 -261 -224 -395 N ATOM 1754 CE2 TRP A 224 53.942 42.970 42.517 1.00 30.42 C ANISOU 1754 CE2 TRP E 224 3885 4698 2975 -218 -329 -98 C ATOM 1755 CE3 TRP A 224 52.134 42.185 43.880 1.00 27.83 C ANISOU 1755 CE3 TRP E 224 3701 3809 3064 31 -475 414 C ATOM 1756 CZ2 TRP A 224 53.084 43.219 41.447 1.00 30.60 C ANISOU 1756 CZ2 TRP E 224 3923 4616 3087 -197 -442 -43 C ATOM 1757 CZ3 TRP A 224 51.272 42.428 42.825 1.00 28.39 C ANISOU 1757 CZ3 TRP E 224 3913 3697 3177 -26 -548 146 C ATOM 1758 CH2 TRP A 224 51.753 42.945 41.611 1.00 29.45 C ANISOU 1758 CH2 TRP E 224 3780 4361 3050 -619 -160 298 C ATOM 1759 N THR A 225 54.021 43.264 49.365 1.00 24.46 N ANISOU 1759 N THR E 225 2994 3587 2711 71 623 -144 N ATOM 1760 CA THR A 225 54.019 42.964 50.791 1.00 23.89 C ANISOU 1760 CA THR E 225 2936 3457 2683 -37 365 -176 C ATOM 1761 C THR A 225 53.514 41.555 51.068 1.00 23.19 C ANISOU 1761 C THR E 225 3060 3332 2421 -189 -249 -227 C ATOM 1762 O THR A 225 54.070 40.846 51.905 1.00 24.92 O ANISOU 1762 O THR E 225 3742 3616 2112 -581 -167 -160 O ATOM 1763 CB THR A 225 53.140 43.982 51.546 1.00 28.76 C ANISOU 1763 CB THR E 225 5097 3622 2209 -1100 151 -226 C ATOM 1764 OG1 THR A 225 53.600 45.294 51.221 1.00 26.14 O ANISOU 1764 OG1 THR E 225 3254 3870 2808 -573 134 514 O ATOM 1765 CG2 THR A 225 53.293 43.818 53.053 1.00 25.10 C ANISOU 1765 CG2 THR E 225 3289 3990 2260 -19 -1080 637 C ATOM 1766 N ILE A 226 52.469 41.150 50.368 1.00 23.82 N ANISOU 1766 N ILE E 226 3298 3556 2197 -70 -148 250 N ATOM 1767 CA ILE A 226 51.868 39.831 50.542 1.00 26.22 C ANISOU 1767 CA ILE E 226 3673 3367 2922 -125 -323 466 C ATOM 1768 C ILE A 226 52.886 38.710 50.362 1.00 27.08 C ANISOU 1768 C ILE E 226 3529 3616 3145 -236 -8 -107 C ATOM 1769 O ILE A 226 52.721 37.628 50.964 1.00 25.56 O ANISOU 1769 O ILE E 226 3398 3644 2671 -280 170 31 O ATOM 1770 CB ILE A 226 50.679 39.623 49.574 1.00 24.10 C ANISOU 1770 CB ILE E 226 3102 3689 2368 264 168 -148 C ATOM 1771 CG1 ILE A 226 49.767 38.459 49.993 1.00 26.09 C ANISOU 1771 CG1 ILE E 226 2996 3888 3031 95 447 -573 C ATOM 1772 CG2 ILE A 226 51.126 39.439 48.110 1.00 22.86 C ANISOU 1772 CG2 ILE E 226 2494 3551 2642 498 325 295 C ATOM 1773 CD1 ILE A 226 48.947 38.773 51.237 1.00 30.57 C ANISOU 1773 CD1 ILE E 226 3755 4324 3538 229 1015 -389 C ATOM 1774 N SER A 227 53.941 38.918 49.561 1.00 25.04 N ANISOU 1774 N SER E 227 3424 3454 2636 -15 -298 -68 N ATOM 1775 CA SER A 227 54.951 37.867 49.407 1.00 26.89 C ANISOU 1775 CA SER E 227 3845 3709 2662 -327 253 -370 C ATOM 1776 C SER A 227 55.665 37.575 50.727 1.00 27.33 C ANISOU 1776 C SER E 227 3780 3607 2999 -575 -69 -80 C ATOM 1777 O SER A 227 56.206 36.490 50.928 1.00 25.90 O ANISOU 1777 O SER E 227 3228 3565 3048 -395 43 -78 O ATOM 1778 CB SER A 227 55.994 38.232 48.348 1.00 28.65 C ANISOU 1778 CB SER E 227 3612 3899 3375 57 326 -525 C ATOM 1779 OG SER A 227 56.875 39.250 48.826 1.00 29.28 O ANISOU 1779 OG SER E 227 4302 3703 3122 -12 499 -34 O ATOM 1780 N CYS A 228 55.679 38.557 51.656 1.00 27.72 N ANISOU 1780 N CYS E 228 3531 3482 3517 -138 -413 144 N ATOM 1781 CA CYS A 228 56.448 38.221 52.861 1.00 30.52 C ANISOU 1781 CA CYS E 228 3796 4297 3502 -259 -491 167 C ATOM 1782 C CYS A 228 55.655 37.261 53.745 1.00 28.64 C ANISOU 1782 C CYS E 228 4034 3652 3198 -282 -635 375 C ATOM 1783 O CYS A 228 56.216 36.724 54.707 1.00 28.04 O ANISOU 1783 O CYS E 228 4053 4283 2318 -141 -620 895 O ATOM 1784 CB CYS A 228 56.932 39.518 53.524 1.00 35.97 C ANISOU 1784 CB CYS E 228 4947 4097 4625 374 -2151 -672 C ATOM 1785 SG CYS A 228 57.903 40.529 52.276 1.00 44.93 S ANISOU 1785 SG CYS E 228 6784 4787 5499 995 -101 253 S ATOM 1786 N LEU A 229 54.390 36.958 53.437 1.00 25.14 N ANISOU 1786 N LEU E 229 3768 3358 2425 -601 -289 556 N ATOM 1787 CA LEU A 229 53.698 35.909 54.198 1.00 26.01 C ANISOU 1787 CA LEU E 229 3763 3876 2245 -645 -166 307 C ATOM 1788 C LEU A 229 54.319 34.536 54.010 1.00 27.05 C ANISOU 1788 C LEU E 229 3811 3617 2851 -359 608 -10 C ATOM 1789 O LEU A 229 54.044 33.610 54.786 1.00 25.11 O ANISOU 1789 O LEU E 229 3310 3704 2526 -28 400 164 O ATOM 1790 CB LEU A 229 52.208 35.854 53.822 1.00 27.99 C ANISOU 1790 CB LEU E 229 3715 4359 2561 -462 -105 389 C ATOM 1791 CG LEU A 229 51.395 37.027 54.398 1.00 35.45 C ANISOU 1791 CG LEU E 229 4502 5677 3289 -1842 -283 498 C ATOM 1792 CD1 LEU A 229 49.944 36.940 53.976 1.00 35.34 C ANISOU 1792 CD1 LEU E 229 4276 6000 3152 -1493 117 -705 C ATOM 1793 CD2 LEU A 229 51.498 37.030 55.916 1.00 30.45 C ANISOU 1793 CD2 LEU E 229 3824 4477 3267 -1275 323 542 C ATOM 1794 N GLN A 230 55.171 34.370 53.004 1.00 26.40 N ANISOU 1794 N GLN E 230 3851 3533 2648 -560 549 -290 N ATOM 1795 CA GLN A 230 55.918 33.132 52.839 1.00 25.65 C ANISOU 1795 CA GLN E 230 3857 3443 2445 -411 8 347 C ATOM 1796 C GLN A 230 56.807 32.854 54.055 1.00 24.61 C ANISOU 1796 C GLN E 230 3239 3277 2836 167 82 -266 C ATOM 1797 O GLN A 230 57.170 31.712 54.327 1.00 26.95 O ANISOU 1797 O GLN E 230 3802 3453 2986 -187 192 -316 O ATOM 1798 CB GLN A 230 56.820 33.184 51.595 1.00 25.56 C ANISOU 1798 CB GLN E 230 4034 3023 2655 -236 224 432 C ATOM 1799 CG GLN A 230 56.057 33.193 50.281 1.00 25.03 C ANISOU 1799 CG GLN E 230 3973 3053 2486 296 372 499 C ATOM 1800 CD GLN A 230 56.973 33.241 49.073 1.00 27.22 C ANISOU 1800 CD GLN E 230 3859 3743 2742 -48 491 -185 C ATOM 1801 OE1 GLN A 230 58.102 32.734 49.133 1.00 28.77 O ANISOU 1801 OE1 GLN E 230 3961 3766 3204 -190 487 95 O ATOM 1802 NE2 GLN A 230 56.501 33.842 47.977 1.00 31.30 N ANISOU 1802 NE2 GLN E 230 4572 4527 2795 -375 440 -383 N ATOM 1803 N LEU A 231 57.170 33.927 54.762 1.00 25.39 N ANISOU 1803 N LEU E 231 3599 3562 2485 206 -28 -133 N ATOM 1804 CA LEU A 231 58.036 33.785 55.918 1.00 24.25 C ANISOU 1804 CA LEU E 231 3256 3484 2474 130 188 -459 C ATOM 1805 C LEU A 231 57.213 33.651 57.199 1.00 24.06 C ANISOU 1805 C LEU E 231 3218 3411 2514 113 235 -303 C ATOM 1806 O LEU A 231 57.758 33.443 58.291 1.00 31.82 O ANISOU 1806 O LEU E 231 4543 5218 2330 -1154 174 -216 O ATOM 1807 CB LEU A 231 58.968 34.993 56.058 1.00 25.21 C ANISOU 1807 CB LEU E 231 2684 3926 2969 149 149 -360 C ATOM 1808 CG LEU A 231 59.841 35.246 54.827 1.00 27.06 C ANISOU 1808 CG LEU E 231 3295 3610 3378 173 658 -285 C ATOM 1809 CD1 LEU A 231 60.718 36.464 55.082 1.00 28.51 C ANISOU 1809 CD1 LEU E 231 3502 4002 3326 534 145 -685 C ATOM 1810 CD2 LEU A 231 60.624 33.981 54.508 1.00 28.42 C ANISOU 1810 CD2 LEU E 231 3397 4006 3397 -320 521 -514 C ATOM 1811 N HIS A 232 55.898 33.768 57.065 1.00 26.95 N ANISOU 1811 N HIS E 232 3167 3463 3609 -99 451 265 N ATOM 1812 CA HIS A 232 55.084 33.694 58.286 1.00 26.73 C ANISOU 1812 CA HIS E 232 2986 3787 3384 -101 213 -20 C ATOM 1813 C HIS A 232 54.890 32.253 58.711 1.00 25.36 C ANISOU 1813 C HIS E 232 3199 3722 2714 -146 -298 93 C ATOM 1814 O HIS A 232 54.731 31.344 57.902 1.00 29.30 O ANISOU 1814 O HIS E 232 4631 3628 2874 -997 159 409 O ATOM 1815 CB HIS A 232 53.754 34.414 58.020 1.00 24.21 C ANISOU 1815 CB HIS E 232 3148 3584 2465 -189 147 217 C ATOM 1816 CG HIS A 232 52.966 34.585 59.282 1.00 24.58 C ANISOU 1816 CG HIS E 232 3459 3392 2489 -228 314 -9 C ATOM 1817 ND1 HIS A 232 52.140 33.586 59.749 1.00 24.87 N ANISOU 1817 ND1 HIS E 232 3275 3272 2904 -316 339 11 N ATOM 1818 CD2 HIS A 232 52.899 35.611 60.156 1.00 23.99 C ANISOU 1818 CD2 HIS E 232 3153 3477 2487 -108 361 69 C ATOM 1819 CE1 HIS A 232 51.579 33.997 60.882 1.00 27.11 C ANISOU 1819 CE1 HIS E 232 3390 3582 3326 73 781 245 C ATOM 1820 NE2 HIS A 232 52.020 35.217 61.149 1.00 27.56 N ANISOU 1820 NE2 HIS E 232 3913 3291 3266 -106 1117 149 N ATOM 1821 N PRO A 233 54.917 31.969 60.016 1.00 29.85 N ANISOU 1821 N PRO E 233 4389 4130 2825 -525 -831 -39 N ATOM 1822 CA PRO A 233 54.770 30.578 60.463 1.00 29.55 C ANISOU 1822 CA PRO E 233 4353 4227 2648 -629 20 -135 C ATOM 1823 C PRO A 233 53.466 29.930 60.012 1.00 30.17 C ANISOU 1823 C PRO E 233 4240 3997 3226 -655 269 54 C ATOM 1824 O PRO A 233 53.443 28.702 59.827 1.00 30.28 O ANISOU 1824 O PRO E 233 4342 3887 3276 -373 1171 -270 O ATOM 1825 CB PRO A 233 54.788 30.671 61.990 1.00 29.53 C ANISOU 1825 CB PRO E 233 4372 4156 2691 -1082 502 167 C ATOM 1826 CG PRO A 233 54.751 32.106 62.332 1.00 33.98 C ANISOU 1826 CG PRO E 233 5727 4093 3092 -287 649 102 C ATOM 1827 CD PRO A 233 55.121 32.911 61.122 1.00 31.71 C ANISOU 1827 CD PRO E 233 5181 4341 2525 -575 -100 46 C ATOM 1828 N LYS A 234 52.367 30.655 59.832 1.00 28.88 N ANISOU 1828 N LYS E 234 3639 4258 3076 -531 1301 -227 N ATOM 1829 CA LYS A 234 51.091 29.984 59.572 1.00 29.54 C ANISOU 1829 CA LYS E 234 3940 4172 3110 -404 1065 -86 C ATOM 1830 C LYS A 234 50.148 30.862 58.756 1.00 33.54 C ANISOU 1830 C LYS E 234 4515 4743 3485 -914 306 503 C ATOM 1831 O LYS A 234 49.278 31.560 59.303 1.00 27.61 O ANISOU 1831 O LYS E 234 2921 4179 3391 248 464 169 O ATOM 1832 CB LYS A 234 50.418 29.601 60.897 1.00 30.48 C ANISOU 1832 CB LYS E 234 3351 4769 3459 -536 1563 245 C ATOM 1833 CG LYS A 234 49.609 28.326 60.767 1.00 38.16 C ANISOU 1833 CG LYS E 234 4449 4908 5142 -7 2316 -28 C ATOM 1834 CD LYS A 234 48.720 28.113 61.980 1.00 47.81 C ANISOU 1834 CD LYS E 234 6546 5808 5814 -229 3168 -1844 C ATOM 1835 CE LYS A 234 49.594 27.965 63.213 1.00 54.11 C ANISOU 1835 CE LYS E 234 8746 6080 5734 -1419 2641 -2081 C ATOM 1836 NZ LYS A 234 49.350 26.614 63.804 1.00 66.62 N ANISOU 1836 NZ LYS E 234 10734 5787 8791 -2122 2186 -2864 N ATOM 1837 N ALA A 235 50.341 30.823 57.445 1.00 27.96 N ANISOU 1837 N ALA E 235 3557 3681 3387 -288 66 568 N ATOM 1838 CA ALA A 235 49.595 31.633 56.497 1.00 31.58 C ANISOU 1838 CA ALA E 235 3988 4098 3913 -355 -424 435 C ATOM 1839 C ALA A 235 48.759 30.786 55.536 1.00 29.07 C ANISOU 1839 C ALA E 235 3748 3818 3480 -355 -57 357 C ATOM 1840 O ALA A 235 49.105 29.687 55.059 1.00 31.00 O ANISOU 1840 O ALA E 235 3926 3599 4253 -14 747 353 O ATOM 1841 CB ALA A 235 50.559 32.525 55.719 1.00 30.40 C ANISOU 1841 CB ALA E 235 4795 3101 3656 -216 -579 613 C ATOM 1842 N ILE A 236 47.570 31.326 55.238 1.00 26.94 N ANISOU 1842 N ILE E 236 3158 3904 3176 100 507 -133 N ATOM 1843 CA ILE A 236 46.622 30.652 54.369 1.00 31.10 C ANISOU 1843 CA ILE E 236 3868 4157 3793 175 -244 -227 C ATOM 1844 C ILE A 236 46.039 31.637 53.370 1.00 29.56 C ANISOU 1844 C ILE E 236 3757 4065 3411 -181 121 1 C ATOM 1845 O ILE A 236 45.583 32.681 53.817 1.00 33.00 O ANISOU 1845 O ILE E 236 5284 4375 2879 -612 -69 189 O ATOM 1846 CB ILE A 236 45.467 30.047 55.189 1.00 31.23 C ANISOU 1846 CB ILE E 236 3621 4325 3921 596 -804 -478 C ATOM 1847 CG1 ILE A 236 45.956 29.286 56.414 1.00 35.13 C ANISOU 1847 CG1 ILE E 236 3770 5456 4123 385 -695 -1035 C ATOM 1848 CG2 ILE A 236 44.570 29.170 54.330 1.00 31.42 C ANISOU 1848 CG2 ILE E 236 2994 5127 3817 -118 -89 1014 C ATOM 1849 CD1 ILE A 236 44.870 28.667 57.278 1.00 55.06 C ANISOU 1849 CD1 ILE E 236 7612 6737 6571 -825 3180 -2168 C ATOM 1850 N MET A 237 46.070 31.293 52.100 1.00 29.36 N ANISOU 1850 N MET E 237 3617 4074 3464 -752 422 95 N ATOM 1851 CA MET A 237 45.410 32.040 51.049 1.00 30.49 C ANISOU 1851 CA MET E 237 3624 4555 3407 -270 224 -150 C ATOM 1852 C MET A 237 44.151 31.260 50.625 1.00 30.72 C ANISOU 1852 C MET E 237 3624 4444 3602 -190 392 -60 C ATOM 1853 O MET A 237 44.288 30.076 50.286 1.00 31.33 O ANISOU 1853 O MET E 237 3859 4527 3519 -259 548 85 O ATOM 1854 CB MET A 237 46.242 32.239 49.792 1.00 32.89 C ANISOU 1854 CB MET E 237 3613 4865 4018 -523 678 -645 C ATOM 1855 CG MET A 237 47.656 32.728 49.938 1.00 37.03 C ANISOU 1855 CG MET E 237 3307 5944 4817 -827 797 294 C ATOM 1856 SD MET A 237 47.794 34.311 50.742 1.00 48.54 S ANISOU 1856 SD MET E 237 5863 5740 6841 -99 -1040 349 S ATOM 1857 CE MET A 237 47.437 35.507 49.471 1.00 42.25 C ANISOU 1857 CE MET E 237 6070 5304 4680 934 -1908 1637 C ATOM 1858 N VAL A 238 43.020 31.941 50.670 1.00 29.35 N ANISOU 1858 N VAL E 238 3627 4330 3193 -186 196 -143 N ATOM 1859 CA VAL A 238 41.751 31.319 50.271 1.00 28.91 C ANISOU 1859 CA VAL E 238 3688 4254 3042 -176 227 13 C ATOM 1860 C VAL A 238 41.247 32.030 49.021 1.00 28.28 C ANISOU 1860 C VAL E 238 3595 4044 3107 -184 263 -10 C ATOM 1861 O VAL A 238 40.981 33.234 49.062 1.00 28.31 O ANISOU 1861 O VAL E 238 3533 4080 3146 -227 80 217 O ATOM 1862 CB VAL A 238 40.698 31.373 51.385 1.00 29.24 C ANISOU 1862 CB VAL E 238 3648 4347 3114 -173 238 -121 C ATOM 1863 CG1 VAL A 238 39.501 30.480 51.059 1.00 27.27 C ANISOU 1863 CG1 VAL E 238 3419 4035 2908 -480 56 -206 C ATOM 1864 CG2 VAL A 238 41.345 30.993 52.715 1.00 26.61 C ANISOU 1864 CG2 VAL E 238 3134 3775 3200 279 288 -355 C ATOM 1865 N CYS A 239 41.139 31.299 47.901 1.00 25.74 N ANISOU 1865 N CYS E 239 3053 3681 3047 -106 288 -148 N ATOM 1866 CA CYS A 239 40.912 32.097 46.698 1.00 29.29 C ANISOU 1866 CA CYS E 239 3473 4457 3199 307 101 -600 C ATOM 1867 C CYS A 239 39.816 31.539 45.809 1.00 28.69 C ANISOU 1867 C CYS E 239 4053 3961 2886 -135 87 142 C ATOM 1868 O CYS A 239 39.410 30.370 45.880 1.00 29.05 O ANISOU 1868 O CYS E 239 3648 3928 3461 -210 517 295 O ATOM 1869 CB CYS A 239 42.270 32.181 45.987 1.00 34.03 C ANISOU 1869 CB CYS E 239 4347 3865 4719 742 1239 -760 C ATOM 1870 SG CYS A 239 42.749 30.665 45.116 1.00 39.99 S ANISOU 1870 SG CYS E 239 5272 5296 4628 -462 850 -44 S ATOM 1871 N ASP A 240 39.305 32.428 44.929 1.00 26.15 N ANISOU 1871 N ASP E 240 3033 4251 2650 -398 564 161 N ATOM 1872 CA ASP A 240 38.296 31.966 43.985 1.00 29.09 C ANISOU 1872 CA ASP E 240 3413 4564 3075 -481 205 457 C ATOM 1873 C ASP A 240 38.942 31.672 42.639 1.00 28.66 C ANISOU 1873 C ASP E 240 3324 4458 3108 105 229 659 C ATOM 1874 O ASP A 240 40.146 31.868 42.470 1.00 28.38 O ANISOU 1874 O ASP E 240 3477 3970 3336 387 396 598 O ATOM 1875 CB ASP A 240 37.187 32.984 43.821 1.00 29.89 C ANISOU 1875 CB ASP E 240 3770 4689 2899 -685 -195 549 C ATOM 1876 CG ASP A 240 37.572 34.277 43.168 1.00 31.16 C ANISOU 1876 CG ASP E 240 4159 4670 3010 -564 -486 520 C ATOM 1877 OD1 ASP A 240 38.743 34.503 42.811 1.00 32.48 O ANISOU 1877 OD1 ASP E 240 4104 4798 3439 -167 -804 258 O ATOM 1878 OD2 ASP A 240 36.642 35.097 43.010 1.00 31.57 O ANISOU 1878 OD2 ASP E 240 4681 4817 2497 -942 -278 564 O ATOM 1879 N GLU A 241 38.152 31.194 41.690 1.00 29.71 N ANISOU 1879 N GLU E 241 3604 4350 3333 116 44 789 N ATOM 1880 CA GLU A 241 38.743 30.805 40.393 1.00 31.31 C ANISOU 1880 CA GLU E 241 4200 4568 3129 131 101 643 C ATOM 1881 C GLU A 241 39.349 31.955 39.609 1.00 29.43 C ANISOU 1881 C GLU E 241 3646 4509 3026 -128 -340 422 C ATOM 1882 O GLU A 241 40.497 31.859 39.140 1.00 29.66 O ANISOU 1882 O GLU E 241 4029 4344 2898 -75 59 731 O ATOM 1883 CB GLU A 241 37.666 30.086 39.562 1.00 31.59 C ANISOU 1883 CB GLU E 241 4093 5054 2857 382 334 599 C ATOM 1884 CG GLU A 241 38.067 29.822 38.118 1.00 39.18 C ANISOU 1884 CG GLU E 241 6070 5726 3091 -330 353 1361 C ATOM 1885 CD GLU A 241 36.899 29.153 37.404 1.00 49.17 C ANISOU 1885 CD GLU E 241 8485 5771 4425 -723 -2413 1325 C ATOM 1886 OE1 GLU A 241 36.671 27.960 37.688 1.00 58.40 O ANISOU 1886 OE1 GLU E 241 8545 5563 8081 -181 -2846 1624 O ATOM 1887 OE2 GLU A 241 36.208 29.813 36.591 1.00 68.54 O ANISOU 1887 OE2 GLU E 241 9711 9225 7105 -1444 -3487 -521 O ATOM 1888 N PRO A 242 38.668 33.080 39.385 1.00 30.69 N ANISOU 1888 N PRO E 242 4110 4639 2911 -380 -720 663 N ATOM 1889 CA PRO A 242 39.257 34.152 38.589 1.00 31.27 C ANISOU 1889 CA PRO E 242 4644 4100 3136 -448 -489 889 C ATOM 1890 C PRO A 242 40.565 34.682 39.171 1.00 29.98 C ANISOU 1890 C PRO E 242 4208 4477 2705 -484 -265 214 C ATOM 1891 O PRO A 242 41.383 35.216 38.398 1.00 31.45 O ANISOU 1891 O PRO E 242 4778 4586 2587 -409 303 684 O ATOM 1892 CB PRO A 242 38.228 35.274 38.634 1.00 33.73 C ANISOU 1892 CB PRO E 242 4340 4658 3819 -618 -690 612 C ATOM 1893 CG PRO A 242 36.985 34.704 39.235 1.00 34.64 C ANISOU 1893 CG PRO E 242 4523 4941 3700 -700 -610 174 C ATOM 1894 CD PRO A 242 37.300 33.376 39.828 1.00 34.24 C ANISOU 1894 CD PRO E 242 5007 5146 2856 -1301 125 244 C ATOM 1895 N SER A 243 40.780 34.567 40.478 1.00 29.23 N ANISOU 1895 N SER E 243 3971 4416 2718 -540 -182 61 N ATOM 1896 CA SER A 243 42.022 35.076 41.058 1.00 27.31 C ANISOU 1896 CA SER E 243 3917 4111 2349 -525 14 50 C ATOM 1897 C SER A 243 43.243 34.240 40.676 1.00 27.62 C ANISOU 1897 C SER E 243 3848 3712 2935 -250 285 29 C ATOM 1898 O SER A 243 44.384 34.661 40.894 1.00 26.17 O ANISOU 1898 O SER E 243 3898 3493 2554 -331 352 425 O ATOM 1899 CB SER A 243 41.889 35.128 42.589 1.00 29.73 C ANISOU 1899 CB SER E 243 4950 3969 2378 -585 1 256 C ATOM 1900 OG SER A 243 42.026 33.816 43.137 1.00 27.83 O ANISOU 1900 OG SER E 243 3599 4346 2629 -370 39 -250 O ATOM 1901 N THR A 244 43.027 33.044 40.121 1.00 26.75 N ANISOU 1901 N THR E 244 3617 3871 2676 -168 129 104 N ATOM 1902 CA THR A 244 44.134 32.131 39.855 1.00 27.91 C ANISOU 1902 CA THR E 244 4136 3994 2473 -596 -30 87 C ATOM 1903 C THR A 244 44.764 32.314 38.473 1.00 25.34 C ANISOU 1903 C THR E 244 3259 3619 2751 131 26 212 C ATOM 1904 O THR A 244 45.606 31.469 38.129 1.00 30.29 O ANISOU 1904 O THR E 244 4601 4276 2633 -678 -13 649 O ATOM 1905 CB THR A 244 43.720 30.643 39.936 1.00 28.25 C ANISOU 1905 CB THR E 244 4132 4062 2537 -640 618 -320 C ATOM 1906 OG1 THR A 244 42.733 30.388 38.918 1.00 31.66 O ANISOU 1906 OG1 THR E 244 4688 4038 3302 -486 317 809 O ATOM 1907 CG2 THR A 244 43.116 30.269 41.291 1.00 32.74 C ANISOU 1907 CG2 THR E 244 4748 4681 3012 -1123 1583 -177 C ATOM 1908 N MET A 245 44.400 33.335 37.716 1.00 27.73 N ANISOU 1908 N MET E 245 3833 3638 3063 254 323 -141 N ATOM 1909 CA MET A 245 44.771 33.532 36.316 1.00 29.15 C ANISOU 1909 CA MET E 245 3841 4124 3111 -106 489 -229 C ATOM 1910 C MET A 245 46.278 33.581 36.066 1.00 28.19 C ANISOU 1910 C MET E 245 3793 3985 2932 -127 329 146 C ATOM 1911 O MET A 245 46.760 33.168 34.996 1.00 28.07 O ANISOU 1911 O MET E 245 3395 4168 3100 -545 -121 637 O ATOM 1912 CB MET A 245 44.167 34.835 35.739 1.00 32.08 C ANISOU 1912 CB MET E 245 4907 4979 2302 -1388 557 16 C ATOM 1913 CG MET A 245 42.677 34.771 35.461 1.00 33.99 C ANISOU 1913 CG MET E 245 4894 4983 3038 -1511 528 382 C ATOM 1914 SD MET A 245 42.168 33.426 34.364 1.00 43.11 S ANISOU 1914 SD MET E 245 7059 5708 3614 -496 -528 370 S ATOM 1915 CE MET A 245 41.637 32.144 35.494 1.00 42.86 C ANISOU 1915 CE MET E 245 5039 5972 5272 -297 -1271 -500 C ATOM 1916 N GLU A 246 47.064 34.102 37.002 1.00 27.84 N ANISOU 1916 N GLU E 246 3908 3836 2832 -253 438 416 N ATOM 1917 CA GLU A 246 48.492 34.274 36.764 1.00 27.58 C ANISOU 1917 CA GLU E 246 3866 3777 2835 -124 306 269 C ATOM 1918 C GLU A 246 49.305 33.130 37.346 1.00 27.70 C ANISOU 1918 C GLU E 246 3831 3611 3081 5 87 364 C ATOM 1919 O GLU A 246 50.539 33.153 37.247 1.00 30.01 O ANISOU 1919 O GLU E 246 3882 4391 3127 -343 502 121 O ATOM 1920 CB GLU A 246 48.948 35.598 37.377 1.00 26.55 C ANISOU 1920 CB GLU E 246 3614 3741 2732 -456 483 478 C ATOM 1921 CG GLU A 246 48.255 36.801 36.739 1.00 29.45 C ANISOU 1921 CG GLU E 246 4390 3866 2933 -516 254 251 C ATOM 1922 CD GLU A 246 48.885 37.207 35.425 1.00 29.68 C ANISOU 1922 CD GLU E 246 3787 4147 3342 -285 257 -45 C ATOM 1923 OE1 GLU A 246 49.865 36.545 35.002 1.00 32.95 O ANISOU 1923 OE1 GLU E 246 4022 4907 3589 -275 356 926 O ATOM 1924 OE2 GLU A 246 48.409 38.187 34.808 1.00 32.32 O ANISOU 1924 OE2 GLU E 246 4831 3772 3677 228 -161 -223 O ATOM 1925 N LEU A 247 48.664 32.130 37.949 1.00 27.85 N ANISOU 1925 N LEU E 247 4243 3797 2543 -168 485 316 N ATOM 1926 CA LEU A 247 49.414 30.983 38.474 1.00 26.84 C ANISOU 1926 CA LEU E 247 4342 3880 1975 -95 222 389 C ATOM 1927 C LEU A 247 49.764 29.986 37.388 1.00 28.12 C ANISOU 1927 C LEU E 247 4599 4000 2084 -399 350 412 C ATOM 1928 O LEU A 247 49.036 29.934 36.392 1.00 27.40 O ANISOU 1928 O LEU E 247 4793 3795 1823 -571 446 390 O ATOM 1929 CB LEU A 247 48.606 30.238 39.551 1.00 26.12 C ANISOU 1929 CB LEU E 247 3883 3889 2151 -158 258 429 C ATOM 1930 CG LEU A 247 48.257 31.038 40.806 1.00 27.37 C ANISOU 1930 CG LEU E 247 4202 4010 2188 143 419 533 C ATOM 1931 CD1 LEU A 247 47.414 30.164 41.739 1.00 25.57 C ANISOU 1931 CD1 LEU E 247 2934 4540 2240 -178 83 230 C ATOM 1932 CD2 LEU A 247 49.530 31.524 41.468 1.00 24.81 C ANISOU 1932 CD2 LEU E 247 3837 3233 2357 45 816 662 C ATOM 1933 N LYS A 248 50.797 29.175 37.551 1.00 28.25 N ANISOU 1933 N LYS E 248 4041 4115 2577 -83 270 586 N ATOM 1934 CA LYS A 248 50.956 28.091 36.577 1.00 27.77 C ANISOU 1934 CA LYS E 248 3864 3955 2733 -359 -276 579 C ATOM 1935 C LYS A 248 49.914 27.004 36.832 1.00 27.06 C ANISOU 1935 C LYS E 248 3758 4145 2381 -282 -377 518 C ATOM 1936 O LYS A 248 49.514 26.781 37.979 1.00 27.94 O ANISOU 1936 O LYS E 248 3636 4469 2510 -630 -64 591 O ATOM 1937 CB LYS A 248 52.325 27.443 36.610 1.00 27.56 C ANISOU 1937 CB LYS E 248 3811 4018 2643 -336 130 12 C ATOM 1938 CG LYS A 248 53.486 28.346 36.201 1.00 30.94 C ANISOU 1938 CG LYS E 248 3946 4092 3718 324 -465 382 C ATOM 1939 CD LYS A 248 54.761 27.543 36.458 1.00 36.79 C ANISOU 1939 CD LYS E 248 3777 4469 5732 267 -268 248 C ATOM 1940 CE LYS A 248 56.003 28.389 36.210 1.00 41.56 C ANISOU 1940 CE LYS E 248 3895 5194 6701 316 1231 655 C ATOM 1941 NZ LYS A 248 56.917 27.654 35.275 1.00 64.44 N ANISOU 1941 NZ LYS E 248 7675 7829 8980 -1186 4287 57 N ATOM 1942 N VAL A 249 49.491 26.347 35.770 1.00 27.82 N ANISOU 1942 N VAL E 249 4064 3966 2541 -418 -418 653 N ATOM 1943 CA VAL A 249 48.554 25.231 35.860 1.00 29.14 C ANISOU 1943 CA VAL E 249 4339 3867 2865 -364 -622 687 C ATOM 1944 C VAL A 249 49.043 24.217 36.871 1.00 29.69 C ANISOU 1944 C VAL E 249 4243 4183 2856 -604 51 363 C ATOM 1945 O VAL A 249 48.288 23.665 37.675 1.00 29.65 O ANISOU 1945 O VAL E 249 4190 4321 2753 -180 -49 692 O ATOM 1946 CB VAL A 249 48.392 24.601 34.458 1.00 30.17 C ANISOU 1946 CB VAL E 249 4621 3819 3023 -532 -573 890 C ATOM 1947 CG1 VAL A 249 47.696 23.251 34.552 1.00 29.07 C ANISOU 1947 CG1 VAL E 249 5318 3551 2176 -649 -309 701 C ATOM 1948 CG2 VAL A 249 47.632 25.530 33.521 1.00 24.16 C ANISOU 1948 CG2 VAL E 249 3130 3405 2647 514 -231 679 C ATOM 1949 N LYS A 250 50.335 23.906 36.899 1.00 27.54 N ANISOU 1949 N LYS E 250 3970 4005 2488 39 -519 338 N ATOM 1950 CA LYS A 250 50.768 22.857 37.844 1.00 27.82 C ANISOU 1950 CA LYS E 250 4165 3806 2600 -394 167 308 C ATOM 1951 C LYS A 250 50.708 23.308 39.301 1.00 27.22 C ANISOU 1951 C LYS E 250 4222 3668 2452 -25 224 26 C ATOM 1952 O LYS A 250 50.577 22.493 40.241 1.00 28.24 O ANISOU 1952 O LYS E 250 3419 4438 2873 -240 412 -535 O ATOM 1953 CB LYS A 250 52.195 22.404 37.537 1.00 30.23 C ANISOU 1953 CB LYS E 250 4164 4250 3073 -540 123 477 C ATOM 1954 CG LYS A 250 53.210 23.546 37.691 1.00 31.70 C ANISOU 1954 CG LYS E 250 4092 4896 3057 -244 -261 487 C ATOM 1955 CD LYS A 250 54.604 22.932 37.538 1.00 35.06 C ANISOU 1955 CD LYS E 250 4216 5425 3681 -254 811 324 C ATOM 1956 CE LYS A 250 55.693 23.954 37.802 1.00 36.44 C ANISOU 1956 CE LYS E 250 4030 6135 3681 24 798 111 C ATOM 1957 NZ LYS A 250 57.033 23.340 37.581 1.00 41.29 N ANISOU 1957 NZ LYS E 250 4044 7263 4381 -820 -949 157 N ATOM 1958 N THR A 251 50.827 24.619 39.514 1.00 27.37 N ANISOU 1958 N THR E 251 3712 3797 2891 137 196 475 N ATOM 1959 CA THR A 251 50.734 25.148 40.869 1.00 31.40 C ANISOU 1959 CA THR E 251 4784 4275 2872 -274 472 537 C ATOM 1960 C THR A 251 49.316 24.971 41.391 1.00 29.52 C ANISOU 1960 C THR E 251 4861 3738 2619 -202 455 249 C ATOM 1961 O THR A 251 49.107 24.524 42.517 1.00 32.25 O ANISOU 1961 O THR E 251 5614 3891 2749 -72 548 83 O ATOM 1962 CB THR A 251 51.074 26.647 40.887 1.00 28.46 C ANISOU 1962 CB THR E 251 4228 4524 2061 80 99 797 C ATOM 1963 OG1 THR A 251 52.410 26.806 40.412 1.00 29.70 O ANISOU 1963 OG1 THR E 251 4389 4539 2356 -373 456 437 O ATOM 1964 CG2 THR A 251 51.005 27.194 42.315 1.00 31.07 C ANISOU 1964 CG2 THR E 251 5112 4743 1949 -1025 259 640 C ATOM 1965 N LEU A 252 48.353 25.339 40.539 1.00 29.85 N ANISOU 1965 N LEU E 252 4893 3879 2568 -589 377 794 N ATOM 1966 CA LEU A 252 46.945 25.217 40.924 1.00 34.76 C ANISOU 1966 CA LEU E 252 4921 5004 3281 -1060 667 206 C ATOM 1967 C LEU A 252 46.598 23.750 41.120 1.00 33.21 C ANISOU 1967 C LEU E 252 3835 5125 3657 -622 356 619 C ATOM 1968 O LEU A 252 45.909 23.346 42.065 1.00 35.21 O ANISOU 1968 O LEU E 252 4810 5168 3402 -383 402 545 O ATOM 1969 CB LEU A 252 46.071 25.937 39.890 1.00 36.74 C ANISOU 1969 CB LEU E 252 5077 5825 3058 -1259 574 306 C ATOM 1970 CG LEU A 252 44.587 26.095 40.222 1.00 39.19 C ANISOU 1970 CG LEU E 252 5216 5905 3768 -1667 697 -49 C ATOM 1971 CD1 LEU A 252 44.390 26.867 41.536 1.00 34.52 C ANISOU 1971 CD1 LEU E 252 4461 5526 3128 -1047 903 -630 C ATOM 1972 CD2 LEU A 252 43.822 26.724 39.056 1.00 35.04 C ANISOU 1972 CD2 LEU E 252 4735 5034 3545 -297 241 214 C ATOM 1973 N ARG A 253 47.085 22.864 40.256 1.00 36.36 N ANISOU 1973 N ARG E 253 5121 5135 3561 -1103 453 433 N ATOM 1974 CA ARG A 253 46.864 21.421 40.363 1.00 38.59 C ANISOU 1974 CA ARG E 253 6027 5184 3451 -732 264 695 C ATOM 1975 C ARG A 253 47.466 20.825 41.634 1.00 38.93 C ANISOU 1975 C ARG E 253 6532 4733 3528 -872 285 679 C ATOM 1976 O ARG A 253 46.874 19.959 42.293 1.00 43.82 O ANISOU 1976 O ARG E 253 8345 4533 3773 -354 382 699 O ATOM 1977 CB ARG A 253 47.421 20.725 39.093 1.00 39.74 C ANISOU 1977 CB ARG E 253 6022 5503 3574 -39 425 1090 C ATOM 1978 CG ARG A 253 47.282 19.219 39.176 1.00 54.89 C ANISOU 1978 CG ARG E 253 9916 5416 5523 -414 1567 1488 C ATOM 1979 CD ARG A 253 48.063 18.467 38.112 1.00 78.02 C ANISOU 1979 CD ARG E 253 15665 7538 6442 -2471 1999 2875 C ATOM 1980 NE ARG A 253 47.125 17.781 37.211 1.00 91.76 N ANISOU 1980 NE ARG E 253 18216 8596 8054 -2693 518 4537 N ATOM 1981 CZ ARG A 253 46.911 16.482 37.120 1.00 97.65 C ANISOU 1981 CZ ARG E 253 19916 8465 8723 -3233 -1149 4968 C ATOM 1982 NH1 ARG A 253 47.577 15.606 37.861 1.00111.61 N ANISOU 1982 NH1 ARG E 253 22556 9699 10151 -3763 -1219 3091 N ATOM 1983 NH2 ARG A 253 46.008 16.038 36.243 1.00109.51 N ANISOU 1983 NH2 ARG E 253 21238 10420 9950 -2615 -1744 6339 N ATOM 1984 N TYR A 254 48.664 21.270 42.019 1.00 37.12 N ANISOU 1984 N TYR E 254 6131 4846 3126 -1609 379 1414 N ATOM 1985 CA TYR A 254 49.328 20.836 43.241 1.00 35.87 C ANISOU 1985 CA TYR E 254 5615 4834 3181 -1309 945 472 C ATOM 1986 C TYR A 254 48.509 21.119 44.501 1.00 37.91 C ANISOU 1986 C TYR E 254 6403 4597 3404 -1551 1324 326 C ATOM 1987 O TYR A 254 48.306 20.271 45.394 1.00 40.95 O ANISOU 1987 O TYR E 254 6914 4843 3804 -1788 1812 35 O ATOM 1988 CB TYR A 254 50.693 21.529 43.361 1.00 36.39 C ANISOU 1988 CB TYR E 254 5681 4772 3376 -1304 537 241 C ATOM 1989 CG TYR A 254 51.369 21.303 44.706 1.00 38.96 C ANISOU 1989 CG TYR E 254 6344 4956 3504 -1260 251 145 C ATOM 1990 CD1 TYR A 254 51.923 20.061 45.022 1.00 39.58 C ANISOU 1990 CD1 TYR E 254 6319 5114 3605 -1409 243 101 C ATOM 1991 CD2 TYR A 254 51.466 22.317 45.661 1.00 38.99 C ANISOU 1991 CD2 TYR E 254 6008 5015 3791 -1020 -21 264 C ATOM 1992 CE1 TYR A 254 52.547 19.833 46.240 1.00 39.41 C ANISOU 1992 CE1 TYR E 254 5976 4999 3999 -1329 -150 339 C ATOM 1993 CE2 TYR A 254 52.086 22.103 46.881 1.00 38.40 C ANISOU 1993 CE2 TYR E 254 5911 4858 3822 -1107 9 202 C ATOM 1994 CZ TYR A 254 52.624 20.861 47.164 1.00 40.32 C ANISOU 1994 CZ TYR E 254 6003 4892 4425 -1207 -391 446 C ATOM 1995 OH TYR A 254 53.245 20.620 48.364 1.00 45.13 O ANISOU 1995 OH TYR E 254 8431 4773 3942 -2493 -374 763 O ATOM 1996 N PHE A 255 48.027 22.372 44.596 1.00 35.08 N ANISOU 1996 N PHE E 255 5750 4409 3169 -1228 493 761 N ATOM 1997 CA PHE A 255 47.276 22.733 45.795 1.00 35.31 C ANISOU 1997 CA PHE E 255 6118 3955 3345 -899 881 713 C ATOM 1998 C PHE A 255 45.880 22.128 45.751 1.00 37.20 C ANISOU 1998 C PHE E 255 6690 3719 3723 -226 1206 146 C ATOM 1999 O PHE A 255 45.303 21.825 46.800 1.00 43.90 O ANISOU 1999 O PHE E 255 7467 5107 4107 -410 1880 93 O ATOM 2000 CB PHE A 255 47.178 24.256 45.940 1.00 30.76 C ANISOU 2000 CB PHE E 255 5648 3871 2168 -513 606 429 C ATOM 2001 CG PHE A 255 48.514 24.856 46.352 1.00 32.15 C ANISOU 2001 CG PHE E 255 5329 4350 2537 -747 575 341 C ATOM 2002 CD1 PHE A 255 48.960 24.705 47.658 1.00 32.72 C ANISOU 2002 CD1 PHE E 255 5091 4551 2790 -971 383 146 C ATOM 2003 CD2 PHE A 255 49.307 25.556 45.462 1.00 33.72 C ANISOU 2003 CD2 PHE E 255 5637 4575 2600 -310 721 593 C ATOM 2004 CE1 PHE A 255 50.180 25.240 48.066 1.00 33.26 C ANISOU 2004 CE1 PHE E 255 5722 4267 2648 -363 397 298 C ATOM 2005 CE2 PHE A 255 50.519 26.092 45.857 1.00 33.15 C ANISOU 2005 CE2 PHE E 255 5674 4244 2679 -442 398 229 C ATOM 2006 CZ PHE A 255 50.965 25.951 47.163 1.00 33.28 C ANISOU 2006 CZ PHE E 255 5897 4050 2699 -507 396 102 C ATOM 2007 N ASN A 256 45.333 21.963 44.549 1.00 37.09 N ANISOU 2007 N ASN E 256 6241 3836 4015 42 1174 699 N ATOM 2008 CA ASN A 256 44.015 21.357 44.424 1.00 42.58 C ANISOU 2008 CA ASN E 256 6272 5204 4702 471 1442 342 C ATOM 2009 C ASN A 256 44.084 19.903 44.875 1.00 43.82 C ANISOU 2009 C ASN E 256 5694 5102 5854 798 1520 286 C ATOM 2010 O ASN A 256 43.076 19.432 45.407 1.00 49.55 O ANISOU 2010 O ASN E 256 5990 5059 7777 1151 2251 909 O ATOM 2011 CB ASN A 256 43.441 21.413 43.009 1.00 45.84 C ANISOU 2011 CB ASN E 256 7020 5227 5172 1072 563 854 C ATOM 2012 CG ASN A 256 42.486 22.586 42.865 1.00 51.15 C ANISOU 2012 CG ASN E 256 7453 6339 5643 319 -365 978 C ATOM 2013 OD1 ASN A 256 41.373 22.619 43.408 1.00 63.15 O ANISOU 2013 OD1 ASN E 256 7543 8146 8305 -609 370 -352 O ATOM 2014 ND2 ASN A 256 42.938 23.593 42.137 1.00 59.01 N ANISOU 2014 ND2 ASN E 256 10319 7443 4660 -2024 1467 -407 N ATOM 2015 N GLU A 257 45.232 19.251 44.674 1.00 43.26 N ANISOU 2015 N GLU E 257 6315 5509 4613 250 2117 -95 N ATOM 2016 CA GLU A 257 45.317 17.869 45.157 1.00 46.91 C ANISOU 2016 CA GLU E 257 6788 5798 5238 -98 2812 -601 C ATOM 2017 C GLU A 257 45.645 17.825 46.641 1.00 49.57 C ANISOU 2017 C GLU E 257 8194 5336 5303 -921 2507 -405 C ATOM 2018 O GLU A 257 45.079 17.070 47.445 1.00 49.09 O ANISOU 2018 O GLU E 257 8394 5604 4654 -481 2513 81 O ATOM 2019 CB GLU A 257 46.324 17.113 44.274 1.00 57.48 C ANISOU 2019 CB GLU E 257 9569 6628 5642 -1616 3645 -717 C ATOM 2020 CG GLU A 257 45.874 17.137 42.804 1.00 69.57 C ANISOU 2020 CG GLU E 257 11906 8594 5933 -2785 2731 806 C ATOM 2021 CD GLU A 257 46.802 16.391 41.873 1.00 79.02 C ANISOU 2021 CD GLU E 257 13844 9722 6456 -4129 2561 1566 C ATOM 2022 OE1 GLU A 257 47.941 16.101 42.312 1.00 96.05 O ANISOU 2022 OE1 GLU E 257 16292 11402 8801 -8311 1429 2019 O ATOM 2023 OE2 GLU A 257 46.428 16.074 40.714 1.00 89.60 O ANISOU 2023 OE2 GLU E 257 17551 9594 6899 -4298 1870 2295 O ATOM 2024 N LEU A 258 46.582 18.649 47.098 1.00 47.38 N ANISOU 2024 N LEU E 258 8517 4891 4593 -940 2611 -410 N ATOM 2025 CA LEU A 258 46.952 18.661 48.499 1.00 50.87 C ANISOU 2025 CA LEU E 258 9305 5186 4839 -1285 2010 -881 C ATOM 2026 C LEU A 258 45.812 19.041 49.434 1.00 50.46 C ANISOU 2026 C LEU E 258 9888 5220 4064 -1167 1960 -398 C ATOM 2027 O LEU A 258 45.804 18.711 50.624 1.00 56.43 O ANISOU 2027 O LEU E 258 11745 5327 4367 -475 2277 -1063 O ATOM 2028 CB LEU A 258 48.118 19.652 48.643 1.00 51.82 C ANISOU 2028 CB LEU E 258 9073 5350 5265 -1419 867 -1596 C ATOM 2029 CG LEU A 258 48.692 19.815 50.053 1.00 55.99 C ANISOU 2029 CG LEU E 258 10130 5524 5618 -1907 118 -1687 C ATOM 2030 CD1 LEU A 258 49.380 18.525 50.471 1.00 64.99 C ANISOU 2030 CD1 LEU E 258 12598 5423 6671 -2252 -809 -1670 C ATOM 2031 CD2 LEU A 258 49.668 20.980 50.137 1.00 50.86 C ANISOU 2031 CD2 LEU E 258 8474 5253 5598 -2781 244 -1079 C ATOM 2032 N GLU A 259 44.793 19.768 48.972 1.00 46.86 N ANISOU 2032 N GLU E 259 8842 4555 4407 -487 1357 1040 N ATOM 2033 CA GLU A 259 43.819 20.303 49.931 1.00 45.60 C ANISOU 2033 CA GLU E 259 8904 4446 3977 14 1545 864 C ATOM 2034 C GLU A 259 42.446 19.728 49.633 1.00 49.17 C ANISOU 2034 C GLU E 259 8743 5471 4468 -133 1080 653 C ATOM 2035 O GLU A 259 41.422 20.143 50.181 1.00 48.07 O ANISOU 2035 O GLU E 259 8710 5793 3760 -122 724 1091 O ATOM 2036 CB GLU A 259 43.861 21.840 49.860 1.00 46.80 C ANISOU 2036 CB GLU E 259 8304 4519 4958 -451 4472 -385 C ATOM 2037 CG GLU A 259 43.691 22.490 51.241 1.00 57.76 C ANISOU 2037 CG GLU E 259 11515 4176 6255 -917 2905 1180 C ATOM 2038 CD GLU A 259 45.016 22.721 51.934 1.00 55.12 C ANISOU 2038 CD GLU E 259 11185 3572 6186 -78 3406 341 C ATOM 2039 OE1 GLU A 259 45.211 22.212 53.035 1.00 65.96 O ANISOU 2039 OE1 GLU E 259 14529 6178 4355 450 2391 1987 O ATOM 2040 OE2 GLU A 259 45.927 23.363 51.384 1.00 69.79 O ANISOU 2040 OE2 GLU E 259 9600 4789 12129 -2508 6009 -1473 O ATOM 2041 N ALA A 260 42.431 18.744 48.715 1.00 44.52 N ANISOU 2041 N ALA E 260 7647 4863 4406 659 1995 297 N ATOM 2042 CA ALA A 260 41.167 18.182 48.255 1.00 46.86 C ANISOU 2042 CA ALA E 260 7440 5203 5160 694 2246 501 C ATOM 2043 C ALA A 260 40.232 17.748 49.378 1.00 49.08 C ANISOU 2043 C ALA E 260 7882 5158 5608 701 2566 260 C ATOM 2044 O ALA A 260 39.027 17.988 49.343 1.00 49.48 O ANISOU 2044 O ALA E 260 7474 4853 6474 1891 2292 -515 O ATOM 2045 CB ALA A 260 41.418 16.981 47.344 1.00 45.90 C ANISOU 2045 CB ALA E 260 7330 5013 5096 694 1846 434 C ATOM 2046 N GLU A 261 40.783 17.092 50.386 1.00 49.76 N ANISOU 2046 N GLU E 261 8015 5128 5762 1212 2289 43 N ATOM 2047 CA GLU A 261 39.940 16.521 51.439 1.00 58.83 C ANISOU 2047 CA GLU E 261 10236 5801 6317 766 3757 -241 C ATOM 2048 C GLU A 261 39.316 17.634 52.275 1.00 57.24 C ANISOU 2048 C GLU E 261 9715 5717 6317 1168 3269 162 C ATOM 2049 O GLU A 261 38.273 17.481 52.910 1.00 52.72 O ANISOU 2049 O GLU E 261 9668 4880 5484 1062 2959 9 O ATOM 2050 CB GLU A 261 40.754 15.583 52.324 1.00 65.59 C ANISOU 2050 CB GLU E 261 11761 5403 7757 725 3823 -1336 C ATOM 2051 CG GLU A 261 40.542 14.097 52.165 1.00 78.63 C ANISOU 2051 CG GLU E 261 14955 5645 9274 230 1777 93 C ATOM 2052 CD GLU A 261 39.408 13.613 51.281 1.00 90.73 C ANISOU 2052 CD GLU E 261 17714 6934 9826 -99 89 1602 C ATOM 2053 OE1 GLU A 261 38.277 13.366 51.771 1.00 93.00 O ANISOU 2053 OE1 GLU E 261 17444 7105 10786 2597 -995 2857 O ATOM 2054 OE2 GLU A 261 39.636 13.449 50.055 1.00105.06 O ANISOU 2054 OE2 GLU E 261 22097 7991 9831 -725 257 1875 O ATOM 2055 N ASN A 262 40.025 18.762 52.237 1.00 55.39 N ANISOU 2055 N ASN E 262 8542 6013 6493 1073 2350 -29 N ATOM 2056 CA ASN A 262 39.685 19.905 53.068 1.00 49.60 C ANISOU 2056 CA ASN E 262 7153 5570 6124 1345 2237 -416 C ATOM 2057 C ASN A 262 38.736 20.867 52.385 1.00 51.02 C ANISOU 2057 C ASN E 262 6661 6390 6334 1264 2201 -590 C ATOM 2058 O ASN A 262 38.352 21.873 52.986 1.00 50.52 O ANISOU 2058 O ASN E 262 5771 7727 5697 206 2684 -634 O ATOM 2059 CB ASN A 262 40.958 20.689 53.446 1.00 44.56 C ANISOU 2059 CB ASN E 262 6658 5448 4826 1299 2615 -1416 C ATOM 2060 CG ASN A 262 41.966 19.810 54.157 1.00 50.37 C ANISOU 2060 CG ASN E 262 7736 5882 5522 772 1870 -1257 C ATOM 2061 OD1 ASN A 262 41.599 19.090 55.084 1.00 60.86 O ANISOU 2061 OD1 ASN E 262 7865 6632 8626 255 2311 -3505 O ATOM 2062 ND2 ASN A 262 43.225 19.837 53.757 1.00 53.11 N ANISOU 2062 ND2 ASN E 262 7280 5719 7181 968 1356 -2464 N ATOM 2063 N ILE A 263 38.360 20.619 51.130 1.00 54.88 N ANISOU 2063 N ILE E 263 7854 6657 6339 921 1957 -511 N ATOM 2064 CA ILE A 263 37.499 21.678 50.576 1.00 58.84 C ANISOU 2064 CA ILE E 263 9072 7101 6182 199 1693 -315 C ATOM 2065 C ILE A 263 36.131 21.106 50.265 1.00 61.53 C ANISOU 2065 C ILE E 263 8805 8054 6522 -134 1228 -518 C ATOM 2066 O ILE A 263 35.340 21.639 49.494 1.00 73.30 O ANISOU 2066 O ILE E 263 11969 8937 6945 -1392 -1345 1505 O ATOM 2067 CB ILE A 263 38.145 22.303 49.345 1.00 60.11 C ANISOU 2067 CB ILE E 263 9075 7875 5889 -323 1516 -647 C ATOM 2068 CG1 ILE A 263 38.466 21.279 48.256 1.00 60.97 C ANISOU 2068 CG1 ILE E 263 8141 8593 6432 -189 1709 -123 C ATOM 2069 CG2 ILE A 263 39.418 23.047 49.702 1.00 53.81 C ANISOU 2069 CG2 ILE E 263 7700 7705 5041 -1213 2539 -212 C ATOM 2070 CD1 ILE A 263 39.926 21.421 47.854 1.00 73.31 C ANISOU 2070 CD1 ILE E 263 6995 13184 7674 -2081 804 -698 C ATOM 2071 N LYS A 264 35.839 19.976 50.900 1.00 68.81 N ANISOU 2071 N LYS E 264 9647 7885 8611 823 2206 -294 N ATOM 2072 CA LYS A 264 34.493 19.410 50.787 1.00 76.55 C ANISOU 2072 CA LYS E 264 9629 8575 10881 860 1904 544 C ATOM 2073 C LYS A 264 33.569 19.942 51.878 1.00 77.52 C ANISOU 2073 C LYS E 264 8825 8920 11709 1188 1942 1056 C ATOM 2074 O LYS A 264 33.938 20.190 53.024 1.00 75.36 O ANISOU 2074 O LYS E 264 8680 8512 11443 798 2272 1025 O ATOM 2075 CB LYS A 264 34.572 17.880 50.827 1.00 76.51 C ANISOU 2075 CB LYS E 264 8786 8559 11725 1096 2521 342 C ATOM 2076 CG LYS A 264 35.818 17.295 50.176 1.00 80.69 C ANISOU 2076 CG LYS E 264 9279 9173 12207 413 2836 -39 C ATOM 2077 CD LYS A 264 35.942 15.807 50.476 1.00 78.42 C ANISOU 2077 CD LYS E 264 8394 9101 12301 798 3041 -22 C ATOM 2078 CE LYS A 264 36.381 15.052 49.230 1.00 78.43 C ANISOU 2078 CE LYS E 264 8762 8938 12101 682 3169 -309 C ATOM 2079 NZ LYS A 264 37.196 15.915 48.330 1.00 84.34 N ANISOU 2079 NZ LYS E 264 9861 10332 11853 -92 2924 -2156 N ATOM 2080 N GLY A 265 32.300 20.135 51.522 1.00 83.82 N ANISOU 2080 N GLY E 265 9209 9687 12953 641 1313 1474 N ATOM 2081 CA GLY A 265 31.318 20.599 52.493 1.00 83.43 C ANISOU 2081 CA GLY E 265 8380 9797 13523 1086 1098 2205 C ATOM 2082 C GLY A 265 31.385 22.114 52.620 1.00 87.07 C ANISOU 2082 C GLY E 265 9740 9860 13482 955 155 2653 C ATOM 2083 O GLY A 265 30.375 22.797 52.439 1.00 86.51 O ANISOU 2083 O GLY E 265 9490 9550 13831 1140 650 2459 O ATOM 2084 N LEU A 266 32.593 22.576 52.923 1.00 87.12 N ANISOU 2084 N LEU E 266 10153 9542 13408 970 -584 2410 N ATOM 2085 CA LEU A 266 32.903 23.993 53.072 1.00 89.29 C ANISOU 2085 CA LEU E 266 11062 9587 13277 985 -987 2797 C ATOM 2086 C LEU A 266 32.465 24.533 54.427 1.00 94.29 C ANISOU 2086 C LEU E 266 12132 10436 13258 560 -957 2916 C ATOM 2087 O LEU A 266 31.334 24.461 54.901 1.00101.99 O ANISOU 2087 O LEU E 266 13306 11900 13546 462 432 1647 O ATOM 2088 CB LEU A 266 32.272 24.784 51.923 1.00 91.54 C ANISOU 2088 CB LEU E 266 12387 9172 13221 91 -931 3141 C ATOM 2089 CG LEU A 266 32.969 24.701 50.566 1.00 90.13 C ANISOU 2089 CG LEU E 266 12137 8943 13166 180 -1012 3032 C ATOM 2090 CD1 LEU A 266 34.473 24.707 50.748 1.00 80.49 C ANISOU 2090 CD1 LEU E 266 12358 8433 9792 236 -1914 3047 C ATOM 2091 CD2 LEU A 266 32.533 23.464 49.794 1.00 86.96 C ANISOU 2091 CD2 LEU E 266 10986 9425 12628 351 -1463 2828 C ATOM 2092 OXT LEU A 266 33.989 24.863 54.270 1.00 99.16 O ANISOU 2092 OXT LEU E 266 11642 11558 14475 367 -2546 3302 O TER 2093 LEU E 266 ATOM 1 N MET A 1 60.779 50.225 53.899 1.00 38.92 N ANISOU 1 N MET F 1 5098 6097 3592 -1489 447 362 N ATOM 2 CA MET A 1 62.051 50.797 53.476 1.00 39.64 C ANISOU 2 CA MET F 1 4671 6407 3983 -879 140 -405 C ATOM 3 C MET A 1 61.759 52.150 52.843 1.00 37.92 C ANISOU 3 C MET F 1 4914 5679 3813 -933 633 -168 C ATOM 4 O MET A 1 60.746 52.269 52.128 1.00 46.58 O ANISOU 4 O MET F 1 5309 7754 4636 -2033 -63 1256 O ATOM 5 CB MET A 1 62.787 49.912 52.463 1.00 40.12 C ANISOU 5 CB MET F 1 4934 6308 4004 -354 -109 -293 C ATOM 6 CG MET A 1 63.992 50.644 51.877 1.00 43.45 C ANISOU 6 CG MET F 1 5363 6642 4505 -613 -169 -839 C ATOM 7 SD MET A 1 64.844 49.696 50.575 1.00 40.76 S ANISOU 7 SD MET F 1 5716 5321 4449 -844 351 -81 S ATOM 8 CE MET A 1 65.566 48.443 51.688 1.00 40.89 C ANISOU 8 CE MET F 1 5132 5850 4556 -1337 -1383 -497 C ATOM 9 N ARG A 2 62.604 53.136 53.094 1.00 32.45 N ANISOU 9 N ARG F 2 4810 4307 3211 -795 419 -513 N ATOM 10 CA ARG A 2 62.410 54.425 52.429 1.00 31.91 C ANISOU 10 CA ARG F 2 5037 4272 2817 -1111 367 -36 C ATOM 11 C ARG A 2 63.494 54.563 51.367 1.00 31.66 C ANISOU 11 C ARG F 2 4806 4445 2778 -1169 640 -178 C ATOM 12 O ARG A 2 64.607 54.075 51.537 1.00 35.19 O ANISOU 12 O ARG F 2 5848 4297 3224 -928 50 -345 O ATOM 13 CB ARG A 2 62.438 55.572 53.431 1.00 30.78 C ANISOU 13 CB ARG F 2 5683 3264 2747 -322 224 278 C ATOM 14 CG ARG A 2 61.387 55.506 54.533 1.00 31.74 C ANISOU 14 CG ARG F 2 6052 3464 2546 -297 -63 449 C ATOM 15 CD ARG A 2 61.618 56.599 55.575 1.00 34.98 C ANISOU 15 CD ARG F 2 6719 3922 2652 -266 253 153 C ATOM 16 NE ARG A 2 61.416 57.921 54.972 1.00 34.41 N ANISOU 16 NE ARG F 2 6379 4594 2103 -53 429 -191 N ATOM 17 CZ ARG A 2 61.782 59.068 55.509 1.00 36.03 C ANISOU 17 CZ ARG F 2 5807 4903 2981 -919 503 344 C ATOM 18 NH1 ARG A 2 62.377 59.045 56.683 1.00 40.91 N ANISOU 18 NH1 ARG F 2 6260 5762 3522 -1418 799 915 N ATOM 19 NH2 ARG A 2 61.572 60.235 54.914 1.00 34.88 N ANISOU 19 NH2 ARG F 2 5784 4351 3119 -751 335 -382 N ATOM 20 N LEU A 3 63.154 55.208 50.259 1.00 31.74 N ANISOU 20 N LEU F 3 4926 4478 2657 -969 591 -365 N ATOM 21 CA LEU A 3 64.140 55.590 49.260 1.00 30.10 C ANISOU 21 CA LEU F 3 4287 4342 2806 -471 790 -760 C ATOM 22 C LEU A 3 64.058 57.118 49.137 1.00 29.83 C ANISOU 22 C LEU F 3 4583 3777 2975 -455 909 -446 C ATOM 23 O LEU A 3 62.962 57.593 48.837 1.00 32.73 O ANISOU 23 O LEU F 3 5431 3887 3119 -772 569 -246 O ATOM 24 CB LEU A 3 63.920 54.920 47.908 1.00 28.39 C ANISOU 24 CB LEU F 3 3943 4351 2491 -526 530 -177 C ATOM 25 CG LEU A 3 64.828 55.333 46.741 1.00 30.84 C ANISOU 25 CG LEU F 3 4457 4660 2600 -868 475 -330 C ATOM 26 CD1 LEU A 3 66.272 54.985 47.023 1.00 32.59 C ANISOU 26 CD1 LEU F 3 4263 4270 3850 -374 15 -436 C ATOM 27 CD2 LEU A 3 64.414 54.648 45.449 1.00 31.39 C ANISOU 27 CD2 LEU F 3 3956 5259 2710 -90 417 -825 C ATOM 28 N ILE A 4 65.163 57.804 49.391 1.00 29.63 N ANISOU 28 N ILE F 4 4344 3841 3072 -259 982 -342 N ATOM 29 CA ILE A 4 65.191 59.258 49.260 1.00 29.55 C ANISOU 29 CA ILE F 4 4606 3487 3133 -143 936 162 C ATOM 30 C ILE A 4 65.928 59.592 47.972 1.00 30.18 C ANISOU 30 C ILE F 4 4166 4260 3043 -442 1143 178 C ATOM 31 O ILE A 4 67.170 59.525 47.902 1.00 32.25 O ANISOU 31 O ILE F 4 4551 4378 3323 -649 453 454 O ATOM 32 CB ILE A 4 65.880 59.949 50.444 1.00 27.05 C ANISOU 32 CB ILE F 4 3924 3415 2937 -176 550 63 C ATOM 33 CG1 ILE A 4 65.514 59.397 51.823 1.00 29.47 C ANISOU 33 CG1 ILE F 4 4697 3441 3059 -175 216 596 C ATOM 34 CG2 ILE A 4 65.650 61.466 50.382 1.00 27.89 C ANISOU 34 CG2 ILE F 4 4136 3481 2980 -8 132 -560 C ATOM 35 CD1 ILE A 4 64.039 59.371 52.149 1.00 33.52 C ANISOU 35 CD1 ILE F 4 5050 4991 2694 -1287 715 -196 C ATOM 36 N PRO A 5 65.208 59.900 46.906 1.00 32.38 N ANISOU 36 N PRO F 5 4856 4317 3131 -679 830 285 N ATOM 37 CA PRO A 5 65.859 60.128 45.610 1.00 30.96 C ANISOU 37 CA PRO F 5 4547 3924 3290 -305 590 340 C ATOM 38 C PRO A 5 66.255 61.595 45.485 1.00 32.73 C ANISOU 38 C PRO F 5 4676 3912 3847 7 682 -203 C ATOM 39 O PRO A 5 65.383 62.462 45.333 1.00 41.35 O ANISOU 39 O PRO F 5 5900 4187 5623 717 832 -29 O ATOM 40 CB PRO A 5 64.777 59.765 44.601 1.00 31.19 C ANISOU 40 CB PRO F 5 4759 4059 3031 -415 332 559 C ATOM 41 CG PRO A 5 63.553 59.448 45.388 1.00 36.93 C ANISOU 41 CG PRO F 5 6032 5134 2865 -1639 480 549 C ATOM 42 CD PRO A 5 63.755 60.039 46.761 1.00 33.62 C ANISOU 42 CD PRO F 5 5289 4328 3157 -800 506 366 C ATOM 43 N LEU A 6 67.558 61.835 45.563 1.00 33.33 N ANISOU 43 N LEU F 6 4570 4819 3274 -481 776 -193 N ATOM 44 CA LEU A 6 68.072 63.180 45.389 1.00 33.33 C ANISOU 44 CA LEU F 6 4731 4654 3278 -246 525 613 C ATOM 45 C LEU A 6 68.913 63.279 44.126 1.00 31.09 C ANISOU 45 C LEU F 6 4147 4368 3297 279 673 476 C ATOM 46 O LEU A 6 69.201 62.342 43.402 1.00 32.27 O ANISOU 46 O LEU F 6 4119 4542 3601 99 1150 523 O ATOM 47 CB LEU A 6 68.871 63.583 46.651 1.00 30.93 C ANISOU 47 CB LEU F 6 3860 4785 3106 349 44 1093 C ATOM 48 CG LEU A 6 68.000 63.592 47.917 1.00 32.11 C ANISOU 48 CG LEU F 6 4765 4312 3124 71 328 1115 C ATOM 49 CD1 LEU A 6 68.854 63.596 49.177 1.00 35.25 C ANISOU 49 CD1 LEU F 6 5001 5247 3147 -439 1216 761 C ATOM 50 CD2 LEU A 6 67.018 64.760 47.911 1.00 35.77 C ANISOU 50 CD2 LEU F 6 4293 4843 4453 743 779 713 C ATOM 51 N THR A 7 69.361 64.508 43.828 1.00 31.68 N ANISOU 51 N THR F 7 4224 4112 3701 321 509 420 N ATOM 52 CA THR A 7 70.122 64.733 42.609 1.00 33.08 C ANISOU 52 CA THR F 7 4689 4514 3367 118 295 845 C ATOM 53 C THR A 7 71.618 64.584 42.806 1.00 31.24 C ANISOU 53 C THR F 7 3910 4252 3706 464 192 409 C ATOM 54 O THR A 7 72.201 63.774 42.081 1.00 35.37 O ANISOU 54 O THR F 7 6266 4839 2335 243 238 189 O ATOM 55 CB THR A 7 69.823 66.139 42.055 1.00 35.77 C ANISOU 55 CB THR F 7 5099 4124 4366 201 -284 440 C ATOM 56 OG1 THR A 7 68.401 66.291 41.999 1.00 47.75 O ANISOU 56 OG1 THR F 7 8771 4110 5264 -541 -867 1016 O ATOM 57 CG2 THR A 7 70.353 66.271 40.634 1.00 37.28 C ANISOU 57 CG2 THR F 7 4307 5762 4097 -525 -261 1003 C ATOM 58 N THR A 8 72.216 65.330 43.735 1.00 30.84 N ANISOU 58 N THR F 8 4104 4019 3596 438 215 699 N ATOM 59 CA THR A 8 73.664 65.372 43.872 1.00 31.16 C ANISOU 59 CA THR F 8 4406 3978 3457 355 94 571 C ATOM 60 C THR A 8 74.112 64.772 45.212 1.00 30.18 C ANISOU 60 C THR F 8 4125 4102 3240 241 452 507 C ATOM 61 O THR A 8 73.348 64.615 46.155 1.00 31.39 O ANISOU 61 O THR F 8 4238 4017 3672 414 -241 687 O ATOM 62 CB THR A 8 74.202 66.808 43.802 1.00 35.03 C ANISOU 62 CB THR F 8 4296 4909 4104 3 -51 1001 C ATOM 63 OG1 THR A 8 73.717 67.477 44.990 1.00 34.44 O ANISOU 63 OG1 THR F 8 4112 4849 4124 424 677 1479 O ATOM 64 CG2 THR A 8 73.665 67.599 42.617 1.00 37.97 C ANISOU 64 CG2 THR F 8 4096 6196 4135 368 -39 1312 C ATOM 65 N ALA A 9 75.404 64.436 45.245 1.00 32.06 N ANISOU 65 N ALA F 9 4160 4378 3641 -281 174 869 N ATOM 66 CA ALA A 9 76.049 63.999 46.471 1.00 31.04 C ANISOU 66 CA ALA F 9 4421 4042 3330 54 124 490 C ATOM 67 C ALA A 9 75.892 65.041 47.574 1.00 32.92 C ANISOU 67 C ALA F 9 3707 5331 3470 167 -40 180 C ATOM 68 O ALA A 9 75.707 64.703 48.748 1.00 32.03 O ANISOU 68 O ALA F 9 3626 5124 3421 -138 -7 107 O ATOM 69 CB ALA A 9 77.519 63.717 46.207 1.00 30.59 C ANISOU 69 CB ALA F 9 3188 4023 4410 94 -250 811 C ATOM 70 N GLU A 10 75.972 66.334 47.229 1.00 33.85 N ANISOU 70 N GLU F 10 3775 5271 3814 125 16 681 N ATOM 71 CA GLU A 10 75.883 67.324 48.302 1.00 39.43 C ANISOU 71 CA GLU F 10 3560 5969 5451 -195 889 8 C ATOM 72 C GLU A 10 74.488 67.265 48.914 1.00 37.01 C ANISOU 72 C GLU F 10 4141 5260 4661 -46 1227 292 C ATOM 73 O GLU A 10 74.386 67.368 50.136 1.00 32.98 O ANISOU 73 O GLU F 10 3149 4745 4635 151 1622 525 O ATOM 74 CB GLU A 10 76.146 68.753 47.871 1.00 42.67 C ANISOU 74 CB GLU F 10 4032 6783 5397 396 705 329 C ATOM 75 CG GLU A 10 76.340 69.037 46.412 1.00 55.83 C ANISOU 75 CG GLU F 10 6703 8353 6159 -877 -1108 26 C ATOM 76 CD GLU A 10 77.561 68.428 45.757 1.00 68.33 C ANISOU 76 CD GLU F 10 9689 9367 6907 -3509 778 -1069 C ATOM 77 OE1 GLU A 10 77.355 67.717 44.748 1.00 57.50 O ANISOU 77 OE1 GLU F 10 7455 8986 5406 -2363 -1163 -518 O ATOM 78 OE2 GLU A 10 78.694 68.669 46.241 1.00 89.46 O ANISOU 78 OE2 GLU F 10 12970 11278 9744 -5873 3114 -2031 O ATOM 79 N GLN A 11 73.469 67.105 48.077 1.00 33.27 N ANISOU 79 N GLN F 11 4292 4510 3841 620 787 482 N ATOM 80 CA GLN A 11 72.146 66.966 48.658 1.00 33.41 C ANISOU 80 CA GLN F 11 4958 4221 3514 370 560 1011 C ATOM 81 C GLN A 11 72.045 65.682 49.479 1.00 32.06 C ANISOU 81 C GLN F 11 5269 3696 3218 185 402 974 C ATOM 82 O GLN A 11 71.401 65.635 50.533 1.00 32.12 O ANISOU 82 O GLN F 11 4172 4714 3319 -288 990 514 O ATOM 83 CB GLN A 11 71.051 66.888 47.596 1.00 34.19 C ANISOU 83 CB GLN F 11 5234 4412 3344 568 454 1209 C ATOM 84 CG GLN A 11 70.699 68.168 46.864 1.00 37.54 C ANISOU 84 CG GLN F 11 5259 4933 4070 883 549 1570 C ATOM 85 CD GLN A 11 69.748 67.854 45.718 1.00 38.16 C ANISOU 85 CD GLN F 11 6373 4487 3639 963 681 1402 C ATOM 86 OE1 GLN A 11 70.090 67.057 44.850 1.00 42.48 O ANISOU 86 OE1 GLN F 11 6455 5597 4087 -229 922 138 O ATOM 87 NE2 GLN A 11 68.568 68.433 45.698 1.00 52.12 N ANISOU 87 NE2 GLN F 11 9658 4581 5564 324 2102 1353 N ATOM 88 N VAL A 12 72.643 64.598 48.997 1.00 32.02 N ANISOU 88 N VAL F 12 4669 3928 3568 125 474 777 N ATOM 89 CA VAL A 12 72.552 63.370 49.805 1.00 30.86 C ANISOU 89 CA VAL F 12 4315 4473 2937 105 733 602 C ATOM 90 C VAL A 12 73.180 63.573 51.172 1.00 31.72 C ANISOU 90 C VAL F 12 4118 4969 2964 -299 730 513 C ATOM 91 O VAL A 12 72.630 63.193 52.232 1.00 33.07 O ANISOU 91 O VAL F 12 5054 4690 2820 -1018 1080 -72 O ATOM 92 CB VAL A 12 73.240 62.216 49.063 1.00 30.93 C ANISOU 92 CB VAL F 12 4292 4529 2930 249 606 644 C ATOM 93 CG1 VAL A 12 73.513 61.020 49.976 1.00 26.77 C ANISOU 93 CG1 VAL F 12 2518 4821 2832 -406 1004 825 C ATOM 94 CG2 VAL A 12 72.376 61.816 47.864 1.00 27.85 C ANISOU 94 CG2 VAL F 12 4346 3318 2917 63 533 331 C ATOM 95 N GLY A 13 74.374 64.176 51.230 1.00 34.20 N ANISOU 95 N GLY F 13 4049 5732 3212 -520 779 305 N ATOM 96 CA GLY A 13 74.988 64.394 52.553 1.00 29.99 C ANISOU 96 CA GLY F 13 3565 4722 3108 -212 638 236 C ATOM 97 C GLY A 13 74.137 65.323 53.397 1.00 32.48 C ANISOU 97 C GLY F 13 4481 4605 3254 -5 535 274 C ATOM 98 O GLY A 13 74.016 65.154 54.617 1.00 29.43 O ANISOU 98 O GLY F 13 3679 4384 3119 -135 1000 386 O ATOM 99 N LYS A 14 73.498 66.348 52.806 1.00 34.10 N ANISOU 99 N LYS F 14 4805 4698 3454 70 236 279 N ATOM 100 CA LYS A 14 72.727 67.233 53.695 1.00 33.19 C ANISOU 100 CA LYS F 14 3933 4702 3977 -10 646 255 C ATOM 101 C LYS A 14 71.534 66.504 54.283 1.00 32.13 C ANISOU 101 C LYS F 14 3945 4509 3753 -74 844 197 C ATOM 102 O LYS A 14 71.150 66.697 55.436 1.00 30.73 O ANISOU 102 O LYS F 14 3695 4154 3826 518 707 190 O ATOM 103 CB LYS A 14 72.284 68.503 52.956 1.00 35.28 C ANISOU 103 CB LYS F 14 3443 5482 4479 324 1177 812 C ATOM 104 CG LYS A 14 73.455 69.466 52.795 1.00 44.78 C ANISOU 104 CG LYS F 14 3870 7448 5695 -306 234 716 C ATOM 105 CD LYS A 14 73.237 70.570 51.782 1.00 51.11 C ANISOU 105 CD LYS F 14 4335 7781 7302 381 -432 799 C ATOM 106 CE LYS A 14 74.327 71.636 51.873 1.00 59.42 C ANISOU 106 CE LYS F 14 4853 9178 8545 -1037 -1909 511 C ATOM 107 NZ LYS A 14 75.283 71.571 50.725 1.00 82.88 N ANISOU 107 NZ LYS F 14 9491 12124 9874 -4405 -260 -1517 N ATOM 108 N TRP A 15 70.930 65.650 53.475 1.00 32.83 N ANISOU 108 N TRP F 15 3964 4686 3826 16 920 319 N ATOM 109 CA TRP A 15 69.734 64.924 53.893 1.00 31.38 C ANISOU 109 CA TRP F 15 3957 4475 3492 36 838 671 C ATOM 110 C TRP A 15 70.094 63.965 55.019 1.00 30.90 C ANISOU 110 C TRP F 15 4466 4001 3273 -274 838 651 C ATOM 111 O TRP A 15 69.457 63.889 56.076 1.00 30.21 O ANISOU 111 O TRP F 15 3919 3861 3699 -145 576 482 O ATOM 112 CB TRP A 15 69.071 64.150 52.717 1.00 32.35 C ANISOU 112 CB TRP F 15 4518 4618 3156 -598 816 601 C ATOM 113 CG TRP A 15 67.661 63.741 53.109 1.00 32.69 C ANISOU 113 CG TRP F 15 4393 4590 3440 -423 1089 0 C ATOM 114 CD1 TRP A 15 66.506 64.401 52.794 1.00 33.69 C ANISOU 114 CD1 TRP F 15 4677 4557 3565 -529 1072 -65 C ATOM 115 CD2 TRP A 15 67.260 62.594 53.885 1.00 33.36 C ANISOU 115 CD2 TRP F 15 4267 4495 3913 -175 1017 -585 C ATOM 116 NE1 TRP A 15 65.413 63.746 53.320 1.00 35.12 N ANISOU 116 NE1 TRP F 15 4626 4609 4109 -443 1009 -286 N ATOM 117 CE2 TRP A 15 65.848 62.633 53.993 1.00 34.81 C ANISOU 117 CE2 TRP F 15 4363 4726 4137 -481 1105 -233 C ATOM 118 CE3 TRP A 15 67.942 61.533 54.499 1.00 29.62 C ANISOU 118 CE3 TRP F 15 3588 4554 3111 -87 1519 -713 C ATOM 119 CZ2 TRP A 15 65.113 61.670 54.684 1.00 32.81 C ANISOU 119 CZ2 TRP F 15 3755 4507 4204 -110 1598 -773 C ATOM 120 CZ3 TRP A 15 67.218 60.581 55.182 1.00 33.75 C ANISOU 120 CZ3 TRP F 15 4283 5014 3525 -980 862 188 C ATOM 121 CH2 TRP A 15 65.816 60.654 55.267 1.00 35.37 C ANISOU 121 CH2 TRP F 15 4813 4770 3856 -814 679 -158 C ATOM 122 N ALA A 16 71.144 63.192 54.754 1.00 30.94 N ANISOU 122 N ALA F 16 4454 4063 3239 -229 793 488 N ATOM 123 CA ALA A 16 71.610 62.207 55.740 1.00 29.29 C ANISOU 123 CA ALA F 16 3856 4129 3145 116 1164 397 C ATOM 124 C ALA A 16 72.020 62.877 57.040 1.00 29.05 C ANISOU 124 C ALA F 16 3699 4539 2798 -316 790 36 C ATOM 125 O ALA A 16 71.676 62.492 58.155 1.00 33.29 O ANISOU 125 O ALA F 16 4768 4944 2935 -1247 418 291 O ATOM 126 CB ALA A 16 72.771 61.443 55.125 1.00 26.10 C ANISOU 126 CB ALA F 16 2751 4510 2657 366 -21 59 C ATOM 127 N ALA A 17 72.801 63.955 56.910 1.00 30.90 N ANISOU 127 N ALA F 17 3685 4787 3270 -548 1021 78 N ATOM 128 CA ALA A 17 73.223 64.679 58.109 1.00 29.58 C ANISOU 128 CA ALA F 17 3656 4664 2920 9 781 291 C ATOM 129 C ALA A 17 72.009 65.242 58.828 1.00 30.77 C ANISOU 129 C ALA F 17 3429 4455 3808 304 1037 159 C ATOM 130 O ALA A 17 71.909 65.157 60.066 1.00 33.56 O ANISOU 130 O ALA F 17 5242 3549 3961 322 391 -19 O ATOM 131 CB ALA A 17 74.231 65.750 57.733 1.00 31.67 C ANISOU 131 CB ALA F 17 3817 5595 2621 -705 945 938 C ATOM 132 N ARG A 18 71.039 65.816 58.136 1.00 33.37 N ANISOU 132 N ARG F 18 4138 4690 3852 -305 976 359 N ATOM 133 CA ARG A 18 69.843 66.318 58.813 1.00 32.76 C ANISOU 133 CA ARG F 18 3847 4462 4140 76 1273 399 C ATOM 134 C ARG A 18 69.089 65.180 59.499 1.00 31.33 C ANISOU 134 C ARG F 18 4125 3797 3982 276 1024 85 C ATOM 135 O ARG A 18 68.541 65.381 60.608 1.00 36.95 O ANISOU 135 O ARG F 18 4887 4509 4643 82 1079 -703 O ATOM 136 CB ARG A 18 68.948 67.049 57.815 1.00 33.91 C ANISOU 136 CB ARG F 18 3988 4728 4170 240 1013 497 C ATOM 137 CG ARG A 18 67.771 67.781 58.452 1.00 37.46 C ANISOU 137 CG ARG F 18 4925 4534 4776 327 1308 593 C ATOM 138 CD ARG A 18 66.982 68.535 57.378 1.00 41.00 C ANISOU 138 CD ARG F 18 5949 4767 4862 140 1220 802 C ATOM 139 NE ARG A 18 66.269 67.604 56.497 1.00 45.31 N ANISOU 139 NE ARG F 18 6946 5829 4442 -324 1671 479 N ATOM 140 CZ ARG A 18 65.397 67.928 55.565 1.00 50.53 C ANISOU 140 CZ ARG F 18 7873 6006 5319 -150 2270 950 C ATOM 141 NH1 ARG A 18 65.101 69.205 55.358 1.00 60.56 N ANISOU 141 NH1 ARG F 18 8888 7188 6934 529 1145 1804 N ATOM 142 NH2 ARG A 18 64.826 66.980 54.841 1.00 58.04 N ANISOU 142 NH2 ARG F 18 9870 5866 6316 -870 4164 -161 N ATOM 143 N HIS A 19 69.041 63.995 58.890 1.00 30.93 N ANISOU 143 N HIS F 19 4001 3875 3875 385 985 358 N ATOM 144 CA HIS A 19 68.363 62.836 59.485 1.00 29.19 C ANISOU 144 CA HIS F 19 4131 3571 3390 299 962 56 C ATOM 145 C HIS A 19 69.037 62.462 60.803 1.00 30.19 C ANISOU 145 C HIS F 19 4403 3642 3426 10 894 90 C ATOM 146 O HIS A 19 68.440 62.260 61.867 1.00 36.06 O ANISOU 146 O HIS F 19 6311 3812 3577 -286 289 203 O ATOM 147 CB HIS A 19 68.352 61.641 58.519 1.00 28.79 C ANISOU 147 CB HIS F 19 4045 3511 3382 510 825 102 C ATOM 148 CG HIS A 19 67.469 60.525 58.979 1.00 30.50 C ANISOU 148 CG HIS F 19 4090 3803 3695 373 813 -201 C ATOM 149 ND1 HIS A 19 66.104 60.625 59.086 1.00 33.56 N ANISOU 149 ND1 HIS F 19 4787 3990 3973 -5 382 44 N ATOM 150 CD2 HIS A 19 67.758 59.256 59.378 1.00 31.72 C ANISOU 150 CD2 HIS F 19 3922 3984 4146 448 549 -610 C ATOM 151 CE1 HIS A 19 65.581 59.491 59.517 1.00 34.20 C ANISOU 151 CE1 HIS F 19 4915 4265 3813 -128 130 -220 C ATOM 152 NE2 HIS A 19 66.572 58.639 59.704 1.00 34.50 N ANISOU 152 NE2 HIS F 19 4320 4316 4472 92 236 -445 N ATOM 153 N ILE A 20 70.368 62.370 60.745 1.00 33.50 N ANISOU 153 N ILE F 20 4840 4222 3665 -726 1231 153 N ATOM 154 CA ILE A 20 71.158 62.043 61.946 1.00 32.34 C ANISOU 154 CA ILE F 20 4869 3846 3575 -275 1542 -52 C ATOM 155 C ILE A 20 70.860 63.062 63.034 1.00 33.02 C ANISOU 155 C ILE F 20 4689 4221 3637 -170 1282 -341 C ATOM 156 O ILE A 20 70.539 62.661 64.156 1.00 35.06 O ANISOU 156 O ILE F 20 5147 4395 3778 -369 1052 -545 O ATOM 157 CB ILE A 20 72.662 61.972 61.614 1.00 31.64 C ANISOU 157 CB ILE F 20 4972 3796 3253 -249 1104 99 C ATOM 158 CG1 ILE A 20 73.039 60.811 60.685 1.00 27.21 C ANISOU 158 CG1 ILE F 20 4083 3578 2679 -480 788 382 C ATOM 159 CG2 ILE A 20 73.480 61.937 62.895 1.00 30.74 C ANISOU 159 CG2 ILE F 20 4222 4101 3356 -234 1397 63 C ATOM 160 CD1 ILE A 20 74.443 60.847 60.124 1.00 27.95 C ANISOU 160 CD1 ILE F 20 3960 3676 2983 -143 98 227 C ATOM 161 N VAL A 21 70.940 64.341 62.699 1.00 33.86 N ANISOU 161 N VAL F 21 4471 4460 3934 -273 1515 -76 N ATOM 162 CA VAL A 21 70.683 65.405 63.670 1.00 34.17 C ANISOU 162 CA VAL F 21 4534 4381 4068 -123 1204 -318 C ATOM 163 C VAL A 21 69.295 65.286 64.290 1.00 36.10 C ANISOU 163 C VAL F 21 5749 4619 3350 -662 814 77 C ATOM 164 O VAL A 21 69.054 65.408 65.498 1.00 37.00 O ANISOU 164 O VAL F 21 6030 4317 3713 -347 2338 -810 O ATOM 165 CB VAL A 21 70.850 66.787 63.000 1.00 37.20 C ANISOU 165 CB VAL F 21 4646 4993 4495 100 1086 -325 C ATOM 166 CG1 VAL A 21 70.253 67.875 63.894 1.00 33.39 C ANISOU 166 CG1 VAL F 21 3606 5524 3557 -231 1759 143 C ATOM 167 CG2 VAL A 21 72.314 67.044 62.675 1.00 37.04 C ANISOU 167 CG2 VAL F 21 4146 5571 4354 -179 1433 -119 C ATOM 168 N ASN A 22 68.305 65.032 63.442 1.00 35.42 N ANISOU 168 N ASN F 22 5578 4810 3072 -833 684 -45 N ATOM 169 CA ASN A 22 66.944 64.920 63.954 1.00 36.23 C ANISOU 169 CA ASN F 22 5802 4366 3596 -598 428 13 C ATOM 170 C ASN A 22 66.795 63.687 64.828 1.00 35.13 C ANISOU 170 C ASN F 22 5692 4331 3324 -622 502 -178 C ATOM 171 O ASN A 22 66.098 63.714 65.846 1.00 37.68 O ANISOU 171 O ASN F 22 5612 5340 3365 -947 734 -548 O ATOM 172 CB ASN A 22 65.968 64.925 62.775 1.00 39.79 C ANISOU 172 CB ASN F 22 6436 4639 4041 -967 142 475 C ATOM 173 CG ASN A 22 65.875 66.275 62.081 1.00 45.83 C ANISOU 173 CG ASN F 22 7258 5374 4783 -947 -662 925 C ATOM 174 OD1 ASN A 22 65.216 66.359 61.045 1.00 54.80 O ANISOU 174 OD1 ASN F 22 8143 7299 5378 -1210 -963 2065 O ATOM 175 ND2 ASN A 22 66.491 67.334 62.591 1.00 45.89 N ANISOU 175 ND2 ASN F 22 7308 5443 4685 354 -589 472 N ATOM 176 N ARG A 23 67.438 62.570 64.496 1.00 35.83 N ANISOU 176 N ARG F 23 5833 4392 3389 -470 976 198 N ATOM 177 CA ARG A 23 67.345 61.431 65.410 1.00 33.81 C ANISOU 177 CA ARG F 23 5251 4775 2818 -351 1334 -299 C ATOM 178 C ARG A 23 68.009 61.755 66.736 1.00 34.96 C ANISOU 178 C ARG F 23 5254 5289 2741 -722 1197 -306 C ATOM 179 O ARG A 23 67.465 61.443 67.794 1.00 36.82 O ANISOU 179 O ARG F 23 5818 5426 2745 -279 1168 -752 O ATOM 180 CB ARG A 23 68.016 60.201 64.797 1.00 35.25 C ANISOU 180 CB ARG F 23 5146 4909 3337 -363 1235 -638 C ATOM 181 CG ARG A 23 67.154 59.692 63.657 1.00 30.89 C ANISOU 181 CG ARG F 23 4207 4471 3060 112 732 -412 C ATOM 182 CD ARG A 23 65.844 59.103 64.202 1.00 38.51 C ANISOU 182 CD ARG F 23 5582 5100 3950 -1057 249 -41 C ATOM 183 NE ARG A 23 65.249 58.312 63.112 1.00 40.05 N ANISOU 183 NE ARG F 23 4953 5583 4681 -1159 237 382 N ATOM 184 CZ ARG A 23 63.957 58.237 62.827 1.00 46.54 C ANISOU 184 CZ ARG F 23 6432 5918 5332 -1957 791 -23 C ATOM 185 NH1 ARG A 23 63.100 58.926 63.585 1.00 45.47 N ANISOU 185 NH1 ARG F 23 6255 5597 5424 -1602 1236 316 N ATOM 186 NH2 ARG A 23 63.553 57.486 61.806 1.00 39.35 N ANISOU 186 NH2 ARG F 23 5844 4406 4700 -1401 167 496 N ATOM 187 N ILE A 24 69.187 62.380 66.677 1.00 36.60 N ANISOU 187 N ILE F 24 5032 5082 3794 -531 1463 -307 N ATOM 188 CA ILE A 24 69.843 62.711 67.936 1.00 36.12 C ANISOU 188 CA ILE F 24 4944 4952 3828 -444 1575 -410 C ATOM 189 C ILE A 24 69.014 63.694 68.746 1.00 37.86 C ANISOU 189 C ILE F 24 5388 5292 3707 -139 1001 -707 C ATOM 190 O ILE A 24 68.823 63.584 69.961 1.00 43.09 O ANISOU 190 O ILE F 24 6870 5635 3868 -744 545 -885 O ATOM 191 CB ILE A 24 71.241 63.298 67.676 1.00 33.76 C ANISOU 191 CB ILE F 24 4106 5106 3616 84 1724 -768 C ATOM 192 CG1 ILE A 24 72.224 62.276 67.115 1.00 32.78 C ANISOU 192 CG1 ILE F 24 4389 4766 3300 68 1392 -388 C ATOM 193 CG2 ILE A 24 71.785 63.954 68.954 1.00 35.69 C ANISOU 193 CG2 ILE F 24 3904 6526 3130 -272 1273 -1019 C ATOM 194 CD1 ILE A 24 73.446 62.864 66.463 1.00 33.70 C ANISOU 194 CD1 ILE F 24 4440 4508 3855 -216 1429 -75 C ATOM 195 N ASN A 25 68.470 64.733 68.106 1.00 39.70 N ANISOU 195 N ASN F 25 5448 5176 4462 -73 823 -715 N ATOM 196 CA ASN A 25 67.779 65.738 68.920 1.00 38.29 C ANISOU 196 CA ASN F 25 4951 5480 4118 -75 1363 -477 C ATOM 197 C ASN A 25 66.477 65.171 69.456 1.00 38.36 C ANISOU 197 C ASN F 25 5064 5487 4025 -82 1665 -1018 C ATOM 198 O ASN A 25 65.998 65.514 70.547 1.00 45.52 O ANISOU 198 O ASN F 25 6670 6190 4436 -504 2035 -1597 O ATOM 199 CB ASN A 25 67.598 67.028 68.118 1.00 38.75 C ANISOU 199 CB ASN F 25 5514 5043 4167 -147 1240 -254 C ATOM 200 CG ASN A 25 68.884 67.818 67.939 1.00 37.94 C ANISOU 200 CG ASN F 25 4753 5011 4650 399 1590 199 C ATOM 201 OD1 ASN A 25 69.827 67.665 68.721 1.00 43.68 O ANISOU 201 OD1 ASN F 25 5939 5284 5373 -193 1400 577 O ATOM 202 ND2 ASN A 25 69.002 68.678 66.938 1.00 38.06 N ANISOU 202 ND2 ASN F 25 5159 4318 4983 639 1083 -371 N ATOM 203 N ALA A 26 65.830 64.242 68.754 1.00 39.03 N ANISOU 203 N ALA F 26 5387 5650 3794 -559 1731 -124 N ATOM 204 CA ALA A 26 64.570 63.728 69.307 1.00 39.56 C ANISOU 204 CA ALA F 26 5776 5022 4232 -740 1787 -16 C ATOM 205 C ALA A 26 64.817 62.754 70.448 1.00 39.68 C ANISOU 205 C ALA F 26 6338 4625 4112 -760 1116 -698 C ATOM 206 O ALA A 26 63.980 62.605 71.328 1.00 47.53 O ANISOU 206 O ALA F 26 9724 4861 3475 -1902 1068 -498 O ATOM 207 CB ALA A 26 63.762 63.029 68.223 1.00 36.18 C ANISOU 207 CB ALA F 26 5123 4342 4282 -55 1936 -723 C ATOM 208 N PHE A 27 65.965 62.084 70.410 1.00 38.35 N ANISOU 208 N PHE F 27 5942 4615 4013 -405 1029 -920 N ATOM 209 CA PHE A 27 66.334 61.086 71.405 1.00 40.04 C ANISOU 209 CA PHE F 27 6188 5010 4013 -384 1177 -579 C ATOM 210 C PHE A 27 66.762 61.722 72.723 1.00 41.26 C ANISOU 210 C PHE F 27 6808 4817 4051 -346 1448 -885 C ATOM 211 O PHE A 27 66.541 61.134 73.781 1.00 41.16 O ANISOU 211 O PHE F 27 7394 4144 4103 -954 1316 -139 O ATOM 212 CB PHE A 27 67.485 60.233 70.896 1.00 37.50 C ANISOU 212 CB PHE F 27 5627 5273 3349 184 623 -681 C ATOM 213 CG PHE A 27 67.977 59.081 71.751 1.00 36.10 C ANISOU 213 CG PHE F 27 4925 5379 3413 -351 584 -349 C ATOM 214 CD1 PHE A 27 67.426 57.825 71.581 1.00 36.57 C ANISOU 214 CD1 PHE F 27 4890 5474 3529 -493 506 -721 C ATOM 215 CD2 PHE A 27 68.975 59.254 72.694 1.00 37.55 C ANISOU 215 CD2 PHE F 27 5136 5593 3540 -1063 296 -375 C ATOM 216 CE1 PHE A 27 67.860 56.765 72.336 1.00 37.05 C ANISOU 216 CE1 PHE F 27 4493 5781 3805 -495 810 -343 C ATOM 217 CE2 PHE A 27 69.426 58.187 73.454 1.00 38.14 C ANISOU 217 CE2 PHE F 27 4737 5829 3926 -1438 374 177 C ATOM 218 CZ PHE A 27 68.876 56.930 73.264 1.00 39.50 C ANISOU 218 CZ PHE F 27 4809 6140 4058 -1157 437 -99 C ATOM 219 N LYS A 28 67.374 62.894 72.626 1.00 44.61 N ANISOU 219 N LYS F 28 6756 5747 4445 -570 1777 -641 N ATOM 220 CA LYS A 28 67.799 63.640 73.814 1.00 46.21 C ANISOU 220 CA LYS F 28 7387 5462 4708 -684 2205 -620 C ATOM 221 C LYS A 28 68.786 62.848 74.669 1.00 44.35 C ANISOU 221 C LYS F 28 7283 5607 3960 -986 1123 -833 C ATOM 222 O LYS A 28 68.459 62.464 75.795 1.00 49.03 O ANISOU 222 O LYS F 28 8259 6865 3505 -1735 1498 -1172 O ATOM 223 CB LYS A 28 66.581 64.030 74.661 1.00 52.78 C ANISOU 223 CB LYS F 28 8806 5571 5675 -713 2907 -1237 C ATOM 224 CG LYS A 28 65.706 65.074 73.999 1.00 62.04 C ANISOU 224 CG LYS F 28 10735 5380 7459 -1095 2638 -533 C ATOM 225 CD LYS A 28 64.228 64.704 74.005 1.00 83.37 C ANISOU 225 CD LYS F 28 14704 6945 10028 -3815 2545 -213 C ATOM 226 CE LYS A 28 63.564 65.024 72.670 1.00 92.61 C ANISOU 226 CE LYS F 28 16511 7514 11163 -4622 2424 933 C ATOM 227 NZ LYS A 28 62.342 64.220 72.383 1.00103.41 N ANISOU 227 NZ LYS F 28 18273 7587 13433 -5443 6133 -1423 N ATOM 228 N PRO A 29 69.978 62.613 74.130 1.00 39.46 N ANISOU 228 N PRO F 29 5785 5362 3845 -424 1002 -725 N ATOM 229 CA PRO A 29 70.955 61.731 74.768 1.00 37.54 C ANISOU 229 CA PRO F 29 5009 5543 3711 -230 939 -695 C ATOM 230 C PRO A 29 71.546 62.348 76.026 1.00 41.25 C ANISOU 230 C PRO F 29 6231 5831 3612 -708 1172 -774 C ATOM 231 O PRO A 29 71.651 63.571 76.104 1.00 43.73 O ANISOU 231 O PRO F 29 5745 6606 4264 -1134 1934 -461 O ATOM 232 CB PRO A 29 72.054 61.619 73.700 1.00 35.65 C ANISOU 232 CB PRO F 29 4574 5268 3702 -35 1111 -669 C ATOM 233 CG PRO A 29 71.961 62.926 72.970 1.00 36.41 C ANISOU 233 CG PRO F 29 5121 5152 3560 33 908 -576 C ATOM 234 CD PRO A 29 70.476 63.180 72.862 1.00 38.15 C ANISOU 234 CD PRO F 29 5260 5248 3985 -108 942 -559 C ATOM 235 N THR A 30 71.924 61.489 76.966 1.00 45.50 N ANISOU 235 N THR F 30 7490 6010 3786 -1299 469 -481 N ATOM 236 CA THR A 30 72.604 61.934 78.176 1.00 46.83 C ANISOU 236 CA THR F 30 7609 6480 3702 -1843 299 -454 C ATOM 237 C THR A 30 73.800 61.034 78.477 1.00 50.02 C ANISOU 237 C THR F 30 8268 6557 4179 -1744 797 -198 C ATOM 238 O THR A 30 74.010 60.020 77.806 1.00 52.51 O ANISOU 238 O THR F 30 8664 6438 4849 -1677 1162 -222 O ATOM 239 CB THR A 30 71.668 61.949 79.399 1.00 44.09 C ANISOU 239 CB THR F 30 6711 6582 3459 -1159 -332 -109 C ATOM 240 OG1 THR A 30 71.215 60.614 79.650 1.00 46.64 O ANISOU 240 OG1 THR F 30 6551 7076 4093 -953 237 201 O ATOM 241 CG2 THR A 30 70.428 62.783 79.122 1.00 42.08 C ANISOU 241 CG2 THR F 30 7296 6431 2261 -443 1449 -777 C ATOM 242 N ALA A 31 74.566 61.423 79.496 1.00 52.97 N ANISOU 242 N ALA F 31 8827 7004 4296 -1634 985 127 N ATOM 243 CA ALA A 31 75.753 60.687 79.912 1.00 53.78 C ANISOU 243 CA ALA F 31 9115 6975 4346 -1331 1698 68 C ATOM 244 C ALA A 31 75.439 59.208 80.120 1.00 54.14 C ANISOU 244 C ALA F 31 9096 7145 4330 -1356 1670 468 C ATOM 245 O ALA A 31 76.241 58.342 79.779 1.00 56.11 O ANISOU 245 O ALA F 31 9632 7247 4442 -738 -88 303 O ATOM 246 CB ALA A 31 76.339 61.276 81.191 1.00 55.18 C ANISOU 246 CB ALA F 31 9035 7432 4499 -1937 1730 -40 C ATOM 247 N ASP A 32 74.264 58.950 80.690 1.00 54.17 N ANISOU 247 N ASP F 32 8981 7218 4383 -1307 1864 231 N ATOM 248 CA ASP A 32 73.855 57.594 81.044 1.00 56.83 C ANISOU 248 CA ASP F 32 9268 7418 4908 -1227 1294 339 C ATOM 249 C ASP A 32 72.944 56.968 79.991 1.00 53.60 C ANISOU 249 C ASP F 32 8274 6953 5141 -1152 740 731 C ATOM 250 O ASP A 32 72.622 55.777 80.072 1.00 51.86 O ANISOU 250 O ASP F 32 8029 7728 3949 -1792 -388 384 O ATOM 251 CB ASP A 32 73.180 57.604 82.419 1.00 62.94 C ANISOU 251 CB ASP F 32 10524 8347 5042 -1065 743 143 C ATOM 252 CG ASP A 32 74.194 57.860 83.526 1.00 73.31 C ANISOU 252 CG ASP F 32 14176 8786 4892 -2321 1926 -630 C ATOM 253 OD1 ASP A 32 75.313 57.286 83.496 1.00 85.57 O ANISOU 253 OD1 ASP F 32 18137 8895 5480 -4880 594 -885 O ATOM 254 OD2 ASP A 32 73.895 58.648 84.457 1.00102.79 O ANISOU 254 OD2 ASP F 32 18775 12167 8113 -4367 5851 -3177 O ATOM 255 N ARG A 33 72.534 57.763 79.005 1.00 47.75 N ANISOU 255 N ARG F 33 7703 6550 3890 -716 804 -507 N ATOM 256 CA ARG A 33 71.736 57.242 77.900 1.00 44.00 C ANISOU 256 CA ARG F 33 6663 6144 3912 -801 287 -402 C ATOM 257 C ARG A 33 72.198 57.947 76.625 1.00 42.40 C ANISOU 257 C ARG F 33 6310 5814 3985 -788 346 -194 C ATOM 258 O ARG A 33 71.554 58.897 76.172 1.00 42.09 O ANISOU 258 O ARG F 33 6755 5625 3612 -979 834 113 O ATOM 259 CB ARG A 33 70.234 57.420 78.113 1.00 46.13 C ANISOU 259 CB ARG F 33 6191 6304 5030 -675 436 -1107 C ATOM 260 CG ARG A 33 69.415 56.420 77.310 1.00 48.91 C ANISOU 260 CG ARG F 33 5890 6223 6471 -488 610 -650 C ATOM 261 CD ARG A 33 67.943 56.821 77.237 1.00 50.23 C ANISOU 261 CD ARG F 33 5725 6018 7342 -54 992 -652 C ATOM 262 NE ARG A 33 67.830 58.235 76.931 1.00 54.48 N ANISOU 262 NE ARG F 33 6214 6723 7762 313 312 -655 N ATOM 263 CZ ARG A 33 67.090 58.852 76.028 1.00 51.40 C ANISOU 263 CZ ARG F 33 5936 6491 7104 380 692 -1028 C ATOM 264 NH1 ARG A 33 66.270 58.242 75.194 1.00 45.95 N ANISOU 264 NH1 ARG F 33 5864 5661 5935 -359 383 -2613 N ATOM 265 NH2 ARG A 33 67.205 60.177 75.987 1.00 51.57 N ANISOU 265 NH2 ARG F 33 6382 6499 6714 886 1086 -1189 N ATOM 266 N PRO A 34 73.327 57.471 76.113 1.00 38.08 N ANISOU 266 N PRO F 34 5036 5895 3539 -293 777 -377 N ATOM 267 CA PRO A 34 73.884 58.051 74.893 1.00 37.24 C ANISOU 267 CA PRO F 34 5165 5475 3510 -542 698 62 C ATOM 268 C PRO A 34 73.132 57.604 73.644 1.00 37.15 C ANISOU 268 C PRO F 34 4964 5495 3654 -911 572 154 C ATOM 269 O PRO A 34 72.533 56.535 73.641 1.00 34.83 O ANISOU 269 O PRO F 34 4961 4858 3415 -1190 232 197 O ATOM 270 CB PRO A 34 75.298 57.456 74.855 1.00 34.64 C ANISOU 270 CB PRO F 34 3958 5439 3767 -423 591 302 C ATOM 271 CG PRO A 34 75.165 56.138 75.557 1.00 34.98 C ANISOU 271 CG PRO F 34 4129 5589 3573 -786 -2 -77 C ATOM 272 CD PRO A 34 74.157 56.380 76.641 1.00 35.93 C ANISOU 272 CD PRO F 34 4820 5946 2885 -437 898 -291 C ATOM 273 N PHE A 35 73.187 58.404 72.590 1.00 33.50 N ANISOU 273 N PHE F 35 4323 4795 3610 -209 1093 92 N ATOM 274 CA PHE A 35 72.775 58.026 71.245 1.00 34.47 C ANISOU 274 CA PHE F 35 4715 4901 3480 -303 1108 -166 C ATOM 275 C PHE A 35 73.928 57.285 70.583 1.00 30.80 C ANISOU 275 C PHE F 35 3745 4708 3249 -133 283 80 C ATOM 276 O PHE A 35 75.056 57.794 70.522 1.00 34.69 O ANISOU 276 O PHE F 35 4370 5498 3313 -953 865 102 O ATOM 277 CB PHE A 35 72.420 59.255 70.426 1.00 31.19 C ANISOU 277 CB PHE F 35 4628 4378 2845 -147 1408 -659 C ATOM 278 CG PHE A 35 71.777 58.882 69.088 1.00 32.85 C ANISOU 278 CG PHE F 35 4726 4756 2998 -563 1396 -552 C ATOM 279 CD1 PHE A 35 70.412 58.688 69.015 1.00 34.09 C ANISOU 279 CD1 PHE F 35 4555 4989 3409 -659 1006 -231 C ATOM 280 CD2 PHE A 35 72.562 58.744 67.962 1.00 32.16 C ANISOU 280 CD2 PHE F 35 4104 5072 3044 -292 1803 -911 C ATOM 281 CE1 PHE A 35 69.811 58.344 67.819 1.00 36.47 C ANISOU 281 CE1 PHE F 35 5383 4816 3659 -970 1408 -344 C ATOM 282 CE2 PHE A 35 71.958 58.400 66.755 1.00 32.59 C ANISOU 282 CE2 PHE F 35 4209 5400 2773 -710 1003 -232 C ATOM 283 CZ PHE A 35 70.584 58.209 66.677 1.00 31.87 C ANISOU 283 CZ PHE F 35 4006 4644 3461 -139 1146 -158 C ATOM 284 N VAL A 36 73.673 56.085 70.084 1.00 31.61 N ANISOU 284 N VAL F 36 4174 4493 3343 -147 942 418 N ATOM 285 CA VAL A 36 74.748 55.265 69.533 1.00 31.43 C ANISOU 285 CA VAL F 36 4778 4483 2682 123 698 564 C ATOM 286 C VAL A 36 74.669 55.269 68.007 1.00 32.63 C ANISOU 286 C VAL F 36 5038 4700 2660 -862 252 757 C ATOM 287 O VAL A 36 73.635 54.865 67.451 1.00 32.32 O ANISOU 287 O VAL F 36 4713 5181 2386 -1089 704 -255 O ATOM 288 CB VAL A 36 74.727 53.834 70.095 1.00 31.27 C ANISOU 288 CB VAL F 36 4827 4559 2494 99 136 -277 C ATOM 289 CG1 VAL A 36 75.914 53.038 69.571 1.00 27.48 C ANISOU 289 CG1 VAL F 36 3380 4632 2430 -165 -163 -417 C ATOM 290 CG2 VAL A 36 74.725 53.859 71.638 1.00 28.93 C ANISOU 290 CG2 VAL F 36 3655 4842 2496 -270 474 -500 C ATOM 291 N LEU A 37 75.739 55.734 67.374 1.00 30.67 N ANISOU 291 N LEU F 37 4517 4144 2994 -623 685 483 N ATOM 292 CA LEU A 37 75.810 55.999 65.949 1.00 28.29 C ANISOU 292 CA LEU F 37 3603 4101 3043 -644 539 372 C ATOM 293 C LEU A 37 76.852 55.119 65.277 1.00 28.55 C ANISOU 293 C LEU F 37 3493 4173 3181 -461 441 330 C ATOM 294 O LEU A 37 78.015 55.236 65.670 1.00 29.10 O ANISOU 294 O LEU F 37 3783 3994 3281 -337 844 224 O ATOM 295 CB LEU A 37 76.266 57.424 65.686 1.00 32.82 C ANISOU 295 CB LEU F 37 3775 4139 4557 -272 387 425 C ATOM 296 CG LEU A 37 75.622 58.405 64.723 1.00 32.63 C ANISOU 296 CG LEU F 37 3723 5069 3608 -636 -25 474 C ATOM 297 CD1 LEU A 37 76.654 59.453 64.310 1.00 32.91 C ANISOU 297 CD1 LEU F 37 4935 4662 2905 -2002 -779 347 C ATOM 298 CD2 LEU A 37 74.989 57.782 63.493 1.00 28.13 C ANISOU 298 CD2 LEU F 37 4074 4126 2488 234 -64 -1156 C ATOM 299 N GLY A 38 76.472 54.314 64.296 1.00 29.00 N ANISOU 299 N GLY F 38 3598 4227 3192 -802 506 96 N ATOM 300 CA GLY A 38 77.441 53.520 63.547 1.00 27.79 C ANISOU 300 CA GLY F 38 3542 4232 2786 -519 8 203 C ATOM 301 C GLY A 38 77.851 54.283 62.285 1.00 28.30 C ANISOU 301 C GLY F 38 3406 4072 3273 -349 -292 388 C ATOM 302 O GLY A 38 77.011 54.940 61.656 1.00 26.56 O ANISOU 302 O GLY F 38 3348 4128 2614 -59 648 328 O ATOM 303 N LEU A 39 79.134 54.225 61.926 1.00 26.66 N ANISOU 303 N LEU F 39 3158 3916 3056 106 -40 -130 N ATOM 304 CA LEU A 39 79.669 55.098 60.893 1.00 26.08 C ANISOU 304 CA LEU F 39 2896 3741 3271 159 -45 -11 C ATOM 305 C LEU A 39 80.580 54.392 59.912 1.00 25.74 C ANISOU 305 C LEU F 39 3267 3450 3064 -333 27 177 C ATOM 306 O LEU A 39 81.304 53.469 60.273 1.00 27.38 O ANISOU 306 O LEU F 39 3133 3840 3430 335 36 -56 O ATOM 307 CB LEU A 39 80.483 56.228 61.558 1.00 28.35 C ANISOU 307 CB LEU F 39 3119 4457 3196 -71 160 283 C ATOM 308 CG LEU A 39 79.650 57.197 62.398 1.00 29.90 C ANISOU 308 CG LEU F 39 3207 4583 3570 -75 755 292 C ATOM 309 CD1 LEU A 39 80.535 58.286 63.012 1.00 28.57 C ANISOU 309 CD1 LEU F 39 3188 5131 2536 -340 361 570 C ATOM 310 CD2 LEU A 39 78.523 57.822 61.579 1.00 29.84 C ANISOU 310 CD2 LEU F 39 3316 4361 3659 -386 957 143 C ATOM 311 N PRO A 40 80.566 54.800 58.658 1.00 27.30 N ANISOU 311 N PRO F 40 3357 4166 2850 -156 495 260 N ATOM 312 CA PRO A 40 81.516 54.314 57.658 1.00 27.80 C ANISOU 312 CA PRO F 40 3695 4172 2697 -269 673 271 C ATOM 313 C PRO A 40 82.561 55.334 57.237 1.00 29.36 C ANISOU 313 C PRO F 40 3953 3855 3348 -565 426 409 C ATOM 314 O PRO A 40 82.518 56.504 57.640 1.00 28.16 O ANISOU 314 O PRO F 40 3646 3956 3097 -554 -80 202 O ATOM 315 CB PRO A 40 80.545 54.110 56.475 1.00 26.34 C ANISOU 315 CB PRO F 40 3850 3430 2729 -341 378 300 C ATOM 316 CG PRO A 40 79.656 55.308 56.584 1.00 26.74 C ANISOU 316 CG PRO F 40 3569 3895 2697 62 756 21 C ATOM 317 CD PRO A 40 79.582 55.710 58.046 1.00 26.74 C ANISOU 317 CD PRO F 40 3568 4218 2373 -160 163 111 C ATOM 318 N THR A 41 83.503 54.893 56.410 1.00 30.65 N ANISOU 318 N THR F 41 4076 4449 3119 -593 654 129 N ATOM 319 CA THR A 41 84.550 55.748 55.881 1.00 32.57 C ANISOU 319 CA THR F 41 4423 4492 3462 -721 316 55 C ATOM 320 C THR A 41 84.492 55.696 54.354 1.00 34.25 C ANISOU 320 C THR F 41 4493 5077 3445 -735 278 149 C ATOM 321 O THR A 41 83.597 55.051 53.793 1.00 39.20 O ANISOU 321 O THR F 41 4684 6525 3685 -983 561 213 O ATOM 322 CB THR A 41 85.975 55.381 56.340 1.00 33.71 C ANISOU 322 CB THR F 41 5253 4338 3216 -1003 374 -341 C ATOM 323 OG1 THR A 41 86.284 54.057 55.884 1.00 36.62 O ANISOU 323 OG1 THR F 41 6285 4357 3273 -747 1025 -314 O ATOM 324 CG2 THR A 41 86.130 55.324 57.847 1.00 31.31 C ANISOU 324 CG2 THR F 41 5179 3499 3219 550 189 -159 C ATOM 325 N GLY A 42 85.414 56.357 53.682 1.00 36.09 N ANISOU 325 N GLY F 42 4541 5612 3561 -598 114 26 N ATOM 326 CA GLY A 42 85.504 56.369 52.241 1.00 36.71 C ANISOU 326 CA GLY F 42 4990 5433 3523 -684 16 166 C ATOM 327 C GLY A 42 84.934 57.623 51.627 1.00 35.57 C ANISOU 327 C GLY F 42 4942 5088 3485 -742 147 -25 C ATOM 328 O GLY A 42 84.496 58.562 52.260 1.00 35.05 O ANISOU 328 O GLY F 42 5529 4786 3001 -940 306 113 O ATOM 329 N GLY A 43 84.926 57.683 50.298 1.00 34.07 N ANISOU 329 N GLY F 43 4938 4519 3487 -272 530 59 N ATOM 330 CA GLY A 43 84.447 58.866 49.594 1.00 33.79 C ANISOU 330 CA GLY F 43 4362 4499 3976 -767 424 439 C ATOM 331 C GLY A 43 82.945 59.041 49.732 1.00 31.78 C ANISOU 331 C GLY F 43 4012 4468 3594 -551 440 29 C ATOM 332 O GLY A 43 82.457 60.171 49.712 1.00 32.96 O ANISOU 332 O GLY F 43 4103 4546 3873 -467 797 284 O ATOM 333 N THR A 44 82.193 57.955 49.868 1.00 30.70 N ANISOU 333 N THR F 44 3928 4790 2946 -615 788 -67 N ATOM 334 CA THR A 44 80.733 58.058 49.895 1.00 31.56 C ANISOU 334 CA THR F 44 4083 4857 3050 -743 580 -30 C ATOM 335 C THR A 44 80.194 58.904 51.026 1.00 27.57 C ANISOU 335 C THR F 44 3397 4242 2838 -98 107 451 C ATOM 336 O THR A 44 79.360 59.782 50.762 1.00 29.25 O ANISOU 336 O THR F 44 2870 4461 3782 -108 348 1007 O ATOM 337 CB THR A 44 80.106 56.643 49.960 1.00 32.96 C ANISOU 337 CB THR F 44 4063 4366 4094 -645 1021 -659 C ATOM 338 OG1 THR A 44 80.335 55.991 48.698 1.00 40.12 O ANISOU 338 OG1 THR F 44 5055 5581 4609 -1401 1930 -1118 O ATOM 339 CG2 THR A 44 78.602 56.695 50.138 1.00 30.57 C ANISOU 339 CG2 THR F 44 4264 4209 3141 -760 433 432 C ATOM 340 N PRO A 45 80.543 58.721 52.297 1.00 27.52 N ANISOU 340 N PRO F 45 3448 4170 2840 -157 392 440 N ATOM 341 CA PRO A 45 79.998 59.628 53.308 1.00 28.21 C ANISOU 341 CA PRO F 45 3447 4269 3002 63 271 322 C ATOM 342 C PRO A 45 80.676 60.990 53.387 1.00 28.67 C ANISOU 342 C PRO F 45 3466 4244 3183 199 52 130 C ATOM 343 O PRO A 45 80.342 61.757 54.297 1.00 29.73 O ANISOU 343 O PRO F 45 3427 4747 3122 -639 856 110 O ATOM 344 CB PRO A 45 80.270 58.853 54.616 1.00 26.66 C ANISOU 344 CB PRO F 45 3291 3904 2934 -104 69 9 C ATOM 345 CG PRO A 45 81.488 58.021 54.323 1.00 26.85 C ANISOU 345 CG PRO F 45 3873 3958 2372 -165 -185 -94 C ATOM 346 CD PRO A 45 81.393 57.657 52.854 1.00 28.88 C ANISOU 346 CD PRO F 45 4611 3828 2536 -229 346 252 C ATOM 347 N MET A 46 81.609 61.402 52.544 1.00 31.24 N ANISOU 347 N MET F 46 3654 5111 3103 -530 326 104 N ATOM 348 CA MET A 46 82.254 62.714 52.723 1.00 32.62 C ANISOU 348 CA MET F 46 3597 4831 3968 -342 -49 882 C ATOM 349 C MET A 46 81.299 63.903 52.790 1.00 34.04 C ANISOU 349 C MET F 46 4307 4874 3754 -194 1028 833 C ATOM 350 O MET A 46 81.417 64.751 53.673 1.00 36.82 O ANISOU 350 O MET F 46 4296 5735 3957 -568 1120 309 O ATOM 351 CB MET A 46 83.255 63.039 51.602 1.00 32.57 C ANISOU 351 CB MET F 46 3155 5559 3662 142 294 281 C ATOM 352 CG MET A 46 84.501 62.174 51.623 1.00 39.33 C ANISOU 352 CG MET F 46 4828 5541 4573 142 -53 -347 C ATOM 353 SD MET A 46 85.546 62.631 53.022 1.00 54.33 S ANISOU 353 SD MET F 46 6699 6308 7636 -571 996 1817 S ATOM 354 CE MET A 46 86.219 64.184 52.450 1.00 56.96 C ANISOU 354 CE MET F 46 5802 8021 7819 43 2212 -1512 C ATOM 355 N THR A 47 80.333 64.017 51.874 1.00 32.40 N ANISOU 355 N THR F 47 3999 4720 3590 -566 433 774 N ATOM 356 CA THR A 47 79.471 65.200 51.975 1.00 31.89 C ANISOU 356 CA THR F 47 3595 4904 3620 -412 345 823 C ATOM 357 C THR A 47 78.589 65.118 53.211 1.00 32.90 C ANISOU 357 C THR F 47 4405 4460 3634 -205 58 935 C ATOM 358 O THR A 47 78.126 66.155 53.718 1.00 33.63 O ANISOU 358 O THR F 47 4046 4683 4048 -241 43 705 O ATOM 359 CB THR A 47 78.569 65.402 50.740 1.00 30.82 C ANISOU 359 CB THR F 47 4163 4178 3369 -198 1031 189 C ATOM 360 OG1 THR A 47 77.758 64.219 50.575 1.00 33.92 O ANISOU 360 OG1 THR F 47 4147 5056 3687 -660 646 709 O ATOM 361 CG2 THR A 47 79.358 65.628 49.449 1.00 31.26 C ANISOU 361 CG2 THR F 47 3715 4857 3305 -117 1007 160 C ATOM 362 N THR A 48 78.317 63.920 53.734 1.00 29.54 N ANISOU 362 N THR F 48 4228 3914 3080 -357 324 878 N ATOM 363 CA THR A 48 77.523 63.845 54.969 1.00 27.79 C ANISOU 363 CA THR F 48 3417 3989 3153 -39 813 442 C ATOM 364 C THR A 48 78.285 64.391 56.175 1.00 28.17 C ANISOU 364 C THR F 48 3178 4078 3446 -129 980 221 C ATOM 365 O THR A 48 77.736 65.147 56.973 1.00 30.90 O ANISOU 365 O THR F 48 4012 4516 3213 -461 995 -116 O ATOM 366 CB THR A 48 77.074 62.394 55.224 1.00 28.55 C ANISOU 366 CB THR F 48 3209 4227 3412 -173 1019 -331 C ATOM 367 OG1 THR A 48 76.236 61.965 54.145 1.00 29.67 O ANISOU 367 OG1 THR F 48 3288 4736 3250 -144 689 174 O ATOM 368 CG2 THR A 48 76.231 62.280 56.483 1.00 27.34 C ANISOU 368 CG2 THR F 48 3844 3330 3213 -240 602 305 C ATOM 369 N TYR A 49 79.550 64.035 56.345 1.00 29.41 N ANISOU 369 N TYR F 49 3728 4195 3251 -350 798 446 N ATOM 370 CA TYR A 49 80.412 64.518 57.420 1.00 29.62 C ANISOU 370 CA TYR F 49 3529 4508 3217 -357 716 488 C ATOM 371 C TYR A 49 80.569 66.033 57.313 1.00 31.06 C ANISOU 371 C TYR F 49 3479 4980 3342 -281 483 -129 C ATOM 372 O TYR A 49 80.449 66.779 58.290 1.00 32.01 O ANISOU 372 O TYR F 49 3581 5256 3326 -193 493 -166 O ATOM 373 CB TYR A 49 81.773 63.816 57.395 1.00 28.70 C ANISOU 373 CB TYR F 49 3729 4516 2661 -593 763 432 C ATOM 374 CG TYR A 49 81.680 62.371 57.837 1.00 28.86 C ANISOU 374 CG TYR F 49 3899 4225 2843 -562 643 535 C ATOM 375 CD1 TYR A 49 81.019 62.029 59.019 1.00 29.67 C ANISOU 375 CD1 TYR F 49 3644 4428 3202 -472 600 139 C ATOM 376 CD2 TYR A 49 82.244 61.341 57.093 1.00 28.94 C ANISOU 376 CD2 TYR F 49 4228 4131 2636 -369 435 627 C ATOM 377 CE1 TYR A 49 80.933 60.703 59.430 1.00 30.68 C ANISOU 377 CE1 TYR F 49 4273 3965 3417 -273 178 282 C ATOM 378 CE2 TYR A 49 82.165 60.001 57.490 1.00 29.44 C ANISOU 378 CE2 TYR F 49 4204 4244 2736 -319 475 638 C ATOM 379 CZ TYR A 49 81.503 59.705 58.659 1.00 30.49 C ANISOU 379 CZ TYR F 49 4441 3847 3297 -119 27 397 C ATOM 380 OH TYR A 49 81.405 58.402 59.082 1.00 29.81 O ANISOU 380 OH TYR F 49 4119 4185 3023 -249 372 598 O ATOM 381 N LYS A 50 80.817 66.502 56.085 1.00 30.55 N ANISOU 381 N LYS F 50 3676 4614 3316 -206 455 -43 N ATOM 382 CA LYS A 50 80.923 67.944 55.866 1.00 33.48 C ANISOU 382 CA LYS F 50 3763 4868 4090 -138 300 528 C ATOM 383 C LYS A 50 79.646 68.634 56.333 1.00 34.21 C ANISOU 383 C LYS F 50 3396 4891 4709 5 747 390 C ATOM 384 O LYS A 50 79.717 69.665 57.026 1.00 34.90 O ANISOU 384 O LYS F 50 3537 5537 4188 130 643 348 O ATOM 385 CB LYS A 50 81.219 68.245 54.398 1.00 36.30 C ANISOU 385 CB LYS F 50 3582 6026 4183 140 229 363 C ATOM 386 CG LYS A 50 80.958 69.691 54.011 1.00 44.99 C ANISOU 386 CG LYS F 50 4759 6862 5473 802 -824 439 C ATOM 387 CD LYS A 50 80.903 69.862 52.499 1.00 58.15 C ANISOU 387 CD LYS F 50 7857 8435 5801 -219 -2354 1304 C ATOM 388 CE LYS A 50 80.879 71.310 52.023 1.00 62.07 C ANISOU 388 CE LYS F 50 7631 9259 6695 -492 -3182 1119 C ATOM 389 NZ LYS A 50 82.011 71.674 51.129 1.00 67.58 N ANISOU 389 NZ LYS F 50 6656 10188 8835 -1236 -2240 -114 N ATOM 390 N ALA A 51 78.472 68.111 55.991 1.00 33.07 N ANISOU 390 N ALA F 51 3618 4766 4180 -56 576 739 N ATOM 391 CA ALA A 51 77.234 68.737 56.441 1.00 38.48 C ANISOU 391 CA ALA F 51 5429 4882 4308 -518 249 671 C ATOM 392 C ALA A 51 76.987 68.563 57.934 1.00 37.45 C ANISOU 392 C ALA F 51 5427 4726 4077 -234 819 774 C ATOM 393 O ALA A 51 76.474 69.465 58.620 1.00 39.04 O ANISOU 393 O ALA F 51 5435 4712 4686 -181 578 452 O ATOM 394 CB ALA A 51 76.048 68.162 55.669 1.00 38.64 C ANISOU 394 CB ALA F 51 6696 4148 3837 -483 1315 -169 C ATOM 395 N LEU A 52 77.331 67.396 58.490 1.00 35.68 N ANISOU 395 N LEU F 52 5046 4696 3814 -349 927 699 N ATOM 396 CA LEU A 52 77.183 67.232 59.935 1.00 33.57 C ANISOU 396 CA LEU F 52 4097 4791 3867 -151 930 194 C ATOM 397 C LEU A 52 78.029 68.271 60.672 1.00 36.49 C ANISOU 397 C LEU F 52 4286 5492 4087 -463 1111 -39 C ATOM 398 O LEU A 52 77.589 68.920 61.626 1.00 38.80 O ANISOU 398 O LEU F 52 4941 5301 4500 -245 1690 70 O ATOM 399 CB LEU A 52 77.609 65.832 60.363 1.00 35.41 C ANISOU 399 CB LEU F 52 4291 4751 4413 -274 184 39 C ATOM 400 CG LEU A 52 76.562 64.737 60.449 1.00 38.29 C ANISOU 400 CG LEU F 52 4407 4980 5163 -433 -340 505 C ATOM 401 CD1 LEU A 52 77.213 63.410 60.815 1.00 45.21 C ANISOU 401 CD1 LEU F 52 4596 5953 6630 -275 -507 2054 C ATOM 402 CD2 LEU A 52 75.471 65.125 61.447 1.00 41.23 C ANISOU 402 CD2 LEU F 52 5482 6511 3672 -1048 -925 517 C ATOM 403 N VAL A 53 79.277 68.432 60.233 1.00 34.15 N ANISOU 403 N VAL F 53 3484 5648 3844 -77 -36 542 N ATOM 404 CA VAL A 53 80.136 69.416 60.896 1.00 34.02 C ANISOU 404 CA VAL F 53 3492 5687 3746 6 -38 663 C ATOM 405 C VAL A 53 79.540 70.819 60.887 1.00 35.71 C ANISOU 405 C VAL F 53 3968 5688 3913 210 505 903 C ATOM 406 O VAL A 53 79.574 71.592 61.863 1.00 37.15 O ANISOU 406 O VAL F 53 5239 5205 3671 335 614 801 O ATOM 407 CB VAL A 53 81.502 69.383 60.194 1.00 34.43 C ANISOU 407 CB VAL F 53 3146 5744 4193 115 -316 640 C ATOM 408 CG1 VAL A 53 82.333 70.597 60.581 1.00 34.38 C ANISOU 408 CG1 VAL F 53 3037 5677 4350 336 -480 1600 C ATOM 409 CG2 VAL A 53 82.197 68.078 60.550 1.00 32.94 C ANISOU 409 CG2 VAL F 53 3012 5751 3754 300 394 532 C ATOM 410 N GLU A 54 78.955 71.152 59.737 1.00 36.62 N ANISOU 410 N GLU F 54 4243 5648 4023 367 921 994 N ATOM 411 CA GLU A 54 78.347 72.447 59.499 1.00 37.38 C ANISOU 411 CA GLU F 54 4634 5511 4059 340 472 836 C ATOM 412 C GLU A 54 77.205 72.693 60.489 1.00 38.61 C ANISOU 412 C GLU F 54 4553 5914 4205 351 560 489 C ATOM 413 O GLU A 54 77.097 73.758 61.113 1.00 41.06 O ANISOU 413 O GLU F 54 4916 6097 4589 -34 1338 407 O ATOM 414 CB GLU A 54 77.826 72.583 58.058 1.00 41.10 C ANISOU 414 CB GLU F 54 5125 6523 3967 353 -3 1093 C ATOM 415 CG GLU A 54 78.701 73.358 57.103 1.00 58.89 C ANISOU 415 CG GLU F 54 8324 8511 5542 -1348 -2116 1608 C ATOM 416 CD GLU A 54 78.380 73.112 55.638 1.00 65.60 C ANISOU 416 CD GLU F 54 9639 10092 5195 -2264 -2694 1559 C ATOM 417 OE1 GLU A 54 77.433 72.370 55.287 1.00 88.06 O ANISOU 417 OE1 GLU F 54 13342 12442 7675 -5923 49 1437 O ATOM 418 OE2 GLU A 54 79.090 73.676 54.769 1.00 87.65 O ANISOU 418 OE2 GLU F 54 14582 11984 6736 -3012 -5420 578 O ATOM 419 N MET A 55 76.355 71.681 60.608 1.00 39.25 N ANISOU 419 N MET F 55 4572 5933 4408 388 290 604 N ATOM 420 CA MET A 55 75.214 71.789 61.512 1.00 40.82 C ANISOU 420 CA MET F 55 5468 5886 4156 -399 382 995 C ATOM 421 C MET A 55 75.639 71.929 62.968 1.00 40.32 C ANISOU 421 C MET F 55 5277 5804 4237 -258 593 957 C ATOM 422 O MET A 55 75.012 72.600 63.806 1.00 41.77 O ANISOU 422 O MET F 55 5137 5985 4748 -205 1262 839 O ATOM 423 CB MET A 55 74.349 70.537 61.311 1.00 37.31 C ANISOU 423 CB MET F 55 5429 5474 3274 -54 447 305 C ATOM 424 CG MET A 55 73.757 70.495 59.904 1.00 37.55 C ANISOU 424 CG MET F 55 5293 5936 3040 76 223 264 C ATOM 425 SD MET A 55 72.676 69.067 59.687 1.00 42.14 S ANISOU 425 SD MET F 55 5526 5570 4915 -157 981 545 S ATOM 426 CE MET A 55 71.193 69.621 60.545 1.00 45.49 C ANISOU 426 CE MET F 55 6271 6996 4015 -1031 738 -217 C ATOM 427 N HIS A 56 76.745 71.248 63.283 1.00 40.28 N ANISOU 427 N HIS F 56 4606 5840 4861 -327 1653 1152 N ATOM 428 CA HIS A 56 77.317 71.301 64.631 1.00 36.50 C ANISOU 428 CA HIS F 56 4299 5254 4317 438 1371 679 C ATOM 429 C HIS A 56 77.784 72.720 64.897 1.00 37.39 C ANISOU 429 C HIS F 56 4325 5505 4376 325 1460 -163 C ATOM 430 O HIS A 56 77.560 73.382 65.910 1.00 42.59 O ANISOU 430 O HIS F 56 5264 6224 4696 -194 2341 -302 O ATOM 431 CB HIS A 56 78.496 70.329 64.765 1.00 35.48 C ANISOU 431 CB HIS F 56 4505 5119 3858 263 1363 337 C ATOM 432 CG HIS A 56 79.201 70.531 66.079 1.00 35.58 C ANISOU 432 CG HIS F 56 4589 4952 3976 201 1449 293 C ATOM 433 ND1 HIS A 56 78.564 70.410 67.298 1.00 35.66 N ANISOU 433 ND1 HIS F 56 4452 5245 3851 87 1267 567 N ATOM 434 CD2 HIS A 56 80.479 70.872 66.360 1.00 37.60 C ANISOU 434 CD2 HIS F 56 5221 4959 4106 -114 1382 360 C ATOM 435 CE1 HIS A 56 79.419 70.654 68.272 1.00 37.12 C ANISOU 435 CE1 HIS F 56 4915 5180 4010 -158 1590 277 C ATOM 436 NE2 HIS A 56 80.597 70.937 67.738 1.00 37.17 N ANISOU 436 NE2 HIS F 56 4672 5325 4126 -86 1582 188 N ATOM 437 N LYS A 57 78.499 73.230 63.884 1.00 41.30 N ANISOU 437 N LYS F 57 4464 6290 4937 -121 1128 -94 N ATOM 438 CA LYS A 57 79.036 74.588 64.058 1.00 43.41 C ANISOU 438 CA LYS F 57 4456 6226 5813 -116 1049 104 C ATOM 439 C LYS A 57 77.898 75.585 64.106 1.00 44.80 C ANISOU 439 C LYS F 57 4939 6334 5749 138 1462 5 C ATOM 440 O LYS A 57 77.990 76.629 64.752 1.00 50.05 O ANISOU 440 O LYS F 57 5462 6879 6674 355 2127 44 O ATOM 441 CB LYS A 57 80.071 74.868 62.962 1.00 44.48 C ANISOU 441 CB LYS F 57 4340 6575 5985 166 906 -158 C ATOM 442 CG LYS A 57 81.203 73.840 63.020 1.00 51.01 C ANISOU 442 CG LYS F 57 6070 6341 6971 -158 1498 -455 C ATOM 443 CD LYS A 57 82.327 74.216 62.075 1.00 56.88 C ANISOU 443 CD LYS F 57 6968 7301 7343 -997 1728 -1021 C ATOM 444 CE LYS A 57 83.678 73.947 62.725 1.00 64.05 C ANISOU 444 CE LYS F 57 8349 7361 8627 -1687 2644 -1279 C ATOM 445 NZ LYS A 57 84.803 74.099 61.741 1.00 78.18 N ANISOU 445 NZ LYS F 57 13083 8827 7794 -4030 3470 -2024 N ATOM 446 N ALA A 58 76.769 75.300 63.471 1.00 42.30 N ANISOU 446 N ALA F 58 4369 5980 5724 145 968 -91 N ATOM 447 CA ALA A 58 75.673 76.255 63.489 1.00 42.20 C ANISOU 447 CA ALA F 58 3914 6116 6006 458 1348 -142 C ATOM 448 C ALA A 58 74.898 76.126 64.787 1.00 43.86 C ANISOU 448 C ALA F 58 5241 5672 5750 264 1375 67 C ATOM 449 O ALA A 58 73.880 76.791 64.982 1.00 47.11 O ANISOU 449 O ALA F 58 5609 5777 6512 631 1364 -245 O ATOM 450 CB ALA A 58 74.758 76.022 62.296 1.00 40.88 C ANISOU 450 CB ALA F 58 4030 5802 5701 512 1062 -162 C ATOM 451 N GLY A 59 75.372 75.262 65.673 1.00 42.92 N ANISOU 451 N GLY F 59 4849 5919 5541 87 1691 300 N ATOM 452 CA GLY A 59 74.718 75.054 66.947 1.00 41.52 C ANISOU 452 CA GLY F 59 5229 5218 5327 449 1947 220 C ATOM 453 C GLY A 59 73.468 74.204 66.836 1.00 42.22 C ANISOU 453 C GLY F 59 5145 5719 5179 358 1743 -268 C ATOM 454 O GLY A 59 72.586 74.335 67.705 1.00 50.77 O ANISOU 454 O GLY F 59 6546 7108 5637 -812 2419 -1105 O ATOM 455 N GLN A 60 73.335 73.334 65.823 1.00 40.36 N ANISOU 455 N GLN F 60 5158 5593 4585 343 1617 281 N ATOM 456 CA GLN A 60 72.084 72.572 65.736 1.00 42.17 C ANISOU 456 CA GLN F 60 5305 5372 5345 297 1772 391 C ATOM 457 C GLN A 60 72.177 71.187 66.365 1.00 42.03 C ANISOU 457 C GLN F 60 5129 5202 5637 118 1539 193 C ATOM 458 O GLN A 60 71.210 70.439 66.553 1.00 41.80 O ANISOU 458 O GLN F 60 5215 5402 5265 4 1695 -339 O ATOM 459 CB GLN A 60 71.665 72.447 64.274 1.00 43.43 C ANISOU 459 CB GLN F 60 4704 6522 5274 -49 1679 279 C ATOM 460 CG GLN A 60 71.492 73.766 63.533 1.00 49.81 C ANISOU 460 CG GLN F 60 5483 7271 6171 -728 312 1074 C ATOM 461 CD GLN A 60 71.416 73.553 62.032 1.00 56.33 C ANISOU 461 CD GLN F 60 6998 8291 6113 -1600 309 1365 C ATOM 462 OE1 GLN A 60 70.670 72.701 61.552 1.00 64.84 O ANISOU 462 OE1 GLN F 60 8153 10132 6352 -3034 1176 828 O ATOM 463 NE2 GLN A 60 72.177 74.290 61.238 1.00 65.00 N ANISOU 463 NE2 GLN F 60 7738 10357 6604 -1472 135 -715 N ATOM 464 N VAL A 61 73.402 70.792 66.726 1.00 40.33 N ANISOU 464 N VAL F 61 4988 4883 5451 458 1903 -213 N ATOM 465 CA VAL A 61 73.580 69.450 67.274 1.00 38.51 C ANISOU 465 CA VAL F 61 4772 5192 4668 108 1718 -6 C ATOM 466 C VAL A 61 74.851 69.386 68.109 1.00 38.79 C ANISOU 466 C VAL F 61 4662 5459 4616 53 1839 17 C ATOM 467 O VAL A 61 75.873 70.025 67.873 1.00 38.01 O ANISOU 467 O VAL F 61 5177 5154 4111 -178 1776 -439 O ATOM 468 CB VAL A 61 73.615 68.415 66.130 1.00 35.87 C ANISOU 468 CB VAL F 61 3459 5851 4319 38 1149 136 C ATOM 469 CG1 VAL A 61 74.873 68.580 65.284 1.00 34.05 C ANISOU 469 CG1 VAL F 61 3899 4739 4300 -57 1588 390 C ATOM 470 CG2 VAL A 61 73.549 66.969 66.615 1.00 38.36 C ANISOU 470 CG2 VAL F 61 4114 5000 5463 207 905 784 C ATOM 471 N SER A 62 74.797 68.564 69.145 1.00 37.71 N ANISOU 471 N SER F 62 5016 5335 3977 -210 1931 -311 N ATOM 472 CA SER A 62 75.978 68.310 69.955 1.00 37.37 C ANISOU 472 CA SER F 62 5117 5136 3946 -253 1835 -455 C ATOM 473 C SER A 62 76.281 66.813 69.983 1.00 36.60 C ANISOU 473 C SER F 62 4929 5187 3790 -330 1269 -663 C ATOM 474 O SER A 62 75.341 66.010 70.060 1.00 36.49 O ANISOU 474 O SER F 62 5074 5273 3517 -543 949 191 O ATOM 475 CB SER A 62 75.762 68.865 71.365 1.00 38.05 C ANISOU 475 CB SER F 62 5419 5105 3934 -500 1942 -461 C ATOM 476 OG SER A 62 76.911 68.572 72.137 1.00 39.31 O ANISOU 476 OG SER F 62 5994 5146 3794 -33 1566 -189 O ATOM 477 N PHE A 63 77.555 66.450 69.929 1.00 34.91 N ANISOU 477 N PHE F 63 4813 5129 3321 -286 441 -70 N ATOM 478 CA PHE A 63 77.943 65.049 69.997 1.00 36.39 C ANISOU 478 CA PHE F 63 4612 5181 4035 -376 400 135 C ATOM 479 C PHE A 63 78.500 64.669 71.368 1.00 36.50 C ANISOU 479 C PHE F 63 4735 4958 4175 -34 786 186 C ATOM 480 O PHE A 63 79.084 63.579 71.474 1.00 38.39 O ANISOU 480 O PHE F 63 5144 4391 5052 -390 1827 750 O ATOM 481 CB PHE A 63 78.964 64.754 68.891 1.00 36.21 C ANISOU 481 CB PHE F 63 4572 4909 4277 -185 524 46 C ATOM 482 CG PHE A 63 78.297 64.922 67.519 1.00 36.61 C ANISOU 482 CG PHE F 63 4825 4951 4133 -434 306 -78 C ATOM 483 CD1 PHE A 63 77.495 63.932 66.984 1.00 36.87 C ANISOU 483 CD1 PHE F 63 5009 5238 3761 -73 617 -241 C ATOM 484 CD2 PHE A 63 78.485 66.084 66.799 1.00 37.65 C ANISOU 484 CD2 PHE F 63 5038 4681 4585 -129 290 152 C ATOM 485 CE1 PHE A 63 76.852 64.058 65.762 1.00 33.38 C ANISOU 485 CE1 PHE F 63 4701 4616 3368 641 566 -647 C ATOM 486 CE2 PHE A 63 77.868 66.239 65.585 1.00 35.30 C ANISOU 486 CE2 PHE F 63 4691 4592 4131 692 760 -337 C ATOM 487 CZ PHE A 63 77.064 65.235 65.065 1.00 35.04 C ANISOU 487 CZ PHE F 63 4500 4689 4124 616 532 -552 C ATOM 488 N LYS A 64 78.330 65.513 72.374 1.00 38.20 N ANISOU 488 N LYS F 64 5030 5353 4130 -38 730 -177 N ATOM 489 CA LYS A 64 78.791 65.274 73.731 1.00 40.02 C ANISOU 489 CA LYS F 64 5502 5507 4198 300 823 -81 C ATOM 490 C LYS A 64 78.335 63.935 74.300 1.00 37.29 C ANISOU 490 C LYS F 64 5325 4801 4043 -159 918 157 C ATOM 491 O LYS A 64 79.076 63.257 75.003 1.00 38.94 O ANISOU 491 O LYS F 64 5244 5721 3830 -406 1042 819 O ATOM 492 CB LYS A 64 78.241 66.354 74.676 1.00 46.94 C ANISOU 492 CB LYS F 64 5209 7329 5298 -39 2426 -724 C ATOM 493 CG LYS A 64 79.268 67.119 75.481 1.00 63.62 C ANISOU 493 CG LYS F 64 6935 9358 7882 -2352 3791 -1694 C ATOM 494 CD LYS A 64 80.203 67.911 74.577 1.00 78.52 C ANISOU 494 CD LYS F 64 7690 11352 10791 -3655 2791 -1979 C ATOM 495 CE LYS A 64 80.922 69.029 75.315 1.00 84.39 C ANISOU 495 CE LYS F 64 7679 12216 12171 -4131 3197 -2918 C ATOM 496 NZ LYS A 64 82.406 68.940 75.142 1.00 86.17 N ANISOU 496 NZ LYS F 64 6178 12119 14443 -3347 2915 -3978 N ATOM 497 N HIS A 65 77.085 63.553 74.010 1.00 36.57 N ANISOU 497 N HIS F 65 5551 4340 4002 -26 1786 -468 N ATOM 498 CA HIS A 65 76.604 62.260 74.505 1.00 38.83 C ANISOU 498 CA HIS F 65 5328 5346 4082 -462 1852 -408 C ATOM 499 C HIS A 65 76.230 61.341 73.349 1.00 38.25 C ANISOU 499 C HIS F 65 5120 5684 3728 -1069 1583 -694 C ATOM 500 O HIS A 65 75.252 60.588 73.381 1.00 41.41 O ANISOU 500 O HIS F 65 5806 6432 3494 -2087 1577 86 O ATOM 501 CB HIS A 65 75.427 62.444 75.476 1.00 40.34 C ANISOU 501 CB HIS F 65 5878 5839 3610 -755 1960 -446 C ATOM 502 CG HIS A 65 75.889 63.307 76.628 1.00 40.80 C ANISOU 502 CG HIS F 65 5719 5801 3983 -378 2110 -308 C ATOM 503 ND1 HIS A 65 77.019 62.989 77.347 1.00 43.19 N ANISOU 503 ND1 HIS F 65 6066 5694 4649 -380 2888 -350 N ATOM 504 CD2 HIS A 65 75.417 64.447 77.161 1.00 40.00 C ANISOU 504 CD2 HIS F 65 5536 5771 3890 -317 1611 -476 C ATOM 505 CE1 HIS A 65 77.223 63.892 78.292 1.00 42.44 C ANISOU 505 CE1 HIS F 65 5471 5790 4863 -448 2721 -458 C ATOM 506 NE2 HIS A 65 76.261 64.792 78.201 1.00 41.61 N ANISOU 506 NE2 HIS F 65 5402 5891 4518 -294 2141 -579 N ATOM 507 N VAL A 66 77.032 61.403 72.290 1.00 37.49 N ANISOU 507 N VAL F 66 5759 5103 3382 -1048 1137 -45 N ATOM 508 CA VAL A 66 76.869 60.503 71.149 1.00 32.58 C ANISOU 508 CA VAL F 66 4729 4641 3010 -406 319 -29 C ATOM 509 C VAL A 66 78.041 59.525 71.196 1.00 33.64 C ANISOU 509 C VAL F 66 4180 4617 3983 -624 -195 260 C ATOM 510 O VAL A 66 79.193 59.936 71.330 1.00 33.70 O ANISOU 510 O VAL F 66 4237 4861 3709 -609 849 178 O ATOM 511 CB VAL A 66 76.796 61.235 69.801 1.00 30.79 C ANISOU 511 CB VAL F 66 3995 4534 3171 -53 257 -274 C ATOM 512 CG1 VAL A 66 76.805 60.226 68.664 1.00 28.54 C ANISOU 512 CG1 VAL F 66 3481 4398 2965 -354 114 -163 C ATOM 513 CG2 VAL A 66 75.543 62.095 69.744 1.00 30.17 C ANISOU 513 CG2 VAL F 66 4545 4483 2433 -485 1011 -15 C ATOM 514 N VAL A 67 77.730 58.246 71.113 1.00 31.87 N ANISOU 514 N VAL F 67 4128 4521 3461 -709 -113 361 N ATOM 515 CA VAL A 67 78.754 57.203 71.088 1.00 30.76 C ANISOU 515 CA VAL F 67 4351 4529 2807 -642 557 496 C ATOM 516 C VAL A 67 78.816 56.676 69.667 1.00 32.92 C ANISOU 516 C VAL F 67 5272 4611 2623 -1317 528 447 C ATOM 517 O VAL A 67 77.748 56.505 69.092 1.00 30.50 O ANISOU 517 O VAL F 67 4243 4471 2876 -943 593 329 O ATOM 518 CB VAL A 67 78.423 56.071 72.076 1.00 29.57 C ANISOU 518 CB VAL F 67 4338 4257 2639 -267 644 21 C ATOM 519 CG1 VAL A 67 79.190 54.791 71.798 1.00 30.25 C ANISOU 519 CG1 VAL F 67 3849 4230 3417 -556 1119 -73 C ATOM 520 CG2 VAL A 67 78.668 56.578 73.507 1.00 30.09 C ANISOU 520 CG2 VAL F 67 4433 4375 2624 -348 692 -66 C ATOM 521 N THR A 68 80.003 56.443 69.128 1.00 28.03 N ANISOU 521 N THR F 68 3537 4225 2890 -529 249 556 N ATOM 522 CA THR A 68 80.093 55.960 67.768 1.00 29.02 C ANISOU 522 CA THR F 68 3571 4427 3030 -384 231 247 C ATOM 523 C THR A 68 80.885 54.656 67.675 1.00 30.37 C ANISOU 523 C THR F 68 3931 4335 3271 -363 415 481 C ATOM 524 O THR A 68 81.798 54.438 68.472 1.00 30.55 O ANISOU 524 O THR F 68 3681 5014 2912 -8 120 888 O ATOM 525 CB THR A 68 80.776 56.975 66.823 1.00 29.30 C ANISOU 525 CB THR F 68 3836 4069 3229 -676 13 152 C ATOM 526 OG1 THR A 68 82.127 57.178 67.284 1.00 32.78 O ANISOU 526 OG1 THR F 68 4298 4521 3636 -1125 476 -23 O ATOM 527 CG2 THR A 68 80.096 58.331 66.823 1.00 29.46 C ANISOU 527 CG2 THR F 68 3888 4619 2685 -190 116 216 C ATOM 528 N PHE A 69 80.524 53.856 66.675 1.00 26.17 N ANISOU 528 N PHE F 69 3142 3973 2828 -405 -171 461 N ATOM 529 CA PHE A 69 81.164 52.616 66.283 1.00 28.36 C ANISOU 529 CA PHE F 69 4053 3805 2918 -327 39 377 C ATOM 530 C PHE A 69 81.451 52.670 64.789 1.00 28.95 C ANISOU 530 C PHE F 69 4260 3775 2963 -296 -115 416 C ATOM 531 O PHE A 69 80.500 52.869 63.999 1.00 28.25 O ANISOU 531 O PHE F 69 3897 3916 2922 -395 166 336 O ATOM 532 CB PHE A 69 80.273 51.413 66.590 1.00 27.11 C ANISOU 532 CB PHE F 69 3946 3445 2910 366 -37 248 C ATOM 533 CG PHE A 69 80.208 51.065 68.074 1.00 29.98 C ANISOU 533 CG PHE F 69 4332 4143 2916 -201 -101 390 C ATOM 534 CD1 PHE A 69 79.188 51.534 68.885 1.00 28.94 C ANISOU 534 CD1 PHE F 69 3373 4621 3001 -218 45 10 C ATOM 535 CD2 PHE A 69 81.186 50.258 68.652 1.00 29.05 C ANISOU 535 CD2 PHE F 69 3395 4491 3153 -163 -363 721 C ATOM 536 CE1 PHE A 69 79.161 51.208 70.243 1.00 32.19 C ANISOU 536 CE1 PHE F 69 4194 4791 3244 -637 -524 139 C ATOM 537 CE2 PHE A 69 81.166 49.932 70.010 1.00 29.75 C ANISOU 537 CE2 PHE F 69 3479 4711 3115 -454 -360 666 C ATOM 538 CZ PHE A 69 80.140 50.413 70.813 1.00 30.71 C ANISOU 538 CZ PHE F 69 3704 4962 3002 -824 566 495 C ATOM 539 N ASN A 70 82.706 52.502 64.389 1.00 30.06 N ANISOU 539 N ASN F 70 4586 4001 2834 -680 375 281 N ATOM 540 CA ASN A 70 83.008 52.489 62.950 1.00 29.07 C ANISOU 540 CA ASN F 70 4588 3587 2872 -24 68 333 C ATOM 541 C ASN A 70 82.961 51.071 62.394 1.00 29.49 C ANISOU 541 C ASN F 70 4517 3953 2734 -58 233 569 C ATOM 542 O ASN A 70 83.202 50.093 63.115 1.00 31.09 O ANISOU 542 O ASN F 70 3473 5192 3147 -294 65 920 O ATOM 543 CB ASN A 70 84.376 53.121 62.710 1.00 29.68 C ANISOU 543 CB ASN F 70 4644 4010 2622 -236 660 -339 C ATOM 544 CG ASN A 70 84.210 54.544 62.218 1.00 30.70 C ANISOU 544 CG ASN F 70 4485 4351 2830 -322 261 -659 C ATOM 545 OD1 ASN A 70 83.949 55.442 63.020 1.00 29.40 O ANISOU 545 OD1 ASN F 70 3944 4144 3082 -610 749 -266 O ATOM 546 ND2 ASN A 70 84.362 54.743 60.904 1.00 31.69 N ANISOU 546 ND2 ASN F 70 4365 4965 2709 -885 503 -33 N ATOM 547 N MET A 71 82.659 50.921 61.115 1.00 30.26 N ANISOU 547 N MET F 71 4718 4257 2522 -619 19 126 N ATOM 548 CA MET A 71 82.478 49.629 60.475 1.00 35.32 C ANISOU 548 CA MET F 71 5264 4956 3202 -786 731 -453 C ATOM 549 C MET A 71 83.763 48.814 60.356 1.00 33.84 C ANISOU 549 C MET F 71 4434 4942 3480 -273 159 -110 C ATOM 550 O MET A 71 83.716 47.582 60.419 1.00 34.08 O ANISOU 550 O MET F 71 4080 5334 3533 -667 -539 991 O ATOM 551 CB MET A 71 81.906 49.791 59.041 1.00 33.33 C ANISOU 551 CB MET F 71 4725 4761 3178 347 567 -368 C ATOM 552 CG MET A 71 80.494 50.324 58.968 1.00 39.27 C ANISOU 552 CG MET F 71 5876 5010 4034 -447 1789 -208 C ATOM 553 SD MET A 71 79.691 50.124 57.359 1.00 43.40 S ANISOU 553 SD MET F 71 6840 5791 3859 -207 1793 -100 S ATOM 554 CE MET A 71 81.128 50.118 56.280 1.00 41.95 C ANISOU 554 CE MET F 71 7854 4657 3430 -390 565 1391 C ATOM 555 N ASP A 72 84.904 49.490 60.142 1.00 27.73 N ANISOU 555 N ASP F 72 3999 3840 2697 424 -414 894 N ATOM 556 CA ASP A 72 86.097 48.715 59.844 1.00 33.08 C ANISOU 556 CA ASP F 72 4116 4226 4227 316 867 -224 C ATOM 557 C ASP A 72 87.403 49.477 60.054 1.00 34.95 C ANISOU 557 C ASP F 72 4227 4434 4617 -87 -49 -111 C ATOM 558 O ASP A 72 87.398 50.675 60.360 1.00 34.87 O ANISOU 558 O ASP F 72 4536 4410 4302 -599 1563 41 O ATOM 559 CB ASP A 72 85.981 48.232 58.397 1.00 44.06 C ANISOU 559 CB ASP F 72 8100 4460 4179 -904 1573 -158 C ATOM 560 CG ASP A 72 85.356 49.217 57.436 1.00 45.45 C ANISOU 560 CG ASP F 72 7717 5146 4405 -817 1610 227 C ATOM 561 OD1 ASP A 72 85.508 50.454 57.589 1.00 53.37 O ANISOU 561 OD1 ASP F 72 7062 6641 6577 -863 359 -146 O ATOM 562 OD2 ASP A 72 84.695 48.753 56.487 1.00 51.96 O ANISOU 562 OD2 ASP F 72 9349 5745 4650 -1909 1927 489 O ATOM 563 N GLU A 73 88.515 48.754 59.893 1.00 36.89 N ANISOU 563 N GLU F 73 5316 4442 4257 -233 830 -91 N ATOM 564 CA GLU A 73 89.881 49.258 59.991 1.00 39.23 C ANISOU 564 CA GLU F 73 6067 4619 4219 -758 722 -146 C ATOM 565 C GLU A 73 90.853 48.295 59.311 1.00 37.56 C ANISOU 565 C GLU F 73 5713 4623 3935 -492 333 21 C ATOM 566 O GLU A 73 90.652 47.075 59.269 1.00 40.77 O ANISOU 566 O GLU F 73 5444 5701 4344 -700 972 -594 O ATOM 567 CB GLU A 73 90.269 49.504 61.454 1.00 34.97 C ANISOU 567 CB GLU F 73 4785 4198 4304 107 553 228 C ATOM 568 CG GLU A 73 91.636 50.123 61.691 1.00 42.01 C ANISOU 568 CG GLU F 73 5410 5682 4869 -845 554 426 C ATOM 569 CD GLU A 73 91.854 51.490 61.046 1.00 41.86 C ANISOU 569 CD GLU F 73 5233 6069 4603 -1168 280 -224 C ATOM 570 OE1 GLU A 73 92.115 51.513 59.814 1.00 39.20 O ANISOU 570 OE1 GLU F 73 4960 5439 4493 -1399 763 -263 O ATOM 571 OE2 GLU A 73 91.768 52.507 61.806 1.00 38.00 O ANISOU 571 OE2 GLU F 73 4982 6112 3345 -1143 204 643 O ATOM 572 N TYR A 74 91.930 48.862 58.753 1.00 37.36 N ANISOU 572 N TYR F 74 5673 4875 3647 -565 541 -202 N ATOM 573 CA TYR A 74 92.987 48.041 58.184 1.00 41.28 C ANISOU 573 CA TYR F 74 5667 5053 4964 -481 541 -711 C ATOM 574 C TYR A 74 93.791 47.332 59.266 1.00 41.19 C ANISOU 574 C TYR F 74 5495 4709 5448 -293 751 -648 C ATOM 575 O TYR A 74 94.061 47.874 60.351 1.00 39.71 O ANISOU 575 O TYR F 74 5055 4567 5465 -126 667 -328 O ATOM 576 CB TYR A 74 93.971 48.869 57.369 1.00 41.08 C ANISOU 576 CB TYR F 74 5489 4886 5233 -454 679 -990 C ATOM 577 CG TYR A 74 93.447 49.325 56.032 1.00 43.17 C ANISOU 577 CG TYR F 74 6067 5477 4860 -1198 336 -1187 C ATOM 578 CD1 TYR A 74 93.026 48.436 55.059 1.00 45.76 C ANISOU 578 CD1 TYR F 74 6685 5643 5060 -1237 755 -1295 C ATOM 579 CD2 TYR A 74 93.379 50.685 55.755 1.00 43.30 C ANISOU 579 CD2 TYR F 74 5970 6098 4385 -1347 42 -628 C ATOM 580 CE1 TYR A 74 92.554 48.914 53.850 1.00 50.27 C ANISOU 580 CE1 TYR F 74 7361 6441 5297 -1381 916 -798 C ATOM 581 CE2 TYR A 74 92.911 51.168 54.553 1.00 46.74 C ANISOU 581 CE2 TYR F 74 6844 6625 4291 -1476 254 -474 C ATOM 582 CZ TYR A 74 92.493 50.269 53.592 1.00 50.91 C ANISOU 582 CZ TYR F 74 7258 7085 5001 -1429 845 -134 C ATOM 583 OH TYR A 74 92.024 50.747 52.383 1.00 55.75 O ANISOU 583 OH TYR F 74 8276 8611 4294 -813 895 -463 O ATOM 584 N VAL A 75 94.176 46.105 58.937 1.00 42.13 N ANISOU 584 N VAL F 75 4919 5224 5863 -261 738 -759 N ATOM 585 CA VAL A 75 95.009 45.327 59.857 1.00 47.19 C ANISOU 585 CA VAL F 75 5788 5097 7045 -33 166 -493 C ATOM 586 C VAL A 75 96.480 45.662 59.608 1.00 48.55 C ANISOU 586 C VAL F 75 6285 5224 6940 -454 735 -542 C ATOM 587 O VAL A 75 96.848 45.741 58.425 1.00 48.47 O ANISOU 587 O VAL F 75 5693 5860 6862 -1170 726 -226 O ATOM 588 CB VAL A 75 94.765 43.817 59.681 1.00 48.86 C ANISOU 588 CB VAL F 75 6013 5205 7348 131 647 -104 C ATOM 589 CG1 VAL A 75 95.906 43.020 60.307 1.00 53.29 C ANISOU 589 CG1 VAL F 75 6667 5126 8455 481 1334 91 C ATOM 590 CG2 VAL A 75 93.419 43.381 60.259 1.00 43.92 C ANISOU 590 CG2 VAL F 75 5319 5653 5715 67 1547 -167 C ATOM 591 N GLY A 76 97.278 45.864 60.642 1.00 50.75 N ANISOU 591 N GLY F 76 7221 5344 6717 -516 356 -120 N ATOM 592 CA GLY A 76 98.710 46.076 60.590 1.00 50.36 C ANISOU 592 CA GLY F 76 6827 5542 6765 -498 1207 -437 C ATOM 593 C GLY A 76 99.159 47.434 60.109 1.00 52.70 C ANISOU 593 C GLY F 76 6657 6001 7365 -559 1338 -104 C ATOM 594 O GLY A 76 100.336 47.734 59.887 1.00 53.35 O ANISOU 594 O GLY F 76 6451 6305 7513 -727 1657 -39 O ATOM 595 N LEU A 77 98.217 48.347 59.910 1.00 51.62 N ANISOU 595 N LEU F 77 6184 6058 7372 -182 2057 -442 N ATOM 596 CA LEU A 77 98.571 49.699 59.482 1.00 51.42 C ANISOU 596 CA LEU F 77 6268 6170 7100 -353 1735 -602 C ATOM 597 C LEU A 77 98.712 50.524 60.747 1.00 48.97 C ANISOU 597 C LEU F 77 5514 6321 6772 -359 1217 -704 C ATOM 598 O LEU A 77 97.813 50.393 61.592 1.00 53.77 O ANISOU 598 O LEU F 77 7868 6544 6016 -2227 1383 112 O ATOM 599 CB LEU A 77 97.475 50.215 58.577 1.00 52.44 C ANISOU 599 CB LEU F 77 7136 6167 6620 -351 1335 -752 C ATOM 600 CG LEU A 77 97.794 51.084 57.372 1.00 54.52 C ANISOU 600 CG LEU F 77 7227 5709 7779 133 600 -1018 C ATOM 601 CD1 LEU A 77 97.001 52.385 57.447 1.00 54.85 C ANISOU 601 CD1 LEU F 77 5875 7127 7838 795 1700 -2120 C ATOM 602 CD2 LEU A 77 99.279 51.376 57.258 1.00 59.94 C ANISOU 602 CD2 LEU F 77 7100 6902 8774 -680 -44 781 C ATOM 603 N PRO A 78 99.750 51.323 60.948 1.00 49.97 N ANISOU 603 N PRO F 78 5464 6640 6884 -337 1061 -178 N ATOM 604 CA PRO A 78 99.790 52.145 62.174 1.00 51.66 C ANISOU 604 CA PRO F 78 5460 6928 7242 -311 1309 -262 C ATOM 605 C PRO A 78 98.604 53.108 62.235 1.00 48.74 C ANISOU 605 C PRO F 78 5262 6812 6445 -642 1623 -73 C ATOM 606 O PRO A 78 98.311 53.759 61.226 1.00 51.65 O ANISOU 606 O PRO F 78 6508 6970 6146 -1049 2070 410 O ATOM 607 CB PRO A 78 101.101 52.912 62.039 1.00 54.45 C ANISOU 607 CB PRO F 78 6132 6946 7612 -961 1705 -379 C ATOM 608 CG PRO A 78 101.916 52.139 61.058 1.00 52.18 C ANISOU 608 CG PRO F 78 5589 6980 7258 -538 1438 -211 C ATOM 609 CD PRO A 78 100.939 51.513 60.104 1.00 49.69 C ANISOU 609 CD PRO F 78 5322 6615 6941 -498 978 73 C ATOM 610 N LYS A 79 97.924 53.219 63.368 1.00 48.19 N ANISOU 610 N LYS F 79 5083 7123 6104 -876 2386 -94 N ATOM 611 CA LYS A 79 96.770 54.097 63.510 1.00 54.40 C ANISOU 611 CA LYS F 79 7407 6964 6298 -1288 1942 -134 C ATOM 612 C LYS A 79 97.039 55.508 62.999 1.00 53.90 C ANISOU 612 C LYS F 79 7398 6095 6984 -536 2690 4 C ATOM 613 O LYS A 79 96.190 56.126 62.345 1.00 58.96 O ANISOU 613 O LYS F 79 8627 5807 7968 -892 2034 91 O ATOM 614 CB LYS A 79 96.331 54.170 64.976 1.00 64.52 C ANISOU 614 CB LYS F 79 10277 7584 6653 -3394 1702 -620 C ATOM 615 CG LYS A 79 95.340 53.098 65.399 1.00 81.09 C ANISOU 615 CG LYS F 79 12443 9681 8687 -6045 205 -51 C ATOM 616 CD LYS A 79 94.582 53.507 66.663 1.00 94.67 C ANISOU 616 CD LYS F 79 16385 10464 9120 -7758 -149 -552 C ATOM 617 CE LYS A 79 93.484 52.510 67.015 1.00100.31 C ANISOU 617 CE LYS F 79 17239 10681 10196 -8238 -1562 180 C ATOM 618 NZ LYS A 79 92.174 53.123 67.404 1.00 99.23 N ANISOU 618 NZ LYS F 79 16487 9198 12017 -7898 -3093 3219 N ATOM 619 N GLU A 80 98.211 56.070 63.274 1.00 55.66 N ANISOU 619 N GLU F 80 7175 6753 7220 -583 2365 620 N ATOM 620 CA GLU A 80 98.500 57.423 62.803 1.00 59.52 C ANISOU 620 CA GLU F 80 7348 7740 7526 -424 2377 1678 C ATOM 621 C GLU A 80 98.875 57.465 61.328 1.00 58.33 C ANISOU 621 C GLU F 80 7538 6988 7636 -723 2023 1750 C ATOM 622 O GLU A 80 99.166 58.551 60.810 1.00 60.27 O ANISOU 622 O GLU F 80 7470 6869 8561 -1035 1553 1201 O ATOM 623 CB GLU A 80 99.622 58.102 63.605 1.00 68.18 C ANISOU 623 CB GLU F 80 7326 10033 8545 -363 3156 1880 C ATOM 624 CG GLU A 80 99.144 59.340 64.355 1.00 79.36 C ANISOU 624 CG GLU F 80 8602 11058 10492 -46 4197 1108 C ATOM 625 CD GLU A 80 99.580 60.685 63.814 1.00 85.38 C ANISOU 625 CD GLU F 80 8638 11323 12480 946 4294 1367 C ATOM 626 OE1 GLU A 80 100.275 61.453 64.536 1.00 99.94 O ANISOU 626 OE1 GLU F 80 8592 11873 17506 -1411 5570 441 O ATOM 627 OE2 GLU A 80 99.226 61.010 62.653 1.00102.82 O ANISOU 627 OE2 GLU F 80 12178 12381 14509 1275 2104 3815 O ATOM 628 N HIS A 81 98.887 56.353 60.603 1.00 57.52 N ANISOU 628 N HIS F 81 7404 6948 7504 -1180 1928 1251 N ATOM 629 CA HIS A 81 99.029 56.506 59.146 1.00 55.43 C ANISOU 629 CA HIS F 81 5668 7555 7838 -647 972 401 C ATOM 630 C HIS A 81 97.852 57.341 58.659 1.00 51.01 C ANISOU 630 C HIS F 81 5461 7634 6288 -559 567 149 C ATOM 631 O HIS A 81 96.704 57.180 59.083 1.00 45.52 O ANISOU 631 O HIS F 81 5018 7368 4909 -184 648 374 O ATOM 632 CB HIS A 81 99.098 55.143 58.463 1.00 57.02 C ANISOU 632 CB HIS F 81 6080 7270 8314 -800 939 -523 C ATOM 633 CG HIS A 81 99.272 55.205 56.978 1.00 60.06 C ANISOU 633 CG HIS F 81 6354 8163 8302 -1518 1174 -661 C ATOM 634 ND1 HIS A 81 100.463 54.869 56.362 1.00 61.95 N ANISOU 634 ND1 HIS F 81 6815 8307 8417 -1426 1148 -885 N ATOM 635 CD2 HIS A 81 98.462 55.557 55.962 1.00 60.36 C ANISOU 635 CD2 HIS F 81 6050 8619 8265 -1854 520 -442 C ATOM 636 CE1 HIS A 81 100.359 55.014 55.048 1.00 62.89 C ANISOU 636 CE1 HIS F 81 6559 8713 8624 -1590 -243 -604 C ATOM 637 NE2 HIS A 81 99.133 55.438 54.773 1.00 62.21 N ANISOU 637 NE2 HIS F 81 6300 8795 8540 -1619 -512 -427 N ATOM 638 N PRO A 82 98.047 58.279 57.748 1.00 54.15 N ANISOU 638 N PRO F 82 6012 8050 6511 -1228 -93 49 N ATOM 639 CA PRO A 82 96.958 59.169 57.352 1.00 54.66 C ANISOU 639 CA PRO F 82 6053 8363 6353 -1964 -1118 871 C ATOM 640 C PRO A 82 95.804 58.477 56.626 1.00 58.22 C ANISOU 640 C PRO F 82 6080 9549 6492 -2448 -1232 928 C ATOM 641 O PRO A 82 94.712 59.058 56.538 1.00 65.27 O ANISOU 641 O PRO F 82 6657 9514 8628 -3346 -253 386 O ATOM 642 CB PRO A 82 97.635 60.128 56.366 1.00 57.60 C ANISOU 642 CB PRO F 82 6202 8897 6785 -2495 -1300 694 C ATOM 643 CG PRO A 82 99.096 59.997 56.631 1.00 61.64 C ANISOU 643 CG PRO F 82 7485 8655 7281 -2687 -1574 473 C ATOM 644 CD PRO A 82 99.304 58.560 57.047 1.00 61.44 C ANISOU 644 CD PRO F 82 7545 8452 7347 -2048 -486 -22 C ATOM 645 N GLU A 83 96.028 57.280 56.111 1.00 60.08 N ANISOU 645 N GLU F 83 6911 10136 5779 -2649 -491 346 N ATOM 646 CA GLU A 83 95.050 56.478 55.397 1.00 58.75 C ANISOU 646 CA GLU F 83 7323 9833 5165 -2875 -527 401 C ATOM 647 C GLU A 83 94.387 55.435 56.283 1.00 49.36 C ANISOU 647 C GLU F 83 6323 7416 5015 -1136 126 106 C ATOM 648 O GLU A 83 93.497 54.692 55.854 1.00 47.67 O ANISOU 648 O GLU F 83 6268 7574 4270 -680 229 332 O ATOM 649 CB GLU A 83 95.690 55.780 54.194 1.00 72.69 C ANISOU 649 CB GLU F 83 9982 12292 5346 -5237 740 -929 C ATOM 650 CG GLU A 83 95.910 56.704 53.004 1.00 77.05 C ANISOU 650 CG GLU F 83 10408 13710 5159 -4911 703 -1110 C ATOM 651 CD GLU A 83 94.836 57.765 52.861 1.00 80.81 C ANISOU 651 CD GLU F 83 10734 13895 6074 -4907 -9 -221 C ATOM 652 OE1 GLU A 83 93.629 57.446 52.803 1.00 89.49 O ANISOU 652 OE1 GLU F 83 13427 14399 6175 -6529 -398 -45 O ATOM 653 OE2 GLU A 83 95.200 58.965 52.797 1.00 90.04 O ANISOU 653 OE2 GLU F 83 11351 16138 6721 -3189 509 -996 O ATOM 654 N SER A 84 94.750 55.325 57.550 1.00 40.77 N ANISOU 654 N SER F 84 4873 5560 5057 -332 490 -137 N ATOM 655 CA SER A 84 93.979 54.462 58.443 1.00 39.95 C ANISOU 655 CA SER F 84 4506 6067 4608 -437 974 -437 C ATOM 656 C SER A 84 92.556 54.988 58.537 1.00 40.12 C ANISOU 656 C SER F 84 4629 6113 4502 -706 506 137 C ATOM 657 O SER A 84 92.305 56.161 58.225 1.00 39.83 O ANISOU 657 O SER F 84 4325 5873 4937 -1163 135 309 O ATOM 658 CB SER A 84 94.613 54.434 59.831 1.00 36.56 C ANISOU 658 CB SER F 84 3963 5194 4736 -166 963 -458 C ATOM 659 OG SER A 84 94.457 55.687 60.479 1.00 34.84 O ANISOU 659 OG SER F 84 4221 4760 4256 -13 543 -616 O ATOM 660 N TYR A 85 91.622 54.139 58.967 1.00 36.91 N ANISOU 660 N TYR F 85 4557 5925 3540 -512 460 563 N ATOM 661 CA TYR A 85 90.254 54.661 59.084 1.00 38.87 C ANISOU 661 CA TYR F 85 4545 6043 4179 -825 976 304 C ATOM 662 C TYR A 85 90.149 55.549 60.320 1.00 36.56 C ANISOU 662 C TYR F 85 4016 5694 4181 -729 923 584 C ATOM 663 O TYR A 85 89.371 56.509 60.329 1.00 35.47 O ANISOU 663 O TYR F 85 4698 5285 3494 -1150 601 460 O ATOM 664 CB TYR A 85 89.236 53.512 59.063 1.00 41.00 C ANISOU 664 CB TYR F 85 4519 6535 4525 -762 1324 -738 C ATOM 665 CG TYR A 85 89.095 52.871 57.687 1.00 45.44 C ANISOU 665 CG TYR F 85 5347 7087 4830 -1091 1841 -806 C ATOM 666 CD1 TYR A 85 89.792 53.404 56.603 1.00 45.44 C ANISOU 666 CD1 TYR F 85 5931 6893 4440 -1465 2026 -799 C ATOM 667 CD2 TYR A 85 88.297 51.771 57.450 1.00 45.14 C ANISOU 667 CD2 TYR F 85 5301 7010 4841 -551 1953 211 C ATOM 668 CE1 TYR A 85 89.689 52.856 55.351 1.00 45.55 C ANISOU 668 CE1 TYR F 85 5920 6908 4481 -1493 2272 -227 C ATOM 669 CE2 TYR A 85 88.183 51.198 56.202 1.00 45.60 C ANISOU 669 CE2 TYR F 85 5642 6929 4757 -819 2032 397 C ATOM 670 CZ TYR A 85 88.883 51.751 55.166 1.00 46.45 C ANISOU 670 CZ TYR F 85 5882 6851 4915 -1443 2206 28 C ATOM 671 OH TYR A 85 88.801 51.217 53.906 1.00 44.32 O ANISOU 671 OH TYR F 85 5391 6372 5076 -1046 2153 -207 O ATOM 672 N TYR A 86 90.922 55.257 61.370 1.00 34.54 N ANISOU 672 N TYR F 86 3497 5354 4274 -575 813 547 N ATOM 673 CA TYR A 86 91.084 56.164 62.493 1.00 33.41 C ANISOU 673 CA TYR F 86 4260 4623 3814 -451 688 435 C ATOM 674 C TYR A 86 91.371 57.569 61.957 1.00 31.85 C ANISOU 674 C TYR F 86 3948 4639 3515 -459 1061 145 C ATOM 675 O TYR A 86 90.724 58.568 62.322 1.00 35.51 O ANISOU 675 O TYR F 86 3996 5070 4426 -291 1607 -120 O ATOM 676 CB TYR A 86 92.222 55.658 63.372 1.00 36.45 C ANISOU 676 CB TYR F 86 5065 4979 3806 -845 382 679 C ATOM 677 CG TYR A 86 92.781 56.672 64.350 1.00 37.16 C ANISOU 677 CG TYR F 86 5383 4560 4175 -1000 727 667 C ATOM 678 CD1 TYR A 86 92.195 56.782 65.609 1.00 37.49 C ANISOU 678 CD1 TYR F 86 5644 4405 4197 -694 821 588 C ATOM 679 CD2 TYR A 86 93.869 57.499 64.071 1.00 37.27 C ANISOU 679 CD2 TYR F 86 4696 4538 4927 -73 415 567 C ATOM 680 CE1 TYR A 86 92.655 57.681 66.554 1.00 39.99 C ANISOU 680 CE1 TYR F 86 5869 5350 3974 -1235 886 920 C ATOM 681 CE2 TYR A 86 94.335 58.404 65.002 1.00 37.76 C ANISOU 681 CE2 TYR F 86 4554 4612 5179 237 399 437 C ATOM 682 CZ TYR A 86 93.726 58.488 66.239 1.00 41.68 C ANISOU 682 CZ TYR F 86 5611 5481 4744 -869 767 708 C ATOM 683 OH TYR A 86 94.187 59.387 67.177 1.00 41.02 O ANISOU 683 OH TYR F 86 4878 5730 4978 98 398 544 O ATOM 684 N SER A 87 92.375 57.663 61.079 1.00 34.05 N ANISOU 684 N SER F 87 4519 4337 4081 -1045 546 605 N ATOM 685 CA SER A 87 92.837 58.966 60.603 1.00 35.21 C ANISOU 685 CA SER F 87 4647 4861 3871 -770 492 380 C ATOM 686 C SER A 87 91.776 59.661 59.758 1.00 33.45 C ANISOU 686 C SER F 87 4273 4825 3612 -579 739 247 C ATOM 687 O SER A 87 91.569 60.859 59.951 1.00 33.44 O ANISOU 687 O SER F 87 3240 5338 4128 -807 228 544 O ATOM 688 CB SER A 87 94.136 58.854 59.802 1.00 36.43 C ANISOU 688 CB SER F 87 4146 4853 4842 -654 427 102 C ATOM 689 OG SER A 87 95.206 58.576 60.698 1.00 40.72 O ANISOU 689 OG SER F 87 5011 5327 5135 -1476 -398 470 O ATOM 690 N PHE A 88 91.159 58.898 58.856 1.00 33.41 N ANISOU 690 N PHE F 88 3834 4886 3972 -1075 640 82 N ATOM 691 CA PHE A 88 90.049 59.415 58.077 1.00 30.53 C ANISOU 691 CA PHE F 88 3381 4744 3476 -631 655 -81 C ATOM 692 C PHE A 88 89.022 60.012 59.032 1.00 27.74 C ANISOU 692 C PHE F 88 2666 4843 3031 -313 829 50 C ATOM 693 O PHE A 88 88.529 61.109 58.775 1.00 30.41 O ANISOU 693 O PHE F 88 3926 4671 2959 -249 399 384 O ATOM 694 CB PHE A 88 89.389 58.306 57.251 1.00 28.25 C ANISOU 694 CB PHE F 88 3563 3873 3299 -85 756 -130 C ATOM 695 CG PHE A 88 88.124 58.731 56.500 1.00 30.86 C ANISOU 695 CG PHE F 88 3418 4455 3853 -457 419 466 C ATOM 696 CD1 PHE A 88 86.818 58.770 57.009 1.00 31.31 C ANISOU 696 CD1 PHE F 88 4064 4487 3345 -831 875 514 C ATOM 697 CD2 PHE A 88 88.299 59.124 55.176 1.00 32.13 C ANISOU 697 CD2 PHE F 88 3623 4395 4192 -326 -162 629 C ATOM 698 CE1 PHE A 88 85.752 59.211 56.257 1.00 36.09 C ANISOU 698 CE1 PHE F 88 4567 5131 4015 -1525 -609 1295 C ATOM 699 CE2 PHE A 88 87.234 59.546 54.414 1.00 31.90 C ANISOU 699 CE2 PHE F 88 3708 4616 3796 -736 341 500 C ATOM 700 CZ PHE A 88 85.956 59.591 54.931 1.00 33.19 C ANISOU 700 CZ PHE F 88 3783 5050 3779 -1242 -189 845 C ATOM 701 N MET A 89 88.566 59.269 60.042 1.00 29.41 N ANISOU 701 N MET F 89 2935 4876 3362 -421 500 79 N ATOM 702 CA MET A 89 87.428 59.680 60.870 1.00 29.82 C ANISOU 702 CA MET F 89 2897 4849 3585 -631 451 92 C ATOM 703 C MET A 89 87.733 60.938 61.680 1.00 28.85 C ANISOU 703 C MET F 89 3158 4680 3123 -736 546 107 C ATOM 704 O MET A 89 86.866 61.806 61.848 1.00 29.56 O ANISOU 704 O MET F 89 3066 4752 3415 -354 467 598 O ATOM 705 CB MET A 89 86.983 58.552 61.819 1.00 30.13 C ANISOU 705 CB MET F 89 3193 4668 3586 -720 301 308 C ATOM 706 CG MET A 89 86.294 57.407 61.070 1.00 30.03 C ANISOU 706 CG MET F 89 2944 4561 3905 -524 144 731 C ATOM 707 SD MET A 89 84.796 57.980 60.229 1.00 31.40 S ANISOU 707 SD MET F 89 4243 4373 3316 -908 432 245 S ATOM 708 CE MET A 89 83.917 58.748 61.581 1.00 30.87 C ANISOU 708 CE MET F 89 4601 4671 2457 -598 -366 517 C ATOM 709 N HIS A 90 88.964 61.043 62.199 1.00 30.25 N ANISOU 709 N HIS F 90 3395 4865 3233 -852 488 354 N ATOM 710 CA HIS A 90 89.316 62.259 62.937 1.00 31.13 C ANISOU 710 CA HIS F 90 3569 5055 3205 -723 689 800 C ATOM 711 C HIS A 90 89.381 63.457 62.003 1.00 30.39 C ANISOU 711 C HIS F 90 3538 4858 3150 -617 691 477 C ATOM 712 O HIS A 90 88.790 64.518 62.201 1.00 32.67 O ANISOU 712 O HIS F 90 3926 4798 3690 -483 810 703 O ATOM 713 CB HIS A 90 90.646 62.035 63.689 1.00 31.72 C ANISOU 713 CB HIS F 90 3515 5022 3515 -1054 337 785 C ATOM 714 CG HIS A 90 90.392 61.170 64.895 1.00 32.17 C ANISOU 714 CG HIS F 90 4100 4569 3556 -480 217 674 C ATOM 715 ND1 HIS A 90 89.853 61.652 66.071 1.00 29.81 N ANISOU 715 ND1 HIS F 90 3433 4288 3604 -380 177 698 N ATOM 716 CD2 HIS A 90 90.575 59.845 65.112 1.00 33.01 C ANISOU 716 CD2 HIS F 90 4532 4539 3470 -153 107 233 C ATOM 717 CE1 HIS A 90 89.732 60.666 66.951 1.00 28.80 C ANISOU 717 CE1 HIS F 90 3279 3942 3724 65 245 308 C ATOM 718 NE2 HIS A 90 90.167 59.554 66.396 1.00 30.26 N ANISOU 718 NE2 HIS F 90 3720 4212 3567 -19 255 -218 N ATOM 719 N ARG A 91 90.122 63.317 60.913 1.00 33.11 N ANISOU 719 N ARG F 91 4353 4960 3268 -1110 444 493 N ATOM 720 CA ARG A 91 90.307 64.408 59.946 1.00 36.54 C ANISOU 720 CA ARG F 91 4700 5273 3912 -1226 -152 447 C ATOM 721 C ARG A 91 89.013 64.904 59.331 1.00 36.40 C ANISOU 721 C ARG F 91 4322 5316 4192 -652 20 690 C ATOM 722 O ARG A 91 88.880 66.105 59.098 1.00 35.21 O ANISOU 722 O ARG F 91 3853 6253 3272 -721 142 1023 O ATOM 723 CB ARG A 91 91.242 63.902 58.851 1.00 43.09 C ANISOU 723 CB ARG F 91 6615 5891 3866 -2657 -136 202 C ATOM 724 CG ARG A 91 91.308 64.692 57.573 1.00 43.92 C ANISOU 724 CG ARG F 91 6204 5813 4670 -1722 -732 -351 C ATOM 725 CD ARG A 91 92.414 64.114 56.689 1.00 46.77 C ANISOU 725 CD ARG F 91 5724 6840 5208 -1314 -893 -1308 C ATOM 726 NE ARG A 91 92.128 62.798 56.141 1.00 47.83 N ANISOU 726 NE ARG F 91 5608 7281 5286 -1124 -1010 -968 N ATOM 727 CZ ARG A 91 92.804 61.663 56.244 1.00 48.30 C ANISOU 727 CZ ARG F 91 5533 7333 5485 -1133 -564 -607 C ATOM 728 NH1 ARG A 91 93.936 61.566 56.931 1.00 47.57 N ANISOU 728 NH1 ARG F 91 4548 7368 6160 -1242 -543 -593 N ATOM 729 NH2 ARG A 91 92.303 60.596 55.627 1.00 47.84 N ANISOU 729 NH2 ARG F 91 6123 6762 5292 -1219 -18 -561 N ATOM 730 N ASN A 92 88.057 64.027 59.044 1.00 32.32 N ANISOU 730 N ASN F 92 4072 4467 3741 -99 -65 946 N ATOM 731 CA ASN A 92 86.800 64.412 58.396 1.00 30.99 C ANISOU 731 CA ASN F 92 4345 4296 3134 -55 -210 654 C ATOM 732 C ASN A 92 85.662 64.675 59.369 1.00 31.42 C ANISOU 732 C ASN F 92 3701 4645 3593 -93 -208 329 C ATOM 733 O ASN A 92 84.632 65.267 59.015 1.00 32.32 O ANISOU 733 O ASN F 92 4081 4476 3724 -48 596 108 O ATOM 734 CB ASN A 92 86.381 63.329 57.375 1.00 35.51 C ANISOU 734 CB ASN F 92 5302 5141 3048 -289 344 650 C ATOM 735 CG ASN A 92 87.347 63.336 56.206 1.00 38.19 C ANISOU 735 CG ASN F 92 5988 5080 3443 157 113 269 C ATOM 736 OD1 ASN A 92 87.406 64.326 55.472 1.00 43.56 O ANISOU 736 OD1 ASN F 92 7035 5406 4112 539 -878 -301 O ATOM 737 ND2 ASN A 92 88.122 62.287 56.010 1.00 37.21 N ANISOU 737 ND2 ASN F 92 6000 4543 3596 -327 826 925 N ATOM 738 N PHE A 93 85.786 64.270 60.629 1.00 31.32 N ANISOU 738 N PHE F 93 3640 5181 3080 -457 518 137 N ATOM 739 CA PHE A 93 84.633 64.491 61.516 1.00 28.57 C ANISOU 739 CA PHE F 93 3360 4444 3050 -53 634 424 C ATOM 740 C PHE A 93 85.025 64.776 62.955 1.00 29.40 C ANISOU 740 C PHE F 93 3412 4803 2958 61 460 346 C ATOM 741 O PHE A 93 84.710 65.833 63.502 1.00 31.72 O ANISOU 741 O PHE F 93 4734 4118 3201 -208 1108 177 O ATOM 742 CB PHE A 93 83.763 63.234 61.434 1.00 30.39 C ANISOU 742 CB PHE F 93 3405 4753 3391 -284 565 244 C ATOM 743 CG PHE A 93 82.482 63.272 62.243 1.00 31.25 C ANISOU 743 CG PHE F 93 3730 4660 3483 -377 581 243 C ATOM 744 CD1 PHE A 93 81.638 64.371 62.157 1.00 29.95 C ANISOU 744 CD1 PHE F 93 3466 4815 3097 -206 1137 161 C ATOM 745 CD2 PHE A 93 82.146 62.204 63.070 1.00 30.73 C ANISOU 745 CD2 PHE F 93 3209 4834 3633 -91 802 -453 C ATOM 746 CE1 PHE A 93 80.466 64.399 62.884 1.00 31.44 C ANISOU 746 CE1 PHE F 93 3859 4705 3380 -265 1086 121 C ATOM 747 CE2 PHE A 93 80.975 62.226 63.802 1.00 31.69 C ANISOU 747 CE2 PHE F 93 3531 4731 3780 -329 747 -274 C ATOM 748 CZ PHE A 93 80.144 63.330 63.704 1.00 30.27 C ANISOU 748 CZ PHE F 93 3337 4728 3437 -361 1314 -233 C ATOM 749 N PHE A 94 85.703 63.836 63.620 1.00 30.65 N ANISOU 749 N PHE F 94 3692 4745 3207 -184 587 693 N ATOM 750 CA PHE A 94 85.888 64.015 65.058 1.00 30.56 C ANISOU 750 CA PHE F 94 3572 4889 3150 -114 485 514 C ATOM 751 C PHE A 94 86.723 65.264 65.344 1.00 30.65 C ANISOU 751 C PHE F 94 3623 4807 3218 -236 584 160 C ATOM 752 O PHE A 94 86.446 65.943 66.345 1.00 33.71 O ANISOU 752 O PHE F 94 4416 4812 3580 -311 1262 241 O ATOM 753 CB PHE A 94 86.534 62.802 65.716 1.00 30.31 C ANISOU 753 CB PHE F 94 3761 4790 2966 -302 103 374 C ATOM 754 CG PHE A 94 85.824 61.474 65.546 1.00 30.45 C ANISOU 754 CG PHE F 94 3625 4942 3003 -409 -384 421 C ATOM 755 CD1 PHE A 94 84.447 61.378 65.689 1.00 33.40 C ANISOU 755 CD1 PHE F 94 4161 5402 3128 -855 168 -429 C ATOM 756 CD2 PHE A 94 86.555 60.329 65.247 1.00 30.80 C ANISOU 756 CD2 PHE F 94 3484 5250 2967 -482 9 -58 C ATOM 757 CE1 PHE A 94 83.811 60.148 65.535 1.00 33.70 C ANISOU 757 CE1 PHE F 94 4110 5756 2937 -1099 -5 -243 C ATOM 758 CE2 PHE A 94 85.926 59.096 65.096 1.00 31.73 C ANISOU 758 CE2 PHE F 94 3582 5591 2883 -645 582 43 C ATOM 759 CZ PHE A 94 84.551 59.012 65.249 1.00 31.82 C ANISOU 759 CZ PHE F 94 3680 5899 2510 -850 -114 199 C ATOM 760 N ASP A 95 87.693 65.639 64.528 1.00 34.08 N ANISOU 760 N ASP F 95 4049 5597 3304 -634 -44 629 N ATOM 761 CA ASP A 95 88.483 66.844 64.757 1.00 34.35 C ANISOU 761 CA ASP F 95 4079 5311 3660 -767 150 542 C ATOM 762 C ASP A 95 87.620 68.096 64.822 1.00 36.57 C ANISOU 762 C ASP F 95 4287 5317 4292 -783 779 50 C ATOM 763 O ASP A 95 88.096 69.115 65.326 1.00 39.69 O ANISOU 763 O ASP F 95 4476 5756 4849 -983 1093 -549 O ATOM 764 CB ASP A 95 89.500 67.086 63.639 1.00 35.67 C ANISOU 764 CB ASP F 95 3774 5708 4073 -1030 780 -226 C ATOM 765 CG ASP A 95 90.708 66.181 63.667 1.00 34.99 C ANISOU 765 CG ASP F 95 3899 5693 3703 -1159 304 312 C ATOM 766 OD1 ASP A 95 90.860 65.363 64.596 1.00 35.39 O ANISOU 766 OD1 ASP F 95 4277 6282 2888 -1864 648 822 O ATOM 767 OD2 ASP A 95 91.533 66.288 62.734 1.00 33.74 O ANISOU 767 OD2 ASP F 95 4027 5208 3586 -667 131 421 O ATOM 768 N HIS A 96 86.395 68.061 64.317 1.00 36.46 N ANISOU 768 N HIS F 96 4684 5293 3875 -526 734 493 N ATOM 769 CA HIS A 96 85.583 69.264 64.221 1.00 35.36 C ANISOU 769 CA HIS F 96 4348 5461 3624 -367 1275 209 C ATOM 770 C HIS A 96 84.352 69.269 65.101 1.00 35.19 C ANISOU 770 C HIS F 96 4029 5694 3647 -425 1626 -52 C ATOM 771 O HIS A 96 83.599 70.251 65.025 1.00 39.30 O ANISOU 771 O HIS F 96 4650 5773 4509 -187 730 -354 O ATOM 772 CB HIS A 96 85.119 69.441 62.754 1.00 33.49 C ANISOU 772 CB HIS F 96 4456 4624 3644 -211 1455 117 C ATOM 773 CG HIS A 96 86.311 69.241 61.855 1.00 38.62 C ANISOU 773 CG HIS F 96 4939 5649 4085 -462 1172 -559 C ATOM 774 ND1 HIS A 96 87.305 70.182 61.710 1.00 40.50 N ANISOU 774 ND1 HIS F 96 4989 6057 4344 -654 1265 -701 N ATOM 775 CD2 HIS A 96 86.668 68.192 61.078 1.00 40.14 C ANISOU 775 CD2 HIS F 96 5023 6117 4113 -720 1221 -1071 C ATOM 776 CE1 HIS A 96 88.225 69.744 60.881 1.00 39.67 C ANISOU 776 CE1 HIS F 96 4932 6129 4012 -470 882 -603 C ATOM 777 NE2 HIS A 96 87.859 68.533 60.478 1.00 37.90 N ANISOU 777 NE2 HIS F 96 4805 5639 3956 -144 387 -484 N ATOM 778 N VAL A 97 84.130 68.228 65.896 1.00 34.62 N ANISOU 778 N VAL F 97 4461 5321 3373 -477 1494 54 N ATOM 779 CA VAL A 97 82.925 68.231 66.730 1.00 36.46 C ANISOU 779 CA VAL F 97 4874 5289 3692 -460 1178 36 C ATOM 780 C VAL A 97 83.265 67.966 68.193 1.00 35.96 C ANISOU 780 C VAL F 97 4654 5581 3426 -439 1679 -336 C ATOM 781 O VAL A 97 84.434 67.773 68.532 1.00 39.41 O ANISOU 781 O VAL F 97 5804 5797 3372 -914 25 271 O ATOM 782 CB VAL A 97 81.893 67.215 66.210 1.00 35.14 C ANISOU 782 CB VAL F 97 5139 5045 3167 -785 1099 236 C ATOM 783 CG1 VAL A 97 81.494 67.550 64.775 1.00 33.93 C ANISOU 783 CG1 VAL F 97 5390 4646 2856 -222 961 -318 C ATOM 784 CG2 VAL A 97 82.431 65.795 66.303 1.00 34.92 C ANISOU 784 CG2 VAL F 97 4327 5855 3086 -666 223 72 C ATOM 785 N ASP A 98 82.254 67.977 69.059 1.00 36.74 N ANISOU 785 N ASP F 98 4927 5302 3730 -197 1333 -352 N ATOM 786 CA ASP A 98 82.503 67.953 70.499 1.00 34.71 C ANISOU 786 CA ASP F 98 4702 4779 3708 -54 1044 -383 C ATOM 787 C ASP A 98 82.349 66.566 71.119 1.00 35.19 C ANISOU 787 C ASP F 98 4413 4907 4051 -182 914 -851 C ATOM 788 O ASP A 98 81.928 66.454 72.273 1.00 35.65 O ANISOU 788 O ASP F 98 4240 5630 3677 -138 1218 -561 O ATOM 789 CB ASP A 98 81.577 68.929 71.238 1.00 34.30 C ANISOU 789 CB ASP F 98 4389 4744 3901 -267 1045 -509 C ATOM 790 CG ASP A 98 80.106 68.637 70.982 1.00 42.85 C ANISOU 790 CG ASP F 98 6236 5461 4584 -1451 1620 -797 C ATOM 791 OD1 ASP A 98 79.799 67.831 70.068 1.00 41.13 O ANISOU 791 OD1 ASP F 98 5685 5525 4418 -1274 1366 -182 O ATOM 792 OD2 ASP A 98 79.258 69.219 71.695 1.00 40.73 O ANISOU 792 OD2 ASP F 98 6312 4815 4350 -870 814 -248 O ATOM 793 N ILE A 99 82.702 65.527 70.363 1.00 33.19 N ANISOU 793 N ILE F 99 4298 4713 3599 -396 1533 -192 N ATOM 794 CA ILE A 99 82.622 64.193 70.939 1.00 33.90 C ANISOU 794 CA ILE F 99 4695 4378 3809 -187 1492 28 C ATOM 795 C ILE A 99 83.872 63.820 71.747 1.00 36.58 C ANISOU 795 C ILE F 99 5231 4990 3677 -1364 534 289 C ATOM 796 O ILE A 99 85.026 63.987 71.352 1.00 35.36 O ANISOU 796 O ILE F 99 4707 4851 3876 -930 742 -274 O ATOM 797 CB ILE A 99 82.426 63.162 69.821 1.00 35.18 C ANISOU 797 CB ILE F 99 3998 5274 4095 -492 1345 -288 C ATOM 798 CG1 ILE A 99 82.071 61.748 70.297 1.00 34.23 C ANISOU 798 CG1 ILE F 99 4305 4669 4033 -422 1095 -6 C ATOM 799 CG2 ILE A 99 83.677 63.126 68.943 1.00 37.02 C ANISOU 799 CG2 ILE F 99 5269 6154 2643 -704 911 -99 C ATOM 800 CD1 ILE A 99 81.720 60.826 69.127 1.00 34.84 C ANISOU 800 CD1 ILE F 99 4107 4388 4744 -137 1473 605 C ATOM 801 N PRO A 100 83.650 63.262 72.939 1.00 36.88 N ANISOU 801 N PRO F 100 5587 5329 3097 -1531 930 -61 N ATOM 802 CA PRO A 100 84.751 62.819 73.779 1.00 35.29 C ANISOU 802 CA PRO F 100 4840 5035 3535 -1196 356 54 C ATOM 803 C PRO A 100 85.405 61.526 73.307 1.00 36.36 C ANISOU 803 C PRO F 100 4851 5250 3715 -1543 965 -480 C ATOM 804 O PRO A 100 84.745 60.635 72.781 1.00 39.45 O ANISOU 804 O PRO F 100 5703 5877 3407 -1736 1727 -330 O ATOM 805 CB PRO A 100 84.103 62.553 75.149 1.00 33.85 C ANISOU 805 CB PRO F 100 4530 5161 3171 -1211 970 -90 C ATOM 806 CG PRO A 100 82.637 62.507 74.909 1.00 37.64 C ANISOU 806 CG PRO F 100 5633 5438 3229 -1814 917 -195 C ATOM 807 CD PRO A 100 82.331 63.044 73.532 1.00 36.80 C ANISOU 807 CD PRO F 100 5032 5463 3487 -1619 913 121 C ATOM 808 N ALA A 101 86.717 61.404 73.519 1.00 30.99 N ANISOU 808 N ALA F 101 3433 5040 3303 -898 -430 305 N ATOM 809 CA ALA A 101 87.461 60.218 73.125 1.00 33.72 C ANISOU 809 CA ALA F 101 4081 5089 3640 -619 200 736 C ATOM 810 C ALA A 101 86.818 58.953 73.667 1.00 30.88 C ANISOU 810 C ALA F 101 3919 4368 3448 -629 404 347 C ATOM 811 O ALA A 101 86.776 57.912 73.015 1.00 32.77 O ANISOU 811 O ALA F 101 4178 4764 3512 -566 682 392 O ATOM 812 CB ALA A 101 88.902 60.310 73.613 1.00 33.55 C ANISOU 812 CB ALA F 101 3964 5017 3766 -861 593 -5 C ATOM 813 N GLU A 102 86.306 59.014 74.898 1.00 30.35 N ANISOU 813 N GLU F 102 4106 4392 3032 -846 605 806 N ATOM 814 CA GLU A 102 85.813 57.750 75.438 1.00 32.82 C ANISOU 814 CA GLU F 102 4063 5216 3191 -999 506 481 C ATOM 815 C GLU A 102 84.566 57.297 74.695 1.00 31.46 C ANISOU 815 C GLU F 102 3864 4733 3355 -396 864 489 C ATOM 816 O GLU A 102 84.193 56.131 74.802 1.00 34.82 O ANISOU 816 O GLU F 102 3726 5192 4311 -1043 -26 703 O ATOM 817 CB GLU A 102 85.519 57.891 76.928 1.00 35.90 C ANISOU 817 CB GLU F 102 4640 5930 3070 -1466 471 632 C ATOM 818 CG GLU A 102 84.593 59.078 77.174 1.00 42.27 C ANISOU 818 CG GLU F 102 6742 5952 3365 -1389 507 -204 C ATOM 819 CD GLU A 102 84.617 59.463 78.646 1.00 50.47 C ANISOU 819 CD GLU F 102 7995 7533 3648 -1747 1074 -687 C ATOM 820 OE1 GLU A 102 85.158 60.549 78.982 1.00 57.34 O ANISOU 820 OE1 GLU F 102 8278 9155 4353 -1924 1846 -96 O ATOM 821 OE2 GLU A 102 84.089 58.657 79.456 1.00 60.07 O ANISOU 821 OE2 GLU F 102 8655 10831 3336 -3672 902 -1579 O ATOM 822 N ASN A 103 83.923 58.191 73.950 1.00 32.64 N ANISOU 822 N ASN F 103 4396 4734 3272 -404 598 409 N ATOM 823 CA ASN A 103 82.724 57.830 73.203 1.00 33.57 C ANISOU 823 CA ASN F 103 5275 4740 2740 -1027 431 227 C ATOM 824 C ASN A 103 83.020 57.259 71.824 1.00 31.50 C ANISOU 824 C ASN F 103 4370 4610 2987 -737 366 81 C ATOM 825 O ASN A 103 82.098 56.811 71.130 1.00 32.15 O ANISOU 825 O ASN F 103 4006 4785 3422 -525 691 -130 O ATOM 826 CB ASN A 103 81.832 59.070 73.057 1.00 34.34 C ANISOU 826 CB ASN F 103 5232 4745 3072 -912 1374 133 C ATOM 827 CG ASN A 103 81.050 59.383 74.316 1.00 36.60 C ANISOU 827 CG ASN F 103 5288 5096 3522 -883 519 -207 C ATOM 828 OD1 ASN A 103 81.330 58.814 75.378 1.00 35.71 O ANISOU 828 OD1 ASN F 103 5044 5400 3123 -644 1347 -82 O ATOM 829 ND2 ASN A 103 80.077 60.277 74.253 1.00 35.38 N ANISOU 829 ND2 ASN F 103 5136 5176 3130 -685 1303 -224 N ATOM 830 N ILE A 104 84.272 57.253 71.363 1.00 32.91 N ANISOU 830 N ILE F 104 4556 4661 3286 -737 274 -56 N ATOM 831 CA ILE A 104 84.619 56.854 69.997 1.00 31.09 C ANISOU 831 CA ILE F 104 4505 4217 3091 -847 319 231 C ATOM 832 C ILE A 104 85.117 55.423 69.979 1.00 31.25 C ANISOU 832 C ILE F 104 4575 3985 3313 -949 706 460 C ATOM 833 O ILE A 104 86.035 55.052 70.715 1.00 32.27 O ANISOU 833 O ILE F 104 4783 4728 2752 -686 460 863 O ATOM 834 CB ILE A 104 85.691 57.762 69.370 1.00 31.31 C ANISOU 834 CB ILE F 104 4726 4326 2846 -1181 253 675 C ATOM 835 CG1 ILE A 104 85.228 59.220 69.261 1.00 31.28 C ANISOU 835 CG1 ILE F 104 4403 4559 2921 -1144 164 242 C ATOM 836 CG2 ILE A 104 86.169 57.241 68.015 1.00 29.67 C ANISOU 836 CG2 ILE F 104 4248 4267 2758 -881 104 781 C ATOM 837 CD1 ILE A 104 86.348 60.184 68.950 1.00 32.42 C ANISOU 837 CD1 ILE F 104 4680 4730 2907 -1500 -179 876 C ATOM 838 N ASN A 105 84.505 54.596 69.142 1.00 30.46 N ANISOU 838 N ASN F 105 4248 4407 2918 -945 333 590 N ATOM 839 CA ASN A 105 84.959 53.219 69.074 1.00 32.34 C ANISOU 839 CA ASN F 105 4321 4452 3516 -907 626 520 C ATOM 840 C ASN A 105 85.321 52.889 67.629 1.00 33.61 C ANISOU 840 C ASN F 105 4711 4436 3624 -724 491 392 C ATOM 841 O ASN A 105 84.565 53.072 66.678 1.00 30.80 O ANISOU 841 O ASN F 105 4042 4434 3227 -644 -297 398 O ATOM 842 CB ASN A 105 83.872 52.279 69.573 1.00 32.61 C ANISOU 842 CB ASN F 105 4246 4368 3777 -697 574 342 C ATOM 843 CG ASN A 105 83.526 52.490 71.024 1.00 35.09 C ANISOU 843 CG ASN F 105 4708 5076 3550 -880 272 688 C ATOM 844 OD1 ASN A 105 84.209 51.911 71.874 1.00 39.39 O ANISOU 844 OD1 ASN F 105 5905 5078 3981 -569 731 944 O ATOM 845 ND2 ASN A 105 82.506 53.291 71.326 1.00 29.24 N ANISOU 845 ND2 ASN F 105 3888 5167 2057 -734 610 859 N ATOM 846 N LEU A 106 86.549 52.396 67.509 1.00 31.95 N ANISOU 846 N LEU F 106 3952 4279 3909 -177 439 403 N ATOM 847 CA LEU A 106 87.142 52.008 66.242 1.00 34.22 C ANISOU 847 CA LEU F 106 4400 4562 4040 -423 543 158 C ATOM 848 C LEU A 106 87.822 50.660 66.447 1.00 34.71 C ANISOU 848 C LEU F 106 4913 4364 3913 -388 534 20 C ATOM 849 O LEU A 106 88.353 50.439 67.533 1.00 36.23 O ANISOU 849 O LEU F 106 4968 4770 4027 -138 604 233 O ATOM 850 CB LEU A 106 88.157 53.027 65.739 1.00 36.38 C ANISOU 850 CB LEU F 106 4510 4684 4630 -584 565 -435 C ATOM 851 CG LEU A 106 87.621 54.264 65.009 1.00 35.72 C ANISOU 851 CG LEU F 106 3771 5352 4451 -70 829 -681 C ATOM 852 CD1 LEU A 106 88.363 55.497 65.519 1.00 42.00 C ANISOU 852 CD1 LEU F 106 3910 6757 5290 -647 1129 138 C ATOM 853 CD2 LEU A 106 87.744 54.149 63.500 1.00 35.07 C ANISOU 853 CD2 LEU F 106 4779 4133 4415 -597 761 -603 C ATOM 854 N LEU A 107 87.817 49.775 65.467 1.00 34.53 N ANISOU 854 N LEU F 107 4691 4414 4014 -459 540 -33 N ATOM 855 CA LEU A 107 88.535 48.515 65.589 1.00 35.05 C ANISOU 855 CA LEU F 107 4619 4356 4344 -516 1190 479 C ATOM 856 C LEU A 107 90.041 48.737 65.641 1.00 37.46 C ANISOU 856 C LEU F 107 4938 4618 4678 -787 937 911 C ATOM 857 O LEU A 107 90.605 49.559 64.903 1.00 38.05 O ANISOU 857 O LEU F 107 5313 4559 4585 -800 755 183 O ATOM 858 CB LEU A 107 88.115 47.616 64.413 1.00 34.30 C ANISOU 858 CB LEU F 107 4586 4483 3964 -534 928 451 C ATOM 859 CG LEU A 107 86.779 46.902 64.690 1.00 34.06 C ANISOU 859 CG LEU F 107 4502 4681 3757 -547 836 807 C ATOM 860 CD1 LEU A 107 86.121 46.442 63.388 1.00 29.82 C ANISOU 860 CD1 LEU F 107 3380 4872 3080 -19 332 269 C ATOM 861 CD2 LEU A 107 86.989 45.756 65.662 1.00 33.01 C ANISOU 861 CD2 LEU F 107 5034 4156 3351 -512 683 489 C ATOM 862 N ASN A 108 90.722 48.010 66.542 1.00 39.13 N ANISOU 862 N ASN F 108 5989 4292 4588 -435 1104 684 N ATOM 863 CA ASN A 108 92.177 48.115 66.642 1.00 39.84 C ANISOU 863 CA ASN F 108 6362 4176 4599 -440 1482 556 C ATOM 864 C ASN A 108 92.843 47.151 65.669 1.00 40.69 C ANISOU 864 C ASN F 108 6208 4324 4928 -519 1857 483 C ATOM 865 O ASN A 108 93.016 45.958 65.936 1.00 43.29 O ANISOU 865 O ASN F 108 6790 3902 5756 -377 1638 598 O ATOM 866 CB ASN A 108 92.644 47.853 68.074 1.00 40.41 C ANISOU 866 CB ASN F 108 6331 4262 4760 21 1660 794 C ATOM 867 CG ASN A 108 94.128 48.080 68.264 1.00 38.84 C ANISOU 867 CG ASN F 108 5505 4307 4946 398 2042 806 C ATOM 868 OD1 ASN A 108 94.881 48.387 67.329 1.00 53.94 O ANISOU 868 OD1 ASN F 108 10729 5477 4290 -2612 3158 -571 O ATOM 869 ND2 ASN A 108 94.564 47.913 69.519 1.00 46.61 N ANISOU 869 ND2 ASN F 108 7358 5603 4750 -825 2625 612 N ATOM 870 N GLY A 109 93.238 47.659 64.504 1.00 40.85 N ANISOU 870 N GLY F 109 6270 4240 5010 -754 1842 113 N ATOM 871 CA GLY A 109 93.846 46.821 63.482 1.00 39.63 C ANISOU 871 CA GLY F 109 5024 4631 5402 78 1429 -31 C ATOM 872 C GLY A 109 95.228 46.339 63.878 1.00 42.22 C ANISOU 872 C GLY F 109 5622 4535 5887 -177 1869 -417 C ATOM 873 O GLY A 109 95.829 45.496 63.217 1.00 38.25 O ANISOU 873 O GLY F 109 4210 4790 5534 -176 293 -952 O ATOM 874 N ASN A 110 95.737 46.879 64.982 1.00 44.46 N ANISOU 874 N ASN F 110 5804 4980 6109 -380 1982 -24 N ATOM 875 CA ASN A 110 97.041 46.483 65.482 1.00 48.58 C ANISOU 875 CA ASN F 110 6429 5414 6615 -1018 1249 443 C ATOM 876 C ASN A 110 96.907 45.611 66.715 1.00 50.82 C ANISOU 876 C ASN F 110 6823 5772 6715 -709 1144 566 C ATOM 877 O ASN A 110 97.917 45.305 67.349 1.00 48.88 O ANISOU 877 O ASN F 110 7062 4473 7037 13 812 -66 O ATOM 878 CB ASN A 110 97.894 47.738 65.756 1.00 50.36 C ANISOU 878 CB ASN F 110 6487 5502 7146 -1451 1298 21 C ATOM 879 CG ASN A 110 98.262 48.439 64.456 1.00 50.62 C ANISOU 879 CG ASN F 110 6301 5774 7159 -1249 1332 -411 C ATOM 880 OD1 ASN A 110 98.926 47.849 63.598 1.00 52.61 O ANISOU 880 OD1 ASN F 110 6575 6222 7194 -811 1545 -529 O ATOM 881 ND2 ASN A 110 97.853 49.690 64.266 1.00 48.08 N ANISOU 881 ND2 ASN F 110 6147 5904 6217 -1209 1853 -182 N ATOM 882 N ALA A 111 95.698 45.188 67.086 1.00 46.92 N ANISOU 882 N ALA F 111 5573 5931 6322 -309 1461 920 N ATOM 883 CA ALA A 111 95.587 44.346 68.282 1.00 48.47 C ANISOU 883 CA ALA F 111 5790 6212 6414 129 1455 1048 C ATOM 884 C ALA A 111 96.417 43.071 68.112 1.00 52.94 C ANISOU 884 C ALA F 111 6797 6316 7001 455 1192 819 C ATOM 885 O ALA A 111 96.551 42.496 67.027 1.00 54.44 O ANISOU 885 O ALA F 111 7637 5640 7410 41 1768 691 O ATOM 886 CB ALA A 111 94.146 44.006 68.622 1.00 45.03 C ANISOU 886 CB ALA F 111 3698 5647 7765 1271 726 1998 C ATOM 887 N PRO A 112 96.999 42.637 69.229 1.00 55.19 N ANISOU 887 N PRO F 112 7572 6396 7003 848 638 742 N ATOM 888 CA PRO A 112 97.845 41.436 69.219 1.00 54.22 C ANISOU 888 CA PRO F 112 6868 6455 7279 743 569 625 C ATOM 889 C PRO A 112 96.988 40.187 69.025 1.00 59.71 C ANISOU 889 C PRO F 112 7025 6982 8682 359 1164 -242 C ATOM 890 O PRO A 112 97.360 39.297 68.253 1.00 77.93 O ANISOU 890 O PRO F 112 8031 7763 13817 567 2677 -2149 O ATOM 891 CB PRO A 112 98.511 41.460 70.596 1.00 57.18 C ANISOU 891 CB PRO F 112 7833 6256 7639 966 1000 896 C ATOM 892 CG PRO A 112 97.491 42.144 71.454 1.00 54.16 C ANISOU 892 CG PRO F 112 7183 6144 7253 1389 1098 1162 C ATOM 893 CD PRO A 112 96.906 43.222 70.576 1.00 53.80 C ANISOU 893 CD PRO F 112 6856 6468 7117 1172 1100 1377 C ATOM 894 N ASP A 113 95.837 40.111 69.688 1.00 58.97 N ANISOU 894 N ASP F 113 7871 6976 7558 -703 978 1015 N ATOM 895 CA ASP A 113 94.920 38.994 69.486 1.00 54.23 C ANISOU 895 CA ASP F 113 7651 6420 6535 -174 564 1816 C ATOM 896 C ASP A 113 93.686 39.443 68.700 1.00 52.93 C ANISOU 896 C ASP F 113 7586 6363 6163 180 639 1741 C ATOM 897 O ASP A 113 92.710 39.897 69.301 1.00 44.98 O ANISOU 897 O ASP F 113 5320 6095 5676 1212 693 1948 O ATOM 898 CB ASP A 113 94.484 38.402 70.823 1.00 54.08 C ANISOU 898 CB ASP F 113 7975 6588 5985 -110 988 1859 C ATOM 899 CG ASP A 113 93.672 37.133 70.670 1.00 58.32 C ANISOU 899 CG ASP F 113 7835 7247 7078 -138 293 1121 C ATOM 900 OD1 ASP A 113 93.217 36.822 69.556 1.00 53.98 O ANISOU 900 OD1 ASP F 113 5905 7266 7339 387 -41 1707 O ATOM 901 OD2 ASP A 113 93.489 36.424 71.682 1.00 61.72 O ANISOU 901 OD2 ASP F 113 8558 8578 6314 -863 -16 -699 O ATOM 902 N ILE A 114 93.761 39.303 67.382 1.00 51.56 N ANISOU 902 N ILE F 114 6967 6312 6311 -162 1211 1397 N ATOM 903 CA ILE A 114 92.700 39.729 66.478 1.00 52.94 C ANISOU 903 CA ILE F 114 7380 6739 5997 -693 1291 1417 C ATOM 904 C ILE A 114 91.332 39.167 66.824 1.00 49.80 C ANISOU 904 C ILE F 114 7019 5918 5983 -7 1190 1105 C ATOM 905 O ILE A 114 90.352 39.923 66.890 1.00 49.57 O ANISOU 905 O ILE F 114 6631 5887 6317 133 1737 1794 O ATOM 906 CB ILE A 114 93.047 39.324 65.030 1.00 55.04 C ANISOU 906 CB ILE F 114 7595 7188 6129 -1136 1136 1055 C ATOM 907 CG1 ILE A 114 94.254 40.091 64.480 1.00 59.43 C ANISOU 907 CG1 ILE F 114 8000 7943 6638 -2048 1462 914 C ATOM 908 CG2 ILE A 114 91.837 39.476 64.121 1.00 45.34 C ANISOU 908 CG2 ILE F 114 6371 5895 4960 -544 270 324 C ATOM 909 CD1 ILE A 114 94.096 41.589 64.711 1.00 67.13 C ANISOU 909 CD1 ILE F 114 7512 7919 10077 -1945 751 1921 C ATOM 910 N ASP A 115 91.198 37.860 67.047 1.00 48.77 N ANISOU 910 N ASP F 115 7171 5406 5955 66 1323 1323 N ATOM 911 CA ASP A 115 89.846 37.382 67.348 1.00 48.39 C ANISOU 911 CA ASP F 115 7228 5264 5896 282 442 1777 C ATOM 912 C ASP A 115 89.304 37.997 68.627 1.00 47.13 C ANISOU 912 C ASP F 115 6772 5891 5245 168 83 1979 C ATOM 913 O ASP A 115 88.099 38.216 68.724 1.00 40.86 O ANISOU 913 O ASP F 115 4896 6366 4264 -85 440 1617 O ATOM 914 CB ASP A 115 89.810 35.857 67.449 1.00 54.10 C ANISOU 914 CB ASP F 115 7425 5973 7156 638 193 1521 C ATOM 915 CG ASP A 115 90.067 35.256 66.075 1.00 57.98 C ANISOU 915 CG ASP F 115 7268 7039 7724 782 726 1041 C ATOM 916 OD1 ASP A 115 90.312 36.028 65.121 1.00 63.54 O ANISOU 916 OD1 ASP F 115 8889 7752 7500 -32 -83 573 O ATOM 917 OD2 ASP A 115 90.026 34.015 65.959 1.00 72.11 O ANISOU 917 OD2 ASP F 115 8323 7947 11127 1838 1191 119 O ATOM 918 N ALA A 116 90.203 38.258 69.562 1.00 45.03 N ANISOU 918 N ALA F 116 6608 5130 5370 362 -231 2216 N ATOM 919 CA ALA A 116 89.802 38.881 70.819 1.00 46.84 C ANISOU 919 CA ALA F 116 7112 5580 5106 -215 11 2295 C ATOM 920 C ALA A 116 89.300 40.310 70.618 1.00 42.63 C ANISOU 920 C ALA F 116 6829 5093 4274 -485 416 1882 C ATOM 921 O ALA A 116 88.274 40.721 71.192 1.00 43.65 O ANISOU 921 O ALA F 116 6664 5785 4135 -790 1404 1188 O ATOM 922 CB ALA A 116 90.981 38.842 71.772 1.00 45.03 C ANISOU 922 CB ALA F 116 5193 5521 6397 378 640 2551 C ATOM 923 N GLU A 117 90.030 41.063 69.805 1.00 40.19 N ANISOU 923 N GLU F 117 5901 5384 3985 -321 1107 1559 N ATOM 924 CA GLU A 117 89.651 42.428 69.421 1.00 42.41 C ANISOU 924 CA GLU F 117 6550 5019 4547 -371 582 1690 C ATOM 925 C GLU A 117 88.225 42.417 68.872 1.00 40.28 C ANISOU 925 C GLU F 117 6191 4878 4236 -462 829 1007 C ATOM 926 O GLU A 117 87.378 43.221 69.288 1.00 37.84 O ANISOU 926 O GLU F 117 5358 4923 4096 -54 799 1325 O ATOM 927 CB GLU A 117 90.656 42.970 68.413 1.00 41.10 C ANISOU 927 CB GLU F 117 6379 4044 5193 -218 420 1696 C ATOM 928 CG GLU A 117 90.433 44.326 67.777 1.00 39.62 C ANISOU 928 CG GLU F 117 5565 4581 4906 -77 1126 1712 C ATOM 929 CD GLU A 117 90.315 45.430 68.811 1.00 43.56 C ANISOU 929 CD GLU F 117 6478 4914 5158 -169 1533 1396 C ATOM 930 OE1 GLU A 117 90.892 45.258 69.911 1.00 40.98 O ANISOU 930 OE1 GLU F 117 5095 5747 4727 12 796 1432 O ATOM 931 OE2 GLU A 117 89.640 46.445 68.519 1.00 41.60 O ANISOU 931 OE2 GLU F 117 5582 5443 4780 120 1472 1403 O ATOM 932 N CYS A 118 87.961 41.493 67.944 1.00 36.59 N ANISOU 932 N CYS F 118 5340 4757 3805 -197 141 868 N ATOM 933 CA CYS A 118 86.664 41.436 67.277 1.00 35.42 C ANISOU 933 CA CYS F 118 4597 4601 4259 145 389 845 C ATOM 934 C CYS A 118 85.568 41.074 68.266 1.00 35.22 C ANISOU 934 C CYS F 118 4292 4824 4266 153 357 926 C ATOM 935 O CYS A 118 84.494 41.678 68.270 1.00 36.37 O ANISOU 935 O CYS F 118 5254 4837 3727 -302 589 909 O ATOM 936 CB CYS A 118 86.727 40.456 66.101 1.00 38.72 C ANISOU 936 CB CYS F 118 6019 4186 4508 272 977 881 C ATOM 937 SG CYS A 118 87.830 41.062 64.776 1.00 42.29 S ANISOU 937 SG CYS F 118 6457 5128 4485 -445 1404 310 S ATOM 938 N ARG A 119 85.813 40.105 69.130 1.00 39.08 N ANISOU 938 N ARG F 119 3719 5677 5451 379 14 1271 N ATOM 939 CA ARG A 119 84.894 39.781 70.217 1.00 44.31 C ANISOU 939 CA ARG F 119 4903 5728 6206 455 -1119 1422 C ATOM 940 C ARG A 119 84.564 40.929 71.161 1.00 43.76 C ANISOU 940 C ARG F 119 5164 6305 5159 166 -1336 1150 C ATOM 941 O ARG A 119 83.431 41.166 71.603 1.00 41.45 O ANISOU 941 O ARG F 119 5564 6327 3860 16 -1556 1553 O ATOM 942 CB ARG A 119 85.548 38.634 71.012 1.00 52.18 C ANISOU 942 CB ARG F 119 6079 6237 7511 557 -1925 2009 C ATOM 943 CG ARG A 119 84.562 37.671 71.645 1.00 62.59 C ANISOU 943 CG ARG F 119 7520 7269 8992 -116 -3727 3064 C ATOM 944 CD ARG A 119 85.290 36.547 72.401 1.00 70.06 C ANISOU 944 CD ARG F 119 8623 7363 10634 217 -4665 3157 C ATOM 945 NE ARG A 119 86.345 35.984 71.552 1.00 77.92 N ANISOU 945 NE ARG F 119 10834 7176 11594 33 -3455 2858 N ATOM 946 CZ ARG A 119 87.624 35.827 71.864 1.00 81.38 C ANISOU 946 CZ ARG F 119 11888 7786 11248 -990 -3153 2568 C ATOM 947 NH1 ARG A 119 88.083 36.183 73.065 1.00 79.87 N ANISOU 947 NH1 ARG F 119 11090 9685 9573 -1384 -5734 3721 N ATOM 948 NH2 ARG A 119 88.455 35.296 70.965 1.00 78.89 N ANISOU 948 NH2 ARG F 119 10717 8579 10677 -1734 -5670 2193 N ATOM 949 N GLN A 120 85.580 41.705 71.532 1.00 43.70 N ANISOU 949 N GLN F 120 5581 6454 4567 -50 -1033 1137 N ATOM 950 CA GLN A 120 85.377 42.833 72.442 1.00 43.77 C ANISOU 950 CA GLN F 120 6264 6209 4159 -91 -698 1472 C ATOM 951 C GLN A 120 84.537 43.943 71.822 1.00 42.63 C ANISOU 951 C GLN F 120 6254 5980 3964 -171 -1138 1024 C ATOM 952 O GLN A 120 83.697 44.567 72.481 1.00 40.35 O ANISOU 952 O GLN F 120 5549 6318 3463 -59 -564 1020 O ATOM 953 CB GLN A 120 86.747 43.382 72.872 1.00 51.15 C ANISOU 953 CB GLN F 120 8110 6639 4685 -934 797 1022 C ATOM 954 CG GLN A 120 87.538 42.386 73.695 1.00 60.59 C ANISOU 954 CG GLN F 120 10526 6828 5666 -1654 -68 1791 C ATOM 955 CD GLN A 120 88.993 42.767 73.877 1.00 66.38 C ANISOU 955 CD GLN F 120 11134 7736 6353 -2259 807 2050 C ATOM 956 OE1 GLN A 120 89.380 43.921 73.674 1.00 80.51 O ANISOU 956 OE1 GLN F 120 11531 10907 8151 -3681 -1848 4294 O ATOM 957 NE2 GLN A 120 89.804 41.779 74.260 1.00 65.48 N ANISOU 957 NE2 GLN F 120 12268 6515 6094 -1355 4376 647 N ATOM 958 N TYR A 121 84.776 44.189 70.527 1.00 39.41 N ANISOU 958 N TYR F 121 5523 5545 3904 -557 -941 999 N ATOM 959 CA TYR A 121 83.979 45.185 69.814 1.00 37.24 C ANISOU 959 CA TYR F 121 4934 5576 3642 -351 -578 889 C ATOM 960 C TYR A 121 82.490 44.859 69.912 1.00 35.57 C ANISOU 960 C TYR F 121 4686 5266 3564 -56 -151 609 C ATOM 961 O TYR A 121 81.675 45.714 70.266 1.00 39.31 O ANISOU 961 O TYR F 121 5066 5420 4451 -17 279 342 O ATOM 962 CB TYR A 121 84.421 45.252 68.356 1.00 32.78 C ANISOU 962 CB TYR F 121 4529 4380 3547 235 -18 741 C ATOM 963 CG TYR A 121 84.251 46.574 67.648 1.00 32.72 C ANISOU 963 CG TYR F 121 4195 4876 3362 79 -13 842 C ATOM 964 CD1 TYR A 121 84.917 47.705 68.118 1.00 32.38 C ANISOU 964 CD1 TYR F 121 4294 4542 3467 -45 155 697 C ATOM 965 CD2 TYR A 121 83.429 46.684 66.522 1.00 29.32 C ANISOU 965 CD2 TYR F 121 4353 3681 3105 719 514 215 C ATOM 966 CE1 TYR A 121 84.778 48.921 67.491 1.00 29.55 C ANISOU 966 CE1 TYR F 121 4346 3796 3086 310 491 52 C ATOM 967 CE2 TYR A 121 83.286 47.896 65.884 1.00 26.68 C ANISOU 967 CE2 TYR F 121 4082 3327 2727 406 295 -193 C ATOM 968 CZ TYR A 121 83.956 48.993 66.376 1.00 29.38 C ANISOU 968 CZ TYR F 121 4160 3638 3366 350 482 232 C ATOM 969 OH TYR A 121 83.836 50.222 65.756 1.00 30.92 O ANISOU 969 OH TYR F 121 3871 4298 3580 135 349 502 O ATOM 970 N GLU A 122 82.117 43.619 69.598 1.00 34.29 N ANISOU 970 N GLU F 122 4451 5144 3434 344 -834 1356 N ATOM 971 CA GLU A 122 80.718 43.204 69.697 1.00 37.50 C ANISOU 971 CA GLU F 122 4800 5818 3630 -156 498 -49 C ATOM 972 C GLU A 122 80.251 43.331 71.144 1.00 36.58 C ANISOU 972 C GLU F 122 4713 5633 3554 185 412 101 C ATOM 973 O GLU A 122 79.127 43.735 71.443 1.00 38.91 O ANISOU 973 O GLU F 122 4594 6036 4155 -416 -691 -119 O ATOM 974 CB GLU A 122 80.495 41.763 69.241 1.00 37.54 C ANISOU 974 CB GLU F 122 4948 5625 3692 -122 635 -69 C ATOM 975 CG GLU A 122 80.764 41.541 67.756 1.00 35.43 C ANISOU 975 CG GLU F 122 4337 5596 3529 370 210 271 C ATOM 976 CD GLU A 122 79.624 41.983 66.866 1.00 39.13 C ANISOU 976 CD GLU F 122 5390 5602 3876 -300 368 243 C ATOM 977 OE1 GLU A 122 78.531 42.281 67.392 1.00 40.51 O ANISOU 977 OE1 GLU F 122 5324 5966 4101 -741 -1057 413 O ATOM 978 OE2 GLU A 122 79.863 42.026 65.630 1.00 37.69 O ANISOU 978 OE2 GLU F 122 5819 4757 3746 -47 903 257 O ATOM 979 N GLU A 123 81.166 42.957 72.051 1.00 41.44 N ANISOU 979 N GLU F 123 5037 6678 4029 -410 -421 951 N ATOM 980 CA GLU A 123 80.738 43.086 73.452 1.00 45.19 C ANISOU 980 CA GLU F 123 6449 6777 3942 -681 -248 1030 C ATOM 981 C GLU A 123 80.501 44.538 73.835 1.00 44.81 C ANISOU 981 C GLU F 123 5963 7095 3967 -1105 -108 473 C ATOM 982 O GLU A 123 79.560 44.870 74.561 1.00 42.83 O ANISOU 982 O GLU F 123 6460 6124 3688 -484 -1306 1300 O ATOM 983 CB GLU A 123 81.788 42.434 74.356 1.00 52.97 C ANISOU 983 CB GLU F 123 7888 7594 4642 -1002 -1478 1840 C ATOM 984 CG GLU A 123 81.373 41.020 74.728 1.00 62.88 C ANISOU 984 CG GLU F 123 8488 7466 7937 376 -1773 1479 C ATOM 985 CD GLU A 123 82.298 39.944 74.207 1.00 75.26 C ANISOU 985 CD GLU F 123 10105 7469 11021 -13 -239 782 C ATOM 986 OE1 GLU A 123 83.431 39.820 74.722 1.00 94.72 O ANISOU 986 OE1 GLU F 123 15817 7792 12381 -1954 62 894 O ATOM 987 OE2 GLU A 123 81.885 39.206 73.273 1.00108.70 O ANISOU 987 OE2 GLU F 123 15891 10579 14830 -1925 4492 -3558 O ATOM 988 N LYS A 124 81.366 45.438 73.347 1.00 43.43 N ANISOU 988 N LYS F 124 6342 6311 3849 -1081 -739 1307 N ATOM 989 CA LYS A 124 81.163 46.849 73.689 1.00 43.60 C ANISOU 989 CA LYS F 124 5986 6783 3799 -1212 -366 1516 C ATOM 990 C LYS A 124 79.828 47.354 73.146 1.00 41.43 C ANISOU 990 C LYS F 124 6080 6378 3283 -809 740 844 C ATOM 991 O LYS A 124 79.116 48.086 73.834 1.00 39.70 O ANISOU 991 O LYS F 124 5588 6905 2593 -416 174 717 O ATOM 992 CB LYS A 124 82.328 47.701 73.177 1.00 48.70 C ANISOU 992 CB LYS F 124 6154 7889 4462 -1797 -661 2218 C ATOM 993 CG LYS A 124 83.096 48.455 74.245 1.00 63.43 C ANISOU 993 CG LYS F 124 7294 10431 6376 -3061 617 2158 C ATOM 994 CD LYS A 124 83.559 49.824 73.767 1.00 65.56 C ANISOU 994 CD LYS F 124 7032 11017 6862 -1995 1436 1559 C ATOM 995 CE LYS A 124 83.417 50.866 74.868 1.00 69.50 C ANISOU 995 CE LYS F 124 8209 12180 6018 -2846 2079 1601 C ATOM 996 NZ LYS A 124 83.975 52.200 74.477 1.00 75.15 N ANISOU 996 NZ LYS F 124 7038 17031 4484 -4576 3724 -1262 N ATOM 997 N ILE A 125 79.458 46.980 71.920 1.00 38.54 N ANISOU 997 N ILE F 125 4878 6076 3689 -691 1108 567 N ATOM 998 CA ILE A 125 78.155 47.426 71.400 1.00 34.53 C ANISOU 998 CA ILE F 125 3711 6172 3237 -519 393 769 C ATOM 999 C ILE A 125 77.041 46.967 72.341 1.00 38.08 C ANISOU 999 C ILE F 125 4373 6461 3635 -657 3 649 C ATOM 1000 O ILE A 125 76.178 47.742 72.776 1.00 40.44 O ANISOU 1000 O ILE F 125 5635 6242 3488 -613 -524 843 O ATOM 1001 CB ILE A 125 77.911 46.902 69.978 1.00 38.18 C ANISOU 1001 CB ILE F 125 4638 6414 3453 -940 800 561 C ATOM 1002 CG1 ILE A 125 78.847 47.504 68.936 1.00 37.72 C ANISOU 1002 CG1 ILE F 125 4797 6191 3344 -1317 1369 -151 C ATOM 1003 CG2 ILE A 125 76.454 47.123 69.587 1.00 31.39 C ANISOU 1003 CG2 ILE F 125 3778 5944 2204 -412 106 304 C ATOM 1004 CD1 ILE A 125 79.086 46.649 67.714 1.00 33.33 C ANISOU 1004 CD1 ILE F 125 3304 5887 3474 -140 1071 460 C ATOM 1005 N ARG A 126 77.096 45.667 72.675 1.00 39.91 N ANISOU 1005 N ARG F 126 5093 6528 3541 -592 -799 1236 N ATOM 1006 CA ARG A 126 76.076 45.111 73.569 1.00 41.68 C ANISOU 1006 CA ARG F 126 4615 6590 4630 -591 -504 396 C ATOM 1007 C ARG A 126 76.162 45.781 74.929 1.00 42.83 C ANISOU 1007 C ARG F 126 6096 6161 4016 -833 -706 654 C ATOM 1008 O ARG A 126 75.161 45.846 75.641 1.00 50.68 O ANISOU 1008 O ARG F 126 8113 7268 3876 -1592 -1649 650 O ATOM 1009 CB ARG A 126 76.182 43.589 73.703 1.00 49.83 C ANISOU 1009 CB ARG F 126 4423 7446 7066 -493 -945 639 C ATOM 1010 CG ARG A 126 76.001 42.879 72.367 1.00 61.30 C ANISOU 1010 CG ARG F 126 5305 8610 9378 -150 1073 -467 C ATOM 1011 CD ARG A 126 76.170 41.371 72.435 1.00 70.98 C ANISOU 1011 CD ARG F 126 6066 8802 12102 403 337 -1383 C ATOM 1012 NE ARG A 126 76.662 40.776 71.185 1.00 75.78 N ANISOU 1012 NE ARG F 126 6410 9126 13256 732 279 -2434 N ATOM 1013 CZ ARG A 126 77.738 39.992 71.127 1.00 80.52 C ANISOU 1013 CZ ARG F 126 7729 9012 13852 270 -308 -2303 C ATOM 1014 NH1 ARG A 126 78.424 39.714 72.236 1.00 75.26 N ANISOU 1014 NH1 ARG F 126 3984 10070 14544 614 -1937 -1211 N ATOM 1015 NH2 ARG A 126 78.142 39.477 69.967 1.00 84.71 N ANISOU 1015 NH2 ARG F 126 8443 9133 14609 154 -560 -3265 N ATOM 1016 N SER A 127 77.317 46.309 75.343 1.00 45.17 N ANISOU 1016 N SER F 127 6405 6105 4654 -537 272 666 N ATOM 1017 CA SER A 127 77.305 46.931 76.685 1.00 45.18 C ANISOU 1017 CA SER F 127 6382 6517 4269 -264 -284 650 C ATOM 1018 C SER A 127 76.389 48.144 76.665 1.00 44.06 C ANISOU 1018 C SER F 127 5846 6620 4274 -268 -1001 7 C ATOM 1019 O SER A 127 75.769 48.456 77.673 1.00 51.05 O ANISOU 1019 O SER F 127 9415 6449 3533 -269 -623 590 O ATOM 1020 CB SER A 127 78.702 47.321 77.155 1.00 46.96 C ANISOU 1020 CB SER F 127 6559 6827 4457 -337 566 241 C ATOM 1021 OG SER A 127 79.205 48.385 76.343 1.00 47.73 O ANISOU 1021 OG SER F 127 5686 6576 5873 44 856 1070 O ATOM 1022 N TYR A 128 76.273 48.841 75.537 1.00 41.48 N ANISOU 1022 N TYR F 128 5253 6118 4389 -622 -1232 -208 N ATOM 1023 CA TYR A 128 75.385 49.989 75.480 1.00 41.75 C ANISOU 1023 CA TYR F 128 5167 6292 4404 -421 -748 -126 C ATOM 1024 C TYR A 128 73.973 49.537 75.136 1.00 43.28 C ANISOU 1024 C TYR F 128 5150 5889 5406 -311 -543 -473 C ATOM 1025 O TYR A 128 73.019 50.254 75.414 1.00 50.69 O ANISOU 1025 O TYR F 128 6660 5912 6687 -290 -152 -716 O ATOM 1026 CB TYR A 128 75.808 51.001 74.421 1.00 40.32 C ANISOU 1026 CB TYR F 128 5256 6154 3908 -642 -520 476 C ATOM 1027 CG TYR A 128 77.045 51.800 74.759 1.00 38.84 C ANISOU 1027 CG TYR F 128 5027 5838 3892 -375 -576 486 C ATOM 1028 CD1 TYR A 128 76.976 52.897 75.607 1.00 40.46 C ANISOU 1028 CD1 TYR F 128 5413 5790 4169 -563 -303 184 C ATOM 1029 CD2 TYR A 128 78.279 51.438 74.212 1.00 36.34 C ANISOU 1029 CD2 TYR F 128 4779 5615 3412 -143 -577 724 C ATOM 1030 CE1 TYR A 128 78.103 53.628 75.918 1.00 41.77 C ANISOU 1030 CE1 TYR F 128 6297 5884 3690 -902 535 585 C ATOM 1031 CE2 TYR A 128 79.405 52.174 74.526 1.00 39.91 C ANISOU 1031 CE2 TYR F 128 4938 5837 4389 -371 -305 415 C ATOM 1032 CZ TYR A 128 79.309 53.259 75.374 1.00 41.74 C ANISOU 1032 CZ TYR F 128 6221 6101 3537 -1268 787 509 C ATOM 1033 OH TYR A 128 80.457 53.969 75.657 1.00 42.11 O ANISOU 1033 OH TYR F 128 6000 5514 4487 -746 719 1670 O ATOM 1034 N GLY A 129 73.856 48.365 74.511 1.00 42.11 N ANISOU 1034 N GLY F 129 5664 6058 4278 -85 -183 498 N ATOM 1035 CA GLY A 129 72.514 47.866 74.242 1.00 40.48 C ANISOU 1035 CA GLY F 129 6175 6021 3184 -368 176 -100 C ATOM 1036 C GLY A 129 72.282 47.771 72.753 1.00 37.91 C ANISOU 1036 C GLY F 129 5236 6069 3100 293 -58 -536 C ATOM 1037 O GLY A 129 72.050 46.689 72.231 1.00 40.86 O ANISOU 1037 O GLY F 129 5364 6091 4071 -64 550 -542 O ATOM 1038 N LYS A 130 72.348 48.888 72.027 1.00 41.09 N ANISOU 1038 N LYS F 130 5571 6204 3836 -158 -867 -467 N ATOM 1039 CA LYS A 130 72.124 48.751 70.593 1.00 39.33 C ANISOU 1039 CA LYS F 130 5076 5865 4003 -166 -797 221 C ATOM 1040 C LYS A 130 72.602 50.005 69.872 1.00 34.07 C ANISOU 1040 C LYS F 130 4613 4869 3463 492 -65 -221 C ATOM 1041 O LYS A 130 72.681 51.049 70.519 1.00 37.69 O ANISOU 1041 O LYS F 130 4983 5663 3676 -107 1081 345 O ATOM 1042 CB LYS A 130 70.645 48.561 70.274 1.00 48.04 C ANISOU 1042 CB LYS F 130 6199 6826 5226 -1318 -1696 846 C ATOM 1043 CG LYS A 130 69.866 49.834 70.619 1.00 56.92 C ANISOU 1043 CG LYS F 130 8814 5910 6904 -696 -2458 1845 C ATOM 1044 CD LYS A 130 68.414 49.656 70.188 1.00 64.23 C ANISOU 1044 CD LYS F 130 10079 6950 7377 -1460 -1556 2019 C ATOM 1045 CE LYS A 130 68.178 48.200 69.794 1.00 66.12 C ANISOU 1045 CE LYS F 130 10805 8179 6139 -1726 -125 739 C ATOM 1046 NZ LYS A 130 68.385 47.967 68.336 1.00 77.00 N ANISOU 1046 NZ LYS F 130 14511 8537 6209 -992 -1736 -441 N ATOM 1047 N ILE A 131 72.881 49.829 68.598 1.00 31.02 N ANISOU 1047 N ILE F 131 3861 4582 3345 -482 133 -47 N ATOM 1048 CA ILE A 131 73.188 50.990 67.760 1.00 31.31 C ANISOU 1048 CA ILE F 131 4012 4209 3678 -423 -81 -152 C ATOM 1049 C ILE A 131 71.859 51.591 67.340 1.00 30.73 C ANISOU 1049 C ILE F 131 3753 4269 3654 -517 150 -164 C ATOM 1050 O ILE A 131 71.013 50.865 66.810 1.00 34.14 O ANISOU 1050 O ILE F 131 3854 5108 4008 -791 188 99 O ATOM 1051 CB ILE A 131 74.080 50.557 66.580 1.00 33.63 C ANISOU 1051 CB ILE F 131 5058 4285 3436 -1033 -124 -9 C ATOM 1052 CG1 ILE A 131 75.443 50.055 67.078 1.00 31.40 C ANISOU 1052 CG1 ILE F 131 4514 4086 3331 -270 -208 42 C ATOM 1053 CG2 ILE A 131 74.224 51.667 65.553 1.00 25.43 C ANISOU 1053 CG2 ILE F 131 4033 3240 2391 138 1295 -502 C ATOM 1054 CD1 ILE A 131 76.319 49.379 66.074 1.00 29.42 C ANISOU 1054 CD1 ILE F 131 4061 4050 3066 284 -38 314 C ATOM 1055 N HIS A 132 71.610 52.877 67.579 1.00 28.52 N ANISOU 1055 N HIS F 132 4089 4323 2422 -235 -296 -275 N ATOM 1056 CA HIS A 132 70.325 53.457 67.199 1.00 30.32 C ANISOU 1056 CA HIS F 132 4157 4435 2930 -299 71 -4 C ATOM 1057 C HIS A 132 70.212 53.750 65.712 1.00 31.66 C ANISOU 1057 C HIS F 132 4407 4647 2975 -666 86 210 C ATOM 1058 O HIS A 132 69.112 53.652 65.150 1.00 33.63 O ANISOU 1058 O HIS F 132 5439 4291 3048 -711 1019 -321 O ATOM 1059 CB HIS A 132 70.107 54.755 67.987 1.00 30.62 C ANISOU 1059 CB HIS F 132 4246 4205 3184 -277 46 -46 C ATOM 1060 CG HIS A 132 70.125 54.464 69.465 1.00 32.30 C ANISOU 1060 CG HIS F 132 4720 4451 3103 -214 79 -368 C ATOM 1061 ND1 HIS A 132 69.069 53.867 70.118 1.00 37.74 N ANISOU 1061 ND1 HIS F 132 5939 5256 3143 -1222 -185 -328 N ATOM 1062 CD2 HIS A 132 71.065 54.690 70.394 1.00 30.12 C ANISOU 1062 CD2 HIS F 132 4730 4248 2467 -1 741 -1297 C ATOM 1063 CE1 HIS A 132 69.363 53.736 71.403 1.00 40.61 C ANISOU 1063 CE1 HIS F 132 6737 5694 3000 -1929 -57 -571 C ATOM 1064 NE2 HIS A 132 70.577 54.230 71.588 1.00 40.22 N ANISOU 1064 NE2 HIS F 132 6345 5845 3092 -1717 -282 -259 N ATOM 1065 N LEU A 133 71.341 54.117 65.110 1.00 31.59 N ANISOU 1065 N LEU F 133 4605 4354 3043 -380 -89 -26 N ATOM 1066 CA LEU A 133 71.388 54.449 63.695 1.00 28.37 C ANISOU 1066 CA LEU F 133 3938 3870 2972 -91 196 10 C ATOM 1067 C LEU A 133 72.739 54.045 63.121 1.00 28.98 C ANISOU 1067 C LEU F 133 3357 4254 3399 -330 353 -398 C ATOM 1068 O LEU A 133 73.763 54.560 63.595 1.00 32.62 O ANISOU 1068 O LEU F 133 4510 4525 3358 -792 898 -113 O ATOM 1069 CB LEU A 133 71.165 55.934 63.482 1.00 29.90 C ANISOU 1069 CB LEU F 133 3627 4260 3473 -104 292 -72 C ATOM 1070 CG LEU A 133 71.295 56.475 62.056 1.00 30.77 C ANISOU 1070 CG LEU F 133 3544 4725 3421 360 627 493 C ATOM 1071 CD1 LEU A 133 70.358 55.777 61.089 1.00 30.36 C ANISOU 1071 CD1 LEU F 133 3154 5025 3356 -426 420 -419 C ATOM 1072 CD2 LEU A 133 71.019 57.984 62.073 1.00 30.54 C ANISOU 1072 CD2 LEU F 133 3610 4669 3327 357 529 -212 C ATOM 1073 N PHE A 134 72.720 53.137 62.148 1.00 30.24 N ANISOU 1073 N PHE F 134 4088 4159 3241 -390 666 -253 N ATOM 1074 CA PHE A 134 73.960 52.711 61.511 1.00 27.13 C ANISOU 1074 CA PHE F 134 3676 3832 2800 -121 279 137 C ATOM 1075 C PHE A 134 73.948 53.255 60.080 1.00 27.18 C ANISOU 1075 C PHE F 134 3808 3450 3069 -186 63 527 C ATOM 1076 O PHE A 134 73.099 52.870 59.281 1.00 27.06 O ANISOU 1076 O PHE F 134 3762 3739 2780 -314 182 84 O ATOM 1077 CB PHE A 134 74.122 51.191 61.504 1.00 26.18 C ANISOU 1077 CB PHE F 134 3256 3825 2867 -375 109 415 C ATOM 1078 CG PHE A 134 75.557 50.705 61.598 1.00 28.15 C ANISOU 1078 CG PHE F 134 3764 3739 3192 -258 -66 289 C ATOM 1079 CD1 PHE A 134 76.555 51.260 60.806 1.00 27.28 C ANISOU 1079 CD1 PHE F 134 3910 3496 2959 7 63 -133 C ATOM 1080 CD2 PHE A 134 75.910 49.686 62.490 1.00 26.16 C ANISOU 1080 CD2 PHE F 134 3356 3681 2900 -3 414 148 C ATOM 1081 CE1 PHE A 134 77.855 50.810 60.911 1.00 29.02 C ANISOU 1081 CE1 PHE F 134 4191 3644 3192 -273 60 88 C ATOM 1082 CE2 PHE A 134 77.220 49.240 62.609 1.00 28.76 C ANISOU 1082 CE2 PHE F 134 4500 3692 2734 -148 175 169 C ATOM 1083 CZ PHE A 134 78.204 49.813 61.818 1.00 30.25 C ANISOU 1083 CZ PHE F 134 4737 3547 3210 -171 -64 52 C ATOM 1084 N MET A 135 74.862 54.144 59.758 1.00 26.32 N ANISOU 1084 N MET F 135 3595 3693 2714 -5 367 190 N ATOM 1085 CA MET A 135 75.044 54.708 58.446 1.00 25.09 C ANISOU 1085 CA MET F 135 3269 3703 2560 -166 605 448 C ATOM 1086 C MET A 135 76.114 53.925 57.706 1.00 25.40 C ANISOU 1086 C MET F 135 3207 3842 2601 -266 460 287 C ATOM 1087 O MET A 135 77.166 53.598 58.254 1.00 25.93 O ANISOU 1087 O MET F 135 3696 3701 2456 163 571 289 O ATOM 1088 CB MET A 135 75.467 56.186 58.534 1.00 25.32 C ANISOU 1088 CB MET F 135 3207 4013 2401 -318 701 302 C ATOM 1089 CG MET A 135 75.536 56.778 57.119 1.00 28.15 C ANISOU 1089 CG MET F 135 3367 4549 2781 -814 4 125 C ATOM 1090 SD MET A 135 75.730 58.574 57.174 1.00 31.02 S ANISOU 1090 SD MET F 135 3750 4653 3384 -375 -86 334 S ATOM 1091 CE MET A 135 77.470 58.668 57.665 1.00 28.43 C ANISOU 1091 CE MET F 135 3016 4068 3717 -83 256 -533 C ATOM 1092 N GLY A 136 75.890 53.586 56.436 1.00 24.78 N ANISOU 1092 N GLY F 136 3188 3786 2439 -503 167 240 N ATOM 1093 CA GLY A 136 76.913 52.852 55.688 1.00 27.87 C ANISOU 1093 CA GLY F 136 3717 4095 2776 -678 220 -175 C ATOM 1094 C GLY A 136 76.809 53.167 54.205 1.00 26.53 C ANISOU 1094 C GLY F 136 3610 3703 2768 -44 526 -170 C ATOM 1095 O GLY A 136 75.957 53.955 53.769 1.00 27.86 O ANISOU 1095 O GLY F 136 3389 3779 3417 81 -146 -182 O ATOM 1096 N GLY A 137 77.677 52.554 53.415 1.00 29.09 N ANISOU 1096 N GLY F 137 4509 3712 2831 -273 435 -262 N ATOM 1097 CA GLY A 137 77.557 52.582 51.954 1.00 28.89 C ANISOU 1097 CA GLY F 137 4062 4089 2827 -596 602 -311 C ATOM 1098 C GLY A 137 77.297 51.161 51.440 1.00 28.78 C ANISOU 1098 C GLY F 137 3846 4271 2819 -450 276 -211 C ATOM 1099 O GLY A 137 76.976 50.268 52.231 1.00 29.61 O ANISOU 1099 O GLY F 137 4311 4132 2806 -454 18 -10 O ATOM 1100 N VAL A 138 77.439 50.951 50.128 1.00 26.82 N ANISOU 1100 N VAL F 138 3435 3959 2794 -174 231 -77 N ATOM 1101 CA VAL A 138 77.199 49.602 49.602 1.00 24.45 C ANISOU 1101 CA VAL F 138 3353 3292 2644 -155 53 295 C ATOM 1102 C VAL A 138 78.177 49.334 48.465 1.00 24.17 C ANISOU 1102 C VAL F 138 3323 3399 2464 47 -81 329 C ATOM 1103 O VAL A 138 78.521 50.246 47.708 1.00 26.46 O ANISOU 1103 O VAL F 138 3429 3798 2826 -189 -351 516 O ATOM 1104 CB VAL A 138 75.721 49.459 49.182 1.00 25.77 C ANISOU 1104 CB VAL F 138 3325 3426 3039 -172 -199 611 C ATOM 1105 CG1 VAL A 138 75.374 50.488 48.110 1.00 28.40 C ANISOU 1105 CG1 VAL F 138 4717 3466 2609 121 -305 480 C ATOM 1106 CG2 VAL A 138 75.385 48.058 48.690 1.00 26.22 C ANISOU 1106 CG2 VAL F 138 3531 4230 2201 -424 148 240 C ATOM 1107 N GLY A 139 78.650 48.090 48.365 1.00 24.37 N ANISOU 1107 N GLY F 139 3893 2966 2402 32 106 679 N ATOM 1108 CA GLY A 139 79.590 47.752 47.307 1.00 26.69 C ANISOU 1108 CA GLY F 139 4036 3470 2635 13 248 245 C ATOM 1109 C GLY A 139 78.852 47.680 45.975 1.00 27.30 C ANISOU 1109 C GLY F 139 4457 3318 2597 -329 173 122 C ATOM 1110 O GLY A 139 77.612 47.612 45.915 1.00 28.89 O ANISOU 1110 O GLY F 139 4748 3244 2984 -395 -207 425 O ATOM 1111 N ASN A 140 79.606 47.694 44.868 1.00 25.69 N ANISOU 1111 N ASN F 140 3631 3502 2629 48 -42 124 N ATOM 1112 CA ASN A 140 79.027 47.572 43.547 1.00 27.00 C ANISOU 1112 CA ASN F 140 3575 4061 2622 -548 93 -99 C ATOM 1113 C ASN A 140 78.263 46.247 43.429 1.00 28.54 C ANISOU 1113 C ASN F 140 3580 3849 3413 -564 68 141 C ATOM 1114 O ASN A 140 77.287 46.154 42.665 1.00 26.79 O ANISOU 1114 O ASN F 140 3564 3855 2759 -580 23 -128 O ATOM 1115 CB ASN A 140 80.106 47.626 42.466 1.00 24.74 C ANISOU 1115 CB ASN F 140 3986 2859 2555 -398 -275 507 C ATOM 1116 CG ASN A 140 80.787 48.970 42.346 1.00 27.52 C ANISOU 1116 CG ASN F 140 4084 3268 3104 -302 -543 -183 C ATOM 1117 OD1 ASN A 140 80.471 49.947 43.046 1.00 28.78 O ANISOU 1117 OD1 ASN F 140 4295 4160 2480 -141 170 318 O ATOM 1118 ND2 ASN A 140 81.764 49.057 41.449 1.00 32.68 N ANISOU 1118 ND2 ASN F 140 4801 4318 3298 -1401 -449 -329 N ATOM 1119 N ASP A 141 78.714 45.237 44.159 1.00 25.43 N ANISOU 1119 N ASP F 141 3624 3714 2323 -341 347 -354 N ATOM 1120 CA ASP A 141 78.009 43.956 44.081 1.00 26.26 C ANISOU 1120 CA ASP F 141 3642 3814 2522 -331 355 -36 C ATOM 1121 C ASP A 141 77.022 43.792 45.226 1.00 26.49 C ANISOU 1121 C ASP F 141 3569 3491 3006 -170 94 -156 C ATOM 1122 O ASP A 141 76.619 42.658 45.527 1.00 25.75 O ANISOU 1122 O ASP F 141 3565 3223 2995 -391 112 560 O ATOM 1123 CB ASP A 141 79.003 42.788 44.081 1.00 26.72 C ANISOU 1123 CB ASP F 141 3547 3842 2765 -309 -249 -384 C ATOM 1124 CG ASP A 141 79.831 42.790 45.355 1.00 26.06 C ANISOU 1124 CG ASP F 141 3097 3817 2989 461 -314 22 C ATOM 1125 OD1 ASP A 141 80.745 41.946 45.488 1.00 34.78 O ANISOU 1125 OD1 ASP F 141 5599 3472 4144 141 402 -150 O ATOM 1126 OD2 ASP A 141 79.611 43.632 46.246 1.00 30.28 O ANISOU 1126 OD2 ASP F 141 4384 3992 3130 256 314 -130 O ATOM 1127 N GLY A 142 76.648 44.883 45.884 1.00 26.48 N ANISOU 1127 N GLY F 142 3962 3312 2788 -208 434 86 N ATOM 1128 CA GLY A 142 75.638 44.845 46.946 1.00 25.59 C ANISOU 1128 CA GLY F 142 3756 3176 2790 -148 467 139 C ATOM 1129 C GLY A 142 76.179 44.483 48.305 1.00 25.67 C ANISOU 1129 C GLY F 142 3392 3211 3151 224 -423 428 C ATOM 1130 O GLY A 142 75.412 44.444 49.297 1.00 27.27 O ANISOU 1130 O GLY F 142 3583 3831 2948 -36 154 66 O ATOM 1131 N HIS A 143 77.481 44.203 48.453 1.00 26.81 N ANISOU 1131 N HIS F 143 3542 3427 3216 -44 -50 594 N ATOM 1132 CA HIS A 143 78.016 43.787 49.767 1.00 27.70 C ANISOU 1132 CA HIS F 143 3694 3720 3113 -107 -43 623 C ATOM 1133 C HIS A 143 78.095 44.946 50.751 1.00 28.72 C ANISOU 1133 C HIS F 143 3819 4031 3063 -16 -117 490 C ATOM 1134 O HIS A 143 78.042 46.121 50.376 1.00 28.56 O ANISOU 1134 O HIS F 143 3322 4544 2984 -223 -216 252 O ATOM 1135 CB HIS A 143 79.414 43.171 49.633 1.00 28.55 C ANISOU 1135 CB HIS F 143 4574 3745 2530 -324 194 700 C ATOM 1136 CG HIS A 143 80.537 44.138 49.413 1.00 35.65 C ANISOU 1136 CG HIS F 143 5284 4866 3394 -1553 -40 960 C ATOM 1137 ND1 HIS A 143 80.975 44.479 48.147 1.00 33.00 N ANISOU 1137 ND1 HIS F 143 4485 4459 3595 -302 -143 483 N ATOM 1138 CD2 HIS A 143 81.344 44.829 50.272 1.00 39.21 C ANISOU 1138 CD2 HIS F 143 5260 5829 3811 -1714 220 735 C ATOM 1139 CE1 HIS A 143 81.978 45.332 48.205 1.00 33.43 C ANISOU 1139 CE1 HIS F 143 4082 4472 4145 252 -361 928 C ATOM 1140 NE2 HIS A 143 82.219 45.569 49.490 1.00 38.04 N ANISOU 1140 NE2 HIS F 143 4721 5393 4340 -876 -18 943 N ATOM 1141 N ILE A 144 78.278 44.600 52.025 1.00 27.69 N ANISOU 1141 N ILE F 144 4000 3529 2989 -166 -216 269 N ATOM 1142 CA ILE A 144 78.347 45.610 53.084 1.00 30.21 C ANISOU 1142 CA ILE F 144 4441 3961 3078 -20 -40 137 C ATOM 1143 C ILE A 144 79.673 45.555 53.822 1.00 30.24 C ANISOU 1143 C ILE F 144 4207 4313 2970 29 -24 347 C ATOM 1144 O ILE A 144 80.146 44.455 54.162 1.00 28.53 O ANISOU 1144 O ILE F 144 3824 4341 2677 -185 -149 407 O ATOM 1145 CB ILE A 144 77.141 45.399 54.009 1.00 35.87 C ANISOU 1145 CB ILE F 144 5317 5273 3038 -1017 499 -391 C ATOM 1146 CG1 ILE A 144 75.852 45.888 53.324 1.00 39.81 C ANISOU 1146 CG1 ILE F 144 6210 5401 3515 -2039 1688 -660 C ATOM 1147 CG2 ILE A 144 77.373 46.029 55.379 1.00 38.08 C ANISOU 1147 CG2 ILE F 144 5980 5485 3002 -1448 680 -144 C ATOM 1148 CD1 ILE A 144 74.587 45.529 54.052 1.00 44.89 C ANISOU 1148 CD1 ILE F 144 5198 7047 4812 -2738 1919 -773 C ATOM 1149 N ALA A 145 80.265 46.731 54.047 1.00 30.04 N ANISOU 1149 N ALA F 145 4019 4709 2687 51 -574 734 N ATOM 1150 CA ALA A 145 81.555 46.823 54.730 1.00 33.88 C ANISOU 1150 CA ALA F 145 4272 4899 3700 -516 -314 528 C ATOM 1151 C ALA A 145 82.542 45.890 54.052 1.00 32.88 C ANISOU 1151 C ALA F 145 3871 4994 3626 -722 282 533 C ATOM 1152 O ALA A 145 82.621 45.921 52.813 1.00 37.05 O ANISOU 1152 O ALA F 145 5636 4738 3703 -722 -285 559 O ATOM 1153 CB ALA A 145 81.408 46.491 56.209 1.00 31.60 C ANISOU 1153 CB ALA F 145 4304 4341 3363 -118 479 935 C ATOM 1154 N PHE A 146 83.273 45.059 54.792 1.00 32.14 N ANISOU 1154 N PHE F 146 4142 4992 3078 -336 1125 474 N ATOM 1155 CA PHE A 146 84.157 44.117 54.107 1.00 32.43 C ANISOU 1155 CA PHE F 146 4183 5097 3041 -475 853 228 C ATOM 1156 C PHE A 146 83.528 42.725 54.070 1.00 31.27 C ANISOU 1156 C PHE F 146 4169 4422 3293 -471 846 212 C ATOM 1157 O PHE A 146 84.220 41.743 53.756 1.00 35.15 O ANISOU 1157 O PHE F 146 4625 4822 3907 -252 620 -501 O ATOM 1158 CB PHE A 146 85.552 43.988 54.725 1.00 32.34 C ANISOU 1158 CB PHE F 146 4126 5133 3028 -936 384 31 C ATOM 1159 CG PHE A 146 86.408 45.204 54.399 1.00 36.84 C ANISOU 1159 CG PHE F 146 4333 5777 3886 -1021 -100 160 C ATOM 1160 CD1 PHE A 146 86.995 45.330 53.155 1.00 42.68 C ANISOU 1160 CD1 PHE F 146 4466 7257 4494 -1295 -187 -795 C ATOM 1161 CD2 PHE A 146 86.602 46.191 55.346 1.00 34.07 C ANISOU 1161 CD2 PHE F 146 3601 5135 4210 121 -789 -10 C ATOM 1162 CE1 PHE A 146 87.771 46.438 52.864 1.00 45.34 C ANISOU 1162 CE1 PHE F 146 4476 7702 5049 -1527 -157 -1240 C ATOM 1163 CE2 PHE A 146 87.373 47.297 55.074 1.00 35.10 C ANISOU 1163 CE2 PHE F 146 3813 5445 4079 116 -1337 176 C ATOM 1164 CZ PHE A 146 87.956 47.408 53.829 1.00 39.62 C ANISOU 1164 CZ PHE F 146 4236 6578 4238 -695 -785 -513 C ATOM 1165 N ASN A 147 82.241 42.632 54.377 1.00 31.88 N ANISOU 1165 N ASN F 147 4445 4628 3040 -483 137 78 N ATOM 1166 CA ASN A 147 81.610 41.322 54.211 1.00 31.70 C ANISOU 1166 CA ASN F 147 4438 4565 3042 -688 276 -26 C ATOM 1167 C ASN A 147 81.528 40.921 52.745 1.00 34.38 C ANISOU 1167 C ASN F 147 4673 5296 3095 -405 194 -487 C ATOM 1168 O ASN A 147 81.389 41.729 51.818 1.00 40.03 O ANISOU 1168 O ASN F 147 6438 5686 3087 254 632 390 O ATOM 1169 CB ASN A 147 80.198 41.369 54.801 1.00 30.43 C ANISOU 1169 CB ASN F 147 4384 4252 2927 -123 -373 45 C ATOM 1170 CG ASN A 147 80.270 41.655 56.290 1.00 30.24 C ANISOU 1170 CG ASN F 147 4651 3873 2967 1 -136 262 C ATOM 1171 OD1 ASN A 147 80.424 40.685 57.045 1.00 32.49 O ANISOU 1171 OD1 ASN F 147 4299 4953 3093 -219 -486 341 O ATOM 1172 ND2 ASN A 147 80.170 42.924 56.670 1.00 30.25 N ANISOU 1172 ND2 ASN F 147 4554 3366 3574 -380 304 317 N ATOM 1173 N GLU A 148 81.597 39.622 52.445 1.00 36.52 N ANISOU 1173 N GLU F 148 4784 5165 3926 -576 621 -647 N ATOM 1174 CA GLU A 148 81.525 39.250 51.044 1.00 37.62 C ANISOU 1174 CA GLU F 148 4800 5496 3996 -506 795 -628 C ATOM 1175 C GLU A 148 80.112 38.904 50.623 1.00 35.13 C ANISOU 1175 C GLU F 148 4193 5501 3653 -282 383 -550 C ATOM 1176 O GLU A 148 79.262 38.701 51.482 1.00 36.10 O ANISOU 1176 O GLU F 148 4942 5346 3428 -441 92 -134 O ATOM 1177 CB GLU A 148 82.517 38.098 50.824 1.00 44.63 C ANISOU 1177 CB GLU F 148 6139 5477 5341 -679 1299 -1418 C ATOM 1178 CG GLU A 148 83.710 38.738 50.092 1.00 62.51 C ANISOU 1178 CG GLU F 148 10150 6335 7266 -2672 -1198 -738 C ATOM 1179 CD GLU A 148 84.904 37.821 49.960 1.00 62.28 C ANISOU 1179 CD GLU F 148 10737 6366 6563 -2751 -91 -994 C ATOM 1180 OE1 GLU A 148 85.007 37.248 48.849 1.00 58.46 O ANISOU 1180 OE1 GLU F 148 8529 7728 5956 -589 -931 32 O ATOM 1181 OE2 GLU A 148 85.658 37.728 50.958 1.00 53.92 O ANISOU 1181 OE2 GLU F 148 7807 6685 5995 -228 -852 -345 O ATOM 1182 N PRO A 149 79.877 38.848 49.324 1.00 32.87 N ANISOU 1182 N PRO F 149 3807 5083 3601 -97 -179 -132 N ATOM 1183 CA PRO A 149 78.609 38.333 48.824 1.00 32.24 C ANISOU 1183 CA PRO F 149 4390 4418 3444 -319 -805 463 C ATOM 1184 C PRO A 149 78.394 36.936 49.408 1.00 31.02 C ANISOU 1184 C PRO F 149 3812 4107 3866 -8 -140 -98 C ATOM 1185 O PRO A 149 79.357 36.191 49.584 1.00 30.07 O ANISOU 1185 O PRO F 149 3975 4089 3359 -109 69 11 O ATOM 1186 CB PRO A 149 78.863 38.245 47.330 1.00 31.62 C ANISOU 1186 CB PRO F 149 4043 4309 3661 -329 -144 -207 C ATOM 1187 CG PRO A 149 79.893 39.294 47.046 1.00 34.44 C ANISOU 1187 CG PRO F 149 4321 5187 3579 -832 -344 -382 C ATOM 1188 CD PRO A 149 80.803 39.234 48.246 1.00 35.77 C ANISOU 1188 CD PRO F 149 4150 5686 3756 -783 18 -291 C ATOM 1189 N ALA A 150 77.156 36.596 49.718 1.00 31.18 N ANISOU 1189 N ALA F 150 3700 4110 4039 -107 -144 333 N ATOM 1190 CA ALA A 150 76.700 35.342 50.323 1.00 28.85 C ANISOU 1190 CA ALA F 150 3788 3648 3525 217 -129 -142 C ATOM 1191 C ALA A 150 77.216 35.237 51.750 1.00 30.57 C ANISOU 1191 C ALA F 150 4376 3691 3548 371 -19 -112 C ATOM 1192 O ALA A 150 77.275 34.134 52.290 1.00 31.66 O ANISOU 1192 O ALA F 150 4014 4233 3783 29 -88 363 O ATOM 1193 CB ALA A 150 77.094 34.110 49.524 1.00 31.71 C ANISOU 1193 CB ALA F 150 3074 4424 4551 -839 652 -1116 C ATOM 1194 N SER A 151 77.577 36.371 52.358 1.00 29.94 N ANISOU 1194 N SER F 151 3870 4227 3279 -100 -355 23 N ATOM 1195 CA SER A 151 77.853 36.355 53.780 1.00 28.79 C ANISOU 1195 CA SER F 151 3667 3912 3359 -130 -366 214 C ATOM 1196 C SER A 151 76.581 35.924 54.517 1.00 27.85 C ANISOU 1196 C SER F 151 3270 4162 3148 -5 -137 69 C ATOM 1197 O SER A 151 75.507 36.271 54.023 1.00 28.87 O ANISOU 1197 O SER F 151 3544 4607 2820 -650 -615 285 O ATOM 1198 CB SER A 151 78.221 37.729 54.349 1.00 29.68 C ANISOU 1198 CB SER F 151 3367 4612 3298 -169 -518 533 C ATOM 1199 OG SER A 151 79.549 38.116 54.026 1.00 34.72 O ANISOU 1199 OG SER F 151 3690 4948 4553 -486 -1143 1135 O ATOM 1200 N SER A 152 76.733 35.253 55.645 1.00 29.45 N ANISOU 1200 N SER F 152 3378 3942 3869 9 -659 386 N ATOM 1201 CA SER A 152 75.630 35.031 56.572 1.00 29.19 C ANISOU 1201 CA SER F 152 3469 4067 3556 16 -643 433 C ATOM 1202 C SER A 152 75.023 36.355 57.012 1.00 29.48 C ANISOU 1202 C SER F 152 3728 3893 3582 34 -663 526 C ATOM 1203 O SER A 152 75.739 37.333 57.299 1.00 29.07 O ANISOU 1203 O SER F 152 3750 3599 3698 168 -539 744 O ATOM 1204 CB SER A 152 76.105 34.257 57.811 1.00 24.29 C ANISOU 1204 CB SER F 152 2261 4031 2936 151 489 373 C ATOM 1205 OG SER A 152 75.048 34.260 58.771 1.00 30.65 O ANISOU 1205 OG SER F 152 4423 4323 2899 148 -104 292 O ATOM 1206 N LEU A 153 73.691 36.416 57.102 1.00 29.06 N ANISOU 1206 N LEU F 153 4048 4037 2954 -219 -370 477 N ATOM 1207 CA LEU A 153 73.036 37.644 57.560 1.00 29.26 C ANISOU 1207 CA LEU F 153 3685 3994 3440 -261 -742 284 C ATOM 1208 C LEU A 153 73.220 37.778 59.063 1.00 29.11 C ANISOU 1208 C LEU F 153 3316 4253 3491 209 -558 101 C ATOM 1209 O LEU A 153 72.861 38.794 59.664 1.00 34.08 O ANISOU 1209 O LEU F 153 4357 4097 4497 304 441 284 O ATOM 1210 CB LEU A 153 71.558 37.632 57.227 1.00 33.10 C ANISOU 1210 CB LEU F 153 3749 4053 4775 -216 131 228 C ATOM 1211 CG LEU A 153 71.072 38.333 55.952 1.00 40.02 C ANISOU 1211 CG LEU F 153 5950 5263 3992 -2329 133 679 C ATOM 1212 CD1 LEU A 153 72.141 38.420 54.880 1.00 36.67 C ANISOU 1212 CD1 LEU F 153 6870 4004 3059 -1329 1626 -51 C ATOM 1213 CD2 LEU A 153 69.828 37.646 55.395 1.00 35.55 C ANISOU 1213 CD2 LEU F 153 2763 5853 4889 200 331 967 C ATOM 1214 N ALA A 154 73.764 36.741 59.693 1.00 28.86 N ANISOU 1214 N ALA F 154 3772 3811 3384 -100 -231 365 N ATOM 1215 CA ALA A 154 74.069 36.853 61.118 1.00 30.37 C ANISOU 1215 CA ALA F 154 3746 4496 3297 -369 -386 198 C ATOM 1216 C ALA A 154 75.566 36.950 61.335 1.00 31.22 C ANISOU 1216 C ALA F 154 4347 4666 2850 -661 -348 317 C ATOM 1217 O ALA A 154 76.039 36.709 62.451 1.00 34.75 O ANISOU 1217 O ALA F 154 5023 4855 3323 -392 -1059 947 O ATOM 1218 CB ALA A 154 73.513 35.653 61.876 1.00 34.29 C ANISOU 1218 CB ALA F 154 4068 5230 3729 -356 -793 160 C ATOM 1219 N SER A 155 76.359 37.276 60.301 1.00 27.85 N ANISOU 1219 N SER F 155 3657 4121 2802 -121 7 9 N ATOM 1220 CA SER A 155 77.813 37.240 60.552 1.00 29.11 C ANISOU 1220 CA SER F 155 3680 4341 3039 -299 -34 162 C ATOM 1221 C SER A 155 78.190 38.353 61.514 1.00 31.02 C ANISOU 1221 C SER F 155 3935 4240 3611 -131 316 360 C ATOM 1222 O SER A 155 77.439 39.311 61.698 1.00 29.07 O ANISOU 1222 O SER F 155 4093 3993 2960 -410 506 489 O ATOM 1223 CB SER A 155 78.522 37.314 59.200 1.00 28.66 C ANISOU 1223 CB SER F 155 3994 4035 2860 -630 -380 718 C ATOM 1224 OG SER A 155 78.008 38.466 58.517 1.00 30.95 O ANISOU 1224 OG SER F 155 3936 4581 3242 -12 18 839 O ATOM 1225 N ARG A 156 79.346 38.271 62.166 1.00 27.27 N ANISOU 1225 N ARG F 156 3264 3955 3142 464 -1 470 N ATOM 1226 CA ARG A 156 79.778 39.198 63.201 1.00 28.27 C ANISOU 1226 CA ARG F 156 3079 4309 3353 470 18 544 C ATOM 1227 C ARG A 156 81.164 39.772 62.905 1.00 27.82 C ANISOU 1227 C ARG F 156 2907 3931 3731 789 -28 347 C ATOM 1228 O ARG A 156 81.797 39.343 61.934 1.00 31.42 O ANISOU 1228 O ARG F 156 4483 3701 3754 -136 705 427 O ATOM 1229 CB ARG A 156 79.818 38.475 64.554 1.00 30.35 C ANISOU 1229 CB ARG F 156 4010 4532 2991 289 -109 187 C ATOM 1230 CG ARG A 156 78.428 38.036 65.036 1.00 32.56 C ANISOU 1230 CG ARG F 156 4808 4586 2978 -232 -361 625 C ATOM 1231 CD ARG A 156 77.751 39.285 65.602 1.00 36.21 C ANISOU 1231 CD ARG F 156 5806 4472 3480 -146 -508 297 C ATOM 1232 NE ARG A 156 76.303 39.204 65.540 1.00 40.57 N ANISOU 1232 NE ARG F 156 6347 4722 4348 -532 -933 182 N ATOM 1233 CZ ARG A 156 75.493 40.183 65.928 1.00 40.13 C ANISOU 1233 CZ ARG F 156 5796 4720 4733 -761 -573 57 C ATOM 1234 NH1 ARG A 156 75.990 41.317 66.403 1.00 37.87 N ANISOU 1234 NH1 ARG F 156 5173 5635 3582 -493 -1594 379 N ATOM 1235 NH2 ARG A 156 74.189 39.983 65.824 1.00 40.93 N ANISOU 1235 NH2 ARG F 156 6082 4379 5092 -499 -635 1412 N ATOM 1236 N THR A 157 81.615 40.712 63.746 1.00 30.93 N ANISOU 1236 N THR F 157 3402 4458 3890 186 411 340 N ATOM 1237 CA THR A 157 82.873 41.420 63.558 1.00 31.02 C ANISOU 1237 CA THR F 157 3752 4415 3620 -155 491 575 C ATOM 1238 C THR A 157 84.012 40.427 63.414 1.00 30.19 C ANISOU 1238 C THR F 157 3483 4497 3492 48 735 555 C ATOM 1239 O THR A 157 84.079 39.480 64.209 1.00 35.36 O ANISOU 1239 O THR F 157 4388 4808 4240 93 111 919 O ATOM 1240 CB THR A 157 83.167 42.372 64.733 1.00 30.76 C ANISOU 1240 CB THR F 157 3447 4291 3950 77 433 279 C ATOM 1241 OG1 THR A 157 82.094 43.317 64.815 1.00 35.13 O ANISOU 1241 OG1 THR F 157 6169 4069 3109 -194 326 -108 O ATOM 1242 CG2 THR A 157 84.453 43.138 64.498 1.00 28.06 C ANISOU 1242 CG2 THR F 157 3457 4294 2910 150 280 74 C ATOM 1243 N ARG A 158 84.875 40.606 62.421 1.00 30.88 N ANISOU 1243 N ARG F 158 3677 4516 3538 -184 889 460 N ATOM 1244 CA ARG A 158 85.881 39.586 62.143 1.00 31.76 C ANISOU 1244 CA ARG F 158 3594 4736 3736 29 1033 278 C ATOM 1245 C ARG A 158 86.922 40.099 61.154 1.00 32.73 C ANISOU 1245 C ARG F 158 3919 4475 4043 -104 855 287 C ATOM 1246 O ARG A 158 86.726 41.120 60.514 1.00 34.08 O ANISOU 1246 O ARG F 158 4434 4672 3844 -90 510 247 O ATOM 1247 CB ARG A 158 85.233 38.314 61.580 1.00 34.38 C ANISOU 1247 CB ARG F 158 3660 5187 4217 9 1226 540 C ATOM 1248 CG ARG A 158 84.738 38.412 60.139 1.00 36.00 C ANISOU 1248 CG ARG F 158 4251 5275 4153 -123 1535 379 C ATOM 1249 CD ARG A 158 83.676 37.359 59.853 1.00 34.46 C ANISOU 1249 CD ARG F 158 4145 5227 3722 -368 735 1012 C ATOM 1250 NE ARG A 158 83.172 37.346 58.466 1.00 33.95 N ANISOU 1250 NE ARG F 158 4630 4450 3821 -159 1221 798 N ATOM 1251 CZ ARG A 158 82.205 38.170 58.055 1.00 36.78 C ANISOU 1251 CZ ARG F 158 6016 4217 3740 -394 521 541 C ATOM 1252 NH1 ARG A 158 81.703 39.030 58.946 1.00 31.31 N ANISOU 1252 NH1 ARG F 158 3855 4426 3616 -117 9 704 N ATOM 1253 NH2 ARG A 158 81.763 38.145 56.818 1.00 31.35 N ANISOU 1253 NH2 ARG F 158 3919 4507 3486 432 -249 696 N ATOM 1254 N ILE A 159 88.022 39.373 61.031 1.00 35.47 N ANISOU 1254 N ILE F 159 4542 4492 4441 -50 1111 179 N ATOM 1255 CA ILE A 159 89.065 39.728 60.090 1.00 35.07 C ANISOU 1255 CA ILE F 159 4407 4135 4782 416 896 -14 C ATOM 1256 C ILE A 159 88.701 39.147 58.718 1.00 37.45 C ANISOU 1256 C ILE F 159 4806 4741 4684 -268 875 -130 C ATOM 1257 O ILE A 159 88.126 38.058 58.659 1.00 39.31 O ANISOU 1257 O ILE F 159 4878 5013 5044 341 1309 -5 O ATOM 1258 CB ILE A 159 90.450 39.198 60.481 1.00 39.65 C ANISOU 1258 CB ILE F 159 5410 4542 5112 -294 284 485 C ATOM 1259 CG1 ILE A 159 91.570 39.794 59.623 1.00 41.71 C ANISOU 1259 CG1 ILE F 159 5362 5294 5191 -823 877 -95 C ATOM 1260 CG2 ILE A 159 90.475 37.676 60.431 1.00 38.23 C ANISOU 1260 CG2 ILE F 159 5699 3317 5509 -405 418 757 C ATOM 1261 CD1 ILE A 159 92.954 39.545 60.187 1.00 40.62 C ANISOU 1261 CD1 ILE F 159 5716 4824 4893 -491 821 -362 C ATOM 1262 N LYS A 160 89.047 39.888 57.685 1.00 40.97 N ANISOU 1262 N LYS F 160 5651 5057 4861 -739 423 378 N ATOM 1263 CA LYS A 160 88.826 39.576 56.298 1.00 43.00 C ANISOU 1263 CA LYS F 160 6809 4735 4795 -446 519 202 C ATOM 1264 C LYS A 160 90.096 39.825 55.468 1.00 44.52 C ANISOU 1264 C LYS F 160 6225 5368 5323 -675 1661 -868 C ATOM 1265 O LYS A 160 90.857 40.750 55.768 1.00 46.37 O ANISOU 1265 O LYS F 160 6438 5703 5476 -894 1992 -589 O ATOM 1266 CB LYS A 160 87.701 40.419 55.671 1.00 40.85 C ANISOU 1266 CB LYS F 160 5643 4962 4918 -153 508 397 C ATOM 1267 CG LYS A 160 86.294 40.178 56.176 1.00 43.72 C ANISOU 1267 CG LYS F 160 6473 4746 5394 -387 258 512 C ATOM 1268 CD LYS A 160 86.014 38.693 56.332 1.00 47.22 C ANISOU 1268 CD LYS F 160 5920 5840 6181 -889 443 211 C ATOM 1269 CE LYS A 160 85.253 38.145 55.145 1.00 51.24 C ANISOU 1269 CE LYS F 160 6579 6643 6247 -1400 612 143 C ATOM 1270 NZ LYS A 160 85.968 38.193 53.843 1.00 52.76 N ANISOU 1270 NZ LYS F 160 8506 5514 6026 -562 306 357 N ATOM 1271 N THR A 161 90.235 38.986 54.439 1.00 46.07 N ANISOU 1271 N THR F 161 6196 5573 5734 95 1582 -914 N ATOM 1272 CA THR A 161 91.257 39.139 53.414 1.00 50.03 C ANISOU 1272 CA THR F 161 6913 6464 5630 -308 1964 -1436 C ATOM 1273 C THR A 161 90.741 39.994 52.270 1.00 49.72 C ANISOU 1273 C THR F 161 6611 6875 5404 41 1749 -1746 C ATOM 1274 O THR A 161 89.817 39.596 51.568 1.00 51.50 O ANISOU 1274 O THR F 161 5747 7772 6050 61 770 -337 O ATOM 1275 CB THR A 161 91.669 37.770 52.855 1.00 50.46 C ANISOU 1275 CB THR F 161 6768 6590 5816 -161 1539 -1616 C ATOM 1276 OG1 THR A 161 92.088 36.948 53.955 1.00 55.20 O ANISOU 1276 OG1 THR F 161 6600 7971 6401 191 1818 -728 O ATOM 1277 CG2 THR A 161 92.850 37.902 51.907 1.00 52.69 C ANISOU 1277 CG2 THR F 161 4577 8539 6904 -166 2426 -3197 C ATOM 1278 N LEU A 162 91.281 41.181 52.061 1.00 50.34 N ANISOU 1278 N LEU F 162 6449 7256 5423 -457 1918 -1694 N ATOM 1279 CA LEU A 162 90.633 42.086 51.109 1.00 52.65 C ANISOU 1279 CA LEU F 162 6286 8091 5628 -161 1548 -1472 C ATOM 1280 C LEU A 162 90.573 41.534 49.696 1.00 52.23 C ANISOU 1280 C LEU F 162 5897 8430 5516 386 1306 -1358 C ATOM 1281 O LEU A 162 91.422 40.700 49.355 1.00 62.49 O ANISOU 1281 O LEU F 162 8039 8700 7004 -362 1496 -2942 O ATOM 1282 CB LEU A 162 91.393 43.418 51.160 1.00 53.19 C ANISOU 1282 CB LEU F 162 6314 8196 5699 -499 1777 -1522 C ATOM 1283 CG LEU A 162 91.443 44.046 52.556 1.00 52.93 C ANISOU 1283 CG LEU F 162 6606 7838 5667 13 1777 -1363 C ATOM 1284 CD1 LEU A 162 92.072 45.421 52.476 1.00 55.07 C ANISOU 1284 CD1 LEU F 162 6561 7050 7311 156 2360 -995 C ATOM 1285 CD2 LEU A 162 90.034 44.053 53.122 1.00 57.05 C ANISOU 1285 CD2 LEU F 162 8865 8972 3838 -1552 778 -482 C ATOM 1286 N THR A 163 89.619 41.952 48.861 1.00 59.10 N ANISOU 1286 N THR F 163 6302 9840 6313 -767 1535 -340 N ATOM 1287 CA THR A 163 89.611 41.457 47.479 1.00 67.97 C ANISOU 1287 CA THR F 163 8737 10769 6321 -2093 2043 -691 C ATOM 1288 C THR A 163 90.505 42.318 46.585 1.00 72.03 C ANISOU 1288 C THR F 163 9650 11375 6344 -2327 1519 -773 C ATOM 1289 O THR A 163 90.655 43.513 46.839 1.00 63.46 O ANISOU 1289 O THR F 163 9754 9523 4834 -2098 377 -773 O ATOM 1290 CB THR A 163 88.207 41.417 46.849 1.00 67.87 C ANISOU 1290 CB THR F 163 8532 10536 6719 -1473 2303 -297 C ATOM 1291 OG1 THR A 163 87.793 42.754 46.506 1.00 77.41 O ANISOU 1291 OG1 THR F 163 9711 11701 8001 -1467 -319 417 O ATOM 1292 CG2 THR A 163 87.152 40.866 47.804 1.00 61.67 C ANISOU 1292 CG2 THR F 163 6295 9323 7815 -351 2422 -293 C ATOM 1293 N HIS A 164 91.090 41.730 45.554 1.00 73.18 N ANISOU 1293 N HIS F 164 8953 11950 6903 -2104 1660 -1261 N ATOM 1294 CA HIS A 164 91.906 42.441 44.580 1.00 79.94 C ANISOU 1294 CA HIS F 164 10826 12269 7277 -2713 673 -1193 C ATOM 1295 C HIS A 164 91.206 43.712 44.115 1.00 75.86 C ANISOU 1295 C HIS F 164 10789 12290 5744 -2880 480 -1278 C ATOM 1296 O HIS A 164 91.772 44.798 44.133 1.00 68.07 O ANISOU 1296 O HIS F 164 10732 12117 3012 -3617 -310 -48 O ATOM 1297 CB HIS A 164 92.180 41.554 43.375 1.00 86.94 C ANISOU 1297 CB HIS F 164 11525 12664 8842 -3047 658 -3009 C ATOM 1298 CG HIS A 164 93.521 41.709 42.733 1.00 98.83 C ANISOU 1298 CG HIS F 164 13596 13511 10445 -4228 -13 -3227 C ATOM 1299 ND1 HIS A 164 94.681 41.953 43.445 1.00104.21 N ANISOU 1299 ND1 HIS F 164 14138 14089 11368 -5006 -781 -2512 N ATOM 1300 CD2 HIS A 164 93.885 41.647 41.423 1.00102.90 C ANISOU 1300 CD2 HIS F 164 14181 14168 10747 -4985 -1232 -3005 C ATOM 1301 CE1 HIS A 164 95.705 42.034 42.603 1.00107.01 C ANISOU 1301 CE1 HIS F 164 14524 14378 11757 -5151 -1430 -2348 C ATOM 1302 NE2 HIS A 164 95.249 41.852 41.368 1.00106.55 N ANISOU 1302 NE2 HIS F 164 14544 14352 11590 -5250 -1668 -2462 N ATOM 1303 N ASP A 165 89.944 43.568 43.723 1.00 72.18 N ANISOU 1303 N ASP F 165 9561 12182 5684 -2138 1484 -1623 N ATOM 1304 CA ASP A 165 89.146 44.741 43.372 1.00 77.60 C ANISOU 1304 CA ASP F 165 11006 12333 6146 -1786 1999 -1092 C ATOM 1305 C ASP A 165 89.179 45.800 44.462 1.00 74.61 C ANISOU 1305 C ASP F 165 9901 12590 5858 -1162 1374 -630 C ATOM 1306 O ASP A 165 89.118 47.008 44.211 1.00 76.73 O ANISOU 1306 O ASP F 165 10896 11798 6461 -813 831 -553 O ATOM 1307 CB ASP A 165 87.709 44.292 43.104 1.00 85.81 C ANISOU 1307 CB ASP F 165 12889 12470 7243 -2487 3699 -1308 C ATOM 1308 CG ASP A 165 87.677 43.253 41.993 1.00 94.21 C ANISOU 1308 CG ASP F 165 14915 12585 8295 -2725 5300 -1274 C ATOM 1309 OD1 ASP A 165 88.641 42.459 41.914 1.00108.17 O ANISOU 1309 OD1 ASP F 165 16354 12710 12037 -2263 7768 -1380 O ATOM 1310 OD2 ASP A 165 86.705 43.248 41.208 1.00 97.35 O ANISOU 1310 OD2 ASP F 165 17132 13617 6241 -2539 4483 -704 O ATOM 1311 N THR A 166 89.275 45.364 45.722 1.00 74.67 N ANISOU 1311 N THR F 166 9546 12954 5873 -1010 1398 -554 N ATOM 1312 CA THR A 166 89.296 46.363 46.790 1.00 68.60 C ANISOU 1312 CA THR F 166 7758 12833 5476 -437 336 -156 C ATOM 1313 C THR A 166 90.695 46.926 47.010 1.00 68.94 C ANISOU 1313 C THR F 166 7970 12883 5341 -542 -156 716 C ATOM 1314 O THR A 166 90.820 48.128 47.247 1.00 68.20 O ANISOU 1314 O THR F 166 7559 12731 5624 -692 -530 1061 O ATOM 1315 CB THR A 166 88.790 45.830 48.147 1.00 72.37 C ANISOU 1315 CB THR F 166 9155 12702 5639 -1043 -61 -362 C ATOM 1316 OG1 THR A 166 87.493 45.236 47.998 1.00 75.94 O ANISOU 1316 OG1 THR F 166 8668 12928 7257 -920 327 -1882 O ATOM 1317 CG2 THR A 166 88.667 47.002 49.117 1.00 74.00 C ANISOU 1317 CG2 THR F 166 9650 13247 5218 -1212 624 39 C ATOM 1318 N ARG A 167 91.724 46.084 46.950 1.00 69.78 N ANISOU 1318 N ARG F 167 8682 12889 4941 -548 562 511 N ATOM 1319 CA ARG A 167 93.065 46.643 47.125 1.00 71.95 C ANISOU 1319 CA ARG F 167 8780 12745 5814 -629 917 -407 C ATOM 1320 C ARG A 167 93.309 47.606 45.958 1.00 74.23 C ANISOU 1320 C ARG F 167 8941 13769 5493 -1343 846 -439 C ATOM 1321 O ARG A 167 93.717 48.756 46.109 1.00 78.16 O ANISOU 1321 O ARG F 167 8228 14833 6636 -2496 226 -189 O ATOM 1322 CB ARG A 167 94.165 45.599 47.170 1.00 77.63 C ANISOU 1322 CB ARG F 167 9638 12639 7221 -665 1124 -961 C ATOM 1323 CG ARG A 167 93.833 44.207 47.636 1.00 81.73 C ANISOU 1323 CG ARG F 167 10758 12178 8116 -257 -90 -165 C ATOM 1324 CD ARG A 167 94.139 43.964 49.100 1.00 87.05 C ANISOU 1324 CD ARG F 167 12778 11970 8326 -590 -56 301 C ATOM 1325 NE ARG A 167 94.954 42.806 49.412 1.00 92.77 N ANISOU 1325 NE ARG F 167 14409 11696 9144 -662 -296 517 N ATOM 1326 CZ ARG A 167 94.687 41.678 50.041 1.00 95.37 C ANISOU 1326 CZ ARG F 167 15380 11275 9580 -374 -904 1145 C ATOM 1327 NH1 ARG A 167 93.497 41.379 50.542 1.00 94.39 N ANISOU 1327 NH1 ARG F 167 15117 11435 9312 -231 -1424 1589 N ATOM 1328 NH2 ARG A 167 95.636 40.753 50.199 1.00110.50 N ANISOU 1328 NH2 ARG F 167 19973 11216 10798 -1808 -3257 4175 N ATOM 1329 N VAL A 168 93.016 47.059 44.785 1.00 80.95 N ANISOU 1329 N VAL F 168 10812 14447 5497 -2185 1339 -777 N ATOM 1330 CA VAL A 168 93.082 47.799 43.545 1.00 84.04 C ANISOU 1330 CA VAL F 168 12024 14446 5461 -2415 1114 -475 C ATOM 1331 C VAL A 168 92.392 49.146 43.681 1.00 84.40 C ANISOU 1331 C VAL F 168 12875 13943 5251 -2397 603 -261 C ATOM 1332 O VAL A 168 93.036 50.174 43.499 1.00 89.82 O ANISOU 1332 O VAL F 168 12314 15343 6472 -1740 2248 -1764 O ATOM 1333 CB VAL A 168 92.412 47.024 42.394 1.00 88.21 C ANISOU 1333 CB VAL F 168 13524 14378 5615 -3379 1719 -807 C ATOM 1334 CG1 VAL A 168 91.893 48.000 41.348 1.00 86.04 C ANISOU 1334 CG1 VAL F 168 14085 12505 6102 -3940 1902 -833 C ATOM 1335 CG2 VAL A 168 93.398 46.026 41.807 1.00 86.16 C ANISOU 1335 CG2 VAL F 168 11934 14947 5855 -1949 1013 -643 C ATOM 1336 N ALA A 169 91.110 49.141 44.005 1.00 91.57 N ANISOU 1336 N ALA F 169 15364 13755 5673 -3339 -113 804 N ATOM 1337 CA ALA A 169 90.375 50.395 44.151 1.00 95.17 C ANISOU 1337 CA ALA F 169 16049 13584 6528 -3524 1372 390 C ATOM 1338 C ALA A 169 90.783 51.216 45.371 1.00102.07 C ANISOU 1338 C ALA F 169 17256 14134 7393 -4115 2423 545 C ATOM 1339 O ALA A 169 90.217 52.277 45.672 1.00106.85 O ANISOU 1339 O ALA F 169 19119 13265 8212 -5055 4172 -586 O ATOM 1340 CB ALA A 169 88.885 50.068 44.185 1.00103.83 C ANISOU 1340 CB ALA F 169 17666 14087 7697 -4586 2652 87 C ATOM 1341 N ASN A 170 91.789 50.763 46.129 1.00106.51 N ANISOU 1341 N ASN F 170 18134 14836 7500 -4499 2029 1062 N ATOM 1342 CA ASN A 170 92.209 51.577 47.276 1.00109.84 C ANISOU 1342 CA ASN F 170 18334 15718 7681 -5454 2226 978 C ATOM 1343 C ASN A 170 93.704 51.875 47.195 1.00112.59 C ANISOU 1343 C ASN F 170 18483 15901 8396 -5599 1805 941 C ATOM 1344 O ASN A 170 94.229 52.725 47.938 1.00116.92 O ANISOU 1344 O ASN F 170 21676 16275 6474 -7495 3171 1897 O ATOM 1345 CB ASN A 170 91.841 50.900 48.596 1.00107.00 C ANISOU 1345 CB ASN F 170 17223 15854 7580 -4994 2601 690 C ATOM 1346 CG ASN A 170 90.410 51.120 49.047 1.00104.44 C ANISOU 1346 CG ASN F 170 16237 15763 7682 -4573 2828 452 C ATOM 1347 OD1 ASN A 170 89.657 51.916 48.494 1.00109.05 O ANISOU 1347 OD1 ASN F 170 16961 15826 8648 -4927 1518 639 O ATOM 1348 ND2 ASN A 170 89.981 50.396 50.086 1.00 90.72 N ANISOU 1348 ND2 ASN F 170 11283 14971 8214 -2336 4491 -806 N ATOM 1349 N SER A 171 94.419 51.213 46.288 1.00110.23 N ANISOU 1349 N SER F 171 17178 15892 8812 -4576 354 679 N ATOM 1350 CA SER A 171 95.861 51.418 46.137 1.00111.31 C ANISOU 1350 CA SER F 171 17038 15580 9674 -4280 -170 887 C ATOM 1351 C SER A 171 96.243 52.887 45.973 1.00111.01 C ANISOU 1351 C SER F 171 17047 15238 9894 -4199 -5 780 C ATOM 1352 O SER A 171 97.379 53.249 46.309 1.00115.28 O ANISOU 1352 O SER F 171 17036 16296 10469 -5295 -2437 1977 O ATOM 1353 CB SER A 171 96.403 50.612 44.948 1.00111.07 C ANISOU 1353 CB SER F 171 16913 15240 10048 -3695 -673 693 C ATOM 1354 OG SER A 171 95.376 49.929 44.242 1.00113.97 O ANISOU 1354 OG SER F 171 18978 14524 9800 -4234 653 538 O ATOM 1355 N ARG A 172 95.333 53.712 45.473 1.00110.85 N ANISOU 1355 N ARG F 172 17451 14821 9847 -3968 200 169 N ATOM 1356 CA ARG A 172 95.449 55.144 45.258 1.00111.98 C ANISOU 1356 CA ARG F 172 17665 14906 9976 -4058 -794 10 C ATOM 1357 C ARG A 172 95.788 55.869 46.553 1.00111.03 C ANISOU 1357 C ARG F 172 16172 15559 10454 -3932 -939 -262 C ATOM 1358 O ARG A 172 96.629 56.763 46.657 1.00112.06 O ANISOU 1358 O ARG F 172 16730 16836 9010 -5744 -1975 -11 O ATOM 1359 CB ARG A 172 94.163 55.719 44.660 1.00116.98 C ANISOU 1359 CB ARG F 172 19431 14785 10230 -3822 -1089 65 C ATOM 1360 CG ARG A 172 92.944 55.748 45.561 1.00128.53 C ANISOU 1360 CG ARG F 172 22686 15019 11132 -4938 -1604 -14 C ATOM 1361 CD ARG A 172 92.410 57.153 45.789 1.00133.23 C ANISOU 1361 CD ARG F 172 24043 14646 11932 -4849 -1006 -529 C ATOM 1362 NE ARG A 172 90.974 57.259 45.564 1.00140.27 N ANISOU 1362 NE ARG F 172 25830 14832 12636 -5439 -672 -487 N ATOM 1363 CZ ARG A 172 90.227 58.360 45.528 1.00142.46 C ANISOU 1363 CZ ARG F 172 26138 14766 13223 -5418 -605 -69 C ATOM 1364 NH1 ARG A 172 90.762 59.576 45.710 1.00146.19 N ANISOU 1364 NH1 ARG F 172 26094 15488 13962 -4749 -833 543 N ATOM 1365 NH2 ARG A 172 88.914 58.280 45.309 1.00148.11 N ANISOU 1365 NH2 ARG F 172 27294 15026 13955 -5942 -745 288 N ATOM 1366 N PHE A 173 95.091 55.455 47.618 1.00 99.08 N ANISOU 1366 N PHE F 173 12166 15154 10327 -1652 -98 -625 N ATOM 1367 CA PHE A 173 95.495 56.040 48.891 1.00 95.56 C ANISOU 1367 CA PHE F 173 11181 14684 10441 -1264 -294 -16 C ATOM 1368 C PHE A 173 96.861 55.507 49.252 1.00 93.43 C ANISOU 1368 C PHE F 173 10204 14403 10892 -1050 -663 -317 C ATOM 1369 O PHE A 173 97.699 56.237 49.786 1.00 90.44 O ANISOU 1369 O PHE F 173 8772 14217 11373 -1673 -2556 -482 O ATOM 1370 CB PHE A 173 94.451 55.720 49.956 1.00 90.93 C ANISOU 1370 CB PHE F 173 10884 13929 9734 -1337 138 461 C ATOM 1371 CG PHE A 173 93.065 56.079 49.428 1.00 92.38 C ANISOU 1371 CG PHE F 173 11175 14171 9755 -1241 -225 1018 C ATOM 1372 CD1 PHE A 173 92.536 57.339 49.627 1.00 91.14 C ANISOU 1372 CD1 PHE F 173 11094 14284 9251 -1076 -347 1420 C ATOM 1373 CD2 PHE A 173 92.331 55.134 48.740 1.00 91.66 C ANISOU 1373 CD2 PHE F 173 10907 13980 9941 -1040 -423 1644 C ATOM 1374 CE1 PHE A 173 91.280 57.655 49.145 1.00 91.11 C ANISOU 1374 CE1 PHE F 173 11004 14444 9172 -992 -551 1730 C ATOM 1375 CE2 PHE A 173 91.072 55.445 48.257 1.00 91.80 C ANISOU 1375 CE2 PHE F 173 10541 14096 10243 -794 -985 2187 C ATOM 1376 CZ PHE A 173 90.545 56.705 48.461 1.00 90.64 C ANISOU 1376 CZ PHE F 173 10223 14319 9898 -703 -1053 2344 C ATOM 1377 N PHE A 174 97.164 54.240 48.965 1.00 98.63 N ANISOU 1377 N PHE F 174 10789 14856 11831 -833 -369 -1379 N ATOM 1378 CA PHE A 174 98.530 53.817 49.352 1.00102.64 C ANISOU 1378 CA PHE F 174 12059 14291 12650 -629 -398 -2078 C ATOM 1379 C PHE A 174 99.477 54.210 48.225 1.00108.34 C ANISOU 1379 C PHE F 174 12786 14844 13533 -651 -1222 -2243 C ATOM 1380 O PHE A 174 100.023 53.373 47.520 1.00113.25 O ANISOU 1380 O PHE F 174 14713 14498 13819 212 -2451 -2631 O ATOM 1381 CB PHE A 174 98.551 52.338 49.715 1.00100.89 C ANISOU 1381 CB PHE F 174 12146 13993 12196 -438 -292 -2674 C ATOM 1382 CG PHE A 174 98.123 52.078 51.164 1.00101.23 C ANISOU 1382 CG PHE F 174 11869 14360 12232 -610 -257 -2760 C ATOM 1383 CD1 PHE A 174 96.799 52.238 51.537 1.00101.15 C ANISOU 1383 CD1 PHE F 174 11722 14554 12156 -813 146 -2915 C ATOM 1384 CD2 PHE A 174 99.049 51.694 52.122 1.00 99.50 C ANISOU 1384 CD2 PHE F 174 11610 14369 11828 -479 172 -2977 C ATOM 1385 CE1 PHE A 174 96.404 52.009 52.841 1.00100.80 C ANISOU 1385 CE1 PHE F 174 11514 14644 12141 -931 174 -2836 C ATOM 1386 CE2 PHE A 174 98.670 51.471 53.431 1.00 98.42 C ANISOU 1386 CE2 PHE F 174 11506 14380 11508 -655 925 -3316 C ATOM 1387 CZ PHE A 174 97.350 51.651 53.789 1.00100.40 C ANISOU 1387 CZ PHE F 174 11676 14579 11892 -1087 596 -3021 C ATOM 1388 N ASP A 175 99.633 55.515 48.124 1.00112.09 N ANISOU 1388 N ASP F 175 12995 15173 14422 -436 -1786 -1485 N ATOM 1389 CA ASP A 175 99.820 56.405 47.011 1.00115.08 C ANISOU 1389 CA ASP F 175 13761 15399 14564 -948 -2093 -893 C ATOM 1390 C ASP A 175 99.973 55.531 45.748 1.00115.71 C ANISOU 1390 C ASP F 175 14276 15528 14161 -1845 -1488 -256 C ATOM 1391 O ASP A 175 101.061 55.197 45.310 1.00101.68 O ANISOU 1391 O ASP F 175 8131 15542 14961 -499 -1721 -833 O ATOM 1392 CB ASP A 175 100.965 57.413 47.107 1.00113.42 C ANISOU 1392 CB ASP F 175 13335 15222 14536 -254 -2220 -790 C ATOM 1393 CG ASP A 175 100.516 58.832 46.744 1.00114.59 C ANISOU 1393 CG ASP F 175 14314 14779 14446 34 -1892 -751 C ATOM 1394 OD1 ASP A 175 99.307 59.030 46.451 1.00117.13 O ANISOU 1394 OD1 ASP F 175 16380 14695 13429 52 333 -1017 O ATOM 1395 OD2 ASP A 175 101.351 59.767 46.736 1.00114.39 O ANISOU 1395 OD2 ASP F 175 13894 14998 14569 1145 -918 -1667 O ATOM 1396 N ASN A 176 98.769 55.227 45.280 1.00121.11 N ANISOU 1396 N ASN F 176 16259 15316 14442 -2523 -1645 359 N ATOM 1397 CA ASN A 176 98.447 54.574 44.022 1.00119.04 C ANISOU 1397 CA ASN F 176 16189 14492 14550 -2736 -1505 839 C ATOM 1398 C ASN A 176 99.324 53.354 43.777 1.00119.68 C ANISOU 1398 C ASN F 176 16495 14491 14488 -2749 -1624 469 C ATOM 1399 O ASN A 176 99.690 53.024 42.652 1.00124.72 O ANISOU 1399 O ASN F 176 17735 14741 14911 -3286 -2318 -305 O ATOM 1400 CB ASN A 176 98.566 55.639 42.919 1.00122.57 C ANISOU 1400 CB ASN F 176 17638 13976 14957 -3487 -2272 1753 C ATOM 1401 CG ASN A 176 98.164 57.016 43.440 1.00119.83 C ANISOU 1401 CG ASN F 176 17236 13557 14738 -3318 -2834 2375 C ATOM 1402 OD1 ASN A 176 99.012 57.863 43.726 1.00112.39 O ANISOU 1402 OD1 ASN F 176 17127 13114 12463 -3026 -3341 3384 O ATOM 1403 ND2 ASN A 176 96.866 57.251 43.593 1.00118.58 N ANISOU 1403 ND2 ASN F 176 15982 13336 15738 -2785 -4764 2945 N ATOM 1404 N ASP A 177 99.639 52.685 44.876 1.00121.16 N ANISOU 1404 N ASP F 177 16699 14395 14941 -2643 -2025 583 N ATOM 1405 CA ASP A 177 100.606 51.602 44.960 1.00120.08 C ANISOU 1405 CA ASP F 177 16473 14274 14877 -2799 -2648 -20 C ATOM 1406 C ASP A 177 99.970 50.361 45.573 1.00116.88 C ANISOU 1406 C ASP F 177 16061 14590 13758 -2498 -1936 -826 C ATOM 1407 O ASP A 177 99.953 50.192 46.795 1.00116.90 O ANISOU 1407 O ASP F 177 15584 15979 12852 -4161 -1973 -6623 O ATOM 1408 CB ASP A 177 101.799 52.126 45.756 1.00123.47 C ANISOU 1408 CB ASP F 177 16783 14388 15742 -4064 -3476 197 C ATOM 1409 CG ASP A 177 102.731 51.073 46.327 1.00128.08 C ANISOU 1409 CG ASP F 177 17759 14285 16618 -4454 -4378 444 C ATOM 1410 OD1 ASP A 177 102.795 49.968 45.740 1.00128.91 O ANISOU 1410 OD1 ASP F 177 17629 14208 17141 -3845 -5296 -103 O ATOM 1411 OD2 ASP A 177 103.402 51.356 47.355 1.00134.42 O ANISOU 1411 OD2 ASP F 177 18686 14781 17606 -5619 -4369 1175 O ATOM 1412 N VAL A 178 99.442 49.496 44.711 1.00118.66 N ANISOU 1412 N VAL F 178 16676 14823 13586 -3116 -1669 -593 N ATOM 1413 CA VAL A 178 98.792 48.247 45.057 1.00114.96 C ANISOU 1413 CA VAL F 178 16440 14173 13065 -2790 -1097 -961 C ATOM 1414 C VAL A 178 99.794 47.160 45.452 1.00114.77 C ANISOU 1414 C VAL F 178 16742 13959 12908 -3083 -1201 -979 C ATOM 1415 O VAL A 178 99.909 46.144 44.762 1.00114.89 O ANISOU 1415 O VAL F 178 16482 13515 13656 -3279 -892 -779 O ATOM 1416 CB VAL A 178 97.950 47.715 43.875 1.00114.12 C ANISOU 1416 CB VAL F 178 16879 14133 12349 -2691 -1395 -955 C ATOM 1417 CG1 VAL A 178 96.532 47.378 44.303 1.00100.42 C ANISOU 1417 CG1 VAL F 178 16419 12787 8949 -1649 -3 -1912 C ATOM 1418 CG2 VAL A 178 97.948 48.741 42.736 1.00108.95 C ANISOU 1418 CG2 VAL F 178 14263 13668 13463 -2327 -635 -648 C ATOM 1419 N ASN A 179 100.507 47.372 46.549 1.00116.58 N ANISOU 1419 N ASN F 179 17945 13795 12556 -3598 -1127 -1455 N ATOM 1420 CA ASN A 179 101.480 46.445 47.107 1.00116.97 C ANISOU 1420 CA ASN F 179 19049 13285 12108 -3906 -966 -1844 C ATOM 1421 C ASN A 179 101.672 46.726 48.602 1.00115.42 C ANISOU 1421 C ASN F 179 18661 12859 12334 -4366 -546 -1960 C ATOM 1422 O ASN A 179 102.187 45.897 49.341 1.00111.17 O ANISOU 1422 O ASN F 179 18670 11973 11594 -4270 -82 -2598 O ATOM 1423 CB ASN A 179 102.839 46.550 46.414 1.00126.19 C ANISOU 1423 CB ASN F 179 20612 14193 13140 -4450 -586 -3101 C ATOM 1424 CG ASN A 179 102.981 45.677 45.183 1.00133.83 C ANISOU 1424 CG ASN F 179 21547 15588 13714 -4664 -1 -3782 C ATOM 1425 OD1 ASN A 179 102.722 44.469 45.214 1.00141.47 O ANISOU 1425 OD1 ASN F 179 22131 16168 15453 -3717 104 -5270 O ATOM 1426 ND2 ASN A 179 103.405 46.281 44.075 1.00140.96 N ANISOU 1426 ND2 ASN F 179 22307 17586 13667 -5567 -254 -4832 N ATOM 1427 N GLN A 180 101.239 47.922 48.968 1.00113.09 N ANISOU 1427 N GLN F 180 18065 12522 12383 -4550 -539 -1364 N ATOM 1428 CA GLN A 180 101.320 48.450 50.318 1.00111.28 C ANISOU 1428 CA GLN F 180 17368 12221 12694 -4603 -233 -1241 C ATOM 1429 C GLN A 180 99.965 48.409 51.026 1.00107.47 C ANISOU 1429 C GLN F 180 16498 11752 12582 -4276 637 -1433 C ATOM 1430 O GLN A 180 99.920 48.268 52.249 1.00110.04 O ANISOU 1430 O GLN F 180 17836 11203 12770 -6924 -34 -201 O ATOM 1431 CB GLN A 180 101.859 49.886 50.290 1.00115.85 C ANISOU 1431 CB GLN F 180 17179 13290 13550 -5064 -396 -286 C ATOM 1432 CG GLN A 180 103.075 50.081 51.190 1.00120.97 C ANISOU 1432 CG GLN F 180 17873 13992 14097 -4886 274 156 C ATOM 1433 CD GLN A 180 103.195 48.981 52.239 1.00126.63 C ANISOU 1433 CD GLN F 180 19208 14437 14468 -4872 -191 735 C ATOM 1434 OE1 GLN A 180 102.622 49.082 53.323 1.00134.88 O ANISOU 1434 OE1 GLN F 180 21173 16732 13344 -5194 390 1458 O ATOM 1435 NE2 GLN A 180 103.929 47.921 51.913 1.00134.37 N ANISOU 1435 NE2 GLN F 180 20493 13494 17068 -4682 -570 1136 N ATOM 1436 N VAL A 181 98.912 48.534 50.225 1.00 91.41 N ANISOU 1436 N VAL F 181 12209 11447 11077 -2514 -691 -1245 N ATOM 1437 CA VAL A 181 97.531 48.340 50.656 1.00 87.48 C ANISOU 1437 CA VAL F 181 12009 11197 10032 -2443 244 -1415 C ATOM 1438 C VAL A 181 97.456 47.123 51.576 1.00 80.41 C ANISOU 1438 C VAL F 181 10823 10634 9095 -1836 1155 -2706 C ATOM 1439 O VAL A 181 97.789 46.034 51.097 1.00 92.19 O ANISOU 1439 O VAL F 181 11677 11840 11511 -1460 997 -4631 O ATOM 1440 CB VAL A 181 96.581 48.133 49.460 1.00 90.28 C ANISOU 1440 CB VAL F 181 12256 11761 10287 -2070 945 -1371 C ATOM 1441 CG1 VAL A 181 95.125 48.319 49.884 1.00 79.58 C ANISOU 1441 CG1 VAL F 181 8542 12793 8903 -2166 3719 -2698 C ATOM 1442 CG2 VAL A 181 96.962 49.057 48.309 1.00 90.23 C ANISOU 1442 CG2 VAL F 181 13190 11625 9469 -2396 839 -1705 C ATOM 1443 N PRO A 182 97.060 47.284 52.825 1.00 78.75 N ANISOU 1443 N PRO F 182 10355 10446 9119 -2988 1354 -2686 N ATOM 1444 CA PRO A 182 97.130 46.181 53.804 1.00 76.52 C ANISOU 1444 CA PRO F 182 10676 9754 8644 -3288 1639 -2374 C ATOM 1445 C PRO A 182 96.418 44.951 53.267 1.00 71.68 C ANISOU 1445 C PRO F 182 10376 9002 7857 -3382 1082 -2873 C ATOM 1446 O PRO A 182 95.493 45.065 52.454 1.00 66.00 O ANISOU 1446 O PRO F 182 9654 8907 6513 -1321 1615 -2978 O ATOM 1447 CB PRO A 182 96.421 46.778 55.021 1.00 75.44 C ANISOU 1447 CB PRO F 182 10308 9585 8770 -2867 1719 -2322 C ATOM 1448 CG PRO A 182 96.626 48.253 54.889 1.00 76.20 C ANISOU 1448 CG PRO F 182 10118 9995 8838 -3110 1344 -2279 C ATOM 1449 CD PRO A 182 96.492 48.505 53.407 1.00 76.74 C ANISOU 1449 CD PRO F 182 10206 10234 8719 -3262 1277 -2719 C ATOM 1450 N LYS A 183 96.833 43.746 53.642 1.00 66.25 N ANISOU 1450 N LYS F 183 10340 8136 6695 -4050 1488 -2470 N ATOM 1451 CA LYS A 183 96.196 42.601 52.995 1.00 67.52 C ANISOU 1451 CA LYS F 183 10571 8502 6581 -3366 1692 -1915 C ATOM 1452 C LYS A 183 94.860 42.287 53.656 1.00 61.25 C ANISOU 1452 C LYS F 183 9080 8020 6172 -2590 2056 -1793 C ATOM 1453 O LYS A 183 93.977 41.703 53.033 1.00 62.32 O ANISOU 1453 O LYS F 183 8010 8614 7056 -1762 3204 -3628 O ATOM 1454 CB LYS A 183 97.100 41.373 53.042 1.00 75.36 C ANISOU 1454 CB LYS F 183 12471 8389 7774 -2993 2715 -2713 C ATOM 1455 CG LYS A 183 98.049 41.318 51.844 1.00 84.45 C ANISOU 1455 CG LYS F 183 14227 9329 8531 -2830 1521 -3164 C ATOM 1456 CD LYS A 183 98.184 42.684 51.191 1.00 95.52 C ANISOU 1456 CD LYS F 183 15282 11438 9573 -3046 265 -1703 C ATOM 1457 CE LYS A 183 98.197 42.624 49.672 1.00101.86 C ANISOU 1457 CE LYS F 183 16632 12453 9618 -3588 396 -1398 C ATOM 1458 NZ LYS A 183 97.878 43.955 49.070 1.00102.56 N ANISOU 1458 NZ LYS F 183 16349 13890 8727 -3036 990 -1168 N ATOM 1459 N TYR A 184 94.746 42.687 54.917 1.00 51.83 N ANISOU 1459 N TYR F 184 7385 6107 6202 -1451 1991 -1376 N ATOM 1460 CA TYR A 184 93.600 42.307 55.718 1.00 55.27 C ANISOU 1460 CA TYR F 184 8249 6086 6665 -1439 1539 -1697 C ATOM 1461 C TYR A 184 92.947 43.514 56.387 1.00 50.14 C ANISOU 1461 C TYR F 184 7486 5664 5900 -936 511 -893 C ATOM 1462 O TYR A 184 93.545 44.581 56.538 1.00 48.87 O ANISOU 1462 O TYR F 184 7286 5065 6217 -912 -386 -628 O ATOM 1463 CB TYR A 184 93.989 41.333 56.825 1.00 53.58 C ANISOU 1463 CB TYR F 184 6222 6312 7825 -223 1467 -2105 C ATOM 1464 CG TYR A 184 94.732 40.096 56.402 1.00 65.46 C ANISOU 1464 CG TYR F 184 7173 6790 10910 -60 1811 -3275 C ATOM 1465 CD1 TYR A 184 94.145 38.839 56.485 1.00 67.60 C ANISOU 1465 CD1 TYR F 184 6973 7049 11662 58 3033 -3556 C ATOM 1466 CD2 TYR A 184 96.039 40.180 55.931 1.00 73.31 C ANISOU 1466 CD2 TYR F 184 8066 7074 12715 -474 2087 -4017 C ATOM 1467 CE1 TYR A 184 94.832 37.701 56.100 1.00 72.07 C ANISOU 1467 CE1 TYR F 184 7801 7118 12467 126 3804 -3699 C ATOM 1468 CE2 TYR A 184 96.737 39.056 55.538 1.00 77.62 C ANISOU 1468 CE2 TYR F 184 8961 6918 13614 -526 2886 -4002 C ATOM 1469 CZ TYR A 184 96.126 37.823 55.628 1.00 77.23 C ANISOU 1469 CZ TYR F 184 8779 7214 13351 -254 4043 -4133 C ATOM 1470 OH TYR A 184 96.834 36.708 55.241 1.00 81.19 O ANISOU 1470 OH TYR F 184 9978 6232 14639 -89 4148 -3058 O ATOM 1471 N ALA A 185 91.696 43.300 56.798 1.00 44.28 N ANISOU 1471 N ALA F 185 6583 5134 5106 -446 559 -397 N ATOM 1472 CA ALA A 185 90.955 44.340 57.499 1.00 41.54 C ANISOU 1472 CA ALA F 185 6004 5031 4749 -416 508 -104 C ATOM 1473 C ALA A 185 90.064 43.712 58.562 1.00 39.24 C ANISOU 1473 C ALA F 185 5740 4871 4300 -717 912 133 C ATOM 1474 O ALA A 185 89.724 42.543 58.406 1.00 40.15 O ANISOU 1474 O ALA F 185 5793 5070 4394 -630 878 -475 O ATOM 1475 CB ALA A 185 90.097 45.155 56.548 1.00 40.34 C ANISOU 1475 CB ALA F 185 5188 5388 4751 -438 771 151 C ATOM 1476 N LEU A 186 89.734 44.515 59.557 1.00 37.19 N ANISOU 1476 N LEU F 186 5393 4789 3950 -862 1160 535 N ATOM 1477 CA LEU A 186 88.715 44.124 60.533 1.00 35.06 C ANISOU 1477 CA LEU F 186 4702 4519 4100 -214 1223 282 C ATOM 1478 C LEU A 186 87.394 44.753 60.084 1.00 33.86 C ANISOU 1478 C LEU F 186 4382 4655 3830 -287 401 524 C ATOM 1479 O LEU A 186 87.435 45.924 59.685 1.00 34.53 O ANISOU 1479 O LEU F 186 4199 5283 3639 -774 52 1064 O ATOM 1480 CB LEU A 186 89.058 44.575 61.943 1.00 36.12 C ANISOU 1480 CB LEU F 186 4452 5494 3779 94 711 865 C ATOM 1481 CG LEU A 186 89.764 43.556 62.833 1.00 39.23 C ANISOU 1481 CG LEU F 186 6353 4183 4371 259 794 461 C ATOM 1482 CD1 LEU A 186 90.615 42.636 61.990 1.00 42.75 C ANISOU 1482 CD1 LEU F 186 9437 3566 3240 -1441 -472 -47 C ATOM 1483 CD2 LEU A 186 90.574 44.246 63.934 1.00 40.18 C ANISOU 1483 CD2 LEU F 186 6145 4354 4767 -1365 226 1002 C ATOM 1484 N THR A 187 86.283 44.024 60.133 1.00 30.92 N ANISOU 1484 N THR F 187 4133 4155 3461 94 150 309 N ATOM 1485 CA THR A 187 85.017 44.631 59.713 1.00 32.43 C ANISOU 1485 CA THR F 187 4606 4346 3371 -190 -100 590 C ATOM 1486 C THR A 187 83.858 44.183 60.568 1.00 30.01 C ANISOU 1486 C THR F 187 4081 4157 3164 -36 197 666 C ATOM 1487 O THR A 187 83.785 43.016 60.980 1.00 30.48 O ANISOU 1487 O THR F 187 3846 4335 3400 -14 462 717 O ATOM 1488 CB THR A 187 84.737 44.258 58.242 1.00 33.44 C ANISOU 1488 CB THR F 187 4926 4319 3459 -409 73 284 C ATOM 1489 OG1 THR A 187 83.517 44.849 57.767 1.00 37.26 O ANISOU 1489 OG1 THR F 187 6156 4383 3620 301 1094 527 O ATOM 1490 CG2 THR A 187 84.581 42.738 58.078 1.00 33.76 C ANISOU 1490 CG2 THR F 187 5268 4475 3086 12 -123 -62 C ATOM 1491 N VAL A 188 82.904 45.058 60.862 1.00 28.57 N ANISOU 1491 N VAL F 188 3740 4203 2911 -94 603 608 N ATOM 1492 CA VAL A 188 81.697 44.533 61.499 1.00 29.31 C ANISOU 1492 CA VAL F 188 3735 4253 3147 34 387 510 C ATOM 1493 C VAL A 188 80.999 43.547 60.573 1.00 30.26 C ANISOU 1493 C VAL F 188 3591 4490 3416 -170 473 -521 C ATOM 1494 O VAL A 188 81.195 43.548 59.343 1.00 29.19 O ANISOU 1494 O VAL F 188 3485 4361 3245 -525 366 186 O ATOM 1495 CB VAL A 188 80.710 45.664 61.841 1.00 29.17 C ANISOU 1495 CB VAL F 188 4038 4367 2679 -104 1059 342 C ATOM 1496 CG1 VAL A 188 81.352 46.632 62.832 1.00 31.08 C ANISOU 1496 CG1 VAL F 188 3683 4932 3194 -158 1065 776 C ATOM 1497 CG2 VAL A 188 80.268 46.389 60.573 1.00 28.12 C ANISOU 1497 CG2 VAL F 188 3455 4019 3209 -169 1025 629 C ATOM 1498 N GLY A 189 80.166 42.693 61.164 1.00 28.38 N ANISOU 1498 N GLY F 189 3717 3841 3224 -117 155 384 N ATOM 1499 CA GLY A 189 79.442 41.722 60.363 1.00 28.02 C ANISOU 1499 CA GLY F 189 3469 4112 3066 46 -121 769 C ATOM 1500 C GLY A 189 78.094 42.197 59.862 1.00 27.71 C ANISOU 1500 C GLY F 189 3463 3891 3172 18 212 417 C ATOM 1501 O GLY A 189 77.639 43.289 60.238 1.00 27.45 O ANISOU 1501 O GLY F 189 3160 3989 3282 -145 31 50 O ATOM 1502 N VAL A 190 77.453 41.383 59.026 1.00 26.82 N ANISOU 1502 N VAL F 190 3465 3926 2798 112 107 420 N ATOM 1503 CA VAL A 190 76.136 41.783 58.521 1.00 26.93 C ANISOU 1503 CA VAL F 190 3389 4048 2796 131 90 577 C ATOM 1504 C VAL A 190 75.121 41.790 59.650 1.00 28.09 C ANISOU 1504 C VAL F 190 3785 3971 2918 -213 119 637 C ATOM 1505 O VAL A 190 74.238 42.643 59.727 1.00 30.94 O ANISOU 1505 O VAL F 190 4716 3911 3129 -189 60 682 O ATOM 1506 CB VAL A 190 75.661 40.865 57.379 1.00 26.99 C ANISOU 1506 CB VAL F 190 3112 3553 3590 -134 386 136 C ATOM 1507 CG1 VAL A 190 74.277 41.280 56.874 1.00 25.38 C ANISOU 1507 CG1 VAL F 190 2744 3342 3558 112 575 -44 C ATOM 1508 CG2 VAL A 190 76.656 40.859 56.219 1.00 27.32 C ANISOU 1508 CG2 VAL F 190 4403 2881 3095 133 365 484 C ATOM 1509 N GLY A 191 75.231 40.832 60.564 1.00 28.27 N ANISOU 1509 N GLY F 191 3208 4106 3427 -304 -227 355 N ATOM 1510 CA GLY A 191 74.395 40.736 61.759 1.00 28.37 C ANISOU 1510 CA GLY F 191 3342 3994 3444 -476 -138 303 C ATOM 1511 C GLY A 191 74.604 41.960 62.635 1.00 28.92 C ANISOU 1511 C GLY F 191 3516 4195 3278 -472 -45 463 C ATOM 1512 O GLY A 191 73.669 42.529 63.204 1.00 30.95 O ANISOU 1512 O GLY F 191 3779 4123 3859 -480 519 391 O ATOM 1513 N THR A 192 75.864 42.384 62.746 1.00 29.18 N ANISOU 1513 N THR F 192 3439 4502 3147 -591 -134 402 N ATOM 1514 CA THR A 192 76.174 43.597 63.502 1.00 29.81 C ANISOU 1514 CA THR F 192 3857 4395 3073 -556 226 626 C ATOM 1515 C THR A 192 75.379 44.779 62.957 1.00 29.87 C ANISOU 1515 C THR F 192 4123 4135 3090 -435 71 136 C ATOM 1516 O THR A 192 74.769 45.573 63.671 1.00 30.88 O ANISOU 1516 O THR F 192 3359 4959 3417 -200 564 -87 O ATOM 1517 CB THR A 192 77.672 43.933 63.402 1.00 30.46 C ANISOU 1517 CB THR F 192 3949 4135 3491 -437 1053 19 C ATOM 1518 OG1 THR A 192 78.432 42.722 63.487 1.00 30.94 O ANISOU 1518 OG1 THR F 192 4233 4289 3235 -315 469 522 O ATOM 1519 CG2 THR A 192 78.107 44.829 64.557 1.00 28.56 C ANISOU 1519 CG2 THR F 192 3804 4881 2167 -406 239 587 C ATOM 1520 N LEU A 193 75.391 44.903 61.622 1.00 29.30 N ANISOU 1520 N LEU F 193 3907 4130 3097 -445 -282 243 N ATOM 1521 CA LEU A 193 74.650 46.002 60.997 1.00 28.61 C ANISOU 1521 CA LEU F 193 3432 4212 3224 9 467 216 C ATOM 1522 C LEU A 193 73.157 45.808 61.196 1.00 28.75 C ANISOU 1522 C LEU F 193 3528 4125 3272 31 128 531 C ATOM 1523 O LEU A 193 72.468 46.766 61.569 1.00 29.30 O ANISOU 1523 O LEU F 193 4126 4214 2793 -10 282 293 O ATOM 1524 CB LEU A 193 74.994 46.030 59.530 1.00 31.34 C ANISOU 1524 CB LEU F 193 4114 4565 3228 132 -171 407 C ATOM 1525 CG LEU A 193 74.759 47.162 58.554 1.00 35.04 C ANISOU 1525 CG LEU F 193 5419 4216 3677 812 52 819 C ATOM 1526 CD1 LEU A 193 73.647 46.801 57.559 1.00 39.91 C ANISOU 1526 CD1 LEU F 193 4504 3781 6878 259 -509 2372 C ATOM 1527 CD2 LEU A 193 74.452 48.497 59.210 1.00 40.58 C ANISOU 1527 CD2 LEU F 193 7843 3165 4409 1560 41 377 C ATOM 1528 N LEU A 194 72.657 44.592 60.937 1.00 28.35 N ANISOU 1528 N LEU F 194 3406 4654 2710 -78 -153 487 N ATOM 1529 CA LEU A 194 71.207 44.401 61.006 1.00 29.18 C ANISOU 1529 CA LEU F 194 3512 4386 3188 42 788 217 C ATOM 1530 C LEU A 194 70.657 44.561 62.408 1.00 27.64 C ANISOU 1530 C LEU F 194 3308 3882 3311 13 459 277 C ATOM 1531 O LEU A 194 69.470 44.845 62.619 1.00 32.48 O ANISOU 1531 O LEU F 194 4441 4208 3691 -751 230 449 O ATOM 1532 CB LEU A 194 70.830 43.011 60.460 1.00 30.39 C ANISOU 1532 CB LEU F 194 3416 4337 3793 268 610 -13 C ATOM 1533 CG LEU A 194 70.954 42.900 58.931 1.00 32.67 C ANISOU 1533 CG LEU F 194 4476 4134 3803 244 1480 184 C ATOM 1534 CD1 LEU A 194 70.687 41.480 58.444 1.00 33.19 C ANISOU 1534 CD1 LEU F 194 3856 4679 4076 -249 1257 200 C ATOM 1535 CD2 LEU A 194 70.024 43.903 58.260 1.00 37.87 C ANISOU 1535 CD2 LEU F 194 5689 4563 4135 478 209 271 C ATOM 1536 N ASP A 195 71.482 44.371 63.425 1.00 30.12 N ANISOU 1536 N ASP F 195 4211 4072 3163 -662 590 131 N ATOM 1537 CA ASP A 195 71.008 44.579 64.781 1.00 29.64 C ANISOU 1537 CA ASP F 195 4302 3758 3203 98 -79 213 C ATOM 1538 C ASP A 195 70.760 46.054 65.074 1.00 29.57 C ANISOU 1538 C ASP F 195 4117 3778 3340 -45 -78 100 C ATOM 1539 O ASP A 195 70.157 46.368 66.114 1.00 32.41 O ANISOU 1539 O ASP F 195 4205 4517 3592 -211 318 -376 O ATOM 1540 CB ASP A 195 72.053 44.088 65.793 1.00 32.84 C ANISOU 1540 CB ASP F 195 4666 4408 3404 87 -719 714 C ATOM 1541 CG ASP A 195 72.070 42.592 65.950 1.00 36.78 C ANISOU 1541 CG ASP F 195 5311 4142 4521 658 -307 529 C ATOM 1542 OD1 ASP A 195 71.132 41.966 65.417 1.00 41.73 O ANISOU 1542 OD1 ASP F 195 4379 5412 6064 -338 -1138 -93 O ATOM 1543 OD2 ASP A 195 73.005 42.086 66.597 1.00 46.56 O ANISOU 1543 OD2 ASP F 195 7158 4576 5955 488 -1854 1342 O ATOM 1544 N ALA A 196 71.210 46.978 64.231 1.00 29.67 N ANISOU 1544 N ALA F 196 3714 4500 3058 -289 263 755 N ATOM 1545 CA ALA A 196 70.922 48.391 64.543 1.00 27.17 C ANISOU 1545 CA ALA F 196 3566 4341 2418 -493 286 664 C ATOM 1546 C ALA A 196 69.430 48.680 64.446 1.00 28.00 C ANISOU 1546 C ALA F 196 3307 4465 2866 -680 569 151 C ATOM 1547 O ALA A 196 68.685 48.000 63.738 1.00 28.87 O ANISOU 1547 O ALA F 196 3380 4911 2678 -817 407 523 O ATOM 1548 CB ALA A 196 71.672 49.301 63.606 1.00 26.85 C ANISOU 1548 CB ALA F 196 3786 3619 2796 -451 4 594 C ATOM 1549 N GLU A 197 68.956 49.682 65.157 1.00 27.17 N ANISOU 1549 N GLU F 197 3167 4506 2651 43 -131 398 N ATOM 1550 CA GLU A 197 67.560 50.065 65.188 1.00 30.24 C ANISOU 1550 CA GLU F 197 3681 4448 3362 63 432 377 C ATOM 1551 C GLU A 197 67.123 50.623 63.842 1.00 30.02 C ANISOU 1551 C GLU F 197 3932 4152 3320 -495 120 257 C ATOM 1552 O GLU A 197 65.996 50.398 63.394 1.00 29.71 O ANISOU 1552 O GLU F 197 3706 5116 2466 -914 330 -139 O ATOM 1553 CB GLU A 197 67.365 51.146 66.253 1.00 40.52 C ANISOU 1553 CB GLU F 197 6248 5074 4074 -980 1874 -674 C ATOM 1554 CG GLU A 197 65.937 51.338 66.714 1.00 60.69 C ANISOU 1554 CG GLU F 197 10960 5871 6230 -2159 2147 -1972 C ATOM 1555 CD GLU A 197 65.830 52.201 67.958 1.00 66.66 C ANISOU 1555 CD GLU F 197 12361 6294 6674 -1720 2370 -2598 C ATOM 1556 OE1 GLU A 197 66.427 51.815 68.995 1.00 68.95 O ANISOU 1556 OE1 GLU F 197 12681 6424 7091 -1696 3962 -2134 O ATOM 1557 OE2 GLU A 197 65.150 53.253 67.880 1.00 72.08 O ANISOU 1557 OE2 GLU F 197 12903 7065 7420 -834 2072 -2632 O ATOM 1558 N GLU A 198 68.002 51.375 63.201 1.00 29.40 N ANISOU 1558 N GLU F 198 4080 4111 2979 -884 400 26 N ATOM 1559 CA GLU A 198 67.744 51.976 61.890 1.00 29.14 C ANISOU 1559 CA GLU F 198 3686 4407 2976 -596 412 4 C ATOM 1560 C GLU A 198 69.028 51.911 61.076 1.00 30.64 C ANISOU 1560 C GLU F 198 3990 4706 2945 -952 421 17 C ATOM 1561 O GLU A 198 70.120 52.103 61.639 1.00 26.56 O ANISOU 1561 O GLU F 198 3260 4014 2819 -140 508 -1 O ATOM 1562 CB GLU A 198 67.251 53.409 62.053 1.00 29.18 C ANISOU 1562 CB GLU F 198 3211 4607 3268 -706 933 303 C ATOM 1563 CG GLU A 198 66.962 54.148 60.745 1.00 32.96 C ANISOU 1563 CG GLU F 198 3877 4954 3691 -308 357 332 C ATOM 1564 CD GLU A 198 66.325 55.498 61.029 1.00 36.62 C ANISOU 1564 CD GLU F 198 5000 4709 4204 -89 1011 746 C ATOM 1565 OE1 GLU A 198 66.749 56.162 61.999 1.00 36.61 O ANISOU 1565 OE1 GLU F 198 5321 4283 4307 -280 1223 248 O ATOM 1566 OE2 GLU A 198 65.394 55.927 60.311 1.00 43.85 O ANISOU 1566 OE2 GLU F 198 7564 4664 4432 -101 1557 743 O ATOM 1567 N VAL A 199 68.910 51.617 59.787 1.00 28.01 N ANISOU 1567 N VAL F 199 3735 3995 2911 -590 355 193 N ATOM 1568 CA VAL A 199 70.059 51.505 58.899 1.00 28.79 C ANISOU 1568 CA VAL F 199 4099 3913 2926 -422 35 243 C ATOM 1569 C VAL A 199 69.869 52.500 57.763 1.00 26.71 C ANISOU 1569 C VAL F 199 3439 3620 3092 -347 251 296 C ATOM 1570 O VAL A 199 68.813 52.454 57.105 1.00 28.14 O ANISOU 1570 O VAL F 199 3635 4215 2844 -635 380 363 O ATOM 1571 CB VAL A 199 70.203 50.090 58.321 1.00 26.90 C ANISOU 1571 CB VAL F 199 3876 3732 2611 -293 -478 289 C ATOM 1572 CG1 VAL A 199 71.338 50.013 57.314 1.00 26.66 C ANISOU 1572 CG1 VAL F 199 4317 4077 1737 -515 -252 492 C ATOM 1573 CG2 VAL A 199 70.455 49.097 59.439 1.00 26.84 C ANISOU 1573 CG2 VAL F 199 3784 4224 2189 -724 -423 415 C ATOM 1574 N MET A 200 70.846 53.365 57.550 1.00 25.82 N ANISOU 1574 N MET F 200 3405 3339 3067 -293 498 -199 N ATOM 1575 CA MET A 200 70.749 54.352 56.470 1.00 26.13 C ANISOU 1575 CA MET F 200 3086 3834 3009 -311 524 -191 C ATOM 1576 C MET A 200 71.932 54.169 55.530 1.00 26.51 C ANISOU 1576 C MET F 200 3359 3860 2853 -621 688 -45 C ATOM 1577 O MET A 200 73.091 54.350 55.932 1.00 26.60 O ANISOU 1577 O MET F 200 3277 3787 3044 -483 920 -67 O ATOM 1578 CB MET A 200 70.694 55.776 57.043 1.00 25.55 C ANISOU 1578 CB MET F 200 3154 3628 2926 -420 893 307 C ATOM 1579 CG MET A 200 70.730 56.888 55.996 1.00 27.01 C ANISOU 1579 CG MET F 200 3214 3595 3455 -318 604 244 C ATOM 1580 SD MET A 200 70.444 58.523 56.699 1.00 28.73 S ANISOU 1580 SD MET F 200 3551 3918 3448 -104 689 149 S ATOM 1581 CE MET A 200 71.954 58.781 57.647 1.00 26.69 C ANISOU 1581 CE MET F 200 2874 4794 2472 -335 27 342 C ATOM 1582 N ILE A 201 71.654 53.791 54.275 1.00 23.46 N ANISOU 1582 N ILE F 201 2655 3502 2756 -211 435 140 N ATOM 1583 CA ILE A 201 72.705 53.513 53.314 1.00 24.79 C ANISOU 1583 CA ILE F 201 3173 3587 2659 -135 141 166 C ATOM 1584 C ILE A 201 72.788 54.658 52.312 1.00 26.52 C ANISOU 1584 C ILE F 201 3302 3637 3138 -120 -129 255 C ATOM 1585 O ILE A 201 71.767 55.038 51.732 1.00 27.81 O ANISOU 1585 O ILE F 201 4090 3835 2643 -342 -290 292 O ATOM 1586 CB ILE A 201 72.446 52.197 52.566 1.00 27.24 C ANISOU 1586 CB ILE F 201 3374 3618 3356 163 152 -363 C ATOM 1587 CG1 ILE A 201 72.222 51.032 53.540 1.00 27.24 C ANISOU 1587 CG1 ILE F 201 3081 3946 3322 -139 251 -186 C ATOM 1588 CG2 ILE A 201 73.568 51.915 51.575 1.00 25.31 C ANISOU 1588 CG2 ILE F 201 3326 3157 3136 -130 215 74 C ATOM 1589 CD1 ILE A 201 73.497 50.710 54.313 1.00 28.28 C ANISOU 1589 CD1 ILE F 201 3584 4313 2850 -494 -85 -87 C ATOM 1590 N LEU A 202 73.989 55.175 52.154 1.00 26.31 N ANISOU 1590 N LEU F 202 3092 3731 3174 -22 64 -128 N ATOM 1591 CA LEU A 202 74.288 56.223 51.204 1.00 26.30 C ANISOU 1591 CA LEU F 202 3483 3728 2784 -398 -43 153 C ATOM 1592 C LEU A 202 74.622 55.572 49.859 1.00 27.46 C ANISOU 1592 C LEU F 202 3413 4048 2970 -16 191 179 C ATOM 1593 O LEU A 202 75.517 54.721 49.800 1.00 28.40 O ANISOU 1593 O LEU F 202 3715 3947 3129 -232 511 123 O ATOM 1594 CB LEU A 202 75.482 57.051 51.644 1.00 27.98 C ANISOU 1594 CB LEU F 202 3026 4205 3402 -8 200 67 C ATOM 1595 CG LEU A 202 75.343 58.253 52.574 1.00 32.57 C ANISOU 1595 CG LEU F 202 4884 4340 3151 -665 1223 -340 C ATOM 1596 CD1 LEU A 202 74.055 58.246 53.361 1.00 29.03 C ANISOU 1596 CD1 LEU F 202 4459 5402 1168 -774 316 322 C ATOM 1597 CD2 LEU A 202 76.551 58.345 53.489 1.00 28.96 C ANISOU 1597 CD2 LEU F 202 4928 4324 1753 -81 81 254 C ATOM 1598 N VAL A 203 73.924 55.997 48.818 1.00 27.08 N ANISOU 1598 N VAL F 203 3379 4070 2841 -319 158 136 N ATOM 1599 CA VAL A 203 74.167 55.399 47.507 1.00 28.32 C ANISOU 1599 CA VAL F 203 3361 4483 2917 -368 193 -54 C ATOM 1600 C VAL A 203 74.504 56.463 46.455 1.00 28.11 C ANISOU 1600 C VAL F 203 3351 4416 2913 -207 204 -341 C ATOM 1601 O VAL A 203 73.602 57.218 46.063 1.00 31.28 O ANISOU 1601 O VAL F 203 4296 4820 2771 -986 -232 601 O ATOM 1602 CB VAL A 203 72.940 54.579 47.065 1.00 31.03 C ANISOU 1602 CB VAL F 203 3660 5547 2583 -1005 156 -265 C ATOM 1603 CG1 VAL A 203 73.287 53.797 45.776 1.00 27.47 C ANISOU 1603 CG1 VAL F 203 3351 4595 2491 -504 -35 175 C ATOM 1604 CG2 VAL A 203 72.419 53.639 48.148 1.00 29.06 C ANISOU 1604 CG2 VAL F 203 3679 5007 2355 -1074 283 118 C ATOM 1605 N LEU A 204 75.769 56.521 46.022 1.00 30.58 N ANISOU 1605 N LEU F 204 3955 4885 2778 -1079 110 214 N ATOM 1606 CA LEU A 204 76.284 57.528 45.117 1.00 30.91 C ANISOU 1606 CA LEU F 204 3857 4859 3028 -978 77 43 C ATOM 1607 C LEU A 204 76.938 56.930 43.882 1.00 29.57 C ANISOU 1607 C LEU F 204 3398 4788 3048 -201 -283 88 C ATOM 1608 O LEU A 204 77.801 56.061 43.988 1.00 31.99 O ANISOU 1608 O LEU F 204 4527 4559 3069 -551 -246 384 O ATOM 1609 CB LEU A 204 77.338 58.395 45.825 1.00 31.23 C ANISOU 1609 CB LEU F 204 3744 4804 3316 -564 188 378 C ATOM 1610 CG LEU A 204 76.864 59.206 47.031 1.00 34.71 C ANISOU 1610 CG LEU F 204 4546 4360 4282 -557 1005 214 C ATOM 1611 CD1 LEU A 204 78.027 59.992 47.618 1.00 33.44 C ANISOU 1611 CD1 LEU F 204 3953 5118 3633 -175 495 933 C ATOM 1612 CD2 LEU A 204 75.701 60.129 46.658 1.00 31.49 C ANISOU 1612 CD2 LEU F 204 4245 4809 2909 -221 105 641 C ATOM 1613 N GLY A 205 76.568 57.396 42.681 1.00 29.39 N ANISOU 1613 N GLY F 205 3684 4477 3005 108 341 145 N ATOM 1614 CA GLY A 205 77.319 56.988 41.500 1.00 29.33 C ANISOU 1614 CA GLY F 205 3309 4893 2943 -186 184 46 C ATOM 1615 C GLY A 205 76.594 55.900 40.732 1.00 29.69 C ANISOU 1615 C GLY F 205 3654 4708 2919 -229 429 95 C ATOM 1616 O GLY A 205 75.944 55.039 41.304 1.00 28.46 O ANISOU 1616 O GLY F 205 3423 4190 3199 -544 655 -51 O ATOM 1617 N SER A 206 76.716 55.980 39.405 1.00 31.83 N ANISOU 1617 N SER F 206 4673 4502 2919 -549 548 -276 N ATOM 1618 CA SER A 206 76.092 54.963 38.561 1.00 29.80 C ANISOU 1618 CA SER F 206 4041 4962 2320 -526 -102 -270 C ATOM 1619 C SER A 206 76.732 53.604 38.791 1.00 31.69 C ANISOU 1619 C SER F 206 4450 4768 2821 -451 78 -368 C ATOM 1620 O SER A 206 76.117 52.587 38.468 1.00 28.29 O ANISOU 1620 O SER F 206 4255 4279 2215 -476 -394 268 O ATOM 1621 CB SER A 206 76.168 55.363 37.078 1.00 33.90 C ANISOU 1621 CB SER F 206 4494 6018 2369 -833 -305 -238 C ATOM 1622 OG SER A 206 77.540 55.352 36.692 1.00 38.87 O ANISOU 1622 OG SER F 206 5664 6409 2695 -1460 -1342 262 O ATOM 1623 N GLN A 207 77.939 53.532 39.353 1.00 30.40 N ANISOU 1623 N GLN F 207 3695 4607 3248 -457 63 -618 N ATOM 1624 CA GLN A 207 78.473 52.205 39.647 1.00 32.40 C ANISOU 1624 CA GLN F 207 4520 4248 3542 -300 14 -920 C ATOM 1625 C GLN A 207 77.667 51.473 40.722 1.00 29.27 C ANISOU 1625 C GLN F 207 4194 3487 3441 -283 30 -247 C ATOM 1626 O GLN A 207 77.833 50.247 40.861 1.00 29.03 O ANISOU 1626 O GLN F 207 4537 3459 3036 -42 551 326 O ATOM 1627 CB GLN A 207 79.952 52.299 40.043 1.00 36.95 C ANISOU 1627 CB GLN F 207 4455 5029 4553 -804 -1270 278 C ATOM 1628 CG GLN A 207 80.199 52.736 41.474 1.00 47.12 C ANISOU 1628 CG GLN F 207 5195 7212 5495 -2280 256 49 C ATOM 1629 CD GLN A 207 80.448 54.228 41.601 1.00 58.32 C ANISOU 1629 CD GLN F 207 5271 8711 8178 -2199 1161 -85 C ATOM 1630 OE1 GLN A 207 79.871 55.041 40.853 1.00 66.79 O ANISOU 1630 OE1 GLN F 207 6080 5957 13342 -1004 1966 -111 O ATOM 1631 NE2 GLN A 207 81.317 54.580 42.557 1.00 76.22 N ANISOU 1631 NE2 GLN F 207 4748 13694 10520 -4923 636 1575 N ATOM 1632 N LYS A 208 76.808 52.142 41.485 1.00 25.90 N ANISOU 1632 N LYS F 208 4036 3076 2728 -346 -118 256 N ATOM 1633 CA LYS A 208 75.975 51.517 42.502 1.00 26.11 C ANISOU 1633 CA LYS F 208 3765 3732 2423 -458 139 294 C ATOM 1634 C LYS A 208 74.569 51.206 42.015 1.00 26.21 C ANISOU 1634 C LYS F 208 3512 3888 2558 -387 -252 646 C ATOM 1635 O LYS A 208 73.680 50.763 42.741 1.00 26.03 O ANISOU 1635 O LYS F 208 3872 3305 2713 -291 -176 195 O ATOM 1636 CB LYS A 208 75.839 52.478 43.691 1.00 26.25 C ANISOU 1636 CB LYS F 208 3674 3411 2887 -397 148 -17 C ATOM 1637 CG LYS A 208 77.199 52.994 44.164 1.00 30.23 C ANISOU 1637 CG LYS F 208 4395 3646 3444 -621 1015 -299 C ATOM 1638 CD LYS A 208 78.083 51.858 44.656 1.00 31.45 C ANISOU 1638 CD LYS F 208 4882 3749 3319 -1187 -14 134 C ATOM 1639 CE LYS A 208 79.264 52.459 45.414 1.00 33.73 C ANISOU 1639 CE LYS F 208 4506 4101 4209 -1327 -214 329 C ATOM 1640 NZ LYS A 208 80.232 51.418 45.823 1.00 36.37 N ANISOU 1640 NZ LYS F 208 5786 3210 4825 -1811 65 -212 N ATOM 1641 N ALA A 209 74.314 51.468 40.749 1.00 27.52 N ANISOU 1641 N ALA F 209 3856 3895 2704 -341 -333 905 N ATOM 1642 CA ALA A 209 72.950 51.368 40.238 1.00 25.88 C ANISOU 1642 CA ALA F 209 3565 3497 2773 -123 -826 957 C ATOM 1643 C ALA A 209 72.406 49.952 40.329 1.00 25.14 C ANISOU 1643 C ALA F 209 3546 3492 2513 -82 -760 754 C ATOM 1644 O ALA A 209 71.226 49.767 40.672 1.00 26.85 O ANISOU 1644 O ALA F 209 3455 3812 2936 -140 -241 8 O ATOM 1645 CB ALA A 209 72.890 51.912 38.803 1.00 23.02 C ANISOU 1645 CB ALA F 209 2921 3511 2316 25 -299 546 C ATOM 1646 N LEU A 210 73.219 48.949 40.034 1.00 25.44 N ANISOU 1646 N LEU F 210 3524 3670 2471 -183 -458 358 N ATOM 1647 CA LEU A 210 72.689 47.569 40.134 1.00 25.96 C ANISOU 1647 CA LEU F 210 3513 3934 2415 -72 -197 183 C ATOM 1648 C LEU A 210 72.417 47.199 41.584 1.00 25.20 C ANISOU 1648 C LEU F 210 3328 3734 2514 20 -310 632 C ATOM 1649 O LEU A 210 71.462 46.482 41.899 1.00 31.16 O ANISOU 1649 O LEU F 210 4203 4560 3078 -900 -917 898 O ATOM 1650 CB LEU A 210 73.641 46.541 39.518 1.00 27.50 C ANISOU 1650 CB LEU F 210 3969 3660 2821 -64 138 434 C ATOM 1651 CG LEU A 210 73.642 46.480 37.992 1.00 30.14 C ANISOU 1651 CG LEU F 210 4555 3985 2914 -429 747 -23 C ATOM 1652 CD1 LEU A 210 74.824 45.667 37.481 1.00 40.51 C ANISOU 1652 CD1 LEU F 210 6486 4436 4470 -530 822 -963 C ATOM 1653 CD2 LEU A 210 72.341 45.898 37.467 1.00 33.37 C ANISOU 1653 CD2 LEU F 210 4280 4458 3940 -58 1358 352 C ATOM 1654 N ALA A 211 73.281 47.698 42.480 1.00 27.48 N ANISOU 1654 N ALA F 211 4486 3291 2663 -308 115 631 N ATOM 1655 CA ALA A 211 73.046 47.441 43.889 1.00 28.29 C ANISOU 1655 CA ALA F 211 3993 4123 2631 -618 294 169 C ATOM 1656 C ALA A 211 71.764 48.116 44.359 1.00 28.10 C ANISOU 1656 C ALA F 211 4031 3919 2728 -565 200 406 C ATOM 1657 O ALA A 211 71.025 47.519 45.154 1.00 28.25 O ANISOU 1657 O ALA F 211 3966 3542 3227 -506 8 452 O ATOM 1658 CB ALA A 211 74.252 47.916 44.678 1.00 25.95 C ANISOU 1658 CB ALA F 211 3715 3845 2298 -492 -138 300 C ATOM 1659 N LEU A 212 71.487 49.337 43.900 1.00 29.74 N ANISOU 1659 N LEU F 212 4595 4129 2575 -549 -229 649 N ATOM 1660 CA LEU A 212 70.296 50.072 44.304 1.00 25.23 C ANISOU 1660 CA LEU F 212 3555 4092 1940 -464 -338 834 C ATOM 1661 C LEU A 212 69.056 49.308 43.841 1.00 26.45 C ANISOU 1661 C LEU F 212 3253 4091 2706 -119 118 416 C ATOM 1662 O LEU A 212 68.063 49.210 44.557 1.00 26.73 O ANISOU 1662 O LEU F 212 3539 3928 2690 -461 108 723 O ATOM 1663 CB LEU A 212 70.206 51.451 43.684 1.00 26.14 C ANISOU 1663 CB LEU F 212 3254 5074 1604 -148 130 1069 C ATOM 1664 CG LEU A 212 69.746 52.638 44.499 1.00 31.40 C ANISOU 1664 CG LEU F 212 4836 4104 2990 228 -696 230 C ATOM 1665 CD1 LEU A 212 68.966 53.622 43.633 1.00 31.16 C ANISOU 1665 CD1 LEU F 212 5718 3975 2147 -356 505 747 C ATOM 1666 CD2 LEU A 212 68.923 52.278 45.732 1.00 29.99 C ANISOU 1666 CD2 LEU F 212 3747 2975 4675 428 -1429 -231 C ATOM 1667 N GLN A 213 69.190 48.821 42.613 1.00 28.60 N ANISOU 1667 N GLN F 213 3647 4297 2922 23 421 291 N ATOM 1668 CA GLN A 213 68.074 48.044 42.051 1.00 28.27 C ANISOU 1668 CA GLN F 213 3770 4308 2664 43 296 648 C ATOM 1669 C GLN A 213 67.831 46.771 42.867 1.00 27.90 C ANISOU 1669 C GLN F 213 3697 3508 3397 162 48 28 C ATOM 1670 O GLN A 213 66.670 46.422 43.124 1.00 26.94 O ANISOU 1670 O GLN F 213 3530 3710 2995 -146 559 542 O ATOM 1671 CB GLN A 213 68.323 47.724 40.565 1.00 29.86 C ANISOU 1671 CB GLN F 213 4273 4258 2815 304 573 427 C ATOM 1672 CG GLN A 213 67.030 47.351 39.837 1.00 39.30 C ANISOU 1672 CG GLN F 213 6207 5403 3322 -880 1789 -170 C ATOM 1673 CD GLN A 213 66.760 45.860 39.900 1.00 45.82 C ANISOU 1673 CD GLN F 213 5764 6136 5508 -1206 2816 22 C ATOM 1674 OE1 GLN A 213 67.683 45.118 40.247 1.00 53.98 O ANISOU 1674 OE1 GLN F 213 5710 6244 8557 -370 2661 187 O ATOM 1675 NE2 GLN A 213 65.554 45.393 39.623 1.00 57.17 N ANISOU 1675 NE2 GLN F 213 6683 8012 7026 -2886 1918 53 N ATOM 1676 N ALA A 214 68.920 46.097 43.237 1.00 28.99 N ANISOU 1676 N ALA F 214 4033 3798 3185 -353 -195 686 N ATOM 1677 CA ALA A 214 68.772 44.867 44.009 1.00 28.54 C ANISOU 1677 CA ALA F 214 3677 3693 3475 -175 -111 350 C ATOM 1678 C ALA A 214 68.187 45.189 45.376 1.00 28.15 C ANISOU 1678 C ALA F 214 3485 3684 3525 -42 -286 270 C ATOM 1679 O ALA A 214 67.398 44.374 45.888 1.00 32.38 O ANISOU 1679 O ALA F 214 3423 5591 3289 -771 170 210 O ATOM 1680 CB ALA A 214 70.084 44.128 44.208 1.00 28.84 C ANISOU 1680 CB ALA F 214 3188 3675 4096 -530 -1297 130 C ATOM 1681 N ALA A 215 68.548 46.331 45.956 1.00 26.92 N ANISOU 1681 N ALA F 215 3358 3711 3160 20 -495 438 N ATOM 1682 CA ALA A 215 68.019 46.707 47.270 1.00 30.50 C ANISOU 1682 CA ALA F 215 4225 3758 3604 -113 -91 36 C ATOM 1683 C ALA A 215 66.526 47.023 47.210 1.00 27.87 C ANISOU 1683 C ALA F 215 3067 3676 3846 215 -514 194 C ATOM 1684 O ALA A 215 65.761 46.605 48.079 1.00 28.10 O ANISOU 1684 O ALA F 215 3415 4015 3248 -44 -217 177 O ATOM 1685 CB ALA A 215 68.777 47.894 47.867 1.00 26.25 C ANISOU 1685 CB ALA F 215 4114 3604 2255 -51 -540 938 C ATOM 1686 N VAL A 216 66.097 47.769 46.193 1.00 26.01 N ANISOU 1686 N VAL F 216 2832 4068 2981 93 223 219 N ATOM 1687 CA VAL A 216 64.766 48.347 46.172 1.00 28.99 C ANISOU 1687 CA VAL F 216 3507 4112 3397 -225 178 765 C ATOM 1688 C VAL A 216 63.786 47.510 45.366 1.00 28.46 C ANISOU 1688 C VAL F 216 3112 4337 3362 -369 41 110 C ATOM 1689 O VAL A 216 62.651 47.279 45.833 1.00 31.65 O ANISOU 1689 O VAL F 216 3387 4551 4086 -556 -656 424 O ATOM 1690 CB VAL A 216 64.836 49.772 45.579 1.00 29.65 C ANISOU 1690 CB VAL F 216 3251 3832 4183 68 523 354 C ATOM 1691 CG1 VAL A 216 63.460 50.385 45.336 1.00 29.03 C ANISOU 1691 CG1 VAL F 216 3443 3719 3869 105 375 13 C ATOM 1692 CG2 VAL A 216 65.651 50.687 46.495 1.00 30.11 C ANISOU 1692 CG2 VAL F 216 3985 3878 3576 615 904 487 C ATOM 1693 N GLU A 217 64.132 47.039 44.172 1.00 29.52 N ANISOU 1693 N GLU F 217 3976 4112 3127 260 137 542 N ATOM 1694 CA GLU A 217 63.135 46.373 43.327 1.00 27.64 C ANISOU 1694 CA GLU F 217 3965 3921 2615 -127 -259 328 C ATOM 1695 C GLU A 217 63.358 44.872 43.287 1.00 27.57 C ANISOU 1695 C GLU F 217 3324 3921 3230 -513 -371 158 C ATOM 1696 O GLU A 217 62.440 44.126 42.972 1.00 30.82 O ANISOU 1696 O GLU F 217 3867 4616 3227 -699 388 516 O ATOM 1697 CB GLU A 217 63.169 46.812 41.857 1.00 28.51 C ANISOU 1697 CB GLU F 217 4447 3723 2661 -394 -510 230 C ATOM 1698 CG GLU A 217 62.505 48.120 41.529 1.00 31.72 C ANISOU 1698 CG GLU F 217 5028 3915 3109 -231 -796 545 C ATOM 1699 CD GLU A 217 62.838 48.603 40.131 1.00 30.22 C ANISOU 1699 CD GLU F 217 4414 4065 3004 153 -513 122 C ATOM 1700 OE1 GLU A 217 63.460 47.848 39.350 1.00 35.52 O ANISOU 1700 OE1 GLU F 217 5903 4209 3386 209 -68 -39 O ATOM 1701 OE2 GLU A 217 62.504 49.741 39.747 1.00 30.37 O ANISOU 1701 OE2 GLU F 217 4816 3827 2895 -71 -240 972 O ATOM 1702 N GLY A 218 64.569 44.414 43.572 1.00 27.03 N ANISOU 1702 N GLY F 218 3319 3806 3146 -253 182 24 N ATOM 1703 CA GLY A 218 64.786 42.976 43.452 1.00 27.96 C ANISOU 1703 CA GLY F 218 3346 4040 3238 -207 332 -278 C ATOM 1704 C GLY A 218 64.212 42.192 44.611 1.00 26.15 C ANISOU 1704 C GLY F 218 3303 3304 3330 261 346 -666 C ATOM 1705 O GLY A 218 63.638 42.733 45.540 1.00 26.74 O ANISOU 1705 O GLY F 218 3373 3412 3376 240 541 -709 O ATOM 1706 N CYS A 219 64.361 40.867 44.576 1.00 24.88 N ANISOU 1706 N CYS F 219 3568 2925 2958 352 743 37 N ATOM 1707 CA CYS A 219 63.887 40.071 45.679 1.00 30.38 C ANISOU 1707 CA CYS F 219 4496 3078 3969 623 -280 303 C ATOM 1708 C CYS A 219 65.015 39.820 46.688 1.00 30.85 C ANISOU 1708 C CYS F 219 4438 3599 3682 74 -540 392 C ATOM 1709 O CYS A 219 66.192 40.058 46.413 1.00 25.68 O ANISOU 1709 O CYS F 219 3123 3511 3124 661 -12 78 O ATOM 1710 CB CYS A 219 63.341 38.722 45.203 1.00 37.11 C ANISOU 1710 CB CYS F 219 3936 4930 5235 -330 -381 641 C ATOM 1711 SG CYS A 219 61.804 38.834 44.249 1.00 58.04 S ANISOU 1711 SG CYS F 219 7872 5748 8434 -1355 2190 1007 S ATOM 1712 N VAL A 220 64.625 39.322 47.849 1.00 27.88 N ANISOU 1712 N VAL F 220 3496 3703 3394 104 59 -12 N ATOM 1713 CA VAL A 220 65.602 39.016 48.892 1.00 26.75 C ANISOU 1713 CA VAL F 220 3323 3784 3057 282 28 -76 C ATOM 1714 C VAL A 220 66.522 37.866 48.487 1.00 26.58 C ANISOU 1714 C VAL F 220 3305 3766 3028 181 527 46 C ATOM 1715 O VAL A 220 66.106 36.757 48.135 1.00 26.98 O ANISOU 1715 O VAL F 220 3141 3674 3436 -52 435 -131 O ATOM 1716 CB VAL A 220 64.883 38.701 50.215 1.00 33.69 C ANISOU 1716 CB VAL F 220 5260 4232 3308 -763 -327 -237 C ATOM 1717 CG1 VAL A 220 65.916 38.263 51.263 1.00 29.53 C ANISOU 1717 CG1 VAL F 220 4246 4100 2875 -432 -540 -467 C ATOM 1718 CG2 VAL A 220 64.087 39.912 50.673 1.00 29.12 C ANISOU 1718 CG2 VAL F 220 4256 4208 2601 -760 -991 -56 C ATOM 1719 N ASN A 221 67.837 38.122 48.527 1.00 23.80 N ANISOU 1719 N ASN F 221 2734 3576 2733 519 250 357 N ATOM 1720 CA ASN A 221 68.751 37.022 48.252 1.00 26.01 C ANISOU 1720 CA ASN F 221 2969 3599 3315 539 773 400 C ATOM 1721 C ASN A 221 70.121 37.332 48.842 1.00 28.17 C ANISOU 1721 C ASN F 221 2942 3749 4012 85 133 543 C ATOM 1722 O ASN A 221 70.545 38.486 48.857 1.00 30.71 O ANISOU 1722 O ASN F 221 3047 3707 4914 270 773 475 O ATOM 1723 CB ASN A 221 68.851 36.739 46.754 1.00 33.22 C ANISOU 1723 CB ASN F 221 5329 3818 3475 153 881 -227 C ATOM 1724 CG ASN A 221 69.803 37.747 46.152 1.00 39.44 C ANISOU 1724 CG ASN F 221 6876 4170 3941 -916 -536 452 C ATOM 1725 OD1 ASN A 221 70.987 37.444 46.031 1.00 50.59 O ANISOU 1725 OD1 ASN F 221 9635 4632 4955 -1970 -966 36 O ATOM 1726 ND2 ASN A 221 69.258 38.906 45.818 1.00 39.14 N ANISOU 1726 ND2 ASN F 221 4934 5456 4482 -196 908 529 N ATOM 1727 N HIS A 222 70.805 36.306 49.345 1.00 24.93 N ANISOU 1727 N HIS F 222 3292 3123 3055 99 244 -201 N ATOM 1728 CA HIS A 222 72.051 36.570 50.056 1.00 28.03 C ANISOU 1728 CA HIS F 222 3672 3846 3130 -342 -116 313 C ATOM 1729 C HIS A 222 73.195 36.954 49.137 1.00 25.51 C ANISOU 1729 C HIS F 222 3150 3788 2756 -191 167 370 C ATOM 1730 O HIS A 222 74.255 37.365 49.594 1.00 26.47 O ANISOU 1730 O HIS F 222 3347 4108 2601 -357 606 -136 O ATOM 1731 CB HIS A 222 72.412 35.327 50.888 1.00 27.71 C ANISOU 1731 CB HIS F 222 3610 4005 2913 -335 -149 269 C ATOM 1732 CG HIS A 222 72.832 34.145 50.068 1.00 30.41 C ANISOU 1732 CG HIS F 222 4463 3639 3452 -122 171 392 C ATOM 1733 ND1 HIS A 222 73.607 33.163 50.623 1.00 30.51 N ANISOU 1733 ND1 HIS F 222 4026 3751 3813 -351 -41 647 N ATOM 1734 CD2 HIS A 222 72.600 33.747 48.775 1.00 28.37 C ANISOU 1734 CD2 HIS F 222 3804 3680 3294 164 -146 175 C ATOM 1735 CE1 HIS A 222 73.855 32.223 49.725 1.00 29.61 C ANISOU 1735 CE1 HIS F 222 3212 3860 4178 -174 -48 794 C ATOM 1736 NE2 HIS A 222 73.260 32.548 48.588 1.00 27.77 N ANISOU 1736 NE2 HIS F 222 3066 3834 3652 142 -437 335 N ATOM 1737 N MET A 223 73.045 36.804 47.817 1.00 25.07 N ANISOU 1737 N MET F 223 3191 3482 2852 -2 648 90 N ATOM 1738 CA MET A 223 74.190 37.140 46.966 1.00 27.84 C ANISOU 1738 CA MET F 223 3817 3836 2926 20 235 -63 C ATOM 1739 C MET A 223 74.334 38.665 46.848 1.00 28.01 C ANISOU 1739 C MET F 223 3332 3791 3519 -420 477 -313 C ATOM 1740 O MET A 223 75.446 39.173 46.653 1.00 32.61 O ANISOU 1740 O MET F 223 4043 4364 3982 -827 -476 -588 O ATOM 1741 CB MET A 223 74.093 36.505 45.581 1.00 31.81 C ANISOU 1741 CB MET F 223 3759 4994 3335 -137 569 -704 C ATOM 1742 CG MET A 223 74.346 35.023 45.431 1.00 35.49 C ANISOU 1742 CG MET F 223 4971 4284 4229 278 1229 -251 C ATOM 1743 SD MET A 223 76.027 34.442 45.754 1.00 45.43 S ANISOU 1743 SD MET F 223 7173 4720 5367 -457 4 786 S ATOM 1744 CE MET A 223 76.998 35.735 45.016 1.00 45.69 C ANISOU 1744 CE MET F 223 6965 6223 4174 -1548 947 -545 C ATOM 1745 N TRP A 224 73.235 39.403 46.954 1.00 26.46 N ANISOU 1745 N TRP F 224 3248 3792 3012 -210 580 -393 N ATOM 1746 CA TRP A 224 73.212 40.853 47.032 1.00 25.51 C ANISOU 1746 CA TRP F 224 2915 3982 2794 -399 599 -47 C ATOM 1747 C TRP A 224 72.817 41.208 48.460 1.00 23.92 C ANISOU 1747 C TRP F 224 2798 3541 2750 126 299 111 C ATOM 1748 O TRP A 224 71.622 41.366 48.741 1.00 28.18 O ANISOU 1748 O TRP F 224 4073 4026 2607 -664 -261 251 O ATOM 1749 CB TRP A 224 72.222 41.452 46.033 1.00 26.22 C ANISOU 1749 CB TRP F 224 3118 4195 2652 -420 353 18 C ATOM 1750 CG TRP A 224 72.681 41.231 44.606 1.00 27.79 C ANISOU 1750 CG TRP F 224 3388 4375 2797 -169 32 -98 C ATOM 1751 CD1 TRP A 224 72.528 40.095 43.871 1.00 28.37 C ANISOU 1751 CD1 TRP F 224 3671 4310 2800 -9 -75 -617 C ATOM 1752 CD2 TRP A 224 73.357 42.152 43.746 1.00 28.12 C ANISOU 1752 CD2 TRP F 224 3668 4114 2901 -141 -221 210 C ATOM 1753 NE1 TRP A 224 73.056 40.238 42.624 1.00 29.97 N ANISOU 1753 NE1 TRP F 224 3806 4833 2747 -261 -224 -395 N ATOM 1754 CE2 TRP A 224 73.580 41.504 42.517 1.00 30.42 C ANISOU 1754 CE2 TRP F 224 3885 4698 2975 -218 -329 -98 C ATOM 1755 CE3 TRP A 224 73.804 43.463 43.880 1.00 27.83 C ANISOU 1755 CE3 TRP F 224 3701 3809 3064 31 -475 414 C ATOM 1756 CZ2 TRP A 224 74.225 42.123 41.447 1.00 30.60 C ANISOU 1756 CZ2 TRP F 224 3923 4616 3087 -197 -442 -43 C ATOM 1757 CZ3 TRP A 224 74.446 44.088 42.825 1.00 28.39 C ANISOU 1757 CZ3 TRP F 224 3913 3697 3177 -26 -548 146 C ATOM 1758 CH2 TRP A 224 74.653 43.413 41.611 1.00 29.45 C ANISOU 1758 CH2 TRP F 224 3780 4361 3050 -619 -160 298 C ATOM 1759 N THR A 225 73.795 41.289 49.365 1.00 24.46 N ANISOU 1759 N THR F 225 2994 3587 2711 71 623 -144 N ATOM 1760 CA THR A 225 73.536 41.441 50.791 1.00 23.89 C ANISOU 1760 CA THR F 225 2936 3457 2683 -37 365 -176 C ATOM 1761 C THR A 225 72.569 42.583 51.068 1.00 23.19 C ANISOU 1761 C THR F 225 3060 3332 2421 -189 -249 -227 C ATOM 1762 O THR A 225 71.677 42.456 51.905 1.00 24.92 O ANISOU 1762 O THR F 225 3742 3616 2112 -581 -167 -160 O ATOM 1763 CB THR A 225 74.858 41.693 51.546 1.00 28.76 C ANISOU 1763 CB THR F 225 5097 3622 2209 -1100 151 -226 C ATOM 1764 OG1 THR A 225 75.764 40.639 51.221 1.00 26.14 O ANISOU 1764 OG1 THR F 225 3254 3870 2808 -573 134 514 O ATOM 1765 CG2 THR A 225 74.639 41.643 53.053 1.00 25.10 C ANISOU 1765 CG2 THR F 225 3289 3990 2260 -19 -1080 637 C ATOM 1766 N ILE A 226 72.740 43.690 50.368 1.00 23.82 N ANISOU 1766 N ILE F 226 3298 3556 2197 -70 -148 250 N ATOM 1767 CA ILE A 226 71.899 44.870 50.542 1.00 26.22 C ANISOU 1767 CA ILE F 226 3673 3367 2922 -125 -323 466 C ATOM 1768 C ILE A 226 70.419 44.549 50.362 1.00 27.08 C ANISOU 1768 C ILE F 226 3529 3616 3145 -236 -8 -107 C ATOM 1769 O ILE A 226 69.564 45.233 50.964 1.00 25.56 O ANISOU 1769 O ILE F 226 3398 3644 2671 -280 170 31 O ATOM 1770 CB ILE A 226 72.313 46.004 49.574 1.00 24.10 C ANISOU 1770 CB ILE F 226 3102 3689 2368 264 168 -148 C ATOM 1771 CG1 ILE A 226 71.761 47.376 49.993 1.00 26.09 C ANISOU 1771 CG1 ILE F 226 2996 3888 3031 95 447 -573 C ATOM 1772 CG2 ILE A 226 71.930 45.709 48.110 1.00 22.86 C ANISOU 1772 CG2 ILE F 226 2494 3551 2642 498 325 295 C ATOM 1773 CD1 ILE A 226 72.443 47.929 51.237 1.00 30.57 C ANISOU 1773 CD1 ILE F 226 3755 4324 3538 229 1015 -389 C ATOM 1774 N SER A 227 70.071 43.531 49.561 1.00 25.04 N ANISOU 1774 N SER F 227 3424 3454 2636 -15 -298 -68 N ATOM 1775 CA SER A 227 68.656 43.182 49.407 1.00 26.89 C ANISOU 1775 CA SER F 227 3845 3709 2662 -327 253 -370 C ATOM 1776 C SER A 227 68.046 42.710 50.727 1.00 27.33 C ANISOU 1776 C SER F 227 3780 3607 2999 -575 -69 -80 C ATOM 1777 O SER A 227 66.836 42.784 50.928 1.00 25.90 O ANISOU 1777 O SER F 227 3228 3565 3048 -395 43 -78 O ATOM 1778 CB SER A 227 68.451 42.096 48.348 1.00 28.65 C ANISOU 1778 CB SER F 227 3612 3899 3375 57 326 -525 C ATOM 1779 OG SER A 227 68.892 40.824 48.826 1.00 29.28 O ANISOU 1779 OG SER F 227 4302 3703 3122 -12 499 -34 O ATOM 1780 N CYS A 228 68.890 42.207 51.656 1.00 27.72 N ANISOU 1780 N CYS F 228 3531 3482 3517 -138 -413 144 N ATOM 1781 CA CYS A 228 68.214 41.709 52.861 1.00 30.52 C ANISOU 1781 CA CYS F 228 3796 4297 3502 -259 -491 167 C ATOM 1782 C CYS A 228 67.779 42.875 53.745 1.00 28.64 C ANISOU 1782 C CYS F 228 4034 3652 3198 -282 -635 375 C ATOM 1783 O CYS A 228 67.034 42.658 54.707 1.00 28.04 O ANISOU 1783 O CYS F 228 4053 4283 2318 -141 -620 895 O ATOM 1784 CB CYS A 228 69.096 40.641 53.524 1.00 35.97 C ANISOU 1784 CB CYS F 228 4947 4097 4625 374 -2151 -672 C ATOM 1785 SG CYS A 228 69.486 39.295 52.276 1.00 44.93 S ANISOU 1785 SG CYS F 228 6784 4787 5499 995 -101 253 S ATOM 1786 N LEU A 229 68.150 44.123 53.437 1.00 25.14 N ANISOU 1786 N LEU F 229 3768 3358 2425 -601 -289 556 N ATOM 1787 CA LEU A 229 67.587 45.246 54.198 1.00 26.01 C ANISOU 1787 CA LEU F 229 3763 3876 2245 -645 -166 307 C ATOM 1788 C LEU A 229 66.088 45.395 54.010 1.00 27.05 C ANISOU 1788 C LEU F 229 3811 3617 2851 -359 608 -10 C ATOM 1789 O LEU A 229 65.423 46.096 54.786 1.00 25.11 O ANISOU 1789 O LEU F 229 3310 3704 2526 -28 400 164 O ATOM 1790 CB LEU A 229 68.284 46.564 53.822 1.00 27.99 C ANISOU 1790 CB LEU F 229 3715 4359 2561 -462 -105 389 C ATOM 1791 CG LEU A 229 69.707 46.682 54.398 1.00 35.45 C ANISOU 1791 CG LEU F 229 4502 5677 3289 -1842 -283 498 C ATOM 1792 CD1 LEU A 229 70.357 47.982 53.976 1.00 35.34 C ANISOU 1792 CD1 LEU F 229 4276 6000 3152 -1493 117 -705 C ATOM 1793 CD2 LEU A 229 69.658 46.591 55.916 1.00 30.45 C ANISOU 1793 CD2 LEU F 229 3824 4477 3267 -1275 323 542 C ATOM 1794 N GLN A 230 65.518 44.740 53.004 1.00 26.40 N ANISOU 1794 N GLN F 230 3851 3533 2648 -560 549 -290 N ATOM 1795 CA GLN A 230 64.072 44.712 52.839 1.00 25.65 C ANISOU 1795 CA GLN F 230 3857 3443 2445 -411 8 347 C ATOM 1796 C GLN A 230 63.387 44.081 54.055 1.00 24.61 C ANISOU 1796 C GLN F 230 3239 3277 2836 167 82 -266 C ATOM 1797 O GLN A 230 62.216 44.338 54.327 1.00 26.95 O ANISOU 1797 O GLN F 230 3802 3453 2986 -187 192 -316 O ATOM 1798 CB GLN A 230 63.666 43.905 51.595 1.00 25.56 C ANISOU 1798 CB GLN F 230 4034 3023 2655 -236 224 432 C ATOM 1799 CG GLN A 230 64.055 44.561 50.281 1.00 25.03 C ANISOU 1799 CG GLN F 230 3973 3053 2486 296 372 499 C ATOM 1800 CD GLN A 230 63.639 43.744 49.073 1.00 27.22 C ANISOU 1800 CD GLN F 230 3859 3743 2742 -48 491 -185 C ATOM 1801 OE1 GLN A 230 62.635 43.020 49.133 1.00 28.77 O ANISOU 1801 OE1 GLN F 230 3961 3766 3204 -190 487 95 O ATOM 1802 NE2 GLN A 230 64.396 43.852 47.977 1.00 31.30 N ANISOU 1802 NE2 GLN F 230 4572 4527 2795 -375 440 -383 N ATOM 1803 N LEU A 231 64.135 43.230 54.762 1.00 25.39 N ANISOU 1803 N LEU F 231 3599 3562 2485 206 -28 -133 N ATOM 1804 CA LEU A 231 63.579 42.551 55.918 1.00 24.25 C ANISOU 1804 CA LEU F 231 3256 3484 2474 130 188 -459 C ATOM 1805 C LEU A 231 63.874 43.331 57.199 1.00 24.06 C ANISOU 1805 C LEU F 231 3218 3411 2514 113 235 -303 C ATOM 1806 O LEU A 231 63.421 42.963 58.291 1.00 31.82 O ANISOU 1806 O LEU F 231 4543 5218 2330 -1154 174 -216 O ATOM 1807 CB LEU A 231 64.159 41.140 56.058 1.00 25.21 C ANISOU 1807 CB LEU F 231 2684 3926 2969 149 149 -360 C ATOM 1808 CG LEU A 231 63.941 40.258 54.827 1.00 27.06 C ANISOU 1808 CG LEU F 231 3295 3610 3378 173 658 -285 C ATOM 1809 CD1 LEU A 231 64.558 38.889 55.082 1.00 28.51 C ANISOU 1809 CD1 LEU F 231 3502 4002 3326 534 145 -685 C ATOM 1810 CD2 LEU A 231 62.454 40.212 54.508 1.00 28.42 C ANISOU 1810 CD2 LEU F 231 3397 4006 3397 -320 521 -514 C ATOM 1811 N HIS A 232 64.633 44.412 57.065 1.00 26.95 N ANISOU 1811 N HIS F 232 3167 3463 3609 -99 451 265 N ATOM 1812 CA HIS A 232 64.976 45.153 58.286 1.00 26.73 C ANISOU 1812 CA HIS F 232 2986 3787 3384 -101 213 -20 C ATOM 1813 C HIS A 232 63.825 46.042 58.711 1.00 25.36 C ANISOU 1813 C HIS F 232 3199 3722 2714 -146 -298 93 C ATOM 1814 O HIS A 232 63.117 46.634 57.902 1.00 29.30 O ANISOU 1814 O HIS F 232 4631 3628 2874 -997 159 409 O ATOM 1815 CB HIS A 232 66.264 45.945 58.020 1.00 24.21 C ANISOU 1815 CB HIS F 232 3148 3584 2465 -189 147 217 C ATOM 1816 CG HIS A 232 66.806 46.542 59.282 1.00 24.58 C ANISOU 1816 CG HIS F 232 3459 3392 2489 -228 314 -9 C ATOM 1817 ND1 HIS A 232 66.354 47.757 59.749 1.00 24.87 N ANISOU 1817 ND1 HIS F 232 3275 3272 2904 -316 339 11 N ATOM 1818 CD2 HIS A 232 67.729 46.087 60.156 1.00 23.99 C ANISOU 1818 CD2 HIS F 232 3153 3477 2487 -108 361 69 C ATOM 1819 CE1 HIS A 232 66.991 48.037 60.882 1.00 27.11 C ANISOU 1819 CE1 HIS F 232 3390 3582 3326 73 781 245 C ATOM 1820 NE2 HIS A 232 67.827 47.045 61.149 1.00 27.56 N ANISOU 1820 NE2 HIS F 232 3913 3291 3266 -106 1117 149 N ATOM 1821 N PRO A 233 63.565 46.161 60.016 1.00 29.85 N ANISOU 1821 N PRO F 233 4389 4130 2825 -525 -831 -39 N ATOM 1822 CA PRO A 233 62.434 46.983 60.463 1.00 29.55 C ANISOU 1822 CA PRO F 233 4353 4227 2648 -629 20 -135 C ATOM 1823 C PRO A 233 62.525 48.437 60.012 1.00 30.17 C ANISOU 1823 C PRO F 233 4240 3997 3226 -655 269 54 C ATOM 1824 O PRO A 233 61.473 49.071 59.827 1.00 30.28 O ANISOU 1824 O PRO F 233 4342 3887 3276 -373 1171 -270 O ATOM 1825 CB PRO A 233 62.506 46.921 61.990 1.00 29.53 C ANISOU 1825 CB PRO F 233 4372 4156 2691 -1082 502 167 C ATOM 1826 CG PRO A 233 63.767 46.236 62.332 1.00 33.98 C ANISOU 1826 CG PRO F 233 5727 4093 3092 -287 649 102 C ATOM 1827 CD PRO A 233 64.279 45.513 61.122 1.00 31.71 C ANISOU 1827 CD PRO F 233 5181 4341 2525 -575 -100 46 C ATOM 1828 N LYS A 234 63.703 49.026 59.832 1.00 28.88 N ANISOU 1828 N LYS F 234 3639 4258 3076 -531 1301 -227 N ATOM 1829 CA LYS A 234 63.759 50.467 59.572 1.00 29.54 C ANISOU 1829 CA LYS F 234 3940 4172 3110 -404 1065 -86 C ATOM 1830 C LYS A 234 64.991 50.844 58.756 1.00 33.54 C ANISOU 1830 C LYS F 234 4515 4743 3485 -914 306 503 C ATOM 1831 O LYS A 234 66.031 51.249 59.303 1.00 27.61 O ANISOU 1831 O LYS F 234 2921 4179 3391 248 464 169 O ATOM 1832 CB LYS A 234 63.764 51.241 60.897 1.00 30.48 C ANISOU 1832 CB LYS F 234 3351 4769 3459 -536 1563 245 C ATOM 1833 CG LYS A 234 63.065 52.579 60.767 1.00 38.16 C ANISOU 1833 CG LYS F 234 4449 4908 5142 -7 2316 -28 C ATOM 1834 CD LYS A 234 63.325 53.455 61.980 1.00 47.81 C ANISOU 1834 CD LYS F 234 6546 5808 5814 -229 3168 -1844 C ATOM 1835 CE LYS A 234 62.759 52.772 63.213 1.00 54.11 C ANISOU 1835 CE LYS F 234 8746 6080 5734 -1419 2641 -2081 C ATOM 1836 NZ LYS A 234 61.711 53.659 63.804 1.00 66.62 N ANISOU 1836 NZ LYS F 234 10734 5787 8791 -2122 2186 -2864 N ATOM 1837 N ALA A 235 64.861 50.697 57.445 1.00 27.96 N ANISOU 1837 N ALA F 235 3557 3681 3387 -288 66 568 N ATOM 1838 CA ALA A 235 65.935 50.938 56.497 1.00 31.58 C ANISOU 1838 CA ALA F 235 3988 4098 3913 -355 -424 435 C ATOM 1839 C ALA A 235 65.620 52.085 55.536 1.00 29.07 C ANISOU 1839 C ALA F 235 3748 3818 3480 -355 -57 357 C ATOM 1840 O ALA A 235 64.495 52.335 55.059 1.00 31.00 O ANISOU 1840 O ALA F 235 3926 3599 4253 -14 747 353 O ATOM 1841 CB ALA A 235 66.226 49.657 55.719 1.00 30.40 C ANISOU 1841 CB ALA F 235 4795 3101 3656 -216 -579 613 C ATOM 1842 N ILE A 236 66.682 52.845 55.238 1.00 26.94 N ANISOU 1842 N ILE F 236 3158 3904 3176 100 507 -133 N ATOM 1843 CA ILE A 236 66.572 54.003 54.369 1.00 31.10 C ANISOU 1843 CA ILE F 236 3868 4157 3793 175 -244 -227 C ATOM 1844 C ILE A 236 67.717 54.015 53.370 1.00 29.56 C ANISOU 1844 C ILE F 236 3757 4065 3411 -181 121 1 C ATOM 1845 O ILE A 236 68.849 53.888 53.817 1.00 33.00 O ANISOU 1845 O ILE F 236 5284 4375 2879 -612 -69 189 O ATOM 1846 CB ILE A 236 66.626 55.306 55.189 1.00 31.23 C ANISOU 1846 CB ILE F 236 3621 4325 3921 596 -804 -478 C ATOM 1847 CG1 ILE A 236 65.722 55.263 56.414 1.00 35.13 C ANISOU 1847 CG1 ILE F 236 3770 5456 4123 385 -695 -1035 C ATOM 1848 CG2 ILE A 236 66.315 56.521 54.330 1.00 31.42 C ANISOU 1848 CG2 ILE F 236 2994 5127 3817 -118 -89 1014 C ATOM 1849 CD1 ILE A 236 65.729 56.513 57.278 1.00 55.06 C ANISOU 1849 CD1 ILE F 236 7612 6737 6571 -825 3180 -2168 C ATOM 1850 N MET A 237 67.404 54.160 52.100 1.00 29.36 N ANISOU 1850 N MET F 237 3617 4074 3464 -752 422 95 N ATOM 1851 CA MET A 237 68.380 54.358 51.049 1.00 30.49 C ANISOU 1851 CA MET F 237 3624 4555 3407 -270 224 -150 C ATOM 1852 C MET A 237 68.334 55.839 50.625 1.00 30.72 C ANISOU 1852 C MET F 237 3624 4444 3602 -190 392 -60 C ATOM 1853 O MET A 237 67.241 56.312 50.286 1.00 31.33 O ANISOU 1853 O MET F 237 3859 4527 3519 -259 548 85 O ATOM 1854 CB MET A 237 68.137 53.538 49.792 1.00 32.89 C ANISOU 1854 CB MET F 237 3613 4865 4018 -523 678 -645 C ATOM 1855 CG MET A 237 67.853 52.069 49.938 1.00 37.03 C ANISOU 1855 CG MET F 237 3307 5944 4817 -827 797 294 C ATOM 1856 SD MET A 237 69.155 51.158 50.742 1.00 48.54 S ANISOU 1856 SD MET F 237 5863 5740 6841 -99 -1040 349 S ATOM 1857 CE MET A 237 70.369 50.869 49.471 1.00 42.25 C ANISOU 1857 CE MET F 237 6070 5304 4680 934 -1908 1637 C ATOM 1858 N VAL A 238 69.490 56.478 50.670 1.00 29.35 N ANISOU 1858 N VAL F 238 3627 4330 3193 -186 196 -143 N ATOM 1859 CA VAL A 238 69.586 57.888 50.271 1.00 28.91 C ANISOU 1859 CA VAL F 238 3688 4254 3042 -176 227 13 C ATOM 1860 C VAL A 238 70.453 57.969 49.021 1.00 28.28 C ANISOU 1860 C VAL F 238 3595 4044 3107 -184 263 -10 C ATOM 1861 O VAL A 238 71.629 57.597 49.062 1.00 28.31 O ANISOU 1861 O VAL F 238 3533 4080 3146 -227 80 217 O ATOM 1862 CB VAL A 238 70.159 58.773 51.385 1.00 29.24 C ANISOU 1862 CB VAL F 238 3648 4347 3114 -173 238 -121 C ATOM 1863 CG1 VAL A 238 69.984 60.256 51.059 1.00 27.27 C ANISOU 1863 CG1 VAL F 238 3419 4035 2908 -480 56 -206 C ATOM 1864 CG2 VAL A 238 69.506 58.402 52.715 1.00 26.61 C ANISOU 1864 CG2 VAL F 238 3134 3775 3200 279 288 -355 C ATOM 1865 N CYS A 239 69.874 58.428 47.901 1.00 25.74 N ANISOU 1865 N CYS F 239 3053 3681 3047 -106 288 -148 N ATOM 1866 CA CYS A 239 70.679 58.225 46.698 1.00 29.29 C ANISOU 1866 CA CYS F 239 3473 4457 3199 307 101 -600 C ATOM 1867 C CYS A 239 70.744 59.453 45.809 1.00 28.69 C ANISOU 1867 C CYS F 239 4053 3961 2886 -135 87 142 C ATOM 1868 O CYS A 239 69.934 60.390 45.880 1.00 29.05 O ANISOU 1868 O CYS F 239 3648 3928 3461 -210 517 295 O ATOM 1869 CB CYS A 239 70.073 57.007 45.987 1.00 34.03 C ANISOU 1869 CB CYS F 239 4347 3865 4719 742 1239 -760 C ATOM 1870 SG CYS A 239 68.520 57.350 45.116 1.00 39.99 S ANISOU 1870 SG CYS F 239 5272 5296 4628 -462 850 -44 S ATOM 1871 N ASP A 240 71.769 59.451 44.929 1.00 26.15 N ANISOU 1871 N ASP F 240 3033 4251 2650 -398 564 161 N ATOM 1872 CA ASP A 240 71.873 60.556 43.985 1.00 29.09 C ANISOU 1872 CA ASP F 240 3413 4564 3075 -481 205 457 C ATOM 1873 C ASP A 240 71.296 60.144 42.639 1.00 28.66 C ANISOU 1873 C ASP F 240 3324 4458 3108 105 229 659 C ATOM 1874 O ASP A 240 70.863 59.003 42.470 1.00 28.38 O ANISOU 1874 O ASP F 240 3477 3970 3336 387 396 598 O ATOM 1875 CB ASP A 240 73.309 61.008 43.821 1.00 29.89 C ANISOU 1875 CB ASP F 240 3770 4689 2899 -685 -195 549 C ATOM 1876 CG ASP A 240 74.237 60.028 43.168 1.00 31.16 C ANISOU 1876 CG ASP F 240 4159 4670 3010 -564 -486 520 C ATOM 1877 OD1 ASP A 240 73.847 58.901 42.811 1.00 32.48 O ANISOU 1877 OD1 ASP F 240 4104 4798 3439 -167 -804 258 O ATOM 1878 OD2 ASP A 240 75.412 60.423 43.010 1.00 31.57 O ANISOU 1878 OD2 ASP F 240 4681 4817 2497 -942 -278 564 O ATOM 1879 N GLU A 241 71.277 61.067 41.690 1.00 29.71 N ANISOU 1879 N GLU F 241 3604 4350 3333 116 44 789 N ATOM 1880 CA GLU A 241 70.644 60.750 40.393 1.00 31.31 C ANISOU 1880 CA GLU F 241 4200 4568 3129 131 101 643 C ATOM 1881 C GLU A 241 71.337 59.650 39.609 1.00 29.43 C ANISOU 1881 C GLU F 241 3646 4509 3026 -128 -340 422 C ATOM 1882 O GLU A 241 70.680 58.704 39.140 1.00 29.66 O ANISOU 1882 O GLU F 241 4029 4344 2898 -75 59 731 O ATOM 1883 CB GLU A 241 70.560 62.042 39.562 1.00 31.59 C ANISOU 1883 CB GLU F 241 4093 5054 2857 382 334 599 C ATOM 1884 CG GLU A 241 70.131 61.827 38.118 1.00 39.18 C ANISOU 1884 CG GLU F 241 6070 5726 3091 -330 353 1361 C ATOM 1885 CD GLU A 241 70.136 63.173 37.404 1.00 49.17 C ANISOU 1885 CD GLU F 241 8485 5771 4425 -723 -2413 1325 C ATOM 1886 OE1 GLU A 241 69.217 63.967 37.688 1.00 58.40 O ANISOU 1886 OE1 GLU F 241 8545 5563 8081 -181 -2846 1624 O ATOM 1887 OE2 GLU A 241 71.053 63.441 36.591 1.00 68.54 O ANISOU 1887 OE2 GLU F 241 9711 9225 7105 -1444 -3487 -521 O ATOM 1888 N PRO A 242 72.652 59.677 39.385 1.00 30.69 N ANISOU 1888 N PRO F 242 4110 4639 2911 -380 -720 663 N ATOM 1889 CA PRO A 242 73.286 58.631 38.589 1.00 31.27 C ANISOU 1889 CA PRO F 242 4644 4100 3136 -448 -489 889 C ATOM 1890 C PRO A 242 73.091 57.233 39.171 1.00 29.98 C ANISOU 1890 C PRO F 242 4208 4477 2705 -484 -265 214 C ATOM 1891 O PRO A 242 73.144 56.258 38.398 1.00 31.45 O ANISOU 1891 O PRO F 242 4778 4586 2587 -409 303 684 O ATOM 1892 CB PRO A 242 74.772 58.961 38.634 1.00 33.73 C ANISOU 1892 CB PRO F 242 4340 4658 3819 -618 -690 612 C ATOM 1893 CG PRO A 242 74.900 60.323 39.235 1.00 34.64 C ANISOU 1893 CG PRO F 242 4523 4941 3700 -700 -610 174 C ATOM 1894 CD PRO A 242 73.592 60.714 39.828 1.00 34.24 C ANISOU 1894 CD PRO F 242 5007 5146 2856 -1301 125 244 C ATOM 1895 N SER A 243 72.884 57.105 40.478 1.00 29.23 N ANISOU 1895 N SER F 243 3971 4416 2718 -540 -182 61 N ATOM 1896 CA SER A 243 72.704 55.775 41.058 1.00 27.31 C ANISOU 1896 CA SER F 243 3917 4111 2349 -525 14 50 C ATOM 1897 C SER A 243 71.369 55.135 40.676 1.00 27.62 C ANISOU 1897 C SER F 243 3848 3712 2935 -250 285 29 C ATOM 1898 O SER A 243 71.163 53.936 40.894 1.00 26.17 O ANISOU 1898 O SER F 243 3898 3493 2554 -331 352 425 O ATOM 1899 CB SER A 243 72.815 55.864 42.589 1.00 29.73 C ANISOU 1899 CB SER F 243 4950 3969 2378 -585 1 256 C ATOM 1900 OG SER A 243 71.611 56.401 43.137 1.00 27.83 O ANISOU 1900 OG SER F 243 3599 4346 2629 -370 39 -250 O ATOM 1901 N THR A 244 70.441 55.920 40.121 1.00 26.75 N ANISOU 1901 N THR F 244 3617 3871 2676 -168 129 104 N ATOM 1902 CA THR A 244 69.097 55.418 39.855 1.00 27.91 C ANISOU 1902 CA THR F 244 4136 3994 2473 -596 -30 87 C ATOM 1903 C THR A 244 68.941 54.781 38.473 1.00 25.34 C ANISOU 1903 C THR F 244 3259 3619 2751 131 26 212 C ATOM 1904 O THR A 244 67.788 54.474 38.129 1.00 30.29 O ANISOU 1904 O THR F 244 4601 4276 2633 -678 -13 649 O ATOM 1905 CB THR A 244 68.016 56.521 39.936 1.00 28.25 C ANISOU 1905 CB THR F 244 4132 4062 2537 -640 618 -320 C ATOM 1906 OG1 THR A 244 68.288 57.503 38.918 1.00 31.66 O ANISOU 1906 OG1 THR F 244 4688 4038 3302 -486 317 809 O ATOM 1907 CG2 THR A 244 67.994 57.231 41.291 1.00 32.74 C ANISOU 1907 CG2 THR F 244 4748 4681 3012 -1123 1583 -177 C ATOM 1908 N MET A 245 70.007 54.586 37.716 1.00 27.73 N ANISOU 1908 N MET F 245 3833 3638 3063 254 323 -141 N ATOM 1909 CA MET A 245 69.992 54.166 36.316 1.00 29.15 C ANISOU 1909 CA MET F 245 3841 4124 3111 -106 489 -229 C ATOM 1910 C MET A 245 69.281 52.836 36.066 1.00 28.19 C ANISOU 1910 C MET F 245 3793 3985 2932 -127 329 146 C ATOM 1911 O MET A 245 68.682 52.625 34.996 1.00 28.07 O ANISOU 1911 O MET F 245 3395 4168 3100 -545 -121 637 O ATOM 1912 CB MET A 245 71.422 54.037 35.739 1.00 32.08 C ANISOU 1912 CB MET F 245 4907 4979 2302 -1388 557 16 C ATOM 1913 CG MET A 245 72.112 55.360 35.461 1.00 33.99 C ANISOU 1913 CG MET F 245 4894 4983 3038 -1511 528 382 C ATOM 1914 SD MET A 245 71.202 56.473 34.364 1.00 43.11 S ANISOU 1914 SD MET F 245 7059 5708 3614 -496 -528 370 S ATOM 1915 CE MET A 245 70.357 57.574 35.494 1.00 42.86 C ANISOU 1915 CE MET F 245 5039 5972 5272 -297 -1271 -500 C ATOM 1916 N GLU A 246 69.339 51.895 37.002 1.00 27.84 N ANISOU 1916 N GLU F 246 3908 3836 2832 -253 438 416 N ATOM 1917 CA GLU A 246 68.774 50.572 36.764 1.00 27.58 C ANISOU 1917 CA GLU F 246 3866 3777 2835 -124 306 269 C ATOM 1918 C GLU A 246 67.377 50.440 37.346 1.00 27.70 C ANISOU 1918 C GLU F 246 3831 3611 3081 5 87 364 C ATOM 1919 O GLU A 246 66.780 49.360 37.247 1.00 30.01 O ANISOU 1919 O GLU F 246 3882 4391 3127 -343 502 121 O ATOM 1920 CB GLU A 246 69.693 49.515 37.377 1.00 26.55 C ANISOU 1920 CB GLU F 246 3614 3741 2732 -456 483 478 C ATOM 1921 CG GLU A 246 71.081 49.514 36.739 1.00 29.45 C ANISOU 1921 CG GLU F 246 4390 3866 2933 -516 254 251 C ATOM 1922 CD GLU A 246 71.118 48.765 35.425 1.00 29.68 C ANISOU 1922 CD GLU F 246 3787 4147 3342 -285 257 -45 C ATOM 1923 OE1 GLU A 246 70.054 48.248 35.002 1.00 32.95 O ANISOU 1923 OE1 GLU F 246 4022 4907 3589 -275 356 926 O ATOM 1924 OE2 GLU A 246 72.204 48.688 34.808 1.00 32.32 O ANISOU 1924 OE2 GLU F 246 4831 3772 3677 228 -161 -223 O ATOM 1925 N LEU A 247 66.831 51.495 37.949 1.00 27.85 N ANISOU 1925 N LEU F 247 4243 3797 2543 -168 485 316 N ATOM 1926 CA LEU A 247 65.463 51.419 38.474 1.00 26.84 C ANISOU 1926 CA LEU F 247 4342 3880 1975 -95 222 389 C ATOM 1927 C LEU A 247 64.425 51.615 37.388 1.00 28.12 C ANISOU 1927 C LEU F 247 4599 4000 2084 -399 350 412 C ATOM 1928 O LEU A 247 64.744 52.271 36.392 1.00 27.40 O ANISOU 1928 O LEU F 247 4793 3795 1823 -571 446 390 O ATOM 1929 CB LEU A 247 65.222 52.492 39.551 1.00 26.12 C ANISOU 1929 CB LEU F 247 3883 3889 2151 -158 258 429 C ATOM 1930 CG LEU A 247 66.089 52.394 40.806 1.00 27.37 C ANISOU 1930 CG LEU F 247 4202 4010 2188 143 419 533 C ATOM 1931 CD1 LEU A 247 65.754 53.561 41.739 1.00 25.57 C ANISOU 1931 CD1 LEU F 247 2934 4540 2240 -178 83 230 C ATOM 1932 CD2 LEU A 247 65.874 51.048 41.468 1.00 24.81 C ANISOU 1932 CD2 LEU F 247 3837 3233 2357 45 816 662 C ATOM 1933 N LYS A 248 63.206 51.126 37.551 1.00 28.25 N ANISOU 1933 N LYS F 248 4041 4115 2577 -83 270 586 N ATOM 1934 CA LYS A 248 62.188 51.530 36.577 1.00 27.77 C ANISOU 1934 CA LYS F 248 3864 3955 2733 -359 -276 579 C ATOM 1935 C LYS A 248 61.767 52.976 36.832 1.00 27.06 C ANISOU 1935 C LYS F 248 3758 4145 2381 -282 -377 518 C ATOM 1936 O LYS A 248 61.774 53.434 37.979 1.00 27.94 O ANISOU 1936 O LYS F 248 3636 4469 2510 -630 -64 591 O ATOM 1937 CB LYS A 248 60.942 50.668 36.610 1.00 27.56 C ANISOU 1937 CB LYS F 248 3811 4018 2643 -336 130 12 C ATOM 1938 CG LYS A 248 61.143 49.211 36.201 1.00 30.94 C ANISOU 1938 CG LYS F 248 3946 4092 3718 324 -465 382 C ATOM 1939 CD LYS A 248 59.810 48.509 36.458 1.00 36.79 C ANISOU 1939 CD LYS F 248 3777 4469 5732 267 -268 248 C ATOM 1940 CE LYS A 248 59.922 47.010 36.210 1.00 41.56 C ANISOU 1940 CE LYS F 248 3895 5194 6701 316 1231 655 C ATOM 1941 NZ LYS A 248 58.829 46.586 35.275 1.00 64.44 N ANISOU 1941 NZ LYS F 248 7675 7829 8980 -1186 4287 57 N ATOM 1942 N VAL A 249 61.410 53.671 35.770 1.00 27.82 N ANISOU 1942 N VAL F 249 4064 3966 2541 -418 -418 653 N ATOM 1943 CA VAL A 249 60.912 55.040 35.860 1.00 29.14 C ANISOU 1943 CA VAL F 249 4339 3867 2865 -364 -622 687 C ATOM 1944 C VAL A 249 59.789 55.124 36.871 1.00 29.69 C ANISOU 1944 C VAL F 249 4243 4183 2856 -604 51 363 C ATOM 1945 O VAL A 249 59.688 56.053 37.675 1.00 29.65 O ANISOU 1945 O VAL F 249 4190 4321 2753 -180 -49 692 O ATOM 1946 CB VAL A 249 60.447 55.495 34.458 1.00 30.17 C ANISOU 1946 CB VAL F 249 4621 3819 3023 -532 -573 890 C ATOM 1947 CG1 VAL A 249 59.626 56.773 34.552 1.00 29.07 C ANISOU 1947 CG1 VAL F 249 5318 3551 2176 -649 -309 701 C ATOM 1948 CG2 VAL A 249 61.632 55.689 33.521 1.00 24.16 C ANISOU 1948 CG2 VAL F 249 3130 3405 2647 514 -231 679 C ATOM 1949 N LYS A 250 58.874 54.160 36.899 1.00 27.54 N ANISOU 1949 N LYS F 250 3970 4005 2488 39 -519 338 N ATOM 1950 CA LYS A 250 57.749 54.310 37.844 1.00 27.82 C ANISOU 1950 CA LYS F 250 4165 3806 2600 -394 167 308 C ATOM 1951 C LYS A 250 58.169 54.136 39.301 1.00 27.22 C ANISOU 1951 C LYS F 250 4222 3668 2452 -25 224 26 C ATOM 1952 O LYS A 250 57.529 54.657 40.241 1.00 28.24 O ANISOU 1952 O LYS F 250 3419 4438 2873 -240 412 -535 O ATOM 1953 CB LYS A 250 56.643 53.300 37.537 1.00 30.23 C ANISOU 1953 CB LYS F 250 4164 4250 3073 -540 123 477 C ATOM 1954 CG LYS A 250 57.124 51.850 37.691 1.00 31.70 C ANISOU 1954 CG LYS F 250 4092 4896 3057 -244 -261 487 C ATOM 1955 CD LYS A 250 55.896 50.950 37.538 1.00 35.06 C ANISOU 1955 CD LYS F 250 4216 5425 3681 -254 811 324 C ATOM 1956 CE LYS A 250 56.236 49.496 37.802 1.00 36.44 C ANISOU 1956 CE LYS F 250 4030 6135 3681 24 798 111 C ATOM 1957 NZ LYS A 250 55.035 48.643 37.581 1.00 41.29 N ANISOU 1957 NZ LYS F 250 4044 7263 4381 -820 -949 157 N ATOM 1958 N THR A 251 59.245 53.378 39.514 1.00 27.37 N ANISOU 1958 N THR F 251 3712 3797 2891 137 196 475 N ATOM 1959 CA THR A 251 59.750 53.194 40.869 1.00 31.40 C ANISOU 1959 CA THR F 251 4784 4275 2872 -274 472 537 C ATOM 1960 C THR A 251 60.306 54.510 41.391 1.00 29.52 C ANISOU 1960 C THR F 251 4861 3738 2619 -202 455 249 C ATOM 1961 O THR A 251 60.023 54.915 42.517 1.00 32.25 O ANISOU 1961 O THR F 251 5614 3891 2749 -72 548 83 O ATOM 1962 CB THR A 251 60.878 52.150 40.887 1.00 28.46 C ANISOU 1962 CB THR F 251 4228 4524 2061 80 99 797 C ATOM 1963 OG1 THR A 251 60.348 50.913 40.412 1.00 29.70 O ANISOU 1963 OG1 THR F 251 4389 4539 2356 -373 456 437 O ATOM 1964 CG2 THR A 251 61.386 51.936 42.315 1.00 31.07 C ANISOU 1964 CG2 THR F 251 5112 4743 1949 -1025 259 640 C ATOM 1965 N LEU A 252 61.106 55.160 40.539 1.00 29.85 N ANISOU 1965 N LEU F 252 4893 3879 2568 -589 377 794 N ATOM 1966 CA LEU A 252 61.704 56.441 40.924 1.00 34.76 C ANISOU 1966 CA LEU F 252 4921 5004 3281 -1060 667 206 C ATOM 1967 C LEU A 252 60.607 57.475 41.120 1.00 33.21 C ANISOU 1967 C LEU F 252 3835 5125 3657 -622 356 619 C ATOM 1968 O LEU A 252 60.602 58.273 42.065 1.00 35.21 O ANISOU 1968 O LEU F 252 4810 5168 3402 -383 402 545 O ATOM 1969 CB LEU A 252 62.765 56.837 39.890 1.00 36.74 C ANISOU 1969 CB LEU F 252 5077 5825 3058 -1259 574 306 C ATOM 1970 CG LEU A 252 63.643 58.044 40.222 1.00 39.19 C ANISOU 1970 CG LEU F 252 5216 5905 3768 -1667 697 -49 C ATOM 1971 CD1 LEU A 252 64.410 57.828 41.536 1.00 34.52 C ANISOU 1971 CD1 LEU F 252 4461 5526 3128 -1047 903 -630 C ATOM 1972 CD2 LEU A 252 64.571 58.392 39.056 1.00 35.04 C ANISOU 1972 CD2 LEU F 252 4735 5034 3545 -297 241 214 C ATOM 1973 N ARG A 253 59.596 57.496 40.256 1.00 36.36 N ANISOU 1973 N ARG F 253 5121 5135 3561 -1103 453 433 N ATOM 1974 CA ARG A 253 58.457 58.409 40.363 1.00 38.59 C ANISOU 1974 CA ARG F 253 6027 5184 3451 -732 264 695 C ATOM 1975 C ARG A 253 57.640 58.185 41.634 1.00 38.93 C ANISOU 1975 C ARG F 253 6532 4733 3528 -872 285 679 C ATOM 1976 O ARG A 253 57.186 59.131 42.293 1.00 43.82 O ANISOU 1976 O ARG F 253 8345 4533 3773 -354 382 699 O ATOM 1977 CB ARG A 253 57.576 58.274 39.093 1.00 39.74 C ANISOU 1977 CB ARG F 253 6022 5503 3574 -39 425 1090 C ATOM 1978 CG ARG A 253 56.341 59.148 39.176 1.00 54.89 C ANISOU 1978 CG ARG F 253 9916 5416 5523 -414 1567 1488 C ATOM 1979 CD ARG A 253 55.299 58.847 38.112 1.00 78.02 C ANISOU 1979 CD ARG F 253 15665 7538 6442 -2471 1999 2875 C ATOM 1980 NE ARG A 253 55.174 60.003 37.211 1.00 91.76 N ANISOU 1980 NE ARG F 253 18216 8596 8054 -2693 518 4537 N ATOM 1981 CZ ARG A 253 54.156 60.838 37.120 1.00 97.65 C ANISOU 1981 CZ ARG F 253 19916 8465 8723 -3233 -1149 4968 C ATOM 1982 NH1 ARG A 253 53.065 60.699 37.861 1.00111.61 N ANISOU 1982 NH1 ARG F 253 22556 9699 10151 -3763 -1219 3091 N ATOM 1983 NH2 ARG A 253 54.223 61.842 36.243 1.00109.51 N ANISOU 1983 NH2 ARG F 253 21238 10420 9950 -2615 -1744 6339 N ATOM 1984 N TYR A 254 57.426 56.925 42.019 1.00 37.12 N ANISOU 1984 N TYR F 254 6131 4846 3126 -1609 379 1414 N ATOM 1985 CA TYR A 254 56.719 56.567 43.241 1.00 35.87 C ANISOU 1985 CA TYR F 254 5615 4834 3181 -1309 945 472 C ATOM 1986 C TYR A 254 57.373 57.135 44.501 1.00 37.91 C ANISOU 1986 C TYR F 254 6403 4597 3404 -1551 1324 326 C ATOM 1987 O TYR A 254 56.740 57.735 45.394 1.00 40.95 O ANISOU 1987 O TYR F 254 6914 4843 3804 -1788 1812 35 O ATOM 1988 CB TYR A 254 56.636 55.039 43.361 1.00 36.39 C ANISOU 1988 CB TYR F 254 5681 4772 3376 -1304 537 241 C ATOM 1989 CG TYR A 254 56.102 54.566 44.706 1.00 38.96 C ANISOU 1989 CG TYR F 254 6344 4956 3504 -1260 251 145 C ATOM 1990 CD1 TYR A 254 54.750 54.707 45.022 1.00 39.58 C ANISOU 1990 CD1 TYR F 254 6319 5114 3605 -1409 243 101 C ATOM 1991 CD2 TYR A 254 56.932 53.975 45.661 1.00 38.99 C ANISOU 1991 CD2 TYR F 254 6008 5015 3791 -1020 -21 264 C ATOM 1992 CE1 TYR A 254 54.240 54.281 46.240 1.00 39.41 C ANISOU 1992 CE1 TYR F 254 5976 4999 3999 -1329 -150 339 C ATOM 1993 CE2 TYR A 254 56.437 53.545 46.881 1.00 38.40 C ANISOU 1993 CE2 TYR F 254 5911 4858 3822 -1107 9 202 C ATOM 1994 CZ TYR A 254 55.092 53.700 47.164 1.00 40.32 C ANISOU 1994 CZ TYR F 254 6003 4892 4425 -1207 -391 446 C ATOM 1995 OH TYR A 254 54.573 53.283 48.364 1.00 45.13 O ANISOU 1995 OH TYR F 254 8431 4773 3942 -2493 -374 763 O ATOM 1996 N PHE A 255 58.699 56.926 44.596 1.00 35.08 N ANISOU 1996 N PHE F 255 5750 4409 3169 -1228 493 761 N ATOM 1997 CA PHE A 255 59.387 57.396 45.795 1.00 35.31 C ANISOU 1997 CA PHE F 255 6118 3955 3345 -899 881 713 C ATOM 1998 C PHE A 255 59.561 58.907 45.751 1.00 37.20 C ANISOU 1998 C PHE F 255 6690 3719 3723 -226 1206 146 C ATOM 1999 O PHE A 255 59.587 59.559 46.800 1.00 43.90 O ANISOU 1999 O PHE F 255 7467 5107 4107 -410 1880 93 O ATOM 2000 CB PHE A 255 60.755 56.719 45.940 1.00 30.76 C ANISOU 2000 CB PHE F 255 5648 3871 2168 -513 606 429 C ATOM 2001 CG PHE A 255 60.607 55.262 46.352 1.00 32.15 C ANISOU 2001 CG PHE F 255 5329 4350 2537 -747 575 341 C ATOM 2002 CD1 PHE A 255 60.253 54.952 47.658 1.00 32.72 C ANISOU 2002 CD1 PHE F 255 5091 4551 2790 -971 383 146 C ATOM 2003 CD2 PHE A 255 60.817 54.226 45.462 1.00 33.72 C ANISOU 2003 CD2 PHE F 255 5637 4575 2600 -310 721 593 C ATOM 2004 CE1 PHE A 255 60.106 53.627 48.066 1.00 33.26 C ANISOU 2004 CE1 PHE F 255 5722 4267 2648 -363 397 298 C ATOM 2005 CE2 PHE A 255 60.675 52.908 45.857 1.00 33.15 C ANISOU 2005 CE2 PHE F 255 5674 4244 2679 -442 398 229 C ATOM 2006 CZ PHE A 255 60.330 52.592 47.163 1.00 33.28 C ANISOU 2006 CZ PHE F 255 5897 4050 2699 -507 396 102 C ATOM 2007 N ASN A 256 59.692 59.464 44.549 1.00 37.09 N ANISOU 2007 N ASN F 256 6241 3836 4015 42 1174 699 N ATOM 2008 CA ASN A 256 59.826 60.908 44.424 1.00 42.58 C ANISOU 2008 CA ASN F 256 6272 5204 4702 471 1442 342 C ATOM 2009 C ASN A 256 58.533 61.575 44.875 1.00 43.82 C ANISOU 2009 C ASN F 256 5694 5102 5854 798 1520 286 C ATOM 2010 O ASN A 256 58.629 62.684 45.407 1.00 49.55 O ANISOU 2010 O ASN F 256 5990 5059 7777 1151 2251 909 O ATOM 2011 CB ASN A 256 60.162 61.377 43.009 1.00 45.84 C ANISOU 2011 CB ASN F 256 7020 5227 5172 1072 563 854 C ATOM 2012 CG ASN A 256 61.655 61.618 42.865 1.00 51.15 C ANISOU 2012 CG ASN F 256 7453 6339 5643 319 -365 978 C ATOM 2013 OD1 ASN A 256 62.240 62.565 43.408 1.00 63.15 O ANISOU 2013 OD1 ASN F 256 7543 8146 8305 -609 370 -352 O ATOM 2014 ND2 ASN A 256 62.301 60.723 42.137 1.00 59.01 N ANISOU 2014 ND2 ASN F 256 10319 7443 4660 -2024 1467 -407 N ATOM 2015 N GLU A 257 57.394 60.907 44.674 1.00 43.26 N ANISOU 2015 N GLU F 257 6315 5509 4613 250 2117 -95 N ATOM 2016 CA GLU A 257 56.154 61.524 45.157 1.00 46.91 C ANISOU 2016 CA GLU F 257 6788 5798 5238 -98 2812 -601 C ATOM 2017 C GLU A 257 55.952 61.262 46.641 1.00 49.57 C ANISOU 2017 C GLU F 257 8194 5336 5303 -921 2507 -405 C ATOM 2018 O GLU A 257 55.582 62.130 47.445 1.00 49.09 O ANISOU 2018 O GLU F 257 8394 5604 4654 -481 2513 81 O ATOM 2019 CB GLU A 257 54.996 61.030 44.274 1.00 57.48 C ANISOU 2019 CB GLU F 257 9569 6628 5642 -1616 3645 -717 C ATOM 2020 CG GLU A 257 55.242 61.408 42.804 1.00 69.57 C ANISOU 2020 CG GLU F 257 11906 8594 5933 -2785 2731 806 C ATOM 2021 CD GLU A 257 54.132 60.977 41.873 1.00 79.02 C ANISOU 2021 CD GLU F 257 13844 9722 6456 -4129 2561 1566 C ATOM 2022 OE1 GLU A 257 53.311 60.136 42.312 1.00 96.05 O ANISOU 2022 OE1 GLU F 257 16292 11402 8801 -8311 1429 2019 O ATOM 2023 OE2 GLU A 257 54.044 61.460 40.714 1.00 89.60 O ANISOU 2023 OE2 GLU F 257 17551 9594 6899 -4298 1870 2295 O ATOM 2024 N LEU A 258 56.197 60.039 47.098 1.00 47.38 N ANISOU 2024 N LEU F 258 8517 4891 4593 -940 2611 -410 N ATOM 2025 CA LEU A 258 56.023 59.713 48.499 1.00 50.87 C ANISOU 2025 CA LEU F 258 9305 5186 4839 -1285 2010 -881 C ATOM 2026 C LEU A 258 56.922 60.510 49.434 1.00 50.46 C ANISOU 2026 C LEU F 258 9888 5220 4064 -1167 1960 -398 C ATOM 2027 O LEU A 258 56.640 60.682 50.624 1.00 56.43 O ANISOU 2027 O LEU F 258 11745 5327 4367 -475 2277 -1063 O ATOM 2028 CB LEU A 258 56.298 58.207 48.643 1.00 51.82 C ANISOU 2028 CB LEU F 258 9073 5350 5265 -1419 867 -1596 C ATOM 2029 CG LEU A 258 56.152 57.629 50.053 1.00 55.99 C ANISOU 2029 CG LEU F 258 10130 5524 5618 -1907 118 -1687 C ATOM 2030 CD1 LEU A 258 54.691 57.678 50.471 1.00 64.99 C ANISOU 2030 CD1 LEU F 258 12598 5423 6671 -2252 -809 -1670 C ATOM 2031 CD2 LEU A 258 56.673 56.201 50.137 1.00 50.86 C ANISOU 2031 CD2 LEU F 258 8474 5253 5598 -2781 244 -1079 C ATOM 2032 N GLU A 259 58.061 61.029 48.972 1.00 46.86 N ANISOU 2032 N GLU F 259 8842 4555 4407 -487 1357 1040 N ATOM 2033 CA GLU A 259 59.011 61.605 49.931 1.00 45.60 C ANISOU 2033 CA GLU F 259 8904 4446 3977 14 1545 864 C ATOM 2034 C GLU A 259 59.200 63.081 49.633 1.00 49.17 C ANISOU 2034 C GLU F 259 8743 5471 4468 -133 1080 653 C ATOM 2035 O GLU A 259 60.071 63.761 50.181 1.00 48.07 O ANISOU 2035 O GLU F 259 8710 5793 3760 -122 724 1091 O ATOM 2036 CB GLU A 259 60.321 60.800 49.860 1.00 46.80 C ANISOU 2036 CB GLU F 259 8304 4519 4958 -451 4472 -385 C ATOM 2037 CG GLU A 259 60.969 60.622 51.241 1.00 57.76 C ANISOU 2037 CG GLU F 259 11515 4176 6255 -917 2905 1180 C ATOM 2038 CD GLU A 259 60.507 59.359 51.934 1.00 55.12 C ANISOU 2038 CD GLU F 259 11185 3572 6186 -78 3406 341 C ATOM 2039 OE1 GLU A 259 59.969 59.445 53.035 1.00 65.96 O ANISOU 2039 OE1 GLU F 259 14529 6178 4355 450 2391 1987 O ATOM 2040 OE2 GLU A 259 60.607 58.249 51.384 1.00 69.79 O ANISOU 2040 OE2 GLU F 259 9600 4789 12129 -2508 6009 -1473 O ATOM 2041 N ALA A 260 58.355 63.586 48.715 1.00 44.52 N ANISOU 2041 N ALA F 260 7647 4863 4406 659 1995 297 N ATOM 2042 CA ALA A 260 58.501 64.962 48.255 1.00 46.86 C ANISOU 2042 CA ALA F 260 7440 5203 5160 694 2246 501 C ATOM 2043 C ALA A 260 58.592 65.989 49.378 1.00 49.08 C ANISOU 2043 C ALA F 260 7882 5158 5608 701 2566 260 C ATOM 2044 O ALA A 260 59.403 66.912 49.343 1.00 49.48 O ANISOU 2044 O ALA F 260 7474 4853 6474 1891 2292 -515 O ATOM 2045 CB ALA A 260 57.335 65.345 47.344 1.00 45.90 C ANISOU 2045 CB ALA F 260 7330 5013 5096 694 1846 434 C ATOM 2046 N GLU A 261 57.749 65.840 50.386 1.00 49.76 N ANISOU 2046 N GLU F 261 8015 5128 5762 1212 2289 43 N ATOM 2047 CA GLU A 261 57.676 66.855 51.439 1.00 58.83 C ANISOU 2047 CA GLU F 261 10236 5801 6317 766 3757 -241 C ATOM 2048 C GLU A 261 58.951 66.839 52.275 1.00 57.24 C ANISOU 2048 C GLU F 261 9715 5717 6317 1168 3269 162 C ATOM 2049 O GLU A 261 59.340 67.819 52.910 1.00 52.72 O ANISOU 2049 O GLU F 261 9668 4880 5484 1062 2959 9 O ATOM 2050 CB GLU A 261 56.456 66.619 52.324 1.00 65.59 C ANISOU 2050 CB GLU F 261 11761 5403 7757 725 3823 -1336 C ATOM 2051 CG GLU A 261 55.275 67.546 52.165 1.00 78.63 C ANISOU 2051 CG GLU F 261 14955 5645 9274 230 1777 93 C ATOM 2052 CD GLU A 261 55.423 68.770 51.281 1.00 90.73 C ANISOU 2052 CD GLU F 261 17714 6934 9826 -99 89 1602 C ATOM 2053 OE1 GLU A 261 55.775 69.873 51.771 1.00 93.00 O ANISOU 2053 OE1 GLU F 261 17444 7105 10786 2597 -995 2857 O ATOM 2054 OE2 GLU A 261 55.167 68.654 50.055 1.00105.06 O ANISOU 2054 OE2 GLU F 261 22097 7991 9831 -725 257 1875 O ATOM 2055 N ASN A 262 59.574 65.661 52.237 1.00 55.39 N ANISOU 2055 N ASN F 262 8542 6013 6493 1073 2350 -29 N ATOM 2056 CA ASN A 262 60.734 65.384 53.068 1.00 49.60 C ANISOU 2056 CA ASN F 262 7153 5570 6124 1345 2237 -416 C ATOM 2057 C ASN A 262 62.041 65.725 52.385 1.00 51.02 C ANISOU 2057 C ASN F 262 6661 6390 6334 1264 2201 -590 C ATOM 2058 O ASN A 262 63.105 65.554 52.986 1.00 50.52 O ANISOU 2058 O ASN F 262 5771 7727 5697 206 2684 -634 O ATOM 2059 CB ASN A 262 60.776 63.889 53.446 1.00 44.56 C ANISOU 2059 CB ASN F 262 6658 5448 4826 1299 2615 -1416 C ATOM 2060 CG ASN A 262 59.511 63.456 54.157 1.00 50.37 C ANISOU 2060 CG ASN F 262 7736 5882 5522 772 1870 -1257 C ATOM 2061 OD1 ASN A 262 59.071 64.134 55.084 1.00 60.86 O ANISOU 2061 OD1 ASN F 262 7865 6632 8626 255 2311 -3505 O ATOM 2062 ND2 ASN A 262 58.905 62.352 53.757 1.00 53.11 N ANISOU 2062 ND2 ASN F 262 7280 5719 7181 968 1356 -2464 N ATOM 2063 N ILE A 263 62.015 66.174 51.130 1.00 54.88 N ANISOU 2063 N ILE F 263 7854 6657 6339 921 1957 -511 N ATOM 2064 CA ILE A 263 63.362 66.391 50.576 1.00 58.84 C ANISOU 2064 CA ILE F 263 9072 7101 6182 199 1693 -315 C ATOM 2065 C ILE A 263 63.551 67.861 50.265 1.00 61.53 C ANISOU 2065 C ILE F 263 8805 8054 6522 -134 1228 -518 C ATOM 2066 O ILE A 263 64.408 68.280 49.494 1.00 73.30 O ANISOU 2066 O ILE F 263 11969 8937 6945 -1392 -1345 1505 O ATOM 2067 CB ILE A 263 63.580 65.519 49.345 1.00 60.11 C ANISOU 2067 CB ILE F 263 9075 7875 5889 -323 1516 -647 C ATOM 2068 CG1 ILE A 263 62.533 65.753 48.256 1.00 60.97 C ANISOU 2068 CG1 ILE F 263 8141 8593 6432 -189 1709 -123 C ATOM 2069 CG2 ILE A 263 63.588 64.044 49.702 1.00 53.81 C ANISOU 2069 CG2 ILE F 263 7700 7705 5041 -1213 2539 -212 C ATOM 2070 CD1 ILE A 263 61.926 64.417 47.854 1.00 73.31 C ANISOU 2070 CD1 ILE F 263 6995 13184 7674 -2081 804 -698 C ATOM 2071 N LYS A 264 62.718 68.679 50.900 1.00 68.81 N ANISOU 2071 N LYS F 264 9647 7885 8611 823 2206 -294 N ATOM 2072 CA LYS A 264 62.901 70.128 50.787 1.00 76.55 C ANISOU 2072 CA LYS F 264 9629 8575 10881 860 1904 544 C ATOM 2073 C LYS A 264 63.824 70.662 51.878 1.00 77.52 C ANISOU 2073 C LYS F 264 8825 8920 11709 1188 1942 1056 C ATOM 2074 O LYS A 264 63.854 70.218 53.024 1.00 75.36 O ANISOU 2074 O LYS F 264 8680 8512 11443 798 2272 1025 O ATOM 2075 CB LYS A 264 61.537 70.824 50.827 1.00 76.51 C ANISOU 2075 CB LYS F 264 8786 8559 11725 1096 2521 342 C ATOM 2076 CG LYS A 264 60.407 70.038 50.176 1.00 80.69 C ANISOU 2076 CG LYS F 264 9279 9173 12207 413 2836 -39 C ATOM 2077 CD LYS A 264 59.056 70.674 50.476 1.00 78.42 C ANISOU 2077 CD LYS F 264 8394 9101 12301 798 3041 -22 C ATOM 2078 CE LYS A 264 58.183 70.672 49.230 1.00 78.43 C ANISOU 2078 CE LYS F 264 8762 8938 12101 682 3169 -309 C ATOM 2079 NZ LYS A 264 58.523 69.534 48.330 1.00 84.34 N ANISOU 2079 NZ LYS F 264 9861 10332 11853 -92 2924 -2156 N ATOM 2080 N GLY A 265 64.625 71.665 51.522 1.00 83.82 N ANISOU 2080 N GLY F 265 9209 9687 12953 641 1313 1474 N ATOM 2081 CA GLY A 265 65.518 72.283 52.493 1.00 83.43 C ANISOU 2081 CA GLY F 265 8380 9797 13523 1086 1098 2205 C ATOM 2082 C GLY A 265 66.797 71.467 52.620 1.00 87.07 C ANISOU 2082 C GLY F 265 9740 9860 13482 955 155 2653 C ATOM 2083 O GLY A 265 67.893 72.001 52.439 1.00 86.51 O ANISOU 2083 O GLY F 265 9490 9550 13831 1140 650 2459 O ATOM 2084 N LEU A 266 66.593 70.190 52.923 1.00 87.12 N ANISOU 2084 N LEU F 266 10153 9542 13408 970 -584 2410 N ATOM 2085 CA LEU A 266 67.665 69.213 53.072 1.00 89.29 C ANISOU 2085 CA LEU F 266 11062 9587 13277 985 -987 2797 C ATOM 2086 C LEU A 266 68.352 69.323 54.427 1.00 94.29 C ANISOU 2086 C LEU F 266 12132 10436 13258 560 -957 2916 C ATOM 2087 O LEU A 266 68.855 70.338 54.901 1.00101.99 O ANISOU 2087 O LEU F 266 13306 11900 13546 462 432 1647 O ATOM 2088 CB LEU A 266 68.666 69.364 51.923 1.00 91.54 C ANISOU 2088 CB LEU F 266 12387 9172 13221 91 -931 3141 C ATOM 2089 CG LEU A 266 68.245 68.802 50.566 1.00 90.13 C ANISOU 2089 CG LEU F 266 12137 8943 13166 180 -1012 3032 C ATOM 2090 CD1 LEU A 266 67.498 67.497 50.748 1.00 80.49 C ANISOU 2090 CD1 LEU F 266 12358 8433 9792 236 -1914 3047 C ATOM 2091 CD2 LEU A 266 67.392 69.798 49.794 1.00 86.96 C ANISOU 2091 CD2 LEU F 266 10986 9425 12628 351 -1463 2828 C ATOM 2092 OXT LEU A 266 67.875 67.838 54.270 1.00 99.16 O ANISOU 2092 OXT LEU F 266 11642 11558 14475 367 -2546 3302 O TER 2093 LEU F 266 END