ATOM 1 N ALA A 2 -9.009 0.366 31.449 1.00 35.86 N ANISOU 1 N ALA A 2 4278 4598 4749 -246 148 -397 N ATOM 2 CA ALA A 2 -8.179 0.887 30.321 1.00 34.44 C ANISOU 2 CA ALA A 2 4140 4407 4539 -226 110 -395 C ATOM 3 C ALA A 2 -7.795 -0.280 29.412 1.00 34.39 C ANISOU 3 C ALA A 2 4165 4380 4521 -257 97 -400 C ATOM 4 O ALA A 2 -7.024 -1.159 29.803 1.00 35.04 O ANISOU 4 O ALA A 2 4279 4442 4592 -274 127 -390 O ATOM 5 CB ALA A 2 -6.949 1.567 30.856 1.00 34.10 C ANISOU 5 CB ALA A 2 4137 4353 4467 -199 131 -380 C ATOM 6 N LYS A 3 -8.340 -0.306 28.207 1.00 33.85 N ANISOU 6 N LYS A 3 4089 4317 4456 -262 52 -415 N ATOM 7 CA LYS A 3 -8.074 -1.418 27.322 1.00 33.72 C ANISOU 7 CA LYS A 3 4101 4281 4430 -295 40 -423 C ATOM 8 C LYS A 3 -7.211 -0.988 26.173 1.00 31.48 C ANISOU 8 C LYS A 3 3869 3982 4111 -275 9 -420 C ATOM 9 O LYS A 3 -7.251 0.177 25.749 1.00 31.45 O ANISOU 9 O LYS A 3 3867 3987 4095 -240 -18 -418 O ATOM 10 CB LYS A 3 -9.368 -2.087 26.815 1.00 35.92 C ANISOU 10 CB LYS A 3 4333 4577 4738 -328 16 -448 C ATOM 11 CG LYS A 3 -10.683 -1.405 27.222 1.00 40.19 C ANISOU 11 CG LYS A 3 4802 5153 5314 -316 3 -461 C ATOM 12 CD LYS A 3 -11.194 -1.913 28.568 1.00 46.48 C ANISOU 12 CD LYS A 3 5563 5954 6143 -339 57 -459 C ATOM 13 CE LYS A 3 -12.411 -1.095 29.077 1.00 45.92 C ANISOU 13 CE LYS A 3 5421 5917 6108 -322 52 -470 C ATOM 14 NZ LYS A 3 -12.991 -1.677 30.338 1.00 48.82 N ANISOU 14 NZ LYS A 3 5753 6286 6509 -349 109 -472 N ATOM 15 N ASN A 4 -6.437 -1.939 25.665 1.00 30.21 N ANISOU 15 N ASN A 4 3752 3793 3931 -298 16 -419 N ATOM 16 CA ASN A 4 -5.622 -1.713 24.495 1.00 28.63 C ANISOU 16 CA ASN A 4 3605 3574 3698 -287 -8 -418 C ATOM 17 C ASN A 4 -4.718 -0.475 24.664 1.00 26.78 C ANISOU 17 C ASN A 4 3397 3335 3443 -246 -1 -403 C ATOM 18 O ASN A 4 -4.651 0.393 23.800 1.00 26.06 O ANISOU 18 O ASN A 4 3327 3243 3333 -221 -30 -405 O ATOM 19 CB ASN A 4 -6.525 -1.594 23.264 1.00 30.04 C ANISOU 19 CB ASN A 4 3773 3766 3874 -290 -63 -438 C ATOM 20 CG ASN A 4 -7.186 -2.905 22.909 1.00 32.71 C ANISOU 20 CG ASN A 4 4095 4103 4228 -337 -69 -458 C ATOM 21 OD1 ASN A 4 -6.585 -3.971 23.040 1.00 35.34 O ANISOU 21 OD1 ASN A 4 4458 4411 4559 -366 -38 -456 O ATOM 22 ND2 ASN A 4 -8.432 -2.840 22.459 1.00 38.02 N ANISOU 22 ND2 ASN A 4 4721 4805 4919 -345 -110 -480 N ATOM 23 N VAL A 5 -4.019 -0.403 25.793 1.00 24.93 N ANISOU 23 N VAL A 5 3165 3097 3211 -239 40 -390 N ATOM 24 CA VAL A 5 -3.212 0.793 26.058 1.00 23.23 C ANISOU 24 CA VAL A 5 2967 2879 2979 -204 50 -381 C ATOM 25 C VAL A 5 -2.013 0.786 25.134 1.00 22.66 C ANISOU 25 C VAL A 5 2953 2778 2878 -201 49 -380 C ATOM 26 O VAL A 5 -1.406 -0.257 24.896 1.00 22.93 O ANISOU 26 O VAL A 5 3013 2794 2906 -222 61 -379 O ATOM 27 CB VAL A 5 -2.790 0.907 27.546 1.00 22.71 C ANISOU 27 CB VAL A 5 2886 2821 2921 -197 91 -371 C ATOM 28 CG1 VAL A 5 -1.865 2.144 27.795 1.00 19.52 C ANISOU 28 CG1 VAL A 5 2502 2414 2501 -166 102 -368 C ATOM 29 CG2 VAL A 5 -4.034 1.007 28.426 1.00 22.95 C ANISOU 29 CG2 VAL A 5 2862 2878 2980 -200 96 -373 C ATOM 30 N GLY A 6 -1.694 1.955 24.585 1.00 21.83 N ANISOU 30 N GLY A 6 2870 2668 2757 -173 37 -380 N ATOM 31 CA GLY A 6 -0.448 2.114 23.885 1.00 21.33 C ANISOU 31 CA GLY A 6 2861 2576 2669 -168 47 -379 C ATOM 32 C GLY A 6 -0.279 3.520 23.355 1.00 21.42 C ANISOU 32 C GLY A 6 2894 2580 2664 -137 39 -380 C ATOM 33 O GLY A 6 -0.713 4.470 23.974 1.00 20.88 O ANISOU 33 O GLY A 6 2800 2527 2606 -116 42 -378 O ATOM 34 N ILE A 7 0.388 3.633 22.217 1.00 20.81 N ANISOU 34 N ILE A 7 2870 2476 2563 -135 34 -382 N ATOM 35 CA ILE A 7 0.722 4.928 21.645 1.00 21.66 C ANISOU 35 CA ILE A 7 3011 2566 2651 -107 36 -381 C ATOM 36 C ILE A 7 -0.451 5.430 20.786 1.00 21.70 C ANISOU 36 C ILE A 7 3018 2580 2646 -86 -9 -380 C ATOM 37 O ILE A 7 -0.890 4.772 19.863 1.00 21.30 O ANISOU 37 O ILE A 7 2982 2528 2583 -97 -41 -384 O ATOM 38 CB ILE A 7 2.071 4.866 20.842 1.00 21.32 C ANISOU 38 CB ILE A 7 3028 2486 2585 -113 59 -384 C ATOM 39 CG1 ILE A 7 3.224 4.488 21.784 1.00 21.56 C ANISOU 39 CG1 ILE A 7 3049 2515 2629 -126 100 -387 C ATOM 40 CG2 ILE A 7 2.350 6.229 20.130 1.00 23.08 C ANISOU 40 CG2 ILE A 7 3296 2686 2787 -85 65 -384 C ATOM 41 CD1 ILE A 7 4.467 3.905 21.069 1.00 20.43 C ANISOU 41 CD1 ILE A 7 2951 2340 2472 -141 122 -392 C ATOM 42 N LEU A 8 -0.977 6.583 21.154 1.00 22.05 N ANISOU 42 N LEU A 8 3045 2636 2696 -56 -11 -376 N ATOM 43 CA LEU A 8 -2.082 7.218 20.456 1.00 22.49 C ANISOU 43 CA LEU A 8 3099 2702 2744 -27 -53 -374 C ATOM 44 C LEU A 8 -1.631 8.144 19.325 1.00 23.92 C ANISOU 44 C LEU A 8 3348 2851 2889 2 -56 -368 C ATOM 45 O LEU A 8 -2.319 8.275 18.285 1.00 24.80 O ANISOU 45 O LEU A 8 3480 2964 2978 22 -98 -367 O ATOM 46 CB LEU A 8 -2.896 8.031 21.462 1.00 20.39 C ANISOU 46 CB LEU A 8 2781 2463 2504 -3 -50 -371 C ATOM 47 CG LEU A 8 -3.747 7.260 22.457 1.00 23.05 C ANISOU 47 CG LEU A 8 3048 2834 2876 -24 -54 -375 C ATOM 48 CD1 LEU A 8 -4.333 8.228 23.425 1.00 18.06 C ANISOU 48 CD1 LEU A 8 2376 2221 2266 2 -41 -372 C ATOM 49 CD2 LEU A 8 -4.875 6.433 21.796 1.00 20.45 C ANISOU 49 CD2 LEU A 8 2690 2527 2553 -36 -103 -383 C ATOM 50 N ALA A 9 -0.495 8.807 19.538 1.00 22.63 N ANISOU 50 N ALA A 9 3221 2660 2719 5 -10 -367 N ATOM 51 CA ALA A 9 -0.055 9.895 18.681 1.00 22.91 C ANISOU 51 CA ALA A 9 3320 2660 2724 34 1 -362 C ATOM 52 C ALA A 9 1.421 10.069 18.906 1.00 23.35 C ANISOU 52 C ALA A 9 3408 2685 2779 16 57 -369 C ATOM 53 O ALA A 9 1.904 9.807 20.019 1.00 22.13 O ANISOU 53 O ALA A 9 3215 2544 2651 -4 84 -376 O ATOM 54 CB ALA A 9 -0.778 11.194 19.058 1.00 22.22 C ANISOU 54 CB ALA A 9 3219 2580 2643 75 0 -354 C ATOM 55 N MET A 10 2.129 10.506 17.863 1.00 23.78 N ANISOU 55 N MET A 10 3533 2699 2803 23 73 -368 N ATOM 56 CA MET A 10 3.559 10.761 17.940 1.00 25.68 C ANISOU 56 CA MET A 10 3806 2908 3044 6 129 -378 C ATOM 57 C MET A 10 3.878 11.954 17.076 1.00 24.88 C ANISOU 57 C MET A 10 3776 2764 2915 32 152 -374 C ATOM 58 O MET A 10 3.237 12.162 16.052 1.00 25.91 O ANISOU 58 O MET A 10 3948 2884 3015 57 121 -362 O ATOM 59 CB MET A 10 4.380 9.615 17.351 1.00 24.69 C ANISOU 59 CB MET A 10 3704 2767 2909 -26 136 -385 C ATOM 60 CG MET A 10 4.355 8.314 18.038 1.00 30.41 C ANISOU 60 CG MET A 10 4377 3520 3656 -54 124 -389 C ATOM 61 SD MET A 10 5.265 7.094 17.034 1.00 29.60 S ANISOU 61 SD MET A 10 4320 3390 3536 -84 134 -395 S ATOM 62 CE MET A 10 6.945 7.535 17.379 1.00 25.19 C ANISOU 62 CE MET A 10 3779 2804 2990 -95 200 -409 C ATOM 63 N ASP A 11 4.859 12.732 17.506 1.00 25.10 N ANISOU 63 N ASP A 11 3816 2768 2952 26 207 -385 N ATOM 64 CA ASP A 11 5.519 13.688 16.624 1.00 25.90 C ANISOU 64 CA ASP A 11 3995 2818 3029 38 247 -385 C ATOM 65 C ASP A 11 7.020 13.700 16.876 1.00 25.34 C ANISOU 65 C ASP A 11 3932 2722 2972 5 307 -407 C ATOM 66 O ASP A 11 7.493 13.172 17.885 1.00 25.29 O ANISOU 66 O ASP A 11 3870 2744 2997 -20 317 -421 O ATOM 67 CB ASP A 11 4.914 15.090 16.751 1.00 25.56 C ANISOU 67 CB ASP A 11 3969 2763 2981 77 255 -376 C ATOM 68 CG ASP A 11 5.028 15.874 15.471 1.00 27.90 C ANISOU 68 CG ASP A 11 4356 3008 3236 104 271 -364 C ATOM 69 OD1 ASP A 11 5.791 15.433 14.580 1.00 29.28 O ANISOU 69 OD1 ASP A 11 4582 3153 3389 86 288 -368 O ATOM 70 OD2 ASP A 11 4.307 16.885 15.320 1.00 29.84 O ANISOU 70 OD2 ASP A 11 4625 3243 3468 146 265 -350 O ATOM 71 N ILE A 12 7.776 14.300 15.956 1.00 26.11 N ANISOU 71 N ILE A 12 4103 2769 3049 6 349 -411 N ATOM 72 CA ILE A 12 9.227 14.163 15.963 1.00 25.18 C ANISOU 72 CA ILE A 12 3996 2627 2945 -28 406 -435 C ATOM 73 C ILE A 12 9.844 15.468 15.561 1.00 26.71 C ANISOU 73 C ILE A 12 4250 2770 3130 -22 466 -443 C ATOM 74 O ILE A 12 9.346 16.138 14.666 1.00 27.00 O ANISOU 74 O ILE A 12 4352 2773 3132 8 464 -426 O ATOM 75 CB ILE A 12 9.722 13.020 14.998 1.00 25.94 C ANISOU 75 CB ILE A 12 4124 2709 3023 -47 400 -434 C ATOM 76 CG1 ILE A 12 11.260 12.915 15.011 1.00 24.12 C ANISOU 76 CG1 ILE A 12 3901 2453 2812 -81 462 -461 C ATOM 77 CG2 ILE A 12 9.160 13.184 13.544 1.00 23.02 C ANISOU 77 CG2 ILE A 12 3837 2305 2605 -22 380 -414 C ATOM 78 CD1 ILE A 12 11.813 11.609 14.326 1.00 25.65 C ANISOU 78 CD1 ILE A 12 4108 2640 2998 -102 458 -463 C ATOM 79 N TYR A 13 10.917 15.840 16.251 1.00 27.25 N ANISOU 79 N TYR A 13 4295 2832 3229 -50 519 -472 N ATOM 80 CA TYR A 13 11.693 16.983 15.848 1.00 27.55 C ANISOU 80 CA TYR A 13 4390 2816 3263 -54 588 -487 C ATOM 81 C TYR A 13 13.169 16.633 15.767 1.00 27.09 C ANISOU 81 C TYR A 13 4328 2739 3225 -95 641 -519 C ATOM 82 O TYR A 13 13.718 16.024 16.682 1.00 26.50 O ANISOU 82 O TYR A 13 4182 2702 3183 -120 637 -539 O ATOM 83 CB TYR A 13 11.474 18.204 16.780 1.00 27.81 C ANISOU 83 CB TYR A 13 4401 2850 3314 -45 612 -497 C ATOM 84 CG TYR A 13 12.288 19.388 16.277 1.00 27.78 C ANISOU 84 CG TYR A 13 4464 2784 3307 -53 690 -514 C ATOM 85 CD1 TYR A 13 11.815 20.166 15.225 1.00 27.70 C ANISOU 85 CD1 TYR A 13 4543 2723 3258 -20 704 -490 C ATOM 86 CD2 TYR A 13 13.548 19.666 16.791 1.00 26.36 C ANISOU 86 CD2 TYR A 13 4260 2594 3159 -94 749 -555 C ATOM 87 CE1 TYR A 13 12.560 21.201 14.713 1.00 28.16 C ANISOU 87 CE1 TYR A 13 4670 2719 3312 -28 781 -504 C ATOM 88 CE2 TYR A 13 14.331 20.723 16.274 1.00 27.80 C ANISOU 88 CE2 TYR A 13 4506 2715 3342 -107 828 -574 C ATOM 89 CZ TYR A 13 13.807 21.479 15.230 1.00 28.81 C ANISOU 89 CZ TYR A 13 4728 2789 3431 -74 845 -547 C ATOM 90 OH TYR A 13 14.507 22.534 14.700 1.00 29.52 O ANISOU 90 OH TYR A 13 4888 2812 3517 -85 927 -563 O ATOM 91 N PHE A 14 13.812 17.043 14.674 1.00 27.37 N ANISOU 91 N PHE A 14 4442 2718 3242 -101 691 -523 N ATOM 92 CA PHE A 14 15.284 17.056 14.604 1.00 27.01 C ANISOU 92 CA PHE A 14 4395 2645 3220 -140 759 -559 C ATOM 93 C PHE A 14 15.780 18.398 14.013 1.00 27.80 C ANISOU 93 C PHE A 14 4570 2679 3312 -143 835 -571 C ATOM 94 O PHE A 14 15.061 19.074 13.255 1.00 27.18 O ANISOU 94 O PHE A 14 4567 2564 3196 -110 835 -544 O ATOM 95 CB PHE A 14 15.828 15.835 13.821 1.00 27.23 C ANISOU 95 CB PHE A 14 4437 2668 3240 -156 753 -558 C ATOM 96 CG PHE A 14 15.217 15.684 12.469 1.00 28.59 C ANISOU 96 CG PHE A 14 4696 2805 3363 -132 736 -527 C ATOM 97 CD1 PHE A 14 15.710 16.422 11.383 1.00 28.77 C ANISOU 97 CD1 PHE A 14 4812 2761 3360 -131 797 -528 C ATOM 98 CD2 PHE A 14 14.124 14.847 12.277 1.00 28.73 C ANISOU 98 CD2 PHE A 14 4705 2855 3355 -109 660 -497 C ATOM 99 CE1 PHE A 14 15.141 16.327 10.130 1.00 28.33 C ANISOU 99 CE1 PHE A 14 4841 2672 3250 -105 780 -500 C ATOM 100 CE2 PHE A 14 13.539 14.736 11.009 1.00 29.17 C ANISOU 100 CE2 PHE A 14 4841 2881 3360 -85 640 -472 C ATOM 101 CZ PHE A 14 14.058 15.472 9.936 1.00 30.32 C ANISOU 101 CZ PHE A 14 5082 2962 3477 -82 698 -472 C ATOM 102 N PRO A 15 16.992 18.817 14.398 1.00 28.36 N ANISOU 102 N PRO A 15 4622 2735 3420 -181 902 -613 N ATOM 103 CA PRO A 15 17.465 20.083 13.868 1.00 29.96 C ANISOU 103 CA PRO A 15 4895 2871 3617 -188 981 -627 C ATOM 104 C PRO A 15 17.601 20.046 12.329 1.00 30.87 C ANISOU 104 C PRO A 15 5116 2924 3691 -178 1012 -607 C ATOM 105 O PRO A 15 18.031 19.022 11.770 1.00 30.92 O ANISOU 105 O PRO A 15 5124 2934 3692 -191 1003 -607 O ATOM 106 CB PRO A 15 18.820 20.286 14.553 1.00 30.07 C ANISOU 106 CB PRO A 15 4854 2888 3682 -237 1041 -682 C ATOM 107 CG PRO A 15 18.950 19.223 15.583 1.00 29.48 C ANISOU 107 CG PRO A 15 4676 2887 3636 -248 986 -693 C ATOM 108 CD PRO A 15 17.948 18.179 15.320 1.00 28.09 C ANISOU 108 CD PRO A 15 4499 2743 3431 -216 907 -650 C ATOM 109 N PRO A 16 17.224 21.149 11.642 1.00 31.47 N ANISOU 109 N PRO A 16 5282 2942 3733 -154 1049 -590 N ATOM 110 CA PRO A 16 17.346 21.167 10.183 1.00 31.70 C ANISOU 110 CA PRO A 16 5419 2909 3716 -141 1080 -570 C ATOM 111 C PRO A 16 18.797 21.170 9.707 1.00 32.89 C ANISOU 111 C PRO A 16 5594 3014 3890 -189 1169 -608 C ATOM 112 O PRO A 16 19.078 20.795 8.581 1.00 33.57 O ANISOU 112 O PRO A 16 5750 3060 3944 -188 1190 -597 O ATOM 113 CB PRO A 16 16.605 22.445 9.775 1.00 32.51 C ANISOU 113 CB PRO A 16 5607 2964 3782 -100 1100 -543 C ATOM 114 CG PRO A 16 16.657 23.335 11.000 1.00 32.13 C ANISOU 114 CG PRO A 16 5501 2931 3777 -113 1124 -569 C ATOM 115 CD PRO A 16 16.637 22.395 12.179 1.00 31.55 C ANISOU 115 CD PRO A 16 5304 2940 3745 -132 1062 -585 C ATOM 116 N THR A 17 19.708 21.578 10.576 1.00 33.82 N ANISOU 116 N THR A 17 5650 3139 4062 -230 1220 -654 N ATOM 117 CA THR A 17 21.123 21.730 10.237 1.00 33.98 C ANISOU 117 CA THR A 17 5682 3116 4113 -278 1312 -698 C ATOM 118 C THR A 17 21.771 20.335 10.246 1.00 34.08 C ANISOU 118 C THR A 17 5633 3169 4148 -301 1285 -712 C ATOM 119 O THR A 17 21.649 19.601 11.232 1.00 32.96 O ANISOU 119 O THR A 17 5393 3098 4034 -303 1224 -719 O ATOM 120 CB THR A 17 21.814 22.700 11.236 1.00 34.39 C ANISOU 120 CB THR A 17 5682 3168 4218 -315 1371 -747 C ATOM 121 OG1 THR A 17 21.329 22.461 12.579 1.00 33.69 O ANISOU 121 OG1 THR A 17 5491 3155 4154 -309 1301 -752 O ATOM 122 CG2 THR A 17 21.463 24.147 10.907 1.00 34.54 C ANISOU 122 CG2 THR A 17 5789 3120 4214 -300 1429 -738 C ATOM 123 N CYS A 18 22.425 19.969 9.142 1.00 33.90 N ANISOU 123 N CYS A 18 5672 3099 4110 -314 1333 -715 N ATOM 124 CA CYS A 18 23.029 18.654 8.995 1.00 34.57 C ANISOU 124 CA CYS A 18 5712 3211 4211 -331 1314 -725 C ATOM 125 C CYS A 18 24.312 18.661 8.160 1.00 34.42 C ANISOU 125 C CYS A 18 5734 3135 4208 -368 1410 -757 C ATOM 126 O CYS A 18 24.660 19.641 7.499 1.00 35.50 O ANISOU 126 O CYS A 18 5952 3202 4333 -379 1491 -766 O ATOM 127 CB CYS A 18 22.021 17.695 8.372 1.00 35.02 C ANISOU 127 CB CYS A 18 5803 3286 4216 -293 1235 -676 C ATOM 128 SG CYS A 18 21.383 18.261 6.754 1.00 39.62 S ANISOU 128 SG CYS A 18 6544 3790 4720 -259 1258 -634 S ATOM 129 N VAL A 19 25.033 17.561 8.225 1.00 33.69 N ANISOU 129 N VAL A 19 5584 3070 4145 -388 1403 -776 N ATOM 130 CA VAL A 19 26.224 17.383 7.426 1.00 32.82 C ANISOU 130 CA VAL A 19 5506 2912 4052 -421 1487 -806 C ATOM 131 C VAL A 19 26.167 15.999 6.772 1.00 32.22 C ANISOU 131 C VAL A 19 5441 2847 3954 -409 1448 -784 C ATOM 132 O VAL A 19 25.882 14.973 7.428 1.00 30.69 O ANISOU 132 O VAL A 19 5171 2718 3773 -397 1372 -775 O ATOM 133 CB VAL A 19 27.509 17.587 8.274 1.00 32.88 C ANISOU 133 CB VAL A 19 5417 2940 4136 -466 1542 -870 C ATOM 134 CG1 VAL A 19 27.605 16.522 9.388 1.00 32.11 C ANISOU 134 CG1 VAL A 19 5195 2930 4076 -463 1466 -880 C ATOM 135 CG2 VAL A 19 28.773 17.603 7.409 1.00 32.80 C ANISOU 135 CG2 VAL A 19 5442 2871 4149 -504 1645 -906 C ATOM 136 N GLN A 20 26.442 15.981 5.473 1.00 32.52 N ANISOU 136 N GLN A 20 5582 2819 3958 -411 1504 -775 N ATOM 137 CA GLN A 20 26.438 14.752 4.709 1.00 32.84 C ANISOU 137 CA GLN A 20 5648 2858 3972 -403 1479 -757 C ATOM 138 C GLN A 20 27.648 13.891 5.057 1.00 32.38 C ANISOU 138 C GLN A 20 5505 2822 3975 -435 1508 -798 C ATOM 139 O GLN A 20 28.760 14.387 5.160 1.00 32.48 O ANISOU 139 O GLN A 20 5494 2812 4036 -469 1590 -843 O ATOM 140 CB GLN A 20 26.311 15.067 3.224 1.00 34.54 C ANISOU 140 CB GLN A 20 6004 2993 4124 -394 1529 -735 C ATOM 141 CG GLN A 20 24.937 15.690 2.874 1.00 37.38 C ANISOU 141 CG GLN A 20 6444 3343 4416 -350 1475 -686 C ATOM 142 CD GLN A 20 23.804 14.662 2.740 1.00 41.28 C ANISOU 142 CD GLN A 20 6936 3883 4866 -315 1366 -646 C ATOM 143 OE1 GLN A 20 24.033 13.457 2.568 1.00 45.43 O ANISOU 143 OE1 GLN A 20 7435 4430 5397 -322 1342 -648 O ATOM 144 NE2 GLN A 20 22.574 15.144 2.810 1.00 45.25 N ANISOU 144 NE2 GLN A 20 7467 4401 5326 -276 1303 -610 N ATOM 145 N GLN A 21 27.410 12.597 5.296 1.00 31.77 N ANISOU 145 N GLN A 21 5378 2793 3899 -421 1440 -784 N ATOM 146 CA GLN A 21 28.472 11.668 5.719 1.00 31.81 C ANISOU 146 CA GLN A 21 5297 2828 3961 -441 1455 -818 C ATOM 147 C GLN A 21 29.566 11.504 4.652 1.00 32.59 C ANISOU 147 C GLN A 21 5450 2865 4069 -467 1550 -842 C ATOM 148 O GLN A 21 30.757 11.432 4.959 1.00 31.81 O ANISOU 148 O GLN A 21 5287 2769 4030 -495 1607 -888 O ATOM 149 CB GLN A 21 27.897 10.282 6.064 1.00 30.42 C ANISOU 149 CB GLN A 21 5075 2706 3775 -418 1366 -790 C ATOM 150 CG GLN A 21 27.146 10.237 7.408 1.00 30.46 C ANISOU 150 CG GLN A 21 4993 2785 3794 -399 1281 -779 C ATOM 151 CD GLN A 21 28.049 10.352 8.617 1.00 29.18 C ANISOU 151 CD GLN A 21 4717 2670 3700 -416 1294 -821 C ATOM 152 OE1 GLN A 21 29.272 10.455 8.491 1.00 29.06 O ANISOU 152 OE1 GLN A 21 4677 2635 3727 -443 1365 -863 O ATOM 153 NE2 GLN A 21 27.455 10.278 9.809 1.00 27.83 N ANISOU 153 NE2 GLN A 21 4472 2562 3539 -401 1223 -813 N ATOM 154 N GLU A 22 29.155 11.418 3.402 1.00 33.94 N ANISOU 154 N GLU A 22 5737 2980 4179 -456 1566 -813 N ATOM 155 CA GLU A 22 30.141 11.402 2.298 1.00 35.84 C ANISOU 155 CA GLU A 22 6046 3151 4421 -481 1667 -835 C ATOM 156 C GLU A 22 31.163 12.561 2.359 1.00 35.87 C ANISOU 156 C GLU A 22 6045 3114 4471 -518 1772 -882 C ATOM 157 O GLU A 22 32.389 12.348 2.224 1.00 35.90 O ANISOU 157 O GLU A 22 6014 3100 4526 -549 1847 -925 O ATOM 158 CB GLU A 22 29.425 11.408 0.960 1.00 37.04 C ANISOU 158 CB GLU A 22 6338 3244 4489 -462 1669 -796 C ATOM 159 CG GLU A 22 30.309 10.858 -0.180 1.00 43.03 C ANISOU 159 CG GLU A 22 7162 3944 5242 -481 1749 -810 C ATOM 160 CD GLU A 22 29.485 10.301 -1.323 1.00 49.36 C ANISOU 160 CD GLU A 22 8078 4716 5960 -456 1714 -768 C ATOM 161 OE1 GLU A 22 29.401 9.042 -1.432 1.00 51.18 O ANISOU 161 OE1 GLU A 22 8287 4972 6187 -449 1671 -760 O ATOM 162 OE2 GLU A 22 28.916 11.127 -2.088 1.00 51.75 O ANISOU 162 OE2 GLU A 22 8491 4970 6201 -441 1730 -744 O ATOM 163 N ALA A 23 30.660 13.776 2.562 1.00 35.86 N ANISOU 163 N ALA A 23 6077 3097 4452 -515 1779 -875 N ATOM 164 CA ALA A 23 31.505 14.978 2.677 1.00 36.71 C ANISOU 164 CA ALA A 23 6183 3164 4601 -551 1878 -919 C ATOM 165 C ALA A 23 32.400 14.925 3.933 1.00 37.33 C ANISOU 165 C ALA A 23 6115 3302 4767 -580 1881 -973 C ATOM 166 O ALA A 23 33.590 15.272 3.888 1.00 37.13 O ANISOU 166 O ALA A 23 6061 3251 4797 -620 1973 -1026 O ATOM 167 CB ALA A 23 30.637 16.239 2.680 1.00 36.83 C ANISOU 167 CB ALA A 23 6267 3152 4575 -535 1875 -894 C ATOM 168 N LEU A 24 31.820 14.475 5.052 1.00 37.17 N ANISOU 168 N LEU A 24 6004 3363 4758 -558 1782 -961 N ATOM 169 CA LEU A 24 32.576 14.251 6.280 1.00 37.21 C ANISOU 169 CA LEU A 24 5869 3434 4836 -576 1767 -1007 C ATOM 170 C LEU A 24 33.703 13.224 6.135 1.00 37.49 C ANISOU 170 C LEU A 24 5845 3480 4918 -591 1798 -1038 C ATOM 171 O LEU A 24 34.801 13.453 6.637 1.00 37.08 O ANISOU 171 O LEU A 24 5712 3444 4934 -622 1848 -1095 O ATOM 172 CB LEU A 24 31.639 13.867 7.419 1.00 36.95 C ANISOU 172 CB LEU A 24 5764 3480 4795 -544 1653 -980 C ATOM 173 CG LEU A 24 32.159 13.905 8.856 1.00 37.37 C ANISOU 173 CG LEU A 24 5681 3606 4910 -556 1625 -1021 C ATOM 174 CD1 LEU A 24 32.755 15.274 9.279 1.00 37.34 C ANISOU 174 CD1 LEU A 24 5656 3585 4946 -593 1695 -1072 C ATOM 175 CD2 LEU A 24 31.000 13.524 9.765 1.00 35.74 C ANISOU 175 CD2 LEU A 24 5437 3465 4678 -519 1514 -981 C ATOM 176 N GLU A 25 33.430 12.100 5.470 1.00 37.77 N ANISOU 176 N GLU A 25 5921 3510 4921 -568 1767 -1004 N ATOM 177 CA GLU A 25 34.492 11.147 5.084 1.00 39.36 C ANISOU 177 CA GLU A 25 6090 3705 5160 -580 1810 -1031 C ATOM 178 C GLU A 25 35.655 11.887 4.396 1.00 40.82 C ANISOU 178 C GLU A 25 6305 3824 5381 -623 1938 -1080 C ATOM 179 O GLU A 25 36.815 11.735 4.785 1.00 40.78 O ANISOU 179 O GLU A 25 6211 3838 5445 -648 1982 -1133 O ATOM 180 CB GLU A 25 33.959 10.063 4.124 1.00 39.39 C ANISOU 180 CB GLU A 25 6174 3685 5109 -554 1781 -985 C ATOM 181 CG GLU A 25 33.077 8.958 4.748 1.00 37.73 C ANISOU 181 CG GLU A 25 5919 3540 4877 -517 1666 -945 C ATOM 182 CD GLU A 25 32.452 8.055 3.689 1.00 39.36 C ANISOU 182 CD GLU A 25 6219 3714 5022 -497 1644 -903 C ATOM 183 OE1 GLU A 25 32.697 8.284 2.485 1.00 39.38 O ANISOU 183 OE1 GLU A 25 6322 3646 4996 -510 1714 -903 O ATOM 184 OE2 GLU A 25 31.720 7.108 4.035 1.00 37.96 O ANISOU 184 OE2 GLU A 25 6019 3579 4825 -471 1560 -871 O ATOM 185 N ALA A 26 35.329 12.686 3.381 1.00 41.67 N ANISOU 185 N ALA A 26 6538 3855 5439 -631 1996 -1063 N ATOM 186 CA ALA A 26 36.364 13.384 2.610 1.00 43.57 C ANISOU 186 CA ALA A 26 6826 4023 5707 -673 2126 -1105 C ATOM 187 C ALA A 26 37.103 14.382 3.495 1.00 44.09 C ANISOU 187 C ALA A 26 6804 4106 5842 -711 2173 -1164 C ATOM 188 O ALA A 26 38.319 14.358 3.545 1.00 44.47 O ANISOU 188 O ALA A 26 6790 4150 5957 -747 2245 -1222 O ATOM 189 CB ALA A 26 35.777 14.056 1.359 1.00 43.57 C ANISOU 189 CB ALA A 26 6989 3936 5632 -669 2175 -1069 C ATOM 190 N HIS A 27 36.363 15.199 4.245 1.00 44.88 N ANISOU 190 N HIS A 27 6892 4231 5928 -703 2126 -1153 N ATOM 191 CA HIS A 27 36.942 16.128 5.223 1.00 45.97 C ANISOU 191 CA HIS A 27 6943 4396 6129 -738 2156 -1210 C ATOM 192 C HIS A 27 37.911 15.466 6.203 1.00 46.64 C ANISOU 192 C HIS A 27 6873 4555 6291 -751 2135 -1262 C ATOM 193 O HIS A 27 38.965 16.037 6.526 1.00 47.03 O ANISOU 193 O HIS A 27 6857 4603 6407 -795 2206 -1329 O ATOM 194 CB HIS A 27 35.830 16.827 6.019 1.00 45.36 C ANISOU 194 CB HIS A 27 6866 4350 6019 -716 2083 -1181 C ATOM 195 CG HIS A 27 36.326 17.649 7.171 1.00 44.87 C ANISOU 195 CG HIS A 27 6704 4326 6017 -748 2096 -1237 C ATOM 196 ND1 HIS A 27 36.717 17.091 8.370 1.00 44.29 N ANISOU 196 ND1 HIS A 27 6491 4343 5995 -747 2033 -1268 N ATOM 197 CD2 HIS A 27 36.482 18.989 7.314 1.00 45.68 C ANISOU 197 CD2 HIS A 27 6830 4391 6135 -782 2164 -1269 C ATOM 198 CE1 HIS A 27 37.099 18.049 9.198 1.00 44.50 C ANISOU 198 CE1 HIS A 27 6457 4387 6065 -780 2059 -1319 C ATOM 199 NE2 HIS A 27 36.954 19.209 8.586 1.00 43.39 N ANISOU 199 NE2 HIS A 27 6412 4169 5904 -803 2139 -1321 N ATOM 200 N ASP A 28 37.517 14.302 6.712 1.00 46.80 N ANISOU 200 N ASP A 28 6836 4643 6303 -712 2034 -1232 N ATOM 201 CA ASP A 28 38.357 13.493 7.595 1.00 48.00 C ANISOU 201 CA ASP A 28 6850 4869 6519 -711 2002 -1271 C ATOM 202 C ASP A 28 39.342 12.778 6.679 1.00 48.92 C ANISOU 202 C ASP A 28 6977 4947 6663 -724 2075 -1292 C ATOM 203 O ASP A 28 39.260 12.892 5.446 1.00 49.92 O ANISOU 203 O ASP A 28 7220 4995 6752 -732 2140 -1272 O ATOM 204 CB ASP A 28 37.515 12.456 8.379 1.00 47.14 C ANISOU 204 CB ASP A 28 6692 4835 6383 -661 1875 -1225 C ATOM 205 CG ASP A 28 36.493 13.087 9.334 1.00 47.07 C ANISOU 205 CG ASP A 28 6668 4868 6348 -646 1800 -1203 C ATOM 206 OD1 ASP A 28 36.614 14.270 9.710 1.00 46.54 O ANISOU 206 OD1 ASP A 28 6593 4792 6300 -674 1836 -1235 O ATOM 207 OD2 ASP A 28 35.561 12.364 9.742 1.00 45.20 O ANISOU 207 OD2 ASP A 28 6426 4674 6075 -605 1704 -1154 O ATOM 208 N GLY A 29 40.285 12.033 7.227 1.00 49.43 N ANISOU 208 N GLY A 29 6928 5065 6790 -724 2067 -1331 N ATOM 209 CA GLY A 29 41.225 11.376 6.305 1.00 51.34 C ANISOU 209 CA GLY A 29 7183 5264 7058 -735 2144 -1351 C ATOM 210 C GLY A 29 40.741 10.027 5.796 1.00 51.38 C ANISOU 210 C GLY A 29 7231 5270 7020 -692 2091 -1296 C ATOM 211 O GLY A 29 41.558 9.180 5.505 1.00 51.80 O ANISOU 211 O GLY A 29 7249 5323 7109 -689 2121 -1315 O ATOM 212 N ALA A 30 39.417 9.846 5.674 1.00 51.74 N ANISOU 212 N ALA A 30 7354 5314 6991 -660 2016 -1230 N ATOM 213 CA ALA A 30 38.763 8.514 5.597 1.00 51.19 C ANISOU 213 CA ALA A 30 7298 5270 6882 -615 1935 -1178 C ATOM 214 C ALA A 30 38.494 7.954 4.193 1.00 51.85 C ANISOU 214 C ALA A 30 7506 5282 6913 -610 1971 -1142 C ATOM 215 O ALA A 30 38.047 8.670 3.285 1.00 52.19 O ANISOU 215 O ALA A 30 7665 5259 6906 -623 2015 -1124 O ATOM 216 CB ALA A 30 37.464 8.504 6.426 1.00 50.16 C ANISOU 216 CB ALA A 30 7160 5191 6706 -583 1822 -1131 C ATOM 217 N SER A 31 38.755 6.659 4.038 1.00 52.27 N ANISOU 217 N SER A 31 7538 5350 6974 -587 1951 -1131 N ATOM 218 CA SER A 31 38.556 5.970 2.766 1.00 52.96 C ANISOU 218 CA SER A 31 7735 5376 7013 -581 1982 -1101 C ATOM 219 C SER A 31 37.066 5.981 2.432 1.00 52.24 C ANISOU 219 C SER A 31 7741 5274 6835 -559 1909 -1040 C ATOM 220 O SER A 31 36.227 5.922 3.340 1.00 51.76 O ANISOU 220 O SER A 31 7636 5271 6760 -536 1816 -1014 O ATOM 221 CB SER A 31 39.096 4.543 2.856 1.00 53.24 C ANISOU 221 CB SER A 31 7715 5437 7079 -558 1966 -1103 C ATOM 222 OG SER A 31 38.785 3.969 4.126 1.00 54.68 O ANISOU 222 OG SER A 31 7794 5702 7280 -527 1868 -1092 O ATOM 223 N LYS A 32 36.739 6.107 1.145 1.00 51.81 N ANISOU 223 N LYS A 32 7818 5147 6722 -565 1953 -1018 N ATOM 224 CA LYS A 32 35.348 6.298 0.715 1.00 51.21 C ANISOU 224 CA LYS A 32 7841 5057 6561 -546 1892 -964 C ATOM 225 C LYS A 32 34.443 5.191 1.255 1.00 49.12 C ANISOU 225 C LYS A 32 7542 4850 6272 -511 1780 -925 C ATOM 226 O LYS A 32 34.808 4.010 1.244 1.00 48.22 O ANISOU 226 O LYS A 32 7396 4750 6177 -501 1771 -926 O ATOM 227 CB LYS A 32 35.234 6.393 -0.819 1.00 51.97 C ANISOU 227 CB LYS A 32 8084 5067 6594 -554 1955 -948 C ATOM 228 CG LYS A 32 33.824 6.810 -1.324 1.00 53.41 C ANISOU 228 CG LYS A 32 8374 5234 6686 -533 1896 -897 C ATOM 229 CD LYS A 32 33.663 6.654 -2.845 1.00 53.71 C ANISOU 229 CD LYS A 32 8559 5195 6654 -533 1943 -877 C ATOM 230 CE LYS A 32 33.937 7.978 -3.553 1.00 58.89 C ANISOU 230 CE LYS A 32 9307 5781 7289 -553 2035 -888 C ATOM 231 NZ LYS A 32 33.860 7.874 -5.056 1.00 62.61 N ANISOU 231 NZ LYS A 32 9929 6173 7689 -553 2089 -871 N ATOM 232 N GLY A 33 33.285 5.594 1.771 1.00 47.44 N ANISOU 232 N GLY A 33 7333 4671 6023 -493 1699 -893 N ATOM 233 CA GLY A 33 32.296 4.646 2.270 1.00 45.07 C ANISOU 233 CA GLY A 33 7007 4422 5696 -463 1594 -855 C ATOM 234 C GLY A 33 32.541 4.150 3.680 1.00 43.43 C ANISOU 234 C GLY A 33 6665 4291 5545 -451 1541 -867 C ATOM 235 O GLY A 33 31.754 3.361 4.199 1.00 42.72 O ANISOU 235 O GLY A 33 6549 4244 5439 -427 1459 -837 O ATOM 236 N LYS A 34 33.614 4.618 4.314 1.00 42.39 N ANISOU 236 N LYS A 34 6450 4176 5480 -467 1588 -912 N ATOM 237 CA LYS A 34 33.849 4.304 5.720 1.00 41.17 C ANISOU 237 CA LYS A 34 6169 4098 5376 -453 1536 -925 C ATOM 238 C LYS A 34 32.636 4.631 6.614 1.00 39.55 C ANISOU 238 C LYS A 34 5943 3943 5142 -434 1444 -894 C ATOM 239 O LYS A 34 32.343 3.904 7.574 1.00 38.53 O ANISOU 239 O LYS A 34 5742 3872 5025 -411 1375 -880 O ATOM 240 CB LYS A 34 35.057 5.045 6.247 1.00 41.66 C ANISOU 240 CB LYS A 34 6150 4171 5506 -476 1597 -982 C ATOM 241 CG LYS A 34 35.613 4.410 7.492 1.00 43.05 C ANISOU 241 CG LYS A 34 6198 4422 5738 -458 1554 -1001 C ATOM 242 CD LYS A 34 36.090 5.450 8.482 1.00 44.10 C ANISOU 242 CD LYS A 34 6246 4595 5917 -475 1561 -1044 C ATOM 243 CE LYS A 34 37.104 4.865 9.448 1.00 47.22 C ANISOU 243 CE LYS A 34 6514 5050 6376 -462 1549 -1081 C ATOM 244 NZ LYS A 34 36.756 3.458 9.823 1.00 49.76 N ANISOU 244 NZ LYS A 34 6812 5410 6686 -420 1480 -1044 N ATOM 245 N TYR A 35 31.942 5.719 6.281 1.00 37.84 N ANISOU 245 N TYR A 35 5792 3700 4888 -443 1448 -881 N ATOM 246 CA TYR A 35 30.807 6.177 7.069 1.00 35.55 C ANISOU 246 CA TYR A 35 5484 3450 4572 -427 1371 -854 C ATOM 247 C TYR A 35 29.499 5.714 6.422 1.00 34.94 C ANISOU 247 C TYR A 35 5491 3359 4426 -406 1314 -803 C ATOM 248 O TYR A 35 28.585 5.228 7.115 1.00 33.94 O ANISOU 248 O TYR A 35 5330 3281 4284 -385 1231 -775 O ATOM 249 CB TYR A 35 30.813 7.723 7.280 1.00 33.93 C ANISOU 249 CB TYR A 35 5287 3231 4372 -445 1406 -874 C ATOM 250 CG TYR A 35 32.050 8.293 7.968 1.00 33.04 C ANISOU 250 CG TYR A 35 5089 3135 4329 -470 1461 -931 C ATOM 251 CD1 TYR A 35 32.396 9.654 7.827 1.00 32.76 C ANISOU 251 CD1 TYR A 35 5077 3065 4306 -498 1527 -960 C ATOM 252 CD2 TYR A 35 32.880 7.489 8.746 1.00 31.87 C ANISOU 252 CD2 TYR A 35 4837 3038 4235 -465 1449 -957 C ATOM 253 CE1 TYR A 35 33.533 10.175 8.434 1.00 32.55 C ANISOU 253 CE1 TYR A 35 4968 3054 4344 -526 1579 -1018 C ATOM 254 CE2 TYR A 35 34.011 7.998 9.367 1.00 32.98 C ANISOU 254 CE2 TYR A 35 4894 3199 4439 -488 1494 -1013 C ATOM 255 CZ TYR A 35 34.343 9.340 9.201 1.00 34.34 C ANISOU 255 CZ TYR A 35 5087 3337 4624 -521 1560 -1046 C ATOM 256 OH TYR A 35 35.483 9.816 9.810 1.00 33.74 O ANISOU 256 OH TYR A 35 4923 3283 4614 -548 1605 -1107 O ATOM 257 N THR A 36 29.398 5.873 5.108 1.00 33.94 N ANISOU 257 N THR A 36 5473 3169 4256 -414 1356 -793 N ATOM 258 CA THR A 36 28.126 5.613 4.425 1.00 34.21 C ANISOU 258 CA THR A 36 5590 3188 4219 -396 1301 -749 C ATOM 259 C THR A 36 27.819 4.128 4.291 1.00 34.06 C ANISOU 259 C THR A 36 5566 3187 4188 -383 1254 -730 C ATOM 260 O THR A 36 26.649 3.753 4.201 1.00 33.91 O ANISOU 260 O THR A 36 5575 3184 4124 -367 1184 -696 O ATOM 261 CB THR A 36 28.057 6.261 3.028 1.00 34.26 C ANISOU 261 CB THR A 36 5723 3120 4174 -404 1358 -742 C ATOM 262 OG1 THR A 36 29.187 5.851 2.263 1.00 34.77 O ANISOU 262 OG1 THR A 36 5815 3139 4257 -424 1439 -768 O ATOM 263 CG2 THR A 36 28.045 7.783 3.135 1.00 34.84 C ANISOU 263 CG2 THR A 36 5818 3173 4247 -411 1394 -752 C ATOM 264 N ILE A 37 28.877 3.310 4.276 1.00 34.32 N ANISOU 264 N ILE A 37 5563 3215 4262 -392 1296 -753 N ATOM 265 CA ILE A 37 28.782 1.855 4.154 1.00 34.54 C ANISOU 265 CA ILE A 37 5585 3253 4285 -381 1266 -739 C ATOM 266 C ILE A 37 29.158 1.207 5.467 1.00 34.03 C ANISOU 266 C ILE A 37 5404 3250 4276 -368 1233 -748 C ATOM 267 O ILE A 37 28.366 0.416 6.008 1.00 34.57 O ANISOU 267 O ILE A 37 5446 3356 4332 -351 1162 -722 O ATOM 268 CB ILE A 37 29.713 1.241 3.030 1.00 34.95 C ANISOU 268 CB ILE A 37 5694 3246 4338 -395 1343 -756 C ATOM 269 CG1 ILE A 37 29.517 1.892 1.643 1.00 37.49 C ANISOU 269 CG1 ILE A 37 6142 3500 4604 -408 1390 -750 C ATOM 270 CG2 ILE A 37 29.594 -0.332 2.975 1.00 35.06 C ANISOU 270 CG2 ILE A 37 5700 3270 4350 -383 1311 -741 C ATOM 271 CD1 ILE A 37 28.096 1.886 1.091 1.00 41.87 C ANISOU 271 CD1 ILE A 37 6776 4050 5082 -395 1323 -712 C ATOM 272 N GLY A 38 30.347 1.533 5.978 1.00 32.96 N ANISOU 272 N GLY A 38 5198 3125 4199 -376 1283 -785 N ATOM 273 CA GLY A 38 30.858 0.918 7.206 1.00 32.56 C ANISOU 273 CA GLY A 38 5037 3134 4202 -360 1255 -797 C ATOM 274 C GLY A 38 29.992 1.209 8.433 1.00 32.03 C ANISOU 274 C GLY A 38 4911 3128 4131 -344 1176 -779 C ATOM 275 O GLY A 38 29.862 0.359 9.332 1.00 31.49 O ANISOU 275 O GLY A 38 4779 3106 4078 -322 1126 -767 O ATOM 276 N LEU A 39 29.421 2.419 8.478 1.00 31.00 N ANISOU 276 N LEU A 39 4803 2994 3980 -354 1169 -777 N ATOM 277 CA LEU A 39 28.445 2.783 9.515 1.00 30.25 C ANISOU 277 CA LEU A 39 4668 2952 3875 -340 1097 -757 C ATOM 278 C LEU A 39 27.050 2.631 8.981 1.00 29.43 C ANISOU 278 C LEU A 39 4636 2836 3712 -332 1046 -716 C ATOM 279 O LEU A 39 26.108 2.449 9.743 1.00 28.92 O ANISOU 279 O LEU A 39 4541 2813 3635 -317 978 -693 O ATOM 280 CB LEU A 39 28.654 4.245 10.001 1.00 30.47 C ANISOU 280 CB LEU A 39 4669 2987 3921 -354 1120 -783 C ATOM 281 CG LEU A 39 29.896 4.565 10.841 1.00 31.53 C ANISOU 281 CG LEU A 39 4712 3152 4118 -363 1155 -829 C ATOM 282 CD1 LEU A 39 29.870 6.045 11.294 1.00 30.75 C ANISOU 282 CD1 LEU A 39 4598 3057 4029 -380 1173 -852 C ATOM 283 CD2 LEU A 39 30.012 3.635 12.069 1.00 33.96 C ANISOU 283 CD2 LEU A 39 4924 3526 4452 -338 1099 -826 C ATOM 284 N GLY A 40 26.910 2.680 7.656 1.00 29.43 N ANISOU 284 N GLY A 40 4732 2777 3672 -342 1078 -708 N ATOM 285 CA GLY A 40 25.592 2.657 7.048 1.00 28.71 C ANISOU 285 CA GLY A 40 4714 2674 3521 -334 1030 -673 C ATOM 286 C GLY A 40 24.828 3.962 7.216 1.00 28.39 C ANISOU 286 C GLY A 40 4691 2638 3458 -330 1010 -664 C ATOM 287 O GLY A 40 23.611 3.980 7.066 1.00 27.68 O ANISOU 287 O GLY A 40 4634 2558 3327 -317 953 -635 O ATOM 288 N GLN A 41 25.542 5.062 7.469 1.00 28.67 N ANISOU 288 N GLN A 41 4708 2664 3521 -342 1062 -691 N ATOM 289 CA GLN A 41 24.914 6.378 7.738 1.00 28.74 C ANISOU 289 CA GLN A 41 4730 2675 3515 -338 1052 -686 C ATOM 290 C GLN A 41 25.028 7.360 6.589 1.00 29.31 C ANISOU 290 C GLN A 41 4901 2681 3554 -346 1111 -688 C ATOM 291 O GLN A 41 26.098 7.490 6.014 1.00 30.59 O ANISOU 291 O GLN A 41 5088 2801 3735 -367 1188 -715 O ATOM 292 CB GLN A 41 25.551 7.001 8.983 1.00 28.13 C ANISOU 292 CB GLN A 41 4559 2636 3493 -345 1065 -716 C ATOM 293 CG GLN A 41 25.238 6.225 10.255 1.00 26.46 C ANISOU 293 CG GLN A 41 4255 2494 3305 -330 998 -708 C ATOM 294 CD GLN A 41 23.755 6.184 10.530 1.00 26.34 C ANISOU 294 CD GLN A 41 4251 2506 3252 -309 922 -670 C ATOM 295 OE1 GLN A 41 23.179 5.115 10.707 1.00 22.72 O ANISOU 295 OE1 GLN A 41 3778 2072 2783 -297 870 -648 O ATOM 296 NE2 GLN A 41 23.127 7.352 10.560 1.00 23.80 N ANISOU 296 NE2 GLN A 41 3955 2176 2911 -305 917 -663 N ATOM 297 N ASP A 42 23.957 8.078 6.270 1.00 29.17 N ANISOU 297 N ASP A 42 4941 2652 3489 -330 1080 -661 N ATOM 298 CA ASP A 42 23.998 9.003 5.133 1.00 30.35 C ANISOU 298 CA ASP A 42 5197 2735 3598 -332 1135 -658 C ATOM 299 C ASP A 42 24.209 10.463 5.513 1.00 31.36 C ANISOU 299 C ASP A 42 5324 2848 3743 -337 1179 -674 C ATOM 300 O ASP A 42 25.000 11.160 4.875 1.00 31.33 O ANISOU 300 O ASP A 42 5375 2788 3742 -356 1263 -694 O ATOM 301 CB ASP A 42 22.739 8.872 4.279 1.00 30.26 C ANISOU 301 CB ASP A 42 5270 2712 3516 -305 1079 -618 C ATOM 302 CG ASP A 42 22.638 7.505 3.603 1.00 33.62 C ANISOU 302 CG ASP A 42 5720 3135 3918 -306 1054 -608 C ATOM 303 OD1 ASP A 42 23.642 7.079 2.955 1.00 36.56 O ANISOU 303 OD1 ASP A 42 6122 3468 4300 -326 1118 -627 O ATOM 304 OD2 ASP A 42 21.577 6.842 3.748 1.00 34.27 O ANISOU 304 OD2 ASP A 42 5791 3255 3976 -289 973 -584 O ATOM 305 N CYS A 43 23.470 10.912 6.526 1.00 31.32 N ANISOU 305 N CYS A 43 5263 2889 3747 -322 1125 -664 N ATOM 306 CA CYS A 43 23.467 12.301 6.955 1.00 32.17 C ANISOU 306 CA CYS A 43 5371 2985 3865 -324 1157 -675 C ATOM 307 C CYS A 43 23.429 12.391 8.498 1.00 31.39 C ANISOU 307 C CYS A 43 5159 2953 3816 -327 1119 -691 C ATOM 308 O CYS A 43 22.958 11.458 9.168 1.00 30.97 O ANISOU 308 O CYS A 43 5043 2956 3770 -315 1050 -678 O ATOM 309 CB CYS A 43 22.284 13.023 6.307 1.00 31.83 C ANISOU 309 CB CYS A 43 5417 2916 3760 -293 1129 -637 C ATOM 310 SG CYS A 43 22.430 14.805 6.344 1.00 35.62 S ANISOU 310 SG CYS A 43 5943 3349 4241 -295 1197 -649 S ATOM 311 N LEU A 44 23.949 13.489 9.045 1.00 31.60 N ANISOU 311 N LEU A 44 5162 2971 3874 -344 1169 -720 N ATOM 312 CA LEU A 44 24.022 13.745 10.504 1.00 30.85 C ANISOU 312 CA LEU A 44 4963 2934 3823 -349 1143 -742 C ATOM 313 C LEU A 44 23.415 15.105 10.860 1.00 30.57 C ANISOU 313 C LEU A 44 4950 2888 3778 -341 1150 -738 C ATOM 314 O LEU A 44 24.007 16.139 10.520 1.00 30.61 O ANISOU 314 O LEU A 44 4997 2843 3792 -360 1227 -762 O ATOM 315 CB LEU A 44 25.494 13.716 10.960 1.00 31.28 C ANISOU 315 CB LEU A 44 4951 2995 3938 -385 1203 -795 C ATOM 316 CG LEU A 44 25.911 13.722 12.439 1.00 30.86 C ANISOU 316 CG LEU A 44 4782 3008 3936 -395 1180 -828 C ATOM 317 CD1 LEU A 44 27.352 13.322 12.501 1.00 32.38 C ANISOU 317 CD1 LEU A 44 4921 3203 4178 -424 1231 -875 C ATOM 318 CD2 LEU A 44 25.742 15.079 13.142 1.00 31.12 C ANISOU 318 CD2 LEU A 44 4802 3042 3980 -404 1199 -847 C ATOM 319 N ALA A 45 22.259 15.095 11.537 1.00 29.04 N ANISOU 319 N ALA A 45 4728 2738 3568 -312 1075 -709 N ATOM 320 CA ALA A 45 21.608 16.302 12.068 1.00 29.95 C ANISOU 320 CA ALA A 45 4850 2852 3677 -300 1074 -705 C ATOM 321 C ALA A 45 22.243 16.705 13.389 1.00 29.93 C ANISOU 321 C ALA A 45 4755 2889 3728 -324 1088 -747 C ATOM 322 O ALA A 45 22.567 15.851 14.219 1.00 30.23 O ANISOU 322 O ALA A 45 4708 2984 3795 -331 1052 -760 O ATOM 323 CB ALA A 45 20.133 16.084 12.269 1.00 29.54 C ANISOU 323 CB ALA A 45 4800 2833 3591 -260 990 -660 C ATOM 324 N PHE A 46 22.436 18.004 13.595 1.00 29.54 N ANISOU 324 N PHE A 46 4725 2810 3689 -337 1142 -769 N ATOM 325 CA PHE A 46 23.113 18.462 14.794 1.00 28.87 C ANISOU 325 CA PHE A 46 4556 2760 3654 -364 1161 -816 C ATOM 326 C PHE A 46 22.539 19.795 15.262 1.00 29.12 C ANISOU 326 C PHE A 46 4608 2777 3681 -358 1178 -817 C ATOM 327 O PHE A 46 22.100 20.616 14.447 1.00 28.65 O ANISOU 327 O PHE A 46 4639 2657 3588 -344 1212 -796 O ATOM 328 CB PHE A 46 24.616 18.577 14.542 1.00 29.01 C ANISOU 328 CB PHE A 46 4560 2751 3712 -408 1242 -869 C ATOM 329 CG PHE A 46 24.964 19.535 13.419 1.00 31.58 C ANISOU 329 CG PHE A 46 4984 2990 4023 -423 1331 -875 C ATOM 330 CD1 PHE A 46 25.109 20.899 13.659 1.00 30.21 C ANISOU 330 CD1 PHE A 46 4834 2782 3862 -441 1391 -901 C ATOM 331 CD2 PHE A 46 25.157 19.061 12.116 1.00 30.53 C ANISOU 331 CD2 PHE A 46 4928 2808 3863 -420 1358 -856 C ATOM 332 CE1 PHE A 46 25.407 21.777 12.628 1.00 30.29 C ANISOU 332 CE1 PHE A 46 4943 2708 3858 -453 1478 -905 C ATOM 333 CE2 PHE A 46 25.456 19.946 11.095 1.00 32.59 C ANISOU 333 CE2 PHE A 46 5287 2987 4107 -431 1443 -860 C ATOM 334 CZ PHE A 46 25.573 21.297 11.352 1.00 30.59 C ANISOU 334 CZ PHE A 46 5057 2698 3866 -447 1503 -883 C ATOM 335 N CYS A 47 22.497 19.971 16.581 1.00 29.36 N ANISOU 335 N CYS A 47 4557 2861 3739 -364 1150 -839 N ATOM 336 CA CYS A 47 22.077 21.228 17.171 1.00 29.79 C ANISOU 336 CA CYS A 47 4619 2904 3794 -363 1170 -849 C ATOM 337 C CYS A 47 23.172 22.250 16.996 1.00 30.19 C ANISOU 337 C CYS A 47 4690 2906 3876 -407 1268 -901 C ATOM 338 O CYS A 47 24.346 22.003 17.329 1.00 29.62 O ANISOU 338 O CYS A 47 4557 2851 3845 -445 1298 -952 O ATOM 339 CB CYS A 47 21.773 21.088 18.661 1.00 29.67 C ANISOU 339 CB CYS A 47 4511 2963 3800 -360 1115 -862 C ATOM 340 SG CYS A 47 20.267 20.201 18.980 1.00 31.12 S ANISOU 340 SG CYS A 47 4679 3197 3949 -310 1011 -801 S ATOM 341 N THR A 48 22.780 23.395 16.447 1.00 30.60 N ANISOU 341 N THR A 48 4827 2893 3906 -399 1318 -890 N ATOM 342 CA THR A 48 23.626 24.563 16.551 1.00 31.18 C ANISOU 342 CA THR A 48 4915 2921 4010 -441 1411 -942 C ATOM 343 C THR A 48 23.410 25.164 17.944 1.00 32.09 C ANISOU 343 C THR A 48 4962 3082 4149 -449 1392 -970 C ATOM 344 O THR A 48 22.721 24.593 18.803 1.00 29.85 O ANISOU 344 O THR A 48 4618 2865 3860 -424 1311 -950 O ATOM 345 CB THR A 48 23.285 25.589 15.486 1.00 31.43 C ANISOU 345 CB THR A 48 5070 2863 4008 -427 1477 -918 C ATOM 346 OG1 THR A 48 21.909 25.934 15.605 1.00 30.12 O ANISOU 346 OG1 THR A 48 4940 2702 3804 -375 1425 -867 O ATOM 347 CG2 THR A 48 23.559 25.043 14.090 1.00 31.92 C ANISOU 347 CG2 THR A 48 5207 2878 4044 -421 1502 -894 C ATOM 348 N GLU A 49 24.034 26.323 18.159 1.00 33.36 N ANISOU 348 N GLU A 49 5135 3204 4337 -487 1473 -1018 N ATOM 349 CA GLU A 49 24.075 26.949 19.452 1.00 33.55 C ANISOU 349 CA GLU A 49 5093 3265 4388 -506 1470 -1058 C ATOM 350 C GLU A 49 22.666 27.354 19.875 1.00 32.73 C ANISOU 350 C GLU A 49 5014 3170 4250 -458 1420 -1011 C ATOM 351 O GLU A 49 22.401 27.499 21.048 1.00 32.71 O ANISOU 351 O GLU A 49 4949 3220 4261 -460 1386 -1028 O ATOM 352 CB GLU A 49 25.036 28.162 19.410 1.00 34.15 C ANISOU 352 CB GLU A 49 5192 3284 4499 -561 1578 -1122 C ATOM 353 CG GLU A 49 25.391 28.738 20.767 1.00 35.62 C ANISOU 353 CG GLU A 49 5298 3514 4721 -595 1582 -1181 C ATOM 354 CD GLU A 49 26.026 30.143 20.688 1.00 35.92 C ANISOU 354 CD GLU A 49 5378 3484 4786 -644 1693 -1236 C ATOM 355 OE1 GLU A 49 26.069 30.722 19.577 1.00 37.88 O ANISOU 355 OE1 GLU A 49 5727 3647 5021 -645 1767 -1220 O ATOM 356 OE2 GLU A 49 26.500 30.644 21.745 1.00 35.56 O ANISOU 356 OE2 GLU A 49 5266 3471 4775 -683 1706 -1297 O ATOM 357 N LEU A 50 21.772 27.476 18.896 1.00 32.42 N ANISOU 357 N LEU A 50 5067 3085 4168 -414 1415 -952 N ATOM 358 CA LEU A 50 20.381 27.867 19.109 1.00 32.32 C ANISOU 358 CA LEU A 50 5084 3074 4121 -362 1370 -903 C ATOM 359 C LEU A 50 19.429 26.739 19.534 1.00 31.84 C ANISOU 359 C LEU A 50 4970 3086 4042 -322 1261 -860 C ATOM 360 O LEU A 50 18.274 27.031 19.837 1.00 31.04 O ANISOU 360 O LEU A 50 4880 2996 3919 -281 1222 -824 O ATOM 361 CB LEU A 50 19.806 28.503 17.830 1.00 32.71 C ANISOU 361 CB LEU A 50 5257 3043 4128 -326 1407 -858 C ATOM 362 CG LEU A 50 20.394 29.830 17.332 1.00 34.81 C ANISOU 362 CG LEU A 50 5605 3221 4401 -351 1519 -886 C ATOM 363 CD1 LEU A 50 19.513 30.483 16.252 1.00 35.39 C ANISOU 363 CD1 LEU A 50 5801 3222 4422 -298 1539 -829 C ATOM 364 CD2 LEU A 50 20.586 30.756 18.470 1.00 33.56 C ANISOU 364 CD2 LEU A 50 5404 3071 4277 -381 1554 -933 C ATOM 365 N GLU A 51 19.907 25.481 19.553 1.00 31.13 N ANISOU 365 N GLU A 51 4823 3044 3962 -333 1219 -863 N ATOM 366 CA GLU A 51 19.050 24.308 19.824 1.00 30.56 C ANISOU 366 CA GLU A 51 4707 3033 3871 -298 1123 -821 C ATOM 367 C GLU A 51 19.643 23.374 20.868 1.00 29.98 C ANISOU 367 C GLU A 51 4530 3034 3828 -321 1082 -851 C ATOM 368 O GLU A 51 20.857 23.211 20.957 1.00 29.94 O ANISOU 368 O GLU A 51 4490 3032 3853 -361 1118 -897 O ATOM 369 CB GLU A 51 18.776 23.546 18.519 1.00 30.41 C ANISOU 369 CB GLU A 51 4748 2988 3819 -274 1103 -778 C ATOM 370 CG GLU A 51 17.982 24.391 17.541 1.00 30.79 C ANISOU 370 CG GLU A 51 4900 2972 3828 -238 1126 -740 C ATOM 371 CD GLU A 51 17.365 23.602 16.419 1.00 33.31 C ANISOU 371 CD GLU A 51 5271 3280 4105 -204 1082 -691 C ATOM 372 OE1 GLU A 51 16.142 23.324 16.463 1.00 33.39 O ANISOU 372 OE1 GLU A 51 5280 3318 4088 -160 1013 -649 O ATOM 373 OE2 GLU A 51 18.098 23.273 15.473 1.00 34.34 O ANISOU 373 OE2 GLU A 51 5445 3375 4229 -220 1118 -696 O ATOM 374 N ASP A 52 18.780 22.812 21.705 1.00 29.61 N ANISOU 374 N ASP A 52 4431 3046 3773 -295 1009 -827 N ATOM 375 CA ASP A 52 19.215 21.870 22.737 1.00 29.09 C ANISOU 375 CA ASP A 52 4272 3052 3728 -308 964 -848 C ATOM 376 C ASP A 52 18.052 20.944 23.054 1.00 27.18 C ANISOU 376 C ASP A 52 4007 2855 3464 -270 882 -799 C ATOM 377 O ASP A 52 16.991 21.079 22.471 1.00 26.26 O ANISOU 377 O ASP A 52 3940 2717 3320 -237 862 -755 O ATOM 378 CB ASP A 52 19.729 22.606 23.991 1.00 29.92 C ANISOU 378 CB ASP A 52 4322 3186 3862 -336 986 -900 C ATOM 379 CG ASP A 52 18.669 23.459 24.669 1.00 31.06 C ANISOU 379 CG ASP A 52 4475 3332 3994 -315 975 -886 C ATOM 380 OD1 ASP A 52 17.445 23.234 24.492 1.00 32.35 O ANISOU 380 OD1 ASP A 52 4662 3499 4131 -274 931 -835 O ATOM 381 OD2 ASP A 52 19.081 24.372 25.419 1.00 37.11 O ANISOU 381 OD2 ASP A 52 5221 4098 4779 -340 1013 -931 O ATOM 382 N VAL A 53 18.255 20.014 23.976 1.00 27.53 N ANISOU 382 N VAL A 53 3976 2963 3520 -273 836 -807 N ATOM 383 CA VAL A 53 17.231 19.033 24.311 1.00 26.72 C ANISOU 383 CA VAL A 53 3849 2902 3399 -242 765 -764 C ATOM 384 C VAL A 53 15.903 19.666 24.767 1.00 27.54 C ANISOU 384 C VAL A 53 3964 3012 3489 -213 742 -737 C ATOM 385 O VAL A 53 14.826 19.185 24.384 1.00 28.34 O ANISOU 385 O VAL A 53 4083 3116 3568 -183 698 -693 O ATOM 386 CB VAL A 53 17.747 17.979 25.299 1.00 25.76 C ANISOU 386 CB VAL A 53 3650 2845 3293 -250 727 -779 C ATOM 387 CG1 VAL A 53 18.756 17.048 24.585 1.00 25.37 C ANISOU 387 CG1 VAL A 53 3598 2789 3253 -264 736 -787 C ATOM 388 CG2 VAL A 53 18.408 18.611 26.464 1.00 27.45 C ANISOU 388 CG2 VAL A 53 3812 3089 3528 -271 746 -827 C ATOM 389 N ILE A 54 15.988 20.766 25.523 1.00 26.97 N ANISOU 389 N ILE A 54 3882 2938 3428 -224 773 -767 N ATOM 390 CA ILE A 54 14.826 21.491 26.003 1.00 26.69 C ANISOU 390 CA ILE A 54 3856 2903 3381 -197 762 -747 C ATOM 391 C ILE A 54 14.088 22.075 24.826 1.00 26.70 C ANISOU 391 C ILE A 54 3935 2847 3361 -170 776 -712 C ATOM 392 O ILE A 54 12.895 21.854 24.692 1.00 26.52 O ANISOU 392 O ILE A 54 3922 2835 3321 -135 733 -671 O ATOM 393 CB ILE A 54 15.205 22.658 27.011 1.00 27.53 C ANISOU 393 CB ILE A 54 3944 3012 3506 -219 804 -792 C ATOM 394 CG1 ILE A 54 16.100 22.157 28.160 1.00 28.13 C ANISOU 394 CG1 ILE A 54 3943 3144 3600 -247 792 -834 C ATOM 395 CG2 ILE A 54 13.961 23.359 27.538 1.00 26.70 C ANISOU 395 CG2 ILE A 54 3847 2907 3389 -189 793 -770 C ATOM 396 CD1 ILE A 54 15.577 20.881 28.870 1.00 31.93 C ANISOU 396 CD1 ILE A 54 4371 3689 4073 -227 721 -807 C ATOM 397 N SER A 55 14.789 22.814 23.959 1.00 26.81 N ANISOU 397 N SER A 55 4008 2803 3376 -186 837 -729 N ATOM 398 CA SER A 55 14.112 23.448 22.828 1.00 26.32 C ANISOU 398 CA SER A 55 4030 2683 3288 -155 854 -695 C ATOM 399 C SER A 55 13.482 22.418 21.869 1.00 27.10 C ANISOU 399 C SER A 55 4151 2786 3361 -128 801 -650 C ATOM 400 O SER A 55 12.328 22.584 21.432 1.00 27.29 O ANISOU 400 O SER A 55 4209 2801 3360 -86 770 -610 O ATOM 401 CB SER A 55 15.057 24.424 22.105 1.00 27.42 C ANISOU 401 CB SER A 55 4232 2754 3432 -180 937 -724 C ATOM 402 OG SER A 55 15.962 23.783 21.213 1.00 24.59 O ANISOU 402 OG SER A 55 3893 2376 3073 -202 955 -731 O ATOM 403 N MET A 56 14.236 21.367 21.535 1.00 25.89 N ANISOU 403 N MET A 56 3979 2646 3211 -150 790 -657 N ATOM 404 CA MET A 56 13.710 20.285 20.699 1.00 26.71 C ANISOU 404 CA MET A 56 4099 2757 3292 -130 740 -619 C ATOM 405 C MET A 56 12.482 19.605 21.299 1.00 25.73 C ANISOU 405 C MET A 56 3929 2685 3161 -102 667 -589 C ATOM 406 O MET A 56 11.563 19.255 20.572 1.00 25.84 O ANISOU 406 O MET A 56 3972 2695 3151 -73 628 -553 O ATOM 407 CB MET A 56 14.788 19.237 20.437 1.00 25.71 C ANISOU 407 CB MET A 56 3952 2640 3177 -160 745 -637 C ATOM 408 CG MET A 56 15.955 19.730 19.562 1.00 26.92 C ANISOU 408 CG MET A 56 4158 2737 3335 -186 817 -663 C ATOM 409 SD MET A 56 16.895 18.275 19.048 1.00 28.07 S ANISOU 409 SD MET A 56 4284 2895 3488 -209 808 -670 S ATOM 410 CE MET A 56 17.737 17.816 20.547 1.00 25.48 C ANISOU 410 CE MET A 56 3851 2630 3202 -236 799 -712 C ATOM 411 N SER A 57 12.476 19.417 22.623 1.00 26.61 N ANISOU 411 N SER A 57 3969 2847 3295 -112 651 -605 N ATOM 412 CA SER A 57 11.299 18.864 23.325 1.00 26.15 C ANISOU 412 CA SER A 57 3866 2837 3235 -89 591 -579 C ATOM 413 C SER A 57 10.121 19.793 23.193 1.00 27.39 C ANISOU 413 C SER A 57 4051 2977 3378 -53 584 -556 C ATOM 414 O SER A 57 8.992 19.333 22.930 1.00 27.50 O ANISOU 414 O SER A 57 4062 3008 3379 -24 535 -522 O ATOM 415 CB SER A 57 11.594 18.676 24.796 1.00 26.80 C ANISOU 415 CB SER A 57 3876 2969 3340 -106 585 -604 C ATOM 416 OG SER A 57 12.671 17.778 24.975 1.00 28.32 O ANISOU 416 OG SER A 57 4035 3181 3543 -134 586 -624 O ATOM 417 N PHE A 58 10.353 21.100 23.405 1.00 27.60 N ANISOU 417 N PHE A 58 4104 2972 3411 -53 635 -574 N ATOM 418 CA PHE A 58 9.297 22.107 23.163 1.00 28.59 C ANISOU 418 CA PHE A 58 4269 3072 3523 -13 637 -551 C ATOM 419 C PHE A 58 8.650 21.954 21.778 1.00 27.95 C ANISOU 419 C PHE A 58 4249 2962 3410 21 613 -514 C ATOM 420 O PHE A 58 7.435 21.943 21.679 1.00 28.31 O ANISOU 420 O PHE A 58 4291 3022 3444 59 569 -484 O ATOM 421 CB PHE A 58 9.794 23.564 23.316 1.00 28.87 C ANISOU 421 CB PHE A 58 4344 3061 3565 -20 708 -577 C ATOM 422 CG PHE A 58 10.077 24.002 24.731 1.00 30.47 C ANISOU 422 CG PHE A 58 4491 3292 3794 -43 728 -612 C ATOM 423 CD1 PHE A 58 9.494 23.376 25.820 1.00 30.68 C ANISOU 423 CD1 PHE A 58 4448 3379 3831 -39 682 -608 C ATOM 424 CD2 PHE A 58 10.918 25.097 24.964 1.00 32.42 C ANISOU 424 CD2 PHE A 58 4762 3502 4053 -69 798 -650 C ATOM 425 CE1 PHE A 58 9.745 23.816 27.134 1.00 33.07 C ANISOU 425 CE1 PHE A 58 4707 3708 4152 -58 701 -640 C ATOM 426 CE2 PHE A 58 11.181 25.563 26.283 1.00 33.59 C ANISOU 426 CE2 PHE A 58 4862 3677 4223 -91 817 -687 C ATOM 427 CZ PHE A 58 10.580 24.917 27.369 1.00 32.75 C ANISOU 427 CZ PHE A 58 4688 3634 4123 -84 766 -681 C ATOM 428 N ASN A 59 9.465 21.897 20.716 1.00 28.18 N ANISOU 428 N ASN A 59 4336 2948 3425 7 643 -518 N ATOM 429 CA ASN A 59 8.945 21.749 19.346 1.00 27.83 C ANISOU 429 CA ASN A 59 4357 2873 3343 39 621 -484 C ATOM 430 C ASN A 59 8.049 20.501 19.173 1.00 27.41 C ANISOU 430 C ASN A 59 4266 2866 3280 53 542 -458 C ATOM 431 O ASN A 59 6.917 20.571 18.644 1.00 26.32 O ANISOU 431 O ASN A 59 4149 2732 3120 95 499 -427 O ATOM 432 CB ASN A 59 10.096 21.667 18.306 1.00 28.58 C ANISOU 432 CB ASN A 59 4514 2919 3426 14 667 -497 C ATOM 433 CG ASN A 59 11.070 22.833 18.380 1.00 29.96 C ANISOU 433 CG ASN A 59 4727 3043 3614 -9 752 -527 C ATOM 434 OD1 ASN A 59 10.670 23.977 18.575 1.00 30.12 O ANISOU 434 OD1 ASN A 59 4775 3037 3632 13 780 -525 O ATOM 435 ND2 ASN A 59 12.359 22.543 18.211 1.00 31.06 N ANISOU 435 ND2 ASN A 59 4867 3168 3768 -52 796 -559 N ATOM 436 N ALA A 60 8.601 19.350 19.566 1.00 26.53 N ANISOU 436 N ALA A 60 4105 2791 3186 19 525 -471 N ATOM 437 CA ALA A 60 7.923 18.062 19.424 1.00 26.17 C ANISOU 437 CA ALA A 60 4024 2785 3134 23 460 -452 C ATOM 438 C ALA A 60 6.609 18.005 20.195 1.00 26.10 C ANISOU 438 C ALA A 60 3963 2821 3135 49 412 -436 C ATOM 439 O ALA A 60 5.655 17.464 19.686 1.00 27.26 O ANISOU 439 O ALA A 60 4108 2983 3266 70 361 -413 O ATOM 440 CB ALA A 60 8.849 16.940 19.883 1.00 25.53 C ANISOU 440 CB ALA A 60 3898 2729 3072 -17 462 -472 C ATOM 441 N VAL A 61 6.563 18.556 21.419 1.00 26.40 N ANISOU 441 N VAL A 61 3955 2878 3197 45 430 -450 N ATOM 442 CA VAL A 61 5.387 18.447 22.306 1.00 25.40 C ANISOU 442 CA VAL A 61 3771 2797 3084 64 391 -438 C ATOM 443 C VAL A 61 4.308 19.427 21.862 1.00 26.82 C ANISOU 443 C VAL A 61 3982 2958 3250 112 381 -417 C ATOM 444 O VAL A 61 3.135 19.092 21.770 1.00 26.98 O ANISOU 444 O VAL A 61 3978 3005 3268 138 331 -396 O ATOM 445 CB VAL A 61 5.749 18.753 23.775 1.00 26.03 C ANISOU 445 CB VAL A 61 3798 2902 3192 44 418 -462 C ATOM 446 CG1 VAL A 61 4.492 19.030 24.619 1.00 24.87 C ANISOU 446 CG1 VAL A 61 3607 2786 3056 71 393 -450 C ATOM 447 CG2 VAL A 61 6.508 17.602 24.373 1.00 22.22 C ANISOU 447 CG2 VAL A 61 3270 2450 2721 8 411 -478 C ATOM 448 N THR A 62 4.724 20.654 21.571 1.00 27.41 N ANISOU 448 N THR A 62 4112 2985 3316 124 431 -423 N ATOM 449 CA THR A 62 3.824 21.668 21.099 1.00 28.50 C ANISOU 449 CA THR A 62 4291 3099 3439 174 428 -401 C ATOM 450 C THR A 62 3.256 21.253 19.734 1.00 28.45 C ANISOU 450 C THR A 62 4329 3083 3398 204 383 -373 C ATOM 451 O THR A 62 2.068 21.431 19.471 1.00 28.77 O ANISOU 451 O THR A 62 4366 3137 3429 248 340 -350 O ATOM 452 CB THR A 62 4.590 22.986 21.026 1.00 29.85 C ANISOU 452 CB THR A 62 4520 3213 3607 173 501 -416 C ATOM 453 OG1 THR A 62 4.753 23.483 22.373 1.00 30.11 O ANISOU 453 OG1 THR A 62 4506 3264 3670 155 531 -440 O ATOM 454 CG2 THR A 62 3.840 23.975 20.219 1.00 32.55 C ANISOU 454 CG2 THR A 62 4927 3517 3923 228 503 -389 C ATOM 455 N SER A 63 4.091 20.683 18.871 1.00 26.82 N ANISOU 455 N SER A 63 4163 2853 3173 180 391 -377 N ATOM 456 CA SER A 63 3.581 20.192 17.577 1.00 27.92 C ANISOU 456 CA SER A 63 4346 2986 3276 205 346 -354 C ATOM 457 C SER A 63 2.580 19.044 17.798 1.00 27.39 C ANISOU 457 C SER A 63 4211 2978 3217 206 272 -344 C ATOM 458 O SER A 63 1.506 19.003 17.190 1.00 28.74 O ANISOU 458 O SER A 63 4388 3162 3368 245 221 -324 O ATOM 459 CB SER A 63 4.738 19.768 16.648 1.00 27.48 C ANISOU 459 CB SER A 63 4349 2892 3199 175 375 -362 C ATOM 460 OG SER A 63 4.223 19.190 15.460 1.00 29.71 O ANISOU 460 OG SER A 63 4670 3172 3444 196 327 -342 O ATOM 461 N LEU A 64 2.907 18.116 18.694 1.00 27.14 N ANISOU 461 N LEU A 64 4113 2983 3216 165 268 -361 N ATOM 462 CA LEU A 64 1.983 17.036 18.957 1.00 26.70 C ANISOU 462 CA LEU A 64 3995 2979 3171 162 208 -354 C ATOM 463 C LEU A 64 0.643 17.582 19.457 1.00 27.31 C ANISOU 463 C LEU A 64 4032 3084 3261 201 178 -342 C ATOM 464 O LEU A 64 -0.417 17.271 18.879 1.00 27.15 O ANISOU 464 O LEU A 64 4002 3085 3229 228 122 -327 O ATOM 465 CB LEU A 64 2.573 15.993 19.933 1.00 26.46 C ANISOU 465 CB LEU A 64 3905 2980 3170 114 215 -372 C ATOM 466 CG LEU A 64 1.741 14.707 20.158 1.00 24.89 C ANISOU 466 CG LEU A 64 3647 2828 2983 102 161 -366 C ATOM 467 CD1 LEU A 64 2.597 13.621 20.728 1.00 23.15 C ANISOU 467 CD1 LEU A 64 3397 2622 2778 58 175 -380 C ATOM 468 CD2 LEU A 64 0.574 14.931 21.087 1.00 28.21 C ANISOU 468 CD2 LEU A 64 4005 3287 3427 121 139 -361 C ATOM 469 N LEU A 65 0.699 18.383 20.528 1.00 27.91 N ANISOU 469 N LEU A 65 4081 3162 3361 204 214 -350 N ATOM 470 CA LEU A 65 -0.498 18.947 21.172 1.00 29.76 C ANISOU 470 CA LEU A 65 4273 3422 3613 239 196 -341 C ATOM 471 C LEU A 65 -1.395 19.634 20.153 1.00 30.63 C ANISOU 471 C LEU A 65 4424 3516 3696 297 165 -319 C ATOM 472 O LEU A 65 -2.614 19.468 20.108 1.00 31.13 O ANISOU 472 O LEU A 65 4449 3613 3766 327 115 -307 O ATOM 473 CB LEU A 65 -0.073 19.978 22.248 1.00 29.38 C ANISOU 473 CB LEU A 65 4217 3360 3585 236 253 -355 C ATOM 474 CG LEU A 65 0.068 19.518 23.701 1.00 30.60 C ANISOU 474 CG LEU A 65 4301 3552 3772 202 266 -373 C ATOM 475 CD1 LEU A 65 0.550 18.106 23.799 1.00 31.96 C ANISOU 475 CD1 LEU A 65 4445 3751 3949 159 246 -381 C ATOM 476 CD2 LEU A 65 0.929 20.452 24.577 1.00 29.59 C ANISOU 476 CD2 LEU A 65 4184 3404 3656 186 329 -395 C ATOM 477 N GLU A 66 -0.729 20.399 19.316 1.00 32.17 N ANISOU 477 N GLU A 66 4703 3659 3863 311 199 -314 N ATOM 478 CA GLU A 66 -1.327 21.249 18.333 1.00 34.06 C ANISOU 478 CA GLU A 66 5002 3870 4069 370 184 -291 C ATOM 479 C GLU A 66 -2.004 20.448 17.201 1.00 34.29 C ANISOU 479 C GLU A 66 5041 3919 4069 389 114 -276 C ATOM 480 O GLU A 66 -3.206 20.585 16.958 1.00 35.31 O ANISOU 480 O GLU A 66 5147 4074 4193 435 62 -262 O ATOM 481 CB GLU A 66 -0.163 22.037 17.777 1.00 34.04 C ANISOU 481 CB GLU A 66 5089 3803 4044 364 249 -294 C ATOM 482 CG GLU A 66 -0.393 23.427 17.658 1.00 38.52 C ANISOU 482 CG GLU A 66 5707 4330 4600 411 283 -282 C ATOM 483 CD GLU A 66 -1.265 23.696 16.507 1.00 41.54 C ANISOU 483 CD GLU A 66 6138 4702 4941 474 237 -253 C ATOM 484 OE1 GLU A 66 -2.353 24.251 16.773 1.00 42.77 O ANISOU 484 OE1 GLU A 66 6268 4877 5106 524 211 -238 O ATOM 485 OE2 GLU A 66 -0.865 23.305 15.376 1.00 42.16 O ANISOU 485 OE2 GLU A 66 6277 4759 4982 472 225 -245 O ATOM 486 N LYS A 67 -1.228 19.597 16.525 1.00 34.49 N ANISOU 486 N LYS A 67 5097 3934 4075 353 112 -283 N ATOM 487 CA LYS A 67 -1.712 18.894 15.325 1.00 34.09 C ANISOU 487 CA LYS A 67 5072 3893 3988 368 51 -272 C ATOM 488 C LYS A 67 -2.705 17.781 15.607 1.00 33.87 C ANISOU 488 C LYS A 67 4960 3928 3982 356 -15 -277 C ATOM 489 O LYS A 67 -3.518 17.435 14.743 1.00 33.79 O ANISOU 489 O LYS A 67 4956 3937 3946 383 -77 -269 O ATOM 490 CB LYS A 67 -0.536 18.403 14.486 1.00 34.42 C ANISOU 490 CB LYS A 67 5180 3897 4002 333 78 -278 C ATOM 491 CG LYS A 67 0.383 19.558 14.090 1.00 34.78 C ANISOU 491 CG LYS A 67 5314 3876 4025 346 148 -274 C ATOM 492 CD LYS A 67 1.262 19.227 12.951 1.00 37.43 C ANISOU 492 CD LYS A 67 5729 4170 4321 329 166 -274 C ATOM 493 CE LYS A 67 2.006 20.470 12.509 1.00 39.35 C ANISOU 493 CE LYS A 67 6063 4345 4542 347 236 -269 C ATOM 494 NZ LYS A 67 3.343 20.519 13.147 1.00 40.75 N ANISOU 494 NZ LYS A 67 6234 4498 4750 292 310 -295 N ATOM 495 N TYR A 68 -2.643 17.208 16.807 1.00 33.09 N ANISOU 495 N TYR A 68 4784 3860 3927 316 -3 -293 N ATOM 496 CA TYR A 68 -3.614 16.180 17.172 1.00 32.94 C ANISOU 496 CA TYR A 68 4685 3898 3932 302 -57 -299 C ATOM 497 C TYR A 68 -4.771 16.799 17.952 1.00 34.00 C ANISOU 497 C TYR A 68 4758 4064 4096 338 -73 -294 C ATOM 498 O TYR A 68 -5.738 16.120 18.284 1.00 34.80 O ANISOU 498 O TYR A 68 4787 4212 4222 333 -116 -300 O ATOM 499 CB TYR A 68 -2.976 15.033 17.957 1.00 30.95 C ANISOU 499 CB TYR A 68 4388 3662 3708 239 -39 -316 C ATOM 500 CG TYR A 68 -1.972 14.180 17.187 1.00 30.27 C ANISOU 500 CG TYR A 68 4350 3554 3599 202 -31 -322 C ATOM 501 CD1 TYR A 68 -0.617 14.492 17.204 1.00 26.65 C ANISOU 501 CD1 TYR A 68 3939 3053 3132 182 28 -328 C ATOM 502 CD2 TYR A 68 -2.383 13.048 16.451 1.00 28.47 C ANISOU 502 CD2 TYR A 68 4115 3344 3357 186 -80 -326 C ATOM 503 CE1 TYR A 68 0.317 13.707 16.497 1.00 26.15 C ANISOU 503 CE1 TYR A 68 3918 2968 3050 149 39 -334 C ATOM 504 CE2 TYR A 68 -1.450 12.248 15.739 1.00 28.68 C ANISOU 504 CE2 TYR A 68 4189 3347 3362 152 -69 -332 C ATOM 505 CZ TYR A 68 -0.098 12.586 15.785 1.00 27.68 C ANISOU 505 CZ TYR A 68 4108 3178 3229 135 -9 -335 C ATOM 506 OH TYR A 68 0.857 11.837 15.130 1.00 27.65 O ANISOU 506 OH TYR A 68 4148 3150 3208 104 8 -342 O ATOM 507 N LYS A 69 -4.667 18.096 18.239 1.00 35.01 N ANISOU 507 N LYS A 69 4915 4164 4225 373 -35 -286 N ATOM 508 CA LYS A 69 -5.744 18.830 18.895 1.00 35.48 C ANISOU 508 CA LYS A 69 4925 4247 4309 415 -44 -280 C ATOM 509 C LYS A 69 -5.977 18.293 20.302 1.00 34.36 C ANISOU 509 C LYS A 69 4697 4143 4217 378 -31 -295 C ATOM 510 O LYS A 69 -7.114 17.958 20.690 1.00 33.95 O ANISOU 510 O LYS A 69 4574 4136 4191 389 -68 -297 O ATOM 511 CB LYS A 69 -7.025 18.797 18.035 1.00 36.69 C ANISOU 511 CB LYS A 69 5064 4428 4447 466 -117 -268 C ATOM 512 CG LYS A 69 -7.103 19.943 17.044 1.00 40.18 C ANISOU 512 CG LYS A 69 5588 4831 4846 532 -120 -246 C ATOM 513 CD LYS A 69 -6.546 19.620 15.695 1.00 45.21 C ANISOU 513 CD LYS A 69 6305 5440 5431 531 -138 -239 C ATOM 514 CE LYS A 69 -7.663 19.316 14.671 1.00 49.89 C ANISOU 514 CE LYS A 69 6892 6068 5997 575 -224 -231 C ATOM 515 NZ LYS A 69 -8.538 20.485 14.325 1.00 50.28 N ANISOU 515 NZ LYS A 69 6961 6112 6030 660 -245 -210 N ATOM 516 N ILE A 70 -4.888 18.225 21.067 1.00 32.43 N ANISOU 516 N ILE A 70 4458 3881 3982 335 25 -307 N ATOM 517 CA ILE A 70 -4.966 17.706 22.415 1.00 31.75 C ANISOU 517 CA ILE A 70 4302 3828 3936 299 42 -321 C ATOM 518 C ILE A 70 -5.021 18.873 23.385 1.00 32.67 C ANISOU 518 C ILE A 70 4411 3934 4071 320 88 -323 C ATOM 519 O ILE A 70 -4.171 19.768 23.336 1.00 32.86 O ANISOU 519 O ILE A 70 4490 3916 4080 324 134 -325 O ATOM 520 CB ILE A 70 -3.753 16.825 22.793 1.00 30.29 C ANISOU 520 CB ILE A 70 4121 3637 3751 240 70 -335 C ATOM 521 CG1 ILE A 70 -3.567 15.672 21.794 1.00 29.01 C ANISOU 521 CG1 ILE A 70 3975 3478 3569 217 32 -334 C ATOM 522 CG2 ILE A 70 -3.915 16.326 24.228 1.00 29.81 C ANISOU 522 CG2 ILE A 70 3990 3610 3726 211 87 -346 C ATOM 523 CD1 ILE A 70 -4.792 14.779 21.651 1.00 25.19 C ANISOU 523 CD1 ILE A 70 3435 3038 3100 218 -25 -333 C ATOM 524 N ASP A 71 -6.023 18.856 24.251 1.00 32.65 N ANISOU 524 N ASP A 71 4339 3966 4099 330 78 -324 N ATOM 525 CA ASP A 71 -6.121 19.803 25.341 1.00 33.74 C ANISOU 525 CA ASP A 71 4462 4100 4259 343 123 -329 C ATOM 526 C ASP A 71 -4.988 19.504 26.345 1.00 32.88 C ANISOU 526 C ASP A 71 4350 3987 4157 290 171 -348 C ATOM 527 O ASP A 71 -4.952 18.413 26.916 1.00 32.88 O ANISOU 527 O ASP A 71 4305 4018 4171 252 161 -356 O ATOM 528 CB ASP A 71 -7.499 19.596 26.003 1.00 35.18 C ANISOU 528 CB ASP A 71 4565 4327 4476 360 98 -329 C ATOM 529 CG ASP A 71 -7.846 20.673 27.026 1.00 38.55 C ANISOU 529 CG ASP A 71 4975 4748 4924 385 141 -332 C ATOM 530 OD1 ASP A 71 -7.004 21.577 27.267 1.00 38.66 O ANISOU 530 OD1 ASP A 71 5038 4724 4926 385 191 -336 O ATOM 531 OD2 ASP A 71 -8.976 20.590 27.593 1.00 40.81 O ANISOU 531 OD2 ASP A 71 5197 5069 5242 401 127 -332 O ATOM 532 N PRO A 72 -4.079 20.474 26.581 1.00 32.64 N ANISOU 532 N PRO A 72 4366 3918 4116 289 223 -356 N ATOM 533 CA PRO A 72 -3.005 20.295 27.570 1.00 32.16 C ANISOU 533 CA PRO A 72 4299 3858 4061 243 265 -378 C ATOM 534 C PRO A 72 -3.507 20.005 28.988 1.00 31.94 C ANISOU 534 C PRO A 72 4206 3869 4061 229 275 -387 C ATOM 535 O PRO A 72 -2.781 19.413 29.767 1.00 30.82 O ANISOU 535 O PRO A 72 4047 3741 3922 190 291 -402 O ATOM 536 CB PRO A 72 -2.255 21.634 27.559 1.00 32.59 C ANISOU 536 CB PRO A 72 4411 3867 4106 254 319 -387 C ATOM 537 CG PRO A 72 -2.695 22.337 26.313 1.00 33.96 C ANISOU 537 CG PRO A 72 4637 4007 4260 301 305 -367 C ATOM 538 CD PRO A 72 -4.053 21.819 25.962 1.00 33.07 C ANISOU 538 CD PRO A 72 4482 3929 4154 333 246 -348 C ATOM 539 N LYS A 73 -4.736 20.405 29.312 1.00 32.48 N ANISOU 539 N LYS A 73 4239 3954 4149 264 265 -378 N ATOM 540 CA LYS A 73 -5.366 20.066 30.597 1.00 33.80 C ANISOU 540 CA LYS A 73 4342 4157 4342 252 273 -385 C ATOM 541 C LYS A 73 -5.642 18.559 30.717 1.00 32.68 C ANISOU 541 C LYS A 73 4155 4052 4210 220 239 -383 C ATOM 542 O LYS A 73 -5.857 18.025 31.811 1.00 32.81 O ANISOU 542 O LYS A 73 4127 4095 4242 198 252 -390 O ATOM 543 CB LYS A 73 -6.680 20.858 30.764 1.00 34.11 C ANISOU 543 CB LYS A 73 4354 4203 4403 300 270 -376 C ATOM 544 CG LYS A 73 -6.454 22.341 30.908 1.00 35.21 C ANISOU 544 CG LYS A 73 4536 4306 4537 330 314 -380 C ATOM 545 CD LYS A 73 -7.769 23.154 30.881 1.00 39.25 C ANISOU 545 CD LYS A 73 5025 4820 5068 387 309 -367 C ATOM 546 CE LYS A 73 -8.010 23.786 29.498 1.00 44.50 C ANISOU 546 CE LYS A 73 5739 5456 5714 437 283 -348 C ATOM 547 NZ LYS A 73 -9.300 24.561 29.443 1.00 49.53 N ANISOU 547 NZ LYS A 73 6352 6098 6371 500 273 -334 N ATOM 548 N GLN A 74 -5.645 17.884 29.573 1.00 32.83 N ANISOU 548 N GLN A 74 4188 4070 4216 218 198 -373 N ATOM 549 CA GLN A 74 -5.909 16.450 29.508 1.00 32.81 C ANISOU 549 CA GLN A 74 4149 4096 4221 187 166 -372 C ATOM 550 C GLN A 74 -4.657 15.546 29.617 1.00 31.46 C ANISOU 550 C GLN A 74 4000 3920 4035 142 177 -379 C ATOM 551 O GLN A 74 -4.711 14.348 29.344 1.00 31.48 O ANISOU 551 O GLN A 74 3986 3937 4037 117 152 -377 O ATOM 552 CB GLN A 74 -6.758 16.145 28.270 1.00 33.91 C ANISOU 552 CB GLN A 74 4284 4242 4359 209 112 -361 C ATOM 553 CG GLN A 74 -8.234 16.533 28.490 1.00 38.75 C ANISOU 553 CG GLN A 74 4843 4880 4999 245 94 -357 C ATOM 554 CD GLN A 74 -8.884 15.738 29.664 1.00 44.39 C ANISOU 554 CD GLN A 74 5487 5630 5747 217 104 -365 C ATOM 555 OE1 GLN A 74 -8.883 14.510 29.666 1.00 48.42 O ANISOU 555 OE1 GLN A 74 5977 6158 6263 180 89 -369 O ATOM 556 NE2 GLN A 74 -9.416 16.446 30.646 1.00 45.26 N ANISOU 556 NE2 GLN A 74 5568 5748 5879 235 135 -368 N ATOM 557 N ILE A 75 -3.546 16.119 30.059 1.00 29.94 N ANISOU 557 N ILE A 75 3840 3708 3830 132 216 -390 N ATOM 558 CA ILE A 75 -2.344 15.352 30.296 1.00 28.76 C ANISOU 558 CA ILE A 75 3704 3557 3668 95 228 -399 C ATOM 559 C ILE A 75 -2.254 15.138 31.797 1.00 27.57 C ANISOU 559 C ILE A 75 3517 3430 3528 78 255 -409 C ATOM 560 O ILE A 75 -2.230 16.113 32.560 1.00 28.03 O ANISOU 560 O ILE A 75 3575 3486 3590 89 286 -419 O ATOM 561 CB ILE A 75 -1.082 16.112 29.814 1.00 28.58 C ANISOU 561 CB ILE A 75 3737 3498 3625 92 255 -410 C ATOM 562 CG1 ILE A 75 -1.242 16.650 28.384 1.00 28.41 C ANISOU 562 CG1 ILE A 75 3761 3444 3588 118 238 -399 C ATOM 563 CG2 ILE A 75 0.186 15.244 30.027 1.00 27.56 C ANISOU 563 CG2 ILE A 75 3615 3370 3486 55 265 -421 C ATOM 564 CD1 ILE A 75 -1.395 15.594 27.295 1.00 27.81 C ANISOU 564 CD1 ILE A 75 3693 3370 3501 110 196 -387 C ATOM 565 N GLY A 76 -2.218 13.872 32.208 1.00 26.59 N ANISOU 565 N GLY A 76 3368 3329 3407 52 244 -406 N ATOM 566 CA GLY A 76 -2.164 13.485 33.623 1.00 23.89 C ANISOU 566 CA GLY A 76 2997 3012 3071 36 267 -412 C ATOM 567 C GLY A 76 -0.800 13.023 34.095 1.00 22.92 C ANISOU 567 C GLY A 76 2891 2889 2929 13 283 -423 C ATOM 568 O GLY A 76 -0.542 12.960 35.295 1.00 22.23 O ANISOU 568 O GLY A 76 2788 2819 2837 6 304 -431 O ATOM 569 N ARG A 77 0.069 12.697 33.146 1.00 22.15 N ANISOU 569 N ARG A 77 2824 2772 2819 3 271 -424 N ATOM 570 CA ARG A 77 1.426 12.239 33.415 1.00 21.88 C ANISOU 570 CA ARG A 77 2805 2738 2770 -16 283 -435 C ATOM 571 C ARG A 77 2.341 12.706 32.264 1.00 21.46 C ANISOU 571 C ARG A 77 2794 2654 2707 -17 285 -444 C ATOM 572 O ARG A 77 1.990 12.580 31.095 1.00 20.60 O ANISOU 572 O ARG A 77 2704 2526 2597 -12 264 -432 O ATOM 573 CB ARG A 77 1.497 10.695 33.626 1.00 21.75 C ANISOU 573 CB ARG A 77 2774 2738 2751 -34 268 -423 C ATOM 574 CG ARG A 77 2.942 10.144 33.879 1.00 21.88 C ANISOU 574 CG ARG A 77 2805 2757 2753 -48 277 -434 C ATOM 575 CD ARG A 77 3.013 8.637 34.222 1.00 21.95 C ANISOU 575 CD ARG A 77 2803 2779 2759 -61 268 -420 C ATOM 576 NE ARG A 77 2.858 8.416 35.664 1.00 25.87 N ANISOU 576 NE ARG A 77 3277 3303 3250 -58 283 -419 N ATOM 577 CZ ARG A 77 3.834 8.010 36.476 1.00 26.04 C ANISOU 577 CZ ARG A 77 3299 3339 3255 -59 291 -426 C ATOM 578 NH1 ARG A 77 5.053 7.788 36.004 1.00 23.22 N ANISOU 578 NH1 ARG A 77 2959 2974 2889 -63 288 -436 N ATOM 579 NH2 ARG A 77 3.597 7.845 37.776 1.00 29.10 N ANISOU 579 NH2 ARG A 77 3672 3751 3634 -54 304 -424 N ATOM 580 N LEU A 78 3.505 13.251 32.622 1.00 21.47 N ANISOU 580 N LEU A 78 2809 2650 2701 -26 310 -466 N ATOM 581 CA LEU A 78 4.505 13.696 31.662 1.00 23.21 C ANISOU 581 CA LEU A 78 3068 2839 2914 -32 322 -478 C ATOM 582 C LEU A 78 5.852 13.186 32.139 1.00 23.84 C ANISOU 582 C LEU A 78 3142 2929 2988 -52 334 -497 C ATOM 583 O LEU A 78 6.286 13.500 33.242 1.00 24.33 O ANISOU 583 O LEU A 78 3185 3013 3048 -56 350 -516 O ATOM 584 CB LEU A 78 4.506 15.226 31.492 1.00 23.29 C ANISOU 584 CB LEU A 78 3101 2823 2924 -19 349 -492 C ATOM 585 CG LEU A 78 5.355 15.814 30.341 1.00 25.67 C ANISOU 585 CG LEU A 78 3451 3082 3218 -23 368 -502 C ATOM 586 CD1 LEU A 78 4.995 17.249 30.102 1.00 29.74 C ANISOU 586 CD1 LEU A 78 3995 3569 3735 -4 393 -506 C ATOM 587 CD2 LEU A 78 6.820 15.788 30.698 1.00 27.71 C ANISOU 587 CD2 LEU A 78 3710 3342 3476 -48 393 -531 C ATOM 588 N GLU A 79 6.514 12.391 31.304 1.00 24.46 N ANISOU 588 N GLU A 79 3237 2995 3062 -63 325 -493 N ATOM 589 CA GLU A 79 7.782 11.779 31.666 1.00 24.79 C ANISOU 589 CA GLU A 79 3270 3048 3100 -78 332 -510 C ATOM 590 C GLU A 79 8.794 11.979 30.546 1.00 25.16 C ANISOU 590 C GLU A 79 3351 3062 3146 -88 347 -523 C ATOM 591 O GLU A 79 8.420 12.038 29.382 1.00 23.83 O ANISOU 591 O GLU A 79 3216 2864 2975 -84 341 -509 O ATOM 592 CB GLU A 79 7.602 10.278 31.906 1.00 26.16 C ANISOU 592 CB GLU A 79 3427 3242 3271 -80 308 -489 C ATOM 593 CG GLU A 79 7.049 9.919 33.240 1.00 29.41 C ANISOU 593 CG GLU A 79 3805 3689 3681 -74 303 -482 C ATOM 594 CD GLU A 79 7.120 8.441 33.495 1.00 33.17 C ANISOU 594 CD GLU A 79 4272 4179 4153 -77 288 -465 C ATOM 595 OE1 GLU A 79 8.257 7.910 33.717 1.00 30.80 O ANISOU 595 OE1 GLU A 79 3971 3887 3846 -80 292 -475 O ATOM 596 OE2 GLU A 79 6.023 7.820 33.459 1.00 34.28 O ANISOU 596 OE2 GLU A 79 4406 4322 4298 -76 274 -442 O ATOM 597 N VAL A 80 10.074 12.090 30.921 1.00 24.59 N ANISOU 597 N VAL A 80 3270 2997 3077 -101 367 -551 N ATOM 598 CA VAL A 80 11.158 12.354 29.973 1.00 24.17 C ANISOU 598 CA VAL A 80 3245 2912 3027 -114 391 -570 C ATOM 599 C VAL A 80 12.238 11.290 30.062 1.00 24.70 C ANISOU 599 C VAL A 80 3294 2994 3095 -123 387 -579 C ATOM 600 O VAL A 80 12.682 10.910 31.168 1.00 24.37 O ANISOU 600 O VAL A 80 3215 2989 3053 -122 380 -590 O ATOM 601 CB VAL A 80 11.834 13.732 30.196 1.00 24.48 C ANISOU 601 CB VAL A 80 3289 2939 3073 -124 429 -607 C ATOM 602 CG1 VAL A 80 12.913 13.986 29.102 1.00 23.55 C ANISOU 602 CG1 VAL A 80 3204 2783 2961 -141 460 -626 C ATOM 603 CG2 VAL A 80 10.805 14.829 30.144 1.00 23.07 C ANISOU 603 CG2 VAL A 80 3131 2743 2892 -111 437 -598 C ATOM 604 N GLY A 81 12.680 10.830 28.894 1.00 24.14 N ANISOU 604 N GLY A 81 3254 2894 3026 -130 392 -573 N ATOM 605 CA GLY A 81 13.862 9.993 28.819 1.00 24.42 C ANISOU 605 CA GLY A 81 3277 2935 3067 -138 397 -586 C ATOM 606 C GLY A 81 14.953 10.791 28.122 1.00 25.07 C ANISOU 606 C GLY A 81 3379 2987 3160 -155 436 -619 C ATOM 607 O GLY A 81 14.710 11.448 27.112 1.00 24.85 O ANISOU 607 O GLY A 81 3394 2918 3128 -159 455 -615 O ATOM 608 N SER A 82 16.154 10.758 28.680 1.00 25.31 N ANISOU 608 N SER A 82 3376 3038 3203 -164 451 -652 N ATOM 609 CA SER A 82 17.273 11.498 28.100 1.00 26.62 C ANISOU 609 CA SER A 82 3553 3177 3384 -184 493 -689 C ATOM 610 C SER A 82 18.525 11.022 28.750 1.00 27.97 C ANISOU 610 C SER A 82 3675 3382 3570 -189 495 -720 C ATOM 611 O SER A 82 18.492 10.632 29.896 1.00 28.23 O ANISOU 611 O SER A 82 3667 3461 3598 -177 468 -721 O ATOM 612 CB SER A 82 17.135 13.007 28.355 1.00 26.41 C ANISOU 612 CB SER A 82 3534 3138 3362 -195 522 -714 C ATOM 613 OG SER A 82 18.048 13.748 27.528 1.00 25.99 O ANISOU 613 OG SER A 82 3507 3045 3323 -218 571 -745 O ATOM 614 N GLU A 83 19.645 11.013 28.040 1.00 29.76 N ANISOU 614 N GLU A 83 3907 3588 3814 -205 527 -746 N ATOM 615 CA GLU A 83 20.895 10.860 28.772 1.00 33.29 C ANISOU 615 CA GLU A 83 4298 4072 4280 -210 531 -787 C ATOM 616 C GLU A 83 21.716 12.146 28.753 1.00 35.22 C ANISOU 616 C GLU A 83 4533 4303 4545 -239 577 -840 C ATOM 617 O GLU A 83 22.899 12.155 29.136 1.00 36.85 O ANISOU 617 O GLU A 83 4693 4535 4773 -250 589 -883 O ATOM 618 CB GLU A 83 21.716 9.663 28.270 1.00 33.23 C ANISOU 618 CB GLU A 83 4281 4064 4282 -203 529 -783 C ATOM 619 CG GLU A 83 22.112 9.750 26.835 1.00 35.81 C ANISOU 619 CG GLU A 83 4653 4334 4618 -221 570 -785 C ATOM 620 CD GLU A 83 22.702 8.465 26.345 1.00 39.82 C ANISOU 620 CD GLU A 83 5158 4839 5132 -210 565 -773 C ATOM 621 OE1 GLU A 83 23.840 8.130 26.750 1.00 44.01 O ANISOU 621 OE1 GLU A 83 5641 5397 5684 -208 570 -804 O ATOM 622 OE2 GLU A 83 22.032 7.802 25.536 1.00 41.70 O ANISOU 622 OE2 GLU A 83 5443 5048 5354 -203 556 -735 O ATOM 623 N THR A 84 21.072 13.232 28.340 1.00 36.72 N ANISOU 623 N THR A 84 4765 4456 4729 -251 603 -837 N ATOM 624 CA THR A 84 21.735 14.506 28.123 1.00 38.99 C ANISOU 624 CA THR A 84 5061 4717 5036 -281 656 -884 C ATOM 625 C THR A 84 21.529 15.364 29.363 1.00 40.98 C ANISOU 625 C THR A 84 5280 5003 5287 -285 650 -910 C ATOM 626 O THR A 84 20.462 15.940 29.548 1.00 41.90 O ANISOU 626 O THR A 84 5424 5109 5387 -276 644 -888 O ATOM 627 CB THR A 84 21.215 15.192 26.836 1.00 38.63 C ANISOU 627 CB THR A 84 5092 4602 4983 -288 694 -865 C ATOM 628 OG1 THR A 84 21.566 14.394 25.668 1.00 38.25 O ANISOU 628 OG1 THR A 84 5075 4522 4935 -287 704 -847 O ATOM 629 CG2 THR A 84 21.801 16.585 26.721 1.00 40.02 C ANISOU 629 CG2 THR A 84 5282 4747 5178 -319 755 -911 C ATOM 630 N VAL A 85 22.562 15.424 30.209 1.00 43.03 N ANISOU 630 N VAL A 85 5480 5305 5565 -299 651 -959 N ATOM 631 CA VAL A 85 22.485 16.011 31.561 1.00 44.96 C ANISOU 631 CA VAL A 85 5683 5595 5804 -301 635 -988 C ATOM 632 C VAL A 85 22.591 17.544 31.533 1.00 45.95 C ANISOU 632 C VAL A 85 5828 5689 5943 -333 688 -1029 C ATOM 633 O VAL A 85 23.601 18.091 31.093 1.00 47.01 O ANISOU 633 O VAL A 85 5956 5801 6104 -365 735 -1076 O ATOM 634 CB VAL A 85 23.555 15.400 32.520 1.00 45.07 C ANISOU 634 CB VAL A 85 5624 5674 5828 -298 607 -1026 C ATOM 635 CG1 VAL A 85 23.137 14.010 33.011 1.00 44.88 C ANISOU 635 CG1 VAL A 85 5583 5689 5780 -258 548 -980 C ATOM 636 CG2 VAL A 85 24.922 15.312 31.815 1.00 47.91 C ANISOU 636 CG2 VAL A 85 5962 6021 6221 -321 642 -1067 C ATOM 637 N ILE A 86 21.524 18.211 31.975 1.00 45.72 N ANISOU 637 N ILE A 86 5823 5653 5895 -324 683 -1011 N ATOM 638 CA ILE A 86 21.446 19.673 32.022 1.00 46.20 C ANISOU 638 CA ILE A 86 5908 5680 5964 -349 733 -1044 C ATOM 639 C ILE A 86 21.651 20.183 33.446 1.00 45.38 C ANISOU 639 C ILE A 86 5757 5628 5860 -360 722 -1087 C ATOM 640 O ILE A 86 22.213 21.247 33.660 1.00 45.91 O ANISOU 640 O ILE A 86 5818 5682 5943 -393 765 -1141 O ATOM 641 CB ILE A 86 20.071 20.180 31.527 1.00 46.22 C ANISOU 641 CB ILE A 86 5975 5638 5947 -329 740 -994 C ATOM 642 CG1 ILE A 86 19.984 20.068 30.012 1.00 47.84 C ANISOU 642 CG1 ILE A 86 6241 5783 6154 -326 766 -964 C ATOM 643 CG2 ILE A 86 19.838 21.658 31.909 1.00 46.98 C ANISOU 643 CG2 ILE A 86 6093 5710 6049 -347 784 -1025 C ATOM 644 CD1 ILE A 86 18.561 20.118 29.522 1.00 48.91 C ANISOU 644 CD1 ILE A 86 6428 5890 6265 -294 748 -906 C ATOM 645 N ASP A 87 21.167 19.422 34.412 1.00 44.20 N ANISOU 645 N ASP A 87 5575 5532 5688 -332 665 -1064 N ATOM 646 CA ASP A 87 21.300 19.782 35.806 1.00 43.72 C ANISOU 646 CA ASP A 87 5471 5524 5618 -336 648 -1101 C ATOM 647 C ASP A 87 21.416 18.452 36.544 1.00 44.18 C ANISOU 647 C ASP A 87 5485 5644 5657 -306 585 -1081 C ATOM 648 O ASP A 87 20.854 17.446 36.105 1.00 42.89 O ANISOU 648 O ASP A 87 5339 5475 5482 -277 558 -1025 O ATOM 649 CB ASP A 87 20.080 20.588 36.266 1.00 42.56 C ANISOU 649 CB ASP A 87 5358 5361 5453 -327 655 -1081 C ATOM 650 CG ASP A 87 20.334 21.378 37.555 1.00 40.68 C ANISOU 650 CG ASP A 87 5087 5160 5209 -344 659 -1134 C ATOM 651 OD1 ASP A 87 20.690 22.565 37.450 1.00 36.30 O ANISOU 651 OD1 ASP A 87 4546 4574 4671 -378 710 -1180 O ATOM 652 OD2 ASP A 87 20.170 20.824 38.669 1.00 35.44 O ANISOU 652 OD2 ASP A 87 4390 4554 4522 -325 613 -1131 O ATOM 653 N LYS A 88 22.164 18.450 37.645 1.00 44.60 N ANISOU 653 N LYS A 88 5484 5755 5706 -311 564 -1127 N ATOM 654 CA LYS A 88 22.340 17.229 38.428 1.00 44.87 C ANISOU 654 CA LYS A 88 5480 5850 5719 -278 506 -1109 C ATOM 655 C LYS A 88 21.157 16.934 39.362 1.00 44.47 C ANISOU 655 C LYS A 88 5442 5823 5631 -247 472 -1067 C ATOM 656 O LYS A 88 20.954 15.773 39.772 1.00 45.10 O ANISOU 656 O LYS A 88 5510 5935 5689 -213 429 -1030 O ATOM 657 CB LYS A 88 23.692 17.266 39.156 1.00 45.48 C ANISOU 657 CB LYS A 88 5493 5983 5805 -292 493 -1176 C ATOM 658 CG LYS A 88 24.858 17.299 38.130 1.00 46.13 C ANISOU 658 CG LYS A 88 5558 6041 5928 -318 526 -1211 C ATOM 659 CD LYS A 88 26.236 17.138 38.747 1.00 46.68 C ANISOU 659 CD LYS A 88 5555 6171 6011 -326 507 -1275 C ATOM 660 CE LYS A 88 26.514 18.175 39.807 1.00 48.23 C ANISOU 660 CE LYS A 88 5721 6402 6203 -353 511 -1339 C ATOM 661 NZ LYS A 88 27.917 18.018 40.285 1.00 48.15 N ANISOU 661 NZ LYS A 88 5634 6450 6209 -362 491 -1407 N ATOM 662 N SER A 89 20.361 17.977 39.634 1.00 42.81 N ANISOU 662 N SER A 89 5259 5591 5415 -259 497 -1071 N ATOM 663 CA SER A 89 19.196 17.905 40.509 1.00 42.01 C ANISOU 663 CA SER A 89 5171 5506 5283 -235 476 -1037 C ATOM 664 C SER A 89 17.840 18.124 39.798 1.00 41.03 C ANISOU 664 C SER A 89 5099 5330 5161 -225 493 -984 C ATOM 665 O SER A 89 16.905 17.311 39.957 1.00 40.93 O ANISOU 665 O SER A 89 5096 5324 5131 -195 466 -931 O ATOM 666 CB SER A 89 19.376 18.906 41.655 1.00 42.16 C ANISOU 666 CB SER A 89 5173 5554 5291 -252 485 -1090 C ATOM 667 OG SER A 89 18.244 18.939 42.474 1.00 43.18 O ANISOU 667 OG SER A 89 5319 5695 5393 -232 473 -1060 O ATOM 668 N LYS A 90 17.736 19.219 39.031 1.00 39.63 N ANISOU 668 N LYS A 90 4953 5100 5004 -247 540 -999 N ATOM 669 CA LYS A 90 16.491 19.633 38.365 1.00 37.58 C ANISOU 669 CA LYS A 90 4741 4790 4746 -235 559 -955 C ATOM 670 C LYS A 90 16.264 18.896 37.015 1.00 37.15 C ANISOU 670 C LYS A 90 4714 4700 4700 -224 553 -910 C ATOM 671 O LYS A 90 17.047 19.034 36.056 1.00 36.91 O ANISOU 671 O LYS A 90 4697 4639 4689 -242 578 -927 O ATOM 672 CB LYS A 90 16.476 21.160 38.199 1.00 37.70 C ANISOU 672 CB LYS A 90 4785 4765 4775 -260 612 -990 C ATOM 673 CG LYS A 90 15.436 21.760 37.222 1.00 35.34 C ANISOU 673 CG LYS A 90 4540 4404 4482 -247 640 -952 C ATOM 674 CD LYS A 90 15.542 23.304 37.278 1.00 36.60 C ANISOU 674 CD LYS A 90 4726 4526 4653 -271 697 -993 C ATOM 675 CE LYS A 90 14.510 24.007 36.420 1.00 35.49 C ANISOU 675 CE LYS A 90 4643 4325 4515 -252 725 -956 C ATOM 676 NZ LYS A 90 13.087 23.545 36.661 1.00 30.33 N ANISOU 676 NZ LYS A 90 3993 3684 3846 -213 689 -900 N ATOM 677 N SER A 91 15.176 18.131 36.959 1.00 35.74 N ANISOU 677 N SER A 91 4546 4524 4508 -195 523 -855 N ATOM 678 CA SER A 91 14.835 17.329 35.781 1.00 34.34 C ANISOU 678 CA SER A 91 4394 4319 4335 -183 511 -812 C ATOM 679 C SER A 91 14.438 18.148 34.552 1.00 33.86 C ANISOU 679 C SER A 91 4383 4197 4285 -187 544 -801 C ATOM 680 O SER A 91 13.920 19.278 34.652 1.00 31.95 O ANISOU 680 O SER A 91 4163 3932 4045 -188 572 -809 O ATOM 681 CB SER A 91 13.711 16.338 36.119 1.00 34.32 C ANISOU 681 CB SER A 91 4388 4337 4317 -155 472 -761 C ATOM 682 OG SER A 91 12.540 17.025 36.537 1.00 34.06 O ANISOU 682 OG SER A 91 4366 4298 4278 -143 478 -747 O ATOM 683 N ILE A 92 14.682 17.546 33.389 1.00 33.19 N ANISOU 683 N ILE A 92 4320 4086 4205 -187 542 -782 N ATOM 684 CA ILE A 92 14.149 18.049 32.131 1.00 33.67 C ANISOU 684 CA ILE A 92 4434 4090 4268 -182 563 -759 C ATOM 685 C ILE A 92 12.591 18.127 32.177 1.00 32.95 C ANISOU 685 C ILE A 92 4358 3995 4165 -153 541 -716 C ATOM 686 O ILE A 92 11.994 19.065 31.612 1.00 32.87 O ANISOU 686 O ILE A 92 4388 3947 4155 -144 564 -708 O ATOM 687 CB ILE A 92 14.625 17.191 30.938 1.00 33.85 C ANISOU 687 CB ILE A 92 4477 4092 4293 -184 557 -743 C ATOM 688 CG1 ILE A 92 16.173 17.186 30.862 1.00 34.00 C ANISOU 688 CG1 ILE A 92 4478 4113 4329 -212 584 -789 C ATOM 689 CG2 ILE A 92 13.926 17.663 29.628 1.00 33.45 C ANISOU 689 CG2 ILE A 92 4487 3985 4236 -173 572 -714 C ATOM 690 CD1 ILE A 92 16.751 16.298 29.744 1.00 35.03 C ANISOU 690 CD1 ILE A 92 4625 4222 4462 -216 583 -776 C ATOM 691 N LYS A 93 11.961 17.158 32.858 1.00 31.73 N ANISOU 691 N LYS A 93 4172 3881 4001 -137 500 -691 N ATOM 692 CA LYS A 93 10.498 17.154 33.049 1.00 31.62 C ANISOU 692 CA LYS A 93 4162 3872 3982 -113 480 -655 C ATOM 693 C LYS A 93 9.999 18.513 33.569 1.00 31.76 C ANISOU 693 C LYS A 93 4188 3877 4002 -108 508 -670 C ATOM 694 O LYS A 93 9.092 19.082 32.996 1.00 31.04 O ANISOU 694 O LYS A 93 4125 3757 3911 -89 514 -649 O ATOM 695 CB LYS A 93 10.056 16.024 33.987 1.00 31.43 C ANISOU 695 CB LYS A 93 4099 3894 3950 -103 443 -636 C ATOM 696 CG LYS A 93 8.524 15.819 34.087 1.00 30.08 C ANISOU 696 CG LYS A 93 3925 3727 3776 -81 422 -599 C ATOM 697 CD LYS A 93 7.890 16.633 35.221 1.00 30.92 C ANISOU 697 CD LYS A 93 4015 3850 3882 -73 435 -609 C ATOM 698 CE LYS A 93 6.341 16.623 35.166 1.00 29.93 C ANISOU 698 CE LYS A 93 3888 3723 3761 -50 421 -575 C ATOM 699 NZ LYS A 93 5.797 15.279 35.499 1.00 26.19 N ANISOU 699 NZ LYS A 93 3388 3278 3284 -46 390 -549 N ATOM 700 N THR A 94 10.630 19.034 34.631 1.00 31.95 N ANISOU 700 N THR A 94 4190 3923 4027 -124 527 -709 N ATOM 701 CA THR A 94 10.261 20.355 35.193 1.00 32.68 C ANISOU 701 CA THR A 94 4293 4003 4122 -123 560 -729 C ATOM 702 C THR A 94 10.277 21.496 34.165 1.00 33.67 C ANISOU 702 C THR A 94 4468 4069 4255 -123 601 -734 C ATOM 703 O THR A 94 9.377 22.320 34.151 1.00 34.24 O ANISOU 703 O THR A 94 4563 4120 4329 -104 616 -722 O ATOM 704 CB THR A 94 11.083 20.733 36.478 1.00 32.20 C ANISOU 704 CB THR A 94 4200 3976 4058 -145 574 -777 C ATOM 705 OG1 THR A 94 12.473 20.892 36.162 1.00 32.17 O ANISOU 705 OG1 THR A 94 4195 3966 4064 -174 594 -818 O ATOM 706 CG2 THR A 94 10.943 19.643 37.547 1.00 31.52 C ANISOU 706 CG2 THR A 94 4071 3946 3957 -137 534 -767 C ATOM 707 N PHE A 95 11.295 21.536 33.308 1.00 34.60 N ANISOU 707 N PHE A 95 4607 4160 4379 -143 621 -752 N ATOM 708 CA PHE A 95 11.342 22.538 32.234 1.00 35.50 C ANISOU 708 CA PHE A 95 4778 4213 4498 -143 664 -753 C ATOM 709 C PHE A 95 10.096 22.503 31.343 1.00 36.21 C ANISOU 709 C PHE A 95 4904 4276 4579 -105 644 -702 C ATOM 710 O PHE A 95 9.485 23.542 31.043 1.00 35.61 O ANISOU 710 O PHE A 95 4866 4162 4501 -86 671 -694 O ATOM 711 CB PHE A 95 12.548 22.277 31.356 1.00 35.12 C ANISOU 711 CB PHE A 95 4745 4142 4456 -168 683 -772 C ATOM 712 CG PHE A 95 13.852 22.637 31.978 1.00 34.57 C ANISOU 712 CG PHE A 95 4649 4086 4401 -207 714 -830 C ATOM 713 CD1 PHE A 95 14.386 23.925 31.793 1.00 34.72 C ANISOU 713 CD1 PHE A 95 4699 4060 4431 -230 776 -868 C ATOM 714 CD2 PHE A 95 14.580 21.689 32.696 1.00 32.24 C ANISOU 714 CD2 PHE A 95 4299 3845 4108 -221 683 -848 C ATOM 715 CE1 PHE A 95 15.620 24.266 32.331 1.00 33.71 C ANISOU 715 CE1 PHE A 95 4543 3946 4320 -270 805 -928 C ATOM 716 CE2 PHE A 95 15.792 22.011 33.255 1.00 31.18 C ANISOU 716 CE2 PHE A 95 4133 3726 3987 -254 707 -905 C ATOM 717 CZ PHE A 95 16.329 23.292 33.067 1.00 35.81 C ANISOU 717 CZ PHE A 95 4746 4273 4588 -282 768 -947 C ATOM 718 N LEU A 96 9.749 21.288 30.900 1.00 37.28 N ANISOU 718 N LEU A 96 5027 4431 4707 -94 598 -669 N ATOM 719 CA LEU A 96 8.567 21.035 30.064 1.00 38.71 C ANISOU 719 CA LEU A 96 5231 4598 4878 -60 568 -623 C ATOM 720 C LEU A 96 7.240 21.425 30.717 1.00 39.02 C ANISOU 720 C LEU A 96 5255 4653 4919 -30 554 -603 C ATOM 721 O LEU A 96 6.233 21.627 30.024 1.00 38.97 O ANISOU 721 O LEU A 96 5271 4628 4907 2 539 -572 O ATOM 722 CB LEU A 96 8.511 19.553 29.672 1.00 38.45 C ANISOU 722 CB LEU A 96 5178 4590 4840 -60 521 -599 C ATOM 723 CG LEU A 96 9.071 19.056 28.331 1.00 41.25 C ANISOU 723 CG LEU A 96 5571 4915 5187 -67 520 -590 C ATOM 724 CD1 LEU A 96 8.394 19.806 27.151 1.00 42.42 C ANISOU 724 CD1 LEU A 96 5780 5015 5323 -40 528 -566 C ATOM 725 CD2 LEU A 96 10.614 19.151 28.264 1.00 43.44 C ANISOU 725 CD2 LEU A 96 5852 5180 5472 -101 558 -628 C ATOM 726 N MET A 97 7.215 21.490 32.049 1.00 39.35 N ANISOU 726 N MET A 97 5254 4730 4967 -39 557 -622 N ATOM 727 CA MET A 97 5.994 21.890 32.729 1.00 40.10 C ANISOU 727 CA MET A 97 5333 4839 5066 -13 551 -607 C ATOM 728 C MET A 97 5.516 23.295 32.349 1.00 41.85 C ANISOU 728 C MET A 97 5598 5015 5289 10 587 -606 C ATOM 729 O MET A 97 4.309 23.562 32.436 1.00 41.35 O ANISOU 729 O MET A 97 5530 4953 5229 43 575 -582 O ATOM 730 CB MET A 97 6.124 21.782 34.248 1.00 39.96 C ANISOU 730 CB MET A 97 5270 4863 5049 -28 554 -630 C ATOM 731 CG MET A 97 5.973 20.368 34.822 1.00 38.48 C ANISOU 731 CG MET A 97 5039 4725 4858 -32 512 -615 C ATOM 732 SD MET A 97 4.475 19.530 34.256 1.00 35.92 S ANISOU 732 SD MET A 97 4703 4409 4537 -2 468 -565 S ATOM 733 CE MET A 97 3.136 20.593 34.857 1.00 36.28 C ANISOU 733 CE MET A 97 4742 4450 4592 28 485 -557 C ATOM 734 N GLN A 98 6.432 24.188 31.950 1.00 43.80 N ANISOU 734 N GLN A 98 5886 5221 5536 -7 634 -633 N ATOM 735 CA GLN A 98 5.998 25.524 31.439 1.00 47.33 C ANISOU 735 CA GLN A 98 6385 5614 5982 18 673 -628 C ATOM 736 C GLN A 98 4.888 25.340 30.399 1.00 47.59 C ANISOU 736 C GLN A 98 6443 5633 6007 64 639 -581 C ATOM 737 O GLN A 98 3.890 26.040 30.423 1.00 48.21 O ANISOU 737 O GLN A 98 6533 5698 6088 101 643 -563 O ATOM 738 CB GLN A 98 7.126 26.342 30.786 1.00 47.61 C ANISOU 738 CB GLN A 98 6475 5598 6018 -5 728 -657 C ATOM 739 CG GLN A 98 8.426 26.485 31.557 1.00 49.48 C ANISOU 739 CG GLN A 98 6689 5846 6265 -56 761 -710 C ATOM 740 CD GLN A 98 9.559 27.022 30.685 1.00 50.78 C ANISOU 740 CD GLN A 98 6902 5960 6431 -82 811 -736 C ATOM 741 OE1 GLN A 98 9.460 28.124 30.130 1.00 56.12 O ANISOU 741 OE1 GLN A 98 7637 6579 7107 -71 859 -736 O ATOM 742 NE2 GLN A 98 10.648 26.247 30.562 1.00 54.72 N ANISOU 742 NE2 GLN A 98 7378 6478 6935 -117 804 -758 N ATOM 743 N LEU A 99 5.064 24.382 29.492 1.00 48.06 N ANISOU 743 N LEU A 99 6508 5696 6057 61 605 -562 N ATOM 744 CA LEU A 99 4.055 24.122 28.468 1.00 48.99 C ANISOU 744 CA LEU A 99 6645 5805 6163 102 566 -521 C ATOM 745 C LEU A 99 2.642 23.773 29.007 1.00 49.55 C ANISOU 745 C LEU A 99 6668 5915 6243 133 523 -496 C ATOM 746 O LEU A 99 1.668 23.843 28.246 1.00 50.13 O ANISOU 746 O LEU A 99 6756 5981 6310 173 495 -466 O ATOM 747 CB LEU A 99 4.556 23.064 27.474 1.00 48.93 C ANISOU 747 CB LEU A 99 6651 5798 6143 87 536 -510 C ATOM 748 CG LEU A 99 5.925 23.240 26.768 1.00 49.68 C ANISOU 748 CG LEU A 99 6793 5853 6231 57 576 -531 C ATOM 749 CD1 LEU A 99 6.092 22.187 25.676 1.00 48.70 C ANISOU 749 CD1 LEU A 99 6685 5728 6092 54 542 -512 C ATOM 750 CD2 LEU A 99 6.146 24.650 26.178 1.00 50.31 C ANISOU 750 CD2 LEU A 99 6943 5870 6303 71 632 -537 C ATOM 751 N PHE A 100 2.530 23.390 30.290 1.00 49.04 N ANISOU 751 N PHE A 100 6547 5894 6193 115 519 -510 N ATOM 752 CA PHE A 100 1.227 23.081 30.922 1.00 49.48 C ANISOU 752 CA PHE A 100 6554 5986 6259 139 489 -491 C ATOM 753 C PHE A 100 0.729 24.119 31.927 1.00 50.00 C ANISOU 753 C PHE A 100 6610 6050 6338 154 523 -503 C ATOM 754 O PHE A 100 -0.467 24.198 32.184 1.00 49.91 O ANISOU 754 O PHE A 100 6572 6055 6338 186 507 -485 O ATOM 755 CB PHE A 100 1.278 21.764 31.692 1.00 49.43 C ANISOU 755 CB PHE A 100 6491 6030 6259 112 459 -493 C ATOM 756 CG PHE A 100 1.351 20.557 30.848 1.00 49.04 C ANISOU 756 CG PHE A 100 6439 5991 6202 103 416 -476 C ATOM 757 CD1 PHE A 100 1.672 19.348 31.427 1.00 49.79 C ANISOU 757 CD1 PHE A 100 6496 6123 6299 75 397 -480 C ATOM 758 CD2 PHE A 100 1.086 20.617 29.491 1.00 49.43 C ANISOU 758 CD2 PHE A 100 6526 6013 6240 125 397 -456 C ATOM 759 CE1 PHE A 100 1.736 18.226 30.680 1.00 51.13 C ANISOU 759 CE1 PHE A 100 6664 6299 6463 66 362 -465 C ATOM 760 CE2 PHE A 100 1.141 19.516 28.720 1.00 51.35 C ANISOU 760 CE2 PHE A 100 6769 6266 6476 115 359 -443 C ATOM 761 CZ PHE A 100 1.480 18.298 29.298 1.00 52.66 C ANISOU 761 CZ PHE A 100 6896 6466 6646 84 343 -448 C ATOM 762 N GLU A 101 1.656 24.848 32.545 1.00 51.09 N ANISOU 762 N GLU A 101 6764 6172 6476 129 571 -536 N ATOM 763 CA GLU A 101 1.335 25.878 33.543 1.00 52.28 C ANISOU 763 CA GLU A 101 6911 6318 6636 137 611 -554 C ATOM 764 C GLU A 101 0.304 26.872 33.001 1.00 52.26 C ANISOU 764 C GLU A 101 6938 6280 6637 189 623 -531 C ATOM 765 O GLU A 101 -0.678 27.184 33.669 1.00 52.51 O ANISOU 765 O GLU A 101 6944 6327 6682 214 625 -523 O ATOM 766 CB GLU A 101 2.619 26.609 33.977 1.00 52.73 C ANISOU 766 CB GLU A 101 6993 6352 6689 100 663 -598 C ATOM 767 CG GLU A 101 3.472 25.878 35.051 1.00 53.58 C ANISOU 767 CG GLU A 101 7059 6506 6795 55 658 -628 C ATOM 768 CD GLU A 101 4.956 26.317 35.071 1.00 53.58 C ANISOU 768 CD GLU A 101 7080 6486 6791 14 696 -672 C ATOM 769 OE1 GLU A 101 5.250 27.537 34.917 1.00 56.40 O ANISOU 769 OE1 GLU A 101 7480 6799 7152 11 747 -693 O ATOM 770 OE2 GLU A 101 5.829 25.428 35.234 1.00 53.09 O ANISOU 770 OE2 GLU A 101 6994 6453 6725 -17 676 -687 O ATOM 771 N LYS A 102 0.537 27.345 31.778 1.00 52.30 N ANISOU 771 N LYS A 102 7001 6240 6631 207 631 -518 N ATOM 772 CA LYS A 102 -0.374 28.244 31.050 1.00 52.55 C ANISOU 772 CA LYS A 102 7071 6236 6661 263 636 -491 C ATOM 773 C LYS A 102 -1.844 27.793 31.005 1.00 52.09 C ANISOU 773 C LYS A 102 6967 6210 6612 307 585 -459 C ATOM 774 O LYS A 102 -2.759 28.630 30.992 1.00 52.86 O ANISOU 774 O LYS A 102 7075 6293 6718 356 595 -444 O ATOM 775 CB LYS A 102 0.169 28.528 29.639 1.00 53.28 C ANISOU 775 CB LYS A 102 7233 6278 6732 273 643 -479 C ATOM 776 CG LYS A 102 0.998 27.374 29.018 1.00 55.10 C ANISOU 776 CG LYS A 102 7461 6524 6951 236 612 -481 C ATOM 777 CD LYS A 102 2.255 27.886 28.281 1.00 57.10 C ANISOU 777 CD LYS A 102 7782 6724 7190 212 659 -499 C ATOM 778 CE LYS A 102 1.951 28.447 26.879 1.00 58.40 C ANISOU 778 CE LYS A 102 8020 6837 7332 256 662 -469 C ATOM 779 NZ LYS A 102 3.138 29.140 26.262 1.00 58.56 N ANISOU 779 NZ LYS A 102 8112 6796 7341 232 723 -489 N ATOM 780 N CYS A 103 -2.068 26.481 30.996 1.00 50.38 N ANISOU 780 N CYS A 103 6703 6041 6399 291 533 -449 N ATOM 781 CA CYS A 103 -3.416 25.915 31.120 1.00 49.75 C ANISOU 781 CA CYS A 103 6567 6001 6334 321 486 -427 C ATOM 782 C CYS A 103 -3.874 25.687 32.568 1.00 47.57 C ANISOU 782 C CYS A 103 6231 5764 6080 306 497 -440 C ATOM 783 O CYS A 103 -5.011 25.302 32.805 1.00 47.85 O ANISOU 783 O CYS A 103 6217 5831 6133 328 469 -425 O ATOM 784 CB CYS A 103 -3.518 24.607 30.317 1.00 49.98 C ANISOU 784 CB CYS A 103 6578 6057 6356 310 427 -410 C ATOM 785 SG CYS A 103 -3.646 24.935 28.539 1.00 55.31 S ANISOU 785 SG CYS A 103 7316 6692 7005 352 401 -384 S ATOM 786 N GLY A 104 -2.984 25.925 33.527 1.00 45.73 N ANISOU 786 N GLY A 104 6002 5530 5845 268 539 -470 N ATOM 787 CA GLY A 104 -3.264 25.657 34.943 1.00 43.35 C ANISOU 787 CA GLY A 104 5650 5264 5556 250 551 -485 C ATOM 788 C GLY A 104 -3.220 24.163 35.259 1.00 41.44 C ANISOU 788 C GLY A 104 5361 5069 5314 219 512 -481 C ATOM 789 O GLY A 104 -3.808 23.712 36.253 1.00 41.32 O ANISOU 789 O GLY A 104 5299 5088 5311 213 511 -482 O ATOM 790 N ASN A 105 -2.550 23.391 34.399 1.00 38.45 N ANISOU 790 N ASN A 105 4997 4689 4922 200 483 -475 N ATOM 791 CA ASN A 105 -2.428 21.961 34.614 1.00 35.71 C ANISOU 791 CA ASN A 105 4613 4380 4574 171 449 -470 C ATOM 792 C ASN A 105 -1.090 21.628 35.274 1.00 34.81 C ANISOU 792 C ASN A 105 4505 4274 4446 128 468 -496 C ATOM 793 O ASN A 105 -0.106 21.315 34.606 1.00 33.52 O ANISOU 793 O ASN A 105 4368 4098 4270 108 462 -502 O ATOM 794 CB ASN A 105 -2.622 21.155 33.311 1.00 35.28 C ANISOU 794 CB ASN A 105 4565 4324 4515 177 402 -448 C ATOM 795 CG ASN A 105 -2.571 19.670 33.550 1.00 31.72 C ANISOU 795 CG ASN A 105 4077 3909 4065 148 371 -443 C ATOM 796 OD1 ASN A 105 -2.864 19.216 34.644 1.00 30.92 O ANISOU 796 OD1 ASN A 105 3938 3838 3973 135 378 -448 O ATOM 797 ND2 ASN A 105 -2.178 18.908 32.546 1.00 29.42 N ANISOU 797 ND2 ASN A 105 3802 3612 3763 137 342 -434 N ATOM 798 N THR A 106 -1.086 21.695 36.601 1.00 33.88 N ANISOU 798 N THR A 106 4362 4179 4329 115 490 -513 N ATOM 799 CA THR A 106 0.106 21.433 37.384 1.00 32.65 C ANISOU 799 CA THR A 106 4208 4039 4159 80 505 -541 C ATOM 800 C THR A 106 0.011 20.100 38.129 1.00 31.82 C ANISOU 800 C THR A 106 4064 3977 4050 63 481 -533 C ATOM 801 O THR A 106 1.037 19.595 38.590 1.00 30.56 O ANISOU 801 O THR A 106 3904 3833 3875 37 480 -549 O ATOM 802 CB THR A 106 0.374 22.565 38.383 1.00 32.81 C ANISOU 802 CB THR A 106 4238 4052 4176 76 551 -571 C ATOM 803 OG1 THR A 106 -0.758 22.720 39.229 1.00 32.62 O ANISOU 803 OG1 THR A 106 4186 4045 4163 95 560 -563 O ATOM 804 CG2 THR A 106 0.616 23.871 37.658 1.00 34.11 C ANISOU 804 CG2 THR A 106 4448 4169 4344 88 582 -581 C ATOM 805 N ASP A 107 -1.209 19.548 38.246 1.00 31.40 N ANISOU 805 N ASP A 107 3980 3941 4011 78 463 -509 N ATOM 806 CA ASP A 107 -1.392 18.208 38.790 1.00 30.99 C ANISOU 806 CA ASP A 107 3896 3923 3957 63 443 -497 C ATOM 807 C ASP A 107 -1.016 17.100 37.781 1.00 30.75 C ANISOU 807 C ASP A 107 3870 3890 3922 50 407 -482 C ATOM 808 O ASP A 107 -1.879 16.391 37.231 1.00 30.91 O ANISOU 808 O ASP A 107 3871 3916 3956 57 380 -460 O ATOM 809 CB ASP A 107 -2.797 18.013 39.346 1.00 31.33 C ANISOU 809 CB ASP A 107 3902 3983 4020 78 445 -482 C ATOM 810 CG ASP A 107 -2.916 16.759 40.205 1.00 32.42 C ANISOU 810 CG ASP A 107 4014 4152 4152 59 440 -475 C ATOM 811 OD1 ASP A 107 -1.911 16.029 40.334 1.00 33.12 O ANISOU 811 OD1 ASP A 107 4115 4249 4220 38 431 -479 O ATOM 812 OD2 ASP A 107 -4.010 16.484 40.748 1.00 33.10 O ANISOU 812 OD2 ASP A 107 4069 4252 4254 66 447 -464 O ATOM 813 N VAL A 108 0.286 16.921 37.587 1.00 30.07 N ANISOU 813 N VAL A 108 3807 3800 3820 31 407 -496 N ATOM 814 CA VAL A 108 0.804 16.021 36.563 1.00 30.07 C ANISOU 814 CA VAL A 108 3818 3791 3815 20 379 -485 C ATOM 815 C VAL A 108 1.885 15.116 37.185 1.00 30.18 C ANISOU 815 C VAL A 108 3828 3827 3812 -3 377 -495 C ATOM 816 O VAL A 108 2.815 15.612 37.803 1.00 31.92 O ANISOU 816 O VAL A 108 4056 4052 4021 -12 396 -520 O ATOM 817 CB VAL A 108 1.355 16.848 35.383 1.00 30.04 C ANISOU 817 CB VAL A 108 3854 3751 3809 26 383 -492 C ATOM 818 CG1 VAL A 108 2.066 15.973 34.330 1.00 31.11 C ANISOU 818 CG1 VAL A 108 4008 3876 3937 12 360 -484 C ATOM 819 CG2 VAL A 108 0.218 17.648 34.742 1.00 30.27 C ANISOU 819 CG2 VAL A 108 3889 3761 3851 56 380 -477 C ATOM 820 N GLU A 109 1.745 13.805 37.052 1.00 28.09 N ANISOU 820 N GLU A 109 3551 3575 3547 -11 354 -476 N ATOM 821 CA GLU A 109 2.778 12.897 37.502 1.00 27.74 C ANISOU 821 CA GLU A 109 3507 3547 3486 -26 350 -482 C ATOM 822 C GLU A 109 3.981 12.799 36.542 1.00 26.81 C ANISOU 822 C GLU A 109 3414 3410 3363 -37 343 -492 C ATOM 823 O GLU A 109 3.924 13.283 35.409 1.00 26.18 O ANISOU 823 O GLU A 109 3355 3302 3290 -34 340 -490 O ATOM 824 CB GLU A 109 2.167 11.509 37.789 1.00 27.49 C ANISOU 824 CB GLU A 109 3457 3531 3455 -31 334 -457 C ATOM 825 CG GLU A 109 1.278 11.529 39.034 1.00 29.04 C ANISOU 825 CG GLU A 109 3631 3750 3653 -25 350 -453 C ATOM 826 CD GLU A 109 0.867 10.162 39.508 1.00 30.88 C ANISOU 826 CD GLU A 109 3851 3998 3884 -32 345 -432 C ATOM 827 OE1 GLU A 109 1.324 9.115 38.952 1.00 26.80 O ANISOU 827 OE1 GLU A 109 3344 3475 3363 -41 329 -421 O ATOM 828 OE2 GLU A 109 0.064 10.138 40.462 1.00 32.23 O ANISOU 828 OE2 GLU A 109 4005 4183 4057 -28 362 -427 O ATOM 829 N GLY A 110 5.071 12.217 37.040 1.00 26.56 N ANISOU 829 N GLY A 110 3379 3395 3317 -47 343 -503 N ATOM 830 CA GLY A 110 6.243 11.863 36.217 1.00 27.28 C ANISOU 830 CA GLY A 110 3487 3472 3405 -57 337 -512 C ATOM 831 C GLY A 110 7.474 12.720 36.482 1.00 27.46 C ANISOU 831 C GLY A 110 3514 3496 3423 -66 357 -549 C ATOM 832 O GLY A 110 7.361 13.885 36.923 1.00 26.73 O ANISOU 832 O GLY A 110 3422 3401 3331 -65 378 -569 O ATOM 833 N VAL A 111 8.649 12.105 36.300 1.00 27.18 N ANISOU 833 N VAL A 111 3479 3465 3382 -74 352 -560 N ATOM 834 CA VAL A 111 9.914 12.838 36.298 1.00 28.01 C ANISOU 834 CA VAL A 111 3585 3568 3488 -87 371 -599 C ATOM 835 C VAL A 111 10.771 12.365 35.104 1.00 28.64 C ANISOU 835 C VAL A 111 3682 3625 3576 -96 370 -600 C ATOM 836 O VAL A 111 10.218 11.923 34.080 1.00 27.74 O ANISOU 836 O VAL A 111 3589 3484 3466 -94 360 -574 O ATOM 837 CB VAL A 111 10.662 12.772 37.698 1.00 28.09 C ANISOU 837 CB VAL A 111 3566 3622 3483 -87 369 -625 C ATOM 838 CG1 VAL A 111 9.813 13.383 38.784 1.00 27.05 C ANISOU 838 CG1 VAL A 111 3426 3508 3343 -79 376 -627 C ATOM 839 CG2 VAL A 111 11.081 11.340 38.081 1.00 28.08 C ANISOU 839 CG2 VAL A 111 3552 3648 3470 -77 344 -609 C ATOM 840 N ASP A 112 12.097 12.442 35.245 1.00 28.97 N ANISOU 840 N ASP A 112 3712 3675 3619 -107 379 -633 N ATOM 841 CA ASP A 112 13.043 11.875 34.274 1.00 29.32 C ANISOU 841 CA ASP A 112 3767 3702 3672 -116 381 -637 C ATOM 842 C ASP A 112 13.408 10.414 34.575 1.00 29.53 C ANISOU 842 C ASP A 112 3777 3754 3691 -105 356 -620 C ATOM 843 O ASP A 112 13.637 10.047 35.737 1.00 30.01 O ANISOU 843 O ASP A 112 3810 3854 3739 -95 343 -625 O ATOM 844 CB ASP A 112 14.337 12.675 34.266 1.00 29.98 C ANISOU 844 CB ASP A 112 3841 3783 3765 -134 408 -685 C ATOM 845 CG ASP A 112 14.176 14.073 33.689 1.00 31.68 C ANISOU 845 CG ASP A 112 4085 3962 3991 -147 442 -703 C ATOM 846 OD1 ASP A 112 13.048 14.488 33.345 1.00 32.73 O ANISOU 846 OD1 ASP A 112 4243 4072 4121 -138 443 -678 O ATOM 847 OD2 ASP A 112 15.202 14.763 33.591 1.00 36.60 O ANISOU 847 OD2 ASP A 112 4703 4576 4625 -167 470 -744 O ATOM 848 N SER A 113 13.474 9.595 33.531 1.00 29.62 N ANISOU 848 N SER A 113 3809 3740 3707 -106 351 -599 N ATOM 849 CA SER A 113 14.066 8.267 33.624 1.00 30.96 C ANISOU 849 CA SER A 113 3968 3924 3873 -97 335 -588 C ATOM 850 C SER A 113 15.433 8.279 32.972 1.00 32.09 C ANISOU 850 C SER A 113 4109 4056 4029 -107 352 -616 C ATOM 851 O SER A 113 15.618 8.846 31.876 1.00 32.20 O ANISOU 851 O SER A 113 4149 4032 4054 -123 373 -625 O ATOM 852 CB SER A 113 13.202 7.223 32.931 1.00 30.60 C ANISOU 852 CB SER A 113 3945 3858 3824 -93 321 -547 C ATOM 853 OG SER A 113 12.006 7.083 33.659 1.00 31.55 O ANISOU 853 OG SER A 113 4059 3994 3935 -85 307 -524 O ATOM 854 N THR A 114 16.381 7.613 33.629 1.00 32.40 N ANISOU 854 N THR A 114 4119 4126 4065 -96 342 -628 N ATOM 855 CA THR A 114 17.725 7.484 33.077 1.00 33.29 C ANISOU 855 CA THR A 114 4222 4234 4194 -103 357 -655 C ATOM 856 C THR A 114 18.369 6.099 33.189 1.00 32.56 C ANISOU 856 C THR A 114 4117 4155 4098 -83 341 -642 C ATOM 857 O THR A 114 18.440 5.505 34.268 1.00 32.27 O ANISOU 857 O THR A 114 4057 4158 4046 -60 318 -634 O ATOM 858 CB THR A 114 18.666 8.491 33.727 1.00 34.05 C ANISOU 858 CB THR A 114 4283 4355 4298 -113 369 -707 C ATOM 859 OG1 THR A 114 17.954 9.724 33.935 1.00 37.97 O ANISOU 859 OG1 THR A 114 4790 4843 4793 -127 383 -717 O ATOM 860 CG2 THR A 114 19.867 8.745 32.824 1.00 34.50 C ANISOU 860 CG2 THR A 114 4338 4391 4381 -132 398 -740 C ATOM 861 N ASN A 115 18.779 5.586 32.035 1.00 31.72 N ANISOU 861 N ASN A 115 4033 4015 4005 -90 355 -636 N ATOM 862 CA ASN A 115 19.979 4.781 31.900 1.00 31.74 C ANISOU 862 CA ASN A 115 4016 4025 4018 -78 357 -648 C ATOM 863 C ASN A 115 20.325 4.819 30.433 1.00 31.80 C ANISOU 863 C ASN A 115 4056 3984 4043 -98 386 -652 C ATOM 864 O ASN A 115 19.648 4.180 29.628 1.00 31.89 O ANISOU 864 O ASN A 115 4106 3962 4047 -100 385 -619 O ATOM 865 CB ASN A 115 19.849 3.322 32.348 1.00 32.14 C ANISOU 865 CB ASN A 115 4067 4091 4055 -48 334 -612 C ATOM 866 CG ASN A 115 21.203 2.553 32.248 1.00 32.40 C ANISOU 866 CG ASN A 115 4076 4134 4100 -30 337 -627 C ATOM 867 OD1 ASN A 115 22.002 2.559 33.190 1.00 32.95 O ANISOU 867 OD1 ASN A 115 4103 4248 4168 -10 323 -650 O ATOM 868 ND2 ASN A 115 21.442 1.897 31.111 1.00 30.72 N ANISOU 868 ND2 ASN A 115 3891 3882 3899 -36 355 -616 N ATOM 869 N ALA A 116 21.376 5.571 30.110 1.00 31.37 N ANISOU 869 N ALA A 116 3985 3925 4010 -115 414 -695 N ATOM 870 CA ALA A 116 21.919 5.661 28.759 1.00 30.62 C ANISOU 870 CA ALA A 116 3919 3783 3932 -134 449 -706 C ATOM 871 C ALA A 116 20.777 5.749 27.719 1.00 29.22 C ANISOU 871 C ALA A 116 3804 3558 3741 -146 454 -672 C ATOM 872 O ALA A 116 19.793 6.494 27.906 1.00 28.58 O ANISOU 872 O ALA A 116 3737 3475 3648 -151 446 -662 O ATOM 873 CB ALA A 116 22.916 4.455 28.500 1.00 30.15 C ANISOU 873 CB ALA A 116 3845 3726 3885 -118 452 -706 C ATOM 874 N CYS A 117 20.867 4.992 26.649 1.00 27.59 N ANISOU 874 N CYS A 117 3632 3315 3534 -148 465 -655 N ATOM 875 CA CYS A 117 19.865 5.097 25.573 1.00 27.72 C ANISOU 875 CA CYS A 117 3708 3288 3536 -159 467 -628 C ATOM 876 C CYS A 117 18.504 4.412 25.894 1.00 26.37 C ANISOU 876 C CYS A 117 3548 3127 3343 -146 428 -587 C ATOM 877 O CYS A 117 17.613 4.368 25.036 1.00 25.99 O ANISOU 877 O CYS A 117 3543 3049 3282 -153 423 -565 O ATOM 878 CB CYS A 117 20.452 4.554 24.265 1.00 28.38 C ANISOU 878 CB CYS A 117 3830 3328 3625 -168 495 -629 C ATOM 879 SG CYS A 117 22.045 5.369 23.885 1.00 33.95 S ANISOU 879 SG CYS A 117 4520 4020 4361 -187 548 -681 S ATOM 880 N TYR A 118 18.343 3.918 27.123 1.00 23.47 N ANISOU 880 N TYR A 118 3142 2802 2973 -128 403 -578 N ATOM 881 CA TYR A 118 17.139 3.168 27.511 1.00 23.10 C ANISOU 881 CA TYR A 118 3102 2765 2910 -118 372 -541 C ATOM 882 C TYR A 118 16.096 4.034 28.246 1.00 21.71 C ANISOU 882 C TYR A 118 2915 2609 2725 -117 357 -536 C ATOM 883 O TYR A 118 14.937 3.632 28.407 1.00 21.03 O ANISOU 883 O TYR A 118 2837 2526 2629 -114 336 -508 O ATOM 884 CB TYR A 118 17.550 1.932 28.348 1.00 22.27 C ANISOU 884 CB TYR A 118 2972 2687 2803 -96 359 -528 C ATOM 885 CG TYR A 118 16.422 1.046 28.783 1.00 23.96 C ANISOU 885 CG TYR A 118 3194 2907 3002 -87 336 -492 C ATOM 886 CD1 TYR A 118 15.891 0.044 27.925 1.00 17.97 C ANISOU 886 CD1 TYR A 118 2472 2117 2240 -95 334 -467 C ATOM 887 CD2 TYR A 118 15.875 1.175 30.084 1.00 25.06 C ANISOU 887 CD2 TYR A 118 3306 3084 3132 -74 318 -484 C ATOM 888 CE1 TYR A 118 14.842 -0.781 28.368 1.00 20.18 C ANISOU 888 CE1 TYR A 118 2756 2401 2509 -91 317 -437 C ATOM 889 CE2 TYR A 118 14.832 0.340 30.524 1.00 22.45 C ANISOU 889 CE2 TYR A 118 2983 2757 2790 -69 303 -452 C ATOM 890 CZ TYR A 118 14.333 -0.627 29.659 1.00 24.07 C ANISOU 890 CZ TYR A 118 3221 2929 2995 -78 304 -430 C ATOM 891 OH TYR A 118 13.302 -1.425 30.107 1.00 26.87 O ANISOU 891 OH TYR A 118 3582 3286 3342 -78 294 -402 O ATOM 892 N GLY A 119 16.505 5.228 28.689 1.00 21.80 N ANISOU 892 N GLY A 119 2907 2634 2743 -122 370 -565 N ATOM 893 CA GLY A 119 15.613 6.125 29.444 1.00 21.49 C ANISOU 893 CA GLY A 119 2856 2613 2697 -121 360 -565 C ATOM 894 C GLY A 119 14.262 6.412 28.820 1.00 20.93 C ANISOU 894 C GLY A 119 2817 2518 2618 -124 351 -540 C ATOM 895 O GLY A 119 13.273 6.532 29.534 1.00 21.23 O ANISOU 895 O GLY A 119 2842 2575 2650 -117 334 -525 O ATOM 896 N GLY A 120 14.205 6.529 27.487 1.00 20.93 N ANISOU 896 N GLY A 120 2858 2478 2618 -134 361 -536 N ATOM 897 CA GLY A 120 12.928 6.815 26.809 1.00 20.57 C ANISOU 897 CA GLY A 120 2843 2411 2561 -134 347 -514 C ATOM 898 C GLY A 120 11.962 5.627 26.886 1.00 19.87 C ANISOU 898 C GLY A 120 2751 2333 2467 -130 317 -483 C ATOM 899 O GLY A 120 10.768 5.796 27.136 1.00 20.51 O ANISOU 899 O GLY A 120 2826 2423 2544 -125 297 -467 O ATOM 900 N THR A 121 12.481 4.424 26.644 1.00 19.13 N ANISOU 900 N THR A 121 2662 2233 2372 -132 316 -476 N ATOM 901 CA THR A 121 11.734 3.192 26.900 1.00 18.73 C ANISOU 901 CA THR A 121 2606 2193 2319 -131 294 -451 C ATOM 902 C THR A 121 11.206 3.067 28.338 1.00 18.92 C ANISOU 902 C THR A 121 2592 2255 2343 -120 283 -442 C ATOM 903 O THR A 121 10.012 2.770 28.528 1.00 18.83 O ANISOU 903 O THR A 121 2576 2249 2330 -121 267 -424 O ATOM 904 CB THR A 121 12.594 1.955 26.529 1.00 19.70 C ANISOU 904 CB THR A 121 2741 2301 2442 -132 303 -447 C ATOM 905 OG1 THR A 121 13.054 2.145 25.189 1.00 19.01 O ANISOU 905 OG1 THR A 121 2693 2177 2353 -143 317 -456 O ATOM 906 CG2 THR A 121 11.777 0.632 26.603 1.00 15.83 C ANISOU 906 CG2 THR A 121 2256 1811 1948 -135 287 -421 C ATOM 907 N ALA A 122 12.092 3.263 29.335 1.00 18.21 N ANISOU 907 N ALA A 122 2474 2190 2255 -109 293 -457 N ATOM 908 CA ALA A 122 11.682 3.161 30.735 1.00 18.95 C ANISOU 908 CA ALA A 122 2537 2321 2344 -96 285 -450 C ATOM 909 C ALA A 122 10.495 4.087 31.013 1.00 18.72 C ANISOU 909 C ALA A 122 2500 2298 2315 -98 278 -447 C ATOM 910 O ALA A 122 9.538 3.701 31.717 1.00 19.73 O ANISOU 910 O ALA A 122 2614 2441 2439 -95 268 -429 O ATOM 911 CB ALA A 122 12.852 3.483 31.705 1.00 18.08 C ANISOU 911 CB ALA A 122 2398 2240 2232 -84 293 -473 C ATOM 912 N ALA A 123 10.572 5.307 30.490 1.00 17.47 N ANISOU 912 N ALA A 123 2351 2127 2161 -103 287 -465 N ATOM 913 CA ALA A 123 9.477 6.263 30.649 1.00 18.12 C ANISOU 913 CA ALA A 123 2429 2211 2244 -101 282 -462 C ATOM 914 C ALA A 123 8.175 5.807 29.972 1.00 18.73 C ANISOU 914 C ALA A 123 2518 2275 2322 -104 263 -437 C ATOM 915 O ALA A 123 7.052 6.026 30.495 1.00 18.05 O ANISOU 915 O ALA A 123 2414 2204 2240 -99 253 -427 O ATOM 916 CB ALA A 123 9.867 7.664 30.154 1.00 16.95 C ANISOU 916 CB ALA A 123 2296 2046 2099 -104 300 -484 C ATOM 917 N LEU A 124 8.325 5.241 28.777 1.00 18.59 N ANISOU 917 N LEU A 124 2530 2230 2302 -113 257 -432 N ATOM 918 CA LEU A 124 7.195 4.805 27.971 1.00 19.00 C ANISOU 918 CA LEU A 124 2595 2270 2354 -118 235 -414 C ATOM 919 C LEU A 124 6.433 3.707 28.688 1.00 19.43 C ANISOU 919 C LEU A 124 2626 2344 2414 -123 224 -398 C ATOM 920 O LEU A 124 5.205 3.735 28.776 1.00 20.19 O ANISOU 920 O LEU A 124 2706 2448 2515 -124 209 -388 O ATOM 921 CB LEU A 124 7.687 4.362 26.575 1.00 17.75 C ANISOU 921 CB LEU A 124 2478 2078 2188 -128 234 -415 C ATOM 922 CG LEU A 124 6.669 3.728 25.611 1.00 20.48 C ANISOU 922 CG LEU A 124 2841 2411 2530 -137 208 -402 C ATOM 923 CD1 LEU A 124 5.553 4.723 25.293 1.00 21.31 C ANISOU 923 CD1 LEU A 124 2945 2520 2634 -126 189 -399 C ATOM 924 CD2 LEU A 124 7.360 3.210 24.336 1.00 19.52 C ANISOU 924 CD2 LEU A 124 2765 2257 2397 -148 212 -405 C ATOM 925 N LEU A 125 7.183 2.753 29.215 1.00 20.31 N ANISOU 925 N LEU A 125 2734 2461 2523 -124 234 -394 N ATOM 926 CA LEU A 125 6.617 1.649 29.951 1.00 20.28 C ANISOU 926 CA LEU A 125 2715 2470 2521 -127 233 -377 C ATOM 927 C LEU A 125 5.979 2.114 31.265 1.00 20.00 C ANISOU 927 C LEU A 125 2647 2464 2488 -118 237 -375 C ATOM 928 O LEU A 125 4.923 1.628 31.635 1.00 19.74 O ANISOU 928 O LEU A 125 2600 2439 2462 -124 233 -362 O ATOM 929 CB LEU A 125 7.683 0.587 30.212 1.00 20.22 C ANISOU 929 CB LEU A 125 2716 2458 2507 -124 245 -373 C ATOM 930 CG LEU A 125 8.381 -0.068 29.003 1.00 23.55 C ANISOU 930 CG LEU A 125 3171 2849 2928 -134 247 -375 C ATOM 931 CD1 LEU A 125 9.254 -1.228 29.496 1.00 22.57 C ANISOU 931 CD1 LEU A 125 3051 2724 2800 -125 261 -367 C ATOM 932 CD2 LEU A 125 7.382 -0.541 27.918 1.00 24.51 C ANISOU 932 CD2 LEU A 125 3313 2948 3052 -154 232 -368 C ATOM 933 N ASN A 126 6.612 3.048 31.972 1.00 19.55 N ANISOU 933 N ASN A 126 2578 2424 2426 -105 246 -389 N ATOM 934 CA ASN A 126 6.026 3.587 33.211 1.00 19.34 C ANISOU 934 CA ASN A 126 2525 2425 2399 -95 252 -389 C ATOM 935 C ASN A 126 4.685 4.245 32.911 1.00 19.88 C ANISOU 935 C ASN A 126 2582 2491 2480 -98 243 -386 C ATOM 936 O ASN A 126 3.750 4.212 33.707 1.00 19.10 O ANISOU 936 O ASN A 126 2461 2408 2386 -97 247 -378 O ATOM 937 CB ASN A 126 6.965 4.650 33.819 1.00 19.99 C ANISOU 937 CB ASN A 126 2599 2522 2474 -84 263 -412 C ATOM 938 CG ASN A 126 8.145 4.046 34.529 1.00 20.09 C ANISOU 938 CG ASN A 126 2610 2551 2474 -75 269 -417 C ATOM 939 OD1 ASN A 126 8.078 2.916 35.001 1.00 22.34 O ANISOU 939 OD1 ASN A 126 2895 2842 2752 -70 269 -399 O ATOM 940 ND2 ASN A 126 9.222 4.803 34.640 1.00 21.91 N ANISOU 940 ND2 ASN A 126 2835 2788 2701 -71 276 -443 N ATOM 941 N CYS A 127 4.603 4.886 31.764 1.00 20.02 N ANISOU 941 N CYS A 127 2616 2488 2501 -100 233 -393 N ATOM 942 CA CYS A 127 3.409 5.632 31.410 1.00 21.18 C ANISOU 942 CA CYS A 127 2754 2635 2659 -96 222 -390 C ATOM 943 C CYS A 127 2.299 4.686 31.000 1.00 20.13 C ANISOU 943 C CYS A 127 2611 2501 2536 -108 204 -376 C ATOM 944 O CYS A 127 1.152 4.877 31.356 1.00 19.97 O ANISOU 944 O CYS A 127 2564 2494 2528 -106 198 -372 O ATOM 945 CB CYS A 127 3.732 6.489 30.224 1.00 22.02 C ANISOU 945 CB CYS A 127 2889 2717 2760 -91 216 -399 C ATOM 946 SG CYS A 127 3.159 8.116 30.352 1.00 34.80 S ANISOU 946 SG CYS A 127 4503 4337 4384 -72 221 -408 S ATOM 947 N VAL A 128 2.642 3.659 30.225 1.00 18.64 N ANISOU 947 N VAL A 128 2444 2295 2343 -122 196 -371 N ATOM 948 CA VAL A 128 1.657 2.633 29.915 1.00 18.37 C ANISOU 948 CA VAL A 128 2400 2261 2320 -140 182 -362 C ATOM 949 C VAL A 128 1.185 2.015 31.238 1.00 18.13 C ANISOU 949 C VAL A 128 2342 2250 2298 -144 200 -353 C ATOM 950 O VAL A 128 -0.001 1.886 31.455 1.00 17.91 O ANISOU 950 O VAL A 128 2287 2233 2287 -151 196 -351 O ATOM 951 CB VAL A 128 2.245 1.550 28.968 1.00 18.04 C ANISOU 951 CB VAL A 128 2390 2194 2270 -156 177 -360 C ATOM 952 CG1 VAL A 128 1.347 0.362 28.909 1.00 19.51 C ANISOU 952 CG1 VAL A 128 2566 2380 2468 -179 171 -353 C ATOM 953 CG2 VAL A 128 2.441 2.150 27.574 1.00 16.28 C ANISOU 953 CG2 VAL A 128 2198 1951 2037 -153 158 -368 C ATOM 954 N ASN A 129 2.108 1.635 32.124 1.00 17.10 N ANISOU 954 N ASN A 129 2218 2124 2155 -138 221 -349 N ATOM 955 CA ASN A 129 1.674 1.025 33.396 1.00 17.05 C ANISOU 955 CA ASN A 129 2194 2133 2151 -140 242 -338 C ATOM 956 C ASN A 129 0.778 2.012 34.188 1.00 17.63 C ANISOU 956 C ASN A 129 2235 2228 2234 -130 247 -342 C ATOM 957 O ASN A 129 -0.202 1.596 34.830 1.00 17.37 O ANISOU 957 O ASN A 129 2181 2205 2214 -138 259 -335 O ATOM 958 CB ASN A 129 2.883 0.603 34.229 1.00 15.62 C ANISOU 958 CB ASN A 129 2027 1957 1950 -127 259 -334 C ATOM 959 CG ASN A 129 3.695 -0.470 33.565 1.00 18.55 C ANISOU 959 CG ASN A 129 2427 2306 2314 -133 258 -328 C ATOM 960 OD1 ASN A 129 3.224 -1.136 32.638 1.00 17.54 O ANISOU 960 OD1 ASN A 129 2309 2158 2196 -153 250 -325 O ATOM 961 ND2 ASN A 129 4.948 -0.628 33.999 1.00 15.56 N ANISOU 961 ND2 ASN A 129 2062 1933 1920 -116 266 -329 N ATOM 962 N TRP A 130 1.091 3.309 34.124 1.00 16.51 N ANISOU 962 N TRP A 130 2092 2092 2088 -114 243 -355 N ATOM 963 CA TRP A 130 0.278 4.304 34.852 1.00 17.97 C ANISOU 963 CA TRP A 130 2250 2295 2283 -102 251 -360 C ATOM 964 C TRP A 130 -1.196 4.313 34.365 1.00 19.79 C ANISOU 964 C TRP A 130 2454 2527 2539 -110 237 -357 C ATOM 965 O TRP A 130 -2.126 4.266 35.191 1.00 20.45 O ANISOU 965 O TRP A 130 2508 2625 2636 -111 252 -354 O ATOM 966 CB TRP A 130 0.900 5.695 34.772 1.00 17.98 C ANISOU 966 CB TRP A 130 2259 2296 2276 -85 252 -375 C ATOM 967 CG TRP A 130 -0.052 6.810 35.260 1.00 17.58 C ANISOU 967 CG TRP A 130 2184 2257 2237 -72 259 -381 C ATOM 968 CD1 TRP A 130 -0.376 7.101 36.557 1.00 16.35 C ANISOU 968 CD1 TRP A 130 2011 2121 2082 -66 282 -382 C ATOM 969 CD2 TRP A 130 -0.776 7.758 34.435 1.00 17.11 C ANISOU 969 CD2 TRP A 130 2120 2189 2192 -61 245 -384 C ATOM 970 NE1 TRP A 130 -1.251 8.192 36.594 1.00 17.84 N ANISOU 970 NE1 TRP A 130 2181 2313 2285 -52 285 -388 N ATOM 971 CE2 TRP A 130 -1.516 8.603 35.312 1.00 17.48 C ANISOU 971 CE2 TRP A 130 2142 2250 2248 -47 261 -388 C ATOM 972 CE3 TRP A 130 -0.874 7.967 33.043 1.00 17.08 C ANISOU 972 CE3 TRP A 130 2133 2166 2190 -58 219 -384 C ATOM 973 CZ2 TRP A 130 -2.354 9.646 34.841 1.00 19.55 C ANISOU 973 CZ2 TRP A 130 2394 2509 2526 -28 254 -391 C ATOM 974 CZ3 TRP A 130 -1.701 9.004 32.569 1.00 18.25 C ANISOU 974 CZ3 TRP A 130 2274 2312 2349 -38 209 -386 C ATOM 975 CH2 TRP A 130 -2.426 9.840 33.471 1.00 18.11 C ANISOU 975 CH2 TRP A 130 2229 2308 2344 -22 226 -389 C ATOM 976 N VAL A 131 -1.393 4.325 33.044 1.00 20.65 N ANISOU 976 N VAL A 131 2572 2621 2653 -114 210 -360 N ATOM 977 CA VAL A 131 -2.722 4.203 32.415 1.00 21.31 C ANISOU 977 CA VAL A 131 2629 2708 2758 -121 189 -360 C ATOM 978 C VAL A 131 -3.487 2.972 32.862 1.00 21.50 C ANISOU 978 C VAL A 131 2630 2738 2799 -146 199 -355 C ATOM 979 O VAL A 131 -4.687 3.065 33.127 1.00 22.86 O ANISOU 979 O VAL A 131 2764 2925 2996 -149 199 -358 O ATOM 980 CB VAL A 131 -2.681 4.291 30.843 1.00 20.96 C ANISOU 980 CB VAL A 131 2607 2648 2709 -121 153 -365 C ATOM 981 CG1 VAL A 131 -4.119 4.219 30.249 1.00 20.24 C ANISOU 981 CG1 VAL A 131 2482 2567 2640 -125 125 -369 C ATOM 982 CG2 VAL A 131 -2.035 5.597 30.371 1.00 21.58 C ANISOU 982 CG2 VAL A 131 2712 2716 2773 -96 149 -370 C ATOM 983 N GLU A 132 -2.803 1.828 32.961 1.00 21.51 N ANISOU 983 N GLU A 132 2656 2728 2790 -163 211 -348 N ATOM 984 CA GLU A 132 -3.416 0.562 33.435 1.00 21.51 C ANISOU 984 CA GLU A 132 2643 2726 2803 -189 230 -341 C ATOM 985 C GLU A 132 -3.571 0.435 34.937 1.00 22.48 C ANISOU 985 C GLU A 132 2755 2861 2926 -185 268 -333 C ATOM 986 O GLU A 132 -4.128 -0.551 35.403 1.00 22.84 O ANISOU 986 O GLU A 132 2793 2903 2983 -206 291 -327 O ATOM 987 CB GLU A 132 -2.573 -0.631 32.935 1.00 20.77 C ANISOU 987 CB GLU A 132 2588 2609 2696 -205 232 -335 C ATOM 988 CG GLU A 132 -2.553 -0.665 31.406 1.00 21.53 C ANISOU 988 CG GLU A 132 2699 2691 2791 -214 197 -344 C ATOM 989 CD GLU A 132 -1.715 -1.770 30.808 1.00 21.83 C ANISOU 989 CD GLU A 132 2776 2704 2816 -230 200 -340 C ATOM 990 OE1 GLU A 132 -1.923 -2.068 29.602 1.00 24.16 O ANISOU 990 OE1 GLU A 132 3082 2986 3112 -245 175 -349 O ATOM 991 OE2 GLU A 132 -0.859 -2.331 31.537 1.00 24.03 O ANISOU 991 OE2 GLU A 132 3075 2975 3081 -224 227 -328 O ATOM 992 N SER A 133 -3.094 1.422 35.709 1.00 21.59 N ANISOU 992 N SER A 133 2643 2761 2799 -160 278 -333 N ATOM 993 CA SER A 133 -3.021 1.295 37.171 1.00 21.86 C ANISOU 993 CA SER A 133 2677 2807 2823 -153 314 -325 C ATOM 994 C SER A 133 -4.302 1.799 37.849 1.00 22.69 C ANISOU 994 C SER A 133 2742 2928 2951 -154 331 -329 C ATOM 995 O SER A 133 -5.147 2.460 37.211 1.00 22.63 O ANISOU 995 O SER A 133 2705 2926 2968 -152 312 -340 O ATOM 996 CB SER A 133 -1.787 2.064 37.729 1.00 21.02 C ANISOU 996 CB SER A 133 2592 2708 2686 -127 316 -328 C ATOM 997 OG SER A 133 -2.050 3.458 37.709 1.00 21.30 O ANISOU 997 OG SER A 133 2611 2755 2728 -112 309 -341 O ATOM 998 N ASN A 134 -4.446 1.476 39.137 1.00 22.85 N ANISOU 998 N ASN A 134 2764 2954 2963 -153 368 -321 N ATOM 999 CA ASN A 134 -5.556 1.982 39.938 1.00 24.42 C ANISOU 999 CA ASN A 134 2929 3168 3183 -152 393 -325 C ATOM 1000 C ASN A 134 -5.531 3.469 40.125 1.00 24.60 C ANISOU 1000 C ASN A 134 2938 3204 3203 -126 386 -336 C ATOM 1001 O ASN A 134 -6.583 4.033 40.357 1.00 24.48 O ANISOU 1001 O ASN A 134 2889 3200 3214 -124 396 -343 O ATOM 1002 CB ASN A 134 -5.644 1.307 41.315 1.00 25.59 C ANISOU 1002 CB ASN A 134 3091 3316 3316 -155 439 -312 C ATOM 1003 CG ASN A 134 -6.085 -0.142 41.217 1.00 30.03 C ANISOU 1003 CG ASN A 134 3659 3861 3892 -185 459 -302 C ATOM 1004 OD1 ASN A 134 -6.679 -0.520 40.223 1.00 37.38 O ANISOU 1004 OD1 ASN A 134 4567 4783 4851 -207 441 -310 O ATOM 1005 ND2 ASN A 134 -5.791 -0.955 42.233 1.00 31.24 N ANISOU 1005 ND2 ASN A 134 3844 4006 4022 -185 497 -285 N ATOM 1006 N SER A 135 -4.345 4.088 40.018 1.00 22.81 N ANISOU 1006 N SER A 135 2740 2978 2948 -108 371 -340 N ATOM 1007 CA SER A 135 -4.193 5.548 40.140 1.00 23.22 C ANISOU 1007 CA SER A 135 2787 3039 2997 -85 367 -354 C ATOM 1008 C SER A 135 -4.523 6.357 38.876 1.00 23.26 C ANISOU 1008 C SER A 135 2779 3037 3021 -78 335 -363 C ATOM 1009 O SER A 135 -4.536 7.581 38.909 1.00 24.16 O ANISOU 1009 O SER A 135 2890 3153 3136 -58 336 -373 O ATOM 1010 CB SER A 135 -2.787 5.898 40.578 1.00 22.01 C ANISOU 1010 CB SER A 135 2667 2889 2807 -72 368 -359 C ATOM 1011 OG SER A 135 -1.904 5.829 39.463 1.00 23.71 O ANISOU 1011 OG SER A 135 2902 3091 3016 -74 339 -362 O ATOM 1012 N TRP A 136 -4.833 5.699 37.768 1.00 23.11 N ANISOU 1012 N TRP A 136 2755 3007 3016 -92 309 -359 N ATOM 1013 CA TRP A 136 -5.113 6.427 36.545 1.00 22.82 C ANISOU 1013 CA TRP A 136 2714 2965 2992 -81 276 -366 C ATOM 1014 C TRP A 136 -6.318 7.342 36.731 1.00 24.24 C ANISOU 1014 C TRP A 136 2855 3157 3198 -64 280 -372 C ATOM 1015 O TRP A 136 -7.321 6.940 37.295 1.00 24.17 O ANISOU 1015 O TRP A 136 2811 3160 3213 -74 296 -371 O ATOM 1016 CB TRP A 136 -5.301 5.459 35.362 1.00 22.56 C ANISOU 1016 CB TRP A 136 2683 2922 2967 -100 246 -363 C ATOM 1017 CG TRP A 136 -5.436 6.179 33.995 1.00 21.10 C ANISOU 1017 CG TRP A 136 2504 2728 2784 -86 208 -369 C ATOM 1018 CD1 TRP A 136 -4.635 7.147 33.503 1.00 20.64 C ANISOU 1018 CD1 TRP A 136 2478 2658 2708 -65 200 -372 C ATOM 1019 CD2 TRP A 136 -6.433 5.934 32.996 1.00 21.66 C ANISOU 1019 CD2 TRP A 136 2552 2803 2876 -90 175 -372 C ATOM 1020 NE1 TRP A 136 -5.079 7.548 32.253 1.00 21.03 N ANISOU 1020 NE1 TRP A 136 2529 2700 2760 -53 165 -374 N ATOM 1021 CE2 TRP A 136 -6.184 6.805 31.930 1.00 22.16 C ANISOU 1021 CE2 TRP A 136 2638 2856 2927 -67 146 -375 C ATOM 1022 CE3 TRP A 136 -7.534 5.060 32.914 1.00 25.38 C ANISOU 1022 CE3 TRP A 136 2984 3286 3375 -113 168 -376 C ATOM 1023 CZ2 TRP A 136 -6.976 6.825 30.781 1.00 23.97 C ANISOU 1023 CZ2 TRP A 136 2854 3088 3165 -61 105 -379 C ATOM 1024 CZ3 TRP A 136 -8.328 5.084 31.768 1.00 23.96 C ANISOU 1024 CZ3 TRP A 136 2784 3111 3208 -110 126 -384 C ATOM 1025 CH2 TRP A 136 -8.051 5.974 30.727 1.00 24.42 C ANISOU 1025 CH2 TRP A 136 2867 3161 3249 -83 93 -385 C ATOM 1026 N ASP A 137 -6.221 8.577 36.247 1.00 25.20 N ANISOU 1026 N ASP A 137 2984 3274 3318 -38 267 -378 N ATOM 1027 CA ASP A 137 -7.328 9.508 36.400 1.00 26.05 C ANISOU 1027 CA ASP A 137 3057 3391 3450 -16 271 -383 C ATOM 1028 C ASP A 137 -8.079 9.730 35.083 1.00 26.78 C ANISOU 1028 C ASP A 137 3133 3482 3560 -2 229 -383 C ATOM 1029 O ASP A 137 -8.885 10.651 34.990 1.00 26.69 O ANISOU 1029 O ASP A 137 3098 3477 3566 25 225 -386 O ATOM 1030 CB ASP A 137 -6.822 10.841 36.918 1.00 26.63 C ANISOU 1030 CB ASP A 137 3150 3458 3509 9 292 -389 C ATOM 1031 CG ASP A 137 -5.865 11.528 35.951 1.00 26.63 C ANISOU 1031 CG ASP A 137 3193 3438 3488 22 274 -392 C ATOM 1032 OD1 ASP A 137 -5.492 10.999 34.883 1.00 28.94 O ANISOU 1032 OD1 ASP A 137 3504 3719 3773 13 244 -388 O ATOM 1033 OD2 ASP A 137 -5.476 12.639 36.261 1.00 27.46 O ANISOU 1033 OD2 ASP A 137 3315 3534 3584 39 292 -400 O ATOM 1034 N GLY A 138 -7.809 8.902 34.075 1.00 25.48 N ANISOU 1034 N GLY A 138 2984 3311 3388 -19 198 -381 N ATOM 1035 CA GLY A 138 -8.553 8.991 32.830 1.00 26.41 C ANISOU 1035 CA GLY A 138 3088 3431 3518 -8 154 -383 C ATOM 1036 C GLY A 138 -7.902 9.922 31.804 1.00 26.41 C ANISOU 1036 C GLY A 138 3132 3410 3492 20 132 -380 C ATOM 1037 O GLY A 138 -8.392 10.019 30.689 1.00 27.43 O ANISOU 1037 O GLY A 138 3260 3539 3623 33 92 -380 O ATOM 1038 N ARG A 139 -6.798 10.588 32.161 1.00 25.13 N ANISOU 1038 N ARG A 139 3011 3230 3307 27 157 -380 N ATOM 1039 CA ARG A 139 -6.130 11.497 31.233 1.00 24.84 C ANISOU 1039 CA ARG A 139 3021 3169 3248 50 146 -379 C ATOM 1040 C ARG A 139 -4.988 10.796 30.447 1.00 23.79 C ANISOU 1040 C ARG A 139 2933 3016 3089 28 136 -378 C ATOM 1041 O ARG A 139 -4.572 9.695 30.785 1.00 23.35 O ANISOU 1041 O ARG A 139 2875 2965 3031 -2 142 -377 O ATOM 1042 CB ARG A 139 -5.574 12.726 31.967 1.00 24.46 C ANISOU 1042 CB ARG A 139 2993 3110 3192 69 183 -384 C ATOM 1043 CG ARG A 139 -6.583 13.696 32.602 1.00 27.60 C ANISOU 1043 CG ARG A 139 3358 3518 3612 98 198 -385 C ATOM 1044 CD ARG A 139 -6.030 14.136 33.974 1.00 28.29 C ANISOU 1044 CD ARG A 139 3448 3608 3695 91 245 -394 C ATOM 1045 NE ARG A 139 -5.588 15.483 33.947 1.00 29.95 N ANISOU 1045 NE ARG A 139 3690 3796 3895 115 266 -400 N ATOM 1046 CZ ARG A 139 -4.723 16.053 34.772 1.00 27.43 C ANISOU 1046 CZ ARG A 139 3391 3468 3562 107 303 -414 C ATOM 1047 NH1 ARG A 139 -4.131 15.405 35.756 1.00 24.70 N ANISOU 1047 NH1 ARG A 139 3038 3138 3208 80 321 -421 N ATOM 1048 NH2 ARG A 139 -4.462 17.327 34.569 1.00 29.92 N ANISOU 1048 NH2 ARG A 139 3737 3759 3871 130 322 -420 N ATOM 1049 N TYR A 140 -4.482 11.480 29.426 1.00 22.97 N ANISOU 1049 N TYR A 140 2874 2888 2966 46 124 -377 N ATOM 1050 CA TYR A 140 -3.372 11.037 28.620 1.00 23.29 C ANISOU 1050 CA TYR A 140 2962 2906 2982 30 120 -377 C ATOM 1051 C TYR A 140 -2.034 10.987 29.366 1.00 22.37 C ANISOU 1051 C TYR A 140 2865 2781 2855 11 157 -385 C ATOM 1052 O TYR A 140 -1.764 11.796 30.256 1.00 22.25 O ANISOU 1052 O TYR A 140 2845 2767 2841 20 187 -392 O ATOM 1053 CB TYR A 140 -3.208 11.964 27.421 1.00 24.25 C ANISOU 1053 CB TYR A 140 3130 3000 3083 57 107 -374 C ATOM 1054 CG TYR A 140 -4.377 11.976 26.461 1.00 25.75 C ANISOU 1054 CG TYR A 140 3309 3198 3275 80 61 -367 C ATOM 1055 CD1 TYR A 140 -4.980 13.181 26.099 1.00 27.90 C ANISOU 1055 CD1 TYR A 140 3591 3465 3546 123 53 -362 C ATOM 1056 CD2 TYR A 140 -4.912 10.800 25.963 1.00 26.64 C ANISOU 1056 CD2 TYR A 140 3401 3327 3393 59 26 -367 C ATOM 1057 CE1 TYR A 140 -6.064 13.216 25.239 1.00 28.85 C ANISOU 1057 CE1 TYR A 140 3699 3597 3667 150 6 -356 C ATOM 1058 CE2 TYR A 140 -5.999 10.819 25.080 1.00 28.83 C ANISOU 1058 CE2 TYR A 140 3664 3618 3672 80 -21 -365 C ATOM 1059 CZ TYR A 140 -6.553 12.043 24.720 1.00 28.95 C ANISOU 1059 CZ TYR A 140 3687 3629 3683 127 -33 -359 C ATOM 1060 OH TYR A 140 -7.620 12.121 23.871 1.00 29.54 O ANISOU 1060 OH TYR A 140 3747 3720 3757 154 -83 -358 O ATOM 1061 N GLY A 141 -1.191 10.032 29.001 1.00 21.33 N ANISOU 1061 N GLY A 141 2754 2640 2710 -13 155 -385 N ATOM 1062 CA GLY A 141 0.234 10.130 29.362 1.00 20.14 C ANISOU 1062 CA GLY A 141 2629 2477 2547 -24 185 -395 C ATOM 1063 C GLY A 141 0.978 10.749 28.213 1.00 20.12 C ANISOU 1063 C GLY A 141 2677 2442 2527 -17 186 -399 C ATOM 1064 O GLY A 141 0.549 10.631 27.081 1.00 20.32 O ANISOU 1064 O GLY A 141 2722 2454 2544 -10 160 -391 O ATOM 1065 N LEU A 142 2.095 11.418 28.494 1.00 20.90 N ANISOU 1065 N LEU A 142 2796 2526 2618 -19 218 -413 N ATOM 1066 CA LEU A 142 2.919 12.025 27.449 1.00 21.48 C ANISOU 1066 CA LEU A 142 2921 2565 2677 -17 230 -419 C ATOM 1067 C LEU A 142 4.382 11.716 27.706 1.00 21.11 C ANISOU 1067 C LEU A 142 2883 2511 2625 -39 256 -436 C ATOM 1068 O LEU A 142 4.933 12.033 28.764 1.00 20.38 O ANISOU 1068 O LEU A 142 2771 2433 2539 -44 279 -451 O ATOM 1069 CB LEU A 142 2.694 13.537 27.383 1.00 21.95 C ANISOU 1069 CB LEU A 142 3000 2606 2735 8 249 -424 C ATOM 1070 CG LEU A 142 3.393 14.384 26.320 1.00 23.66 C ANISOU 1070 CG LEU A 142 3275 2779 2935 15 269 -429 C ATOM 1071 CD1 LEU A 142 2.949 13.974 24.964 1.00 21.51 C ANISOU 1071 CD1 LEU A 142 3036 2490 2646 25 237 -413 C ATOM 1072 CD2 LEU A 142 3.111 15.898 26.592 1.00 23.46 C ANISOU 1072 CD2 LEU A 142 3264 2737 2912 39 295 -434 C ATOM 1073 N VAL A 143 5.008 11.058 26.749 1.00 20.35 N ANISOU 1073 N VAL A 143 2818 2396 2520 -51 251 -434 N ATOM 1074 CA VAL A 143 6.387 10.636 26.930 1.00 20.98 C ANISOU 1074 CA VAL A 143 2901 2471 2598 -70 274 -450 C ATOM 1075 C VAL A 143 7.240 11.452 25.968 1.00 21.47 C ANISOU 1075 C VAL A 143 3012 2494 2652 -71 301 -463 C ATOM 1076 O VAL A 143 6.891 11.583 24.781 1.00 22.23 O ANISOU 1076 O VAL A 143 3149 2562 2734 -63 290 -452 O ATOM 1077 CB VAL A 143 6.522 9.097 26.612 1.00 21.13 C ANISOU 1077 CB VAL A 143 2917 2495 2615 -85 254 -439 C ATOM 1078 CG1 VAL A 143 7.959 8.657 26.730 1.00 18.84 C ANISOU 1078 CG1 VAL A 143 2632 2201 2327 -99 277 -455 C ATOM 1079 CG2 VAL A 143 5.641 8.296 27.575 1.00 20.26 C ANISOU 1079 CG2 VAL A 143 2763 2419 2514 -85 235 -426 C ATOM 1080 N ILE A 144 8.350 11.976 26.463 1.00 21.48 N ANISOU 1080 N ILE A 144 3010 2492 2659 -82 335 -488 N ATOM 1081 CA ILE A 144 9.344 12.645 25.621 1.00 22.48 C ANISOU 1081 CA ILE A 144 3180 2580 2782 -90 370 -506 C ATOM 1082 C ILE A 144 10.648 11.876 25.675 1.00 22.54 C ANISOU 1082 C ILE A 144 3178 2591 2796 -111 385 -523 C ATOM 1083 O ILE A 144 11.112 11.512 26.758 1.00 23.27 O ANISOU 1083 O ILE A 144 3227 2716 2899 -118 385 -536 O ATOM 1084 CB ILE A 144 9.604 14.111 26.029 1.00 23.50 C ANISOU 1084 CB ILE A 144 3317 2696 2917 -88 407 -527 C ATOM 1085 CG1 ILE A 144 8.369 14.998 25.752 1.00 23.85 C ANISOU 1085 CG1 ILE A 144 3382 2727 2953 -61 397 -509 C ATOM 1086 CG2 ILE A 144 10.772 14.706 25.199 1.00 23.88 C ANISOU 1086 CG2 ILE A 144 3408 2701 2963 -103 451 -550 C ATOM 1087 CD1 ILE A 144 7.367 15.021 26.893 1.00 27.10 C ANISOU 1087 CD1 ILE A 144 3747 3177 3374 -48 376 -500 C ATOM 1088 N CYS A 145 11.202 11.577 24.499 1.00 22.43 N ANISOU 1088 N CYS A 145 3204 2543 2774 -119 396 -523 N ATOM 1089 CA CYS A 145 12.594 11.119 24.381 1.00 23.30 C ANISOU 1089 CA CYS A 145 3312 2648 2894 -138 422 -545 C ATOM 1090 C CYS A 145 13.374 12.236 23.705 1.00 22.98 C ANISOU 1090 C CYS A 145 3312 2566 2855 -148 469 -568 C ATOM 1091 O CYS A 145 12.982 12.671 22.641 1.00 23.09 O ANISOU 1091 O CYS A 145 3380 2542 2853 -141 476 -555 O ATOM 1092 CB CYS A 145 12.696 9.849 23.534 1.00 22.40 C ANISOU 1092 CB CYS A 145 3217 2522 2772 -143 405 -529 C ATOM 1093 SG CYS A 145 11.557 8.615 24.001 1.00 27.26 S ANISOU 1093 SG CYS A 145 3804 3172 3383 -134 355 -498 S ATOM 1094 N THR A 146 14.473 12.693 24.299 1.00 23.73 N ANISOU 1094 N THR A 146 3382 2667 2969 -164 503 -603 N ATOM 1095 CA THR A 146 15.208 13.838 23.701 1.00 24.07 C ANISOU 1095 CA THR A 146 3462 2667 3016 -178 557 -630 C ATOM 1096 C THR A 146 16.680 13.664 23.974 1.00 24.50 C ANISOU 1096 C THR A 146 3487 2729 3094 -203 589 -669 C ATOM 1097 O THR A 146 17.081 13.256 25.071 1.00 22.66 O ANISOU 1097 O THR A 146 3194 2542 2875 -205 574 -685 O ATOM 1098 CB THR A 146 14.703 15.246 24.211 1.00 25.11 C ANISOU 1098 CB THR A 146 3600 2793 3149 -172 575 -639 C ATOM 1099 OG1 THR A 146 15.345 16.315 23.474 1.00 27.71 O ANISOU 1099 OG1 THR A 146 3977 3070 3480 -186 632 -661 O ATOM 1100 CG2 THR A 146 14.961 15.419 25.699 1.00 23.80 C ANISOU 1100 CG2 THR A 146 3370 2674 3000 -179 571 -664 C ATOM 1101 N ASP A 147 17.506 13.900 22.954 1.00 25.22 N ANISOU 1101 N ASP A 147 3617 2775 3189 -219 633 -684 N ATOM 1102 CA ASP A 147 18.948 13.749 23.148 1.00 26.45 C ANISOU 1102 CA ASP A 147 3740 2938 3372 -243 667 -726 C ATOM 1103 C ASP A 147 19.693 14.514 22.071 1.00 27.36 C ANISOU 1103 C ASP A 147 3909 2995 3493 -263 730 -748 C ATOM 1104 O ASP A 147 19.187 14.716 20.983 1.00 26.07 O ANISOU 1104 O ASP A 147 3813 2786 3306 -255 740 -723 O ATOM 1105 CB ASP A 147 19.391 12.267 23.137 1.00 25.89 C ANISOU 1105 CB ASP A 147 3640 2891 3305 -239 640 -716 C ATOM 1106 CG ASP A 147 19.378 11.621 24.532 1.00 26.87 C ANISOU 1106 CG ASP A 147 3693 3079 3437 -228 598 -719 C ATOM 1107 OD1 ASP A 147 20.028 12.131 25.474 1.00 25.77 O ANISOU 1107 OD1 ASP A 147 3507 2969 3315 -237 609 -755 O ATOM 1108 OD2 ASP A 147 18.690 10.588 24.698 1.00 25.98 O ANISOU 1108 OD2 ASP A 147 3574 2988 3311 -209 555 -685 O ATOM 1109 N SER A 148 20.883 14.978 22.431 1.00 29.75 N ANISOU 1109 N SER A 148 4178 3300 3825 -290 773 -796 N ATOM 1110 CA SER A 148 21.792 15.605 21.489 1.00 32.96 C ANISOU 1110 CA SER A 148 4626 3652 4244 -316 843 -825 C ATOM 1111 C SER A 148 23.209 15.378 21.989 1.00 35.13 C ANISOU 1111 C SER A 148 4837 3954 4558 -342 868 -876 C ATOM 1112 O SER A 148 23.546 15.693 23.137 1.00 35.56 O ANISOU 1112 O SER A 148 4828 4052 4632 -350 859 -909 O ATOM 1113 CB SER A 148 21.543 17.110 21.407 1.00 33.02 C ANISOU 1113 CB SER A 148 4676 3622 4250 -326 888 -839 C ATOM 1114 OG SER A 148 22.538 17.739 20.602 1.00 35.02 O ANISOU 1114 OG SER A 148 4965 3822 4519 -356 963 -872 O ATOM 1115 N ALA A 149 24.050 14.840 21.124 1.00 37.53 N ANISOU 1115 N ALA A 149 5155 4231 4873 -354 899 -886 N ATOM 1116 CA ALA A 149 25.476 14.790 21.415 1.00 39.32 C ANISOU 1116 CA ALA A 149 5325 4474 5141 -381 936 -941 C ATOM 1117 C ALA A 149 26.182 14.492 20.119 1.00 40.63 C ANISOU 1117 C ALA A 149 5536 4587 5314 -395 987 -945 C ATOM 1118 O ALA A 149 25.876 13.508 19.446 1.00 39.42 O ANISOU 1118 O ALA A 149 5413 4423 5140 -376 964 -908 O ATOM 1119 CB ALA A 149 25.805 13.711 22.483 1.00 39.48 C ANISOU 1119 CB ALA A 149 5259 4567 5174 -364 879 -946 C ATOM 1120 N VAL A 150 27.090 15.390 19.744 1.00 42.64 N ANISOU 1120 N VAL A 150 5801 4805 5596 -430 1062 -992 N ATOM 1121 CA VAL A 150 28.088 15.089 18.707 1.00 43.97 C ANISOU 1121 CA VAL A 150 5993 4931 5783 -450 1121 -1011 C ATOM 1122 C VAL A 150 29.481 15.451 19.293 1.00 45.65 C ANISOU 1122 C VAL A 150 6126 5167 6050 -486 1164 -1083 C ATOM 1123 O VAL A 150 29.729 16.608 19.655 1.00 44.63 O ANISOU 1123 O VAL A 150 5989 5028 5940 -514 1205 -1123 O ATOM 1124 CB VAL A 150 27.786 15.809 17.329 1.00 44.24 C ANISOU 1124 CB VAL A 150 6139 4879 5791 -460 1182 -993 C ATOM 1125 CG1 VAL A 150 28.706 15.277 16.219 1.00 43.57 C ANISOU 1125 CG1 VAL A 150 6084 4752 5719 -475 1237 -1005 C ATOM 1126 CG2 VAL A 150 26.288 15.685 16.926 1.00 43.82 C ANISOU 1126 CG2 VAL A 150 6156 4812 5683 -423 1131 -927 C ATOM 1127 N TYR A 151 30.355 14.448 19.436 1.00 47.27 N ANISOU 1127 N TYR A 151 6271 5407 6284 -482 1153 -1102 N ATOM 1128 CA TYR A 151 31.715 14.696 19.917 1.00 49.23 C ANISOU 1128 CA TYR A 151 6437 5681 6586 -513 1191 -1172 C ATOM 1129 C TYR A 151 32.445 15.581 18.909 1.00 49.70 C ANISOU 1129 C TYR A 151 6545 5669 6669 -557 1292 -1210 C ATOM 1130 O TYR A 151 32.474 15.271 17.720 1.00 49.49 O ANISOU 1130 O TYR A 151 6587 5585 6630 -557 1330 -1186 O ATOM 1131 CB TYR A 151 32.462 13.378 20.186 1.00 50.41 C ANISOU 1131 CB TYR A 151 6516 5879 6758 -493 1157 -1179 C ATOM 1132 CG TYR A 151 31.768 12.507 21.225 1.00 52.23 C ANISOU 1132 CG TYR A 151 6704 6177 6965 -449 1063 -1142 C ATOM 1133 CD1 TYR A 151 31.304 13.048 22.448 1.00 55.08 C ANISOU 1133 CD1 TYR A 151 7023 6587 7317 -445 1020 -1150 C ATOM 1134 CD2 TYR A 151 31.563 11.150 20.991 1.00 54.08 C ANISOU 1134 CD2 TYR A 151 6943 6423 7183 -414 1022 -1098 C ATOM 1135 CE1 TYR A 151 30.639 12.237 23.405 1.00 53.69 C ANISOU 1135 CE1 TYR A 151 6813 6469 7116 -404 938 -1114 C ATOM 1136 CE2 TYR A 151 30.918 10.330 21.936 1.00 54.06 C ANISOU 1136 CE2 TYR A 151 6907 6477 7158 -375 942 -1063 C ATOM 1137 CZ TYR A 151 30.463 10.874 23.131 1.00 53.34 C ANISOU 1137 CZ TYR A 151 6776 6433 7057 -370 901 -1071 C ATOM 1138 OH TYR A 151 29.829 10.035 24.035 1.00 54.32 O ANISOU 1138 OH TYR A 151 6873 6608 7157 -332 828 -1035 O ATOM 1139 N ALA A 152 32.985 16.701 19.389 1.00 50.17 N ANISOU 1139 N ALA A 152 6573 5729 6762 -595 1337 -1268 N ATOM 1140 CA ALA A 152 33.632 17.709 18.539 1.00 50.49 C ANISOU 1140 CA ALA A 152 6661 5697 6825 -642 1441 -1308 C ATOM 1141 C ALA A 152 34.859 17.179 17.800 1.00 50.85 C ANISOU 1141 C ALA A 152 6686 5724 6912 -663 1499 -1342 C ATOM 1142 O ALA A 152 35.167 17.638 16.695 1.00 51.08 O ANISOU 1142 O ALA A 152 6787 5677 6944 -689 1583 -1349 O ATOM 1143 CB ALA A 152 33.994 18.956 19.365 1.00 50.49 C ANISOU 1143 CB ALA A 152 6619 5710 6856 -681 1474 -1369 C ATOM 1144 N GLU A 153 35.557 16.226 18.416 1.00 51.30 N ANISOU 1144 N GLU A 153 6646 5847 6999 -649 1456 -1364 N ATOM 1145 CA GLU A 153 36.720 15.580 17.797 1.00 52.88 C ANISOU 1145 CA GLU A 153 6815 6038 7242 -662 1503 -1396 C ATOM 1146 C GLU A 153 36.700 14.061 18.006 1.00 52.41 C ANISOU 1146 C GLU A 153 6713 6028 7173 -614 1430 -1360 C ATOM 1147 O GLU A 153 35.789 13.521 18.658 1.00 51.54 O ANISOU 1147 O GLU A 153 6598 5960 7025 -573 1345 -1312 O ATOM 1148 CB GLU A 153 38.027 16.188 18.335 1.00 53.96 C ANISOU 1148 CB GLU A 153 6855 6201 7446 -708 1553 -1487 C ATOM 1149 CG GLU A 153 38.282 17.633 17.863 1.00 57.70 C ANISOU 1149 CG GLU A 153 7378 6607 7938 -765 1652 -1530 C ATOM 1150 CD GLU A 153 39.071 18.483 18.867 1.00 62.51 C ANISOU 1150 CD GLU A 153 7891 7260 8599 -808 1670 -1615 C ATOM 1151 OE1 GLU A 153 40.228 18.106 19.193 1.00 63.82 O ANISOU 1151 OE1 GLU A 153 7956 7472 8821 -822 1678 -1675 O ATOM 1152 OE2 GLU A 153 38.536 19.540 19.309 1.00 63.75 O ANISOU 1152 OE2 GLU A 153 8074 7406 8741 -826 1678 -1623 O ATOM 1153 N GLY A 154 37.701 13.375 17.454 1.00 52.60 N ANISOU 1153 N GLY A 154 6709 6044 7233 -618 1468 -1383 N ATOM 1154 CA GLY A 154 37.879 11.943 17.697 1.00 52.23 C ANISOU 1154 CA GLY A 154 6613 6044 7187 -573 1408 -1359 C ATOM 1155 C GLY A 154 37.028 11.092 16.770 1.00 51.73 C ANISOU 1155 C GLY A 154 6645 5937 7073 -543 1391 -1285 C ATOM 1156 O GLY A 154 36.219 11.633 16.013 1.00 51.69 O ANISOU 1156 O GLY A 154 6740 5872 7027 -552 1415 -1251 O ATOM 1157 N PRO A 155 37.181 9.751 16.851 1.00 51.40 N ANISOU 1157 N PRO A 155 6573 5926 7031 -504 1347 -1260 N ATOM 1158 CA PRO A 155 36.602 8.751 15.941 1.00 50.77 C ANISOU 1158 CA PRO A 155 6571 5807 6912 -477 1336 -1200 C ATOM 1159 C PRO A 155 35.093 8.548 16.100 1.00 49.71 C ANISOU 1159 C PRO A 155 6497 5675 6714 -449 1266 -1133 C ATOM 1160 O PRO A 155 34.455 7.879 15.263 1.00 50.23 O ANISOU 1160 O PRO A 155 6640 5703 6741 -433 1258 -1084 O ATOM 1161 CB PRO A 155 37.325 7.442 16.340 1.00 51.15 C ANISOU 1161 CB PRO A 155 6543 5904 6989 -443 1304 -1205 C ATOM 1162 CG PRO A 155 38.404 7.834 17.299 1.00 51.63 C ANISOU 1162 CG PRO A 155 6487 6023 7106 -454 1308 -1272 C ATOM 1163 CD PRO A 155 37.947 9.110 17.932 1.00 51.76 C ANISOU 1163 CD PRO A 155 6500 6052 7114 -480 1301 -1292 C ATOM 1164 N ALA A 156 34.541 9.100 17.169 1.00 48.23 N ANISOU 1164 N ALA A 156 6274 5534 6517 -444 1215 -1133 N ATOM 1165 CA ALA A 156 33.126 8.968 17.465 1.00 46.74 C ANISOU 1165 CA ALA A 156 6129 5355 6275 -418 1148 -1075 C ATOM 1166 C ALA A 156 32.268 10.114 16.900 1.00 45.07 C ANISOU 1166 C ALA A 156 6004 5092 6030 -439 1174 -1059 C ATOM 1167 O ALA A 156 31.045 10.025 16.935 1.00 44.95 O ANISOU 1167 O ALA A 156 6034 5075 5969 -418 1125 -1009 O ATOM 1168 CB ALA A 156 32.924 8.828 18.987 1.00 46.84 C ANISOU 1168 CB ALA A 156 6057 5448 6291 -395 1075 -1079 C ATOM 1169 N ARG A 157 32.908 11.168 16.389 1.00 43.39 N ANISOU 1169 N ARG A 157 5811 4834 5840 -478 1253 -1101 N ATOM 1170 CA ARG A 157 32.219 12.307 15.775 1.00 42.01 C ANISOU 1170 CA ARG A 157 5725 4602 5636 -496 1290 -1088 C ATOM 1171 C ARG A 157 31.176 11.965 14.673 1.00 40.61 C ANISOU 1171 C ARG A 157 5656 4373 5400 -476 1278 -1025 C ATOM 1172 O ARG A 157 30.084 12.579 14.644 1.00 40.00 O ANISOU 1172 O ARG A 157 5634 4282 5283 -465 1254 -993 O ATOM 1173 CB ARG A 157 33.217 13.358 15.259 1.00 42.60 C ANISOU 1173 CB ARG A 157 5811 4628 5747 -543 1390 -1144 C ATOM 1174 CG ARG A 157 32.535 14.500 14.474 1.00 43.35 C ANISOU 1174 CG ARG A 157 6014 4652 5806 -557 1437 -1126 C ATOM 1175 CD ARG A 157 33.443 15.715 14.248 1.00 44.02 C ANISOU 1175 CD ARG A 157 6103 4693 5930 -607 1535 -1186 C ATOM 1176 NE ARG A 157 34.464 15.492 13.221 1.00 43.89 N ANISOU 1176 NE ARG A 157 6112 4626 5939 -632 1618 -1212 N ATOM 1177 CZ ARG A 157 35.642 16.113 13.207 1.00 45.12 C ANISOU 1177 CZ ARG A 157 6228 4765 6150 -678 1700 -1280 C ATOM 1178 NH1 ARG A 157 35.937 16.988 14.168 1.00 45.02 N ANISOU 1178 NH1 ARG A 157 6151 4784 6172 -704 1707 -1329 N ATOM 1179 NH2 ARG A 157 36.525 15.870 12.241 1.00 44.31 N ANISOU 1179 NH2 ARG A 157 6152 4614 6071 -699 1778 -1302 N ATOM 1180 N PRO A 158 31.513 11.041 13.739 1.00 38.69 N ANISOU 1180 N PRO A 158 5449 4101 5152 -470 1298 -1012 N ATOM 1181 CA PRO A 158 30.500 10.682 12.743 1.00 37.57 C ANISOU 1181 CA PRO A 158 5408 3917 4952 -451 1279 -956 C ATOM 1182 C PRO A 158 29.251 9.971 13.274 1.00 36.08 C ANISOU 1182 C PRO A 158 5213 3770 4725 -415 1183 -904 C ATOM 1183 O PRO A 158 28.247 9.932 12.569 1.00 35.13 O ANISOU 1183 O PRO A 158 5172 3621 4556 -400 1162 -862 O ATOM 1184 CB PRO A 158 31.278 9.782 11.754 1.00 37.55 C ANISOU 1184 CB PRO A 158 5431 3878 4957 -456 1323 -960 C ATOM 1185 CG PRO A 158 32.704 10.155 11.984 1.00 37.98 C ANISOU 1185 CG PRO A 158 5420 3934 5075 -487 1391 -1024 C ATOM 1186 CD PRO A 158 32.794 10.371 13.442 1.00 39.15 C ANISOU 1186 CD PRO A 158 5466 4156 5254 -482 1343 -1047 C ATOM 1187 N THR A 159 29.309 9.427 14.495 1.00 35.43 N ANISOU 1187 N THR A 159 5039 3757 4666 -399 1128 -910 N ATOM 1188 CA THR A 159 28.175 8.743 15.093 1.00 34.52 C ANISOU 1188 CA THR A 159 4912 3683 4519 -368 1043 -865 C ATOM 1189 C THR A 159 27.345 9.651 16.004 1.00 33.31 C ANISOU 1189 C THR A 159 4741 3560 4356 -363 1007 -859 C ATOM 1190 O THR A 159 26.800 9.152 16.983 1.00 32.95 O ANISOU 1190 O THR A 159 4646 3568 4306 -341 943 -842 O ATOM 1191 CB THR A 159 28.612 7.557 15.993 1.00 35.27 C ANISOU 1191 CB THR A 159 4924 3837 4640 -347 1000 -868 C ATOM 1192 OG1 THR A 159 29.425 8.072 17.057 1.00 36.31 O ANISOU 1192 OG1 THR A 159 4969 4013 4813 -357 1007 -913 O ATOM 1193 CG2 THR A 159 29.399 6.490 15.196 1.00 35.37 C ANISOU 1193 CG2 THR A 159 4948 3825 4665 -346 1030 -870 C ATOM 1194 N GLY A 160 27.256 10.951 15.707 1.00 31.03 N ANISOU 1194 N GLY A 160 4492 3235 4062 -381 1050 -874 N ATOM 1195 CA GLY A 160 26.438 11.873 16.500 1.00 29.15 C ANISOU 1195 CA GLY A 160 4245 3019 3813 -376 1021 -868 C ATOM 1196 C GLY A 160 25.039 11.998 15.931 1.00 27.92 C ANISOU 1196 C GLY A 160 4165 2839 3606 -354 986 -816 C ATOM 1197 O GLY A 160 24.716 11.356 14.902 1.00 28.05 O ANISOU 1197 O GLY A 160 4243 2823 3593 -344 982 -786 O ATOM 1198 N GLY A 161 24.204 12.816 16.580 1.00 25.85 N ANISOU 1198 N GLY A 161 3898 2592 3331 -344 961 -806 N ATOM 1199 CA GLY A 161 22.861 13.142 16.087 1.00 23.94 C ANISOU 1199 CA GLY A 161 3724 2329 3044 -321 930 -762 C ATOM 1200 C GLY A 161 22.055 13.850 17.164 1.00 24.48 C ANISOU 1200 C GLY A 161 3757 2432 3111 -309 895 -757 C ATOM 1201 O GLY A 161 22.556 14.058 18.270 1.00 23.62 O ANISOU 1201 O GLY A 161 3576 2364 3034 -320 894 -788 O ATOM 1202 N ALA A 162 20.808 14.202 16.845 1.00 24.07 N ANISOU 1202 N ALA A 162 3755 2368 3022 -285 864 -719 N ATOM 1203 CA ALA A 162 19.934 14.925 17.772 1.00 25.03 C ANISOU 1203 CA ALA A 162 3852 2518 3142 -270 834 -711 C ATOM 1204 C ALA A 162 18.503 14.750 17.344 1.00 24.85 C ANISOU 1204 C ALA A 162 3870 2493 3078 -237 781 -662 C ATOM 1205 O ALA A 162 18.209 14.816 16.155 1.00 24.54 O ANISOU 1205 O ALA A 162 3907 2410 3009 -227 791 -641 O ATOM 1206 CB ALA A 162 20.274 16.428 17.791 1.00 24.11 C ANISOU 1206 CB ALA A 162 3763 2363 3034 -285 896 -739 C ATOM 1207 N ALA A 163 17.616 14.544 18.316 1.00 24.06 N ANISOU 1207 N ALA A 163 3721 2443 2979 -219 725 -646 N ATOM 1208 CA ALA A 163 16.175 14.630 18.063 1.00 23.86 C ANISOU 1208 CA ALA A 163 3725 2419 2921 -188 677 -606 C ATOM 1209 C ALA A 163 15.409 14.606 19.352 1.00 23.48 C ANISOU 1209 C ALA A 163 3612 2425 2884 -176 633 -599 C ATOM 1210 O ALA A 163 15.964 14.255 20.391 1.00 23.71 O ANISOU 1210 O ALA A 163 3576 2493 2940 -189 630 -621 O ATOM 1211 CB ALA A 163 15.692 13.497 17.179 1.00 23.83 C ANISOU 1211 CB ALA A 163 3750 2412 2891 -177 638 -576 C ATOM 1212 N ALA A 164 14.145 15.004 19.264 1.00 23.73 N ANISOU 1212 N ALA A 164 3664 2458 2895 -148 600 -571 N ATOM 1213 CA ALA A 164 13.140 14.791 20.309 1.00 23.64 C ANISOU 1213 CA ALA A 164 3598 2496 2889 -131 550 -556 C ATOM 1214 C ALA A 164 11.931 14.134 19.661 1.00 23.68 C ANISOU 1214 C ALA A 164 3623 2507 2868 -108 496 -519 C ATOM 1215 O ALA A 164 11.554 14.503 18.549 1.00 23.74 O ANISOU 1215 O ALA A 164 3695 2477 2848 -92 498 -502 O ATOM 1216 CB ALA A 164 12.731 16.092 20.942 1.00 23.14 C ANISOU 1216 CB ALA A 164 3532 2431 2831 -120 568 -563 C ATOM 1217 N ILE A 165 11.367 13.135 20.348 1.00 23.61 N ANISOU 1217 N ILE A 165 3560 2544 2867 -106 449 -507 N ATOM 1218 CA ILE A 165 10.108 12.500 19.968 1.00 23.29 C ANISOU 1218 CA ILE A 165 3523 2519 2809 -87 395 -477 C ATOM 1219 C ILE A 165 9.101 12.672 21.129 1.00 23.54 C ANISOU 1219 C ILE A 165 3498 2593 2854 -73 365 -469 C ATOM 1220 O ILE A 165 9.469 12.569 22.292 1.00 22.36 O ANISOU 1220 O ILE A 165 3298 2473 2726 -85 374 -483 O ATOM 1221 CB ILE A 165 10.329 11.011 19.637 1.00 24.53 C ANISOU 1221 CB ILE A 165 3671 2687 2964 -103 372 -471 C ATOM 1222 CG1 ILE A 165 11.031 10.923 18.265 1.00 26.28 C ANISOU 1222 CG1 ILE A 165 3961 2861 3166 -111 398 -474 C ATOM 1223 CG2 ILE A 165 8.979 10.199 19.630 1.00 21.14 C ANISOU 1223 CG2 ILE A 165 3220 2285 2526 -91 314 -447 C ATOM 1224 CD1 ILE A 165 11.714 9.669 18.036 1.00 27.28 C ANISOU 1224 CD1 ILE A 165 4080 2988 3296 -131 399 -479 C ATOM 1225 N ALA A 166 7.849 12.975 20.806 1.00 24.29 N ANISOU 1225 N ALA A 166 3604 2691 2936 -47 332 -447 N ATOM 1226 CA ALA A 166 6.794 13.022 21.827 1.00 24.36 C ANISOU 1226 CA ALA A 166 3557 2740 2958 -34 303 -439 C ATOM 1227 C ALA A 166 5.749 11.971 21.490 1.00 23.90 C ANISOU 1227 C ALA A 166 3482 2705 2893 -29 250 -419 C ATOM 1228 O ALA A 166 5.388 11.802 20.321 1.00 25.02 O ANISOU 1228 O ALA A 166 3666 2828 3013 -20 228 -408 O ATOM 1229 CB ALA A 166 6.164 14.402 21.920 1.00 24.08 C ANISOU 1229 CB ALA A 166 3538 2693 2920 -5 313 -435 C ATOM 1230 N MET A 167 5.292 11.246 22.509 1.00 23.18 N ANISOU 1230 N MET A 167 3332 2654 2822 -38 231 -417 N ATOM 1231 CA MET A 167 4.314 10.148 22.314 1.00 22.87 C ANISOU 1231 CA MET A 167 3270 2638 2783 -41 185 -403 C ATOM 1232 C MET A 167 3.203 10.320 23.326 1.00 21.89 C ANISOU 1232 C MET A 167 3091 2549 2676 -29 168 -397 C ATOM 1233 O MET A 167 3.464 10.444 24.510 1.00 19.86 O ANISOU 1233 O MET A 167 2799 2311 2436 -35 188 -405 O ATOM 1234 CB MET A 167 4.959 8.759 22.476 1.00 21.90 C ANISOU 1234 CB MET A 167 3134 2522 2665 -69 186 -407 C ATOM 1235 CG MET A 167 5.960 8.423 21.390 1.00 22.56 C ANISOU 1235 CG MET A 167 3269 2570 2731 -82 202 -412 C ATOM 1236 SD MET A 167 6.826 6.872 21.681 1.00 23.28 S ANISOU 1236 SD MET A 167 3345 2668 2832 -110 211 -416 S ATOM 1237 CE MET A 167 8.158 7.347 22.796 1.00 21.94 C ANISOU 1237 CE MET A 167 3151 2506 2681 -115 255 -435 C ATOM 1238 N LEU A 168 1.971 10.326 22.833 1.00 21.75 N ANISOU 1238 N LEU A 168 3067 2542 2656 -11 129 -385 N ATOM 1239 CA LEU A 168 0.767 10.393 23.666 1.00 21.46 C ANISOU 1239 CA LEU A 168 2975 2539 2640 0 110 -380 C ATOM 1240 C LEU A 168 0.294 8.964 23.919 1.00 21.22 C ANISOU 1240 C LEU A 168 2908 2534 2622 -25 87 -378 C ATOM 1241 O LEU A 168 0.198 8.162 22.974 1.00 20.07 O ANISOU 1241 O LEU A 168 2781 2381 2464 -37 63 -377 O ATOM 1242 CB LEU A 168 -0.332 11.165 22.923 1.00 21.29 C ANISOU 1242 CB LEU A 168 2963 2516 2609 35 79 -371 C ATOM 1243 CG LEU A 168 -1.502 11.674 23.781 1.00 23.08 C ANISOU 1243 CG LEU A 168 3136 2772 2859 56 69 -368 C ATOM 1244 CD1 LEU A 168 -1.102 12.856 24.689 1.00 20.43 C ANISOU 1244 CD1 LEU A 168 2801 2429 2532 70 112 -373 C ATOM 1245 CD2 LEU A 168 -2.701 12.035 22.843 1.00 23.05 C ANISOU 1245 CD2 LEU A 168 3135 2775 2847 91 23 -358 C ATOM 1246 N ILE A 169 -0.024 8.668 25.181 1.00 20.63 N ANISOU 1246 N ILE A 169 2782 2486 2570 -34 98 -379 N ATOM 1247 CA ILE A 169 -0.270 7.316 25.654 1.00 20.35 C ANISOU 1247 CA ILE A 169 2715 2469 2547 -61 92 -378 C ATOM 1248 C ILE A 169 -1.691 7.268 26.201 1.00 21.83 C ANISOU 1248 C ILE A 169 2850 2687 2757 -56 74 -375 C ATOM 1249 O ILE A 169 -2.116 8.161 26.935 1.00 21.75 O ANISOU 1249 O ILE A 169 2816 2689 2759 -36 85 -375 O ATOM 1250 CB ILE A 169 0.762 6.909 26.782 1.00 19.99 C ANISOU 1250 CB ILE A 169 2661 2428 2506 -77 128 -381 C ATOM 1251 CG1 ILE A 169 2.237 7.122 26.316 1.00 19.69 C ANISOU 1251 CG1 ILE A 169 2668 2363 2451 -80 150 -389 C ATOM 1252 CG2 ILE A 169 0.517 5.478 27.305 1.00 20.39 C ANISOU 1252 CG2 ILE A 169 2686 2493 2567 -101 126 -376 C ATOM 1253 CD1 ILE A 169 2.607 6.536 24.930 1.00 19.15 C ANISOU 1253 CD1 ILE A 169 2642 2268 2365 -90 136 -388 C ATOM 1254 N GLY A 170 -2.442 6.244 25.829 1.00 22.51 N ANISOU 1254 N GLY A 170 2917 2784 2852 -74 47 -375 N ATOM 1255 CA GLY A 170 -3.808 6.128 26.323 1.00 23.58 C ANISOU 1255 CA GLY A 170 2996 2948 3013 -73 33 -376 C ATOM 1256 C GLY A 170 -4.440 4.826 25.844 1.00 23.94 C ANISOU 1256 C GLY A 170 3025 3001 3068 -103 9 -381 C ATOM 1257 O GLY A 170 -3.861 4.132 25.042 1.00 24.20 O ANISOU 1257 O GLY A 170 3095 3016 3085 -120 0 -382 O ATOM 1258 N PRO A 171 -5.661 4.534 26.310 1.00 25.05 N ANISOU 1258 N PRO A 171 3112 3169 3238 -110 -1 -386 N ATOM 1259 CA PRO A 171 -6.401 3.323 25.981 1.00 25.43 C ANISOU 1259 CA PRO A 171 3134 3226 3301 -143 -19 -396 C ATOM 1260 C PRO A 171 -6.920 3.408 24.549 1.00 27.14 C ANISOU 1260 C PRO A 171 3362 3444 3505 -136 -72 -405 C ATOM 1261 O PRO A 171 -6.906 4.492 23.933 1.00 26.72 O ANISOU 1261 O PRO A 171 3329 3388 3434 -99 -93 -401 O ATOM 1262 CB PRO A 171 -7.543 3.327 26.997 1.00 25.46 C ANISOU 1262 CB PRO A 171 3073 3259 3342 -147 -7 -400 C ATOM 1263 CG PRO A 171 -7.788 4.760 27.262 1.00 26.51 C ANISOU 1263 CG PRO A 171 3195 3402 3477 -105 -9 -396 C ATOM 1264 CD PRO A 171 -6.453 5.460 27.148 1.00 24.22 C ANISOU 1264 CD PRO A 171 2963 3086 3155 -86 8 -385 C ATOM 1265 N ASP A 172 -7.298 2.260 23.994 1.00 28.25 N ANISOU 1265 N ASP A 172 3496 3586 3650 -170 -90 -418 N ATOM 1266 CA ASP A 172 -7.909 2.221 22.659 1.00 29.30 C ANISOU 1266 CA ASP A 172 3635 3728 3771 -167 -145 -431 C ATOM 1267 C ASP A 172 -6.979 2.760 21.564 1.00 28.67 C ANISOU 1267 C ASP A 172 3627 3621 3647 -144 -160 -423 C ATOM 1268 O ASP A 172 -7.367 3.623 20.770 1.00 30.15 O ANISOU 1268 O ASP A 172 3825 3814 3816 -109 -198 -423 O ATOM 1269 CB ASP A 172 -9.244 2.991 22.720 1.00 29.87 C ANISOU 1269 CB ASP A 172 3647 3835 3866 -139 -178 -440 C ATOM 1270 CG ASP A 172 -10.138 2.495 23.853 1.00 32.54 C ANISOU 1270 CG ASP A 172 3915 4199 4251 -163 -155 -449 C ATOM 1271 OD1 ASP A 172 -10.297 1.256 23.993 1.00 33.50 O ANISOU 1271 OD1 ASP A 172 4023 4318 4388 -210 -142 -460 O ATOM 1272 OD2 ASP A 172 -10.651 3.340 24.620 1.00 34.72 O ANISOU 1272 OD2 ASP A 172 4153 4492 4548 -137 -143 -444 O ATOM 1273 N ALA A 173 -5.747 2.250 21.519 1.00 26.90 N ANISOU 1273 N ALA A 173 3452 3364 3404 -162 -129 -416 N ATOM 1274 CA ALA A 173 -4.691 2.878 20.727 1.00 25.27 C ANISOU 1274 CA ALA A 173 3313 3127 3160 -140 -126 -407 C ATOM 1275 C ALA A 173 -4.556 2.153 19.401 1.00 24.38 C ANISOU 1275 C ALA A 173 3245 3000 3021 -158 -154 -417 C ATOM 1276 O ALA A 173 -4.980 1.015 19.294 1.00 24.78 O ANISOU 1276 O ALA A 173 3277 3057 3083 -194 -164 -430 O ATOM 1277 CB ALA A 173 -3.349 2.853 21.497 1.00 23.75 C ANISOU 1277 CB ALA A 173 3147 2912 2966 -146 -72 -396 C ATOM 1278 N PRO A 174 -3.988 2.817 18.381 1.00 23.77 N ANISOU 1278 N PRO A 174 3227 2898 2905 -134 -166 -412 N ATOM 1279 CA PRO A 174 -3.628 2.100 17.149 1.00 23.58 C ANISOU 1279 CA PRO A 174 3256 2853 2850 -152 -184 -421 C ATOM 1280 C PRO A 174 -2.354 1.287 17.285 1.00 23.58 C ANISOU 1280 C PRO A 174 3294 2820 2847 -181 -137 -418 C ATOM 1281 O PRO A 174 -2.065 0.437 16.436 1.00 23.82 O ANISOU 1281 O PRO A 174 3361 2831 2857 -204 -144 -427 O ATOM 1282 CB PRO A 174 -3.401 3.231 16.148 1.00 22.80 C ANISOU 1282 CB PRO A 174 3214 2738 2712 -111 -202 -413 C ATOM 1283 CG PRO A 174 -2.908 4.395 17.017 1.00 23.35 C ANISOU 1283 CG PRO A 174 3279 2802 2793 -82 -164 -398 C ATOM 1284 CD PRO A 174 -3.726 4.265 18.281 1.00 23.11 C ANISOU 1284 CD PRO A 174 3168 2806 2805 -88 -161 -400 C ATOM 1285 N ILE A 175 -1.588 1.581 18.332 1.00 22.77 N ANISOU 1285 N ILE A 175 3180 2711 2760 -176 -92 -407 N ATOM 1286 CA ILE A 175 -0.321 0.920 18.590 1.00 23.41 C ANISOU 1286 CA ILE A 175 3289 2765 2840 -195 -48 -404 C ATOM 1287 C ILE A 175 -0.418 0.323 20.000 1.00 22.56 C ANISOU 1287 C ILE A 175 3130 2675 2767 -211 -21 -400 C ATOM 1288 O ILE A 175 -0.306 1.048 20.989 1.00 22.82 O ANISOU 1288 O ILE A 175 3136 2721 2814 -193 -2 -392 O ATOM 1289 CB ILE A 175 0.851 1.930 18.477 1.00 23.30 C ANISOU 1289 CB ILE A 175 3318 2727 2810 -171 -17 -396 C ATOM 1290 CG1 ILE A 175 0.938 2.520 17.052 1.00 23.50 C ANISOU 1290 CG1 ILE A 175 3403 2729 2797 -154 -38 -398 C ATOM 1291 CG2 ILE A 175 2.160 1.269 18.909 1.00 23.99 C ANISOU 1291 CG2 ILE A 175 3420 2793 2902 -188 28 -395 C ATOM 1292 CD1 ILE A 175 1.505 3.930 16.946 1.00 22.48 C ANISOU 1292 CD1 ILE A 175 3304 2583 2653 -121 -19 -391 C ATOM 1293 N VAL A 176 -0.640 -0.982 20.096 1.00 22.09 N ANISOU 1293 N VAL A 176 3061 2615 2720 -244 -17 -406 N ATOM 1294 CA VAL A 176 -1.031 -1.587 21.370 1.00 22.39 C ANISOU 1294 CA VAL A 176 3049 2670 2788 -259 4 -402 C ATOM 1295 C VAL A 176 0.095 -2.453 21.893 1.00 23.23 C ANISOU 1295 C VAL A 176 3177 2754 2895 -272 47 -393 C ATOM 1296 O VAL A 176 0.684 -3.261 21.172 1.00 22.62 O ANISOU 1296 O VAL A 176 3139 2649 2804 -288 54 -397 O ATOM 1297 CB VAL A 176 -2.366 -2.391 21.279 1.00 23.50 C ANISOU 1297 CB VAL A 176 3151 2828 2948 -288 -21 -415 C ATOM 1298 CG1 VAL A 176 -2.775 -3.009 22.665 1.00 24.34 C ANISOU 1298 CG1 VAL A 176 3212 2949 3087 -304 11 -410 C ATOM 1299 CG2 VAL A 176 -3.486 -1.521 20.726 1.00 23.90 C ANISOU 1299 CG2 VAL A 176 3176 2905 2998 -271 -69 -425 C ATOM 1300 N PHE A 177 0.437 -2.236 23.157 1.00 23.35 N ANISOU 1300 N PHE A 177 3168 2781 2924 -260 76 -383 N ATOM 1301 CA PHE A 177 1.422 -3.081 23.812 1.00 23.27 C ANISOU 1301 CA PHE A 177 3171 2755 2915 -265 113 -373 C ATOM 1302 C PHE A 177 0.866 -4.479 23.988 1.00 23.61 C ANISOU 1302 C PHE A 177 3207 2791 2971 -297 123 -374 C ATOM 1303 O PHE A 177 -0.245 -4.649 24.508 1.00 23.08 O ANISOU 1303 O PHE A 177 3102 2744 2924 -310 117 -376 O ATOM 1304 CB PHE A 177 1.832 -2.454 25.157 1.00 22.86 C ANISOU 1304 CB PHE A 177 3094 2723 2870 -242 137 -363 C ATOM 1305 CG PHE A 177 2.795 -1.326 24.999 1.00 21.15 C ANISOU 1305 CG PHE A 177 2894 2503 2640 -217 141 -366 C ATOM 1306 CD1 PHE A 177 2.378 -0.104 24.494 1.00 20.91 C ANISOU 1306 CD1 PHE A 177 2862 2479 2604 -202 120 -372 C ATOM 1307 CD2 PHE A 177 4.117 -1.488 25.316 1.00 20.30 C ANISOU 1307 CD2 PHE A 177 2803 2384 2524 -208 168 -363 C ATOM 1308 CE1 PHE A 177 3.280 0.957 24.305 1.00 21.05 C ANISOU 1308 CE1 PHE A 177 2901 2489 2610 -181 130 -376 C ATOM 1309 CE2 PHE A 177 5.028 -0.410 25.156 1.00 21.83 C ANISOU 1309 CE2 PHE A 177 3010 2574 2709 -189 175 -370 C ATOM 1310 CZ PHE A 177 4.609 0.774 24.636 1.00 21.80 C ANISOU 1310 CZ PHE A 177 3010 2572 2701 -178 159 -377 C ATOM 1311 N GLU A 178 1.609 -5.485 23.513 1.00 23.87 N ANISOU 1311 N GLU A 178 3280 2795 2995 -311 140 -373 N ATOM 1312 CA GLU A 178 1.271 -6.874 23.829 1.00 23.91 C ANISOU 1312 CA GLU A 178 3286 2787 3013 -340 161 -371 C ATOM 1313 C GLU A 178 1.991 -7.112 25.116 1.00 22.97 C ANISOU 1313 C GLU A 178 3162 2670 2898 -321 198 -352 C ATOM 1314 O GLU A 178 3.159 -7.432 25.119 1.00 22.28 O ANISOU 1314 O GLU A 178 3103 2563 2799 -307 218 -344 O ATOM 1315 CB GLU A 178 1.774 -7.844 22.754 1.00 24.88 C ANISOU 1315 CB GLU A 178 3456 2872 3123 -360 166 -378 C ATOM 1316 CG GLU A 178 1.142 -7.704 21.396 1.00 25.45 C ANISOU 1316 CG GLU A 178 3543 2941 3184 -379 127 -399 C ATOM 1317 CD GLU A 178 1.573 -8.844 20.469 1.00 26.74 C ANISOU 1317 CD GLU A 178 3756 3068 3337 -405 139 -407 C ATOM 1318 OE1 GLU A 178 2.649 -8.756 19.847 1.00 25.33 O ANISOU 1318 OE1 GLU A 178 3620 2866 3139 -392 149 -405 O ATOM 1319 OE2 GLU A 178 0.843 -9.847 20.392 1.00 32.09 O ANISOU 1319 OE2 GLU A 178 4429 3737 4027 -440 143 -418 O ATOM 1320 N SER A 179 1.272 -6.926 26.210 1.00 23.99 N ANISOU 1320 N SER A 179 3252 2823 3042 -318 205 -346 N ATOM 1321 CA SER A 179 1.849 -6.647 27.517 1.00 25.92 C ANISOU 1321 CA SER A 179 3484 3080 3283 -290 229 -330 C ATOM 1322 C SER A 179 2.756 -7.710 28.072 1.00 25.57 C ANISOU 1322 C SER A 179 3468 3016 3233 -283 264 -314 C ATOM 1323 O SER A 179 3.703 -7.381 28.755 1.00 25.81 O ANISOU 1323 O SER A 179 3501 3055 3252 -253 276 -304 O ATOM 1324 CB SER A 179 0.728 -6.387 28.520 1.00 26.25 C ANISOU 1324 CB SER A 179 3482 3148 3343 -294 234 -327 C ATOM 1325 OG SER A 179 -0.176 -5.483 27.924 1.00 31.64 O ANISOU 1325 OG SER A 179 4137 3849 4034 -299 200 -342 O ATOM 1326 N LYS A 180 2.474 -8.981 27.789 1.00 25.02 N ANISOU 1326 N LYS A 180 3419 2919 3168 -310 282 -312 N ATOM 1327 CA LYS A 180 3.257 -10.060 28.365 1.00 25.54 C ANISOU 1327 CA LYS A 180 3515 2961 3226 -300 318 -294 C ATOM 1328 C LYS A 180 4.395 -10.534 27.449 1.00 24.75 C ANISOU 1328 C LYS A 180 3458 2833 3115 -294 322 -295 C ATOM 1329 O LYS A 180 5.287 -11.295 27.853 1.00 23.48 O ANISOU 1329 O LYS A 180 3322 2653 2946 -275 350 -280 O ATOM 1330 CB LYS A 180 2.313 -11.215 28.759 1.00 28.28 C ANISOU 1330 CB LYS A 180 3865 3290 3588 -331 346 -289 C ATOM 1331 CG LYS A 180 1.321 -10.787 29.864 1.00 31.73 C ANISOU 1331 CG LYS A 180 4262 3756 4038 -332 353 -285 C ATOM 1332 CD LYS A 180 0.781 -11.980 30.643 1.00 38.71 C ANISOU 1332 CD LYS A 180 5158 4619 4932 -351 397 -272 C ATOM 1333 CE LYS A 180 0.402 -11.567 32.067 1.00 42.04 C ANISOU 1333 CE LYS A 180 5556 5066 5354 -332 416 -258 C ATOM 1334 NZ LYS A 180 -0.641 -10.510 32.014 1.00 43.93 N ANISOU 1334 NZ LYS A 180 5743 5338 5611 -345 389 -276 N ATOM 1335 N LEU A 181 4.386 -10.034 26.229 1.00 23.73 N ANISOU 1335 N LEU A 181 3336 2698 2983 -306 295 -313 N ATOM 1336 CA LEU A 181 5.313 -10.496 25.218 1.00 24.92 C ANISOU 1336 CA LEU A 181 3528 2817 3122 -307 301 -318 C ATOM 1337 C LEU A 181 6.527 -9.560 25.206 1.00 23.83 C ANISOU 1337 C LEU A 181 3390 2690 2973 -272 297 -318 C ATOM 1338 O LEU A 181 6.610 -8.644 24.385 1.00 23.26 O ANISOU 1338 O LEU A 181 3320 2623 2896 -273 274 -333 O ATOM 1339 CB LEU A 181 4.627 -10.499 23.835 1.00 24.47 C ANISOU 1339 CB LEU A 181 3485 2747 3064 -341 275 -340 C ATOM 1340 CG LEU A 181 4.644 -11.708 22.911 1.00 29.01 C ANISOU 1340 CG LEU A 181 4104 3283 3637 -371 289 -348 C ATOM 1341 CD1 LEU A 181 4.478 -11.324 21.440 1.00 23.85 C ANISOU 1341 CD1 LEU A 181 3473 2620 2970 -389 258 -370 C ATOM 1342 CD2 LEU A 181 5.891 -12.599 23.076 1.00 28.98 C ANISOU 1342 CD2 LEU A 181 4137 3247 3628 -353 328 -333 C ATOM 1343 N ARG A 182 7.450 -9.829 26.129 1.00 24.48 N ANISOU 1343 N ARG A 182 3471 2776 3053 -242 319 -303 N ATOM 1344 CA ARG A 182 8.683 -9.078 26.326 1.00 24.49 C ANISOU 1344 CA ARG A 182 3466 2792 3048 -209 320 -306 C ATOM 1345 C ARG A 182 9.705 -9.825 27.131 1.00 23.84 C ANISOU 1345 C ARG A 182 3390 2705 2961 -178 346 -290 C ATOM 1346 O ARG A 182 9.410 -10.771 27.862 1.00 24.38 O ANISOU 1346 O ARG A 182 3466 2767 3030 -174 364 -272 O ATOM 1347 CB ARG A 182 8.442 -7.770 27.034 1.00 24.56 C ANISOU 1347 CB ARG A 182 3435 2839 3056 -195 302 -311 C ATOM 1348 CG ARG A 182 7.535 -7.856 28.175 1.00 29.39 C ANISOU 1348 CG ARG A 182 4021 3473 3672 -194 303 -299 C ATOM 1349 CD ARG A 182 6.550 -6.694 27.941 1.00 33.26 C ANISOU 1349 CD ARG A 182 4485 3984 4168 -207 277 -311 C ATOM 1350 NE ARG A 182 6.806 -5.656 28.886 1.00 29.45 N ANISOU 1350 NE ARG A 182 3974 3535 3683 -183 273 -312 N ATOM 1351 CZ ARG A 182 6.114 -4.536 29.008 1.00 31.93 C ANISOU 1351 CZ ARG A 182 4261 3870 4001 -184 256 -321 C ATOM 1352 NH1 ARG A 182 5.095 -4.218 28.188 1.00 30.89 N ANISOU 1352 NH1 ARG A 182 4126 3733 3876 -204 236 -329 N ATOM 1353 NH2 ARG A 182 6.497 -3.708 29.957 1.00 27.23 N ANISOU 1353 NH2 ARG A 182 3644 3301 3401 -161 259 -323 N ATOM 1354 N GLY A 183 10.918 -9.337 27.032 1.00 22.59 N ANISOU 1354 N GLY A 183 3228 2554 2800 -153 347 -299 N ATOM 1355 CA GLY A 183 11.954 -9.819 27.865 1.00 21.75 C ANISOU 1355 CA GLY A 183 3119 2456 2691 -116 364 -287 C ATOM 1356 C GLY A 183 12.974 -8.733 28.051 1.00 21.26 C ANISOU 1356 C GLY A 183 3028 2420 2628 -93 354 -304 C ATOM 1357 O GLY A 183 13.262 -7.994 27.113 1.00 20.62 O ANISOU 1357 O GLY A 183 2950 2332 2551 -106 349 -324 O ATOM 1358 N SER A 184 13.530 -8.675 29.261 1.00 21.11 N ANISOU 1358 N SER A 184 2985 2432 2603 -58 354 -297 N ATOM 1359 CA SER A 184 14.496 -7.648 29.642 1.00 21.94 C ANISOU 1359 CA SER A 184 3057 2570 2709 -36 345 -317 C ATOM 1360 C SER A 184 15.802 -8.317 30.060 1.00 22.16 C ANISOU 1360 C SER A 184 3081 2604 2736 3 356 -314 C ATOM 1361 O SER A 184 15.823 -9.504 30.373 1.00 21.69 O ANISOU 1361 O SER A 184 3043 2529 2669 20 369 -291 O ATOM 1362 CB SER A 184 13.982 -6.755 30.778 1.00 22.30 C ANISOU 1362 CB SER A 184 3069 2658 2746 -29 328 -319 C ATOM 1363 OG SER A 184 12.990 -5.828 30.343 1.00 24.25 O ANISOU 1363 OG SER A 184 3311 2905 2998 -59 316 -329 O ATOM 1364 N HIS A 185 16.884 -7.543 30.013 1.00 22.03 N ANISOU 1364 N HIS A 185 3037 2608 2726 17 352 -340 N ATOM 1365 CA HIS A 185 18.182 -7.966 30.494 1.00 22.85 C ANISOU 1365 CA HIS A 185 3123 2729 2832 58 357 -344 C ATOM 1366 C HIS A 185 18.886 -6.753 31.053 1.00 23.74 C ANISOU 1366 C HIS A 185 3188 2885 2947 68 341 -374 C ATOM 1367 O HIS A 185 19.033 -5.738 30.374 1.00 22.89 O ANISOU 1367 O HIS A 185 3071 2775 2853 42 344 -402 O ATOM 1368 CB HIS A 185 19.048 -8.534 29.348 1.00 22.81 C ANISOU 1368 CB HIS A 185 3138 2687 2842 56 379 -352 C ATOM 1369 CG HIS A 185 20.381 -9.009 29.820 1.00 24.18 C ANISOU 1369 CG HIS A 185 3289 2879 3021 102 383 -357 C ATOM 1370 ND1 HIS A 185 20.577 -10.281 30.316 1.00 26.46 N ANISOU 1370 ND1 HIS A 185 3596 3158 3299 138 391 -328 N ATOM 1371 CD2 HIS A 185 21.571 -8.377 29.911 1.00 23.24 C ANISOU 1371 CD2 HIS A 185 3128 2787 2915 119 380 -387 C ATOM 1372 CE1 HIS A 185 21.840 -10.413 30.681 1.00 27.55 C ANISOU 1372 CE1 HIS A 185 3703 3320 3444 180 389 -339 C ATOM 1373 NE2 HIS A 185 22.460 -9.270 30.451 1.00 27.65 N ANISOU 1373 NE2 HIS A 185 3677 3357 3472 168 382 -377 N ATOM 1374 N MET A 186 19.324 -6.865 32.295 1.00 25.61 N ANISOU 1374 N MET A 186 3398 3163 3170 106 327 -371 N ATOM 1375 CA MET A 186 19.971 -5.779 32.994 1.00 28.33 C ANISOU 1375 CA MET A 186 3696 3555 3515 117 310 -402 C ATOM 1376 C MET A 186 21.083 -6.391 33.788 1.00 29.28 C ANISOU 1376 C MET A 186 3792 3706 3628 168 301 -403 C ATOM 1377 O MET A 186 20.961 -7.535 34.279 1.00 29.16 O ANISOU 1377 O MET A 186 3800 3685 3595 200 302 -369 O ATOM 1378 CB MET A 186 18.979 -5.028 33.922 1.00 28.69 C ANISOU 1378 CB MET A 186 3732 3628 3542 108 293 -399 C ATOM 1379 CG MET A 186 17.767 -4.449 33.177 1.00 27.70 C ANISOU 1379 CG MET A 186 3628 3474 3424 62 300 -396 C ATOM 1380 SD MET A 186 17.164 -2.843 33.749 1.00 32.24 S ANISOU 1380 SD MET A 186 4175 4079 3995 43 287 -419 S ATOM 1381 CE MET A 186 15.766 -2.645 32.607 1.00 27.90 C ANISOU 1381 CE MET A 186 3660 3486 3455 0 295 -405 C ATOM 1382 N ALA A 187 22.156 -5.621 33.925 1.00 30.72 N ANISOU 1382 N ALA A 187 3928 3922 3822 177 292 -442 N ATOM 1383 CA ALA A 187 23.420 -6.117 34.465 1.00 32.26 C ANISOU 1383 CA ALA A 187 4091 4149 4018 225 282 -452 C ATOM 1384 C ALA A 187 24.313 -4.952 34.845 1.00 33.27 C ANISOU 1384 C ALA A 187 4159 4324 4157 224 267 -503 C ATOM 1385 O ALA A 187 24.136 -3.821 34.346 1.00 33.17 O ANISOU 1385 O ALA A 187 4138 4306 4161 180 276 -532 O ATOM 1386 CB ALA A 187 24.127 -6.991 33.411 1.00 32.51 C ANISOU 1386 CB ALA A 187 4138 4141 4072 233 307 -448 C ATOM 1387 N HIS A 188 25.267 -5.229 35.731 1.00 34.63 N ANISOU 1387 N HIS A 188 4294 4544 4320 272 244 -514 N ATOM 1388 CA HIS A 188 26.291 -4.264 36.091 1.00 35.88 C ANISOU 1388 CA HIS A 188 4388 4751 4493 273 228 -569 C ATOM 1389 C HIS A 188 27.508 -4.470 35.199 1.00 36.59 C ANISOU 1389 C HIS A 188 4451 4830 4621 277 248 -597 C ATOM 1390 O HIS A 188 28.269 -5.420 35.395 1.00 35.97 O ANISOU 1390 O HIS A 188 4360 4763 4543 326 240 -587 O ATOM 1391 CB HIS A 188 26.693 -4.431 37.553 1.00 36.54 C ANISOU 1391 CB HIS A 188 4441 4899 4545 326 188 -570 C ATOM 1392 CG HIS A 188 27.859 -3.584 37.969 1.00 37.55 C ANISOU 1392 CG HIS A 188 4497 5083 4687 331 168 -630 C ATOM 1393 ND1 HIS A 188 27.911 -2.221 37.754 1.00 38.37 N ANISOU 1393 ND1 HIS A 188 4572 5195 4811 281 177 -679 N ATOM 1394 CD2 HIS A 188 29.015 -3.909 38.596 1.00 39.16 C ANISOU 1394 CD2 HIS A 188 4651 5338 4889 381 140 -652 C ATOM 1395 CE1 HIS A 188 29.038 -1.741 38.246 1.00 37.79 C ANISOU 1395 CE1 HIS A 188 4433 5175 4748 295 156 -730 C ATOM 1396 NE2 HIS A 188 29.722 -2.743 38.771 1.00 39.62 N ANISOU 1396 NE2 HIS A 188 4649 5438 4968 357 131 -716 N ATOM 1397 N VAL A 189 27.681 -3.583 34.221 1.00 37.16 N ANISOU 1397 N VAL A 189 4516 4878 4726 227 276 -631 N ATOM 1398 CA VAL A 189 28.868 -3.619 33.355 1.00 38.78 C ANISOU 1398 CA VAL A 189 4692 5071 4971 223 301 -665 C ATOM 1399 C VAL A 189 29.455 -2.228 33.156 1.00 39.32 C ANISOU 1399 C VAL A 189 4715 5157 5068 183 314 -726 C ATOM 1400 O VAL A 189 28.772 -1.205 33.295 1.00 40.11 O ANISOU 1400 O VAL A 189 4823 5256 5159 146 314 -737 O ATOM 1401 CB VAL A 189 28.580 -4.229 31.957 1.00 38.64 C ANISOU 1401 CB VAL A 189 4729 4982 4970 201 342 -640 C ATOM 1402 CG1 VAL A 189 28.313 -5.724 32.069 1.00 39.45 C ANISOU 1402 CG1 VAL A 189 4871 5066 5054 243 337 -588 C ATOM 1403 CG2 VAL A 189 27.407 -3.482 31.237 1.00 38.75 C ANISOU 1403 CG2 VAL A 189 4791 4953 4978 144 360 -631 C ATOM 1404 N TYR A 190 30.727 -2.207 32.808 1.00 39.91 N ANISOU 1404 N TYR A 190 4742 5243 5178 189 328 -766 N ATOM 1405 CA TYR A 190 31.423 -0.983 32.493 1.00 39.85 C ANISOU 1405 CA TYR A 190 4691 5246 5205 148 350 -829 C ATOM 1406 C TYR A 190 31.821 -0.985 31.012 1.00 40.47 C ANISOU 1406 C TYR A 190 4792 5264 5319 115 405 -840 C ATOM 1407 O TYR A 190 32.997 -0.831 30.669 1.00 41.46 O ANISOU 1407 O TYR A 190 4869 5399 5484 112 427 -885 O ATOM 1408 CB TYR A 190 32.648 -0.848 33.398 1.00 39.63 C ANISOU 1408 CB TYR A 190 4577 5289 5190 180 322 -877 C ATOM 1409 CG TYR A 190 32.369 -0.309 34.804 1.00 37.47 C ANISOU 1409 CG TYR A 190 4275 5078 4884 194 273 -889 C ATOM 1410 CD1 TYR A 190 32.528 -1.123 35.926 1.00 36.94 C ANISOU 1410 CD1 TYR A 190 4189 5063 4785 257 224 -868 C ATOM 1411 CD2 TYR A 190 31.985 1.030 35.007 1.00 37.94 C ANISOU 1411 CD2 TYR A 190 4328 5143 4942 145 280 -923 C ATOM 1412 CE1 TYR A 190 32.300 -0.627 37.233 1.00 38.83 C ANISOU 1412 CE1 TYR A 190 4405 5360 4989 271 180 -880 C ATOM 1413 CE2 TYR A 190 31.778 1.545 36.294 1.00 37.19 C ANISOU 1413 CE2 TYR A 190 4207 5106 4818 157 239 -938 C ATOM 1414 CZ TYR A 190 31.935 0.704 37.409 1.00 38.23 C ANISOU 1414 CZ TYR A 190 4321 5291 4915 219 188 -917 C ATOM 1415 OH TYR A 190 31.734 1.185 38.685 1.00 36.97 O ANISOU 1415 OH TYR A 190 4140 5187 4720 232 147 -931 O ATOM 1416 N ASP A 191 30.822 -1.142 30.146 1.00 40.51 N ANISOU 1416 N ASP A 191 4870 5209 5311 89 428 -801 N ATOM 1417 CA ASP A 191 31.025 -1.179 28.696 1.00 41.64 C ANISOU 1417 CA ASP A 191 5051 5290 5480 58 480 -804 C ATOM 1418 C ASP A 191 31.164 0.218 28.089 1.00 42.19 C ANISOU 1418 C ASP A 191 5119 5339 5571 3 517 -848 C ATOM 1419 O ASP A 191 32.044 0.465 27.238 1.00 42.46 O ANISOU 1419 O ASP A 191 5143 5349 5641 -18 562 -883 O ATOM 1420 CB ASP A 191 29.890 -1.933 28.010 1.00 40.95 C ANISOU 1420 CB ASP A 191 5044 5149 5366 54 485 -747 C ATOM 1421 CG ASP A 191 28.507 -1.366 28.338 1.00 41.29 C ANISOU 1421 CG ASP A 191 5124 5189 5377 33 464 -721 C ATOM 1422 OD1 ASP A 191 27.599 -1.551 27.496 1.00 42.41 O ANISOU 1422 OD1 ASP A 191 5329 5282 5505 11 477 -690 O ATOM 1423 OD2 ASP A 191 28.332 -0.729 29.408 1.00 39.89 O ANISOU 1423 OD2 ASP A 191 4912 5058 5188 38 434 -734 O ATOM 1424 N PHE A 192 30.290 1.118 28.548 1.00 41.71 N ANISOU 1424 N PHE A 192 5072 5287 5488 -19 501 -846 N ATOM 1425 CA PHE A 192 30.235 2.489 28.097 1.00 41.47 C ANISOU 1425 CA PHE A 192 5049 5236 5471 -68 534 -881 C ATOM 1426 C PHE A 192 29.537 3.260 29.196 1.00 41.55 C ANISOU 1426 C PHE A 192 5044 5284 5457 -71 500 -884 C ATOM 1427 O PHE A 192 28.402 2.937 29.583 1.00 40.49 O ANISOU 1427 O PHE A 192 4945 5150 5289 -57 469 -838 O ATOM 1428 CB PHE A 192 29.438 2.571 26.793 1.00 41.74 C ANISOU 1428 CB PHE A 192 5165 5199 5497 -97 568 -851 C ATOM 1429 CG PHE A 192 29.307 3.967 26.234 1.00 42.37 C ANISOU 1429 CG PHE A 192 5266 5248 5586 -144 606 -881 C ATOM 1430 CD1 PHE A 192 30.109 4.379 25.164 1.00 44.91 C ANISOU 1430 CD1 PHE A 192 5599 5528 5937 -174 664 -913 C ATOM 1431 CD2 PHE A 192 28.362 4.853 26.744 1.00 41.75 C ANISOU 1431 CD2 PHE A 192 5201 5177 5484 -157 589 -874 C ATOM 1432 CE1 PHE A 192 29.975 5.670 24.622 1.00 44.62 C ANISOU 1432 CE1 PHE A 192 5592 5457 5907 -215 706 -938 C ATOM 1433 CE2 PHE A 192 28.225 6.144 26.211 1.00 44.12 C ANISOU 1433 CE2 PHE A 192 5527 5444 5791 -196 627 -898 C ATOM 1434 CZ PHE A 192 29.030 6.548 25.159 1.00 42.21 C ANISOU 1434 CZ PHE A 192 5301 5160 5578 -225 686 -929 C ATOM 1435 N TYR A 193 30.224 4.271 29.712 1.00 42.02 N ANISOU 1435 N TYR A 193 5052 5377 5537 -90 506 -940 N ATOM 1436 CA TYR A 193 29.711 5.078 30.819 1.00 42.28 C ANISOU 1436 CA TYR A 193 5065 5449 5549 -93 477 -951 C ATOM 1437 C TYR A 193 30.375 6.459 30.785 1.00 43.26 C ANISOU 1437 C TYR A 193 5156 5577 5702 -137 511 -1017 C ATOM 1438 O TYR A 193 31.377 6.658 30.075 1.00 41.98 O ANISOU 1438 O TYR A 193 4973 5397 5579 -158 553 -1057 O ATOM 1439 CB TYR A 193 29.911 4.366 32.177 1.00 42.05 C ANISOU 1439 CB TYR A 193 4989 5490 5500 -45 420 -945 C ATOM 1440 CG TYR A 193 31.336 3.872 32.470 1.00 42.94 C ANISOU 1440 CG TYR A 193 5030 5645 5639 -19 411 -983 C ATOM 1441 CD1 TYR A 193 32.078 4.397 33.543 1.00 42.74 C ANISOU 1441 CD1 TYR A 193 4934 5687 5619 -12 384 -1036 C ATOM 1442 CD2 TYR A 193 31.934 2.873 31.681 1.00 43.49 C ANISOU 1442 CD2 TYR A 193 5104 5691 5729 0 429 -969 C ATOM 1443 CE1 TYR A 193 33.381 3.949 33.819 1.00 42.15 C ANISOU 1443 CE1 TYR A 193 4789 5658 5570 15 371 -1074 C ATOM 1444 CE2 TYR A 193 33.249 2.415 31.943 1.00 43.69 C ANISOU 1444 CE2 TYR A 193 5061 5757 5781 29 420 -1006 C ATOM 1445 CZ TYR A 193 33.962 2.957 33.008 1.00 44.47 C ANISOU 1445 CZ TYR A 193 5085 5925 5886 37 390 -1058 C ATOM 1446 OH TYR A 193 35.242 2.494 33.261 1.00 43.49 O ANISOU 1446 OH TYR A 193 4888 5846 5790 68 378 -1094 O ATOM 1447 N LYS A 194 29.804 7.396 31.549 1.00 43.73 N ANISOU 1447 N LYS A 194 5213 5656 5745 -151 498 -1030 N ATOM 1448 CA LYS A 194 30.290 8.776 31.618 1.00 45.51 C ANISOU 1448 CA LYS A 194 5414 5883 5996 -195 532 -1092 C ATOM 1449 C LYS A 194 30.599 9.179 33.075 1.00 45.88 C ANISOU 1449 C LYS A 194 5398 6003 6033 -186 492 -1131 C ATOM 1450 O LYS A 194 29.781 9.810 33.743 1.00 45.31 O ANISOU 1450 O LYS A 194 5341 5940 5935 -192 477 -1124 O ATOM 1451 CB LYS A 194 29.287 9.724 30.939 1.00 45.26 C ANISOU 1451 CB LYS A 194 5452 5792 5954 -229 568 -1074 C ATOM 1452 CG LYS A 194 29.043 9.371 29.466 1.00 46.52 C ANISOU 1452 CG LYS A 194 5675 5880 6118 -238 606 -1040 C ATOM 1453 CD LYS A 194 28.409 10.507 28.665 1.00 46.62 C ANISOU 1453 CD LYS A 194 5751 5833 6129 -275 652 -1039 C ATOM 1454 CE LYS A 194 28.241 10.091 27.192 1.00 49.66 C ANISOU 1454 CE LYS A 194 6201 6153 6515 -280 687 -1007 C ATOM 1455 NZ LYS A 194 27.586 11.174 26.406 1.00 54.20 N ANISOU 1455 NZ LYS A 194 6843 6669 7083 -308 728 -1001 N ATOM 1456 N PRO A 195 31.791 8.785 33.572 1.00 47.38 N ANISOU 1456 N PRO A 195 5513 6245 6242 -169 473 -1172 N ATOM 1457 CA PRO A 195 32.166 8.894 34.996 1.00 48.00 C ANISOU 1457 CA PRO A 195 5529 6404 6306 -148 423 -1206 C ATOM 1458 C PRO A 195 32.811 10.217 35.409 1.00 49.52 C ANISOU 1458 C PRO A 195 5673 6619 6522 -193 443 -1286 C ATOM 1459 O PRO A 195 32.923 10.509 36.607 1.00 48.96 O ANISOU 1459 O PRO A 195 5561 6610 6433 -183 403 -1315 O ATOM 1460 CB PRO A 195 33.157 7.745 35.166 1.00 48.09 C ANISOU 1460 CB PRO A 195 5487 6456 6329 -103 393 -1210 C ATOM 1461 CG PRO A 195 33.819 7.610 33.791 1.00 47.67 C ANISOU 1461 CG PRO A 195 5442 6350 6321 -126 450 -1221 C ATOM 1462 CD PRO A 195 32.870 8.170 32.762 1.00 47.60 C ANISOU 1462 CD PRO A 195 5515 6262 6309 -165 499 -1190 C ATOM 1463 N ASN A 196 33.235 10.984 34.404 1.00 51.01 N ANISOU 1463 N ASN A 196 5871 6757 6752 -243 509 -1322 N ATOM 1464 CA ASN A 196 33.845 12.299 34.565 1.00 53.12 C ANISOU 1464 CA ASN A 196 6103 7030 7050 -296 546 -1400 C ATOM 1465 C ASN A 196 32.755 13.357 34.376 1.00 53.46 C ANISOU 1465 C ASN A 196 6216 7022 7076 -330 579 -1383 C ATOM 1466 O ASN A 196 32.322 13.639 33.247 1.00 52.62 O ANISOU 1466 O ASN A 196 6174 6843 6978 -352 630 -1357 O ATOM 1467 CB ASN A 196 34.958 12.470 33.520 1.00 53.65 C ANISOU 1467 CB ASN A 196 6145 7065 7174 -331 607 -1446 C ATOM 1468 CG ASN A 196 35.903 13.623 33.836 1.00 55.19 C ANISOU 1468 CG ASN A 196 6278 7282 7408 -383 640 -1540 C ATOM 1469 OD1 ASN A 196 35.564 14.558 34.570 1.00 54.95 O ANISOU 1469 OD1 ASN A 196 6246 7268 7364 -407 635 -1569 O ATOM 1470 ND2 ASN A 196 37.103 13.562 33.258 1.00 56.32 N ANISOU 1470 ND2 ASN A 196 6371 7424 7604 -403 678 -1592 N ATOM 1471 N LEU A 197 32.293 13.915 35.489 1.00 54.66 N ANISOU 1471 N LEU A 197 6356 7212 7199 -330 547 -1396 N ATOM 1472 CA LEU A 197 31.130 14.797 35.477 1.00 56.14 C ANISOU 1472 CA LEU A 197 6609 7358 7364 -349 569 -1371 C ATOM 1473 C LEU A 197 31.374 16.064 34.665 1.00 57.28 C ANISOU 1473 C LEU A 197 6779 7442 7544 -409 647 -1415 C ATOM 1474 O LEU A 197 30.430 16.665 34.159 1.00 57.12 O ANISOU 1474 O LEU A 197 6829 7363 7510 -422 679 -1382 O ATOM 1475 CB LEU A 197 30.693 15.139 36.915 1.00 56.29 C ANISOU 1475 CB LEU A 197 6606 7434 7348 -337 522 -1383 C ATOM 1476 CG LEU A 197 29.643 14.258 37.621 1.00 56.34 C ANISOU 1476 CG LEU A 197 6639 7465 7302 -284 463 -1313 C ATOM 1477 CD1 LEU A 197 29.822 12.739 37.406 1.00 56.45 C ANISOU 1477 CD1 LEU A 197 6645 7495 7307 -234 425 -1265 C ATOM 1478 CD2 LEU A 197 29.625 14.582 39.105 1.00 56.30 C ANISOU 1478 CD2 LEU A 197 6596 7529 7267 -274 419 -1344 C ATOM 1479 N ALA A 198 32.645 16.442 34.530 1.00 59.29 N ANISOU 1479 N ALA A 198 6976 7710 7843 -443 679 -1488 N ATOM 1480 CA ALA A 198 33.030 17.693 33.885 1.00 61.26 C ANISOU 1480 CA ALA A 198 7242 7905 8128 -505 758 -1541 C ATOM 1481 C ALA A 198 33.200 17.641 32.343 1.00 62.25 C ANISOU 1481 C ALA A 198 7420 7951 8281 -523 825 -1521 C ATOM 1482 O ALA A 198 33.490 18.674 31.727 1.00 62.90 O ANISOU 1482 O ALA A 198 7528 7980 8392 -573 899 -1560 O ATOM 1483 CB ALA A 198 34.287 18.266 34.563 1.00 61.96 C ANISOU 1483 CB ALA A 198 7242 8047 8254 -541 766 -1639 C ATOM 1484 N SER A 199 33.006 16.466 31.729 1.00 63.10 N ANISOU 1484 N SER A 199 7550 8048 8377 -484 802 -1462 N ATOM 1485 CA SER A 199 33.167 16.305 30.264 1.00 63.97 C ANISOU 1485 CA SER A 199 7713 8085 8507 -497 861 -1441 C ATOM 1486 C SER A 199 32.196 15.321 29.625 1.00 64.17 C ANISOU 1486 C SER A 199 7804 8080 8497 -455 834 -1353 C ATOM 1487 O SER A 199 31.723 14.399 30.286 1.00 64.29 O ANISOU 1487 O SER A 199 7804 8140 8482 -410 767 -1312 O ATOM 1488 CB SER A 199 34.597 15.881 29.909 1.00 64.63 C ANISOU 1488 CB SER A 199 7732 8185 8640 -510 886 -1493 C ATOM 1489 OG SER A 199 34.754 14.481 29.991 1.00 63.23 O ANISOU 1489 OG SER A 199 7527 8044 8452 -460 832 -1456 O ATOM 1490 N GLU A 200 31.940 15.508 28.326 1.00 65.01 N ANISOU 1490 N GLU A 200 7986 8110 8607 -470 889 -1327 N ATOM 1491 CA GLU A 200 31.045 14.637 27.541 1.00 65.21 C ANISOU 1491 CA GLU A 200 8078 8099 8599 -436 870 -1250 C ATOM 1492 C GLU A 200 31.707 13.334 27.068 1.00 65.22 C ANISOU 1492 C GLU A 200 8057 8110 8614 -413 858 -1236 C ATOM 1493 O GLU A 200 31.020 12.442 26.555 1.00 64.77 O ANISOU 1493 O GLU A 200 8046 8034 8530 -382 834 -1174 O ATOM 1494 CB GLU A 200 30.481 15.402 26.335 1.00 65.46 C ANISOU 1494 CB GLU A 200 8204 8046 8623 -460 931 -1228 C ATOM 1495 CG GLU A 200 29.080 16.008 26.539 1.00 67.69 C ANISOU 1495 CG GLU A 200 8544 8310 8866 -448 913 -1185 C ATOM 1496 CD GLU A 200 27.938 15.119 26.015 1.00 70.51 C ANISOU 1496 CD GLU A 200 8959 8649 9183 -409 872 -1107 C ATOM 1497 OE1 GLU A 200 26.752 15.454 26.275 1.00 70.61 O ANISOU 1497 OE1 GLU A 200 9008 8657 9165 -394 847 -1070 O ATOM 1498 OE2 GLU A 200 28.221 14.094 25.340 1.00 71.37 O ANISOU 1498 OE2 GLU A 200 9075 8748 9294 -395 867 -1084 O ATOM 1499 N TYR A 201 33.031 13.237 27.233 1.00 65.94 N ANISOU 1499 N TYR A 201 8075 8231 8747 -427 876 -1295 N ATOM 1500 CA TYR A 201 33.796 12.049 26.817 1.00 66.09 C ANISOU 1500 CA TYR A 201 8065 8261 8786 -403 870 -1290 C ATOM 1501 C TYR A 201 33.482 10.860 27.731 1.00 64.71 C ANISOU 1501 C TYR A 201 7855 8148 8583 -347 788 -1251 C ATOM 1502 O TYR A 201 33.489 10.996 28.963 1.00 64.85 O ANISOU 1502 O TYR A 201 7819 8230 8592 -334 740 -1270 O ATOM 1503 CB TYR A 201 35.325 12.323 26.698 1.00 68.15 C ANISOU 1503 CB TYR A 201 8254 8535 9104 -434 917 -1368 C ATOM 1504 CG TYR A 201 36.180 12.197 27.979 1.00 71.00 C ANISOU 1504 CG TYR A 201 8505 8986 9487 -422 870 -1423 C ATOM 1505 CD1 TYR A 201 36.923 13.293 28.465 1.00 73.34 C ANISOU 1505 CD1 TYR A 201 8744 9305 9818 -466 900 -1503 C ATOM 1506 CD2 TYR A 201 36.283 10.972 28.680 1.00 72.92 C ANISOU 1506 CD2 TYR A 201 8702 9290 9714 -365 799 -1396 C ATOM 1507 CE1 TYR A 201 37.715 13.179 29.638 1.00 73.97 C ANISOU 1507 CE1 TYR A 201 8721 9472 9914 -454 852 -1557 C ATOM 1508 CE2 TYR A 201 37.062 10.852 29.854 1.00 73.27 C ANISOU 1508 CE2 TYR A 201 8648 9418 9772 -348 752 -1445 C ATOM 1509 CZ TYR A 201 37.775 11.952 30.323 1.00 73.43 C ANISOU 1509 CZ TYR A 201 8610 9465 9825 -392 776 -1526 C ATOM 1510 OH TYR A 201 38.548 11.821 31.466 1.00 73.16 O ANISOU 1510 OH TYR A 201 8479 9518 9802 -374 724 -1576 O ATOM 1511 N PRO A 202 33.161 9.702 27.126 1.00 63.26 N ANISOU 1511 N PRO A 202 7709 7944 8384 -315 773 -1195 N ATOM 1512 CA PRO A 202 32.877 8.506 27.906 1.00 62.06 C ANISOU 1512 CA PRO A 202 7532 7842 8206 -262 703 -1155 C ATOM 1513 C PRO A 202 34.116 7.630 28.098 1.00 61.46 C ANISOU 1513 C PRO A 202 7385 7806 8162 -236 694 -1183 C ATOM 1514 O PRO A 202 35.110 7.781 27.357 1.00 61.64 O ANISOU 1514 O PRO A 202 7387 7806 8227 -260 746 -1224 O ATOM 1515 CB PRO A 202 31.859 7.776 27.031 1.00 61.49 C ANISOU 1515 CB PRO A 202 7545 7717 8103 -246 702 -1084 C ATOM 1516 CG PRO A 202 32.212 8.188 25.615 1.00 62.00 C ANISOU 1516 CG PRO A 202 7657 7711 8190 -283 774 -1097 C ATOM 1517 CD PRO A 202 33.014 9.455 25.676 1.00 63.06 C ANISOU 1517 CD PRO A 202 7757 7844 8360 -327 823 -1166 C ATOM 1518 N VAL A 203 34.064 6.736 29.085 1.00 60.03 N ANISOU 1518 N VAL A 203 7165 7683 7959 -186 629 -1161 N ATOM 1519 CA VAL A 203 34.970 5.602 29.094 1.00 59.27 C ANISOU 1519 CA VAL A 203 7024 7613 7883 -147 616 -1163 C ATOM 1520 C VAL A 203 34.294 4.486 28.298 1.00 58.61 C ANISOU 1520 C VAL A 203 7011 7481 7776 -123 617 -1094 C ATOM 1521 O VAL A 203 33.133 4.148 28.541 1.00 57.74 O ANISOU 1521 O VAL A 203 6952 7363 7624 -106 584 -1038 O ATOM 1522 CB VAL A 203 35.365 5.127 30.499 1.00 59.49 C ANISOU 1522 CB VAL A 203 6979 7726 7899 -100 549 -1175 C ATOM 1523 CG1 VAL A 203 36.180 3.841 30.395 1.00 59.00 C ANISOU 1523 CG1 VAL A 203 6884 7682 7853 -51 535 -1165 C ATOM 1524 CG2 VAL A 203 36.185 6.202 31.218 1.00 60.10 C ANISOU 1524 CG2 VAL A 203 6979 7855 8003 -128 549 -1254 C ATOM 1525 N VAL A 204 35.019 3.964 27.314 1.00 58.33 N ANISOU 1525 N VAL A 204 6981 7411 7771 -125 659 -1100 N ATOM 1526 CA VAL A 204 34.511 2.906 26.456 1.00 57.88 C ANISOU 1526 CA VAL A 204 6991 7303 7697 -106 667 -1042 C ATOM 1527 C VAL A 204 35.471 1.724 26.488 1.00 58.07 C ANISOU 1527 C VAL A 204 6972 7349 7744 -62 660 -1044 C ATOM 1528 O VAL A 204 36.699 1.883 26.426 1.00 58.30 O ANISOU 1528 O VAL A 204 6936 7398 7818 -66 685 -1098 O ATOM 1529 CB VAL A 204 34.281 3.364 24.976 1.00 57.90 C ANISOU 1529 CB VAL A 204 7067 7225 7707 -152 733 -1039 C ATOM 1530 CG1 VAL A 204 33.531 2.266 24.166 1.00 57.59 C ANISOU 1530 CG1 VAL A 204 7105 7137 7639 -133 732 -975 C ATOM 1531 CG2 VAL A 204 33.521 4.689 24.908 1.00 57.30 C ANISOU 1531 CG2 VAL A 204 7028 7127 7615 -194 748 -1046 C ATOM 1532 N ASP A 205 34.876 0.545 26.613 1.00 57.44 N ANISOU 1532 N ASP A 205 6927 7265 7632 -20 628 -985 N ATOM 1533 CA ASP A 205 35.575 -0.724 26.627 1.00 57.80 C ANISOU 1533 CA ASP A 205 6949 7322 7691 29 620 -972 C ATOM 1534 C ASP A 205 34.980 -1.487 25.438 1.00 57.28 C ANISOU 1534 C ASP A 205 6970 7183 7612 22 652 -925 C ATOM 1535 O ASP A 205 33.980 -2.198 25.590 1.00 56.28 O ANISOU 1535 O ASP A 205 6895 7043 7446 41 623 -869 O ATOM 1536 CB ASP A 205 35.305 -1.418 27.977 1.00 57.84 C ANISOU 1536 CB ASP A 205 6925 7387 7664 86 551 -944 C ATOM 1537 CG ASP A 205 36.071 -2.726 28.156 1.00 59.05 C ANISOU 1537 CG ASP A 205 7049 7558 7828 147 538 -930 C ATOM 1538 OD1 ASP A 205 36.166 -3.520 27.192 1.00 59.51 O ANISOU 1538 OD1 ASP A 205 7150 7565 7896 151 574 -906 O ATOM 1539 OD2 ASP A 205 36.543 -2.982 29.291 1.00 59.31 O ANISOU 1539 OD2 ASP A 205 7022 7658 7856 194 490 -940 O ATOM 1540 N GLY A 206 35.583 -1.303 24.256 1.00 57.09 N ANISOU 1540 N GLY A 206 6963 7110 7620 -9 715 -949 N ATOM 1541 CA GLY A 206 35.029 -1.803 22.986 1.00 56.88 C ANISOU 1541 CA GLY A 206 7025 7009 7578 -26 752 -913 C ATOM 1542 C GLY A 206 34.813 -3.304 22.997 1.00 56.82 C ANISOU 1542 C GLY A 206 7044 6992 7553 21 732 -864 C ATOM 1543 O GLY A 206 33.785 -3.814 22.529 1.00 56.27 O ANISOU 1543 O GLY A 206 7049 6882 7449 15 727 -816 O ATOM 1544 N LYS A 207 35.817 -3.990 23.539 1.00 57.29 N ANISOU 1544 N LYS A 207 7039 7090 7639 66 722 -878 N ATOM 1545 CA LYS A 207 35.802 -5.416 23.843 1.00 57.10 C ANISOU 1545 CA LYS A 207 7024 7069 7601 122 698 -836 C ATOM 1546 C LYS A 207 34.524 -5.815 24.615 1.00 55.86 C ANISOU 1546 C LYS A 207 6906 6925 7394 140 645 -783 C ATOM 1547 O LYS A 207 33.729 -6.641 24.132 1.00 55.53 O ANISOU 1547 O LYS A 207 6935 6838 7326 142 649 -736 O ATOM 1548 CB LYS A 207 37.095 -5.741 24.627 1.00 58.25 C ANISOU 1548 CB LYS A 207 7076 7275 7782 172 683 -870 C ATOM 1549 CG LYS A 207 37.022 -6.828 25.702 1.00 60.38 C ANISOU 1549 CG LYS A 207 7328 7585 8027 243 629 -832 C ATOM 1550 CD LYS A 207 37.866 -6.428 26.935 1.00 63.12 C ANISOU 1550 CD LYS A 207 7575 8018 8389 279 585 -872 C ATOM 1551 CE LYS A 207 37.937 -7.557 27.970 1.00 64.81 C ANISOU 1551 CE LYS A 207 7773 8272 8578 358 534 -834 C ATOM 1552 NZ LYS A 207 36.578 -7.961 28.479 1.00 64.03 N ANISOU 1552 NZ LYS A 207 7744 8162 8423 365 501 -773 N ATOM 1553 N LEU A 208 34.324 -5.210 25.787 1.00 54.29 N ANISOU 1553 N LEU A 208 6663 6785 7181 149 598 -792 N ATOM 1554 CA LEU A 208 33.213 -5.574 26.665 1.00 53.03 C ANISOU 1554 CA LEU A 208 6531 6644 6976 170 550 -745 C ATOM 1555 C LEU A 208 31.886 -5.180 26.058 1.00 51.65 C ANISOU 1555 C LEU A 208 6430 6422 6772 123 557 -718 C ATOM 1556 O LEU A 208 30.883 -5.886 26.230 1.00 51.33 O ANISOU 1556 O LEU A 208 6438 6366 6699 134 538 -669 O ATOM 1557 CB LEU A 208 33.333 -4.888 28.019 1.00 52.86 C ANISOU 1557 CB LEU A 208 6446 6694 6945 186 502 -768 C ATOM 1558 CG LEU A 208 33.150 -5.695 29.301 1.00 53.16 C ANISOU 1558 CG LEU A 208 6468 6779 6951 246 450 -735 C ATOM 1559 CD1 LEU A 208 32.780 -4.744 30.419 1.00 50.86 C ANISOU 1559 CD1 LEU A 208 6143 6542 6638 240 409 -752 C ATOM 1560 CD2 LEU A 208 32.143 -6.829 29.188 1.00 52.77 C ANISOU 1560 CD2 LEU A 208 6493 6689 6868 264 446 -670 C ATOM 1561 N SER A 209 31.888 -4.049 25.356 1.00 50.12 N ANISOU 1561 N SER A 209 6244 6207 6593 72 587 -750 N ATOM 1562 CA SER A 209 30.655 -3.470 24.845 1.00 48.57 C ANISOU 1562 CA SER A 209 6110 5975 6370 30 590 -729 C ATOM 1563 C SER A 209 29.978 -4.365 23.800 1.00 46.97 C ANISOU 1563 C SER A 209 5986 5710 6150 22 609 -689 C ATOM 1564 O SER A 209 28.767 -4.532 23.841 1.00 46.34 O ANISOU 1564 O SER A 209 5951 5617 6038 14 587 -652 O ATOM 1565 CB SER A 209 30.888 -2.058 24.301 1.00 48.15 C ANISOU 1565 CB SER A 209 6053 5909 6335 -18 622 -772 C ATOM 1566 OG SER A 209 31.259 -2.147 22.951 1.00 49.25 O ANISOU 1566 OG SER A 209 6233 5990 6490 -42 675 -780 O ATOM 1567 N GLN A 210 30.744 -4.941 22.875 1.00 46.24 N ANISOU 1567 N GLN A 210 5908 5581 6080 23 651 -697 N ATOM 1568 CA GLN A 210 30.144 -5.873 21.900 1.00 45.26 C ANISOU 1568 CA GLN A 210 5860 5399 5938 16 668 -662 C ATOM 1569 C GLN A 210 29.625 -7.128 22.573 1.00 43.59 C ANISOU 1569 C GLN A 210 5660 5197 5705 55 636 -618 C ATOM 1570 O GLN A 210 28.499 -7.507 22.350 1.00 42.70 O ANISOU 1570 O GLN A 210 5602 5059 5563 41 624 -584 O ATOM 1571 CB GLN A 210 31.079 -6.203 20.728 1.00 46.66 C ANISOU 1571 CB GLN A 210 6056 5531 6142 8 725 -682 C ATOM 1572 CG GLN A 210 31.009 -5.169 19.556 1.00 50.05 C ANISOU 1572 CG GLN A 210 6527 5917 6573 -44 767 -706 C ATOM 1573 CD GLN A 210 29.569 -4.765 19.134 1.00 52.78 C ANISOU 1573 CD GLN A 210 6940 6237 6878 -76 748 -677 C ATOM 1574 OE1 GLN A 210 28.907 -3.926 19.788 1.00 53.11 O ANISOU 1574 OE1 GLN A 210 6966 6308 6906 -85 715 -676 O ATOM 1575 NE2 GLN A 210 29.093 -5.355 18.028 1.00 53.38 N ANISOU 1575 NE2 GLN A 210 7090 6257 6933 -91 767 -657 N ATOM 1576 N THR A 211 30.439 -7.734 23.433 1.00 42.98 N ANISOU 1576 N THR A 211 5531 5158 5642 104 623 -620 N ATOM 1577 CA THR A 211 30.012 -8.839 24.296 1.00 42.12 C ANISOU 1577 CA THR A 211 5428 5064 5510 147 591 -578 C ATOM 1578 C THR A 211 28.734 -8.517 25.120 1.00 40.85 C ANISOU 1578 C THR A 211 5280 4926 5314 138 549 -552 C ATOM 1579 O THR A 211 27.837 -9.358 25.220 1.00 39.92 O ANISOU 1579 O THR A 211 5208 4787 5172 144 539 -512 O ATOM 1580 CB THR A 211 31.197 -9.345 25.178 1.00 43.30 C ANISOU 1580 CB THR A 211 5512 5259 5679 207 580 -590 C ATOM 1581 OG1 THR A 211 32.223 -9.866 24.315 1.00 44.61 O ANISOU 1581 OG1 THR A 211 5677 5394 5878 217 623 -606 O ATOM 1582 CG2 THR A 211 30.779 -10.477 26.147 1.00 43.80 C ANISOU 1582 CG2 THR A 211 5589 5338 5716 259 549 -544 C ATOM 1583 N CYS A 212 28.652 -7.293 25.661 1.00 39.13 N ANISOU 1583 N CYS A 212 5023 4747 5096 121 529 -578 N ATOM 1584 CA CYS A 212 27.506 -6.842 26.473 1.00 38.08 C ANISOU 1584 CA CYS A 212 4896 4639 4934 112 492 -558 C ATOM 1585 C CYS A 212 26.221 -6.648 25.688 1.00 35.10 C ANISOU 1585 C CYS A 212 4581 4218 4538 68 498 -537 C ATOM 1586 O CYS A 212 25.153 -7.008 26.168 1.00 34.28 O ANISOU 1586 O CYS A 212 4501 4116 4408 70 474 -505 O ATOM 1587 CB CYS A 212 27.839 -5.526 27.214 1.00 38.33 C ANISOU 1587 CB CYS A 212 4870 4722 4973 104 474 -596 C ATOM 1588 SG CYS A 212 29.018 -5.806 28.536 1.00 44.89 S ANISOU 1588 SG CYS A 212 5624 5621 5813 163 446 -615 S ATOM 1589 N TYR A 213 26.332 -6.043 24.512 1.00 32.86 N ANISOU 1589 N TYR A 213 4322 3897 4265 31 528 -558 N ATOM 1590 CA TYR A 213 25.185 -5.726 23.708 1.00 31.94 C ANISOU 1590 CA TYR A 213 4262 3744 4130 -9 530 -543 C ATOM 1591 C TYR A 213 24.532 -6.982 23.135 1.00 31.95 C ANISOU 1591 C TYR A 213 4319 3704 4115 -9 535 -508 C ATOM 1592 O TYR A 213 23.311 -7.174 23.249 1.00 31.40 O ANISOU 1592 O TYR A 213 4278 3628 4023 -22 513 -482 O ATOM 1593 CB TYR A 213 25.587 -4.762 22.589 1.00 31.84 C ANISOU 1593 CB TYR A 213 4266 3701 4130 -44 564 -575 C ATOM 1594 CG TYR A 213 24.451 -4.477 21.654 1.00 32.16 C ANISOU 1594 CG TYR A 213 4369 3702 4147 -78 564 -559 C ATOM 1595 CD1 TYR A 213 24.173 -5.324 20.587 1.00 34.60 C ANISOU 1595 CD1 TYR A 213 4738 3963 4447 -90 582 -543 C ATOM 1596 CD2 TYR A 213 23.642 -3.372 21.835 1.00 32.50 C ANISOU 1596 CD2 TYR A 213 4413 3757 4178 -98 546 -562 C ATOM 1597 CE1 TYR A 213 23.111 -5.070 19.738 1.00 33.40 C ANISOU 1597 CE1 TYR A 213 4641 3779 4270 -119 575 -530 C ATOM 1598 CE2 TYR A 213 22.582 -3.113 20.984 1.00 32.72 C ANISOU 1598 CE2 TYR A 213 4497 3754 4183 -124 541 -547 C ATOM 1599 CZ TYR A 213 22.312 -3.966 19.953 1.00 31.88 C ANISOU 1599 CZ TYR A 213 4445 3603 4065 -134 553 -532 C ATOM 1600 OH TYR A 213 21.249 -3.690 19.112 1.00 33.00 O ANISOU 1600 OH TYR A 213 4639 3718 4182 -158 543 -520 O ATOM 1601 N LEU A 214 25.357 -7.833 22.513 1.00 31.50 N ANISOU 1601 N LEU A 214 4277 3618 4073 4 566 -511 N ATOM 1602 CA LEU A 214 24.917 -9.136 22.033 1.00 31.59 C ANISOU 1602 CA LEU A 214 4340 3589 4073 6 575 -481 C ATOM 1603 C LEU A 214 24.379 -10.048 23.126 1.00 30.70 C ANISOU 1603 C LEU A 214 4222 3497 3946 37 549 -447 C ATOM 1604 O LEU A 214 23.381 -10.715 22.912 1.00 29.08 O ANISOU 1604 O LEU A 214 4061 3266 3722 22 545 -421 O ATOM 1605 CB LEU A 214 26.067 -9.829 21.279 1.00 32.12 C ANISOU 1605 CB LEU A 214 4418 3624 4162 20 618 -493 C ATOM 1606 CG LEU A 214 26.146 -9.710 19.756 1.00 33.43 C ANISOU 1606 CG LEU A 214 4638 3735 4329 -17 655 -507 C ATOM 1607 CD1 LEU A 214 25.612 -8.430 19.140 1.00 33.85 C ANISOU 1607 CD1 LEU A 214 4708 3782 4371 -58 652 -524 C ATOM 1608 CD2 LEU A 214 27.585 -10.017 19.285 1.00 33.57 C ANISOU 1608 CD2 LEU A 214 4639 3737 4378 2 700 -531 C ATOM 1609 N MET A 215 25.041 -10.094 24.281 1.00 30.49 N ANISOU 1609 N MET A 215 4143 3516 3926 79 534 -448 N ATOM 1610 CA MET A 215 24.496 -10.810 25.437 1.00 32.54 C ANISOU 1610 CA MET A 215 4399 3798 4166 110 509 -415 C ATOM 1611 C MET A 215 23.083 -10.326 25.847 1.00 29.36 C ANISOU 1611 C MET A 215 4009 3406 3741 82 481 -400 C ATOM 1612 O MET A 215 22.217 -11.149 26.162 1.00 28.78 O ANISOU 1612 O MET A 215 3966 3319 3650 84 477 -368 O ATOM 1613 CB MET A 215 25.398 -10.665 26.657 1.00 32.14 C ANISOU 1613 CB MET A 215 4288 3803 4122 160 489 -424 C ATOM 1614 CG MET A 215 26.559 -11.625 26.767 1.00 38.52 C ANISOU 1614 CG MET A 215 5082 4610 4944 210 505 -421 C ATOM 1615 SD MET A 215 27.384 -11.438 28.394 1.00 41.80 S ANISOU 1615 SD MET A 215 5425 5102 5356 272 467 -428 S ATOM 1616 CE MET A 215 25.958 -11.818 29.450 1.00 42.42 C ANISOU 1616 CE MET A 215 5538 5189 5392 277 439 -383 C ATOM 1617 N ALA A 216 22.876 -9.005 25.860 1.00 26.18 N ANISOU 1617 N ALA A 216 3582 3027 3340 57 467 -423 N ATOM 1618 CA ALA A 216 21.572 -8.401 26.178 1.00 25.05 C ANISOU 1618 CA ALA A 216 3446 2894 3178 31 443 -413 C ATOM 1619 C ALA A 216 20.514 -8.714 25.112 1.00 23.80 C ANISOU 1619 C ALA A 216 3342 2689 3010 -8 450 -399 C ATOM 1620 O ALA A 216 19.393 -9.118 25.420 1.00 23.88 O ANISOU 1620 O ALA A 216 3370 2696 3006 -18 437 -376 O ATOM 1621 CB ALA A 216 21.729 -6.889 26.310 1.00 23.88 C ANISOU 1621 CB ALA A 216 3261 2775 3036 16 433 -444 C ATOM 1622 N LEU A 217 20.888 -8.528 23.853 1.00 22.50 N ANISOU 1622 N LEU A 217 3204 2489 2854 -31 473 -417 N ATOM 1623 CA LEU A 217 20.012 -8.855 22.740 1.00 22.57 C ANISOU 1623 CA LEU A 217 3268 2455 2852 -66 479 -409 C ATOM 1624 C LEU A 217 19.583 -10.334 22.736 1.00 22.08 C ANISOU 1624 C LEU A 217 3241 2366 2783 -62 487 -382 C ATOM 1625 O LEU A 217 18.381 -10.607 22.714 1.00 20.75 O ANISOU 1625 O LEU A 217 3094 2190 2602 -84 472 -366 O ATOM 1626 CB LEU A 217 20.645 -8.467 21.398 1.00 22.15 C ANISOU 1626 CB LEU A 217 3243 2366 2805 -86 506 -432 C ATOM 1627 CG LEU A 217 19.827 -8.835 20.151 1.00 24.26 C ANISOU 1627 CG LEU A 217 3572 2588 3056 -121 511 -427 C ATOM 1628 CD1 LEU A 217 18.466 -8.077 20.128 1.00 23.77 C ANISOU 1628 CD1 LEU A 217 3516 2539 2976 -146 477 -421 C ATOM 1629 CD2 LEU A 217 20.632 -8.581 18.867 1.00 23.81 C ANISOU 1629 CD2 LEU A 217 3550 2495 3004 -135 545 -449 C ATOM 1630 N ASP A 218 20.546 -11.269 22.770 1.00 22.10 N ANISOU 1630 N ASP A 218 3247 2353 2796 -33 511 -377 N ATOM 1631 CA ASP A 218 20.225 -12.709 22.901 1.00 23.67 C ANISOU 1631 CA ASP A 218 3480 2525 2990 -24 525 -350 C ATOM 1632 C ASP A 218 19.292 -12.969 24.066 1.00 23.74 C ANISOU 1632 C ASP A 218 3477 2559 2986 -16 502 -325 C ATOM 1633 O ASP A 218 18.349 -13.754 23.973 1.00 22.97 O ANISOU 1633 O ASP A 218 3413 2436 2879 -35 506 -307 O ATOM 1634 CB ASP A 218 21.483 -13.549 23.215 1.00 25.00 C ANISOU 1634 CB ASP A 218 3640 2689 3172 23 549 -345 C ATOM 1635 CG ASP A 218 22.441 -13.674 22.036 1.00 25.19 C ANISOU 1635 CG ASP A 218 3684 2676 3211 17 583 -366 C ATOM 1636 OD1 ASP A 218 22.036 -13.297 20.923 1.00 26.27 O ANISOU 1636 OD1 ASP A 218 3854 2785 3342 -24 590 -380 O ATOM 1637 OD2 ASP A 218 23.623 -14.101 22.256 1.00 26.10 O ANISOU 1637 OD2 ASP A 218 3779 2795 3343 58 603 -369 O ATOM 1638 N SER A 219 19.619 -12.359 25.200 1.00 23.41 N ANISOU 1638 N SER A 219 3387 2565 2944 14 483 -326 N ATOM 1639 CA SER A 219 18.912 -12.666 26.425 1.00 24.72 C ANISOU 1639 CA SER A 219 3543 2755 3096 30 467 -301 C ATOM 1640 C SER A 219 17.488 -12.126 26.408 1.00 23.42 C ANISOU 1640 C SER A 219 3382 2595 2922 -11 447 -299 C ATOM 1641 O SER A 219 16.560 -12.850 26.739 1.00 24.16 O ANISOU 1641 O SER A 219 3497 2676 3007 -21 450 -277 O ATOM 1642 CB SER A 219 19.686 -12.189 27.653 1.00 25.00 C ANISOU 1642 CB SER A 219 3528 2842 3129 75 450 -304 C ATOM 1643 OG SER A 219 18.928 -12.468 28.813 1.00 30.31 O ANISOU 1643 OG SER A 219 4197 3534 3783 89 437 -279 O ATOM 1644 N CYS A 220 17.314 -10.864 26.005 1.00 22.96 N ANISOU 1644 N CYS A 220 3304 2553 2866 -33 430 -322 N ATOM 1645 CA CYS A 220 15.970 -10.316 25.766 1.00 21.35 C ANISOU 1645 CA CYS A 220 3106 2351 2656 -71 411 -322 C ATOM 1646 C CYS A 220 15.158 -11.171 24.787 1.00 22.14 C ANISOU 1646 C CYS A 220 3252 2406 2753 -105 421 -316 C ATOM 1647 O CYS A 220 13.992 -11.472 25.050 1.00 21.91 O ANISOU 1647 O CYS A 220 3228 2376 2719 -125 412 -304 O ATOM 1648 CB CYS A 220 16.038 -8.874 25.272 1.00 20.61 C ANISOU 1648 CB CYS A 220 2993 2271 2565 -86 397 -348 C ATOM 1649 SG CYS A 220 16.654 -7.712 26.551 1.00 19.54 S ANISOU 1649 SG CYS A 220 2800 2193 2432 -57 382 -360 S ATOM 1650 N TYR A 221 15.763 -11.570 23.667 1.00 21.72 N ANISOU 1650 N TYR A 221 3232 2317 2703 -114 440 -326 N ATOM 1651 CA TYR A 221 15.047 -12.399 22.678 1.00 22.43 C ANISOU 1651 CA TYR A 221 3370 2364 2788 -149 449 -324 C ATOM 1652 C TYR A 221 14.582 -13.734 23.253 1.00 23.45 C ANISOU 1652 C TYR A 221 3518 2476 2918 -147 465 -301 C ATOM 1653 O TYR A 221 13.433 -14.116 23.093 1.00 23.60 O ANISOU 1653 O TYR A 221 3551 2483 2933 -180 459 -297 O ATOM 1654 CB TYR A 221 15.924 -12.603 21.467 1.00 22.67 C ANISOU 1654 CB TYR A 221 3435 2358 2821 -154 472 -339 C ATOM 1655 CG TYR A 221 15.276 -13.274 20.274 1.00 22.08 C ANISOU 1655 CG TYR A 221 3412 2240 2737 -193 479 -345 C ATOM 1656 CD1 TYR A 221 14.123 -12.752 19.706 1.00 20.64 C ANISOU 1656 CD1 TYR A 221 3238 2062 2543 -229 450 -354 C ATOM 1657 CD2 TYR A 221 15.866 -14.381 19.680 1.00 22.70 C ANISOU 1657 CD2 TYR A 221 3532 2275 2818 -192 513 -343 C ATOM 1658 CE1 TYR A 221 13.553 -13.297 18.574 1.00 20.38 C ANISOU 1658 CE1 TYR A 221 3251 1994 2499 -264 451 -364 C ATOM 1659 CE2 TYR A 221 15.274 -14.981 18.541 1.00 24.70 C ANISOU 1659 CE2 TYR A 221 3836 2489 3060 -231 519 -352 C ATOM 1660 CZ TYR A 221 14.126 -14.413 17.991 1.00 22.46 C ANISOU 1660 CZ TYR A 221 3557 2213 2762 -268 486 -364 C ATOM 1661 OH TYR A 221 13.510 -14.975 16.899 1.00 24.60 O ANISOU 1661 OH TYR A 221 3876 2451 3020 -306 486 -376 O ATOM 1662 N LYS A 222 15.479 -14.405 23.971 1.00 25.38 N ANISOU 1662 N LYS A 222 3759 2719 3165 -107 487 -285 N ATOM 1663 CA LYS A 222 15.229 -15.681 24.669 1.00 27.77 C ANISOU 1663 CA LYS A 222 4083 3003 3465 -93 509 -259 C ATOM 1664 C LYS A 222 14.058 -15.548 25.638 1.00 26.09 C ANISOU 1664 C LYS A 222 3852 2814 3247 -104 493 -246 C ATOM 1665 O LYS A 222 13.140 -16.373 25.622 1.00 26.41 O ANISOU 1665 O LYS A 222 3919 2829 3288 -131 507 -236 O ATOM 1666 CB LYS A 222 16.541 -16.102 25.399 1.00 28.67 C ANISOU 1666 CB LYS A 222 4187 3125 3582 -35 526 -246 C ATOM 1667 CG LYS A 222 16.526 -17.356 26.293 1.00 32.70 C ANISOU 1667 CG LYS A 222 4721 3619 4086 -4 551 -214 C ATOM 1668 CD LYS A 222 17.374 -17.205 27.661 1.00 33.69 C ANISOU 1668 CD LYS A 222 4810 3786 4203 60 541 -197 C ATOM 1669 CE LYS A 222 18.655 -16.290 27.567 1.00 39.31 C ANISOU 1669 CE LYS A 222 5478 4533 4924 90 524 -221 C ATOM 1670 NZ LYS A 222 19.098 -15.651 28.875 1.00 40.22 N ANISOU 1670 NZ LYS A 222 5545 4706 5029 134 498 -217 N ATOM 1671 N HIS A 223 14.072 -14.494 26.466 1.00 25.07 N ANISOU 1671 N HIS A 223 3677 2733 3115 -86 468 -248 N ATOM 1672 CA HIS A 223 12.987 -14.244 27.424 1.00 23.87 C ANISOU 1672 CA HIS A 223 3505 2607 2958 -95 455 -237 C ATOM 1673 C HIS A 223 11.650 -13.983 26.760 1.00 22.43 C ANISOU 1673 C HIS A 223 3325 2416 2780 -147 441 -249 C ATOM 1674 O HIS A 223 10.625 -14.561 27.164 1.00 21.69 O ANISOU 1674 O HIS A 223 3238 2315 2688 -168 450 -238 O ATOM 1675 CB HIS A 223 13.364 -13.135 28.405 1.00 25.06 C ANISOU 1675 CB HIS A 223 3609 2810 3103 -64 432 -240 C ATOM 1676 CG HIS A 223 14.425 -13.554 29.376 1.00 29.52 C ANISOU 1676 CG HIS A 223 4167 3389 3659 -10 441 -224 C ATOM 1677 ND1 HIS A 223 14.277 -14.638 30.212 1.00 34.85 N ANISOU 1677 ND1 HIS A 223 4866 4052 4324 13 463 -195 N ATOM 1678 CD2 HIS A 223 15.634 -13.026 29.666 1.00 34.09 C ANISOU 1678 CD2 HIS A 223 4718 3996 4237 27 432 -235 C ATOM 1679 CE1 HIS A 223 15.362 -14.781 30.949 1.00 34.40 C ANISOU 1679 CE1 HIS A 223 4798 4015 4257 66 463 -186 C ATOM 1680 NE2 HIS A 223 16.203 -13.819 30.634 1.00 34.07 N ANISOU 1680 NE2 HIS A 223 4721 4000 4223 75 443 -211 N ATOM 1681 N LEU A 224 11.677 -13.180 25.702 1.00 20.38 N ANISOU 1681 N LEU A 224 3064 2158 2524 -168 422 -272 N ATOM 1682 CA LEU A 224 10.483 -12.899 24.895 1.00 19.26 C ANISOU 1682 CA LEU A 224 2925 2010 2383 -213 402 -287 C ATOM 1683 C LEU A 224 9.942 -14.169 24.198 1.00 21.59 C ANISOU 1683 C LEU A 224 3261 2260 2680 -247 422 -287 C ATOM 1684 O LEU A 224 8.714 -14.414 24.178 1.00 21.74 O ANISOU 1684 O LEU A 224 3277 2278 2704 -282 415 -290 O ATOM 1685 CB LEU A 224 10.744 -11.738 23.878 1.00 18.74 C ANISOU 1685 CB LEU A 224 2856 1951 2314 -221 379 -310 C ATOM 1686 CG LEU A 224 9.599 -11.447 22.888 1.00 20.23 C ANISOU 1686 CG LEU A 224 3053 2133 2499 -262 354 -326 C ATOM 1687 CD1 LEU A 224 8.430 -11.440 23.707 1.00 26.47 C ANISOU 1687 CD1 LEU A 224 3815 2946 3297 -273 343 -318 C ATOM 1688 CD2 LEU A 224 9.592 -10.195 21.882 1.00 8.20 C ANISOU 1688 CD2 LEU A 224 1531 617 967 -269 327 -346 C ATOM 1689 N CYS A 225 10.844 -14.951 23.603 1.00 22.42 N ANISOU 1689 N CYS A 225 3405 2329 2784 -239 448 -286 N ATOM 1690 CA CYS A 225 10.475 -16.237 23.019 1.00 24.49 C ANISOU 1690 CA CYS A 225 3711 2546 3048 -269 474 -286 C ATOM 1691 C CYS A 225 9.822 -17.142 24.042 1.00 24.87 C ANISOU 1691 C CYS A 225 3762 2587 3102 -271 497 -266 C ATOM 1692 O CYS A 225 8.820 -17.774 23.720 1.00 26.54 O ANISOU 1692 O CYS A 225 3988 2777 3319 -314 504 -274 O ATOM 1693 CB CYS A 225 11.704 -16.964 22.392 1.00 23.91 C ANISOU 1693 CB CYS A 225 3679 2433 2973 -250 505 -285 C ATOM 1694 SG CYS A 225 12.343 -16.106 20.886 1.00 27.91 S ANISOU 1694 SG CYS A 225 4199 2932 3471 -261 489 -313 S ATOM 1695 N ASN A 226 10.391 -17.241 25.242 1.00 26.11 N ANISOU 1695 N ASN A 226 3906 2759 3256 -227 511 -242 N ATOM 1696 CA ASN A 226 9.805 -18.063 26.319 1.00 28.37 C ANISOU 1696 CA ASN A 226 4198 3037 3543 -224 537 -219 C ATOM 1697 C ASN A 226 8.400 -17.634 26.670 1.00 28.47 C ANISOU 1697 C ASN A 226 4182 3072 3564 -260 520 -226 C ATOM 1698 O ASN A 226 7.488 -18.457 26.736 1.00 28.98 O ANISOU 1698 O ASN A 226 4263 3112 3637 -294 543 -225 O ATOM 1699 CB ASN A 226 10.662 -18.045 27.592 1.00 29.66 C ANISOU 1699 CB ASN A 226 4351 3222 3697 -163 546 -192 C ATOM 1700 CG ASN A 226 11.995 -18.763 27.420 1.00 34.22 C ANISOU 1700 CG ASN A 226 4959 3773 4270 -122 571 -180 C ATOM 1701 OD1 ASN A 226 12.183 -19.575 26.502 1.00 38.73 O ANISOU 1701 OD1 ASN A 226 5571 4299 4846 -140 594 -186 O ATOM 1702 ND2 ASN A 226 12.949 -18.440 28.298 1.00 40.31 N ANISOU 1702 ND2 ASN A 226 5710 4575 5032 -66 564 -166 N ATOM 1703 N LYS A 227 8.219 -16.331 26.855 1.00 28.04 N ANISOU 1703 N LYS A 227 4083 3064 3508 -254 483 -236 N ATOM 1704 CA LYS A 227 6.900 -15.760 27.051 1.00 27.77 C ANISOU 1704 CA LYS A 227 4014 3054 3483 -286 462 -247 C ATOM 1705 C LYS A 227 5.937 -16.092 25.887 1.00 27.89 C ANISOU 1705 C LYS A 227 4040 3048 3508 -342 453 -272 C ATOM 1706 O LYS A 227 4.792 -16.490 26.113 1.00 26.37 O ANISOU 1706 O LYS A 227 3837 2852 3329 -377 460 -277 O ATOM 1707 CB LYS A 227 7.032 -14.237 27.282 1.00 28.58 C ANISOU 1707 CB LYS A 227 4073 3205 3582 -265 424 -255 C ATOM 1708 CG LYS A 227 7.567 -13.935 28.689 1.00 27.54 C ANISOU 1708 CG LYS A 227 3922 3102 3441 -220 431 -233 C ATOM 1709 CD LYS A 227 6.506 -14.324 29.740 1.00 31.36 C ANISOU 1709 CD LYS A 227 4396 3590 3928 -231 450 -220 C ATOM 1710 CE LYS A 227 6.949 -14.115 31.216 1.00 35.43 C ANISOU 1710 CE LYS A 227 4900 4133 4428 -186 460 -197 C ATOM 1711 NZ LYS A 227 7.707 -12.818 31.440 1.00 39.87 N ANISOU 1711 NZ LYS A 227 5430 4737 4982 -154 428 -206 N ATOM 1712 N PHE A 228 6.414 -15.955 24.650 1.00 27.00 N ANISOU 1712 N PHE A 228 3948 2920 3390 -351 438 -289 N ATOM 1713 CA PHE A 228 5.592 -16.321 23.491 1.00 28.09 C ANISOU 1713 CA PHE A 228 4102 3039 3533 -401 426 -315 C ATOM 1714 C PHE A 228 5.133 -17.781 23.528 1.00 29.00 C ANISOU 1714 C PHE A 228 4251 3112 3658 -434 466 -314 C ATOM 1715 O PHE A 228 3.967 -18.071 23.286 1.00 28.84 O ANISOU 1715 O PHE A 228 4219 3090 3650 -480 461 -332 O ATOM 1716 CB PHE A 228 6.350 -16.090 22.219 1.00 26.10 C ANISOU 1716 CB PHE A 228 3880 2770 3267 -400 413 -330 C ATOM 1717 CG PHE A 228 5.510 -16.212 20.984 1.00 26.45 C ANISOU 1717 CG PHE A 228 3937 2803 3308 -448 389 -359 C ATOM 1718 CD1 PHE A 228 4.680 -15.157 20.575 1.00 25.64 C ANISOU 1718 CD1 PHE A 228 3802 2736 3203 -460 341 -376 C ATOM 1719 CD2 PHE A 228 5.578 -17.347 20.202 1.00 24.84 C ANISOU 1719 CD2 PHE A 228 3781 2554 3102 -477 413 -370 C ATOM 1720 CE1 PHE A 228 3.944 -15.237 19.415 1.00 26.06 C ANISOU 1720 CE1 PHE A 228 3867 2783 3249 -498 313 -404 C ATOM 1721 CE2 PHE A 228 4.850 -17.437 19.021 1.00 25.08 C ANISOU 1721 CE2 PHE A 228 3826 2577 3125 -520 387 -401 C ATOM 1722 CZ PHE A 228 4.032 -16.380 18.623 1.00 26.28 C ANISOU 1722 CZ PHE A 228 3943 2769 3273 -530 335 -418 C ATOM 1723 N GLU A 229 6.059 -18.686 23.833 1.00 31.35 N ANISOU 1723 N GLU A 229 4587 3375 3951 -409 508 -293 N ATOM 1724 CA GLU A 229 5.739 -20.110 23.911 1.00 34.34 C ANISOU 1724 CA GLU A 229 5004 3705 4337 -436 555 -289 C ATOM 1725 C GLU A 229 4.636 -20.367 24.941 1.00 34.44 C ANISOU 1725 C GLU A 229 4994 3727 4364 -455 572 -282 C ATOM 1726 O GLU A 229 3.709 -21.141 24.675 1.00 35.07 O ANISOU 1726 O GLU A 229 5085 3782 4459 -506 592 -299 O ATOM 1727 CB GLU A 229 6.997 -20.925 24.205 1.00 34.03 C ANISOU 1727 CB GLU A 229 5009 3630 4289 -393 597 -263 C ATOM 1728 CG GLU A 229 7.037 -22.272 23.490 1.00 38.54 C ANISOU 1728 CG GLU A 229 5640 4141 4864 -423 639 -270 C ATOM 1729 CD GLU A 229 8.249 -23.127 23.872 1.00 39.53 C ANISOU 1729 CD GLU A 229 5809 4230 4982 -374 684 -241 C ATOM 1730 OE1 GLU A 229 9.106 -22.664 24.676 1.00 46.56 O ANISOU 1730 OE1 GLU A 229 6681 5146 5865 -315 679 -216 O ATOM 1731 OE2 GLU A 229 8.338 -24.282 23.388 1.00 45.13 O ANISOU 1731 OE2 GLU A 229 6570 4883 5694 -393 726 -243 O ATOM 1732 N LYS A 230 4.703 -19.705 26.103 1.00 34.57 N ANISOU 1732 N LYS A 230 4978 3780 4378 -419 567 -261 N ATOM 1733 CA LYS A 230 3.608 -19.805 27.085 1.00 35.61 C ANISOU 1733 CA LYS A 230 5084 3923 4523 -437 583 -255 C ATOM 1734 C LYS A 230 2.304 -19.181 26.588 1.00 34.80 C ANISOU 1734 C LYS A 230 4935 3849 4439 -486 547 -288 C ATOM 1735 O LYS A 230 1.240 -19.746 26.788 1.00 34.84 O ANISOU 1735 O LYS A 230 4931 3842 4463 -529 568 -299 O ATOM 1736 CB LYS A 230 3.984 -19.209 28.456 1.00 35.76 C ANISOU 1736 CB LYS A 230 5081 3975 4531 -386 585 -226 C ATOM 1737 CG LYS A 230 5.057 -19.994 29.201 1.00 37.56 C ANISOU 1737 CG LYS A 230 5353 4177 4741 -336 624 -191 C ATOM 1738 CD LYS A 230 5.509 -19.233 30.452 1.00 39.13 C ANISOU 1738 CD LYS A 230 5526 4417 4924 -282 614 -168 C ATOM 1739 CE LYS A 230 7.007 -19.452 30.746 1.00 43.55 C ANISOU 1739 CE LYS A 230 6112 4973 5462 -220 620 -144 C ATOM 1740 NZ LYS A 230 7.678 -18.104 30.970 1.00 47.56 N ANISOU 1740 NZ LYS A 230 6576 5534 5959 -183 574 -150 N ATOM 1741 N LEU A 231 2.391 -18.034 25.928 1.00 33.97 N ANISOU 1741 N LEU A 231 4801 3779 4328 -479 494 -304 N ATOM 1742 CA LEU A 231 1.221 -17.305 25.472 1.00 33.94 C ANISOU 1742 CA LEU A 231 4750 3808 4338 -513 453 -333 C ATOM 1743 C LEU A 231 0.517 -18.051 24.368 1.00 34.52 C ANISOU 1743 C LEU A 231 4838 3855 4421 -569 450 -365 C ATOM 1744 O LEU A 231 -0.673 -18.291 24.456 1.00 34.29 O ANISOU 1744 O LEU A 231 4780 3833 4414 -612 451 -384 O ATOM 1745 CB LEU A 231 1.625 -15.934 24.930 1.00 34.43 C ANISOU 1745 CB LEU A 231 4789 3906 4386 -486 400 -339 C ATOM 1746 CG LEU A 231 1.472 -14.608 25.700 1.00 35.78 C ANISOU 1746 CG LEU A 231 4912 4125 4557 -454 374 -331 C ATOM 1747 CD1 LEU A 231 1.016 -14.745 27.170 1.00 37.88 C ANISOU 1747 CD1 LEU A 231 5155 4404 4834 -445 405 -312 C ATOM 1748 CD2 LEU A 231 2.761 -13.780 25.574 1.00 35.38 C ANISOU 1748 CD2 LEU A 231 4873 4086 4486 -407 359 -320 C ATOM 1749 N GLU A 232 1.258 -18.383 23.308 1.00 34.11 N ANISOU 1749 N GLU A 232 4830 3777 4354 -571 445 -373 N ATOM 1750 CA GLU A 232 0.635 -18.881 22.088 1.00 34.98 C ANISOU 1750 CA GLU A 232 4954 3870 4467 -623 430 -409 C ATOM 1751 C GLU A 232 0.866 -20.384 21.858 1.00 33.88 C ANISOU 1751 C GLU A 232 4871 3671 4332 -652 483 -411 C ATOM 1752 O GLU A 232 0.333 -20.959 20.910 1.00 33.89 O ANISOU 1752 O GLU A 232 4888 3653 4335 -701 477 -443 O ATOM 1753 CB GLU A 232 1.094 -18.055 20.880 1.00 34.96 C ANISOU 1753 CB GLU A 232 4962 3881 4442 -611 380 -423 C ATOM 1754 CG GLU A 232 0.712 -16.564 20.935 1.00 36.11 C ANISOU 1754 CG GLU A 232 5055 4080 4584 -588 327 -426 C ATOM 1755 CD GLU A 232 0.661 -15.918 19.546 1.00 38.30 C ANISOU 1755 CD GLU A 232 5344 4369 4841 -595 276 -451 C ATOM 1756 OE1 GLU A 232 0.783 -16.638 18.514 1.00 41.27 O ANISOU 1756 OE1 GLU A 232 5764 4713 5205 -623 278 -470 O ATOM 1757 OE2 GLU A 232 0.521 -14.674 19.473 1.00 43.64 O ANISOU 1757 OE2 GLU A 232 5991 5082 5510 -570 236 -450 O ATOM 1758 N GLY A 233 1.656 -21.007 22.723 1.00 32.89 N ANISOU 1758 N GLY A 233 4776 3517 4203 -620 533 -377 N ATOM 1759 CA GLY A 233 1.860 -22.467 22.670 1.00 34.00 C ANISOU 1759 CA GLY A 233 4973 3597 4349 -642 593 -374 C ATOM 1760 C GLY A 233 2.661 -22.957 21.473 1.00 34.55 C ANISOU 1760 C GLY A 233 5097 3630 4402 -647 596 -386 C ATOM 1761 O GLY A 233 2.528 -24.115 21.057 1.00 33.54 O ANISOU 1761 O GLY A 233 5012 3451 4279 -684 635 -399 O ATOM 1762 N LYS A 234 3.484 -22.063 20.914 1.00 33.85 N ANISOU 1762 N LYS A 234 5006 3562 4294 -611 559 -383 N ATOM 1763 CA LYS A 234 4.391 -22.401 19.827 1.00 35.05 C ANISOU 1763 CA LYS A 234 5208 3680 4428 -608 564 -392 C ATOM 1764 C LYS A 234 5.676 -21.610 19.987 1.00 33.81 C ANISOU 1764 C LYS A 234 5050 3540 4256 -545 554 -367 C ATOM 1765 O LYS A 234 5.680 -20.544 20.581 1.00 33.17 O ANISOU 1765 O LYS A 234 4923 3504 4175 -516 524 -356 O ATOM 1766 CB LYS A 234 3.758 -22.106 18.463 1.00 35.77 C ANISOU 1766 CB LYS A 234 5301 3779 4510 -653 520 -433 C ATOM 1767 CG LYS A 234 3.273 -20.688 18.274 1.00 40.14 C ANISOU 1767 CG LYS A 234 5802 4391 5057 -644 456 -443 C ATOM 1768 CD LYS A 234 2.377 -20.580 17.035 1.00 46.17 C ANISOU 1768 CD LYS A 234 6566 5163 5812 -693 412 -486 C ATOM 1769 CE LYS A 234 1.837 -19.155 16.869 1.00 47.36 C ANISOU 1769 CE LYS A 234 6668 5373 5956 -679 348 -494 C ATOM 1770 NZ LYS A 234 1.118 -18.952 15.550 1.00 49.52 N ANISOU 1770 NZ LYS A 234 6947 5657 6212 -715 298 -533 N ATOM 1771 N GLU A 235 6.756 -22.142 19.439 1.00 33.12 N ANISOU 1771 N GLU A 235 5012 3414 4160 -527 582 -362 N ATOM 1772 CA GLU A 235 8.061 -21.510 19.504 1.00 32.06 C ANISOU 1772 CA GLU A 235 4877 3291 4015 -471 579 -344 C ATOM 1773 C GLU A 235 8.091 -20.272 18.597 1.00 29.91 C ANISOU 1773 C GLU A 235 4586 3050 3729 -474 528 -365 C ATOM 1774 O GLU A 235 7.623 -20.323 17.456 1.00 29.75 O ANISOU 1774 O GLU A 235 4589 3018 3698 -513 510 -394 O ATOM 1775 CB GLU A 235 9.112 -22.511 19.064 1.00 33.51 C ANISOU 1775 CB GLU A 235 5118 3421 4195 -455 626 -337 C ATOM 1776 CG GLU A 235 10.395 -22.385 19.855 1.00 38.30 C ANISOU 1776 CG GLU A 235 5717 4033 4802 -388 645 -306 C ATOM 1777 CD GLU A 235 11.463 -23.391 19.430 1.00 44.82 C ANISOU 1777 CD GLU A 235 6597 4806 5627 -367 694 -299 C ATOM 1778 OE1 GLU A 235 11.471 -23.818 18.246 1.00 45.86 O ANISOU 1778 OE1 GLU A 235 6771 4901 5753 -401 704 -322 O ATOM 1779 OE2 GLU A 235 12.304 -23.733 20.295 1.00 47.16 O ANISOU 1779 OE2 GLU A 235 6894 5099 5928 -314 720 -270 O ATOM 1780 N PHE A 236 8.614 -19.165 19.115 1.00 27.75 N ANISOU 1780 N PHE A 236 4275 2816 3452 -432 506 -352 N ATOM 1781 CA PHE A 236 8.746 -17.923 18.332 1.00 26.73 C ANISOU 1781 CA PHE A 236 4133 2713 3310 -429 465 -369 C ATOM 1782 C PHE A 236 9.895 -18.014 17.347 1.00 26.44 C ANISOU 1782 C PHE A 236 4140 2644 3260 -417 483 -376 C ATOM 1783 O PHE A 236 10.931 -18.606 17.644 1.00 27.54 O ANISOU 1783 O PHE A 236 4298 2760 3406 -387 522 -361 O ATOM 1784 CB PHE A 236 8.966 -16.714 19.281 1.00 25.19 C ANISOU 1784 CB PHE A 236 3885 2568 3119 -391 442 -354 C ATOM 1785 CG PHE A 236 8.825 -15.349 18.604 1.00 24.90 C ANISOU 1785 CG PHE A 236 3832 2559 3070 -391 400 -370 C ATOM 1786 CD1 PHE A 236 7.605 -14.698 18.574 1.00 22.12 C ANISOU 1786 CD1 PHE A 236 3449 2239 2717 -413 359 -381 C ATOM 1787 CD2 PHE A 236 9.942 -14.711 18.013 1.00 25.64 C ANISOU 1787 CD2 PHE A 236 3941 2647 3153 -367 404 -374 C ATOM 1788 CE1 PHE A 236 7.473 -13.413 17.967 1.00 20.54 C ANISOU 1788 CE1 PHE A 236 3238 2062 2503 -407 321 -393 C ATOM 1789 CE2 PHE A 236 9.823 -13.435 17.419 1.00 23.45 C ANISOU 1789 CE2 PHE A 236 3656 2392 2863 -366 370 -387 C ATOM 1790 CZ PHE A 236 8.573 -12.807 17.376 1.00 22.54 C ANISOU 1790 CZ PHE A 236 3515 2306 2744 -384 329 -395 C ATOM 1791 N SER A 237 9.723 -17.428 16.171 1.00 26.61 N ANISOU 1791 N SER A 237 4180 2665 3264 -437 456 -399 N ATOM 1792 CA SER A 237 10.843 -17.146 15.297 1.00 26.09 C ANISOU 1792 CA SER A 237 4149 2579 3186 -421 471 -405 C ATOM 1793 C SER A 237 10.635 -15.802 14.633 1.00 25.77 C ANISOU 1793 C SER A 237 4099 2564 3127 -422 430 -419 C ATOM 1794 O SER A 237 9.597 -15.179 14.746 1.00 25.77 O ANISOU 1794 O SER A 237 4071 2598 3124 -435 389 -425 O ATOM 1795 CB SER A 237 11.020 -18.244 14.210 1.00 26.85 C ANISOU 1795 CB SER A 237 4311 2621 3271 -450 500 -421 C ATOM 1796 OG SER A 237 10.069 -18.076 13.155 1.00 27.18 O ANISOU 1796 OG SER A 237 4375 2662 3291 -492 465 -448 O ATOM 1797 N ILE A 238 11.632 -15.376 13.897 1.00 26.02 N ANISOU 1797 N ILE A 238 4160 2579 3148 -406 445 -425 N ATOM 1798 CA ILE A 238 11.551 -14.156 13.089 1.00 26.98 C ANISOU 1798 CA ILE A 238 4290 2714 3247 -407 415 -438 C ATOM 1799 C ILE A 238 10.280 -14.075 12.226 1.00 27.51 C ANISOU 1799 C ILE A 238 4377 2786 3290 -443 372 -457 C ATOM 1800 O ILE A 238 9.839 -12.981 11.896 1.00 27.07 O ANISOU 1800 O ILE A 238 4312 2755 3218 -439 335 -462 O ATOM 1801 CB ILE A 238 12.885 -14.031 12.263 1.00 28.38 C ANISOU 1801 CB ILE A 238 4511 2857 3416 -392 453 -445 C ATOM 1802 CG1 ILE A 238 13.746 -12.968 12.857 1.00 27.94 C ANISOU 1802 CG1 ILE A 238 4418 2825 3374 -356 461 -437 C ATOM 1803 CG2 ILE A 238 12.736 -14.101 10.669 1.00 30.20 C ANISOU 1803 CG2 ILE A 238 4810 3052 3610 -420 450 -467 C ATOM 1804 CD1 ILE A 238 14.018 -13.245 14.263 1.00 28.93 C ANISOU 1804 CD1 ILE A 238 4490 2974 3528 -331 470 -419 C ATOM 1805 N ASN A 239 9.699 -15.232 11.867 1.00 27.43 N ANISOU 1805 N ASN A 239 4392 2752 3276 -478 376 -468 N ATOM 1806 CA ASN A 239 8.472 -15.292 11.056 1.00 28.02 C ANISOU 1806 CA ASN A 239 4483 2835 3330 -516 333 -491 C ATOM 1807 C ASN A 239 7.238 -14.849 11.833 1.00 28.04 C ANISOU 1807 C ASN A 239 4423 2885 3347 -522 290 -489 C ATOM 1808 O ASN A 239 6.208 -14.572 11.229 1.00 28.84 O ANISOU 1808 O ASN A 239 4522 3005 3431 -544 244 -508 O ATOM 1809 CB ASN A 239 8.190 -16.736 10.565 1.00 28.85 C ANISOU 1809 CB ASN A 239 4627 2900 3432 -556 354 -508 C ATOM 1810 CG ASN A 239 9.194 -17.226 9.509 1.00 32.64 C ANISOU 1810 CG ASN A 239 5179 3330 3892 -559 392 -517 C ATOM 1811 OD1 ASN A 239 9.685 -16.453 8.678 1.00 35.89 O ANISOU 1811 OD1 ASN A 239 5622 3737 4278 -546 385 -523 O ATOM 1812 ND2 ASN A 239 9.481 -18.530 9.537 1.00 37.00 N ANISOU 1812 ND2 ASN A 239 5762 3842 4457 -576 436 -519 N ATOM 1813 N ASP A 240 7.308 -14.830 13.166 1.00 27.09 N ANISOU 1813 N ASP A 240 4252 2785 3256 -503 304 -467 N ATOM 1814 CA ASP A 240 6.140 -14.433 13.973 1.00 26.72 C ANISOU 1814 CA ASP A 240 4146 2782 3226 -509 270 -465 C ATOM 1815 C ASP A 240 5.971 -12.938 14.231 1.00 26.20 C ANISOU 1815 C ASP A 240 4043 2757 3156 -479 235 -458 C ATOM 1816 O ASP A 240 5.025 -12.524 14.921 1.00 25.62 O ANISOU 1816 O ASP A 240 3918 2721 3096 -480 208 -456 O ATOM 1817 CB ASP A 240 6.117 -15.210 15.287 1.00 27.29 C ANISOU 1817 CB ASP A 240 4188 2854 3329 -506 304 -447 C ATOM 1818 CG ASP A 240 6.059 -16.685 15.047 1.00 27.18 C ANISOU 1818 CG ASP A 240 4211 2798 3321 -539 338 -455 C ATOM 1819 OD1 ASP A 240 5.046 -17.134 14.480 1.00 29.28 O ANISOU 1819 OD1 ASP A 240 4481 3061 3582 -582 317 -480 O ATOM 1820 OD2 ASP A 240 7.044 -17.366 15.370 1.00 28.13 O ANISOU 1820 OD2 ASP A 240 4355 2886 3447 -521 385 -439 O ATOM 1821 N ALA A 241 6.856 -12.133 13.655 1.00 25.50 N ANISOU 1821 N ALA A 241 3981 2659 3047 -454 238 -456 N ATOM 1822 CA ALA A 241 6.638 -10.696 13.659 1.00 25.76 C ANISOU 1822 CA ALA A 241 3992 2725 3072 -430 206 -454 C ATOM 1823 C ALA A 241 6.795 -10.159 12.261 1.00 25.61 C ANISOU 1823 C ALA A 241 4027 2688 3015 -431 189 -467 C ATOM 1824 O ALA A 241 7.581 -10.688 11.461 1.00 24.74 O ANISOU 1824 O ALA A 241 3971 2539 2890 -438 217 -474 O ATOM 1825 CB ALA A 241 7.594 -9.977 14.619 1.00 24.75 C ANISOU 1825 CB ALA A 241 3835 2608 2960 -393 232 -435 C ATOM 1826 N ASP A 242 6.056 -9.095 11.994 1.00 25.03 N ANISOU 1826 N ASP A 242 3940 2643 2927 -420 145 -471 N ATOM 1827 CA ASP A 242 6.069 -8.459 10.693 1.00 26.48 C ANISOU 1827 CA ASP A 242 4177 2814 3070 -415 123 -481 C ATOM 1828 C ASP A 242 7.251 -7.513 10.535 1.00 26.12 C ANISOU 1828 C ASP A 242 4158 2750 3015 -384 155 -471 C ATOM 1829 O ASP A 242 7.856 -7.423 9.454 1.00 26.59 O ANISOU 1829 O ASP A 242 4282 2777 3045 -385 170 -479 O ATOM 1830 CB ASP A 242 4.731 -7.762 10.519 1.00 26.09 C ANISOU 1830 CB ASP A 242 4102 2804 3009 -411 62 -488 C ATOM 1831 CG ASP A 242 3.601 -8.756 10.526 1.00 29.53 C ANISOU 1831 CG ASP A 242 4512 3254 3454 -448 33 -505 C ATOM 1832 OD1 ASP A 242 2.885 -8.970 11.551 1.00 33.10 O ANISOU 1832 OD1 ASP A 242 4900 3734 3940 -455 25 -502 O ATOM 1833 OD2 ASP A 242 3.486 -9.408 9.498 1.00 29.52 O ANISOU 1833 OD2 ASP A 242 4557 3231 3426 -472 23 -524 O ATOM 1834 N TYR A 243 7.591 -6.838 11.634 1.00 24.96 N ANISOU 1834 N TYR A 243 3964 2625 2896 -361 169 -457 N ATOM 1835 CA TYR A 243 8.687 -5.887 11.647 1.00 23.86 C ANISOU 1835 CA TYR A 243 3838 2472 2755 -335 202 -451 C ATOM 1836 C TYR A 243 9.476 -6.020 12.926 1.00 22.58 C ANISOU 1836 C TYR A 243 3629 2321 2631 -323 237 -441 C ATOM 1837 O TYR A 243 8.915 -6.345 13.973 1.00 22.35 O ANISOU 1837 O TYR A 243 3546 2320 2624 -325 225 -433 O ATOM 1838 CB TYR A 243 8.141 -4.461 11.505 1.00 24.20 C ANISOU 1838 CB TYR A 243 3877 2536 2783 -313 171 -448 C ATOM 1839 CG TYR A 243 7.488 -4.251 10.174 1.00 26.98 C ANISOU 1839 CG TYR A 243 4283 2877 3090 -317 136 -457 C ATOM 1840 CD1 TYR A 243 6.099 -4.311 10.046 1.00 26.59 C ANISOU 1840 CD1 TYR A 243 4213 2858 3033 -323 79 -461 C ATOM 1841 CD2 TYR A 243 8.265 -4.043 9.017 1.00 26.96 C ANISOU 1841 CD2 TYR A 243 4356 2834 3055 -314 160 -462 C ATOM 1842 CE1 TYR A 243 5.496 -4.173 8.798 1.00 30.41 C ANISOU 1842 CE1 TYR A 243 4746 3335 3472 -324 40 -471 C ATOM 1843 CE2 TYR A 243 7.660 -3.887 7.762 1.00 29.42 C ANISOU 1843 CE2 TYR A 243 4724 3134 3319 -316 126 -470 C ATOM 1844 CZ TYR A 243 6.278 -3.962 7.671 1.00 29.13 C ANISOU 1844 CZ TYR A 243 4664 3133 3273 -319 63 -475 C ATOM 1845 OH TYR A 243 5.646 -3.805 6.455 1.00 31.85 O ANISOU 1845 OH TYR A 243 5061 3473 3567 -317 22 -484 O ATOM 1846 N PHE A 244 10.787 -5.839 12.809 1.00 21.72 N ANISOU 1846 N PHE A 244 3539 2188 2526 -312 281 -443 N ATOM 1847 CA PHE A 244 11.671 -5.733 13.943 1.00 21.46 C ANISOU 1847 CA PHE A 244 3462 2168 2525 -295 311 -436 C ATOM 1848 C PHE A 244 12.323 -4.367 13.913 1.00 21.15 C ANISOU 1848 C PHE A 244 3422 2130 2484 -276 327 -441 C ATOM 1849 O PHE A 244 12.969 -4.000 12.915 1.00 20.58 O ANISOU 1849 O PHE A 244 3400 2024 2394 -277 351 -451 O ATOM 1850 CB PHE A 244 12.756 -6.817 13.921 1.00 21.72 C ANISOU 1850 CB PHE A 244 3509 2173 2571 -298 354 -438 C ATOM 1851 CG PHE A 244 12.242 -8.212 14.232 1.00 22.32 C ANISOU 1851 CG PHE A 244 3579 2247 2655 -313 349 -431 C ATOM 1852 CD1 PHE A 244 11.662 -8.975 13.237 1.00 21.01 C ANISOU 1852 CD1 PHE A 244 3460 2055 2468 -340 339 -439 C ATOM 1853 CD2 PHE A 244 12.357 -8.745 15.529 1.00 21.57 C ANISOU 1853 CD2 PHE A 244 3436 2172 2586 -301 358 -418 C ATOM 1854 CE1 PHE A 244 11.207 -10.263 13.512 1.00 23.17 C ANISOU 1854 CE1 PHE A 244 3730 2321 2750 -358 341 -436 C ATOM 1855 CE2 PHE A 244 11.892 -10.012 15.836 1.00 21.61 C ANISOU 1855 CE2 PHE A 244 3441 2170 2599 -316 360 -411 C ATOM 1856 CZ PHE A 244 11.308 -10.774 14.845 1.00 23.95 C ANISOU 1856 CZ PHE A 244 3783 2440 2879 -346 353 -420 C ATOM 1857 N VAL A 245 12.161 -3.632 15.018 1.00 20.75 N ANISOU 1857 N VAL A 245 3318 2115 2453 -261 318 -436 N ATOM 1858 CA VAL A 245 12.723 -2.281 15.194 1.00 19.68 C ANISOU 1858 CA VAL A 245 3174 1983 2320 -245 334 -442 C ATOM 1859 C VAL A 245 13.724 -2.242 16.329 1.00 19.75 C ANISOU 1859 C VAL A 245 3133 2010 2360 -232 362 -446 C ATOM 1860 O VAL A 245 13.481 -2.787 17.392 1.00 19.22 O ANISOU 1860 O VAL A 245 3022 1972 2310 -227 350 -437 O ATOM 1861 CB VAL A 245 11.618 -1.247 15.497 1.00 20.23 C ANISOU 1861 CB VAL A 245 3224 2080 2382 -235 297 -436 C ATOM 1862 CG1 VAL A 245 12.138 0.181 15.240 1.00 17.56 C ANISOU 1862 CG1 VAL A 245 2902 1730 2038 -222 318 -445 C ATOM 1863 CG2 VAL A 245 10.409 -1.496 14.612 1.00 20.37 C ANISOU 1863 CG2 VAL A 245 3273 2093 2373 -244 256 -432 C ATOM 1864 N PHE A 246 14.855 -1.590 16.095 1.00 19.72 N ANISOU 1864 N PHE A 246 3139 1990 2363 -227 399 -461 N ATOM 1865 CA PHE A 246 15.959 -1.618 17.010 1.00 19.92 C ANISOU 1865 CA PHE A 246 3121 2032 2418 -216 427 -471 C ATOM 1866 C PHE A 246 16.387 -0.197 17.365 1.00 19.94 C ANISOU 1866 C PHE A 246 3103 2045 2429 -210 442 -487 C ATOM 1867 O PHE A 246 16.213 0.766 16.592 1.00 19.71 O ANISOU 1867 O PHE A 246 3112 1994 2384 -214 449 -492 O ATOM 1868 CB PHE A 246 17.180 -2.329 16.395 1.00 19.74 C ANISOU 1868 CB PHE A 246 3121 1977 2403 -220 468 -482 C ATOM 1869 CG PHE A 246 16.920 -3.764 15.996 1.00 19.78 C ANISOU 1869 CG PHE A 246 3151 1964 2401 -227 463 -470 C ATOM 1870 CD1 PHE A 246 16.369 -4.063 14.748 1.00 18.17 C ANISOU 1870 CD1 PHE A 246 3010 1726 2169 -245 457 -468 C ATOM 1871 CD2 PHE A 246 17.202 -4.814 16.889 1.00 18.32 C ANISOU 1871 CD2 PHE A 246 2931 1796 2235 -216 464 -461 C ATOM 1872 CE1 PHE A 246 16.097 -5.399 14.373 1.00 18.29 C ANISOU 1872 CE1 PHE A 246 3050 1723 2177 -256 454 -460 C ATOM 1873 CE2 PHE A 246 16.932 -6.163 16.525 1.00 19.92 C ANISOU 1873 CE2 PHE A 246 3161 1977 2431 -224 464 -450 C ATOM 1874 CZ PHE A 246 16.381 -6.446 15.264 1.00 20.20 C ANISOU 1874 CZ PHE A 246 3256 1977 2440 -246 460 -451 C ATOM 1875 N HIS A 247 16.985 -0.109 18.537 1.00 20.46 N ANISOU 1875 N HIS A 247 3112 2143 2519 -198 448 -494 N ATOM 1876 CA HIS A 247 17.849 0.990 18.927 1.00 21.34 C ANISOU 1876 CA HIS A 247 3199 2263 2648 -195 475 -518 C ATOM 1877 C HIS A 247 18.874 1.137 17.811 1.00 21.45 C ANISOU 1877 C HIS A 247 3253 2234 2664 -207 521 -538 C ATOM 1878 O HIS A 247 19.534 0.150 17.417 1.00 19.89 O ANISOU 1878 O HIS A 247 3065 2018 2472 -208 539 -539 O ATOM 1879 CB HIS A 247 18.528 0.575 20.227 1.00 21.60 C ANISOU 1879 CB HIS A 247 3168 2336 2705 -181 473 -525 C ATOM 1880 CG HIS A 247 19.688 1.426 20.612 1.00 25.76 C ANISOU 1880 CG HIS A 247 3661 2872 3254 -180 504 -557 C ATOM 1881 ND1 HIS A 247 19.594 2.800 20.746 1.00 28.44 N ANISOU 1881 ND1 HIS A 247 3997 3215 3595 -187 513 -574 N ATOM 1882 CD2 HIS A 247 20.953 1.095 20.966 1.00 26.71 C ANISOU 1882 CD2 HIS A 247 3746 3004 3398 -173 527 -579 C ATOM 1883 CE1 HIS A 247 20.757 3.278 21.145 1.00 26.18 C ANISOU 1883 CE1 HIS A 247 3674 2940 3332 -189 542 -607 C ATOM 1884 NE2 HIS A 247 21.592 2.264 21.304 1.00 29.08 N ANISOU 1884 NE2 HIS A 247 4019 3316 3715 -180 548 -610 N ATOM 1885 N SER A 248 19.028 2.355 17.281 1.00 21.60 N ANISOU 1885 N SER A 248 3299 2232 2678 -215 545 -552 N ATOM 1886 CA SER A 248 19.712 2.494 15.995 1.00 22.61 C ANISOU 1886 CA SER A 248 3484 2309 2798 -228 589 -565 C ATOM 1887 C SER A 248 20.789 3.552 16.052 1.00 25.09 C ANISOU 1887 C SER A 248 3785 2613 3135 -237 639 -598 C ATOM 1888 O SER A 248 20.660 4.560 15.357 1.00 26.37 O ANISOU 1888 O SER A 248 3994 2743 3282 -245 662 -603 O ATOM 1889 CB SER A 248 18.716 2.942 14.930 1.00 22.12 C ANISOU 1889 CB SER A 248 3491 2215 2697 -232 575 -548 C ATOM 1890 OG SER A 248 17.632 2.029 14.825 1.00 24.20 O ANISOU 1890 OG SER A 248 3765 2490 2941 -228 527 -523 O ATOM 1891 N PRO A 249 21.842 3.354 16.880 1.00 25.71 N ANISOU 1891 N PRO A 249 3802 2718 3249 -235 656 -621 N ATOM 1892 CA PRO A 249 22.859 4.413 16.969 1.00 26.37 C ANISOU 1892 CA PRO A 249 3867 2795 3358 -248 704 -659 C ATOM 1893 C PRO A 249 23.562 4.648 15.618 1.00 27.64 C ANISOU 1893 C PRO A 249 4089 2896 3516 -266 764 -674 C ATOM 1894 O PRO A 249 23.841 5.782 15.252 1.00 27.25 O ANISOU 1894 O PRO A 249 4065 2821 3469 -280 803 -693 O ATOM 1895 CB PRO A 249 23.843 3.903 18.027 1.00 25.87 C ANISOU 1895 CB PRO A 249 3724 2774 3331 -239 704 -680 C ATOM 1896 CG PRO A 249 23.464 2.476 18.290 1.00 26.49 C ANISOU 1896 CG PRO A 249 3793 2870 3401 -219 666 -651 C ATOM 1897 CD PRO A 249 22.137 2.190 17.728 1.00 25.22 C ANISOU 1897 CD PRO A 249 3686 2691 3203 -219 633 -615 C ATOM 1898 N TYR A 250 23.829 3.564 14.894 1.00 27.67 N ANISOU 1898 N TYR A 250 4122 2878 3515 -265 772 -665 N ATOM 1899 CA TYR A 250 24.286 3.647 13.522 1.00 27.95 C ANISOU 1899 CA TYR A 250 4228 2853 3537 -280 824 -672 C ATOM 1900 C TYR A 250 23.717 2.413 12.831 1.00 27.71 C ANISOU 1900 C TYR A 250 4242 2806 3479 -274 799 -643 C ATOM 1901 O TYR A 250 23.412 1.420 13.491 1.00 26.94 O ANISOU 1901 O TYR A 250 4107 2742 3386 -260 758 -627 O ATOM 1902 CB TYR A 250 25.825 3.704 13.432 1.00 28.82 C ANISOU 1902 CB TYR A 250 4309 2952 3690 -293 888 -712 C ATOM 1903 CG TYR A 250 26.549 2.601 14.184 1.00 30.07 C ANISOU 1903 CG TYR A 250 4397 3147 3882 -278 876 -720 C ATOM 1904 CD1 TYR A 250 26.729 2.669 15.562 1.00 31.25 C ANISOU 1904 CD1 TYR A 250 4462 3355 4057 -264 845 -730 C ATOM 1905 CD2 TYR A 250 27.048 1.496 13.511 1.00 31.09 C ANISOU 1905 CD2 TYR A 250 4548 3250 4014 -275 897 -716 C ATOM 1906 CE1 TYR A 250 27.386 1.658 16.256 1.00 31.97 C ANISOU 1906 CE1 TYR A 250 4493 3481 4175 -244 832 -735 C ATOM 1907 CE2 TYR A 250 27.695 0.472 14.199 1.00 31.99 C ANISOU 1907 CE2 TYR A 250 4601 3396 4157 -255 887 -720 C ATOM 1908 CZ TYR A 250 27.866 0.566 15.552 1.00 32.17 C ANISOU 1908 CZ TYR A 250 4541 3478 4203 -238 854 -729 C ATOM 1909 OH TYR A 250 28.512 -0.442 16.222 1.00 32.55 O ANISOU 1909 OH TYR A 250 4534 3558 4277 -213 843 -731 O ATOM 1910 N ASN A 251 23.565 2.482 11.515 1.00 27.30 N ANISOU 1910 N ASN A 251 4274 2702 3395 -284 823 -637 N ATOM 1911 CA ASN A 251 22.820 1.478 10.790 1.00 27.08 C ANISOU 1911 CA ASN A 251 4298 2659 3333 -281 794 -611 C ATOM 1912 C ASN A 251 23.475 0.104 10.717 1.00 27.94 C ANISOU 1912 C ASN A 251 4393 2763 3460 -280 807 -613 C ATOM 1913 O ASN A 251 22.773 -0.909 10.706 1.00 27.55 O ANISOU 1913 O ASN A 251 4352 2722 3393 -274 768 -591 O ATOM 1914 CB ASN A 251 22.394 1.985 9.414 1.00 26.57 C ANISOU 1914 CB ASN A 251 4331 2542 3222 -290 811 -604 C ATOM 1915 CG ASN A 251 21.686 0.914 8.594 1.00 26.78 C ANISOU 1915 CG ASN A 251 4413 2552 3211 -290 781 -583 C ATOM 1916 OD1 ASN A 251 22.311 0.238 7.780 1.00 26.75 O ANISOU 1916 OD1 ASN A 251 4450 2512 3203 -300 818 -590 O ATOM 1917 ND2 ASN A 251 20.391 0.711 8.856 1.00 22.37 N ANISOU 1917 ND2 ASN A 251 3850 2022 2629 -282 714 -559 N ATOM 1918 N LYS A 252 24.808 0.058 10.690 1.00 28.28 N ANISOU 1918 N LYS A 252 4413 2794 3540 -284 863 -641 N ATOM 1919 CA LYS A 252 25.499 -1.222 10.703 1.00 28.91 C ANISOU 1919 CA LYS A 252 4473 2871 3640 -277 878 -644 C ATOM 1920 C LYS A 252 25.147 -2.077 11.927 1.00 28.39 C ANISOU 1920 C LYS A 252 4340 2857 3589 -256 826 -627 C ATOM 1921 O LYS A 252 25.128 -3.295 11.825 1.00 28.32 O ANISOU 1921 O LYS A 252 4339 2842 3579 -248 819 -614 O ATOM 1922 CB LYS A 252 27.008 -1.018 10.630 1.00 29.37 C ANISOU 1922 CB LYS A 252 4501 2916 3742 -282 945 -680 C ATOM 1923 CG LYS A 252 27.886 -2.317 10.667 1.00 31.66 C ANISOU 1923 CG LYS A 252 4765 3204 4061 -269 966 -686 C ATOM 1924 CD LYS A 252 27.619 -3.333 9.520 1.00 34.90 C ANISOU 1924 CD LYS A 252 5254 3565 4440 -275 979 -669 C ATOM 1925 CE LYS A 252 27.442 -2.697 8.156 1.00 35.94 C ANISOU 1925 CE LYS A 252 5479 3640 4535 -299 1016 -673 C ATOM 1926 NZ LYS A 252 28.723 -2.250 7.609 1.00 34.88 N ANISOU 1926 NZ LYS A 252 5350 3473 4430 -311 1095 -707 N ATOM 1927 N LEU A 253 24.876 -1.439 13.070 1.00 27.55 N ANISOU 1927 N LEU A 253 4172 2798 3496 -247 793 -627 N ATOM 1928 CA LEU A 253 24.558 -2.176 14.305 1.00 27.10 C ANISOU 1928 CA LEU A 253 4055 2791 3451 -225 746 -611 C ATOM 1929 C LEU A 253 23.168 -2.748 14.176 1.00 26.16 C ANISOU 1929 C LEU A 253 3972 2672 3296 -225 698 -578 C ATOM 1930 O LEU A 253 22.892 -3.851 14.664 1.00 26.41 O ANISOU 1930 O LEU A 253 3987 2718 3330 -213 674 -559 O ATOM 1931 CB LEU A 253 24.679 -1.292 15.557 1.00 27.19 C ANISOU 1931 CB LEU A 253 3995 2853 3483 -216 728 -624 C ATOM 1932 CG LEU A 253 24.360 -1.930 16.921 1.00 27.42 C ANISOU 1932 CG LEU A 253 3963 2934 3520 -191 681 -608 C ATOM 1933 CD1 LEU A 253 25.341 -3.096 17.289 1.00 31.91 C ANISOU 1933 CD1 LEU A 253 4497 3514 4116 -167 694 -611 C ATOM 1934 CD2 LEU A 253 24.356 -0.939 18.032 1.00 27.83 C ANISOU 1934 CD2 LEU A 253 3957 3032 3585 -185 662 -621 C ATOM 1935 N VAL A 254 22.304 -2.026 13.474 1.00 25.48 N ANISOU 1935 N VAL A 254 3937 2567 3178 -240 685 -570 N ATOM 1936 CA VAL A 254 20.954 -2.529 13.167 1.00 25.35 C ANISOU 1936 CA VAL A 254 3958 2549 3127 -244 639 -543 C ATOM 1937 C VAL A 254 21.005 -3.800 12.313 1.00 26.26 C ANISOU 1937 C VAL A 254 4121 2629 3229 -252 651 -537 C ATOM 1938 O VAL A 254 20.312 -4.774 12.633 1.00 25.67 O ANISOU 1938 O VAL A 254 4040 2566 3148 -250 619 -518 O ATOM 1939 CB VAL A 254 20.030 -1.448 12.523 1.00 25.13 C ANISOU 1939 CB VAL A 254 3976 2508 3064 -253 621 -538 C ATOM 1940 CG1 VAL A 254 18.636 -2.033 12.170 1.00 24.10 C ANISOU 1940 CG1 VAL A 254 3876 2380 2900 -258 570 -515 C ATOM 1941 CG2 VAL A 254 19.872 -0.237 13.470 1.00 24.24 C ANISOU 1941 CG2 VAL A 254 3815 2431 2966 -245 609 -543 C ATOM 1942 N GLN A 255 21.814 -3.784 11.235 1.00 26.24 N ANISOU 1942 N GLN A 255 4168 2580 3222 -262 701 -552 N ATOM 1943 CA GLN A 255 22.039 -4.972 10.416 1.00 27.56 C ANISOU 1943 CA GLN A 255 4382 2710 3379 -269 721 -550 C ATOM 1944 C GLN A 255 22.550 -6.141 11.235 1.00 26.87 C ANISOU 1944 C GLN A 255 4246 2640 3324 -252 725 -545 C ATOM 1945 O GLN A 255 22.053 -7.242 11.086 1.00 28.58 O ANISOU 1945 O GLN A 255 4485 2846 3529 -255 710 -531 O ATOM 1946 CB GLN A 255 23.011 -4.689 9.241 1.00 27.55 C ANISOU 1946 CB GLN A 255 4435 2657 3374 -281 784 -571 C ATOM 1947 CG GLN A 255 22.601 -3.524 8.301 1.00 30.67 C ANISOU 1947 CG GLN A 255 4894 3027 3733 -294 790 -575 C ATOM 1948 CD GLN A 255 23.746 -3.153 7.346 1.00 31.12 C ANISOU 1948 CD GLN A 255 4996 3034 3794 -304 864 -598 C ATOM 1949 OE1 GLN A 255 24.466 -4.028 6.882 1.00 31.50 O ANISOU 1949 OE1 GLN A 255 5062 3055 3853 -308 902 -606 O ATOM 1950 NE2 GLN A 255 23.931 -1.850 7.083 1.00 36.55 N ANISOU 1950 NE2 GLN A 255 5701 3709 4475 -310 889 -609 N ATOM 1951 N LYS A 256 23.556 -5.915 12.073 1.00 26.82 N ANISOU 1951 N LYS A 256 4176 2658 3356 -235 745 -559 N ATOM 1952 CA LYS A 256 24.121 -6.972 12.913 1.00 27.87 C ANISOU 1952 CA LYS A 256 4260 2810 3518 -210 747 -553 C ATOM 1953 C LYS A 256 23.131 -7.539 13.938 1.00 27.00 C ANISOU 1953 C LYS A 256 4121 2736 3401 -199 694 -526 C ATOM 1954 O LYS A 256 23.145 -8.740 14.215 1.00 26.63 O ANISOU 1954 O LYS A 256 4073 2685 3360 -186 694 -512 O ATOM 1955 CB LYS A 256 25.409 -6.500 13.617 1.00 28.09 C ANISOU 1955 CB LYS A 256 4221 2863 3589 -191 775 -577 C ATOM 1956 CG LYS A 256 26.607 -6.354 12.651 1.00 29.96 C ANISOU 1956 CG LYS A 256 4481 3060 3843 -200 840 -605 C ATOM 1957 CD LYS A 256 27.882 -5.857 13.324 1.00 30.65 C ANISOU 1957 CD LYS A 256 4494 3175 3976 -184 868 -635 C ATOM 1958 CE LYS A 256 29.020 -5.854 12.256 1.00 34.29 C ANISOU 1958 CE LYS A 256 4984 3590 4457 -196 939 -663 C ATOM 1959 NZ LYS A 256 30.333 -5.458 12.816 1.00 37.95 N ANISOU 1959 NZ LYS A 256 5370 4078 4969 -183 970 -698 N ATOM 1960 N SER A 257 22.321 -6.645 14.523 1.00 26.50 N ANISOU 1960 N SER A 257 4034 2707 3329 -202 655 -521 N ATOM 1961 CA SER A 257 21.312 -6.986 15.524 1.00 25.04 C ANISOU 1961 CA SER A 257 3820 2558 3138 -194 608 -498 C ATOM 1962 C SER A 257 20.259 -7.931 14.948 1.00 24.49 C ANISOU 1962 C SER A 257 3800 2465 3042 -211 589 -479 C ATOM 1963 O SER A 257 19.960 -8.961 15.562 1.00 24.35 O ANISOU 1963 O SER A 257 3769 2454 3029 -202 578 -462 O ATOM 1964 CB SER A 257 20.650 -5.723 16.063 1.00 25.27 C ANISOU 1964 CB SER A 257 3821 2621 3160 -197 577 -499 C ATOM 1965 OG SER A 257 21.573 -4.990 16.861 1.00 26.60 O ANISOU 1965 OG SER A 257 3933 2819 3355 -181 590 -517 O ATOM 1966 N PHE A 258 19.738 -7.613 13.765 1.00 23.74 N ANISOU 1966 N PHE A 258 3763 2339 2919 -236 588 -484 N ATOM 1967 CA PHE A 258 18.709 -8.446 13.151 1.00 24.48 C ANISOU 1967 CA PHE A 258 3903 2412 2986 -256 566 -473 C ATOM 1968 C PHE A 258 19.310 -9.786 12.741 1.00 24.91 C ANISOU 1968 C PHE A 258 3987 2431 3048 -257 601 -472 C ATOM 1969 O PHE A 258 18.690 -10.838 12.935 1.00 25.04 O ANISOU 1969 O PHE A 258 4011 2442 3060 -263 588 -459 O ATOM 1970 CB PHE A 258 18.048 -7.783 11.951 1.00 23.66 C ANISOU 1970 CB PHE A 258 3856 2286 2846 -278 553 -480 C ATOM 1971 CG PHE A 258 16.975 -8.631 11.312 1.00 26.09 C ANISOU 1971 CG PHE A 258 4207 2578 3127 -301 526 -474 C ATOM 1972 CD1 PHE A 258 17.163 -9.166 10.033 1.00 26.29 C ANISOU 1972 CD1 PHE A 258 4302 2557 3128 -319 548 -484 C ATOM 1973 CD2 PHE A 258 15.786 -8.906 11.992 1.00 23.24 C ANISOU 1973 CD2 PHE A 258 3817 2249 2766 -307 481 -461 C ATOM 1974 CE1 PHE A 258 16.204 -9.954 9.446 1.00 24.72 C ANISOU 1974 CE1 PHE A 258 4142 2346 2904 -343 523 -483 C ATOM 1975 CE2 PHE A 258 14.810 -9.682 11.421 1.00 26.52 C ANISOU 1975 CE2 PHE A 258 4265 2651 3159 -331 457 -460 C ATOM 1976 CZ PHE A 258 15.011 -10.217 10.120 1.00 25.19 C ANISOU 1976 CZ PHE A 258 4167 2439 2966 -351 476 -473 C ATOM 1977 N ALA A 259 20.542 -9.733 12.238 1.00 25.19 N ANISOU 1977 N ALA A 259 4035 2439 3095 -249 648 -488 N ATOM 1978 CA ALA A 259 21.257 -10.949 11.846 1.00 25.73 C ANISOU 1978 CA ALA A 259 4131 2472 3175 -245 688 -489 C ATOM 1979 C ALA A 259 21.501 -11.852 13.056 1.00 25.21 C ANISOU 1979 C ALA A 259 4015 2428 3135 -216 686 -472 C ATOM 1980 O ALA A 259 21.405 -13.079 12.955 1.00 26.22 O ANISOU 1980 O ALA A 259 4169 2531 3262 -216 698 -462 O ATOM 1981 CB ALA A 259 22.569 -10.596 11.162 1.00 26.29 C ANISOU 1981 CB ALA A 259 4215 2515 3259 -240 742 -511 C ATOM 1982 N ARG A 260 21.803 -11.250 14.203 1.00 24.74 N ANISOU 1982 N ARG A 260 3889 2415 3096 -192 671 -470 N ATOM 1983 CA ARG A 260 22.019 -12.024 15.411 1.00 24.06 C ANISOU 1983 CA ARG A 260 3758 2353 3029 -160 665 -453 C ATOM 1984 C ARG A 260 20.746 -12.796 15.785 1.00 23.99 C ANISOU 1984 C ARG A 260 3764 2346 3003 -172 634 -429 C ATOM 1985 O ARG A 260 20.814 -13.904 16.334 1.00 23.14 O ANISOU 1985 O ARG A 260 3656 2233 2904 -154 643 -412 O ATOM 1986 CB ARG A 260 22.494 -11.102 16.548 1.00 25.09 C ANISOU 1986 CB ARG A 260 3816 2536 3179 -134 648 -458 C ATOM 1987 CG ARG A 260 22.773 -11.798 17.867 1.00 24.15 C ANISOU 1987 CG ARG A 260 3652 2450 3076 -95 638 -440 C ATOM 1988 CD ARG A 260 24.090 -12.602 17.805 1.00 27.93 C ANISOU 1988 CD ARG A 260 4123 2911 3579 -62 678 -445 C ATOM 1989 NE ARG A 260 24.281 -13.418 19.009 1.00 27.25 N ANISOU 1989 NE ARG A 260 4004 2849 3500 -20 668 -423 N ATOM 1990 CZ ARG A 260 25.392 -14.094 19.294 1.00 29.69 C ANISOU 1990 CZ ARG A 260 4293 3157 3831 22 693 -423 C ATOM 1991 NH1 ARG A 260 26.442 -14.048 18.478 1.00 25.32 N ANISOU 1991 NH1 ARG A 260 3743 2580 3298 24 732 -447 N ATOM 1992 NH2 ARG A 260 25.443 -14.833 20.404 1.00 30.52 N ANISOU 1992 NH2 ARG A 260 4376 3285 3937 64 679 -399 N ATOM 1993 N LEU A 261 19.580 -12.240 15.452 1.00 23.07 N ANISOU 1993 N LEU A 261 3665 2236 2864 -202 601 -430 N ATOM 1994 CA LEU A 261 18.331 -12.922 15.771 1.00 23.17 C ANISOU 1994 CA LEU A 261 3687 2253 2865 -219 573 -413 C ATOM 1995 C LEU A 261 18.200 -14.195 14.908 1.00 23.38 C ANISOU 1995 C LEU A 261 3773 2228 2882 -239 598 -412 C ATOM 1996 O LEU A 261 17.682 -15.199 15.373 1.00 22.94 O ANISOU 1996 O LEU A 261 3723 2166 2829 -241 598 -397 O ATOM 1997 CB LEU A 261 17.108 -12.028 15.605 1.00 21.77 C ANISOU 1997 CB LEU A 261 3507 2096 2667 -244 530 -415 C ATOM 1998 CG LEU A 261 17.000 -10.739 16.429 1.00 21.85 C ANISOU 1998 CG LEU A 261 3464 2154 2685 -230 504 -416 C ATOM 1999 CD1 LEU A 261 15.623 -10.207 16.172 1.00 19.69 C ANISOU 1999 CD1 LEU A 261 3197 1893 2391 -255 463 -415 C ATOM 2000 CD2 LEU A 261 17.197 -11.051 17.944 1.00 21.34 C ANISOU 2000 CD2 LEU A 261 3346 2125 2640 -199 500 -399 C ATOM 2001 N LEU A 262 18.668 -14.154 13.670 1.00 24.16 N ANISOU 2001 N LEU A 262 3920 2289 2970 -254 622 -430 N ATOM 2002 CA LEU A 262 18.663 -15.372 12.817 1.00 25.52 C ANISOU 2002 CA LEU A 262 4153 2410 3132 -272 651 -433 C ATOM 2003 C LEU A 262 19.565 -16.473 13.358 1.00 26.11 C ANISOU 2003 C LEU A 262 4222 2467 3232 -241 692 -421 C ATOM 2004 O LEU A 262 19.198 -17.647 13.323 1.00 26.70 O ANISOU 2004 O LEU A 262 4328 2513 3305 -251 706 -412 O ATOM 2005 CB LEU A 262 19.051 -15.081 11.351 1.00 26.14 C ANISOU 2005 CB LEU A 262 4290 2450 3191 -293 674 -455 C ATOM 2006 CG LEU A 262 17.991 -14.600 10.350 1.00 26.88 C ANISOU 2006 CG LEU A 262 4428 2539 3248 -331 640 -467 C ATOM 2007 CD1 LEU A 262 16.862 -15.614 10.213 1.00 29.03 C ANISOU 2007 CD1 LEU A 262 4726 2799 3505 -362 620 -465 C ATOM 2008 CD2 LEU A 262 17.412 -13.256 10.783 1.00 28.46 C ANISOU 2008 CD2 LEU A 262 4586 2784 3441 -328 596 -465 C ATOM 2009 N TYR A 263 20.748 -16.091 13.835 1.00 26.80 N ANISOU 2009 N TYR A 263 4270 2570 3343 -203 712 -422 N ATOM 2010 CA TYR A 263 21.640 -17.013 14.526 1.00 27.06 C ANISOU 2010 CA TYR A 263 4285 2597 3401 -162 743 -408 C ATOM 2011 C TYR A 263 20.914 -17.649 15.712 1.00 27.26 C ANISOU 2011 C TYR A 263 4288 2642 3427 -149 721 -382 C ATOM 2012 O TYR A 263 20.927 -18.868 15.868 1.00 26.66 O ANISOU 2012 O TYR A 263 4239 2537 3355 -140 746 -367 O ATOM 2013 CB TYR A 263 22.911 -16.291 14.979 1.00 27.94 C ANISOU 2013 CB TYR A 263 4342 2736 3537 -124 755 -418 C ATOM 2014 CG TYR A 263 23.797 -17.141 15.854 1.00 30.35 C ANISOU 2014 CG TYR A 263 4618 3047 3868 -73 776 -403 C ATOM 2015 CD1 TYR A 263 24.378 -18.319 15.349 1.00 34.40 C ANISOU 2015 CD1 TYR A 263 5171 3511 4388 -60 822 -399 C ATOM 2016 CD2 TYR A 263 24.034 -16.800 17.188 1.00 30.58 C ANISOU 2016 CD2 TYR A 263 4582 3129 3909 -35 750 -392 C ATOM 2017 CE1 TYR A 263 25.184 -19.132 16.145 1.00 31.89 C ANISOU 2017 CE1 TYR A 263 4829 3196 4092 -6 841 -383 C ATOM 2018 CE2 TYR A 263 24.849 -17.587 17.999 1.00 31.47 C ANISOU 2018 CE2 TYR A 263 4669 3248 4039 19 766 -377 C ATOM 2019 CZ TYR A 263 25.424 -18.759 17.463 1.00 33.07 C ANISOU 2019 CZ TYR A 263 4913 3402 4252 34 811 -371 C ATOM 2020 OH TYR A 263 26.234 -19.563 18.240 1.00 33.65 O ANISOU 2020 OH TYR A 263 4964 3481 4342 93 826 -354 O ATOM 2021 N ASN A 264 20.263 -16.828 16.534 1.00 26.25 N ANISOU 2021 N ASN A 264 4116 2563 3295 -150 679 -376 N ATOM 2022 CA ASN A 264 19.472 -17.357 17.633 1.00 26.94 C ANISOU 2022 CA ASN A 264 4186 2668 3381 -142 660 -351 C ATOM 2023 C ASN A 264 18.433 -18.372 17.155 1.00 26.39 C ANISOU 2023 C ASN A 264 4169 2561 3298 -180 667 -346 C ATOM 2024 O ASN A 264 18.305 -19.435 17.746 1.00 25.69 O ANISOU 2024 O ASN A 264 4093 2455 3214 -167 685 -326 O ATOM 2025 CB ASN A 264 18.800 -16.232 18.414 1.00 26.97 C ANISOU 2025 CB ASN A 264 4140 2726 3380 -145 615 -350 C ATOM 2026 CG ASN A 264 19.696 -15.658 19.481 1.00 28.32 C ANISOU 2026 CG ASN A 264 4253 2941 3566 -98 609 -346 C ATOM 2027 OD1 ASN A 264 19.969 -16.293 20.508 1.00 30.62 O ANISOU 2027 OD1 ASN A 264 4525 3244 3863 -61 614 -325 O ATOM 2028 ND2 ASN A 264 20.165 -14.459 19.247 1.00 30.38 N ANISOU 2028 ND2 ASN A 264 4487 3226 3832 -99 599 -367 N ATOM 2029 N ASP A 265 17.708 -18.046 16.089 1.00 26.49 N ANISOU 2029 N ASP A 265 4213 2558 3293 -226 652 -365 N ATOM 2030 CA ASP A 265 16.737 -18.973 15.511 1.00 27.58 C ANISOU 2030 CA ASP A 265 4401 2661 3419 -269 657 -369 C ATOM 2031 C ASP A 265 17.436 -20.277 15.079 1.00 29.02 C ANISOU 2031 C ASP A 265 4632 2787 3606 -261 709 -366 C ATOM 2032 O ASP A 265 16.938 -21.363 15.380 1.00 28.97 O ANISOU 2032 O ASP A 265 4650 2756 3602 -271 727 -354 O ATOM 2033 CB ASP A 265 16.000 -18.340 14.323 1.00 27.11 C ANISOU 2033 CB ASP A 265 4369 2597 3336 -314 629 -393 C ATOM 2034 CG ASP A 265 14.895 -17.379 14.754 1.00 27.28 C ANISOU 2034 CG ASP A 265 4349 2666 3350 -329 577 -394 C ATOM 2035 OD1 ASP A 265 14.790 -17.077 15.968 1.00 24.79 O ANISOU 2035 OD1 ASP A 265 3983 2388 3048 -305 563 -377 O ATOM 2036 OD2 ASP A 265 14.147 -16.899 13.868 1.00 26.03 O ANISOU 2036 OD2 ASP A 265 4210 2508 3170 -363 548 -412 O ATOM 2037 N PHE A 266 18.607 -20.167 14.447 1.00 29.86 N ANISOU 2037 N PHE A 266 4754 2874 3719 -241 739 -376 N ATOM 2038 CA PHE A 266 19.424 -21.356 14.111 1.00 31.50 C ANISOU 2038 CA PHE A 266 5003 3029 3936 -224 793 -372 C ATOM 2039 C PHE A 266 19.642 -22.203 15.349 1.00 32.19 C ANISOU 2039 C PHE A 266 5071 3120 4040 -183 810 -342 C ATOM 2040 O PHE A 266 19.308 -23.395 15.355 1.00 31.99 O ANISOU 2040 O PHE A 266 5087 3053 4014 -192 838 -332 O ATOM 2041 CB PHE A 266 20.785 -20.974 13.496 1.00 31.84 C ANISOU 2041 CB PHE A 266 5047 3061 3990 -199 824 -386 C ATOM 2042 CG PHE A 266 21.795 -22.102 13.517 1.00 33.46 C ANISOU 2042 CG PHE A 266 5274 3225 4213 -163 878 -376 C ATOM 2043 CD1 PHE A 266 22.921 -22.034 14.348 1.00 32.71 C ANISOU 2043 CD1 PHE A 266 5130 3153 4144 -103 891 -364 C ATOM 2044 CD2 PHE A 266 21.599 -23.250 12.735 1.00 32.28 C ANISOU 2044 CD2 PHE A 266 5194 3015 4056 -188 916 -381 C ATOM 2045 CE1 PHE A 266 23.847 -23.074 14.387 1.00 33.35 C ANISOU 2045 CE1 PHE A 266 5230 3198 4244 -64 940 -354 C ATOM 2046 CE2 PHE A 266 22.529 -24.317 12.761 1.00 33.39 C ANISOU 2046 CE2 PHE A 266 5359 3114 4215 -151 970 -370 C ATOM 2047 CZ PHE A 266 23.650 -24.233 13.589 1.00 34.03 C ANISOU 2047 CZ PHE A 266 5389 3219 4322 -87 982 -356 C ATOM 2048 N LEU A 267 20.146 -21.579 16.418 1.00 32.06 N ANISOU 2048 N LEU A 267 4993 3151 4036 -138 791 -328 N ATOM 2049 CA LEU A 267 20.408 -22.304 17.660 1.00 33.27 C ANISOU 2049 CA LEU A 267 5128 3312 4200 -90 803 -298 C ATOM 2050 C LEU A 267 19.188 -23.005 18.257 1.00 34.26 C ANISOU 2050 C LEU A 267 5272 3428 4316 -113 798 -280 C ATOM 2051 O LEU A 267 19.337 -24.024 18.943 1.00 34.50 O ANISOU 2051 O LEU A 267 5320 3437 4351 -82 826 -254 O ATOM 2052 CB LEU A 267 21.028 -21.402 18.710 1.00 32.98 C ANISOU 2052 CB LEU A 267 5021 3336 4173 -43 775 -291 C ATOM 2053 CG LEU A 267 22.411 -20.831 18.415 1.00 32.32 C ANISOU 2053 CG LEU A 267 4908 3265 4107 -10 787 -307 C ATOM 2054 CD1 LEU A 267 22.794 -19.881 19.549 1.00 32.56 C ANISOU 2054 CD1 LEU A 267 4866 3362 4145 27 751 -304 C ATOM 2055 CD2 LEU A 267 23.439 -21.945 18.272 1.00 32.38 C ANISOU 2055 CD2 LEU A 267 4940 3232 4130 32 835 -298 C ATOM 2056 N ARG A 268 17.998 -22.473 17.981 1.00 34.75 N ANISOU 2056 N ARG A 268 5333 3506 4366 -165 764 -293 N ATOM 2057 CA ARG A 268 16.766 -23.023 18.524 1.00 35.89 C ANISOU 2057 CA ARG A 268 5487 3646 4504 -194 758 -281 C ATOM 2058 C ARG A 268 16.055 -23.895 17.503 1.00 37.16 C ANISOU 2058 C ARG A 268 5708 3754 4658 -249 780 -298 C ATOM 2059 O ARG A 268 14.907 -24.290 17.713 1.00 38.04 O ANISOU 2059 O ARG A 268 5827 3859 4766 -288 775 -299 O ATOM 2060 CB ARG A 268 15.840 -21.889 19.003 1.00 35.53 C ANISOU 2060 CB ARG A 268 5392 3656 4453 -213 706 -286 C ATOM 2061 CG ARG A 268 16.388 -21.089 20.220 1.00 35.09 C ANISOU 2061 CG ARG A 268 5276 3654 4402 -161 684 -269 C ATOM 2062 CD ARG A 268 15.824 -19.657 20.236 1.00 37.84 C ANISOU 2062 CD ARG A 268 5578 4053 4745 -180 635 -284 C ATOM 2063 NE ARG A 268 14.383 -19.727 20.370 1.00 38.53 N ANISOU 2063 NE ARG A 268 5666 4145 4827 -224 616 -285 N ATOM 2064 CZ ARG A 268 13.521 -19.279 19.473 1.00 40.22 C ANISOU 2064 CZ ARG A 268 5889 4360 5034 -272 591 -309 C ATOM 2065 NH1 ARG A 268 13.935 -18.638 18.377 1.00 37.38 N ANISOU 2065 NH1 ARG A 268 5541 3996 4666 -283 580 -330 N ATOM 2066 NH2 ARG A 268 12.229 -19.449 19.703 1.00 40.68 N ANISOU 2066 NH2 ARG A 268 5940 4424 5091 -308 576 -310 N ATOM 2067 N ASN A 269 16.753 -24.215 16.414 1.00 38.24 N ANISOU 2067 N ASN A 269 5886 3850 4792 -255 808 -314 N ATOM 2068 CA ASN A 269 16.182 -24.920 15.261 1.00 39.59 C ANISOU 2068 CA ASN A 269 6117 3972 4952 -310 826 -338 C ATOM 2069 C ASN A 269 14.794 -24.433 14.919 1.00 38.87 C ANISOU 2069 C ASN A 269 6018 3903 4848 -369 781 -359 C ATOM 2070 O ASN A 269 13.875 -25.251 14.736 1.00 38.92 O ANISOU 2070 O ASN A 269 6055 3882 4852 -413 791 -368 O ATOM 2071 CB ASN A 269 16.135 -26.454 15.432 1.00 41.04 C ANISOU 2071 CB ASN A 269 6353 4097 5143 -312 880 -325 C ATOM 2072 CG ASN A 269 17.100 -26.970 16.471 1.00 44.24 C ANISOU 2072 CG ASN A 269 6748 4497 5564 -243 913 -290 C ATOM 2073 OD1 ASN A 269 16.800 -26.950 17.662 1.00 48.35 O ANISOU 2073 OD1 ASN A 269 7237 5045 6088 -218 903 -265 O ATOM 2074 ND2 ASN A 269 18.249 -27.484 16.025 1.00 48.88 N ANISOU 2074 ND2 ASN A 269 7364 5048 6158 -209 955 -288 N ATOM 2075 N ALA A 270 14.645 -23.107 14.851 1.00 37.33 N ANISOU 2075 N ALA A 270 5780 3759 4646 -368 733 -368 N ATOM 2076 CA ALA A 270 13.359 -22.490 14.598 1.00 36.53 C ANISOU 2076 CA ALA A 270 5661 3687 4532 -414 684 -386 C ATOM 2077 C ALA A 270 12.988 -22.586 13.125 1.00 36.62 C ANISOU 2077 C ALA A 270 5722 3671 4521 -462 676 -419 C ATOM 2078 O ALA A 270 13.848 -22.779 12.265 1.00 36.66 O ANISOU 2078 O ALA A 270 5769 3642 4518 -456 704 -428 O ATOM 2079 CB ALA A 270 13.368 -21.059 15.060 1.00 36.26 C ANISOU 2079 CB ALA A 270 5568 3711 4497 -391 639 -381 C ATOM 2080 N SER A 271 11.703 -22.433 12.836 1.00 36.36 N ANISOU 2080 N SER A 271 5682 3655 4478 -509 638 -438 N ATOM 2081 CA SER A 271 11.195 -22.670 11.494 1.00 36.82 C ANISOU 2081 CA SER A 271 5790 3690 4512 -558 626 -472 C ATOM 2082 C SER A 271 11.520 -21.572 10.480 1.00 36.46 C ANISOU 2082 C SER A 271 5755 3658 4439 -553 596 -487 C ATOM 2083 O SER A 271 11.280 -21.752 9.268 1.00 37.43 O ANISOU 2083 O SER A 271 5929 3758 4536 -587 589 -515 O ATOM 2084 CB SER A 271 9.695 -22.962 11.536 1.00 37.13 C ANISOU 2084 CB SER A 271 5814 3743 4551 -610 595 -491 C ATOM 2085 OG SER A 271 8.957 -21.814 11.850 1.00 38.27 O ANISOU 2085 OG SER A 271 5902 3945 4692 -607 538 -492 O ATOM 2086 N SER A 272 12.061 -20.439 10.947 1.00 34.49 N ANISOU 2086 N SER A 272 5465 3445 4195 -512 579 -471 N ATOM 2087 CA SER A 272 12.556 -19.420 10.027 1.00 32.93 C ANISOU 2087 CA SER A 272 5286 3253 3974 -503 564 -483 C ATOM 2088 C SER A 272 13.821 -19.879 9.311 1.00 32.78 C ANISOU 2088 C SER A 272 5319 3185 3951 -489 617 -487 C ATOM 2089 O SER A 272 14.288 -19.236 8.366 1.00 31.97 O ANISOU 2089 O SER A 272 5248 3073 3827 -488 617 -500 O ATOM 2090 CB SER A 272 12.875 -18.110 10.779 1.00 32.04 C ANISOU 2090 CB SER A 272 5115 3188 3872 -464 541 -467 C ATOM 2091 OG SER A 272 13.834 -18.364 11.802 1.00 29.34 O ANISOU 2091 OG SER A 272 4743 2846 3559 -424 577 -443 O ATOM 2092 N ILE A 273 14.420 -20.953 9.803 1.00 34.17 N ANISOU 2092 N ILE A 273 5504 3329 4150 -475 666 -473 N ATOM 2093 CA ILE A 273 15.722 -21.376 9.295 1.00 34.59 C ANISOU 2093 CA ILE A 273 5597 3339 4208 -453 721 -474 C ATOM 2094 C ILE A 273 15.493 -22.484 8.276 1.00 36.51 C ANISOU 2094 C ILE A 273 5913 3526 4433 -492 749 -495 C ATOM 2095 O ILE A 273 15.095 -23.584 8.631 1.00 35.99 O ANISOU 2095 O ILE A 273 5860 3437 4378 -508 769 -491 O ATOM 2096 CB ILE A 273 16.691 -21.802 10.436 1.00 34.70 C ANISOU 2096 CB ILE A 273 5576 3353 4257 -401 759 -446 C ATOM 2097 CG1 ILE A 273 16.979 -20.613 11.385 1.00 31.39 C ANISOU 2097 CG1 ILE A 273 5084 2991 3852 -364 729 -431 C ATOM 2098 CG2 ILE A 273 18.017 -22.352 9.858 1.00 34.75 C ANISOU 2098 CG2 ILE A 273 5622 3312 4271 -378 819 -449 C ATOM 2099 CD1 ILE A 273 17.718 -19.442 10.746 1.00 31.89 C ANISOU 2099 CD1 ILE A 273 5144 3065 3907 -352 726 -444 C ATOM 2100 N ASP A 274 15.725 -22.175 7.004 1.00 37.87 N ANISOU 2100 N ASP A 274 6136 3676 4575 -510 752 -518 N ATOM 2101 CA ASP A 274 15.566 -23.207 5.985 1.00 39.96 C ANISOU 2101 CA ASP A 274 6475 3887 4819 -549 780 -541 C ATOM 2102 C ASP A 274 16.819 -24.052 5.779 1.00 40.71 C ANISOU 2102 C ASP A 274 6609 3927 4930 -525 853 -536 C ATOM 2103 O ASP A 274 17.909 -23.765 6.313 1.00 39.99 O ANISOU 2103 O ASP A 274 6487 3842 4866 -476 881 -517 O ATOM 2104 CB ASP A 274 15.039 -22.636 4.646 1.00 40.41 C ANISOU 2104 CB ASP A 274 6581 3944 4829 -585 745 -571 C ATOM 2105 CG ASP A 274 16.064 -21.793 3.902 1.00 42.43 C ANISOU 2105 CG ASP A 274 6862 4189 5069 -560 765 -574 C ATOM 2106 OD1 ASP A 274 15.655 -21.027 2.998 1.00 45.13 O ANISOU 2106 OD1 ASP A 274 7235 4541 5372 -578 730 -592 O ATOM 2107 OD2 ASP A 274 17.270 -21.879 4.203 1.00 44.98 O ANISOU 2107 OD2 ASP A 274 7178 4494 5420 -523 816 -561 O ATOM 2108 N GLU A 275 16.600 -25.127 5.021 1.00 42.01 N ANISOU 2108 N GLU A 275 6840 4041 5081 -560 883 -556 N ATOM 2109 CA GLU A 275 17.596 -26.030 4.482 1.00 42.73 C ANISOU 2109 CA GLU A 275 6988 4070 5178 -550 953 -560 C ATOM 2110 C GLU A 275 18.977 -25.433 4.257 1.00 40.89 C ANISOU 2110 C GLU A 275 6751 3830 4955 -505 988 -553 C ATOM 2111 O GLU A 275 19.935 -25.824 4.917 1.00 41.29 O ANISOU 2111 O GLU A 275 6778 3868 5041 -460 1032 -532 O ATOM 2112 CB GLU A 275 17.043 -26.609 3.157 1.00 44.69 C ANISOU 2112 CB GLU A 275 7318 4275 5386 -607 958 -597 C ATOM 2113 CG GLU A 275 16.292 -25.545 2.283 1.00 49.30 C ANISOU 2113 CG GLU A 275 7914 4894 5925 -638 894 -620 C ATOM 2114 CD GLU A 275 14.768 -25.439 2.560 1.00 54.85 C ANISOU 2114 CD GLU A 275 8585 5638 6615 -678 826 -631 C ATOM 2115 OE1 GLU A 275 14.290 -25.847 3.648 1.00 57.04 O ANISOU 2115 OE1 GLU A 275 8814 5934 6925 -676 820 -615 O ATOM 2116 OE2 GLU A 275 14.046 -24.919 1.676 1.00 57.95 O ANISOU 2116 OE2 GLU A 275 9004 6048 6967 -710 778 -657 O ATOM 2117 N ALA A 276 19.061 -24.502 3.314 1.00 39.49 N ANISOU 2117 N ALA A 276 6597 3659 4747 -518 971 -571 N ATOM 2118 CA ALA A 276 20.288 -23.811 2.965 1.00 39.13 C ANISOU 2118 CA ALA A 276 6552 3607 4710 -484 1005 -571 C ATOM 2119 C ALA A 276 20.886 -22.960 4.083 1.00 37.97 C ANISOU 2119 C ALA A 276 6320 3509 4599 -435 994 -547 C ATOM 2120 O ALA A 276 22.125 -22.845 4.202 1.00 37.37 O ANISOU 2120 O ALA A 276 6226 3422 4550 -397 1039 -542 O ATOM 2121 CB ALA A 276 20.060 -22.947 1.724 1.00 39.66 C ANISOU 2121 CB ALA A 276 6669 3671 4728 -512 985 -595 C ATOM 2122 N ALA A 277 20.012 -22.337 4.876 1.00 36.92 N ANISOU 2122 N ALA A 277 6131 3430 4466 -438 933 -535 N ATOM 2123 CA ALA A 277 20.444 -21.524 6.004 1.00 35.44 C ANISOU 2123 CA ALA A 277 5864 3293 4310 -396 916 -515 C ATOM 2124 C ALA A 277 21.088 -22.453 7.026 1.00 35.11 C ANISOU 2124 C ALA A 277 5789 3242 4308 -356 952 -492 C ATOM 2125 O ALA A 277 22.170 -22.164 7.513 1.00 33.64 O ANISOU 2125 O ALA A 277 5562 3068 4152 -312 976 -484 O ATOM 2126 CB ALA A 277 19.263 -20.796 6.613 1.00 35.21 C ANISOU 2126 CB ALA A 277 5790 3319 4271 -410 847 -508 C ATOM 2127 N LYS A 278 20.431 -23.579 7.331 1.00 36.50 N ANISOU 2127 N LYS A 278 5986 3399 4486 -372 956 -485 N ATOM 2128 CA LYS A 278 21.017 -24.571 8.259 1.00 38.26 C ANISOU 2128 CA LYS A 278 6190 3605 4741 -331 994 -461 C ATOM 2129 C LYS A 278 22.446 -24.908 7.873 1.00 38.58 C ANISOU 2129 C LYS A 278 6248 3610 4802 -294 1056 -463 C ATOM 2130 O LYS A 278 23.374 -24.786 8.704 1.00 38.23 O ANISOU 2130 O LYS A 278 6150 3586 4790 -239 1070 -446 O ATOM 2131 CB LYS A 278 20.190 -25.854 8.337 1.00 39.02 C ANISOU 2131 CB LYS A 278 6328 3665 4832 -360 1008 -457 C ATOM 2132 CG LYS A 278 19.289 -25.938 9.554 1.00 41.37 C ANISOU 2132 CG LYS A 278 6581 4001 5139 -358 972 -436 C ATOM 2133 CD LYS A 278 18.939 -27.395 9.895 1.00 47.44 C ANISOU 2133 CD LYS A 278 7386 4723 5916 -367 1010 -425 C ATOM 2134 CE LYS A 278 17.610 -27.483 10.655 1.00 51.91 C ANISOU 2134 CE LYS A 278 7928 5316 6479 -397 972 -418 C ATOM 2135 NZ LYS A 278 16.533 -26.696 9.963 1.00 53.35 N ANISOU 2135 NZ LYS A 278 8108 5528 6636 -452 916 -446 N ATOM 2136 N GLU A 279 22.609 -25.265 6.597 1.00 39.16 N ANISOU 2136 N GLU A 279 6392 3632 4855 -324 1091 -487 N ATOM 2137 CA GLU A 279 23.897 -25.647 6.004 1.00 40.49 C ANISOU 2137 CA GLU A 279 6589 3756 5040 -298 1157 -495 C ATOM 2138 C GLU A 279 24.899 -24.499 6.089 1.00 39.53 C ANISOU 2138 C GLU A 279 6415 3668 4938 -265 1159 -499 C ATOM 2139 O GLU A 279 26.082 -24.716 6.320 1.00 40.13 O ANISOU 2139 O GLU A 279 6467 3734 5047 -219 1203 -495 O ATOM 2140 CB GLU A 279 23.693 -26.115 4.545 1.00 41.33 C ANISOU 2140 CB GLU A 279 6787 3804 5112 -346 1187 -523 C ATOM 2141 CG GLU A 279 24.830 -26.973 3.950 1.00 47.20 C ANISOU 2141 CG GLU A 279 7576 4484 5872 -324 1267 -530 C ATOM 2142 CD GLU A 279 24.453 -28.447 3.626 1.00 54.37 C ANISOU 2142 CD GLU A 279 8554 5330 6772 -347 1306 -533 C ATOM 2143 OE1 GLU A 279 23.262 -28.869 3.731 1.00 56.68 O ANISOU 2143 OE1 GLU A 279 8867 5624 7044 -388 1274 -535 O ATOM 2144 OE2 GLU A 279 25.377 -29.200 3.228 1.00 57.26 O ANISOU 2144 OE2 GLU A 279 8957 5645 7155 -325 1374 -536 O ATOM 2145 N LYS A 280 24.432 -23.263 5.932 1.00 38.73 N ANISOU 2145 N LYS A 280 6292 3606 4816 -286 1112 -508 N ATOM 2146 CA LYS A 280 25.306 -22.096 6.127 1.00 37.44 C ANISOU 2146 CA LYS A 280 6075 3477 4672 -258 1112 -513 C ATOM 2147 C LYS A 280 25.798 -21.938 7.571 1.00 36.59 C ANISOU 2147 C LYS A 280 5878 3419 4605 -206 1097 -492 C ATOM 2148 O LYS A 280 26.925 -21.519 7.806 1.00 36.90 O ANISOU 2148 O LYS A 280 5874 3472 4675 -170 1122 -497 O ATOM 2149 CB LYS A 280 24.585 -20.829 5.704 1.00 37.98 C ANISOU 2149 CB LYS A 280 6146 3576 4710 -292 1064 -525 C ATOM 2150 CG LYS A 280 24.347 -20.683 4.211 1.00 39.57 C ANISOU 2150 CG LYS A 280 6431 3735 4868 -334 1080 -549 C ATOM 2151 CD LYS A 280 25.301 -19.672 3.642 1.00 43.29 C ANISOU 2151 CD LYS A 280 6901 4202 5344 -325 1111 -566 C ATOM 2152 CE LYS A 280 24.639 -18.875 2.528 1.00 46.31 C ANISOU 2152 CE LYS A 280 7346 4575 5675 -365 1090 -582 C ATOM 2153 NZ LYS A 280 24.461 -19.728 1.334 1.00 47.77 N ANISOU 2153 NZ LYS A 280 7624 4701 5824 -396 1120 -598 N ATOM 2154 N PHE A 281 24.944 -22.244 8.538 1.00 35.81 N ANISOU 2154 N PHE A 281 5753 3348 4504 -203 1056 -470 N ATOM 2155 CA PHE A 281 25.294 -22.054 9.938 1.00 35.86 C ANISOU 2155 CA PHE A 281 5681 3405 4540 -155 1035 -448 C ATOM 2156 C PHE A 281 26.038 -23.253 10.539 1.00 36.83 C ANISOU 2156 C PHE A 281 5798 3505 4691 -105 1075 -429 C ATOM 2157 O PHE A 281 26.799 -23.117 11.501 1.00 37.07 O ANISOU 2157 O PHE A 281 5765 3570 4749 -53 1072 -417 O ATOM 2158 CB PHE A 281 24.020 -21.847 10.752 1.00 35.27 C ANISOU 2158 CB PHE A 281 5583 3369 4449 -172 976 -432 C ATOM 2159 CG PHE A 281 23.529 -20.436 10.799 1.00 34.30 C ANISOU 2159 CG PHE A 281 5426 3293 4313 -191 927 -441 C ATOM 2160 CD1 PHE A 281 22.213 -20.147 10.468 1.00 34.39 C ANISOU 2160 CD1 PHE A 281 5462 3312 4293 -237 885 -445 C ATOM 2161 CD2 PHE A 281 24.363 -19.405 11.203 1.00 32.86 C ANISOU 2161 CD2 PHE A 281 5185 3150 4151 -163 923 -448 C ATOM 2162 CE1 PHE A 281 21.742 -18.837 10.532 1.00 34.27 C ANISOU 2162 CE1 PHE A 281 5416 3339 4265 -251 841 -452 C ATOM 2163 CE2 PHE A 281 23.904 -18.104 11.267 1.00 33.24 C ANISOU 2163 CE2 PHE A 281 5205 3237 4187 -180 882 -457 C ATOM 2164 CZ PHE A 281 22.586 -17.824 10.933 1.00 33.87 C ANISOU 2164 CZ PHE A 281 5313 3322 4235 -222 841 -457 C ATOM 2165 N THR A 282 25.804 -24.439 9.999 1.00 38.16 N ANISOU 2165 N THR A 282 6034 3617 4850 -120 1111 -427 N ATOM 2166 CA THR A 282 26.413 -25.652 10.588 1.00 39.30 C ANISOU 2166 CA THR A 282 6180 3733 5017 -71 1151 -405 C ATOM 2167 C THR A 282 27.911 -25.560 10.900 1.00 39.40 C ANISOU 2167 C THR A 282 6144 3757 5068 -8 1182 -405 C ATOM 2168 O THR A 282 28.301 -25.984 11.979 1.00 39.82 O ANISOU 2168 O THR A 282 6157 3831 5141 48 1179 -380 O ATOM 2169 CB THR A 282 26.031 -26.924 9.831 1.00 39.84 C ANISOU 2169 CB THR A 282 6336 3731 5072 -100 1195 -406 C ATOM 2170 OG1 THR A 282 24.612 -27.031 9.882 1.00 41.12 O ANISOU 2170 OG1 THR A 282 6523 3896 5206 -151 1157 -404 O ATOM 2171 CG2 THR A 282 26.653 -28.217 10.477 1.00 40.54 C ANISOU 2171 CG2 THR A 282 6432 3785 5184 -43 1241 -380 C ATOM 2172 N PRO A 283 28.745 -24.980 10.004 1.00 39.63 N ANISOU 2172 N PRO A 283 6175 3776 5108 -14 1212 -433 N ATOM 2173 CA PRO A 283 30.149 -24.837 10.436 1.00 40.17 C ANISOU 2173 CA PRO A 283 6180 3864 5217 47 1237 -436 C ATOM 2174 C PRO A 283 30.359 -24.143 11.797 1.00 40.47 C ANISOU 2174 C PRO A 283 6126 3977 5273 90 1187 -424 C ATOM 2175 O PRO A 283 31.424 -24.321 12.400 1.00 41.14 O ANISOU 2175 O PRO A 283 6158 4082 5392 151 1201 -420 O ATOM 2176 CB PRO A 283 30.798 -24.025 9.303 1.00 40.21 C ANISOU 2176 CB PRO A 283 6195 3854 5228 20 1268 -473 C ATOM 2177 CG PRO A 283 29.944 -24.331 8.083 1.00 40.28 C ANISOU 2177 CG PRO A 283 6300 3808 5197 -43 1283 -484 C ATOM 2178 CD PRO A 283 28.536 -24.466 8.635 1.00 40.07 C ANISOU 2178 CD PRO A 283 6284 3801 5139 -71 1226 -463 C ATOM 2179 N TYR A 284 29.358 -23.392 12.283 1.00 39.90 N ANISOU 2179 N TYR A 284 6035 3947 5178 61 1129 -418 N ATOM 2180 CA TYR A 284 29.488 -22.609 13.531 1.00 39.90 C ANISOU 2180 CA TYR A 284 5952 4020 5190 94 1080 -409 C ATOM 2181 C TYR A 284 28.804 -23.242 14.747 1.00 39.76 C ANISOU 2181 C TYR A 284 5924 4023 5161 121 1047 -373 C ATOM 2182 O TYR A 284 28.848 -22.682 15.843 1.00 39.15 O ANISOU 2182 O TYR A 284 5784 4005 5089 150 1006 -364 O ATOM 2183 CB TYR A 284 29.020 -21.158 13.314 1.00 39.47 C ANISOU 2183 CB TYR A 284 5874 4003 5122 50 1041 -431 C ATOM 2184 CG TYR A 284 29.738 -20.573 12.139 1.00 40.13 C ANISOU 2184 CG TYR A 284 5972 4060 5215 27 1080 -464 C ATOM 2185 CD1 TYR A 284 30.985 -19.973 12.298 1.00 40.67 C ANISOU 2185 CD1 TYR A 284 5978 4154 5319 58 1099 -486 C ATOM 2186 CD2 TYR A 284 29.222 -20.714 10.848 1.00 41.55 C ANISOU 2186 CD2 TYR A 284 6233 4187 5368 -25 1104 -476 C ATOM 2187 CE1 TYR A 284 31.696 -19.509 11.206 1.00 42.21 C ANISOU 2187 CE1 TYR A 284 6192 4321 5527 36 1146 -518 C ATOM 2188 CE2 TYR A 284 29.917 -20.238 9.742 1.00 41.74 C ANISOU 2188 CE2 TYR A 284 6280 4182 5397 -45 1147 -506 C ATOM 2189 CZ TYR A 284 31.159 -19.641 9.932 1.00 41.76 C ANISOU 2189 CZ TYR A 284 6220 4207 5439 -14 1171 -526 C ATOM 2190 OH TYR A 284 31.857 -19.162 8.852 1.00 42.56 O ANISOU 2190 OH TYR A 284 6346 4278 5548 -35 1220 -556 O ATOM 2191 N SER A 285 28.212 -24.422 14.552 1.00 39.74 N ANISOU 2191 N SER A 285 5987 3969 5143 111 1070 -353 N ATOM 2192 CA SER A 285 27.472 -25.094 15.612 1.00 40.18 C ANISOU 2192 CA SER A 285 6047 4033 5186 130 1049 -319 C ATOM 2193 C SER A 285 28.355 -25.511 16.810 1.00 40.85 C ANISOU 2193 C SER A 285 6082 4147 5291 213 1049 -294 C ATOM 2194 O SER A 285 27.847 -25.717 17.914 1.00 39.94 O ANISOU 2194 O SER A 285 5953 4058 5164 236 1021 -266 O ATOM 2195 CB SER A 285 26.734 -26.309 15.049 1.00 40.72 C ANISOU 2195 CB SER A 285 6200 4033 5238 98 1084 -308 C ATOM 2196 OG SER A 285 27.654 -27.318 14.704 1.00 40.51 O ANISOU 2196 OG SER A 285 6205 3957 5230 136 1142 -304 O ATOM 2197 N SER A 286 29.666 -25.635 16.593 1.00 41.58 N ANISOU 2197 N SER A 286 6150 4236 5413 259 1081 -306 N ATOM 2198 CA SER A 286 30.590 -25.975 17.691 1.00 43.05 C ANISOU 2198 CA SER A 286 6284 4455 5619 344 1076 -286 C ATOM 2199 C SER A 286 31.085 -24.761 18.506 1.00 43.07 C ANISOU 2199 C SER A 286 6193 4540 5633 369 1025 -300 C ATOM 2200 O SER A 286 31.837 -24.936 19.468 1.00 43.76 O ANISOU 2200 O SER A 286 6229 4665 5732 440 1011 -288 O ATOM 2201 CB SER A 286 31.796 -26.764 17.161 1.00 43.44 C ANISOU 2201 CB SER A 286 6343 4465 5698 390 1133 -291 C ATOM 2202 OG SER A 286 32.549 -25.963 16.266 1.00 45.96 O ANISOU 2202 OG SER A 286 6635 4789 6041 368 1150 -332 O ATOM 2203 N LEU A 287 30.689 -23.540 18.133 1.00 42.39 N ANISOU 2203 N LEU A 287 6084 4481 5541 313 998 -328 N ATOM 2204 CA LEU A 287 31.159 -22.357 18.843 1.00 42.14 C ANISOU 2204 CA LEU A 287 5967 4522 5520 330 955 -346 C ATOM 2205 C LEU A 287 30.445 -22.253 20.193 1.00 42.09 C ANISOU 2205 C LEU A 287 5938 4565 5492 351 903 -318 C ATOM 2206 O LEU A 287 29.239 -22.509 20.282 1.00 41.90 O ANISOU 2206 O LEU A 287 5959 4521 5438 315 891 -297 O ATOM 2207 CB LEU A 287 30.908 -21.091 18.033 1.00 41.49 C ANISOU 2207 CB LEU A 287 5878 4450 5438 265 947 -382 C ATOM 2208 CG LEU A 287 31.741 -20.737 16.807 1.00 42.55 C ANISOU 2208 CG LEU A 287 6017 4553 5596 242 993 -418 C ATOM 2209 CD1 LEU A 287 31.209 -19.418 16.285 1.00 42.01 C ANISOU 2209 CD1 LEU A 287 5946 4500 5515 180 973 -444 C ATOM 2210 CD2 LEU A 287 33.240 -20.625 17.099 1.00 41.84 C ANISOU 2210 CD2 LEU A 287 5856 4493 5549 298 1010 -439 C ATOM 2211 N SER A 288 31.176 -21.890 21.246 1.00 42.22 N ANISOU 2211 N SER A 288 5881 4641 5518 407 872 -319 N ATOM 2212 CA SER A 288 30.522 -21.599 22.529 1.00 42.39 C ANISOU 2212 CA SER A 288 5877 4714 5515 424 821 -297 C ATOM 2213 C SER A 288 29.838 -20.233 22.404 1.00 42.20 C ANISOU 2213 C SER A 288 5829 4722 5481 362 787 -322 C ATOM 2214 O SER A 288 30.156 -19.460 21.494 1.00 41.48 O ANISOU 2214 O SER A 288 5728 4625 5408 323 800 -357 O ATOM 2215 CB SER A 288 31.527 -21.566 23.682 1.00 42.48 C ANISOU 2215 CB SER A 288 5819 4786 5537 503 794 -294 C ATOM 2216 OG SER A 288 32.409 -20.463 23.559 1.00 42.02 O ANISOU 2216 OG SER A 288 5686 4774 5506 500 780 -339 O ATOM 2217 N LEU A 289 28.909 -19.932 23.313 1.00 42.62 N ANISOU 2217 N LEU A 289 5878 4808 5509 355 746 -303 N ATOM 2218 CA LEU A 289 28.300 -18.594 23.347 1.00 42.53 C ANISOU 2218 CA LEU A 289 5837 4832 5489 306 712 -325 C ATOM 2219 C LEU A 289 29.374 -17.532 23.415 1.00 42.35 C ANISOU 2219 C LEU A 289 5742 4857 5493 318 701 -364 C ATOM 2220 O LEU A 289 29.349 -16.592 22.631 1.00 41.98 O ANISOU 2220 O LEU A 289 5689 4806 5455 269 707 -395 O ATOM 2221 CB LEU A 289 27.275 -18.433 24.496 1.00 42.86 C ANISOU 2221 CB LEU A 289 5875 4908 5501 307 671 -299 C ATOM 2222 CG LEU A 289 25.784 -18.543 24.137 1.00 44.15 C ANISOU 2222 CG LEU A 289 6095 5039 5642 248 670 -284 C ATOM 2223 CD1 LEU A 289 24.901 -18.339 25.375 1.00 45.67 C ANISOU 2223 CD1 LEU A 289 6274 5269 5810 255 633 -261 C ATOM 2224 CD2 LEU A 289 25.380 -17.564 23.031 1.00 43.26 C ANISOU 2224 CD2 LEU A 289 5989 4914 5534 183 669 -315 C ATOM 2225 N ASP A 290 30.342 -17.696 24.316 1.00 43.33 N ANISOU 2225 N ASP A 290 5812 5025 5629 383 686 -365 N ATOM 2226 CA ASP A 290 31.446 -16.726 24.428 1.00 44.44 C ANISOU 2226 CA ASP A 290 5874 5214 5798 395 676 -408 C ATOM 2227 C ASP A 290 32.132 -16.491 23.088 1.00 43.51 C ANISOU 2227 C ASP A 290 5761 5057 5712 363 723 -442 C ATOM 2228 O ASP A 290 32.316 -15.354 22.671 1.00 43.67 O ANISOU 2228 O ASP A 290 5754 5093 5747 323 724 -479 O ATOM 2229 CB ASP A 290 32.476 -17.168 25.480 1.00 46.01 C ANISOU 2229 CB ASP A 290 6015 5460 6006 476 657 -404 C ATOM 2230 CG ASP A 290 32.087 -16.754 26.885 1.00 49.45 C ANISOU 2230 CG ASP A 290 6417 5959 6414 502 601 -392 C ATOM 2231 OD1 ASP A 290 31.793 -15.548 27.084 1.00 51.08 O ANISOU 2231 OD1 ASP A 290 6590 6201 6618 463 576 -418 O ATOM 2232 OD2 ASP A 290 32.079 -17.637 27.788 1.00 52.93 O ANISOU 2232 OD2 ASP A 290 6868 6410 6834 562 586 -356 O ATOM 2233 N GLU A 291 32.489 -17.588 22.422 1.00 43.35 N ANISOU 2233 N GLU A 291 5784 4985 5702 381 766 -429 N ATOM 2234 CA GLU A 291 33.042 -17.592 21.057 1.00 42.69 C ANISOU 2234 CA GLU A 291 5724 4852 5645 351 820 -455 C ATOM 2235 C GLU A 291 32.125 -16.956 20.007 1.00 41.45 C ANISOU 2235 C GLU A 291 5622 4657 5471 272 832 -465 C ATOM 2236 O GLU A 291 32.607 -16.213 19.129 1.00 40.25 O ANISOU 2236 O GLU A 291 5463 4493 5339 238 860 -501 O ATOM 2237 CB GLU A 291 33.396 -19.029 20.642 1.00 42.50 C ANISOU 2237 CB GLU A 291 5747 4774 5627 386 862 -431 C ATOM 2238 CG GLU A 291 34.663 -19.531 21.334 1.00 44.90 C ANISOU 2238 CG GLU A 291 5990 5111 5960 467 863 -434 C ATOM 2239 CD GLU A 291 34.830 -21.048 21.334 1.00 45.49 C ANISOU 2239 CD GLU A 291 6112 5140 6032 518 893 -397 C ATOM 2240 OE1 GLU A 291 33.956 -21.793 20.820 1.00 47.36 O ANISOU 2240 OE1 GLU A 291 6432 5317 6245 489 916 -370 O ATOM 2241 OE2 GLU A 291 35.844 -21.496 21.903 1.00 48.24 O ANISOU 2241 OE2 GLU A 291 6413 5516 6402 591 892 -397 O ATOM 2242 N SER A 292 30.816 -17.231 20.107 1.00 40.50 N ANISOU 2242 N SER A 292 5554 4518 5314 245 812 -434 N ATOM 2243 CA SER A 292 29.834 -16.647 19.170 1.00 40.42 C ANISOU 2243 CA SER A 292 5595 4477 5284 175 814 -442 C ATOM 2244 C SER A 292 29.835 -15.114 19.111 1.00 41.06 C ANISOU 2244 C SER A 292 5637 4594 5369 141 795 -473 C ATOM 2245 O SER A 292 29.530 -14.543 18.050 1.00 41.45 O ANISOU 2245 O SER A 292 5724 4612 5412 92 813 -490 O ATOM 2246 CB SER A 292 28.413 -17.154 19.416 1.00 39.49 C ANISOU 2246 CB SER A 292 5529 4344 5131 153 790 -407 C ATOM 2247 OG SER A 292 27.862 -16.613 20.606 1.00 39.37 O ANISOU 2247 OG SER A 292 5473 4384 5103 164 741 -396 O ATOM 2248 N TYR A 293 30.182 -14.444 20.207 1.00 41.51 N ANISOU 2248 N TYR A 293 5624 4714 5436 168 761 -483 N ATOM 2249 CA TYR A 293 30.102 -12.968 20.207 1.00 42.95 C ANISOU 2249 CA TYR A 293 5772 4927 5621 133 744 -513 C ATOM 2250 C TYR A 293 31.246 -12.300 19.448 1.00 44.72 C ANISOU 2250 C TYR A 293 5970 5144 5879 121 785 -557 C ATOM 2251 O TYR A 293 31.073 -11.201 18.901 1.00 45.71 O ANISOU 2251 O TYR A 293 6100 5263 6003 78 792 -581 O ATOM 2252 CB TYR A 293 30.032 -12.354 21.609 1.00 42.05 C ANISOU 2252 CB TYR A 293 5593 4882 5502 158 695 -513 C ATOM 2253 CG TYR A 293 29.119 -12.994 22.631 1.00 39.97 C ANISOU 2253 CG TYR A 293 5341 4637 5210 181 657 -472 C ATOM 2254 CD1 TYR A 293 29.627 -13.337 23.886 1.00 40.51 C ANISOU 2254 CD1 TYR A 293 5360 4754 5279 239 630 -463 C ATOM 2255 CD2 TYR A 293 27.768 -13.214 22.380 1.00 38.66 C ANISOU 2255 CD2 TYR A 293 5233 4442 5014 147 647 -445 C ATOM 2256 CE1 TYR A 293 28.833 -13.907 24.867 1.00 42.11 C ANISOU 2256 CE1 TYR A 293 5576 4970 5452 263 600 -425 C ATOM 2257 CE2 TYR A 293 26.933 -13.785 23.374 1.00 39.65 C ANISOU 2257 CE2 TYR A 293 5367 4583 5114 167 617 -410 C ATOM 2258 CZ TYR A 293 27.489 -14.132 24.614 1.00 41.61 C ANISOU 2258 CZ TYR A 293 5571 4875 5363 225 597 -399 C ATOM 2259 OH TYR A 293 26.743 -14.709 25.627 1.00 42.08 O ANISOU 2259 OH TYR A 293 5643 4948 5396 248 573 -363 O ATOM 2260 N GLN A 294 32.414 -12.942 19.412 1.00 46.91 N ANISOU 2260 N GLN A 294 6217 5418 6187 160 814 -568 N ATOM 2261 CA GLN A 294 33.563 -12.381 18.668 1.00 48.08 C ANISOU 2261 CA GLN A 294 6338 5557 6374 148 860 -613 C ATOM 2262 C GLN A 294 33.892 -13.015 17.311 1.00 47.95 C ANISOU 2262 C GLN A 294 6383 5470 6366 132 921 -616 C ATOM 2263 O GLN A 294 34.942 -12.733 16.754 1.00 48.67 O ANISOU 2263 O GLN A 294 6448 5551 6492 129 966 -652 O ATOM 2264 CB GLN A 294 34.833 -12.360 19.531 1.00 49.08 C ANISOU 2264 CB GLN A 294 6372 5737 6539 200 853 -638 C ATOM 2265 CG GLN A 294 35.234 -10.973 20.030 1.00 51.54 C ANISOU 2265 CG GLN A 294 6612 6101 6869 182 836 -680 C ATOM 2266 CD GLN A 294 34.846 -10.751 21.478 1.00 54.35 C ANISOU 2266 CD GLN A 294 6921 6524 7207 211 771 -668 C ATOM 2267 OE1 GLN A 294 34.889 -11.681 22.288 1.00 56.02 O ANISOU 2267 OE1 GLN A 294 7120 6758 7409 265 744 -639 O ATOM 2268 NE2 GLN A 294 34.462 -9.518 21.815 1.00 54.65 N ANISOU 2268 NE2 GLN A 294 6936 6591 7236 176 749 -688 N ATOM 2269 N SER A 295 33.024 -13.851 16.757 1.00 47.36 N ANISOU 2269 N SER A 295 6387 5347 6260 118 926 -583 N ATOM 2270 CA SER A 295 33.349 -14.450 15.460 1.00 47.03 C ANISOU 2270 CA SER A 295 6407 5239 6224 101 985 -589 C ATOM 2271 C SER A 295 32.861 -13.621 14.274 1.00 46.68 C ANISOU 2271 C SER A 295 6421 5155 6160 39 1008 -606 C ATOM 2272 O SER A 295 31.662 -13.519 14.025 1.00 45.61 O ANISOU 2272 O SER A 295 6340 5006 5985 6 982 -586 O ATOM 2273 CB SER A 295 32.846 -15.880 15.356 1.00 47.15 C ANISOU 2273 CB SER A 295 6481 5215 6220 119 990 -551 C ATOM 2274 OG SER A 295 32.866 -16.302 14.006 1.00 46.41 O ANISOU 2274 OG SER A 295 6462 5054 6120 88 1042 -558 O ATOM 2275 N ARG A 296 33.814 -13.060 13.530 1.00 46.76 N ANISOU 2275 N ARG A 296 6422 5147 6198 24 1059 -643 N ATOM 2276 CA ARG A 296 33.517 -12.273 12.344 1.00 46.92 C ANISOU 2276 CA ARG A 296 6503 5126 6200 -30 1090 -659 C ATOM 2277 C ARG A 296 32.858 -13.138 11.292 1.00 45.87 C ANISOU 2277 C ARG A 296 6468 4929 6031 -51 1110 -639 C ATOM 2278 O ARG A 296 31.960 -12.672 10.591 1.00 45.92 O ANISOU 2278 O ARG A 296 6537 4911 5998 -92 1101 -634 O ATOM 2279 CB ARG A 296 34.801 -11.671 11.773 1.00 47.96 C ANISOU 2279 CB ARG A 296 6605 5244 6372 -37 1152 -704 C ATOM 2280 CG ARG A 296 34.632 -10.299 11.158 1.00 51.90 C ANISOU 2280 CG ARG A 296 7127 5733 6861 -85 1168 -728 C ATOM 2281 CD ARG A 296 35.758 -9.378 11.633 1.00 56.71 C ANISOU 2281 CD ARG A 296 7648 6379 7520 -81 1190 -772 C ATOM 2282 NE ARG A 296 36.090 -9.692 13.026 1.00 61.19 N ANISOU 2282 NE ARG A 296 8124 7013 8112 -34 1143 -769 N ATOM 2283 CZ ARG A 296 37.300 -9.582 13.579 1.00 63.75 C ANISOU 2283 CZ ARG A 296 8359 7374 8488 -7 1159 -803 C ATOM 2284 NH1 ARG A 296 38.338 -9.140 12.871 1.00 64.65 N ANISOU 2284 NH1 ARG A 296 8457 7465 8641 -25 1225 -846 N ATOM 2285 NH2 ARG A 296 37.466 -9.911 14.857 1.00 64.01 N ANISOU 2285 NH2 ARG A 296 8318 7469 8534 40 1107 -795 N ATOM 2286 N ASP A 297 33.320 -14.387 11.177 1.00 45.14 N ANISOU 2286 N ASP A 297 6388 4810 5952 -22 1137 -628 N ATOM 2287 CA ASP A 297 32.800 -15.334 10.186 1.00 44.03 C ANISOU 2287 CA ASP A 297 6340 4607 5781 -41 1162 -612 C ATOM 2288 C ASP A 297 31.330 -15.620 10.444 1.00 42.03 C ANISOU 2288 C ASP A 297 6127 4358 5483 -59 1106 -580 C ATOM 2289 O ASP A 297 30.520 -15.575 9.523 1.00 40.64 O ANISOU 2289 O ASP A 297 6027 4146 5269 -100 1107 -577 O ATOM 2290 CB ASP A 297 33.603 -16.635 10.204 1.00 44.92 C ANISOU 2290 CB ASP A 297 6450 4694 5921 1 1201 -606 C ATOM 2291 CG ASP A 297 34.960 -16.512 9.495 1.00 48.23 C ANISOU 2291 CG ASP A 297 6856 5087 6381 8 1273 -641 C ATOM 2292 OD1 ASP A 297 35.824 -17.416 9.695 1.00 50.06 O ANISOU 2292 OD1 ASP A 297 7062 5311 6647 52 1304 -640 O ATOM 2293 OD2 ASP A 297 35.149 -15.530 8.734 1.00 48.49 O ANISOU 2293 OD2 ASP A 297 6905 5106 6412 -30 1300 -668 O ATOM 2294 N LEU A 298 30.998 -15.900 11.709 1.00 41.05 N ANISOU 2294 N LEU A 298 5953 4281 5364 -27 1058 -557 N ATOM 2295 CA LEU A 298 29.594 -16.009 12.147 1.00 39.95 C ANISOU 2295 CA LEU A 298 5836 4155 5187 -45 1003 -529 C ATOM 2296 C LEU A 298 28.791 -14.775 11.744 1.00 38.88 C ANISOU 2296 C LEU A 298 5718 4030 5024 -89 975 -539 C ATOM 2297 O LEU A 298 27.715 -14.900 11.166 1.00 37.27 O ANISOU 2297 O LEU A 298 5574 3803 4782 -124 957 -528 O ATOM 2298 CB LEU A 298 29.501 -16.188 13.663 1.00 40.02 C ANISOU 2298 CB LEU A 298 5778 4221 5208 -3 959 -508 C ATOM 2299 CG LEU A 298 28.390 -17.023 14.312 1.00 40.90 C ANISOU 2299 CG LEU A 298 5912 4335 5295 1 923 -472 C ATOM 2300 CD1 LEU A 298 28.103 -16.468 15.665 1.00 40.28 C ANISOU 2300 CD1 LEU A 298 5768 4321 5218 24 872 -461 C ATOM 2301 CD2 LEU A 298 27.109 -17.176 13.499 1.00 41.11 C ANISOU 2301 CD2 LEU A 298 6011 4326 5282 -51 912 -465 C ATOM 2302 N GLU A 299 29.317 -13.583 12.039 1.00 39.41 N ANISOU 2302 N GLU A 299 5733 4133 5110 -88 972 -561 N ATOM 2303 CA GLU A 299 28.619 -12.330 11.646 1.00 39.83 C ANISOU 2303 CA GLU A 299 5804 4192 5137 -126 951 -570 C ATOM 2304 C GLU A 299 28.224 -12.307 10.187 1.00 39.43 C ANISOU 2304 C GLU A 299 5844 4085 5054 -166 978 -576 C ATOM 2305 O GLU A 299 27.078 -11.992 9.853 1.00 39.00 O ANISOU 2305 O GLU A 299 5831 4027 4960 -193 943 -565 O ATOM 2306 CB GLU A 299 29.441 -11.093 11.973 1.00 40.66 C ANISOU 2306 CB GLU A 299 5850 4329 5271 -123 963 -599 C ATOM 2307 CG GLU A 299 29.444 -10.755 13.444 1.00 43.10 C ANISOU 2307 CG GLU A 299 6075 4704 5597 -95 917 -593 C ATOM 2308 CD GLU A 299 29.774 -9.300 13.691 1.00 47.59 C ANISOU 2308 CD GLU A 299 6600 5302 6179 -108 916 -621 C ATOM 2309 OE1 GLU A 299 30.613 -8.758 12.939 1.00 48.38 O ANISOU 2309 OE1 GLU A 299 6707 5378 6299 -123 967 -651 O ATOM 2310 OE2 GLU A 299 29.188 -8.707 14.640 1.00 50.36 O ANISOU 2310 OE2 GLU A 299 6912 5700 6523 -104 869 -613 O ATOM 2311 N LYS A 300 29.158 -12.689 9.317 1.00 39.58 N ANISOU 2311 N LYS A 300 5893 4059 5086 -166 1039 -594 N ATOM 2312 CA LYS A 300 28.938 -12.572 7.880 1.00 39.01 C ANISOU 2312 CA LYS A 300 5909 3931 4980 -203 1071 -604 C ATOM 2313 C LYS A 300 27.940 -13.589 7.381 1.00 37.03 C ANISOU 2313 C LYS A 300 5728 3651 4692 -219 1052 -584 C ATOM 2314 O LYS A 300 27.104 -13.294 6.550 1.00 36.57 O ANISOU 2314 O LYS A 300 5734 3571 4590 -251 1037 -583 O ATOM 2315 CB LYS A 300 30.265 -12.662 7.103 1.00 40.95 C ANISOU 2315 CB LYS A 300 6168 4137 5254 -200 1148 -631 C ATOM 2316 CG LYS A 300 31.436 -11.917 7.771 1.00 45.22 C ANISOU 2316 CG LYS A 300 6623 4712 5847 -178 1172 -655 C ATOM 2317 CD LYS A 300 32.378 -11.305 6.717 1.00 50.99 C ANISOU 2317 CD LYS A 300 7383 5400 6590 -198 1245 -689 C ATOM 2318 CE LYS A 300 33.866 -11.381 7.127 1.00 53.98 C ANISOU 2318 CE LYS A 300 7684 5793 7033 -170 1293 -716 C ATOM 2319 NZ LYS A 300 34.755 -10.591 6.189 1.00 53.16 N ANISOU 2319 NZ LYS A 300 7601 5652 6946 -195 1367 -753 N ATOM 2320 N VAL A 301 28.021 -14.807 7.883 1.00 36.75 N ANISOU 2320 N VAL A 301 5680 3612 4671 -196 1053 -568 N ATOM 2321 CA VAL A 301 27.035 -15.821 7.515 1.00 35.91 C ANISOU 2321 CA VAL A 301 5635 3478 4532 -215 1036 -552 C ATOM 2322 C VAL A 301 25.632 -15.441 8.034 1.00 34.85 C ANISOU 2322 C VAL A 301 5492 3381 4369 -232 965 -535 C ATOM 2323 O VAL A 301 24.634 -15.595 7.321 1.00 34.69 O ANISOU 2323 O VAL A 301 5531 3341 4309 -266 944 -533 O ATOM 2324 CB VAL A 301 27.446 -17.220 8.019 1.00 35.59 C ANISOU 2324 CB VAL A 301 5584 3424 4516 -184 1057 -537 C ATOM 2325 CG1 VAL A 301 26.265 -18.144 8.011 1.00 36.60 C ANISOU 2325 CG1 VAL A 301 5755 3536 4614 -204 1029 -518 C ATOM 2326 CG2 VAL A 301 28.564 -17.785 7.156 1.00 37.28 C ANISOU 2326 CG2 VAL A 301 5832 3585 4747 -176 1130 -554 C ATOM 2327 N SER A 302 25.559 -14.960 9.273 1.00 33.93 N ANISOU 2327 N SER A 302 5299 3319 4273 -209 929 -524 N ATOM 2328 CA SER A 302 24.265 -14.509 9.844 1.00 33.71 C ANISOU 2328 CA SER A 302 5257 3330 4223 -223 865 -509 C ATOM 2329 C SER A 302 23.677 -13.420 8.951 1.00 34.06 C ANISOU 2329 C SER A 302 5341 3369 4234 -256 849 -521 C ATOM 2330 O SER A 302 22.504 -13.473 8.611 1.00 33.40 O ANISOU 2330 O SER A 302 5292 3284 4116 -282 811 -515 O ATOM 2331 CB SER A 302 24.423 -13.979 11.269 1.00 32.90 C ANISOU 2331 CB SER A 302 5068 3286 4147 -192 836 -499 C ATOM 2332 OG SER A 302 24.987 -14.939 12.133 1.00 32.06 O ANISOU 2332 OG SER A 302 4926 3187 4068 -155 848 -486 O ATOM 2333 N GLN A 303 24.531 -12.462 8.567 1.00 35.58 N ANISOU 2333 N GLN A 303 5528 3556 4436 -254 880 -541 N ATOM 2334 CA GLN A 303 24.204 -11.395 7.614 1.00 37.69 C ANISOU 2334 CA GLN A 303 5842 3808 4671 -279 878 -553 C ATOM 2335 C GLN A 303 23.676 -11.864 6.250 1.00 37.41 C ANISOU 2335 C GLN A 303 5901 3724 4591 -309 887 -557 C ATOM 2336 O GLN A 303 22.637 -11.379 5.808 1.00 36.89 O ANISOU 2336 O GLN A 303 5870 3662 4485 -329 846 -553 O ATOM 2337 CB GLN A 303 25.380 -10.407 7.474 1.00 37.98 C ANISOU 2337 CB GLN A 303 5857 3841 4732 -272 925 -575 C ATOM 2338 CG GLN A 303 25.438 -9.426 8.694 1.00 41.71 C ANISOU 2338 CG GLN A 303 6246 4371 5231 -255 895 -575 C ATOM 2339 CD GLN A 303 26.432 -8.275 8.554 1.00 41.67 C ANISOU 2339 CD GLN A 303 6220 4365 5249 -255 937 -601 C ATOM 2340 OE1 GLN A 303 26.041 -7.118 8.296 1.00 46.98 O ANISOU 2340 OE1 GLN A 303 6909 5039 5901 -269 928 -606 O ATOM 2341 NE2 GLN A 303 27.723 -8.578 8.739 1.00 48.04 N ANISOU 2341 NE2 GLN A 303 6988 5166 6098 -238 985 -619 N ATOM 2342 N GLN A 304 24.382 -12.803 5.602 1.00 37.72 N ANISOU 2342 N GLN A 304 5979 3717 4634 -310 938 -565 N ATOM 2343 CA GLN A 304 23.903 -13.494 4.384 1.00 38.59 C ANISOU 2343 CA GLN A 304 6180 3779 4703 -338 947 -571 C ATOM 2344 C GLN A 304 22.515 -14.158 4.487 1.00 37.88 C ANISOU 2344 C GLN A 304 6108 3702 4584 -357 890 -558 C ATOM 2345 O GLN A 304 21.671 -14.050 3.591 1.00 38.41 O ANISOU 2345 O GLN A 304 6236 3754 4604 -385 864 -563 O ATOM 2346 CB GLN A 304 24.897 -14.616 4.007 1.00 38.96 C ANISOU 2346 CB GLN A 304 6252 3781 4771 -330 1011 -579 C ATOM 2347 CG GLN A 304 26.240 -14.155 3.485 1.00 42.19 C ANISOU 2347 CG GLN A 304 6667 4162 5202 -321 1080 -599 C ATOM 2348 CD GLN A 304 27.239 -15.297 3.324 1.00 42.48 C ANISOU 2348 CD GLN A 304 6711 4160 5269 -305 1142 -605 C ATOM 2349 OE1 GLN A 304 26.866 -16.460 3.096 1.00 45.82 O ANISOU 2349 OE1 GLN A 304 7172 4557 5679 -313 1143 -598 O ATOM 2350 NE2 GLN A 304 28.521 -14.963 3.455 1.00 47.92 N ANISOU 2350 NE2 GLN A 304 7360 4847 6001 -284 1194 -620 N ATOM 2351 N LEU A 305 22.318 -14.911 5.557 1.00 36.72 N ANISOU 2351 N LEU A 305 5908 3578 4465 -343 872 -542 N ATOM 2352 CA LEU A 305 21.037 -15.523 5.898 1.00 37.15 C ANISOU 2352 CA LEU A 305 5962 3649 4503 -360 822 -530 C ATOM 2353 C LEU A 305 19.867 -14.539 6.094 1.00 36.08 C ANISOU 2353 C LEU A 305 5808 3556 4343 -373 756 -525 C ATOM 2354 O LEU A 305 18.745 -14.754 5.626 1.00 35.70 O ANISOU 2354 O LEU A 305 5794 3509 4263 -401 717 -528 O ATOM 2355 CB LEU A 305 21.245 -16.144 7.260 1.00 37.22 C ANISOU 2355 CB LEU A 305 5904 3684 4553 -332 820 -511 C ATOM 2356 CG LEU A 305 20.798 -17.517 7.532 1.00 41.04 C ANISOU 2356 CG LEU A 305 6402 4150 5041 -339 823 -501 C ATOM 2357 CD1 LEU A 305 19.398 -17.689 6.933 1.00 44.11 C ANISOU 2357 CD1 LEU A 305 6833 4535 5390 -383 780 -508 C ATOM 2358 CD2 LEU A 305 21.909 -18.363 6.894 1.00 42.11 C ANISOU 2358 CD2 LEU A 305 6580 4232 5188 -330 890 -510 C ATOM 2359 N ALA A 306 20.152 -13.481 6.849 1.00 35.56 N ANISOU 2359 N ALA A 306 5684 3529 4298 -350 744 -520 N ATOM 2360 CA ALA A 306 19.157 -12.505 7.287 1.00 35.64 C ANISOU 2360 CA ALA A 306 5663 3583 4295 -353 687 -513 C ATOM 2361 C ALA A 306 18.744 -11.564 6.163 1.00 36.82 C ANISOU 2361 C ALA A 306 5868 3721 4401 -370 672 -524 C ATOM 2362 O ALA A 306 17.661 -10.968 6.226 1.00 35.86 O ANISOU 2362 O ALA A 306 5739 3627 4257 -377 619 -519 O ATOM 2363 CB ALA A 306 19.728 -11.724 8.463 1.00 34.21 C ANISOU 2363 CB ALA A 306 5405 3443 4150 -323 687 -505 C ATOM 2364 N LYS A 307 19.601 -11.481 5.125 1.00 38.93 N ANISOU 2364 N LYS A 307 6194 3943 4655 -374 722 -538 N ATOM 2365 CA LYS A 307 19.524 -10.482 4.030 1.00 40.33 C ANISOU 2365 CA LYS A 307 6432 4100 4790 -382 724 -548 C ATOM 2366 C LYS A 307 18.118 -10.224 3.510 1.00 41.10 C ANISOU 2366 C LYS A 307 6564 4212 4840 -399 660 -546 C ATOM 2367 O LYS A 307 17.658 -9.072 3.503 1.00 41.32 O ANISOU 2367 O LYS A 307 6588 4262 4851 -390 630 -542 O ATOM 2368 CB LYS A 307 20.457 -10.885 2.881 1.00 41.75 C ANISOU 2368 CB LYS A 307 6685 4222 4957 -391 787 -565 C ATOM 2369 CG LYS A 307 20.611 -9.931 1.656 1.00 42.53 C ANISOU 2369 CG LYS A 307 6861 4288 5011 -398 807 -575 C ATOM 2370 CD LYS A 307 21.031 -10.834 0.454 1.00 47.64 C ANISOU 2370 CD LYS A 307 7593 4877 5630 -417 852 -590 C ATOM 2371 CE LYS A 307 21.875 -10.149 -0.653 1.00 49.67 C ANISOU 2371 CE LYS A 307 7923 5086 5863 -418 913 -604 C ATOM 2372 NZ LYS A 307 22.521 -11.196 -1.531 1.00 46.87 N ANISOU 2372 NZ LYS A 307 7632 4677 5499 -433 970 -619 N ATOM 2373 N THR A 308 17.426 -11.284 3.114 1.00 41.31 N ANISOU 2373 N THR A 308 6622 4229 4847 -421 639 -550 N ATOM 2374 CA THR A 308 16.093 -11.155 2.513 1.00 41.79 C ANISOU 2374 CA THR A 308 6715 4304 4861 -438 576 -554 C ATOM 2375 C THR A 308 15.010 -10.745 3.537 1.00 40.75 C ANISOU 2375 C THR A 308 6511 4229 4744 -432 513 -541 C ATOM 2376 O THR A 308 14.099 -9.923 3.231 1.00 40.55 O ANISOU 2376 O THR A 308 6494 4228 4687 -430 462 -540 O ATOM 2377 CB THR A 308 15.697 -12.455 1.743 1.00 43.53 C ANISOU 2377 CB THR A 308 6990 4494 5055 -470 575 -569 C ATOM 2378 OG1 THR A 308 14.467 -12.247 1.017 1.00 45.94 O ANISOU 2378 OG1 THR A 308 7331 4814 5311 -487 512 -578 O ATOM 2379 CG2 THR A 308 15.568 -13.693 2.702 1.00 44.62 C ANISOU 2379 CG2 THR A 308 7077 4640 5236 -478 579 -563 C ATOM 2380 N TYR A 309 15.115 -11.310 4.747 1.00 37.64 N ANISOU 2380 N TYR A 309 6048 3857 4397 -426 518 -530 N ATOM 2381 CA TYR A 309 14.211 -10.979 5.808 1.00 35.50 C ANISOU 2381 CA TYR A 309 5706 3637 4144 -420 469 -518 C ATOM 2382 C TYR A 309 14.416 -9.511 6.227 1.00 33.38 C ANISOU 2382 C TYR A 309 5406 3395 3882 -393 462 -509 C ATOM 2383 O TYR A 309 13.451 -8.842 6.584 1.00 32.06 O ANISOU 2383 O TYR A 309 5208 3265 3709 -388 412 -503 O ATOM 2384 CB TYR A 309 14.446 -11.889 7.005 1.00 35.78 C ANISOU 2384 CB TYR A 309 5684 3684 4226 -415 486 -507 C ATOM 2385 CG TYR A 309 14.072 -13.331 6.807 1.00 36.47 C ANISOU 2385 CG TYR A 309 5796 3749 4313 -442 492 -513 C ATOM 2386 CD1 TYR A 309 15.009 -14.329 6.988 1.00 37.50 C ANISOU 2386 CD1 TYR A 309 5935 3847 4467 -437 546 -511 C ATOM 2387 CD2 TYR A 309 12.781 -13.693 6.466 1.00 34.43 C ANISOU 2387 CD2 TYR A 309 5548 3502 4031 -471 444 -523 C ATOM 2388 CE1 TYR A 309 14.666 -15.671 6.828 1.00 39.97 C ANISOU 2388 CE1 TYR A 309 6273 4134 4780 -462 556 -517 C ATOM 2389 CE2 TYR A 309 12.427 -15.012 6.308 1.00 38.12 C ANISOU 2389 CE2 TYR A 309 6036 3946 4500 -501 453 -532 C ATOM 2390 CZ TYR A 309 13.376 -15.992 6.493 1.00 38.20 C ANISOU 2390 CZ TYR A 309 6061 3920 4534 -496 511 -528 C ATOM 2391 OH TYR A 309 13.027 -17.318 6.331 1.00 46.03 O ANISOU 2391 OH TYR A 309 7078 4883 5526 -526 525 -537 O ATOM 2392 N TYR A 310 15.667 -9.035 6.158 1.00 32.03 N ANISOU 2392 N TYR A 310 5243 3203 3725 -377 515 -511 N ATOM 2393 CA TYR A 310 16.032 -7.660 6.557 1.00 30.95 C ANISOU 2393 CA TYR A 310 5078 3083 3597 -355 520 -507 C ATOM 2394 C TYR A 310 15.292 -6.634 5.710 1.00 31.06 C ANISOU 2394 C TYR A 310 5139 3097 3566 -354 487 -508 C ATOM 2395 O TYR A 310 14.708 -5.715 6.247 1.00 29.53 O ANISOU 2395 O TYR A 310 4910 2937 3375 -341 454 -500 O ATOM 2396 CB TYR A 310 17.544 -7.419 6.536 1.00 29.78 C ANISOU 2396 CB TYR A 310 4931 2908 3474 -344 587 -516 C ATOM 2397 CG TYR A 310 17.962 -5.976 6.849 1.00 31.42 C ANISOU 2397 CG TYR A 310 5117 3130 3692 -328 599 -517 C ATOM 2398 CD1 TYR A 310 18.365 -5.587 8.149 1.00 28.30 C ANISOU 2398 CD1 TYR A 310 4641 2771 3340 -311 602 -514 C ATOM 2399 CD2 TYR A 310 17.946 -4.989 5.851 1.00 30.39 C ANISOU 2399 CD2 TYR A 310 5049 2974 3525 -328 609 -523 C ATOM 2400 CE1 TYR A 310 18.769 -4.272 8.417 1.00 26.39 C ANISOU 2400 CE1 TYR A 310 4381 2539 3108 -300 617 -520 C ATOM 2401 CE2 TYR A 310 18.335 -3.674 6.134 1.00 30.47 C ANISOU 2401 CE2 TYR A 310 5042 2991 3546 -316 627 -525 C ATOM 2402 CZ TYR A 310 18.718 -3.323 7.421 1.00 28.28 C ANISOU 2402 CZ TYR A 310 4682 2749 3314 -303 630 -525 C ATOM 2403 OH TYR A 310 19.111 -2.020 7.654 1.00 31.02 O ANISOU 2403 OH TYR A 310 5016 3099 3670 -295 651 -532 O ATOM 2404 N ASP A 311 15.299 -6.808 4.384 1.00 32.65 N ANISOU 2404 N ASP A 311 5422 3259 3723 -367 496 -518 N ATOM 2405 CA ASP A 311 14.609 -5.862 3.508 1.00 33.25 C ANISOU 2405 CA ASP A 311 5552 3334 3749 -361 464 -517 C ATOM 2406 C ASP A 311 13.097 -5.838 3.781 1.00 31.90 C ANISOU 2406 C ASP A 311 5351 3207 3564 -361 386 -511 C ATOM 2407 O ASP A 311 12.463 -4.802 3.660 1.00 32.16 O ANISOU 2407 O ASP A 311 5388 3258 3574 -344 351 -504 O ATOM 2408 CB ASP A 311 14.910 -6.135 2.014 1.00 36.04 C ANISOU 2408 CB ASP A 311 6006 3636 4052 -373 488 -530 C ATOM 2409 CG ASP A 311 16.427 -6.288 1.705 1.00 40.76 C ANISOU 2409 CG ASP A 311 6633 4186 4668 -375 573 -539 C ATOM 2410 OD1 ASP A 311 16.765 -7.119 0.817 1.00 47.39 O ANISOU 2410 OD1 ASP A 311 7533 4986 5486 -392 600 -551 O ATOM 2411 OD2 ASP A 311 17.286 -5.581 2.312 1.00 45.85 O ANISOU 2411 OD2 ASP A 311 7240 4832 5349 -361 613 -537 O ATOM 2412 N ALA A 312 12.503 -6.969 4.140 1.00 30.85 N ANISOU 2412 N ALA A 312 5187 3090 3444 -381 360 -514 N ATOM 2413 CA ALA A 312 11.067 -6.985 4.446 1.00 29.56 C ANISOU 2413 CA ALA A 312 4987 2971 3274 -385 289 -512 C ATOM 2414 C ALA A 312 10.743 -6.471 5.872 1.00 28.47 C ANISOU 2414 C ALA A 312 4759 2878 3179 -369 272 -498 C ATOM 2415 O ALA A 312 9.780 -5.750 6.077 1.00 29.14 O ANISOU 2415 O ALA A 312 4818 2997 3256 -357 224 -492 O ATOM 2416 CB ALA A 312 10.499 -8.400 4.253 1.00 30.69 C ANISOU 2416 CB ALA A 312 5134 3111 3416 -419 271 -525 C ATOM 2417 N LYS A 313 11.548 -6.858 6.854 1.00 26.72 N ANISOU 2417 N LYS A 313 4492 2658 3004 -367 313 -492 N ATOM 2418 CA LYS A 313 11.185 -6.666 8.266 1.00 25.63 C ANISOU 2418 CA LYS A 313 4270 2562 2905 -356 296 -480 C ATOM 2419 C LYS A 313 11.889 -5.496 8.942 1.00 25.00 C ANISOU 2419 C LYS A 313 4160 2493 2846 -330 320 -472 C ATOM 2420 O LYS A 313 11.446 -5.041 9.992 1.00 24.12 O ANISOU 2420 O LYS A 313 3987 2419 2757 -318 300 -463 O ATOM 2421 CB LYS A 313 11.436 -7.948 9.069 1.00 24.36 C ANISOU 2421 CB LYS A 313 4074 2402 2780 -369 317 -477 C ATOM 2422 CG LYS A 313 10.601 -9.162 8.593 1.00 24.22 C ANISOU 2422 CG LYS A 313 4077 2376 2749 -401 295 -487 C ATOM 2423 CD LYS A 313 10.833 -10.364 9.520 1.00 24.65 C ANISOU 2423 CD LYS A 313 4097 2428 2840 -410 321 -481 C ATOM 2424 CE LYS A 313 10.220 -11.641 8.943 1.00 23.38 C ANISOU 2424 CE LYS A 313 3968 2247 2667 -445 313 -494 C ATOM 2425 NZ LYS A 313 8.745 -11.616 9.072 1.00 23.55 N ANISOU 2425 NZ LYS A 313 3960 2304 2684 -464 257 -501 N ATOM 2426 N VAL A 314 13.000 -5.036 8.367 1.00 24.92 N ANISOU 2426 N VAL A 314 4190 2449 2828 -323 367 -478 N ATOM 2427 CA VAL A 314 13.842 -4.056 9.074 1.00 24.53 C ANISOU 2427 CA VAL A 314 4107 2407 2805 -303 399 -476 C ATOM 2428 C VAL A 314 14.077 -2.781 8.277 1.00 25.59 C ANISOU 2428 C VAL A 314 4291 2520 2912 -292 413 -480 C ATOM 2429 O VAL A 314 14.008 -1.691 8.821 1.00 24.76 O ANISOU 2429 O VAL A 314 4158 2434 2817 -276 410 -476 O ATOM 2430 CB VAL A 314 15.200 -4.667 9.564 1.00 24.46 C ANISOU 2430 CB VAL A 314 4076 2385 2834 -302 454 -482 C ATOM 2431 CG1 VAL A 314 15.962 -3.646 10.418 1.00 22.55 C ANISOU 2431 CG1 VAL A 314 3786 2160 2621 -285 479 -485 C ATOM 2432 CG2 VAL A 314 14.959 -5.916 10.391 1.00 21.93 C ANISOU 2432 CG2 VAL A 314 3713 2083 2538 -308 442 -475 C ATOM 2433 N GLN A 315 14.299 -2.922 6.973 1.00 26.55 N ANISOU 2433 N GLN A 315 4491 2600 2996 -301 430 -487 N ATOM 2434 CA GLN A 315 14.703 -1.777 6.152 1.00 26.90 C ANISOU 2434 CA GLN A 315 4595 2613 3013 -290 457 -490 C ATOM 2435 C GLN A 315 13.779 -0.540 6.223 1.00 26.45 C ANISOU 2435 C GLN A 315 4537 2578 2935 -269 417 -479 C ATOM 2436 O GLN A 315 14.278 0.588 6.189 1.00 26.29 O ANISOU 2436 O GLN A 315 4532 2542 2915 -256 450 -480 O ATOM 2437 CB GLN A 315 14.968 -2.224 4.699 1.00 28.11 C ANISOU 2437 CB GLN A 315 4840 2718 3122 -302 478 -498 C ATOM 2438 CG GLN A 315 15.457 -1.136 3.754 1.00 28.90 C ANISOU 2438 CG GLN A 315 5015 2777 3189 -292 516 -501 C ATOM 2439 CD GLN A 315 14.355 -0.195 3.335 1.00 35.02 C ANISOU 2439 CD GLN A 315 5822 3564 3919 -272 466 -488 C ATOM 2440 OE1 GLN A 315 13.180 -0.579 3.301 1.00 37.26 O ANISOU 2440 OE1 GLN A 315 6095 3879 4184 -270 399 -482 O ATOM 2441 NE2 GLN A 315 14.723 1.077 3.020 1.00 35.68 N ANISOU 2441 NE2 GLN A 315 5946 3624 3989 -255 499 -485 N ATOM 2442 N PRO A 316 12.449 -0.734 6.288 1.00 26.53 N ANISOU 2442 N PRO A 316 4531 2621 2928 -265 350 -470 N ATOM 2443 CA PRO A 316 11.555 0.423 6.445 1.00 26.13 C ANISOU 2443 CA PRO A 316 4473 2594 2863 -241 312 -459 C ATOM 2444 C PRO A 316 11.670 1.158 7.788 1.00 25.29 C ANISOU 2444 C PRO A 316 4290 2518 2800 -228 320 -454 C ATOM 2445 O PRO A 316 11.019 2.183 7.963 1.00 25.72 O ANISOU 2445 O PRO A 316 4338 2588 2845 -206 296 -445 O ATOM 2446 CB PRO A 316 10.154 -0.191 6.363 1.00 26.21 C ANISOU 2446 CB PRO A 316 4463 2638 2856 -244 239 -456 C ATOM 2447 CG PRO A 316 10.348 -1.543 5.689 1.00 26.59 C ANISOU 2447 CG PRO A 316 4545 2665 2891 -272 244 -467 C ATOM 2448 CD PRO A 316 11.678 -2.000 6.200 1.00 27.44 C ANISOU 2448 CD PRO A 316 4634 2752 3038 -284 309 -473 C ATOM 2449 N THR A 317 12.459 0.633 8.726 1.00 24.56 N ANISOU 2449 N THR A 317 4144 2436 2754 -240 351 -460 N ATOM 2450 CA THR A 317 12.661 1.276 10.050 1.00 22.43 C ANISOU 2450 CA THR A 317 3803 2196 2524 -230 360 -459 C ATOM 2451 C THR A 317 13.911 2.138 10.049 1.00 23.29 C ANISOU 2451 C THR A 317 3925 2278 2646 -227 422 -471 C ATOM 2452 O THR A 317 14.340 2.607 11.100 1.00 23.21 O ANISOU 2452 O THR A 317 3859 2289 2670 -223 439 -476 O ATOM 2453 CB THR A 317 12.808 0.230 11.179 1.00 22.40 C ANISOU 2453 CB THR A 317 3728 2223 2560 -241 356 -459 C ATOM 2454 OG1 THR A 317 14.098 -0.398 11.104 1.00 20.20 O ANISOU 2454 OG1 THR A 317 3456 1920 2299 -251 407 -471 O ATOM 2455 CG2 THR A 317 11.716 -0.848 11.109 1.00 18.83 C ANISOU 2455 CG2 THR A 317 3267 1789 2098 -252 307 -452 C ATOM 2456 N THR A 318 14.534 2.339 8.881 1.00 23.29 N ANISOU 2456 N THR A 318 4000 2230 2620 -232 460 -478 N ATOM 2457 CA THR A 318 15.869 2.924 8.894 1.00 23.55 C ANISOU 2457 CA THR A 318 4040 2235 2674 -237 529 -495 C ATOM 2458 C THR A 318 15.967 4.360 8.374 1.00 24.79 C ANISOU 2458 C THR A 318 4248 2362 2810 -225 557 -496 C ATOM 2459 O THR A 318 17.015 5.002 8.485 1.00 24.44 O ANISOU 2459 O THR A 318 4203 2295 2787 -232 617 -513 O ATOM 2460 CB THR A 318 16.874 2.018 8.100 1.00 23.62 C ANISOU 2460 CB THR A 318 4088 2204 2681 -255 574 -507 C ATOM 2461 OG1 THR A 318 16.441 1.921 6.750 1.00 21.44 O ANISOU 2461 OG1 THR A 318 3899 1893 2352 -256 566 -501 O ATOM 2462 CG2 THR A 318 16.991 0.617 8.731 1.00 21.34 C ANISOU 2462 CG2 THR A 318 3747 1940 2420 -264 559 -508 C ATOM 2463 N LEU A 319 14.873 4.855 7.802 1.00 25.86 N ANISOU 2463 N LEU A 319 4426 2495 2902 -207 516 -479 N ATOM 2464 CA LEU A 319 14.882 6.142 7.103 1.00 26.06 C ANISOU 2464 CA LEU A 319 4520 2485 2897 -191 542 -475 C ATOM 2465 C LEU A 319 15.459 7.257 7.993 1.00 25.04 C ANISOU 2465 C LEU A 319 4351 2358 2805 -189 584 -486 C ATOM 2466 O LEU A 319 16.503 7.860 7.685 1.00 23.93 O ANISOU 2466 O LEU A 319 4242 2177 2672 -200 653 -503 O ATOM 2467 CB LEU A 319 13.457 6.512 6.668 1.00 26.56 C ANISOU 2467 CB LEU A 319 4613 2561 2915 -163 477 -453 C ATOM 2468 CG LEU A 319 13.136 7.447 5.478 1.00 30.87 C ANISOU 2468 CG LEU A 319 5260 3067 3404 -139 483 -441 C ATOM 2469 CD1 LEU A 319 11.856 8.263 5.751 1.00 28.44 C ANISOU 2469 CD1 LEU A 319 4940 2788 3080 -103 426 -421 C ATOM 2470 CD2 LEU A 319 14.292 8.304 4.960 1.00 32.52 C ANISOU 2470 CD2 LEU A 319 5531 3217 3609 -144 569 -451 C ATOM 2471 N VAL A 320 14.762 7.549 9.085 1.00 23.89 N ANISOU 2471 N VAL A 320 4137 2258 2680 -178 544 -480 N ATOM 2472 CA VAL A 320 15.194 8.653 9.948 1.00 23.33 C ANISOU 2472 CA VAL A 320 4030 2192 2641 -176 579 -492 C ATOM 2473 C VAL A 320 16.565 8.426 10.600 1.00 23.92 C ANISOU 2473 C VAL A 320 4057 2269 2765 -202 633 -521 C ATOM 2474 O VAL A 320 17.420 9.291 10.530 1.00 24.87 O ANISOU 2474 O VAL A 320 4193 2358 2897 -211 693 -540 O ATOM 2475 CB VAL A 320 14.054 9.140 10.910 1.00 23.05 C ANISOU 2475 CB VAL A 320 3943 2203 2614 -155 526 -478 C ATOM 2476 CG1 VAL A 320 14.526 10.286 11.776 1.00 19.81 C ANISOU 2476 CG1 VAL A 320 3500 1794 2233 -155 565 -493 C ATOM 2477 CG2 VAL A 320 12.841 9.612 10.068 1.00 21.44 C ANISOU 2477 CG2 VAL A 320 3798 1989 2360 -124 484 -453 C ATOM 2478 N PRO A 321 16.795 7.273 11.263 1.00 24.12 N ANISOU 2478 N PRO A 321 4019 2328 2817 -213 612 -525 N ATOM 2479 CA PRO A 321 18.169 7.095 11.779 1.00 23.69 C ANISOU 2479 CA PRO A 321 3922 2274 2806 -233 664 -554 C ATOM 2480 C PRO A 321 19.352 7.260 10.771 1.00 24.39 C ANISOU 2480 C PRO A 321 4067 2308 2894 -250 736 -574 C ATOM 2481 O PRO A 321 20.412 7.765 11.171 1.00 23.43 O ANISOU 2481 O PRO A 321 3915 2179 2806 -264 789 -603 O ATOM 2482 CB PRO A 321 18.140 5.680 12.372 1.00 23.29 C ANISOU 2482 CB PRO A 321 3816 2260 2773 -235 629 -549 C ATOM 2483 CG PRO A 321 16.698 5.442 12.728 1.00 22.33 C ANISOU 2483 CG PRO A 321 3679 2173 2633 -220 559 -522 C ATOM 2484 CD PRO A 321 15.909 6.159 11.657 1.00 24.97 C ANISOU 2484 CD PRO A 321 4089 2476 2922 -208 549 -507 C ATOM 2485 N LYS A 322 19.181 6.845 9.508 1.00 24.01 N ANISOU 2485 N LYS A 322 4097 2220 2807 -250 741 -562 N ATOM 2486 CA LYS A 322 20.243 6.959 8.497 1.00 25.54 C ANISOU 2486 CA LYS A 322 4350 2357 2995 -266 812 -580 C ATOM 2487 C LYS A 322 20.426 8.423 8.064 1.00 25.63 C ANISOU 2487 C LYS A 322 4417 2327 2994 -265 862 -587 C ATOM 2488 O LYS A 322 21.536 8.821 7.754 1.00 26.68 O ANISOU 2488 O LYS A 322 4568 2424 3147 -285 936 -613 O ATOM 2489 CB LYS A 322 19.985 6.072 7.262 1.00 25.28 C ANISOU 2489 CB LYS A 322 4392 2294 2920 -267 803 -566 C ATOM 2490 CG LYS A 322 20.283 4.566 7.481 1.00 26.27 C ANISOU 2490 CG LYS A 322 4477 2439 3066 -276 787 -568 C ATOM 2491 CD LYS A 322 19.701 3.695 6.356 1.00 27.42 C ANISOU 2491 CD LYS A 322 4694 2562 3164 -275 762 -552 C ATOM 2492 CE LYS A 322 20.493 3.847 5.054 1.00 32.11 C ANISOU 2492 CE LYS A 322 5377 3091 3732 -287 828 -563 C ATOM 2493 NZ LYS A 322 21.963 3.525 5.184 1.00 31.61 N ANISOU 2493 NZ LYS A 322 5285 3010 3717 -305 900 -592 N ATOM 2494 N GLN A 323 19.347 9.199 8.061 1.00 25.48 N ANISOU 2494 N GLN A 323 4424 2313 2944 -243 825 -565 N ATOM 2495 CA GLN A 323 19.363 10.618 7.629 1.00 26.53 C ANISOU 2495 CA GLN A 323 4619 2403 3058 -236 869 -566 C ATOM 2496 C GLN A 323 19.681 11.617 8.743 1.00 26.55 C ANISOU 2496 C GLN A 323 4562 2424 3103 -242 894 -586 C ATOM 2497 O GLN A 323 20.007 12.776 8.458 1.00 27.23 O ANISOU 2497 O GLN A 323 4694 2468 3185 -245 950 -596 O ATOM 2498 CB GLN A 323 18.001 10.988 7.001 1.00 26.90 C ANISOU 2498 CB GLN A 323 4730 2444 3046 -201 816 -530 C ATOM 2499 CG GLN A 323 17.715 10.220 5.657 1.00 27.37 C ANISOU 2499 CG GLN A 323 4873 2475 3053 -195 800 -514 C ATOM 2500 CD GLN A 323 18.682 10.684 4.559 1.00 33.16 C ANISOU 2500 CD GLN A 323 5697 3136 3766 -208 885 -526 C ATOM 2501 OE1 GLN A 323 19.207 11.799 4.610 1.00 33.88 O ANISOU 2501 OE1 GLN A 323 5811 3194 3868 -212 946 -538 O ATOM 2502 NE2 GLN A 323 18.946 9.824 3.602 1.00 33.56 N ANISOU 2502 NE2 GLN A 323 5800 3161 3789 -217 893 -525 N ATOM 2503 N VAL A 324 19.542 11.191 10.003 1.00 25.72 N ANISOU 2503 N VAL A 324 4359 2379 3035 -244 852 -592 N ATOM 2504 CA VAL A 324 19.734 12.078 11.164 1.00 25.07 C ANISOU 2504 CA VAL A 324 4215 2322 2989 -249 865 -612 C ATOM 2505 C VAL A 324 20.941 11.672 12.032 1.00 24.91 C ANISOU 2505 C VAL A 324 4112 2329 3025 -276 894 -649 C ATOM 2506 O VAL A 324 21.647 12.532 12.612 1.00 25.03 O ANISOU 2506 O VAL A 324 4095 2343 3073 -293 939 -682 O ATOM 2507 CB VAL A 324 18.424 12.154 12.020 1.00 25.16 C ANISOU 2507 CB VAL A 324 4184 2383 2992 -223 790 -587 C ATOM 2508 CG1 VAL A 324 18.643 12.844 13.350 1.00 25.05 C ANISOU 2508 CG1 VAL A 324 4096 2403 3017 -230 798 -609 C ATOM 2509 CG2 VAL A 324 17.292 12.818 11.242 1.00 26.01 C ANISOU 2509 CG2 VAL A 324 4368 2466 3051 -193 767 -555 C ATOM 2510 N GLY A 325 21.158 10.376 12.179 1.00 23.27 N ANISOU 2510 N GLY A 325 3864 2149 2827 -278 865 -647 N ATOM 2511 CA GLY A 325 22.214 9.924 13.048 1.00 23.36 C ANISOU 2511 CA GLY A 325 3795 2193 2889 -294 882 -679 C ATOM 2512 C GLY A 325 21.694 9.355 14.343 1.00 24.10 C ANISOU 2512 C GLY A 325 3806 2353 2997 -281 818 -670 C ATOM 2513 O GLY A 325 20.518 9.034 14.457 1.00 22.71 O ANISOU 2513 O GLY A 325 3637 2197 2795 -261 760 -637 O ATOM 2514 N ASN A 326 22.594 9.261 15.319 1.00 24.40 N ANISOU 2514 N ASN A 326 3767 2426 3078 -291 830 -701 N ATOM 2515 CA ASN A 326 22.308 8.733 16.620 1.00 24.31 C ANISOU 2515 CA ASN A 326 3677 2477 3081 -278 778 -696 C ATOM 2516 C ASN A 326 21.445 9.661 17.449 1.00 24.75 C ANISOU 2516 C ASN A 326 3715 2558 3130 -269 750 -690 C ATOM 2517 O ASN A 326 21.828 10.794 17.776 1.00 24.78 O ANISOU 2517 O ASN A 326 3710 2556 3150 -281 785 -718 O ATOM 2518 CB ASN A 326 23.610 8.423 17.340 1.00 24.66 C ANISOU 2518 CB ASN A 326 3650 2551 3170 -288 801 -734 C ATOM 2519 CG ASN A 326 23.422 7.556 18.557 1.00 25.78 C ANISOU 2519 CG ASN A 326 3720 2754 3321 -269 746 -725 C ATOM 2520 OD1 ASN A 326 22.304 7.154 18.923 1.00 24.33 O ANISOU 2520 OD1 ASN A 326 3537 2592 3115 -252 693 -691 O ATOM 2521 ND2 ASN A 326 24.525 7.250 19.197 1.00 26.75 N ANISOU 2521 ND2 ASN A 326 3779 2906 3478 -272 759 -757 N ATOM 2522 N MET A 327 20.268 9.159 17.815 1.00 24.21 N ANISOU 2522 N MET A 327 3639 2517 3041 -248 690 -655 N ATOM 2523 CA MET A 327 19.308 9.959 18.578 1.00 23.56 C ANISOU 2523 CA MET A 327 3542 2459 2951 -237 661 -645 C ATOM 2524 C MET A 327 19.168 9.401 19.992 1.00 22.61 C ANISOU 2524 C MET A 327 3343 2400 2847 -227 620 -645 C ATOM 2525 O MET A 327 18.261 9.772 20.715 1.00 23.57 O ANISOU 2525 O MET A 327 3446 2547 2961 -215 588 -632 O ATOM 2526 CB MET A 327 17.970 9.984 17.836 1.00 23.74 C ANISOU 2526 CB MET A 327 3622 2463 2936 -219 627 -607 C ATOM 2527 CG MET A 327 18.051 10.695 16.483 1.00 23.51 C ANISOU 2527 CG MET A 327 3677 2373 2884 -222 667 -605 C ATOM 2528 SD MET A 327 16.553 10.534 15.491 1.00 24.54 S ANISOU 2528 SD MET A 327 3874 2485 2964 -198 618 -561 S ATOM 2529 CE MET A 327 17.087 9.126 14.453 1.00 17.56 C ANISOU 2529 CE MET A 327 3023 1580 2069 -209 622 -557 C ATOM 2530 N TYR A 328 20.070 8.503 20.368 1.00 22.99 N ANISOU 2530 N TYR A 328 3348 2469 2916 -231 622 -659 N ATOM 2531 CA TYR A 328 20.204 8.038 21.740 1.00 22.94 C ANISOU 2531 CA TYR A 328 3270 2520 2925 -221 592 -665 C ATOM 2532 C TYR A 328 18.834 7.530 22.225 1.00 22.37 C ANISOU 2532 C TYR A 328 3194 2473 2832 -202 537 -627 C ATOM 2533 O TYR A 328 18.311 6.586 21.623 1.00 20.50 O ANISOU 2533 O TYR A 328 2985 2224 2580 -196 516 -599 O ATOM 2534 CB TYR A 328 20.852 9.141 22.613 1.00 24.39 C ANISOU 2534 CB TYR A 328 3412 2725 3131 -232 615 -705 C ATOM 2535 CG TYR A 328 22.145 9.627 21.977 1.00 26.09 C ANISOU 2535 CG TYR A 328 3635 2909 3370 -255 675 -745 C ATOM 2536 CD1 TYR A 328 23.333 8.906 22.140 1.00 27.58 C ANISOU 2536 CD1 TYR A 328 3781 3115 3585 -258 687 -770 C ATOM 2537 CD2 TYR A 328 22.162 10.750 21.126 1.00 28.64 C ANISOU 2537 CD2 TYR A 328 4012 3181 3689 -272 721 -756 C ATOM 2538 CE1 TYR A 328 24.516 9.316 21.544 1.00 28.37 C ANISOU 2538 CE1 TYR A 328 3883 3187 3710 -281 745 -809 C ATOM 2539 CE2 TYR A 328 23.367 11.169 20.488 1.00 29.67 C ANISOU 2539 CE2 TYR A 328 4153 3278 3843 -298 784 -795 C ATOM 2540 CZ TYR A 328 24.522 10.449 20.717 1.00 29.86 C ANISOU 2540 CZ TYR A 328 4126 3324 3896 -304 795 -822 C ATOM 2541 OH TYR A 328 25.701 10.824 20.120 1.00 31.50 O ANISOU 2541 OH TYR A 328 4337 3500 4131 -329 859 -862 O ATOM 2542 N THR A 329 18.230 8.135 23.253 1.00 20.96 N ANISOU 2542 N THR A 329 2985 2327 2653 -195 517 -626 N ATOM 2543 CA THR A 329 16.962 7.599 23.779 1.00 20.33 C ANISOU 2543 CA THR A 329 2895 2272 2557 -178 469 -592 C ATOM 2544 C THR A 329 15.821 7.589 22.755 1.00 19.94 C ANISOU 2544 C THR A 329 2899 2192 2485 -175 453 -562 C ATOM 2545 O THR A 329 14.906 6.760 22.865 1.00 19.81 O ANISOU 2545 O THR A 329 2879 2189 2457 -166 416 -535 O ATOM 2546 CB THR A 329 16.465 8.304 25.055 1.00 20.40 C ANISOU 2546 CB THR A 329 2864 2319 2568 -171 454 -598 C ATOM 2547 OG1 THR A 329 16.180 9.688 24.781 1.00 21.81 O ANISOU 2547 OG1 THR A 329 3067 2474 2744 -176 476 -609 O ATOM 2548 CG2 THR A 329 17.494 8.194 26.227 1.00 20.76 C ANISOU 2548 CG2 THR A 329 2851 2405 2631 -170 459 -626 C ATOM 2549 N ALA A 330 15.859 8.520 21.793 1.00 19.35 N ANISOU 2549 N ALA A 330 2874 2077 2401 -181 480 -569 N ATOM 2550 CA ALA A 330 14.814 8.648 20.773 1.00 19.17 C ANISOU 2550 CA ALA A 330 2906 2026 2353 -173 462 -543 C ATOM 2551 C ALA A 330 15.085 7.769 19.554 1.00 19.66 C ANISOU 2551 C ALA A 330 3013 2055 2401 -180 467 -534 C ATOM 2552 O ALA A 330 14.239 7.660 18.679 1.00 19.11 O ANISOU 2552 O ALA A 330 2988 1967 2307 -173 445 -514 O ATOM 2553 CB ALA A 330 14.672 10.104 20.322 1.00 19.51 C ANISOU 2553 CB ALA A 330 2988 2038 2388 -170 490 -551 C ATOM 2554 N SER A 331 16.275 7.190 19.485 1.00 19.00 N ANISOU 2554 N SER A 331 2920 1966 2334 -192 495 -552 N ATOM 2555 CA SER A 331 16.696 6.368 18.340 1.00 20.48 C ANISOU 2555 CA SER A 331 3151 2119 2510 -200 508 -548 C ATOM 2556 C SER A 331 15.691 5.266 17.923 1.00 19.51 C ANISOU 2556 C SER A 331 3047 2000 2367 -195 464 -519 C ATOM 2557 O SER A 331 15.282 5.175 16.754 1.00 19.05 O ANISOU 2557 O SER A 331 3048 1909 2283 -197 460 -508 O ATOM 2558 CB SER A 331 18.042 5.740 18.688 1.00 19.97 C ANISOU 2558 CB SER A 331 3052 2061 2473 -209 537 -571 C ATOM 2559 OG SER A 331 18.578 5.081 17.576 1.00 26.47 O ANISOU 2559 OG SER A 331 3921 2848 3290 -217 560 -571 O ATOM 2560 N LEU A 332 15.291 4.434 18.885 1.00 18.93 N ANISOU 2560 N LEU A 332 2924 1965 2303 -189 432 -508 N ATOM 2561 CA LEU A 332 14.384 3.326 18.603 1.00 17.79 C ANISOU 2561 CA LEU A 332 2790 1824 2145 -190 395 -485 C ATOM 2562 C LEU A 332 13.045 3.874 18.124 1.00 18.54 C ANISOU 2562 C LEU A 332 2911 1917 2216 -183 362 -469 C ATOM 2563 O LEU A 332 12.404 3.277 17.244 1.00 17.55 O ANISOU 2563 O LEU A 332 2822 1777 2071 -188 340 -457 O ATOM 2564 CB LEU A 332 14.167 2.498 19.862 1.00 18.08 C ANISOU 2564 CB LEU A 332 2769 1902 2198 -184 374 -476 C ATOM 2565 CG LEU A 332 13.011 1.489 19.889 1.00 15.41 C ANISOU 2565 CG LEU A 332 2430 1575 1851 -186 336 -453 C ATOM 2566 CD1 LEU A 332 13.190 0.382 18.782 1.00 13.17 C ANISOU 2566 CD1 LEU A 332 2192 1258 1555 -199 340 -449 C ATOM 2567 CD2 LEU A 332 12.927 0.916 21.286 1.00 14.95 C ANISOU 2567 CD2 LEU A 332 2316 1554 1809 -178 325 -446 C ATOM 2568 N TYR A 333 12.624 4.991 18.732 1.00 17.59 N ANISOU 2568 N TYR A 333 2770 1814 2101 -172 357 -471 N ATOM 2569 CA TYR A 333 11.299 5.606 18.460 1.00 18.35 C ANISOU 2569 CA TYR A 333 2881 1914 2179 -159 324 -455 C ATOM 2570 C TYR A 333 11.298 6.332 17.136 1.00 18.60 C ANISOU 2570 C TYR A 333 2981 1904 2182 -154 335 -455 C ATOM 2571 O TYR A 333 10.284 6.378 16.479 1.00 18.66 O ANISOU 2571 O TYR A 333 3015 1908 2167 -144 301 -441 O ATOM 2572 CB TYR A 333 10.773 6.444 19.667 1.00 18.02 C ANISOU 2572 CB TYR A 333 2790 1906 2152 -147 315 -455 C ATOM 2573 CG TYR A 333 10.727 5.489 20.828 1.00 18.00 C ANISOU 2573 CG TYR A 333 2731 1941 2169 -151 301 -452 C ATOM 2574 CD1 TYR A 333 9.755 4.491 20.870 1.00 18.29 C ANISOU 2574 CD1 TYR A 333 2755 1994 2203 -154 266 -435 C ATOM 2575 CD2 TYR A 333 11.754 5.450 21.772 1.00 19.34 C ANISOU 2575 CD2 TYR A 333 2864 2127 2358 -154 326 -467 C ATOM 2576 CE1 TYR A 333 9.752 3.511 21.868 1.00 16.37 C ANISOU 2576 CE1 TYR A 333 2469 1777 1974 -159 260 -429 C ATOM 2577 CE2 TYR A 333 11.768 4.443 22.780 1.00 17.30 C ANISOU 2577 CE2 TYR A 333 2563 1900 2112 -154 314 -461 C ATOM 2578 CZ TYR A 333 10.739 3.502 22.805 1.00 17.04 C ANISOU 2578 CZ TYR A 333 2524 1877 2074 -156 283 -440 C ATOM 2579 OH TYR A 333 10.727 2.526 23.777 1.00 20.85 O ANISOU 2579 OH TYR A 333 2971 2384 2566 -156 277 -432 O ATOM 2580 N ALA A 334 12.453 6.845 16.722 1.00 19.43 N ANISOU 2580 N ALA A 334 3116 1977 2290 -162 384 -472 N ATOM 2581 CA ALA A 334 12.612 7.366 15.346 1.00 20.04 C ANISOU 2581 CA ALA A 334 3271 2006 2337 -159 404 -472 C ATOM 2582 C ALA A 334 12.639 6.272 14.288 1.00 20.69 C ANISOU 2582 C ALA A 334 3397 2068 2398 -169 394 -465 C ATOM 2583 O ALA A 334 12.192 6.492 13.154 1.00 21.39 O ANISOU 2583 O ALA A 334 3548 2128 2450 -161 384 -456 O ATOM 2584 CB ALA A 334 13.841 8.203 15.246 1.00 19.89 C ANISOU 2584 CB ALA A 334 3271 1957 2330 -168 466 -494 C ATOM 2585 N ALA A 335 13.198 5.115 14.632 1.00 20.12 N ANISOU 2585 N ALA A 335 3294 2006 2345 -185 399 -471 N ATOM 2586 CA ALA A 335 13.139 3.936 13.740 1.00 20.73 C ANISOU 2586 CA ALA A 335 3407 2066 2404 -196 388 -466 C ATOM 2587 C ALA A 335 11.681 3.482 13.598 1.00 21.22 C ANISOU 2587 C ALA A 335 3466 2151 2447 -191 327 -448 C ATOM 2588 O ALA A 335 11.221 3.154 12.510 1.00 22.36 O ANISOU 2588 O ALA A 335 3662 2275 2559 -193 307 -443 O ATOM 2589 CB ALA A 335 14.014 2.819 14.293 1.00 19.09 C ANISOU 2589 CB ALA A 335 3162 1867 2224 -210 407 -474 C ATOM 2590 N PHE A 336 10.942 3.501 14.711 1.00 21.43 N ANISOU 2590 N PHE A 336 3431 2220 2494 -184 297 -441 N ATOM 2591 CA PHE A 336 9.523 3.170 14.719 1.00 21.75 C ANISOU 2591 CA PHE A 336 3455 2286 2523 -180 241 -428 C ATOM 2592 C PHE A 336 8.716 4.190 13.906 1.00 23.04 C ANISOU 2592 C PHE A 336 3660 2440 2656 -159 217 -421 C ATOM 2593 O PHE A 336 7.805 3.816 13.114 1.00 22.83 O ANISOU 2593 O PHE A 336 3657 2414 2602 -157 175 -415 O ATOM 2594 CB PHE A 336 9.004 3.088 16.154 1.00 20.18 C ANISOU 2594 CB PHE A 336 3181 2131 2354 -176 225 -423 C ATOM 2595 CG PHE A 336 7.575 2.668 16.251 1.00 22.55 C ANISOU 2595 CG PHE A 336 3457 2459 2652 -176 174 -413 C ATOM 2596 CD1 PHE A 336 7.136 1.453 15.683 1.00 23.56 C ANISOU 2596 CD1 PHE A 336 3597 2584 2771 -195 152 -413 C ATOM 2597 CD2 PHE A 336 6.651 3.461 16.905 1.00 24.11 C ANISOU 2597 CD2 PHE A 336 3617 2686 2858 -158 151 -407 C ATOM 2598 CE1 PHE A 336 5.798 1.062 15.773 1.00 21.21 C ANISOU 2598 CE1 PHE A 336 3271 2314 2475 -199 106 -409 C ATOM 2599 CE2 PHE A 336 5.297 3.068 17.000 1.00 25.85 C ANISOU 2599 CE2 PHE A 336 3808 2934 3080 -159 105 -401 C ATOM 2600 CZ PHE A 336 4.877 1.889 16.427 1.00 19.56 C ANISOU 2600 CZ PHE A 336 3020 2135 2276 -180 82 -403 C ATOM 2601 N ALA A 337 9.044 5.466 14.093 1.00 22.38 N ANISOU 2601 N ALA A 337 3584 2346 2573 -142 243 -423 N ATOM 2602 CA ALA A 337 8.415 6.537 13.318 1.00 23.22 C ANISOU 2602 CA ALA A 337 3738 2437 2648 -116 228 -414 C ATOM 2603 C ALA A 337 8.675 6.401 11.802 1.00 22.82 C ANISOU 2603 C ALA A 337 3773 2344 2555 -116 234 -414 C ATOM 2604 O ALA A 337 7.792 6.638 11.000 1.00 22.84 O ANISOU 2604 O ALA A 337 3813 2345 2523 -97 195 -403 O ATOM 2605 CB ALA A 337 8.879 7.963 13.854 1.00 22.66 C ANISOU 2605 CB ALA A 337 3666 2355 2589 -101 268 -418 C ATOM 2606 N SER A 338 9.898 6.035 11.437 1.00 23.57 N ANISOU 2606 N SER A 338 3897 2406 2652 -137 283 -425 N ATOM 2607 CA SER A 338 10.254 5.621 10.081 1.00 24.20 C ANISOU 2607 CA SER A 338 4055 2445 2694 -144 294 -427 C ATOM 2608 C SER A 338 9.330 4.509 9.571 1.00 24.38 C ANISOU 2608 C SER A 338 4080 2485 2696 -151 238 -423 C ATOM 2609 O SER A 338 8.808 4.591 8.461 1.00 24.51 O ANISOU 2609 O SER A 338 4157 2486 2668 -140 211 -418 O ATOM 2610 CB SER A 338 11.701 5.154 10.025 1.00 23.67 C ANISOU 2610 CB SER A 338 3998 2350 2647 -168 355 -443 C ATOM 2611 OG SER A 338 12.581 6.190 10.394 1.00 22.98 O ANISOU 2611 OG SER A 338 3909 2245 2578 -165 409 -453 O ATOM 2612 N LEU A 339 9.103 3.480 10.382 1.00 24.32 N ANISOU 2612 N LEU A 339 4010 2511 2721 -170 219 -425 N ATOM 2613 CA LEU A 339 8.227 2.390 9.966 1.00 24.51 C ANISOU 2613 CA LEU A 339 4032 2551 2730 -183 170 -425 C ATOM 2614 C LEU A 339 6.799 2.859 9.648 1.00 26.00 C ANISOU 2614 C LEU A 339 4219 2766 2894 -161 107 -417 C ATOM 2615 O LEU A 339 6.216 2.473 8.619 1.00 27.32 O ANISOU 2615 O LEU A 339 4428 2927 3024 -162 71 -420 O ATOM 2616 CB LEU A 339 8.194 1.264 11.013 1.00 24.06 C ANISOU 2616 CB LEU A 339 3906 2522 2713 -205 167 -428 C ATOM 2617 CG LEU A 339 7.167 0.141 10.801 1.00 23.66 C ANISOU 2617 CG LEU A 339 3840 2491 2657 -224 120 -431 C ATOM 2618 CD1 LEU A 339 7.423 -0.577 9.467 1.00 22.84 C ANISOU 2618 CD1 LEU A 339 3809 2353 2517 -240 121 -440 C ATOM 2619 CD2 LEU A 339 7.290 -0.834 11.923 1.00 23.00 C ANISOU 2619 CD2 LEU A 339 3696 2428 2615 -243 131 -431 C ATOM 2620 N VAL A 340 6.227 3.660 10.540 1.00 27.04 N ANISOU 2620 N VAL A 340 4299 2927 3047 -141 93 -409 N ATOM 2621 CA VAL A 340 4.887 4.216 10.342 1.00 27.52 C ANISOU 2621 CA VAL A 340 4350 3016 3091 -114 35 -402 C ATOM 2622 C VAL A 340 4.865 5.089 9.067 1.00 28.34 C ANISOU 2622 C VAL A 340 4539 3088 3142 -85 29 -395 C ATOM 2623 O VAL A 340 3.939 5.000 8.251 1.00 29.61 O ANISOU 2623 O VAL A 340 4724 3260 3268 -71 -24 -394 O ATOM 2624 CB VAL A 340 4.426 5.039 11.569 1.00 27.22 C ANISOU 2624 CB VAL A 340 4246 3009 3087 -95 33 -394 C ATOM 2625 CG1 VAL A 340 3.093 5.750 11.291 1.00 25.29 C ANISOU 2625 CG1 VAL A 340 3995 2790 2825 -61 -23 -386 C ATOM 2626 CG2 VAL A 340 4.318 4.156 12.844 1.00 27.37 C ANISOU 2626 CG2 VAL A 340 4185 3062 3153 -121 35 -399 C ATOM 2627 N HIS A 341 5.898 5.895 8.874 1.00 27.63 N ANISOU 2627 N HIS A 341 4497 2958 3045 -77 86 -393 N ATOM 2628 CA HIS A 341 5.948 6.775 7.712 1.00 28.41 C ANISOU 2628 CA HIS A 341 4684 3020 3092 -48 91 -384 C ATOM 2629 C HIS A 341 5.881 5.938 6.430 1.00 28.99 C ANISOU 2629 C HIS A 341 4821 3076 3120 -59 68 -390 C ATOM 2630 O HIS A 341 5.125 6.262 5.505 1.00 28.71 O ANISOU 2630 O HIS A 341 4834 3040 3036 -31 24 -383 O ATOM 2631 CB HIS A 341 7.238 7.582 7.738 1.00 27.73 C ANISOU 2631 CB HIS A 341 4637 2887 3012 -49 168 -386 C ATOM 2632 CG HIS A 341 7.487 8.363 6.493 1.00 29.32 C ANISOU 2632 CG HIS A 341 4941 3039 3159 -25 189 -378 C ATOM 2633 ND1 HIS A 341 6.690 9.419 6.111 1.00 31.69 N ANISOU 2633 ND1 HIS A 341 5277 3338 3427 20 161 -361 N ATOM 2634 CD2 HIS A 341 8.469 8.273 5.563 1.00 31.15 C ANISOU 2634 CD2 HIS A 341 5251 3220 3364 -38 238 -384 C ATOM 2635 CE1 HIS A 341 7.156 9.928 4.981 1.00 34.28 C ANISOU 2635 CE1 HIS A 341 5705 3615 3706 35 192 -355 C ATOM 2636 NE2 HIS A 341 8.239 9.255 4.634 1.00 33.48 N ANISOU 2636 NE2 HIS A 341 5632 3482 3608 -1 241 -370 N ATOM 2637 N ASN A 342 6.671 4.859 6.404 1.00 29.03 N ANISOU 2637 N ASN A 342 4824 3066 3139 -98 98 -403 N ATOM 2638 CA ASN A 342 6.877 4.051 5.215 1.00 29.60 C ANISOU 2638 CA ASN A 342 4964 3112 3170 -114 94 -411 C ATOM 2639 C ASN A 342 5.787 3.014 5.007 1.00 30.36 C ANISOU 2639 C ASN A 342 5033 3245 3258 -127 25 -420 C ATOM 2640 O ASN A 342 5.561 2.614 3.895 1.00 30.85 O ANISOU 2640 O ASN A 342 5155 3294 3273 -130 1 -426 O ATOM 2641 CB ASN A 342 8.198 3.291 5.301 1.00 28.91 C ANISOU 2641 CB ASN A 342 4885 2992 3106 -149 158 -424 C ATOM 2642 CG ASN A 342 9.400 4.131 4.976 1.00 30.56 C ANISOU 2642 CG ASN A 342 5150 3153 3310 -143 230 -423 C ATOM 2643 OD1 ASN A 342 9.392 4.930 4.031 1.00 29.99 O ANISOU 2643 OD1 ASN A 342 5157 3048 3191 -120 238 -416 O ATOM 2644 ND2 ASN A 342 10.481 3.923 5.743 1.00 29.20 N ANISOU 2644 ND2 ASN A 342 4939 2972 3185 -164 287 -432 N ATOM 2645 N LYS A 343 5.151 2.524 6.075 1.00 31.06 N ANISOU 2645 N LYS A 343 5032 3379 3392 -140 -3 -423 N ATOM 2646 CA LYS A 343 4.252 1.376 5.936 1.00 31.34 C ANISOU 2646 CA LYS A 343 5035 3444 3426 -164 -55 -436 C ATOM 2647 C LYS A 343 2.860 1.569 6.539 1.00 32.84 C ANISOU 2647 C LYS A 343 5153 3690 3635 -151 -118 -435 C ATOM 2648 O LYS A 343 2.112 0.600 6.650 1.00 32.74 O ANISOU 2648 O LYS A 343 5099 3705 3635 -176 -156 -449 O ATOM 2649 CB LYS A 343 4.876 0.087 6.509 1.00 30.43 C ANISOU 2649 CB LYS A 343 4888 3324 3350 -208 -21 -447 C ATOM 2650 CG LYS A 343 6.348 -0.229 6.148 1.00 31.11 C ANISOU 2650 CG LYS A 343 5028 3359 3434 -224 48 -450 C ATOM 2651 CD LYS A 343 6.727 -0.220 4.627 1.00 35.38 C ANISOU 2651 CD LYS A 343 5671 3857 3915 -222 57 -455 C ATOM 2652 CE LYS A 343 5.970 -1.165 3.815 1.00 33.55 C ANISOU 2652 CE LYS A 343 5463 3633 3652 -241 8 -470 C ATOM 2653 NZ LYS A 343 4.509 -0.910 3.896 1.00 38.83 N ANISOU 2653 NZ LYS A 343 6090 4351 4312 -226 -69 -471 N ATOM 2654 N HIS A 344 2.502 2.802 6.916 1.00 34.01 N ANISOU 2654 N HIS A 344 5286 3851 3786 -111 -127 -420 N ATOM 2655 CA HIS A 344 1.248 3.052 7.638 1.00 35.58 C ANISOU 2655 CA HIS A 344 5406 4101 4010 -96 -177 -418 C ATOM 2656 C HIS A 344 -0.002 2.372 7.050 1.00 37.56 C ANISOU 2656 C HIS A 344 5639 4389 4244 -103 -251 -434 C ATOM 2657 O HIS A 344 -0.857 1.849 7.813 1.00 38.28 O ANISOU 2657 O HIS A 344 5649 4522 4374 -120 -280 -444 O ATOM 2658 CB HIS A 344 1.009 4.564 7.876 1.00 35.47 C ANISOU 2658 CB HIS A 344 5395 4091 3991 -46 -178 -400 C ATOM 2659 CG HIS A 344 0.786 5.364 6.627 1.00 36.36 C ANISOU 2659 CG HIS A 344 5588 4184 4043 -5 -203 -391 C ATOM 2660 ND1 HIS A 344 1.804 6.018 5.962 1.00 36.70 N ANISOU 2660 ND1 HIS A 344 5718 4174 4052 9 -154 -381 N ATOM 2661 CD2 HIS A 344 -0.351 5.650 5.946 1.00 37.05 C ANISOU 2661 CD2 HIS A 344 5684 4299 4096 28 -273 -390 C ATOM 2662 CE1 HIS A 344 1.305 6.652 4.913 1.00 39.23 C ANISOU 2662 CE1 HIS A 344 6103 4486 4316 50 -190 -372 C ATOM 2663 NE2 HIS A 344 -0.001 6.444 4.882 1.00 36.91 N ANISOU 2663 NE2 HIS A 344 5762 4243 4020 64 -266 -378 N ATOM 2664 N SER A 345 -0.109 2.352 5.720 1.00 38.75 N ANISOU 2664 N SER A 345 5863 4524 4337 -92 -281 -440 N ATOM 2665 CA SER A 345 -1.325 1.828 5.078 1.00 40.39 C ANISOU 2665 CA SER A 345 6055 4769 4522 -95 -359 -458 C ATOM 2666 C SER A 345 -1.397 0.290 5.130 1.00 40.47 C ANISOU 2666 C SER A 345 6037 4786 4552 -154 -361 -484 C ATOM 2667 O SER A 345 -2.457 -0.297 4.906 1.00 41.44 O ANISOU 2667 O SER A 345 6123 4947 4676 -169 -420 -506 O ATOM 2668 CB SER A 345 -1.507 2.385 3.656 1.00 40.94 C ANISOU 2668 CB SER A 345 6213 4825 4518 -58 -397 -456 C ATOM 2669 OG SER A 345 -0.477 1.938 2.798 1.00 42.70 O ANISOU 2669 OG SER A 345 6523 4997 4703 -78 -357 -459 O ATOM 2670 N ASP A 346 -0.291 -0.353 5.493 1.00 39.40 N ANISOU 2670 N ASP A 346 5916 4615 4439 -188 -296 -483 N ATOM 2671 CA ASP A 346 -0.284 -1.800 5.612 1.00 39.32 C ANISOU 2671 CA ASP A 346 5884 4604 4450 -242 -288 -505 C ATOM 2672 C ASP A 346 0.039 -2.340 6.999 1.00 37.19 C ANISOU 2672 C ASP A 346 5546 4340 4245 -268 -243 -500 C ATOM 2673 O ASP A 346 0.234 -3.533 7.153 1.00 37.65 O ANISOU 2673 O ASP A 346 5596 4388 4321 -310 -223 -513 O ATOM 2674 CB ASP A 346 0.677 -2.356 4.575 1.00 40.63 C ANISOU 2674 CB ASP A 346 6140 4721 4576 -260 -257 -512 C ATOM 2675 CG ASP A 346 0.240 -2.011 3.167 1.00 45.45 C ANISOU 2675 CG ASP A 346 6822 5329 5118 -238 -307 -520 C ATOM 2676 OD1 ASP A 346 -0.947 -2.295 2.838 1.00 47.58 O ANISOU 2676 OD1 ASP A 346 7062 5639 5376 -242 -377 -539 O ATOM 2677 OD2 ASP A 346 1.066 -1.427 2.408 1.00 49.07 O ANISOU 2677 OD2 ASP A 346 7365 5746 5534 -216 -277 -507 O ATOM 2678 N LEU A 347 0.078 -1.465 8.009 1.00 35.58 N ANISOU 2678 N LEU A 347 5296 4151 4072 -241 -226 -481 N ATOM 2679 CA LEU A 347 0.499 -1.842 9.366 1.00 32.77 C ANISOU 2679 CA LEU A 347 4882 3798 3770 -259 -180 -473 C ATOM 2680 C LEU A 347 -0.626 -2.381 10.233 1.00 32.05 C ANISOU 2680 C LEU A 347 4707 3750 3720 -279 -208 -483 C ATOM 2681 O LEU A 347 -0.387 -3.112 11.180 1.00 31.52 O ANISOU 2681 O LEU A 347 4602 3684 3692 -304 -174 -482 O ATOM 2682 CB LEU A 347 1.194 -0.651 10.058 1.00 32.51 C ANISOU 2682 CB LEU A 347 4846 3758 3750 -225 -142 -451 C ATOM 2683 CG LEU A 347 2.712 -0.509 9.859 1.00 31.06 C ANISOU 2683 CG LEU A 347 4718 3526 3555 -225 -80 -444 C ATOM 2684 CD1 LEU A 347 3.288 0.814 10.477 1.00 27.74 C ANISOU 2684 CD1 LEU A 347 4293 3101 3146 -191 -48 -428 C ATOM 2685 CD2 LEU A 347 3.435 -1.733 10.412 1.00 30.99 C ANISOU 2685 CD2 LEU A 347 4695 3504 3577 -261 -39 -449 C ATOM 2686 N ALA A 348 -1.861 -2.029 9.910 1.00 32.06 N ANISOU 2686 N ALA A 348 4680 3789 3713 -265 -269 -493 N ATOM 2687 CA ALA A 348 -3.023 -2.540 10.653 1.00 32.10 C ANISOU 2687 CA ALA A 348 4601 3837 3759 -286 -296 -507 C ATOM 2688 C ALA A 348 -3.023 -4.068 10.673 1.00 31.81 C ANISOU 2688 C ALA A 348 4558 3789 3739 -343 -281 -528 C ATOM 2689 O ALA A 348 -2.832 -4.693 9.643 1.00 31.90 O ANISOU 2689 O ALA A 348 4623 3781 3718 -363 -292 -543 O ATOM 2690 CB ALA A 348 -4.329 -2.000 10.060 1.00 31.95 C ANISOU 2690 CB ALA A 348 4557 3859 3724 -263 -370 -520 C ATOM 2691 N GLY A 349 -3.201 -4.651 11.856 1.00 30.72 N ANISOU 2691 N GLY A 349 4361 3661 3649 -366 -251 -526 N ATOM 2692 CA GLY A 349 -3.104 -6.091 12.030 1.00 30.53 C ANISOU 2692 CA GLY A 349 4336 3621 3645 -418 -224 -541 C ATOM 2693 C GLY A 349 -1.719 -6.691 12.235 1.00 29.95 C ANISOU 2693 C GLY A 349 4309 3500 3570 -428 -160 -527 C ATOM 2694 O GLY A 349 -1.608 -7.891 12.516 1.00 29.43 O ANISOU 2694 O GLY A 349 4242 3417 3522 -466 -130 -535 O ATOM 2695 N LYS A 350 -0.662 -5.884 12.117 1.00 28.69 N ANISOU 2695 N LYS A 350 4192 3319 3391 -394 -136 -506 N ATOM 2696 CA LYS A 350 0.710 -6.428 12.131 1.00 27.88 C ANISOU 2696 CA LYS A 350 4137 3173 3285 -401 -79 -496 C ATOM 2697 C LYS A 350 1.368 -6.463 13.528 1.00 27.24 C ANISOU 2697 C LYS A 350 4020 3091 3241 -393 -29 -475 C ATOM 2698 O LYS A 350 0.981 -5.719 14.416 1.00 26.68 O ANISOU 2698 O LYS A 350 3899 3049 3189 -372 -35 -465 O ATOM 2699 CB LYS A 350 1.607 -5.671 11.143 1.00 27.52 C ANISOU 2699 CB LYS A 350 4161 3099 3198 -375 -73 -490 C ATOM 2700 CG LYS A 350 1.068 -5.640 9.677 1.00 29.20 C ANISOU 2700 CG LYS A 350 4423 3308 3363 -379 -120 -509 C ATOM 2701 CD LYS A 350 1.091 -6.999 9.042 1.00 30.84 C ANISOU 2701 CD LYS A 350 4663 3493 3562 -423 -115 -530 C ATOM 2702 CE LYS A 350 0.448 -6.984 7.610 1.00 33.00 C ANISOU 2702 CE LYS A 350 4983 3769 3785 -428 -170 -553 C ATOM 2703 NZ LYS A 350 1.223 -6.067 6.722 1.00 34.26 N ANISOU 2703 NZ LYS A 350 5215 3902 3899 -393 -163 -541 N ATOM 2704 N ARG A 351 2.351 -7.342 13.705 1.00 25.50 N ANISOU 2704 N ARG A 351 3825 2837 3026 -407 18 -471 N ATOM 2705 CA ARG A 351 3.123 -7.354 14.918 1.00 25.12 C ANISOU 2705 CA ARG A 351 3751 2787 3005 -392 62 -451 C ATOM 2706 C ARG A 351 4.483 -6.685 14.709 1.00 24.97 C ANISOU 2706 C ARG A 351 3770 2746 2972 -365 92 -441 C ATOM 2707 O ARG A 351 5.222 -6.993 13.759 1.00 25.18 O ANISOU 2707 O ARG A 351 3853 2739 2977 -371 108 -448 O ATOM 2708 CB ARG A 351 3.304 -8.762 15.491 1.00 24.79 C ANISOU 2708 CB ARG A 351 3706 2729 2986 -419 97 -450 C ATOM 2709 CG ARG A 351 4.401 -8.809 16.580 1.00 22.93 C ANISOU 2709 CG ARG A 351 3459 2487 2768 -397 144 -429 C ATOM 2710 CD ARG A 351 4.616 -10.215 17.146 1.00 23.80 C ANISOU 2710 CD ARG A 351 3571 2576 2896 -417 181 -424 C ATOM 2711 NE ARG A 351 3.477 -10.568 17.982 1.00 26.17 N ANISOU 2711 NE ARG A 351 3824 2899 3219 -434 172 -424 N ATOM 2712 CZ ARG A 351 2.785 -11.706 17.902 1.00 29.14 C ANISOU 2712 CZ ARG A 351 4203 3263 3606 -471 178 -435 C ATOM 2713 NH1 ARG A 351 3.123 -12.657 17.024 1.00 27.03 N ANISOU 2713 NH1 ARG A 351 3986 2959 3327 -495 193 -447 N ATOM 2714 NH2 ARG A 351 1.767 -11.908 18.740 1.00 27.14 N ANISOU 2714 NH2 ARG A 351 3902 3033 3377 -486 175 -435 N ATOM 2715 N VAL A 352 4.797 -5.764 15.610 1.00 22.88 N ANISOU 2715 N VAL A 352 3471 2500 2721 -337 103 -428 N ATOM 2716 CA VAL A 352 6.058 -5.048 15.549 1.00 22.69 C ANISOU 2716 CA VAL A 352 3471 2458 2690 -314 134 -423 C ATOM 2717 C VAL A 352 6.822 -5.349 16.839 1.00 21.63 C ANISOU 2717 C VAL A 352 3302 2331 2584 -304 171 -411 C ATOM 2718 O VAL A 352 6.316 -5.101 17.936 1.00 21.76 O ANISOU 2718 O VAL A 352 3269 2379 2620 -297 164 -403 O ATOM 2719 CB VAL A 352 5.838 -3.497 15.438 1.00 22.72 C ANISOU 2719 CB VAL A 352 3471 2479 2683 -286 115 -420 C ATOM 2720 CG1 VAL A 352 7.195 -2.730 15.333 1.00 23.12 C ANISOU 2720 CG1 VAL A 352 3549 2507 2728 -267 154 -419 C ATOM 2721 CG2 VAL A 352 4.970 -3.146 14.249 1.00 23.82 C ANISOU 2721 CG2 VAL A 352 3642 2616 2791 -288 72 -429 C ATOM 2722 N VAL A 353 8.042 -5.855 16.699 1.00 20.93 N ANISOU 2722 N VAL A 353 3242 2216 2497 -303 209 -411 N ATOM 2723 CA VAL A 353 8.907 -6.141 17.852 1.00 20.71 C ANISOU 2723 CA VAL A 353 3183 2194 2491 -288 241 -401 C ATOM 2724 C VAL A 353 9.925 -5.007 17.954 1.00 20.17 C ANISOU 2724 C VAL A 353 3113 2128 2423 -264 260 -405 C ATOM 2725 O VAL A 353 10.491 -4.588 16.952 1.00 21.23 O ANISOU 2725 O VAL A 353 3289 2237 2541 -264 271 -415 O ATOM 2726 CB VAL A 353 9.582 -7.560 17.732 1.00 21.72 C ANISOU 2726 CB VAL A 353 3337 2293 2624 -298 273 -399 C ATOM 2727 CG1 VAL A 353 10.707 -7.763 18.782 1.00 21.15 C ANISOU 2727 CG1 VAL A 353 3240 2226 2571 -273 306 -390 C ATOM 2728 CG2 VAL A 353 8.513 -8.671 17.841 1.00 19.07 C ANISOU 2728 CG2 VAL A 353 2997 1956 2293 -325 260 -397 C ATOM 2729 N MET A 354 10.117 -4.516 19.171 1.00 19.13 N ANISOU 2729 N MET A 354 2935 2025 2308 -246 264 -399 N ATOM 2730 CA MET A 354 10.967 -3.365 19.466 1.00 18.58 C ANISOU 2730 CA MET A 354 2853 1964 2242 -226 280 -407 C ATOM 2731 C MET A 354 12.074 -3.820 20.392 1.00 17.73 C ANISOU 2731 C MET A 354 2720 1865 2153 -212 308 -406 C ATOM 2732 O MET A 354 11.799 -4.489 21.381 1.00 19.77 O ANISOU 2732 O MET A 354 2949 2143 2421 -207 305 -393 O ATOM 2733 CB MET A 354 10.167 -2.312 20.212 1.00 15.41 C ANISOU 2733 CB MET A 354 2414 1596 1845 -216 258 -404 C ATOM 2734 CG MET A 354 8.947 -1.814 19.510 1.00 19.48 C ANISOU 2734 CG MET A 354 2943 2113 2346 -223 224 -403 C ATOM 2735 SD MET A 354 9.304 -0.570 18.307 1.00 20.12 S ANISOU 2735 SD MET A 354 3071 2168 2404 -215 228 -414 S ATOM 2736 CE MET A 354 9.335 0.914 19.319 1.00 20.23 C ANISOU 2736 CE MET A 354 3046 2209 2431 -194 234 -416 C ATOM 2737 N PHE A 355 13.294 -3.407 20.108 1.00 17.88 N ANISOU 2737 N PHE A 355 2747 1870 2175 -203 336 -419 N ATOM 2738 CA PHE A 355 14.441 -3.672 20.983 1.00 18.16 C ANISOU 2738 CA PHE A 355 2752 1919 2228 -185 359 -423 C ATOM 2739 C PHE A 355 15.156 -2.386 21.395 1.00 17.75 C ANISOU 2739 C PHE A 355 2674 1886 2186 -174 371 -441 C ATOM 2740 O PHE A 355 15.682 -1.641 20.567 1.00 16.04 O ANISOU 2740 O PHE A 355 2481 1646 1966 -181 389 -458 O ATOM 2741 CB PHE A 355 15.456 -4.648 20.347 1.00 18.82 C ANISOU 2741 CB PHE A 355 2863 1971 2317 -185 389 -427 C ATOM 2742 CG PHE A 355 16.680 -4.922 21.232 1.00 17.94 C ANISOU 2742 CG PHE A 355 2715 1877 2224 -160 410 -432 C ATOM 2743 CD1 PHE A 355 16.549 -5.645 22.420 1.00 18.30 C ANISOU 2743 CD1 PHE A 355 2729 1950 2275 -142 400 -415 C ATOM 2744 CD2 PHE A 355 17.917 -4.392 20.910 1.00 18.82 C ANISOU 2744 CD2 PHE A 355 2822 1981 2348 -154 438 -455 C ATOM 2745 CE1 PHE A 355 17.624 -5.877 23.253 1.00 17.63 C ANISOU 2745 CE1 PHE A 355 2611 1886 2203 -113 412 -420 C ATOM 2746 CE2 PHE A 355 19.041 -4.642 21.730 1.00 18.75 C ANISOU 2746 CE2 PHE A 355 2772 1994 2357 -130 452 -463 C ATOM 2747 CZ PHE A 355 18.884 -5.363 22.913 1.00 16.42 C ANISOU 2747 CZ PHE A 355 2446 1728 2064 -107 436 -445 C ATOM 2748 N SER A 356 15.190 -2.177 22.703 1.00 18.30 N ANISOU 2748 N SER A 356 2696 1994 2265 -158 362 -439 N ATOM 2749 CA SER A 356 15.746 -0.991 23.314 1.00 18.73 C ANISOU 2749 CA SER A 356 2717 2071 2328 -149 369 -459 C ATOM 2750 C SER A 356 16.975 -1.388 24.116 1.00 19.26 C ANISOU 2750 C SER A 356 2749 2158 2409 -130 384 -469 C ATOM 2751 O SER A 356 16.961 -2.365 24.831 1.00 18.69 O ANISOU 2751 O SER A 356 2662 2101 2337 -115 376 -453 O ATOM 2752 CB SER A 356 14.697 -0.317 24.220 1.00 18.39 C ANISOU 2752 CB SER A 356 2647 2059 2280 -146 344 -451 C ATOM 2753 OG SER A 356 15.182 0.920 24.721 1.00 19.54 O ANISOU 2753 OG SER A 356 2768 2224 2433 -141 353 -472 O ATOM 2754 N TYR A 357 18.045 -0.616 23.975 1.00 21.03 N ANISOU 2754 N TYR A 357 2960 2382 2646 -130 408 -498 N ATOM 2755 CA TYR A 357 19.282 -0.871 24.686 1.00 22.38 C ANISOU 2755 CA TYR A 357 3091 2577 2834 -111 419 -515 C ATOM 2756 C TYR A 357 19.761 0.404 25.319 1.00 23.10 C ANISOU 2756 C TYR A 357 3145 2696 2935 -112 424 -545 C ATOM 2757 O TYR A 357 19.574 1.467 24.747 1.00 24.27 O ANISOU 2757 O TYR A 357 3311 2826 3083 -131 437 -559 O ATOM 2758 CB TYR A 357 20.384 -1.362 23.711 1.00 22.78 C ANISOU 2758 CB TYR A 357 3161 2596 2898 -114 452 -528 C ATOM 2759 CG TYR A 357 21.640 -1.811 24.439 1.00 24.01 C ANISOU 2759 CG TYR A 357 3272 2779 3074 -89 461 -544 C ATOM 2760 CD1 TYR A 357 21.672 -3.040 25.098 1.00 23.81 C ANISOU 2760 CD1 TYR A 357 3236 2769 3044 -62 446 -521 C ATOM 2761 CD2 TYR A 357 22.776 -0.989 24.499 1.00 22.63 C ANISOU 2761 CD2 TYR A 357 3062 2616 2920 -92 483 -583 C ATOM 2762 CE1 TYR A 357 22.806 -3.447 25.795 1.00 24.73 C ANISOU 2762 CE1 TYR A 357 3308 2913 3174 -32 449 -534 C ATOM 2763 CE2 TYR A 357 23.925 -1.400 25.185 1.00 22.97 C ANISOU 2763 CE2 TYR A 357 3056 2690 2981 -66 485 -601 C ATOM 2764 CZ TYR A 357 23.930 -2.636 25.821 1.00 25.16 C ANISOU 2764 CZ TYR A 357 3324 2984 3252 -33 466 -574 C ATOM 2765 OH TYR A 357 25.046 -3.075 26.528 1.00 26.80 O ANISOU 2765 OH TYR A 357 3483 3225 3474 0 463 -589 O ATOM 2766 N GLY A 358 20.407 0.297 26.472 1.00 24.01 N ANISOU 2766 N GLY A 358 3210 2853 3057 -91 415 -556 N ATOM 2767 CA GLY A 358 21.230 1.386 27.001 1.00 26.52 C ANISOU 2767 CA GLY A 358 3487 3198 3390 -94 425 -595 C ATOM 2768 C GLY A 358 22.398 0.703 27.671 1.00 28.20 C ANISOU 2768 C GLY A 358 3656 3442 3615 -68 423 -609 C ATOM 2769 O GLY A 358 22.212 -0.286 28.396 1.00 28.50 O ANISOU 2769 O GLY A 358 3685 3501 3641 -40 400 -583 O ATOM 2770 N SER A 359 23.599 1.211 27.403 1.00 29.31 N ANISOU 2770 N SER A 359 3771 3585 3781 -75 449 -649 N ATOM 2771 CA SER A 359 24.840 0.751 28.011 1.00 30.23 C ANISOU 2771 CA SER A 359 3836 3736 3914 -49 447 -672 C ATOM 2772 C SER A 359 24.804 0.790 29.551 1.00 30.33 C ANISOU 2772 C SER A 359 3802 3810 3913 -22 409 -674 C ATOM 2773 O SER A 359 24.162 1.670 30.143 1.00 28.82 O ANISOU 2773 O SER A 359 3605 3636 3709 -34 396 -679 O ATOM 2774 CB SER A 359 25.981 1.635 27.516 1.00 30.99 C ANISOU 2774 CB SER A 359 3907 3826 4042 -72 483 -723 C ATOM 2775 OG SER A 359 26.174 1.437 26.119 1.00 35.63 O ANISOU 2775 OG SER A 359 4539 4358 4640 -91 522 -721 O ATOM 2776 N GLY A 360 25.506 -0.168 30.171 1.00 30.07 N ANISOU 2776 N GLY A 360 3739 3807 3881 16 392 -669 N ATOM 2777 CA GLY A 360 25.648 -0.217 31.619 1.00 29.69 C ANISOU 2777 CA GLY A 360 3648 3818 3816 49 356 -673 C ATOM 2778 C GLY A 360 25.136 -1.385 32.469 1.00 30.26 C ANISOU 2778 C GLY A 360 3732 3908 3858 90 326 -628 C ATOM 2779 O GLY A 360 25.617 -1.529 33.588 1.00 30.92 O ANISOU 2779 O GLY A 360 3777 4042 3929 125 298 -636 O ATOM 2780 N SER A 361 24.199 -2.237 32.024 1.00 29.74 N ANISOU 2780 N SER A 361 3719 3803 3778 90 330 -581 N ATOM 2781 CA SER A 361 23.428 -2.164 30.783 1.00 29.03 C ANISOU 2781 CA SER A 361 3680 3657 3694 52 354 -566 C ATOM 2782 C SER A 361 21.962 -2.471 31.116 1.00 29.29 C ANISOU 2782 C SER A 361 3748 3680 3701 48 338 -525 C ATOM 2783 O SER A 361 21.667 -3.150 32.111 1.00 28.74 O ANISOU 2783 O SER A 361 3675 3635 3611 77 319 -501 O ATOM 2784 CB SER A 361 23.952 -3.165 29.747 1.00 29.81 C ANISOU 2784 CB SER A 361 3805 3715 3808 57 378 -556 C ATOM 2785 OG SER A 361 24.215 -4.437 30.327 1.00 31.76 O ANISOU 2785 OG SER A 361 4050 3973 4044 100 366 -529 O ATOM 2786 N THR A 362 21.047 -1.933 30.307 1.00 27.93 N ANISOU 2786 N THR A 362 3608 3474 3529 12 348 -520 N ATOM 2787 CA THR A 362 19.612 -2.100 30.537 1.00 26.46 C ANISOU 2787 CA THR A 362 3449 3280 3324 3 335 -487 C ATOM 2788 C THR A 362 18.970 -2.318 29.193 1.00 24.60 C ANISOU 2788 C THR A 362 3261 2994 3093 -26 349 -474 C ATOM 2789 O THR A 362 19.191 -1.535 28.278 1.00 25.24 O ANISOU 2789 O THR A 362 3353 3054 3185 -49 365 -495 O ATOM 2790 CB THR A 362 19.004 -0.844 31.165 1.00 26.76 C ANISOU 2790 CB THR A 362 3469 3343 3355 -10 323 -501 C ATOM 2791 OG1 THR A 362 19.223 0.263 30.274 1.00 27.63 O ANISOU 2791 OG1 THR A 362 3584 3433 3481 -39 341 -530 O ATOM 2792 CG2 THR A 362 19.656 -0.560 32.518 1.00 27.74 C ANISOU 2792 CG2 THR A 362 3547 3520 3471 16 307 -519 C ATOM 2793 N ALA A 363 18.230 -3.402 29.026 1.00 21.79 N ANISOU 2793 N ALA A 363 2935 2617 2727 -25 346 -441 N ATOM 2794 CA ALA A 363 17.664 -3.664 27.729 1.00 20.14 C ANISOU 2794 CA ALA A 363 2770 2362 2519 -52 356 -433 C ATOM 2795 C ALA A 363 16.327 -4.348 27.859 1.00 19.46 C ANISOU 2795 C ALA A 363 2706 2266 2421 -61 344 -402 C ATOM 2796 O ALA A 363 16.097 -5.082 28.824 1.00 18.96 O ANISOU 2796 O ALA A 363 2635 2220 2350 -42 338 -382 O ATOM 2797 CB ALA A 363 18.638 -4.502 26.855 1.00 18.86 C ANISOU 2797 CB ALA A 363 2629 2169 2368 -47 380 -436 C ATOM 2798 N THR A 364 15.455 -4.072 26.889 1.00 18.28 N ANISOU 2798 N THR A 364 2585 2091 2270 -90 341 -401 N ATOM 2799 CA THR A 364 14.149 -4.700 26.806 1.00 18.02 C ANISOU 2799 CA THR A 364 2572 2046 2230 -105 330 -378 C ATOM 2800 C THR A 364 13.745 -4.888 25.366 1.00 18.44 C ANISOU 2800 C THR A 364 2666 2060 2282 -132 332 -380 C ATOM 2801 O THR A 364 13.870 -3.976 24.539 1.00 18.54 O ANISOU 2801 O THR A 364 2689 2061 2293 -144 332 -397 O ATOM 2802 CB THR A 364 13.050 -3.845 27.494 1.00 18.13 C ANISOU 2802 CB THR A 364 2562 2088 2240 -111 310 -375 C ATOM 2803 OG1 THR A 364 13.381 -3.707 28.870 1.00 18.89 O ANISOU 2803 OG1 THR A 364 2625 2221 2333 -86 308 -373 O ATOM 2804 CG2 THR A 364 11.644 -4.536 27.423 1.00 14.79 C ANISOU 2804 CG2 THR A 364 2152 1654 1814 -129 299 -355 C ATOM 2805 N MET A 365 13.264 -6.083 25.075 1.00 18.50 N ANISOU 2805 N MET A 365 2699 2045 2286 -142 335 -364 N ATOM 2806 CA MET A 365 12.619 -6.358 23.801 1.00 19.43 C ANISOU 2806 CA MET A 365 2855 2130 2399 -171 331 -366 C ATOM 2807 C MET A 365 11.130 -6.512 24.100 1.00 18.63 C ANISOU 2807 C MET A 365 2745 2039 2295 -188 309 -354 C ATOM 2808 O MET A 365 10.777 -7.299 24.971 1.00 20.24 O ANISOU 2808 O MET A 365 2937 2251 2501 -184 314 -339 O ATOM 2809 CB MET A 365 13.181 -7.661 23.191 1.00 18.08 C ANISOU 2809 CB MET A 365 2719 1922 2228 -174 353 -361 C ATOM 2810 CG MET A 365 12.487 -8.023 21.892 1.00 20.34 C ANISOU 2810 CG MET A 365 3049 2175 2505 -206 348 -365 C ATOM 2811 SD MET A 365 13.184 -9.422 20.989 1.00 20.93 S ANISOU 2811 SD MET A 365 3173 2201 2578 -214 379 -364 S ATOM 2812 CE MET A 365 14.614 -8.632 20.266 1.00 22.65 C ANISOU 2812 CE MET A 365 3401 2407 2798 -201 400 -384 C ATOM 2813 N PHE A 366 10.272 -5.744 23.427 1.00 17.56 N ANISOU 2813 N PHE A 366 2614 1904 2154 -205 287 -363 N ATOM 2814 CA PHE A 366 8.840 -5.784 23.733 1.00 18.44 C ANISOU 2814 CA PHE A 366 2708 2031 2268 -220 265 -356 C ATOM 2815 C PHE A 366 8.023 -5.815 22.429 1.00 19.25 C ANISOU 2815 C PHE A 366 2838 2114 2362 -246 244 -365 C ATOM 2816 O PHE A 366 8.462 -5.342 21.397 1.00 20.61 O ANISOU 2816 O PHE A 366 3040 2268 2522 -248 242 -376 O ATOM 2817 CB PHE A 366 8.416 -4.590 24.681 1.00 17.28 C ANISOU 2817 CB PHE A 366 2519 1922 2125 -205 252 -356 C ATOM 2818 CG PHE A 366 8.698 -3.210 24.117 1.00 17.45 C ANISOU 2818 CG PHE A 366 2544 1945 2140 -198 243 -371 C ATOM 2819 CD1 PHE A 366 9.961 -2.631 24.237 1.00 14.83 C ANISOU 2819 CD1 PHE A 366 2213 1613 1809 -182 262 -381 C ATOM 2820 CD2 PHE A 366 7.688 -2.474 23.493 1.00 18.31 C ANISOU 2820 CD2 PHE A 366 2656 2057 2245 -206 218 -375 C ATOM 2821 CE1 PHE A 366 10.208 -1.347 23.749 1.00 14.79 C ANISOU 2821 CE1 PHE A 366 2214 1605 1800 -178 262 -395 C ATOM 2822 CE2 PHE A 366 7.935 -1.191 22.987 1.00 18.52 C ANISOU 2822 CE2 PHE A 366 2692 2080 2264 -196 215 -386 C ATOM 2823 CZ PHE A 366 9.198 -0.622 23.130 1.00 15.71 C ANISOU 2823 CZ PHE A 366 2340 1719 1909 -184 240 -396 C ATOM 2824 N SER A 367 6.812 -6.328 22.472 1.00 20.48 N ANISOU 2824 N SER A 367 2984 2276 2523 -267 228 -362 N ATOM 2825 CA SER A 367 6.083 -6.465 21.227 1.00 20.94 C ANISOU 2825 CA SER A 367 3067 2318 2570 -291 204 -374 C ATOM 2826 C SER A 367 4.866 -5.557 21.219 1.00 20.73 C ANISOU 2826 C SER A 367 3011 2320 2546 -292 168 -379 C ATOM 2827 O SER A 367 4.273 -5.299 22.283 1.00 20.97 O ANISOU 2827 O SER A 367 2999 2378 2592 -286 167 -372 O ATOM 2828 CB SER A 367 5.706 -7.942 21.003 1.00 20.74 C ANISOU 2828 CB SER A 367 3060 2270 2550 -320 214 -374 C ATOM 2829 OG SER A 367 5.042 -8.090 19.762 1.00 24.07 O ANISOU 2829 OG SER A 367 3507 2679 2959 -345 188 -390 O ATOM 2830 N LEU A 368 4.548 -5.039 20.024 1.00 21.09 N ANISOU 2830 N LEU A 368 3082 2357 2574 -296 142 -391 N ATOM 2831 CA LEU A 368 3.357 -4.234 19.738 1.00 21.67 C ANISOU 2831 CA LEU A 368 3134 2454 2645 -294 102 -397 C ATOM 2832 C LEU A 368 2.474 -4.882 18.679 1.00 23.97 C ANISOU 2832 C LEU A 368 3442 2738 2927 -321 71 -411 C ATOM 2833 O LEU A 368 2.968 -5.523 17.741 1.00 24.12 O ANISOU 2833 O LEU A 368 3509 2728 2929 -336 77 -418 O ATOM 2834 CB LEU A 368 3.747 -2.820 19.215 1.00 20.03 C ANISOU 2834 CB LEU A 368 2945 2245 2419 -267 93 -398 C ATOM 2835 CG LEU A 368 4.808 -2.029 20.017 1.00 18.52 C ANISOU 2835 CG LEU A 368 2746 2057 2235 -243 124 -392 C ATOM 2836 CD1 LEU A 368 5.343 -0.768 19.240 1.00 18.67 C ANISOU 2836 CD1 LEU A 368 2799 2061 2234 -223 125 -396 C ATOM 2837 CD2 LEU A 368 4.247 -1.663 21.403 1.00 15.03 C ANISOU 2837 CD2 LEU A 368 2247 1649 1814 -233 125 -384 C ATOM 2838 N ARG A 369 1.175 -4.646 18.795 1.00 25.45 N ANISOU 2838 N ARG A 369 3590 2955 3125 -327 37 -417 N ATOM 2839 CA ARG A 369 0.232 -5.016 17.743 1.00 28.23 C ANISOU 2839 CA ARG A 369 3951 3309 3465 -348 -3 -435 C ATOM 2840 C ARG A 369 -0.360 -3.742 17.231 1.00 28.51 C ANISOU 2840 C ARG A 369 3981 3366 3487 -320 -44 -438 C ATOM 2841 O ARG A 369 -0.845 -2.931 18.019 1.00 27.69 O ANISOU 2841 O ARG A 369 3832 3289 3399 -299 -50 -431 O ATOM 2842 CB ARG A 369 -0.897 -5.891 18.294 1.00 28.48 C ANISOU 2842 CB ARG A 369 3935 3361 3527 -380 -10 -445 C ATOM 2843 CG ARG A 369 -0.431 -7.281 18.559 1.00 34.02 C ANISOU 2843 CG ARG A 369 4655 4035 4238 -410 29 -445 C ATOM 2844 CD ARG A 369 -1.288 -8.340 17.826 1.00 36.89 C ANISOU 2844 CD ARG A 369 5022 4392 4604 -454 11 -470 C ATOM 2845 NE ARG A 369 -1.008 -8.419 16.407 1.00 34.65 N ANISOU 2845 NE ARG A 369 4792 4089 4287 -460 -13 -484 N ATOM 2846 CZ ARG A 369 -0.531 -9.504 15.790 1.00 37.82 C ANISOU 2846 CZ ARG A 369 5239 4454 4677 -489 7 -493 C ATOM 2847 NH1 ARG A 369 -0.231 -10.611 16.467 1.00 35.06 N ANISOU 2847 NH1 ARG A 369 4891 4082 4348 -511 53 -488 N ATOM 2848 NH2 ARG A 369 -0.352 -9.486 14.476 1.00 37.00 N ANISOU 2848 NH2 ARG A 369 5186 4334 4539 -493 -17 -508 N ATOM 2849 N LEU A 370 -0.310 -3.556 15.922 1.00 29.32 N ANISOU 2849 N LEU A 370 4130 3454 3555 -317 -71 -447 N ATOM 2850 CA LEU A 370 -0.875 -2.362 15.333 1.00 31.05 C ANISOU 2850 CA LEU A 370 4353 3690 3755 -285 -112 -448 C ATOM 2851 C LEU A 370 -2.297 -2.653 14.803 1.00 33.13 C ANISOU 2851 C LEU A 370 4586 3984 4019 -298 -168 -467 C ATOM 2852 O LEU A 370 -2.604 -3.774 14.380 1.00 31.99 O ANISOU 2852 O LEU A 370 4446 3835 3875 -336 -177 -485 O ATOM 2853 CB LEU A 370 0.046 -1.779 14.261 1.00 30.90 C ANISOU 2853 CB LEU A 370 4408 3638 3695 -266 -106 -444 C ATOM 2854 CG LEU A 370 1.539 -1.430 14.532 1.00 31.25 C ANISOU 2854 CG LEU A 370 4487 3650 3736 -254 -51 -430 C ATOM 2855 CD1 LEU A 370 1.827 -0.071 14.019 1.00 29.58 C ANISOU 2855 CD1 LEU A 370 4310 3429 3499 -218 -54 -423 C ATOM 2856 CD2 LEU A 370 2.055 -1.527 15.978 1.00 25.51 C ANISOU 2856 CD2 LEU A 370 3715 2932 3045 -255 -10 -420 C ATOM 2857 N CYS A 371 -3.148 -1.629 14.851 1.00 34.53 N ANISOU 2857 N CYS A 371 4731 4192 4197 -267 -204 -465 N ATOM 2858 CA CYS A 371 -4.591 -1.772 14.705 1.00 37.47 C ANISOU 2858 CA CYS A 371 5051 4604 4583 -274 -256 -484 C ATOM 2859 C CYS A 371 -5.171 -0.615 13.921 1.00 37.85 C ANISOU 2859 C CYS A 371 5109 4670 4603 -229 -308 -483 C ATOM 2860 O CYS A 371 -4.691 0.526 14.027 1.00 37.13 O ANISOU 2860 O CYS A 371 5041 4569 4499 -188 -294 -463 O ATOM 2861 CB CYS A 371 -5.260 -1.766 16.083 1.00 36.99 C ANISOU 2861 CB CYS A 371 4910 4571 4571 -279 -240 -482 C ATOM 2862 SG CYS A 371 -4.795 -3.155 17.127 1.00 45.67 S ANISOU 2862 SG CYS A 371 5994 5654 5704 -328 -181 -481 S ATOM 2863 N GLU A 372 -6.220 -0.912 13.160 1.00 39.51 N ANISOU 2863 N GLU A 372 5301 4907 4804 -236 -366 -506 N ATOM 2864 CA GLU A 372 -7.001 0.114 12.475 1.00 41.75 C ANISOU 2864 CA GLU A 372 5583 5217 5063 -189 -424 -507 C ATOM 2865 C GLU A 372 -7.763 0.884 13.538 1.00 41.42 C ANISOU 2865 C GLU A 372 5466 5208 5062 -163 -425 -498 C ATOM 2866 O GLU A 372 -8.291 0.292 14.471 1.00 41.52 O ANISOU 2866 O GLU A 372 5412 5242 5122 -193 -410 -508 O ATOM 2867 CB GLU A 372 -7.968 -0.522 11.461 1.00 42.71 C ANISOU 2867 CB GLU A 372 5695 5365 5168 -206 -490 -538 C ATOM 2868 CG GLU A 372 -9.245 0.285 11.229 1.00 47.31 C ANISOU 2868 CG GLU A 372 6227 5997 5752 -165 -557 -546 C ATOM 2869 CD GLU A 372 -9.734 0.224 9.798 1.00 54.77 C ANISOU 2869 CD GLU A 372 7208 6955 6646 -152 -628 -566 C ATOM 2870 OE1 GLU A 372 -10.968 0.081 9.590 1.00 56.19 O ANISOU 2870 OE1 GLU A 372 7325 7184 6839 -152 -688 -593 O ATOM 2871 OE2 GLU A 372 -8.881 0.329 8.876 1.00 57.66 O ANISOU 2871 OE2 GLU A 372 7664 7284 6958 -142 -622 -556 O ATOM 2872 N ASN A 373 -7.788 2.203 13.419 1.00 41.92 N ANISOU 2872 N ASN A 373 5545 5273 5107 -107 -436 -479 N ATOM 2873 CA ASN A 373 -8.444 3.038 14.414 1.00 42.02 C ANISOU 2873 CA ASN A 373 5494 5314 5157 -77 -432 -470 C ATOM 2874 C ASN A 373 -8.872 4.287 13.692 1.00 42.72 C ANISOU 2874 C ASN A 373 5606 5412 5213 -14 -475 -459 C ATOM 2875 O ASN A 373 -8.337 4.581 12.634 1.00 42.55 O ANISOU 2875 O ASN A 373 5661 5364 5141 6 -488 -452 O ATOM 2876 CB ASN A 373 -7.434 3.395 15.499 1.00 41.88 C ANISOU 2876 CB ASN A 373 5487 5269 5157 -78 -362 -448 C ATOM 2877 CG ASN A 373 -8.041 3.447 16.883 1.00 43.51 C ANISOU 2877 CG ASN A 373 5614 5503 5417 -85 -339 -448 C ATOM 2878 OD1 ASN A 373 -8.882 2.622 17.232 1.00 47.65 O ANISOU 2878 OD1 ASN A 373 6077 6055 5974 -117 -352 -467 O ATOM 2879 ND2 ASN A 373 -7.586 4.406 17.700 1.00 44.79 N ANISOU 2879 ND2 ASN A 373 5777 5655 5587 -57 -301 -429 N ATOM 2880 N GLN A 374 -9.828 5.034 14.230 1.00 43.45 N ANISOU 2880 N GLN A 374 5637 5539 5333 21 -495 -457 N ATOM 2881 CA GLN A 374 -10.214 6.266 13.556 1.00 45.31 C ANISOU 2881 CA GLN A 374 5900 5779 5536 88 -534 -444 C ATOM 2882 C GLN A 374 -9.237 7.383 13.909 1.00 43.52 C ANISOU 2882 C GLN A 374 5728 5511 5296 122 -479 -414 C ATOM 2883 O GLN A 374 -8.625 7.378 14.968 1.00 43.34 O ANISOU 2883 O GLN A 374 5690 5473 5303 100 -420 -407 O ATOM 2884 CB GLN A 374 -11.672 6.657 13.844 1.00 46.23 C ANISOU 2884 CB GLN A 374 5931 5950 5686 119 -582 -455 C ATOM 2885 CG GLN A 374 -11.976 7.210 15.266 1.00 48.90 C ANISOU 2885 CG GLN A 374 6203 6300 6077 128 -540 -446 C ATOM 2886 CD GLN A 374 -13.483 7.279 15.543 1.00 49.51 C ANISOU 2886 CD GLN A 374 6183 6434 6195 145 -586 -465 C ATOM 2887 OE1 GLN A 374 -14.047 8.356 15.763 1.00 54.47 O ANISOU 2887 OE1 GLN A 374 6789 7077 6832 202 -597 -453 O ATOM 2888 NE2 GLN A 374 -14.145 6.121 15.502 1.00 53.64 N ANISOU 2888 NE2 GLN A 374 6649 6988 6744 96 -612 -496 N ATOM 2889 N SER A 375 -9.056 8.295 12.970 1.00 42.64 N ANISOU 2889 N SER A 375 5686 5380 5136 172 -498 -398 N ATOM 2890 CA SER A 375 -8.351 9.542 13.188 1.00 41.39 C ANISOU 2890 CA SER A 375 5578 5184 4963 212 -453 -372 C ATOM 2891 C SER A 375 -8.994 10.305 14.371 1.00 40.34 C ANISOU 2891 C SER A 375 5376 5074 4877 237 -436 -366 C ATOM 2892 O SER A 375 -10.199 10.167 14.621 1.00 40.85 O ANISOU 2892 O SER A 375 5364 5185 4970 248 -479 -378 O ATOM 2893 CB SER A 375 -8.370 10.344 11.877 1.00 41.80 C ANISOU 2893 CB SER A 375 5712 5217 4954 268 -487 -358 C ATOM 2894 OG SER A 375 -7.887 11.663 12.032 1.00 43.48 O ANISOU 2894 OG SER A 375 5973 5394 5154 314 -446 -334 O ATOM 2895 N PRO A 376 -8.200 11.109 15.113 1.00 38.67 N ANISOU 2895 N PRO A 376 5188 4831 4675 246 -373 -350 N ATOM 2896 CA PRO A 376 -6.820 11.498 14.849 1.00 37.10 C ANISOU 2896 CA PRO A 376 5073 4577 4446 240 -320 -338 C ATOM 2897 C PRO A 376 -5.777 10.452 15.273 1.00 35.52 C ANISOU 2897 C PRO A 376 4876 4362 4259 176 -277 -348 C ATOM 2898 O PRO A 376 -4.602 10.599 14.943 1.00 35.32 O ANISOU 2898 O PRO A 376 4917 4293 4209 166 -236 -343 O ATOM 2899 CB PRO A 376 -6.675 12.779 15.672 1.00 37.40 C ANISOU 2899 CB PRO A 376 5109 4599 4500 274 -275 -324 C ATOM 2900 CG PRO A 376 -7.489 12.486 16.908 1.00 37.79 C ANISOU 2900 CG PRO A 376 5061 4692 4604 260 -277 -333 C ATOM 2901 CD PRO A 376 -8.702 11.702 16.378 1.00 38.27 C ANISOU 2901 CD PRO A 376 5070 4799 4670 259 -348 -347 C ATOM 2902 N PHE A 377 -6.221 9.420 15.984 1.00 33.74 N ANISOU 2902 N PHE A 377 4579 4169 4071 135 -285 -363 N ATOM 2903 CA PHE A 377 -5.342 8.399 16.570 1.00 32.07 C ANISOU 2903 CA PHE A 377 4361 3946 3877 79 -244 -371 C ATOM 2904 C PHE A 377 -5.340 7.143 15.686 1.00 31.27 C ANISOU 2904 C PHE A 377 4277 3846 3759 44 -275 -385 C ATOM 2905 O PHE A 377 -5.772 6.068 16.107 1.00 31.43 O ANISOU 2905 O PHE A 377 4245 3890 3806 5 -283 -399 O ATOM 2906 CB PHE A 377 -5.767 8.069 18.038 1.00 30.16 C ANISOU 2906 CB PHE A 377 4038 3735 3688 57 -222 -377 C ATOM 2907 CG PHE A 377 -5.802 9.283 18.986 1.00 30.38 C ANISOU 2907 CG PHE A 377 4047 3763 3734 90 -190 -366 C ATOM 2908 CD1 PHE A 377 -6.728 9.337 20.034 1.00 30.92 C ANISOU 2908 CD1 PHE A 377 4039 3866 3843 92 -191 -370 C ATOM 2909 CD2 PHE A 377 -4.914 10.338 18.850 1.00 28.69 C ANISOU 2909 CD2 PHE A 377 3891 3512 3498 114 -155 -354 C ATOM 2910 CE1 PHE A 377 -6.756 10.417 20.916 1.00 30.70 C ANISOU 2910 CE1 PHE A 377 3996 3836 3831 119 -159 -362 C ATOM 2911 CE2 PHE A 377 -4.937 11.428 19.719 1.00 29.30 C ANISOU 2911 CE2 PHE A 377 3953 3587 3591 140 -123 -348 C ATOM 2912 CZ PHE A 377 -5.875 11.471 20.745 1.00 29.75 C ANISOU 2912 CZ PHE A 377 3937 3680 3688 144 -126 -351 C ATOM 2913 N SER A 378 -4.840 7.306 14.464 1.00 31.36 N ANISOU 2913 N SER A 378 4365 3828 3722 57 -286 -381 N ATOM 2914 CA SER A 378 -4.792 6.268 13.453 1.00 30.99 C ANISOU 2914 CA SER A 378 4349 3776 3648 29 -315 -395 C ATOM 2915 C SER A 378 -3.382 6.273 12.913 1.00 30.26 C ANISOU 2915 C SER A 378 4339 3633 3525 18 -270 -388 C ATOM 2916 O SER A 378 -2.702 7.314 12.944 1.00 30.34 O ANISOU 2916 O SER A 378 4392 3614 3523 45 -234 -373 O ATOM 2917 CB SER A 378 -5.771 6.592 12.314 1.00 31.89 C ANISOU 2917 CB SER A 378 4480 3910 3727 65 -385 -398 C ATOM 2918 OG SER A 378 -5.334 7.722 11.554 1.00 32.50 O ANISOU 2918 OG SER A 378 4635 3954 3759 113 -380 -380 O ATOM 2919 N LEU A 379 -2.934 5.128 12.419 1.00 29.09 N ANISOU 2919 N LEU A 379 4215 3472 3367 -23 -268 -400 N ATOM 2920 CA LEU A 379 -1.613 5.020 11.810 1.00 29.06 C ANISOU 2920 CA LEU A 379 4288 3419 3333 -35 -225 -397 C ATOM 2921 C LEU A 379 -1.420 6.020 10.652 1.00 30.10 C ANISOU 2921 C LEU A 379 4502 3522 3412 8 -234 -385 C ATOM 2922 O LEU A 379 -0.360 6.643 10.526 1.00 29.04 O ANISOU 2922 O LEU A 379 4422 3346 3264 16 -183 -376 O ATOM 2923 CB LEU A 379 -1.347 3.559 11.362 1.00 28.62 C ANISOU 2923 CB LEU A 379 4245 3357 3274 -83 -228 -413 C ATOM 2924 CG LEU A 379 -1.446 2.539 12.524 1.00 27.71 C ANISOU 2924 CG LEU A 379 4057 3261 3208 -123 -210 -421 C ATOM 2925 CD1 LEU A 379 -1.580 1.074 12.070 1.00 27.36 C ANISOU 2925 CD1 LEU A 379 4015 3217 3163 -168 -223 -440 C ATOM 2926 CD2 LEU A 379 -0.267 2.713 13.497 1.00 27.86 C ANISOU 2926 CD2 LEU A 379 4073 3259 3252 -130 -144 -411 C ATOM 2927 N SER A 380 -2.439 6.156 9.804 1.00 31.01 N ANISOU 2927 N SER A 380 4627 3659 3497 34 -298 -388 N ATOM 2928 CA SER A 380 -2.360 7.066 8.652 1.00 32.11 C ANISOU 2928 CA SER A 380 4851 3771 3579 80 -312 -375 C ATOM 2929 C SER A 380 -2.254 8.508 9.081 1.00 31.00 C ANISOU 2929 C SER A 380 4721 3617 3442 126 -285 -355 C ATOM 2930 O SER A 380 -1.398 9.241 8.599 1.00 31.56 O ANISOU 2930 O SER A 380 4868 3640 3482 144 -243 -342 O ATOM 2931 CB SER A 380 -3.544 6.842 7.704 1.00 32.69 C ANISOU 2931 CB SER A 380 4926 3878 3618 101 -395 -385 C ATOM 2932 OG SER A 380 -3.480 5.497 7.215 1.00 35.87 O ANISOU 2932 OG SER A 380 5332 4284 4013 52 -412 -407 O ATOM 2933 N ASN A 381 -3.090 8.918 10.022 1.00 31.12 N ANISOU 2933 N ASN A 381 4659 3669 3495 143 -301 -352 N ATOM 2934 CA ASN A 381 -2.975 10.268 10.511 1.00 31.19 C ANISOU 2934 CA ASN A 381 4678 3663 3511 184 -269 -334 C ATOM 2935 C ASN A 381 -1.679 10.550 11.293 1.00 30.22 C ANISOU 2935 C ASN A 381 4566 3504 3412 159 -188 -332 C ATOM 2936 O ASN A 381 -1.155 11.660 11.238 1.00 30.69 O ANISOU 2936 O ASN A 381 4674 3528 3458 187 -148 -320 O ATOM 2937 CB ASN A 381 -4.191 10.683 11.310 1.00 31.87 C ANISOU 2937 CB ASN A 381 4681 3795 3631 212 -304 -332 C ATOM 2938 CG ASN A 381 -4.174 12.135 11.616 1.00 32.86 C ANISOU 2938 CG ASN A 381 4827 3902 3756 262 -276 -313 C ATOM 2939 OD1 ASN A 381 -4.112 12.965 10.701 1.00 33.17 O ANISOU 2939 OD1 ASN A 381 4942 3912 3748 307 -281 -298 O ATOM 2940 ND2 ASN A 381 -4.220 12.474 12.905 1.00 34.44 N ANISOU 2940 ND2 ASN A 381 4965 4115 4004 255 -244 -314 N ATOM 2941 N ILE A 382 -1.132 9.542 11.972 1.00 29.36 N ANISOU 2941 N ILE A 382 4417 3402 3337 107 -163 -346 N ATOM 2942 CA ILE A 382 0.170 9.716 12.618 1.00 27.60 C ANISOU 2942 CA ILE A 382 4205 3148 3133 83 -91 -347 C ATOM 2943 C ILE A 382 1.232 10.006 11.551 1.00 28.59 C ANISOU 2943 C ILE A 382 4428 3220 3217 84 -55 -344 C ATOM 2944 O ILE A 382 2.018 10.950 11.706 1.00 28.05 O ANISOU 2944 O ILE A 382 4393 3116 3148 95 -2 -340 O ATOM 2945 CB ILE A 382 0.556 8.515 13.526 1.00 27.03 C ANISOU 2945 CB ILE A 382 4075 3095 3101 32 -74 -361 C ATOM 2946 CG1 ILE A 382 -0.391 8.458 14.751 1.00 26.95 C ANISOU 2946 CG1 ILE A 382 3974 3132 3134 33 -93 -362 C ATOM 2947 CG2 ILE A 382 2.023 8.623 13.997 1.00 23.50 C ANISOU 2947 CG2 ILE A 382 3646 2615 2666 10 -5 -365 C ATOM 2948 CD1 ILE A 382 -0.268 7.180 15.664 1.00 25.79 C ANISOU 2948 CD1 ILE A 382 3768 3008 3024 -13 -84 -372 C ATOM 2949 N ALA A 383 1.220 9.234 10.460 1.00 28.37 N ANISOU 2949 N ALA A 383 4443 3182 3154 73 -82 -349 N ATOM 2950 CA ALA A 383 2.208 9.409 9.363 1.00 30.22 C ANISOU 2950 CA ALA A 383 4775 3363 3346 73 -46 -347 C ATOM 2951 C ALA A 383 2.085 10.795 8.734 1.00 30.57 C ANISOU 2951 C ALA A 383 4887 3377 3352 124 -39 -330 C ATOM 2952 O ALA A 383 3.080 11.460 8.428 1.00 30.96 O ANISOU 2952 O ALA A 383 4999 3376 3387 126 21 -326 O ATOM 2953 CB ALA A 383 2.030 8.321 8.291 1.00 30.05 C ANISOU 2953 CB ALA A 383 4788 3341 3289 55 -84 -355 C ATOM 2954 N SER A 384 0.851 11.234 8.578 1.00 31.47 N ANISOU 2954 N SER A 384 4984 3520 3451 166 -98 -319 N ATOM 2955 CA SER A 384 0.567 12.541 7.989 1.00 32.53 C ANISOU 2955 CA SER A 384 5182 3630 3548 224 -98 -299 C ATOM 2956 C SER A 384 1.035 13.684 8.889 1.00 32.57 C ANISOU 2956 C SER A 384 5178 3613 3583 236 -37 -293 C ATOM 2957 O SER A 384 1.720 14.605 8.429 1.00 31.90 O ANISOU 2957 O SER A 384 5172 3476 3473 255 14 -283 O ATOM 2958 CB SER A 384 -0.920 12.644 7.706 1.00 32.43 C ANISOU 2958 CB SER A 384 5141 3663 3519 268 -181 -292 C ATOM 2959 OG SER A 384 -1.231 13.946 7.304 1.00 38.04 O ANISOU 2959 OG SER A 384 5905 4350 4198 330 -180 -270 O ATOM 2960 N VAL A 385 0.682 13.613 10.180 1.00 32.52 N ANISOU 2960 N VAL A 385 5079 3645 3631 223 -39 -299 N ATOM 2961 CA VAL A 385 1.087 14.639 11.136 1.00 32.44 C ANISOU 2961 CA VAL A 385 5054 3620 3652 230 17 -298 C ATOM 2962 C VAL A 385 2.617 14.747 11.236 1.00 31.80 C ANISOU 2962 C VAL A 385 5011 3492 3579 193 96 -309 C ATOM 2963 O VAL A 385 3.168 15.848 11.169 1.00 31.59 O ANISOU 2963 O VAL A 385 5036 3423 3545 209 150 -305 O ATOM 2964 CB VAL A 385 0.444 14.393 12.523 1.00 32.23 C ANISOU 2964 CB VAL A 385 4921 3646 3681 219 0 -305 C ATOM 2965 CG1 VAL A 385 1.153 15.210 13.614 1.00 32.89 C ANISOU 2965 CG1 VAL A 385 4985 3712 3798 209 65 -311 C ATOM 2966 CG2 VAL A 385 -1.048 14.705 12.462 1.00 32.65 C ANISOU 2966 CG2 VAL A 385 4940 3737 3729 266 -66 -293 C ATOM 2967 N MET A 386 3.305 13.614 11.377 1.00 30.72 N ANISOU 2967 N MET A 386 4851 3363 3459 143 106 -326 N ATOM 2968 CA MET A 386 4.770 13.638 11.528 1.00 30.24 C ANISOU 2968 CA MET A 386 4815 3264 3412 107 179 -340 C ATOM 2969 C MET A 386 5.509 14.220 10.306 1.00 30.17 C ANISOU 2969 C MET A 386 4913 3193 3359 118 222 -336 C ATOM 2970 O MET A 386 6.617 14.722 10.445 1.00 30.40 O ANISOU 2970 O MET A 386 4968 3183 3399 99 291 -347 O ATOM 2971 CB MET A 386 5.359 12.255 11.857 1.00 29.05 C ANISOU 2971 CB MET A 386 4621 3133 3285 58 180 -357 C ATOM 2972 CG MET A 386 4.914 11.613 13.163 1.00 28.14 C ANISOU 2972 CG MET A 386 4407 3071 3216 40 156 -363 C ATOM 2973 SD MET A 386 5.904 10.138 13.540 1.00 30.41 S ANISOU 2973 SD MET A 386 4660 3365 3529 -13 176 -381 S ATOM 2974 CE MET A 386 5.502 9.124 12.109 1.00 25.17 C ANISOU 2974 CE MET A 386 4049 2693 2823 -18 133 -377 C ATOM 2975 N ASP A 387 4.932 14.102 9.112 1.00 31.75 N ANISOU 2975 N ASP A 387 5174 3382 3507 145 181 -321 N ATOM 2976 CA ASP A 387 5.473 14.784 7.898 1.00 31.90 C ANISOU 2976 CA ASP A 387 5307 3340 3476 165 220 -312 C ATOM 2977 C ASP A 387 6.982 14.599 7.745 1.00 32.00 C ANISOU 2977 C ASP A 387 5353 3307 3498 121 298 -331 C ATOM 2978 O ASP A 387 7.735 15.552 7.501 1.00 32.24 O ANISOU 2978 O ASP A 387 5444 3286 3522 126 366 -332 O ATOM 2979 CB ASP A 387 5.109 16.280 7.942 1.00 32.53 C ANISOU 2979 CB ASP A 387 5425 3395 3542 214 240 -295 C ATOM 2980 CG ASP A 387 5.086 16.939 6.553 1.00 35.69 C ANISOU 2980 CG ASP A 387 5944 3742 3874 255 249 -275 C ATOM 2981 OD1 ASP A 387 4.884 16.224 5.541 1.00 38.18 O ANISOU 2981 OD1 ASP A 387 6303 4057 4146 259 210 -271 O ATOM 2982 OD2 ASP A 387 5.266 18.183 6.488 1.00 37.70 O ANISOU 2982 OD2 ASP A 387 6254 3954 4118 285 297 -264 O ATOM 2983 N VAL A 388 7.425 13.356 7.921 1.00 31.77 N ANISOU 2983 N VAL A 388 5282 3297 3490 79 292 -347 N ATOM 2984 CA VAL A 388 8.842 13.026 7.935 1.00 32.02 C ANISOU 2984 CA VAL A 388 5326 3298 3543 36 361 -367 C ATOM 2985 C VAL A 388 9.484 13.366 6.567 1.00 32.41 C ANISOU 2985 C VAL A 388 5489 3282 3542 42 405 -364 C ATOM 2986 O VAL A 388 10.616 13.854 6.509 1.00 31.47 O ANISOU 2986 O VAL A 388 5403 3118 3436 22 483 -378 O ATOM 2987 CB VAL A 388 9.063 11.517 8.329 1.00 30.97 C ANISOU 2987 CB VAL A 388 5129 3201 3439 -4 337 -382 C ATOM 2988 CG1 VAL A 388 10.414 11.020 7.830 1.00 30.38 C ANISOU 2988 CG1 VAL A 388 5092 3085 3366 -39 399 -399 C ATOM 2989 CG2 VAL A 388 8.923 11.306 9.874 1.00 31.33 C ANISOU 2989 CG2 VAL A 388 5066 3296 3541 -19 326 -391 C ATOM 2990 N GLY A 389 8.730 13.125 5.490 1.00 33.81 N ANISOU 2990 N GLY A 389 5726 3456 3664 69 356 -347 N ATOM 2991 CA GLY A 389 9.125 13.528 4.132 1.00 35.24 C ANISOU 2991 CA GLY A 389 6028 3577 3787 84 390 -338 C ATOM 2992 C GLY A 389 9.423 15.013 4.028 1.00 35.85 C ANISOU 2992 C GLY A 389 6166 3604 3852 112 450 -329 C ATOM 2993 O GLY A 389 10.522 15.409 3.646 1.00 36.42 O ANISOU 2993 O GLY A 389 6296 3620 3922 92 531 -339 O ATOM 2994 N GLY A 390 8.441 15.832 4.395 1.00 36.33 N ANISOU 2994 N GLY A 390 6211 3685 3907 156 413 -310 N ATOM 2995 CA GLY A 390 8.601 17.283 4.527 1.00 35.66 C ANISOU 2995 CA GLY A 390 6172 3558 3820 183 468 -301 C ATOM 2996 C GLY A 390 9.763 17.764 5.381 1.00 35.11 C ANISOU 2996 C GLY A 390 6070 3464 3806 142 554 -326 C ATOM 2997 O GLY A 390 10.496 18.649 4.969 1.00 35.42 O ANISOU 2997 O GLY A 390 6183 3440 3834 142 632 -329 O ATOM 2998 N LYS A 391 9.941 17.202 6.574 1.00 33.95 N ANISOU 2998 N LYS A 391 5814 3366 3720 107 544 -347 N ATOM 2999 CA LYS A 391 11.043 17.621 7.460 1.00 32.99 C ANISOU 2999 CA LYS A 391 5653 3230 3653 67 619 -376 C ATOM 3000 C LYS A 391 12.415 17.337 6.824 1.00 33.39 C ANISOU 3000 C LYS A 391 5752 3232 3705 26 693 -398 C ATOM 3001 O LYS A 391 13.370 18.122 6.939 1.00 31.96 O ANISOU 3001 O LYS A 391 5593 3006 3543 6 775 -417 O ATOM 3002 CB LYS A 391 10.916 16.931 8.823 1.00 32.74 C ANISOU 3002 CB LYS A 391 5498 3265 3677 41 583 -392 C ATOM 3003 CG LYS A 391 9.908 17.619 9.751 1.00 32.25 C ANISOU 3003 CG LYS A 391 5384 3238 3632 72 547 -380 C ATOM 3004 CD LYS A 391 9.369 16.686 10.872 1.00 31.67 C ANISOU 3004 CD LYS A 391 5199 3238 3597 57 487 -386 C ATOM 3005 CE LYS A 391 8.142 17.356 11.551 1.00 33.02 C ANISOU 3005 CE LYS A 391 5332 3441 3774 97 444 -369 C ATOM 3006 NZ LYS A 391 7.357 16.389 12.380 1.00 34.23 N ANISOU 3006 NZ LYS A 391 5392 3662 3952 90 378 -368 N ATOM 3007 N LEU A 392 12.478 16.214 6.107 1.00 33.92 N ANISOU 3007 N LEU A 392 5834 3304 3749 15 664 -395 N ATOM 3008 CA LEU A 392 13.707 15.805 5.467 1.00 35.17 C ANISOU 3008 CA LEU A 392 6035 3420 3908 -22 729 -415 C ATOM 3009 C LEU A 392 14.032 16.685 4.267 1.00 37.22 C ANISOU 3009 C LEU A 392 6422 3604 4118 -4 790 -405 C ATOM 3010 O LEU A 392 15.201 16.978 4.029 1.00 37.39 O ANISOU 3010 O LEU A 392 6476 3576 4155 -35 877 -427 O ATOM 3011 CB LEU A 392 13.647 14.334 5.088 1.00 34.34 C ANISOU 3011 CB LEU A 392 5911 3343 3795 -38 683 -416 C ATOM 3012 CG LEU A 392 13.661 13.360 6.283 1.00 33.11 C ANISOU 3012 CG LEU A 392 5635 3251 3694 -65 646 -431 C ATOM 3013 CD1 LEU A 392 13.407 11.944 5.746 1.00 31.00 C ANISOU 3013 CD1 LEU A 392 5367 3004 3409 -75 597 -427 C ATOM 3014 CD2 LEU A 392 14.975 13.400 7.054 1.00 28.41 C ANISOU 3014 CD2 LEU A 392 4988 2650 3157 -106 714 -465 C ATOM 3015 N LYS A 393 13.006 17.109 3.536 1.00 39.41 N ANISOU 3015 N LYS A 393 6768 3872 4335 47 746 -372 N ATOM 3016 CA LYS A 393 13.185 18.025 2.404 1.00 42.86 C ANISOU 3016 CA LYS A 393 7335 4235 4715 74 799 -356 C ATOM 3017 C LYS A 393 13.606 19.422 2.863 1.00 42.86 C ANISOU 3017 C LYS A 393 7354 4192 4738 77 876 -362 C ATOM 3018 O LYS A 393 14.310 20.102 2.125 1.00 43.97 O ANISOU 3018 O LYS A 393 7590 4260 4856 73 959 -365 O ATOM 3019 CB LYS A 393 11.917 18.137 1.542 1.00 43.09 C ANISOU 3019 CB LYS A 393 7432 4270 4671 135 724 -318 C ATOM 3020 CG LYS A 393 11.502 16.840 0.835 1.00 46.35 C ANISOU 3020 CG LYS A 393 7849 4714 5049 133 654 -314 C ATOM 3021 CD LYS A 393 10.308 17.050 -0.132 1.00 47.32 C ANISOU 3021 CD LYS A 393 8047 4839 5092 196 582 -280 C ATOM 3022 CE LYS A 393 8.977 17.336 0.625 1.00 51.94 C ANISOU 3022 CE LYS A 393 8558 5487 5689 238 497 -264 C ATOM 3023 NZ LYS A 393 8.127 16.086 0.809 1.00 53.16 N ANISOU 3023 NZ LYS A 393 8634 5716 5850 230 398 -268 N ATOM 3024 N ALA A 394 13.205 19.828 4.074 1.00 42.45 N ANISOU 3024 N ALA A 394 7215 4181 4732 80 855 -368 N ATOM 3025 CA ALA A 394 13.447 21.188 4.589 1.00 42.71 C ANISOU 3025 CA ALA A 394 7263 4178 4786 85 920 -374 C ATOM 3026 C ALA A 394 14.767 21.384 5.343 1.00 42.46 C ANISOU 3026 C ALA A 394 7180 4131 4820 24 1005 -419 C ATOM 3027 O ALA A 394 14.942 22.380 6.048 1.00 44.03 O ANISOU 3027 O ALA A 394 7364 4316 5050 19 1050 -432 O ATOM 3028 CB ALA A 394 12.253 21.656 5.477 1.00 42.10 C ANISOU 3028 CB ALA A 394 7126 4150 4720 125 855 -356 C ATOM 3029 N ARG A 395 15.692 20.447 5.208 1.00 42.26 N ANISOU 3029 N ARG A 395 7128 4110 4817 -22 1026 -444 N ATOM 3030 CA ARG A 395 16.990 20.513 5.892 1.00 41.83 C ANISOU 3030 CA ARG A 395 7017 4049 4827 -80 1100 -491 C ATOM 3031 C ARG A 395 17.966 21.516 5.246 1.00 42.01 C ANISOU 3031 C ARG A 395 7130 3986 4846 -99 1216 -508 C ATOM 3032 O ARG A 395 17.779 21.916 4.108 1.00 42.76 O ANISOU 3032 O ARG A 395 7340 4023 4883 -72 1242 -483 O ATOM 3033 CB ARG A 395 17.638 19.129 5.905 1.00 41.16 C ANISOU 3033 CB ARG A 395 6875 3998 4767 -116 1084 -510 C ATOM 3034 CG ARG A 395 16.919 18.111 6.785 1.00 41.25 C ANISOU 3034 CG ARG A 395 6782 4093 4799 -111 987 -503 C ATOM 3035 CD ARG A 395 17.660 16.786 6.722 1.00 40.06 C ANISOU 3035 CD ARG A 395 6587 3964 4670 -146 982 -522 C ATOM 3036 NE ARG A 395 17.459 16.088 5.449 1.00 40.63 N ANISOU 3036 NE ARG A 395 6737 4010 4689 -133 966 -501 N ATOM 3037 CZ ARG A 395 18.055 14.939 5.129 1.00 40.94 C ANISOU 3037 CZ ARG A 395 6762 4056 4737 -159 967 -514 C ATOM 3038 NH1 ARG A 395 18.908 14.365 5.971 1.00 38.95 N ANISOU 3038 NH1 ARG A 395 6421 3835 4545 -194 985 -545 N ATOM 3039 NH2 ARG A 395 17.807 14.360 3.959 1.00 41.65 N ANISOU 3039 NH2 ARG A 395 6930 4122 4774 -147 951 -495 N ATOM 3040 N HIS A 396 19.020 21.879 5.974 1.00 41.55 N ANISOU 3040 N HIS A 396 7018 3922 4849 -148 1286 -554 N ATOM 3041 CA HIS A 396 20.027 22.818 5.488 1.00 42.52 C ANISOU 3041 CA HIS A 396 7211 3964 4979 -176 1403 -579 C ATOM 3042 C HIS A 396 21.380 22.247 5.778 1.00 41.68 C ANISOU 3042 C HIS A 396 7039 3865 4931 -238 1456 -630 C ATOM 3043 O HIS A 396 21.734 22.039 6.932 1.00 41.13 O ANISOU 3043 O HIS A 396 6857 3849 4919 -266 1440 -663 O ATOM 3044 CB HIS A 396 19.885 24.186 6.172 1.00 42.91 C ANISOU 3044 CB HIS A 396 7263 3992 5048 -173 1446 -589 C ATOM 3045 CG HIS A 396 18.573 24.850 5.903 1.00 46.27 C ANISOU 3045 CG HIS A 396 7755 4407 5419 -107 1400 -539 C ATOM 3046 ND1 HIS A 396 18.212 25.301 4.648 1.00 49.56 N ANISOU 3046 ND1 HIS A 396 8305 4758 5767 -67 1423 -502 N ATOM 3047 CD2 HIS A 396 17.531 25.128 6.719 1.00 48.13 C ANISOU 3047 CD2 HIS A 396 7941 4689 5657 -72 1332 -520 C ATOM 3048 CE1 HIS A 396 16.999 25.821 4.704 1.00 50.99 C ANISOU 3048 CE1 HIS A 396 8512 4949 5911 -7 1367 -462 C ATOM 3049 NE2 HIS A 396 16.568 25.739 5.952 1.00 50.57 N ANISOU 3049 NE2 HIS A 396 8349 4963 5903 -10 1314 -473 N ATOM 3050 N GLU A 397 22.129 22.011 4.718 1.00 41.13 N ANISOU 3050 N GLU A 397 7042 3742 4845 -256 1519 -637 N ATOM 3051 CA GLU A 397 23.394 21.307 4.783 1.00 41.52 C ANISOU 3051 CA GLU A 397 7036 3795 4944 -308 1565 -681 C ATOM 3052 C GLU A 397 24.526 22.260 5.150 1.00 41.04 C ANISOU 3052 C GLU A 397 6961 3695 4939 -358 1674 -734 C ATOM 3053 O GLU A 397 24.604 23.373 4.609 1.00 40.96 O ANISOU 3053 O GLU A 397 7044 3611 4907 -356 1751 -732 O ATOM 3054 CB GLU A 397 23.667 20.634 3.429 1.00 40.80 C ANISOU 3054 CB GLU A 397 7034 3660 4809 -305 1589 -665 C ATOM 3055 CG GLU A 397 24.862 19.702 3.399 1.00 43.13 C ANISOU 3055 CG GLU A 397 7273 3965 5151 -352 1626 -705 C ATOM 3056 CD GLU A 397 25.155 19.146 1.999 1.00 44.92 C ANISOU 3056 CD GLU A 397 7600 4137 5331 -349 1661 -691 C ATOM 3057 OE1 GLU A 397 26.355 18.959 1.657 1.00 48.58 O ANISOU 3057 OE1 GLU A 397 8063 4567 5829 -391 1745 -728 O ATOM 3058 OE2 GLU A 397 24.187 18.897 1.235 1.00 48.25 O ANISOU 3058 OE2 GLU A 397 8100 4552 5682 -306 1605 -644 O ATOM 3059 N TYR A 398 25.397 21.810 6.057 1.00 39.87 N ANISOU 3059 N TYR A 398 6696 3595 4860 -401 1680 -782 N ATOM 3060 CA TYR A 398 26.615 22.532 6.428 1.00 39.74 C ANISOU 3060 CA TYR A 398 6646 3549 4905 -456 1781 -844 C ATOM 3061 C TYR A 398 27.791 21.851 5.750 1.00 39.79 C ANISOU 3061 C TYR A 398 6654 3531 4935 -493 1843 -874 C ATOM 3062 O TYR A 398 27.816 20.628 5.644 1.00 39.15 O ANISOU 3062 O TYR A 398 6533 3490 4852 -485 1788 -864 O ATOM 3063 CB TYR A 398 26.857 22.478 7.942 1.00 38.79 C ANISOU 3063 CB TYR A 398 6386 3506 4848 -479 1742 -883 C ATOM 3064 CG TYR A 398 26.248 23.589 8.769 1.00 38.57 C ANISOU 3064 CG TYR A 398 6347 3483 4822 -470 1736 -883 C ATOM 3065 CD1 TYR A 398 26.945 24.117 9.856 1.00 38.35 C ANISOU 3065 CD1 TYR A 398 6231 3482 4858 -512 1768 -941 C ATOM 3066 CD2 TYR A 398 24.996 24.114 8.472 1.00 39.09 C ANISOU 3066 CD2 TYR A 398 6492 3530 4831 -418 1698 -829 C ATOM 3067 CE1 TYR A 398 26.417 25.136 10.634 1.00 38.01 C ANISOU 3067 CE1 TYR A 398 6180 3443 4819 -506 1766 -945 C ATOM 3068 CE2 TYR A 398 24.454 25.150 9.233 1.00 40.97 C ANISOU 3068 CE2 TYR A 398 6722 3770 5074 -408 1697 -831 C ATOM 3069 CZ TYR A 398 25.170 25.646 10.315 1.00 38.99 C ANISOU 3069 CZ TYR A 398 6385 3543 4886 -453 1732 -889 C ATOM 3070 OH TYR A 398 24.646 26.643 11.075 1.00 40.14 O ANISOU 3070 OH TYR A 398 6524 3690 5037 -445 1733 -892 O ATOM 3071 N ALA A 399 28.787 22.621 5.321 1.00 39.68 N ANISOU 3071 N ALA A 399 6681 3448 4947 -535 1961 -915 N ATOM 3072 CA ALA A 399 30.033 21.987 4.878 1.00 40.16 C ANISOU 3072 CA ALA A 399 6718 3494 5047 -577 2025 -955 C ATOM 3073 C ALA A 399 30.718 21.385 6.104 1.00 39.24 C ANISOU 3073 C ALA A 399 6444 3461 5006 -606 1990 -1004 C ATOM 3074 O ALA A 399 30.572 21.901 7.219 1.00 38.84 O ANISOU 3074 O ALA A 399 6317 3453 4986 -614 1963 -1025 O ATOM 3075 CB ALA A 399 30.950 23.008 4.168 1.00 40.58 C ANISOU 3075 CB ALA A 399 6850 3454 5116 -619 2168 -992 C ATOM 3076 N PRO A 400 31.465 20.290 5.926 1.00 39.62 N ANISOU 3076 N PRO A 400 6440 3532 5081 -621 1988 -1023 N ATOM 3077 CA PRO A 400 32.089 19.700 7.129 1.00 39.56 C ANISOU 3077 CA PRO A 400 6281 3608 5141 -640 1947 -1066 C ATOM 3078 C PRO A 400 32.856 20.704 7.980 1.00 40.14 C ANISOU 3078 C PRO A 400 6286 3686 5278 -686 2006 -1131 C ATOM 3079 O PRO A 400 32.872 20.581 9.207 1.00 39.12 O ANISOU 3079 O PRO A 400 6046 3632 5184 -689 1948 -1154 O ATOM 3080 CB PRO A 400 33.022 18.633 6.553 1.00 39.42 C ANISOU 3080 CB PRO A 400 6242 3588 5149 -655 1976 -1085 C ATOM 3081 CG PRO A 400 32.353 18.230 5.278 1.00 38.96 C ANISOU 3081 CG PRO A 400 6309 3477 5017 -623 1970 -1028 C ATOM 3082 CD PRO A 400 31.740 19.484 4.717 1.00 40.04 C ANISOU 3082 CD PRO A 400 6564 3545 5106 -615 2015 -1004 C ATOM 3083 N GLU A 401 33.465 21.691 7.314 1.00 40.89 N ANISOU 3083 N GLU A 401 6452 3701 5384 -723 2123 -1161 N ATOM 3084 CA GLU A 401 34.116 22.817 7.967 1.00 41.65 C ANISOU 3084 CA GLU A 401 6506 3787 5534 -771 2193 -1223 C ATOM 3085 C GLU A 401 33.275 23.534 8.990 1.00 39.94 C ANISOU 3085 C GLU A 401 6261 3606 5308 -755 2137 -1213 C ATOM 3086 O GLU A 401 33.670 23.646 10.138 1.00 39.15 O ANISOU 3086 O GLU A 401 6050 3567 5260 -779 2114 -1260 O ATOM 3087 CB GLU A 401 34.564 23.853 6.940 1.00 43.22 C ANISOU 3087 CB GLU A 401 6820 3877 5725 -803 2327 -1238 C ATOM 3088 CG GLU A 401 35.954 24.280 7.198 1.00 49.20 C ANISOU 3088 CG GLU A 401 7508 4622 6563 -872 2425 -1324 C ATOM 3089 CD GLU A 401 36.820 23.078 7.529 1.00 54.16 C ANISOU 3089 CD GLU A 401 8016 5318 7244 -883 2392 -1358 C ATOM 3090 OE1 GLU A 401 37.441 22.524 6.588 1.00 55.05 O ANISOU 3090 OE1 GLU A 401 8164 5392 7360 -893 2447 -1362 O ATOM 3091 OE2 GLU A 401 36.832 22.673 8.726 1.00 57.33 O ANISOU 3091 OE2 GLU A 401 8293 5812 7679 -878 2309 -1379 O ATOM 3092 N LYS A 402 32.141 24.042 8.528 1.00 38.86 N ANISOU 3092 N LYS A 402 6232 3429 5105 -715 2118 -1154 N ATOM 3093 CA LYS A 402 31.229 24.838 9.309 1.00 38.83 C ANISOU 3093 CA LYS A 402 6227 3443 5084 -694 2076 -1137 C ATOM 3094 C LYS A 402 30.600 23.969 10.416 1.00 37.51 C ANISOU 3094 C LYS A 402 5953 3380 4920 -662 1946 -1119 C ATOM 3095 O LYS A 402 30.318 24.456 11.516 1.00 37.73 O ANISOU 3095 O LYS A 402 5918 3451 4966 -665 1913 -1136 O ATOM 3096 CB LYS A 402 30.164 25.398 8.361 1.00 39.26 C ANISOU 3096 CB LYS A 402 6427 3429 5062 -648 2083 -1071 C ATOM 3097 CG LYS A 402 29.318 26.523 8.941 1.00 41.18 C ANISOU 3097 CG LYS A 402 6697 3663 5288 -630 2073 -1057 C ATOM 3098 CD LYS A 402 28.820 27.479 7.835 1.00 46.72 C ANISOU 3098 CD LYS A 402 7557 4263 5931 -605 2141 -1017 C ATOM 3099 CE LYS A 402 29.986 27.946 6.905 1.00 50.09 C ANISOU 3099 CE LYS A 402 8054 4601 6378 -655 2280 -1056 C ATOM 3100 NZ LYS A 402 29.829 29.340 6.337 1.00 53.18 N ANISOU 3100 NZ LYS A 402 8572 4892 6741 -655 2380 -1048 N ATOM 3101 N PHE A 403 30.369 22.697 10.098 1.00 35.67 N ANISOU 3101 N PHE A 403 5706 3182 4665 -633 1878 -1084 N ATOM 3102 CA PHE A 403 29.985 21.688 11.059 1.00 34.62 C ANISOU 3102 CA PHE A 403 5470 3143 4540 -609 1768 -1072 C ATOM 3103 C PHE A 403 31.006 21.529 12.205 1.00 35.27 C ANISOU 3103 C PHE A 403 5418 3288 4694 -647 1769 -1139 C ATOM 3104 O PHE A 403 30.621 21.619 13.368 1.00 35.10 O ANISOU 3104 O PHE A 403 5322 3329 4684 -639 1707 -1146 O ATOM 3105 CB PHE A 403 29.738 20.350 10.342 1.00 34.40 C ANISOU 3105 CB PHE A 403 5463 3127 4480 -578 1717 -1029 C ATOM 3106 CG PHE A 403 29.679 19.170 11.264 1.00 33.37 C ANISOU 3106 CG PHE A 403 5222 3086 4370 -563 1624 -1027 C ATOM 3107 CD1 PHE A 403 28.663 19.060 12.194 1.00 32.09 C ANISOU 3107 CD1 PHE A 403 5018 2983 4191 -531 1533 -998 C ATOM 3108 CD2 PHE A 403 30.651 18.191 11.217 1.00 35.17 C ANISOU 3108 CD2 PHE A 403 5389 3338 4635 -579 1632 -1054 C ATOM 3109 CE1 PHE A 403 28.600 17.967 13.071 1.00 33.59 C ANISOU 3109 CE1 PHE A 403 5112 3253 4397 -516 1451 -995 C ATOM 3110 CE2 PHE A 403 30.607 17.093 12.070 1.00 36.26 C ANISOU 3110 CE2 PHE A 403 5431 3556 4789 -561 1548 -1050 C ATOM 3111 CZ PHE A 403 29.576 16.989 13.021 1.00 35.30 C ANISOU 3111 CZ PHE A 403 5272 3492 4647 -530 1458 -1020 C ATOM 3112 N VAL A 404 32.287 21.303 11.888 1.00 35.98 N ANISOU 3112 N VAL A 404 5475 3364 4832 -688 1837 -1190 N ATOM 3113 CA VAL A 404 33.356 21.197 12.915 1.00 36.68 C ANISOU 3113 CA VAL A 404 5433 3513 4992 -725 1842 -1261 C ATOM 3114 C VAL A 404 33.485 22.468 13.793 1.00 37.36 C ANISOU 3114 C VAL A 404 5486 3602 5106 -758 1875 -1309 C ATOM 3115 O VAL A 404 33.625 22.362 15.019 1.00 37.04 O ANISOU 3115 O VAL A 404 5341 3638 5095 -763 1821 -1340 O ATOM 3116 CB VAL A 404 34.707 20.755 12.278 1.00 37.22 C ANISOU 3116 CB VAL A 404 5478 3559 5107 -761 1917 -1308 C ATOM 3117 CG1 VAL A 404 35.872 20.808 13.264 1.00 37.56 C ANISOU 3117 CG1 VAL A 404 5387 3659 5225 -802 1932 -1388 C ATOM 3118 CG2 VAL A 404 34.564 19.314 11.787 1.00 38.58 C ANISOU 3118 CG2 VAL A 404 5650 3752 5256 -724 1861 -1264 C ATOM 3119 N GLU A 405 33.378 23.653 13.185 1.00 38.04 N ANISOU 3119 N GLU A 405 5667 3607 5179 -779 1961 -1313 N ATOM 3120 CA GLU A 405 33.354 24.921 13.966 1.00 39.86 C ANISOU 3120 CA GLU A 405 5883 3831 5431 -808 1995 -1353 C ATOM 3121 C GLU A 405 32.183 24.971 14.926 1.00 38.70 C ANISOU 3121 C GLU A 405 5714 3740 5252 -766 1897 -1315 C ATOM 3122 O GLU A 405 32.338 25.378 16.089 1.00 38.96 O ANISOU 3122 O GLU A 405 5665 3824 5316 -786 1877 -1357 O ATOM 3123 CB GLU A 405 33.265 26.145 13.066 1.00 40.48 C ANISOU 3123 CB GLU A 405 6086 3804 5490 -827 2102 -1350 C ATOM 3124 CG GLU A 405 34.434 26.307 12.117 1.00 45.72 C ANISOU 3124 CG GLU A 405 6783 4401 6188 -875 2218 -1393 C ATOM 3125 CD GLU A 405 34.327 27.597 11.306 1.00 53.02 C ANISOU 3125 CD GLU A 405 7837 5217 7092 -893 2329 -1390 C ATOM 3126 OE1 GLU A 405 34.008 28.659 11.898 1.00 55.28 O ANISOU 3126 OE1 GLU A 405 8133 5489 7381 -906 2350 -1407 O ATOM 3127 OE2 GLU A 405 34.552 27.542 10.074 1.00 57.81 O ANISOU 3127 OE2 GLU A 405 8540 5749 7676 -894 2398 -1370 O ATOM 3128 N THR A 406 31.007 24.586 14.433 1.00 38.16 N ANISOU 3128 N THR A 406 5717 3660 5120 -711 1838 -1237 N ATOM 3129 CA THR A 406 29.804 24.499 15.281 1.00 37.74 C ANISOU 3129 CA THR A 406 5642 3661 5035 -667 1741 -1195 C ATOM 3130 C THR A 406 29.971 23.541 16.464 1.00 37.20 C ANISOU 3130 C THR A 406 5446 3695 4993 -660 1652 -1211 C ATOM 3131 O THR A 406 29.477 23.813 17.533 1.00 38.09 O ANISOU 3131 O THR A 406 5510 3855 5106 -651 1603 -1215 O ATOM 3132 CB THR A 406 28.573 24.111 14.471 1.00 37.24 C ANISOU 3132 CB THR A 406 5671 3574 4905 -609 1691 -1112 C ATOM 3133 OG1 THR A 406 28.425 25.047 13.399 1.00 39.23 O ANISOU 3133 OG1 THR A 406 6047 3731 5129 -610 1773 -1096 O ATOM 3134 CG2 THR A 406 27.299 24.136 15.353 1.00 36.11 C ANISOU 3134 CG2 THR A 406 5505 3482 4733 -566 1599 -1072 C ATOM 3135 N MET A 407 30.653 22.418 16.261 1.00 37.52 N ANISOU 3135 N MET A 407 5437 3766 5052 -662 1634 -1219 N ATOM 3136 CA MET A 407 30.877 21.431 17.326 1.00 36.12 C ANISOU 3136 CA MET A 407 5144 3683 4898 -651 1552 -1232 C ATOM 3137 C MET A 407 31.853 21.925 18.382 1.00 36.50 C ANISOU 3137 C MET A 407 5092 3773 5001 -694 1574 -1311 C ATOM 3138 O MET A 407 31.712 21.589 19.557 1.00 35.64 O ANISOU 3138 O MET A 407 4900 3742 4900 -681 1503 -1320 O ATOM 3139 CB MET A 407 31.372 20.106 16.751 1.00 36.73 C ANISOU 3139 CB MET A 407 5203 3774 4980 -639 1533 -1219 C ATOM 3140 CG MET A 407 30.338 19.326 15.929 1.00 35.88 C ANISOU 3140 CG MET A 407 5172 3646 4815 -592 1485 -1141 C ATOM 3141 SD MET A 407 28.844 19.014 16.889 1.00 38.53 S ANISOU 3141 SD MET A 407 5488 4043 5109 -542 1371 -1086 S ATOM 3142 CE MET A 407 27.635 20.122 16.173 1.00 35.75 C ANISOU 3142 CE MET A 407 5258 3621 4705 -523 1393 -1040 C ATOM 3143 N LYS A 408 32.848 22.712 17.947 1.00 37.08 N ANISOU 3143 N LYS A 408 5177 3798 5116 -746 1674 -1369 N ATOM 3144 CA LYS A 408 33.775 23.397 18.845 1.00 38.35 C ANISOU 3144 CA LYS A 408 5251 3989 5331 -795 1709 -1453 C ATOM 3145 C LYS A 408 33.024 24.406 19.700 1.00 37.73 C ANISOU 3145 C LYS A 408 5181 3918 5237 -796 1694 -1455 C ATOM 3146 O LYS A 408 33.246 24.475 20.904 1.00 38.53 O ANISOU 3146 O LYS A 408 5191 4088 5360 -806 1652 -1496 O ATOM 3147 CB LYS A 408 34.901 24.096 18.066 1.00 38.92 C ANISOU 3147 CB LYS A 408 5346 3993 5447 -854 1831 -1513 C ATOM 3148 CG LYS A 408 35.831 23.131 17.291 1.00 39.78 C ANISOU 3148 CG LYS A 408 5433 4098 5582 -860 1856 -1523 C ATOM 3149 CD LYS A 408 36.865 23.899 16.457 1.00 42.44 C ANISOU 3149 CD LYS A 408 5805 4360 5962 -920 1986 -1581 C ATOM 3150 CE LYS A 408 38.067 23.032 16.154 1.00 46.75 C ANISOU 3150 CE LYS A 408 6279 4927 6557 -938 2009 -1621 C ATOM 3151 NZ LYS A 408 38.683 23.386 14.832 1.00 51.45 N ANISOU 3151 NZ LYS A 408 6956 5427 7166 -973 2128 -1635 N ATOM 3152 N LEU A 409 32.153 25.190 19.065 1.00 37.40 N ANISOU 3152 N LEU A 409 5250 3805 5156 -783 1729 -1413 N ATOM 3153 CA LEU A 409 31.270 26.116 19.750 1.00 37.94 C ANISOU 3153 CA LEU A 409 5342 3871 5202 -774 1714 -1402 C ATOM 3154 C LEU A 409 30.434 25.385 20.818 1.00 37.38 C ANISOU 3154 C LEU A 409 5209 3887 5107 -728 1597 -1367 C ATOM 3155 O LEU A 409 30.379 25.793 21.985 1.00 37.64 O ANISOU 3155 O LEU A 409 5180 3968 5152 -739 1570 -1400 O ATOM 3156 CB LEU A 409 30.369 26.795 18.708 1.00 37.53 C ANISOU 3156 CB LEU A 409 5426 3730 5103 -750 1757 -1345 C ATOM 3157 CG LEU A 409 29.317 27.825 19.128 1.00 37.86 C ANISOU 3157 CG LEU A 409 5520 3750 5116 -731 1754 -1321 C ATOM 3158 CD1 LEU A 409 29.927 28.868 20.014 1.00 35.86 C ANISOU 3158 CD1 LEU A 409 5220 3500 4905 -783 1806 -1397 C ATOM 3159 CD2 LEU A 409 28.750 28.488 17.895 1.00 38.94 C ANISOU 3159 CD2 LEU A 409 5793 3789 5213 -711 1815 -1274 C ATOM 3160 N MET A 410 29.793 24.293 20.421 1.00 37.36 N ANISOU 3160 N MET A 410 5224 3903 5070 -680 1529 -1302 N ATOM 3161 CA MET A 410 28.967 23.518 21.354 1.00 36.67 C ANISOU 3161 CA MET A 410 5083 3891 4958 -637 1423 -1265 C ATOM 3162 C MET A 410 29.813 23.012 22.515 1.00 36.98 C ANISOU 3162 C MET A 410 5001 4015 5035 -654 1384 -1319 C ATOM 3163 O MET A 410 29.396 23.069 23.654 1.00 36.06 O ANISOU 3163 O MET A 410 4834 3955 4912 -642 1329 -1323 O ATOM 3164 CB MET A 410 28.267 22.376 20.618 1.00 37.10 C ANISOU 3164 CB MET A 410 5177 3946 4974 -589 1368 -1193 C ATOM 3165 CG MET A 410 27.231 22.856 19.579 1.00 36.65 C ANISOU 3165 CG MET A 410 5238 3817 4870 -562 1387 -1134 C ATOM 3166 SD MET A 410 26.237 24.193 20.283 1.00 37.98 S ANISOU 3166 SD MET A 410 5438 3973 5021 -553 1390 -1127 S ATOM 3167 CE MET A 410 24.934 23.276 21.118 1.00 37.09 C ANISOU 3167 CE MET A 410 5283 3935 4874 -498 1269 -1070 C ATOM 3168 N GLU A 411 31.034 22.582 22.226 1.00 38.36 N ANISOU 3168 N GLU A 411 5130 4197 5249 -682 1417 -1364 N ATOM 3169 CA GLU A 411 31.956 22.136 23.256 1.00 40.48 C ANISOU 3169 CA GLU A 411 5280 4544 5556 -697 1384 -1421 C ATOM 3170 C GLU A 411 32.215 23.252 24.278 1.00 41.24 C ANISOU 3170 C GLU A 411 5332 4661 5674 -735 1404 -1484 C ATOM 3171 O GLU A 411 32.231 22.984 25.488 1.00 40.98 O ANISOU 3171 O GLU A 411 5220 4706 5642 -724 1339 -1504 O ATOM 3172 CB GLU A 411 33.239 21.634 22.602 1.00 41.05 C ANISOU 3172 CB GLU A 411 5319 4608 5671 -723 1430 -1460 C ATOM 3173 CG GLU A 411 34.242 20.951 23.521 1.00 44.09 C ANISOU 3173 CG GLU A 411 5579 5077 6094 -728 1388 -1513 C ATOM 3174 CD GLU A 411 35.388 20.310 22.735 1.00 44.69 C ANISOU 3174 CD GLU A 411 5628 5141 6210 -744 1431 -1541 C ATOM 3175 OE1 GLU A 411 36.148 21.031 22.044 1.00 50.55 O ANISOU 3175 OE1 GLU A 411 6391 5827 6987 -793 1525 -1588 O ATOM 3176 OE2 GLU A 411 35.539 19.080 22.809 1.00 49.11 O ANISOU 3176 OE2 GLU A 411 6148 5745 6767 -708 1374 -1516 O ATOM 3177 N HIS A 412 32.349 24.492 23.789 1.00 41.27 N ANISOU 3177 N HIS A 412 5395 4594 5690 -775 1494 -1513 N ATOM 3178 CA HIS A 412 32.538 25.685 24.642 1.00 42.19 C ANISOU 3178 CA HIS A 412 5486 4716 5828 -816 1527 -1575 C ATOM 3179 C HIS A 412 31.346 26.028 25.543 1.00 42.50 C ANISOU 3179 C HIS A 412 5539 4782 5827 -784 1469 -1540 C ATOM 3180 O HIS A 412 31.537 26.438 26.696 1.00 42.38 O ANISOU 3180 O HIS A 412 5460 4818 5825 -803 1449 -1589 O ATOM 3181 CB HIS A 412 32.879 26.913 23.797 1.00 41.95 C ANISOU 3181 CB HIS A 412 5532 4591 5817 -864 1645 -1607 C ATOM 3182 CG HIS A 412 34.320 26.992 23.398 1.00 42.34 C ANISOU 3182 CG HIS A 412 5536 4627 5925 -920 1718 -1681 C ATOM 3183 ND1 HIS A 412 34.857 26.231 22.378 1.00 44.50 N ANISOU 3183 ND1 HIS A 412 5824 4876 6210 -916 1742 -1666 N ATOM 3184 CD2 HIS A 412 35.338 27.742 23.882 1.00 41.49 C ANISOU 3184 CD2 HIS A 412 5367 4527 5869 -983 1775 -1775 C ATOM 3185 CE1 HIS A 412 36.143 26.512 22.252 1.00 42.91 C ANISOU 3185 CE1 HIS A 412 5571 4668 6067 -973 1812 -1746 C ATOM 3186 NE2 HIS A 412 36.457 27.423 23.155 1.00 41.63 N ANISOU 3186 NE2 HIS A 412 5360 4527 5931 -1015 1832 -1814 N ATOM 3187 N ARG A 413 30.132 25.882 25.003 1.00 42.84 N ANISOU 3187 N ARG A 413 5664 4789 5823 -737 1445 -1459 N ATOM 3188 CA ARG A 413 28.906 26.201 25.721 1.00 43.44 C ANISOU 3188 CA ARG A 413 5762 4883 5862 -704 1396 -1420 C ATOM 3189 C ARG A 413 28.468 25.086 26.695 1.00 44.34 C ANISOU 3189 C ARG A 413 5804 5086 5955 -662 1288 -1391 C ATOM 3190 O ARG A 413 27.540 25.290 27.471 1.00 43.92 O ANISOU 3190 O ARG A 413 5753 5058 5876 -637 1245 -1367 O ATOM 3191 CB ARG A 413 27.761 26.551 24.747 1.00 42.83 C ANISOU 3191 CB ARG A 413 5798 4731 5743 -669 1414 -1347 C ATOM 3192 CG ARG A 413 28.135 27.394 23.506 1.00 43.61 C ANISOU 3192 CG ARG A 413 5986 4731 5851 -697 1517 -1357 C ATOM 3193 CD ARG A 413 27.815 28.934 23.575 1.00 43.33 C ANISOU 3193 CD ARG A 413 6014 4633 5815 -718 1590 -1376 C ATOM 3194 NE ARG A 413 28.810 29.661 24.333 1.00 40.83 N ANISOU 3194 NE ARG A 413 5638 4332 5545 -779 1640 -1465 N ATOM 3195 CZ ARG A 413 29.046 30.983 24.329 1.00 41.76 C ANISOU 3195 CZ ARG A 413 5797 4390 5680 -820 1729 -1510 C ATOM 3196 NH1 ARG A 413 28.377 31.871 23.565 1.00 37.17 N ANISOU 3196 NH1 ARG A 413 5329 3720 5074 -806 1789 -1473 N ATOM 3197 NH2 ARG A 413 30.002 31.418 25.141 1.00 37.49 N ANISOU 3197 NH2 ARG A 413 5180 3881 5184 -877 1757 -1596 N ATOM 3198 N TYR A 414 29.123 23.916 26.654 1.00 46.58 N ANISOU 3198 N TYR A 414 6031 5416 6252 -653 1249 -1393 N ATOM 3199 CA TYR A 414 28.720 22.757 27.499 1.00 47.45 C ANISOU 3199 CA TYR A 414 6082 5605 6340 -610 1151 -1361 C ATOM 3200 C TYR A 414 29.018 22.975 28.982 1.00 48.03 C ANISOU 3200 C TYR A 414 6074 5753 6423 -621 1114 -1411 C ATOM 3201 O TYR A 414 30.174 23.136 29.374 1.00 48.54 O ANISOU 3201 O TYR A 414 6071 5848 6525 -657 1133 -1483 O ATOM 3202 CB TYR A 414 29.343 21.427 27.015 1.00 48.19 C ANISOU 3202 CB TYR A 414 6143 5723 6444 -594 1124 -1347 C ATOM 3203 CG TYR A 414 28.989 20.204 27.872 1.00 47.88 C ANISOU 3203 CG TYR A 414 6049 5761 6384 -549 1029 -1313 C ATOM 3204 CD1 TYR A 414 27.785 19.521 27.684 1.00 49.46 C ANISOU 3204 CD1 TYR A 414 6294 5958 6543 -503 978 -1236 C ATOM 3205 CD2 TYR A 414 29.869 19.729 28.863 1.00 50.89 C ANISOU 3205 CD2 TYR A 414 6334 6216 6784 -552 992 -1360 C ATOM 3206 CE1 TYR A 414 27.450 18.402 28.457 1.00 50.70 C ANISOU 3206 CE1 TYR A 414 6406 6179 6680 -464 900 -1205 C ATOM 3207 CE2 TYR A 414 29.544 18.611 29.656 1.00 50.58 C ANISOU 3207 CE2 TYR A 414 6252 6244 6722 -507 909 -1326 C ATOM 3208 CZ TYR A 414 28.333 17.952 29.444 1.00 51.22 C ANISOU 3208 CZ TYR A 414 6384 6315 6764 -465 867 -1249 C ATOM 3209 OH TYR A 414 27.989 16.839 30.209 1.00 50.83 O ANISOU 3209 OH TYR A 414 6298 6324 6690 -423 792 -1214 O ATOM 3210 N GLY A 415 27.962 22.971 29.794 1.00 48.65 N ANISOU 3210 N GLY A 415 6157 5861 6467 -589 1060 -1376 N ATOM 3211 CA GLY A 415 28.067 23.259 31.225 1.00 49.36 C ANISOU 3211 CA GLY A 415 6183 6017 6556 -596 1025 -1418 C ATOM 3212 C GLY A 415 28.549 24.662 31.570 1.00 50.71 C ANISOU 3212 C GLY A 415 6350 6166 6751 -649 1089 -1490 C ATOM 3213 O GLY A 415 29.107 24.876 32.653 1.00 51.68 O ANISOU 3213 O GLY A 415 6404 6347 6884 -669 1070 -1550 O ATOM 3214 N ALA A 416 28.330 25.615 30.658 1.00 50.75 N ANISOU 3214 N ALA A 416 6432 6087 6763 -671 1166 -1487 N ATOM 3215 CA ALA A 416 28.819 26.982 30.809 1.00 51.12 C ANISOU 3215 CA ALA A 416 6488 6098 6837 -726 1242 -1555 C ATOM 3216 C ALA A 416 27.673 27.920 31.144 1.00 50.84 C ANISOU 3216 C ALA A 416 6514 6030 6774 -713 1255 -1529 C ATOM 3217 O ALA A 416 26.527 27.649 30.781 1.00 50.50 O ANISOU 3217 O ALA A 416 6527 5965 6696 -666 1227 -1453 O ATOM 3218 CB ALA A 416 29.508 27.438 29.530 1.00 51.51 C ANISOU 3218 CB ALA A 416 6585 6069 6917 -762 1333 -1575 C ATOM 3219 N LYS A 417 27.980 29.019 31.833 1.00 50.57 N ANISOU 3219 N LYS A 417 6466 5992 6756 -756 1297 -1594 N ATOM 3220 CA LYS A 417 26.979 30.043 32.160 1.00 50.00 C ANISOU 3220 CA LYS A 417 6453 5881 6662 -748 1321 -1578 C ATOM 3221 C LYS A 417 27.296 31.397 31.520 1.00 50.16 C ANISOU 3221 C LYS A 417 6538 5814 6708 -795 1430 -1617 C ATOM 3222 O LYS A 417 28.350 31.587 30.893 1.00 49.00 O ANISOU 3222 O LYS A 417 6384 5636 6596 -840 1490 -1665 O ATOM 3223 CB LYS A 417 26.830 30.216 33.684 1.00 50.68 C ANISOU 3223 CB LYS A 417 6480 6039 6738 -751 1274 -1614 C ATOM 3224 CG LYS A 417 28.152 30.228 34.452 1.00 52.47 C ANISOU 3224 CG LYS A 417 6615 6327 6997 -801 1271 -1708 C ATOM 3225 CD LYS A 417 28.118 31.072 35.696 1.00 54.20 C ANISOU 3225 CD LYS A 417 6806 6576 7211 -828 1273 -1765 C ATOM 3226 CE LYS A 417 29.387 30.858 36.530 1.00 56.06 C ANISOU 3226 CE LYS A 417 6939 6890 7472 -868 1248 -1854 C ATOM 3227 NZ LYS A 417 30.654 31.129 35.760 1.00 58.22 N ANISOU 3227 NZ LYS A 417 7189 7133 7797 -923 1315 -1918 N ATOM 3228 N GLU A 418 26.364 32.333 31.686 1.00 49.78 N ANISOU 3228 N GLU A 418 6553 5721 6639 -783 1458 -1596 N ATOM 3229 CA GLU A 418 26.560 33.728 31.291 1.00 50.81 C ANISOU 3229 CA GLU A 418 6748 5767 6789 -825 1563 -1635 C ATOM 3230 C GLU A 418 27.043 33.936 29.850 1.00 49.54 C ANISOU 3230 C GLU A 418 6654 5524 6646 -841 1641 -1626 C ATOM 3231 O GLU A 418 28.165 34.391 29.611 1.00 49.98 O ANISOU 3231 O GLU A 418 6693 5554 6742 -902 1711 -1696 O ATOM 3232 CB GLU A 418 27.483 34.445 32.287 1.00 51.49 C ANISOU 3232 CB GLU A 418 6772 5884 6908 -890 1595 -1737 C ATOM 3233 CG GLU A 418 27.111 35.899 32.514 1.00 54.16 C ANISOU 3233 CG GLU A 418 7173 6157 7249 -916 1673 -1764 C ATOM 3234 CD GLU A 418 28.009 36.584 33.526 1.00 55.67 C ANISOU 3234 CD GLU A 418 7299 6381 7471 -984 1702 -1870 C ATOM 3235 OE1 GLU A 418 28.460 35.906 34.493 1.00 59.00 O ANISOU 3235 OE1 GLU A 418 7625 6899 7895 -990 1629 -1906 O ATOM 3236 OE2 GLU A 418 28.248 37.805 33.355 1.00 59.70 O ANISOU 3236 OE2 GLU A 418 7859 6820 8003 -1031 1799 -1916 O ATOM 3237 N PHE A 419 26.185 33.596 28.896 1.00 47.56 N ANISOU 3237 N PHE A 419 6476 5230 6363 -788 1628 -1542 N ATOM 3238 CA PHE A 419 26.428 33.913 27.488 1.00 46.01 C ANISOU 3238 CA PHE A 419 6365 4944 6171 -795 1706 -1523 C ATOM 3239 C PHE A 419 25.121 34.139 26.752 1.00 45.01 C ANISOU 3239 C PHE A 419 6341 4761 6001 -732 1702 -1436 C ATOM 3240 O PHE A 419 24.072 33.709 27.195 1.00 44.58 O ANISOU 3240 O PHE A 419 6278 4747 5916 -680 1626 -1383 O ATOM 3241 CB PHE A 419 27.244 32.818 26.800 1.00 45.08 C ANISOU 3241 CB PHE A 419 6212 4849 6069 -801 1687 -1522 C ATOM 3242 CG PHE A 419 26.513 31.506 26.656 1.00 43.10 C ANISOU 3242 CG PHE A 419 5945 4647 5783 -739 1588 -1447 C ATOM 3243 CD1 PHE A 419 25.695 31.269 25.549 1.00 40.88 C ANISOU 3243 CD1 PHE A 419 5751 4315 5467 -690 1584 -1369 C ATOM 3244 CD2 PHE A 419 26.660 30.500 27.624 1.00 40.89 C ANISOU 3244 CD2 PHE A 419 5565 4465 5504 -728 1499 -1456 C ATOM 3245 CE1 PHE A 419 25.014 30.059 25.415 1.00 41.95 C ANISOU 3245 CE1 PHE A 419 5871 4496 5573 -638 1494 -1304 C ATOM 3246 CE2 PHE A 419 25.986 29.291 27.504 1.00 40.64 C ANISOU 3246 CE2 PHE A 419 5523 4476 5444 -674 1413 -1388 C ATOM 3247 CZ PHE A 419 25.171 29.065 26.388 1.00 41.47 C ANISOU 3247 CZ PHE A 419 5712 4528 5517 -631 1412 -1314 C ATOM 3248 N VAL A 420 25.202 34.823 25.627 1.00 44.72 N ANISOU 3248 N VAL A 420 6400 4630 5962 -738 1787 -1423 N ATOM 3249 CA VAL A 420 24.076 35.003 24.745 1.00 44.25 C ANISOU 3249 CA VAL A 420 6442 4512 5859 -676 1786 -1340 C ATOM 3250 C VAL A 420 24.469 34.273 23.464 1.00 44.11 C ANISOU 3250 C VAL A 420 6461 4465 5833 -668 1794 -1310 C ATOM 3251 O VAL A 420 25.589 34.423 22.960 1.00 44.59 O ANISOU 3251 O VAL A 420 6525 4492 5925 -719 1865 -1358 O ATOM 3252 CB VAL A 420 23.795 36.512 24.443 1.00 45.01 C ANISOU 3252 CB VAL A 420 6638 4511 5951 -682 1885 -1346 C ATOM 3253 CG1 VAL A 420 22.584 36.686 23.527 1.00 44.38 C ANISOU 3253 CG1 VAL A 420 6663 4376 5822 -609 1876 -1258 C ATOM 3254 CG2 VAL A 420 23.605 37.323 25.750 1.00 44.76 C ANISOU 3254 CG2 VAL A 420 6568 4503 5934 -703 1892 -1392 C ATOM 3255 N THR A 421 23.558 33.455 22.952 1.00 42.69 N ANISOU 3255 N THR A 421 6306 4302 5614 -605 1722 -1233 N ATOM 3256 CA THR A 421 23.792 32.818 21.673 1.00 41.70 C ANISOU 3256 CA THR A 421 6229 4142 5473 -592 1730 -1198 C ATOM 3257 C THR A 421 23.799 33.858 20.559 1.00 42.62 C ANISOU 3257 C THR A 421 6471 4149 5575 -592 1831 -1185 C ATOM 3258 O THR A 421 23.245 34.948 20.720 1.00 42.35 O ANISOU 3258 O THR A 421 6493 4067 5530 -580 1872 -1180 O ATOM 3259 CB THR A 421 22.736 31.724 21.370 1.00 41.13 C ANISOU 3259 CB THR A 421 6159 4111 5359 -525 1629 -1120 C ATOM 3260 OG1 THR A 421 21.455 32.337 21.143 1.00 36.19 O ANISOU 3260 OG1 THR A 421 5608 3450 4694 -469 1618 -1062 O ATOM 3261 CG2 THR A 421 22.679 30.707 22.523 1.00 38.55 C ANISOU 3261 CG2 THR A 421 5715 3889 5044 -523 1534 -1129 C ATOM 3262 N SER A 422 24.441 33.493 19.451 1.00 43.04 N ANISOU 3262 N SER A 422 6566 4160 5627 -605 1871 -1181 N ATOM 3263 CA SER A 422 24.514 34.295 18.233 1.00 44.27 C ANISOU 3263 CA SER A 422 6848 4210 5763 -601 1965 -1163 C ATOM 3264 C SER A 422 23.568 33.742 17.152 1.00 44.50 C ANISOU 3264 C SER A 422 6958 4218 5732 -531 1916 -1077 C ATOM 3265 O SER A 422 23.714 32.589 16.709 1.00 44.03 O ANISOU 3265 O SER A 422 6871 4195 5663 -521 1863 -1056 O ATOM 3266 CB SER A 422 25.967 34.337 17.746 1.00 44.51 C ANISOU 3266 CB SER A 422 6873 4204 5834 -670 2056 -1226 C ATOM 3267 OG SER A 422 26.048 34.720 16.393 1.00 46.36 O ANISOU 3267 OG SER A 422 7230 4344 6042 -660 2133 -1197 O ATOM 3268 N LYS A 423 22.595 34.568 16.751 1.00 45.13 N ANISOU 3268 N LYS A 423 7135 4241 5771 -481 1933 -1028 N ATOM 3269 CA LYS A 423 21.481 34.148 15.890 1.00 45.40 C ANISOU 3269 CA LYS A 423 7240 4266 5745 -405 1872 -945 C ATOM 3270 C LYS A 423 21.777 34.383 14.432 1.00 46.86 C ANISOU 3270 C LYS A 423 7545 4362 5897 -396 1942 -921 C ATOM 3271 O LYS A 423 21.126 33.822 13.549 1.00 47.54 O ANISOU 3271 O LYS A 423 7686 4443 5934 -343 1893 -861 O ATOM 3272 CB LYS A 423 20.188 34.883 16.260 1.00 45.27 C ANISOU 3272 CB LYS A 423 7259 4242 5699 -345 1842 -903 C ATOM 3273 CG LYS A 423 19.560 34.496 17.610 1.00 43.63 C ANISOU 3273 CG LYS A 423 6942 4128 5510 -335 1752 -907 C ATOM 3274 CD LYS A 423 20.161 35.295 18.766 1.00 42.89 C ANISOU 3274 CD LYS A 423 6793 4039 5463 -391 1805 -977 C ATOM 3275 CE LYS A 423 19.519 34.959 20.103 1.00 36.73 C ANISOU 3275 CE LYS A 423 5914 3347 4695 -378 1721 -980 C ATOM 3276 NZ LYS A 423 20.520 35.170 21.193 1.00 36.06 N ANISOU 3276 NZ LYS A 423 5743 3296 4661 -449 1753 -1061 N ATOM 3277 N GLU A 424 22.777 35.221 14.191 1.00 48.75 N ANISOU 3277 N GLU A 424 7827 4531 6165 -451 2060 -971 N ATOM 3278 CA GLU A 424 23.198 35.631 12.854 1.00 49.53 C ANISOU 3278 CA GLU A 424 8050 4532 6238 -452 2152 -958 C ATOM 3279 C GLU A 424 23.627 34.456 11.946 1.00 49.09 C ANISOU 3279 C GLU A 424 7996 4490 6167 -453 2125 -941 C ATOM 3280 O GLU A 424 24.622 33.762 12.208 1.00 48.29 O ANISOU 3280 O GLU A 424 7809 4428 6110 -508 2130 -991 O ATOM 3281 CB GLU A 424 24.264 36.752 12.977 1.00 51.56 C ANISOU 3281 CB GLU A 424 8333 4717 6540 -523 2289 -1027 C ATOM 3282 CG GLU A 424 24.766 37.072 14.468 1.00 54.13 C ANISOU 3282 CG GLU A 424 8538 5099 6932 -583 2292 -1103 C ATOM 3283 CD GLU A 424 23.808 37.936 15.338 1.00 58.85 C ANISOU 3283 CD GLU A 424 9139 5701 7521 -551 2272 -1090 C ATOM 3284 OE1 GLU A 424 23.231 38.918 14.801 1.00 63.46 O ANISOU 3284 OE1 GLU A 424 9840 6203 8070 -513 2328 -1054 O ATOM 3285 OE2 GLU A 424 23.656 37.670 16.574 1.00 57.25 O ANISOU 3285 OE2 GLU A 424 8825 5582 7347 -563 2206 -1117 O ATOM 3286 N GLY A 425 22.837 34.228 10.894 1.00 48.48 N ANISOU 3286 N GLY A 425 8015 4381 6023 -389 2094 -871 N ATOM 3287 CA GLY A 425 23.080 33.152 9.931 1.00 48.19 C ANISOU 3287 CA GLY A 425 7998 4352 5961 -381 2066 -848 C ATOM 3288 C GLY A 425 22.400 31.815 10.230 1.00 47.57 C ANISOU 3288 C GLY A 425 7836 4370 5869 -346 1930 -815 C ATOM 3289 O GLY A 425 22.358 30.932 9.364 1.00 47.53 O ANISOU 3289 O GLY A 425 7860 4368 5830 -328 1897 -785 O ATOM 3290 N ILE A 426 21.881 31.658 11.450 1.00 46.63 N ANISOU 3290 N ILE A 426 7615 4328 5774 -340 1856 -822 N ATOM 3291 CA ILE A 426 21.330 30.370 11.901 1.00 46.16 C ANISOU 3291 CA ILE A 426 7464 4364 5712 -317 1734 -799 C ATOM 3292 C ILE A 426 19.807 30.431 12.023 1.00 45.52 C ANISOU 3292 C ILE A 426 7401 4308 5585 -244 1648 -738 C ATOM 3293 O ILE A 426 19.108 29.583 11.478 1.00 44.26 O ANISOU 3293 O ILE A 426 7254 4177 5387 -202 1571 -692 O ATOM 3294 CB ILE A 426 21.938 29.927 13.245 1.00 45.81 C ANISOU 3294 CB ILE A 426 7278 4397 5730 -366 1707 -855 C ATOM 3295 CG1 ILE A 426 23.464 29.950 13.174 1.00 48.09 C ANISOU 3295 CG1 ILE A 426 7540 4663 6068 -438 1794 -922 C ATOM 3296 CG2 ILE A 426 21.477 28.527 13.617 1.00 44.96 C ANISOU 3296 CG2 ILE A 426 7086 4379 5618 -345 1593 -831 C ATOM 3297 CD1 ILE A 426 24.125 30.005 14.554 1.00 50.15 C ANISOU 3297 CD1 ILE A 426 7679 4985 6391 -489 1792 -987 C ATOM 3298 N LEU A 427 19.299 31.458 12.708 1.00 45.27 N ANISOU 3298 N LEU A 427 7373 4265 5561 -230 1664 -741 N ATOM 3299 CA LEU A 427 17.860 31.581 12.933 1.00 45.00 C ANISOU 3299 CA LEU A 427 7347 4259 5492 -161 1585 -688 C ATOM 3300 C LEU A 427 17.100 31.476 11.620 1.00 45.45 C ANISOU 3300 C LEU A 427 7511 4277 5482 -98 1561 -625 C ATOM 3301 O LEU A 427 16.007 30.926 11.588 1.00 44.49 O ANISOU 3301 O LEU A 427 7371 4202 5330 -45 1466 -580 O ATOM 3302 CB LEU A 427 17.523 32.912 13.610 1.00 45.30 C ANISOU 3302 CB LEU A 427 7404 4265 5542 -153 1633 -699 C ATOM 3303 CG LEU A 427 16.715 32.994 14.909 1.00 45.02 C ANISOU 3303 CG LEU A 427 7282 4296 5527 -136 1569 -699 C ATOM 3304 CD1 LEU A 427 16.315 34.454 15.141 1.00 44.30 C ANISOU 3304 CD1 LEU A 427 7255 4145 5434 -115 1632 -698 C ATOM 3305 CD2 LEU A 427 15.497 32.076 15.004 1.00 43.13 C ANISOU 3305 CD2 LEU A 427 6999 4127 5261 -80 1448 -648 C ATOM 3306 N ASP A 428 17.690 31.998 10.541 1.00 46.58 N ANISOU 3306 N ASP A 428 7764 4334 5601 -105 1647 -623 N ATOM 3307 CA ASP A 428 17.091 31.927 9.201 1.00 47.73 C ANISOU 3307 CA ASP A 428 8023 4435 5676 -46 1632 -566 C ATOM 3308 C ASP A 428 16.822 30.473 8.785 1.00 46.68 C ANISOU 3308 C ASP A 428 7850 4364 5522 -34 1537 -544 C ATOM 3309 O ASP A 428 15.926 30.197 7.976 1.00 46.85 O ANISOU 3309 O ASP A 428 7931 4385 5485 26 1478 -492 O ATOM 3310 CB ASP A 428 17.990 32.558 8.111 1.00 49.12 C ANISOU 3310 CB ASP A 428 8321 4509 5833 -67 1749 -575 C ATOM 3311 CG ASP A 428 19.145 33.431 8.663 1.00 53.12 C ANISOU 3311 CG ASP A 428 8816 4969 6398 -138 1867 -639 C ATOM 3312 OD1 ASP A 428 19.029 34.046 9.765 1.00 55.73 O ANISOU 3312 OD1 ASP A 428 9086 5320 6768 -153 1874 -666 O ATOM 3313 OD2 ASP A 428 20.174 33.531 7.930 1.00 57.00 O ANISOU 3313 OD2 ASP A 428 9365 5399 6894 -180 1958 -664 O ATOM 3314 N LEU A 429 17.629 29.555 9.307 1.00 45.60 N ANISOU 3314 N LEU A 429 7616 4278 5432 -91 1525 -584 N ATOM 3315 CA LEU A 429 17.547 28.128 8.913 1.00 45.21 C ANISOU 3315 CA LEU A 429 7530 4281 5369 -89 1449 -569 C ATOM 3316 C LEU A 429 16.433 27.364 9.644 1.00 44.60 C ANISOU 3316 C LEU A 429 7363 4293 5291 -55 1328 -544 C ATOM 3317 O LEU A 429 15.897 26.384 9.120 1.00 45.01 O ANISOU 3317 O LEU A 429 7414 4378 5311 -29 1255 -514 O ATOM 3318 CB LEU A 429 18.895 27.437 9.125 1.00 44.33 C ANISOU 3318 CB LEU A 429 7354 4183 5307 -159 1490 -622 C ATOM 3319 CG LEU A 429 20.097 28.108 8.459 1.00 45.95 C ANISOU 3319 CG LEU A 429 7633 4304 5523 -202 1614 -655 C ATOM 3320 CD1 LEU A 429 21.386 27.360 8.805 1.00 45.31 C ANISOU 3320 CD1 LEU A 429 7467 4249 5498 -270 1644 -710 C ATOM 3321 CD2 LEU A 429 19.888 28.230 6.946 1.00 44.92 C ANISOU 3321 CD2 LEU A 429 7642 4101 5324 -166 1642 -613 C ATOM 3322 N LEU A 430 16.085 27.827 10.850 1.00 44.36 N ANISOU 3322 N LEU A 430 7261 4299 5295 -56 1313 -558 N ATOM 3323 CA LEU A 430 15.037 27.188 11.649 1.00 43.41 C ANISOU 3323 CA LEU A 430 7054 4260 5179 -28 1208 -538 C ATOM 3324 C LEU A 430 13.667 27.456 11.050 1.00 43.13 C ANISOU 3324 C LEU A 430 7080 4219 5089 47 1152 -482 C ATOM 3325 O LEU A 430 13.401 28.538 10.559 1.00 44.33 O ANISOU 3325 O LEU A 430 7322 4309 5213 81 1197 -463 O ATOM 3326 CB LEU A 430 15.082 27.675 13.097 1.00 42.82 C ANISOU 3326 CB LEU A 430 6893 4222 5155 -51 1215 -571 C ATOM 3327 CG LEU A 430 16.439 27.573 13.810 1.00 43.07 C ANISOU 3327 CG LEU A 430 6859 4264 5243 -123 1271 -633 C ATOM 3328 CD1 LEU A 430 16.322 27.912 15.280 1.00 43.24 C ANISOU 3328 CD1 LEU A 430 6790 4333 5305 -139 1258 -662 C ATOM 3329 CD2 LEU A 430 17.102 26.201 13.639 1.00 43.28 C ANISOU 3329 CD2 LEU A 430 6832 4331 5282 -154 1239 -646 C ATOM 3330 N ALA A 431 12.798 26.463 11.093 1.00 42.44 N ANISOU 3330 N ALA A 431 6944 4195 4988 74 1053 -455 N ATOM 3331 CA ALA A 431 11.436 26.631 10.607 1.00 42.36 C ANISOU 3331 CA ALA A 431 6973 4192 4930 145 988 -406 C ATOM 3332 C ALA A 431 10.636 27.606 11.504 1.00 42.50 C ANISOU 3332 C ALA A 431 6965 4219 4964 177 983 -399 C ATOM 3333 O ALA A 431 10.982 27.801 12.678 1.00 40.98 O ANISOU 3333 O ALA A 431 6697 4052 4821 141 1004 -432 O ATOM 3334 CB ALA A 431 10.745 25.274 10.512 1.00 42.19 C ANISOU 3334 CB ALA A 431 6893 4240 4897 156 886 -388 C ATOM 3335 N PRO A 432 9.556 28.211 10.955 1.00 42.75 N ANISOU 3335 N PRO A 432 7059 4232 4952 248 954 -356 N ATOM 3336 CA PRO A 432 8.749 29.151 11.727 1.00 42.82 C ANISOU 3336 CA PRO A 432 7050 4246 4974 285 951 -347 C ATOM 3337 C PRO A 432 8.148 28.427 12.917 1.00 42.07 C ANISOU 3337 C PRO A 432 6827 4238 4919 275 879 -357 C ATOM 3338 O PRO A 432 7.726 27.282 12.766 1.00 41.86 O ANISOU 3338 O PRO A 432 6753 4267 4886 276 802 -346 O ATOM 3339 CB PRO A 432 7.642 29.548 10.741 1.00 43.14 C ANISOU 3339 CB PRO A 432 7172 4266 4955 369 910 -295 C ATOM 3340 CG PRO A 432 8.240 29.281 9.386 1.00 44.08 C ANISOU 3340 CG PRO A 432 7388 4334 5026 366 935 -284 C ATOM 3341 CD PRO A 432 9.016 28.026 9.594 1.00 43.57 C ANISOU 3341 CD PRO A 432 7252 4312 4991 300 919 -315 C ATOM 3342 N GLY A 433 8.134 29.085 14.082 1.00 41.69 N ANISOU 3342 N GLY A 433 6728 4200 4911 261 907 -378 N ATOM 3343 CA GLY A 433 7.592 28.511 15.320 1.00 40.12 C ANISOU 3343 CA GLY A 433 6413 4079 4751 250 850 -389 C ATOM 3344 C GLY A 433 8.577 27.719 16.174 1.00 39.12 C ANISOU 3344 C GLY A 433 6204 3993 4668 178 859 -433 C ATOM 3345 O GLY A 433 8.234 27.306 17.280 1.00 39.24 O ANISOU 3345 O GLY A 433 6128 4068 4714 166 821 -444 O ATOM 3346 N THR A 434 9.796 27.512 15.672 1.00 38.37 N ANISOU 3346 N THR A 434 6140 3864 4574 133 911 -457 N ATOM 3347 CA THR A 434 10.816 26.718 16.364 1.00 37.00 C ANISOU 3347 CA THR A 434 5891 3727 4440 68 919 -498 C ATOM 3348 C THR A 434 11.336 27.433 17.618 1.00 36.63 C ANISOU 3348 C THR A 434 5794 3686 4436 33 968 -541 C ATOM 3349 O THR A 434 11.653 28.609 17.576 1.00 36.51 O ANISOU 3349 O THR A 434 5833 3616 4424 30 1040 -555 O ATOM 3350 CB THR A 434 12.013 26.369 15.405 1.00 36.66 C ANISOU 3350 CB THR A 434 5899 3642 4389 32 968 -515 C ATOM 3351 OG1 THR A 434 11.535 25.642 14.277 1.00 35.30 O ANISOU 3351 OG1 THR A 434 5772 3468 4174 62 920 -478 O ATOM 3352 CG2 THR A 434 13.063 25.515 16.095 1.00 36.15 C ANISOU 3352 CG2 THR A 434 5753 3618 4364 -29 973 -557 C ATOM 3353 N TYR A 435 11.429 26.712 18.728 1.00 35.91 N ANISOU 3353 N TYR A 435 5605 3663 4377 5 930 -562 N ATOM 3354 CA TYR A 435 12.044 27.248 19.933 1.00 35.87 C ANISOU 3354 CA TYR A 435 5548 3670 4411 -34 971 -608 C ATOM 3355 C TYR A 435 13.558 27.214 19.773 1.00 36.15 C ANISOU 3355 C TYR A 435 5586 3682 4468 -92 1035 -654 C ATOM 3356 O TYR A 435 14.111 26.307 19.075 1.00 36.01 O ANISOU 3356 O TYR A 435 5573 3666 4443 -108 1023 -652 O ATOM 3357 CB TYR A 435 11.580 26.458 21.168 1.00 36.32 C ANISOU 3357 CB TYR A 435 5503 3809 4489 -38 906 -612 C ATOM 3358 CG TYR A 435 10.102 26.644 21.457 1.00 36.08 C ANISOU 3358 CG TYR A 435 5464 3801 4445 15 856 -574 C ATOM 3359 CD1 TYR A 435 9.128 25.999 20.694 1.00 36.48 C ANISOU 3359 CD1 TYR A 435 5529 3864 4468 58 793 -528 C ATOM 3360 CD2 TYR A 435 9.681 27.499 22.467 1.00 37.34 C ANISOU 3360 CD2 TYR A 435 5600 3967 4621 23 873 -586 C ATOM 3361 CE1 TYR A 435 7.758 26.182 20.963 1.00 36.06 C ANISOU 3361 CE1 TYR A 435 5461 3835 4407 107 746 -497 C ATOM 3362 CE2 TYR A 435 8.334 27.694 22.739 1.00 38.21 C ANISOU 3362 CE2 TYR A 435 5698 4096 4723 73 831 -553 C ATOM 3363 CZ TYR A 435 7.381 27.041 21.982 1.00 37.55 C ANISOU 3363 CZ TYR A 435 5625 4029 4615 115 767 -509 C ATOM 3364 OH TYR A 435 6.044 27.252 22.270 1.00 39.72 O ANISOU 3364 OH TYR A 435 5880 4325 4886 164 726 -480 O ATOM 3365 N TYR A 436 14.221 28.194 20.391 1.00 35.55 N ANISOU 3365 N TYR A 436 5508 3581 4418 -125 1102 -697 N ATOM 3366 CA TYR A 436 15.679 28.328 20.350 1.00 35.96 C ANISOU 3366 CA TYR A 436 5556 3610 4497 -184 1170 -750 C ATOM 3367 C TYR A 436 16.238 28.968 21.604 1.00 35.55 C ANISOU 3367 C TYR A 436 5447 3578 4484 -225 1206 -806 C ATOM 3368 O TYR A 436 15.527 29.694 22.293 1.00 36.30 O ANISOU 3368 O TYR A 436 5539 3676 4578 -205 1204 -802 O ATOM 3369 CB TYR A 436 16.158 29.088 19.084 1.00 37.72 C ANISOU 3369 CB TYR A 436 5885 3743 4703 -187 1250 -748 C ATOM 3370 CG TYR A 436 15.778 30.541 19.059 1.00 39.02 C ANISOU 3370 CG TYR A 436 6119 3846 4860 -169 1311 -746 C ATOM 3371 CD1 TYR A 436 16.640 31.509 19.571 1.00 39.14 C ANISOU 3371 CD1 TYR A 436 6136 3829 4908 -216 1395 -801 C ATOM 3372 CD2 TYR A 436 14.536 30.947 18.552 1.00 41.62 C ANISOU 3372 CD2 TYR A 436 6511 4152 5150 -102 1284 -690 C ATOM 3373 CE1 TYR A 436 16.284 32.844 19.576 1.00 41.20 C ANISOU 3373 CE1 TYR A 436 6463 4029 5162 -200 1455 -800 C ATOM 3374 CE2 TYR A 436 14.159 32.289 18.560 1.00 42.01 C ANISOU 3374 CE2 TYR A 436 6626 4143 5193 -80 1341 -685 C ATOM 3375 CZ TYR A 436 15.050 33.230 19.071 1.00 42.26 C ANISOU 3375 CZ TYR A 436 6662 4137 5257 -130 1429 -740 C ATOM 3376 OH TYR A 436 14.711 34.562 19.097 1.00 43.54 O ANISOU 3376 OH TYR A 436 6892 4236 5413 -111 1493 -738 O ATOM 3377 N LEU A 437 17.514 28.710 21.881 1.00 35.21 N ANISOU 3377 N LEU A 437 5359 3547 4471 -280 1237 -859 N ATOM 3378 CA LEU A 437 18.202 29.232 23.057 1.00 35.35 C ANISOU 3378 CA LEU A 437 5316 3589 4525 -325 1268 -920 C ATOM 3379 C LEU A 437 18.673 30.643 22.819 1.00 36.75 C ANISOU 3379 C LEU A 437 5557 3692 4715 -351 1368 -954 C ATOM 3380 O LEU A 437 19.482 30.874 21.915 1.00 37.03 O ANISOU 3380 O LEU A 437 5642 3671 4755 -377 1432 -971 O ATOM 3381 CB LEU A 437 19.424 28.379 23.387 1.00 34.53 C ANISOU 3381 CB LEU A 437 5138 3531 4452 -372 1262 -966 C ATOM 3382 CG LEU A 437 20.152 28.699 24.703 1.00 34.66 C ANISOU 3382 CG LEU A 437 5074 3591 4504 -416 1274 -1032 C ATOM 3383 CD1 LEU A 437 19.233 28.431 25.922 1.00 31.93 C ANISOU 3383 CD1 LEU A 437 4671 3313 4149 -389 1203 -1016 C ATOM 3384 CD2 LEU A 437 21.442 27.894 24.807 1.00 35.46 C ANISOU 3384 CD2 LEU A 437 5110 3730 4634 -458 1273 -1077 C ATOM 3385 N LYS A 438 18.196 31.573 23.644 1.00 37.69 N ANISOU 3385 N LYS A 438 5674 3807 4838 -347 1384 -967 N ATOM 3386 CA LYS A 438 18.617 32.978 23.581 1.00 38.80 C ANISOU 3386 CA LYS A 438 5872 3877 4993 -375 1483 -1005 C ATOM 3387 C LYS A 438 19.846 33.275 24.438 1.00 38.17 C ANISOU 3387 C LYS A 438 5727 3817 4957 -447 1528 -1089 C ATOM 3388 O LYS A 438 20.779 33.901 23.971 1.00 38.99 O ANISOU 3388 O LYS A 438 5867 3866 5082 -491 1613 -1131 O ATOM 3389 CB LYS A 438 17.465 33.897 23.976 1.00 38.79 C ANISOU 3389 CB LYS A 438 5910 3854 4975 -332 1485 -977 C ATOM 3390 CG LYS A 438 16.291 33.887 22.997 1.00 39.82 C ANISOU 3390 CG LYS A 438 6117 3950 5062 -260 1457 -900 C ATOM 3391 CD LYS A 438 15.161 34.822 23.483 1.00 42.09 C ANISOU 3391 CD LYS A 438 6435 4220 5338 -216 1460 -876 C ATOM 3392 CE LYS A 438 14.256 35.243 22.307 1.00 47.22 C ANISOU 3392 CE LYS A 438 7187 4808 5947 -149 1466 -811 C ATOM 3393 NZ LYS A 438 13.555 36.554 22.529 1.00 49.69 N ANISOU 3393 NZ LYS A 438 7559 5068 6254 -116 1514 -801 N ATOM 3394 N GLU A 439 19.846 32.843 25.692 1.00 37.77 N ANISOU 3394 N GLU A 439 5584 3846 4920 -458 1472 -1114 N ATOM 3395 CA GLU A 439 20.984 33.089 26.575 1.00 38.28 C ANISOU 3395 CA GLU A 439 5580 3940 5023 -523 1504 -1197 C ATOM 3396 C GLU A 439 20.927 32.186 27.787 1.00 37.09 C ANISOU 3396 C GLU A 439 5326 3890 4876 -521 1418 -1208 C ATOM 3397 O GLU A 439 19.880 31.643 28.105 1.00 36.36 O ANISOU 3397 O GLU A 439 5222 3835 4758 -472 1347 -1156 O ATOM 3398 CB GLU A 439 21.070 34.578 26.996 1.00 39.13 C ANISOU 3398 CB GLU A 439 5726 3995 5146 -552 1587 -1241 C ATOM 3399 CG GLU A 439 20.103 35.010 28.064 1.00 40.41 C ANISOU 3399 CG GLU A 439 5872 4186 5296 -526 1555 -1232 C ATOM 3400 CD GLU A 439 20.231 36.489 28.413 1.00 41.85 C ANISOU 3400 CD GLU A 439 6099 4309 5493 -556 1644 -1277 C ATOM 3401 OE1 GLU A 439 20.848 36.798 29.459 1.00 43.75 O ANISOU 3401 OE1 GLU A 439 6279 4586 5759 -605 1657 -1346 O ATOM 3402 OE2 GLU A 439 19.753 37.342 27.622 1.00 45.92 O ANISOU 3402 OE2 GLU A 439 6711 4741 5995 -532 1704 -1246 O ATOM 3403 N VAL A 440 22.079 31.967 28.405 1.00 37.20 N ANISOU 3403 N VAL A 440 5267 3947 4922 -573 1423 -1276 N ATOM 3404 CA VAL A 440 22.167 31.324 29.705 1.00 36.85 C ANISOU 3404 CA VAL A 440 5127 3995 4881 -576 1353 -1299 C ATOM 3405 C VAL A 440 22.747 32.404 30.653 1.00 38.07 C ANISOU 3405 C VAL A 440 5256 4150 5060 -628 1405 -1378 C ATOM 3406 O VAL A 440 23.853 32.906 30.415 1.00 38.14 O ANISOU 3406 O VAL A 440 5259 4131 5100 -683 1471 -1441 O ATOM 3407 CB VAL A 440 23.056 30.061 29.653 1.00 36.81 C ANISOU 3407 CB VAL A 440 5051 4047 4889 -588 1308 -1313 C ATOM 3408 CG1 VAL A 440 23.134 29.392 31.018 1.00 36.61 C ANISOU 3408 CG1 VAL A 440 4934 4116 4861 -586 1234 -1334 C ATOM 3409 CG2 VAL A 440 22.521 29.057 28.597 1.00 35.16 C ANISOU 3409 CG2 VAL A 440 4878 3826 4657 -543 1268 -1238 C ATOM 3410 N ASP A 441 21.991 32.799 31.682 1.00 38.00 N ANISOU 3410 N ASP A 441 5235 4168 5036 -612 1380 -1377 N ATOM 3411 CA ASP A 441 22.433 33.896 32.564 1.00 39.61 C ANISOU 3411 CA ASP A 441 5424 4367 5258 -660 1432 -1451 C ATOM 3412 C ASP A 441 23.502 33.452 33.570 1.00 40.12 C ANISOU 3412 C ASP A 441 5388 4513 5343 -703 1399 -1523 C ATOM 3413 O ASP A 441 23.947 32.296 33.543 1.00 39.41 O ANISOU 3413 O ASP A 441 5242 4479 5254 -694 1341 -1515 O ATOM 3414 CB ASP A 441 21.237 34.565 33.281 1.00 40.16 C ANISOU 3414 CB ASP A 441 5524 4431 5305 -628 1425 -1425 C ATOM 3415 CG ASP A 441 20.641 33.696 34.420 1.00 41.01 C ANISOU 3415 CG ASP A 441 5565 4628 5389 -595 1331 -1404 C ATOM 3416 OD1 ASP A 441 21.256 32.689 34.876 1.00 42.16 O ANISOU 3416 OD1 ASP A 441 5635 4846 5537 -604 1273 -1422 O ATOM 3417 OD2 ASP A 441 19.533 34.042 34.875 1.00 42.28 O ANISOU 3417 OD2 ASP A 441 5750 4784 5529 -560 1318 -1370 O ATOM 3418 N SER A 442 23.882 34.352 34.484 1.00 40.57 N ANISOU 3418 N SER A 442 5424 4579 5414 -747 1434 -1594 N ATOM 3419 CA SER A 442 24.989 34.087 35.411 1.00 41.03 C ANISOU 3419 CA SER A 442 5387 4710 5492 -792 1410 -1674 C ATOM 3420 C SER A 442 24.676 33.059 36.509 1.00 40.97 C ANISOU 3420 C SER A 442 5309 4802 5457 -758 1306 -1657 C ATOM 3421 O SER A 442 25.595 32.624 37.219 1.00 41.69 O ANISOU 3421 O SER A 442 5319 4963 5559 -784 1271 -1714 O ATOM 3422 CB SER A 442 25.526 35.396 36.028 1.00 41.53 C ANISOU 3422 CB SER A 442 5450 4751 5578 -855 1481 -1762 C ATOM 3423 OG SER A 442 24.606 35.927 36.974 1.00 42.05 O ANISOU 3423 OG SER A 442 5533 4828 5618 -835 1467 -1754 O ATOM 3424 N LEU A 443 23.403 32.674 36.652 1.00 39.90 N ANISOU 3424 N LEU A 443 5203 4673 5286 -698 1259 -1580 N ATOM 3425 CA LEU A 443 23.017 31.580 37.566 1.00 39.34 C ANISOU 3425 CA LEU A 443 5074 4687 5185 -660 1164 -1552 C ATOM 3426 C LEU A 443 22.590 30.296 36.804 1.00 39.57 C ANISOU 3426 C LEU A 443 5108 4726 5201 -610 1110 -1473 C ATOM 3427 O LEU A 443 21.840 29.455 37.345 1.00 38.11 O ANISOU 3427 O LEU A 443 4904 4590 4987 -566 1041 -1425 O ATOM 3428 CB LEU A 443 21.942 32.035 38.569 1.00 39.27 C ANISOU 3428 CB LEU A 443 5081 4692 5147 -636 1148 -1536 C ATOM 3429 CG LEU A 443 22.277 33.290 39.403 1.00 39.04 C ANISOU 3429 CG LEU A 443 5050 4654 5128 -684 1200 -1613 C ATOM 3430 CD1 LEU A 443 21.124 33.705 40.327 1.00 39.59 C ANISOU 3430 CD1 LEU A 443 5142 4732 5168 -655 1187 -1590 C ATOM 3431 CD2 LEU A 443 23.596 33.116 40.185 1.00 38.21 C ANISOU 3431 CD2 LEU A 443 4864 4618 5038 -732 1181 -1700 C ATOM 3432 N TYR A 444 23.096 30.168 35.565 1.00 39.53 N ANISOU 3432 N TYR A 444 5130 4674 5217 -621 1145 -1464 N ATOM 3433 CA TYR A 444 22.872 29.009 34.673 1.00 39.92 C ANISOU 3433 CA TYR A 444 5187 4723 5256 -583 1105 -1399 C ATOM 3434 C TYR A 444 21.448 28.856 34.150 1.00 39.94 C ANISOU 3434 C TYR A 444 5253 4692 5231 -529 1086 -1314 C ATOM 3435 O TYR A 444 21.117 27.846 33.542 1.00 40.11 O ANISOU 3435 O TYR A 444 5279 4720 5240 -496 1045 -1259 O ATOM 3436 CB TYR A 444 23.298 27.703 35.327 1.00 39.55 C ANISOU 3436 CB TYR A 444 5064 4762 5203 -568 1026 -1399 C ATOM 3437 CG TYR A 444 24.770 27.559 35.631 1.00 40.94 C ANISOU 3437 CG TYR A 444 5170 4979 5408 -611 1032 -1475 C ATOM 3438 CD1 TYR A 444 25.309 28.028 36.842 1.00 41.70 C ANISOU 3438 CD1 TYR A 444 5211 5126 5508 -641 1025 -1545 C ATOM 3439 CD2 TYR A 444 25.617 26.908 34.740 1.00 41.24 C ANISOU 3439 CD2 TYR A 444 5192 5008 5468 -620 1040 -1478 C ATOM 3440 CE1 TYR A 444 26.672 27.865 37.139 1.00 42.46 C ANISOU 3440 CE1 TYR A 444 5235 5267 5632 -679 1023 -1618 C ATOM 3441 CE2 TYR A 444 26.982 26.744 35.024 1.00 41.32 C ANISOU 3441 CE2 TYR A 444 5131 5059 5509 -657 1043 -1549 C ATOM 3442 CZ TYR A 444 27.495 27.218 36.218 1.00 41.91 C ANISOU 3442 CZ TYR A 444 5147 5188 5588 -685 1032 -1619 C ATOM 3443 OH TYR A 444 28.823 27.031 36.489 1.00 43.89 O ANISOU 3443 OH TYR A 444 5321 5484 5869 -719 1030 -1691 O ATOM 3444 N ARG A 445 20.616 29.862 34.370 1.00 40.54 N ANISOU 3444 N ARG A 445 5375 4730 5297 -521 1118 -1305 N ATOM 3445 CA ARG A 445 19.222 29.809 33.966 1.00 40.25 C ANISOU 3445 CA ARG A 445 5391 4665 5235 -467 1099 -1230 C ATOM 3446 C ARG A 445 19.124 30.020 32.466 1.00 39.49 C ANISOU 3446 C ARG A 445 5368 4494 5142 -457 1141 -1194 C ATOM 3447 O ARG A 445 19.727 30.951 31.943 1.00 39.13 O ANISOU 3447 O ARG A 445 5363 4390 5116 -491 1216 -1230 O ATOM 3448 CB ARG A 445 18.446 30.908 34.699 1.00 40.49 C ANISOU 3448 CB ARG A 445 5449 4678 5259 -462 1127 -1238 C ATOM 3449 CG ARG A 445 18.351 30.704 36.211 1.00 43.49 C ANISOU 3449 CG ARG A 445 5766 5131 5627 -465 1084 -1265 C ATOM 3450 CD ARG A 445 18.660 31.982 36.967 1.00 49.00 C ANISOU 3450 CD ARG A 445 6469 5812 6336 -504 1140 -1331 C ATOM 3451 NE ARG A 445 17.585 32.965 36.885 1.00 52.21 N ANISOU 3451 NE ARG A 445 6940 6163 6734 -480 1180 -1302 N ATOM 3452 CZ ARG A 445 17.684 34.235 37.288 1.00 55.13 C ANISOU 3452 CZ ARG A 445 7338 6496 7114 -508 1245 -1350 C ATOM 3453 NH1 ARG A 445 18.829 34.703 37.780 1.00 53.92 N ANISOU 3453 NH1 ARG A 445 7152 6354 6979 -568 1279 -1431 N ATOM 3454 NH2 ARG A 445 16.631 35.049 37.181 1.00 56.48 N ANISOU 3454 NH2 ARG A 445 7568 6616 7277 -477 1277 -1316 N ATOM 3455 N ARG A 446 18.334 29.184 31.790 1.00 38.83 N ANISOU 3455 N ARG A 446 5304 4410 5039 -412 1095 -1125 N ATOM 3456 CA ARG A 446 18.206 29.219 30.314 1.00 38.70 C ANISOU 3456 CA ARG A 446 5358 4328 5017 -396 1123 -1087 C ATOM 3457 C ARG A 446 16.918 29.885 29.800 1.00 38.67 C ANISOU 3457 C ARG A 446 5427 4273 4992 -350 1135 -1033 C ATOM 3458 O ARG A 446 15.832 29.624 30.304 1.00 38.29 O ANISOU 3458 O ARG A 446 5366 4256 4928 -311 1085 -995 O ATOM 3459 CB ARG A 446 18.347 27.798 29.744 1.00 38.32 C ANISOU 3459 CB ARG A 446 5286 4312 4962 -380 1067 -1052 C ATOM 3460 CG ARG A 446 19.430 26.998 30.464 1.00 37.41 C ANISOU 3460 CG ARG A 446 5089 4261 4864 -411 1039 -1097 C ATOM 3461 CD ARG A 446 19.400 25.560 30.039 1.00 38.85 C ANISOU 3461 CD ARG A 446 5248 4476 5036 -388 980 -1057 C ATOM 3462 NE ARG A 446 19.782 25.454 28.647 1.00 36.93 N ANISOU 3462 NE ARG A 446 5057 4178 4796 -392 1014 -1042 N ATOM 3463 CZ ARG A 446 21.034 25.349 28.213 1.00 38.20 C ANISOU 3463 CZ ARG A 446 5205 4328 4982 -429 1052 -1084 C ATOM 3464 NH1 ARG A 446 22.053 25.309 29.068 1.00 36.43 N ANISOU 3464 NH1 ARG A 446 4911 4148 4783 -464 1054 -1145 N ATOM 3465 NH2 ARG A 446 21.260 25.258 26.911 1.00 38.08 N ANISOU 3465 NH2 ARG A 446 5246 4258 4965 -429 1085 -1065 N ATOM 3466 N PHE A 447 17.039 30.716 28.769 1.00 39.12 N ANISOU 3466 N PHE A 447 5562 4252 5049 -352 1200 -1029 N ATOM 3467 CA PHE A 447 15.899 31.499 28.256 1.00 39.29 C ANISOU 3467 CA PHE A 447 5659 4220 5051 -306 1218 -982 C ATOM 3468 C PHE A 447 15.702 31.225 26.776 1.00 39.19 C ANISOU 3468 C PHE A 447 5714 4158 5019 -278 1221 -934 C ATOM 3469 O PHE A 447 16.666 31.251 26.000 1.00 39.01 O ANISOU 3469 O PHE A 447 5719 4098 5004 -309 1267 -955 O ATOM 3470 CB PHE A 447 16.123 33.001 28.503 1.00 40.55 C ANISOU 3470 CB PHE A 447 5863 4321 5223 -329 1304 -1022 C ATOM 3471 CG PHE A 447 16.325 33.344 29.966 1.00 42.26 C ANISOU 3471 CG PHE A 447 6017 4583 5455 -360 1303 -1075 C ATOM 3472 CD1 PHE A 447 17.585 33.213 30.571 1.00 43.90 C ANISOU 3472 CD1 PHE A 447 6166 4825 5690 -421 1319 -1144 C ATOM 3473 CD2 PHE A 447 15.247 33.751 30.752 1.00 43.69 C ANISOU 3473 CD2 PHE A 447 6196 4779 5627 -326 1284 -1055 C ATOM 3474 CE1 PHE A 447 17.777 33.507 31.938 1.00 43.02 C ANISOU 3474 CE1 PHE A 447 5997 4760 5587 -448 1313 -1195 C ATOM 3475 CE2 PHE A 447 15.425 34.036 32.119 1.00 46.78 C ANISOU 3475 CE2 PHE A 447 6533 5214 6028 -354 1283 -1104 C ATOM 3476 CZ PHE A 447 16.703 33.902 32.710 1.00 45.46 C ANISOU 3476 CZ PHE A 447 6309 5081 5882 -415 1295 -1174 C ATOM 3477 N TYR A 448 14.444 30.995 26.399 1.00 38.21 N ANISOU 3477 N TYR A 448 5617 4034 4868 -219 1174 -871 N ATOM 3478 CA TYR A 448 14.081 30.508 25.060 1.00 38.17 C ANISOU 3478 CA TYR A 448 5667 3999 4837 -184 1154 -819 C ATOM 3479 C TYR A 448 13.193 31.490 24.366 1.00 38.84 C ANISOU 3479 C TYR A 448 5838 4020 4898 -136 1183 -781 C ATOM 3480 O TYR A 448 12.398 32.156 25.003 1.00 39.73 O ANISOU 3480 O TYR A 448 5950 4134 5011 -110 1183 -773 O ATOM 3481 CB TYR A 448 13.398 29.123 25.131 1.00 35.22 C ANISOU 3481 CB TYR A 448 5241 3692 4450 -156 1060 -779 C ATOM 3482 CG TYR A 448 14.379 28.099 25.605 1.00 34.14 C ANISOU 3482 CG TYR A 448 5031 3608 4332 -198 1036 -812 C ATOM 3483 CD1 TYR A 448 14.583 27.897 26.964 1.00 33.31 C ANISOU 3483 CD1 TYR A 448 4848 3562 4245 -220 1015 -845 C ATOM 3484 CD2 TYR A 448 15.164 27.368 24.693 1.00 33.06 C ANISOU 3484 CD2 TYR A 448 4908 3460 4195 -216 1040 -812 C ATOM 3485 CE1 TYR A 448 15.526 26.994 27.415 1.00 31.80 C ANISOU 3485 CE1 TYR A 448 4592 3420 4069 -255 994 -877 C ATOM 3486 CE2 TYR A 448 16.114 26.455 25.143 1.00 31.33 C ANISOU 3486 CE2 TYR A 448 4621 3288 3994 -252 1021 -844 C ATOM 3487 CZ TYR A 448 16.296 26.287 26.498 1.00 31.11 C ANISOU 3487 CZ TYR A 448 4516 3321 3984 -269 997 -876 C ATOM 3488 OH TYR A 448 17.220 25.407 26.981 1.00 29.92 O ANISOU 3488 OH TYR A 448 4298 3218 3850 -298 976 -907 O ATOM 3489 N GLY A 449 13.339 31.585 23.060 1.00 40.00 N ANISOU 3489 N GLY A 449 6062 4110 5024 -122 1209 -757 N ATOM 3490 CA GLY A 449 12.372 32.279 22.250 1.00 41.56 C ANISOU 3490 CA GLY A 449 6345 4256 5191 -62 1218 -708 C ATOM 3491 C GLY A 449 11.744 31.352 21.243 1.00 43.11 C ANISOU 3491 C GLY A 449 6562 4464 5354 -19 1152 -654 C ATOM 3492 O GLY A 449 11.974 30.142 21.250 1.00 42.16 O ANISOU 3492 O GLY A 449 6387 4395 5236 -36 1099 -653 O ATOM 3493 N LYS A 450 10.969 31.938 20.344 1.00 44.99 N ANISOU 3493 N LYS A 450 6883 4652 5558 37 1158 -610 N ATOM 3494 CA LYS A 450 10.242 31.182 19.372 1.00 46.48 C ANISOU 3494 CA LYS A 450 7097 4853 5712 83 1093 -559 C ATOM 3495 C LYS A 450 10.240 31.919 18.040 1.00 48.73 C ANISOU 3495 C LYS A 450 7502 5055 5958 117 1141 -531 C ATOM 3496 O LYS A 450 9.869 33.099 17.993 1.00 48.68 O ANISOU 3496 O LYS A 450 7557 4997 5943 149 1188 -522 O ATOM 3497 CB LYS A 450 8.813 30.954 19.868 1.00 45.90 C ANISOU 3497 CB LYS A 450 6978 4831 5632 137 1015 -523 C ATOM 3498 CG LYS A 450 7.826 30.527 18.796 1.00 46.57 C ANISOU 3498 CG LYS A 450 7103 4917 5676 198 953 -469 C ATOM 3499 CD LYS A 450 6.620 29.819 19.415 1.00 46.35 C ANISOU 3499 CD LYS A 450 6994 4963 5653 230 864 -446 C ATOM 3500 CE LYS A 450 5.501 29.652 18.414 1.00 47.12 C ANISOU 3500 CE LYS A 450 7132 5061 5712 298 805 -395 C ATOM 3501 NZ LYS A 450 4.293 29.166 19.122 1.00 47.45 N ANISOU 3501 NZ LYS A 450 7092 5169 5767 327 730 -379 N ATOM 3502 N LYS A 451 10.725 31.226 16.999 1.00 50.26 N ANISOU 3502 N LYS A 451 7733 5235 6129 108 1135 -521 N ATOM 3503 CA LYS A 451 10.352 31.438 15.575 1.00 53.13 C ANISOU 3503 CA LYS A 451 8203 5543 6440 158 1137 -477 C ATOM 3504 C LYS A 451 11.371 32.131 14.671 1.00 54.65 C ANISOU 3504 C LYS A 451 8497 5647 6619 135 1236 -491 C ATOM 3505 O LYS A 451 11.549 33.358 14.772 1.00 56.56 O ANISOU 3505 O LYS A 451 8797 5828 6866 137 1314 -502 O ATOM 3506 CB LYS A 451 8.944 32.046 15.434 1.00 53.56 C ANISOU 3506 CB LYS A 451 8291 5594 6466 239 1098 -430 C ATOM 3507 CG LYS A 451 8.603 32.609 14.070 1.00 56.12 C ANISOU 3507 CG LYS A 451 8739 5850 6734 297 1116 -387 C ATOM 3508 CD LYS A 451 8.703 34.144 14.084 1.00 59.76 C ANISOU 3508 CD LYS A 451 9283 6231 7192 315 1208 -389 C ATOM 3509 CE LYS A 451 9.138 34.698 12.731 1.00 63.39 C ANISOU 3509 CE LYS A 451 9879 6602 7605 335 1272 -369 C ATOM 3510 NZ LYS A 451 8.095 34.565 11.655 1.00 66.44 N ANISOU 3510 NZ LYS A 451 10331 6984 7929 420 1207 -308 N TER 3511 LYS A 451 ATOM 1 N ALA A 2 -4.188 -7.985 40.829 1.00 35.86 N ANISOU 1 N ALA B 2 4278 4598 4749 -246 148 -397 N ATOM 2 CA ALA A 2 -3.321 -7.527 41.957 1.00 34.44 C ANISOU 2 CA ALA B 2 4140 4407 4539 -226 110 -395 C ATOM 3 C ALA A 2 -4.140 -6.611 42.866 1.00 34.39 C ANISOU 3 C ALA B 2 4165 4380 4521 -257 97 -400 C ATOM 4 O ALA A 2 -4.516 -5.503 42.475 1.00 35.04 O ANISOU 4 O ALA B 2 4279 4442 4592 -274 127 -390 O ATOM 5 CB ALA A 2 -2.117 -6.801 41.422 1.00 34.10 C ANISOU 5 CB ALA B 2 4137 4353 4467 -199 131 -380 C ATOM 6 N LYS A 3 -4.435 -7.070 44.071 1.00 33.85 N ANISOU 6 N LYS B 3 4089 4317 4456 -262 52 -415 N ATOM 7 CA LYS A 3 -5.265 -6.283 44.956 1.00 33.72 C ANISOU 7 CA LYS B 3 4101 4281 4430 -295 40 -423 C ATOM 8 C LYS A 3 -4.461 -5.751 46.105 1.00 31.48 C ANISOU 8 C LYS B 3 3869 3982 4111 -275 9 -420 C ATOM 9 O LYS A 3 -3.472 -6.368 46.529 1.00 31.45 O ANISOU 9 O LYS B 3 3867 3987 4095 -240 -18 -418 O ATOM 10 CB LYS A 3 -6.491 -7.069 45.463 1.00 35.92 C ANISOU 10 CB LYS B 3 4333 4577 4738 -328 16 -448 C ATOM 11 CG LYS A 3 -6.558 -8.549 45.056 1.00 40.19 C ANISOU 11 CG LYS B 3 4802 5153 5314 -316 3 -461 C ATOM 12 CD LYS A 3 -7.254 -8.738 43.710 1.00 46.48 C ANISOU 12 CD LYS B 3 5563 5954 6143 -339 57 -459 C ATOM 13 CE LYS A 3 -7.154 -10.201 43.201 1.00 45.92 C ANISOU 13 CE LYS B 3 5421 5917 6108 -322 52 -470 C ATOM 14 NZ LYS A 3 -7.948 -10.412 41.940 1.00 48.82 N ANISOU 14 NZ LYS B 3 5753 6286 6509 -349 109 -472 N ATOM 15 N ASN A 4 -4.898 -4.605 46.613 1.00 30.21 N ANISOU 15 N ASN B 4 3752 3793 3931 -298 16 -419 N ATOM 16 CA ASN A 4 -4.294 -4.012 47.783 1.00 28.63 C ANISOU 16 CA ASN B 4 3605 3574 3698 -287 -8 -418 C ATOM 17 C ASN A 4 -2.770 -3.848 47.614 1.00 26.78 C ANISOU 17 C ASN B 4 3397 3335 3443 -246 -1 -403 C ATOM 18 O ASN A 4 -1.985 -4.224 48.478 1.00 26.06 O ANISOU 18 O ASN B 4 3327 3243 3333 -221 -30 -405 O ATOM 19 CB ASN A 4 -4.643 -4.854 49.014 1.00 30.04 C ANISOU 19 CB ASN B 4 3773 3766 3874 -290 -63 -438 C ATOM 20 CG ASN A 4 -6.109 -4.771 49.369 1.00 32.71 C ANISOU 20 CG ASN B 4 4095 4103 4228 -337 -69 -458 C ATOM 21 OD1 ASN A 4 -6.731 -3.717 49.238 1.00 35.34 O ANISOU 21 OD1 ASN B 4 4458 4411 4559 -366 -38 -456 O ATOM 22 ND2 ASN A 4 -6.676 -5.882 49.819 1.00 38.02 N ANISOU 22 ND2 ASN B 4 4721 4805 4919 -345 -110 -480 N ATOM 23 N VAL A 5 -2.359 -3.279 46.485 1.00 24.93 N ANISOU 23 N VAL B 5 3165 3097 3211 -239 40 -390 N ATOM 24 CA VAL A 5 -0.919 -3.178 46.220 1.00 23.23 C ANISOU 24 CA VAL B 5 2967 2879 2979 -204 50 -381 C ATOM 25 C VAL A 5 -0.326 -2.136 47.144 1.00 22.66 C ANISOU 25 C VAL B 5 2953 2778 2878 -201 49 -380 C ATOM 26 O VAL A 5 -0.926 -1.089 47.382 1.00 22.93 O ANISOU 26 O VAL B 5 3013 2794 2906 -222 61 -379 O ATOM 27 CB VAL A 5 -0.610 -2.870 44.732 1.00 22.71 C ANISOU 27 CB VAL B 5 2886 2821 2921 -197 91 -371 C ATOM 28 CG1 VAL A 5 0.924 -2.687 44.483 1.00 19.52 C ANISOU 28 CG1 VAL B 5 2502 2414 2501 -166 102 -368 C ATOM 29 CG2 VAL A 5 -1.145 -3.997 43.852 1.00 22.95 C ANISOU 29 CG2 VAL B 5 2862 2878 2980 -200 96 -373 C ATOM 30 N GLY A 6 0.846 -2.445 47.693 1.00 21.83 N ANISOU 30 N GLY B 6 2870 2668 2757 -173 37 -380 N ATOM 31 CA GLY A 6 1.607 -1.445 48.393 1.00 21.33 C ANISOU 31 CA GLY B 6 2861 2576 2669 -168 47 -379 C ATOM 32 C GLY A 6 2.909 -2.002 48.923 1.00 21.42 C ANISOU 32 C GLY B 6 2894 2580 2664 -137 39 -380 C ATOM 33 O GLY A 6 3.515 -2.852 48.304 1.00 20.88 O ANISOU 33 O GLY B 6 2800 2527 2606 -116 42 -378 O ATOM 34 N ILE A 7 3.340 -1.480 50.061 1.00 20.81 N ANISOU 34 N ILE B 7 2870 2476 2563 -135 34 -382 N ATOM 35 CA ILE A 7 4.629 -1.839 50.633 1.00 21.66 C ANISOU 35 CA ILE B 7 3011 2566 2651 -107 36 -381 C ATOM 36 C ILE A 7 4.477 -3.106 51.492 1.00 21.70 C ANISOU 36 C ILE B 7 3018 2580 2646 -86 -9 -380 C ATOM 37 O ILE A 7 3.688 -3.157 52.415 1.00 21.30 O ANISOU 37 O ILE B 7 2982 2528 2583 -97 -41 -384 O ATOM 38 CB ILE A 7 5.250 -0.639 51.436 1.00 21.32 C ANISOU 38 CB ILE B 7 3028 2486 2585 -113 59 -384 C ATOM 39 CG1 ILE A 7 5.499 0.548 50.494 1.00 21.56 C ANISOU 39 CG1 ILE B 7 3049 2515 2629 -126 100 -387 C ATOM 40 CG2 ILE A 7 6.569 -1.079 52.148 1.00 23.08 C ANISOU 40 CG2 ILE B 7 3296 2686 2787 -85 65 -384 C ATOM 41 CD1 ILE A 7 5.615 1.916 51.209 1.00 20.43 C ANISOU 41 CD1 ILE B 7 2951 2340 2472 -141 122 -392 C ATOM 42 N LEU A 8 5.213 -4.138 51.124 1.00 22.05 N ANISOU 42 N LEU B 8 3045 2636 2696 -56 -11 -376 N ATOM 43 CA LEU A 8 5.210 -5.412 51.822 1.00 22.49 C ANISOU 43 CA LEU B 8 3099 2702 2744 -27 -53 -374 C ATOM 44 C LEU A 8 6.237 -5.484 52.953 1.00 23.92 C ANISOU 44 C LEU B 8 3348 2851 2889 2 -56 -368 C ATOM 45 O LEU A 8 6.007 -6.146 53.993 1.00 24.80 O ANISOU 45 O LEU B 8 3480 2964 2978 22 -98 -367 O ATOM 46 CB LEU A 8 5.507 -6.524 50.816 1.00 20.39 C ANISOU 46 CB LEU B 8 2781 2463 2504 -3 -50 -371 C ATOM 47 CG LEU A 8 4.414 -6.875 49.821 1.00 23.05 C ANISOU 47 CG LEU B 8 3048 2834 2876 -24 -54 -375 C ATOM 48 CD1 LEU A 8 4.959 -7.866 48.853 1.00 18.06 C ANISOU 48 CD1 LEU B 8 2376 2221 2266 2 -41 -372 C ATOM 49 CD2 LEU A 8 3.134 -7.438 50.482 1.00 20.45 C ANISOU 49 CD2 LEU B 8 2690 2527 2553 -36 -103 -383 C ATOM 50 N ALA A 9 7.380 -4.832 52.740 1.00 22.63 N ANISOU 50 N ALA B 9 3221 2660 2719 5 -10 -367 N ATOM 51 CA ALA A 9 8.542 -4.995 53.597 1.00 22.91 C ANISOU 51 CA ALA B 9 3320 2660 2724 34 1 -362 C ATOM 52 C ALA A 9 9.430 -3.804 53.372 1.00 23.35 C ANISOU 52 C ALA B 9 3408 2685 2779 16 57 -369 C ATOM 53 O ALA A 9 9.445 -3.255 52.259 1.00 22.13 O ANISOU 53 O ALA B 9 3215 2544 2651 -4 84 -376 O ATOM 54 CB ALA A 9 9.305 -6.271 53.220 1.00 22.22 C ANISOU 54 CB ALA B 9 3219 2580 2643 75 0 -354 C ATOM 55 N MET A 10 10.163 -3.409 54.415 1.00 23.78 N ANISOU 55 N MET B 10 3533 2699 2803 23 73 -368 N ATOM 56 CA MET A 10 11.099 -2.298 54.338 1.00 25.68 C ANISOU 56 CA MET B 10 3806 2908 3044 6 129 -378 C ATOM 57 C MET A 10 12.291 -2.619 55.202 1.00 24.88 C ANISOU 57 C MET B 10 3776 2764 2915 32 152 -374 C ATOM 58 O MET A 10 12.151 -3.278 56.226 1.00 25.91 O ANISOU 58 O MET B 10 3948 2884 3015 57 121 -362 O ATOM 59 CB MET A 10 10.517 -1.014 54.927 1.00 24.69 C ANISOU 59 CB MET B 10 3704 2767 2909 -26 136 -385 C ATOM 60 CG MET A 10 9.378 -0.385 54.240 1.00 30.41 C ANISOU 60 CG MET B 10 4377 3520 3656 -54 124 -389 C ATOM 61 SD MET A 10 8.776 1.013 55.244 1.00 29.60 S ANISOU 61 SD MET B 10 4320 3390 3536 -84 134 -395 S ATOM 62 CE MET A 10 9.998 2.247 54.899 1.00 25.19 C ANISOU 62 CE MET B 10 3779 2804 2990 -95 200 -409 C ATOM 63 N ASP A 11 13.456 -2.158 54.772 1.00 25.10 N ANISOU 63 N ASP B 11 3816 2768 2952 26 207 -385 N ATOM 64 CA ASP A 11 14.614 -2.064 55.654 1.00 25.90 C ANISOU 64 CA ASP B 11 3995 2818 3029 38 247 -385 C ATOM 65 C ASP A 11 15.375 -0.771 55.402 1.00 25.34 C ANISOU 65 C ASP B 11 3932 2722 2972 5 307 -407 C ATOM 66 O ASP A 11 15.154 -0.097 54.393 1.00 25.29 O ANISOU 66 O ASP B 11 3870 2744 2997 -20 317 -421 O ATOM 67 CB ASP A 11 15.525 -3.289 55.527 1.00 25.56 C ANISOU 67 CB ASP B 11 3969 2763 2981 77 255 -376 C ATOM 68 CG ASP A 11 16.261 -3.583 56.807 1.00 27.90 C ANISOU 68 CG ASP B 11 4356 3008 3236 104 271 -364 C ATOM 69 OD1 ASP A 11 16.261 -2.701 57.698 1.00 29.28 O ANISOU 69 OD1 ASP B 11 4582 3153 3389 86 288 -368 O ATOM 70 OD2 ASP A 11 16.776 -4.713 56.958 1.00 29.84 O ANISOU 70 OD2 ASP B 11 4625 3243 3468 146 265 -350 O ATOM 71 N ILE A 12 16.272 -0.416 56.322 1.00 26.11 N ANISOU 71 N ILE B 12 4103 2769 3049 6 349 -411 N ATOM 72 CA ILE A 12 16.879 0.909 56.315 1.00 25.18 C ANISOU 72 CA ILE B 12 3996 2627 2945 -28 406 -435 C ATOM 73 C ILE A 12 18.318 0.791 56.717 1.00 26.71 C ANISOU 73 C ILE B 12 4250 2770 3130 -22 466 -443 C ATOM 74 O ILE A 12 18.649 0.025 57.612 1.00 27.00 O ANISOU 74 O ILE B 12 4352 2773 3132 8 464 -426 O ATOM 75 CB ILE A 12 16.137 1.909 57.280 1.00 25.94 C ANISOU 75 CB ILE B 12 4124 2709 3023 -47 400 -434 C ATOM 76 CG1 ILE A 12 16.815 3.294 57.267 1.00 24.12 C ANISOU 76 CG1 ILE B 12 3901 2453 2812 -81 462 -461 C ATOM 77 CG2 ILE A 12 15.998 1.341 58.734 1.00 23.02 C ANISOU 77 CG2 ILE B 12 3837 2305 2605 -22 380 -414 C ATOM 78 CD1 ILE A 12 15.960 4.426 57.952 1.00 25.65 C ANISOU 78 CD1 ILE B 12 4108 2640 2998 -102 458 -463 C ATOM 79 N TYR A 13 19.176 1.534 56.027 1.00 27.25 N ANISOU 79 N TYR B 13 4295 2832 3229 -50 519 -472 N ATOM 80 CA TYR A 13 20.554 1.635 56.430 1.00 27.55 C ANISOU 80 CA TYR B 13 4390 2816 3263 -54 588 -487 C ATOM 81 C TYR A 13 20.989 3.088 56.511 1.00 27.09 C ANISOU 81 C TYR B 13 4328 2739 3225 -95 641 -519 C ATOM 82 O TYR A 13 20.736 3.868 55.596 1.00 26.50 O ANISOU 82 O TYR B 13 4182 2702 3183 -120 637 -539 O ATOM 83 CB TYR A 13 21.502 0.835 55.498 1.00 27.81 C ANISOU 83 CB TYR B 13 4401 2850 3314 -45 612 -497 C ATOM 84 CG TYR A 13 22.934 0.948 56.001 1.00 27.78 C ANISOU 84 CG TYR B 13 4464 2784 3307 -53 690 -514 C ATOM 85 CD1 TYR A 13 23.372 0.149 57.053 1.00 27.70 C ANISOU 85 CD1 TYR B 13 4543 2723 3258 -20 704 -490 C ATOM 86 CD2 TYR A 13 23.805 1.900 55.487 1.00 26.36 C ANISOU 86 CD2 TYR B 13 4260 2594 3159 -94 749 -555 C ATOM 87 CE1 TYR A 13 24.641 0.277 57.565 1.00 28.16 C ANISOU 87 CE1 TYR B 13 4670 2719 3312 -28 781 -504 C ATOM 88 CE2 TYR A 13 25.112 2.050 56.004 1.00 27.80 C ANISOU 88 CE2 TYR B 13 4506 2715 3342 -107 828 -574 C ATOM 89 CZ TYR A 13 25.505 1.218 57.048 1.00 28.81 C ANISOU 89 CZ TYR B 13 4728 2789 3431 -74 845 -547 C ATOM 90 OH TYR A 13 26.769 1.296 57.578 1.00 29.52 O ANISOU 90 OH TYR B 13 4888 2812 3517 -85 927 -563 O ATOM 91 N PHE A 14 21.666 3.440 57.604 1.00 27.37 N ANISOU 91 N PHE B 14 4442 2718 3242 -101 691 -523 N ATOM 92 CA PHE A 14 22.413 4.708 57.674 1.00 27.01 C ANISOU 92 CA PHE B 14 4395 2645 3220 -140 759 -559 C ATOM 93 C PHE A 14 23.823 4.467 58.265 1.00 27.80 C ANISOU 93 C PHE B 14 4570 2679 3312 -143 835 -571 C ATOM 94 O PHE A 14 24.049 3.506 59.023 1.00 27.18 O ANISOU 94 O PHE B 14 4567 2564 3196 -110 835 -544 O ATOM 95 CB PHE A 14 21.627 5.790 58.457 1.00 27.23 C ANISOU 95 CB PHE B 14 4437 2668 3240 -156 753 -558 C ATOM 96 CG PHE A 14 21.191 5.336 59.809 1.00 28.59 C ANISOU 96 CG PHE B 14 4696 2805 3363 -132 736 -527 C ATOM 97 CD1 PHE A 14 22.077 5.394 60.895 1.00 28.77 C ANISOU 97 CD1 PHE B 14 4812 2761 3360 -131 797 -528 C ATOM 98 CD2 PHE A 14 19.920 4.808 60.001 1.00 28.73 C ANISOU 98 CD2 PHE B 14 4705 2855 3355 -109 660 -497 C ATOM 99 CE1 PHE A 14 21.710 4.949 62.148 1.00 28.33 C ANISOU 99 CE1 PHE B 14 4841 2672 3250 -105 780 -500 C ATOM 100 CE2 PHE A 14 19.531 4.357 61.269 1.00 29.17 C ANISOU 100 CE2 PHE B 14 4841 2881 3360 -85 640 -472 C ATOM 101 CZ PHE A 14 20.428 4.439 62.342 1.00 30.32 C ANISOU 101 CZ PHE B 14 5082 2962 3477 -82 698 -472 C ATOM 102 N PRO A 15 24.792 5.307 57.880 1.00 28.36 N ANISOU 102 N PRO B 15 4622 2735 3420 -181 902 -613 N ATOM 103 CA PRO A 15 26.125 5.084 58.410 1.00 29.96 C ANISOU 103 CA PRO B 15 4895 2871 3617 -188 981 -627 C ATOM 104 C PRO A 15 26.161 5.220 59.949 1.00 30.87 C ANISOU 104 C PRO B 15 5116 2924 3691 -178 1012 -607 C ATOM 105 O PRO A 15 25.489 6.104 60.508 1.00 30.92 O ANISOU 105 O PRO B 15 5124 2934 3692 -191 1003 -607 O ATOM 106 CB PRO A 15 26.978 6.156 57.725 1.00 30.07 C ANISOU 106 CB PRO B 15 4854 2888 3682 -237 1041 -682 C ATOM 107 CG PRO A 15 26.123 6.800 56.695 1.00 29.48 C ANISOU 107 CG PRO B 15 4676 2887 3636 -248 986 -693 C ATOM 108 CD PRO A 15 24.717 6.454 56.958 1.00 28.09 C ANISOU 108 CD PRO B 15 4499 2743 3431 -216 907 -650 C ATOM 109 N PRO A 16 26.928 4.342 60.636 1.00 31.47 N ANISOU 109 N PRO B 16 5282 2942 3733 -154 1049 -590 N ATOM 110 CA PRO A 16 27.004 4.439 62.095 1.00 31.70 C ANISOU 110 CA PRO B 16 5419 2909 3716 -141 1080 -570 C ATOM 111 C PRO A 16 27.732 5.694 62.571 1.00 32.89 C ANISOU 111 C PRO B 16 5594 3014 3890 -189 1169 -608 C ATOM 112 O PRO A 16 27.548 6.125 63.697 1.00 33.57 O ANISOU 112 O PRO B 16 5750 3060 3944 -188 1190 -597 O ATOM 113 CB PRO A 16 27.740 3.158 62.503 1.00 32.51 C ANISOU 113 CB PRO B 16 5607 2964 3782 -100 1100 -543 C ATOM 114 CG PRO A 16 28.537 2.758 61.278 1.00 32.13 C ANISOU 114 CG PRO B 16 5501 2931 3777 -113 1124 -569 C ATOM 115 CD PRO A 16 27.713 3.211 60.099 1.00 31.55 C ANISOU 115 CD PRO B 16 5304 2940 3745 -132 1062 -585 C ATOM 116 N THR A 17 28.541 6.279 61.702 1.00 33.82 N ANISOU 116 N THR B 17 5650 3139 4062 -230 1220 -654 N ATOM 117 CA THR A 17 29.380 7.428 62.041 1.00 33.98 C ANISOU 117 CA THR B 17 5682 3116 4113 -278 1312 -698 C ATOM 118 C THR A 17 28.496 8.687 62.032 1.00 34.08 C ANISOU 118 C THR B 17 5633 3169 4148 -301 1285 -712 C ATOM 119 O THR A 17 27.799 8.948 61.046 1.00 32.96 O ANISOU 119 O THR B 17 5393 3098 4034 -303 1224 -719 O ATOM 120 CB THR A 17 30.566 7.541 61.042 1.00 34.39 C ANISOU 120 CB THR B 17 5682 3168 4218 -315 1371 -747 C ATOM 121 OG1 THR A 17 30.116 7.241 59.699 1.00 33.69 O ANISOU 121 OG1 THR B 17 5491 3155 4154 -309 1301 -752 O ATOM 122 CG2 THR A 17 31.643 6.514 61.371 1.00 34.54 C ANISOU 122 CG2 THR B 17 5789 3120 4214 -300 1429 -738 C ATOM 123 N CYS A 18 28.506 9.436 63.136 1.00 33.90 N ANISOU 123 N CYS B 18 5672 3099 4110 -314 1333 -715 N ATOM 124 CA CYS A 18 27.669 10.617 63.283 1.00 34.57 C ANISOU 124 CA CYS B 18 5712 3211 4211 -331 1314 -725 C ATOM 125 C CYS A 18 28.317 11.724 64.118 1.00 34.42 C ANISOU 125 C CYS B 18 5734 3135 4208 -368 1410 -757 C ATOM 126 O CYS A 18 29.340 11.536 64.779 1.00 35.50 O ANISOU 126 O CYS B 18 5952 3202 4333 -379 1491 -766 O ATOM 127 CB CYS A 18 26.335 10.223 63.906 1.00 35.02 C ANISOU 127 CB CYS B 18 5803 3286 4216 -293 1235 -676 C ATOM 128 SG CYS A 18 26.506 9.388 65.524 1.00 39.62 S ANISOU 128 SG CYS B 18 6544 3790 4720 -259 1258 -634 S ATOM 129 N VAL A 19 27.725 12.899 64.053 1.00 33.69 N ANISOU 129 N VAL B 19 5584 3070 4145 -388 1403 -776 N ATOM 130 CA VAL A 19 28.166 14.019 64.852 1.00 32.82 C ANISOU 130 CA VAL B 19 5506 2912 4052 -421 1487 -806 C ATOM 131 C VAL A 19 26.939 14.662 65.506 1.00 32.22 C ANISOU 131 C VAL B 19 5441 2847 3954 -409 1448 -784 C ATOM 132 O VAL A 19 25.908 14.928 64.850 1.00 30.69 O ANISOU 132 O VAL B 19 5171 2718 3773 -397 1372 -775 O ATOM 133 CB VAL A 19 28.985 15.030 64.004 1.00 32.88 C ANISOU 133 CB VAL B 19 5417 2940 4136 -466 1542 -870 C ATOM 134 CG1 VAL A 19 28.111 15.646 62.890 1.00 32.11 C ANISOU 134 CG1 VAL B 19 5195 2930 4076 -463 1466 -880 C ATOM 135 CG2 VAL A 19 29.631 16.117 64.869 1.00 32.80 C ANISOU 135 CG2 VAL B 19 5442 2871 4149 -504 1645 -906 C ATOM 136 N GLN A 20 27.061 14.909 66.805 1.00 32.52 N ANISOU 136 N GLN B 20 5582 2819 3958 -411 1504 -775 N ATOM 137 CA GLN A 20 25.995 15.520 67.569 1.00 32.84 C ANISOU 137 CA GLN B 20 5648 2858 3972 -403 1479 -757 C ATOM 138 C GLN A 20 25.854 16.998 67.221 1.00 32.38 C ANISOU 138 C GLN B 20 5505 2822 3975 -435 1508 -798 C ATOM 139 O GLN A 20 26.839 17.713 67.118 1.00 32.48 O ANISOU 139 O GLN B 20 5494 2812 4036 -469 1590 -843 O ATOM 140 CB GLN A 20 26.204 15.252 69.054 1.00 34.54 C ANISOU 140 CB GLN B 20 6004 2993 4124 -394 1529 -735 C ATOM 141 CG GLN A 20 26.056 13.751 69.404 1.00 37.38 C ANISOU 141 CG GLN B 20 6444 3343 4416 -350 1475 -686 C ATOM 142 CD GLN A 20 24.600 13.284 69.538 1.00 41.28 C ANISOU 142 CD GLN B 20 6936 3883 4866 -315 1366 -646 C ATOM 143 OE1 GLN A 20 23.671 14.085 69.710 1.00 45.43 O ANISOU 143 OE1 GLN B 20 7435 4430 5397 -322 1342 -648 O ATOM 144 NE2 GLN A 20 24.402 11.978 69.468 1.00 45.25 N ANISOU 144 NE2 GLN B 20 7467 4401 5326 -276 1303 -610 N ATOM 145 N GLN A 21 24.614 17.439 66.982 1.00 31.77 N ANISOU 145 N GLN B 21 5378 2793 3899 -421 1440 -784 N ATOM 146 CA GLN A 21 24.341 18.823 66.559 1.00 31.81 C ANISOU 146 CA GLN B 21 5297 2828 3961 -441 1455 -818 C ATOM 147 C GLN A 21 24.746 19.853 67.626 1.00 32.59 C ANISOU 147 C GLN B 21 5450 2865 4069 -467 1550 -842 C ATOM 148 O GLN A 21 25.279 20.920 67.319 1.00 31.81 O ANISOU 148 O GLN B 21 5287 2769 4030 -495 1607 -888 O ATOM 149 CB GLN A 21 22.853 19.019 66.214 1.00 30.42 C ANISOU 149 CB GLN B 21 5075 2706 3775 -418 1366 -790 C ATOM 150 CG GLN A 21 22.438 18.391 64.870 1.00 30.46 C ANISOU 150 CG GLN B 21 4993 2785 3794 -399 1281 -779 C ATOM 151 CD GLN A 21 22.990 19.115 63.661 1.00 29.18 C ANISOU 151 CD GLN B 21 4717 2670 3700 -416 1294 -821 C ATOM 152 OE1 GLN A 21 23.690 20.123 63.787 1.00 29.06 O ANISOU 152 OE1 GLN B 21 4677 2635 3727 -443 1365 -863 O ATOM 153 NE2 GLN A 21 22.629 18.638 62.469 1.00 27.83 N ANISOU 153 NE2 GLN B 21 4472 2562 3539 -401 1223 -813 N ATOM 154 N GLU A 22 24.466 19.540 68.876 1.00 33.94 N ANISOU 154 N GLU B 22 5737 2980 4179 -456 1566 -813 N ATOM 155 CA GLU A 22 24.945 20.402 69.980 1.00 35.84 C ANISOU 155 CA GLU B 22 6046 3151 4421 -481 1667 -835 C ATOM 156 C GLU A 22 26.460 20.707 69.919 1.00 35.87 C ANISOU 156 C GLU B 22 6045 3114 4471 -518 1772 -882 C ATOM 157 O GLU A 22 26.888 21.876 70.054 1.00 35.90 O ANISOU 157 O GLU B 22 6014 3100 4526 -549 1847 -925 O ATOM 158 CB GLU A 22 24.592 19.779 71.318 1.00 37.04 C ANISOU 158 CB GLU B 22 6338 3244 4489 -462 1669 -796 C ATOM 159 CG GLU A 22 24.558 20.819 72.458 1.00 43.03 C ANISOU 159 CG GLU B 22 7162 3944 5242 -481 1749 -810 C ATOM 160 CD GLU A 22 23.663 20.384 73.601 1.00 49.36 C ANISOU 160 CD GLU B 22 8078 4716 5960 -456 1714 -768 C ATOM 161 OE1 GLU A 22 22.531 20.941 73.710 1.00 51.18 O ANISOU 161 OE1 GLU B 22 8287 4972 6187 -449 1671 -760 O ATOM 162 OE2 GLU A 22 24.094 19.478 74.366 1.00 51.75 O ANISOU 162 OE2 GLU B 22 8491 4970 6201 -441 1730 -744 O ATOM 163 N ALA A 23 27.260 19.664 69.716 1.00 35.86 N ANISOU 163 N ALA B 23 6077 3097 4452 -515 1779 -875 N ATOM 164 CA ALA A 23 28.724 19.795 69.601 1.00 36.71 C ANISOU 164 CA ALA B 23 6183 3164 4601 -551 1878 -919 C ATOM 165 C ALA A 23 29.125 20.597 68.345 1.00 37.33 C ANISOU 165 C ALA B 23 6115 3302 4767 -580 1881 -973 C ATOM 166 O ALA A 23 30.021 21.454 68.390 1.00 37.13 O ANISOU 166 O ALA B 23 6061 3251 4797 -620 1973 -1026 O ATOM 167 CB ALA A 23 29.382 18.413 69.598 1.00 36.83 C ANISOU 167 CB ALA B 23 6267 3152 4575 -535 1875 -894 C ATOM 168 N LEU A 24 28.446 20.319 67.226 1.00 37.17 N ANISOU 168 N LEU B 24 6004 3363 4758 -558 1782 -961 N ATOM 169 CA LEU A 24 28.630 21.086 65.998 1.00 37.21 C ANISOU 169 CA LEU B 24 5869 3434 4836 -576 1767 -1007 C ATOM 170 C LEU A 24 28.304 22.576 66.143 1.00 37.49 C ANISOU 170 C LEU B 24 5845 3480 4918 -591 1798 -1038 C ATOM 171 O LEU A 24 29.051 23.412 65.641 1.00 37.08 O ANISOU 171 O LEU B 24 5712 3444 4934 -622 1848 -1095 O ATOM 172 CB LEU A 24 27.829 20.467 64.859 1.00 36.95 C ANISOU 172 CB LEU B 24 5764 3480 4795 -544 1653 -980 C ATOM 173 CG LEU A 24 28.122 20.898 63.422 1.00 37.37 C ANISOU 173 CG LEU B 24 5681 3606 4910 -556 1625 -1021 C ATOM 174 CD1 LEU A 24 29.605 20.730 62.999 1.00 37.34 C ANISOU 174 CD1 LEU B 24 5656 3585 4946 -593 1695 -1072 C ATOM 175 CD2 LEU A 24 27.212 20.085 62.513 1.00 35.74 C ANISOU 175 CD2 LEU B 24 5437 3465 4678 -519 1514 -981 C ATOM 176 N GLU A 25 27.194 22.901 66.808 1.00 37.77 N ANISOU 176 N GLU B 25 5921 3510 4921 -568 1767 -1004 N ATOM 177 CA GLU A 25 26.900 24.297 67.194 1.00 39.36 C ANISOU 177 CA GLU B 25 6090 3705 5160 -580 1810 -1031 C ATOM 178 C GLU A 25 28.122 24.935 67.882 1.00 40.82 C ANISOU 178 C GLU B 25 6305 3824 5381 -623 1938 -1080 C ATOM 179 O GLU A 25 28.570 26.015 67.493 1.00 40.78 O ANISOU 179 O GLU B 25 6211 3838 5445 -648 1982 -1133 O ATOM 180 CB GLU A 25 25.694 24.378 68.154 1.00 39.39 C ANISOU 180 CB GLU B 25 6174 3685 5109 -554 1781 -985 C ATOM 181 CG GLU A 25 24.296 24.167 67.530 1.00 37.73 C ANISOU 181 CG GLU B 25 5919 3540 4877 -517 1666 -945 C ATOM 182 CD GLU A 25 23.202 24.077 68.589 1.00 39.36 C ANISOU 182 CD GLU B 25 6219 3714 5022 -497 1644 -903 C ATOM 183 OE1 GLU A 25 23.523 24.174 69.793 1.00 39.38 O ANISOU 183 OE1 GLU B 25 6322 3646 4996 -510 1714 -903 O ATOM 184 OE2 GLU A 25 22.016 23.916 68.243 1.00 37.96 O ANISOU 184 OE2 GLU B 25 6019 3579 4825 -471 1560 -871 O ATOM 185 N ALA A 26 28.651 24.253 68.897 1.00 41.67 N ANISOU 185 N ALA B 26 6538 3855 5439 -631 1996 -1063 N ATOM 186 CA ALA A 26 29.773 24.800 69.668 1.00 43.57 C ANISOU 186 CA ALA B 26 6826 4023 5707 -673 2126 -1105 C ATOM 187 C ALA A 26 31.007 24.941 68.783 1.00 44.09 C ANISOU 187 C ALA B 26 6804 4106 5842 -711 2173 -1164 C ATOM 188 O ALA A 26 31.594 26.006 68.733 1.00 44.47 O ANISOU 188 O ALA B 26 6790 4150 5957 -747 2245 -1222 O ATOM 189 CB ALA A 26 30.061 23.956 70.919 1.00 43.57 C ANISOU 189 CB ALA B 26 6989 3936 5632 -669 2175 -1069 C ATOM 190 N HIS A 27 31.344 23.892 68.033 1.00 44.88 N ANISOU 190 N HIS B 27 6892 4231 5928 -703 2126 -1153 N ATOM 191 CA HIS A 27 32.438 23.929 67.055 1.00 45.97 C ANISOU 191 CA HIS B 27 6943 4396 6129 -738 2156 -1210 C ATOM 192 C HIS A 27 32.349 25.099 66.075 1.00 46.64 C ANISOU 192 C HIS B 27 6873 4555 6291 -751 2135 -1262 C ATOM 193 O HIS A 27 33.371 25.726 65.752 1.00 47.03 O ANISOU 193 O HIS B 27 6857 4603 6407 -795 2206 -1329 O ATOM 194 CB HIS A 27 32.488 22.616 66.259 1.00 45.36 C ANISOU 194 CB HIS B 27 6866 4350 6019 -716 2083 -1181 C ATOM 195 CG HIS A 27 33.447 22.635 65.107 1.00 44.87 C ANISOU 195 CG HIS B 27 6704 4326 6017 -748 2096 -1237 C ATOM 196 ND1 HIS A 27 33.160 23.252 63.908 1.00 44.29 N ANISOU 196 ND1 HIS B 27 6491 4343 5995 -747 2033 -1268 N ATOM 197 CD2 HIS A 27 34.686 22.100 64.964 1.00 45.68 C ANISOU 197 CD2 HIS B 27 6830 4391 6135 -782 2164 -1269 C ATOM 198 CE1 HIS A 27 34.180 23.104 63.080 1.00 44.50 C ANISOU 198 CE1 HIS B 27 6457 4387 6065 -780 2059 -1319 C ATOM 199 NE2 HIS A 27 35.112 22.399 63.692 1.00 43.39 N ANISOU 199 NE2 HIS B 27 6412 4169 5904 -803 2139 -1321 N ATOM 200 N ASP A 28 31.144 25.340 65.566 1.00 46.80 N ANISOU 200 N ASP B 28 6836 4643 6303 -712 2034 -1232 N ATOM 201 CA ASP A 28 30.864 26.472 64.683 1.00 48.00 C ANISOU 201 CA ASP B 28 6850 4869 6519 -711 2002 -1271 C ATOM 202 C ASP A 28 30.737 27.682 65.599 1.00 48.92 C ANISOU 202 C ASP B 28 6977 4947 6663 -724 2075 -1292 C ATOM 203 O ASP A 28 30.795 27.554 66.832 1.00 49.92 O ANISOU 203 O ASP B 28 7220 4995 6752 -732 2140 -1272 O ATOM 204 CB ASP A 28 29.545 26.261 63.899 1.00 47.14 C ANISOU 204 CB ASP B 28 6692 4835 6383 -661 1875 -1225 C ATOM 205 CG ASP A 28 29.580 25.060 62.944 1.00 47.07 C ANISOU 205 CG ASP B 28 6668 4868 6348 -646 1800 -1203 C ATOM 206 OD1 ASP A 28 30.665 24.574 62.568 1.00 46.54 O ANISOU 206 OD1 ASP B 28 6593 4792 6300 -674 1836 -1235 O ATOM 207 OD2 ASP A 28 28.488 24.615 62.536 1.00 45.20 O ANISOU 207 OD2 ASP B 28 6426 4674 6075 -605 1704 -1154 O ATOM 208 N GLY A 29 30.563 28.871 65.051 1.00 49.43 N ANISOU 208 N GLY B 29 6928 5065 6790 -724 2067 -1331 N ATOM 209 CA GLY A 29 30.464 30.014 65.973 1.00 51.34 C ANISOU 209 CA GLY B 29 7183 5264 7058 -735 2144 -1351 C ATOM 210 C GLY A 29 29.054 30.269 66.482 1.00 51.38 C ANISOU 210 C GLY B 29 7231 5270 7020 -692 2091 -1296 C ATOM 211 O GLY A 29 28.729 31.400 66.773 1.00 51.80 O ANISOU 211 O GLY B 29 7249 5323 7109 -689 2121 -1315 O ATOM 212 N ALA A 30 28.235 29.213 66.604 1.00 51.74 N ANISOU 212 N ALA B 30 7354 5314 6991 -660 2016 -1230 N ATOM 213 CA ALA A 30 26.755 29.313 66.681 1.00 51.19 C ANISOU 213 CA ALA B 30 7298 5270 6882 -615 1935 -1178 C ATOM 214 C ALA A 30 26.135 29.360 68.085 1.00 51.85 C ANISOU 214 C ALA B 30 7506 5282 6913 -610 1971 -1142 C ATOM 215 O ALA A 30 26.532 28.615 68.993 1.00 52.19 O ANISOU 215 O ALA B 30 7665 5259 6906 -623 2015 -1124 O ATOM 216 CB ALA A 30 26.097 28.193 65.852 1.00 50.16 C ANISOU 216 CB ALA B 30 7160 5191 6706 -583 1822 -1131 C ATOM 217 N SER A 31 25.144 30.233 68.240 1.00 52.27 N ANISOU 217 N SER B 31 7538 5350 6974 -587 1951 -1131 N ATOM 218 CA SER A 31 24.448 30.405 69.512 1.00 52.96 C ANISOU 218 CA SER B 31 7735 5376 7013 -581 1982 -1101 C ATOM 219 C SER A 31 23.713 29.110 69.846 1.00 52.24 C ANISOU 219 C SER B 31 7741 5274 6835 -559 1909 -1040 C ATOM 220 O SER A 31 23.242 28.412 68.938 1.00 51.76 O ANISOU 220 O SER B 31 7636 5271 6760 -536 1816 -1014 O ATOM 221 CB SER A 31 23.482 31.587 69.422 1.00 53.24 C ANISOU 221 CB SER B 31 7715 5437 7079 -558 1966 -1103 C ATOM 222 OG SER A 31 22.830 31.604 68.152 1.00 54.68 O ANISOU 222 OG SER B 31 7794 5702 7280 -527 1868 -1092 O ATOM 223 N LYS A 32 23.658 28.763 71.133 1.00 51.81 N ANISOU 223 N LYS B 32 7818 5147 6722 -565 1953 -1018 N ATOM 224 CA LYS A 32 23.128 27.463 71.563 1.00 51.21 C ANISOU 224 CA LYS B 32 7841 5057 6561 -546 1892 -964 C ATOM 225 C LYS A 32 21.717 27.233 71.023 1.00 49.12 C ANISOU 225 C LYS B 32 7542 4850 6272 -511 1780 -925 C ATOM 226 O LYS A 32 20.877 28.140 71.034 1.00 48.22 O ANISOU 226 O LYS B 32 7396 4750 6177 -501 1771 -926 O ATOM 227 CB LYS A 32 23.153 27.317 73.097 1.00 51.97 C ANISOU 227 CB LYS B 32 8084 5067 6594 -554 1955 -948 C ATOM 228 CG LYS A 32 22.810 25.887 73.602 1.00 53.41 C ANISOU 228 CG LYS B 32 8374 5234 6686 -533 1896 -897 C ATOM 229 CD LYS A 32 22.594 25.826 75.123 1.00 53.71 C ANISOU 229 CD LYS B 32 8559 5195 6654 -533 1943 -877 C ATOM 230 CE LYS A 32 23.878 25.401 75.831 1.00 58.89 C ANISOU 230 CE LYS B 32 9307 5781 7289 -553 2035 -888 C ATOM 231 NZ LYS A 32 23.749 25.387 77.334 1.00 62.61 N ANISOU 231 NZ LYS B 32 9929 6173 7689 -553 2089 -871 N ATOM 232 N GLY A 33 21.487 26.029 70.507 1.00 47.44 N ANISOU 232 N GLY B 33 7333 4671 6023 -493 1699 -893 N ATOM 233 CA GLY A 33 20.172 25.646 70.008 1.00 45.07 C ANISOU 233 CA GLY B 33 7007 4422 5696 -463 1594 -855 C ATOM 234 C GLY A 33 19.864 26.106 68.598 1.00 43.43 C ANISOU 234 C GLY B 33 6665 4291 5545 -451 1541 -867 C ATOM 235 O GLY A 33 18.788 25.819 68.079 1.00 42.72 O ANISOU 235 O GLY B 33 6549 4244 5439 -427 1459 -837 O ATOM 236 N LYS A 34 20.806 26.802 67.964 1.00 42.39 N ANISOU 236 N LYS B 34 6450 4176 5480 -467 1588 -912 N ATOM 237 CA LYS A 34 20.652 27.162 66.558 1.00 41.17 C ANISOU 237 CA LYS B 34 6169 4098 5376 -453 1536 -925 C ATOM 238 C LYS A 34 20.329 25.948 65.664 1.00 39.55 C ANISOU 238 C LYS B 34 5943 3943 5142 -434 1444 -894 C ATOM 239 O LYS A 34 19.552 26.058 64.704 1.00 38.53 O ANISOU 239 O LYS B 34 5742 3872 5025 -411 1375 -880 O ATOM 240 CB LYS A 34 21.898 27.838 66.031 1.00 41.66 C ANISOU 240 CB LYS B 34 6150 4171 5506 -476 1597 -982 C ATOM 241 CG LYS A 34 21.626 28.637 64.786 1.00 43.05 C ANISOU 241 CG LYS B 34 6198 4422 5738 -458 1554 -1001 C ATOM 242 CD LYS A 34 22.765 28.530 63.796 1.00 44.10 C ANISOU 242 CD LYS B 34 6246 4595 5917 -475 1561 -1044 C ATOM 243 CE LYS A 34 22.765 29.701 62.830 1.00 47.22 C ANISOU 243 CE LYS B 34 6514 5050 6376 -462 1549 -1081 C ATOM 244 NZ LYS A 34 21.373 30.103 62.455 1.00 49.76 N ANISOU 244 NZ LYS B 34 6812 5410 6686 -420 1480 -1044 N ATOM 245 N TYR A 35 20.924 24.803 65.997 1.00 37.84 N ANISOU 245 N TYR B 35 5792 3700 4888 -443 1448 -881 N ATOM 246 CA TYR A 35 20.753 23.591 65.209 1.00 35.55 C ANISOU 246 CA TYR B 35 5484 3450 4572 -427 1371 -854 C ATOM 247 C TYR A 35 19.698 22.690 65.856 1.00 34.94 C ANISOU 247 C TYR B 35 5491 3359 4426 -406 1314 -803 C ATOM 248 O TYR A 35 18.820 22.141 65.163 1.00 33.94 O ANISOU 248 O TYR B 35 5330 3281 4284 -385 1231 -775 O ATOM 249 CB TYR A 35 22.095 22.823 64.998 1.00 33.93 C ANISOU 249 CB TYR B 35 5287 3231 4372 -445 1406 -874 C ATOM 250 CG TYR A 35 23.207 23.610 64.310 1.00 33.04 C ANISOU 250 CG TYR B 35 5089 3135 4329 -470 1461 -931 C ATOM 251 CD1 TYR A 35 24.559 23.229 64.451 1.00 32.76 C ANISOU 251 CD1 TYR B 35 5077 3065 4306 -498 1527 -960 C ATOM 252 CD2 TYR A 35 22.926 24.730 63.532 1.00 31.87 C ANISOU 252 CD2 TYR B 35 4837 3038 4235 -465 1449 -957 C ATOM 253 CE1 TYR A 35 25.578 23.953 63.844 1.00 32.55 C ANISOU 253 CE1 TYR B 35 4968 3054 4344 -526 1579 -1018 C ATOM 254 CE2 TYR A 35 23.932 25.455 62.911 1.00 32.98 C ANISOU 254 CE2 TYR B 35 4894 3199 4439 -488 1494 -1013 C ATOM 255 CZ TYR A 35 25.260 25.072 63.077 1.00 34.34 C ANISOU 255 CZ TYR B 35 5087 3337 4624 -521 1560 -1046 C ATOM 256 OH TYR A 35 26.242 25.821 62.468 1.00 33.74 O ANISOU 256 OH TYR B 35 4923 3283 4614 -548 1605 -1107 O ATOM 257 N THR A 36 19.785 22.523 67.170 1.00 33.94 N ANISOU 257 N THR B 36 5473 3169 4256 -414 1356 -793 N ATOM 258 CA THR A 36 18.924 21.551 67.853 1.00 34.21 C ANISOU 258 CA THR B 36 5590 3188 4219 -396 1301 -749 C ATOM 259 C THR A 36 17.484 22.028 67.987 1.00 34.06 C ANISOU 259 C THR B 36 5566 3187 4188 -383 1254 -730 C ATOM 260 O THR A 36 16.575 21.202 68.077 1.00 33.91 O ANISOU 260 O THR B 36 5575 3184 4124 -367 1184 -696 O ATOM 261 CB THR A 36 19.451 21.168 69.250 1.00 34.26 C ANISOU 261 CB THR B 36 5723 3120 4174 -404 1358 -742 C ATOM 262 OG1 THR A 36 19.661 22.351 70.015 1.00 34.77 O ANISOU 262 OG1 THR B 36 5815 3139 4257 -424 1439 -768 O ATOM 263 CG2 THR A 36 20.763 20.396 69.143 1.00 34.84 C ANISOU 263 CG2 THR B 36 5818 3173 4247 -411 1394 -752 C ATOM 264 N ILE A 37 17.305 23.353 68.002 1.00 34.32 N ANISOU 264 N ILE B 37 5563 3215 4262 -392 1296 -753 N ATOM 265 CA ILE A 37 15.997 23.998 68.124 1.00 34.54 C ANISOU 265 CA ILE B 37 5585 3253 4285 -381 1266 -739 C ATOM 266 C ILE A 37 15.624 24.648 66.811 1.00 34.03 C ANISOU 266 C ILE B 37 5404 3250 4276 -368 1233 -748 C ATOM 267 O ILE A 37 14.543 24.358 66.270 1.00 34.57 O ANISOU 267 O ILE B 37 5446 3356 4332 -351 1162 -722 O ATOM 268 CB ILE A 37 15.931 25.112 69.248 1.00 34.95 C ANISOU 268 CB ILE B 37 5694 3246 4338 -395 1343 -756 C ATOM 269 CG1 ILE A 37 16.397 24.616 70.635 1.00 37.49 C ANISOU 269 CG1 ILE B 37 6142 3500 4604 -408 1390 -750 C ATOM 270 CG2 ILE A 37 14.509 25.795 69.303 1.00 35.06 C ANISOU 270 CG2 ILE B 37 5700 3270 4350 -383 1311 -741 C ATOM 271 CD1 ILE A 37 15.681 23.389 71.187 1.00 41.87 C ANISOU 271 CD1 ILE B 37 6776 4050 5082 -395 1323 -712 C ATOM 272 N GLY A 38 16.501 25.515 66.300 1.00 32.96 N ANISOU 272 N GLY B 38 5198 3125 4199 -376 1283 -785 N ATOM 273 CA GLY A 38 16.224 26.265 65.072 1.00 32.56 C ANISOU 273 CA GLY B 38 5037 3134 4202 -360 1255 -797 C ATOM 274 C GLY A 38 16.043 25.369 63.845 1.00 32.03 C ANISOU 274 C GLY B 38 4911 3128 4131 -344 1176 -779 C ATOM 275 O GLY A 38 15.242 25.682 62.946 1.00 31.49 O ANISOU 275 O GLY B 38 4779 3106 4078 -322 1126 -767 O ATOM 276 N LEU A 39 16.805 24.270 63.800 1.00 31.00 N ANISOU 276 N LEU B 39 4803 2994 3980 -354 1169 -777 N ATOM 277 CA LEU A 39 16.633 23.243 62.763 1.00 30.25 C ANISOU 277 CA LEU B 39 4668 2952 3875 -340 1097 -757 C ATOM 278 C LEU A 39 15.804 22.110 63.297 1.00 29.43 C ANISOU 278 C LEU B 39 4636 2836 3712 -332 1046 -716 C ATOM 279 O LEU A 39 15.175 21.386 62.535 1.00 28.92 O ANISOU 279 O LEU B 39 4541 2813 3635 -317 978 -693 O ATOM 280 CB LEU A 39 18.003 22.693 62.277 1.00 30.47 C ANISOU 280 CB LEU B 39 4669 2987 3921 -354 1120 -783 C ATOM 281 CG LEU A 39 18.901 23.608 61.437 1.00 31.53 C ANISOU 281 CG LEU B 39 4712 3152 4118 -363 1155 -829 C ATOM 282 CD1 LEU A 39 20.170 22.846 60.984 1.00 30.75 C ANISOU 282 CD1 LEU B 39 4598 3057 4029 -380 1173 -852 C ATOM 283 CD2 LEU A 39 18.154 24.174 60.209 1.00 33.96 C ANISOU 283 CD2 LEU B 39 4924 3526 4452 -338 1099 -826 C ATOM 284 N GLY A 40 15.776 21.965 64.622 1.00 29.43 N ANISOU 284 N GLY B 40 4732 2777 3672 -342 1078 -708 N ATOM 285 CA GLY A 40 15.097 20.835 65.230 1.00 28.71 C ANISOU 285 CA GLY B 40 4714 2674 3521 -334 1030 -673 C ATOM 286 C GLY A 40 15.845 19.521 65.062 1.00 28.39 C ANISOU 286 C GLY B 40 4691 2638 3458 -330 1010 -664 C ATOM 287 O GLY A 40 15.252 18.458 65.212 1.00 27.68 O ANISOU 287 O GLY B 40 4634 2558 3327 -317 953 -635 O ATOM 288 N GLN A 41 17.155 19.589 64.809 1.00 28.67 N ANISOU 288 N GLN B 41 4708 2664 3521 -342 1062 -691 N ATOM 289 CA GLN A 41 17.980 18.387 64.540 1.00 28.74 C ANISOU 289 CA GLN B 41 4730 2675 3515 -338 1052 -686 C ATOM 290 C GLN A 41 18.888 17.995 65.689 1.00 29.31 C ANISOU 290 C GLN B 41 4901 2681 3554 -346 1111 -688 C ATOM 291 O GLN A 41 19.536 18.857 66.264 1.00 30.59 O ANISOU 291 O GLN B 41 5088 2801 3735 -367 1188 -715 O ATOM 292 CB GLN A 41 18.839 18.627 63.295 1.00 28.13 C ANISOU 292 CB GLN B 41 4559 2636 3493 -345 1065 -716 C ATOM 293 CG GLN A 41 18.010 18.744 62.023 1.00 26.46 C ANISOU 293 CG GLN B 41 4255 2494 3305 -330 998 -708 C ATOM 294 CD GLN A 41 17.233 17.480 61.748 1.00 26.34 C ANISOU 294 CD GLN B 41 4251 2506 3252 -309 922 -670 C ATOM 295 OE1 GLN A 41 16.019 17.516 61.571 1.00 22.72 O ANISOU 295 OE1 GLN B 41 3778 2072 2783 -297 870 -648 O ATOM 296 NE2 GLN A 41 17.931 16.353 61.718 1.00 23.80 N ANISOU 296 NE2 GLN B 41 3955 2176 2911 -305 917 -663 N ATOM 297 N ASP A 42 18.974 16.708 66.008 1.00 29.17 N ANISOU 297 N ASP B 42 4941 2652 3489 -330 1080 -661 N ATOM 298 CA ASP A 42 19.796 16.281 67.145 1.00 30.35 C ANISOU 298 CA ASP B 42 5197 2735 3598 -332 1135 -658 C ATOM 299 C ASP A 42 21.166 15.734 66.765 1.00 31.36 C ANISOU 299 C ASP B 42 5324 2848 3743 -337 1179 -674 C ATOM 300 O ASP A 42 22.165 16.071 67.403 1.00 31.33 O ANISOU 300 O ASP B 42 5375 2788 3742 -356 1263 -694 O ATOM 301 CB ASP A 42 19.053 15.257 67.999 1.00 30.26 C ANISOU 301 CB ASP B 42 5270 2712 3516 -305 1079 -618 C ATOM 302 CG ASP A 42 17.819 15.853 68.675 1.00 33.62 C ANISOU 302 CG ASP B 42 5720 3135 3918 -306 1054 -608 C ATOM 303 OD1 ASP A 42 17.952 16.935 69.323 1.00 36.56 O ANISOU 303 OD1 ASP B 42 6122 3468 4300 -326 1118 -627 O ATOM 304 OD2 ASP A 42 16.714 15.265 68.530 1.00 34.27 O ANISOU 304 OD2 ASP B 42 5791 3255 3976 -289 973 -584 O ATOM 305 N CYS A 43 21.185 14.870 65.752 1.00 31.32 N ANISOU 305 N CYS B 43 5263 2889 3747 -322 1125 -664 N ATOM 306 CA CYS A 43 22.386 14.173 65.323 1.00 32.17 C ANISOU 306 CA CYS B 43 5371 2985 3865 -324 1157 -675 C ATOM 307 C CYS A 43 22.445 14.095 63.780 1.00 31.39 C ANISOU 307 C CYS B 43 5159 2953 3816 -327 1119 -691 C ATOM 308 O CYS A 43 21.402 14.153 63.110 1.00 30.97 O ANISOU 308 O CYS B 43 5043 2956 3770 -315 1050 -678 O ATOM 309 CB CYS A 43 22.420 12.787 65.971 1.00 31.83 C ANISOU 309 CB CYS B 43 5417 2916 3760 -293 1129 -637 C ATOM 310 SG CYS A 43 24.036 12.022 65.934 1.00 35.62 S ANISOU 310 SG CYS B 43 5943 3349 4241 -295 1197 -649 S ATOM 311 N LEU A 44 23.656 13.996 63.233 1.00 31.60 N ANISOU 311 N LEU B 44 5162 2971 3874 -344 1169 -720 N ATOM 312 CA LEU A 44 23.915 13.931 61.774 1.00 30.85 C ANISOU 312 CA LEU B 44 4963 2934 3823 -349 1143 -742 C ATOM 313 C LEU A 44 24.789 12.725 61.418 1.00 30.57 C ANISOU 313 C LEU B 44 4950 2888 3778 -341 1150 -738 C ATOM 314 O LEU A 44 25.980 12.721 61.758 1.00 30.61 O ANISOU 314 O LEU B 44 4997 2843 3792 -360 1227 -762 O ATOM 315 CB LEU A 44 24.625 15.220 61.318 1.00 31.28 C ANISOU 315 CB LEU B 44 4951 2995 3938 -385 1203 -795 C ATOM 316 CG LEU A 44 24.839 15.579 59.839 1.00 30.86 C ANISOU 316 CG LEU B 44 4782 3008 3936 -395 1180 -828 C ATOM 317 CD1 LEU A 44 25.213 17.027 59.777 1.00 32.38 C ANISOU 317 CD1 LEU B 44 4921 3203 4178 -424 1231 -875 C ATOM 318 CD2 LEU A 44 25.930 14.754 59.136 1.00 31.12 C ANISOU 318 CD2 LEU B 44 4802 3042 3980 -404 1199 -847 C ATOM 319 N ALA A 45 24.202 11.729 60.741 1.00 29.04 N ANISOU 319 N ALA B 45 4728 2738 3568 -312 1075 -709 N ATOM 320 CA ALA A 45 24.922 10.562 60.210 1.00 29.95 C ANISOU 320 CA ALA B 45 4850 2852 3677 -300 1074 -705 C ATOM 321 C ALA A 45 25.588 10.911 58.889 1.00 29.93 C ANISOU 321 C ALA B 45 4755 2889 3728 -324 1088 -747 C ATOM 322 O ALA A 45 25.011 11.618 58.059 1.00 30.23 O ANISOU 322 O ALA B 45 4708 2984 3795 -331 1052 -760 O ATOM 323 CB ALA A 45 23.996 9.394 60.009 1.00 29.54 C ANISOU 323 CB ALA B 45 4800 2833 3591 -260 990 -660 C ATOM 324 N PHE A 46 26.810 10.428 58.683 1.00 29.54 N ANISOU 324 N PHE B 46 4725 2810 3689 -337 1142 -769 N ATOM 325 CA PHE A 46 27.545 10.785 57.484 1.00 28.87 C ANISOU 325 CA PHE B 46 4556 2760 3654 -364 1161 -816 C ATOM 326 C PHE A 46 28.412 9.622 57.016 1.00 29.12 C ANISOU 326 C PHE B 46 4608 2777 3681 -358 1178 -817 C ATOM 327 O PHE A 46 28.904 8.831 57.831 1.00 28.65 O ANISOU 327 O PHE B 46 4639 2657 3588 -344 1212 -796 O ATOM 328 CB PHE A 46 28.396 12.030 57.736 1.00 29.01 C ANISOU 328 CB PHE B 46 4560 2751 3712 -408 1242 -869 C ATOM 329 CG PHE A 46 29.400 11.852 58.859 1.00 31.58 C ANISOU 329 CG PHE B 46 4984 2990 4023 -423 1331 -875 C ATOM 330 CD1 PHE A 46 30.654 11.296 58.619 1.00 30.21 C ANISOU 330 CD1 PHE B 46 4834 2782 3862 -441 1391 -901 C ATOM 331 CD2 PHE A 46 29.086 12.256 60.162 1.00 30.53 C ANISOU 331 CD2 PHE B 46 4928 2808 3863 -420 1358 -856 C ATOM 332 CE1 PHE A 46 31.563 11.115 59.650 1.00 30.29 C ANISOU 332 CE1 PHE B 46 4943 2708 3858 -453 1478 -905 C ATOM 333 CE2 PHE A 46 30.002 12.073 61.183 1.00 32.59 C ANISOU 333 CE2 PHE B 46 5287 2987 4107 -431 1443 -860 C ATOM 334 CZ PHE A 46 31.230 11.498 60.926 1.00 30.59 C ANISOU 334 CZ PHE B 46 5057 2698 3866 -447 1503 -883 C ATOM 335 N CYS A 47 28.544 9.497 55.697 1.00 29.36 N ANISOU 335 N CYS B 47 4557 2861 3739 -364 1150 -839 N ATOM 336 CA CYS A 47 29.422 8.505 55.107 1.00 29.79 C ANISOU 336 CA CYS B 47 4619 2904 3794 -363 1170 -849 C ATOM 337 C CYS A 47 30.855 8.943 55.282 1.00 30.19 C ANISOU 337 C CYS B 47 4690 2906 3876 -407 1268 -901 C ATOM 338 O CYS A 47 31.228 10.083 54.949 1.00 29.62 O ANISOU 338 O CYS B 47 4557 2851 3845 -445 1298 -952 O ATOM 339 CB CYS A 47 29.149 8.312 53.617 1.00 29.67 C ANISOU 339 CB CYS B 47 4511 2963 3800 -360 1115 -862 C ATOM 340 SG CYS A 47 27.628 7.451 53.298 1.00 31.12 S ANISOU 340 SG CYS B 47 4679 3197 3949 -310 1011 -801 S ATOM 341 N THR A 48 31.651 8.031 55.831 1.00 30.60 N ANISOU 341 N THR B 48 4827 2893 3906 -399 1318 -890 N ATOM 342 CA THR A 48 33.085 8.179 55.727 1.00 31.18 C ANISOU 342 CA THR B 48 4915 2921 4010 -441 1411 -942 C ATOM 343 C THR A 48 33.498 7.692 54.334 1.00 32.09 C ANISOU 343 C THR B 48 4962 3082 4149 -449 1392 -970 C ATOM 344 O THR A 48 32.659 7.380 53.475 1.00 29.85 O ANISOU 344 O THR B 48 4618 2865 3860 -424 1311 -950 O ATOM 345 CB THR A 48 33.803 7.371 56.792 1.00 31.43 C ANISOU 345 CB THR B 48 5070 2863 4008 -427 1477 -918 C ATOM 346 OG1 THR A 48 33.414 6.007 56.673 1.00 30.12 O ANISOU 346 OG1 THR B 48 4940 2702 3804 -375 1425 -867 O ATOM 347 CG2 THR A 48 33.467 7.881 58.188 1.00 31.92 C ANISOU 347 CG2 THR B 48 5207 2878 4044 -421 1502 -894 C ATOM 348 N GLU A 49 34.813 7.653 54.119 1.00 33.36 N ANISOU 348 N GLU B 49 5135 3204 4337 -487 1473 -1018 N ATOM 349 CA GLU A 49 35.376 7.375 52.826 1.00 33.55 C ANISOU 349 CA GLU B 49 5093 3265 4388 -506 1470 -1058 C ATOM 350 C GLU A 49 35.022 5.952 52.403 1.00 32.73 C ANISOU 350 C GLU B 49 5014 3170 4250 -458 1420 -1011 C ATOM 351 O GLU A 49 35.015 5.650 51.230 1.00 32.71 O ANISOU 351 O GLU B 49 4949 3220 4261 -460 1386 -1028 O ATOM 352 CB GLU A 49 36.907 7.601 52.868 1.00 34.15 C ANISOU 352 CB GLU B 49 5192 3284 4499 -561 1578 -1122 C ATOM 353 CG GLU A 49 37.583 7.620 51.511 1.00 35.62 C ANISOU 353 CG GLU B 49 5298 3514 4721 -595 1582 -1181 C ATOM 354 CD GLU A 49 39.118 7.468 51.590 1.00 35.92 C ANISOU 354 CD GLU B 49 5378 3484 4786 -644 1693 -1236 C ATOM 355 OE1 GLU A 49 39.641 7.215 52.701 1.00 37.88 O ANISOU 355 OE1 GLU B 49 5727 3647 5021 -645 1767 -1220 O ATOM 356 OE2 GLU A 49 39.788 7.628 50.533 1.00 35.56 O ANISOU 356 OE2 GLU B 49 5266 3471 4775 -683 1706 -1297 O ATOM 357 N LEU A 50 34.681 5.117 53.382 1.00 32.42 N ANISOU 357 N LEU B 50 5067 3085 4168 -414 1415 -952 N ATOM 358 CA LEU A 50 34.324 3.717 53.169 1.00 32.32 C ANISOU 358 CA LEU B 50 5084 3074 4121 -362 1370 -903 C ATOM 359 C LEU A 50 32.871 3.456 52.744 1.00 31.84 C ANISOU 359 C LEU B 50 4970 3086 4042 -322 1261 -860 C ATOM 360 O LEU A 50 32.547 2.310 52.441 1.00 31.04 O ANISOU 360 O LEU B 50 4880 2996 3919 -281 1222 -824 O ATOM 361 CB LEU A 50 34.587 2.901 54.448 1.00 32.71 C ANISOU 361 CB LEU B 50 5257 3043 4128 -326 1407 -858 C ATOM 362 CG LEU A 50 36.031 2.747 54.946 1.00 34.81 C ANISOU 362 CG LEU B 50 5605 3221 4401 -351 1519 -886 C ATOM 363 CD1 LEU A 50 36.156 1.657 56.026 1.00 35.39 C ANISOU 363 CD1 LEU B 50 5801 3222 4422 -298 1539 -829 C ATOM 364 CD2 LEU A 50 36.928 2.450 53.808 1.00 33.56 C ANISOU 364 CD2 LEU B 50 5404 3071 4277 -381 1554 -933 C ATOM 365 N GLU A 51 32.021 4.499 52.725 1.00 31.13 N ANISOU 365 N GLU B 51 4823 3044 3962 -333 1219 -863 N ATOM 366 CA GLU A 51 30.576 4.344 52.454 1.00 30.56 C ANISOU 366 CA GLU B 51 4707 3033 3871 -298 1123 -821 C ATOM 367 C GLU A 51 30.064 5.324 51.410 1.00 29.98 C ANISOU 367 C GLU B 51 4530 3034 3828 -321 1082 -851 C ATOM 368 O GLU A 51 30.530 6.457 51.321 1.00 29.94 O ANISOU 368 O GLU B 51 4490 3032 3853 -361 1118 -897 O ATOM 369 CB GLU A 51 29.779 4.487 53.759 1.00 30.41 C ANISOU 369 CB GLU B 51 4748 2988 3819 -274 1103 -778 C ATOM 370 CG GLU A 51 30.114 3.377 54.737 1.00 30.79 C ANISOU 370 CG GLU B 51 4900 2972 3828 -238 1126 -740 C ATOM 371 CD GLU A 51 29.122 3.238 55.859 1.00 33.31 C ANISOU 371 CD GLU B 51 5271 3280 4105 -204 1082 -691 C ATOM 372 OE1 GLU A 51 28.270 2.317 55.815 1.00 33.39 O ANISOU 372 OE1 GLU B 51 5280 3318 4088 -160 1013 -649 O ATOM 373 OE2 GLU A 51 29.204 4.037 56.805 1.00 34.34 O ANISOU 373 OE2 GLU B 51 5445 3375 4229 -220 1118 -696 O ATOM 374 N ASP A 52 29.146 4.858 50.573 1.00 29.61 N ANISOU 374 N ASP B 52 4431 3046 3773 -295 1009 -827 N ATOM 375 CA ASP A 52 28.547 5.706 49.541 1.00 29.09 C ANISOU 375 CA ASP B 52 4272 3052 3728 -308 964 -848 C ATOM 376 C ASP A 52 27.164 5.161 49.224 1.00 27.18 C ANISOU 376 C ASP B 52 4007 2855 3464 -270 882 -799 C ATOM 377 O ASP A 52 26.750 4.175 49.807 1.00 26.26 O ANISOU 377 O ASP B 52 3940 2717 3320 -237 862 -755 O ATOM 378 CB ASP A 52 29.442 5.783 48.287 1.00 29.92 C ANISOU 378 CB ASP B 52 4322 3186 3862 -336 986 -900 C ATOM 379 CG ASP A 52 29.651 4.438 47.609 1.00 31.06 C ANISOU 379 CG ASP B 52 4475 3332 3994 -315 975 -886 C ATOM 380 OD1 ASP A 52 28.844 3.491 47.786 1.00 32.35 O ANISOU 380 OD1 ASP B 52 4662 3499 4131 -274 931 -835 O ATOM 381 OD2 ASP A 52 30.647 4.339 46.859 1.00 37.11 O ANISOU 381 OD2 ASP B 52 5221 4098 4779 -340 1013 -931 O ATOM 382 N VAL A 53 26.460 5.802 48.302 1.00 27.53 N ANISOU 382 N VAL B 53 3976 2963 3520 -273 836 -807 N ATOM 383 CA VAL A 53 25.099 5.406 47.967 1.00 26.72 C ANISOU 383 CA VAL B 53 3849 2902 3399 -242 765 -764 C ATOM 384 C VAL A 53 24.983 3.939 47.511 1.00 27.54 C ANISOU 384 C VAL B 53 3964 3012 3489 -213 742 -737 C ATOM 385 O VAL A 53 24.028 3.247 47.894 1.00 28.34 O ANISOU 385 O VAL B 53 4083 3116 3568 -183 698 -693 O ATOM 386 CB VAL A 53 24.444 6.380 46.979 1.00 25.76 C ANISOU 386 CB VAL B 53 3650 2845 3293 -250 727 -779 C ATOM 387 CG1 VAL A 53 24.142 7.719 47.693 1.00 25.37 C ANISOU 387 CG1 VAL B 53 3598 2789 3253 -264 736 -787 C ATOM 388 CG2 VAL A 53 25.322 6.636 45.814 1.00 27.45 C ANISOU 388 CG2 VAL B 53 3812 3089 3528 -271 746 -827 C ATOM 389 N ILE A 54 25.978 3.463 46.755 1.00 26.97 N ANISOU 389 N ILE B 54 3882 2938 3428 -224 773 -767 N ATOM 390 CA ILE A 54 26.025 2.094 46.275 1.00 26.69 C ANISOU 390 CA ILE B 54 3856 2903 3381 -197 762 -747 C ATOM 391 C ILE A 54 26.162 1.163 47.452 1.00 26.70 C ANISOU 391 C ILE B 54 3935 2847 3361 -170 776 -712 C ATOM 392 O ILE A 54 25.374 0.240 47.586 1.00 26.52 O ANISOU 392 O ILE B 54 3922 2835 3321 -135 733 -671 O ATOM 393 CB ILE A 54 27.225 1.839 45.267 1.00 27.53 C ANISOU 393 CB ILE B 54 3944 3012 3506 -219 804 -792 C ATOM 394 CG1 ILE A 54 27.239 2.865 44.118 1.00 28.13 C ANISOU 394 CG1 ILE B 54 3943 3144 3600 -247 792 -834 C ATOM 395 CG2 ILE A 54 27.210 0.411 44.740 1.00 26.70 C ANISOU 395 CG2 ILE B 54 3847 2907 3389 -189 793 -770 C ATOM 396 CD1 ILE A 54 25.872 3.050 43.408 1.00 31.93 C ANISOU 396 CD1 ILE B 54 4371 3689 4073 -227 721 -807 C ATOM 397 N SER A 55 27.152 1.401 48.319 1.00 26.81 N ANISOU 397 N SER B 55 4008 2803 3376 -186 837 -729 N ATOM 398 CA SER A 55 27.363 0.497 49.450 1.00 26.32 C ANISOU 398 CA SER B 55 4030 2683 3288 -155 854 -695 C ATOM 399 C SER A 55 26.156 0.467 50.409 1.00 27.10 C ANISOU 399 C SER B 55 4151 2786 3361 -128 801 -650 C ATOM 400 O SER A 55 25.722 -0.616 50.846 1.00 27.29 O ANISOU 400 O SER B 55 4209 2801 3360 -86 770 -610 O ATOM 401 CB SER A 55 28.680 0.828 50.173 1.00 27.42 C ANISOU 401 CB SER B 55 4232 2754 3432 -180 937 -724 C ATOM 402 OG SER A 55 28.578 1.932 51.065 1.00 24.59 O ANISOU 402 OG SER B 55 3893 2376 3073 -202 955 -731 O ATOM 403 N MET A 56 25.622 1.645 50.743 1.00 25.89 N ANISOU 403 N MET B 56 3979 2646 3211 -150 790 -657 N ATOM 404 CA MET A 56 24.422 1.731 51.579 1.00 26.71 C ANISOU 404 CA MET B 56 4099 2757 3292 -130 740 -619 C ATOM 405 C MET A 56 23.219 1.007 50.979 1.00 25.73 C ANISOU 405 C MET B 56 3929 2685 3161 -102 667 -589 C ATOM 406 O MET A 56 22.457 0.386 51.706 1.00 25.84 O ANISOU 406 O MET B 56 3972 2695 3151 -73 628 -553 O ATOM 407 CB MET A 56 24.054 3.188 51.841 1.00 25.71 C ANISOU 407 CB MET B 56 3952 2640 3177 -160 745 -637 C ATOM 408 CG MET A 56 25.064 3.952 52.716 1.00 26.92 C ANISOU 408 CG MET B 56 4158 2737 3335 -186 817 -663 C ATOM 409 SD MET A 56 24.274 5.494 53.230 1.00 28.07 S ANISOU 409 SD MET B 56 4284 2895 3488 -209 808 -670 S ATOM 410 CE MET A 56 24.298 6.453 51.731 1.00 25.48 C ANISOU 410 CE MET B 56 3851 2630 3202 -236 799 -712 C ATOM 411 N SER A 57 23.054 1.096 49.655 1.00 26.61 N ANISOU 411 N SER B 57 3969 2847 3295 -112 651 -605 N ATOM 412 CA SER A 57 21.986 0.353 48.953 1.00 26.15 C ANISOU 412 CA SER B 57 3866 2837 3235 -89 591 -579 C ATOM 413 C SER A 57 22.202 -1.131 49.085 1.00 27.39 C ANISOU 413 C SER B 57 4051 2977 3378 -53 584 -556 C ATOM 414 O SER A 57 21.239 -1.879 49.348 1.00 27.50 O ANISOU 414 O SER B 57 4062 3008 3379 -24 535 -522 O ATOM 415 CB SER A 57 21.971 0.703 47.482 1.00 26.80 C ANISOU 415 CB SER B 57 3876 2969 3340 -106 585 -604 C ATOM 416 OG SER A 57 21.732 2.084 47.303 1.00 28.32 O ANISOU 416 OG SER B 57 4035 3181 3543 -134 586 -624 O ATOM 417 N PHE A 58 23.450 -1.584 48.873 1.00 27.60 N ANISOU 417 N PHE B 58 4104 2972 3411 -53 635 -574 N ATOM 418 CA PHE A 58 23.794 -3.002 49.115 1.00 28.59 C ANISOU 418 CA PHE B 58 4269 3072 3523 -13 637 -551 C ATOM 419 C PHE A 58 23.338 -3.486 50.500 1.00 27.95 C ANISOU 419 C PHE B 58 4249 2962 3410 21 613 -514 C ATOM 420 O PHE A 58 22.721 -4.533 50.599 1.00 28.31 O ANISOU 420 O PHE B 58 4291 3022 3444 59 569 -484 O ATOM 421 CB PHE A 58 25.304 -3.300 48.962 1.00 28.87 C ANISOU 421 CB PHE B 58 4344 3061 3565 -20 708 -577 C ATOM 422 CG PHE A 58 25.825 -3.274 47.547 1.00 30.47 C ANISOU 422 CG PHE B 58 4491 3292 3794 -43 728 -612 C ATOM 423 CD1 PHE A 58 24.991 -3.466 46.458 1.00 30.68 C ANISOU 423 CD1 PHE B 58 4448 3379 3831 -39 682 -608 C ATOM 424 CD2 PHE A 58 27.194 -3.093 47.314 1.00 32.42 C ANISOU 424 CD2 PHE B 58 4762 3502 4053 -69 798 -650 C ATOM 425 CE1 PHE A 58 25.498 -3.469 45.144 1.00 33.07 C ANISOU 425 CE1 PHE B 58 4707 3708 4152 -58 701 -640 C ATOM 426 CE2 PHE A 58 27.729 -3.098 45.995 1.00 33.59 C ANISOU 426 CE2 PHE B 58 4862 3677 4223 -91 817 -687 C ATOM 427 CZ PHE A 58 26.869 -3.296 44.909 1.00 32.75 C ANISOU 427 CZ PHE B 58 4688 3634 4123 -84 766 -681 C ATOM 428 N ASN A 59 23.696 -2.752 51.562 1.00 28.18 N ANISOU 428 N ASN B 59 4336 2948 3425 7 643 -518 N ATOM 429 CA ASN A 59 23.308 -3.128 52.932 1.00 27.83 C ANISOU 429 CA ASN B 59 4357 2873 3343 39 621 -484 C ATOM 430 C ASN A 59 21.779 -3.280 53.105 1.00 27.41 C ANISOU 430 C ASN B 59 4266 2866 3280 53 542 -458 C ATOM 431 O ASN A 59 21.274 -4.295 53.634 1.00 26.32 O ANISOU 431 O ASN B 59 4149 2732 3120 95 499 -427 O ATOM 432 CB ASN A 59 23.812 -2.090 53.972 1.00 28.58 C ANISOU 432 CB ASN B 59 4514 2919 3426 14 667 -497 C ATOM 433 CG ASN A 59 25.309 -1.830 53.898 1.00 29.96 C ANISOU 433 CG ASN B 59 4727 3043 3614 -9 752 -527 C ATOM 434 OD1 ASN A 59 26.100 -2.748 53.703 1.00 30.12 O ANISOU 434 OD1 ASN B 59 4775 3037 3632 13 780 -525 O ATOM 435 ND2 ASN A 59 25.702 -0.568 54.067 1.00 31.06 N ANISOU 435 ND2 ASN B 59 4867 3168 3768 -52 796 -559 N ATOM 436 N ALA A 60 21.058 -2.226 52.712 1.00 26.53 N ANISOU 436 N ALA B 60 4105 2791 3186 19 525 -471 N ATOM 437 CA ALA A 60 19.604 -2.169 52.854 1.00 26.17 C ANISOU 437 CA ALA B 60 4024 2785 3134 23 460 -452 C ATOM 438 C ALA A 60 18.897 -3.279 52.083 1.00 26.10 C ANISOU 438 C ALA B 60 3963 2821 3135 49 412 -436 C ATOM 439 O ALA A 60 17.952 -3.835 52.592 1.00 27.26 O ANISOU 439 O ALA B 60 4108 2983 3266 70 361 -413 O ATOM 440 CB ALA A 60 19.095 -0.807 52.395 1.00 25.53 C ANISOU 440 CB ALA B 60 3898 2729 3072 -17 462 -472 C ATOM 441 N VAL A 61 19.351 -3.594 50.859 1.00 26.40 N ANISOU 441 N VAL B 61 3955 2878 3197 45 430 -450 N ATOM 442 CA VAL A 61 18.669 -4.558 49.972 1.00 25.40 C ANISOU 442 CA VAL B 61 3771 2797 3084 64 391 -438 C ATOM 443 C VAL A 61 18.978 -5.983 50.416 1.00 26.82 C ANISOU 443 C VAL B 61 3982 2958 3250 112 381 -417 C ATOM 444 O VAL A 61 18.102 -6.831 50.508 1.00 26.98 O ANISOU 444 O VAL B 61 3978 3005 3268 138 331 -396 O ATOM 445 CB VAL A 61 19.115 -4.398 48.503 1.00 26.03 C ANISOU 445 CB VAL B 61 3798 2902 3192 44 418 -462 C ATOM 446 CG1 VAL A 61 18.726 -5.625 47.659 1.00 24.87 C ANISOU 446 CG1 VAL B 61 3607 2786 3056 71 393 -450 C ATOM 447 CG2 VAL A 61 18.498 -3.165 47.905 1.00 22.22 C ANISOU 447 CG2 VAL B 61 3270 2450 2721 8 411 -478 C ATOM 448 N THR A 62 20.249 -6.236 50.707 1.00 27.41 N ANISOU 448 N THR B 62 4112 2985 3316 124 431 -423 N ATOM 449 CA THR A 62 20.677 -7.522 51.179 1.00 28.50 C ANISOU 449 CA THR B 62 4291 3099 3439 174 428 -401 C ATOM 450 C THR A 62 20.034 -7.807 52.544 1.00 28.45 C ANISOU 450 C THR B 62 4329 3083 3398 204 383 -373 C ATOM 451 O THR A 62 19.594 -8.925 52.807 1.00 28.77 O ANISOU 451 O THR B 62 4366 3137 3429 248 340 -350 O ATOM 452 CB THR A 62 22.201 -7.518 51.252 1.00 29.85 C ANISOU 452 CB THR B 62 4520 3213 3607 173 501 -416 C ATOM 453 OG1 THR A 62 22.713 -7.625 49.905 1.00 30.11 O ANISOU 453 OG1 THR B 62 4506 3264 3670 155 531 -440 O ATOM 454 CG2 THR A 62 22.683 -8.662 52.059 1.00 32.55 C ANISOU 454 CG2 THR B 62 4927 3517 3923 228 503 -389 C ATOM 455 N SER A 63 19.957 -6.799 53.407 1.00 26.82 N ANISOU 455 N SER B 63 4163 2853 3173 180 391 -377 N ATOM 456 CA SER A 63 19.277 -6.995 54.701 1.00 27.92 C ANISOU 456 CA SER B 63 4346 2986 3276 205 346 -354 C ATOM 457 C SER A 63 17.783 -7.288 54.480 1.00 27.39 C ANISOU 457 C SER B 63 4211 2978 3217 206 272 -344 C ATOM 458 O SER A 63 17.210 -8.197 55.088 1.00 28.74 O ANISOU 458 O SER B 63 4388 3162 3368 245 221 -324 O ATOM 459 CB SER A 63 19.489 -5.781 55.630 1.00 27.48 C ANISOU 459 CB SER B 63 4349 2892 3199 175 375 -362 C ATOM 460 OG SER A 63 18.731 -5.938 56.818 1.00 29.71 O ANISOU 460 OG SER B 63 4670 3172 3444 196 327 -342 O ATOM 461 N LEU A 64 17.142 -6.540 53.584 1.00 27.14 N ANISOU 461 N LEU B 64 4113 2983 3216 165 268 -361 N ATOM 462 CA LEU A 64 15.745 -6.801 53.321 1.00 26.70 C ANISOU 462 CA LEU B 64 3995 2979 3171 162 208 -354 C ATOM 463 C LEU A 64 15.548 -8.234 52.821 1.00 27.31 C ANISOU 463 C LEU B 64 4032 3084 3261 201 178 -342 C ATOM 464 O LEU A 64 14.749 -8.997 53.399 1.00 27.15 O ANISOU 464 O LEU B 64 4002 3085 3229 228 122 -327 O ATOM 465 CB LEU A 64 15.137 -5.768 52.345 1.00 26.46 C ANISOU 465 CB LEU B 64 3905 2980 3170 114 215 -372 C ATOM 466 CG LEU A 64 13.607 -5.846 52.120 1.00 24.89 C ANISOU 466 CG LEU B 64 3647 2828 2983 102 161 -366 C ATOM 467 CD1 LEU A 64 13.095 -4.561 51.550 1.00 23.15 C ANISOU 467 CD1 LEU B 64 3397 2622 2778 58 175 -380 C ATOM 468 CD2 LEU A 64 13.218 -6.968 51.191 1.00 28.21 C ANISOU 468 CD2 LEU B 64 4005 3287 3427 121 139 -361 C ATOM 469 N LEU A 65 16.270 -8.586 51.750 1.00 27.91 N ANISOU 469 N LEU B 65 4081 3162 3361 204 214 -350 N ATOM 470 CA LEU A 65 16.160 -9.905 51.106 1.00 29.76 C ANISOU 470 CA LEU B 65 4273 3422 3613 239 196 -341 C ATOM 471 C LEU A 65 16.306 -11.025 52.125 1.00 30.63 C ANISOU 471 C LEU B 65 4424 3516 3696 297 165 -319 C ATOM 472 O LEU A 65 15.553 -11.998 52.170 1.00 31.13 O ANISOU 472 O LEU B 65 4449 3613 3766 327 115 -307 O ATOM 473 CB LEU A 65 17.265 -10.052 50.030 1.00 29.38 C ANISOU 473 CB LEU B 65 4217 3360 3585 236 253 -355 C ATOM 474 CG LEU A 65 16.937 -9.700 48.577 1.00 30.60 C ANISOU 474 CG LEU B 65 4301 3552 3772 202 266 -373 C ATOM 475 CD1 LEU A 65 15.955 -8.577 48.479 1.00 31.96 C ANISOU 475 CD1 LEU B 65 4445 3751 3949 159 246 -381 C ATOM 476 CD2 LEU A 65 18.176 -9.421 47.701 1.00 29.59 C ANISOU 476 CD2 LEU B 65 4184 3404 3656 186 329 -395 C ATOM 477 N GLU A 66 17.302 -10.831 52.962 1.00 32.17 N ANISOU 477 N GLU B 66 4703 3659 3863 311 199 -314 N ATOM 478 CA GLU A 66 17.739 -11.774 53.945 1.00 34.06 C ANISOU 478 CA GLU B 66 5002 3870 4069 370 184 -291 C ATOM 479 C GLU A 66 16.706 -11.960 55.077 1.00 34.29 C ANISOU 479 C GLU B 66 5041 3919 4069 389 114 -276 C ATOM 480 O GLU A 66 16.224 -13.069 55.320 1.00 35.31 O ANISOU 480 O GLU B 66 5147 4074 4193 435 62 -262 O ATOM 481 CB GLU A 66 19.003 -11.160 54.501 1.00 34.04 C ANISOU 481 CB GLU B 66 5089 3803 4044 364 249 -294 C ATOM 482 CG GLU A 66 20.092 -12.054 54.620 1.00 38.52 C ANISOU 482 CG GLU B 66 5707 4330 4600 411 283 -282 C ATOM 483 CD GLU A 66 19.889 -12.944 55.771 1.00 41.54 C ANISOU 483 CD GLU B 66 6138 4702 4941 474 237 -253 C ATOM 484 OE1 GLU A 66 19.825 -14.163 55.505 1.00 42.77 O ANISOU 484 OE1 GLU B 66 6268 4877 5106 524 211 -238 O ATOM 485 OE2 GLU A 66 19.750 -12.402 56.902 1.00 42.16 O ANISOU 485 OE2 GLU B 66 6277 4759 4982 472 225 -245 O ATOM 486 N LYS A 67 16.357 -10.862 55.753 1.00 34.49 N ANISOU 486 N LYS B 67 5097 3934 4075 353 112 -283 N ATOM 487 CA LYS A 67 15.507 -10.930 56.953 1.00 34.09 C ANISOU 487 CA LYS B 67 5072 3893 3988 368 51 -272 C ATOM 488 C LYS A 67 14.046 -11.233 56.671 1.00 33.87 C ANISOU 488 C LYS B 67 4960 3928 3982 356 -15 -277 C ATOM 489 O LYS A 67 13.340 -11.764 57.535 1.00 33.79 O ANISOU 489 O LYS B 67 4956 3937 3946 383 -77 -269 O ATOM 490 CB LYS A 67 15.669 -9.666 57.792 1.00 34.42 C ANISOU 490 CB LYS B 67 5180 3897 4002 333 78 -278 C ATOM 491 CG LYS A 67 17.129 -9.447 58.188 1.00 34.78 C ANISOU 491 CG LYS B 67 5314 3876 4025 346 148 -274 C ATOM 492 CD LYS A 67 17.282 -8.521 59.327 1.00 37.43 C ANISOU 492 CD LYS B 67 5729 4170 4321 329 166 -274 C ATOM 493 CE LYS A 67 18.731 -8.498 59.769 1.00 39.35 C ANISOU 493 CE LYS B 67 6063 4345 4542 347 236 -269 C ATOM 494 NZ LYS A 67 19.441 -7.364 59.131 1.00 40.75 N ANISOU 494 NZ LYS B 67 6234 4498 4750 292 310 -295 N ATOM 495 N TYR A 68 13.581 -10.893 55.471 1.00 33.09 N ANISOU 495 N TYR B 68 4784 3860 3927 316 -3 -293 N ATOM 496 CA TYR A 68 12.205 -11.220 55.106 1.00 32.94 C ANISOU 496 CA TYR B 68 4685 3898 3932 302 -57 -299 C ATOM 497 C TYR A 68 12.163 -12.531 54.326 1.00 34.00 C ANISOU 497 C TYR B 68 4758 4064 4096 338 -73 -294 C ATOM 498 O TYR A 68 11.091 -13.029 53.994 1.00 34.80 O ANISOU 498 O TYR B 68 4787 4212 4222 333 -116 -300 O ATOM 499 CB TYR A 68 11.531 -10.094 54.321 1.00 30.95 C ANISOU 499 CB TYR B 68 4388 3662 3708 239 -39 -316 C ATOM 500 CG TYR A 68 11.294 -8.798 55.091 1.00 30.27 C ANISOU 500 CG TYR B 68 4350 3554 3599 202 -31 -322 C ATOM 501 CD1 TYR A 68 12.242 -7.780 55.074 1.00 26.65 C ANISOU 501 CD1 TYR B 68 3939 3053 3132 182 28 -328 C ATOM 502 CD2 TYR A 68 10.108 -8.588 55.827 1.00 28.47 C ANISOU 502 CD2 TYR B 68 4115 3344 3357 186 -80 -326 C ATOM 503 CE1 TYR A 68 12.029 -6.579 55.781 1.00 26.15 C ANISOU 503 CE1 TYR B 68 3918 2968 3050 149 39 -334 C ATOM 504 CE2 TYR A 68 9.882 -7.380 56.539 1.00 28.68 C ANISOU 504 CE2 TYR B 68 4189 3347 3362 152 -69 -332 C ATOM 505 CZ TYR A 68 10.851 -6.378 56.493 1.00 27.68 C ANISOU 505 CZ TYR B 68 4108 3178 3229 135 -9 -335 C ATOM 506 OH TYR A 68 10.680 -5.176 57.148 1.00 27.65 O ANISOU 506 OH TYR B 68 4148 3150 3208 104 8 -342 O ATOM 507 N LYS A 69 13.338 -13.090 54.039 1.00 35.01 N ANISOU 507 N LYS B 69 4915 4164 4225 373 -35 -286 N ATOM 508 CA LYS A 69 13.435 -14.389 53.383 1.00 35.48 C ANISOU 508 CA LYS B 69 4925 4247 4309 415 -44 -280 C ATOM 509 C LYS A 69 12.854 -14.323 51.976 1.00 34.36 C ANISOU 509 C LYS B 69 4697 4143 4217 378 -31 -295 C ATOM 510 O LYS A 69 11.995 -15.140 51.588 1.00 33.95 O ANISOU 510 O LYS B 69 4574 4136 4191 389 -68 -297 O ATOM 511 CB LYS A 69 12.766 -15.482 54.243 1.00 36.69 C ANISOU 511 CB LYS B 69 5064 4428 4447 466 -117 -268 C ATOM 512 CG LYS A 69 13.720 -16.123 55.234 1.00 40.18 C ANISOU 512 CG LYS B 69 5588 4831 4846 532 -120 -246 C ATOM 513 CD LYS A 69 13.718 -15.479 56.583 1.00 45.21 C ANISOU 513 CD LYS B 69 6305 5440 5431 531 -138 -239 C ATOM 514 CE LYS A 69 12.897 -16.294 57.607 1.00 49.89 C ANISOU 514 CE LYS B 69 6892 6068 5997 575 -224 -231 C ATOM 515 NZ LYS A 69 13.472 -17.637 57.953 1.00 50.28 N ANISOU 515 NZ LYS B 69 6961 6112 6030 660 -245 -210 N ATOM 516 N ILE A 70 13.339 -13.346 51.211 1.00 32.43 N ANISOU 516 N ILE B 70 4458 3881 3982 335 25 -307 N ATOM 517 CA ILE A 70 12.851 -13.154 49.863 1.00 31.75 C ANISOU 517 CA ILE B 70 4302 3828 3936 299 42 -321 C ATOM 518 C ILE A 70 13.834 -13.785 48.893 1.00 32.67 C ANISOU 518 C ILE B 70 4411 3934 4071 320 88 -323 C ATOM 519 O ILE A 70 15.034 -13.496 48.942 1.00 32.86 O ANISOU 519 O ILE B 70 4490 3916 4080 324 134 -325 O ATOM 520 CB ILE A 70 12.694 -11.663 49.485 1.00 30.29 C ANISOU 520 CB ILE B 70 4121 3637 3751 240 70 -335 C ATOM 521 CG1 ILE A 70 11.789 -10.925 50.484 1.00 29.01 C ANISOU 521 CG1 ILE B 70 3975 3478 3569 217 32 -334 C ATOM 522 CG2 ILE A 70 12.181 -11.553 48.050 1.00 29.81 C ANISOU 522 CG2 ILE B 70 3990 3610 3726 211 87 -346 C ATOM 523 CD1 ILE A 70 10.403 -11.539 50.627 1.00 25.19 C ANISOU 523 CD1 ILE B 70 3435 3038 3100 218 -25 -333 C ATOM 524 N ASP A 71 13.318 -14.644 48.027 1.00 32.65 N ANISOU 524 N ASP B 71 4339 3966 4099 330 78 -324 N ATOM 525 CA ASP A 71 14.089 -15.202 46.937 1.00 33.74 C ANISOU 525 CA ASP B 71 4462 4100 4259 343 123 -329 C ATOM 526 C ASP A 71 14.397 -14.072 45.933 1.00 32.88 C ANISOU 526 C ASP B 71 4350 3987 4157 290 171 -348 C ATOM 527 O ASP A 71 13.470 -13.495 45.362 1.00 32.88 O ANISOU 527 O ASP B 71 4305 4018 4171 252 161 -356 O ATOM 528 CB ASP A 71 13.221 -16.292 46.275 1.00 35.18 C ANISOU 528 CB ASP B 71 4565 4327 4476 360 98 -329 C ATOM 529 CG ASP A 71 13.980 -17.131 45.252 1.00 38.55 C ANISOU 529 CG ASP B 71 4975 4748 4924 385 141 -332 C ATOM 530 OD1 ASP A 71 15.184 -16.854 45.011 1.00 38.66 O ANISOU 530 OD1 ASP B 71 5038 4724 4926 385 191 -336 O ATOM 531 OD2 ASP A 71 13.343 -18.068 44.685 1.00 40.81 O ANISOU 531 OD2 ASP B 71 5197 5069 5242 401 127 -332 O ATOM 532 N PRO A 72 15.692 -13.770 45.697 1.00 32.64 N ANISOU 532 N PRO B 72 4366 3918 4116 289 223 -356 N ATOM 533 CA PRO A 72 16.073 -12.750 44.708 1.00 32.16 C ANISOU 533 CA PRO B 72 4299 3858 4061 243 265 -378 C ATOM 534 C PRO A 72 15.571 -13.040 43.290 1.00 31.94 C ANISOU 534 C PRO B 72 4206 3869 4061 229 275 -387 C ATOM 535 O PRO A 72 15.422 -12.115 42.511 1.00 30.82 O ANISOU 535 O PRO B 72 4047 3741 3922 190 291 -402 O ATOM 536 CB PRO A 72 17.608 -12.770 44.719 1.00 32.59 C ANISOU 536 CB PRO B 72 4411 3867 4106 254 319 -387 C ATOM 537 CG PRO A 72 17.997 -13.502 45.965 1.00 33.96 C ANISOU 537 CG PRO B 72 4637 4007 4260 301 305 -367 C ATOM 538 CD PRO A 72 16.869 -14.419 46.316 1.00 33.07 C ANISOU 538 CD PRO B 72 4482 3929 4154 333 246 -348 C ATOM 539 N LYS A 73 15.303 -14.304 42.966 1.00 32.48 N ANISOU 539 N LYS B 73 4239 3954 4149 264 265 -378 N ATOM 540 CA LYS A 73 14.695 -14.680 41.681 1.00 33.80 C ANISOU 540 CA LYS B 73 4342 4157 4342 252 273 -385 C ATOM 541 C LYS A 73 13.252 -14.166 41.561 1.00 32.68 C ANISOU 541 C LYS B 73 4155 4052 4210 220 239 -383 C ATOM 542 O LYS A 73 12.682 -14.085 40.467 1.00 32.81 O ANISOU 542 O LYS B 73 4127 4095 4242 198 252 -390 O ATOM 543 CB LYS A 73 14.724 -16.214 41.514 1.00 34.11 C ANISOU 543 CB LYS B 73 4354 4203 4403 300 270 -376 C ATOM 544 CG LYS A 73 16.121 -16.760 41.370 1.00 35.21 C ANISOU 544 CG LYS B 73 4536 4306 4537 330 314 -380 C ATOM 545 CD LYS A 73 16.167 -18.305 41.397 1.00 39.25 C ANISOU 545 CD LYS B 73 5025 4820 5068 387 309 -367 C ATOM 546 CE LYS A 73 16.594 -18.830 42.780 1.00 44.50 C ANISOU 546 CE LYS B 73 5739 5456 5714 437 283 -348 C ATOM 547 NZ LYS A 73 16.620 -20.335 42.835 1.00 49.53 N ANISOU 547 NZ LYS B 73 6352 6098 6371 500 273 -334 N ATOM 548 N GLN A 74 12.665 -13.831 42.705 1.00 32.83 N ANISOU 548 N GLN B 74 4188 4070 4216 218 198 -373 N ATOM 549 CA GLN A 74 11.292 -13.342 42.770 1.00 32.81 C ANISOU 549 CA GLN B 74 4149 4096 4221 187 166 -372 C ATOM 550 C GLN A 74 11.135 -11.806 42.661 1.00 31.46 C ANISOU 550 C GLN B 74 4000 3920 4035 142 177 -379 C ATOM 551 O GLN A 74 10.070 -11.254 42.934 1.00 31.48 O ANISOU 551 O GLN B 74 3986 3937 4037 117 152 -377 O ATOM 552 CB GLN A 74 10.603 -13.925 44.008 1.00 33.91 C ANISOU 552 CB GLN B 74 4284 4242 4359 209 112 -361 C ATOM 553 CG GLN A 74 10.201 -15.397 43.788 1.00 38.75 C ANISOU 553 CG GLN B 74 4843 4880 4999 245 94 -357 C ATOM 554 CD GLN A 74 9.188 -15.563 42.614 1.00 44.39 C ANISOU 554 CD GLN B 74 5487 5630 5747 217 104 -365 C ATOM 555 OE1 GLN A 74 8.125 -14.948 42.612 1.00 48.42 O ANISOU 555 OE1 GLN B 74 5977 6158 6263 180 89 -369 O ATOM 556 NE2 GLN A 74 9.535 -16.377 41.632 1.00 45.26 N ANISOU 556 NE2 GLN B 74 5568 5748 5879 235 135 -368 N ATOM 557 N ILE A 75 12.186 -11.130 42.219 1.00 29.94 N ANISOU 557 N ILE B 75 3840 3708 3830 132 216 -390 N ATOM 558 CA ILE A 75 12.123 -9.706 41.982 1.00 28.76 C ANISOU 558 CA ILE B 75 3704 3557 3668 95 228 -399 C ATOM 559 C ILE A 75 11.983 -9.521 40.481 1.00 27.57 C ANISOU 559 C ILE B 75 3517 3430 3528 78 255 -409 C ATOM 560 O ILE A 75 12.839 -9.988 39.718 1.00 28.03 O ANISOU 560 O ILE B 75 3575 3486 3590 89 286 -419 O ATOM 561 CB ILE A 75 13.412 -8.993 42.464 1.00 28.58 C ANISOU 561 CB ILE B 75 3737 3498 3625 92 255 -410 C ATOM 562 CG1 ILE A 75 13.798 -9.401 43.894 1.00 28.41 C ANISOU 562 CG1 ILE B 75 3761 3444 3588 118 238 -399 C ATOM 563 CG2 ILE A 75 13.295 -7.461 42.251 1.00 27.56 C ANISOU 563 CG2 ILE B 75 3615 3370 3486 55 265 -421 C ATOM 564 CD1 ILE A 75 12.807 -9.005 44.983 1.00 27.81 C ANISOU 564 CD1 ILE B 75 3693 3370 3501 110 196 -387 C ATOM 565 N GLY A 76 10.905 -8.857 40.070 1.00 26.59 N ANISOU 565 N GLY B 76 3368 3329 3407 52 244 -406 N ATOM 566 CA GLY A 76 10.596 -8.617 38.655 1.00 23.89 C ANISOU 566 CA GLY B 76 2997 3012 3071 36 267 -412 C ATOM 567 C GLY A 76 10.878 -7.204 38.183 1.00 22.92 C ANISOU 567 C GLY B 76 2891 2889 2929 13 283 -423 C ATOM 568 O GLY A 76 10.953 -6.949 36.983 1.00 22.23 O ANISOU 568 O GLY B 76 2788 2819 2837 6 304 -431 O ATOM 569 N ARG A 77 11.030 -6.289 39.132 1.00 22.15 N ANISOU 569 N ARG B 77 2824 2772 2819 3 271 -424 N ATOM 570 CA ARG A 77 11.312 -4.885 38.863 1.00 21.88 C ANISOU 570 CA ARG B 77 2805 2738 2770 -16 283 -435 C ATOM 571 C ARG A 77 12.174 -4.326 40.014 1.00 21.46 C ANISOU 571 C ARG B 77 2794 2654 2707 -17 285 -444 C ATOM 572 O ARG A 77 11.890 -4.567 41.183 1.00 20.60 O ANISOU 572 O ARG B 77 2704 2526 2597 -12 264 -432 O ATOM 573 CB ARG A 77 10.011 -4.051 38.652 1.00 21.75 C ANISOU 573 CB ARG B 77 2774 2738 2751 -34 268 -423 C ATOM 574 CG ARG A 77 10.256 -2.524 38.399 1.00 21.88 C ANISOU 574 CG ARG B 77 2805 2757 2753 -48 277 -434 C ATOM 575 CD ARG A 77 8.986 -1.709 38.056 1.00 21.95 C ANISOU 575 CD ARG B 77 2803 2779 2759 -61 268 -420 C ATOM 576 NE ARG A 77 8.717 -1.733 36.614 1.00 25.87 N ANISOU 576 NE ARG B 77 3277 3303 3250 -58 283 -419 N ATOM 577 CZ ARG A 77 8.854 -0.685 35.802 1.00 26.04 C ANISOU 577 CZ ARG B 77 3299 3339 3255 -59 291 -426 C ATOM 578 NH1 ARG A 77 9.271 0.482 36.274 1.00 23.22 N ANISOU 578 NH1 ARG B 77 2959 2974 2889 -63 288 -436 N ATOM 579 NH2 ARG A 77 8.592 -0.807 34.502 1.00 29.10 N ANISOU 579 NH2 ARG B 77 3672 3751 3634 -54 304 -424 N ATOM 580 N LEU A 78 13.228 -3.590 39.656 1.00 21.47 N ANISOU 580 N LEU B 78 2809 2650 2701 -26 310 -466 N ATOM 581 CA LEU A 78 14.114 -2.947 40.616 1.00 23.21 C ANISOU 581 CA LEU B 78 3068 2839 2914 -32 322 -478 C ATOM 582 C LEU A 78 14.345 -1.525 40.139 1.00 23.84 C ANISOU 582 C LEU B 78 3142 2929 2988 -52 334 -497 C ATOM 583 O LEU A 78 14.834 -1.306 39.036 1.00 24.33 O ANISOU 583 O LEU B 78 3185 3013 3048 -56 350 -516 O ATOM 584 CB LEU A 78 15.439 -3.711 40.786 1.00 23.29 C ANISOU 584 CB LEU B 78 3101 2823 2924 -19 349 -492 C ATOM 585 CG LEU A 78 16.373 -3.269 41.937 1.00 25.67 C ANISOU 585 CG LEU B 78 3451 3082 3218 -23 368 -502 C ATOM 586 CD1 LEU A 78 17.436 -4.299 42.176 1.00 29.74 C ANISOU 586 CD1 LEU B 78 3995 3569 3735 -4 393 -506 C ATOM 587 CD2 LEU A 78 17.083 -1.988 41.580 1.00 27.71 C ANISOU 587 CD2 LEU B 78 3710 3342 3476 -48 393 -531 C ATOM 588 N GLU A 79 13.988 -0.554 40.974 1.00 24.46 N ANISOU 588 N GLU B 79 3237 2995 3062 -63 325 -493 N ATOM 589 CA GLU A 79 14.092 0.850 40.612 1.00 24.79 C ANISOU 589 CA GLU B 79 3270 3048 3100 -78 332 -510 C ATOM 590 C GLU A 79 14.771 1.626 41.732 1.00 25.16 C ANISOU 590 C GLU B 79 3351 3062 3146 -88 347 -523 C ATOM 591 O GLU A 79 14.635 1.273 42.896 1.00 23.83 O ANISOU 591 O GLU B 79 3216 2864 2975 -84 341 -509 O ATOM 592 CB GLU A 79 12.702 1.445 40.372 1.00 26.16 C ANISOU 592 CB GLU B 79 3427 3242 3271 -80 308 -489 C ATOM 593 CG GLU A 79 12.115 1.145 39.038 1.00 29.41 C ANISOU 593 CG GLU B 79 3805 3689 3681 -74 303 -482 C ATOM 594 CD GLU A 79 10.870 1.946 38.783 1.00 33.17 C ANISOU 594 CD GLU B 79 4272 4179 4153 -77 288 -465 C ATOM 595 OE1 GLU A 79 10.979 3.196 38.561 1.00 30.80 O ANISOU 595 OE1 GLU B 79 3971 3887 3846 -80 292 -475 O ATOM 596 OE2 GLU A 79 9.784 1.306 38.819 1.00 34.28 O ANISOU 596 OE2 GLU B 79 4406 4322 4298 -76 274 -442 O ATOM 597 N VAL A 80 15.507 2.679 41.357 1.00 24.59 N ANISOU 597 N VAL B 80 3270 2997 3077 -101 367 -551 N ATOM 598 CA VAL A 80 16.278 3.486 42.305 1.00 24.17 C ANISOU 598 CA VAL B 80 3245 2912 3027 -114 391 -570 C ATOM 599 C VAL A 80 15.896 4.953 42.216 1.00 24.70 C ANISOU 599 C VAL B 80 3294 2994 3095 -123 387 -579 C ATOM 600 O VAL A 80 15.789 5.528 41.110 1.00 24.37 O ANISOU 600 O VAL B 80 3215 2989 3053 -122 380 -590 O ATOM 601 CB VAL A 80 17.809 3.383 42.082 1.00 24.48 C ANISOU 601 CB VAL B 80 3289 2939 3073 -124 429 -607 C ATOM 602 CG1 VAL A 80 18.569 4.190 43.176 1.00 23.55 C ANISOU 602 CG1 VAL B 80 3204 2783 2961 -141 460 -626 C ATOM 603 CG2 VAL A 80 18.245 1.943 42.134 1.00 23.07 C ANISOU 603 CG2 VAL B 80 3131 2743 2892 -111 437 -598 C ATOM 604 N GLY A 81 15.719 5.566 43.384 1.00 24.14 N ANISOU 604 N GLY B 81 3254 2894 3026 -130 392 -573 N ATOM 605 CA GLY A 81 15.585 7.008 43.459 1.00 24.42 C ANISOU 605 CA GLY B 81 3277 2935 3067 -138 397 -586 C ATOM 606 C GLY A 81 16.822 7.554 44.156 1.00 25.07 C ANISOU 606 C GLY B 81 3379 2987 3160 -155 436 -619 C ATOM 607 O GLY A 81 17.269 7.015 45.166 1.00 24.85 O ANISOU 607 O GLY B 81 3394 2918 3128 -159 455 -615 O ATOM 608 N SER A 82 17.394 8.611 43.598 1.00 25.31 N ANISOU 608 N SER B 82 3376 3038 3203 -164 451 -652 N ATOM 609 CA SER A 82 18.594 9.210 44.178 1.00 26.62 C ANISOU 609 CA SER B 82 3553 3177 3384 -184 493 -689 C ATOM 610 C SER A 82 18.808 10.532 43.528 1.00 27.97 C ANISOU 610 C SER B 82 3675 3382 3570 -189 495 -720 C ATOM 611 O SER A 82 18.454 10.699 42.382 1.00 28.23 O ANISOU 611 O SER B 82 3667 3461 3598 -177 468 -721 O ATOM 612 CB SER A 82 19.832 8.336 43.923 1.00 26.41 C ANISOU 612 CB SER B 82 3534 3138 3362 -195 522 -714 C ATOM 613 OG SER A 82 20.930 8.756 44.750 1.00 25.99 O ANISOU 613 OG SER B 82 3507 3045 3323 -218 571 -745 O ATOM 614 N GLU A 83 19.360 11.507 44.238 1.00 29.76 N ANISOU 614 N GLU B 83 3907 3588 3814 -205 527 -746 N ATOM 615 CA GLU A 83 19.853 12.666 43.506 1.00 33.29 C ANISOU 615 CA GLU B 83 4298 4072 4280 -210 531 -787 C ATOM 616 C GLU A 83 21.377 12.734 43.525 1.00 35.22 C ANISOU 616 C GLU B 83 4533 4303 4545 -239 577 -840 C ATOM 617 O GLU A 83 21.976 13.754 43.142 1.00 36.85 O ANISOU 617 O GLU B 83 4693 4535 4773 -250 589 -883 O ATOM 618 CB GLU A 83 19.226 13.975 44.008 1.00 33.23 C ANISOU 618 CB GLU B 83 4281 4064 4282 -203 529 -783 C ATOM 619 CG GLU A 83 19.500 14.275 45.443 1.00 35.81 C ANISOU 619 CG GLU B 83 4653 4334 4618 -221 570 -785 C ATOM 620 CD GLU A 83 18.682 15.428 45.933 1.00 39.82 C ANISOU 620 CD GLU B 83 5158 4839 5132 -210 565 -773 C ATOM 621 OE1 GLU A 83 18.961 16.581 45.528 1.00 44.01 O ANISOU 621 OE1 GLU B 83 5641 5397 5684 -208 570 -804 O ATOM 622 OE2 GLU A 83 17.773 15.179 46.742 1.00 41.70 O ANISOU 622 OE2 GLU B 83 5443 5048 5354 -203 556 -735 O ATOM 623 N THR A 84 21.995 11.633 43.938 1.00 36.72 N ANISOU 623 N THR B 84 4765 4456 4729 -251 603 -837 N ATOM 624 CA THR A 84 23.430 11.570 44.155 1.00 38.99 C ANISOU 624 CA THR B 84 5061 4717 5036 -281 656 -884 C ATOM 625 C THR A 84 24.070 10.963 42.915 1.00 40.98 C ANISOU 625 C THR B 84 5280 5003 5287 -285 650 -910 C ATOM 626 O THR A 84 24.035 9.751 42.730 1.00 41.90 O ANISOU 626 O THR B 84 5424 5109 5387 -276 644 -888 O ATOM 627 CB THR A 84 23.764 10.777 45.442 1.00 38.63 C ANISOU 627 CB THR B 84 5092 4602 4983 -288 694 -865 C ATOM 628 OG1 THR A 84 23.249 11.480 46.610 1.00 38.25 O ANISOU 628 OG1 THR B 84 5075 4522 4935 -287 704 -847 O ATOM 629 CG2 THR A 84 25.264 10.588 45.557 1.00 40.02 C ANISOU 629 CG2 THR B 84 5282 4747 5178 -319 755 -911 C ATOM 630 N VAL A 85 24.639 11.827 42.069 1.00 43.03 N ANISOU 630 N VAL B 85 5480 5305 5565 -299 651 -959 N ATOM 631 CA VAL A 85 25.108 11.467 40.717 1.00 44.96 C ANISOU 631 CA VAL B 85 5683 5595 5804 -301 635 -988 C ATOM 632 C VAL A 85 26.489 10.792 40.745 1.00 45.95 C ANISOU 632 C VAL B 85 5828 5689 5943 -333 688 -1029 C ATOM 633 O VAL A 85 27.468 11.394 41.185 1.00 47.01 O ANISOU 633 O VAL B 85 5956 5801 6104 -365 735 -1076 O ATOM 634 CB VAL A 85 25.114 12.699 39.758 1.00 45.07 C ANISOU 634 CB VAL B 85 5624 5674 5828 -298 607 -1026 C ATOM 635 CG1 VAL A 85 23.702 13.032 39.267 1.00 44.88 C ANISOU 635 CG1 VAL B 85 5583 5689 5780 -258 548 -980 C ATOM 636 CG2 VAL A 85 25.722 13.927 40.463 1.00 47.91 C ANISOU 636 CG2 VAL B 85 5962 6021 6221 -321 642 -1067 C ATOM 637 N ILE A 86 26.533 9.535 40.303 1.00 45.72 N ANISOU 637 N ILE B 86 5823 5653 5895 -324 683 -1011 N ATOM 638 CA ILE A 86 27.760 8.736 40.256 1.00 46.20 C ANISOU 638 CA ILE B 86 5908 5680 5964 -349 733 -1044 C ATOM 639 C ILE A 86 28.304 8.659 38.832 1.00 45.38 C ANISOU 639 C ILE B 86 5757 5628 5860 -360 722 -1087 C ATOM 640 O ILE A 86 29.507 8.614 38.618 1.00 45.91 O ANISOU 640 O ILE B 86 5818 5682 5943 -393 765 -1141 O ATOM 641 CB ILE A 86 27.512 7.292 40.751 1.00 46.22 C ANISOU 641 CB ILE B 86 5975 5638 5947 -329 740 -994 C ATOM 642 CG1 ILE A 86 27.371 7.273 42.266 1.00 47.84 C ANISOU 642 CG1 ILE B 86 6241 5783 6154 -326 766 -964 C ATOM 643 CG2 ILE A 86 28.675 6.351 40.369 1.00 46.98 C ANISOU 643 CG2 ILE B 86 6093 5710 6049 -347 784 -1025 C ATOM 644 CD1 ILE A 86 26.703 6.015 42.756 1.00 48.91 C ANISOU 644 CD1 ILE B 86 6428 5890 6265 -294 748 -906 C ATOM 645 N ASP A 87 27.403 8.620 37.866 1.00 44.20 N ANISOU 645 N ASP B 87 5575 5532 5688 -332 665 -1064 N ATOM 646 CA ASP A 87 27.782 8.555 36.472 1.00 43.72 C ANISOU 646 CA ASP B 87 5471 5524 5618 -336 648 -1101 C ATOM 647 C ASP A 87 26.688 9.321 35.734 1.00 44.18 C ANISOU 647 C ASP B 87 5485 5644 5657 -306 585 -1081 C ATOM 648 O ASP A 87 25.536 9.337 36.173 1.00 42.89 O ANISOU 648 O ASP B 87 5339 5475 5482 -277 558 -1025 O ATOM 649 CB ASP A 87 27.870 7.096 36.012 1.00 42.56 C ANISOU 649 CB ASP B 87 5358 5361 5453 -327 655 -1081 C ATOM 650 CG ASP A 87 28.681 6.921 34.723 1.00 40.68 C ANISOU 650 CG ASP B 87 5087 5160 5209 -344 659 -1134 C ATOM 651 OD1 ASP A 87 29.887 6.636 34.828 1.00 36.30 O ANISOU 651 OD1 ASP B 87 4546 4574 4671 -378 710 -1180 O ATOM 652 OD2 ASP A 87 28.119 7.056 33.609 1.00 35.44 O ANISOU 652 OD2 ASP B 87 4390 4554 4522 -325 613 -1131 O ATOM 653 N LYS A 88 27.060 9.970 34.633 1.00 44.60 N ANISOU 653 N LYS B 88 5484 5755 5706 -311 564 -1127 N ATOM 654 CA LYS A 88 26.091 10.733 33.850 1.00 44.87 C ANISOU 654 CA LYS B 88 5480 5850 5719 -278 506 -1109 C ATOM 655 C LYS A 88 25.244 9.856 32.916 1.00 44.47 C ANISOU 655 C LYS B 88 5442 5823 5631 -247 472 -1067 C ATOM 656 O LYS A 88 24.137 10.260 32.506 1.00 45.10 O ANISOU 656 O LYS B 88 5510 5935 5689 -213 429 -1030 O ATOM 657 CB LYS A 88 26.799 11.885 33.122 1.00 45.48 C ANISOU 657 CB LYS B 88 5493 5983 5805 -292 493 -1176 C ATOM 658 CG LYS A 88 27.410 12.878 34.148 1.00 46.13 C ANISOU 658 CG LYS B 88 5558 6041 5928 -318 526 -1211 C ATOM 659 CD LYS A 88 27.960 14.152 33.531 1.00 46.68 C ANISOU 659 CD LYS B 88 5555 6171 6011 -326 507 -1275 C ATOM 660 CE LYS A 88 28.997 13.874 32.471 1.00 48.23 C ANISOU 660 CE LYS B 88 5721 6402 6203 -353 511 -1339 C ATOM 661 NZ LYS A 88 29.563 15.168 31.993 1.00 48.15 N ANISOU 661 NZ LYS B 88 5634 6450 6209 -362 491 -1407 N ATOM 662 N SER A 89 25.749 8.645 32.644 1.00 42.81 N ANISOU 662 N SER B 89 5259 5591 5415 -259 497 -1071 N ATOM 663 CA SER A 89 25.104 7.672 31.769 1.00 42.01 C ANISOU 663 CA SER B 89 5171 5506 5283 -235 476 -1037 C ATOM 664 C SER A 89 24.616 6.388 32.480 1.00 41.03 C ANISOU 664 C SER B 89 5099 5330 5161 -225 493 -984 C ATOM 665 O SER A 89 23.444 5.985 32.321 1.00 40.93 O ANISOU 665 O SER B 89 5096 5324 5131 -195 466 -931 O ATOM 666 CB SER A 89 26.061 7.327 30.623 1.00 42.16 C ANISOU 666 CB SER B 89 5173 5554 5291 -252 485 -1090 C ATOM 667 OG SER A 89 25.524 6.330 29.804 1.00 43.18 O ANISOU 667 OG SER B 89 5319 5695 5393 -232 473 -1060 O ATOM 668 N LYS A 90 25.512 5.750 33.247 1.00 39.63 N ANISOU 668 N LYS B 90 4953 5100 5004 -247 540 -999 N ATOM 669 CA LYS A 90 25.248 4.465 33.913 1.00 37.58 C ANISOU 669 CA LYS B 90 4741 4790 4746 -235 559 -955 C ATOM 670 C LYS A 90 24.496 4.637 35.263 1.00 37.15 C ANISOU 670 C LYS B 90 4714 4700 4700 -224 553 -910 C ATOM 671 O LYS A 90 25.007 5.246 36.222 1.00 36.91 O ANISOU 671 O LYS B 90 4697 4639 4689 -242 578 -927 O ATOM 672 CB LYS A 90 26.563 3.689 34.079 1.00 37.70 C ANISOU 672 CB LYS B 90 4785 4765 4775 -260 612 -990 C ATOM 673 CG LYS A 90 26.563 2.488 35.056 1.00 35.34 C ANISOU 673 CG LYS B 90 4540 4404 4482 -247 640 -952 C ATOM 674 CD LYS A 90 27.953 1.808 35.000 1.00 36.60 C ANISOU 674 CD LYS B 90 4726 4526 4653 -271 697 -993 C ATOM 675 CE LYS A 90 28.046 0.563 35.858 1.00 35.49 C ANISOU 675 CE LYS B 90 4643 4325 4515 -252 725 -956 C ATOM 676 NZ LYS A 90 26.934 -0.439 35.617 1.00 30.33 N ANISOU 676 NZ LYS B 90 3993 3684 3846 -213 689 -900 N ATOM 677 N SER A 91 23.290 4.077 35.319 1.00 35.74 N ANISOU 677 N SER B 91 4546 4524 4508 -195 523 -855 N ATOM 678 CA SER A 91 22.425 4.183 36.497 1.00 34.34 C ANISOU 678 CA SER B 91 4394 4319 4335 -183 511 -812 C ATOM 679 C SER A 91 22.936 3.430 37.726 1.00 33.86 C ANISOU 679 C SER B 91 4383 4197 4285 -187 544 -801 C ATOM 680 O SER A 91 23.655 2.416 37.626 1.00 31.95 O ANISOU 680 O SER B 91 4163 3932 4045 -188 572 -809 O ATOM 681 CB SER A 91 21.005 3.705 36.159 1.00 34.32 C ANISOU 681 CB SER B 91 4388 4337 4317 -155 472 -761 C ATOM 682 OG SER A 91 21.014 2.347 35.741 1.00 34.06 O ANISOU 682 OG SER B 91 4366 4298 4278 -143 478 -747 O ATOM 683 N ILE A 92 22.536 3.942 38.889 1.00 33.19 N ANISOU 683 N ILE B 92 4320 4086 4205 -187 542 -782 N ATOM 684 CA ILE A 92 22.705 3.229 40.147 1.00 33.67 C ANISOU 684 CA ILE B 92 4434 4090 4268 -182 563 -759 C ATOM 685 C ILE A 92 21.994 1.841 40.101 1.00 32.95 C ANISOU 685 C ILE B 92 4358 3995 4165 -153 541 -716 C ATOM 686 O ILE A 92 22.508 0.855 40.666 1.00 32.87 O ANISOU 686 O ILE B 92 4388 3947 4155 -144 564 -708 O ATOM 687 CB ILE A 92 22.200 4.070 41.340 1.00 33.85 C ANISOU 687 CB ILE B 92 4477 4092 4293 -184 557 -743 C ATOM 688 CG1 ILE A 92 22.970 5.413 41.416 1.00 34.00 C ANISOU 688 CG1 ILE B 92 4478 4113 4329 -212 584 -789 C ATOM 689 CG2 ILE A 92 22.260 3.229 42.650 1.00 33.45 C ANISOU 689 CG2 ILE B 92 4487 3985 4236 -173 572 -714 C ATOM 690 CD1 ILE A 92 22.490 6.358 42.534 1.00 35.03 C ANISOU 690 CD1 ILE B 92 4625 4222 4462 -216 583 -776 C ATOM 691 N LYS A 93 20.840 1.780 39.420 1.00 31.73 N ANISOU 691 N LYS B 93 4172 3881 4001 -137 500 -691 N ATOM 692 CA LYS A 93 20.105 0.515 39.229 1.00 31.62 C ANISOU 692 CA LYS B 93 4162 3872 3982 -113 480 -655 C ATOM 693 C LYS A 93 21.032 -0.597 38.709 1.00 31.76 C ANISOU 693 C LYS B 93 4188 3877 4002 -108 508 -670 C ATOM 694 O LYS A 93 21.071 -1.667 39.282 1.00 31.04 O ANISOU 694 O LYS B 93 4125 3757 3911 -89 514 -649 O ATOM 695 CB LYS A 93 18.905 0.697 38.291 1.00 31.43 C ANISOU 695 CB LYS B 93 4099 3894 3950 -103 443 -636 C ATOM 696 CG LYS A 93 17.962 -0.528 38.191 1.00 30.08 C ANISOU 696 CG LYS B 93 3925 3727 3776 -81 422 -599 C ATOM 697 CD LYS A 93 18.350 -1.484 37.057 1.00 30.92 C ANISOU 697 CD LYS B 93 4015 3850 3882 -73 435 -609 C ATOM 698 CE LYS A 93 17.566 -2.820 37.112 1.00 29.93 C ANISOU 698 CE LYS B 93 3888 3723 3761 -50 421 -575 C ATOM 699 NZ LYS A 93 16.130 -2.619 36.779 1.00 26.19 N ANISOU 699 NZ LYS B 93 3388 3278 3284 -46 390 -549 N ATOM 700 N THR A 94 21.799 -0.311 37.647 1.00 31.95 N ANISOU 700 N THR B 94 4190 3923 4027 -124 527 -709 N ATOM 701 CA THR A 94 22.758 -1.291 37.085 1.00 32.68 C ANISOU 701 CA THR B 94 4293 4003 4122 -123 560 -729 C ATOM 702 C THR A 94 23.755 -1.848 38.113 1.00 33.67 C ANISOU 702 C THR B 94 4468 4069 4255 -123 601 -734 C ATOM 703 O THR A 94 24.018 -3.039 38.127 1.00 34.24 O ANISOU 703 O THR B 94 4563 4120 4329 -104 616 -722 O ATOM 704 CB THR A 94 23.497 -0.768 35.800 1.00 32.20 C ANISOU 704 CB THR B 94 4200 3976 4058 -145 574 -777 C ATOM 705 OG1 THR A 94 24.329 0.356 36.116 1.00 32.17 O ANISOU 705 OG1 THR B 94 4195 3966 4064 -174 594 -818 O ATOM 706 CG2 THR A 94 22.483 -0.345 34.731 1.00 31.52 C ANISOU 706 CG2 THR B 94 4071 3946 3957 -137 534 -767 C ATOM 707 N PHE A 95 24.298 -0.986 38.970 1.00 34.60 N ANISOU 707 N PHE B 95 4607 4160 4379 -143 621 -752 N ATOM 708 CA PHE A 95 25.189 -1.447 40.044 1.00 35.50 C ANISOU 708 CA PHE B 95 4778 4213 4498 -143 664 -753 C ATOM 709 C PHE A 95 24.536 -2.508 40.935 1.00 36.21 C ANISOU 709 C PHE B 95 4904 4276 4579 -105 644 -702 C ATOM 710 O PHE A 95 25.130 -3.557 41.235 1.00 35.61 O ANISOU 710 O PHE B 95 4866 4162 4501 -86 671 -694 O ATOM 711 CB PHE A 95 25.566 -0.272 40.922 1.00 35.12 C ANISOU 711 CB PHE B 95 4745 4142 4456 -168 683 -772 C ATOM 712 CG PHE A 95 26.530 0.678 40.300 1.00 34.57 C ANISOU 712 CG PHE B 95 4649 4086 4401 -207 714 -830 C ATOM 713 CD1 PHE A 95 27.913 0.496 40.485 1.00 34.72 C ANISOU 713 CD1 PHE B 95 4699 4060 4431 -230 776 -868 C ATOM 714 CD2 PHE A 95 26.073 1.782 39.582 1.00 32.24 C ANISOU 714 CD2 PHE B 95 4299 3845 4108 -221 683 -848 C ATOM 715 CE1 PHE A 95 28.825 1.394 39.947 1.00 33.71 C ANISOU 715 CE1 PHE B 95 4543 3946 4320 -270 805 -928 C ATOM 716 CE2 PHE A 95 26.958 2.671 39.023 1.00 31.18 C ANISOU 716 CE2 PHE B 95 4133 3726 3987 -254 707 -905 C ATOM 717 CZ PHE A 95 28.336 2.495 39.211 1.00 35.81 C ANISOU 717 CZ PHE B 95 4746 4273 4588 -282 768 -947 C ATOM 718 N LEU A 96 23.310 -2.201 41.378 1.00 37.28 N ANISOU 718 N LEU B 96 5027 4431 4707 -94 598 -669 N ATOM 719 CA LEU A 96 22.500 -3.098 42.214 1.00 38.71 C ANISOU 719 CA LEU B 96 5231 4598 4878 -60 568 -623 C ATOM 720 C LEU A 96 22.175 -4.442 41.561 1.00 39.02 C ANISOU 720 C LEU B 96 5255 4653 4919 -30 554 -603 C ATOM 721 O LEU A 96 21.846 -5.416 42.254 1.00 38.97 O ANISOU 721 O LEU B 96 5271 4628 4907 2 539 -572 O ATOM 722 CB LEU A 96 21.189 -2.406 42.606 1.00 38.45 C ANISOU 722 CB LEU B 96 5178 4590 4840 -60 521 -599 C ATOM 723 CG LEU A 96 21.038 -1.672 43.947 1.00 41.25 C ANISOU 723 CG LEU B 96 5571 4915 5187 -67 520 -590 C ATOM 724 CD1 LEU A 96 21.349 -2.634 45.127 1.00 42.42 C ANISOU 724 CD1 LEU B 96 5780 5015 5323 -40 528 -566 C ATOM 725 CD2 LEU A 96 21.892 -0.384 44.014 1.00 43.44 C ANISOU 725 CD2 LEU B 96 5852 5180 5472 -101 558 -628 C ATOM 726 N MET A 97 22.218 -4.497 40.229 1.00 39.35 N ANISOU 726 N MET B 97 5254 4730 4967 -39 557 -622 N ATOM 727 CA MET A 97 21.954 -5.754 39.549 1.00 40.10 C ANISOU 727 CA MET B 97 5333 4839 5066 -13 551 -607 C ATOM 728 C MET A 97 22.932 -6.871 39.929 1.00 41.85 C ANISOU 728 C MET B 97 5598 5015 5289 10 587 -606 C ATOM 729 O MET A 97 22.560 -8.049 39.842 1.00 41.35 O ANISOU 729 O MET B 97 5530 4953 5229 43 575 -582 O ATOM 730 CB MET A 97 21.926 -5.587 38.030 1.00 39.96 C ANISOU 730 CB MET B 97 5270 4863 5049 -28 554 -630 C ATOM 731 CG MET A 97 20.626 -5.011 37.456 1.00 38.48 C ANISOU 731 CG MET B 97 5039 4725 4858 -32 512 -615 C ATOM 732 SD MET A 97 19.151 -5.890 38.022 1.00 35.92 S ANISOU 732 SD MET B 97 4703 4409 4537 -2 468 -565 S ATOM 733 CE MET A 97 19.402 -7.581 37.421 1.00 36.28 C ANISOU 733 CE MET B 97 4742 4450 4592 28 485 -557 C ATOM 734 N GLN A 98 24.163 -6.524 40.328 1.00 43.80 N ANISOU 734 N GLN B 98 5886 5221 5536 -7 634 -633 N ATOM 735 CA GLN A 98 25.103 -7.568 40.839 1.00 47.33 C ANISOU 735 CA GLN B 98 6385 5614 5982 18 673 -628 C ATOM 736 C GLN A 98 24.389 -8.437 41.879 1.00 47.59 C ANISOU 736 C GLN B 98 6443 5633 6007 64 639 -581 C ATOM 737 O GLN A 98 24.496 -9.651 41.855 1.00 48.21 O ANISOU 737 O GLN B 98 6533 5698 6088 101 643 -563 O ATOM 738 CB GLN A 98 26.376 -7.000 41.492 1.00 47.61 C ANISOU 738 CB GLN B 98 6475 5598 6018 -5 728 -657 C ATOM 739 CG GLN A 98 27.150 -5.945 40.721 1.00 49.48 C ANISOU 739 CG GLN B 98 6689 5846 6265 -56 761 -710 C ATOM 740 CD GLN A 98 28.181 -5.233 41.593 1.00 50.78 C ANISOU 740 CD GLN B 98 6902 5960 6431 -82 811 -736 C ATOM 741 OE1 GLN A 98 29.086 -5.869 42.148 1.00 56.12 O ANISOU 741 OE1 GLN B 98 7637 6579 7107 -71 859 -736 O ATOM 742 NE2 GLN A 98 28.055 -3.902 41.716 1.00 54.72 N ANISOU 742 NE2 GLN B 98 7378 6478 6935 -117 804 -758 N ATOM 743 N LEU A 99 23.647 -7.805 42.786 1.00 48.06 N ANISOU 743 N LEU B 99 6508 5696 6057 61 605 -562 N ATOM 744 CA LEU A 99 22.918 -8.549 43.810 1.00 48.99 C ANISOU 744 CA LEU B 99 6645 5805 6163 102 566 -521 C ATOM 745 C LEU A 99 21.909 -9.598 43.271 1.00 49.55 C ANISOU 745 C LEU B 99 6668 5915 6243 133 523 -496 C ATOM 746 O LEU A 99 21.483 -10.477 44.032 1.00 50.13 O ANISOU 746 O LEU B 99 6756 5981 6310 173 495 -466 O ATOM 747 CB LEU A 99 22.252 -7.586 44.804 1.00 48.93 C ANISOU 747 CB LEU B 99 6651 5798 6143 87 536 -510 C ATOM 748 CG LEU A 99 23.089 -6.489 45.510 1.00 49.68 C ANISOU 748 CG LEU B 99 6793 5853 6231 57 576 -531 C ATOM 749 CD1 LEU A 99 22.261 -5.818 46.602 1.00 48.70 C ANISOU 749 CD1 LEU B 99 6685 5728 6092 54 542 -512 C ATOM 750 CD2 LEU A 99 24.421 -7.002 46.100 1.00 50.31 C ANISOU 750 CD2 LEU B 99 6943 5870 6303 71 632 -537 C ATOM 751 N PHE A 100 21.521 -9.504 41.988 1.00 49.04 N ANISOU 751 N PHE B 100 6547 5894 6193 115 519 -510 N ATOM 752 CA PHE A 100 20.602 -10.478 41.356 1.00 49.48 C ANISOU 752 CA PHE B 100 6554 5986 6259 139 489 -491 C ATOM 753 C PHE A 100 21.252 -11.428 40.351 1.00 50.00 C ANISOU 753 C PHE B 100 6610 6050 6338 154 523 -503 C ATOM 754 O PHE A 100 20.723 -12.503 40.094 1.00 49.91 O ANISOU 754 O PHE B 100 6572 6055 6338 186 507 -485 O ATOM 755 CB PHE A 100 19.487 -9.775 40.586 1.00 49.43 C ANISOU 755 CB PHE B 100 6491 6030 6259 112 459 -493 C ATOM 756 CG PHE A 100 18.478 -9.108 41.430 1.00 49.04 C ANISOU 756 CG PHE B 100 6439 5991 6202 103 416 -476 C ATOM 757 CD1 PHE A 100 17.592 -8.226 40.851 1.00 49.79 C ANISOU 757 CD1 PHE B 100 6496 6123 6299 75 397 -480 C ATOM 758 CD2 PHE A 100 18.398 -9.368 42.787 1.00 49.43 C ANISOU 758 CD2 PHE B 100 6526 6013 6240 125 397 -456 C ATOM 759 CE1 PHE A 100 16.652 -7.610 41.598 1.00 51.13 C ANISOU 759 CE1 PHE B 100 6664 6299 6463 66 362 -465 C ATOM 760 CE2 PHE A 100 17.472 -8.770 43.558 1.00 51.35 C ANISOU 760 CE2 PHE B 100 6769 6266 6476 115 359 -443 C ATOM 761 CZ PHE A 100 16.587 -7.867 42.980 1.00 52.66 C ANISOU 761 CZ PHE B 100 6896 6466 6646 84 343 -448 C ATOM 762 N GLU A 101 22.347 -10.990 39.733 1.00 51.09 N ANISOU 762 N GLU B 101 6764 6172 6476 129 571 -536 N ATOM 763 CA GLU A 101 23.078 -11.783 38.735 1.00 52.28 C ANISOU 763 CA GLU B 101 6911 6318 6636 137 611 -554 C ATOM 764 C GLU A 101 23.424 -13.173 39.277 1.00 52.26 C ANISOU 764 C GLU B 101 6938 6280 6637 189 623 -531 C ATOM 765 O GLU A 101 23.203 -14.179 38.609 1.00 52.51 O ANISOU 765 O GLU B 101 6944 6327 6682 214 625 -523 O ATOM 766 CB GLU A 101 24.354 -11.036 38.301 1.00 52.73 C ANISOU 766 CB GLU B 101 6993 6352 6689 100 663 -598 C ATOM 767 CG GLU A 101 24.147 -9.932 37.227 1.00 53.58 C ANISOU 767 CG GLU B 101 7059 6506 6795 55 658 -628 C ATOM 768 CD GLU A 101 25.269 -8.866 37.207 1.00 53.58 C ANISOU 768 CD GLU B 101 7080 6486 6791 14 696 -672 C ATOM 769 OE1 GLU A 101 26.473 -9.222 37.361 1.00 56.40 O ANISOU 769 OE1 GLU B 101 7480 6799 7152 11 747 -693 O ATOM 770 OE2 GLU A 101 24.936 -7.666 37.044 1.00 53.09 O ANISOU 770 OE2 GLU B 101 6994 6453 6725 -17 676 -687 O ATOM 771 N LYS A 102 23.950 -13.207 40.500 1.00 52.30 N ANISOU 771 N LYS B 102 7001 6240 6631 207 631 -518 N ATOM 772 CA LYS A 102 24.273 -14.446 41.228 1.00 52.55 C ANISOU 772 CA LYS B 102 7071 6236 6661 263 636 -491 C ATOM 773 C LYS A 102 23.147 -15.493 41.273 1.00 52.09 C ANISOU 773 C LYS B 102 6967 6210 6612 307 585 -459 C ATOM 774 O LYS A 102 23.415 -16.704 41.286 1.00 52.86 O ANISOU 774 O LYS B 102 7075 6293 6718 356 595 -444 O ATOM 775 CB LYS A 102 24.790 -14.118 42.639 1.00 53.28 C ANISOU 775 CB LYS B 102 7233 6278 6732 273 643 -479 C ATOM 776 CG LYS A 102 24.206 -12.823 43.260 1.00 55.10 C ANISOU 776 CG LYS B 102 7461 6524 6951 236 612 -481 C ATOM 777 CD LYS A 102 25.277 -11.990 43.997 1.00 57.10 C ANISOU 777 CD LYS B 102 7782 6724 7190 212 659 -499 C ATOM 778 CE LYS A 102 25.611 -12.534 45.399 1.00 58.40 C ANISOU 778 CE LYS B 102 8020 6837 7332 256 662 -469 C ATOM 779 NZ LYS A 102 26.805 -11.852 46.016 1.00 58.56 N ANISOU 779 NZ LYS B 102 8112 6796 7341 232 723 -489 N ATOM 780 N CYS A 103 21.899 -15.031 41.282 1.00 50.38 N ANISOU 780 N CYS B 103 6703 6041 6399 291 533 -449 N ATOM 781 CA CYS A 103 20.735 -15.916 41.158 1.00 49.75 C ANISOU 781 CA CYS B 103 6567 6001 6334 321 486 -427 C ATOM 782 C CYS A 103 20.309 -16.198 39.710 1.00 47.57 C ANISOU 782 C CYS B 103 6231 5764 6080 306 497 -440 C ATOM 783 O CYS A 103 19.407 -16.991 39.473 1.00 47.85 O ANISOU 783 O CYS B 103 6217 5831 6133 328 469 -425 O ATOM 784 CB CYS A 103 19.551 -15.350 41.961 1.00 49.98 C ANISOU 784 CB CYS B 103 6578 6057 6356 310 427 -410 C ATOM 785 SG CYS A 103 19.771 -15.625 43.739 1.00 55.31 S ANISOU 785 SG CYS B 103 7316 6692 7005 352 401 -384 S ATOM 786 N GLY A 104 20.960 -15.547 38.751 1.00 45.73 N ANISOU 786 N GLY B 104 6002 5530 5845 268 539 -470 N ATOM 787 CA GLY A 104 20.588 -15.655 37.335 1.00 43.35 C ANISOU 787 CA GLY B 104 5650 5264 5556 250 551 -485 C ATOM 788 C GLY A 104 19.316 -14.870 37.019 1.00 41.44 C ANISOU 788 C GLY B 104 5361 5069 5314 219 512 -481 C ATOM 789 O GLY A 104 18.631 -15.154 36.025 1.00 41.32 O ANISOU 789 O GLY B 104 5299 5088 5311 213 511 -482 O ATOM 790 N ASN A 105 18.982 -13.904 37.879 1.00 38.45 N ANISOU 790 N ASN B 105 4997 4689 4922 200 483 -475 N ATOM 791 CA ASN A 105 17.805 -13.083 37.664 1.00 35.71 C ANISOU 791 CA ASN B 105 4613 4380 4574 171 449 -470 C ATOM 792 C ASN A 105 18.185 -11.758 37.004 1.00 34.81 C ANISOU 792 C ASN B 105 4505 4274 4446 128 468 -496 C ATOM 793 O ASN A 105 18.406 -10.749 37.672 1.00 33.52 O ANISOU 793 O ASN B 105 4368 4098 4270 108 462 -502 O ATOM 794 CB ASN A 105 17.010 -12.848 38.967 1.00 35.28 C ANISOU 794 CB ASN B 105 4565 4324 4515 177 402 -448 C ATOM 795 CG ASN A 105 15.749 -12.062 38.728 1.00 31.72 C ANISOU 795 CG ASN B 105 4077 3909 4065 148 371 -443 C ATOM 796 OD1 ASN A 105 15.210 -12.088 37.634 1.00 30.92 O ANISOU 796 OD1 ASN B 105 3938 3838 3973 135 378 -448 O ATOM 797 ND2 ASN A 105 15.286 -11.340 39.732 1.00 29.42 N ANISOU 797 ND2 ASN B 105 3802 3612 3763 137 342 -434 N ATOM 798 N THR A 106 18.245 -11.788 35.677 1.00 33.88 N ANISOU 798 N THR B 106 4362 4179 4329 115 490 -513 N ATOM 799 CA THR A 106 18.615 -10.625 34.894 1.00 32.65 C ANISOU 799 CA THR B 106 4208 4039 4159 80 505 -541 C ATOM 800 C THR A 106 17.413 -10.040 34.149 1.00 31.82 C ANISOU 800 C THR B 106 4064 3977 4050 63 481 -533 C ATOM 801 O THR A 106 17.488 -8.899 33.688 1.00 30.56 O ANISOU 801 O THR B 106 3904 3833 3875 37 480 -549 O ATOM 802 CB THR A 106 19.729 -10.959 33.895 1.00 32.81 C ANISOU 802 CB THR B 106 4238 4052 4176 76 551 -571 C ATOM 803 OG1 THR A 106 19.297 -12.016 33.049 1.00 32.62 O ANISOU 803 OG1 THR B 106 4186 4045 4163 95 560 -563 O ATOM 804 CG2 THR A 106 20.981 -11.402 34.620 1.00 34.11 C ANISOU 804 CG2 THR B 106 4448 4169 4344 88 582 -581 C ATOM 805 N ASP A 107 16.325 -10.821 34.032 1.00 31.40 N ANISOU 805 N ASP B 107 3980 3941 4011 78 463 -509 N ATOM 806 CA ASP A 107 15.073 -10.310 33.488 1.00 30.99 C ANISOU 806 CA ASP B 107 3896 3923 3957 63 443 -497 C ATOM 807 C ASP A 107 14.301 -9.430 34.497 1.00 30.75 C ANISOU 807 C ASP B 107 3870 3890 3922 50 407 -482 C ATOM 808 O ASP A 107 13.256 -9.823 35.047 1.00 30.91 O ANISOU 808 O ASP B 107 3871 3916 3956 57 380 -460 O ATOM 809 CB ASP A 107 14.201 -11.429 32.932 1.00 31.33 C ANISOU 809 CB ASP B 107 3902 3983 4020 78 445 -482 C ATOM 810 CG ASP A 107 13.056 -10.905 32.073 1.00 32.42 C ANISOU 810 CG ASP B 107 4014 4152 4152 59 440 -475 C ATOM 811 OD1 ASP A 107 12.926 -9.669 31.944 1.00 33.12 O ANISOU 811 OD1 ASP B 107 4115 4249 4220 38 431 -479 O ATOM 812 OD2 ASP A 107 12.271 -11.715 31.530 1.00 33.10 O ANISOU 812 OD2 ASP B 107 4069 4252 4254 66 447 -464 O ATOM 813 N VAL A 108 14.797 -8.213 34.691 1.00 30.07 N ANISOU 813 N VAL B 108 3807 3800 3820 31 407 -496 N ATOM 814 CA VAL A 108 14.277 -7.314 35.715 1.00 30.07 C ANISOU 814 CA VAL B 108 3818 3791 3815 20 379 -485 C ATOM 815 C VAL A 108 14.033 -5.926 35.093 1.00 30.18 C ANISOU 815 C VAL B 108 3828 3827 3812 -3 377 -495 C ATOM 816 O VAL A 108 14.928 -5.368 34.475 1.00 31.92 O ANISOU 816 O VAL B 108 4056 4052 4021 -12 396 -520 O ATOM 817 CB VAL A 108 15.268 -7.251 36.895 1.00 30.04 C ANISOU 817 CB VAL B 108 3854 3751 3809 26 383 -492 C ATOM 818 CG1 VAL A 108 14.866 -6.197 37.948 1.00 31.11 C ANISOU 818 CG1 VAL B 108 4008 3876 3937 12 360 -484 C ATOM 819 CG2 VAL A 108 15.393 -8.635 37.536 1.00 30.27 C ANISOU 819 CG2 VAL B 108 3889 3761 3851 56 380 -477 C ATOM 820 N GLU A 109 12.828 -5.391 35.226 1.00 28.09 N ANISOU 820 N GLU B 109 3551 3575 3547 -11 354 -476 N ATOM 821 CA GLU A 109 12.558 -4.043 34.776 1.00 27.74 C ANISOU 821 CA GLU B 109 3507 3547 3486 -26 350 -482 C ATOM 822 C GLU A 109 13.075 -2.952 35.736 1.00 26.81 C ANISOU 822 C GLU B 109 3414 3410 3363 -37 343 -492 C ATOM 823 O GLU A 109 13.465 -3.243 36.869 1.00 26.18 O ANISOU 823 O GLU B 109 3355 3302 3290 -34 340 -490 O ATOM 824 CB GLU A 109 11.051 -3.878 34.489 1.00 27.49 C ANISOU 824 CB GLU B 109 3457 3531 3455 -31 334 -457 C ATOM 825 CG GLU A 109 10.623 -4.658 33.244 1.00 29.04 C ANISOU 825 CG GLU B 109 3631 3750 3653 -25 350 -453 C ATOM 826 CD GLU A 109 9.234 -4.330 32.770 1.00 30.88 C ANISOU 826 CD GLU B 109 3851 3998 3884 -32 345 -432 C ATOM 827 OE1 GLU A 109 8.556 -3.411 33.326 1.00 26.80 O ANISOU 827 OE1 GLU B 109 3344 3475 3363 -41 329 -421 O ATOM 828 OE2 GLU A 109 8.812 -5.014 31.816 1.00 32.23 O ANISOU 828 OE2 GLU B 109 4005 4183 4057 -28 362 -427 O ATOM 829 N GLY A 110 13.116 -1.717 35.238 1.00 26.56 N ANISOU 829 N GLY B 110 3379 3395 3317 -47 343 -503 N ATOM 830 CA GLY A 110 13.395 -0.525 36.061 1.00 27.28 C ANISOU 830 CA GLY B 110 3487 3472 3405 -57 337 -512 C ATOM 831 C GLY A 110 14.753 0.113 35.796 1.00 27.46 C ANISOU 831 C GLY B 110 3514 3496 3423 -66 357 -549 C ATOM 832 O GLY A 110 15.705 -0.568 35.355 1.00 26.73 O ANISOU 832 O GLY B 110 3422 3401 3331 -65 378 -569 O ATOM 833 N VAL A 111 14.808 1.438 35.978 1.00 27.18 N ANISOU 833 N VAL B 111 3479 3465 3382 -74 352 -560 N ATOM 834 CA VAL A 111 16.075 2.167 35.980 1.00 28.01 C ANISOU 834 CA VAL B 111 3585 3568 3488 -87 371 -599 C ATOM 835 C VAL A 111 16.094 3.145 37.174 1.00 28.64 C ANISOU 835 C VAL B 111 3682 3625 3576 -96 370 -600 C ATOM 836 O VAL A 111 15.435 2.888 38.198 1.00 27.74 O ANISOU 836 O VAL B 111 3589 3484 3466 -94 360 -574 O ATOM 837 CB VAL A 111 16.392 2.848 34.580 1.00 28.09 C ANISOU 837 CB VAL B 111 3566 3622 3483 -87 369 -625 C ATOM 838 CG1 VAL A 111 16.497 1.807 33.494 1.00 27.05 C ANISOU 838 CG1 VAL B 111 3426 3508 3343 -79 376 -627 C ATOM 839 CG2 VAL A 111 15.361 3.926 34.197 1.00 28.08 C ANISOU 839 CG2 VAL B 111 3552 3648 3470 -77 344 -609 C ATOM 840 N ASP A 112 16.824 4.255 37.033 1.00 28.97 N ANISOU 840 N ASP B 112 3712 3675 3619 -107 379 -633 N ATOM 841 CA ASP A 112 16.806 5.358 38.004 1.00 29.32 C ANISOU 841 CA ASP B 112 3767 3702 3672 -116 381 -637 C ATOM 842 C ASP A 112 15.723 6.405 37.703 1.00 29.53 C ANISOU 842 C ASP B 112 3777 3754 3691 -105 356 -620 C ATOM 843 O ASP A 112 15.519 6.786 36.541 1.00 30.01 O ANISOU 843 O ASP B 112 3810 3854 3739 -95 343 -625 O ATOM 844 CB ASP A 112 18.145 6.079 38.012 1.00 29.98 C ANISOU 844 CB ASP B 112 3841 3783 3765 -134 408 -685 C ATOM 845 CG ASP A 112 19.276 5.240 38.589 1.00 31.68 C ANISOU 845 CG ASP B 112 4085 3962 3991 -147 442 -703 C ATOM 846 OD1 ASP A 112 19.071 4.056 38.933 1.00 32.73 O ANISOU 846 OD1 ASP B 112 4243 4072 4121 -138 443 -678 O ATOM 847 OD2 ASP A 112 20.386 5.784 38.687 1.00 36.60 O ANISOU 847 OD2 ASP B 112 4703 4576 4625 -167 470 -744 O ATOM 848 N SER A 113 15.047 6.871 38.747 1.00 29.62 N ANISOU 848 N SER B 113 3809 3740 3707 -106 351 -599 N ATOM 849 CA SER A 113 14.192 8.048 38.654 1.00 30.96 C ANISOU 849 CA SER B 113 3968 3924 3873 -97 335 -588 C ATOM 850 C SER A 113 14.886 9.226 39.306 1.00 32.09 C ANISOU 850 C SER B 113 4109 4056 4029 -107 352 -616 C ATOM 851 O SER A 113 15.470 9.103 40.402 1.00 32.20 O ANISOU 851 O SER B 113 4149 4032 4054 -123 373 -625 O ATOM 852 CB SER A 113 12.856 7.822 39.347 1.00 30.60 C ANISOU 852 CB SER B 113 3945 3858 3824 -93 321 -547 C ATOM 853 OG SER A 113 12.137 6.856 38.619 1.00 31.55 O ANISOU 853 OG SER B 113 4059 3994 3935 -85 307 -524 O ATOM 854 N THR A 114 14.784 10.380 38.649 1.00 32.40 N ANISOU 854 N THR B 114 4119 4126 4065 -96 342 -628 N ATOM 855 CA THR A 114 15.344 11.608 39.201 1.00 33.29 C ANISOU 855 CA THR B 114 4222 4234 4194 -103 357 -655 C ATOM 856 C THR A 114 14.466 12.859 39.089 1.00 32.56 C ANISOU 856 C THR B 114 4117 4155 4098 -83 341 -642 C ATOM 857 O THR A 114 13.987 13.217 38.010 1.00 32.27 O ANISOU 857 O THR B 114 4057 4158 4046 -60 318 -634 O ATOM 858 CB THR A 114 16.686 11.920 38.551 1.00 34.05 C ANISOU 858 CB THR B 114 4283 4355 4298 -113 369 -707 C ATOM 859 OG1 THR A 114 17.398 10.687 38.343 1.00 37.97 O ANISOU 859 OG1 THR B 114 4790 4843 4793 -127 383 -717 O ATOM 860 CG2 THR A 114 17.507 12.833 39.454 1.00 34.50 C ANISOU 860 CG2 THR B 114 4338 4391 4381 -132 398 -740 C ATOM 861 N ASN A 115 14.227 13.470 40.243 1.00 31.72 N ANISOU 861 N ASN B 115 4033 4015 4005 -90 355 -636 N ATOM 862 CA ASN A 115 14.130 14.912 40.378 1.00 31.74 C ANISOU 862 CA ASN B 115 4016 4025 4018 -78 357 -648 C ATOM 863 C ASN A 115 14.336 15.192 41.845 1.00 31.80 C ANISOU 863 C ASN B 115 4056 3984 4043 -98 386 -652 C ATOM 864 O ASN A 115 13.444 14.926 42.650 1.00 31.89 O ANISOU 864 O ASN B 115 4106 3962 4047 -100 385 -619 O ATOM 865 CB ASN A 115 12.801 15.529 39.930 1.00 32.14 C ANISOU 865 CB ASN B 115 4067 4091 4055 -48 334 -612 C ATOM 866 CG ASN A 115 12.812 17.086 40.030 1.00 32.40 C ANISOU 866 CG ASN B 115 4076 4134 4100 -30 337 -627 C ATOM 867 OD1 ASN A 115 13.217 17.775 39.088 1.00 32.95 O ANISOU 867 OD1 ASN B 115 4103 4248 4168 -10 323 -650 O ATOM 868 ND2 ASN A 115 12.364 17.621 41.167 1.00 30.72 N ANISOU 868 ND2 ASN B 115 3891 3882 3899 -36 355 -616 N ATOM 869 N ALA A 116 15.513 15.727 42.168 1.00 31.37 N ANISOU 869 N ALA B 116 3985 3925 4010 -115 414 -695 N ATOM 870 CA ALA A 116 15.862 16.152 43.519 1.00 30.62 C ANISOU 870 CA ALA B 116 3919 3783 3932 -134 449 -706 C ATOM 871 C ALA A 116 15.367 15.119 44.559 1.00 29.22 C ANISOU 871 C ALA B 116 3804 3558 3741 -146 454 -672 C ATOM 872 O ALA A 116 15.520 13.894 44.372 1.00 28.58 O ANISOU 872 O ALA B 116 3737 3475 3648 -151 446 -662 O ATOM 873 CB ALA A 116 15.316 17.618 43.778 1.00 30.15 C ANISOU 873 CB ALA B 116 3845 3726 3885 -118 452 -706 C ATOM 874 N CYS A 117 14.757 15.575 45.629 1.00 27.59 N ANISOU 874 N CYS B 117 3632 3315 3534 -148 465 -655 N ATOM 875 CA CYS A 117 14.347 14.655 46.705 1.00 27.72 C ANISOU 875 CA CYS B 117 3708 3288 3536 -159 467 -628 C ATOM 876 C CYS A 117 13.073 13.819 46.384 1.00 26.37 C ANISOU 876 C CYS B 117 3548 3127 3343 -146 428 -587 C ATOM 877 O CYS A 117 12.589 13.069 47.242 1.00 25.99 O ANISOU 877 O CYS B 117 3543 3049 3282 -153 423 -565 O ATOM 878 CB CYS A 117 14.170 15.435 48.013 1.00 28.38 C ANISOU 878 CB CYS B 117 3830 3328 3625 -168 495 -629 C ATOM 879 SG CYS A 117 15.672 16.407 48.393 1.00 33.95 S ANISOU 879 SG CYS B 117 4520 4020 4361 -187 548 -681 S ATOM 880 N TYR A 118 12.565 13.926 45.155 1.00 23.47 N ANISOU 880 N TYR B 118 3142 2802 2973 -128 403 -578 N ATOM 881 CA TYR A 118 11.313 13.259 44.767 1.00 23.10 C ANISOU 881 CA TYR B 118 3102 2765 2910 -118 372 -541 C ATOM 882 C TYR A 118 11.542 11.923 44.032 1.00 21.71 C ANISOU 882 C TYR B 118 2915 2609 2725 -117 357 -536 C ATOM 883 O TYR A 118 10.614 11.120 43.871 1.00 21.03 O ANISOU 883 O TYR B 118 2837 2526 2629 -114 336 -508 O ATOM 884 CB TYR A 118 10.448 14.233 43.930 1.00 22.27 C ANISOU 884 CB TYR B 118 2972 2687 2803 -96 359 -528 C ATOM 885 CG TYR A 118 9.117 13.699 43.495 1.00 23.96 C ANISOU 885 CG TYR B 118 3194 2907 3002 -87 336 -492 C ATOM 886 CD1 TYR A 118 7.984 13.740 44.353 1.00 17.97 C ANISOU 886 CD1 TYR B 118 2472 2117 2240 -95 334 -467 C ATOM 887 CD2 TYR A 118 8.955 13.161 42.194 1.00 25.06 C ANISOU 887 CD2 TYR B 118 3306 3084 3132 -74 318 -484 C ATOM 888 CE1 TYR A 118 6.745 13.244 43.910 1.00 20.18 C ANISOU 888 CE1 TYR B 118 2756 2401 2509 -91 317 -437 C ATOM 889 CE2 TYR A 118 7.710 12.675 41.754 1.00 22.45 C ANISOU 889 CE2 TYR B 118 2983 2757 2790 -69 303 -452 C ATOM 890 CZ TYR A 118 6.623 12.726 42.619 1.00 24.07 C ANISOU 890 CZ TYR B 118 3221 2929 2995 -78 304 -430 C ATOM 891 OH TYR A 118 5.417 12.232 42.171 1.00 26.87 O ANISOU 891 OH TYR B 118 3582 3286 3342 -78 294 -402 O ATOM 892 N GLY A 119 12.780 11.680 43.589 1.00 21.80 N ANISOU 892 N GLY B 119 2907 2634 2743 -122 370 -565 N ATOM 893 CA GLY A 119 13.111 10.459 42.834 1.00 21.49 C ANISOU 893 CA GLY B 119 2856 2613 2697 -121 360 -565 C ATOM 894 C GLY A 119 12.684 9.145 43.458 1.00 20.93 C ANISOU 894 C GLY B 119 2817 2518 2618 -124 351 -540 C ATOM 895 O GLY A 119 12.293 8.229 42.744 1.00 21.23 O ANISOU 895 O GLY B 119 2842 2575 2650 -117 334 -525 O ATOM 896 N GLY A 120 12.757 9.037 44.791 1.00 20.93 N ANISOU 896 N GLY B 120 2858 2478 2618 -134 361 -536 N ATOM 897 CA GLY A 120 12.366 7.788 45.469 1.00 20.57 C ANISOU 897 CA GLY B 120 2843 2411 2561 -134 347 -514 C ATOM 898 C GLY A 120 10.854 7.546 45.392 1.00 19.87 C ANISOU 898 C GLY B 120 2751 2333 2467 -130 317 -483 C ATOM 899 O GLY A 120 10.403 6.427 45.142 1.00 20.51 O ANISOU 899 O GLY B 120 2826 2423 2544 -125 297 -467 O ATOM 900 N THR A 121 10.072 8.597 45.634 1.00 19.13 N ANISOU 900 N THR B 121 2662 2233 2372 -132 316 -476 N ATOM 901 CA THR A 121 8.631 8.566 45.378 1.00 18.73 C ANISOU 901 CA THR B 121 2606 2193 2319 -131 294 -451 C ATOM 902 C THR A 121 8.259 8.171 43.940 1.00 18.92 C ANISOU 902 C THR B 121 2592 2255 2343 -120 283 -442 C ATOM 903 O THR A 121 7.405 7.286 43.750 1.00 18.83 O ANISOU 903 O THR B 121 2576 2249 2330 -121 267 -424 O ATOM 904 CB THR A 121 7.990 9.929 45.749 1.00 19.70 C ANISOU 904 CB THR B 121 2741 2301 2442 -132 303 -447 C ATOM 905 OG1 THR A 121 8.385 10.233 47.089 1.00 19.01 O ANISOU 905 OG1 THR B 121 2693 2177 2353 -143 317 -456 O ATOM 906 CG2 THR A 121 6.436 9.883 45.675 1.00 15.83 C ANISOU 906 CG2 THR B 121 2256 1811 1948 -135 287 -421 C ATOM 907 N ALA A 122 8.872 8.840 42.943 1.00 18.21 N ANISOU 907 N ALA B 122 2474 2190 2255 -109 293 -457 N ATOM 908 CA ALA A 122 8.578 8.536 41.543 1.00 18.95 C ANISOU 908 CA ALA B 122 2537 2321 2344 -96 285 -450 C ATOM 909 C ALA A 122 8.787 7.045 41.265 1.00 18.72 C ANISOU 909 C ALA B 122 2500 2298 2315 -98 278 -447 C ATOM 910 O ALA A 122 7.974 6.410 40.561 1.00 19.73 O ANISOU 910 O ALA B 122 2614 2441 2439 -95 268 -429 O ATOM 911 CB ALA A 122 9.442 9.389 40.573 1.00 18.08 C ANISOU 911 CB ALA B 122 2398 2240 2232 -84 293 -473 C ATOM 912 N ALA A 123 9.882 6.502 41.788 1.00 17.47 N ANISOU 912 N ALA B 123 2351 2127 2161 -103 287 -465 N ATOM 913 CA ALA A 123 10.162 5.076 41.629 1.00 18.12 C ANISOU 913 CA ALA B 123 2429 2211 2244 -101 282 -462 C ATOM 914 C ALA A 123 9.116 4.176 42.306 1.00 18.73 C ANISOU 914 C ALA B 123 2518 2275 2322 -104 263 -437 C ATOM 915 O ALA A 123 8.745 3.094 41.783 1.00 18.05 O ANISOU 915 O ALA B 123 2414 2204 2240 -99 253 -427 O ATOM 916 CB ALA A 123 11.571 4.713 42.124 1.00 16.95 C ANISOU 916 CB ALA B 123 2296 2046 2099 -104 300 -484 C ATOM 917 N LEU A 124 8.701 4.589 43.501 1.00 18.59 N ANISOU 917 N LEU B 124 2530 2230 2302 -113 257 -432 N ATOM 918 CA LEU A 124 7.759 3.829 44.307 1.00 19.00 C ANISOU 918 CA LEU B 124 2595 2270 2354 -118 235 -414 C ATOM 919 C LEU A 124 6.427 3.718 43.590 1.00 19.43 C ANISOU 919 C LEU B 124 2626 2344 2414 -123 224 -398 C ATOM 920 O LEU A 124 5.837 2.640 43.502 1.00 20.19 O ANISOU 920 O LEU B 124 2706 2448 2515 -124 209 -388 O ATOM 921 CB LEU A 124 7.621 4.476 45.703 1.00 17.75 C ANISOU 921 CB LEU B 124 2478 2078 2188 -128 234 -415 C ATOM 922 CG LEU A 124 6.563 3.912 46.667 1.00 20.48 C ANISOU 922 CG LEU B 124 2841 2411 2530 -137 208 -402 C ATOM 923 CD1 LEU A 124 6.867 2.448 46.985 1.00 21.31 C ANISOU 923 CD1 LEU B 124 2945 2520 2634 -126 189 -399 C ATOM 924 CD2 LEU A 124 6.460 4.769 47.942 1.00 19.52 C ANISOU 924 CD2 LEU B 124 2765 2257 2397 -148 212 -405 C ATOM 925 N LEU A 125 5.976 4.844 43.063 1.00 20.31 N ANISOU 925 N LEU B 125 2734 2461 2523 -124 234 -394 N ATOM 926 CA LEU A 125 4.737 4.906 42.327 1.00 20.28 C ANISOU 926 CA LEU B 125 2715 2470 2521 -127 233 -377 C ATOM 927 C LEU A 125 4.820 4.121 41.013 1.00 20.00 C ANISOU 927 C LEU B 125 2647 2464 2488 -118 237 -375 C ATOM 928 O LEU A 125 3.871 3.449 40.643 1.00 19.74 O ANISOU 928 O LEU B 125 2600 2439 2462 -124 233 -362 O ATOM 929 CB LEU A 125 4.350 6.360 42.066 1.00 20.22 C ANISOU 929 CB LEU B 125 2716 2458 2507 -124 245 -373 C ATOM 930 CG LEU A 125 4.132 7.292 43.275 1.00 23.55 C ANISOU 930 CG LEU B 125 3171 2849 2928 -134 247 -375 C ATOM 931 CD1 LEU A 125 3.564 8.628 42.782 1.00 22.57 C ANISOU 931 CD1 LEU B 125 3051 2724 2800 -125 261 -367 C ATOM 932 CD2 LEU A 125 3.222 6.663 44.360 1.00 24.51 C ANISOU 932 CD2 LEU B 125 3313 2948 3052 -154 232 -368 C ATOM 933 N ASN A 126 5.946 4.202 40.306 1.00 19.55 N ANISOU 933 N ASN B 126 2578 2424 2426 -105 246 -389 N ATOM 934 CA ASN A 126 6.119 3.425 39.067 1.00 19.34 C ANISOU 934 CA ASN B 126 2525 2425 2399 -95 252 -389 C ATOM 935 C ASN A 126 6.019 1.935 39.367 1.00 19.88 C ANISOU 935 C ASN B 126 2582 2491 2480 -98 243 -386 C ATOM 936 O ASN A 126 5.523 1.142 38.571 1.00 19.10 O ANISOU 936 O ASN B 126 2461 2408 2386 -97 247 -378 O ATOM 937 CB ASN A 126 7.510 3.707 38.459 1.00 19.99 C ANISOU 937 CB ASN B 126 2599 2522 2474 -84 263 -412 C ATOM 938 CG ASN A 126 7.576 5.031 37.749 1.00 20.09 C ANISOU 938 CG ASN B 126 2610 2551 2474 -75 269 -417 C ATOM 939 OD1 ASN A 126 6.564 5.538 37.277 1.00 22.34 O ANISOU 939 OD1 ASN B 126 2895 2842 2752 -70 269 -399 O ATOM 940 ND2 ASN A 126 8.771 5.585 37.638 1.00 21.91 N ANISOU 940 ND2 ASN B 126 2835 2788 2701 -71 276 -443 N ATOM 941 N CYS A 127 6.533 1.543 40.514 1.00 20.02 N ANISOU 941 N CYS B 127 2616 2488 2501 -100 233 -393 N ATOM 942 CA CYS A 127 6.582 0.136 40.868 1.00 21.18 C ANISOU 942 CA CYS B 127 2754 2635 2659 -96 222 -390 C ATOM 943 C CYS A 127 5.208 -0.352 41.278 1.00 20.13 C ANISOU 943 C CYS B 127 2611 2501 2536 -108 204 -376 C ATOM 944 O CYS A 127 4.800 -1.441 40.922 1.00 19.97 O ANISOU 944 O CYS B 127 2564 2494 2528 -106 198 -372 O ATOM 945 CB CYS A 127 7.486 -0.012 42.054 1.00 22.02 C ANISOU 945 CB CYS B 127 2889 2717 2760 -91 216 -399 C ATOM 946 SG CYS A 127 8.608 -1.322 41.926 1.00 34.80 S ANISOU 946 SG CYS B 127 4503 4337 4384 -72 221 -408 S ATOM 947 N VAL A 128 4.490 0.459 42.053 1.00 18.64 N ANISOU 947 N VAL B 128 2444 2295 2343 -122 196 -371 N ATOM 948 CA VAL A 128 3.109 0.119 42.363 1.00 18.37 C ANISOU 948 CA VAL B 128 2400 2261 2320 -140 182 -362 C ATOM 949 C VAL A 128 2.338 0.019 41.040 1.00 18.13 C ANISOU 949 C VAL B 128 2342 2250 2298 -144 200 -353 C ATOM 950 O VAL A 128 1.633 -0.944 40.823 1.00 17.91 O ANISOU 950 O VAL B 128 2287 2233 2287 -151 196 -351 O ATOM 951 CB VAL A 128 2.465 1.169 43.310 1.00 18.04 C ANISOU 951 CB VAL B 128 2390 2194 2270 -156 177 -360 C ATOM 952 CG1 VAL A 128 0.987 0.986 43.369 1.00 19.51 C ANISOU 952 CG1 VAL B 128 2566 2380 2468 -179 171 -353 C ATOM 953 CG2 VAL A 128 3.082 1.039 44.704 1.00 16.28 C ANISOU 953 CG2 VAL B 128 2198 1951 2037 -153 158 -368 C ATOM 954 N ASN A 129 2.470 1.008 40.154 1.00 17.10 N ANISOU 954 N ASN B 129 2218 2124 2155 -138 221 -349 N ATOM 955 CA ASN A 129 1.725 0.937 38.882 1.00 17.05 C ANISOU 955 CA ASN B 129 2194 2133 2151 -140 242 -338 C ATOM 956 C ASN A 129 2.131 -0.332 38.090 1.00 17.63 C ANISOU 956 C ASN B 129 2235 2228 2234 -130 247 -342 C ATOM 957 O ASN A 129 1.281 -0.973 37.448 1.00 17.37 O ANISOU 957 O ASN B 129 2181 2205 2214 -138 259 -335 O ATOM 958 CB ASN A 129 1.964 2.195 38.049 1.00 15.62 C ANISOU 958 CB ASN B 129 2027 1957 1950 -127 259 -334 C ATOM 959 CG ASN A 129 1.440 3.435 38.713 1.00 18.55 C ANISOU 959 CG ASN B 129 2427 2306 2314 -133 258 -328 C ATOM 960 OD1 ASN A 129 0.628 3.360 39.640 1.00 17.54 O ANISOU 960 OD1 ASN B 129 2309 2158 2196 -153 250 -325 O ATOM 961 ND2 ASN A 129 1.930 4.599 38.279 1.00 15.56 N ANISOU 961 ND2 ASN B 129 2062 1933 1920 -116 266 -329 N ATOM 962 N TRP A 130 3.411 -0.710 38.154 1.00 16.51 N ANISOU 962 N TRP B 130 2092 2092 2088 -114 243 -355 N ATOM 963 CA TRP A 130 3.866 -1.911 37.426 1.00 17.97 C ANISOU 963 CA TRP B 130 2250 2295 2283 -102 251 -360 C ATOM 964 C TRP A 130 3.137 -3.192 37.913 1.00 19.79 C ANISOU 964 C TRP B 130 2454 2527 2539 -110 237 -357 C ATOM 965 O TRP A 130 2.631 -3.974 37.087 1.00 20.45 O ANISOU 965 O TRP B 130 2508 2625 2636 -111 252 -354 O ATOM 966 CB TRP A 130 5.382 -2.068 37.506 1.00 17.98 C ANISOU 966 CB TRP B 130 2259 2296 2276 -85 252 -375 C ATOM 967 CG TRP A 130 5.872 -3.450 37.018 1.00 17.58 C ANISOU 967 CG TRP B 130 2184 2257 2237 -72 259 -381 C ATOM 968 CD1 TRP A 130 5.962 -3.876 35.721 1.00 16.35 C ANISOU 968 CD1 TRP B 130 2011 2121 2082 -66 282 -382 C ATOM 969 CD2 TRP A 130 6.331 -4.551 37.843 1.00 17.11 C ANISOU 969 CD2 TRP B 130 2120 2189 2192 -61 245 -384 C ATOM 970 NE1 TRP A 130 6.469 -5.179 35.684 1.00 17.84 N ANISOU 970 NE1 TRP B 130 2181 2313 2285 -52 285 -388 N ATOM 971 CE2 TRP A 130 6.692 -5.614 36.966 1.00 17.48 C ANISOU 971 CE2 TRP B 130 2142 2250 2248 -47 261 -388 C ATOM 972 CE3 TRP A 130 6.463 -4.740 39.235 1.00 17.08 C ANISOU 972 CE3 TRP B 130 2133 2166 2190 -58 219 -384 C ATOM 973 CZ2 TRP A 130 7.177 -6.862 37.437 1.00 19.55 C ANISOU 973 CZ2 TRP B 130 2394 2509 2526 -28 254 -391 C ATOM 974 CZ3 TRP A 130 6.947 -5.975 39.709 1.00 18.25 C ANISOU 974 CZ3 TRP B 130 2274 2312 2349 -38 209 -386 C ATOM 975 CH2 TRP A 130 7.309 -7.021 38.807 1.00 18.11 C ANISOU 975 CH2 TRP B 130 2229 2308 2344 -22 226 -389 C ATOM 976 N VAL A 131 3.049 -3.369 39.234 1.00 20.65 N ANISOU 976 N VAL B 131 2572 2621 2653 -114 210 -360 N ATOM 977 CA VAL A 131 2.279 -4.459 39.863 1.00 21.31 C ANISOU 977 CA VAL B 131 2629 2708 2758 -121 189 -360 C ATOM 978 C VAL A 131 0.830 -4.506 39.416 1.00 21.50 C ANISOU 978 C VAL B 131 2630 2738 2799 -146 199 -355 C ATOM 979 O VAL A 131 0.311 -5.592 39.151 1.00 22.86 O ANISOU 979 O VAL B 131 2764 2925 2996 -149 199 -358 O ATOM 980 CB VAL A 131 2.376 -4.467 41.435 1.00 20.96 C ANISOU 980 CB VAL B 131 2607 2648 2709 -121 153 -365 C ATOM 981 CG1 VAL A 131 1.594 -5.677 42.029 1.00 20.24 C ANISOU 981 CG1 VAL B 131 2482 2567 2640 -125 125 -369 C ATOM 982 CG2 VAL A 131 3.830 -4.561 41.907 1.00 21.58 C ANISOU 982 CG2 VAL B 131 2712 2716 2773 -96 149 -370 C ATOM 983 N GLU A 132 0.182 -3.341 39.317 1.00 21.51 N ANISOU 983 N GLU B 132 2656 2728 2790 -163 211 -348 N ATOM 984 CA GLU A 132 -1.221 -3.239 38.843 1.00 21.51 C ANISOU 984 CA GLU B 132 2643 2726 2803 -189 230 -341 C ATOM 985 C GLU A 132 -1.409 -3.310 37.341 1.00 22.48 C ANISOU 985 C GLU B 132 2755 2861 2926 -185 268 -333 C ATOM 986 O GLU A 132 -2.541 -3.299 36.875 1.00 22.84 O ANISOU 986 O GLU B 132 2793 2903 2983 -206 291 -327 O ATOM 987 CB GLU A 132 -1.833 -1.913 39.343 1.00 20.77 C ANISOU 987 CB GLU B 132 2588 2609 2696 -205 232 -335 C ATOM 988 CG GLU A 132 -1.852 -1.878 40.872 1.00 21.53 C ANISOU 988 CG GLU B 132 2699 2691 2791 -214 197 -344 C ATOM 989 CD GLU A 132 -2.390 -0.600 41.470 1.00 21.83 C ANISOU 989 CD GLU B 132 2776 2704 2816 -230 200 -340 C ATOM 990 OE1 GLU A 132 -2.752 -0.631 42.676 1.00 24.16 O ANISOU 990 OE1 GLU B 132 3082 2986 3112 -245 175 -349 O ATOM 991 OE2 GLU A 132 -2.448 0.422 40.741 1.00 24.03 O ANISOU 991 OE2 GLU B 132 3075 2975 3081 -224 227 -328 O ATOM 992 N SER A 133 -0.316 -3.390 36.569 1.00 21.59 N ANISOU 992 N SER B 133 2643 2761 2799 -160 278 -333 N ATOM 993 CA SER A 133 -0.389 -3.264 35.107 1.00 21.86 C ANISOU 993 CA SER B 133 2677 2807 2823 -153 314 -325 C ATOM 994 C SER A 133 -0.593 -4.625 34.429 1.00 22.69 C ANISOU 994 C SER B 133 2742 2928 2951 -154 331 -329 C ATOM 995 O SER A 133 -0.443 -5.687 35.067 1.00 22.63 O ANISOU 995 O SER B 133 2705 2926 2968 -152 312 -340 O ATOM 996 CB SER A 133 0.894 -2.580 34.549 1.00 21.02 C ANISOU 996 CB SER B 133 2592 2708 2686 -127 316 -328 C ATOM 997 OG SER A 133 1.970 -3.504 34.569 1.00 21.30 O ANISOU 997 OG SER B 133 2611 2755 2728 -112 309 -341 O ATOM 998 N ASN A 134 -0.945 -4.588 33.141 1.00 22.85 N ANISOU 998 N ASN B 134 2764 2954 2963 -153 368 -321 N ATOM 999 CA ASN A 134 -1.062 -5.803 32.340 1.00 24.42 C ANISOU 999 CA ASN B 134 2929 3168 3183 -152 393 -325 C ATOM 1000 C ASN A 134 0.239 -6.524 32.153 1.00 24.60 C ANISOU 1000 C ASN B 134 2938 3204 3203 -126 386 -336 C ATOM 1001 O ASN A 134 0.201 -7.718 31.921 1.00 24.48 O ANISOU 1001 O ASN B 134 2889 3200 3214 -124 396 -343 O ATOM 1002 CB ASN A 134 -1.690 -5.541 30.963 1.00 25.59 C ANISOU 1002 CB ASN B 134 3091 3316 3316 -155 439 -312 C ATOM 1003 CG ASN A 134 -3.165 -5.199 31.061 1.00 30.03 C ANISOU 1003 CG ASN B 134 3659 3861 3892 -185 459 -302 C ATOM 1004 OD1 ASN A 134 -3.790 -5.524 32.055 1.00 37.38 O ANISOU 1004 OD1 ASN B 134 4567 4783 4851 -207 441 -310 O ATOM 1005 ND2 ASN A 134 -3.723 -4.538 30.045 1.00 31.24 N ANISOU 1005 ND2 ASN B 134 3844 4006 4022 -185 497 -285 N ATOM 1006 N SER A 135 1.368 -5.807 32.260 1.00 22.81 N ANISOU 1006 N SER B 135 2740 2978 2948 -108 371 -340 N ATOM 1007 CA SER A 135 2.708 -6.405 32.138 1.00 23.22 C ANISOU 1007 CA SER B 135 2787 3039 2997 -85 367 -354 C ATOM 1008 C SER A 135 3.244 -7.096 33.402 1.00 23.26 C ANISOU 1008 C SER B 135 2779 3037 3021 -78 335 -363 C ATOM 1009 O SER A 135 4.297 -7.719 33.369 1.00 24.16 O ANISOU 1009 O SER B 135 2890 3153 3136 -58 336 -373 O ATOM 1010 CB SER A 135 3.714 -5.363 31.700 1.00 22.01 C ANISOU 1010 CB SER B 135 2667 2889 2807 -72 368 -359 C ATOM 1011 OG SER A 135 4.096 -4.563 32.815 1.00 23.71 O ANISOU 1011 OG SER B 135 2902 3091 3016 -74 339 -362 O ATOM 1012 N TRP A 136 2.519 -7.035 34.510 1.00 23.11 N ANISOU 1012 N TRP B 136 2755 3007 3016 -92 309 -359 N ATOM 1013 CA TRP A 136 3.009 -7.641 35.733 1.00 22.82 C ANISOU 1013 CA TRP B 136 2714 2965 2992 -81 276 -366 C ATOM 1014 C TRP A 136 3.199 -9.143 35.547 1.00 24.24 C ANISOU 1014 C TRP B 136 2855 3157 3198 -64 280 -372 C ATOM 1015 O TRP A 136 2.350 -9.810 34.983 1.00 24.17 O ANISOU 1015 O TRP B 136 2811 3160 3213 -74 296 -371 O ATOM 1016 CB TRP A 136 2.077 -7.320 36.916 1.00 22.56 C ANISOU 1016 CB TRP B 136 2683 2922 2967 -100 246 -363 C ATOM 1017 CG TRP A 136 2.633 -7.797 38.283 1.00 21.10 C ANISOU 1017 CG TRP B 136 2504 2728 2784 -86 208 -369 C ATOM 1018 CD1 TRP A 136 3.872 -7.588 38.775 1.00 20.64 C ANISOU 1018 CD1 TRP B 136 2478 2658 2708 -65 200 -372 C ATOM 1019 CD2 TRP A 136 1.922 -8.538 39.282 1.00 21.66 C ANISOU 1019 CD2 TRP B 136 2552 2803 2876 -90 175 -372 C ATOM 1020 NE1 TRP A 136 3.997 -8.173 40.025 1.00 21.03 N ANISOU 1020 NE1 TRP B 136 2529 2700 2760 -53 165 -374 N ATOM 1021 CE2 TRP A 136 2.801 -8.758 40.348 1.00 22.16 C ANISOU 1021 CE2 TRP B 136 2638 2856 2927 -67 146 -375 C ATOM 1022 CE3 TRP A 136 0.615 -9.055 39.364 1.00 25.38 C ANISOU 1022 CE3 TRP B 136 2984 3286 3375 -113 168 -376 C ATOM 1023 CZ2 TRP A 136 2.423 -9.454 41.497 1.00 23.97 C ANISOU 1023 CZ2 TRP B 136 2854 3088 3165 -61 105 -379 C ATOM 1024 CZ3 TRP A 136 0.239 -9.754 40.510 1.00 23.96 C ANISOU 1024 CZ3 TRP B 136 2784 3111 3208 -110 126 -384 C ATOM 1025 CH2 TRP A 136 1.148 -9.959 41.551 1.00 24.42 C ANISOU 1025 CH2 TRP B 136 2867 3161 3249 -83 93 -385 C ATOM 1026 N ASP A 137 4.317 -9.676 36.031 1.00 25.20 N ANISOU 1026 N ASP B 137 2984 3274 3318 -38 267 -378 N ATOM 1027 CA ASP A 137 4.570 -11.100 35.878 1.00 26.05 C ANISOU 1027 CA ASP B 137 3057 3391 3450 -16 271 -383 C ATOM 1028 C ASP A 137 4.387 -11.862 37.195 1.00 26.78 C ANISOU 1028 C ASP B 137 3133 3482 3560 -2 229 -383 C ATOM 1029 O ASP A 137 4.782 -13.020 37.288 1.00 26.69 O ANISOU 1029 O ASP B 137 3098 3477 3566 25 225 -386 O ATOM 1030 CB ASP A 137 5.978 -11.329 35.360 1.00 26.63 C ANISOU 1030 CB ASP B 137 3150 3458 3509 9 292 -389 C ATOM 1031 CG ASP A 137 7.051 -10.843 36.327 1.00 26.63 C ANISOU 1031 CG ASP B 137 3193 3438 3488 22 274 -392 C ATOM 1032 OD1 ASP A 137 6.779 -10.256 37.395 1.00 28.94 O ANISOU 1032 OD1 ASP B 137 3504 3719 3773 13 244 -388 O ATOM 1033 OD2 ASP A 137 8.208 -11.062 36.017 1.00 27.46 O ANISOU 1033 OD2 ASP B 137 3315 3534 3584 39 292 -400 O ATOM 1034 N GLY A 138 3.805 -11.214 38.203 1.00 25.48 N ANISOU 1034 N GLY B 138 2984 3311 3388 -19 198 -381 N ATOM 1035 CA GLY A 138 3.510 -11.903 39.448 1.00 26.41 C ANISOU 1035 CA GLY B 138 3088 3431 3518 -8 154 -383 C ATOM 1036 C GLY A 138 4.642 -11.804 40.474 1.00 26.41 C ANISOU 1036 C GLY B 138 3132 3410 3492 20 132 -380 C ATOM 1037 O GLY A 138 4.481 -12.277 41.589 1.00 27.43 O ANISOU 1037 O GLY B 138 3260 3539 3623 33 92 -380 O ATOM 1038 N ARG A 139 5.770 -11.181 40.117 1.00 25.13 N ANISOU 1038 N ARG B 139 3011 3230 3307 27 157 -380 N ATOM 1039 CA ARG A 139 6.892 -11.057 41.045 1.00 24.84 C ANISOU 1039 CA ARG B 139 3021 3169 3248 50 146 -379 C ATOM 1040 C ARG A 139 6.856 -9.718 41.831 1.00 23.79 C ANISOU 1040 C ARG B 139 2933 3016 3089 28 136 -378 C ATOM 1041 O ARG A 139 6.110 -8.807 41.493 1.00 23.35 O ANISOU 1041 O ARG B 139 2875 2965 3031 -2 142 -377 O ATOM 1042 CB ARG A 139 8.234 -11.190 40.311 1.00 24.46 C ANISOU 1042 CB ARG B 139 2993 3110 3192 69 183 -384 C ATOM 1043 CG ARG A 139 8.570 -12.549 39.676 1.00 27.60 C ANISOU 1043 CG ARG B 139 3358 3518 3612 98 198 -385 C ATOM 1044 CD ARG A 139 9.227 -12.290 38.304 1.00 28.29 C ANISOU 1044 CD ARG B 139 3448 3608 3695 91 245 -394 C ATOM 1045 NE ARG A 139 10.615 -12.581 38.331 1.00 29.95 N ANISOU 1045 NE ARG B 139 3690 3796 3895 115 266 -400 N ATOM 1046 CZ ARG A 139 11.541 -12.117 37.506 1.00 27.43 C ANISOU 1046 CZ ARG B 139 3391 3468 3562 107 303 -414 C ATOM 1047 NH1 ARG A 139 11.276 -11.280 36.522 1.00 24.70 N ANISOU 1047 NH1 ARG B 139 3038 3138 3208 80 321 -421 N ATOM 1048 NH2 ARG A 139 12.775 -12.528 37.709 1.00 29.92 N ANISOU 1048 NH2 ARG B 139 3737 3759 3871 130 322 -420 N ATOM 1049 N TYR A 140 7.701 -9.622 42.852 1.00 22.97 N ANISOU 1049 N TYR B 140 2874 2888 2966 46 124 -377 N ATOM 1050 CA TYR A 140 7.872 -8.439 43.658 1.00 23.29 C ANISOU 1050 CA TYR B 140 2962 2906 2982 30 120 -377 C ATOM 1051 C TYR A 140 8.498 -7.255 42.912 1.00 22.37 C ANISOU 1051 C TYR B 140 2865 2781 2855 11 157 -385 C ATOM 1052 O TYR A 140 9.334 -7.426 42.022 1.00 22.25 O ANISOU 1052 O TYR B 140 2845 2767 2841 20 187 -392 O ATOM 1053 CB TYR A 140 8.757 -8.760 44.857 1.00 24.25 C ANISOU 1053 CB TYR B 140 3130 3000 3083 57 107 -374 C ATOM 1054 CG TYR A 140 8.183 -9.779 45.817 1.00 25.75 C ANISOU 1054 CG TYR B 140 3309 3198 3275 80 61 -367 C ATOM 1055 CD1 TYR A 140 8.925 -10.903 46.179 1.00 27.90 C ANISOU 1055 CD1 TYR B 140 3591 3465 3546 123 53 -362 C ATOM 1056 CD2 TYR A 140 6.897 -9.654 46.315 1.00 26.64 C ANISOU 1056 CD2 TYR B 140 3401 3327 3393 59 26 -367 C ATOM 1057 CE1 TYR A 140 8.413 -11.860 47.039 1.00 28.85 C ANISOU 1057 CE1 TYR B 140 3699 3597 3667 150 6 -356 C ATOM 1058 CE2 TYR A 140 6.370 -10.605 47.198 1.00 28.83 C ANISOU 1058 CE2 TYR B 140 3664 3618 3672 80 -21 -365 C ATOM 1059 CZ TYR A 140 7.153 -11.697 47.558 1.00 28.95 C ANISOU 1059 CZ TYR B 140 3687 3629 3683 127 -33 -359 C ATOM 1060 OH TYR A 140 6.687 -12.660 48.407 1.00 29.54 O ANISOU 1060 OH TYR B 140 3747 3720 3757 154 -83 -358 O ATOM 1061 N GLY A 141 8.092 -6.047 43.277 1.00 21.33 N ANISOU 1061 N GLY B 141 2754 2640 2710 -13 155 -385 N ATOM 1062 CA GLY A 141 8.890 -4.862 42.916 1.00 20.14 C ANISOU 1062 CA GLY B 141 2629 2477 2547 -24 185 -395 C ATOM 1063 C GLY A 141 9.798 -4.528 44.065 1.00 20.12 C ANISOU 1063 C GLY B 141 2677 2442 2527 -17 186 -399 C ATOM 1064 O GLY A 141 9.481 -4.840 45.197 1.00 20.32 O ANISOU 1064 O GLY B 141 2722 2454 2544 -10 160 -391 O ATOM 1065 N LEU A 142 10.936 -3.895 43.784 1.00 20.90 N ANISOU 1065 N LEU B 142 2796 2526 2618 -19 218 -413 N ATOM 1066 CA LEU A 142 11.873 -3.485 44.829 1.00 21.48 C ANISOU 1066 CA LEU B 142 2921 2565 2677 -17 230 -419 C ATOM 1067 C LEU A 142 12.337 -2.063 44.572 1.00 21.11 C ANISOU 1067 C LEU B 142 2883 2511 2625 -39 256 -436 C ATOM 1068 O LEU A 142 12.887 -1.744 43.514 1.00 20.38 O ANISOU 1068 O LEU B 142 2771 2433 2539 -44 279 -451 O ATOM 1069 CB LEU A 142 13.070 -4.435 44.895 1.00 21.95 C ANISOU 1069 CB LEU B 142 3000 2606 2735 8 249 -424 C ATOM 1070 CG LEU A 142 14.153 -4.254 45.958 1.00 23.66 C ANISOU 1070 CG LEU B 142 3275 2779 2935 15 269 -429 C ATOM 1071 CD1 LEU A 142 13.576 -4.433 47.314 1.00 21.51 C ANISOU 1071 CD1 LEU B 142 3036 2490 2646 25 237 -413 C ATOM 1072 CD2 LEU A 142 15.324 -5.255 45.686 1.00 23.46 C ANISOU 1072 CD2 LEU B 142 3264 2737 2912 39 295 -434 C ATOM 1073 N VAL A 143 12.081 -1.192 45.529 1.00 20.35 N ANISOU 1073 N VAL B 143 2818 2396 2520 -51 251 -434 N ATOM 1074 CA VAL A 143 12.405 0.213 45.348 1.00 20.98 C ANISOU 1074 CA VAL B 143 2901 2471 2598 -70 274 -450 C ATOM 1075 C VAL A 143 13.538 0.544 46.310 1.00 21.47 C ANISOU 1075 C VAL B 143 3012 2494 2652 -71 301 -463 C ATOM 1076 O VAL A 143 13.477 0.176 47.497 1.00 22.23 O ANISOU 1076 O VAL B 143 3149 2562 2734 -63 290 -452 O ATOM 1077 CB VAL A 143 11.139 1.100 45.666 1.00 21.13 C ANISOU 1077 CB VAL B 143 2917 2495 2615 -85 254 -439 C ATOM 1078 CG1 VAL A 143 11.477 2.564 45.548 1.00 18.84 C ANISOU 1078 CG1 VAL B 143 2632 2201 2327 -99 277 -455 C ATOM 1079 CG2 VAL A 143 10.005 0.737 44.703 1.00 20.26 C ANISOU 1079 CG2 VAL B 143 2763 2419 2514 -85 235 -426 C ATOM 1080 N ILE A 144 14.547 1.243 45.815 1.00 21.48 N ANISOU 1080 N ILE B 144 3010 2492 2659 -82 335 -488 N ATOM 1081 CA ILE A 144 15.623 1.770 46.657 1.00 22.48 C ANISOU 1081 CA ILE B 144 3180 2580 2782 -90 370 -506 C ATOM 1082 C ILE A 144 15.609 3.283 46.603 1.00 22.54 C ANISOU 1082 C ILE B 144 3178 2591 2796 -111 385 -523 C ATOM 1083 O ILE A 144 15.526 3.867 45.520 1.00 23.27 O ANISOU 1083 O ILE B 144 3227 2716 2899 -118 385 -536 O ATOM 1084 CB ILE A 144 17.022 1.262 46.249 1.00 23.50 C ANISOU 1084 CB ILE B 144 3317 2696 2917 -88 407 -527 C ATOM 1085 CG1 ILE A 144 17.173 -0.251 46.526 1.00 23.85 C ANISOU 1085 CG1 ILE B 144 3382 2727 2953 -61 397 -509 C ATOM 1086 CG2 ILE A 144 18.122 1.976 47.079 1.00 23.88 C ANISOU 1086 CG2 ILE B 144 3408 2701 2963 -103 451 -550 C ATOM 1087 CD1 ILE A 144 16.692 -1.130 45.385 1.00 27.10 C ANISOU 1087 CD1 ILE B 144 3747 3177 3374 -48 376 -500 C ATOM 1088 N CYS A 145 15.627 3.913 47.779 1.00 22.43 N ANISOU 1088 N CYS B 145 3204 2543 2774 -119 396 -523 N ATOM 1089 CA CYS A 145 15.926 5.347 47.897 1.00 23.30 C ANISOU 1089 CA CYS B 145 3312 2648 2894 -138 422 -545 C ATOM 1090 C CYS A 145 17.284 5.464 48.573 1.00 22.98 C ANISOU 1090 C CYS B 145 3312 2566 2855 -148 469 -568 C ATOM 1091 O CYS A 145 17.464 4.907 49.637 1.00 23.09 O ANISOU 1091 O CYS B 145 3380 2542 2853 -141 476 -555 O ATOM 1092 CB CYS A 145 14.877 6.071 48.744 1.00 22.40 C ANISOU 1092 CB CYS B 145 3217 2522 2772 -143 405 -529 C ATOM 1093 SG CYS A 145 13.239 5.701 48.277 1.00 27.26 S ANISOU 1093 SG CYS B 145 3804 3172 3383 -134 355 -498 S ATOM 1094 N THR A 146 18.229 6.187 47.979 1.00 23.73 N ANISOU 1094 N THR B 146 3382 2667 2969 -164 503 -603 N ATOM 1095 CA THR A 146 19.588 6.252 48.577 1.00 24.07 C ANISOU 1095 CA THR B 146 3462 2667 3016 -178 557 -630 C ATOM 1096 C THR A 146 20.173 7.613 48.304 1.00 24.50 C ANISOU 1096 C THR B 146 3487 2729 3094 -203 589 -669 C ATOM 1097 O THR A 146 20.021 8.165 47.207 1.00 22.66 O ANISOU 1097 O THR B 146 3194 2542 2875 -205 574 -685 O ATOM 1098 CB THR A 146 20.555 5.110 48.067 1.00 25.11 C ANISOU 1098 CB THR B 146 3600 2793 3149 -172 575 -639 C ATOM 1099 OG1 THR A 146 21.802 5.132 48.804 1.00 27.71 O ANISOU 1099 OG1 THR B 146 3977 3070 3480 -186 632 -661 O ATOM 1100 CG2 THR A 146 20.834 5.247 46.579 1.00 23.80 C ANISOU 1100 CG2 THR B 146 3370 2674 3000 -179 571 -664 C ATOM 1101 N ASP A 147 20.791 8.211 49.324 1.00 25.22 N ANISOU 1101 N ASP B 147 3617 2775 3189 -219 633 -684 N ATOM 1102 CA ASP A 147 21.381 9.535 49.130 1.00 26.45 C ANISOU 1102 CA ASP B 147 3740 2938 3372 -243 667 -726 C ATOM 1103 C ASP A 147 22.416 9.798 50.207 1.00 27.36 C ANISOU 1103 C ASP B 147 3909 2995 3493 -263 730 -748 C ATOM 1104 O ASP A 147 22.338 9.258 51.295 1.00 26.07 O ANISOU 1104 O ASP B 147 3813 2786 3306 -255 740 -723 O ATOM 1105 CB ASP A 147 20.319 10.660 49.141 1.00 25.89 C ANISOU 1105 CB ASP B 147 3640 2891 3305 -239 640 -716 C ATOM 1106 CG ASP A 147 19.753 10.971 47.746 1.00 26.87 C ANISOU 1106 CG ASP B 147 3693 3079 3437 -228 598 -719 C ATOM 1107 OD1 ASP A 147 20.520 11.279 46.804 1.00 25.77 O ANISOU 1107 OD1 ASP B 147 3507 2969 3315 -237 609 -755 O ATOM 1108 OD2 ASP A 147 18.514 10.892 47.580 1.00 25.98 O ANISOU 1108 OD2 ASP B 147 3574 2988 3311 -209 555 -685 O ATOM 1109 N SER A 148 23.413 10.596 49.847 1.00 29.75 N ANISOU 1109 N SER B 148 4178 3300 3825 -290 773 -796 N ATOM 1110 CA SER A 148 24.410 11.070 50.789 1.00 32.96 C ANISOU 1110 CA SER B 148 4626 3652 4244 -316 843 -825 C ATOM 1111 C SER A 148 24.922 12.411 50.289 1.00 35.13 C ANISOU 1111 C SER B 148 4837 3954 4558 -342 868 -876 C ATOM 1112 O SER A 148 25.364 12.545 49.141 1.00 35.56 O ANISOU 1112 O SER B 148 4828 4052 4632 -350 859 -909 O ATOM 1113 CB SER A 148 25.589 10.102 50.871 1.00 33.02 C ANISOU 1113 CB SER B 148 4676 3622 4250 -326 888 -839 C ATOM 1114 OG SER A 148 26.631 10.649 51.676 1.00 35.02 O ANISOU 1114 OG SER B 148 4965 3822 4519 -356 963 -872 O ATOM 1115 N ALA A 149 24.877 13.408 51.154 1.00 37.53 N ANISOU 1115 N ALA B 149 5155 4231 4873 -354 899 -886 N ATOM 1116 CA ALA A 149 25.547 14.668 50.863 1.00 39.32 C ANISOU 1116 CA ALA B 149 5325 4474 5141 -381 936 -941 C ATOM 1117 C ALA A 149 25.641 15.428 52.159 1.00 40.63 C ANISOU 1117 C ALA B 149 5536 4587 5314 -395 987 -945 C ATOM 1118 O ALA A 149 24.636 15.655 52.832 1.00 39.42 O ANISOU 1118 O ALA B 149 5413 4423 5140 -376 964 -908 O ATOM 1119 CB ALA A 149 24.777 15.492 49.795 1.00 39.48 C ANISOU 1119 CB ALA B 149 5259 4567 5174 -364 879 -946 C ATOM 1120 N VAL A 150 26.873 15.766 52.534 1.00 42.64 N ANISOU 1120 N VAL B 150 5801 4805 5596 -430 1062 -992 N ATOM 1121 CA VAL A 150 27.111 16.780 53.571 1.00 43.97 C ANISOU 1121 CA VAL B 150 5993 4931 5783 -450 1121 -1011 C ATOM 1122 C VAL A 150 28.121 17.806 52.985 1.00 45.65 C ANISOU 1122 C VAL B 150 6126 5167 6050 -486 1164 -1083 C ATOM 1123 O VAL A 150 29.247 17.442 52.623 1.00 44.63 O ANISOU 1123 O VAL B 150 5989 5028 5940 -514 1205 -1123 O ATOM 1124 CB VAL A 150 27.584 16.159 54.949 1.00 44.24 C ANISOU 1124 CB VAL B 150 6139 4879 5791 -460 1182 -993 C ATOM 1125 CG1 VAL A 150 27.583 17.222 56.059 1.00 43.57 C ANISOU 1125 CG1 VAL B 150 6084 4752 5719 -475 1237 -1005 C ATOM 1126 CG2 VAL A 150 26.728 14.924 55.352 1.00 43.82 C ANISOU 1126 CG2 VAL B 150 6156 4812 5683 -423 1131 -927 C ATOM 1127 N TYR A 151 27.690 19.064 52.842 1.00 47.27 N ANISOU 1127 N TYR B 151 6271 5407 6284 -482 1153 -1102 N ATOM 1128 CA TYR A 151 28.585 20.118 52.361 1.00 49.23 C ANISOU 1128 CA TYR B 151 6437 5681 6586 -513 1191 -1172 C ATOM 1129 C TYR A 151 29.716 20.308 53.369 1.00 49.70 C ANISOU 1129 C TYR B 151 6545 5669 6669 -557 1292 -1210 C ATOM 1130 O TYR A 151 29.462 20.488 54.558 1.00 49.49 O ANISOU 1130 O TYR B 151 6587 5585 6630 -557 1330 -1186 O ATOM 1131 CB TYR A 151 27.817 21.424 52.092 1.00 50.41 C ANISOU 1131 CB TYR B 151 6516 5879 6758 -493 1157 -1179 C ATOM 1132 CG TYR A 151 26.715 21.258 51.053 1.00 52.23 C ANISOU 1132 CG TYR B 151 6704 6177 6965 -449 1063 -1142 C ATOM 1133 CD1 TYR A 151 26.952 20.586 49.830 1.00 55.08 C ANISOU 1133 CD1 TYR B 151 7023 6587 7317 -445 1020 -1150 C ATOM 1134 CD2 TYR A 151 25.438 21.759 51.287 1.00 54.08 C ANISOU 1134 CD2 TYR B 151 6943 6423 7183 -414 1022 -1098 C ATOM 1135 CE1 TYR A 151 25.917 20.416 48.873 1.00 53.69 C ANISOU 1135 CE1 TYR B 151 6813 6469 7116 -404 938 -1114 C ATOM 1136 CE2 TYR A 151 24.405 21.611 50.342 1.00 54.06 C ANISOU 1136 CE2 TYR B 151 6907 6477 7158 -375 942 -1063 C ATOM 1137 CZ TYR A 151 24.649 20.945 49.147 1.00 53.34 C ANISOU 1137 CZ TYR B 151 6776 6433 7057 -370 901 -1071 C ATOM 1138 OH TYR A 151 23.605 20.815 48.243 1.00 54.32 O ANISOU 1138 OH TYR B 151 6873 6608 7157 -332 828 -1035 O ATOM 1139 N ALA A 152 30.956 20.215 52.889 1.00 50.17 N ANISOU 1139 N ALA B 152 6573 5729 6762 -595 1337 -1268 N ATOM 1140 CA ALA A 152 32.152 20.272 53.739 1.00 50.49 C ANISOU 1140 CA ALA B 152 6661 5697 6825 -642 1441 -1308 C ATOM 1141 C ALA A 152 32.307 21.599 54.478 1.00 50.85 C ANISOU 1141 C ALA B 152 6686 5724 6912 -663 1499 -1342 C ATOM 1142 O ALA A 152 32.858 21.637 55.583 1.00 51.08 O ANISOU 1142 O ALA B 152 6787 5677 6944 -689 1583 -1349 O ATOM 1143 CB ALA A 152 33.413 19.962 52.913 1.00 50.49 C ANISOU 1143 CB ALA B 152 6619 5710 6856 -681 1474 -1369 C ATOM 1144 N GLU A 153 31.831 22.680 53.862 1.00 51.30 N ANISOU 1144 N GLU B 153 6646 5847 6999 -649 1456 -1364 N ATOM 1145 CA GLU A 153 31.853 24.010 54.481 1.00 52.88 C ANISOU 1145 CA GLU B 153 6815 6038 7242 -662 1503 -1396 C ATOM 1146 C GLU A 153 30.527 24.753 54.272 1.00 52.41 C ANISOU 1146 C GLU B 153 6713 6028 7173 -614 1430 -1360 C ATOM 1147 O GLU A 153 29.604 24.234 53.620 1.00 51.54 O ANISOU 1147 O GLU B 153 6598 5960 7025 -573 1345 -1312 O ATOM 1148 CB GLU A 153 33.033 24.838 53.943 1.00 53.96 C ANISOU 1148 CB GLU B 153 6855 6201 7446 -708 1553 -1487 C ATOM 1149 CG GLU A 153 34.412 24.337 54.415 1.00 57.70 C ANISOU 1149 CG GLU B 153 7378 6607 7938 -765 1652 -1530 C ATOM 1150 CD GLU A 153 35.542 24.595 53.411 1.00 62.51 C ANISOU 1150 CD GLU B 153 7891 7260 8599 -808 1670 -1615 C ATOM 1151 OE1 GLU A 153 35.794 25.785 53.085 1.00 63.82 O ANISOU 1151 OE1 GLU B 153 7956 7472 8821 -822 1678 -1675 O ATOM 1152 OE2 GLU A 153 36.190 23.603 52.969 1.00 63.75 O ANISOU 1152 OE2 GLU B 153 8074 7406 8741 -826 1678 -1623 O ATOM 1153 N GLY A 154 30.434 25.963 54.824 1.00 52.60 N ANISOU 1153 N GLY B 154 6709 6044 7233 -618 1468 -1383 N ATOM 1154 CA GLY A 154 29.282 26.833 54.581 1.00 52.23 C ANISOU 1154 CA GLY B 154 6613 6044 7187 -573 1408 -1359 C ATOM 1155 C GLY A 154 28.120 26.521 55.508 1.00 51.73 C ANISOU 1155 C GLY B 154 6645 5937 7073 -543 1391 -1285 C ATOM 1156 O GLY A 154 28.184 25.550 56.265 1.00 51.69 O ANISOU 1156 O GLY B 154 6740 5872 7027 -552 1415 -1251 O ATOM 1157 N PRO A 155 27.035 27.324 55.427 1.00 51.40 N ANISOU 1157 N PRO B 155 6573 5926 7031 -504 1347 -1260 N ATOM 1158 CA PRO A 155 25.880 27.323 56.337 1.00 50.77 C ANISOU 1158 CA PRO B 155 6571 5807 6912 -477 1336 -1200 C ATOM 1159 C PRO A 155 24.949 26.117 56.178 1.00 49.71 C ANISOU 1159 C PRO B 155 6497 5675 6714 -449 1266 -1133 C ATOM 1160 O PRO A 155 24.051 25.899 57.015 1.00 50.23 O ANISOU 1160 O PRO B 155 6640 5703 6741 -433 1258 -1084 O ATOM 1161 CB PRO A 155 25.107 28.603 55.938 1.00 51.15 C ANISOU 1161 CB PRO B 155 6543 5904 6989 -443 1304 -1205 C ATOM 1162 CG PRO A 155 25.986 29.342 54.979 1.00 51.63 C ANISOU 1162 CG PRO B 155 6487 6023 7106 -454 1308 -1272 C ATOM 1163 CD PRO A 155 26.863 28.308 54.346 1.00 51.76 C ANISOU 1163 CD PRO B 155 6500 6052 7114 -480 1301 -1292 C ATOM 1164 N ALA A 156 25.151 25.363 55.109 1.00 48.23 N ANISOU 1164 N ALA B 156 6274 5534 6517 -444 1215 -1133 N ATOM 1165 CA ALA A 156 24.330 24.204 54.813 1.00 46.74 C ANISOU 1165 CA ALA B 156 6129 5355 6275 -418 1148 -1075 C ATOM 1166 C ALA A 156 24.893 22.888 55.378 1.00 45.07 C ANISOU 1166 C ALA B 156 6004 5092 6030 -439 1174 -1059 C ATOM 1167 O ALA A 156 24.204 21.873 55.343 1.00 44.95 O ANISOU 1167 O ALA B 156 6034 5075 5969 -418 1125 -1009 O ATOM 1168 CB ALA A 156 24.107 24.099 53.291 1.00 46.84 C ANISOU 1168 CB ALA B 156 6057 5448 6291 -395 1075 -1079 C ATOM 1169 N ARG A 157 26.126 22.915 55.889 1.00 43.39 N ANISOU 1169 N ARG B 157 5811 4834 5840 -478 1253 -1101 N ATOM 1170 CA ARG A 157 26.768 21.749 56.503 1.00 42.01 C ANISOU 1170 CA ARG B 157 5725 4602 5636 -496 1290 -1088 C ATOM 1171 C ARG A 157 25.950 21.017 57.605 1.00 40.61 C ANISOU 1171 C ARG B 157 5656 4373 5400 -476 1278 -1025 C ATOM 1172 O ARG A 157 25.936 19.764 57.634 1.00 40.00 O ANISOU 1172 O ARG B 157 5634 4282 5283 -465 1254 -993 O ATOM 1173 CB ARG A 157 28.177 22.088 57.019 1.00 42.60 C ANISOU 1173 CB ARG B 157 5811 4628 5747 -543 1390 -1144 C ATOM 1174 CG ARG A 157 28.825 20.926 57.804 1.00 43.35 C ANISOU 1174 CG ARG B 157 6014 4652 5806 -557 1437 -1126 C ATOM 1175 CD ARG A 157 30.331 21.105 58.030 1.00 44.02 C ANISOU 1175 CD ARG B 157 6103 4693 5930 -607 1535 -1186 C ATOM 1176 NE ARG A 157 30.648 22.101 59.057 1.00 43.89 N ANISOU 1176 NE ARG B 157 6112 4626 5939 -632 1618 -1212 N ATOM 1177 CZ ARG A 157 31.775 22.810 59.071 1.00 45.12 C ANISOU 1177 CZ ARG B 157 6228 4765 6150 -678 1700 -1280 C ATOM 1178 NH1 ARG A 157 32.681 22.628 58.110 1.00 45.02 N ANISOU 1178 NH1 ARG B 157 6151 4784 6172 -704 1707 -1329 N ATOM 1179 NH2 ARG A 157 32.006 23.697 60.037 1.00 44.31 N ANISOU 1179 NH2 ARG B 157 6152 4614 6071 -699 1778 -1302 N ATOM 1180 N PRO A 158 25.318 21.771 58.539 1.00 38.69 N ANISOU 1180 N PRO B 158 5449 4101 5152 -470 1298 -1012 N ATOM 1181 CA PRO A 158 24.501 21.073 59.535 1.00 37.57 C ANISOU 1181 CA PRO B 158 5408 3917 4952 -451 1279 -956 C ATOM 1182 C PRO A 158 23.261 20.347 59.004 1.00 36.08 C ANISOU 1182 C PRO B 158 5213 3770 4725 -415 1183 -904 C ATOM 1183 O PRO A 158 22.725 19.497 59.709 1.00 35.13 O ANISOU 1183 O PRO B 158 5172 3621 4556 -400 1162 -862 O ATOM 1184 CB PRO A 158 24.110 22.197 60.524 1.00 37.55 C ANISOU 1184 CB PRO B 158 5431 3878 4957 -456 1323 -960 C ATOM 1185 CG PRO A 158 25.146 23.245 60.294 1.00 37.98 C ANISOU 1185 CG PRO B 158 5420 3934 5075 -487 1391 -1024 C ATOM 1186 CD PRO A 158 25.379 23.215 58.836 1.00 39.15 C ANISOU 1186 CD PRO B 158 5466 4156 5254 -482 1343 -1047 C ATOM 1187 N THR A 159 22.819 20.669 57.783 1.00 35.43 N ANISOU 1187 N THR B 159 5039 3757 4666 -399 1128 -910 N ATOM 1188 CA THR A 159 21.659 20.029 57.185 1.00 34.52 C ANISOU 1188 CA THR B 159 4912 3683 4519 -368 1043 -865 C ATOM 1189 C THR A 159 22.030 18.856 56.274 1.00 33.31 C ANISOU 1189 C THR B 159 4741 3560 4356 -363 1007 -859 C ATOM 1190 O THR A 159 21.326 18.633 55.295 1.00 32.95 O ANISOU 1190 O THR B 159 4646 3568 4306 -341 943 -842 O ATOM 1191 CB THR A 159 20.851 21.000 56.285 1.00 35.27 C ANISOU 1191 CB THR B 159 4924 3837 4640 -347 1000 -868 C ATOM 1192 OG1 THR A 159 21.703 21.447 55.221 1.00 36.31 O ANISOU 1192 OG1 THR B 159 4969 4013 4813 -357 1007 -913 O ATOM 1193 CG2 THR A 159 20.320 22.215 57.082 1.00 35.37 C ANISOU 1193 CG2 THR B 159 4948 3825 4665 -346 1030 -870 C ATOM 1194 N GLY A 160 23.112 18.129 56.571 1.00 31.03 N ANISOU 1194 N GLY B 160 4492 3235 4062 -381 1050 -874 N ATOM 1195 CA GLY A 160 23.501 16.959 55.778 1.00 29.15 C ANISOU 1195 CA GLY B 160 4245 3019 3813 -376 1021 -868 C ATOM 1196 C GLY A 160 22.910 15.685 56.347 1.00 27.92 C ANISOU 1196 C GLY B 160 4165 2839 3606 -354 986 -816 C ATOM 1197 O GLY A 160 22.193 15.727 57.376 1.00 28.05 O ANISOU 1197 O GLY B 160 4243 2823 3593 -344 982 -786 O ATOM 1198 N GLY A 161 23.201 14.553 55.698 1.00 25.85 N ANISOU 1198 N GLY B 161 3898 2592 3331 -344 961 -806 N ATOM 1199 CA GLY A 161 22.812 13.227 56.191 1.00 23.94 C ANISOU 1199 CA GLY B 161 3724 2329 3044 -321 930 -762 C ATOM 1200 C GLY A 161 23.022 12.175 55.114 1.00 24.48 C ANISOU 1200 C GLY B 161 3757 2432 3111 -309 895 -757 C ATOM 1201 O GLY A 161 23.453 12.505 54.008 1.00 23.62 O ANISOU 1201 O GLY B 161 3576 2364 3034 -320 894 -788 O ATOM 1202 N ALA A 162 22.703 10.919 55.433 1.00 24.07 N ANISOU 1202 N ALA B 162 3755 2368 3022 -285 864 -719 N ATOM 1203 CA ALA A 162 22.892 9.801 54.506 1.00 25.03 C ANISOU 1203 CA ALA B 162 3852 2518 3142 -270 834 -711 C ATOM 1204 C ALA A 162 22.025 8.649 54.934 1.00 24.85 C ANISOU 1204 C ALA B 162 3870 2493 3078 -237 781 -662 C ATOM 1205 O ALA A 162 21.936 8.361 56.123 1.00 24.54 O ANISOU 1205 O ALA B 162 3907 2410 3009 -227 791 -641 O ATOM 1206 CB ALA A 162 24.364 9.344 54.487 1.00 24.11 C ANISOU 1206 CB ALA B 162 3763 2363 3034 -285 896 -739 C ATOM 1207 N ALA A 163 21.403 7.984 53.962 1.00 24.06 N ANISOU 1207 N ALA B 163 3721 2443 2979 -219 725 -646 N ATOM 1208 CA ALA A 163 20.757 6.693 54.215 1.00 23.86 C ANISOU 1208 CA ALA B 163 3725 2419 2921 -188 677 -606 C ATOM 1209 C ALA A 163 20.354 6.042 52.926 1.00 23.48 C ANISOU 1209 C ALA B 163 3612 2425 2884 -176 633 -599 C ATOM 1210 O ALA A 163 20.327 6.698 51.887 1.00 23.71 O ANISOU 1210 O ALA B 163 3576 2493 2940 -189 630 -621 O ATOM 1211 CB ALA A 163 19.535 6.841 55.099 1.00 23.83 C ANISOU 1211 CB ALA B 163 3750 2412 2891 -177 638 -576 C ATOM 1212 N ALA A 164 20.066 4.748 53.014 1.00 23.73 N ANISOU 1212 N ALA B 164 3664 2458 2895 -148 600 -571 N ATOM 1213 CA ALA A 164 19.379 3.984 51.969 1.00 23.64 C ANISOU 1213 CA ALA B 164 3598 2496 2889 -131 550 -556 C ATOM 1214 C ALA A 164 18.206 3.266 52.617 1.00 23.68 C ANISOU 1214 C ALA B 164 3623 2507 2868 -108 496 -519 C ATOM 1215 O ALA A 164 18.337 2.755 53.729 1.00 23.74 O ANISOU 1215 O ALA B 164 3695 2477 2848 -92 498 -502 O ATOM 1216 CB ALA A 164 20.302 2.979 51.336 1.00 23.14 C ANISOU 1216 CB ALA B 164 3532 2431 2831 -120 568 -563 C ATOM 1217 N ILE A 165 17.059 3.277 51.930 1.00 23.61 N ANISOU 1217 N ILE B 165 3560 2544 2867 -106 449 -507 N ATOM 1218 CA ILE A 165 15.879 2.504 52.310 1.00 23.29 C ANISOU 1218 CA ILE B 165 3523 2519 2809 -87 395 -477 C ATOM 1219 C ILE A 165 15.525 1.546 51.149 1.00 23.54 C ANISOU 1219 C ILE B 165 3498 2593 2854 -73 365 -469 C ATOM 1220 O ILE A 165 15.620 1.916 49.986 1.00 22.36 O ANISOU 1220 O ILE B 165 3298 2473 2726 -85 374 -483 O ATOM 1221 CB ILE A 165 14.700 3.440 52.641 1.00 24.53 C ANISOU 1221 CB ILE B 165 3671 2687 2964 -103 372 -471 C ATOM 1222 CG1 ILE A 165 14.975 4.092 54.013 1.00 26.28 C ANISOU 1222 CG1 ILE B 165 3961 2861 3166 -111 398 -474 C ATOM 1223 CG2 ILE A 165 13.322 2.677 52.648 1.00 21.14 C ANISOU 1223 CG2 ILE B 165 3220 2285 2526 -91 314 -447 C ATOM 1224 CD1 ILE A 165 14.231 5.310 54.242 1.00 27.28 C ANISOU 1224 CD1 ILE B 165 4080 2988 3296 -131 399 -479 C ATOM 1225 N ALA A 166 15.161 0.310 51.472 1.00 24.29 N ANISOU 1225 N ALA B 166 3604 2691 2936 -47 332 -447 N ATOM 1226 CA ALA A 166 14.674 -0.627 50.451 1.00 24.36 C ANISOU 1226 CA ALA B 166 3557 2740 2958 -34 303 -439 C ATOM 1227 C ALA A 166 13.242 -1.007 50.788 1.00 23.90 C ANISOU 1227 C ALA B 166 3482 2705 2893 -29 250 -419 C ATOM 1228 O ALA A 166 12.915 -1.235 51.957 1.00 25.02 O ANISOU 1228 O ALA B 166 3666 2828 3013 -20 228 -408 O ATOM 1229 CB ALA A 166 15.554 -1.863 50.358 1.00 24.08 C ANISOU 1229 CB ALA B 166 3538 2693 2920 -5 313 -435 C ATOM 1230 N MET A 167 12.385 -1.040 49.769 1.00 23.18 N ANISOU 1230 N MET B 167 3332 2654 2822 -38 231 -417 N ATOM 1231 CA MET A 167 10.945 -1.338 49.964 1.00 22.87 C ANISOU 1231 CA MET B 167 3270 2638 2783 -41 185 -403 C ATOM 1232 C MET A 167 10.539 -2.386 48.952 1.00 21.89 C ANISOU 1232 C MET B 167 3091 2549 2676 -29 168 -397 C ATOM 1233 O MET A 167 10.777 -2.222 47.768 1.00 19.86 O ANISOU 1233 O MET B 167 2799 2311 2436 -35 188 -405 O ATOM 1234 CB MET A 167 10.065 -0.085 49.802 1.00 21.90 C ANISOU 1234 CB MET B 167 3134 2522 2665 -69 186 -407 C ATOM 1235 CG MET A 167 10.275 0.950 50.888 1.00 22.56 C ANISOU 1235 CG MET B 167 3269 2570 2731 -82 202 -412 C ATOM 1236 SD MET A 167 9.364 2.475 50.597 1.00 23.28 S ANISOU 1236 SD MET B 167 3345 2668 2832 -110 211 -416 S ATOM 1237 CE MET A 167 10.442 3.392 49.482 1.00 21.94 C ANISOU 1237 CE MET B 167 3151 2506 2681 -115 255 -435 C ATOM 1238 N LEU A 168 9.928 -3.456 49.445 1.00 21.75 N ANISOU 1238 N LEU B 168 3067 2542 2656 -11 129 -385 N ATOM 1239 CA LEU A 168 9.384 -4.532 48.612 1.00 21.46 C ANISOU 1239 CA LEU B 168 2975 2539 2640 0 110 -380 C ATOM 1240 C LEU A 168 7.910 -4.227 48.359 1.00 21.22 C ANISOU 1240 C LEU B 168 2908 2534 2622 -25 87 -378 C ATOM 1241 O LEU A 168 7.167 -3.910 49.304 1.00 20.07 O ANISOU 1241 O LEU B 168 2781 2381 2464 -37 63 -377 O ATOM 1242 CB LEU A 168 9.503 -5.870 49.355 1.00 21.29 C ANISOU 1242 CB LEU B 168 2963 2516 2609 35 79 -371 C ATOM 1243 CG LEU A 168 9.359 -7.138 48.497 1.00 23.08 C ANISOU 1243 CG LEU B 168 3136 2772 2859 56 69 -368 C ATOM 1244 CD1 LEU A 168 10.583 -7.382 47.589 1.00 20.43 C ANISOU 1244 CD1 LEU B 168 2801 2429 2532 70 112 -373 C ATOM 1245 CD2 LEU A 168 9.072 -8.357 49.435 1.00 23.05 C ANISOU 1245 CD2 LEU B 168 3135 2775 2847 91 23 -358 C ATOM 1246 N ILE A 169 7.495 -4.355 47.097 1.00 20.63 N ANISOU 1246 N ILE B 169 2782 2486 2570 -34 98 -379 N ATOM 1247 CA ILE A 169 6.201 -3.892 46.624 1.00 20.35 C ANISOU 1247 CA ILE B 169 2715 2469 2547 -61 92 -378 C ATOM 1248 C ILE A 169 5.449 -5.098 46.077 1.00 21.83 C ANISOU 1248 C ILE B 169 2850 2687 2757 -56 74 -375 C ATOM 1249 O ILE A 169 6.010 -5.913 45.343 1.00 21.75 O ANISOU 1249 O ILE B 169 2816 2689 2759 -36 85 -375 O ATOM 1250 CB ILE A 169 6.364 -2.795 45.496 1.00 19.99 C ANISOU 1250 CB ILE B 169 2661 2428 2506 -77 128 -381 C ATOM 1251 CG1 ILE A 169 7.286 -1.624 45.962 1.00 19.69 C ANISOU 1251 CG1 ILE B 169 2668 2363 2451 -80 150 -389 C ATOM 1252 CG2 ILE A 169 5.003 -2.291 44.973 1.00 20.39 C ANISOU 1252 CG2 ILE B 169 2686 2493 2567 -101 126 -376 C ATOM 1253 CD1 ILE A 169 6.964 -1.010 47.348 1.00 19.15 C ANISOU 1253 CD1 ILE B 169 2642 2268 2365 -90 136 -388 C ATOM 1254 N GLY A 170 4.186 -5.237 46.449 1.00 22.51 N ANISOU 1254 N GLY B 170 2917 2784 2852 -74 47 -375 N ATOM 1255 CA GLY A 170 3.403 -6.362 45.955 1.00 23.58 C ANISOU 1255 CA GLY B 170 2996 2948 3013 -73 33 -376 C ATOM 1256 C GLY A 170 1.959 -6.258 46.434 1.00 23.94 C ANISOU 1256 C GLY B 170 3025 3001 3068 -103 9 -381 C ATOM 1257 O GLY A 170 1.648 -5.410 47.236 1.00 24.20 O ANISOU 1257 O GLY B 170 3095 3016 3085 -120 0 -382 O ATOM 1258 N PRO A 171 1.096 -7.170 45.968 1.00 25.05 N ANISOU 1258 N PRO B 171 3112 3169 3238 -110 -1 -386 N ATOM 1259 CA PRO A 171 -0.323 -7.205 46.297 1.00 25.43 C ANISOU 1259 CA PRO B 171 3134 3226 3301 -143 -19 -396 C ATOM 1260 C PRO A 171 -0.509 -7.697 47.729 1.00 27.14 C ANISOU 1260 C PRO B 171 3362 3444 3505 -136 -72 -405 C ATOM 1261 O PRO A 171 0.437 -8.227 48.345 1.00 26.72 O ANISOU 1261 O PRO B 171 3329 3388 3434 -99 -93 -401 O ATOM 1262 CB PRO A 171 -0.890 -8.196 45.281 1.00 25.46 C ANISOU 1262 CB PRO B 171 3073 3259 3342 -147 -7 -400 C ATOM 1263 CG PRO A 171 0.228 -9.125 45.016 1.00 26.51 C ANISOU 1263 CG PRO B 171 3195 3402 3477 -105 -9 -396 C ATOM 1264 CD PRO A 171 1.502 -8.318 45.130 1.00 24.22 C ANISOU 1264 CD PRO B 171 2963 3086 3155 -86 8 -385 C ATOM 1265 N ASP A 172 -1.692 -7.450 48.284 1.00 28.25 N ANISOU 1265 N ASP B 172 3496 3586 3650 -170 -90 -418 N ATOM 1266 CA ASP A 172 -2.031 -7.960 49.619 1.00 29.30 C ANISOU 1266 CA ASP B 172 3635 3728 3771 -167 -145 -431 C ATOM 1267 C ASP A 172 -1.099 -7.424 50.714 1.00 28.67 C ANISOU 1267 C ASP B 172 3627 3621 3647 -144 -160 -423 C ATOM 1268 O ASP A 172 -0.546 -8.191 51.508 1.00 30.15 O ANISOU 1268 O ASP B 172 3825 3814 3816 -109 -198 -423 O ATOM 1269 CB ASP A 172 -2.032 -9.501 49.558 1.00 29.87 C ANISOU 1269 CB ASP B 172 3647 3835 3866 -139 -178 -440 C ATOM 1270 CG ASP A 172 -2.908 -10.027 48.425 1.00 32.54 C ANISOU 1270 CG ASP B 172 3915 4199 4251 -163 -155 -449 C ATOM 1271 OD1 ASP A 172 -4.061 -9.545 48.285 1.00 33.50 O ANISOU 1271 OD1 ASP B 172 4023 4318 4388 -210 -142 -460 O ATOM 1272 OD2 ASP A 172 -2.433 -10.894 47.658 1.00 34.72 O ANISOU 1272 OD2 ASP B 172 4153 4492 4548 -137 -143 -444 O ATOM 1273 N ALA A 173 -0.925 -6.102 50.759 1.00 26.90 N ANISOU 1273 N ALA B 173 3452 3364 3404 -162 -129 -416 N ATOM 1274 CA ALA A 173 0.147 -5.502 51.551 1.00 25.27 C ANISOU 1274 CA ALA B 173 3313 3127 3160 -140 -126 -407 C ATOM 1275 C ALA A 173 -0.413 -5.022 52.877 1.00 24.38 C ANISOU 1275 C ALA B 173 3245 3000 3021 -158 -154 -417 C ATOM 1276 O ALA A 173 -1.611 -4.820 52.984 1.00 24.78 O ANISOU 1276 O ALA B 173 3277 3057 3083 -194 -164 -430 O ATOM 1277 CB ALA A 173 0.796 -4.327 50.781 1.00 23.75 C ANISOU 1277 CB ALA B 173 3147 2912 2966 -146 -72 -396 C ATOM 1278 N PRO A 174 0.446 -4.862 53.897 1.00 23.77 N ANISOU 1278 N PRO B 174 3227 2898 2905 -134 -166 -412 N ATOM 1279 CA PRO A 174 0.005 -4.192 55.129 1.00 23.58 C ANISOU 1279 CA PRO B 174 3256 2853 2850 -152 -184 -421 C ATOM 1280 C PRO A 174 -0.062 -2.682 54.993 1.00 23.58 C ANISOU 1280 C PRO B 174 3294 2820 2847 -181 -137 -418 C ATOM 1281 O PRO A 174 -0.654 -2.007 55.842 1.00 23.82 O ANISOU 1281 O PRO B 174 3361 2831 2857 -204 -144 -427 O ATOM 1282 CB PRO A 174 1.098 -4.561 56.130 1.00 22.80 C ANISOU 1282 CB PRO B 174 3214 2738 2712 -111 -202 -413 C ATOM 1283 CG PRO A 174 2.352 -4.716 55.261 1.00 23.35 C ANISOU 1283 CG PRO B 174 3279 2802 2793 -82 -164 -398 C ATOM 1284 CD PRO A 174 1.831 -5.359 53.997 1.00 23.11 C ANISOU 1284 CD PRO B 174 3168 2806 2805 -88 -161 -400 C ATOM 1285 N ILE A 175 0.575 -2.166 53.946 1.00 22.77 N ANISOU 1285 N ILE B 175 3180 2711 2760 -176 -92 -407 N ATOM 1286 CA ILE A 175 0.636 -0.738 53.688 1.00 23.41 C ANISOU 1286 CA ILE B 175 3289 2765 2840 -195 -48 -404 C ATOM 1287 C ILE A 175 0.071 -0.523 52.278 1.00 22.56 C ANISOU 1287 C ILE B 175 3130 2675 2767 -211 -21 -400 C ATOM 1288 O ILE A 175 0.755 -0.789 51.289 1.00 22.82 O ANISOU 1288 O ILE B 175 3136 2721 2814 -193 -2 -392 O ATOM 1289 CB ILE A 175 2.097 -0.228 53.801 1.00 23.30 C ANISOU 1289 CB ILE B 175 3318 2727 2810 -171 -17 -396 C ATOM 1290 CG1 ILE A 175 2.651 -0.448 55.226 1.00 23.50 C ANISOU 1290 CG1 ILE B 175 3403 2729 2797 -154 -38 -398 C ATOM 1291 CG2 ILE A 175 2.179 1.236 53.369 1.00 23.99 C ANISOU 1291 CG2 ILE B 175 3420 2793 2902 -188 28 -395 C ATOM 1292 CD1 ILE A 175 4.156 -0.662 55.332 1.00 22.48 C ANISOU 1292 CD1 ILE B 175 3304 2583 2653 -121 -19 -391 C ATOM 1293 N VAL A 176 -1.170 -0.063 52.182 1.00 22.09 N ANISOU 1293 N VAL B 176 3061 2615 2720 -244 -17 -406 N ATOM 1294 CA VAL A 176 -1.890 -0.099 50.908 1.00 22.39 C ANISOU 1294 CA VAL B 176 3049 2670 2788 -259 4 -402 C ATOM 1295 C VAL A 176 -2.077 1.309 50.385 1.00 23.23 C ANISOU 1295 C VAL B 176 3177 2754 2895 -272 47 -393 C ATOM 1296 O VAL A 176 -2.482 2.223 51.106 1.00 22.62 O ANISOU 1296 O VAL B 176 3139 2649 2804 -288 54 -397 O ATOM 1297 CB VAL A 176 -3.254 -0.854 50.999 1.00 23.50 C ANISOU 1297 CB VAL B 176 3151 2828 2948 -288 -21 -415 C ATOM 1298 CG1 VAL A 176 -3.993 -0.899 49.613 1.00 24.34 C ANISOU 1298 CG1 VAL B 176 3212 2949 3087 -304 11 -410 C ATOM 1299 CG2 VAL A 176 -3.060 -2.258 51.552 1.00 23.90 C ANISOU 1299 CG2 VAL B 176 3176 2905 2998 -271 -69 -425 C ATOM 1300 N PHE A 177 -1.718 1.496 49.121 1.00 23.35 N ANISOU 1300 N PHE B 177 3168 2781 2924 -260 76 -383 N ATOM 1301 CA PHE A 177 -1.957 2.772 48.466 1.00 23.27 C ANISOU 1301 CA PHE B 177 3171 2755 2915 -265 113 -373 C ATOM 1302 C PHE A 177 -3.446 2.989 48.290 1.00 23.61 C ANISOU 1302 C PHE B 177 3207 2791 2971 -297 123 -374 C ATOM 1303 O PHE A 177 -4.149 2.112 47.770 1.00 23.08 O ANISOU 1303 O PHE B 177 3102 2744 2924 -310 117 -376 O ATOM 1304 CB PHE A 177 -1.209 2.814 47.121 1.00 22.86 C ANISOU 1304 CB PHE B 177 3094 2723 2870 -242 137 -363 C ATOM 1305 CG PHE A 177 0.249 3.084 47.279 1.00 21.15 C ANISOU 1305 CG PHE B 177 2894 2503 2640 -217 141 -366 C ATOM 1306 CD1 PHE A 177 1.099 2.111 47.784 1.00 20.91 C ANISOU 1306 CD1 PHE B 177 2862 2479 2604 -202 120 -372 C ATOM 1307 CD2 PHE A 177 0.770 4.309 46.962 1.00 20.30 C ANISOU 1307 CD2 PHE B 177 2803 2384 2524 -208 168 -363 C ATOM 1308 CE1 PHE A 177 2.469 2.362 47.973 1.00 21.05 C ANISOU 1308 CE1 PHE B 177 2901 2489 2610 -181 130 -376 C ATOM 1309 CE2 PHE A 177 2.159 4.559 47.122 1.00 21.83 C ANISOU 1309 CE2 PHE B 177 3010 2574 2709 -189 175 -370 C ATOM 1310 CZ PHE A 177 2.975 3.605 47.642 1.00 21.80 C ANISOU 1310 CZ PHE B 177 3010 2572 2701 -178 159 -377 C ATOM 1311 N GLU A 178 -3.946 4.136 48.765 1.00 23.87 N ANISOU 1311 N GLU B 178 3280 2795 2995 -311 140 -373 N ATOM 1312 CA GLU A 178 -5.318 4.538 48.449 1.00 23.91 C ANISOU 1312 CA GLU B 178 3286 2787 3013 -340 161 -371 C ATOM 1313 C GLU A 178 -5.164 5.280 47.162 1.00 22.97 C ANISOU 1313 C GLU B 178 3162 2670 2898 -321 198 -352 C ATOM 1314 O GLU A 178 -4.857 6.452 47.159 1.00 22.28 O ANISOU 1314 O GLU B 178 3103 2563 2799 -307 218 -344 O ATOM 1315 CB GLU A 178 -5.906 5.458 49.524 1.00 24.88 C ANISOU 1315 CB GLU B 178 3456 2872 3123 -360 166 -378 C ATOM 1316 CG GLU A 178 -6.101 4.841 50.882 1.00 25.45 C ANISOU 1316 CG GLU B 178 3543 2941 3184 -379 127 -399 C ATOM 1317 CD GLU A 178 -6.873 5.784 51.809 1.00 26.74 C ANISOU 1317 CD GLU B 178 3756 3068 3337 -405 139 -407 C ATOM 1318 OE1 GLU A 178 -6.258 6.672 52.431 1.00 25.33 O ANISOU 1318 OE1 GLU B 178 3620 2866 3139 -392 149 -405 O ATOM 1319 OE2 GLU A 178 -8.106 5.654 51.886 1.00 32.09 O ANISOU 1319 OE2 GLU B 178 4429 3737 4027 -440 143 -418 O ATOM 1320 N SER A 179 -5.362 4.565 46.068 1.00 23.99 N ANISOU 1320 N SER B 179 3252 2823 3042 -318 205 -346 N ATOM 1321 CA SER A 179 -4.832 4.925 44.761 1.00 25.92 C ANISOU 1321 CA SER B 179 3484 3080 3283 -290 229 -330 C ATOM 1322 C SER A 179 -5.299 6.242 44.206 1.00 25.57 C ANISOU 1322 C SER B 179 3468 3016 3233 -283 264 -314 C ATOM 1323 O SER A 179 -4.541 6.897 43.523 1.00 25.81 O ANISOU 1323 O SER B 179 3501 3055 3252 -253 276 -304 O ATOM 1324 CB SER A 179 -5.167 3.824 43.758 1.00 26.25 C ANISOU 1324 CB SER B 179 3482 3148 3343 -294 234 -327 C ATOM 1325 OG SER A 179 -4.836 2.589 44.354 1.00 31.64 O ANISOU 1325 OG SER B 179 4137 3849 4034 -299 200 -342 O ATOM 1326 N LYS A 180 -6.541 6.633 44.489 1.00 25.02 N ANISOU 1326 N LYS B 180 3419 2919 3168 -310 282 -312 N ATOM 1327 CA LYS A 180 -7.084 7.851 43.913 1.00 25.54 C ANISOU 1327 CA LYS B 180 3515 2961 3226 -300 318 -294 C ATOM 1328 C LYS A 180 -6.925 9.073 44.829 1.00 24.75 C ANISOU 1328 C LYS B 180 3458 2833 3115 -294 322 -295 C ATOM 1329 O LYS A 180 -7.138 10.226 44.425 1.00 23.48 O ANISOU 1329 O LYS B 180 3322 2653 2946 -275 350 -280 O ATOM 1330 CB LYS A 180 -8.556 7.611 43.519 1.00 28.28 C ANISOU 1330 CB LYS B 180 3865 3290 3588 -331 346 -289 C ATOM 1331 CG LYS A 180 -8.681 6.538 42.414 1.00 31.73 C ANISOU 1331 CG LYS B 180 4262 3756 4038 -332 353 -285 C ATOM 1332 CD LYS A 180 -9.984 6.666 41.635 1.00 38.71 C ANISOU 1332 CD LYS B 180 5158 4619 4932 -351 397 -272 C ATOM 1333 CE LYS A 180 -9.816 6.132 40.211 1.00 42.04 C ANISOU 1333 CE LYS B 180 5556 5066 5354 -332 416 -258 C ATOM 1334 NZ LYS A 180 -9.422 4.700 40.264 1.00 43.93 N ANISOU 1334 NZ LYS B 180 5743 5338 5611 -345 389 -276 N ATOM 1335 N LEU A 181 -6.497 8.815 46.049 1.00 23.73 N ANISOU 1335 N LEU B 181 3336 2698 2983 -306 295 -313 N ATOM 1336 CA LEU A 181 -6.433 9.849 47.060 1.00 24.92 C ANISOU 1336 CA LEU B 181 3528 2817 3122 -307 301 -318 C ATOM 1337 C LEU A 181 -5.016 10.433 47.072 1.00 23.83 C ANISOU 1337 C LEU B 181 3390 2690 2973 -272 297 -318 C ATOM 1338 O LEU A 181 -4.181 10.046 47.893 1.00 23.26 O ANISOU 1338 O LEU B 181 3320 2623 2896 -273 274 -333 O ATOM 1339 CB LEU A 181 -6.779 9.257 48.443 1.00 24.47 C ANISOU 1339 CB LEU B 181 3485 2747 3064 -341 275 -340 C ATOM 1340 CG LEU A 181 -7.817 9.876 49.367 1.00 29.01 C ANISOU 1340 CG LEU B 181 4104 3283 3637 -371 289 -348 C ATOM 1341 CD1 LEU A 181 -7.568 9.540 50.838 1.00 23.85 C ANISOU 1341 CD1 LEU B 181 3473 2620 2970 -389 258 -370 C ATOM 1342 CD2 LEU A 181 -7.966 11.401 49.202 1.00 28.98 C ANISOU 1342 CD2 LEU B 181 4137 3247 3628 -353 328 -333 C ATOM 1343 N ARG A 182 -4.787 11.366 46.149 1.00 24.48 N ANISOU 1343 N ARG B 182 3471 2776 3053 -242 319 -303 N ATOM 1344 CA ARG A 182 -3.520 12.059 45.952 1.00 24.49 C ANISOU 1344 CA ARG B 182 3466 2792 3048 -209 320 -306 C ATOM 1345 C ARG A 182 -3.656 13.317 45.147 1.00 23.84 C ANISOU 1345 C ARG B 182 3390 2705 2961 -178 346 -290 C ATOM 1346 O ARG A 182 -4.623 13.535 44.416 1.00 24.38 O ANISOU 1346 O ARG B 182 3466 2767 3030 -174 364 -272 O ATOM 1347 CB ARG A 182 -2.508 11.196 45.244 1.00 24.56 C ANISOU 1347 CB ARG B 182 3435 2839 3056 -195 302 -311 C ATOM 1348 CG ARG A 182 -3.036 10.453 44.103 1.00 29.39 C ANISOU 1348 CG ARG B 182 4021 3473 3672 -194 303 -299 C ATOM 1349 CD ARG A 182 -2.522 9.019 44.337 1.00 33.26 C ANISOU 1349 CD ARG B 182 4485 3984 4168 -207 277 -311 C ATOM 1350 NE ARG A 182 -1.495 8.722 43.392 1.00 29.45 N ANISOU 1350 NE ARG B 182 3974 3535 3683 -183 273 -312 N ATOM 1351 CZ ARG A 182 -0.871 7.563 43.270 1.00 31.93 C ANISOU 1351 CZ ARG B 182 4261 3870 4001 -184 256 -321 C ATOM 1352 NH1 ARG A 182 -1.105 6.521 44.090 1.00 30.89 N ANISOU 1352 NH1 ARG B 182 4126 3733 3876 -204 236 -329 N ATOM 1353 NH2 ARG A 182 0.037 7.481 42.321 1.00 27.23 N ANISOU 1353 NH2 ARG B 182 3644 3301 3401 -161 259 -323 N ATOM 1354 N GLY A 183 -2.627 14.124 45.246 1.00 22.59 N ANISOU 1354 N GLY B 183 3228 2554 2800 -153 347 -299 N ATOM 1355 CA GLY A 183 -2.526 15.262 44.413 1.00 21.75 C ANISOU 1355 CA GLY B 183 3119 2456 2691 -116 364 -287 C ATOM 1356 C GLY A 183 -1.076 15.602 44.227 1.00 21.26 C ANISOU 1356 C GLY B 183 3028 2420 2628 -93 354 -304 C ATOM 1357 O GLY A 183 -0.292 15.482 45.165 1.00 20.62 O ANISOU 1357 O GLY B 183 2950 2332 2551 -106 349 -324 O ATOM 1358 N SER A 184 -0.748 16.055 43.017 1.00 21.11 N ANISOU 1358 N SER B 184 2985 2432 2603 -58 354 -297 N ATOM 1359 CA SER A 184 0.625 16.378 42.636 1.00 21.94 C ANISOU 1359 CA SER B 184 3057 2570 2709 -36 345 -317 C ATOM 1360 C SER A 184 0.698 17.843 42.218 1.00 22.16 C ANISOU 1360 C SER B 184 3081 2604 2736 3 356 -314 C ATOM 1361 O SER A 184 -0.319 18.455 41.905 1.00 21.69 O ANISOU 1361 O SER B 184 3043 2529 2669 20 369 -291 O ATOM 1362 CB SER A 184 1.141 15.486 41.500 1.00 22.30 C ANISOU 1362 CB SER B 184 3069 2658 2746 -29 328 -319 C ATOM 1363 OG SER A 184 1.448 14.164 41.935 1.00 24.25 O ANISOU 1363 OG SER B 184 3311 2905 2998 -59 316 -329 O ATOM 1364 N HIS A 185 1.910 18.393 42.265 1.00 22.03 N ANISOU 1364 N HIS B 185 3037 2608 2726 17 352 -340 N ATOM 1365 CA HIS A 185 2.192 19.729 41.784 1.00 22.85 C ANISOU 1365 CA HIS B 185 3123 2729 2832 58 357 -344 C ATOM 1366 C HIS A 185 3.595 19.732 41.225 1.00 23.74 C ANISOU 1366 C HIS B 185 3188 2885 2947 68 341 -374 C ATOM 1367 O HIS A 185 4.547 19.352 41.904 1.00 22.89 O ANISOU 1367 O HIS B 185 3071 2775 2853 42 344 -402 O ATOM 1368 CB HIS A 185 2.133 20.763 42.930 1.00 22.81 C ANISOU 1368 CB HIS B 185 3138 2687 2842 56 379 -352 C ATOM 1369 CG HIS A 185 2.388 22.155 42.458 1.00 24.18 C ANISOU 1369 CG HIS B 185 3289 2879 3021 102 383 -357 C ATOM 1370 ND1 HIS A 185 1.385 22.961 41.962 1.00 26.46 N ANISOU 1370 ND1 HIS B 185 3596 3158 3299 138 391 -328 N ATOM 1371 CD2 HIS A 185 3.531 22.870 42.367 1.00 23.24 C ANISOU 1371 CD2 HIS B 185 3128 2787 2915 119 380 -387 C ATOM 1372 CE1 HIS A 185 1.902 24.120 41.597 1.00 27.55 C ANISOU 1372 CE1 HIS B 185 3703 3320 3444 180 389 -339 C ATOM 1373 NE2 HIS A 185 3.202 24.086 41.827 1.00 27.65 N ANISOU 1373 NE2 HIS B 185 3677 3357 3472 168 382 -377 N ATOM 1374 N MET A 186 3.717 20.168 39.983 1.00 25.61 N ANISOU 1374 N MET B 186 3398 3163 3170 106 327 -371 N ATOM 1375 CA MET A 186 4.981 20.185 39.284 1.00 28.33 C ANISOU 1375 CA MET B 186 3696 3555 3515 117 310 -402 C ATOM 1376 C MET A 186 5.007 21.454 38.490 1.00 29.28 C ANISOU 1376 C MET B 186 3792 3706 3628 168 301 -403 C ATOM 1377 O MET A 186 3.955 21.920 37.999 1.00 29.16 O ANISOU 1377 O MET B 186 3800 3685 3595 200 302 -369 O ATOM 1378 CB MET A 186 5.135 18.950 38.356 1.00 28.69 C ANISOU 1378 CB MET B 186 3732 3628 3542 108 293 -399 C ATOM 1379 CG MET A 186 5.031 17.611 39.101 1.00 27.70 C ANISOU 1379 CG MET B 186 3628 3474 3424 62 300 -396 C ATOM 1380 SD MET A 186 6.120 16.286 38.529 1.00 32.24 S ANISOU 1380 SD MET B 186 4175 4079 3995 43 287 -419 S ATOM 1381 CE MET A 186 5.592 14.976 39.671 1.00 27.90 C ANISOU 1381 CE MET B 186 3660 3486 3455 0 295 -405 C ATOM 1382 N ALA A 187 6.210 21.998 38.353 1.00 30.72 N ANISOU 1382 N ALA B 187 3928 3922 3822 177 292 -442 N ATOM 1383 CA ALA A 187 6.413 23.341 37.813 1.00 32.26 C ANISOU 1383 CA ALA B 187 4091 4149 4018 225 282 -452 C ATOM 1384 C ALA A 187 7.868 23.532 37.433 1.00 33.27 C ANISOU 1384 C ALA B 187 4159 4324 4157 224 267 -503 C ATOM 1385 O ALA A 187 8.759 22.813 37.932 1.00 33.17 O ANISOU 1385 O ALA B 187 4138 4306 4161 180 276 -532 O ATOM 1386 CB ALA A 187 6.009 24.390 38.867 1.00 32.51 C ANISOU 1386 CB ALA B 187 4138 4141 4072 233 307 -448 C ATOM 1387 N HIS A 188 8.105 24.496 36.547 1.00 34.63 N ANISOU 1387 N HIS B 188 4294 4544 4320 272 244 -514 N ATOM 1388 CA HIS A 188 9.453 24.901 36.187 1.00 35.88 C ANISOU 1388 CA HIS B 188 4388 4751 4493 273 228 -569 C ATOM 1389 C HIS A 188 9.883 26.058 37.079 1.00 36.59 C ANISOU 1389 C HIS B 188 4451 4830 4621 277 248 -597 C ATOM 1390 O HIS A 188 9.441 27.192 36.883 1.00 35.97 O ANISOU 1390 O HIS B 188 4360 4763 4543 326 240 -587 O ATOM 1391 CB HIS A 188 9.509 25.332 34.725 1.00 36.54 C ANISOU 1391 CB HIS B 188 4441 4899 4545 326 188 -570 C ATOM 1392 CG HIS A 188 10.826 25.919 34.309 1.00 37.55 C ANISOU 1392 CG HIS B 188 4497 5083 4687 331 168 -630 C ATOM 1393 ND1 HIS A 188 12.032 25.282 34.524 1.00 38.37 N ANISOU 1393 ND1 HIS B 188 4572 5195 4811 281 177 -679 N ATOM 1394 CD2 HIS A 188 11.122 27.082 33.682 1.00 39.16 C ANISOU 1394 CD2 HIS B 188 4651 5338 4889 381 140 -652 C ATOM 1395 CE1 HIS A 188 13.011 26.018 34.032 1.00 37.79 C ANISOU 1395 CE1 HIS B 188 4433 5175 4748 295 156 -730 C ATOM 1396 NE2 HIS A 188 12.485 27.111 33.507 1.00 39.62 N ANISOU 1396 NE2 HIS B 188 4649 5438 4968 357 131 -716 N ATOM 1397 N VAL A 189 10.738 25.764 38.057 1.00 37.16 N ANISOU 1397 N VAL B 189 4516 4878 4726 227 276 -631 N ATOM 1398 CA VAL A 189 11.300 26.810 38.923 1.00 38.78 C ANISOU 1398 CA VAL B 189 4692 5071 4971 223 301 -665 C ATOM 1399 C VAL A 189 12.798 26.623 39.122 1.00 39.32 C ANISOU 1399 C VAL B 189 4715 5157 5068 183 314 -726 C ATOM 1400 O VAL A 189 13.342 25.520 38.983 1.00 40.11 O ANISOU 1400 O VAL B 189 4823 5256 5159 146 314 -737 O ATOM 1401 CB VAL A 189 10.628 26.865 40.321 1.00 38.64 C ANISOU 1401 CB VAL B 189 4729 4982 4970 201 342 -640 C ATOM 1402 CG1 VAL A 189 9.199 27.382 40.209 1.00 39.45 C ANISOU 1402 CG1 VAL B 189 4871 5066 5054 243 337 -588 C ATOM 1403 CG2 VAL A 189 10.688 25.476 41.041 1.00 38.75 C ANISOU 1403 CG2 VAL B 189 4791 4953 4978 144 360 -631 C ATOM 1404 N TYR A 190 13.452 27.714 39.470 1.00 39.91 N ANISOU 1404 N TYR B 190 4742 5243 5178 189 328 -766 N ATOM 1405 CA TYR A 190 14.860 27.705 39.785 1.00 39.85 C ANISOU 1405 CA TYR B 190 4691 5246 5205 148 350 -829 C ATOM 1406 C TYR A 190 15.057 28.050 41.266 1.00 40.47 C ANISOU 1406 C TYR B 190 4792 5264 5319 115 405 -840 C ATOM 1407 O TYR A 190 15.779 28.992 41.609 1.00 41.46 O ANISOU 1407 O TYR B 190 4869 5399 5484 112 427 -885 O ATOM 1408 CB TYR A 190 15.590 28.698 38.880 1.00 39.63 C ANISOU 1408 CB TYR B 190 4577 5289 5190 180 322 -877 C ATOM 1409 CG TYR A 190 15.917 28.187 37.474 1.00 37.47 C ANISOU 1409 CG TYR B 190 4275 5078 4884 194 273 -889 C ATOM 1410 CD1 TYR A 190 15.291 28.732 36.352 1.00 36.94 C ANISOU 1410 CD1 TYR B 190 4189 5063 4785 257 224 -868 C ATOM 1411 CD2 TYR A 190 16.884 27.185 37.271 1.00 37.94 C ANISOU 1411 CD2 TYR B 190 4328 5143 4942 145 280 -923 C ATOM 1412 CE1 TYR A 190 15.607 28.286 35.045 1.00 38.83 C ANISOU 1412 CE1 TYR B 190 4405 5360 4989 271 180 -880 C ATOM 1413 CE2 TYR A 190 17.227 26.748 35.984 1.00 37.19 C ANISOU 1413 CE2 TYR B 190 4207 5106 4818 157 239 -938 C ATOM 1414 CZ TYR A 190 16.577 27.305 34.869 1.00 38.23 C ANISOU 1414 CZ TYR B 190 4321 5291 4915 219 188 -917 C ATOM 1415 OH TYR A 190 16.893 26.890 33.593 1.00 36.97 O ANISOU 1415 OH TYR B 190 4140 5187 4720 232 147 -931 O ATOM 1416 N ASP A 191 14.422 27.264 42.132 1.00 40.51 N ANISOU 1416 N ASP B 191 4870 5209 5311 89 428 -801 N ATOM 1417 CA ASP A 191 14.491 27.458 43.582 1.00 41.64 C ANISOU 1417 CA ASP B 191 5051 5290 5480 58 480 -804 C ATOM 1418 C ASP A 191 15.771 26.880 44.189 1.00 42.19 C ANISOU 1418 C ASP B 191 5119 5339 5571 3 517 -848 C ATOM 1419 O ASP A 191 16.425 27.518 45.040 1.00 42.46 O ANISOU 1419 O ASP B 191 5143 5349 5641 -18 562 -883 O ATOM 1420 CB ASP A 191 13.271 26.852 44.268 1.00 40.95 C ANISOU 1420 CB ASP B 191 5044 5149 5366 54 485 -747 C ATOM 1421 CG ASP A 191 13.071 25.371 43.940 1.00 41.29 C ANISOU 1421 CG ASP B 191 5124 5189 5377 33 464 -721 C ATOM 1422 OD1 ASP A 191 12.456 24.677 44.782 1.00 42.41 O ANISOU 1422 OD1 ASP B 191 5329 5282 5505 11 477 -690 O ATOM 1423 OD2 ASP A 191 13.535 24.901 42.870 1.00 39.89 O ANISOU 1423 OD2 ASP B 191 4912 5058 5188 38 434 -734 O ATOM 1424 N PHE A 192 16.113 25.673 43.730 1.00 41.71 N ANISOU 1424 N PHE B 192 5072 5287 5488 -19 501 -846 N ATOM 1425 CA PHE A 192 17.273 24.940 44.181 1.00 41.47 C ANISOU 1425 CA PHE B 192 5049 5236 5471 -68 534 -881 C ATOM 1426 C PHE A 192 17.592 23.950 43.082 1.00 41.55 C ANISOU 1426 C PHE B 192 5044 5284 5457 -71 500 -884 C ATOM 1427 O PHE A 192 16.745 23.128 42.695 1.00 40.49 O ANISOU 1427 O PHE B 192 4945 5150 5289 -57 469 -838 O ATOM 1428 CB PHE A 192 16.946 24.209 45.485 1.00 41.74 C ANISOU 1428 CB PHE B 192 5165 5199 5497 -97 568 -851 C ATOM 1429 CG PHE A 192 18.089 23.397 46.044 1.00 42.37 C ANISOU 1429 CG PHE B 192 5266 5248 5586 -144 606 -881 C ATOM 1430 CD1 PHE A 192 18.847 23.886 47.114 1.00 44.91 C ANISOU 1430 CD1 PHE B 192 5599 5528 5937 -174 664 -913 C ATOM 1431 CD2 PHE A 192 18.384 22.136 45.534 1.00 41.75 C ANISOU 1431 CD2 PHE B 192 5201 5177 5484 -157 589 -874 C ATOM 1432 CE1 PHE A 192 19.898 23.124 47.656 1.00 44.62 C ANISOU 1432 CE1 PHE B 192 5592 5457 5907 -215 706 -938 C ATOM 1433 CE2 PHE A 192 19.433 21.372 46.067 1.00 44.12 C ANISOU 1433 CE2 PHE B 192 5527 5444 5791 -196 627 -898 C ATOM 1434 CZ PHE A 192 20.186 21.867 47.119 1.00 42.21 C ANISOU 1434 CZ PHE B 192 5301 5160 5578 -225 686 -929 C ATOM 1435 N TYR A 193 18.811 24.039 42.566 1.00 42.02 N ANISOU 1435 N TYR B 193 5052 5377 5537 -90 506 -940 N ATOM 1436 CA TYR A 193 19.253 23.191 41.459 1.00 42.28 C ANISOU 1436 CA TYR B 193 5065 5449 5549 -93 477 -951 C ATOM 1437 C TYR A 193 20.781 23.076 41.493 1.00 43.26 C ANISOU 1437 C TYR B 193 5156 5577 5702 -137 511 -1017 C ATOM 1438 O TYR A 193 21.454 23.844 42.203 1.00 41.98 O ANISOU 1438 O TYR B 193 4973 5397 5579 -158 553 -1057 O ATOM 1439 CB TYR A 193 18.737 23.721 40.101 1.00 42.05 C ANISOU 1439 CB TYR B 193 4989 5490 5500 -45 420 -945 C ATOM 1440 CG TYR A 193 19.021 25.202 39.808 1.00 42.94 C ANISOU 1440 CG TYR B 193 5030 5645 5639 -19 411 -983 C ATOM 1441 CD1 TYR A 193 19.847 25.582 38.735 1.00 42.74 C ANISOU 1441 CD1 TYR B 193 4934 5687 5619 -12 384 -1036 C ATOM 1442 CD2 TYR A 193 18.455 26.219 40.597 1.00 43.49 C ANISOU 1442 CD2 TYR B 193 5104 5691 5729 0 429 -969 C ATOM 1443 CE1 TYR A 193 20.110 26.934 38.459 1.00 42.15 C ANISOU 1443 CE1 TYR B 193 4789 5658 5570 15 371 -1074 C ATOM 1444 CE2 TYR A 193 18.716 27.587 40.335 1.00 43.69 C ANISOU 1444 CE2 TYR B 193 5061 5757 5781 29 420 -1006 C ATOM 1445 CZ TYR A 193 19.542 27.933 39.270 1.00 44.47 C ANISOU 1445 CZ TYR B 193 5085 5925 5886 37 390 -1058 C ATOM 1446 OH TYR A 193 19.781 29.273 39.017 1.00 43.49 O ANISOU 1446 OH TYR B 193 4888 5846 5790 68 378 -1094 O ATOM 1447 N LYS A 194 21.307 22.113 40.729 1.00 43.73 N ANISOU 1447 N LYS B 194 5213 5656 5745 -151 498 -1030 N ATOM 1448 CA LYS A 194 22.745 21.844 40.660 1.00 45.51 C ANISOU 1448 CA LYS B 194 5414 5883 5996 -195 532 -1092 C ATOM 1449 C LYS A 194 23.249 21.910 39.203 1.00 45.88 C ANISOU 1449 C LYS B 194 5398 6003 6033 -186 492 -1131 C ATOM 1450 O LYS A 194 23.386 20.886 38.535 1.00 45.31 O ANISOU 1450 O LYS B 194 5341 5940 5935 -192 477 -1124 O ATOM 1451 CB LYS A 194 23.065 20.501 41.339 1.00 45.26 C ANISOU 1451 CB LYS B 194 5452 5792 5954 -229 568 -1074 C ATOM 1452 CG LYS A 194 22.637 20.466 42.812 1.00 46.52 C ANISOU 1452 CG LYS B 194 5675 5880 6118 -238 606 -1040 C ATOM 1453 CD LYS A 194 23.304 19.349 43.613 1.00 46.62 C ANISOU 1453 CD LYS B 194 5751 5833 6129 -275 652 -1039 C ATOM 1454 CE LYS A 194 22.860 19.412 45.086 1.00 49.66 C ANISOU 1454 CE LYS B 194 6201 6153 6515 -280 687 -1007 C ATOM 1455 NZ LYS A 194 23.470 18.303 45.872 1.00 54.20 N ANISOU 1455 NZ LYS B 194 6843 6669 7083 -308 728 -1001 N ATOM 1456 N PRO A 195 23.504 23.139 38.706 1.00 47.38 N ANISOU 1456 N PRO B 195 5513 6245 6242 -169 473 -1172 N ATOM 1457 CA PRO A 195 23.785 23.410 37.282 1.00 48.00 C ANISOU 1457 CA PRO B 195 5529 6404 6306 -148 423 -1206 C ATOM 1458 C PRO A 195 25.254 23.307 36.869 1.00 49.52 C ANISOU 1458 C PRO B 195 5673 6619 6522 -193 443 -1286 C ATOM 1459 O PRO A 195 25.563 23.258 35.671 1.00 48.96 O ANISOU 1459 O PRO B 195 5561 6610 6433 -183 403 -1315 O ATOM 1460 CB PRO A 195 23.286 24.842 37.112 1.00 48.09 C ANISOU 1460 CB PRO B 195 5487 6456 6329 -103 393 -1210 C ATOM 1461 CG PRO A 195 23.500 25.483 38.487 1.00 47.67 C ANISOU 1461 CG PRO B 195 5442 6350 6321 -126 450 -1221 C ATOM 1462 CD PRO A 195 23.510 24.381 39.516 1.00 47.60 C ANISOU 1462 CD PRO B 195 5515 6262 6309 -165 499 -1190 C ATOM 1463 N ASN A 196 26.130 23.290 37.874 1.00 51.01 N ANISOU 1463 N ASN B 196 5871 6757 6752 -243 509 -1322 N ATOM 1464 CA ASN A 196 27.574 23.161 37.713 1.00 53.12 C ANISOU 1464 CA ASN B 196 6103 7030 7050 -296 546 -1400 C ATOM 1465 C ASN A 196 27.945 21.688 37.902 1.00 53.46 C ANISOU 1465 C ASN B 196 6216 7022 7076 -330 579 -1383 C ATOM 1466 O ASN A 196 27.973 21.172 39.031 1.00 52.62 O ANISOU 1466 O ASN B 196 6174 6843 6978 -352 630 -1357 O ATOM 1467 CB ASN A 196 28.278 24.040 38.758 1.00 53.65 C ANISOU 1467 CB ASN B 196 6145 7065 7174 -331 607 -1446 C ATOM 1468 CG ASN A 196 29.749 24.281 38.442 1.00 55.19 C ANISOU 1468 CG ASN B 196 6278 7282 7408 -383 640 -1540 C ATOM 1469 OD1 ASN A 196 30.390 23.520 37.708 1.00 54.95 O ANISOU 1469 OD1 ASN B 196 6246 7268 7364 -407 635 -1569 O ATOM 1470 ND2 ASN A 196 30.297 25.351 39.020 1.00 56.32 N ANISOU 1470 ND2 ASN B 196 6371 7424 7604 -403 678 -1592 N ATOM 1471 N LEU A 197 28.197 21.009 36.789 1.00 54.66 N ANISOU 1471 N LEU B 197 6356 7212 7199 -330 547 -1396 N ATOM 1472 CA LEU A 197 28.380 19.561 36.801 1.00 56.14 C ANISOU 1472 CA LEU B 197 6609 7358 7364 -349 569 -1371 C ATOM 1473 C LEU A 197 29.599 19.139 37.613 1.00 57.28 C ANISOU 1473 C LEU B 197 6779 7442 7544 -409 647 -1415 C ATOM 1474 O LEU A 197 29.647 18.021 38.119 1.00 57.12 O ANISOU 1474 O LEU B 197 6829 7363 7510 -422 679 -1382 O ATOM 1475 CB LEU A 197 28.457 19.011 35.363 1.00 56.29 C ANISOU 1475 CB LEU B 197 6606 7434 7348 -337 522 -1383 C ATOM 1476 CG LEU A 197 27.169 18.543 34.657 1.00 56.34 C ANISOU 1476 CG LEU B 197 6639 7465 7302 -284 463 -1313 C ATOM 1477 CD1 LEU A 197 25.943 19.457 34.872 1.00 56.45 C ANISOU 1477 CD1 LEU B 197 6645 7495 7307 -234 425 -1265 C ATOM 1478 CD2 LEU A 197 27.441 18.365 33.173 1.00 56.30 C ANISOU 1478 CD2 LEU B 197 6596 7529 7267 -274 419 -1344 C ATOM 1479 N ALA A 198 30.562 20.050 37.748 1.00 59.29 N ANISOU 1479 N ALA B 198 6976 7710 7843 -443 679 -1488 N ATOM 1480 CA ALA A 198 31.838 19.758 38.393 1.00 61.26 C ANISOU 1480 CA ALA B 198 7242 7905 8128 -505 758 -1541 C ATOM 1481 C ALA A 198 31.878 19.932 39.935 1.00 62.25 C ANISOU 1481 C ALA B 198 7420 7951 8281 -523 825 -1521 C ATOM 1482 O ALA A 198 32.917 19.666 40.551 1.00 62.90 O ANISOU 1482 O ALA B 198 7528 7980 8392 -573 899 -1560 O ATOM 1483 CB ALA A 198 32.962 20.560 37.715 1.00 61.96 C ANISOU 1483 CB ALA B 198 7242 8047 8254 -541 766 -1639 C ATOM 1484 N SER A 199 30.763 20.351 40.549 1.00 63.10 N ANISOU 1484 N SER B 199 7550 8048 8377 -484 802 -1462 N ATOM 1485 CA SER A 199 30.704 20.571 42.014 1.00 63.97 C ANISOU 1485 CA SER B 199 7713 8085 8507 -497 861 -1441 C ATOM 1486 C SER A 199 29.366 20.222 42.653 1.00 64.17 C ANISOU 1486 C SER B 199 7804 8080 8497 -455 834 -1353 C ATOM 1487 O SER A 199 28.331 20.273 41.992 1.00 64.29 O ANISOU 1487 O SER B 199 7804 8140 8482 -410 767 -1312 O ATOM 1488 CB SER A 199 31.052 22.021 42.369 1.00 64.63 C ANISOU 1488 CB SER B 199 7732 8185 8640 -510 886 -1493 C ATOM 1489 OG SER A 199 29.918 22.857 42.287 1.00 63.23 O ANISOU 1489 OG SER B 199 7527 8044 8452 -460 832 -1456 O ATOM 1490 N GLU A 200 29.400 19.907 43.952 1.00 65.01 N ANISOU 1490 N GLU B 200 7986 8110 8607 -470 889 -1327 N ATOM 1491 CA GLU A 200 28.199 19.567 44.737 1.00 65.21 C ANISOU 1491 CA GLU B 200 8078 8099 8599 -436 870 -1250 C ATOM 1492 C GLU A 200 27.401 20.792 45.210 1.00 65.22 C ANISOU 1492 C GLU B 200 8057 8110 8614 -413 858 -1236 C ATOM 1493 O GLU A 200 26.285 20.643 45.723 1.00 64.77 O ANISOU 1493 O GLU B 200 8046 8034 8530 -382 834 -1174 O ATOM 1494 CB GLU A 200 28.579 18.696 45.943 1.00 65.46 C ANISOU 1494 CB GLU B 200 8204 8046 8623 -460 931 -1228 C ATOM 1495 CG GLU A 200 28.403 17.180 45.739 1.00 67.69 C ANISOU 1495 CG GLU B 200 8544 8310 8866 -448 913 -1185 C ATOM 1496 CD GLU A 200 27.062 16.636 46.263 1.00 70.51 C ANISOU 1496 CD GLU B 200 8959 8649 9183 -409 872 -1107 C ATOM 1497 OE1 GLU A 200 26.760 15.441 46.003 1.00 70.61 O ANISOU 1497 OE1 GLU B 200 9008 8657 9165 -394 847 -1070 O ATOM 1498 OE2 GLU A 200 26.316 17.393 46.938 1.00 71.37 O ANISOU 1498 OE2 GLU B 200 9075 8748 9294 -395 867 -1084 O ATOM 1499 N TYR A 201 27.979 21.987 45.045 1.00 65.94 N ANISOU 1499 N TYR B 201 8075 8231 8747 -427 876 -1295 N ATOM 1500 CA TYR A 201 27.333 23.244 45.461 1.00 66.09 C ANISOU 1500 CA TYR B 201 8065 8261 8786 -403 870 -1290 C ATOM 1501 C TYR A 201 26.146 23.566 44.547 1.00 64.71 C ANISOU 1501 C TYR B 201 7855 8148 8583 -347 788 -1251 C ATOM 1502 O TYR A 201 26.267 23.504 43.315 1.00 64.85 O ANISOU 1502 O TYR B 201 7819 8230 8592 -334 740 -1270 O ATOM 1503 CB TYR A 201 28.335 24.431 45.580 1.00 68.15 C ANISOU 1503 CB TYR B 201 8254 8535 9104 -434 917 -1368 C ATOM 1504 CG TYR A 201 28.653 25.234 44.299 1.00 71.00 C ANISOU 1504 CG TYR B 201 8505 8986 9487 -422 870 -1423 C ATOM 1505 CD1 TYR A 201 29.974 25.330 43.813 1.00 73.34 C ANISOU 1505 CD1 TYR B 201 8744 9305 9818 -466 900 -1503 C ATOM 1506 CD2 TYR A 201 27.644 25.936 43.598 1.00 72.92 C ANISOU 1506 CD2 TYR B 201 8702 9290 9714 -365 799 -1396 C ATOM 1507 CE1 TYR A 201 30.271 26.073 42.640 1.00 73.97 C ANISOU 1507 CE1 TYR B 201 8721 9472 9914 -454 852 -1557 C ATOM 1508 CE2 TYR A 201 27.929 26.671 42.424 1.00 73.27 C ANISOU 1508 CE2 TYR B 201 8648 9418 9772 -348 752 -1445 C ATOM 1509 CZ TYR A 201 29.238 26.738 41.955 1.00 73.43 C ANISOU 1509 CZ TYR B 201 8610 9465 9825 -392 776 -1526 C ATOM 1510 OH TYR A 201 29.511 27.473 40.812 1.00 73.16 O ANISOU 1510 OH TYR B 201 8479 9518 9802 -374 724 -1576 O ATOM 1511 N PRO A 202 24.983 23.867 45.152 1.00 63.26 N ANISOU 1511 N PRO B 202 7709 7944 8384 -315 773 -1195 N ATOM 1512 CA PRO A 202 23.805 24.219 44.372 1.00 62.06 C ANISOU 1512 CA PRO B 202 7532 7842 8206 -262 703 -1155 C ATOM 1513 C PRO A 202 23.666 25.730 44.180 1.00 61.46 C ANISOU 1513 C PRO B 202 7385 7806 8162 -236 694 -1183 C ATOM 1514 O PRO A 202 24.294 26.516 44.921 1.00 61.64 O ANISOU 1514 O PRO B 202 7387 7806 8227 -260 746 -1224 O ATOM 1515 CB PRO A 202 22.664 23.703 45.247 1.00 61.49 C ANISOU 1515 CB PRO B 202 7545 7717 8103 -246 702 -1084 C ATOM 1516 CG PRO A 202 23.197 23.802 46.663 1.00 62.00 C ANISOU 1516 CG PRO B 202 7657 7711 8190 -283 774 -1097 C ATOM 1517 CD PRO A 202 24.695 23.863 46.602 1.00 63.06 C ANISOU 1517 CD PRO B 202 7757 7844 8360 -327 823 -1166 C ATOM 1518 N VAL A 203 22.866 26.132 43.193 1.00 60.03 N ANISOU 1518 N VAL B 203 7165 7683 7959 -186 629 -1161 N ATOM 1519 CA VAL A 203 22.336 27.484 43.184 1.00 59.27 C ANISOU 1519 CA VAL B 203 7024 7613 7883 -147 616 -1163 C ATOM 1520 C VAL A 203 21.032 27.456 43.980 1.00 58.61 C ANISOU 1520 C VAL B 203 7011 7481 7776 -123 617 -1094 C ATOM 1521 O VAL A 203 20.159 26.620 43.737 1.00 57.74 O ANISOU 1521 O VAL B 203 6952 7363 7624 -106 584 -1038 O ATOM 1522 CB VAL A 203 22.123 28.063 41.779 1.00 59.49 C ANISOU 1522 CB VAL B 203 6979 7726 7899 -100 549 -1175 C ATOM 1523 CG1 VAL A 203 21.416 29.412 41.883 1.00 59.00 C ANISOU 1523 CG1 VAL B 203 6884 7682 7853 -51 535 -1165 C ATOM 1524 CG2 VAL A 203 23.464 28.236 41.060 1.00 60.10 C ANISOU 1524 CG2 VAL B 203 6979 7855 8003 -128 549 -1254 C ATOM 1525 N VAL A 204 20.942 28.345 44.964 1.00 58.33 N ANISOU 1525 N VAL B 204 6981 7411 7771 -125 659 -1100 N ATOM 1526 CA VAL A 204 19.772 28.434 45.822 1.00 57.88 C ANISOU 1526 CA VAL B 204 6991 7303 7697 -106 667 -1042 C ATOM 1527 C VAL A 204 19.229 29.857 45.790 1.00 58.07 C ANISOU 1527 C VAL B 204 6972 7349 7744 -62 660 -1044 C ATOM 1528 O VAL A 204 19.980 30.841 45.852 1.00 58.30 O ANISOU 1528 O VAL B 204 6936 7398 7818 -66 685 -1098 O ATOM 1529 CB VAL A 204 20.054 28.006 47.302 1.00 57.90 C ANISOU 1529 CB VAL B 204 7067 7225 7707 -152 733 -1039 C ATOM 1530 CG1 VAL A 204 18.728 27.906 48.112 1.00 57.59 C ANISOU 1530 CG1 VAL B 204 7105 7137 7639 -133 732 -975 C ATOM 1531 CG2 VAL A 204 20.821 26.686 47.370 1.00 57.30 C ANISOU 1531 CG2 VAL B 204 7028 7127 7615 -194 748 -1046 C ATOM 1532 N ASP A 205 17.910 29.931 45.665 1.00 57.44 N ANISOU 1532 N ASP B 205 6927 7265 7632 -20 628 -985 N ATOM 1533 CA ASP A 205 17.160 31.171 45.651 1.00 57.80 C ANISOU 1533 CA ASP B 205 6949 7322 7691 29 620 -972 C ATOM 1534 C ASP A 205 16.202 31.037 46.840 1.00 57.28 C ANISOU 1534 C ASP B 205 6970 7183 7612 22 652 -925 C ATOM 1535 O ASP A 205 15.086 30.527 46.688 1.00 56.28 O ANISOU 1535 O ASP B 205 6895 7043 7446 41 623 -869 O ATOM 1536 CB ASP A 205 16.424 31.284 44.301 1.00 57.84 C ANISOU 1536 CB ASP B 205 6925 7387 7664 86 551 -944 C ATOM 1537 CG ASP A 205 15.675 32.601 44.122 1.00 59.05 C ANISOU 1537 CG ASP B 205 7049 7558 7828 147 538 -930 C ATOM 1538 OD1 ASP A 205 15.035 33.081 45.086 1.00 59.51 O ANISOU 1538 OD1 ASP B 205 7150 7565 7896 151 574 -906 O ATOM 1539 OD2 ASP A 205 15.689 33.138 42.987 1.00 59.31 O ANISOU 1539 OD2 ASP B 205 7022 7658 7856 194 490 -940 O ATOM 1540 N GLY A 206 16.663 31.467 48.022 1.00 57.09 N ANISOU 1540 N GLY B 206 6963 7110 7620 -9 715 -949 N ATOM 1541 CA GLY A 206 15.953 31.237 49.292 1.00 56.88 C ANISOU 1541 CA GLY B 206 7025 7009 7578 -26 752 -913 C ATOM 1542 C GLY A 206 14.545 31.801 49.281 1.00 56.82 C ANISOU 1542 C GLY B 206 7044 6992 7553 21 732 -864 C ATOM 1543 O GLY A 206 13.589 31.166 49.749 1.00 56.27 O ANISOU 1543 O GLY B 206 7049 6882 7449 15 727 -816 O ATOM 1544 N LYS A 207 14.453 33.013 48.739 1.00 57.29 N ANISOU 1544 N LYS B 207 7039 7090 7639 66 722 -878 N ATOM 1545 CA LYS A 207 13.211 33.713 48.435 1.00 57.10 C ANISOU 1545 CA LYS B 207 7024 7069 7601 122 698 -836 C ATOM 1546 C LYS A 207 12.226 32.806 47.663 1.00 55.86 C ANISOU 1546 C LYS B 207 6906 6925 7394 140 645 -783 C ATOM 1547 O LYS A 207 11.113 32.531 48.146 1.00 55.53 O ANISOU 1547 O LYS B 207 6935 6838 7326 142 649 -736 O ATOM 1548 CB LYS A 207 13.576 34.996 47.651 1.00 58.25 C ANISOU 1548 CB LYS B 207 7076 7275 7782 172 683 -870 C ATOM 1549 CG LYS A 207 12.598 35.476 46.576 1.00 60.38 C ANISOU 1549 CG LYS B 207 7328 7585 8027 243 629 -832 C ATOM 1550 CD LYS A 207 13.366 36.007 45.343 1.00 63.12 C ANISOU 1550 CD LYS B 207 7575 8018 8389 279 585 -872 C ATOM 1551 CE LYS A 207 12.424 36.633 44.308 1.00 64.81 C ANISOU 1551 CE LYS B 207 7773 8272 8578 358 534 -834 C ATOM 1552 NZ LYS A 207 11.395 35.658 43.799 1.00 64.03 N ANISOU 1552 NZ LYS B 207 7744 8162 8423 365 501 -773 N ATOM 1553 N LEU A 208 12.650 32.330 46.491 1.00 54.29 N ANISOU 1553 N LEU B 208 6663 6785 7181 149 598 -792 N ATOM 1554 CA LEU A 208 11.779 31.550 45.613 1.00 53.03 C ANISOU 1554 CA LEU B 208 6531 6644 6976 170 550 -745 C ATOM 1555 C LEU A 208 11.457 30.204 46.220 1.00 51.65 C ANISOU 1555 C LEU B 208 6430 6422 6772 123 557 -718 C ATOM 1556 O LEU A 208 10.344 29.688 46.048 1.00 51.33 O ANISOU 1556 O LEU B 208 6438 6366 6699 134 538 -669 O ATOM 1557 CB LEU A 208 12.433 31.311 44.259 1.00 52.86 C ANISOU 1557 CB LEU B 208 6446 6694 6945 186 502 -768 C ATOM 1558 CG LEU A 208 11.643 31.556 42.977 1.00 53.16 C ANISOU 1558 CG LEU B 208 6468 6779 6951 246 450 -735 C ATOM 1559 CD1 LEU A 208 12.282 30.760 41.859 1.00 50.86 C ANISOU 1559 CD1 LEU B 208 6143 6542 6638 240 409 -752 C ATOM 1560 CD2 LEU A 208 10.157 31.251 43.090 1.00 52.77 C ANISOU 1560 CD2 LEU B 208 6493 6689 6868 264 446 -670 C ATOM 1561 N SER A 209 12.437 29.640 46.922 1.00 50.12 N ANISOU 1561 N SER B 209 6244 6207 6593 72 587 -750 N ATOM 1562 CA SER A 209 12.322 28.283 47.433 1.00 48.57 C ANISOU 1562 CA SER B 209 6110 5975 6370 30 590 -729 C ATOM 1563 C SER A 209 11.209 28.144 48.478 1.00 46.97 C ANISOU 1563 C SER B 209 5986 5710 6150 22 609 -689 C ATOM 1564 O SER A 209 10.459 27.179 48.437 1.00 46.34 O ANISOU 1564 O SER B 209 5951 5617 6038 14 587 -652 O ATOM 1565 CB SER A 209 13.662 27.779 47.977 1.00 48.15 C ANISOU 1565 CB SER B 209 6053 5909 6335 -18 622 -772 C ATOM 1566 OG SER A 209 13.770 28.145 49.327 1.00 49.25 O ANISOU 1566 OG SER B 209 6233 5990 6490 -42 675 -780 O ATOM 1567 N GLN A 210 11.093 29.096 49.403 1.00 46.24 N ANISOU 1567 N GLN B 210 5908 5581 6080 23 651 -697 N ATOM 1568 CA GLN A 210 9.986 29.042 50.378 1.00 45.26 C ANISOU 1568 CA GLN B 210 5860 5399 5938 16 668 -662 C ATOM 1569 C GLN A 210 8.639 29.220 49.705 1.00 43.59 C ANISOU 1569 C GLN B 210 5660 5197 5705 55 636 -618 C ATOM 1570 O GLN A 210 7.748 28.434 49.928 1.00 42.70 O ANISOU 1570 O GLN B 210 5602 5059 5563 41 624 -584 O ATOM 1571 CB GLN A 210 10.168 30.017 51.550 1.00 46.66 C ANISOU 1571 CB GLN B 210 6056 5531 6142 8 725 -682 C ATOM 1572 CG GLN A 210 11.028 29.439 52.722 1.00 50.05 C ANISOU 1572 CG GLN B 210 6527 5917 6573 -44 767 -706 C ATOM 1573 CD GLN A 210 10.658 27.990 53.144 1.00 52.78 C ANISOU 1573 CD GLN B 210 6940 6237 6878 -76 748 -677 C ATOM 1574 OE1 GLN A 210 11.053 26.997 52.490 1.00 53.11 O ANISOU 1574 OE1 GLN B 210 6966 6308 6906 -85 715 -676 O ATOM 1575 NE2 GLN A 210 9.909 27.873 54.250 1.00 53.38 N ANISOU 1575 NE2 GLN B 210 7090 6257 6933 -91 767 -657 N ATOM 1576 N THR A 211 8.522 30.228 48.845 1.00 42.98 N ANISOU 1576 N THR B 211 5531 5158 5642 104 623 -620 N ATOM 1577 CA THR A 211 7.351 30.411 47.982 1.00 42.12 C ANISOU 1577 CA THR B 211 5428 5064 5510 147 591 -578 C ATOM 1578 C THR A 211 6.991 29.143 47.158 1.00 40.85 C ANISOU 1578 C THR B 211 5280 4926 5314 138 549 -552 C ATOM 1579 O THR A 211 5.814 28.787 47.058 1.00 39.92 O ANISOU 1579 O THR B 211 5208 4787 5172 144 539 -512 O ATOM 1580 CB THR A 211 7.506 31.690 47.100 1.00 43.30 C ANISOU 1580 CB THR B 211 5512 5259 5679 207 580 -590 C ATOM 1581 OG1 THR A 211 7.567 32.839 47.963 1.00 44.61 O ANISOU 1581 OG1 THR B 211 5677 5394 5878 217 623 -606 O ATOM 1582 CG2 THR A 211 6.316 31.894 46.131 1.00 43.80 C ANISOU 1582 CG2 THR B 211 5589 5338 5716 259 549 -544 C ATOM 1583 N CYS A 212 8.010 28.460 46.617 1.00 39.13 N ANISOU 1583 N CYS B 212 5023 4747 5096 121 529 -578 N ATOM 1584 CA CYS A 212 7.828 27.242 45.805 1.00 38.08 C ANISOU 1584 CA CYS B 212 4896 4639 4934 112 492 -558 C ATOM 1585 C CYS A 212 7.353 26.032 46.590 1.00 35.10 C ANISOU 1585 C CYS B 212 4581 4218 4538 68 498 -537 C ATOM 1586 O CYS A 212 6.507 25.287 46.110 1.00 34.28 O ANISOU 1586 O CYS B 212 4501 4116 4408 70 474 -505 O ATOM 1587 CB CYS A 212 9.134 26.872 45.064 1.00 38.33 C ANISOU 1587 CB CYS B 212 4870 4722 4973 104 474 -596 C ATOM 1588 SG CYS A 212 9.481 28.033 43.742 1.00 44.89 S ANISOU 1588 SG CYS B 212 5624 5621 5813 163 446 -615 S ATOM 1589 N TYR A 213 7.933 25.826 47.766 1.00 32.86 N ANISOU 1589 N TYR B 213 4322 3897 4265 31 528 -558 N ATOM 1590 CA TYR A 213 7.634 24.674 48.570 1.00 31.94 C ANISOU 1590 CA TYR B 213 4262 3744 4130 -9 530 -543 C ATOM 1591 C TYR A 213 6.219 24.736 49.143 1.00 31.95 C ANISOU 1591 C TYR B 213 4319 3704 4115 -9 535 -508 C ATOM 1592 O TYR A 213 5.443 23.775 49.029 1.00 31.40 O ANISOU 1592 O TYR B 213 4278 3628 4023 -22 513 -482 O ATOM 1593 CB TYR A 213 8.669 24.540 49.689 1.00 31.84 C ANISOU 1593 CB TYR B 213 4266 3701 4130 -44 564 -575 C ATOM 1594 CG TYR A 213 8.348 23.414 50.624 1.00 32.16 C ANISOU 1594 CG TYR B 213 4369 3702 4147 -78 564 -559 C ATOM 1595 CD1 TYR A 213 7.476 23.596 51.691 1.00 34.60 C ANISOU 1595 CD1 TYR B 213 4738 3963 4447 -90 582 -543 C ATOM 1596 CD2 TYR A 213 8.901 22.161 50.443 1.00 32.50 C ANISOU 1596 CD2 TYR B 213 4413 3757 4178 -98 546 -562 C ATOM 1597 CE1 TYR A 213 7.165 22.550 52.540 1.00 33.40 C ANISOU 1597 CE1 TYR B 213 4641 3779 4270 -119 575 -530 C ATOM 1598 CE2 TYR A 213 8.595 21.113 51.294 1.00 32.72 C ANISOU 1598 CE2 TYR B 213 4497 3754 4183 -124 541 -547 C ATOM 1599 CZ TYR A 213 7.721 21.306 52.325 1.00 31.88 C ANISOU 1599 CZ TYR B 213 4445 3603 4065 -134 553 -532 C ATOM 1600 OH TYR A 213 7.429 20.247 53.166 1.00 33.00 O ANISOU 1600 OH TYR B 213 4639 3718 4182 -158 543 -520 O ATOM 1601 N LEU A 214 5.895 25.876 49.765 1.00 31.50 N ANISOU 1601 N LEU B 214 4277 3618 4073 4 566 -511 N ATOM 1602 CA LEU A 214 4.546 26.147 50.245 1.00 31.59 C ANISOU 1602 CA LEU B 214 4340 3589 4073 6 575 -481 C ATOM 1603 C LEU A 214 3.488 26.137 49.152 1.00 30.70 C ANISOU 1603 C LEU B 214 4222 3497 3946 37 549 -447 C ATOM 1604 O LEU A 214 2.411 25.606 49.366 1.00 29.08 O ANISOU 1604 O LEU B 214 4061 3266 3722 22 545 -421 O ATOM 1605 CB LEU A 214 4.521 27.489 50.999 1.00 32.12 C ANISOU 1605 CB LEU B 214 4418 3624 4162 20 618 -493 C ATOM 1606 CG LEU A 214 4.664 27.498 52.522 1.00 33.43 C ANISOU 1606 CG LEU B 214 4638 3735 4329 -17 655 -507 C ATOM 1607 CD1 LEU A 214 5.505 26.396 53.138 1.00 33.85 C ANISOU 1607 CD1 LEU B 214 4708 3782 4371 -58 652 -524 C ATOM 1608 CD2 LEU A 214 5.118 28.898 52.993 1.00 33.57 C ANISOU 1608 CD2 LEU B 214 4639 3737 4378 2 700 -531 C ATOM 1609 N MET A 215 3.779 26.733 47.997 1.00 30.49 N ANISOU 1609 N MET B 215 4143 3516 3926 79 534 -448 N ATOM 1610 CA MET A 215 2.886 26.619 46.841 1.00 32.54 C ANISOU 1610 CA MET B 215 4399 3798 4166 110 509 -415 C ATOM 1611 C MET A 215 2.599 25.153 46.431 1.00 29.36 C ANISOU 1611 C MET B 215 4009 3406 3741 82 481 -400 C ATOM 1612 O MET A 215 1.453 24.815 46.116 1.00 28.78 O ANISOU 1612 O MET B 215 3966 3319 3650 84 477 -368 O ATOM 1613 CB MET A 215 3.463 27.328 45.621 1.00 32.14 C ANISOU 1613 CB MET B 215 4288 3803 4122 160 489 -424 C ATOM 1614 CG MET A 215 3.212 28.813 45.511 1.00 38.52 C ANISOU 1614 CG MET B 215 5082 4610 4944 210 505 -421 C ATOM 1615 SD MET A 215 3.786 29.434 43.884 1.00 41.80 S ANISOU 1615 SD MET B 215 5425 5102 5356 272 467 -428 S ATOM 1616 CE MET A 215 2.744 28.389 42.828 1.00 42.42 C ANISOU 1616 CE MET B 215 5538 5189 5392 277 439 -383 C ATOM 1617 N ALA A 216 3.639 24.314 46.418 1.00 26.18 N ANISOU 1617 N ALA B 216 3582 3027 3340 57 467 -423 N ATOM 1618 CA ALA A 216 3.511 22.882 46.100 1.00 25.05 C ANISOU 1618 CA ALA B 216 3446 2894 3178 31 443 -413 C ATOM 1619 C ALA A 216 2.710 22.123 47.166 1.00 23.80 C ANISOU 1619 C ALA B 216 3342 2689 3010 -8 450 -399 C ATOM 1620 O ALA A 216 1.800 21.354 46.858 1.00 23.88 O ANISOU 1620 O ALA B 216 3370 2696 3006 -18 437 -376 O ATOM 1621 CB ALA A 216 4.898 22.262 45.968 1.00 23.88 C ANISOU 1621 CB ALA B 216 3261 2775 3036 16 433 -444 C ATOM 1622 N LEU A 217 3.059 22.354 48.425 1.00 22.50 N ANISOU 1622 N LEU B 217 3204 2489 2854 -31 473 -417 N ATOM 1623 CA LEU A 217 2.337 21.758 49.538 1.00 22.57 C ANISOU 1623 CA LEU B 217 3268 2455 2852 -66 479 -409 C ATOM 1624 C LEU A 217 0.842 22.126 49.542 1.00 22.08 C ANISOU 1624 C LEU B 217 3241 2366 2783 -62 487 -382 C ATOM 1625 O LEU A 217 0.005 21.222 49.564 1.00 20.75 O ANISOU 1625 O LEU B 217 3094 2190 2602 -84 472 -366 O ATOM 1626 CB LEU A 217 2.990 22.113 50.880 1.00 22.15 C ANISOU 1626 CB LEU B 217 3243 2366 2805 -86 506 -432 C ATOM 1627 CG LEU A 217 2.262 21.588 52.127 1.00 24.26 C ANISOU 1627 CG LEU B 217 3572 2588 3056 -121 511 -427 C ATOM 1628 CD1 LEU A 217 2.238 20.031 52.150 1.00 23.77 C ANISOU 1628 CD1 LEU B 217 3516 2539 2976 -146 477 -421 C ATOM 1629 CD2 LEU A 217 2.885 22.158 53.411 1.00 23.81 C ANISOU 1629 CD2 LEU B 217 3550 2495 3004 -135 545 -449 C ATOM 1630 N ASP A 218 0.514 23.428 49.508 1.00 22.10 N ANISOU 1630 N ASP B 218 3247 2353 2796 -33 511 -377 N ATOM 1631 CA ASP A 218 -0.894 23.870 49.377 1.00 23.67 C ANISOU 1631 CA ASP B 218 3480 2525 2990 -24 525 -350 C ATOM 1632 C ASP A 218 -1.585 23.192 48.212 1.00 23.74 C ANISOU 1632 C ASP B 218 3477 2559 2986 -16 502 -325 C ATOM 1633 O ASP A 218 -2.737 22.768 48.305 1.00 22.97 O ANISOU 1633 O ASP B 218 3413 2436 2879 -35 506 -307 O ATOM 1634 CB ASP A 218 -0.992 25.379 49.063 1.00 25.00 C ANISOU 1634 CB ASP B 218 3640 2689 3172 23 549 -345 C ATOM 1635 CG ASP A 218 -0.622 26.271 50.242 1.00 25.19 C ANISOU 1635 CG ASP B 218 3684 2676 3211 17 583 -366 C ATOM 1636 OD1 ASP A 218 -0.498 25.732 51.355 1.00 26.27 O ANISOU 1636 OD1 ASP B 218 3854 2785 3342 -24 590 -380 O ATOM 1637 OD2 ASP A 218 -0.400 27.509 50.022 1.00 26.10 O ANISOU 1637 OD2 ASP B 218 3779 2795 3343 58 603 -369 O ATOM 1638 N SER A 219 -0.894 23.170 47.078 1.00 23.41 N ANISOU 1638 N SER B 219 3387 2565 2944 14 483 -326 N ATOM 1639 CA SER A 219 -1.513 22.711 45.853 1.00 24.72 C ANISOU 1639 CA SER B 219 3543 2755 3096 30 467 -301 C ATOM 1640 C SER A 219 -1.757 21.208 45.870 1.00 23.42 C ANISOU 1640 C SER B 219 3382 2595 2922 -11 447 -299 C ATOM 1641 O SER A 219 -2.848 20.766 45.539 1.00 24.16 O ANISOU 1641 O SER B 219 3497 2676 3007 -21 450 -277 O ATOM 1642 CB SER A 219 -0.713 23.143 44.625 1.00 25.00 C ANISOU 1642 CB SER B 219 3528 2842 3129 75 450 -304 C ATOM 1643 OG SER A 219 -1.334 22.626 43.465 1.00 30.31 O ANISOU 1643 OG SER B 219 4197 3534 3783 89 437 -279 O ATOM 1644 N CYS A 220 -0.752 20.426 46.273 1.00 22.96 N ANISOU 1644 N CYS B 220 3304 2553 2866 -33 430 -322 N ATOM 1645 CA CYS A 220 -0.949 18.988 46.512 1.00 21.35 C ANISOU 1645 CA CYS B 220 3106 2351 2656 -71 411 -322 C ATOM 1646 C CYS A 220 -2.095 18.713 47.491 1.00 22.14 C ANISOU 1646 C CYS B 220 3252 2406 2753 -105 421 -316 C ATOM 1647 O CYS A 220 -2.939 17.853 47.228 1.00 21.91 O ANISOU 1647 O CYS B 220 3228 2376 2719 -125 412 -304 O ATOM 1648 CB CYS A 220 0.334 18.326 47.006 1.00 20.61 C ANISOU 1648 CB CYS B 220 2993 2271 2565 -86 397 -348 C ATOM 1649 SG CYS A 220 1.648 18.279 45.727 1.00 19.54 S ANISOU 1649 SG CYS B 220 2800 2193 2432 -57 382 -360 S ATOM 1650 N TYR A 221 -2.138 19.436 48.611 1.00 21.72 N ANISOU 1650 N TYR B 221 3232 2317 2703 -114 440 -326 N ATOM 1651 CA TYR A 221 -3.214 19.231 49.600 1.00 22.43 C ANISOU 1651 CA TYR B 221 3370 2364 2788 -149 449 -324 C ATOM 1652 C TYR A 221 -4.603 19.495 49.025 1.00 23.45 C ANISOU 1652 C TYR B 221 3518 2476 2918 -147 465 -301 C ATOM 1653 O TYR A 221 -5.508 18.691 49.185 1.00 23.60 O ANISOU 1653 O TYR B 221 3551 2483 2933 -180 459 -297 O ATOM 1654 CB TYR A 221 -2.953 20.092 50.811 1.00 22.67 C ANISOU 1654 CB TYR B 221 3435 2358 2821 -154 472 -339 C ATOM 1655 CG TYR A 221 -3.858 19.866 52.004 1.00 22.08 C ANISOU 1655 CG TYR B 221 3412 2240 2737 -193 479 -345 C ATOM 1656 CD1 TYR A 221 -3.982 18.607 52.572 1.00 20.64 C ANISOU 1656 CD1 TYR B 221 3238 2062 2543 -229 450 -354 C ATOM 1657 CD2 TYR A 221 -4.521 20.931 52.598 1.00 22.70 C ANISOU 1657 CD2 TYR B 221 3532 2275 2818 -192 513 -343 C ATOM 1658 CE1 TYR A 221 -4.739 18.386 53.704 1.00 20.38 C ANISOU 1658 CE1 TYR B 221 3251 1994 2499 -264 451 -364 C ATOM 1659 CE2 TYR A 221 -5.337 20.718 53.737 1.00 24.70 C ANISOU 1659 CE2 TYR B 221 3836 2489 3060 -231 519 -352 C ATOM 1660 CZ TYR A 221 -5.419 19.440 54.287 1.00 22.46 C ANISOU 1660 CZ TYR B 221 3557 2213 2762 -268 486 -364 C ATOM 1661 OH TYR A 221 -6.214 19.187 55.379 1.00 24.60 O ANISOU 1661 OH TYR B 221 3876 2451 3020 -306 486 -376 O ATOM 1662 N LYS A 222 -4.736 20.608 48.307 1.00 25.38 N ANISOU 1662 N LYS B 222 3759 2719 3165 -107 487 -285 N ATOM 1663 CA LYS A 222 -5.966 21.029 47.609 1.00 27.77 C ANISOU 1663 CA LYS B 222 4083 3003 3465 -93 509 -259 C ATOM 1664 C LYS A 222 -6.436 19.949 46.640 1.00 26.09 C ANISOU 1664 C LYS B 222 3852 2814 3247 -104 493 -246 C ATOM 1665 O LYS A 222 -7.609 19.566 46.656 1.00 26.41 O ANISOU 1665 O LYS B 222 3919 2829 3288 -131 507 -236 O ATOM 1666 CB LYS A 222 -5.674 22.376 46.879 1.00 28.67 C ANISOU 1666 CB LYS B 222 4187 3125 3582 -35 526 -246 C ATOM 1667 CG LYS A 222 -6.768 22.990 45.985 1.00 32.70 C ANISOU 1667 CG LYS B 222 4721 3619 4086 -4 551 -214 C ATOM 1668 CD LYS A 222 -6.213 23.649 44.617 1.00 33.69 C ANISOU 1668 CD LYS B 222 4810 3786 4203 60 541 -197 C ATOM 1669 CE LYS A 222 -4.780 24.301 44.711 1.00 39.31 C ANISOU 1669 CE LYS B 222 5478 4533 4924 90 524 -221 C ATOM 1670 NZ LYS A 222 -4.005 24.365 43.403 1.00 40.22 N ANISOU 1670 NZ LYS B 222 5545 4706 5029 134 498 -217 N ATOM 1671 N HIS A 223 -5.516 19.434 45.812 1.00 25.07 N ANISOU 1671 N HIS B 223 3677 2733 3115 -86 468 -248 N ATOM 1672 CA HIS A 223 -5.842 18.369 44.854 1.00 23.87 C ANISOU 1672 CA HIS B 223 3505 2607 2958 -95 455 -237 C ATOM 1673 C HIS A 223 -6.285 17.081 45.518 1.00 22.43 C ANISOU 1673 C HIS B 223 3325 2416 2780 -147 441 -249 C ATOM 1674 O HIS A 223 -7.298 16.482 45.114 1.00 21.69 O ANISOU 1674 O HIS B 223 3238 2315 2688 -168 450 -238 O ATOM 1675 CB HIS A 223 -4.693 18.141 43.873 1.00 25.06 C ANISOU 1675 CB HIS B 223 3609 2810 3103 -64 432 -240 C ATOM 1676 CG HIS A 223 -4.526 19.269 42.902 1.00 29.52 C ANISOU 1676 CG HIS B 223 4167 3389 3659 -10 441 -224 C ATOM 1677 ND1 HIS A 223 -5.538 19.683 42.066 1.00 34.85 N ANISOU 1677 ND1 HIS B 223 4866 4052 4324 13 463 -195 N ATOM 1678 CD2 HIS A 223 -3.464 20.052 42.612 1.00 34.09 C ANISOU 1678 CD2 HIS B 223 4718 3996 4237 27 432 -235 C ATOM 1679 CE1 HIS A 223 -5.120 20.694 41.329 1.00 34.40 C ANISOU 1679 CE1 HIS B 223 4798 4015 4257 66 463 -186 C ATOM 1680 NE2 HIS A 223 -3.866 20.942 41.644 1.00 34.07 N ANISOU 1680 NE2 HIS B 223 4721 4000 4223 75 443 -211 N ATOM 1681 N LEU A 224 -5.576 16.703 46.576 1.00 20.38 N ANISOU 1681 N LEU B 224 3064 2158 2524 -168 422 -272 N ATOM 1682 CA LEU A 224 -5.929 15.528 47.383 1.00 19.26 C ANISOU 1682 CA LEU B 224 2925 2010 2383 -213 402 -287 C ATOM 1683 C LEU A 224 -7.300 15.695 48.080 1.00 21.59 C ANISOU 1683 C LEU B 224 3261 2260 2680 -247 422 -287 C ATOM 1684 O LEU A 224 -8.126 14.754 48.100 1.00 21.74 O ANISOU 1684 O LEU B 224 3277 2278 2704 -282 415 -290 O ATOM 1685 CB LEU A 224 -4.793 15.174 48.400 1.00 18.74 C ANISOU 1685 CB LEU B 224 2856 1951 2314 -221 379 -310 C ATOM 1686 CG LEU A 224 -5.114 14.036 49.390 1.00 20.23 C ANISOU 1686 CG LEU B 224 3053 2133 2499 -262 354 -326 C ATOM 1687 CD1 LEU A 224 -5.692 13.021 48.571 1.00 26.47 C ANISOU 1687 CD1 LEU B 224 3815 2946 3297 -273 343 -318 C ATOM 1688 CD2 LEU A 224 -4.033 13.404 50.396 1.00 8.20 C ANISOU 1688 CD2 LEU B 224 1531 617 967 -269 327 -346 C ATOM 1689 N CYS A 225 -7.526 16.867 48.675 1.00 22.42 N ANISOU 1689 N CYS B 225 3405 2329 2784 -239 448 -286 N ATOM 1690 CA CYS A 225 -8.824 17.190 49.259 1.00 24.49 C ANISOU 1690 CA CYS B 225 3711 2546 3048 -269 474 -286 C ATOM 1691 C CYS A 225 -9.934 17.077 48.236 1.00 24.87 C ANISOU 1691 C CYS B 225 3762 2587 3102 -271 497 -266 C ATOM 1692 O CYS A 225 -10.983 16.525 48.558 1.00 26.54 O ANISOU 1692 O CYS B 225 3988 2777 3319 -314 504 -274 O ATOM 1693 CB CYS A 225 -8.839 18.618 49.886 1.00 23.91 C ANISOU 1693 CB CYS B 225 3679 2433 2973 -250 505 -285 C ATOM 1694 SG CYS A 225 -7.777 18.742 51.392 1.00 27.91 S ANISOU 1694 SG CYS B 225 4199 2932 3471 -261 489 -313 S ATOM 1695 N ASN A 226 -9.736 17.619 47.036 1.00 26.11 N ANISOU 1695 N ASN B 226 3906 2759 3256 -227 511 -242 N ATOM 1696 CA ASN A 226 -10.741 17.523 45.959 1.00 28.37 C ANISOU 1696 CA ASN B 226 4198 3037 3543 -224 537 -219 C ATOM 1697 C ASN A 226 -11.071 16.092 45.608 1.00 28.47 C ANISOU 1697 C ASN B 226 4182 3072 3564 -260 520 -226 C ATOM 1698 O ASN A 226 -12.240 15.713 45.542 1.00 28.98 O ANISOU 1698 O ASN B 226 4263 3112 3637 -294 543 -225 O ATOM 1699 CB ASN A 226 -10.296 18.256 44.686 1.00 29.66 C ANISOU 1699 CB ASN B 226 4351 3222 3697 -163 546 -192 C ATOM 1700 CG ASN A 226 -10.252 19.769 44.858 1.00 34.22 C ANISOU 1700 CG ASN B 226 4959 3773 4270 -122 571 -180 C ATOM 1701 OD1 ASN A 226 -10.861 20.338 45.776 1.00 38.73 O ANISOU 1701 OD1 ASN B 226 5571 4299 4846 -140 594 -186 O ATOM 1702 ND2 ASN A 226 -9.495 20.434 43.980 1.00 40.31 N ANISOU 1702 ND2 ASN B 226 5710 4575 5032 -66 564 -166 N ATOM 1703 N LYS A 227 -10.034 15.283 45.423 1.00 28.04 N ANISOU 1703 N LYS B 227 4083 3064 3508 -254 483 -236 N ATOM 1704 CA LYS A 227 -10.199 13.856 45.227 1.00 27.77 C ANISOU 1704 CA LYS B 227 4014 3054 3483 -286 462 -247 C ATOM 1705 C LYS A 227 -10.968 13.188 46.391 1.00 27.89 C ANISOU 1705 C LYS B 227 4040 3048 3508 -342 453 -272 C ATOM 1706 O LYS A 227 -11.885 12.395 46.165 1.00 26.37 O ANISOU 1706 O LYS B 227 3837 2852 3329 -377 460 -277 O ATOM 1707 CB LYS A 227 -8.814 13.208 44.996 1.00 28.58 C ANISOU 1707 CB LYS B 227 4073 3205 3582 -265 424 -255 C ATOM 1708 CG LYS A 227 -8.285 13.521 43.589 1.00 27.54 C ANISOU 1708 CG LYS B 227 3922 3102 3441 -220 431 -233 C ATOM 1709 CD LYS A 227 -9.152 12.796 42.538 1.00 31.36 C ANISOU 1709 CD LYS B 227 4396 3590 3928 -231 450 -220 C ATOM 1710 CE LYS A 227 -8.749 13.075 41.062 1.00 35.43 C ANISOU 1710 CE LYS B 227 4900 4133 4428 -186 460 -197 C ATOM 1711 NZ LYS A 227 -7.247 13.083 40.838 1.00 39.87 N ANISOU 1711 NZ LYS B 227 5430 4737 4982 -154 428 -206 N ATOM 1712 N PHE A 228 -10.610 13.532 47.628 1.00 27.00 N ANISOU 1712 N PHE B 228 3948 2920 3390 -351 438 -289 N ATOM 1713 CA PHE A 228 -11.338 13.003 48.787 1.00 28.09 C ANISOU 1713 CA PHE B 228 4102 3039 3533 -401 426 -315 C ATOM 1714 C PHE A 228 -12.832 13.336 48.750 1.00 29.00 C ANISOU 1714 C PHE B 228 4251 3112 3658 -434 466 -314 C ATOM 1715 O PHE A 228 -13.666 12.471 48.992 1.00 28.84 O ANISOU 1715 O PHE B 228 4219 3090 3650 -480 461 -332 O ATOM 1716 CB PHE A 228 -10.759 13.544 50.059 1.00 26.10 C ANISOU 1716 CB PHE B 228 3880 2770 3267 -400 413 -330 C ATOM 1717 CG PHE A 228 -11.285 12.878 51.294 1.00 26.45 C ANISOU 1717 CG PHE B 228 3937 2803 3308 -448 389 -359 C ATOM 1718 CD1 PHE A 228 -10.786 11.631 51.703 1.00 25.64 C ANISOU 1718 CD1 PHE B 228 3802 2736 3203 -460 341 -376 C ATOM 1719 CD2 PHE A 228 -12.234 13.504 52.076 1.00 24.84 C ANISOU 1719 CD2 PHE B 228 3781 2554 3102 -477 413 -370 C ATOM 1720 CE1 PHE A 228 -11.224 11.034 52.863 1.00 26.06 C ANISOU 1720 CE1 PHE B 228 3867 2783 3249 -498 313 -404 C ATOM 1721 CE2 PHE A 228 -12.676 12.919 53.257 1.00 25.08 C ANISOU 1721 CE2 PHE B 228 3826 2577 3125 -520 387 -401 C ATOM 1722 CZ PHE A 228 -12.169 11.682 53.655 1.00 26.28 C ANISOU 1722 CZ PHE B 228 3943 2769 3273 -530 335 -418 C ATOM 1723 N GLU A 229 -13.153 14.590 48.445 1.00 31.35 N ANISOU 1723 N GLU B 229 4587 3375 3951 -409 508 -293 N ATOM 1724 CA GLU A 229 -14.546 15.025 48.367 1.00 34.34 C ANISOU 1724 CA GLU B 229 5004 3705 4337 -436 555 -289 C ATOM 1725 C GLU A 229 -15.320 14.198 47.337 1.00 34.44 C ANISOU 1725 C GLU B 229 4994 3727 4364 -455 572 -282 C ATOM 1726 O GLU A 229 -16.454 13.783 47.603 1.00 35.07 O ANISOU 1726 O GLU B 229 5085 3782 4459 -506 592 -299 O ATOM 1727 CB GLU A 229 -14.623 16.522 48.073 1.00 34.03 C ANISOU 1727 CB GLU B 229 5009 3630 4289 -393 597 -263 C ATOM 1728 CG GLU A 229 -15.770 17.230 48.788 1.00 38.54 C ANISOU 1728 CG GLU B 229 5640 4141 4864 -423 639 -270 C ATOM 1729 CD GLU A 229 -15.904 18.707 48.406 1.00 39.53 C ANISOU 1729 CD GLU B 229 5809 4230 4982 -374 684 -241 C ATOM 1730 OE1 GLU A 229 -15.075 19.218 47.602 1.00 46.56 O ANISOU 1730 OE1 GLU B 229 6681 5146 5865 -315 679 -216 O ATOM 1731 OE2 GLU A 229 -16.860 19.362 48.890 1.00 45.13 O ANISOU 1731 OE2 GLU B 229 6570 4883 5694 -393 726 -243 O ATOM 1732 N LYS A 230 -14.714 13.925 46.175 1.00 34.57 N ANISOU 1732 N LYS B 230 4978 3780 4378 -419 567 -261 N ATOM 1733 CA LYS A 230 -15.348 13.027 45.193 1.00 35.61 C ANISOU 1733 CA LYS B 230 5084 3923 4523 -437 583 -255 C ATOM 1734 C LYS A 230 -15.459 11.586 45.690 1.00 34.80 C ANISOU 1734 C LYS B 230 4935 3849 4439 -486 547 -288 C ATOM 1735 O LYS A 230 -16.481 10.947 45.490 1.00 34.84 O ANISOU 1735 O LYS B 230 4931 3842 4463 -529 568 -299 O ATOM 1736 CB LYS A 230 -14.643 13.055 43.822 1.00 35.76 C ANISOU 1736 CB LYS B 230 5081 3975 4531 -386 585 -226 C ATOM 1737 CG LYS A 230 -14.787 14.376 43.077 1.00 37.56 C ANISOU 1737 CG LYS B 230 5353 4177 4741 -336 624 -191 C ATOM 1738 CD LYS A 230 -13.902 14.387 41.826 1.00 39.13 C ANISOU 1738 CD LYS B 230 5526 4417 4924 -282 614 -168 C ATOM 1739 CE LYS A 230 -13.342 15.794 41.532 1.00 43.55 C ANISOU 1739 CE LYS B 230 6112 4973 5462 -220 620 -144 C ATOM 1740 NZ LYS A 230 -11.840 15.701 41.308 1.00 47.56 N ANISOU 1740 NZ LYS B 230 6576 5534 5959 -183 574 -150 N ATOM 1741 N LEU A 231 -14.422 11.088 46.350 1.00 33.97 N ANISOU 1741 N LEU B 231 4801 3779 4328 -479 494 -304 N ATOM 1742 CA LEU A 231 -14.376 9.710 46.806 1.00 33.94 C ANISOU 1742 CA LEU B 231 4750 3808 4338 -513 453 -333 C ATOM 1743 C LEU A 231 -15.374 9.473 47.910 1.00 34.52 C ANISOU 1743 C LEU B 231 4838 3855 4421 -569 450 -365 C ATOM 1744 O LEU A 231 -16.177 8.563 47.822 1.00 34.29 O ANISOU 1744 O LEU B 231 4780 3833 4414 -612 451 -384 O ATOM 1745 CB LEU A 231 -12.987 9.374 47.348 1.00 34.43 C ANISOU 1745 CB LEU B 231 4789 3906 4386 -486 400 -339 C ATOM 1746 CG LEU A 231 -11.915 8.579 46.578 1.00 35.78 C ANISOU 1746 CG LEU B 231 4912 4125 4557 -454 374 -331 C ATOM 1747 CD1 LEU A 231 -12.262 8.252 45.108 1.00 37.88 C ANISOU 1747 CD1 LEU B 231 5155 4404 4834 -445 405 -312 C ATOM 1748 CD2 LEU A 231 -10.553 9.281 46.704 1.00 35.38 C ANISOU 1748 CD2 LEU B 231 4873 4086 4486 -407 359 -320 C ATOM 1749 N GLU A 232 -15.291 10.281 48.970 1.00 34.11 N ANISOU 1749 N GLU B 232 4830 3777 4354 -571 445 -373 N ATOM 1750 CA GLU A 232 -16.034 9.990 50.190 1.00 34.98 C ANISOU 1750 CA GLU B 232 4954 3870 4467 -623 430 -409 C ATOM 1751 C GLU A 232 -17.220 10.942 50.420 1.00 33.88 C ANISOU 1751 C GLU B 232 4871 3671 4332 -652 483 -411 C ATOM 1752 O GLU A 232 -17.985 10.768 51.368 1.00 33.89 O ANISOU 1752 O GLU B 232 4888 3653 4335 -701 477 -443 O ATOM 1753 CB GLU A 232 -15.089 9.975 51.398 1.00 34.96 C ANISOU 1753 CB GLU B 232 4962 3881 4442 -611 380 -423 C ATOM 1754 CG GLU A 232 -13.989 8.899 51.343 1.00 36.11 C ANISOU 1754 CG GLU B 232 5055 4080 4584 -588 327 -426 C ATOM 1755 CD GLU A 232 -13.455 8.531 52.732 1.00 38.30 C ANISOU 1755 CD GLU B 232 5344 4369 4841 -595 276 -451 C ATOM 1756 OE1 GLU A 232 -14.017 8.997 53.764 1.00 41.27 O ANISOU 1756 OE1 GLU B 232 5764 4713 5205 -623 278 -470 O ATOM 1757 OE2 GLU A 232 -12.448 7.788 52.805 1.00 43.64 O ANISOU 1757 OE2 GLU B 232 5991 5082 5510 -570 236 -450 O ATOM 1758 N GLY A 233 -17.365 11.938 49.555 1.00 32.89 N ANISOU 1758 N GLY B 233 4776 3517 4203 -620 533 -377 N ATOM 1759 CA GLY A 233 -18.527 12.844 49.608 1.00 34.00 C ANISOU 1759 CA GLY B 233 4973 3597 4349 -642 593 -374 C ATOM 1760 C GLY A 233 -18.551 13.783 50.805 1.00 34.55 C ANISOU 1760 C GLY B 233 5097 3630 4402 -647 596 -386 C ATOM 1761 O GLY A 233 -19.620 14.247 51.221 1.00 33.54 O ANISOU 1761 O GLY B 233 5012 3451 4279 -684 635 -399 O ATOM 1762 N LYS A 234 -17.365 14.049 51.364 1.00 33.85 N ANISOU 1762 N LYS B 234 5006 3562 4294 -611 559 -383 N ATOM 1763 CA LYS A 234 -17.204 15.003 52.451 1.00 35.05 C ANISOU 1763 CA LYS B 234 5208 3680 4428 -608 564 -392 C ATOM 1764 C LYS A 234 -15.877 15.721 52.291 1.00 33.81 C ANISOU 1764 C LYS B 234 5050 3540 4256 -545 554 -367 C ATOM 1765 O LYS A 234 -14.952 15.191 51.697 1.00 33.17 O ANISOU 1765 O LYS B 234 4923 3504 4175 -516 524 -356 O ATOM 1766 CB LYS A 234 -17.265 14.308 53.815 1.00 35.77 C ANISOU 1766 CB LYS B 234 5301 3779 4510 -653 520 -433 C ATOM 1767 CG LYS A 234 -16.280 13.178 54.004 1.00 40.14 C ANISOU 1767 CG LYS B 234 5802 4391 5057 -644 456 -443 C ATOM 1768 CD LYS A 234 -16.634 12.349 55.243 1.00 46.17 C ANISOU 1768 CD LYS B 234 6566 5163 5812 -693 412 -486 C ATOM 1769 CE LYS A 234 -15.670 11.168 55.409 1.00 47.36 C ANISOU 1769 CE LYS B 234 6668 5373 5956 -679 348 -494 C ATOM 1770 NZ LYS A 234 -15.854 10.444 56.728 1.00 49.52 N ANISOU 1770 NZ LYS B 234 6947 5657 6212 -715 298 -533 N ATOM 1771 N GLU A 235 -15.798 16.922 52.839 1.00 33.12 N ANISOU 1771 N GLU B 235 5012 3414 4160 -527 582 -362 N ATOM 1772 CA GLU A 235 -14.598 17.736 52.774 1.00 32.06 C ANISOU 1772 CA GLU B 235 4877 3291 4015 -471 579 -344 C ATOM 1773 C GLU A 235 -13.511 17.143 53.681 1.00 29.91 C ANISOU 1773 C GLU B 235 4586 3050 3729 -474 528 -365 C ATOM 1774 O GLU A 235 -13.789 16.763 54.822 1.00 29.75 O ANISOU 1774 O GLU B 235 4589 3018 3698 -513 510 -394 O ATOM 1775 CB GLU A 235 -14.939 19.147 53.214 1.00 33.51 C ANISOU 1775 CB GLU B 235 5118 3421 4195 -455 626 -337 C ATOM 1776 CG GLU A 235 -14.188 20.195 52.423 1.00 38.30 C ANISOU 1776 CG GLU B 235 5717 4033 4802 -388 645 -306 C ATOM 1777 CD GLU A 235 -14.526 21.623 52.848 1.00 44.82 C ANISOU 1777 CD GLU B 235 6597 4806 5627 -367 694 -299 C ATOM 1778 OE1 GLU A 235 -14.891 21.843 54.032 1.00 45.86 O ANISOU 1778 OE1 GLU B 235 6771 4901 5753 -401 704 -322 O ATOM 1779 OE2 GLU A 235 -14.401 22.522 51.983 1.00 47.16 O ANISOU 1779 OE2 GLU B 235 6894 5099 5928 -314 720 -270 O ATOM 1780 N PHE A 236 -12.290 17.042 53.163 1.00 27.75 N ANISOU 1780 N PHE B 236 4275 2816 3452 -432 506 -352 N ATOM 1781 CA PHE A 236 -11.149 16.536 53.946 1.00 26.73 C ANISOU 1781 CA PHE B 236 4133 2713 3310 -429 465 -369 C ATOM 1782 C PHE A 236 -10.653 17.576 54.931 1.00 26.44 C ANISOU 1782 C PHE B 236 4140 2644 3260 -417 483 -376 C ATOM 1783 O PHE A 236 -10.648 18.770 54.634 1.00 27.54 O ANISOU 1783 O PHE B 236 4298 2760 3406 -387 522 -361 O ATOM 1784 CB PHE A 236 -9.992 16.122 52.997 1.00 25.19 C ANISOU 1784 CB PHE B 236 3885 2568 3119 -391 442 -354 C ATOM 1785 CG PHE A 236 -8.880 15.317 53.674 1.00 24.90 C ANISOU 1785 CG PHE B 236 3832 2559 3070 -391 400 -370 C ATOM 1786 CD1 PHE A 236 -8.926 13.935 53.704 1.00 22.12 C ANISOU 1786 CD1 PHE B 236 3449 2239 2717 -413 359 -381 C ATOM 1787 CD2 PHE A 236 -7.769 15.966 54.265 1.00 25.64 C ANISOU 1787 CD2 PHE B 236 3941 2647 3153 -367 404 -374 C ATOM 1788 CE1 PHE A 236 -7.879 13.178 54.311 1.00 20.54 C ANISOU 1788 CE1 PHE B 236 3238 2062 2503 -407 321 -393 C ATOM 1789 CE2 PHE A 236 -6.724 15.224 54.859 1.00 23.45 C ANISOU 1789 CE2 PHE B 236 3656 2392 2863 -366 370 -387 C ATOM 1790 CZ PHE A 236 -6.805 13.828 54.902 1.00 22.54 C ANISOU 1790 CZ PHE B 236 3515 2306 2744 -384 329 -395 C ATOM 1791 N SER A 237 -10.232 17.134 56.107 1.00 26.61 N ANISOU 1791 N SER B 237 4180 2665 3264 -437 456 -399 N ATOM 1792 CA SER A 237 -9.427 17.963 56.981 1.00 26.09 C ANISOU 1792 CA SER B 237 4149 2579 3186 -421 471 -405 C ATOM 1793 C SER A 237 -8.367 17.111 57.645 1.00 25.77 C ANISOU 1793 C SER B 237 4099 2564 3127 -422 430 -419 C ATOM 1794 O SER A 237 -8.347 15.901 57.532 1.00 25.77 O ANISOU 1794 O SER B 237 4071 2598 3124 -435 389 -425 O ATOM 1795 CB SER A 237 -10.290 18.666 58.068 1.00 26.85 C ANISOU 1795 CB SER B 237 4311 2621 3271 -450 500 -421 C ATOM 1796 OG SER A 237 -10.620 17.758 59.123 1.00 27.18 O ANISOU 1796 OG SER B 237 4375 2662 3291 -492 465 -448 O ATOM 1797 N ILE A 238 -7.500 17.762 58.381 1.00 26.02 N ANISOU 1797 N ILE B 238 4160 2579 3148 -406 445 -425 N ATOM 1798 CA ILE A 238 -6.484 17.081 59.189 1.00 26.98 C ANISOU 1798 CA ILE B 238 4290 2714 3247 -407 415 -438 C ATOM 1799 C ILE A 238 -7.049 15.940 60.052 1.00 27.51 C ANISOU 1799 C ILE B 238 4377 2786 3290 -443 372 -457 C ATOM 1800 O ILE A 238 -6.322 15.011 60.382 1.00 27.07 O ANISOU 1800 O ILE B 238 4312 2755 3218 -439 335 -462 O ATOM 1801 CB ILE A 238 -5.709 18.174 60.015 1.00 28.38 C ANISOU 1801 CB ILE B 238 4511 2857 3416 -392 453 -445 C ATOM 1802 CG1 ILE A 238 -4.358 18.388 59.421 1.00 27.94 C ANISOU 1802 CG1 ILE B 238 4418 2825 3374 -356 461 -437 C ATOM 1803 CG2 ILE A 238 -5.844 18.080 61.609 1.00 30.20 C ANISOU 1803 CG2 ILE B 238 4810 3052 3610 -420 450 -467 C ATOM 1804 CD1 ILE A 238 -4.462 18.762 58.015 1.00 28.93 C ANISOU 1804 CD1 ILE B 238 4490 2974 3528 -331 470 -419 C ATOM 1805 N ASN A 239 -8.342 16.016 60.411 1.00 27.43 N ANISOU 1805 N ASN B 239 4392 2752 3276 -478 376 -468 N ATOM 1806 CA ASN A 239 -9.007 14.983 61.222 1.00 28.02 C ANISOU 1806 CA ASN B 239 4483 2835 3330 -516 333 -491 C ATOM 1807 C ASN A 239 -9.241 13.693 60.445 1.00 28.04 C ANISOU 1807 C ASN B 239 4423 2885 3347 -522 290 -489 C ATOM 1808 O ASN A 239 -9.516 12.662 61.049 1.00 28.84 O ANISOU 1808 O ASN B 239 4522 3005 3431 -544 244 -508 O ATOM 1809 CB ASN A 239 -10.399 15.461 61.713 1.00 28.85 C ANISOU 1809 CB ASN B 239 4627 2900 3432 -556 354 -508 C ATOM 1810 CG ASN A 239 -10.321 16.575 62.769 1.00 32.64 C ANISOU 1810 CG ASN B 239 5179 3330 3892 -559 392 -517 C ATOM 1811 OD1 ASN A 239 -9.406 16.614 63.600 1.00 35.89 O ANISOU 1811 OD1 ASN B 239 5622 3737 4278 -546 385 -523 O ATOM 1812 ND2 ASN A 239 -11.307 17.476 62.741 1.00 37.00 N ANISOU 1812 ND2 ASN B 239 5762 3842 4457 -576 436 -519 N ATOM 1813 N ASP A 240 -9.189 13.744 59.112 1.00 27.09 N ANISOU 1813 N ASP B 240 4252 2785 3256 -503 304 -467 N ATOM 1814 CA ASP A 240 -9.429 12.534 58.305 1.00 26.72 C ANISOU 1814 CA ASP B 240 4146 2782 3226 -509 270 -465 C ATOM 1815 C ASP A 240 -8.219 11.640 58.047 1.00 26.20 C ANISOU 1815 C ASP B 240 4043 2757 3156 -479 235 -458 C ATOM 1816 O ASP A 240 -8.334 10.614 57.357 1.00 25.62 O ANISOU 1816 O ASP B 240 3918 2721 3096 -480 208 -456 O ATOM 1817 CB ASP A 240 -10.114 12.902 56.991 1.00 27.29 C ANISOU 1817 CB ASP B 240 4188 2854 3329 -506 304 -447 C ATOM 1818 CG ASP A 240 -11.420 13.590 57.231 1.00 27.18 C ANISOU 1818 CG ASP B 240 4211 2798 3321 -539 338 -455 C ATOM 1819 OD1 ASP A 240 -12.315 12.937 57.798 1.00 29.28 O ANISOU 1819 OD1 ASP B 240 4481 3061 3582 -582 317 -480 O ATOM 1820 OD2 ASP A 240 -11.517 14.783 56.908 1.00 28.13 O ANISOU 1820 OD2 ASP B 240 4355 2886 3447 -521 385 -439 O ATOM 1821 N ALA A 241 -7.079 12.004 58.623 1.00 25.50 N ANISOU 1821 N ALA B 241 3981 2659 3047 -454 238 -456 N ATOM 1822 CA ALA A 241 -5.944 11.097 58.619 1.00 25.76 C ANISOU 1822 CA ALA B 241 3992 2725 3072 -430 206 -454 C ATOM 1823 C ALA A 241 -5.400 10.964 60.017 1.00 25.61 C ANISOU 1823 C ALA B 241 4027 2688 3015 -431 189 -467 C ATOM 1824 O ALA A 241 -5.466 11.909 60.817 1.00 24.74 O ANISOU 1824 O ALA B 241 3971 2539 2890 -438 217 -474 O ATOM 1825 CB ALA A 241 -4.843 11.565 57.659 1.00 24.75 C ANISOU 1825 CB ALA B 241 3835 2608 2960 -393 232 -435 C ATOM 1826 N ASP A 242 -4.848 9.792 60.284 1.00 25.03 N ANISOU 1826 N ASP B 242 3940 2643 2927 -420 145 -471 N ATOM 1827 CA ASP A 242 -4.291 9.485 61.585 1.00 26.48 C ANISOU 1827 CA ASP B 242 4177 2814 3070 -415 123 -481 C ATOM 1828 C ASP A 242 -2.881 10.036 61.743 1.00 26.12 C ANISOU 1828 C ASP B 242 4158 2750 3015 -384 155 -471 C ATOM 1829 O ASP A 242 -2.501 10.515 62.824 1.00 26.59 O ANISOU 1829 O ASP B 242 4282 2777 3045 -385 170 -479 O ATOM 1830 CB ASP A 242 -4.357 7.978 61.759 1.00 26.09 C ANISOU 1830 CB ASP B 242 4102 2804 3009 -411 62 -488 C ATOM 1831 CG ASP A 242 -5.782 7.497 61.752 1.00 29.53 C ANISOU 1831 CG ASP B 242 4512 3254 3454 -448 33 -505 C ATOM 1832 OD1 ASP A 242 -6.326 6.983 60.727 1.00 33.10 O ANISOU 1832 OD1 ASP B 242 4900 3734 3940 -455 25 -502 O ATOM 1833 OD2 ASP A 242 -6.405 7.723 62.780 1.00 29.52 O ANISOU 1833 OD2 ASP B 242 4557 3231 3426 -472 23 -524 O ATOM 1834 N TYR A 243 -2.126 9.993 60.644 1.00 24.96 N ANISOU 1834 N TYR B 243 3964 2625 2896 -361 169 -457 N ATOM 1835 CA TYR A 243 -0.755 10.467 60.631 1.00 23.86 C ANISOU 1835 CA TYR B 243 3838 2472 2755 -335 202 -451 C ATOM 1836 C TYR A 243 -0.475 11.216 59.352 1.00 22.58 C ANISOU 1836 C TYR B 243 3629 2321 2631 -323 237 -441 C ATOM 1837 O TYR A 243 -1.037 10.893 58.305 1.00 22.35 O ANISOU 1837 O TYR B 243 3546 2320 2624 -325 225 -433 O ATOM 1838 CB TYR A 243 0.207 9.281 60.773 1.00 24.20 C ANISOU 1838 CB TYR B 243 3877 2536 2783 -313 171 -448 C ATOM 1839 CG TYR A 243 0.063 8.610 62.104 1.00 26.98 C ANISOU 1839 CG TYR B 243 4283 2877 3090 -317 136 -457 C ATOM 1840 CD1 TYR A 243 -0.684 7.437 62.232 1.00 26.59 C ANISOU 1840 CD1 TYR B 243 4213 2858 3033 -323 79 -461 C ATOM 1841 CD2 TYR A 243 0.631 9.179 63.261 1.00 26.96 C ANISOU 1841 CD2 TYR B 243 4356 2834 3055 -314 160 -462 C ATOM 1842 CE1 TYR A 243 -0.866 6.846 63.480 1.00 30.41 C ANISOU 1842 CE1 TYR B 243 4746 3335 3472 -324 40 -471 C ATOM 1843 CE2 TYR A 243 0.464 8.577 64.516 1.00 29.42 C ANISOU 1843 CE2 TYR B 243 4724 3134 3319 -316 126 -470 C ATOM 1844 CZ TYR A 243 -0.292 7.418 64.607 1.00 29.13 C ANISOU 1844 CZ TYR B 243 4664 3133 3273 -319 63 -475 C ATOM 1845 OH TYR A 243 -0.472 6.792 65.823 1.00 31.85 O ANISOU 1845 OH TYR B 243 5061 3473 3567 -317 22 -484 O ATOM 1846 N PHE A 244 0.337 12.261 59.469 1.00 21.72 N ANISOU 1846 N PHE B 244 3539 2188 2526 -312 281 -443 N ATOM 1847 CA PHE A 244 0.871 12.974 58.335 1.00 21.46 C ANISOU 1847 CA PHE B 244 3462 2168 2525 -295 311 -436 C ATOM 1848 C PHE A 244 2.380 12.856 58.365 1.00 21.15 C ANISOU 1848 C PHE B 244 3422 2130 2484 -276 327 -441 C ATOM 1849 O PHE A 244 3.020 13.231 59.363 1.00 20.58 O ANISOU 1849 O PHE B 244 3400 2024 2394 -277 351 -451 O ATOM 1850 CB PHE A 244 0.474 14.456 58.357 1.00 21.72 C ANISOU 1850 CB PHE B 244 3509 2173 2571 -298 354 -438 C ATOM 1851 CG PHE A 244 -0.991 14.708 58.046 1.00 22.32 C ANISOU 1851 CG PHE B 244 3579 2247 2655 -313 349 -431 C ATOM 1852 CD1 PHE A 244 -1.942 14.587 59.041 1.00 21.01 C ANISOU 1852 CD1 PHE B 244 3460 2055 2468 -340 339 -439 C ATOM 1853 CD2 PHE A 244 -1.395 15.074 56.749 1.00 21.57 C ANISOU 1853 CD2 PHE B 244 3436 2172 2586 -301 358 -418 C ATOM 1854 CE1 PHE A 244 -3.285 14.837 58.766 1.00 23.17 C ANISOU 1854 CE1 PHE B 244 3730 2321 2750 -358 341 -436 C ATOM 1855 CE2 PHE A 244 -2.725 15.305 56.442 1.00 21.61 C ANISOU 1855 CE2 PHE B 244 3441 2170 2599 -316 360 -411 C ATOM 1856 CZ PHE A 244 -3.677 15.180 57.433 1.00 23.95 C ANISOU 1856 CZ PHE B 244 3783 2440 2879 -346 353 -420 C ATOM 1857 N VAL A 245 2.935 12.348 57.260 1.00 20.75 N ANISOU 1857 N VAL B 245 3318 2115 2453 -261 318 -436 N ATOM 1858 CA VAL A 245 4.386 12.159 57.084 1.00 19.68 C ANISOU 1858 CA VAL B 245 3174 1983 2320 -245 334 -442 C ATOM 1859 C VAL A 245 4.920 13.006 55.949 1.00 19.75 C ANISOU 1859 C VAL B 245 3133 2010 2360 -232 362 -446 C ATOM 1860 O VAL A 245 4.327 13.068 54.886 1.00 19.22 O ANISOU 1860 O VAL B 245 3022 1972 2310 -227 350 -437 O ATOM 1861 CB VAL A 245 4.729 10.685 56.781 1.00 20.23 C ANISOU 1861 CB VAL B 245 3224 2080 2382 -235 297 -436 C ATOM 1862 CG1 VAL A 245 6.226 10.421 57.038 1.00 17.56 C ANISOU 1862 CG1 VAL B 245 2902 1730 2038 -222 318 -445 C ATOM 1863 CG2 VAL A 245 3.909 9.762 57.666 1.00 20.37 C ANISOU 1863 CG2 VAL B 245 3273 2093 2373 -244 256 -432 C ATOM 1864 N PHE A 246 6.051 13.660 56.183 1.00 19.72 N ANISOU 1864 N PHE B 246 3139 1990 2363 -227 399 -461 N ATOM 1865 CA PHE A 246 6.578 14.630 55.268 1.00 19.92 C ANISOU 1865 CA PHE B 246 3121 2032 2418 -216 427 -471 C ATOM 1866 C PHE A 246 8.023 14.290 54.913 1.00 19.94 C ANISOU 1866 C PHE B 246 3103 2045 2429 -210 442 -487 C ATOM 1867 O PHE A 246 8.770 13.658 55.686 1.00 19.71 O ANISOU 1867 O PHE B 246 3112 1994 2384 -214 449 -492 O ATOM 1868 CB PHE A 246 6.573 16.043 55.883 1.00 19.74 C ANISOU 1868 CB PHE B 246 3121 1977 2403 -220 468 -482 C ATOM 1869 CG PHE A 246 5.200 16.535 56.282 1.00 19.78 C ANISOU 1869 CG PHE B 246 3151 1964 2401 -227 463 -470 C ATOM 1870 CD1 PHE A 246 4.666 16.207 57.530 1.00 18.17 C ANISOU 1870 CD1 PHE B 246 3010 1726 2169 -245 457 -468 C ATOM 1871 CD2 PHE A 246 4.432 17.304 55.389 1.00 18.32 C ANISOU 1871 CD2 PHE B 246 2931 1796 2235 -216 464 -461 C ATOM 1872 CE1 PHE A 246 3.373 16.640 57.905 1.00 18.29 C ANISOU 1872 CE1 PHE B 246 3050 1723 2177 -256 454 -460 C ATOM 1873 CE2 PHE A 246 3.129 17.745 55.753 1.00 19.92 C ANISOU 1873 CE2 PHE B 246 3161 1977 2431 -224 464 -450 C ATOM 1874 CZ PHE A 246 2.608 17.409 57.014 1.00 20.20 C ANISOU 1874 CZ PHE B 246 3256 1977 2440 -246 460 -451 C ATOM 1875 N HIS A 247 8.398 14.764 53.741 1.00 20.46 N ANISOU 1875 N HIS B 247 3112 2143 2519 -198 448 -494 N ATOM 1876 CA HIS A 247 9.782 14.963 53.351 1.00 21.34 C ANISOU 1876 CA HIS B 247 3199 2263 2648 -195 475 -518 C ATOM 1877 C HIS A 247 10.422 15.777 54.467 1.00 21.45 C ANISOU 1877 C HIS B 247 3253 2234 2664 -207 521 -538 C ATOM 1878 O HIS A 247 9.897 16.842 54.861 1.00 19.89 O ANISOU 1878 O HIS B 247 3065 2018 2472 -208 539 -539 O ATOM 1879 CB HIS A 247 9.762 15.758 52.051 1.00 21.60 C ANISOU 1879 CB HIS B 247 3168 2336 2705 -181 473 -525 C ATOM 1880 CG HIS A 247 11.079 16.337 51.666 1.00 25.76 C ANISOU 1880 CG HIS B 247 3661 2872 3254 -180 504 -557 C ATOM 1881 ND1 HIS A 247 12.222 15.569 51.532 1.00 28.44 N ANISOU 1881 ND1 HIS B 247 3997 3215 3595 -187 513 -574 N ATOM 1882 CD2 HIS A 247 11.425 17.598 51.312 1.00 26.71 C ANISOU 1882 CD2 HIS B 247 3746 3004 3398 -173 527 -579 C ATOM 1883 CE1 HIS A 247 13.217 16.337 51.133 1.00 26.18 C ANISOU 1883 CE1 HIS B 247 3674 2940 3332 -189 542 -607 C ATOM 1884 NE2 HIS A 247 12.757 17.567 50.974 1.00 29.08 N ANISOU 1884 NE2 HIS B 247 4019 3316 3715 -180 548 -610 N ATOM 1885 N SER A 248 11.553 15.301 54.997 1.00 21.60 N ANISOU 1885 N SER B 248 3299 2232 2678 -215 545 -552 N ATOM 1886 CA SER A 248 12.016 15.824 56.283 1.00 22.61 C ANISOU 1886 CA SER B 248 3484 2309 2798 -228 589 -565 C ATOM 1887 C SER A 248 13.471 16.228 56.226 1.00 25.09 C ANISOU 1887 C SER B 248 3785 2613 3135 -237 639 -598 C ATOM 1888 O SER A 248 14.279 15.612 56.921 1.00 26.37 O ANISOU 1888 O SER B 248 3994 2743 3282 -245 662 -603 O ATOM 1889 CB SER A 248 11.906 14.738 57.348 1.00 22.12 C ANISOU 1889 CB SER B 248 3491 2215 2697 -232 575 -548 C ATOM 1890 OG SER A 248 10.573 14.255 57.453 1.00 24.20 O ANISOU 1890 OG SER B 248 3765 2490 2941 -228 527 -523 O ATOM 1891 N PRO A 249 13.826 17.239 55.398 1.00 25.71 N ANISOU 1891 N PRO B 249 3802 2718 3249 -235 656 -621 N ATOM 1892 CA PRO A 249 15.251 17.590 55.309 1.00 26.37 C ANISOU 1892 CA PRO B 249 3867 2795 3358 -248 704 -659 C ATOM 1893 C PRO A 249 15.806 18.081 56.660 1.00 27.64 C ANISOU 1893 C PRO B 249 4089 2896 3516 -266 764 -674 C ATOM 1894 O PRO A 249 16.928 17.756 57.026 1.00 27.25 O ANISOU 1894 O PRO B 249 4065 2821 3469 -280 803 -693 O ATOM 1895 CB PRO A 249 15.302 18.697 54.251 1.00 25.87 C ANISOU 1895 CB PRO B 249 3724 2774 3331 -239 704 -680 C ATOM 1896 CG PRO A 249 13.876 19.082 53.988 1.00 26.49 C ANISOU 1896 CG PRO B 249 3793 2870 3401 -219 666 -651 C ATOM 1897 CD PRO A 249 12.965 18.076 54.550 1.00 25.22 C ANISOU 1897 CD PRO B 249 3686 2691 3203 -219 633 -615 C ATOM 1898 N TYR A 250 15.001 18.855 57.384 1.00 27.67 N ANISOU 1898 N TYR B 250 4122 2878 3515 -265 772 -665 N ATOM 1899 CA TYR A 250 15.301 19.209 58.756 1.00 27.95 C ANISOU 1899 CA TYR B 250 4228 2853 3537 -280 824 -672 C ATOM 1900 C TYR A 250 13.948 19.333 59.447 1.00 27.71 C ANISOU 1900 C TYR B 250 4242 2806 3479 -274 799 -643 C ATOM 1901 O TYR A 250 12.936 19.565 58.787 1.00 26.94 O ANISOU 1901 O TYR B 250 4107 2742 3386 -260 758 -627 O ATOM 1902 CB TYR A 250 16.120 20.513 58.846 1.00 28.82 C ANISOU 1902 CB TYR B 250 4309 2952 3690 -293 888 -712 C ATOM 1903 CG TYR A 250 15.527 21.692 58.094 1.00 30.07 C ANISOU 1903 CG TYR B 250 4397 3147 3882 -278 876 -720 C ATOM 1904 CD1 TYR A 250 15.676 21.813 56.716 1.00 31.25 C ANISOU 1904 CD1 TYR B 250 4462 3355 4057 -264 845 -730 C ATOM 1905 CD2 TYR A 250 14.820 22.676 58.767 1.00 31.09 C ANISOU 1905 CD2 TYR B 250 4548 3250 4014 -275 897 -716 C ATOM 1906 CE1 TYR A 250 15.129 22.888 56.022 1.00 31.97 C ANISOU 1906 CE1 TYR B 250 4493 3481 4175 -244 832 -735 C ATOM 1907 CE2 TYR A 250 14.256 23.749 58.079 1.00 31.99 C ANISOU 1907 CE2 TYR B 250 4601 3396 4157 -255 887 -720 C ATOM 1908 CZ TYR A 250 14.423 23.850 56.726 1.00 32.17 C ANISOU 1908 CZ TYR B 250 4541 3478 4203 -238 854 -729 C ATOM 1909 OH TYR A 250 13.873 24.913 56.056 1.00 32.55 O ANISOU 1909 OH TYR B 250 4534 3558 4277 -213 843 -731 O ATOM 1910 N ASN A 251 13.932 19.167 60.763 1.00 27.30 N ANISOU 1910 N ASN B 251 4274 2702 3395 -284 823 -637 N ATOM 1911 CA ASN A 251 12.690 19.024 61.488 1.00 27.08 C ANISOU 1911 CA ASN B 251 4298 2659 3333 -281 794 -611 C ATOM 1912 C ASN A 251 11.828 20.278 61.561 1.00 27.94 C ANISOU 1912 C ASN B 251 4393 2763 3460 -280 807 -613 C ATOM 1913 O ASN A 251 10.599 20.176 61.572 1.00 27.55 O ANISOU 1913 O ASN B 251 4352 2722 3393 -274 768 -591 O ATOM 1914 CB ASN A 251 12.916 18.401 62.864 1.00 26.57 C ANISOU 1914 CB ASN B 251 4331 2542 3222 -290 811 -604 C ATOM 1915 CG ASN A 251 11.635 18.324 63.684 1.00 26.78 C ANISOU 1915 CG ASN B 251 4413 2552 3211 -290 781 -583 C ATOM 1916 OD1 ASN A 251 11.362 19.203 64.498 1.00 26.75 O ANISOU 1916 OD1 ASN B 251 4450 2512 3203 -300 818 -590 O ATOM 1917 ND2 ASN A 251 10.811 17.304 63.422 1.00 22.37 N ANISOU 1917 ND2 ASN B 251 3850 2022 2629 -282 714 -559 N ATOM 1918 N LYS A 252 12.454 21.455 61.588 1.00 28.28 N ANISOU 1918 N LYS B 252 4413 2794 3540 -284 863 -641 N ATOM 1919 CA LYS A 252 11.691 22.694 61.575 1.00 28.91 C ANISOU 1919 CA LYS B 252 4473 2871 3640 -277 878 -644 C ATOM 1920 C LYS A 252 10.775 22.816 60.351 1.00 28.39 C ANISOU 1920 C LYS B 252 4340 2857 3589 -256 826 -627 C ATOM 1921 O LYS A 252 9.710 23.409 60.453 1.00 28.32 O ANISOU 1921 O LYS B 252 4339 2842 3579 -248 819 -614 O ATOM 1922 CB LYS A 252 12.622 23.899 61.648 1.00 29.37 C ANISOU 1922 CB LYS B 252 4501 2916 3742 -282 945 -680 C ATOM 1923 CG LYS A 252 11.936 25.308 61.611 1.00 31.66 C ANISOU 1923 CG LYS B 252 4765 3204 4061 -269 966 -686 C ATOM 1924 CD LYS A 252 10.923 25.585 62.758 1.00 34.90 C ANISOU 1924 CD LYS B 252 5254 3565 4440 -275 979 -669 C ATOM 1925 CE LYS A 252 11.385 25.114 64.122 1.00 35.94 C ANISOU 1925 CE LYS B 252 5479 3640 4535 -299 1016 -673 C ATOM 1926 NZ LYS A 252 12.413 26.000 64.669 1.00 34.88 N ANISOU 1926 NZ LYS B 252 5350 3473 4430 -311 1095 -707 N ATOM 1927 N LEU A 253 11.192 22.263 59.208 1.00 27.55 N ANISOU 1927 N LEU B 253 4172 2798 3496 -247 793 -627 N ATOM 1928 CA LEU A 253 10.395 22.356 57.973 1.00 27.10 C ANISOU 1928 CA LEU B 253 4055 2791 3451 -225 746 -611 C ATOM 1929 C LEU A 253 9.204 21.438 58.102 1.00 26.16 C ANISOU 1929 C LEU B 253 3972 2672 3296 -225 698 -578 C ATOM 1930 O LEU A 253 8.111 21.751 57.614 1.00 26.41 O ANISOU 1930 O LEU B 253 3987 2718 3330 -213 674 -559 O ATOM 1931 CB LEU A 253 11.221 22.019 56.721 1.00 27.19 C ANISOU 1931 CB LEU B 253 3995 2853 3483 -216 728 -624 C ATOM 1932 CG LEU A 253 10.509 22.061 55.357 1.00 27.42 C ANISOU 1932 CG LEU B 253 3963 2934 3520 -191 681 -608 C ATOM 1933 CD1 LEU A 253 9.989 23.494 54.989 1.00 31.91 C ANISOU 1933 CD1 LEU B 253 4497 3514 4116 -167 694 -611 C ATOM 1934 CD2 LEU A 253 11.365 21.562 54.246 1.00 27.83 C ANISOU 1934 CD2 LEU B 253 3957 3032 3585 -185 662 -621 C ATOM 1935 N VAL A 254 9.397 20.329 58.804 1.00 25.48 N ANISOU 1935 N VAL B 254 3937 2567 3178 -240 685 -570 N ATOM 1936 CA VAL A 254 8.287 19.411 59.111 1.00 25.35 C ANISOU 1936 CA VAL B 254 3958 2549 3127 -244 639 -543 C ATOM 1937 C VAL A 254 7.212 20.091 59.965 1.00 26.26 C ANISOU 1937 C VAL B 254 4121 2629 3229 -252 651 -537 C ATOM 1938 O VAL A 254 6.022 19.978 59.645 1.00 25.67 O ANISOU 1938 O VAL B 254 4040 2566 3148 -250 619 -518 O ATOM 1939 CB VAL A 254 8.761 18.070 59.755 1.00 25.13 C ANISOU 1939 CB VAL B 254 3976 2508 3064 -253 621 -538 C ATOM 1940 CG1 VAL A 254 7.557 17.156 60.108 1.00 24.10 C ANISOU 1940 CG1 VAL B 254 3876 2380 2900 -258 570 -515 C ATOM 1941 CG2 VAL A 254 9.731 17.328 58.808 1.00 24.24 C ANISOU 1941 CG2 VAL B 254 3815 2431 2966 -245 609 -543 C ATOM 1942 N GLN A 255 7.630 20.783 61.043 1.00 26.24 N ANISOU 1942 N GLN B 255 4168 2580 3222 -262 701 -552 N ATOM 1943 CA GLN A 255 6.714 21.572 61.862 1.00 27.56 C ANISOU 1943 CA GLN B 255 4382 2710 3379 -269 721 -550 C ATOM 1944 C GLN A 255 5.957 22.599 61.043 1.00 26.87 C ANISOU 1944 C GLN B 255 4246 2640 3324 -252 725 -545 C ATOM 1945 O GLN A 255 4.755 22.719 61.192 1.00 28.58 O ANISOU 1945 O GLN B 255 4485 2846 3529 -255 710 -531 O ATOM 1946 CB GLN A 255 7.445 22.273 63.037 1.00 27.55 C ANISOU 1946 CB GLN B 255 4435 2657 3374 -281 784 -571 C ATOM 1947 CG GLN A 255 8.249 21.335 63.977 1.00 30.67 C ANISOU 1947 CG GLN B 255 4894 3027 3733 -294 790 -575 C ATOM 1948 CD GLN A 255 9.142 22.141 64.932 1.00 31.12 C ANISOU 1948 CD GLN B 255 4996 3034 3794 -304 864 -598 C ATOM 1949 OE1 GLN A 255 8.745 23.202 65.396 1.00 31.50 O ANISOU 1949 OE1 GLN B 255 5062 3055 3853 -308 902 -606 O ATOM 1950 NE2 GLN A 255 10.363 21.650 65.195 1.00 36.55 N ANISOU 1950 NE2 GLN B 255 5701 3709 4475 -310 889 -609 N ATOM 1951 N LYS A 256 6.655 23.358 60.205 1.00 26.82 N ANISOU 1951 N LYS B 256 4176 2658 3356 -235 745 -559 N ATOM 1952 CA LYS A 256 6.023 24.375 59.365 1.00 27.87 C ANISOU 1952 CA LYS B 256 4260 2810 3518 -210 747 -553 C ATOM 1953 C LYS A 256 5.037 23.802 58.340 1.00 27.00 C ANISOU 1953 C LYS B 256 4121 2736 3401 -199 694 -526 C ATOM 1954 O LYS A 256 4.003 24.414 58.063 1.00 26.63 O ANISOU 1954 O LYS B 256 4073 2685 3360 -186 694 -512 O ATOM 1955 CB LYS A 256 7.075 25.255 58.661 1.00 28.09 C ANISOU 1955 CB LYS B 256 4221 2863 3589 -191 775 -577 C ATOM 1956 CG LYS A 256 7.801 26.219 59.627 1.00 29.96 C ANISOU 1956 CG LYS B 256 4481 3060 3843 -200 840 -605 C ATOM 1957 CD LYS A 256 8.869 27.075 58.954 1.00 30.65 C ANISOU 1957 CD LYS B 256 4494 3175 3976 -184 868 -635 C ATOM 1958 CE LYS A 256 9.440 28.059 60.022 1.00 34.29 C ANISOU 1958 CE LYS B 256 4984 3590 4457 -196 939 -663 C ATOM 1959 NZ LYS A 256 10.440 28.998 59.462 1.00 37.95 N ANISOU 1959 NZ LYS B 256 5370 4078 4969 -183 970 -698 N ATOM 1960 N SER A 257 5.406 22.653 57.755 1.00 26.50 N ANISOU 1960 N SER B 257 4034 2707 3329 -202 655 -521 N ATOM 1961 CA SER A 257 4.606 21.950 56.754 1.00 25.04 C ANISOU 1961 CA SER B 257 3820 2558 3138 -194 608 -498 C ATOM 1962 C SER A 257 3.261 21.510 57.330 1.00 24.49 C ANISOU 1962 C SER B 257 3800 2465 3042 -211 589 -479 C ATOM 1963 O SER A 257 2.220 21.766 56.716 1.00 24.35 O ANISOU 1963 O SER B 257 3769 2454 3029 -202 578 -462 O ATOM 1964 CB SER A 257 5.369 20.745 56.215 1.00 25.27 C ANISOU 1964 CB SER B 257 3821 2621 3160 -197 577 -499 C ATOM 1965 OG SER A 257 6.465 21.178 55.417 1.00 26.60 O ANISOU 1965 OG SER B 257 3933 2819 3355 -181 590 -517 O ATOM 1966 N PHE A 258 3.276 20.900 58.513 1.00 23.74 N ANISOU 1966 N PHE B 258 3763 2339 2919 -236 588 -484 N ATOM 1967 CA PHE A 258 2.040 20.425 59.127 1.00 24.48 C ANISOU 1967 CA PHE B 258 3903 2412 2986 -256 566 -473 C ATOM 1968 C PHE A 258 1.180 21.616 59.537 1.00 24.91 C ANISOU 1968 C PHE B 258 3987 2431 3048 -257 601 -472 C ATOM 1969 O PHE A 258 -0.041 21.605 59.343 1.00 25.04 O ANISOU 1969 O PHE B 258 4011 2442 3060 -263 588 -459 O ATOM 1970 CB PHE A 258 2.284 19.522 60.327 1.00 23.66 C ANISOU 1970 CB PHE B 258 3856 2286 2846 -278 553 -480 C ATOM 1971 CG PHE A 258 1.013 19.016 60.966 1.00 26.09 C ANISOU 1971 CG PHE B 258 4207 2578 3127 -301 526 -474 C ATOM 1972 CD1 PHE A 258 0.644 19.447 62.245 1.00 26.29 C ANISOU 1972 CD1 PHE B 258 4302 2557 3128 -319 548 -484 C ATOM 1973 CD2 PHE A 258 0.180 18.124 60.286 1.00 23.24 C ANISOU 1973 CD2 PHE B 258 3817 2249 2766 -307 481 -461 C ATOM 1974 CE1 PHE A 258 -0.518 19.010 62.832 1.00 24.72 C ANISOU 1974 CE1 PHE B 258 4142 2346 2904 -343 523 -483 C ATOM 1975 CE2 PHE A 258 -0.980 17.667 60.857 1.00 26.52 C ANISOU 1975 CE2 PHE B 258 4265 2651 3159 -331 457 -460 C ATOM 1976 CZ PHE A 258 -1.343 18.108 62.158 1.00 25.19 C ANISOU 1976 CZ PHE B 258 4167 2439 2966 -351 476 -473 C ATOM 1977 N ALA A 259 1.842 22.656 60.040 1.00 25.19 N ANISOU 1977 N ALA B 259 4035 2439 3095 -249 648 -488 N ATOM 1978 CA ALA A 259 1.146 23.884 60.432 1.00 25.73 C ANISOU 1978 CA ALA B 259 4131 2472 3175 -245 688 -489 C ATOM 1979 C ALA A 259 0.486 24.546 59.222 1.00 25.21 C ANISOU 1979 C ALA B 259 4015 2428 3135 -216 686 -472 C ATOM 1980 O ALA A 259 -0.624 25.077 59.323 1.00 26.22 O ANISOU 1980 O ALA B 259 4169 2531 3262 -216 698 -462 O ATOM 1981 CB ALA A 259 2.108 24.843 61.116 1.00 26.29 C ANISOU 1981 CB ALA B 259 4215 2515 3259 -240 742 -511 C ATOM 1982 N ARG A 260 1.159 24.507 58.075 1.00 24.74 N ANISOU 1982 N ARG B 260 3889 2415 3096 -192 671 -470 N ATOM 1983 CA ARG A 260 0.596 25.081 56.867 1.00 24.06 C ANISOU 1983 CA ARG B 260 3758 2353 3029 -160 665 -453 C ATOM 1984 C ARG A 260 -0.709 24.365 56.493 1.00 23.99 C ANISOU 1984 C ARG B 260 3764 2346 3003 -172 634 -429 C ATOM 1985 O ARG A 260 -1.634 24.977 55.944 1.00 23.14 O ANISOU 1985 O ARG B 260 3656 2233 2904 -154 643 -412 O ATOM 1986 CB ARG A 260 1.632 25.031 55.730 1.00 25.09 C ANISOU 1986 CB ARG B 260 3816 2536 3179 -134 648 -458 C ATOM 1987 CG ARG A 260 1.169 25.621 54.411 1.00 24.15 C ANISOU 1987 CG ARG B 260 3652 2450 3076 -95 638 -440 C ATOM 1988 CD ARG A 260 1.131 27.164 54.473 1.00 27.93 C ANISOU 1988 CD ARG B 260 4123 2911 3579 -62 678 -445 C ATOM 1989 NE ARG A 260 0.520 27.737 53.269 1.00 27.25 N ANISOU 1989 NE ARG B 260 4004 2849 3500 -20 668 -423 N ATOM 1990 CZ ARG A 260 0.490 29.037 52.984 1.00 29.69 C ANISOU 1990 CZ ARG B 260 4293 3157 3831 22 693 -423 C ATOM 1991 NH1 ARG A 260 1.055 29.923 53.800 1.00 25.32 N ANISOU 1991 NH1 ARG B 260 3743 2580 3298 24 732 -447 N ATOM 1992 NH2 ARG A 260 -0.124 29.451 51.874 1.00 30.52 N ANISOU 1992 NH2 ARG B 260 4376 3285 3937 64 679 -399 N ATOM 1993 N LEU A 261 -0.810 23.077 56.826 1.00 23.07 N ANISOU 1993 N LEU B 261 3665 2236 2864 -202 601 -430 N ATOM 1994 CA LEU A 261 -2.025 22.336 56.507 1.00 23.17 C ANISOU 1994 CA LEU B 261 3687 2253 2865 -219 573 -413 C ATOM 1995 C LEU A 261 -3.193 22.859 57.370 1.00 23.38 C ANISOU 1995 C LEU B 261 3773 2228 2882 -239 598 -412 C ATOM 1996 O LEU A 261 -4.322 22.913 56.905 1.00 22.94 O ANISOU 1996 O LEU B 261 3723 2166 2829 -241 598 -397 O ATOM 1997 CB LEU A 261 -1.863 20.830 56.673 1.00 21.77 C ANISOU 1997 CB LEU B 261 3507 2096 2667 -244 530 -415 C ATOM 1998 CG LEU A 261 -0.800 20.092 55.849 1.00 21.85 C ANISOU 1998 CG LEU B 261 3464 2154 2685 -230 504 -416 C ATOM 1999 CD1 LEU A 261 -1.028 18.633 56.106 1.00 19.69 C ANISOU 1999 CD1 LEU B 261 3197 1893 2391 -255 463 -415 C ATOM 2000 CD2 LEU A 261 -0.972 20.419 54.334 1.00 21.34 C ANISOU 2000 CD2 LEU B 261 3346 2125 2640 -199 500 -399 C ATOM 2001 N LEU A 262 -2.924 23.244 58.608 1.00 24.16 N ANISOU 2001 N LEU B 262 3920 2289 2970 -254 622 -430 N ATOM 2002 CA LEU A 262 -3.981 23.849 59.461 1.00 25.52 C ANISOU 2002 CA LEU B 262 4153 2410 3132 -272 651 -433 C ATOM 2003 C LEU A 262 -4.484 25.180 58.920 1.00 26.11 C ANISOU 2003 C LEU B 262 4222 2467 3232 -241 692 -421 C ATOM 2004 O LEU A 262 -5.684 25.449 58.955 1.00 26.70 O ANISOU 2004 O LEU B 262 4328 2513 3305 -251 706 -412 O ATOM 2005 CB LEU A 262 -3.535 24.039 60.927 1.00 26.14 C ANISOU 2005 CB LEU B 262 4290 2450 3191 -293 674 -455 C ATOM 2006 CG LEU A 262 -3.648 22.881 61.928 1.00 26.88 C ANISOU 2006 CG LEU B 262 4428 2539 3248 -331 640 -467 C ATOM 2007 CD1 LEU A 262 -5.091 22.410 62.065 1.00 29.03 C ANISOU 2007 CD1 LEU B 262 4726 2799 3505 -362 620 -465 C ATOM 2008 CD2 LEU A 262 -2.774 21.707 61.495 1.00 28.46 C ANISOU 2008 CD2 LEU B 262 4586 2784 3441 -328 596 -465 C ATOM 2009 N TYR A 263 -3.561 26.014 58.443 1.00 26.80 N ANISOU 2009 N TYR B 263 4270 2570 3343 -203 712 -422 N ATOM 2010 CA TYR A 263 -3.914 27.247 57.752 1.00 27.06 C ANISOU 2010 CA TYR B 263 4285 2597 3401 -162 743 -408 C ATOM 2011 C TYR A 263 -4.827 26.937 56.566 1.00 27.26 C ANISOU 2011 C TYR B 263 4288 2642 3427 -149 721 -382 C ATOM 2012 O TYR A 263 -5.877 27.557 56.410 1.00 26.66 O ANISOU 2012 O TYR B 263 4239 2537 3355 -140 746 -367 O ATOM 2013 CB TYR A 263 -2.653 27.987 57.299 1.00 27.94 C ANISOU 2013 CB TYR B 263 4342 2736 3537 -124 755 -418 C ATOM 2014 CG TYR A 263 -2.946 29.179 56.424 1.00 30.35 C ANISOU 2014 CG TYR B 263 4618 3047 3868 -73 776 -403 C ATOM 2015 CD1 TYR A 263 -3.676 30.271 56.929 1.00 34.40 C ANISOU 2015 CD1 TYR B 263 5171 3511 4388 -60 822 -399 C ATOM 2016 CD2 TYR A 263 -2.532 29.214 55.090 1.00 30.58 C ANISOU 2016 CD2 TYR B 263 4582 3129 3909 -35 750 -392 C ATOM 2017 CE1 TYR A 263 -3.977 31.376 56.133 1.00 31.89 C ANISOU 2017 CE1 TYR B 263 4829 3196 4092 -6 841 -383 C ATOM 2018 CE2 TYR A 263 -2.806 30.313 54.279 1.00 31.47 C ANISOU 2018 CE2 TYR B 263 4669 3248 4039 19 766 -377 C ATOM 2019 CZ TYR A 263 -3.534 31.397 54.815 1.00 33.07 C ANISOU 2019 CZ TYR B 263 4913 3402 4252 34 811 -371 C ATOM 2020 OH TYR A 263 -3.825 32.501 54.038 1.00 33.65 O ANISOU 2020 OH TYR B 263 4964 3481 4342 93 826 -354 O ATOM 2021 N ASN A 264 -4.442 25.962 55.744 1.00 26.25 N ANISOU 2021 N ASN B 264 4116 2563 3295 -150 679 -376 N ATOM 2022 CA ASN A 264 -5.296 25.542 54.645 1.00 26.94 C ANISOU 2022 CA ASN B 264 4186 2668 3381 -142 660 -351 C ATOM 2023 C ASN A 264 -6.694 25.149 55.123 1.00 26.39 C ANISOU 2023 C ASN B 264 4169 2561 3298 -180 667 -346 C ATOM 2024 O ASN A 264 -7.679 25.570 54.532 1.00 25.69 O ANISOU 2024 O ASN B 264 4093 2455 3214 -167 685 -326 O ATOM 2025 CB ASN A 264 -4.657 24.397 53.864 1.00 26.97 C ANISOU 2025 CB ASN B 264 4140 2726 3380 -145 615 -350 C ATOM 2026 CG ASN A 264 -3.712 24.886 52.797 1.00 28.32 C ANISOU 2026 CG ASN B 264 4253 2941 3566 -98 609 -346 C ATOM 2027 OD1 ASN A 264 -4.126 25.440 51.770 1.00 30.62 O ANISOU 2027 OD1 ASN B 264 4525 3244 3863 -61 614 -325 O ATOM 2028 ND2 ASN A 264 -2.439 24.693 53.031 1.00 30.38 N ANISOU 2028 ND2 ASN B 264 4487 3226 3832 -99 599 -367 N ATOM 2029 N ASP A 265 -6.774 24.359 56.189 1.00 26.49 N ANISOU 2029 N ASP B 265 4213 2558 3293 -226 652 -365 N ATOM 2030 CA ASP A 265 -8.063 23.981 56.767 1.00 27.58 C ANISOU 2030 CA ASP B 265 4401 2661 3419 -269 657 -369 C ATOM 2031 C ASP A 265 -8.842 25.239 57.199 1.00 29.02 C ANISOU 2031 C ASP B 265 4632 2787 3606 -261 709 -366 C ATOM 2032 O ASP A 265 -10.032 25.350 56.898 1.00 28.97 O ANISOU 2032 O ASP B 265 4650 2756 3602 -271 727 -354 O ATOM 2033 CB ASP A 265 -7.883 23.026 57.955 1.00 27.11 C ANISOU 2033 CB ASP B 265 4369 2597 3336 -314 629 -393 C ATOM 2034 CG ASP A 265 -7.603 21.589 57.524 1.00 27.28 C ANISOU 2034 CG ASP B 265 4349 2666 3350 -329 577 -394 C ATOM 2035 OD1 ASP A 265 -7.394 21.347 56.310 1.00 24.79 O ANISOU 2035 OD1 ASP B 265 3983 2388 3048 -305 563 -377 O ATOM 2036 OD2 ASP A 265 -7.561 20.701 58.410 1.00 26.03 O ANISOU 2036 OD2 ASP B 265 4210 2508 3170 -363 548 -412 O ATOM 2037 N PHE A 266 -8.162 26.198 57.831 1.00 29.86 N ANISOU 2037 N PHE B 266 4754 2874 3719 -241 739 -376 N ATOM 2038 CA PHE A 266 -8.783 27.500 58.167 1.00 31.50 C ANISOU 2038 CA PHE B 266 5003 3029 3936 -224 793 -372 C ATOM 2039 C PHE A 266 -9.407 28.112 56.929 1.00 32.19 C ANISOU 2039 C PHE B 266 5071 3120 4040 -183 810 -342 C ATOM 2040 O PHE A 266 -10.607 28.419 56.923 1.00 31.99 O ANISOU 2040 O PHE B 266 5087 3053 4014 -192 838 -332 O ATOM 2041 CB PHE A 266 -7.772 28.487 58.782 1.00 31.84 C ANISOU 2041 CB PHE B 266 5047 3061 3990 -199 824 -386 C ATOM 2042 CG PHE A 266 -8.243 29.926 58.761 1.00 33.46 C ANISOU 2042 CG PHE B 266 5274 3225 4213 -163 878 -376 C ATOM 2043 CD1 PHE A 266 -7.622 30.867 57.930 1.00 32.71 C ANISOU 2043 CD1 PHE B 266 5130 3153 4144 -103 891 -364 C ATOM 2044 CD2 PHE A 266 -9.336 30.330 59.543 1.00 32.28 C ANISOU 2044 CD2 PHE B 266 5194 3015 4056 -188 916 -381 C ATOM 2045 CE1 PHE A 266 -8.059 32.189 57.891 1.00 33.35 C ANISOU 2045 CE1 PHE B 266 5230 3198 4244 -64 940 -354 C ATOM 2046 CE2 PHE A 266 -9.795 31.669 59.517 1.00 33.39 C ANISOU 2046 CE2 PHE B 266 5359 3114 4215 -151 970 -370 C ATOM 2047 CZ PHE A 266 -9.161 32.598 58.689 1.00 34.03 C ANISOU 2047 CZ PHE B 266 5389 3219 4322 -87 982 -356 C ATOM 2048 N LEU A 267 -8.615 28.236 55.860 1.00 32.06 N ANISOU 2048 N LEU B 267 4993 3151 4036 -138 791 -328 N ATOM 2049 CA LEU A 267 -9.112 28.826 54.618 1.00 33.27 C ANISOU 2049 CA LEU B 267 5128 3312 4200 -90 803 -298 C ATOM 2050 C LEU A 267 -10.329 28.120 54.021 1.00 34.26 C ANISOU 2050 C LEU B 267 5272 3428 4316 -113 798 -280 C ATOM 2051 O LEU A 267 -11.137 28.758 53.335 1.00 34.50 O ANISOU 2051 O LEU B 267 5320 3437 4351 -82 826 -254 O ATOM 2052 CB LEU A 267 -8.021 28.912 53.568 1.00 32.98 C ANISOU 2052 CB LEU B 267 5021 3336 4173 -43 775 -291 C ATOM 2053 CG LEU A 267 -6.835 29.824 53.863 1.00 32.32 C ANISOU 2053 CG LEU B 267 4908 3265 4107 -10 787 -307 C ATOM 2054 CD1 LEU A 267 -5.820 29.681 52.729 1.00 32.56 C ANISOU 2054 CD1 LEU B 267 4866 3362 4145 27 751 -304 C ATOM 2055 CD2 LEU A 267 -7.285 31.271 54.006 1.00 32.38 C ANISOU 2055 CD2 LEU B 267 4940 3232 4130 32 835 -298 C ATOM 2056 N ARG A 268 -10.463 26.823 54.297 1.00 34.75 N ANISOU 2056 N ARG B 268 5333 3506 4366 -165 764 -293 N ATOM 2057 CA ARG A 268 -11.556 26.031 53.754 1.00 35.89 C ANISOU 2057 CA ARG B 268 5487 3646 4504 -194 758 -281 C ATOM 2058 C ARG A 268 -12.666 25.852 54.775 1.00 37.16 C ANISOU 2058 C ARG B 268 5708 3754 4658 -249 780 -298 C ATOM 2059 O ARG A 268 -13.582 25.055 54.565 1.00 38.04 O ANISOU 2059 O ARG B 268 5827 3859 4766 -288 775 -299 O ATOM 2060 CB ARG A 268 -11.036 24.662 53.275 1.00 35.53 C ANISOU 2060 CB ARG B 268 5392 3656 4453 -213 706 -286 C ATOM 2061 CG ARG A 268 -10.070 24.737 52.058 1.00 35.09 C ANISOU 2061 CG ARG B 268 5276 3654 4402 -161 684 -269 C ATOM 2062 CD ARG A 268 -9.111 23.532 52.042 1.00 37.84 C ANISOU 2062 CD ARG B 268 5578 4053 4745 -180 635 -284 C ATOM 2063 NE ARG A 268 -9.893 22.320 51.908 1.00 38.53 N ANISOU 2063 NE ARG B 268 5666 4145 4827 -224 616 -285 N ATOM 2064 CZ ARG A 268 -9.936 21.349 52.805 1.00 40.22 C ANISOU 2064 CZ ARG B 268 5889 4360 5034 -272 591 -309 C ATOM 2065 NH1 ARG A 268 -9.173 21.387 53.901 1.00 37.38 N ANISOU 2065 NH1 ARG B 268 5541 3996 4666 -283 580 -330 N ATOM 2066 NH2 ARG A 268 -10.729 20.315 52.575 1.00 40.68 N ANISOU 2066 NH2 ARG B 268 5940 4424 5091 -308 576 -310 N ATOM 2067 N ASN A 269 -12.594 26.616 55.864 1.00 38.24 N ANISOU 2067 N ASN B 269 5886 3850 4792 -255 808 -314 N ATOM 2068 CA ASN A 269 -13.490 26.474 57.017 1.00 39.59 C ANISOU 2068 CA ASN B 269 6117 3972 4952 -310 826 -338 C ATOM 2069 C ASN A 269 -13.763 25.028 57.359 1.00 38.87 C ANISOU 2069 C ASN B 269 6018 3903 4848 -369 781 -359 C ATOM 2070 O ASN A 269 -14.931 24.642 57.542 1.00 38.92 O ANISOU 2070 O ASN B 269 6055 3882 4852 -413 791 -368 O ATOM 2071 CB ASN A 269 -14.842 27.200 56.846 1.00 41.04 C ANISOU 2071 CB ASN B 269 6353 4097 5143 -312 880 -325 C ATOM 2072 CG ASN A 269 -14.807 28.294 55.807 1.00 44.24 C ANISOU 2072 CG ASN B 269 6748 4497 5564 -243 913 -290 C ATOM 2073 OD1 ASN A 269 -14.939 28.024 54.616 1.00 48.35 O ANISOU 2073 OD1 ASN B 269 7237 5045 6088 -218 903 -265 O ATOM 2074 ND2 ASN A 269 -14.677 29.546 56.253 1.00 48.88 N ANISOU 2074 ND2 ASN B 269 7364 5048 6158 -209 955 -288 N ATOM 2075 N ALA A 270 -12.689 24.236 57.427 1.00 37.33 N ANISOU 2075 N ALA B 270 5780 3759 4646 -368 733 -368 N ATOM 2076 CA ALA A 270 -12.797 22.814 57.680 1.00 36.53 C ANISOU 2076 CA ALA B 270 5661 3687 4532 -414 684 -386 C ATOM 2077 C ALA A 270 -13.066 22.541 59.153 1.00 36.62 C ANISOU 2077 C ALA B 270 5722 3671 4521 -462 676 -419 C ATOM 2078 O ALA A 270 -12.803 23.382 60.013 1.00 36.66 O ANISOU 2078 O ALA B 270 5769 3642 4518 -456 704 -428 O ATOM 2079 CB ALA A 270 -11.554 22.107 57.218 1.00 36.26 C ANISOU 2079 CB ALA B 270 5568 3711 4497 -391 639 -381 C ATOM 2080 N SER A 271 -13.576 21.352 59.442 1.00 36.36 N ANISOU 2080 N SER B 271 5682 3655 4478 -509 638 -438 N ATOM 2081 CA SER A 271 -14.035 21.030 60.784 1.00 36.82 C ANISOU 2081 CA SER B 271 5790 3690 4512 -558 626 -472 C ATOM 2082 C SER A 271 -12.922 20.763 61.798 1.00 36.46 C ANISOU 2082 C SER B 271 5755 3658 4439 -553 596 -487 C ATOM 2083 O SER A 271 -13.198 20.645 63.010 1.00 37.43 O ANISOU 2083 O SER B 271 5929 3758 4536 -587 589 -515 O ATOM 2084 CB SER A 271 -15.038 19.877 60.742 1.00 37.13 C ANISOU 2084 CB SER B 271 5814 3743 4551 -610 595 -491 C ATOM 2085 OG SER A 271 -14.413 18.664 60.428 1.00 38.27 O ANISOU 2085 OG SER B 271 5902 3945 4692 -607 538 -492 O ATOM 2086 N SER A 272 -11.670 20.665 61.331 1.00 34.49 N ANISOU 2086 N SER B 272 5465 3445 4195 -512 579 -471 N ATOM 2087 CA SER A 272 -10.540 20.584 62.251 1.00 32.93 C ANISOU 2087 CA SER B 272 5286 3253 3974 -503 564 -483 C ATOM 2088 C SER A 272 -10.305 21.909 62.967 1.00 32.78 C ANISOU 2088 C SER B 272 5319 3185 3951 -489 617 -487 C ATOM 2089 O SER A 272 -9.515 21.992 63.912 1.00 31.97 O ANISOU 2089 O SER B 272 5248 3073 3827 -488 617 -500 O ATOM 2090 CB SER A 272 -9.246 20.205 61.499 1.00 32.04 C ANISOU 2090 CB SER B 272 5115 3188 3872 -464 541 -467 C ATOM 2091 OG SER A 272 -8.987 21.163 60.476 1.00 29.34 O ANISOU 2091 OG SER B 272 4743 2846 3559 -424 577 -443 O ATOM 2092 N ILE A 273 -10.936 22.965 62.475 1.00 34.17 N ANISOU 2092 N ILE B 273 5504 3329 4150 -475 666 -473 N ATOM 2093 CA ILE A 273 -10.651 24.304 62.983 1.00 34.59 C ANISOU 2093 CA ILE B 273 5597 3339 4208 -453 721 -474 C ATOM 2094 C ILE A 273 -11.725 24.659 64.002 1.00 36.51 C ANISOU 2094 C ILE B 273 5913 3526 4433 -492 749 -495 C ATOM 2095 O ILE A 273 -12.877 24.865 63.647 1.00 35.99 O ANISOU 2095 O ILE B 273 5860 3437 4378 -508 769 -491 O ATOM 2096 CB ILE A 273 -10.536 25.356 61.842 1.00 34.70 C ANISOU 2096 CB ILE B 273 5576 3353 4257 -401 759 -446 C ATOM 2097 CG1 ILE A 273 -9.362 25.011 60.893 1.00 31.39 C ANISOU 2097 CG1 ILE B 273 5084 2991 3852 -364 729 -431 C ATOM 2098 CG2 ILE A 273 -10.349 26.779 62.420 1.00 34.75 C ANISOU 2098 CG2 ILE B 273 5622 3312 4271 -378 819 -449 C ATOM 2099 CD1 ILE A 273 -7.978 25.065 61.532 1.00 31.89 C ANISOU 2099 CD1 ILE B 273 5144 3065 3907 -352 726 -444 C ATOM 2100 N ASP A 274 -11.342 24.706 65.274 1.00 37.87 N ANISOU 2100 N ASP B 274 6136 3676 4575 -510 752 -518 N ATOM 2101 CA ASP A 274 -12.315 25.084 66.293 1.00 39.96 C ANISOU 2101 CA ASP B 274 6475 3887 4819 -549 780 -541 C ATOM 2102 C ASP A 274 -12.420 26.592 66.499 1.00 40.71 C ANISOU 2102 C ASP B 274 6609 3927 4930 -525 853 -536 C ATOM 2103 O ASP A 274 -11.627 27.392 65.965 1.00 39.99 O ANISOU 2103 O ASP B 274 6487 3842 4866 -476 881 -517 O ATOM 2104 CB ASP A 274 -12.084 24.342 67.632 1.00 40.41 C ANISOU 2104 CB ASP B 274 6581 3944 4829 -585 745 -571 C ATOM 2105 CG ASP A 274 -10.841 24.808 68.376 1.00 42.43 C ANISOU 2105 CG ASP B 274 6862 4189 5069 -560 765 -574 C ATOM 2106 OD1 ASP A 274 -10.382 24.071 69.280 1.00 45.13 O ANISOU 2106 OD1 ASP B 274 7235 4541 5372 -578 730 -592 O ATOM 2107 OD2 ASP A 274 -10.313 25.896 68.075 1.00 44.98 O ANISOU 2107 OD2 ASP B 274 7178 4494 5420 -523 816 -561 O ATOM 2108 N GLU A 275 -13.461 26.940 67.257 1.00 42.01 N ANISOU 2108 N GLU B 275 6840 4041 5081 -560 883 -556 N ATOM 2109 CA GLU A 275 -13.745 28.254 67.796 1.00 42.73 C ANISOU 2109 CA GLU B 275 6988 4070 5178 -550 953 -560 C ATOM 2110 C GLU A 275 -12.537 29.151 68.021 1.00 40.89 C ANISOU 2110 C GLU B 275 6751 3830 4955 -505 988 -553 C ATOM 2111 O GLU A 275 -12.397 30.176 67.361 1.00 41.29 O ANISOU 2111 O GLU B 275 6778 3868 5041 -460 1032 -532 O ATOM 2112 CB GLU A 275 -14.523 28.064 69.121 1.00 44.69 C ANISOU 2112 CB GLU B 275 7318 4275 5386 -607 958 -597 C ATOM 2113 CG GLU A 275 -13.977 26.882 69.995 1.00 49.30 C ANISOU 2113 CG GLU B 275 7914 4894 5925 -638 894 -620 C ATOM 2114 CD GLU A 275 -14.647 25.509 69.718 1.00 54.85 C ANISOU 2114 CD GLU B 275 8585 5638 6615 -678 826 -631 C ATOM 2115 OE1 GLU A 275 -15.239 25.299 68.630 1.00 57.04 O ANISOU 2115 OE1 GLU B 275 8814 5934 6925 -676 820 -615 O ATOM 2116 OE2 GLU A 275 -14.557 24.624 70.602 1.00 57.95 O ANISOU 2116 OE2 GLU B 275 9004 6048 6967 -710 778 -657 O ATOM 2117 N ALA A 276 -11.689 28.758 68.964 1.00 39.49 N ANISOU 2117 N ALA B 276 6597 3659 4747 -518 971 -571 N ATOM 2118 CA ALA A 276 -10.477 29.475 69.313 1.00 39.13 C ANISOU 2118 CA ALA B 276 6552 3607 4710 -484 1005 -571 C ATOM 2119 C ALA A 276 -9.441 29.568 68.195 1.00 37.97 C ANISOU 2119 C ALA B 276 6320 3509 4599 -435 994 -547 C ATOM 2120 O ALA A 276 -8.722 30.583 68.076 1.00 37.37 O ANISOU 2120 O ALA B 276 6226 3422 4550 -397 1039 -542 O ATOM 2121 CB ALA A 276 -9.843 28.846 70.554 1.00 39.66 C ANISOU 2121 CB ALA B 276 6669 3671 4728 -512 985 -595 C ATOM 2122 N ALA A 277 -9.338 28.499 67.402 1.00 36.92 N ANISOU 2122 N ALA B 277 6131 3430 4466 -438 933 -535 N ATOM 2123 CA ALA A 277 -8.418 28.467 66.274 1.00 35.44 C ANISOU 2123 CA ALA B 277 5864 3293 4310 -396 916 -515 C ATOM 2124 C ALA A 277 -8.901 29.489 65.252 1.00 35.11 C ANISOU 2124 C ALA B 277 5789 3242 4308 -356 952 -492 C ATOM 2125 O ALA A 277 -8.110 30.282 64.765 1.00 33.64 O ANISOU 2125 O ALA B 277 5562 3068 4152 -312 976 -484 O ATOM 2126 CB ALA A 277 -8.378 27.080 65.665 1.00 35.21 C ANISOU 2126 CB ALA B 277 5790 3319 4271 -410 847 -508 C ATOM 2127 N LYS A 278 -10.205 29.483 64.947 1.00 36.50 N ANISOU 2127 N LYS B 278 5986 3399 4486 -372 956 -485 N ATOM 2128 CA LYS A 278 -10.771 30.487 64.019 1.00 38.26 C ANISOU 2128 CA LYS B 278 6190 3605 4741 -331 994 -461 C ATOM 2129 C LYS A 278 -10.348 31.893 64.405 1.00 38.58 C ANISOU 2129 C LYS B 278 6248 3610 4802 -294 1056 -463 C ATOM 2130 O LYS A 278 -9.778 32.635 63.574 1.00 38.23 O ANISOU 2130 O LYS B 278 6150 3586 4790 -239 1070 -446 O ATOM 2131 CB LYS A 278 -12.295 30.412 63.941 1.00 39.02 C ANISOU 2131 CB LYS B 278 6328 3665 4832 -360 1008 -457 C ATOM 2132 CG LYS A 278 -12.818 29.674 62.724 1.00 41.37 C ANISOU 2132 CG LYS B 278 6581 4001 5139 -358 972 -436 C ATOM 2133 CD LYS A 278 -14.255 30.099 62.383 1.00 47.44 C ANISOU 2133 CD LYS B 278 7386 4723 5916 -367 1010 -425 C ATOM 2134 CE LYS A 278 -14.996 28.992 61.623 1.00 51.91 C ANISOU 2134 CE LYS B 278 7928 5316 6479 -397 972 -418 C ATOM 2135 NZ LYS A 278 -14.853 27.666 62.315 1.00 53.35 N ANISOU 2135 NZ LYS B 278 8108 5528 6636 -452 916 -446 N ATOM 2136 N GLU A 279 -10.576 32.212 65.681 1.00 39.16 N ANISOU 2136 N GLU B 279 6392 3632 4855 -324 1091 -487 N ATOM 2137 CA GLU A 279 -10.262 33.519 66.274 1.00 40.49 C ANISOU 2137 CA GLU B 279 6589 3756 5040 -298 1157 -495 C ATOM 2138 C GLU A 279 -8.767 33.813 66.189 1.00 39.53 C ANISOU 2138 C GLU B 279 6415 3668 4938 -265 1159 -499 C ATOM 2139 O GLU A 279 -8.364 34.946 65.958 1.00 40.13 O ANISOU 2139 O GLU B 279 6467 3734 5047 -219 1203 -495 O ATOM 2140 CB GLU A 279 -10.770 33.576 67.733 1.00 41.33 C ANISOU 2140 CB GLU B 279 6787 3804 5112 -346 1187 -523 C ATOM 2141 CG GLU A 279 -10.944 34.990 68.328 1.00 47.20 C ANISOU 2141 CG GLU B 279 7576 4484 5872 -324 1267 -530 C ATOM 2142 CD GLU A 279 -12.409 35.400 68.652 1.00 54.37 C ANISOU 2142 CD GLU B 279 8554 5330 6772 -347 1306 -533 C ATOM 2143 OE1 GLU A 279 -13.370 34.580 68.547 1.00 56.68 O ANISOU 2143 OE1 GLU B 279 8867 5624 7044 -388 1274 -535 O ATOM 2144 OE2 GLU A 279 -12.599 36.577 69.050 1.00 57.26 O ANISOU 2144 OE2 GLU B 279 8957 5645 7155 -325 1374 -536 O ATOM 2145 N LYS A 280 -7.930 32.790 66.346 1.00 38.73 N ANISOU 2145 N LYS B 280 6292 3606 4816 -286 1112 -508 N ATOM 2146 CA LYS A 280 -6.483 32.964 66.151 1.00 37.44 C ANISOU 2146 CA LYS B 280 6075 3477 4672 -258 1112 -513 C ATOM 2147 C LYS A 280 -6.100 33.311 64.707 1.00 36.59 C ANISOU 2147 C LYS B 280 5878 3419 4605 -206 1097 -492 C ATOM 2148 O LYS A 280 -5.174 34.077 64.472 1.00 36.90 O ANISOU 2148 O LYS B 280 5874 3472 4675 -170 1122 -497 O ATOM 2149 CB LYS A 280 -5.746 31.706 66.574 1.00 37.98 C ANISOU 2149 CB LYS B 280 6146 3576 4710 -292 1064 -525 C ATOM 2150 CG LYS A 280 -5.739 31.427 68.067 1.00 39.57 C ANISOU 2150 CG LYS B 280 6431 3735 4868 -334 1080 -549 C ATOM 2151 CD LYS A 280 -4.386 31.747 68.636 1.00 43.29 C ANISOU 2151 CD LYS B 280 6901 4202 5344 -325 1111 -566 C ATOM 2152 CE LYS A 280 -4.027 30.775 69.750 1.00 46.31 C ANISOU 2152 CE LYS B 280 7346 4575 5675 -365 1090 -582 C ATOM 2153 NZ LYS A 280 -4.854 31.048 70.944 1.00 47.77 N ANISOU 2153 NZ LYS B 280 7624 4701 5824 -396 1120 -598 N ATOM 2154 N PHE A 281 -6.792 32.724 63.740 1.00 35.81 N ANISOU 2154 N PHE B 281 5753 3348 4504 -203 1056 -470 N ATOM 2155 CA PHE A 281 -6.452 32.932 62.340 1.00 35.86 C ANISOU 2155 CA PHE B 281 5681 3405 4540 -155 1035 -448 C ATOM 2156 C PHE A 281 -7.119 34.176 61.739 1.00 36.83 C ANISOU 2156 C PHE B 281 5798 3505 4691 -105 1075 -429 C ATOM 2157 O PHE A 281 -6.620 34.767 60.777 1.00 37.07 O ANISOU 2157 O PHE B 281 5765 3570 4749 -53 1072 -417 O ATOM 2158 CB PHE A 281 -6.910 31.725 61.526 1.00 35.27 C ANISOU 2158 CB PHE B 281 5583 3369 4449 -172 976 -432 C ATOM 2159 CG PHE A 281 -5.934 30.595 61.479 1.00 34.30 C ANISOU 2159 CG PHE B 281 5426 3293 4313 -191 927 -441 C ATOM 2160 CD1 PHE A 281 -6.341 29.311 61.810 1.00 34.39 C ANISOU 2160 CD1 PHE B 281 5462 3312 4293 -237 885 -445 C ATOM 2161 CD2 PHE A 281 -4.624 30.801 61.075 1.00 32.86 C ANISOU 2161 CD2 PHE B 281 5185 3150 4151 -163 923 -448 C ATOM 2162 CE1 PHE A 281 -5.442 28.248 61.746 1.00 34.27 C ANISOU 2162 CE1 PHE B 281 5416 3339 4265 -251 841 -452 C ATOM 2163 CE2 PHE A 281 -3.727 29.753 61.011 1.00 33.24 C ANISOU 2163 CE2 PHE B 281 5205 3237 4187 -180 882 -457 C ATOM 2164 CZ PHE A 281 -4.143 28.472 61.345 1.00 33.87 C ANISOU 2164 CZ PHE B 281 5313 3322 4235 -222 841 -457 C ATOM 2165 N THR A 282 -8.263 34.566 62.279 1.00 38.16 N ANISOU 2165 N THR B 282 6034 3617 4850 -120 1111 -427 N ATOM 2166 CA THR A 282 -9.009 35.700 61.690 1.00 39.30 C ANISOU 2166 CA THR B 282 6180 3733 5017 -71 1151 -405 C ATOM 2167 C THR A 282 -8.180 36.952 61.378 1.00 39.40 C ANISOU 2167 C THR B 282 6144 3757 5068 -8 1182 -405 C ATOM 2168 O THR A 282 -8.352 37.501 60.299 1.00 39.82 O ANISOU 2168 O THR B 282 6157 3831 5141 48 1179 -380 O ATOM 2169 CB THR A 282 -10.301 36.005 62.447 1.00 39.84 C ANISOU 2169 CB THR B 282 6336 3731 5072 -100 1195 -406 C ATOM 2170 OG1 THR A 282 -11.104 34.830 62.396 1.00 41.12 O ANISOU 2170 OG1 THR B 282 6523 3896 5206 -151 1157 -404 O ATOM 2171 CG2 THR A 282 -11.110 37.191 61.801 1.00 40.54 C ANISOU 2171 CG2 THR B 282 6432 3785 5184 -43 1241 -380 C ATOM 2172 N PRO A 283 -7.261 37.384 62.274 1.00 39.63 N ANISOU 2172 N PRO B 283 6175 3776 5108 -14 1212 -433 N ATOM 2173 CA PRO A 283 -6.435 38.528 61.842 1.00 40.17 C ANISOU 2173 CA PRO B 283 6180 3864 5217 47 1237 -436 C ATOM 2174 C PRO A 283 -5.729 38.363 60.481 1.00 40.47 C ANISOU 2174 C PRO B 283 6126 3977 5273 90 1187 -424 C ATOM 2175 O PRO A 283 -5.351 39.374 59.878 1.00 41.14 O ANISOU 2175 O PRO B 283 6158 4082 5392 151 1201 -420 O ATOM 2176 CB PRO A 283 -5.407 38.684 62.975 1.00 40.21 C ANISOU 2176 CB PRO B 283 6195 3854 5228 20 1268 -473 C ATOM 2177 CG PRO A 283 -6.099 38.098 64.195 1.00 40.28 C ANISOU 2177 CG PRO B 283 6300 3808 5197 -43 1283 -484 C ATOM 2178 CD PRO A 283 -6.920 36.946 63.643 1.00 40.07 C ANISOU 2178 CD PRO B 283 6284 3801 5139 -71 1226 -463 C ATOM 2179 N TYR A 284 -5.579 37.121 59.995 1.00 39.90 N ANISOU 2179 N TYR B 284 6035 3947 5178 61 1129 -418 N ATOM 2180 CA TYR A 284 -4.836 36.842 58.747 1.00 39.90 C ANISOU 2180 CA TYR B 284 5952 4020 5190 94 1080 -409 C ATOM 2181 C TYR A 284 -5.726 36.566 57.531 1.00 39.76 C ANISOU 2181 C TYR B 284 5924 4023 5161 121 1047 -373 C ATOM 2182 O TYR A 284 -5.219 36.324 56.435 1.00 39.15 O ANISOU 2182 O TYR B 284 5784 4005 5089 150 1006 -364 O ATOM 2183 CB TYR A 284 -3.813 35.711 58.964 1.00 39.47 C ANISOU 2183 CB TYR B 284 5874 4003 5122 50 1041 -431 C ATOM 2184 CG TYR A 284 -2.948 36.040 60.139 1.00 40.13 C ANISOU 2184 CG TYR B 284 5972 4060 5215 27 1080 -464 C ATOM 2185 CD1 TYR A 284 -1.805 36.820 59.980 1.00 40.67 C ANISOU 2185 CD1 TYR B 284 5978 4154 5319 58 1099 -486 C ATOM 2186 CD2 TYR A 284 -3.328 35.664 61.430 1.00 41.55 C ANISOU 2186 CD2 TYR B 284 6233 4187 5368 -25 1104 -476 C ATOM 2187 CE1 TYR A 284 -1.047 37.204 61.072 1.00 42.21 C ANISOU 2187 CE1 TYR B 284 6192 4321 5527 36 1146 -518 C ATOM 2188 CE2 TYR A 284 -2.568 36.028 62.536 1.00 41.74 C ANISOU 2188 CE2 TYR B 284 6280 4182 5397 -45 1147 -506 C ATOM 2189 CZ TYR A 284 -1.430 36.805 62.346 1.00 41.76 C ANISOU 2189 CZ TYR B 284 6220 4207 5439 -14 1171 -526 C ATOM 2190 OH TYR A 284 -0.666 37.170 63.426 1.00 42.56 O ANISOU 2190 OH TYR B 284 6346 4278 5548 -35 1220 -556 O ATOM 2191 N SER A 285 -7.044 36.643 57.726 1.00 39.74 N ANISOU 2191 N SER B 285 5987 3969 5143 111 1070 -353 N ATOM 2192 CA SER A 285 -7.996 36.338 56.666 1.00 40.18 C ANISOU 2192 CA SER B 285 6047 4033 5186 130 1049 -319 C ATOM 2193 C SER A 285 -7.916 37.312 55.468 1.00 40.85 C ANISOU 2193 C SER B 285 6082 4147 5291 213 1049 -294 C ATOM 2194 O SER A 285 -8.348 36.975 54.364 1.00 39.94 O ANISOU 2194 O SER B 285 5953 4058 5164 236 1021 -266 O ATOM 2195 CB SER A 285 -9.417 36.307 57.229 1.00 40.72 C ANISOU 2195 CB SER B 285 6200 4033 5238 98 1084 -308 C ATOM 2196 OG SER A 285 -9.831 37.608 57.574 1.00 40.51 O ANISOU 2196 OG SER B 285 6205 3957 5230 136 1142 -304 O ATOM 2197 N SER A 286 -7.368 38.509 55.685 1.00 41.58 N ANISOU 2197 N SER B 286 6150 4236 5413 259 1081 -306 N ATOM 2198 CA SER A 286 -7.200 39.479 54.587 1.00 43.05 C ANISOU 2198 CA SER B 286 6284 4455 5619 344 1076 -286 C ATOM 2199 C SER A 286 -5.901 39.301 53.772 1.00 43.07 C ANISOU 2199 C SER B 286 6193 4540 5633 369 1025 -300 C ATOM 2200 O SER A 286 -5.677 40.040 52.810 1.00 43.76 O ANISOU 2200 O SER B 286 6229 4665 5732 440 1011 -288 O ATOM 2201 CB SER A 286 -7.280 40.918 55.117 1.00 43.44 C ANISOU 2201 CB SER B 286 6343 4465 5698 390 1133 -291 C ATOM 2202 OG SER A 286 -6.210 41.170 56.012 1.00 45.96 O ANISOU 2202 OG SER B 286 6635 4789 6041 368 1150 -332 O ATOM 2203 N LEU A 287 -5.042 38.347 54.145 1.00 42.39 N ANISOU 2203 N LEU B 287 6084 4481 5541 313 998 -328 N ATOM 2204 CA LEU A 287 -3.782 38.163 53.435 1.00 42.14 C ANISOU 2204 CA LEU B 287 5967 4522 5520 330 955 -346 C ATOM 2205 C LEU A 287 -4.049 37.493 52.085 1.00 42.09 C ANISOU 2205 C LEU B 287 5938 4565 5492 351 903 -318 C ATOM 2206 O LEU A 287 -4.874 36.576 51.996 1.00 41.90 O ANISOU 2206 O LEU B 287 5959 4521 5438 315 891 -297 O ATOM 2207 CB LEU A 287 -2.811 37.313 54.245 1.00 41.49 C ANISOU 2207 CB LEU B 287 5878 4450 5438 265 947 -382 C ATOM 2208 CG LEU A 287 -2.088 37.857 55.471 1.00 42.55 C ANISOU 2208 CG LEU B 287 6017 4553 5596 242 993 -418 C ATOM 2209 CD1 LEU A 287 -1.212 36.737 55.993 1.00 42.01 C ANISOU 2209 CD1 LEU B 287 5946 4500 5515 180 973 -444 C ATOM 2210 CD2 LEU A 287 -1.242 39.099 55.179 1.00 41.84 C ANISOU 2210 CD2 LEU B 287 5856 4493 5549 298 1010 -439 C ATOM 2211 N SER A 288 -3.369 37.944 51.032 1.00 42.22 N ANISOU 2211 N SER B 288 5881 4641 5518 407 872 -319 N ATOM 2212 CA SER A 288 -3.444 37.232 49.749 1.00 42.39 C ANISOU 2212 CA SER B 288 5877 4714 5515 424 821 -297 C ATOM 2213 C SER A 288 -2.603 35.957 49.874 1.00 42.20 C ANISOU 2213 C SER B 288 5829 4722 5481 362 787 -322 C ATOM 2214 O SER A 288 -1.775 35.846 50.784 1.00 41.48 O ANISOU 2214 O SER B 288 5728 4625 5408 323 800 -357 O ATOM 2215 CB SER A 288 -2.913 38.086 48.596 1.00 42.48 C ANISOU 2215 CB SER B 288 5819 4786 5537 503 794 -294 C ATOM 2216 OG SER A 288 -1.517 38.299 48.719 1.00 42.02 O ANISOU 2216 OG SER B 288 5686 4774 5506 500 780 -339 O ATOM 2217 N LEU A 289 -2.807 35.002 48.965 1.00 42.62 N ANISOU 2217 N LEU B 289 5878 4808 5509 355 746 -303 N ATOM 2218 CA LEU A 289 -1.953 33.806 48.931 1.00 42.53 C ANISOU 2218 CA LEU B 289 5837 4832 5489 306 712 -325 C ATOM 2219 C LEU A 289 -0.496 34.205 48.863 1.00 42.35 C ANISOU 2219 C LEU B 289 5742 4857 5493 318 701 -364 C ATOM 2220 O LEU A 289 0.305 33.713 49.647 1.00 41.98 O ANISOU 2220 O LEU B 289 5689 4806 5455 269 707 -395 O ATOM 2221 CB LEU A 289 -2.326 32.837 47.782 1.00 42.86 C ANISOU 2221 CB LEU B 289 5875 4908 5501 307 671 -299 C ATOM 2222 CG LEU A 289 -3.167 31.601 48.141 1.00 44.15 C ANISOU 2222 CG LEU B 289 6095 5039 5642 248 670 -284 C ATOM 2223 CD1 LEU A 289 -3.432 30.734 46.903 1.00 45.67 C ANISOU 2223 CD1 LEU B 289 6274 5269 5810 255 633 -261 C ATOM 2224 CD2 LEU A 289 -2.521 30.762 49.247 1.00 43.26 C ANISOU 2224 CD2 LEU B 289 5989 4914 5534 183 669 -315 C ATOM 2225 N ASP A 290 -0.154 35.125 47.962 1.00 43.33 N ANISOU 2225 N ASP B 290 5812 5025 5629 383 686 -365 N ATOM 2226 CA ASP A 290 1.238 35.596 47.850 1.00 44.44 C ANISOU 2226 CA ASP B 290 5874 5214 5798 395 676 -408 C ATOM 2227 C ASP A 290 1.784 36.073 49.190 1.00 43.51 C ANISOU 2227 C ASP B 290 5761 5057 5712 363 723 -442 C ATOM 2228 O ASP A 290 2.861 35.663 49.607 1.00 43.67 O ANISOU 2228 O ASP B 290 5754 5093 5747 323 724 -479 O ATOM 2229 CB ASP A 290 1.370 36.709 46.798 1.00 46.01 C ANISOU 2229 CB ASP B 290 6015 5460 6006 476 657 -404 C ATOM 2230 CG ASP A 290 1.534 36.165 45.393 1.00 49.45 C ANISOU 2230 CG ASP B 290 6417 5959 6414 502 601 -392 C ATOM 2231 OD1 ASP A 290 2.432 35.308 45.194 1.00 51.08 O ANISOU 2231 OD1 ASP B 290 6590 6201 6618 463 576 -418 O ATOM 2232 OD2 ASP A 290 0.765 36.600 44.490 1.00 52.93 O ANISOU 2232 OD2 ASP B 290 6868 6410 6834 562 586 -356 O ATOM 2233 N GLU A 291 1.013 36.930 49.856 1.00 43.35 N ANISOU 2233 N GLU B 291 5784 4985 5702 381 766 -429 N ATOM 2234 CA GLU A 291 1.286 37.411 51.221 1.00 42.69 C ANISOU 2234 CA GLU B 291 5724 4852 5645 351 820 -455 C ATOM 2235 C GLU A 291 1.378 36.299 52.271 1.00 41.45 C ANISOU 2235 C GLU B 291 5622 4657 5471 272 832 -465 C ATOM 2236 O GLU A 291 2.263 36.345 53.149 1.00 40.25 O ANISOU 2236 O GLU B 291 5463 4493 5339 238 860 -501 O ATOM 2237 CB GLU A 291 0.218 38.436 51.636 1.00 42.50 C ANISOU 2237 CB GLU B 291 5747 4774 5627 386 862 -431 C ATOM 2238 CG GLU A 291 0.417 39.785 50.944 1.00 44.90 C ANISOU 2238 CG GLU B 291 5990 5111 5960 467 863 -434 C ATOM 2239 CD GLU A 291 -0.813 40.688 50.944 1.00 45.49 C ANISOU 2239 CD GLU B 291 6112 5140 6032 518 893 -397 C ATOM 2240 OE1 GLU A 291 -1.895 40.303 51.458 1.00 47.36 O ANISOU 2240 OE1 GLU B 291 6432 5317 6245 489 916 -370 O ATOM 2241 OE2 GLU A 291 -0.694 41.790 50.375 1.00 48.24 O ANISOU 2241 OE2 GLU B 291 6413 5516 6402 591 892 -397 O ATOM 2242 N SER A 292 0.486 35.303 52.171 1.00 40.50 N ANISOU 2242 N SER B 292 5554 4518 5314 245 812 -434 N ATOM 2243 CA SER A 292 0.500 34.160 53.108 1.00 40.42 C ANISOU 2243 CA SER B 292 5595 4477 5284 175 814 -442 C ATOM 2244 C SER A 292 1.828 33.395 53.167 1.00 41.06 C ANISOU 2244 C SER B 292 5637 4594 5369 141 795 -473 C ATOM 2245 O SER A 292 2.170 32.845 54.228 1.00 41.45 O ANISOU 2245 O SER B 292 5724 4612 5412 92 813 -490 O ATOM 2246 CB SER A 292 -0.649 33.183 52.862 1.00 39.49 C ANISOU 2246 CB SER B 292 5529 4344 5131 153 790 -407 C ATOM 2247 OG SER A 292 -0.456 32.436 51.672 1.00 39.37 O ANISOU 2247 OG SER B 292 5473 4384 5103 164 741 -396 O ATOM 2248 N TYR A 293 2.582 33.360 52.071 1.00 41.51 N ANISOU 2248 N TYR B 293 5624 4714 5436 168 761 -483 N ATOM 2249 CA TYR A 293 3.820 32.553 52.071 1.00 42.95 C ANISOU 2249 CA TYR B 293 5772 4927 5621 133 744 -513 C ATOM 2250 C TYR A 293 4.971 33.210 52.830 1.00 44.72 C ANISOU 2250 C TYR B 293 5970 5144 5879 121 785 -557 C ATOM 2251 O TYR A 293 5.836 32.511 53.377 1.00 45.71 O ANISOU 2251 O TYR B 293 6100 5263 6003 78 792 -581 O ATOM 2252 CB TYR A 293 4.317 32.185 50.669 1.00 42.05 C ANISOU 2252 CB TYR B 293 5593 4882 5502 158 695 -513 C ATOM 2253 CG TYR A 293 3.306 31.715 49.647 1.00 39.97 C ANISOU 2253 CG TYR B 293 5341 4637 5210 181 657 -472 C ATOM 2254 CD1 TYR A 293 3.263 32.326 48.392 1.00 40.51 C ANISOU 2254 CD1 TYR B 293 5360 4754 5279 239 630 -463 C ATOM 2255 CD2 TYR A 293 2.440 30.655 49.898 1.00 38.66 C ANISOU 2255 CD2 TYR B 293 5233 4442 5014 147 647 -445 C ATOM 2256 CE1 TYR A 293 2.373 31.924 47.411 1.00 42.11 C ANISOU 2256 CE1 TYR B 293 5576 4970 5452 263 600 -425 C ATOM 2257 CE2 TYR A 293 1.528 30.217 48.904 1.00 39.65 C ANISOU 2257 CE2 TYR B 293 5367 4583 5114 167 617 -410 C ATOM 2258 CZ TYR A 293 1.506 30.872 47.664 1.00 41.61 C ANISOU 2258 CZ TYR B 293 5571 4875 5363 225 597 -399 C ATOM 2259 OH TYR A 293 0.633 30.515 46.651 1.00 42.08 O ANISOU 2259 OH TYR B 293 5643 4948 5396 248 573 -363 O ATOM 2260 N GLN A 294 4.999 34.542 52.866 1.00 46.91 N ANISOU 2260 N GLN B 294 6217 5418 6187 160 814 -568 N ATOM 2261 CA GLN A 294 6.059 35.257 53.610 1.00 48.08 C ANISOU 2261 CA GLN B 294 6338 5557 6374 148 860 -613 C ATOM 2262 C GLN A 294 5.675 35.859 54.967 1.00 47.95 C ANISOU 2262 C GLN B 294 6383 5470 6366 132 921 -616 C ATOM 2263 O GLN A 294 6.444 36.627 55.524 1.00 48.67 O ANISOU 2263 O GLN B 294 6448 5551 6492 129 966 -652 O ATOM 2264 CB GLN A 294 6.712 36.346 52.747 1.00 49.08 C ANISOU 2264 CB GLN B 294 6372 5737 6539 200 853 -638 C ATOM 2265 CG GLN A 294 8.114 36.000 52.248 1.00 51.54 C ANISOU 2265 CG GLN B 294 6612 6101 6869 182 836 -680 C ATOM 2266 CD GLN A 294 8.112 35.553 50.800 1.00 54.35 C ANISOU 2266 CD GLN B 294 6921 6524 7207 211 771 -668 C ATOM 2267 OE1 GLN A 294 7.328 36.055 49.990 1.00 56.02 O ANISOU 2267 OE1 GLN B 294 7120 6758 7409 265 744 -639 O ATOM 2268 NE2 GLN A 294 8.988 34.604 50.463 1.00 54.65 N ANISOU 2268 NE2 GLN B 294 6936 6591 7236 176 749 -688 N ATOM 2269 N SER A 295 4.517 35.525 55.521 1.00 47.36 N ANISOU 2269 N SER B 295 6387 5347 6260 118 926 -583 N ATOM 2270 CA SER A 295 4.160 36.106 56.818 1.00 47.03 C ANISOU 2270 CA SER B 295 6407 5239 6224 101 985 -589 C ATOM 2271 C SER A 295 4.634 35.269 58.004 1.00 46.68 C ANISOU 2271 C SER B 295 6421 5155 6160 39 1008 -606 C ATOM 2272 O SER A 295 4.123 34.180 58.253 1.00 45.61 O ANISOU 2272 O SER B 295 6340 5006 5985 6 982 -586 O ATOM 2273 CB SER A 295 2.671 36.385 56.922 1.00 47.15 C ANISOU 2273 CB SER B 295 6481 5215 6220 119 990 -551 C ATOM 2274 OG SER A 295 2.315 36.614 58.272 1.00 46.41 O ANISOU 2274 OG SER B 295 6462 5054 6120 88 1042 -558 O ATOM 2275 N ARG A 296 5.597 35.814 58.748 1.00 46.76 N ANISOU 2275 N ARG B 296 6422 5147 6198 24 1059 -643 N ATOM 2276 CA ARG A 296 6.130 35.163 59.934 1.00 46.92 C ANISOU 2276 CA ARG B 296 6503 5126 6200 -30 1090 -659 C ATOM 2277 C ARG A 296 5.051 35.025 60.986 1.00 45.87 C ANISOU 2277 C ARG B 296 6468 4929 6031 -51 1110 -639 C ATOM 2278 O ARG A 296 5.006 34.014 61.687 1.00 45.92 O ANISOU 2278 O ARG B 296 6537 4911 5998 -92 1101 -634 O ATOM 2279 CB ARG A 296 7.293 35.974 60.505 1.00 47.96 C ANISOU 2279 CB ARG B 296 6605 5244 6372 -37 1152 -704 C ATOM 2280 CG ARG A 296 8.397 35.142 61.120 1.00 51.90 C ANISOU 2280 CG ARG B 296 7127 5733 6861 -85 1168 -728 C ATOM 2281 CD ARG A 296 9.757 35.656 60.645 1.00 56.71 C ANISOU 2281 CD ARG B 296 7648 6379 7520 -81 1190 -772 C ATOM 2282 NE ARG A 296 9.651 36.101 59.252 1.00 61.19 N ANISOU 2282 NE ARG B 296 8124 7013 8112 -34 1143 -769 N ATOM 2283 CZ ARG A 296 10.352 37.094 58.699 1.00 63.75 C ANISOU 2283 CZ ARG B 296 8359 7374 8488 -7 1159 -803 C ATOM 2284 NH1 ARG A 296 11.254 37.772 59.407 1.00 64.65 N ANISOU 2284 NH1 ARG B 296 8457 7465 8641 -25 1225 -846 N ATOM 2285 NH2 ARG A 296 10.150 37.402 57.421 1.00 64.01 N ANISOU 2285 NH2 ARG B 296 8318 7469 8534 40 1107 -795 N ATOM 2286 N ASP A 297 4.200 36.049 61.101 1.00 45.14 N ANISOU 2286 N ASP B 297 6388 4810 5952 -22 1137 -628 N ATOM 2287 CA ASP A 297 3.120 36.073 62.092 1.00 44.03 C ANISOU 2287 CA ASP B 297 6340 4607 5781 -41 1162 -612 C ATOM 2288 C ASP A 297 2.138 34.943 61.834 1.00 42.03 C ANISOU 2288 C ASP B 297 6127 4358 5483 -59 1106 -580 C ATOM 2289 O ASP A 297 1.772 34.219 62.755 1.00 40.64 O ANISOU 2289 O ASP B 297 6027 4146 5269 -100 1107 -577 O ATOM 2290 CB ASP A 297 2.395 37.419 62.074 1.00 44.92 C ANISOU 2290 CB ASP B 297 6450 4694 5921 1 1201 -606 C ATOM 2291 CG ASP A 297 3.180 38.532 62.783 1.00 48.23 C ANISOU 2291 CG ASP B 297 6856 5087 6381 8 1273 -641 C ATOM 2292 OD1 ASP A 297 2.829 39.732 62.583 1.00 50.06 O ANISOU 2292 OD1 ASP B 297 7062 5311 6647 52 1304 -640 O ATOM 2293 OD2 ASP A 297 4.125 38.205 63.544 1.00 48.49 O ANISOU 2293 OD2 ASP B 297 6905 5106 6412 -30 1300 -668 O ATOM 2294 N LEU A 298 1.729 34.795 60.569 1.00 41.05 N ANISOU 2294 N LEU B 298 5953 4281 5364 -27 1058 -557 N ATOM 2295 CA LEU A 298 0.933 33.634 60.131 1.00 39.95 C ANISOU 2295 CA LEU B 298 5836 4155 5187 -45 1003 -529 C ATOM 2296 C LEU A 298 1.600 32.321 60.534 1.00 38.88 C ANISOU 2296 C LEU B 298 5718 4030 5024 -89 975 -539 C ATOM 2297 O LEU A 298 0.954 31.452 61.112 1.00 37.27 O ANISOU 2297 O LEU B 298 5574 3803 4782 -124 957 -528 O ATOM 2298 CB LEU A 298 0.731 33.643 58.615 1.00 40.02 C ANISOU 2298 CB LEU B 298 5778 4221 5208 -3 959 -508 C ATOM 2299 CG LEU A 298 -0.547 33.098 57.966 1.00 40.90 C ANISOU 2299 CG LEU B 298 5912 4335 5295 1 923 -472 C ATOM 2300 CD1 LEU A 298 -0.210 32.572 56.613 1.00 40.28 C ANISOU 2300 CD1 LEU B 298 5768 4321 5218 24 872 -461 C ATOM 2301 CD2 LEU A 298 -1.320 32.065 58.779 1.00 41.11 C ANISOU 2301 CD2 LEU B 298 6011 4326 5282 -51 912 -465 C ATOM 2302 N GLU A 299 2.895 32.181 60.239 1.00 39.41 N ANISOU 2302 N GLU B 299 5733 4133 5110 -88 972 -561 N ATOM 2303 CA GLU A 299 3.631 30.950 60.632 1.00 39.83 C ANISOU 2303 CA GLU B 299 5804 4192 5137 -126 951 -570 C ATOM 2304 C GLU A 299 3.454 30.596 62.091 1.00 39.43 C ANISOU 2304 C GLU B 299 5844 4085 5054 -166 978 -576 C ATOM 2305 O GLU A 299 3.154 29.446 62.425 1.00 39.00 O ANISOU 2305 O GLU B 299 5831 4027 4960 -193 943 -565 O ATOM 2306 CB GLU A 299 5.114 31.043 60.305 1.00 40.66 C ANISOU 2306 CB GLU B 299 5850 4329 5271 -123 963 -599 C ATOM 2307 CG GLU A 299 5.408 30.877 58.834 1.00 43.10 C ANISOU 2307 CG GLU B 299 6075 4704 5597 -95 917 -593 C ATOM 2308 CD GLU A 299 6.833 30.435 58.587 1.00 47.59 C ANISOU 2308 CD GLU B 299 6600 5302 6179 -108 916 -621 C ATOM 2309 OE1 GLU A 299 7.722 30.891 59.339 1.00 48.38 O ANISOU 2309 OE1 GLU B 299 6707 5378 6299 -123 967 -651 O ATOM 2310 OE2 GLU A 299 7.054 29.631 57.638 1.00 50.36 O ANISOU 2310 OE2 GLU B 299 6912 5700 6523 -104 869 -613 O ATOM 2311 N LYS A 300 3.590 31.596 62.961 1.00 39.58 N ANISOU 2311 N LYS B 300 5893 4059 5086 -166 1039 -594 N ATOM 2312 CA LYS A 300 3.581 31.347 64.398 1.00 39.01 C ANISOU 2312 CA LYS B 300 5909 3931 4980 -203 1071 -604 C ATOM 2313 C LYS A 300 2.202 30.991 64.897 1.00 37.03 C ANISOU 2313 C LYS B 300 5728 3651 4692 -219 1052 -584 C ATOM 2314 O LYS A 300 2.039 30.120 65.728 1.00 36.57 O ANISOU 2314 O LYS B 300 5734 3571 4590 -251 1037 -583 O ATOM 2315 CB LYS A 300 4.167 32.541 65.175 1.00 40.95 C ANISOU 2315 CB LYS B 300 6168 4137 5254 -200 1148 -631 C ATOM 2316 CG LYS A 300 5.398 33.183 64.507 1.00 45.22 C ANISOU 2316 CG LYS B 300 6623 4712 5847 -178 1172 -655 C ATOM 2317 CD LYS A 300 6.399 33.693 65.561 1.00 50.99 C ANISOU 2317 CD LYS B 300 7383 5400 6590 -198 1245 -689 C ATOM 2318 CE LYS A 300 7.077 35.019 65.151 1.00 53.98 C ANISOU 2318 CE LYS B 300 7684 5793 7033 -170 1293 -716 C ATOM 2319 NZ LYS A 300 8.205 35.394 66.089 1.00 53.16 N ANISOU 2319 NZ LYS B 300 7601 5652 6946 -195 1367 -753 N ATOM 2320 N VAL A 301 1.187 31.670 64.395 1.00 36.75 N ANISOU 2320 N VAL B 301 5680 3612 4671 -196 1053 -568 N ATOM 2321 CA VAL A 301 -0.184 31.323 64.763 1.00 35.91 C ANISOU 2321 CA VAL B 301 5635 3478 4532 -215 1036 -552 C ATOM 2322 C VAL A 301 -0.556 29.918 64.244 1.00 34.85 C ANISOU 2322 C VAL B 301 5492 3381 4369 -232 965 -535 C ATOM 2323 O VAL A 301 -1.189 29.131 64.957 1.00 34.69 O ANISOU 2323 O VAL B 301 5531 3341 4309 -266 944 -533 O ATOM 2324 CB VAL A 301 -1.190 32.379 64.259 1.00 35.59 C ANISOU 2324 CB VAL B 301 5584 3424 4516 -184 1057 -537 C ATOM 2325 CG1 VAL A 301 -2.581 31.818 64.267 1.00 36.60 C ANISOU 2325 CG1 VAL B 301 5755 3536 4614 -204 1029 -518 C ATOM 2326 CG2 VAL A 301 -1.120 33.630 65.122 1.00 37.28 C ANISOU 2326 CG2 VAL B 301 5832 3585 4747 -176 1130 -554 C ATOM 2327 N SER A 302 -0.176 29.615 63.005 1.00 33.93 N ANISOU 2327 N SER B 302 5299 3319 4273 -209 929 -524 N ATOM 2328 CA SER A 302 -0.433 28.269 62.434 1.00 33.71 C ANISOU 2328 CA SER B 302 5257 3330 4223 -223 865 -509 C ATOM 2329 C SER A 302 0.216 27.215 63.327 1.00 34.06 C ANISOU 2329 C SER B 302 5341 3369 4234 -256 849 -521 C ATOM 2330 O SER A 302 -0.416 26.226 63.667 1.00 33.40 O ANISOU 2330 O SER B 302 5292 3284 4116 -282 811 -515 O ATOM 2331 CB SER A 302 0.105 28.140 61.009 1.00 32.90 C ANISOU 2331 CB SER B 302 5068 3286 4147 -192 836 -499 C ATOM 2332 OG SER A 302 -0.444 29.109 60.145 1.00 32.06 O ANISOU 2332 OG SER B 302 4926 3187 4068 -155 848 -486 O ATOM 2333 N GLN A 303 1.473 27.475 63.711 1.00 35.58 N ANISOU 2333 N GLN B 303 5528 3556 4436 -254 880 -541 N ATOM 2334 CA GLN A 303 2.234 26.659 64.664 1.00 37.69 C ANISOU 2334 CA GLN B 303 5842 3808 4671 -279 878 -553 C ATOM 2335 C GLN A 303 1.563 26.436 66.028 1.00 37.41 C ANISOU 2335 C GLN B 303 5901 3724 4591 -309 887 -557 C ATOM 2336 O GLN A 303 1.464 25.294 66.470 1.00 36.89 O ANISOU 2336 O GLN B 303 5870 3662 4485 -329 846 -553 O ATOM 2337 CB GLN A 303 3.677 27.183 64.804 1.00 37.98 C ANISOU 2337 CB GLN B 303 5857 3841 4732 -272 925 -575 C ATOM 2338 CG GLN A 303 4.556 26.743 63.584 1.00 41.71 C ANISOU 2338 CG GLN B 303 6246 4371 5231 -255 895 -575 C ATOM 2339 CD GLN A 303 6.050 27.028 63.724 1.00 41.67 C ANISOU 2339 CD GLN B 303 6220 4365 5249 -255 937 -601 C ATOM 2340 OE1 GLN A 303 6.856 26.111 63.982 1.00 46.98 O ANISOU 2340 OE1 GLN B 303 6909 5039 5901 -269 928 -606 O ATOM 2341 NE2 GLN A 303 6.433 28.298 63.539 1.00 48.04 N ANISOU 2341 NE2 GLN B 303 6988 5166 6098 -238 985 -619 N ATOM 2342 N GLN A 304 1.103 27.517 66.676 1.00 37.72 N ANISOU 2342 N GLN B 304 5979 3717 4634 -310 938 -565 N ATOM 2343 CA GLN A 304 0.265 27.448 67.894 1.00 38.59 C ANISOU 2343 CA GLN B 304 6180 3779 4703 -338 947 -571 C ATOM 2344 C GLN A 304 -1.004 26.578 67.791 1.00 37.88 C ANISOU 2344 C GLN B 304 6108 3702 4584 -357 890 -558 C ATOM 2345 O GLN A 304 -1.332 25.793 68.687 1.00 38.41 O ANISOU 2345 O GLN B 304 6236 3754 4604 -385 864 -563 O ATOM 2346 CB GLN A 304 -0.209 28.869 68.271 1.00 38.96 C ANISOU 2346 CB GLN B 304 6252 3781 4771 -330 1011 -579 C ATOM 2347 CG GLN A 304 0.861 29.802 68.793 1.00 42.19 C ANISOU 2347 CG GLN B 304 6667 4162 5202 -321 1080 -599 C ATOM 2348 CD GLN A 304 0.372 31.238 68.954 1.00 42.48 C ANISOU 2348 CD GLN B 304 6711 4160 5269 -305 1142 -605 C ATOM 2349 OE1 GLN A 304 -0.822 31.497 69.182 1.00 45.82 O ANISOU 2349 OE1 GLN B 304 7172 4557 5679 -313 1143 -598 O ATOM 2350 NE2 GLN A 304 1.302 32.181 68.823 1.00 47.92 N ANISOU 2350 NE2 GLN B 304 7360 4847 6001 -284 1194 -620 N ATOM 2351 N LEU A 305 -1.754 26.783 66.721 1.00 36.72 N ANISOU 2351 N LEU B 305 5908 3578 4465 -343 872 -542 N ATOM 2352 CA LEU A 305 -2.925 25.980 66.380 1.00 37.15 C ANISOU 2352 CA LEU B 305 5962 3649 4503 -360 822 -530 C ATOM 2353 C LEU A 305 -2.658 24.475 66.184 1.00 36.08 C ANISOU 2353 C LEU B 305 5808 3556 4343 -373 756 -525 C ATOM 2354 O LEU A 305 -3.405 23.611 66.652 1.00 35.70 O ANISOU 2354 O LEU B 305 5794 3509 4263 -401 717 -528 O ATOM 2355 CB LEU A 305 -3.359 26.471 65.018 1.00 37.22 C ANISOU 2355 CB LEU B 305 5904 3684 4553 -332 820 -511 C ATOM 2356 CG LEU A 305 -4.771 26.770 64.746 1.00 41.04 C ANISOU 2356 CG LEU B 305 6402 4150 5041 -339 823 -501 C ATOM 2357 CD1 LEU A 305 -5.620 25.644 65.345 1.00 44.11 C ANISOU 2357 CD1 LEU B 305 6833 4535 5390 -383 780 -508 C ATOM 2358 CD2 LEU A 305 -4.948 28.155 65.384 1.00 42.11 C ANISOU 2358 CD2 LEU B 305 6580 4232 5188 -330 890 -510 C ATOM 2359 N ALA A 306 -1.599 24.193 65.429 1.00 35.56 N ANISOU 2359 N ALA B 306 5684 3529 4298 -350 744 -520 N ATOM 2360 CA ALA A 306 -1.251 22.843 64.991 1.00 35.64 C ANISOU 2360 CA ALA B 306 5663 3583 4295 -353 687 -513 C ATOM 2361 C ALA A 306 -0.643 22.015 66.115 1.00 36.82 C ANISOU 2361 C ALA B 306 5868 3721 4401 -370 672 -524 C ATOM 2362 O ALA A 306 -0.668 20.779 66.052 1.00 35.86 O ANISOU 2362 O ALA B 306 5739 3627 4257 -377 619 -519 O ATOM 2363 CB ALA A 306 -0.289 22.947 63.815 1.00 34.21 C ANISOU 2363 CB ALA B 306 5405 3443 4150 -323 687 -505 C ATOM 2364 N LYS A 307 -0.142 22.715 67.153 1.00 38.93 N ANISOU 2364 N LYS B 307 6194 3943 4655 -374 722 -538 N ATOM 2365 CA LYS A 307 0.684 22.149 68.248 1.00 40.33 C ANISOU 2365 CA LYS B 307 6432 4100 4790 -382 724 -548 C ATOM 2366 C LYS A 307 0.205 20.803 68.768 1.00 41.10 C ANISOU 2366 C LYS B 307 6564 4212 4840 -399 660 -546 C ATOM 2367 O LYS A 307 0.972 19.828 68.775 1.00 41.32 O ANISOU 2367 O LYS B 307 6588 4262 4851 -390 630 -542 O ATOM 2368 CB LYS A 307 0.802 23.159 69.397 1.00 41.75 C ANISOU 2368 CB LYS B 307 6685 4222 4957 -391 787 -565 C ATOM 2369 CG LYS A 307 1.705 22.815 70.622 1.00 42.53 C ANISOU 2369 CG LYS B 307 6861 4288 5011 -398 807 -575 C ATOM 2370 CD LYS A 307 1.133 23.630 71.824 1.00 47.64 C ANISOU 2370 CD LYS B 307 7593 4877 5630 -417 852 -590 C ATOM 2371 CE LYS A 307 2.148 24.019 72.931 1.00 49.67 C ANISOU 2371 CE LYS B 307 7923 5086 5863 -418 913 -604 C ATOM 2372 NZ LYS A 307 1.564 25.102 73.809 1.00 46.87 N ANISOU 2372 NZ LYS B 307 7632 4677 5499 -433 970 -619 N ATOM 2373 N THR A 308 -1.059 20.733 69.164 1.00 41.31 N ANISOU 2373 N THR B 308 6622 4229 4847 -421 639 -550 N ATOM 2374 CA THR A 308 -1.614 19.514 69.765 1.00 41.79 C ANISOU 2374 CA THR B 308 6715 4304 4861 -438 576 -554 C ATOM 2375 C THR A 308 -1.800 18.372 68.741 1.00 40.75 C ANISOU 2375 C THR B 308 6511 4229 4744 -432 513 -541 C ATOM 2376 O THR A 308 -1.544 17.172 69.047 1.00 40.55 O ANISOU 2376 O THR B 308 6494 4228 4687 -430 462 -540 O ATOM 2377 CB THR A 308 -2.938 19.821 70.535 1.00 43.53 C ANISOU 2377 CB THR B 308 6990 4494 5055 -470 575 -569 C ATOM 2378 OG1 THR A 308 -3.373 18.652 71.261 1.00 45.94 O ANISOU 2378 OG1 THR B 308 7331 4814 5311 -487 512 -578 O ATOM 2379 CG2 THR A 308 -4.074 20.329 69.576 1.00 44.62 C ANISOU 2379 CG2 THR B 308 7077 4640 5236 -478 579 -563 C ATOM 2380 N TYR A 309 -2.237 18.745 67.531 1.00 37.64 N ANISOU 2380 N TYR B 309 6048 3857 4397 -426 518 -530 N ATOM 2381 CA TYR A 309 -2.403 17.797 66.470 1.00 35.50 C ANISOU 2381 CA TYR B 309 5706 3637 4144 -420 469 -518 C ATOM 2382 C TYR A 309 -1.029 17.240 66.051 1.00 33.38 C ANISOU 2382 C TYR B 309 5406 3395 3882 -393 462 -509 C ATOM 2383 O TYR A 309 -0.932 16.070 65.694 1.00 32.06 O ANISOU 2383 O TYR B 309 5208 3265 3709 -388 412 -503 O ATOM 2384 CB TYR A 309 -3.073 18.455 65.273 1.00 35.78 C ANISOU 2384 CB TYR B 309 5684 3684 4226 -415 486 -507 C ATOM 2385 CG TYR A 309 -4.509 18.852 65.471 1.00 36.47 C ANISOU 2385 CG TYR B 309 5796 3749 4313 -442 492 -513 C ATOM 2386 CD1 TYR A 309 -4.905 20.163 65.290 1.00 37.50 C ANISOU 2386 CD1 TYR B 309 5935 3847 4467 -437 546 -511 C ATOM 2387 CD2 TYR A 309 -5.468 17.915 65.812 1.00 34.43 C ANISOU 2387 CD2 TYR B 309 5548 3502 4031 -471 444 -523 C ATOM 2388 CE1 TYR A 309 -6.238 20.537 65.450 1.00 39.97 C ANISOU 2388 CE1 TYR B 309 6273 4134 4780 -462 556 -517 C ATOM 2389 CE2 TYR A 309 -6.787 18.268 65.970 1.00 38.12 C ANISOU 2389 CE2 TYR B 309 6036 3946 4500 -501 453 -532 C ATOM 2390 CZ TYR A 309 -7.161 19.580 65.785 1.00 38.20 C ANISOU 2390 CZ TYR B 309 6061 3920 4534 -496 511 -528 C ATOM 2391 OH TYR A 309 -8.484 19.941 65.947 1.00 46.03 O ANISOU 2391 OH TYR B 309 7078 4883 5526 -526 525 -537 O ATOM 2392 N TYR A 310 0.009 18.086 66.120 1.00 32.03 N ANISOU 2392 N TYR B 310 5243 3203 3725 -377 515 -511 N ATOM 2393 CA TYR A 310 1.382 17.714 65.721 1.00 30.95 C ANISOU 2393 CA TYR B 310 5078 3083 3597 -355 520 -507 C ATOM 2394 C TYR A 310 1.901 16.560 66.568 1.00 31.06 C ANISOU 2394 C TYR B 310 5139 3097 3566 -354 487 -508 C ATOM 2395 O TYR A 310 2.405 15.595 66.031 1.00 29.53 O ANISOU 2395 O TYR B 310 4910 2937 3375 -341 454 -500 O ATOM 2396 CB TYR A 310 2.347 18.903 65.742 1.00 29.78 C ANISOU 2396 CB TYR B 310 4931 2908 3474 -344 587 -516 C ATOM 2397 CG TYR A 310 3.806 18.544 65.429 1.00 31.42 C ANISOU 2397 CG TYR B 310 5117 3130 3692 -328 599 -517 C ATOM 2398 CD1 TYR A 310 4.344 18.698 64.129 1.00 28.30 C ANISOU 2398 CD1 TYR B 310 4641 2771 3340 -311 602 -514 C ATOM 2399 CD2 TYR A 310 4.652 18.036 66.427 1.00 30.39 C ANISOU 2399 CD2 TYR B 310 5049 2974 3525 -328 609 -523 C ATOM 2400 CE1 TYR A 310 5.685 18.390 63.861 1.00 26.39 C ANISOU 2400 CE1 TYR B 310 4381 2539 3108 -300 617 -520 C ATOM 2401 CE2 TYR A 310 5.986 17.716 66.144 1.00 30.47 C ANISOU 2401 CE2 TYR B 310 5042 2991 3546 -316 627 -525 C ATOM 2402 CZ TYR A 310 6.481 17.872 64.857 1.00 28.28 C ANISOU 2402 CZ TYR B 310 4682 2749 3314 -303 630 -525 C ATOM 2403 OH TYR A 310 7.806 17.561 64.624 1.00 31.02 O ANISOU 2403 OH TYR B 310 5016 3099 3670 -295 651 -532 O ATOM 2404 N ASP A 311 1.754 16.653 67.894 1.00 32.65 N ANISOU 2404 N ASP B 311 5422 3259 3723 -367 496 -518 N ATOM 2405 CA ASP A 311 2.228 15.583 68.770 1.00 33.25 C ANISOU 2405 CA ASP B 311 5552 3334 3749 -361 464 -517 C ATOM 2406 C ASP A 311 1.493 14.261 68.497 1.00 31.90 C ANISOU 2406 C ASP B 311 5351 3207 3564 -361 386 -511 C ATOM 2407 O ASP A 311 2.073 13.194 68.618 1.00 32.16 O ANISOU 2407 O ASP B 311 5388 3258 3574 -344 351 -504 O ATOM 2408 CB ASP A 311 2.142 15.980 70.264 1.00 36.04 C ANISOU 2408 CB ASP B 311 6006 3636 4052 -373 488 -530 C ATOM 2409 CG ASP A 311 2.768 17.370 70.573 1.00 40.76 C ANISOU 2409 CG ASP B 311 6633 4186 4668 -375 573 -539 C ATOM 2410 OD1 ASP A 311 2.217 18.078 71.461 1.00 47.39 O ANISOU 2410 OD1 ASP B 311 7533 4986 5486 -392 600 -551 O ATOM 2411 OD2 ASP A 311 3.810 17.761 69.966 1.00 45.85 O ANISOU 2411 OD2 ASP B 311 7240 4832 5349 -361 613 -537 O ATOM 2412 N ALA A 312 0.216 14.312 68.138 1.00 30.85 N ANISOU 2412 N ALA B 312 5187 3090 3444 -381 360 -514 N ATOM 2413 CA ALA A 312 -0.516 13.077 67.832 1.00 29.56 C ANISOU 2413 CA ALA B 312 4987 2971 3274 -385 289 -512 C ATOM 2414 C ALA A 312 -0.233 12.539 66.406 1.00 28.47 C ANISOU 2414 C ALA B 312 4759 2878 3179 -369 272 -498 C ATOM 2415 O ALA A 312 -0.090 11.345 66.201 1.00 29.14 O ANISOU 2415 O ALA B 312 4818 2997 3256 -357 224 -492 O ATOM 2416 CB ALA A 312 -2.025 13.292 68.025 1.00 30.69 C ANISOU 2416 CB ALA B 312 5134 3111 3416 -419 271 -525 C ATOM 2417 N LYS A 313 -0.165 13.430 65.424 1.00 26.72 N ANISOU 2417 N LYS B 313 4492 2658 3004 -367 313 -492 N ATOM 2418 CA LYS A 313 -0.180 13.019 64.012 1.00 25.63 C ANISOU 2418 CA LYS B 313 4270 2562 2905 -356 296 -480 C ATOM 2419 C LYS A 313 1.185 13.044 63.336 1.00 25.00 C ANISOU 2419 C LYS B 313 4160 2493 2846 -330 320 -472 C ATOM 2420 O LYS A 313 1.357 12.433 62.286 1.00 24.12 O ANISOU 2420 O LYS B 313 3987 2419 2757 -318 300 -463 O ATOM 2421 CB LYS A 313 -1.165 13.878 63.209 1.00 24.36 C ANISOU 2421 CB LYS B 313 4074 2402 2780 -369 317 -477 C ATOM 2422 CG LYS A 313 -2.634 13.762 63.685 1.00 24.22 C ANISOU 2422 CG LYS B 313 4077 2376 2749 -401 295 -487 C ATOM 2423 CD LYS A 313 -3.559 14.564 62.758 1.00 24.65 C ANISOU 2423 CD LYS B 313 4097 2428 2840 -410 321 -481 C ATOM 2424 CE LYS A 313 -4.971 14.671 63.335 1.00 23.38 C ANISOU 2424 CE LYS B 313 3968 2247 2667 -445 313 -494 C ATOM 2425 NZ LYS A 313 -5.687 13.381 63.206 1.00 23.55 N ANISOU 2425 NZ LYS B 313 3960 2304 2684 -464 257 -501 N ATOM 2426 N VAL A 314 2.139 13.776 63.911 1.00 24.92 N ANISOU 2426 N VAL B 314 4190 2449 2828 -323 367 -478 N ATOM 2427 CA VAL A 314 3.408 14.016 63.204 1.00 24.53 C ANISOU 2427 CA VAL B 314 4107 2407 2805 -303 399 -476 C ATOM 2428 C VAL A 314 4.630 13.582 64.001 1.00 25.59 C ANISOU 2428 C VAL B 314 4291 2520 2912 -292 413 -480 C ATOM 2429 O VAL A 314 5.540 12.977 63.457 1.00 24.76 O ANISOU 2429 O VAL B 314 4158 2434 2817 -276 410 -476 O ATOM 2430 CB VAL A 314 3.558 15.497 62.714 1.00 24.46 C ANISOU 2430 CB VAL B 314 4076 2385 2834 -302 454 -482 C ATOM 2431 CG1 VAL A 314 4.823 15.646 61.860 1.00 22.55 C ANISOU 2431 CG1 VAL B 314 3786 2160 2621 -285 479 -485 C ATOM 2432 CG2 VAL A 314 2.356 15.913 61.887 1.00 21.93 C ANISOU 2432 CG2 VAL B 314 3713 2083 2538 -308 442 -475 C ATOM 2433 N GLN A 315 4.619 13.844 65.305 1.00 26.55 N ANISOU 2433 N GLN B 315 4491 2600 2996 -301 430 -487 N ATOM 2434 CA GLN A 315 5.813 13.622 66.126 1.00 26.90 C ANISOU 2434 CA GLN B 315 4595 2613 3013 -290 457 -490 C ATOM 2435 C GLN A 315 6.422 12.203 66.055 1.00 26.45 C ANISOU 2435 C GLN B 315 4537 2578 2935 -269 417 -479 C ATOM 2436 O GLN A 315 7.648 12.071 66.089 1.00 26.29 O ANISOU 2436 O GLN B 315 4532 2542 2915 -256 450 -480 O ATOM 2437 CB GLN A 315 5.558 14.075 67.579 1.00 28.11 C ANISOU 2437 CB GLN B 315 4840 2718 3122 -302 478 -498 C ATOM 2438 CG GLN A 315 6.745 13.954 68.524 1.00 28.90 C ANISOU 2438 CG GLN B 315 5015 2777 3189 -292 516 -501 C ATOM 2439 CD GLN A 315 7.009 12.529 68.943 1.00 35.02 C ANISOU 2439 CD GLN B 315 5822 3564 3919 -272 466 -488 C ATOM 2440 OE1 GLN A 315 6.089 11.704 68.977 1.00 37.26 O ANISOU 2440 OE1 GLN B 315 6095 3879 4184 -270 399 -482 O ATOM 2441 NE2 GLN A 315 8.294 12.212 69.258 1.00 35.68 N ANISOU 2441 NE2 GLN B 315 5946 3624 3989 -255 499 -485 N ATOM 2442 N PRO A 316 5.589 11.148 65.990 1.00 26.53 N ANISOU 2442 N PRO B 316 4531 2621 2928 -265 350 -470 N ATOM 2443 CA PRO A 316 6.144 9.795 65.833 1.00 26.13 C ANISOU 2443 CA PRO B 316 4473 2594 2863 -241 312 -459 C ATOM 2444 C PRO A 316 6.838 9.528 64.490 1.00 25.29 C ANISOU 2444 C PRO B 316 4290 2518 2800 -228 320 -454 C ATOM 2445 O PRO A 316 7.400 8.451 64.315 1.00 25.72 O ANISOU 2445 O PRO B 316 4338 2588 2845 -206 296 -445 O ATOM 2446 CB PRO A 316 4.912 8.889 65.915 1.00 26.21 C ANISOU 2446 CB PRO B 316 4463 2638 2856 -244 239 -456 C ATOM 2447 CG PRO A 316 3.838 9.733 66.589 1.00 26.59 C ANISOU 2447 CG PRO B 316 4545 2665 2891 -272 244 -467 C ATOM 2448 CD PRO A 316 4.107 11.113 66.078 1.00 27.44 C ANISOU 2448 CD PRO B 316 4634 2752 3038 -284 309 -473 C ATOM 2449 N THR A 317 6.778 10.473 63.552 1.00 24.56 N ANISOU 2449 N THR B 317 4144 2436 2754 -240 351 -460 N ATOM 2450 CA THR A 317 7.436 10.327 62.228 1.00 22.43 C ANISOU 2450 CA THR B 317 3803 2196 2524 -230 360 -459 C ATOM 2451 C THR A 317 8.807 10.978 62.229 1.00 23.29 C ANISOU 2451 C THR B 317 3925 2278 2646 -227 422 -471 C ATOM 2452 O THR A 317 9.428 11.115 61.178 1.00 23.21 O ANISOU 2452 O THR B 317 3859 2289 2670 -223 439 -476 O ATOM 2453 CB THR A 317 6.603 10.977 61.099 1.00 22.40 C ANISOU 2453 CB THR B 317 3728 2223 2560 -241 356 -459 C ATOM 2454 OG1 THR A 317 6.704 12.408 61.174 1.00 20.20 O ANISOU 2454 OG1 THR B 317 3456 1920 2299 -251 407 -471 O ATOM 2455 CG2 THR A 317 5.124 10.570 61.169 1.00 18.83 C ANISOU 2455 CG2 THR B 317 3267 1789 2098 -252 307 -452 C ATOM 2456 N THR A 318 9.293 11.417 63.397 1.00 23.29 N ANISOU 2456 N THR B 318 4000 2230 2620 -232 460 -478 N ATOM 2457 CA THR A 318 10.467 12.281 63.384 1.00 23.55 C ANISOU 2457 CA THR B 318 4040 2235 2674 -237 529 -495 C ATOM 2458 C THR A 318 11.759 11.648 63.904 1.00 24.79 C ANISOU 2458 C THR B 318 4248 2362 2810 -225 557 -496 C ATOM 2459 O THR A 318 12.839 12.234 63.793 1.00 24.44 O ANISOU 2459 O THR B 318 4203 2295 2787 -232 617 -513 O ATOM 2460 CB THR A 318 10.185 13.604 64.178 1.00 23.62 C ANISOU 2460 CB THR B 318 4088 2204 2681 -255 574 -507 C ATOM 2461 OG1 THR A 318 9.884 13.278 65.528 1.00 21.44 O ANISOU 2461 OG1 THR B 318 3899 1893 2352 -256 566 -501 O ATOM 2462 CG2 THR A 318 9.030 14.406 63.547 1.00 21.34 C ANISOU 2462 CG2 THR B 318 3747 1940 2420 -264 559 -508 C ATOM 2463 N LEU A 319 11.641 10.453 64.476 1.00 25.86 N ANISOU 2463 N LEU B 319 4426 2495 2902 -207 516 -479 N ATOM 2464 CA LEU A 319 12.760 9.817 65.175 1.00 26.06 C ANISOU 2464 CA LEU B 319 4520 2485 2897 -191 542 -475 C ATOM 2465 C LEU A 319 14.014 9.759 64.285 1.00 25.04 C ANISOU 2465 C LEU B 319 4351 2358 2805 -189 584 -486 C ATOM 2466 O LEU A 319 15.058 10.362 64.593 1.00 23.93 O ANISOU 2466 O LEU B 319 4242 2177 2672 -200 653 -503 O ATOM 2467 CB LEU A 319 12.368 8.398 65.610 1.00 26.56 C ANISOU 2467 CB LEU B 319 4613 2561 2915 -163 477 -453 C ATOM 2468 CG LEU A 319 13.017 7.653 66.800 1.00 30.87 C ANISOU 2468 CG LEU B 319 5260 3067 3404 -139 483 -441 C ATOM 2469 CD1 LEU A 319 13.084 6.136 66.527 1.00 28.44 C ANISOU 2469 CD1 LEU B 319 4940 2788 3080 -103 426 -421 C ATOM 2470 CD2 LEU A 319 14.337 8.225 67.318 1.00 32.52 C ANISOU 2470 CD2 LEU B 319 5531 3217 3609 -144 569 -451 C ATOM 2471 N VAL A 320 13.919 9.010 63.193 1.00 23.89 N ANISOU 2471 N VAL B 320 4137 2258 2680 -178 544 -480 N ATOM 2472 CA VAL A 320 15.091 8.832 62.330 1.00 23.33 C ANISOU 2472 CA VAL B 320 4030 2192 2641 -176 579 -492 C ATOM 2473 C VAL A 320 15.580 10.133 61.678 1.00 23.92 C ANISOU 2473 C VAL B 320 4057 2269 2765 -202 633 -521 C ATOM 2474 O VAL A 320 16.756 10.441 61.748 1.00 24.87 O ANISOU 2474 O VAL B 320 4193 2358 2897 -211 693 -540 O ATOM 2475 CB VAL A 320 14.942 7.601 61.368 1.00 23.05 C ANISOU 2475 CB VAL B 320 3943 2203 2614 -155 526 -478 C ATOM 2476 CG1 VAL A 320 16.171 7.437 60.502 1.00 19.81 C ANISOU 2476 CG1 VAL B 320 3500 1794 2233 -155 565 -493 C ATOM 2477 CG2 VAL A 320 14.745 6.315 62.210 1.00 21.44 C ANISOU 2477 CG2 VAL B 320 3798 1989 2360 -124 484 -453 C ATOM 2478 N PRO A 321 14.696 10.908 61.015 1.00 24.12 N ANISOU 2478 N PRO B 321 4019 2328 2817 -213 612 -525 N ATOM 2479 CA PRO A 321 15.229 12.187 60.499 1.00 23.69 C ANISOU 2479 CA PRO B 321 3922 2274 2806 -233 664 -554 C ATOM 2480 C PRO A 321 15.963 13.129 61.507 1.00 24.39 C ANISOU 2480 C PRO B 321 4067 2308 2894 -250 736 -574 C ATOM 2481 O PRO A 321 16.931 13.795 61.107 1.00 23.43 O ANISOU 2481 O PRO B 321 3915 2179 2806 -264 789 -603 O ATOM 2482 CB PRO A 321 13.989 12.870 59.906 1.00 23.29 C ANISOU 2482 CB PRO B 321 3816 2260 2773 -235 629 -549 C ATOM 2483 CG PRO A 321 13.062 11.740 59.550 1.00 22.33 C ANISOU 2483 CG PRO B 321 3679 2173 2633 -220 559 -522 C ATOM 2484 CD PRO A 321 13.288 10.698 60.621 1.00 24.97 C ANISOU 2484 CD PRO B 321 4089 2476 2922 -208 549 -507 C ATOM 2485 N LYS A 322 15.518 13.189 62.770 1.00 24.01 N ANISOU 2485 N LYS B 322 4097 2220 2807 -250 741 -562 N ATOM 2486 CA LYS A 322 16.148 14.051 63.781 1.00 25.54 C ANISOU 2486 CA LYS B 322 4350 2357 2995 -266 812 -580 C ATOM 2487 C LYS A 322 17.508 13.478 64.214 1.00 25.63 C ANISOU 2487 C LYS B 322 4417 2327 2994 -265 862 -587 C ATOM 2488 O LYS A 322 18.407 14.240 64.524 1.00 26.68 O ANISOU 2488 O LYS B 322 4568 2424 3147 -285 936 -613 O ATOM 2489 CB LYS A 322 15.251 14.272 65.016 1.00 25.28 C ANISOU 2489 CB LYS B 322 4392 2294 2920 -267 803 -566 C ATOM 2490 CG LYS A 322 14.096 15.283 64.797 1.00 26.27 C ANISOU 2490 CG LYS B 322 4477 2439 3066 -276 787 -568 C ATOM 2491 CD LYS A 322 13.050 15.214 65.922 1.00 27.42 C ANISOU 2491 CD LYS B 322 4694 2562 3164 -275 762 -552 C ATOM 2492 CE LYS A 322 13.578 15.824 67.224 1.00 32.11 C ANISOU 2492 CE LYS B 322 5377 3091 3732 -287 828 -563 C ATOM 2493 NZ LYS A 322 14.034 17.258 67.094 1.00 31.61 N ANISOU 2493 NZ LYS B 322 5285 3010 3717 -305 900 -592 N ATOM 2494 N GLN A 323 17.640 12.155 64.217 1.00 25.48 N ANISOU 2494 N GLN B 323 4424 2313 2944 -243 825 -565 N ATOM 2495 CA GLN A 323 18.877 11.460 64.649 1.00 26.53 C ANISOU 2495 CA GLN B 323 4619 2403 3058 -236 869 -566 C ATOM 2496 C GLN A 323 19.901 11.236 63.535 1.00 26.55 C ANISOU 2496 C GLN B 323 4562 2424 3103 -242 894 -586 C ATOM 2497 O GLN A 323 21.068 10.939 63.820 1.00 27.23 O ANISOU 2497 O GLN B 323 4694 2468 3185 -245 950 -596 O ATOM 2498 CB GLN A 323 18.516 10.095 65.277 1.00 26.90 C ANISOU 2498 CB GLN B 323 4730 2444 3046 -201 816 -530 C ATOM 2499 CG GLN A 323 17.708 10.232 66.621 1.00 27.37 C ANISOU 2499 CG GLN B 323 4873 2475 3053 -195 800 -514 C ATOM 2500 CD GLN A 323 18.594 10.837 67.719 1.00 33.16 C ANISOU 2500 CD GLN B 323 5697 3136 3766 -208 885 -526 C ATOM 2501 OE1 GLN A 323 19.822 10.734 67.668 1.00 33.88 O ANISOU 2501 OE1 GLN B 323 5811 3194 3868 -212 946 -538 O ATOM 2502 NE2 GLN A 323 17.981 11.496 68.676 1.00 33.56 N ANISOU 2502 NE2 GLN B 323 5800 3161 3789 -217 893 -525 N ATOM 2503 N VAL A 324 19.463 11.328 62.275 1.00 25.72 N ANISOU 2503 N VAL B 324 4359 2379 3035 -244 852 -592 N ATOM 2504 CA VAL A 324 20.327 11.051 61.114 1.00 25.07 C ANISOU 2504 CA VAL B 324 4215 2322 2989 -249 865 -612 C ATOM 2505 C VAL A 324 20.579 12.299 60.246 1.00 24.91 C ANISOU 2505 C VAL B 324 4112 2329 3025 -276 894 -649 C ATOM 2506 O VAL A 324 21.677 12.481 59.666 1.00 25.03 O ANISOU 2506 O VAL B 324 4095 2343 3073 -293 939 -682 O ATOM 2507 CB VAL A 324 19.738 9.879 60.258 1.00 25.16 C ANISOU 2507 CB VAL B 324 4184 2383 2992 -223 790 -587 C ATOM 2508 CG1 VAL A 324 20.445 9.723 58.928 1.00 25.05 C ANISOU 2508 CG1 VAL B 324 4096 2403 3017 -230 798 -609 C ATOM 2509 CG2 VAL A 324 19.747 8.566 61.036 1.00 26.01 C ANISOU 2509 CG2 VAL B 324 4368 2466 3051 -193 767 -555 C ATOM 2510 N GLY A 325 19.565 13.135 60.099 1.00 23.27 N ANISOU 2510 N GLY B 325 3864 2149 2827 -278 865 -647 N ATOM 2511 CA GLY A 325 19.701 14.276 59.230 1.00 23.36 C ANISOU 2511 CA GLY B 325 3795 2193 2889 -294 882 -679 C ATOM 2512 C GLY A 325 18.949 14.110 57.935 1.00 24.10 C ANISOU 2512 C GLY B 325 3806 2353 2997 -281 818 -670 C ATOM 2513 O GLY A 325 18.083 13.252 57.821 1.00 22.71 O ANISOU 2513 O GLY B 325 3637 2197 2795 -261 760 -637 O ATOM 2514 N ASN A 326 19.317 14.936 56.959 1.00 24.40 N ANISOU 2514 N ASN B 326 3767 2426 3078 -291 830 -701 N ATOM 2515 CA ASN A 326 18.717 14.953 55.658 1.00 24.31 C ANISOU 2515 CA ASN B 326 3677 2477 3081 -278 778 -696 C ATOM 2516 C ASN A 326 19.089 13.741 54.829 1.00 24.75 C ANISOU 2516 C ASN B 326 3715 2558 3130 -269 750 -690 C ATOM 2517 O ASN A 326 20.262 13.507 54.502 1.00 24.78 O ANISOU 2517 O ASN B 326 3710 2556 3150 -281 785 -718 O ATOM 2518 CB ASN A 326 19.100 16.235 54.938 1.00 24.66 C ANISOU 2518 CB ASN B 326 3650 2551 3170 -288 801 -734 C ATOM 2519 CG ASN A 326 18.255 16.506 53.721 1.00 25.78 C ANISOU 2519 CG ASN B 326 3720 2754 3321 -269 746 -725 C ATOM 2520 OD1 ASN A 326 17.348 15.739 53.355 1.00 24.33 O ANISOU 2520 OD1 ASN B 326 3537 2592 3115 -252 693 -691 O ATOM 2521 ND2 ASN A 326 18.541 17.614 53.081 1.00 26.75 N ANISOU 2521 ND2 ASN B 326 3779 2906 3478 -272 759 -757 N ATOM 2522 N MET A 327 18.066 12.973 54.463 1.00 24.21 N ANISOU 2522 N MET B 327 3639 2517 3041 -248 690 -655 N ATOM 2523 CA MET A 327 18.279 11.742 53.700 1.00 23.56 C ANISOU 2523 CA MET B 327 3542 2459 2951 -237 661 -645 C ATOM 2524 C MET A 327 17.725 11.899 52.286 1.00 22.61 C ANISOU 2524 C MET B 327 3343 2400 2847 -227 620 -645 C ATOM 2525 O MET A 327 17.593 10.928 51.563 1.00 23.57 O ANISOU 2525 O MET B 327 3446 2547 2961 -215 588 -632 O ATOM 2526 CB MET A 327 17.631 10.570 54.442 1.00 23.74 C ANISOU 2526 CB MET B 327 3622 2463 2936 -219 627 -607 C ATOM 2527 CG MET A 327 18.288 10.285 55.795 1.00 23.51 C ANISOU 2527 CG MET B 327 3677 2373 2884 -222 667 -605 C ATOM 2528 SD MET A 327 17.399 9.068 56.787 1.00 24.54 S ANISOU 2528 SD MET B 327 3874 2485 2964 -198 618 -561 S ATOM 2529 CE MET A 327 16.447 10.235 57.825 1.00 17.56 C ANISOU 2529 CE MET B 327 3023 1580 2069 -209 622 -557 C ATOM 2530 N TYR A 328 17.399 13.130 51.910 1.00 22.99 N ANISOU 2530 N TYR B 328 3348 2469 2916 -231 622 -659 N ATOM 2531 CA TYR A 328 17.063 13.478 50.538 1.00 22.94 C ANISOU 2531 CA TYR B 328 3270 2520 2925 -221 592 -665 C ATOM 2532 C TYR A 328 15.938 12.546 50.053 1.00 22.37 C ANISOU 2532 C TYR B 328 3194 2473 2832 -202 537 -627 C ATOM 2533 O TYR A 328 14.859 12.565 50.655 1.00 20.50 O ANISOU 2533 O TYR B 328 2985 2224 2580 -196 516 -599 O ATOM 2534 CB TYR A 328 18.342 13.488 49.665 1.00 24.39 C ANISOU 2534 CB TYR B 328 3412 2725 3131 -232 615 -705 C ATOM 2535 CG TYR A 328 19.410 14.365 50.301 1.00 26.09 C ANISOU 2535 CG TYR B 328 3635 2909 3370 -255 675 -745 C ATOM 2536 CD1 TYR A 328 19.379 15.754 50.138 1.00 27.58 C ANISOU 2536 CD1 TYR B 328 3781 3115 3585 -258 687 -770 C ATOM 2537 CD2 TYR A 328 20.391 13.818 51.152 1.00 28.64 C ANISOU 2537 CD2 TYR B 328 4012 3181 3689 -272 721 -756 C ATOM 2538 CE1 TYR A 328 20.326 16.573 50.734 1.00 28.37 C ANISOU 2538 CE1 TYR B 328 3883 3187 3710 -281 745 -809 C ATOM 2539 CE2 TYR A 328 21.356 14.652 51.790 1.00 29.67 C ANISOU 2539 CE2 TYR B 328 4153 3278 3843 -298 784 -795 C ATOM 2540 CZ TYR A 328 21.310 16.012 51.561 1.00 29.86 C ANISOU 2540 CZ TYR B 328 4126 3324 3896 -304 795 -822 C ATOM 2541 OH TYR A 328 22.224 16.846 52.158 1.00 31.50 O ANISOU 2541 OH TYR B 328 4337 3500 4131 -329 859 -862 O ATOM 2542 N THR A 329 16.160 11.720 49.025 1.00 20.96 N ANISOU 2542 N THR B 329 2985 2327 2653 -195 517 -626 N ATOM 2543 CA THR A 329 15.062 10.890 48.499 1.00 20.33 C ANISOU 2543 CA THR B 329 2895 2272 2557 -178 469 -592 C ATOM 2544 C THR A 329 14.483 9.907 49.523 1.00 19.94 C ANISOU 2544 C THR B 329 2899 2192 2485 -175 453 -562 C ATOM 2545 O THR A 329 13.307 9.529 49.413 1.00 19.81 O ANISOU 2545 O THR B 329 2879 2189 2457 -166 416 -535 O ATOM 2546 CB THR A 329 15.424 10.107 47.223 1.00 20.40 C ANISOU 2546 CB THR B 329 2864 2319 2568 -171 454 -598 C ATOM 2547 OG1 THR A 329 16.480 9.168 47.497 1.00 21.81 O ANISOU 2547 OG1 THR B 329 3067 2474 2744 -176 476 -609 O ATOM 2548 CG2 THR A 329 15.843 11.053 46.051 1.00 20.76 C ANISOU 2548 CG2 THR B 329 2851 2405 2631 -170 459 -626 C ATOM 2549 N ALA A 330 15.308 9.474 50.485 1.00 19.35 N ANISOU 2549 N ALA B 330 2874 2077 2401 -181 480 -569 N ATOM 2550 CA ALA A 330 14.896 8.505 51.505 1.00 19.17 C ANISOU 2550 CA ALA B 330 2906 2026 2353 -173 462 -543 C ATOM 2551 C ALA A 330 14.271 9.179 52.724 1.00 19.66 C ANISOU 2551 C ALA B 330 3013 2055 2401 -180 467 -534 C ATOM 2552 O ALA A 330 13.753 8.501 53.599 1.00 19.11 O ANISOU 2552 O ALA B 330 2988 1967 2307 -173 445 -514 O ATOM 2553 CB ALA A 330 16.086 7.654 51.956 1.00 19.51 C ANISOU 2553 CB ALA B 330 2988 2038 2388 -170 490 -551 C ATOM 2554 N SER A 331 14.364 10.500 52.793 1.00 19.00 N ANISOU 2554 N SER B 331 2920 1966 2334 -192 495 -552 N ATOM 2555 CA SER A 331 13.863 11.275 53.938 1.00 20.48 C ANISOU 2555 CA SER B 331 3151 2119 2510 -200 508 -548 C ATOM 2556 C SER A 331 12.406 10.956 54.355 1.00 19.51 C ANISOU 2556 C SER B 331 3047 2000 2367 -195 464 -519 C ATOM 2557 O SER A 331 12.123 10.647 55.524 1.00 19.05 O ANISOU 2557 O SER B 331 3048 1909 2283 -197 460 -508 O ATOM 2558 CB SER A 331 13.992 12.755 53.590 1.00 19.97 C ANISOU 2558 CB SER B 331 3052 2061 2473 -209 537 -571 C ATOM 2559 OG SER A 331 13.689 13.549 54.702 1.00 26.47 O ANISOU 2559 OG SER B 331 3921 2848 3290 -217 560 -571 O ATOM 2560 N LEU A 332 11.485 11.025 53.393 1.00 18.93 N ANISOU 2560 N LEU B 332 2924 1965 2303 -189 432 -508 N ATOM 2561 CA LEU A 332 10.072 10.794 53.675 1.00 17.79 C ANISOU 2561 CA LEU B 332 2790 1824 2145 -190 395 -485 C ATOM 2562 C LEU A 332 9.877 9.360 54.154 1.00 18.54 C ANISOU 2562 C LEU B 332 2911 1917 2216 -183 362 -469 C ATOM 2563 O LEU A 332 9.040 9.104 55.034 1.00 17.55 O ANISOU 2563 O LEU B 332 2822 1777 2071 -188 340 -457 O ATOM 2564 CB LEU A 332 9.247 11.020 52.416 1.00 18.08 C ANISOU 2564 CB LEU B 332 2769 1902 2198 -184 374 -476 C ATOM 2565 CG LEU A 332 7.795 10.523 52.389 1.00 15.41 C ANISOU 2565 CG LEU B 332 2430 1575 1851 -186 336 -453 C ATOM 2566 CD1 LEU A 332 6.926 11.232 53.496 1.00 13.17 C ANISOU 2566 CD1 LEU B 332 2192 1258 1555 -199 340 -449 C ATOM 2567 CD2 LEU A 332 7.257 10.737 50.992 1.00 14.95 C ANISOU 2567 CD2 LEU B 332 2316 1554 1809 -178 325 -446 C ATOM 2568 N TYR A 333 10.634 8.437 53.546 1.00 17.59 N ANISOU 2568 N TYR B 333 2770 1814 2101 -172 357 -471 N ATOM 2569 CA TYR A 333 10.504 6.982 53.818 1.00 18.35 C ANISOU 2569 CA TYR B 333 2881 1914 2179 -159 324 -455 C ATOM 2570 C TYR A 333 11.133 6.618 55.142 1.00 18.60 C ANISOU 2570 C TYR B 333 2981 1904 2182 -154 335 -455 C ATOM 2571 O TYR A 333 10.666 5.717 55.799 1.00 18.66 O ANISOU 2571 O TYR B 333 3015 1908 2167 -144 301 -441 O ATOM 2572 CB TYR A 333 10.967 6.108 52.611 1.00 18.02 C ANISOU 2572 CB TYR B 333 2790 1906 2152 -147 315 -455 C ATOM 2573 CG TYR A 333 10.117 6.545 51.450 1.00 18.00 C ANISOU 2573 CG TYR B 333 2731 1941 2169 -151 301 -452 C ATOM 2574 CD1 TYR A 333 8.767 6.203 51.408 1.00 18.29 C ANISOU 2574 CD1 TYR B 333 2755 1994 2203 -154 266 -435 C ATOM 2575 CD2 TYR A 333 10.597 7.454 50.506 1.00 19.34 C ANISOU 2575 CD2 TYR B 333 2864 2127 2358 -154 326 -467 C ATOM 2576 CE1 TYR A 333 7.917 6.690 50.410 1.00 16.37 C ANISOU 2576 CE1 TYR B 333 2469 1777 1974 -159 260 -429 C ATOM 2577 CE2 TYR A 333 9.732 7.970 49.498 1.00 17.30 C ANISOU 2577 CE2 TYR B 333 2563 1900 2112 -154 314 -461 C ATOM 2578 CZ TYR A 333 8.402 7.549 49.473 1.00 17.04 C ANISOU 2578 CZ TYR B 333 2524 1877 2074 -156 283 -440 C ATOM 2579 OH TYR A 333 7.551 8.027 48.501 1.00 20.85 O ANISOU 2579 OH TYR B 333 2971 2384 2566 -156 277 -432 O ATOM 2580 N ALA A 334 12.154 7.362 55.556 1.00 19.43 N ANISOU 2580 N ALA B 334 3116 1977 2290 -162 384 -472 N ATOM 2581 CA ALA A 334 12.685 7.239 56.932 1.00 20.04 C ANISOU 2581 CA ALA B 334 3271 2006 2337 -159 404 -472 C ATOM 2582 C ALA A 334 11.751 7.810 57.990 1.00 20.69 C ANISOU 2582 C ALA B 334 3397 2068 2398 -169 394 -465 C ATOM 2583 O ALA A 334 11.718 7.313 59.124 1.00 21.39 O ANISOU 2583 O ALA B 334 3548 2128 2450 -161 384 -456 O ATOM 2584 CB ALA A 334 14.024 7.885 57.032 1.00 19.89 C ANISOU 2584 CB ALA B 334 3271 1957 2330 -168 466 -494 C ATOM 2585 N ALA A 335 11.029 8.872 57.646 1.00 20.12 N ANISOU 2585 N ALA B 335 3294 2006 2345 -185 399 -471 N ATOM 2586 CA ALA A 335 9.978 9.411 58.538 1.00 20.73 C ANISOU 2586 CA ALA B 335 3407 2066 2404 -196 388 -466 C ATOM 2587 C ALA A 335 8.856 8.375 58.680 1.00 21.22 C ANISOU 2587 C ALA B 335 3466 2151 2447 -191 327 -448 C ATOM 2588 O ALA A 335 8.342 8.141 59.768 1.00 22.36 O ANISOU 2588 O ALA B 335 3662 2275 2559 -193 307 -443 O ATOM 2589 CB ALA A 335 9.448 10.727 57.985 1.00 19.09 C ANISOU 2589 CB ALA B 335 3162 1867 2224 -210 407 -474 C ATOM 2590 N PHE A 336 8.503 7.726 57.567 1.00 21.43 N ANISOU 2590 N PHE B 336 3431 2220 2494 -184 297 -441 N ATOM 2591 CA PHE A 336 7.507 6.662 57.559 1.00 21.75 C ANISOU 2591 CA PHE B 336 3455 2286 2523 -180 241 -428 C ATOM 2592 C PHE A 336 7.987 5.453 58.372 1.00 23.04 C ANISOU 2592 C PHE B 336 3660 2440 2656 -159 217 -421 C ATOM 2593 O PHE A 336 7.207 4.851 59.164 1.00 22.83 O ANISOU 2593 O PHE B 336 3657 2414 2602 -157 175 -415 O ATOM 2594 CB PHE A 336 7.176 6.254 56.124 1.00 20.18 C ANISOU 2594 CB PHE B 336 3181 2131 2354 -176 225 -423 C ATOM 2595 CG PHE A 336 6.098 5.226 56.027 1.00 22.55 C ANISOU 2595 CG PHE B 336 3457 2459 2652 -176 174 -413 C ATOM 2596 CD1 PHE A 336 4.826 5.453 56.595 1.00 23.56 C ANISOU 2596 CD1 PHE B 336 3597 2584 2771 -195 152 -413 C ATOM 2597 CD2 PHE A 336 6.323 4.029 55.373 1.00 24.11 C ANISOU 2597 CD2 PHE B 336 3617 2686 2858 -158 151 -407 C ATOM 2598 CE1 PHE A 336 3.819 4.490 56.505 1.00 21.21 C ANISOU 2598 CE1 PHE B 336 3271 2314 2475 -199 106 -409 C ATOM 2599 CE2 PHE A 336 5.305 3.053 55.278 1.00 25.85 C ANISOU 2599 CE2 PHE B 336 3808 2934 3080 -159 105 -401 C ATOM 2600 CZ PHE A 336 4.074 3.279 55.851 1.00 19.56 C ANISOU 2600 CZ PHE B 336 3020 2135 2276 -180 82 -403 C ATOM 2601 N ALA A 337 9.256 5.099 58.185 1.00 22.38 N ANISOU 2601 N ALA B 337 3584 2346 2573 -142 243 -423 N ATOM 2602 CA ALA A 337 9.869 4.019 58.960 1.00 23.22 C ANISOU 2602 CA ALA B 337 3738 2437 2648 -116 228 -414 C ATOM 2603 C ALA A 337 9.881 4.312 60.476 1.00 22.82 C ANISOU 2603 C ALA B 337 3773 2344 2555 -116 234 -414 C ATOM 2604 O ALA A 337 9.645 3.429 61.278 1.00 22.84 O ANISOU 2604 O ALA B 337 3813 2345 2523 -97 195 -403 O ATOM 2605 CB ALA A 337 11.336 3.708 58.424 1.00 22.66 C ANISOU 2605 CB ALA B 337 3666 2355 2589 -101 268 -418 C ATOM 2606 N SER A 338 10.175 5.554 60.841 1.00 23.57 N ANISOU 2606 N SER B 338 3897 2406 2652 -137 283 -425 N ATOM 2607 CA SER A 338 9.995 6.070 62.197 1.00 24.20 C ANISOU 2607 CA SER B 338 4055 2445 2694 -144 294 -427 C ATOM 2608 C SER A 338 8.570 5.826 62.707 1.00 24.38 C ANISOU 2608 C SER B 338 4080 2485 2696 -151 238 -423 C ATOM 2609 O SER A 338 8.380 5.332 63.817 1.00 24.51 O ANISOU 2609 O SER B 338 4157 2486 2668 -140 211 -418 O ATOM 2610 CB SER A 338 10.314 7.556 62.253 1.00 23.67 C ANISOU 2610 CB SER B 338 3998 2350 2647 -168 355 -443 C ATOM 2611 OG SER A 338 11.651 7.800 61.884 1.00 22.98 O ANISOU 2611 OG SER B 338 3909 2245 2578 -165 409 -453 O ATOM 2612 N LEU A 339 7.565 6.143 61.896 1.00 24.32 N ANISOU 2612 N LEU B 339 4010 2511 2721 -170 219 -425 N ATOM 2613 CA LEU A 339 6.183 5.930 62.312 1.00 24.51 C ANISOU 2613 CA LEU B 339 4032 2551 2730 -183 170 -425 C ATOM 2614 C LEU A 339 5.875 4.459 62.630 1.00 26.00 C ANISOU 2614 C LEU B 339 4219 2766 2894 -161 107 -417 C ATOM 2615 O LEU A 339 5.250 4.147 63.659 1.00 27.32 O ANISOU 2615 O LEU B 339 4428 2927 3024 -162 71 -420 O ATOM 2616 CB LEU A 339 5.192 6.464 61.265 1.00 24.06 C ANISOU 2616 CB LEU B 339 3906 2522 2713 -205 167 -428 C ATOM 2617 CG LEU A 339 3.706 6.136 61.477 1.00 23.66 C ANISOU 2617 CG LEU B 339 3840 2491 2657 -224 120 -431 C ATOM 2618 CD1 LEU A 339 3.212 6.717 62.811 1.00 22.84 C ANISOU 2618 CD1 LEU B 339 3809 2353 2517 -240 121 -440 C ATOM 2619 CD2 LEU A 339 2.923 6.730 60.355 1.00 23.00 C ANISOU 2619 CD2 LEU B 339 3696 2428 2615 -243 131 -431 C ATOM 2620 N VAL A 340 6.283 3.563 61.738 1.00 27.04 N ANISOU 2620 N VAL B 340 4299 2927 3047 -141 93 -409 N ATOM 2621 CA VAL A 340 6.095 2.124 61.936 1.00 27.52 C ANISOU 2621 CA VAL B 340 4350 3016 3091 -114 35 -402 C ATOM 2622 C VAL A 340 6.840 1.669 63.211 1.00 28.34 C ANISOU 2622 C VAL B 340 4539 3088 3142 -85 29 -395 C ATOM 2623 O VAL A 340 6.300 0.911 64.027 1.00 29.61 O ANISOU 2623 O VAL B 340 4724 3260 3268 -71 -24 -394 O ATOM 2624 CB VAL A 340 6.577 1.314 60.709 1.00 27.22 C ANISOU 2624 CB VAL B 340 4246 3009 3087 -95 33 -394 C ATOM 2625 CG1 VAL A 340 6.526 -0.196 60.987 1.00 25.29 C ANISOU 2625 CG1 VAL B 340 3995 2790 2825 -61 -23 -386 C ATOM 2626 CG2 VAL A 340 5.758 1.661 59.434 1.00 27.37 C ANISOU 2626 CG2 VAL B 340 4185 3062 3153 -121 35 -399 C ATOM 2627 N HIS A 341 8.054 2.160 63.404 1.00 27.63 N ANISOU 2627 N HIS B 341 4497 2958 3045 -77 86 -393 N ATOM 2628 CA HIS A 341 8.841 1.764 64.566 1.00 28.41 C ANISOU 2628 CA HIS B 341 4684 3020 3092 -48 91 -384 C ATOM 2629 C HIS A 341 8.083 2.124 65.848 1.00 28.99 C ANISOU 2629 C HIS B 341 4821 3076 3120 -59 68 -390 C ATOM 2630 O HIS A 341 7.986 1.307 66.773 1.00 28.71 O ANISOU 2630 O HIS B 341 4834 3040 3036 -31 24 -383 O ATOM 2631 CB HIS A 341 10.185 2.477 64.540 1.00 27.73 C ANISOU 2631 CB HIS B 341 4637 2887 3012 -49 168 -386 C ATOM 2632 CG HIS A 341 10.986 2.302 65.785 1.00 29.32 C ANISOU 2632 CG HIS B 341 4941 3039 3159 -25 189 -378 C ATOM 2633 ND1 HIS A 341 11.502 1.084 66.167 1.00 31.69 N ANISOU 2633 ND1 HIS B 341 5277 3338 3427 20 161 -361 N ATOM 2634 CD2 HIS A 341 11.399 3.198 66.715 1.00 31.15 C ANISOU 2634 CD2 HIS B 341 5251 3220 3364 -38 238 -384 C ATOM 2635 CE1 HIS A 341 12.176 1.233 67.297 1.00 34.28 C ANISOU 2635 CE1 HIS B 341 5705 3615 3706 35 192 -355 C ATOM 2636 NE2 HIS A 341 12.135 2.508 67.644 1.00 33.48 N ANISOU 2636 NE2 HIS B 341 5632 3482 3608 -1 241 -370 N ATOM 2637 N ASN A 342 7.544 3.348 65.874 1.00 29.03 N ANISOU 2637 N ASN B 342 4824 3066 3139 -98 98 -403 N ATOM 2638 CA ASN A 342 6.947 3.930 67.063 1.00 29.60 C ANISOU 2638 CA ASN B 342 4964 3112 3170 -114 94 -411 C ATOM 2639 C ASN A 342 5.504 3.505 67.271 1.00 30.36 C ANISOU 2639 C ASN B 342 5033 3245 3258 -127 25 -420 C ATOM 2640 O ASN A 342 5.044 3.509 68.383 1.00 30.85 O ANISOU 2640 O ASN B 342 5155 3294 3273 -130 1 -426 O ATOM 2641 CB ASN A 342 6.949 5.454 66.977 1.00 28.91 C ANISOU 2641 CB ASN B 342 4885 2992 3106 -149 158 -424 C ATOM 2642 CG ASN A 342 8.278 6.075 67.302 1.00 30.56 C ANISOU 2642 CG ASN B 342 5150 3153 3310 -143 230 -423 C ATOM 2643 OD1 ASN A 342 8.965 5.669 68.247 1.00 29.99 O ANISOU 2643 OD1 ASN B 342 5157 3048 3191 -120 238 -416 O ATOM 2644 ND2 ASN A 342 8.638 7.115 66.535 1.00 29.20 N ANISOU 2644 ND2 ASN B 342 4939 2972 3185 -164 287 -432 N ATOM 2645 N LYS A 343 4.761 3.199 66.203 1.00 31.06 N ANISOU 2645 N LYS B 343 5032 3379 3392 -140 -3 -423 N ATOM 2646 CA LYS A 343 3.318 2.994 66.342 1.00 31.34 C ANISOU 2646 CA LYS B 343 5035 3444 3426 -164 -55 -436 C ATOM 2647 C LYS A 343 2.789 1.692 65.739 1.00 32.84 C ANISOU 2647 C LYS B 343 5153 3690 3635 -151 -118 -435 C ATOM 2648 O LYS A 343 1.576 1.529 65.628 1.00 32.74 O ANISOU 2648 O LYS B 343 5099 3705 3635 -176 -156 -449 O ATOM 2649 CB LYS A 343 2.513 4.179 65.769 1.00 30.43 C ANISOU 2649 CB LYS B 343 4888 3324 3350 -208 -21 -447 C ATOM 2650 CG LYS A 343 2.976 5.612 66.130 1.00 31.11 C ANISOU 2650 CG LYS B 343 5028 3359 3434 -224 48 -450 C ATOM 2651 CD LYS A 343 3.173 5.936 67.651 1.00 35.38 C ANISOU 2651 CD LYS B 343 5671 3857 3915 -222 57 -455 C ATOM 2652 CE LYS A 343 1.976 5.753 68.463 1.00 33.55 C ANISOU 2652 CE LYS B 343 5463 3633 3652 -241 8 -470 C ATOM 2653 NZ LYS A 343 1.466 4.360 68.382 1.00 38.83 N ANISOU 2653 NZ LYS B 343 6090 4351 4312 -226 -69 -471 N ATOM 2654 N HIS A 344 3.678 0.766 65.362 1.00 34.01 N ANISOU 2654 N HIS B 344 5286 3851 3786 -111 -127 -420 N ATOM 2655 CA HIS A 344 3.267 -0.445 64.640 1.00 35.58 C ANISOU 2655 CA HIS B 344 5406 4101 4010 -96 -177 -418 C ATOM 2656 C HIS A 344 2.053 -1.188 65.228 1.00 37.56 C ANISOU 2656 C HIS B 344 5639 4389 4244 -103 -251 -434 C ATOM 2657 O HIS A 344 1.173 -1.667 64.465 1.00 38.28 O ANISOU 2657 O HIS B 344 5649 4522 4374 -120 -280 -444 O ATOM 2658 CB HIS A 344 4.457 -1.408 64.402 1.00 35.47 C ANISOU 2658 CB HIS B 344 5395 4091 3991 -46 -178 -400 C ATOM 2659 CG HIS A 344 5.038 -2.001 65.651 1.00 36.36 C ANISOU 2659 CG HIS B 344 5588 4184 4043 -5 -203 -391 C ATOM 2660 ND1 HIS A 344 6.114 -1.447 66.316 1.00 36.70 N ANISOU 2660 ND1 HIS B 344 5718 4174 4052 9 -154 -381 N ATOM 2661 CD2 HIS A 344 4.718 -3.129 66.332 1.00 37.05 C ANISOU 2661 CD2 HIS B 344 5684 4299 4096 28 -273 -390 C ATOM 2662 CE1 HIS A 344 6.413 -2.196 67.365 1.00 39.23 C ANISOU 2662 CE1 HIS B 344 6103 4486 4316 50 -190 -372 C ATOM 2663 NE2 HIS A 344 5.580 -3.223 67.396 1.00 36.91 N ANISOU 2663 NE2 HIS B 344 5762 4243 4020 64 -266 -378 N ATOM 2664 N SER A 345 1.982 -1.270 66.558 1.00 38.75 N ANISOU 2664 N SER B 345 5863 4524 4337 -92 -281 -440 N ATOM 2665 CA SER A 345 0.921 -2.061 67.200 1.00 40.39 C ANISOU 2665 CA SER B 345 6055 4769 4522 -95 -359 -458 C ATOM 2666 C SER A 345 -0.447 -1.355 67.148 1.00 40.47 C ANISOU 2666 C SER B 345 6037 4786 4552 -154 -361 -484 C ATOM 2667 O SER A 345 -1.486 -1.979 67.372 1.00 41.44 O ANISOU 2667 O SER B 345 6123 4947 4676 -169 -420 -506 O ATOM 2668 CB SER A 345 1.312 -2.498 68.622 1.00 40.94 C ANISOU 2668 CB SER B 345 6213 4825 4518 -58 -397 -456 C ATOM 2669 OG SER A 345 1.440 -1.382 69.480 1.00 42.70 O ANISOU 2669 OG SER B 345 6523 4997 4703 -78 -357 -459 O ATOM 2670 N ASP A 346 -0.451 -0.076 66.785 1.00 39.40 N ANISOU 2670 N ASP B 346 5916 4615 4439 -188 -296 -483 N ATOM 2671 CA ASP A 346 -1.701 0.654 66.666 1.00 39.32 C ANISOU 2671 CA ASP B 346 5884 4604 4450 -242 -288 -505 C ATOM 2672 C ASP A 346 -2.007 1.204 65.279 1.00 37.19 C ANISOU 2672 C ASP B 346 5546 4340 4245 -268 -243 -500 C ATOM 2673 O ASP A 346 -2.943 1.969 65.125 1.00 37.65 O ANISOU 2673 O ASP B 346 5596 4388 4321 -310 -223 -513 O ATOM 2674 CB ASP A 346 -1.702 1.764 67.703 1.00 40.63 C ANISOU 2674 CB ASP B 346 6140 4721 4576 -260 -257 -512 C ATOM 2675 CG ASP A 346 -1.622 1.213 69.111 1.00 45.45 C ANISOU 2675 CG ASP B 346 6822 5329 5118 -238 -307 -520 C ATOM 2676 OD1 ASP A 346 -2.461 0.327 69.440 1.00 47.58 O ANISOU 2676 OD1 ASP B 346 7062 5639 5376 -242 -377 -539 O ATOM 2677 OD2 ASP A 346 -0.703 1.637 69.870 1.00 49.07 O ANISOU 2677 OD2 ASP B 346 7365 5746 5534 -216 -277 -507 O ATOM 2678 N LEU A 347 -1.230 0.800 64.269 1.00 35.58 N ANISOU 2678 N LEU B 347 5296 4151 4072 -241 -226 -481 N ATOM 2679 CA LEU A 347 -1.346 1.353 62.912 1.00 32.77 C ANISOU 2679 CA LEU B 347 4882 3798 3770 -259 -180 -473 C ATOM 2680 C LEU A 347 -2.375 0.648 62.045 1.00 32.05 C ANISOU 2680 C LEU B 347 4707 3750 3720 -279 -208 -483 C ATOM 2681 O LEU A 347 -2.889 1.221 61.098 1.00 31.52 O ANISOU 2681 O LEU B 347 4602 3684 3692 -304 -174 -482 O ATOM 2682 CB LEU A 347 0.033 1.360 62.220 1.00 32.51 C ANISOU 2682 CB LEU B 347 4846 3758 3750 -225 -142 -451 C ATOM 2683 CG LEU A 347 0.915 2.603 62.419 1.00 31.06 C ANISOU 2683 CG LEU B 347 4718 3526 3555 -225 -80 -444 C ATOM 2684 CD1 LEU A 347 2.349 2.440 61.801 1.00 27.74 C ANISOU 2684 CD1 LEU B 347 4293 3101 3146 -191 -48 -428 C ATOM 2685 CD2 LEU A 347 0.217 3.841 61.866 1.00 30.99 C ANISOU 2685 CD2 LEU B 347 4695 3504 3577 -261 -39 -449 C ATOM 2686 N ALA A 348 -2.688 -0.597 62.368 1.00 32.06 N ANISOU 2686 N ALA B 348 4680 3789 3713 -265 -269 -493 N ATOM 2687 CA ALA A 348 -3.711 -1.348 61.625 1.00 32.10 C ANISOU 2687 CA ALA B 348 4601 3837 3759 -286 -296 -507 C ATOM 2688 C ALA A 348 -5.034 -0.584 61.605 1.00 31.81 C ANISOU 2688 C ALA B 348 4558 3789 3739 -343 -281 -528 C ATOM 2689 O ALA A 348 -5.480 -0.106 62.635 1.00 31.90 O ANISOU 2689 O ALA B 348 4623 3781 3718 -363 -292 -543 O ATOM 2690 CB ALA A 348 -3.897 -2.749 62.218 1.00 31.95 C ANISOU 2690 CB ALA B 348 4557 3859 3724 -263 -370 -520 C ATOM 2691 N GLY A 349 -5.628 -0.447 60.422 1.00 30.72 N ANISOU 2691 N GLY B 349 4361 3661 3649 -366 -251 -526 N ATOM 2692 CA GLY A 349 -6.827 0.357 60.248 1.00 30.53 C ANISOU 2692 CA GLY B 349 4336 3621 3645 -418 -224 -541 C ATOM 2693 C GLY A 349 -6.654 1.857 60.043 1.00 29.95 C ANISOU 2693 C GLY B 349 4309 3500 3570 -428 -160 -527 C ATOM 2694 O GLY A 349 -7.638 2.553 59.762 1.00 29.43 O ANISOU 2694 O GLY B 349 4242 3417 3522 -466 -130 -535 O ATOM 2695 N LYS A 350 -5.427 2.369 60.161 1.00 28.69 N ANISOU 2695 N LYS B 350 4192 3319 3391 -394 -136 -506 N ATOM 2696 CA LYS A 350 -5.212 3.829 60.147 1.00 27.88 C ANISOU 2696 CA LYS B 350 4137 3173 3285 -401 -79 -496 C ATOM 2697 C LYS A 350 -4.913 4.416 58.750 1.00 27.24 C ANISOU 2697 C LYS B 350 4020 3091 3241 -393 -29 -475 C ATOM 2698 O LYS A 350 -4.462 3.709 57.862 1.00 26.68 O ANISOU 2698 O LYS B 350 3899 3049 3189 -372 -35 -465 O ATOM 2699 CB LYS A 350 -4.108 4.227 61.135 1.00 27.52 C ANISOU 2699 CB LYS B 350 4161 3099 3198 -375 -73 -490 C ATOM 2700 CG LYS A 350 -4.350 3.745 62.601 1.00 29.20 C ANISOU 2700 CG LYS B 350 4423 3308 3363 -379 -120 -509 C ATOM 2701 CD LYS A 350 -5.516 4.444 63.236 1.00 30.84 C ANISOU 2701 CD LYS B 350 4663 3493 3562 -423 -115 -530 C ATOM 2702 CE LYS A 350 -5.824 3.880 64.668 1.00 33.00 C ANISOU 2702 CE LYS B 350 4983 3769 3785 -428 -170 -553 C ATOM 2703 NZ LYS A 350 -4.643 4.093 65.556 1.00 34.26 N ANISOU 2703 NZ LYS B 350 5215 3902 3899 -393 -163 -541 N ATOM 2704 N ARG A 351 -5.183 5.707 58.573 1.00 25.50 N ANISOU 2704 N ARG B 351 3825 2837 3026 -407 18 -471 N ATOM 2705 CA ARG A 351 -4.807 6.382 57.360 1.00 25.12 C ANISOU 2705 CA ARG B 351 3751 2787 3005 -392 62 -451 C ATOM 2706 C ARG A 351 -3.548 7.225 57.569 1.00 24.97 C ANISOU 2706 C ARG B 351 3770 2746 2972 -365 92 -441 C ATOM 2707 O ARG A 351 -3.445 8.019 58.519 1.00 25.18 O ANISOU 2707 O ARG B 351 3853 2739 2977 -371 108 -448 O ATOM 2708 CB ARG A 351 -5.936 7.242 56.787 1.00 24.79 C ANISOU 2708 CB ARG B 351 3706 2729 2986 -419 97 -450 C ATOM 2709 CG ARG A 351 -5.428 8.216 55.698 1.00 22.93 C ANISOU 2709 CG ARG B 351 3459 2487 2768 -397 144 -429 C ATOM 2710 CD ARG A 351 -6.538 9.105 55.132 1.00 23.80 C ANISOU 2710 CD ARG B 351 3571 2576 2896 -417 181 -424 C ATOM 2711 NE ARG A 351 -7.414 8.295 54.296 1.00 26.17 N ANISOU 2711 NE ARG B 351 3824 2899 3219 -434 172 -424 N ATOM 2712 CZ ARG A 351 -8.745 8.265 54.376 1.00 29.14 C ANISOU 2712 CZ ARG B 351 4203 3263 3606 -471 178 -435 C ATOM 2713 NH1 ARG A 351 -9.400 9.033 55.254 1.00 27.03 N ANISOU 2713 NH1 ARG B 351 3986 2959 3327 -495 193 -447 N ATOM 2714 NH2 ARG A 351 -9.429 7.484 53.538 1.00 27.14 N ANISOU 2714 NH2 ARG B 351 3902 3033 3377 -486 175 -435 N ATOM 2715 N VAL A 352 -2.593 7.036 56.668 1.00 22.88 N ANISOU 2715 N VAL B 352 3471 2500 2721 -337 103 -428 N ATOM 2716 CA VAL A 352 -1.343 7.770 56.729 1.00 22.69 C ANISOU 2716 CA VAL B 352 3471 2458 2690 -314 134 -423 C ATOM 2717 C VAL A 352 -1.221 8.583 55.439 1.00 21.63 C ANISOU 2717 C VAL B 352 3302 2331 2584 -304 171 -411 C ATOM 2718 O VAL A 352 -1.260 8.020 54.342 1.00 21.76 O ANISOU 2718 O VAL B 352 3269 2379 2620 -297 164 -403 O ATOM 2719 CB VAL A 352 -0.109 6.804 56.840 1.00 22.72 C ANISOU 2719 CB VAL B 352 3471 2479 2683 -286 115 -420 C ATOM 2720 CG1 VAL A 352 1.233 7.596 56.945 1.00 23.12 C ANISOU 2720 CG1 VAL B 352 3549 2507 2728 -267 154 -419 C ATOM 2721 CG2 VAL A 352 -0.240 5.877 58.029 1.00 23.82 C ANISOU 2721 CG2 VAL B 352 3642 2616 2791 -288 72 -429 C ATOM 2722 N VAL A 353 -1.050 9.892 55.579 1.00 20.93 N ANISOU 2722 N VAL B 353 3242 2216 2497 -303 209 -411 N ATOM 2723 CA VAL A 353 -0.865 10.784 54.426 1.00 20.71 C ANISOU 2723 CA VAL B 353 3183 2194 2491 -288 241 -401 C ATOM 2724 C VAL A 353 0.626 11.099 54.324 1.00 20.17 C ANISOU 2724 C VAL B 353 3113 2128 2423 -264 260 -405 C ATOM 2725 O VAL A 353 1.272 11.379 55.326 1.00 21.23 O ANISOU 2725 O VAL B 353 3289 2237 2541 -264 271 -415 O ATOM 2726 CB VAL A 353 -1.756 12.078 54.546 1.00 21.72 C ANISOU 2726 CB VAL B 353 3337 2293 2624 -298 273 -399 C ATOM 2727 CG1 VAL A 353 -1.369 13.154 53.496 1.00 21.15 C ANISOU 2727 CG1 VAL B 353 3240 2226 2571 -273 306 -390 C ATOM 2728 CG2 VAL A 353 -3.253 11.708 54.437 1.00 19.07 C ANISOU 2728 CG2 VAL B 353 2997 1956 2293 -325 260 -397 C ATOM 2729 N MET A 354 1.148 11.020 53.107 1.00 19.13 N ANISOU 2729 N MET B 354 2935 2025 2308 -246 264 -399 N ATOM 2730 CA MET A 354 2.569 11.180 52.812 1.00 18.58 C ANISOU 2730 CA MET B 354 2853 1964 2242 -226 280 -407 C ATOM 2731 C MET A 354 2.729 12.366 51.886 1.00 17.73 C ANISOU 2731 C MET B 354 2720 1865 2153 -212 308 -406 C ATOM 2732 O MET A 354 2.012 12.463 50.897 1.00 19.77 O ANISOU 2732 O MET B 354 2949 2143 2421 -207 305 -393 O ATOM 2733 CB MET A 354 3.081 9.961 52.066 1.00 15.41 C ANISOU 2733 CB MET B 354 2414 1596 1845 -216 258 -404 C ATOM 2734 CG MET A 354 2.903 8.655 52.768 1.00 19.48 C ANISOU 2734 CG MET B 354 2943 2113 2346 -223 224 -403 C ATOM 2735 SD MET A 354 4.158 8.342 53.971 1.00 20.12 S ANISOU 2735 SD MET B 354 3071 2168 2404 -215 228 -414 S ATOM 2736 CE MET A 354 5.459 7.627 52.959 1.00 20.23 C ANISOU 2736 CE MET B 354 3046 2209 2431 -194 234 -416 C ATOM 2737 N PHE A 355 3.696 13.216 52.170 1.00 17.88 N ANISOU 2737 N PHE B 355 2747 1870 2175 -203 336 -419 N ATOM 2738 CA PHE A 355 4.040 14.342 51.295 1.00 18.16 C ANISOU 2738 CA PHE B 355 2752 1919 2228 -185 359 -423 C ATOM 2739 C PHE A 355 5.512 14.318 50.883 1.00 17.75 C ANISOU 2739 C PHE B 355 2674 1886 2186 -174 371 -441 C ATOM 2740 O PHE A 355 6.420 14.401 51.711 1.00 16.04 O ANISOU 2740 O PHE B 355 2481 1646 1966 -181 389 -458 O ATOM 2741 CB PHE A 355 3.703 15.709 51.931 1.00 18.82 C ANISOU 2741 CB PHE B 355 2863 1971 2317 -185 389 -427 C ATOM 2742 CG PHE A 355 4.077 16.906 51.046 1.00 17.94 C ANISOU 2742 CG PHE B 355 2715 1877 2224 -160 410 -432 C ATOM 2743 CD1 PHE A 355 3.386 17.154 49.858 1.00 18.30 C ANISOU 2743 CD1 PHE B 355 2729 1950 2275 -142 400 -415 C ATOM 2744 CD2 PHE A 355 5.155 17.713 51.368 1.00 18.82 C ANISOU 2744 CD2 PHE B 355 2822 1981 2348 -154 438 -455 C ATOM 2745 CE1 PHE A 355 3.722 18.201 49.025 1.00 17.63 C ANISOU 2745 CE1 PHE B 355 2611 1886 2203 -113 412 -420 C ATOM 2746 CE2 PHE A 355 5.500 18.811 50.548 1.00 18.75 C ANISOU 2746 CE2 PHE B 355 2772 1994 2357 -130 452 -463 C ATOM 2747 CZ PHE A 355 4.798 19.036 49.365 1.00 16.42 C ANISOU 2747 CZ PHE B 355 2446 1728 2064 -107 436 -445 C ATOM 2748 N SER A 356 5.710 14.243 49.575 1.00 18.30 N ANISOU 2748 N SER B 356 2696 1994 2265 -158 362 -439 N ATOM 2749 CA SER A 356 7.015 14.132 48.964 1.00 18.73 C ANISOU 2749 CA SER B 356 2717 2071 2328 -149 369 -459 C ATOM 2750 C SER A 356 7.285 15.395 48.162 1.00 19.26 C ANISOU 2750 C SER B 356 2749 2158 2409 -130 384 -469 C ATOM 2751 O SER A 356 6.432 15.871 47.447 1.00 18.69 O ANISOU 2751 O SER B 356 2662 2101 2337 -115 376 -453 O ATOM 2752 CB SER A 356 7.074 12.886 48.058 1.00 18.39 C ANISOU 2752 CB SER B 356 2647 2059 2280 -146 344 -451 C ATOM 2753 OG SER A 356 8.388 12.688 47.557 1.00 19.54 O ANISOU 2753 OG SER B 356 2768 2224 2433 -141 353 -472 O ATOM 2754 N TYR A 357 8.489 15.935 48.303 1.00 21.03 N ANISOU 2754 N TYR B 357 2960 2382 2646 -130 408 -498 N ATOM 2755 CA TYR A 357 8.887 17.134 47.592 1.00 22.38 C ANISOU 2755 CA TYR B 357 3091 2577 2834 -111 419 -515 C ATOM 2756 C TYR A 357 10.230 16.912 46.959 1.00 23.10 C ANISOU 2756 C TYR B 357 3145 2696 2935 -112 424 -545 C ATOM 2757 O TYR A 357 11.057 16.218 47.531 1.00 24.27 O ANISOU 2757 O TYR B 357 3311 2826 3083 -131 437 -559 O ATOM 2758 CB TYR A 357 9.012 18.334 48.567 1.00 22.78 C ANISOU 2758 CB TYR B 357 3161 2596 2898 -114 452 -528 C ATOM 2759 CG TYR A 357 9.252 19.646 47.839 1.00 24.01 C ANISOU 2759 CG TYR B 357 3272 2779 3074 -89 461 -544 C ATOM 2760 CD1 TYR A 357 8.203 20.288 47.180 1.00 23.81 C ANISOU 2760 CD1 TYR B 357 3236 2769 3044 -62 446 -521 C ATOM 2761 CD2 TYR A 357 10.531 20.219 47.779 1.00 22.63 C ANISOU 2761 CD2 TYR B 357 3062 2616 2920 -92 483 -583 C ATOM 2762 CE1 TYR A 357 8.418 21.474 46.483 1.00 24.73 C ANISOU 2762 CE1 TYR B 357 3308 2913 3174 -32 449 -534 C ATOM 2763 CE2 TYR A 357 10.750 21.420 47.093 1.00 22.97 C ANISOU 2763 CE2 TYR B 357 3056 2690 2981 -66 485 -601 C ATOM 2764 CZ TYR A 357 9.682 22.042 46.457 1.00 25.16 C ANISOU 2764 CZ TYR B 357 3324 2984 3252 -33 466 -574 C ATOM 2765 OH TYR A 357 9.860 23.228 45.750 1.00 26.80 O ANISOU 2765 OH TYR B 357 3483 3225 3474 0 463 -589 O ATOM 2766 N GLY A 358 10.461 17.524 45.806 1.00 24.01 N ANISOU 2766 N GLY B 358 3210 2853 3057 -91 415 -556 N ATOM 2767 CA GLY A 358 11.815 17.693 45.277 1.00 26.52 C ANISOU 2767 CA GLY B 358 3487 3198 3390 -94 425 -595 C ATOM 2768 C GLY A 358 11.808 19.046 44.607 1.00 28.20 C ANISOU 2768 C GLY B 358 3656 3442 3615 -68 423 -609 C ATOM 2769 O GLY A 358 10.858 19.379 43.882 1.00 28.50 O ANISOU 2769 O GLY B 358 3685 3501 3641 -40 400 -583 O ATOM 2770 N SER A 359 12.848 19.832 44.875 1.00 29.31 N ANISOU 2770 N SER B 359 3771 3585 3781 -75 449 -649 N ATOM 2771 CA SER A 359 13.070 21.137 44.267 1.00 30.23 C ANISOU 2771 CA SER B 359 3836 3736 3914 -49 447 -672 C ATOM 2772 C SER A 359 13.086 21.086 42.727 1.00 30.33 C ANISOU 2772 C SER B 359 3802 3810 3913 -22 409 -674 C ATOM 2773 O SER A 359 13.527 20.090 42.135 1.00 28.82 O ANISOU 2773 O SER B 359 3605 3636 3709 -34 396 -679 O ATOM 2774 CB SER A 359 14.406 21.683 44.762 1.00 30.99 C ANISOU 2774 CB SER B 359 3907 3826 4042 -72 483 -723 C ATOM 2775 OG SER A 359 14.331 21.949 46.159 1.00 35.63 O ANISOU 2775 OG SER B 359 4539 4358 4640 -91 522 -721 O ATOM 2776 N GLY A 360 12.608 22.173 42.107 1.00 30.07 N ANISOU 2776 N GLY B 360 3739 3807 3881 16 392 -669 N ATOM 2777 CA GLY A 360 12.636 22.320 40.659 1.00 29.69 C ANISOU 2777 CA GLY B 360 3648 3818 3816 49 356 -673 C ATOM 2778 C GLY A 360 11.369 22.461 39.809 1.00 30.26 C ANISOU 2778 C GLY B 360 3732 3908 3858 90 326 -628 C ATOM 2779 O GLY A 360 11.484 22.949 38.690 1.00 30.92 O ANISOU 2779 O GLY B 360 3777 4042 3929 125 298 -636 O ATOM 2780 N SER A 361 10.162 22.075 40.254 1.00 29.74 N ANISOU 2780 N SER B 361 3719 3803 3778 90 330 -581 N ATOM 2781 CA SER A 361 9.840 21.371 41.495 1.00 29.03 C ANISOU 2781 CA SER B 361 3680 3657 3694 52 354 -566 C ATOM 2782 C SER A 361 8.841 20.255 41.162 1.00 29.29 C ANISOU 2782 C SER B 361 3748 3680 3701 48 338 -525 C ATOM 2783 O SER A 361 8.106 20.339 40.167 1.00 28.74 O ANISOU 2783 O SER B 361 3675 3635 3611 77 319 -501 O ATOM 2784 CB SER A 361 9.235 22.326 42.531 1.00 29.81 C ANISOU 2784 CB SER B 361 3805 3715 3808 57 378 -556 C ATOM 2785 OG SER A 361 8.265 23.189 41.951 1.00 31.76 O ANISOU 2785 OG SER B 361 4050 3973 4044 100 366 -529 O ATOM 2786 N THR A 362 8.849 19.194 41.971 1.00 27.93 N ANISOU 2786 N THR B 362 3608 3474 3529 12 348 -520 N ATOM 2787 CA THR A 362 7.987 18.034 41.741 1.00 26.46 C ANISOU 2787 CA THR B 362 3449 3280 3324 3 335 -487 C ATOM 2788 C THR A 362 7.478 17.587 43.085 1.00 24.60 C ANISOU 2788 C THR B 362 3261 2994 3093 -26 349 -474 C ATOM 2789 O THR A 362 8.266 17.387 44.000 1.00 25.24 O ANISOU 2789 O THR B 362 3353 3054 3185 -49 365 -495 O ATOM 2790 CB THR A 362 8.771 16.880 41.113 1.00 26.76 C ANISOU 2790 CB THR B 362 3469 3343 3355 -10 323 -501 C ATOM 2791 OG1 THR A 362 9.839 16.516 42.004 1.00 27.63 O ANISOU 2791 OG1 THR B 362 3584 3433 3481 -39 341 -530 O ATOM 2792 CG2 THR A 362 9.343 17.303 39.760 1.00 27.74 C ANISOU 2792 CG2 THR B 362 3547 3520 3471 16 307 -519 C ATOM 2793 N ALA A 363 6.169 17.489 43.252 1.00 21.79 N ANISOU 2793 N ALA B 363 2935 2617 2727 -25 346 -441 N ATOM 2794 CA ALA A 363 5.659 17.129 44.549 1.00 20.14 C ANISOU 2794 CA ALA B 363 2770 2362 2519 -52 356 -433 C ATOM 2795 C ALA A 363 4.398 16.314 44.419 1.00 19.46 C ANISOU 2795 C ALA B 363 2706 2266 2421 -61 344 -402 C ATOM 2796 O ALA A 363 3.647 16.481 43.454 1.00 18.96 O ANISOU 2796 O ALA B 363 2635 2220 2350 -42 338 -382 O ATOM 2797 CB ALA A 363 5.420 18.392 45.423 1.00 18.86 C ANISOU 2797 CB ALA B 363 2629 2169 2368 -47 380 -436 C ATOM 2798 N THR A 364 4.201 15.420 45.389 1.00 18.28 N ANISOU 2798 N THR B 364 2585 2091 2270 -90 341 -401 N ATOM 2799 CA THR A 364 3.004 14.603 45.472 1.00 18.02 C ANISOU 2799 CA THR B 364 2572 2046 2230 -105 330 -378 C ATOM 2800 C THR A 364 2.639 14.348 46.912 1.00 18.44 C ANISOU 2800 C THR B 364 2666 2060 2282 -132 332 -380 C ATOM 2801 O THR A 364 3.492 14.000 47.739 1.00 18.54 O ANISOU 2801 O THR B 364 2689 2061 2293 -144 332 -397 O ATOM 2802 CB THR A 364 3.195 13.224 44.784 1.00 18.13 C ANISOU 2802 CB THR B 364 2562 2088 2240 -111 310 -375 C ATOM 2803 OG1 THR A 364 3.480 13.442 43.408 1.00 18.89 O ANISOU 2803 OG1 THR B 364 2625 2221 2333 -86 308 -373 O ATOM 2804 CG2 THR A 364 1.894 12.352 44.855 1.00 14.79 C ANISOU 2804 CG2 THR B 364 2152 1654 1814 -129 299 -355 C ATOM 2805 N MET A 365 1.364 14.528 47.203 1.00 18.50 N ANISOU 2805 N MET B 365 2699 2045 2286 -142 335 -364 N ATOM 2806 CA MET A 365 0.803 14.107 48.477 1.00 19.43 C ANISOU 2806 CA MET B 365 2855 2130 2399 -171 331 -366 C ATOM 2807 C MET A 365 -0.075 12.895 48.178 1.00 18.63 C ANISOU 2807 C MET B 365 2745 2039 2295 -188 309 -354 C ATOM 2808 O MET A 365 -0.933 12.983 47.307 1.00 20.24 O ANISOU 2808 O MET B 365 2937 2251 2501 -184 314 -339 O ATOM 2809 CB MET A 365 -0.044 15.246 49.087 1.00 18.08 C ANISOU 2809 CB MET B 365 2719 1922 2228 -174 353 -361 C ATOM 2810 CG MET A 365 -0.705 14.826 50.386 1.00 20.34 C ANISOU 2810 CG MET B 365 3049 2175 2505 -206 348 -365 C ATOM 2811 SD MET A 365 -1.568 16.129 51.289 1.00 20.93 S ANISOU 2811 SD MET B 365 3173 2201 2578 -214 379 -364 S ATOM 2812 CE MET A 365 -0.169 16.972 52.012 1.00 22.65 C ANISOU 2812 CE MET B 365 3401 2407 2798 -201 400 -384 C ATOM 2813 N PHE A 366 0.162 11.768 48.851 1.00 17.56 N ANISOU 2813 N PHE B 366 2614 1904 2154 -205 287 -363 N ATOM 2814 CA PHE A 366 -0.589 10.548 48.545 1.00 18.44 C ANISOU 2814 CA PHE B 366 2708 2031 2268 -220 265 -356 C ATOM 2815 C PHE A 366 -1.024 9.856 49.849 1.00 19.25 C ANISOU 2815 C PHE B 366 2838 2114 2362 -246 244 -365 C ATOM 2816 O PHE A 366 -0.395 9.999 50.881 1.00 20.61 O ANISOU 2816 O PHE B 366 3040 2268 2522 -248 242 -376 O ATOM 2817 CB PHE A 366 0.233 9.583 47.597 1.00 17.28 C ANISOU 2817 CB PHE B 366 2519 1922 2125 -205 252 -356 C ATOM 2818 CG PHE A 366 1.569 9.138 48.161 1.00 17.45 C ANISOU 2818 CG PHE B 366 2544 1945 2140 -198 243 -371 C ATOM 2819 CD1 PHE A 366 2.702 9.942 48.041 1.00 14.83 C ANISOU 2819 CD1 PHE B 366 2213 1613 1809 -182 262 -381 C ATOM 2820 CD2 PHE A 366 1.701 7.895 48.785 1.00 18.31 C ANISOU 2820 CD2 PHE B 366 2656 2057 2245 -206 218 -375 C ATOM 2821 CE1 PHE A 366 3.937 9.514 48.529 1.00 14.79 C ANISOU 2821 CE1 PHE B 366 2214 1605 1800 -178 262 -395 C ATOM 2822 CE2 PHE A 366 2.936 7.467 49.291 1.00 18.52 C ANISOU 2822 CE2 PHE B 366 2692 2080 2264 -196 215 -386 C ATOM 2823 CZ PHE A 366 4.060 8.277 49.148 1.00 15.71 C ANISOU 2823 CZ PHE B 366 2340 1719 1909 -184 240 -396 C ATOM 2824 N SER A 367 -2.074 9.063 49.806 1.00 20.48 N ANISOU 2824 N SER B 367 2984 2276 2523 -267 228 -362 N ATOM 2825 CA SER A 367 -2.557 8.501 51.051 1.00 20.94 C ANISOU 2825 CA SER B 367 3067 2318 2570 -291 204 -374 C ATOM 2826 C SER A 367 -2.379 6.993 51.059 1.00 20.73 C ANISOU 2826 C SER B 367 3011 2320 2546 -292 168 -379 C ATOM 2827 O SER A 367 -2.453 6.350 49.995 1.00 20.97 O ANISOU 2827 O SER B 367 2999 2378 2592 -286 167 -372 O ATOM 2828 CB SER A 367 -4.025 8.913 51.275 1.00 20.74 C ANISOU 2828 CB SER B 367 3060 2270 2550 -320 214 -374 C ATOM 2829 OG SER A 367 -4.485 8.411 52.516 1.00 24.07 O ANISOU 2829 OG SER B 367 3507 2679 2959 -345 188 -390 O ATOM 2830 N LEU A 368 -2.090 6.458 52.254 1.00 21.09 N ANISOU 2830 N LEU B 368 3082 2357 2574 -296 142 -391 N ATOM 2831 CA LEU A 368 -1.988 5.024 52.540 1.00 21.67 C ANISOU 2831 CA LEU B 368 3134 2454 2645 -294 102 -397 C ATOM 2832 C LEU A 368 -2.991 4.584 53.599 1.00 23.97 C ANISOU 2832 C LEU B 368 3442 2738 2927 -321 71 -411 C ATOM 2833 O LEU A 368 -3.299 5.332 54.537 1.00 24.12 O ANISOU 2833 O LEU B 368 3509 2728 2929 -336 77 -418 O ATOM 2834 CB LEU A 368 -0.569 4.655 53.063 1.00 20.03 C ANISOU 2834 CB LEU B 368 2945 2245 2419 -267 93 -398 C ATOM 2835 CG LEU A 368 0.647 5.178 52.261 1.00 18.52 C ANISOU 2835 CG LEU B 368 2746 2057 2235 -243 124 -392 C ATOM 2836 CD1 LEU A 368 2.006 5.011 53.038 1.00 18.67 C ANISOU 2836 CD1 LEU B 368 2799 2061 2234 -223 125 -396 C ATOM 2837 CD2 LEU A 368 0.683 4.510 50.875 1.00 15.03 C ANISOU 2837 CD2 LEU B 368 2247 1649 1814 -233 125 -384 C ATOM 2838 N ARG A 369 -3.436 3.341 53.483 1.00 25.45 N ANISOU 2838 N ARG B 369 3590 2955 3125 -327 37 -417 N ATOM 2839 CA ARG A 369 -4.228 2.709 54.535 1.00 28.23 C ANISOU 2839 CA ARG B 369 3951 3309 3465 -348 -3 -435 C ATOM 2840 C ARG A 369 -3.421 1.559 55.047 1.00 28.51 C ANISOU 2840 C ARG B 369 3981 3366 3487 -320 -44 -438 C ATOM 2841 O ARG A 369 -2.961 0.734 54.259 1.00 27.69 O ANISOU 2841 O ARG B 369 3832 3289 3399 -299 -50 -431 O ATOM 2842 CB ARG A 369 -5.550 2.169 53.984 1.00 28.48 C ANISOU 2842 CB ARG B 369 3935 3361 3527 -380 -10 -445 C ATOM 2843 CG ARG A 369 -6.521 3.267 53.719 1.00 34.02 C ANISOU 2843 CG ARG B 369 4655 4035 4238 -410 29 -445 C ATOM 2844 CD ARG A 369 -7.867 3.055 54.452 1.00 36.89 C ANISOU 2844 CD ARG B 369 5022 4392 4604 -454 11 -470 C ATOM 2845 NE ARG A 369 -7.795 3.337 55.871 1.00 34.65 N ANISOU 2845 NE ARG B 369 4792 4089 4287 -460 -13 -484 N ATOM 2846 CZ ARG A 369 -8.496 4.292 56.488 1.00 37.82 C ANISOU 2846 CZ ARG B 369 5239 4454 4677 -489 7 -493 C ATOM 2847 NH1 ARG A 369 -9.305 5.105 55.811 1.00 35.06 N ANISOU 2847 NH1 ARG B 369 4891 4082 4348 -511 53 -488 N ATOM 2848 NH2 ARG A 369 -8.391 4.438 57.802 1.00 37.00 N ANISOU 2848 NH2 ARG B 369 5186 4334 4539 -493 -17 -508 N ATOM 2849 N LEU A 370 -3.235 1.510 56.356 1.00 29.32 N ANISOU 2849 N LEU B 370 4130 3454 3555 -317 -71 -447 N ATOM 2850 CA LEU A 370 -2.483 0.423 56.945 1.00 31.05 C ANISOU 2850 CA LEU B 370 4353 3690 3755 -285 -112 -448 C ATOM 2851 C LEU A 370 -3.446 -0.663 57.475 1.00 33.13 C ANISOU 2851 C LEU B 370 4586 3984 4019 -298 -168 -467 C ATOM 2852 O LEU A 370 -4.570 -0.368 57.898 1.00 31.99 O ANISOU 2852 O LEU B 370 4446 3835 3875 -336 -177 -485 O ATOM 2853 CB LEU A 370 -1.518 0.929 58.017 1.00 30.90 C ANISOU 2853 CB LEU B 370 4408 3638 3695 -266 -106 -444 C ATOM 2854 CG LEU A 370 -0.469 2.048 57.746 1.00 31.25 C ANISOU 2854 CG LEU B 370 4487 3650 3736 -254 -51 -430 C ATOM 2855 CD1 LEU A 370 0.852 1.618 58.259 1.00 29.58 C ANISOU 2855 CD1 LEU B 370 4310 3429 3499 -218 -54 -423 C ATOM 2856 CD2 LEU A 370 -0.295 2.543 56.300 1.00 25.51 C ANISOU 2856 CD2 LEU B 370 3715 2932 3045 -255 -10 -420 C ATOM 2857 N CYS A 371 -2.985 -1.912 57.427 1.00 34.53 N ANISOU 2857 N CYS B 371 4731 4192 4197 -267 -204 -465 N ATOM 2858 CA CYS A 371 -3.830 -3.090 57.573 1.00 37.47 C ANISOU 2858 CA CYS B 371 5051 4604 4583 -274 -256 -484 C ATOM 2859 C CYS A 371 -3.118 -4.171 58.357 1.00 37.85 C ANISOU 2859 C CYS B 371 5109 4670 4603 -229 -308 -483 C ATOM 2860 O CYS A 371 -1.890 -4.326 58.251 1.00 37.13 O ANISOU 2860 O CYS B 371 5041 4569 4499 -188 -294 -463 O ATOM 2861 CB CYS A 371 -4.159 -3.672 56.195 1.00 36.99 C ANISOU 2861 CB CYS B 371 4910 4571 4571 -279 -240 -482 C ATOM 2862 SG CYS A 371 -5.130 -2.575 55.151 1.00 45.67 S ANISOU 2862 SG CYS B 371 5994 5654 5704 -328 -181 -481 S ATOM 2863 N GLU A 372 -3.900 -4.931 59.118 1.00 39.51 N ANISOU 2863 N GLU B 372 5301 4907 4804 -236 -366 -506 N ATOM 2864 CA GLU A 372 -3.402 -6.120 59.803 1.00 41.75 C ANISOU 2864 CA GLU B 372 5583 5217 5063 -189 -424 -507 C ATOM 2865 C GLU A 372 -3.116 -7.165 58.740 1.00 41.42 C ANISOU 2865 C GLU B 372 5466 5208 5062 -163 -425 -498 C ATOM 2866 O GLU A 372 -3.893 -7.326 57.807 1.00 41.52 O ANISOU 2866 O GLU B 372 5412 5242 5122 -193 -410 -508 O ATOM 2867 CB GLU A 372 -4.436 -6.639 60.817 1.00 42.71 C ANISOU 2867 CB GLU B 372 5695 5365 5168 -206 -490 -538 C ATOM 2868 CG GLU A 372 -4.376 -8.149 61.049 1.00 47.31 C ANISOU 2868 CG GLU B 372 6227 5997 5752 -165 -557 -546 C ATOM 2869 CD GLU A 372 -4.673 -8.542 62.480 1.00 54.77 C ANISOU 2869 CD GLU B 372 7208 6955 6646 -152 -628 -566 C ATOM 2870 OE1 GLU A 372 -5.414 -9.539 62.688 1.00 56.19 O ANISOU 2870 OE1 GLU B 372 7325 7184 6839 -152 -688 -593 O ATOM 2871 OE2 GLU A 372 -4.156 -7.856 63.402 1.00 57.66 O ANISOU 2871 OE2 GLU B 372 7664 7284 6958 -142 -622 -556 O ATOM 2872 N ASN A 373 -1.986 -7.846 58.859 1.00 41.92 N ANISOU 2872 N ASN B 373 5545 5273 5107 -107 -436 -479 N ATOM 2873 CA ASN A 373 -1.591 -8.832 57.864 1.00 42.02 C ANISOU 2873 CA ASN B 373 5494 5314 5157 -77 -432 -470 C ATOM 2874 C ASN A 373 -0.723 -9.827 58.586 1.00 42.72 C ANISOU 2874 C ASN B 373 5606 5412 5213 -14 -475 -459 C ATOM 2875 O ASN A 373 -0.201 -9.511 59.644 1.00 42.55 O ANISOU 2875 O ASN B 373 5661 5364 5141 6 -488 -452 O ATOM 2876 CB ASN A 373 -0.777 -8.136 56.779 1.00 41.88 C ANISOU 2876 CB ASN B 373 5487 5269 5157 -78 -362 -448 C ATOM 2877 CG ASN A 373 -1.035 -8.687 55.395 1.00 43.51 C ANISOU 2877 CG ASN B 373 5614 5503 5417 -85 -339 -448 C ATOM 2878 OD1 ASN A 373 -2.170 -9.003 55.046 1.00 47.65 O ANISOU 2878 OD1 ASN B 373 6077 6055 5974 -117 -352 -467 O ATOM 2879 ND2 ASN A 373 0.023 -8.773 54.578 1.00 44.79 N ANISOU 2879 ND2 ASN B 373 5777 5655 5587 -57 -301 -429 N ATOM 2880 N GLN A 374 -0.554 -11.028 58.048 1.00 43.45 N ANISOU 2880 N GLN B 374 5637 5539 5333 21 -495 -457 N ATOM 2881 CA GLN A 374 0.320 -11.979 58.722 1.00 45.31 C ANISOU 2881 CA GLN B 374 5900 5779 5536 88 -534 -444 C ATOM 2882 C GLN A 374 1.775 -11.691 58.369 1.00 43.52 C ANISOU 2882 C GLN B 374 5728 5511 5296 122 -479 -414 C ATOM 2883 O GLN A 374 2.077 -11.158 57.310 1.00 43.34 O ANISOU 2883 O GLN B 374 5690 5473 5303 100 -420 -407 O ATOM 2884 CB GLN A 374 -0.071 -13.437 58.434 1.00 46.23 C ANISOU 2884 CB GLN B 374 5931 5950 5686 119 -582 -455 C ATOM 2885 CG GLN A 374 0.256 -13.977 57.012 1.00 48.90 C ANISOU 2885 CG GLN B 374 6203 6300 6077 128 -540 -446 C ATOM 2886 CD GLN A 374 -0.438 -15.316 56.735 1.00 49.51 C ANISOU 2886 CD GLN B 374 6183 6434 6195 145 -586 -465 C ATOM 2887 OE1 GLN A 374 0.213 -16.343 56.515 1.00 54.47 O ANISOU 2887 OE1 GLN B 374 6789 7077 6832 202 -597 -453 O ATOM 2888 NE2 GLN A 374 -1.772 -15.310 56.776 1.00 53.64 N ANISOU 2888 NE2 GLN B 374 6649 6988 6744 96 -612 -496 N ATOM 2889 N SER A 375 2.656 -11.990 59.308 1.00 42.64 N ANISOU 2889 N SER B 375 5686 5380 5136 172 -498 -398 N ATOM 2890 CA SER A 375 4.088 -12.003 59.090 1.00 41.39 C ANISOU 2890 CA SER B 375 5578 5184 4963 212 -453 -372 C ATOM 2891 C SER A 375 4.427 -12.942 57.907 1.00 40.34 C ANISOU 2891 C SER B 375 5376 5074 4877 237 -436 -366 C ATOM 2892 O SER A 375 3.705 -13.916 57.657 1.00 40.85 O ANISOU 2892 O SER B 375 5364 5185 4970 248 -479 -378 O ATOM 2893 CB SER A 375 4.773 -12.421 60.401 1.00 41.80 C ANISOU 2893 CB SER B 375 5712 5217 4954 268 -487 -358 C ATOM 2894 OG SER A 375 6.157 -12.662 60.246 1.00 43.48 O ANISOU 2894 OG SER B 375 5973 5394 5154 314 -446 -334 O ATOM 2895 N PRO A 376 5.521 -12.656 57.165 1.00 38.67 N ANISOU 2895 N PRO B 376 5188 4831 4675 246 -373 -350 N ATOM 2896 CA PRO A 376 6.548 -11.655 57.429 1.00 37.10 C ANISOU 2896 CA PRO B 376 5073 4577 4446 240 -320 -338 C ATOM 2897 C PRO A 376 6.163 -10.229 57.005 1.00 35.52 C ANISOU 2897 C PRO B 376 4876 4362 4259 176 -277 -348 C ATOM 2898 O PRO A 376 6.878 -9.285 57.335 1.00 35.32 O ANISOU 2898 O PRO B 376 4917 4293 4209 166 -236 -343 O ATOM 2899 CB PRO A 376 7.729 -12.170 56.606 1.00 37.40 C ANISOU 2899 CB PRO B 376 5109 4599 4500 274 -275 -324 C ATOM 2900 CG PRO A 376 7.069 -12.729 55.370 1.00 37.79 C ANISOU 2900 CG PRO B 376 5061 4692 4604 260 -277 -333 C ATOM 2901 CD PRO A 376 5.783 -13.387 55.900 1.00 38.27 C ANISOU 2901 CD PRO B 376 5070 4799 4670 259 -348 -347 C ATOM 2902 N PHE A 377 5.047 -10.098 56.294 1.00 33.74 N ANISOU 2902 N PHE B 377 4579 4169 4071 135 -285 -363 N ATOM 2903 CA PHE A 377 4.603 -8.826 55.708 1.00 32.07 C ANISOU 2903 CA PHE B 377 4361 3946 3877 79 -244 -371 C ATOM 2904 C PHE A 377 3.516 -8.196 56.592 1.00 31.27 C ANISOU 2904 C PHE B 377 4277 3846 3759 44 -275 -385 C ATOM 2905 O PHE A 377 2.369 -8.033 56.171 1.00 31.43 O ANISOU 2905 O PHE B 377 4245 3890 3806 5 -283 -399 O ATOM 2906 CB PHE A 377 4.104 -9.029 54.240 1.00 30.16 C ANISOU 2906 CB PHE B 377 4038 3735 3688 57 -222 -377 C ATOM 2907 CG PHE A 377 5.138 -9.666 53.292 1.00 30.38 C ANISOU 2907 CG PHE B 377 4047 3763 3734 90 -190 -366 C ATOM 2908 CD1 PHE A 377 4.722 -10.495 52.244 1.00 30.92 C ANISOU 2908 CD1 PHE B 377 4039 3866 3843 92 -191 -370 C ATOM 2909 CD2 PHE A 377 6.496 -9.425 53.428 1.00 28.69 C ANISOU 2909 CD2 PHE B 377 3891 3512 3498 114 -155 -354 C ATOM 2910 CE1 PHE A 377 5.643 -11.059 51.362 1.00 30.70 C ANISOU 2910 CE1 PHE B 377 3996 3836 3831 119 -159 -362 C ATOM 2911 CE2 PHE A 377 7.428 -9.990 52.559 1.00 29.30 C ANISOU 2911 CE2 PHE B 377 3953 3587 3591 140 -123 -348 C ATOM 2912 CZ PHE A 377 6.997 -10.823 51.533 1.00 29.75 C ANISOU 2912 CZ PHE B 377 3937 3680 3688 144 -126 -351 C ATOM 2913 N SER A 378 3.907 -7.845 57.814 1.00 31.36 N ANISOU 2913 N SER B 378 4365 3828 3722 57 -286 -381 N ATOM 2914 CA SER A 378 3.032 -7.284 58.825 1.00 30.99 C ANISOU 2914 CA SER B 378 4349 3776 3648 29 -315 -395 C ATOM 2915 C SER A 378 3.742 -6.065 59.365 1.00 30.26 C ANISOU 2915 C SER B 378 4339 3633 3525 18 -270 -388 C ATOM 2916 O SER A 378 4.983 -5.997 59.334 1.00 30.34 O ANISOU 2916 O SER B 378 4392 3614 3523 45 -234 -373 O ATOM 2917 CB SER A 378 2.823 -8.294 59.964 1.00 31.89 C ANISOU 2917 CB SER B 378 4480 3910 3727 65 -385 -398 C ATOM 2918 OG SER A 378 4.020 -8.480 60.724 1.00 32.50 O ANISOU 2918 OG SER B 378 4635 3954 3759 113 -380 -380 O ATOM 2919 N LEU A 379 2.974 -5.105 59.859 1.00 29.09 N ANISOU 2919 N LEU B 379 4215 3472 3367 -23 -268 -400 N ATOM 2920 CA LEU A 379 3.541 -3.907 60.468 1.00 29.06 C ANISOU 2920 CA LEU B 379 4288 3419 3333 -35 -225 -397 C ATOM 2921 C LEU A 379 4.503 -4.240 61.626 1.00 30.10 C ANISOU 2921 C LEU B 379 4502 3522 3412 8 -234 -385 C ATOM 2922 O LEU A 379 5.573 -3.633 61.752 1.00 29.04 O ANISOU 2922 O LEU B 379 4422 3346 3264 16 -183 -376 O ATOM 2923 CB LEU A 379 2.409 -2.946 60.916 1.00 28.62 C ANISOU 2923 CB LEU B 379 4245 3357 3274 -83 -228 -413 C ATOM 2924 CG LEU A 379 1.476 -2.522 59.754 1.00 27.71 C ANISOU 2924 CG LEU B 379 4057 3261 3208 -123 -210 -421 C ATOM 2925 CD1 LEU A 379 0.140 -1.905 60.208 1.00 27.36 C ANISOU 2925 CD1 LEU B 379 4015 3217 3163 -168 -223 -440 C ATOM 2926 CD2 LEU A 379 2.216 -1.588 58.781 1.00 27.86 C ANISOU 2926 CD2 LEU B 379 4073 3259 3252 -130 -144 -411 C ATOM 2927 N SER A 380 4.112 -5.190 62.474 1.00 31.01 N ANISOU 2927 N SER B 380 4627 3659 3497 34 -298 -388 N ATOM 2928 CA SER A 380 4.939 -5.577 63.626 1.00 32.11 C ANISOU 2928 CA SER B 380 4851 3771 3579 80 -312 -375 C ATOM 2929 C SER A 380 6.241 -6.206 63.197 1.00 31.00 C ANISOU 2929 C SER B 380 4721 3617 3442 126 -285 -355 C ATOM 2930 O SER A 380 7.304 -5.831 63.679 1.00 31.56 O ANISOU 2930 O SER B 380 4868 3640 3482 144 -243 -342 O ATOM 2931 CB SER A 380 4.153 -6.490 64.574 1.00 32.69 C ANISOU 2931 CB SER B 380 4926 3878 3618 101 -395 -385 C ATOM 2932 OG SER A 380 3.021 -5.762 65.063 1.00 35.87 O ANISOU 2932 OG SER B 380 5332 4284 4013 52 -412 -407 O ATOM 2933 N ASN A 381 6.178 -7.135 62.256 1.00 31.12 N ANISOU 2933 N ASN B 381 4659 3669 3495 143 -301 -352 N ATOM 2934 CA ASN A 381 7.405 -7.710 61.767 1.00 31.19 C ANISOU 2934 CA ASN B 381 4678 3663 3511 184 -269 -334 C ATOM 2935 C ASN A 381 8.297 -6.729 60.985 1.00 30.22 C ANISOU 2935 C ASN B 381 4566 3504 3412 159 -188 -332 C ATOM 2936 O ASN A 381 9.520 -6.830 61.040 1.00 30.69 O ANISOU 2936 O ASN B 381 4674 3528 3458 187 -148 -320 O ATOM 2937 CB ASN A 381 7.156 -8.971 60.968 1.00 31.87 C ANISOU 2937 CB ASN B 381 4681 3795 3631 212 -304 -332 C ATOM 2938 CG ASN A 381 8.422 -9.682 60.662 1.00 32.86 C ANISOU 2938 CG ASN B 381 4827 3902 3756 262 -276 -313 C ATOM 2939 OD1 ASN A 381 9.172 -10.044 61.577 1.00 33.17 O ANISOU 2939 OD1 ASN B 381 4942 3912 3748 307 -281 -298 O ATOM 2940 ND2 ASN A 381 8.693 -9.892 59.373 1.00 34.44 N ANISOU 2940 ND2 ASN B 381 4965 4115 4004 255 -244 -314 N ATOM 2941 N ILE A 382 7.698 -5.751 60.306 1.00 29.36 N ANISOU 2941 N ILE B 382 4417 3402 3337 107 -163 -346 N ATOM 2942 CA ILE A 382 8.499 -4.711 59.660 1.00 27.60 C ANISOU 2942 CA ILE B 382 4205 3148 3133 83 -91 -347 C ATOM 2943 C ILE A 382 9.281 -3.936 60.727 1.00 28.59 C ANISOU 2943 C ILE B 382 4428 3220 3217 84 -55 -344 C ATOM 2944 O ILE A 382 10.492 -3.727 60.572 1.00 28.05 O ANISOU 2944 O ILE B 382 4393 3116 3148 95 -2 -340 O ATOM 2945 CB ILE A 382 7.652 -3.776 58.752 1.00 27.03 C ANISOU 2945 CB ILE B 382 4075 3095 3101 32 -74 -361 C ATOM 2946 CG1 ILE A 382 7.129 -4.568 57.527 1.00 26.95 C ANISOU 2946 CG1 ILE B 382 3974 3132 3134 33 -93 -362 C ATOM 2947 CG2 ILE A 382 8.479 -2.560 58.281 1.00 23.50 C ANISOU 2947 CG2 ILE B 382 3646 2615 2666 10 -5 -365 C ATOM 2948 CD1 ILE A 382 6.084 -3.822 56.614 1.00 25.79 C ANISOU 2948 CD1 ILE B 382 3768 3008 3024 -13 -84 -372 C ATOM 2949 N ALA A 383 8.607 -3.560 61.818 1.00 28.37 N ANISOU 2949 N ALA B 383 4443 3182 3154 73 -82 -349 N ATOM 2950 CA ALA A 383 9.252 -2.792 62.915 1.00 30.22 C ANISOU 2950 CA ALA B 383 4775 3363 3346 73 -46 -347 C ATOM 2951 C ALA A 383 10.391 -3.592 63.544 1.00 30.57 C ANISOU 2951 C ALA B 383 4887 3377 3352 124 -39 -330 C ATOM 2952 O ALA A 383 11.465 -3.063 63.850 1.00 30.96 O ANISOU 2952 O ALA B 383 4999 3376 3387 126 21 -326 O ATOM 2953 CB ALA A 383 8.221 -2.402 63.987 1.00 30.05 C ANISOU 2953 CB ALA B 383 4788 3341 3289 55 -84 -355 C ATOM 2954 N SER A 384 10.154 -4.880 63.700 1.00 31.47 N ANISOU 2954 N SER B 384 4984 3520 3451 166 -98 -319 N ATOM 2955 CA SER A 384 11.144 -5.779 64.289 1.00 32.53 C ANISOU 2955 CA SER B 384 5182 3630 3548 224 -98 -299 C ATOM 2956 C SER A 384 12.368 -5.946 63.389 1.00 32.57 C ANISOU 2956 C SER B 384 5178 3613 3583 236 -37 -293 C ATOM 2957 O SER A 384 13.508 -5.813 63.849 1.00 31.90 O ANISOU 2957 O SER B 384 5172 3476 3473 255 14 -283 O ATOM 2958 CB SER A 384 10.490 -7.119 64.572 1.00 32.43 C ANISOU 2958 CB SER B 384 5141 3663 3519 268 -181 -292 C ATOM 2959 OG SER A 384 11.462 -8.039 64.974 1.00 38.04 O ANISOU 2959 OG SER B 384 5905 4350 4198 330 -180 -270 O ATOM 2960 N VAL A 385 12.130 -6.216 62.098 1.00 32.52 N ANISOU 2960 N VAL B 385 5079 3645 3631 223 -39 -299 N ATOM 2961 CA VAL A 385 13.221 -6.378 61.142 1.00 32.44 C ANISOU 2961 CA VAL B 385 5054 3620 3652 230 17 -298 C ATOM 2962 C VAL A 385 14.080 -5.107 61.042 1.00 31.80 C ANISOU 2962 C VAL B 385 5011 3492 3579 193 96 -309 C ATOM 2963 O VAL A 385 15.309 -5.180 61.109 1.00 31.59 O ANISOU 2963 O VAL B 385 5036 3423 3545 209 150 -305 O ATOM 2964 CB VAL A 385 12.687 -6.812 59.755 1.00 32.23 C ANISOU 2964 CB VAL B 385 4921 3646 3681 219 0 -305 C ATOM 2965 CG1 VAL A 385 13.749 -6.606 58.664 1.00 32.89 C ANISOU 2965 CG1 VAL B 385 4985 3712 3798 209 65 -311 C ATOM 2966 CG2 VAL A 385 12.211 -8.260 59.816 1.00 32.65 C ANISOU 2966 CG2 VAL B 385 4940 3737 3729 266 -66 -293 C ATOM 2967 N MET A 386 13.443 -3.945 60.901 1.00 30.72 N ANISOU 2967 N MET B 386 4851 3363 3459 143 106 -326 N ATOM 2968 CA MET A 386 14.196 -2.688 60.750 1.00 30.24 C ANISOU 2968 CA MET B 386 4815 3264 3412 107 179 -340 C ATOM 2969 C MET A 386 15.069 -2.339 61.972 1.00 30.17 C ANISOU 2969 C MET B 386 4913 3193 3359 118 222 -336 C ATOM 2970 O MET A 386 16.058 -1.631 61.833 1.00 30.40 O ANISOU 2970 O MET B 386 4968 3183 3399 99 291 -347 O ATOM 2971 CB MET A 386 13.293 -1.486 60.421 1.00 29.05 C ANISOU 2971 CB MET B 386 4621 3133 3285 58 180 -357 C ATOM 2972 CG MET A 386 12.514 -1.551 59.115 1.00 28.14 C ANISOU 2972 CG MET B 386 4407 3071 3216 40 156 -363 C ATOM 2973 SD MET A 386 11.732 0.044 58.738 1.00 30.41 S ANISOU 2973 SD MET B 386 4660 3365 3529 -13 176 -381 S ATOM 2974 CE MET A 386 10.653 0.203 60.169 1.00 25.17 C ANISOU 2974 CE MET B 386 4049 2693 2823 -18 133 -377 C ATOM 2975 N ASP A 387 14.679 -2.780 63.166 1.00 31.75 N ANISOU 2975 N ASP B 387 5174 3382 3507 145 181 -321 N ATOM 2976 CA ASP A 387 15.540 -2.652 64.380 1.00 31.90 C ANISOU 2976 CA ASP B 387 5307 3340 3476 165 220 -312 C ATOM 2977 C ASP A 387 16.134 -1.253 64.533 1.00 32.00 C ANISOU 2977 C ASP B 387 5353 3307 3498 121 298 -331 C ATOM 2978 O ASP A 387 17.336 -1.077 64.777 1.00 32.24 O ANISOU 2978 O ASP B 387 5444 3286 3522 126 366 -332 O ATOM 2979 CB ASP A 387 16.653 -3.715 64.336 1.00 32.53 C ANISOU 2979 CB ASP B 387 5425 3395 3542 214 240 -295 C ATOM 2980 CG ASP A 387 17.213 -4.065 65.725 1.00 35.69 C ANISOU 2980 CG ASP B 387 5944 3742 3874 255 249 -275 C ATOM 2981 OD1 ASP A 387 16.492 -3.882 66.737 1.00 38.18 O ANISOU 2981 OD1 ASP B 387 6303 4057 4146 259 210 -271 O ATOM 2982 OD2 ASP A 387 18.380 -4.531 65.790 1.00 37.70 O ANISOU 2982 OD2 ASP B 387 6254 3954 4118 285 297 -264 O ATOM 2983 N VAL A 388 15.279 -0.248 64.357 1.00 31.77 N ANISOU 2983 N VAL B 388 5282 3297 3490 79 292 -347 N ATOM 2984 CA VAL A 388 15.702 1.144 64.343 1.00 32.02 C ANISOU 2984 CA VAL B 388 5326 3298 3543 36 361 -367 C ATOM 2985 C VAL A 388 16.317 1.530 65.711 1.00 32.41 C ANISOU 2985 C VAL B 388 5489 3282 3542 42 405 -364 C ATOM 2986 O VAL A 388 17.306 2.267 65.769 1.00 31.47 O ANISOU 2986 O VAL B 388 5403 3118 3436 22 483 -378 O ATOM 2987 CB VAL A 388 14.506 2.090 63.949 1.00 30.97 C ANISOU 2987 CB VAL B 388 5129 3201 3439 -4 337 -382 C ATOM 2988 CG1 VAL A 388 14.751 3.509 64.448 1.00 30.38 C ANISOU 2988 CG1 VAL B 388 5092 3085 3366 -39 399 -399 C ATOM 2989 CG2 VAL A 388 14.253 2.075 62.404 1.00 31.33 C ANISOU 2989 CG2 VAL B 388 5066 3296 3541 -19 326 -391 C ATOM 2990 N GLY A 389 15.732 0.998 66.788 1.00 33.81 N ANISOU 2990 N GLY B 389 5726 3456 3664 69 356 -347 N ATOM 2991 CA GLY A 389 16.278 1.138 68.146 1.00 35.24 C ANISOU 2991 CA GLY B 389 6028 3577 3787 84 390 -338 C ATOM 2992 C GLY A 389 17.713 0.654 68.250 1.00 35.85 C ANISOU 2992 C GLY B 389 6166 3604 3852 112 450 -329 C ATOM 2993 O GLY A 389 18.606 1.408 68.632 1.00 36.42 O ANISOU 2993 O GLY B 389 6296 3620 3922 92 531 -339 O ATOM 2994 N GLY A 390 17.931 -0.606 67.883 1.00 36.33 N ANISOU 2994 N GLY B 390 6211 3685 3907 156 413 -310 N ATOM 2995 CA GLY A 390 19.268 -1.193 67.751 1.00 35.66 C ANISOU 2995 CA GLY B 390 6172 3558 3820 183 468 -301 C ATOM 2996 C GLY A 390 20.266 -0.427 66.897 1.00 35.11 C ANISOU 2996 C GLY B 390 6070 3464 3806 142 554 -326 C ATOM 2997 O GLY A 390 21.398 -0.235 67.309 1.00 35.42 O ANISOU 2997 O GLY B 390 6183 3440 3834 142 632 -329 O ATOM 2998 N LYS A 391 19.868 0.008 65.704 1.00 33.95 N ANISOU 2998 N LYS B 391 5814 3366 3720 107 544 -347 N ATOM 2999 CA LYS A 391 20.782 0.753 64.818 1.00 32.99 C ANISOU 2999 CA LYS B 391 5653 3230 3653 67 619 -376 C ATOM 3000 C LYS A 391 21.222 2.083 65.454 1.00 33.39 C ANISOU 3000 C LYS B 391 5752 3232 3705 26 693 -398 C ATOM 3001 O LYS A 391 22.379 2.518 65.339 1.00 31.96 O ANISOU 3001 O LYS B 391 5593 3006 3543 6 775 -417 O ATOM 3002 CB LYS A 391 20.121 0.988 63.455 1.00 32.74 C ANISOU 3002 CB LYS B 391 5498 3265 3677 41 583 -392 C ATOM 3003 CG LYS A 391 20.212 -0.229 62.527 1.00 32.25 C ANISOU 3003 CG LYS B 391 5384 3238 3632 72 547 -380 C ATOM 3004 CD LYS A 391 19.135 -0.229 61.406 1.00 31.67 C ANISOU 3004 CD LYS B 391 5199 3238 3597 57 487 -386 C ATOM 3005 CE LYS A 391 19.102 -1.627 60.727 1.00 33.02 C ANISOU 3005 CE LYS B 391 5332 3441 3774 97 444 -369 C ATOM 3006 NZ LYS A 391 17.872 -1.823 59.898 1.00 34.23 N ANISOU 3006 NZ LYS B 391 5392 3662 3952 90 378 -368 N ATOM 3007 N LEU A 392 20.281 2.699 66.171 1.00 33.92 N ANISOU 3007 N LEU B 392 5834 3304 3749 15 664 -395 N ATOM 3008 CA LEU A 392 20.541 3.968 66.811 1.00 35.17 C ANISOU 3008 CA LEU B 392 6035 3420 3908 -22 729 -415 C ATOM 3009 C LEU A 392 21.466 3.810 68.011 1.00 37.22 C ANISOU 3009 C LEU B 392 6422 3604 4118 -4 790 -405 C ATOM 3010 O LEU A 392 22.304 4.675 68.249 1.00 37.39 O ANISOU 3010 O LEU B 392 6476 3576 4155 -35 877 -427 O ATOM 3011 CB LEU A 392 19.237 4.652 67.190 1.00 34.34 C ANISOU 3011 CB LEU B 392 5911 3343 3795 -38 683 -416 C ATOM 3012 CG LEU A 392 18.401 5.151 65.995 1.00 33.11 C ANISOU 3012 CG LEU B 392 5635 3251 3694 -65 646 -431 C ATOM 3013 CD1 LEU A 392 17.047 5.639 66.532 1.00 31.00 C ANISOU 3013 CD1 LEU B 392 5367 3004 3409 -75 597 -427 C ATOM 3014 CD2 LEU A 392 19.092 6.269 65.224 1.00 28.41 C ANISOU 3014 CD2 LEU B 392 4988 2650 3157 -106 714 -465 C ATOM 3015 N LYS A 393 21.320 2.709 68.742 1.00 39.41 N ANISOU 3015 N LYS B 393 6768 3872 4335 47 746 -372 N ATOM 3016 CA LYS A 393 22.203 2.406 69.874 1.00 42.86 C ANISOU 3016 CA LYS B 393 7335 4235 4715 74 799 -356 C ATOM 3017 C LYS A 393 23.623 2.072 69.415 1.00 42.86 C ANISOU 3017 C LYS B 393 7354 4192 4738 77 876 -362 C ATOM 3018 O LYS A 393 24.564 2.342 70.153 1.00 43.97 O ANISOU 3018 O LYS B 393 7590 4260 4856 73 959 -365 O ATOM 3019 CB LYS A 393 21.666 1.252 70.736 1.00 43.09 C ANISOU 3019 CB LYS B 393 7432 4270 4671 135 724 -318 C ATOM 3020 CG LYS A 393 20.335 1.541 71.443 1.00 46.35 C ANISOU 3020 CG LYS B 393 7849 4714 5049 133 654 -314 C ATOM 3021 CD LYS A 393 19.920 0.402 72.410 1.00 47.32 C ANISOU 3021 CD LYS B 393 8047 4839 5092 196 582 -280 C ATOM 3022 CE LYS A 393 19.502 -0.894 71.653 1.00 51.94 C ANISOU 3022 CE LYS B 393 8558 5487 5689 238 497 -264 C ATOM 3023 NZ LYS A 393 17.994 -1.005 71.469 1.00 53.16 N ANISOU 3023 NZ LYS B 393 8634 5716 5850 230 398 -268 N ATOM 3024 N ALA A 394 23.774 1.522 68.204 1.00 42.45 N ANISOU 3024 N ALA B 394 7215 4181 4732 80 855 -368 N ATOM 3025 CA ALA A 394 25.073 1.051 67.689 1.00 42.71 C ANISOU 3025 CA ALA B 394 7263 4178 4786 85 920 -374 C ATOM 3026 C ALA A 394 25.903 2.097 66.935 1.00 42.46 C ANISOU 3026 C ALA B 394 7180 4131 4820 24 1005 -419 C ATOM 3027 O ALA A 394 26.853 1.750 66.230 1.00 44.03 O ANISOU 3027 O ALA B 394 7364 4316 5050 19 1050 -432 O ATOM 3028 CB ALA A 394 24.881 -0.217 66.801 1.00 42.10 C ANISOU 3028 CB ALA B 394 7126 4150 4720 125 855 -356 C ATOM 3029 N ARG A 395 25.554 3.366 67.070 1.00 42.26 N ANISOU 3029 N ARG B 395 7128 4110 4817 -22 1026 -444 N ATOM 3030 CA ARG A 395 26.260 4.457 66.386 1.00 41.83 C ANISOU 3030 CA ARG B 395 7017 4049 4827 -80 1100 -491 C ATOM 3031 C ARG A 395 27.616 4.801 67.032 1.00 42.01 C ANISOU 3031 C ARG B 395 7130 3986 4846 -99 1216 -508 C ATOM 3032 O ARG A 395 27.869 4.439 68.170 1.00 42.76 O ANISOU 3032 O ARG B 395 7340 4023 4883 -72 1242 -483 O ATOM 3033 CB ARG A 395 25.385 5.710 66.373 1.00 41.16 C ANISOU 3033 CB ARG B 395 6875 3998 4767 -116 1084 -510 C ATOM 3034 CG ARG A 395 24.144 5.597 65.493 1.00 41.25 C ANISOU 3034 CG ARG B 395 6782 4093 4799 -111 987 -503 C ATOM 3035 CD ARG A 395 23.367 6.901 65.556 1.00 40.06 C ANISOU 3035 CD ARG B 395 6587 3964 4670 -146 982 -522 C ATOM 3036 NE ARG A 395 22.662 7.076 66.829 1.00 40.63 N ANISOU 3036 NE ARG B 395 6737 4010 4689 -133 966 -501 N ATOM 3037 CZ ARG A 395 21.965 8.167 67.149 1.00 40.94 C ANISOU 3037 CZ ARG B 395 6762 4056 4737 -159 967 -514 C ATOM 3038 NH1 ARG A 395 21.894 9.192 66.307 1.00 38.95 N ANISOU 3038 NH1 ARG B 395 6421 3835 4545 -194 985 -545 N ATOM 3039 NH2 ARG A 395 21.340 8.241 68.319 1.00 41.65 N ANISOU 3039 NH2 ARG B 395 6930 4122 4774 -147 951 -495 N ATOM 3040 N HIS A 396 28.458 5.532 66.304 1.00 41.55 N ANISOU 3040 N HIS B 396 7018 3922 4849 -148 1286 -554 N ATOM 3041 CA HIS A 396 29.774 5.935 66.790 1.00 42.52 C ANISOU 3041 CA HIS B 396 7211 3964 4979 -176 1403 -579 C ATOM 3042 C HIS A 396 29.956 7.392 66.500 1.00 41.68 C ANISOU 3042 C HIS B 396 7039 3865 4931 -238 1456 -630 C ATOM 3043 O HIS A 396 29.953 7.803 65.346 1.00 41.13 O ANISOU 3043 O HIS B 396 6857 3849 4919 -266 1440 -663 O ATOM 3044 CB HIS A 396 30.888 5.128 66.106 1.00 42.91 C ANISOU 3044 CB HIS B 396 7263 3992 5048 -173 1446 -589 C ATOM 3045 CG HIS A 396 30.807 3.660 66.375 1.00 46.27 C ANISOU 3045 CG HIS B 396 7755 4407 5419 -107 1400 -539 C ATOM 3046 ND1 HIS A 396 31.017 3.122 67.630 1.00 49.56 N ANISOU 3046 ND1 HIS B 396 8305 4758 5767 -67 1423 -502 N ATOM 3047 CD2 HIS A 396 30.527 2.618 65.559 1.00 48.13 C ANISOU 3047 CD2 HIS B 396 7941 4689 5657 -72 1332 -520 C ATOM 3048 CE1 HIS A 396 30.861 1.811 67.574 1.00 50.99 C ANISOU 3048 CE1 HIS B 396 8512 4949 5911 -7 1367 -462 C ATOM 3049 NE2 HIS A 396 30.575 1.479 66.326 1.00 50.57 N ANISOU 3049 NE2 HIS B 396 8349 4963 5903 -10 1314 -473 N ATOM 3050 N GLU A 397 30.127 8.159 67.560 1.00 41.13 N ANISOU 3050 N GLU B 397 7042 3742 4845 -256 1519 -637 N ATOM 3051 CA GLU A 397 30.149 9.606 67.495 1.00 41.52 C ANISOU 3051 CA GLU B 397 7036 3795 4944 -308 1565 -681 C ATOM 3052 C GLU A 397 31.541 10.110 67.128 1.00 41.04 C ANISOU 3052 C GLU B 397 6961 3695 4939 -358 1674 -734 C ATOM 3053 O GLU A 397 32.544 9.621 67.669 1.00 40.96 O ANISOU 3053 O GLU B 397 7044 3611 4907 -356 1751 -732 O ATOM 3054 CB GLU A 397 29.703 10.179 68.849 1.00 40.80 C ANISOU 3054 CB GLU B 397 7034 3660 4809 -305 1589 -665 C ATOM 3055 CG GLU A 397 29.493 11.680 68.879 1.00 43.13 C ANISOU 3055 CG GLU B 397 7273 3965 5151 -352 1626 -705 C ATOM 3056 CD GLU A 397 29.158 12.212 70.279 1.00 44.92 C ANISOU 3056 CD GLU B 397 7600 4137 5331 -349 1661 -691 C ATOM 3057 OE1 GLU A 397 29.596 13.345 70.621 1.00 48.58 O ANISOU 3057 OE1 GLU B 397 8063 4567 5829 -391 1745 -728 O ATOM 3058 OE2 GLU A 397 28.459 11.498 71.043 1.00 48.25 O ANISOU 3058 OE2 GLU B 397 8100 4552 5682 -306 1605 -644 O ATOM 3059 N TYR A 398 31.587 11.089 66.221 1.00 39.87 N ANISOU 3059 N TYR B 398 6696 3595 4860 -401 1680 -782 N ATOM 3060 CA TYR A 398 32.821 11.783 65.850 1.00 39.74 C ANISOU 3060 CA TYR B 398 6646 3549 4905 -456 1781 -844 C ATOM 3061 C TYR A 398 32.819 13.142 66.528 1.00 39.79 C ANISOU 3061 C TYR B 398 6654 3531 4935 -493 1843 -874 C ATOM 3062 O TYR A 398 31.772 13.775 66.634 1.00 39.15 O ANISOU 3062 O TYR B 398 6533 3490 4852 -485 1788 -864 O ATOM 3063 CB TYR A 398 32.895 12.020 64.336 1.00 38.79 C ANISOU 3063 CB TYR B 398 6386 3506 4848 -479 1742 -883 C ATOM 3064 CG TYR A 398 33.553 10.937 63.509 1.00 38.57 C ANISOU 3064 CG TYR B 398 6347 3483 4822 -470 1736 -883 C ATOM 3065 CD1 TYR A 398 34.358 11.277 62.422 1.00 38.35 C ANISOU 3065 CD1 TYR B 398 6231 3482 4858 -512 1768 -941 C ATOM 3066 CD2 TYR A 398 33.381 9.590 63.806 1.00 39.09 C ANISOU 3066 CD2 TYR B 398 6492 3530 4831 -418 1698 -829 C ATOM 3067 CE1 TYR A 398 34.977 10.310 61.644 1.00 38.01 C ANISOU 3067 CE1 TYR B 398 6180 3443 4819 -506 1766 -945 C ATOM 3068 CE2 TYR A 398 34.008 8.603 63.045 1.00 40.97 C ANISOU 3068 CE2 TYR B 398 6722 3770 5074 -408 1697 -831 C ATOM 3069 CZ TYR A 398 34.795 8.975 61.963 1.00 38.99 C ANISOU 3069 CZ TYR B 398 6385 3543 4886 -453 1732 -889 C ATOM 3070 OH TYR A 398 35.397 8.023 61.203 1.00 40.14 O ANISOU 3070 OH TYR B 398 6524 3690 5037 -445 1733 -892 O ATOM 3071 N ALA A 399 33.984 13.620 66.957 1.00 39.68 N ANISOU 3071 N ALA B 399 6681 3448 4947 -535 1961 -915 N ATOM 3072 CA ALA A 399 34.058 15.016 67.400 1.00 40.16 C ANISOU 3072 CA ALA B 399 6718 3494 5047 -577 2025 -955 C ATOM 3073 C ALA A 399 33.879 15.910 66.174 1.00 39.24 C ANISOU 3073 C ALA B 399 6444 3461 5006 -606 1990 -1004 C ATOM 3074 O ALA A 399 34.253 15.526 65.059 1.00 38.84 O ANISOU 3074 O ALA B 399 6317 3453 4986 -614 1963 -1025 O ATOM 3075 CB ALA A 399 35.401 15.299 68.110 1.00 40.58 C ANISOU 3075 CB ALA B 399 6850 3454 5116 -619 2168 -992 C ATOM 3076 N PRO A 400 33.304 17.104 66.352 1.00 39.62 N ANISOU 3076 N PRO B 400 6440 3532 5081 -621 1988 -1023 N ATOM 3077 CA PRO A 400 33.105 17.940 65.149 1.00 39.56 C ANISOU 3077 CA PRO B 400 6281 3608 5141 -640 1947 -1066 C ATOM 3078 C PRO A 400 34.358 18.102 64.298 1.00 40.14 C ANISOU 3078 C PRO B 400 6286 3686 5278 -686 2006 -1131 C ATOM 3079 O PRO A 400 34.260 18.177 63.071 1.00 39.12 O ANISOU 3079 O PRO B 400 6046 3632 5184 -689 1948 -1154 O ATOM 3080 CB PRO A 400 32.648 19.281 65.725 1.00 39.42 C ANISOU 3080 CB PRO B 400 6242 3588 5149 -655 1976 -1085 C ATOM 3081 CG PRO A 400 31.964 18.904 67.000 1.00 38.96 C ANISOU 3081 CG PRO B 400 6309 3477 5017 -623 1970 -1028 C ATOM 3082 CD PRO A 400 32.744 17.746 67.561 1.00 40.04 C ANISOU 3082 CD PRO B 400 6564 3545 5106 -615 2015 -1004 C ATOM 3083 N GLU A 401 35.517 18.136 64.964 1.00 40.89 N ANISOU 3083 N GLU B 401 6452 3701 5384 -723 2123 -1161 N ATOM 3084 CA GLU A 401 36.818 18.137 64.311 1.00 41.65 C ANISOU 3084 CA GLU B 401 6506 3787 5534 -771 2193 -1223 C ATOM 3085 C GLU A 401 37.019 17.050 63.288 1.00 39.94 C ANISOU 3085 C GLU B 401 6261 3606 5308 -755 2137 -1213 C ATOM 3086 O GLU A 401 37.313 17.336 62.140 1.00 39.15 O ANISOU 3086 O GLU B 401 6050 3567 5260 -779 2114 -1260 O ATOM 3087 CB GLU A 401 37.939 18.007 65.338 1.00 43.22 C ANISOU 3087 CB GLU B 401 6820 3877 5725 -803 2327 -1238 C ATOM 3088 CG GLU A 401 39.004 18.997 65.080 1.00 49.20 C ANISOU 3088 CG GLU B 401 7508 4622 6563 -872 2425 -1324 C ATOM 3089 CD GLU A 401 38.396 20.348 64.749 1.00 54.16 C ANISOU 3089 CD GLU B 401 8016 5318 7244 -883 2392 -1358 C ATOM 3090 OE1 GLU A 401 38.227 21.163 65.690 1.00 55.05 O ANISOU 3090 OE1 GLU B 401 8164 5392 7360 -893 2447 -1362 O ATOM 3091 OE2 GLU A 401 38.051 20.561 63.552 1.00 57.33 O ANISOU 3091 OE2 GLU B 401 8293 5812 7679 -878 2309 -1379 O ATOM 3092 N LYS A 402 36.891 15.814 63.750 1.00 38.86 N ANISOU 3092 N LYS B 402 6232 3429 5105 -715 2118 -1154 N ATOM 3093 CA LYS A 402 37.125 14.626 62.969 1.00 38.83 C ANISOU 3093 CA LYS B 402 6227 3443 5084 -694 2076 -1137 C ATOM 3094 C LYS A 402 36.058 14.516 61.862 1.00 37.51 C ANISOU 3094 C LYS B 402 5953 3380 4920 -662 1946 -1119 C ATOM 3095 O LYS A 402 36.339 14.028 60.762 1.00 37.73 O ANISOU 3095 O LYS B 402 5918 3451 4966 -665 1913 -1136 O ATOM 3096 CB LYS A 402 37.077 13.424 63.917 1.00 39.26 C ANISOU 3096 CB LYS B 402 6427 3429 5062 -648 2083 -1071 C ATOM 3097 CG LYS A 402 37.629 12.129 63.337 1.00 41.18 C ANISOU 3097 CG LYS B 402 6697 3663 5288 -630 2073 -1057 C ATOM 3098 CD LYS A 402 38.207 11.219 64.443 1.00 46.72 C ANISOU 3098 CD LYS B 402 7557 4263 5931 -605 2141 -1017 C ATOM 3099 CE LYS A 402 39.195 11.996 65.373 1.00 50.09 C ANISOU 3099 CE LYS B 402 8054 4601 6378 -655 2280 -1056 C ATOM 3100 NZ LYS A 402 40.324 11.163 65.941 1.00 53.18 N ANISOU 3100 NZ LYS B 402 8572 4892 6741 -655 2380 -1048 N ATOM 3101 N PHE A 403 34.841 14.952 62.180 1.00 35.67 N ANISOU 3101 N PHE B 403 5706 3182 4665 -633 1878 -1084 N ATOM 3102 CA PHE A 403 33.775 15.124 61.219 1.00 34.62 C ANISOU 3102 CA PHE B 403 5470 3143 4540 -609 1768 -1072 C ATOM 3103 C PHE A 403 34.148 16.087 60.073 1.00 35.27 C ANISOU 3103 C PHE B 403 5418 3288 4694 -647 1769 -1139 C ATOM 3104 O PHE A 403 34.033 15.709 58.910 1.00 35.10 O ANISOU 3104 O PHE B 403 5322 3329 4684 -639 1707 -1146 O ATOM 3105 CB PHE A 403 32.493 15.579 61.936 1.00 34.40 C ANISOU 3105 CB PHE B 403 5463 3127 4480 -578 1717 -1029 C ATOM 3106 CG PHE A 403 31.441 16.118 61.014 1.00 33.37 C ANISOU 3106 CG PHE B 403 5222 3086 4370 -563 1624 -1027 C ATOM 3107 CD1 PHE A 403 30.838 15.293 60.084 1.00 32.09 C ANISOU 3107 CD1 PHE B 403 5018 2983 4191 -531 1533 -998 C ATOM 3108 CD2 PHE A 403 31.079 17.449 61.061 1.00 35.17 C ANISOU 3108 CD2 PHE B 403 5389 3338 4635 -579 1632 -1054 C ATOM 3109 CE1 PHE A 403 29.860 15.785 59.207 1.00 33.59 C ANISOU 3109 CE1 PHE B 403 5112 3253 4397 -516 1451 -995 C ATOM 3110 CE2 PHE A 403 30.106 17.960 60.208 1.00 36.26 C ANISOU 3110 CE2 PHE B 403 5431 3556 4789 -561 1548 -1050 C ATOM 3111 CZ PHE A 403 29.501 17.119 59.257 1.00 35.30 C ANISOU 3111 CZ PHE B 403 5272 3492 4647 -530 1458 -1020 C ATOM 3112 N VAL A 404 34.592 17.310 60.390 1.00 35.98 N ANISOU 3112 N VAL B 404 5475 3364 4832 -688 1837 -1190 N ATOM 3113 CA VAL A 404 35.035 18.289 59.363 1.00 36.68 C ANISOU 3113 CA VAL B 404 5433 3513 4992 -725 1842 -1261 C ATOM 3114 C VAL A 404 36.200 17.765 58.485 1.00 37.36 C ANISOU 3114 C VAL B 404 5486 3602 5106 -758 1875 -1309 C ATOM 3115 O VAL A 404 36.179 17.939 57.259 1.00 37.04 O ANISOU 3115 O VAL B 404 5341 3638 5095 -763 1821 -1340 O ATOM 3116 CB VAL A 404 35.328 19.680 60.000 1.00 37.22 C ANISOU 3116 CB VAL B 404 5478 3559 5107 -761 1917 -1308 C ATOM 3117 CG1 VAL A 404 35.956 20.662 59.014 1.00 37.56 C ANISOU 3117 CG1 VAL B 404 5387 3659 5225 -802 1932 -1388 C ATOM 3118 CG2 VAL A 404 34.008 20.276 60.491 1.00 38.58 C ANISOU 3118 CG2 VAL B 404 5650 3752 5256 -724 1861 -1264 C ATOM 3119 N GLU A 405 37.173 17.080 59.093 1.00 38.04 N ANISOU 3119 N GLU B 405 5667 3607 5179 -779 1961 -1313 N ATOM 3120 CA GLU A 405 38.259 16.425 58.312 1.00 39.86 C ANISOU 3120 CA GLU B 405 5883 3831 5431 -808 1995 -1353 C ATOM 3121 C GLU A 405 37.717 15.386 57.352 1.00 38.70 C ANISOU 3121 C GLU B 405 5714 3740 5252 -766 1897 -1315 C ATOM 3122 O GLU A 405 38.147 15.317 56.189 1.00 38.96 O ANISOU 3122 O GLU B 405 5665 3824 5316 -786 1877 -1357 O ATOM 3123 CB GLU A 405 39.275 15.736 59.212 1.00 40.48 C ANISOU 3123 CB GLU B 405 6086 3804 5490 -827 2102 -1350 C ATOM 3124 CG GLU A 405 40.000 16.667 60.161 1.00 45.72 C ANISOU 3124 CG GLU B 405 6783 4401 6188 -875 2218 -1393 C ATOM 3125 CD GLU A 405 41.063 15.930 60.972 1.00 53.02 C ANISOU 3125 CD GLU B 405 7837 5217 7092 -893 2329 -1390 C ATOM 3126 OE1 GLU A 405 41.823 15.122 60.380 1.00 55.28 O ANISOU 3126 OE1 GLU B 405 8133 5489 7381 -906 2350 -1407 O ATOM 3127 OE2 GLU A 405 41.128 16.152 62.204 1.00 57.81 O ANISOU 3127 OE2 GLU B 405 8540 5749 7676 -894 2398 -1370 O ATOM 3128 N THR A 406 36.796 14.560 57.845 1.00 38.16 N ANISOU 3128 N THR B 406 5717 3660 5120 -711 1838 -1237 N ATOM 3129 CA THR A 406 36.119 13.562 56.997 1.00 37.74 C ANISOU 3129 CA THR B 406 5642 3661 5035 -667 1741 -1195 C ATOM 3130 C THR A 406 35.373 14.185 55.814 1.00 37.20 C ANISOU 3130 C THR B 406 5446 3695 4993 -660 1652 -1211 C ATOM 3131 O THR A 406 35.361 13.621 54.745 1.00 38.09 O ANISOU 3131 O THR B 406 5510 3855 5106 -651 1603 -1215 O ATOM 3132 CB THR A 406 35.167 12.689 57.807 1.00 37.24 C ANISOU 3132 CB THR B 406 5671 3574 4905 -609 1691 -1112 C ATOM 3133 OG1 THR A 406 35.904 12.093 58.879 1.00 39.23 O ANISOU 3133 OG1 THR B 406 6047 3731 5129 -610 1773 -1096 O ATOM 3134 CG2 THR A 406 34.552 11.574 56.925 1.00 36.11 C ANISOU 3134 CG2 THR B 406 5505 3482 4733 -566 1599 -1072 C ATOM 3135 N MET A 407 34.741 15.337 56.017 1.00 37.52 N ANISOU 3135 N MET B 407 5437 3766 5052 -662 1634 -1219 N ATOM 3136 CA MET A 407 33.998 16.025 54.952 1.00 36.12 C ANISOU 3136 CA MET B 407 5144 3683 4898 -651 1552 -1232 C ATOM 3137 C MET A 407 34.914 16.623 53.896 1.00 36.50 C ANISOU 3137 C MET B 407 5092 3773 5001 -694 1574 -1311 C ATOM 3138 O MET A 407 34.553 16.669 52.721 1.00 35.64 O ANISOU 3138 O MET B 407 4900 3742 4900 -681 1503 -1320 O ATOM 3139 CB MET A 407 33.098 17.116 55.527 1.00 36.73 C ANISOU 3139 CB MET B 407 5203 3774 4980 -639 1533 -1219 C ATOM 3140 CG MET A 407 31.906 16.610 56.349 1.00 35.88 C ANISOU 3140 CG MET B 407 5172 3646 4815 -592 1485 -1141 C ATOM 3141 SD MET A 407 30.889 15.473 55.389 1.00 38.53 S ANISOU 3141 SD MET B 407 5488 4043 5109 -542 1371 -1086 S ATOM 3142 CE MET A 407 31.244 13.872 56.105 1.00 35.75 C ANISOU 3142 CE MET B 407 5258 3621 4705 -523 1393 -1040 C ATOM 3143 N LYS A 408 36.093 17.091 54.331 1.00 37.08 N ANISOU 3143 N LYS B 408 5177 3798 5116 -746 1674 -1369 N ATOM 3144 CA LYS A 408 37.150 17.552 53.433 1.00 38.35 C ANISOU 3144 CA LYS B 408 5251 3989 5331 -795 1709 -1453 C ATOM 3145 C LYS A 408 37.648 16.397 52.578 1.00 37.73 C ANISOU 3145 C LYS B 408 5181 3918 5237 -796 1694 -1455 C ATOM 3146 O LYS A 408 37.819 16.554 51.374 1.00 38.53 O ANISOU 3146 O LYS B 408 5191 4088 5360 -806 1652 -1496 O ATOM 3147 CB LYS A 408 38.318 18.177 54.212 1.00 38.92 C ANISOU 3147 CB LYS B 408 5346 3993 5447 -854 1831 -1513 C ATOM 3148 CG LYS A 408 37.948 19.465 54.987 1.00 39.78 C ANISOU 3148 CG LYS B 408 5433 4098 5582 -860 1856 -1523 C ATOM 3149 CD LYS A 408 39.130 19.977 55.821 1.00 42.44 C ANISOU 3149 CD LYS B 408 5805 4360 5962 -920 1986 -1581 C ATOM 3150 CE LYS A 408 38.980 21.451 56.124 1.00 46.75 C ANISOU 3150 CE LYS B 408 6279 4927 6557 -938 2009 -1621 C ATOM 3151 NZ LYS A 408 39.594 21.807 57.446 1.00 51.45 N ANISOU 3151 NZ LYS B 408 6956 5427 7166 -973 2128 -1635 N ATOM 3152 N LEU A 409 37.892 15.250 53.213 1.00 37.40 N ANISOU 3152 N LEU B 409 5250 3805 5156 -783 1729 -1413 N ATOM 3153 CA LEU A 409 38.252 14.023 52.528 1.00 37.94 C ANISOU 3153 CA LEU B 409 5342 3871 5202 -774 1714 -1402 C ATOM 3154 C LEU A 409 37.201 13.664 51.460 1.00 37.38 C ANISOU 3154 C LEU B 409 5209 3887 5107 -728 1597 -1367 C ATOM 3155 O LEU A 409 37.527 13.412 50.293 1.00 37.64 O ANISOU 3155 O LEU B 409 5180 3968 5152 -739 1570 -1400 O ATOM 3156 CB LEU A 409 38.390 12.903 53.570 1.00 37.53 C ANISOU 3156 CB LEU B 409 5426 3730 5103 -750 1757 -1345 C ATOM 3157 CG LEU A 409 38.756 11.477 53.150 1.00 37.86 C ANISOU 3157 CG LEU B 409 5520 3750 5116 -731 1754 -1321 C ATOM 3158 CD1 LEU A 409 39.964 11.484 52.264 1.00 35.86 C ANISOU 3158 CD1 LEU B 409 5220 3500 4905 -783 1806 -1397 C ATOM 3159 CD2 LEU A 409 39.046 10.654 54.383 1.00 38.94 C ANISOU 3159 CD2 LEU B 409 5793 3789 5213 -711 1815 -1274 C ATOM 3160 N MET A 410 35.935 13.655 51.857 1.00 37.36 N ANISOU 3160 N MET B 410 5224 3903 5070 -680 1529 -1302 N ATOM 3161 CA MET A 410 34.851 13.327 50.924 1.00 36.67 C ANISOU 3161 CA MET B 410 5083 3891 4958 -637 1423 -1265 C ATOM 3162 C MET A 410 34.835 14.313 49.763 1.00 36.98 C ANISOU 3162 C MET B 410 5001 4015 5035 -654 1384 -1319 C ATOM 3163 O MET A 410 34.676 13.923 48.624 1.00 36.06 O ANISOU 3163 O MET B 410 4834 3955 4912 -642 1329 -1323 O ATOM 3164 CB MET A 410 33.512 13.292 51.660 1.00 37.10 C ANISOU 3164 CB MET B 410 5177 3946 4974 -589 1368 -1193 C ATOM 3165 CG MET A 410 33.409 12.155 52.699 1.00 36.65 C ANISOU 3165 CG MET B 410 5238 3817 4870 -562 1387 -1134 C ATOM 3166 SD MET A 410 34.070 10.625 51.995 1.00 37.98 S ANISOU 3166 SD MET B 410 5438 3973 5021 -553 1390 -1127 S ATOM 3167 CE MET A 410 32.625 9.955 51.160 1.00 37.09 C ANISOU 3167 CE MET B 410 5283 3935 4874 -498 1269 -1070 C ATOM 3168 N GLU A 411 35.074 15.585 50.052 1.00 38.36 N ANISOU 3168 N GLU B 411 5130 4197 5249 -682 1417 -1364 N ATOM 3169 CA GLU A 411 35.148 16.607 49.022 1.00 40.48 C ANISOU 3169 CA GLU B 411 5280 4544 5556 -697 1384 -1421 C ATOM 3170 C GLU A 411 36.244 16.273 48.000 1.00 41.24 C ANISOU 3170 C GLU B 411 5332 4661 5674 -735 1404 -1484 C ATOM 3171 O GLU A 411 36.020 16.421 46.790 1.00 40.98 O ANISOU 3171 O GLU B 411 5220 4706 5642 -724 1339 -1504 O ATOM 3172 CB GLU A 411 35.355 17.969 49.676 1.00 41.05 C ANISOU 3172 CB GLU B 411 5319 4608 5671 -723 1430 -1460 C ATOM 3173 CG GLU A 411 35.265 19.179 48.757 1.00 44.09 C ANISOU 3173 CG GLU B 411 5579 5077 6094 -728 1388 -1513 C ATOM 3174 CD GLU A 411 35.283 20.492 49.543 1.00 44.69 C ANISOU 3174 CD GLU B 411 5628 5141 6210 -744 1431 -1541 C ATOM 3175 OE1 GLU A 411 36.287 20.790 50.234 1.00 50.55 O ANISOU 3175 OE1 GLU B 411 6391 5827 6987 -793 1525 -1588 O ATOM 3176 OE2 GLU A 411 34.293 21.238 49.469 1.00 49.11 O ANISOU 3176 OE2 GLU B 411 6148 5745 6767 -708 1374 -1516 O ATOM 3177 N HIS A 412 37.385 15.769 48.489 1.00 41.27 N ANISOU 3177 N HIS B 412 5395 4594 5690 -775 1494 -1513 N ATOM 3178 CA HIS A 412 38.513 15.336 47.636 1.00 42.19 C ANISOU 3178 CA HIS B 412 5486 4716 5828 -816 1527 -1575 C ATOM 3179 C HIS A 412 38.214 14.132 46.735 1.00 42.50 C ANISOU 3179 C HIS B 412 5539 4782 5827 -784 1469 -1540 C ATOM 3180 O HIS A 412 38.664 14.093 45.582 1.00 42.38 O ANISOU 3180 O HIS B 412 5460 4818 5825 -803 1449 -1589 O ATOM 3181 CB HIS A 412 39.747 15.018 48.481 1.00 41.95 C ANISOU 3181 CB HIS B 412 5532 4591 5817 -864 1645 -1607 C ATOM 3182 CG HIS A 412 40.536 16.226 48.880 1.00 42.34 C ANISOU 3182 CG HIS B 412 5536 4627 5925 -920 1718 -1681 C ATOM 3183 ND1 HIS A 412 40.145 17.072 49.900 1.00 44.50 N ANISOU 3183 ND1 HIS B 412 5824 4876 6210 -916 1742 -1666 N ATOM 3184 CD2 HIS A 412 41.694 16.733 48.396 1.00 41.49 C ANISOU 3184 CD2 HIS B 412 5367 4527 5869 -983 1775 -1775 C ATOM 3185 CE1 HIS A 412 41.032 18.045 50.026 1.00 42.91 C ANISOU 3185 CE1 HIS B 412 5571 4668 6067 -973 1812 -1746 C ATOM 3186 NE2 HIS A 412 41.977 17.861 49.123 1.00 41.63 N ANISOU 3186 NE2 HIS B 412 5360 4527 5931 -1015 1832 -1814 N ATOM 3187 N ARG A 413 37.480 13.154 47.275 1.00 42.84 N ANISOU 3187 N ARG B 413 5664 4789 5823 -737 1445 -1459 N ATOM 3188 CA ARG A 413 37.144 11.933 46.557 1.00 43.44 C ANISOU 3188 CA ARG B 413 5762 4883 5862 -704 1396 -1420 C ATOM 3189 C ARG A 413 35.959 12.111 45.583 1.00 44.34 C ANISOU 3189 C ARG B 413 5804 5086 5955 -662 1288 -1391 C ATOM 3190 O ARG A 413 35.672 11.205 44.807 1.00 43.92 O ANISOU 3190 O ARG B 413 5753 5058 5876 -637 1245 -1367 O ATOM 3191 CB ARG A 413 36.874 10.766 47.531 1.00 42.83 C ANISOU 3191 CB ARG B 413 5798 4731 5743 -669 1414 -1347 C ATOM 3192 CG ARG A 413 37.791 10.669 48.772 1.00 43.61 C ANISOU 3192 CG ARG B 413 5986 4731 5851 -697 1517 -1357 C ATOM 3193 CD ARG A 413 38.965 9.621 48.703 1.00 43.33 C ANISOU 3193 CD ARG B 413 6014 4633 5815 -718 1590 -1376 C ATOM 3194 NE ARG A 413 40.092 10.120 47.945 1.00 40.83 N ANISOU 3194 NE ARG B 413 5638 4332 5545 -779 1640 -1465 N ATOM 3195 CZ ARG A 413 41.355 9.663 47.949 1.00 41.76 C ANISOU 3195 CZ ARG B 413 5797 4390 5680 -820 1729 -1510 C ATOM 3196 NH1 ARG A 413 41.790 8.640 48.713 1.00 37.17 N ANISOU 3196 NH1 ARG B 413 5329 3720 5074 -806 1789 -1473 N ATOM 3197 NH2 ARG A 413 42.210 10.273 47.137 1.00 37.49 N ANISOU 3197 NH2 ARG B 413 5180 3881 5184 -877 1757 -1596 N ATOM 3198 N TYR A 414 35.273 13.263 45.624 1.00 46.58 N ANISOU 3198 N TYR B 414 6031 5416 6252 -653 1249 -1393 N ATOM 3199 CA TYR A 414 34.068 13.494 44.779 1.00 47.45 C ANISOU 3199 CA TYR B 414 6082 5605 6340 -610 1151 -1361 C ATOM 3200 C TYR A 414 34.406 13.643 43.296 1.00 48.03 C ANISOU 3200 C TYR B 414 6074 5753 6423 -621 1114 -1411 C ATOM 3201 O TYR A 414 35.123 14.563 42.904 1.00 48.54 O ANISOU 3201 O TYR B 414 6071 5848 6525 -657 1133 -1483 O ATOM 3202 CB TYR A 414 33.228 14.698 45.263 1.00 48.19 C ANISOU 3202 CB TYR B 414 6143 5723 6444 -594 1124 -1347 C ATOM 3203 CG TYR A 414 31.992 15.003 44.406 1.00 47.88 C ANISOU 3203 CG TYR B 414 6049 5761 6384 -549 1029 -1313 C ATOM 3204 CD1 TYR A 414 30.798 14.302 44.594 1.00 49.46 C ANISOU 3204 CD1 TYR B 414 6294 5958 6543 -503 978 -1236 C ATOM 3205 CD2 TYR A 414 32.020 16.003 43.415 1.00 50.89 C ANISOU 3205 CD2 TYR B 414 6334 6216 6784 -552 992 -1360 C ATOM 3206 CE1 TYR A 414 29.662 14.571 43.821 1.00 50.70 C ANISOU 3206 CE1 TYR B 414 6406 6179 6680 -464 900 -1205 C ATOM 3207 CE2 TYR A 414 30.890 16.280 42.622 1.00 50.58 C ANISOU 3207 CE2 TYR B 414 6252 6244 6722 -507 909 -1326 C ATOM 3208 CZ TYR A 414 29.713 15.561 42.834 1.00 51.22 C ANISOU 3208 CZ TYR B 414 6384 6315 6764 -465 867 -1249 C ATOM 3209 OH TYR A 414 28.577 15.820 42.069 1.00 50.83 O ANISOU 3209 OH TYR B 414 6298 6324 6690 -423 792 -1214 O ATOM 3210 N GLY A 415 33.874 12.730 42.484 1.00 48.65 N ANISOU 3210 N GLY B 415 6157 5861 6467 -589 1060 -1376 N ATOM 3211 CA GLY A 415 34.176 12.677 41.053 1.00 49.36 C ANISOU 3211 CA GLY B 415 6183 6017 6556 -596 1025 -1418 C ATOM 3212 C GLY A 415 35.632 12.393 40.708 1.00 50.71 C ANISOU 3212 C GLY B 415 6350 6166 6751 -649 1089 -1490 C ATOM 3213 O GLY A 415 36.097 12.769 39.625 1.00 51.68 O ANISOU 3213 O GLY B 415 6404 6347 6884 -669 1070 -1550 O ATOM 3214 N ALA A 416 36.348 11.727 41.620 1.00 50.75 N ANISOU 3214 N ALA B 416 6432 6087 6763 -671 1166 -1487 N ATOM 3215 CA ALA A 416 37.777 11.467 41.469 1.00 51.12 C ANISOU 3215 CA ALA B 416 6488 6098 6837 -726 1242 -1555 C ATOM 3216 C ALA A 416 38.016 10.006 41.134 1.00 50.84 C ANISOU 3216 C ALA B 416 6514 6030 6774 -713 1255 -1529 C ATOM 3217 O ALA A 416 37.208 9.149 41.497 1.00 50.50 O ANISOU 3217 O ALA B 416 6527 5965 6696 -666 1227 -1453 O ATOM 3218 CB ALA A 416 38.516 11.836 42.748 1.00 51.51 C ANISOU 3218 CB ALA B 416 6585 6069 6917 -762 1333 -1575 C ATOM 3219 N LYS A 417 39.121 9.722 40.445 1.00 50.57 N ANISOU 3219 N LYS B 417 6466 5992 6756 -756 1297 -1594 N ATOM 3220 CA LYS A 417 39.507 8.343 40.118 1.00 50.00 C ANISOU 3220 CA LYS B 417 6453 5881 6662 -748 1321 -1578 C ATOM 3221 C LYS A 417 40.839 7.941 40.758 1.00 50.16 C ANISOU 3221 C LYS B 417 6538 5814 6708 -795 1430 -1617 C ATOM 3222 O LYS A 417 41.530 8.758 41.385 1.00 49.00 O ANISOU 3222 O LYS B 417 6384 5636 6596 -840 1490 -1665 O ATOM 3223 CB LYS A 417 39.583 8.127 38.594 1.00 50.68 C ANISOU 3223 CB LYS B 417 6480 6039 6738 -751 1274 -1614 C ATOM 3224 CG LYS A 417 40.254 9.266 37.826 1.00 52.47 C ANISOU 3224 CG LYS B 417 6615 6327 6997 -801 1271 -1708 C ATOM 3225 CD LYS A 417 40.968 8.815 36.582 1.00 54.20 C ANISOU 3225 CD LYS B 417 6806 6576 7211 -828 1273 -1765 C ATOM 3226 CE LYS A 417 41.417 10.021 35.748 1.00 56.06 C ANISOU 3226 CE LYS B 417 6939 6890 7472 -868 1248 -1854 C ATOM 3227 NZ LYS A 417 42.285 10.983 36.518 1.00 58.22 N ANISOU 3227 NZ LYS B 417 7189 7133 7797 -923 1315 -1918 N ATOM 3228 N GLU A 418 41.183 6.665 40.592 1.00 49.78 N ANISOU 3228 N GLU B 418 6553 5721 6639 -783 1458 -1596 N ATOM 3229 CA GLU A 418 42.489 6.138 40.987 1.00 50.81 C ANISOU 3229 CA GLU B 418 6748 5767 6789 -825 1563 -1635 C ATOM 3230 C GLU A 418 42.911 6.452 42.428 1.00 49.54 C ANISOU 3230 C GLU B 418 6654 5524 6646 -841 1641 -1626 C ATOM 3231 O GLU A 418 43.866 7.196 42.667 1.00 49.98 O ANISOU 3231 O GLU B 418 6693 5554 6742 -902 1711 -1696 O ATOM 3232 CB GLU A 418 43.572 6.578 39.991 1.00 51.49 C ANISOU 3232 CB GLU B 418 6772 5884 6908 -890 1595 -1737 C ATOM 3233 CG GLU A 418 44.645 5.529 39.764 1.00 54.16 C ANISOU 3233 CG GLU B 418 7173 6157 7249 -916 1673 -1764 C ATOM 3234 CD GLU A 418 45.687 5.964 38.752 1.00 55.67 C ANISOU 3234 CD GLU B 418 7299 6381 7471 -984 1702 -1870 C ATOM 3235 OE1 GLU A 418 45.325 6.694 37.785 1.00 59.00 O ANISOU 3235 OE1 GLU B 418 7625 6899 7895 -990 1629 -1906 O ATOM 3236 OE2 GLU A 418 46.864 5.561 38.923 1.00 59.70 O ANISOU 3236 OE2 GLU B 418 7859 6820 8003 -1031 1799 -1916 O ATOM 3237 N PHE A 419 42.187 5.879 43.382 1.00 47.56 N ANISOU 3237 N PHE B 419 6476 5230 6363 -788 1628 -1542 N ATOM 3238 CA PHE A 419 42.584 5.931 44.790 1.00 46.01 C ANISOU 3238 CA PHE B 419 6365 4944 6171 -795 1706 -1523 C ATOM 3239 C PHE A 419 42.126 4.686 45.526 1.00 45.01 C ANISOU 3239 C PHE B 419 6341 4761 6001 -732 1702 -1436 C ATOM 3240 O PHE A 419 41.229 3.992 45.083 1.00 44.58 O ANISOU 3240 O PHE B 419 6278 4747 5916 -680 1626 -1383 O ATOM 3241 CB PHE A 419 42.043 7.185 45.478 1.00 45.08 C ANISOU 3241 CB PHE B 419 6212 4849 6069 -801 1687 -1522 C ATOM 3242 CG PHE A 419 40.541 7.208 45.622 1.00 43.10 C ANISOU 3242 CG PHE B 419 5945 4647 5783 -739 1588 -1447 C ATOM 3243 CD1 PHE A 419 39.927 6.618 46.729 1.00 40.88 C ANISOU 3243 CD1 PHE B 419 5751 4315 5467 -690 1584 -1369 C ATOM 3244 CD2 PHE A 419 39.744 7.838 44.654 1.00 40.89 C ANISOU 3244 CD2 PHE B 419 5565 4465 5504 -728 1499 -1456 C ATOM 3245 CE1 PHE A 419 38.539 6.633 46.863 1.00 41.95 C ANISOU 3245 CE1 PHE B 419 5871 4496 5573 -638 1494 -1304 C ATOM 3246 CE2 PHE A 419 38.360 7.859 44.774 1.00 40.64 C ANISOU 3246 CE2 PHE B 419 5523 4476 5444 -674 1413 -1388 C ATOM 3247 CZ PHE A 419 37.757 7.266 45.890 1.00 41.47 C ANISOU 3247 CZ PHE B 419 5712 4528 5517 -631 1412 -1314 C ATOM 3248 N VAL A 420 42.759 4.414 46.651 1.00 44.72 N ANISOU 3248 N VAL B 420 6400 4630 5962 -738 1787 -1423 N ATOM 3249 CA VAL A 420 42.351 3.349 47.533 1.00 44.25 C ANISOU 3249 CA VAL B 420 6442 4512 5859 -676 1786 -1340 C ATOM 3250 C VAL A 420 41.916 4.054 48.814 1.00 44.11 C ANISOU 3250 C VAL B 420 6461 4465 5833 -668 1794 -1310 C ATOM 3251 O VAL A 420 42.606 4.949 49.318 1.00 44.59 O ANISOU 3251 O VAL B 420 6525 4492 5925 -719 1865 -1358 O ATOM 3252 CB VAL A 420 43.518 2.351 47.835 1.00 45.01 C ANISOU 3252 CB VAL B 420 6638 4511 5951 -682 1885 -1346 C ATOM 3253 CG1 VAL A 420 43.063 1.215 48.751 1.00 44.38 C ANISOU 3253 CG1 VAL B 420 6663 4376 5822 -609 1876 -1258 C ATOM 3254 CG2 VAL A 420 44.125 1.781 46.528 1.00 44.76 C ANISOU 3254 CG2 VAL B 420 6568 4503 5934 -703 1892 -1392 C ATOM 3255 N THR A 421 40.752 3.674 49.326 1.00 42.69 N ANISOU 3255 N THR B 421 6306 4302 5614 -605 1722 -1233 N ATOM 3256 CA THR A 421 40.317 4.195 50.605 1.00 41.70 C ANISOU 3256 CA THR B 421 6229 4142 5473 -592 1730 -1198 C ATOM 3257 C THR A 421 41.221 3.682 51.719 1.00 42.62 C ANISOU 3257 C THR B 421 6471 4149 5575 -592 1831 -1185 C ATOM 3258 O THR A 421 41.888 2.657 51.558 1.00 42.35 O ANISOU 3258 O THR B 421 6493 4067 5530 -580 1872 -1180 O ATOM 3259 CB THR A 421 38.842 3.828 50.908 1.00 41.13 C ANISOU 3259 CB THR B 421 6159 4111 5359 -525 1629 -1120 C ATOM 3260 OG1 THR A 421 38.732 2.412 51.135 1.00 36.19 O ANISOU 3260 OG1 THR B 421 5608 3450 4694 -469 1618 -1062 O ATOM 3261 CG2 THR A 421 37.933 4.287 49.755 1.00 38.55 C ANISOU 3261 CG2 THR B 421 5715 3889 5044 -523 1534 -1129 C ATOM 3262 N SER A 422 41.226 4.420 52.827 1.00 43.04 N ANISOU 3262 N SER B 422 6566 4160 5627 -605 1871 -1181 N ATOM 3263 CA SER A 422 41.957 4.082 54.045 1.00 44.27 C ANISOU 3263 CA SER B 422 6848 4210 5763 -601 1965 -1163 C ATOM 3264 C SER A 422 41.005 3.539 55.126 1.00 44.50 C ANISOU 3264 C SER B 422 6958 4218 5732 -531 1916 -1077 C ATOM 3265 O SER A 422 40.080 4.242 55.569 1.00 44.03 O ANISOU 3265 O SER B 422 6871 4195 5663 -521 1863 -1056 O ATOM 3266 CB SER A 422 42.720 5.320 54.532 1.00 44.51 C ANISOU 3266 CB SER B 422 6873 4204 5834 -670 2056 -1226 C ATOM 3267 OG SER A 422 43.092 5.198 55.885 1.00 46.36 O ANISOU 3267 OG SER B 422 7230 4344 6042 -660 2133 -1197 O ATOM 3268 N LYS A 423 41.234 2.284 55.527 1.00 45.13 N ANISOU 3268 N LYS B 423 7135 4241 5771 -481 1933 -1028 N ATOM 3269 CA LYS A 423 40.314 1.529 56.388 1.00 45.40 C ANISOU 3269 CA LYS B 423 7240 4266 5745 -405 1872 -945 C ATOM 3270 C LYS A 423 40.665 1.668 57.846 1.00 46.86 C ANISOU 3270 C LYS B 423 7545 4362 5897 -396 1942 -921 C ATOM 3271 O LYS A 423 39.854 1.385 58.729 1.00 47.54 O ANISOU 3271 O LYS B 423 7686 4443 5934 -343 1893 -861 O ATOM 3272 CB LYS A 423 40.304 0.042 56.018 1.00 45.27 C ANISOU 3272 CB LYS B 423 7259 4242 5699 -345 1842 -903 C ATOM 3273 CG LYS A 423 39.654 -0.309 54.668 1.00 43.63 C ANISOU 3273 CG LYS B 423 6942 4128 5510 -335 1752 -907 C ATOM 3274 CD LYS A 423 40.647 -0.188 53.512 1.00 42.89 C ANISOU 3274 CD LYS B 423 6793 4039 5463 -391 1805 -977 C ATOM 3275 CE LYS A 423 40.035 -0.576 52.175 1.00 36.73 C ANISOU 3275 CE LYS B 423 5914 3347 4695 -378 1721 -980 C ATOM 3276 NZ LYS A 423 40.718 0.186 51.085 1.00 36.06 N ANISOU 3276 NZ LYS B 423 5743 3296 4661 -449 1753 -1061 N ATOM 3277 N GLU A 424 41.891 2.115 58.087 1.00 48.75 N ANISOU 3277 N GLU B 424 7827 4531 6165 -451 2060 -971 N ATOM 3278 CA GLU A 424 42.456 2.275 59.424 1.00 49.53 C ANISOU 3278 CA GLU B 424 8050 4532 6238 -452 2152 -958 C ATOM 3279 C GLU A 424 41.653 3.234 60.332 1.00 49.09 C ANISOU 3279 C GLU B 424 7996 4490 6167 -453 2125 -941 C ATOM 3280 O GLU A 424 41.550 4.442 60.070 1.00 48.29 O ANISOU 3280 O GLU B 424 7809 4428 6110 -508 2130 -991 O ATOM 3281 CB GLU A 424 43.960 2.637 59.301 1.00 51.56 C ANISOU 3281 CB GLU B 424 8333 4717 6540 -523 2289 -1027 C ATOM 3282 CG GLU A 424 44.488 2.912 57.810 1.00 54.13 C ANISOU 3282 CG GLU B 424 8538 5099 6932 -583 2292 -1103 C ATOM 3283 CD GLU A 424 44.758 1.650 56.940 1.00 58.85 C ANISOU 3283 CD GLU B 424 9139 5701 7521 -551 2272 -1090 C ATOM 3284 OE1 GLU A 424 45.319 0.660 57.477 1.00 63.46 O ANISOU 3284 OE1 GLU B 424 9840 6203 8070 -513 2328 -1054 O ATOM 3285 OE2 GLU A 424 44.451 1.652 55.704 1.00 57.25 O ANISOU 3285 OE2 GLU B 424 8825 5582 7347 -563 2206 -1117 O ATOM 3286 N GLY A 425 41.061 2.663 61.384 1.00 48.48 N ANISOU 3286 N GLY B 425 8015 4381 6023 -389 2094 -871 N ATOM 3287 CA GLY A 425 40.250 3.412 62.347 1.00 48.19 C ANISOU 3287 CA GLY B 425 7998 4352 5961 -381 2066 -848 C ATOM 3288 C GLY A 425 38.753 3.491 62.048 1.00 47.57 C ANISOU 3288 C GLY B 425 7836 4370 5869 -346 1930 -815 C ATOM 3289 O GLY A 425 37.967 3.897 62.914 1.00 47.53 O ANISOU 3289 O GLY B 425 7860 4368 5830 -328 1897 -785 O ATOM 3290 N ILE A 426 38.357 3.121 60.828 1.00 46.63 N ANISOU 3290 N ILE B 426 7615 4328 5774 -340 1856 -822 N ATOM 3291 CA ILE A 426 36.966 3.287 60.377 1.00 46.16 C ANISOU 3291 CA ILE B 426 7464 4364 5712 -317 1734 -799 C ATOM 3292 C ILE A 426 36.258 1.938 60.255 1.00 45.52 C ANISOU 3292 C ILE B 426 7401 4308 5585 -244 1648 -738 C ATOM 3293 O ILE A 426 35.174 1.757 60.800 1.00 44.26 O ANISOU 3293 O ILE B 426 7254 4177 5387 -202 1571 -692 O ATOM 3294 CB ILE A 426 36.887 4.035 59.033 1.00 45.81 C ANISOU 3294 CB ILE B 426 7278 4397 5730 -366 1707 -855 C ATOM 3295 CG1 ILE A 426 37.669 5.345 59.104 1.00 48.09 C ANISOU 3295 CG1 ILE B 426 7540 4663 6068 -438 1794 -922 C ATOM 3296 CG2 ILE A 426 35.444 4.336 58.661 1.00 44.96 C ANISOU 3296 CG2 ILE B 426 7086 4379 5618 -345 1593 -831 C ATOM 3297 CD1 ILE A 426 38.048 5.890 57.724 1.00 50.15 C ANISOU 3297 CD1 ILE B 426 7679 4985 6391 -489 1792 -987 C ATOM 3298 N LEU A 427 36.893 0.984 59.570 1.00 45.27 N ANISOU 3298 N LEU B 427 7373 4265 5561 -230 1664 -741 N ATOM 3299 CA LEU A 427 36.280 -0.323 59.345 1.00 45.00 C ANISOU 3299 CA LEU B 427 7347 4259 5492 -161 1585 -688 C ATOM 3300 C LEU A 427 35.809 -0.929 60.658 1.00 45.45 C ANISOU 3300 C LEU B 427 7511 4277 5482 -98 1561 -625 C ATOM 3301 O LEU A 427 34.786 -1.601 60.690 1.00 44.49 O ANISOU 3301 O LEU B 427 7371 4202 5330 -45 1466 -580 O ATOM 3302 CB LEU A 427 37.264 -1.281 58.668 1.00 45.30 C ANISOU 3302 CB LEU B 427 7404 4265 5542 -153 1633 -699 C ATOM 3303 CG LEU A 427 36.931 -2.021 57.369 1.00 45.02 C ANISOU 3303 CG LEU B 427 7282 4296 5527 -136 1569 -699 C ATOM 3304 CD1 LEU A 427 37.996 -3.098 57.137 1.00 44.30 C ANISOU 3304 CD1 LEU B 427 7255 4145 5434 -115 1632 -698 C ATOM 3305 CD2 LEU A 427 35.527 -2.617 57.274 1.00 43.13 C ANISOU 3305 CD2 LEU B 427 6999 4127 5261 -80 1448 -648 C ATOM 3306 N ASP A 428 36.556 -0.679 61.737 1.00 46.58 N ANISOU 3306 N ASP B 428 7764 4334 5601 -105 1647 -623 N ATOM 3307 CA ASP A 428 36.195 -1.162 63.077 1.00 47.73 C ANISOU 3307 CA ASP B 428 8023 4435 5676 -46 1632 -566 C ATOM 3308 C ASP A 428 34.801 -0.668 63.493 1.00 46.68 C ANISOU 3308 C ASP B 428 7850 4364 5522 -34 1537 -544 C ATOM 3309 O ASP A 428 34.114 -1.306 64.302 1.00 46.85 O ANISOU 3309 O ASP B 428 7931 4385 5485 26 1478 -492 O ATOM 3310 CB ASP A 428 37.191 -0.699 64.167 1.00 49.12 C ANISOU 3310 CB ASP B 428 8321 4509 5833 -67 1749 -575 C ATOM 3311 CG ASP A 428 38.525 -0.135 63.615 1.00 53.12 C ANISOU 3311 CG ASP B 428 8816 4969 6398 -138 1867 -639 C ATOM 3312 OD1 ASP A 428 38.999 -0.543 62.513 1.00 55.73 O ANISOU 3312 OD1 ASP B 428 9086 5320 6768 -153 1874 -666 O ATOM 3313 OD2 ASP A 428 39.126 0.706 64.348 1.00 57.00 O ANISOU 3313 OD2 ASP B 428 9365 5399 6894 -180 1958 -664 O ATOM 3314 N LEU A 429 34.410 0.490 62.971 1.00 45.60 N ANISOU 3314 N LEU B 429 7616 4278 5432 -91 1525 -584 N ATOM 3315 CA LEU A 429 33.133 1.132 63.365 1.00 45.21 C ANISOU 3315 CA LEU B 429 7530 4281 5369 -89 1449 -569 C ATOM 3316 C LEU A 429 31.914 0.549 62.634 1.00 44.60 C ANISOU 3316 C LEU B 429 7363 4293 5291 -55 1328 -544 C ATOM 3317 O LEU A 429 30.798 0.575 63.158 1.00 45.01 O ANISOU 3317 O LEU B 429 7414 4378 5311 -29 1255 -514 O ATOM 3318 CB LEU A 429 33.209 2.645 63.153 1.00 44.33 C ANISOU 3318 CB LEU B 429 7354 4183 5307 -159 1490 -622 C ATOM 3319 CG LEU A 429 34.391 3.351 63.819 1.00 45.95 C ANISOU 3319 CG LEU B 429 7633 4304 5523 -202 1614 -655 C ATOM 3320 CD1 LEU A 429 34.387 4.841 63.473 1.00 45.31 C ANISOU 3320 CD1 LEU B 429 7467 4249 5498 -270 1644 -710 C ATOM 3321 CD2 LEU A 429 34.392 3.109 65.332 1.00 44.92 C ANISOU 3321 CD2 LEU B 429 7642 4101 5324 -166 1642 -613 C ATOM 3322 N LEU A 430 32.141 0.017 61.428 1.00 44.36 N ANISOU 3322 N LEU B 430 7261 4299 5295 -56 1313 -558 N ATOM 3323 CA LEU A 430 31.064 -0.572 60.629 1.00 43.41 C ANISOU 3323 CA LEU B 430 7054 4260 5179 -28 1208 -538 C ATOM 3324 C LEU A 430 30.611 -1.892 61.228 1.00 43.13 C ANISOU 3324 C LEU B 430 7080 4219 5089 47 1152 -482 C ATOM 3325 O LEU A 430 31.415 -2.663 61.719 1.00 44.33 O ANISOU 3325 O LEU B 430 7322 4309 5213 81 1197 -463 O ATOM 3326 CB LEU A 430 31.508 -0.776 59.181 1.00 42.82 C ANISOU 3326 CB LEU B 430 6893 4222 5155 -51 1215 -571 C ATOM 3327 CG LEU A 430 32.098 0.450 58.468 1.00 43.07 C ANISOU 3327 CG LEU B 430 6859 4264 5243 -123 1271 -633 C ATOM 3328 CD1 LEU A 430 32.333 0.179 56.998 1.00 43.24 C ANISOU 3328 CD1 LEU B 430 6790 4333 5305 -139 1258 -662 C ATOM 3329 CD2 LEU A 430 31.242 1.710 58.639 1.00 43.28 C ANISOU 3329 CD2 LEU B 430 6832 4331 5282 -154 1239 -646 C ATOM 3330 N ALA A 431 29.317 -2.148 61.185 1.00 42.44 N ANISOU 3330 N ALA B 431 6944 4195 4988 74 1053 -455 N ATOM 3331 CA ALA A 431 28.781 -3.412 61.671 1.00 42.36 C ANISOU 3331 CA ALA B 431 6973 4192 4930 145 988 -406 C ATOM 3332 C ALA A 431 29.225 -4.592 60.774 1.00 42.50 C ANISOU 3332 C ALA B 431 6965 4219 4964 177 983 -399 C ATOM 3333 O ALA A 431 29.567 -4.390 59.600 1.00 40.98 O ANISOU 3333 O ALA B 431 6697 4052 4821 141 1004 -432 O ATOM 3334 CB ALA A 431 27.260 -3.332 61.766 1.00 42.19 C ANISOU 3334 CB ALA B 431 6893 4240 4897 156 886 -388 C ATOM 3335 N PRO A 432 29.209 -5.830 61.323 1.00 42.75 N ANISOU 3335 N PRO B 432 7059 4232 4952 248 954 -356 N ATOM 3336 CA PRO A 432 29.620 -6.999 60.551 1.00 42.82 C ANISOU 3336 CA PRO B 432 7050 4246 4974 285 951 -347 C ATOM 3337 C PRO A 432 28.692 -7.157 59.361 1.00 42.07 C ANISOU 3337 C PRO B 432 6827 4238 4919 275 879 -357 C ATOM 3338 O PRO A 432 27.490 -6.950 59.512 1.00 41.86 O ANISOU 3338 O PRO B 432 6753 4267 4886 276 802 -346 O ATOM 3339 CB PRO A 432 29.410 -8.156 61.537 1.00 43.14 C ANISOU 3339 CB PRO B 432 7172 4266 4955 369 910 -295 C ATOM 3340 CG PRO A 432 29.478 -7.504 62.892 1.00 44.08 C ANISOU 3340 CG PRO B 432 7388 4334 5026 366 935 -284 C ATOM 3341 CD PRO A 432 28.779 -6.205 62.684 1.00 43.57 C ANISOU 3341 CD PRO B 432 7252 4312 4991 300 919 -315 C ATOM 3342 N GLY A 433 29.255 -7.498 58.196 1.00 41.69 N ANISOU 3342 N GLY B 433 6728 4200 4911 261 907 -378 N ATOM 3343 CA GLY A 433 28.487 -7.681 56.958 1.00 40.12 C ANISOU 3343 CA GLY B 433 6413 4079 4751 250 850 -389 C ATOM 3344 C GLY A 433 28.294 -6.432 56.104 1.00 39.12 C ANISOU 3344 C GLY B 433 6204 3993 4668 178 859 -433 C ATOM 3345 O GLY A 433 27.765 -6.522 54.998 1.00 39.24 O ANISOU 3345 O GLY B 433 6128 4068 4714 166 821 -444 O ATOM 3346 N THR A 434 28.724 -5.272 56.606 1.00 38.37 N ANISOU 3346 N THR B 434 6140 3864 4574 133 911 -457 N ATOM 3347 CA THR A 434 28.546 -3.992 55.914 1.00 37.00 C ANISOU 3347 CA THR B 434 5891 3727 4440 68 919 -498 C ATOM 3348 C THR A 434 29.426 -3.899 54.660 1.00 36.63 C ANISOU 3348 C THR B 434 5794 3686 4436 33 968 -541 C ATOM 3349 O THR A 434 30.603 -4.213 54.702 1.00 36.51 O ANISOU 3349 O THR B 434 5833 3616 4424 30 1040 -555 O ATOM 3350 CB THR A 434 28.843 -2.781 56.873 1.00 36.66 C ANISOU 3350 CB THR B 434 5899 3642 4389 32 968 -515 C ATOM 3351 OG1 THR A 434 27.974 -2.831 58.001 1.00 35.30 O ANISOU 3351 OG1 THR B 434 5772 3468 4174 62 920 -478 O ATOM 3352 CG2 THR A 434 28.628 -1.445 56.183 1.00 36.15 C ANISOU 3352 CG2 THR B 434 5753 3618 4364 -29 973 -557 C ATOM 3353 N TYR A 435 28.848 -3.458 53.550 1.00 35.91 N ANISOU 3353 N TYR B 435 5605 3663 4377 5 930 -562 N ATOM 3354 CA TYR A 435 29.619 -3.194 52.345 1.00 35.87 C ANISOU 3354 CA TYR B 435 5548 3670 4411 -34 971 -608 C ATOM 3355 C TYR A 435 30.347 -1.865 52.505 1.00 36.15 C ANISOU 3355 C TYR B 435 5586 3682 4468 -92 1035 -654 C ATOM 3356 O TYR A 435 29.838 -0.933 53.203 1.00 36.01 O ANISOU 3356 O TYR B 435 5573 3666 4443 -108 1023 -652 O ATOM 3357 CB TYR A 435 28.703 -3.200 51.110 1.00 36.32 C ANISOU 3357 CB TYR B 435 5503 3809 4489 -38 906 -612 C ATOM 3358 CG TYR A 435 28.125 -4.573 50.821 1.00 36.08 C ANISOU 3358 CG TYR B 435 5464 3801 4445 15 856 -574 C ATOM 3359 CD1 TYR A 435 27.080 -5.094 51.584 1.00 36.48 C ANISOU 3359 CD1 TYR B 435 5529 3864 4468 58 793 -528 C ATOM 3360 CD2 TYR A 435 28.655 -5.366 49.811 1.00 37.34 C ANISOU 3360 CD2 TYR B 435 5600 3967 4621 23 873 -586 C ATOM 3361 CE1 TYR A 435 26.553 -6.372 51.315 1.00 36.06 C ANISOU 3361 CE1 TYR B 435 5461 3835 4407 107 746 -497 C ATOM 3362 CE2 TYR A 435 28.151 -6.630 49.539 1.00 38.21 C ANISOU 3362 CE2 TYR B 435 5698 4096 4723 73 831 -553 C ATOM 3363 CZ TYR A 435 27.109 -7.128 50.296 1.00 37.55 C ANISOU 3363 CZ TYR B 435 5625 4029 4615 115 767 -509 C ATOM 3364 OH TYR A 435 26.623 -8.392 50.008 1.00 39.72 O ANISOU 3364 OH TYR B 435 5880 4325 4886 164 726 -480 O ATOM 3365 N TYR A 436 31.527 -1.781 51.887 1.00 35.55 N ANISOU 3365 N TYR B 436 5508 3581 4418 -125 1102 -697 N ATOM 3366 CA TYR A 436 32.372 -0.586 51.928 1.00 35.96 C ANISOU 3366 CA TYR B 436 5556 3610 4497 -184 1170 -750 C ATOM 3367 C TYR A 436 33.206 -0.421 50.674 1.00 35.55 C ANISOU 3367 C TYR B 436 5447 3578 4484 -225 1206 -806 C ATOM 3368 O TYR A 436 33.479 -1.400 49.985 1.00 36.30 O ANISOU 3368 O TYR B 436 5539 3676 4578 -205 1204 -802 O ATOM 3369 CB TYR A 436 33.270 -0.551 53.194 1.00 37.72 C ANISOU 3369 CB TYR B 436 5885 3743 4703 -187 1250 -748 C ATOM 3370 CG TYR A 436 34.338 -1.606 53.219 1.00 39.02 C ANISOU 3370 CG TYR B 436 6119 3846 4860 -169 1311 -746 C ATOM 3371 CD1 TYR A 436 35.608 -1.344 52.707 1.00 39.14 C ANISOU 3371 CD1 TYR B 436 6136 3829 4908 -216 1395 -801 C ATOM 3372 CD2 TYR A 436 34.069 -2.885 53.726 1.00 41.62 C ANISOU 3372 CD2 TYR B 436 6511 4152 5150 -102 1284 -690 C ATOM 3373 CE1 TYR A 436 36.586 -2.320 52.702 1.00 41.20 C ANISOU 3373 CE1 TYR B 436 6463 4029 5162 -200 1455 -800 C ATOM 3374 CE2 TYR A 436 35.043 -3.882 53.718 1.00 42.01 C ANISOU 3374 CE2 TYR B 436 6626 4143 5193 -80 1341 -685 C ATOM 3375 CZ TYR A 436 36.303 -3.581 53.207 1.00 42.26 C ANISOU 3375 CZ TYR B 436 6662 4137 5257 -130 1429 -740 C ATOM 3376 OH TYR A 436 37.287 -4.541 53.181 1.00 43.54 O ANISOU 3376 OH TYR B 436 6892 4236 5413 -111 1493 -738 O ATOM 3377 N LEU A 437 33.621 0.813 50.397 1.00 35.21 N ANISOU 3377 N LEU B 437 5359 3547 4471 -280 1237 -859 N ATOM 3378 CA LEU A 437 34.417 1.147 49.221 1.00 35.35 C ANISOU 3378 CA LEU B 437 5316 3589 4525 -325 1268 -920 C ATOM 3379 C LEU A 437 35.874 0.850 49.459 1.00 36.75 C ANISOU 3379 C LEU B 437 5557 3692 4715 -351 1368 -954 C ATOM 3380 O LEU A 437 36.479 1.435 50.363 1.00 37.03 O ANISOU 3380 O LEU B 437 5642 3671 4755 -377 1432 -971 O ATOM 3381 CB LEU A 437 34.289 2.632 48.891 1.00 34.53 C ANISOU 3381 CB LEU B 437 5138 3531 4452 -372 1262 -966 C ATOM 3382 CG LEU A 437 34.930 3.103 47.575 1.00 34.66 C ANISOU 3382 CG LEU B 437 5074 3591 4504 -416 1274 -1032 C ATOM 3383 CD1 LEU A 437 34.238 2.441 46.356 1.00 31.93 C ANISOU 3383 CD1 LEU B 437 4671 3313 4149 -389 1203 -1016 C ATOM 3384 CD2 LEU A 437 34.878 4.622 47.471 1.00 35.46 C ANISOU 3384 CD2 LEU B 437 5110 3730 4634 -458 1273 -1077 C ATOM 3385 N LYS A 438 36.441 -0.028 48.634 1.00 37.69 N ANISOU 3385 N LYS B 438 5674 3807 4838 -347 1384 -967 N ATOM 3386 CA LYS A 438 37.868 -0.366 48.697 1.00 38.80 C ANISOU 3386 CA LYS B 438 5872 3877 4993 -375 1483 -1005 C ATOM 3387 C LYS A 438 38.740 0.550 47.840 1.00 38.17 C ANISOU 3387 C LYS B 438 5727 3817 4957 -447 1528 -1089 C ATOM 3388 O LYS A 438 39.749 1.045 48.307 1.00 38.99 O ANISOU 3388 O LYS B 438 5867 3866 5082 -491 1613 -1131 O ATOM 3389 CB LYS A 438 38.088 -1.823 48.302 1.00 38.79 C ANISOU 3389 CB LYS B 438 5910 3854 4975 -332 1485 -977 C ATOM 3390 CG LYS A 438 37.492 -2.835 49.281 1.00 39.82 C ANISOU 3390 CG LYS B 438 6117 3950 5062 -260 1457 -900 C ATOM 3391 CD LYS A 438 37.737 -4.281 48.795 1.00 42.09 C ANISOU 3391 CD LYS B 438 6435 4220 5338 -216 1460 -876 C ATOM 3392 CE LYS A 438 37.649 -5.275 49.971 1.00 47.22 C ANISOU 3392 CE LYS B 438 7187 4808 5947 -149 1466 -811 C ATOM 3393 NZ LYS A 438 38.434 -6.538 49.749 1.00 49.69 N ANISOU 3393 NZ LYS B 438 7559 5068 6254 -116 1514 -801 N ATOM 3394 N GLU A 439 38.366 0.766 46.586 1.00 37.77 N ANISOU 3394 N GLU B 439 5584 3846 4920 -458 1472 -1114 N ATOM 3395 CA GLU A 439 39.148 1.628 45.703 1.00 38.28 C ANISOU 3395 CA GLU B 439 5580 3940 5023 -523 1504 -1197 C ATOM 3396 C GLU A 439 38.337 2.030 44.491 1.00 37.09 C ANISOU 3396 C GLU B 439 5326 3890 4876 -521 1418 -1208 C ATOM 3397 O GLU A 439 37.344 1.395 44.173 1.00 36.36 O ANISOU 3397 O GLU B 439 5222 3835 4758 -472 1347 -1156 O ATOM 3398 CB GLU A 439 40.480 0.958 45.282 1.00 39.13 C ANISOU 3398 CB GLU B 439 5726 3995 5146 -552 1587 -1241 C ATOM 3399 CG GLU A 439 40.371 -0.095 44.214 1.00 40.41 C ANISOU 3399 CG GLU B 439 5872 4186 5296 -526 1555 -1232 C ATOM 3400 CD GLU A 439 41.716 -0.724 43.865 1.00 41.85 C ANISOU 3400 CD GLU B 439 6099 4309 5493 -556 1644 -1277 C ATOM 3401 OE1 GLU A 439 42.292 -0.344 42.819 1.00 43.75 O ANISOU 3401 OE1 GLU B 439 6279 4586 5759 -605 1657 -1346 O ATOM 3402 OE2 GLU A 439 42.216 -1.564 44.656 1.00 45.92 O ANISOU 3402 OE2 GLU B 439 6711 4741 5995 -532 1704 -1246 O ATOM 3403 N VAL A 440 38.724 3.137 43.873 1.00 37.20 N ANISOU 3403 N VAL B 440 5267 3947 4922 -573 1423 -1276 N ATOM 3404 CA VAL A 440 38.211 3.535 42.573 1.00 36.85 C ANISOU 3404 CA VAL B 440 5127 3995 4881 -576 1353 -1299 C ATOM 3405 C VAL A 440 39.436 3.497 41.625 1.00 38.07 C ANISOU 3405 C VAL B 440 5256 4150 5060 -628 1405 -1378 C ATOM 3406 O VAL A 440 40.424 4.204 41.863 1.00 38.14 O ANISOU 3406 O VAL B 440 5259 4131 5100 -683 1471 -1441 O ATOM 3407 CB VAL A 440 37.562 4.937 42.625 1.00 36.81 C ANISOU 3407 CB VAL B 440 5051 4047 4889 -588 1308 -1313 C ATOM 3408 CG1 VAL A 440 37.021 5.339 41.260 1.00 36.61 C ANISOU 3408 CG1 VAL B 440 4934 4116 4861 -586 1234 -1334 C ATOM 3409 CG2 VAL A 440 36.425 4.975 43.681 1.00 35.16 C ANISOU 3409 CG2 VAL B 440 4878 3826 4657 -543 1268 -1238 C ATOM 3410 N ASP A 441 39.400 2.645 40.596 1.00 38.00 N ANISOU 3410 N ASP B 441 5235 4168 5036 -612 1380 -1377 N ATOM 3411 CA ASP A 441 40.571 2.480 39.714 1.00 39.61 C ANISOU 3411 CA ASP B 441 5424 4367 5258 -660 1432 -1451 C ATOM 3412 C ASP A 441 40.721 3.627 38.708 1.00 40.12 C ANISOU 3412 C ASP B 441 5388 4513 5343 -703 1399 -1523 C ATOM 3413 O ASP A 441 39.943 4.591 38.735 1.00 39.41 O ANISOU 3413 O ASP B 441 5242 4479 5254 -694 1341 -1515 O ATOM 3414 CB ASP A 441 40.553 1.109 38.997 1.00 40.16 C ANISOU 3414 CB ASP B 441 5524 4431 5305 -628 1425 -1425 C ATOM 3415 CG ASP A 441 39.502 1.028 37.858 1.00 41.01 C ANISOU 3415 CG ASP B 441 5565 4628 5389 -595 1331 -1404 C ATOM 3416 OD1 ASP A 441 38.937 2.064 37.402 1.00 42.16 O ANISOU 3416 OD1 ASP B 441 5635 4846 5537 -604 1273 -1422 O ATOM 3417 OD2 ASP A 441 39.248 -0.105 37.403 1.00 42.28 O ANISOU 3417 OD2 ASP B 441 5750 4784 5529 -560 1318 -1370 O ATOM 3418 N SER A 442 41.691 3.506 37.794 1.00 40.57 N ANISOU 3418 N SER B 442 5424 4579 5414 -747 1434 -1594 N ATOM 3419 CA SER A 442 42.015 4.598 36.867 1.00 41.03 C ANISOU 3419 CA SER B 442 5387 4710 5492 -792 1410 -1674 C ATOM 3420 C SER A 442 40.968 4.841 35.769 1.00 40.97 C ANISOU 3420 C SER B 442 5309 4802 5457 -758 1306 -1657 C ATOM 3421 O SER A 442 41.051 5.854 35.059 1.00 41.69 O ANISOU 3421 O SER B 442 5319 4963 5559 -784 1271 -1714 O ATOM 3422 CB SER A 442 43.417 4.408 36.250 1.00 41.53 C ANISOU 3422 CB SER B 442 5450 4751 5578 -855 1481 -1762 C ATOM 3423 OG SER A 442 43.417 3.346 35.304 1.00 42.05 O ANISOU 3423 OG SER B 442 5533 4828 5618 -835 1467 -1754 O ATOM 3424 N LEU A 443 39.998 3.931 35.626 1.00 39.90 N ANISOU 3424 N LEU B 443 5203 4673 5286 -698 1259 -1580 N ATOM 3425 CA LEU A 443 38.858 4.143 34.712 1.00 39.34 C ANISOU 3425 CA LEU B 443 5074 4687 5185 -660 1164 -1552 C ATOM 3426 C LEU A 443 37.532 4.416 35.474 1.00 39.57 C ANISOU 3426 C LEU B 443 5108 4726 5201 -610 1110 -1473 C ATOM 3427 O LEU A 443 36.429 4.186 34.933 1.00 38.11 O ANISOU 3427 O LEU B 443 4904 4590 4987 -566 1041 -1425 O ATOM 3428 CB LEU A 443 38.714 2.985 33.709 1.00 39.27 C ANISOU 3428 CB LEU B 443 5081 4692 5147 -636 1148 -1536 C ATOM 3429 CG LEU A 443 39.968 2.647 32.875 1.00 39.04 C ANISOU 3429 CG LEU B 443 5050 4654 5128 -684 1200 -1613 C ATOM 3430 CD1 LEU A 443 39.751 1.441 31.951 1.00 39.59 C ANISOU 3430 CD1 LEU B 443 5142 4732 5168 -655 1187 -1590 C ATOM 3431 CD2 LEU A 443 40.477 3.877 32.093 1.00 38.21 C ANISOU 3431 CD2 LEU B 443 4864 4618 5038 -732 1181 -1700 C ATOM 3432 N TYR A 444 37.674 4.918 36.713 1.00 39.53 N ANISOU 3432 N TYR B 444 5130 4674 5217 -621 1145 -1464 N ATOM 3433 CA TYR A 444 36.559 5.303 37.605 1.00 39.92 C ANISOU 3433 CA TYR B 444 5187 4723 5256 -583 1105 -1399 C ATOM 3434 C TYR A 444 35.714 4.147 38.128 1.00 39.94 C ANISOU 3434 C TYR B 444 5253 4692 5231 -529 1086 -1314 C ATOM 3435 O TYR A 444 34.674 4.365 38.736 1.00 40.11 O ANISOU 3435 O TYR B 444 5279 4720 5240 -496 1045 -1259 O ATOM 3436 CB TYR A 444 35.640 6.325 36.951 1.00 39.55 C ANISOU 3436 CB TYR B 444 5064 4762 5203 -568 1026 -1399 C ATOM 3437 CG TYR A 444 36.252 7.672 36.647 1.00 40.94 C ANISOU 3437 CG TYR B 444 5170 4979 5408 -611 1032 -1475 C ATOM 3438 CD1 TYR A 444 36.927 7.904 35.436 1.00 41.70 C ANISOU 3438 CD1 TYR B 444 5211 5126 5508 -641 1025 -1545 C ATOM 3439 CD2 TYR A 444 36.111 8.731 37.538 1.00 41.24 C ANISOU 3439 CD2 TYR B 444 5192 5008 5468 -620 1040 -1478 C ATOM 3440 CE1 TYR A 444 37.468 9.166 35.139 1.00 42.46 C ANISOU 3440 CE1 TYR B 444 5235 5267 5632 -679 1023 -1618 C ATOM 3441 CE2 TYR A 444 36.652 9.995 37.254 1.00 41.32 C ANISOU 3441 CE2 TYR B 444 5131 5059 5509 -657 1043 -1549 C ATOM 3442 CZ TYR A 444 37.319 10.202 36.060 1.00 41.91 C ANISOU 3442 CZ TYR B 444 5147 5188 5588 -685 1032 -1619 C ATOM 3443 OH TYR A 444 37.821 11.446 35.789 1.00 43.89 O ANISOU 3443 OH TYR B 444 5321 5484 5869 -719 1030 -1691 O ATOM 3444 N ARG A 445 36.169 2.923 37.908 1.00 40.54 N ANISOU 3444 N ARG B 445 5375 4730 5297 -521 1118 -1305 N ATOM 3445 CA ARG A 445 35.426 1.742 38.312 1.00 40.25 C ANISOU 3445 CA ARG B 445 5391 4665 5235 -467 1099 -1230 C ATOM 3446 C ARG A 445 35.560 1.552 39.812 1.00 39.49 C ANISOU 3446 C ARG B 445 5368 4494 5142 -457 1141 -1194 C ATOM 3447 O ARG A 445 36.668 1.609 40.335 1.00 39.13 O ANISOU 3447 O ARG B 445 5363 4390 5116 -491 1216 -1230 O ATOM 3448 CB ARG A 445 35.990 0.521 37.579 1.00 40.49 C ANISOU 3448 CB ARG B 445 5449 4678 5259 -462 1127 -1238 C ATOM 3449 CG ARG A 445 35.766 0.540 36.067 1.00 43.49 C ANISOU 3449 CG ARG B 445 5766 5131 5627 -465 1084 -1265 C ATOM 3450 CD ARG A 445 37.027 0.169 35.311 1.00 49.00 C ANISOU 3450 CD ARG B 445 6469 5812 6336 -504 1140 -1331 C ATOM 3451 NE ARG A 445 37.341 -1.253 35.393 1.00 52.21 N ANISOU 3451 NE ARG B 445 6940 6163 6734 -480 1180 -1302 N ATOM 3452 CZ ARG A 445 38.490 -1.803 34.990 1.00 55.13 C ANISOU 3452 CZ ARG B 445 7338 6496 7114 -508 1245 -1350 C ATOM 3453 NH1 ARG A 445 39.468 -1.045 34.498 1.00 53.92 N ANISOU 3453 NH1 ARG B 445 7152 6354 6979 -568 1279 -1431 N ATOM 3454 NH2 ARG A 445 38.669 -3.122 35.097 1.00 56.48 N ANISOU 3454 NH2 ARG B 445 7568 6616 7277 -477 1277 -1316 N ATOM 3455 N ARG A 446 34.441 1.286 40.488 1.00 38.83 N ANISOU 3455 N ARG B 446 5304 4410 5039 -412 1095 -1125 N ATOM 3456 CA ARG A 446 34.407 1.157 41.964 1.00 38.70 C ANISOU 3456 CA ARG B 446 5358 4328 5017 -396 1123 -1087 C ATOM 3457 C ARG A 446 34.340 -0.291 42.478 1.00 38.67 C ANISOU 3457 C ARG B 446 5427 4273 4992 -350 1135 -1033 C ATOM 3458 O ARG A 446 33.571 -1.101 41.974 1.00 38.29 O ANISOU 3458 O ARG B 446 5366 4256 4928 -311 1085 -995 O ATOM 3459 CB ARG A 446 33.247 1.990 42.534 1.00 38.32 C ANISOU 3459 CB ARG B 446 5286 4312 4962 -380 1067 -1052 C ATOM 3460 CG ARG A 446 33.096 3.328 41.814 1.00 37.41 C ANISOU 3460 CG ARG B 446 5089 4261 4864 -411 1039 -1097 C ATOM 3461 CD ARG A 446 31.836 4.021 42.239 1.00 38.85 C ANISOU 3461 CD ARG B 446 5248 4476 5036 -388 980 -1057 C ATOM 3462 NE ARG A 446 31.935 4.405 43.631 1.00 36.93 N ANISOU 3462 NE ARG B 446 5057 4178 4796 -392 1014 -1042 N ATOM 3463 CZ ARG A 446 32.470 5.541 44.065 1.00 38.20 C ANISOU 3463 CZ ARG B 446 5205 4328 4982 -429 1052 -1084 C ATOM 3464 NH1 ARG A 446 32.945 6.444 43.210 1.00 36.43 N ANISOU 3464 NH1 ARG B 446 4911 4148 4783 -464 1054 -1145 N ATOM 3465 NH2 ARG A 446 32.504 5.783 45.367 1.00 38.08 N ANISOU 3465 NH2 ARG B 446 5246 4258 4965 -429 1085 -1065 N ATOM 3466 N PHE A 447 35.120 -0.602 43.509 1.00 39.12 N ANISOU 3466 N PHE B 447 5562 4252 5049 -352 1200 -1029 N ATOM 3467 CA PHE A 447 35.228 -1.981 44.022 1.00 39.29 C ANISOU 3467 CA PHE B 447 5659 4220 5051 -306 1218 -982 C ATOM 3468 C PHE A 447 34.893 -2.014 45.502 1.00 39.19 C ANISOU 3468 C PHE B 447 5714 4158 5019 -278 1221 -934 C ATOM 3469 O PHE A 447 35.397 -1.192 46.278 1.00 39.01 O ANISOU 3469 O PHE B 447 5719 4098 5004 -309 1267 -955 O ATOM 3470 CB PHE A 447 36.641 -2.538 43.775 1.00 40.55 C ANISOU 3470 CB PHE B 447 5863 4321 5223 -329 1304 -1022 C ATOM 3471 CG PHE A 447 37.039 -2.534 42.312 1.00 42.26 C ANISOU 3471 CG PHE B 447 6017 4583 5455 -360 1303 -1075 C ATOM 3472 CD1 PHE A 447 37.556 -1.377 41.707 1.00 43.90 C ANISOU 3472 CD1 PHE B 447 6166 4825 5690 -421 1319 -1144 C ATOM 3473 CD2 PHE A 447 36.853 -3.671 41.526 1.00 43.69 C ANISOU 3473 CD2 PHE B 447 6196 4779 5627 -326 1284 -1055 C ATOM 3474 CE1 PHE A 447 37.906 -1.358 40.340 1.00 43.02 C ANISOU 3474 CE1 PHE B 447 5997 4760 5587 -448 1313 -1195 C ATOM 3475 CE2 PHE A 447 37.189 -3.660 40.159 1.00 46.78 C ANISOU 3475 CE2 PHE B 447 6533 5214 6028 -354 1283 -1104 C ATOM 3476 CZ PHE A 447 37.711 -2.486 39.568 1.00 45.46 C ANISOU 3476 CZ PHE B 447 6309 5081 5882 -415 1295 -1174 C ATOM 3477 N TYR A 448 34.064 -2.989 45.879 1.00 38.21 N ANISOU 3477 N TYR B 448 5617 4034 4868 -219 1174 -871 N ATOM 3478 CA TYR A 448 33.461 -3.059 47.218 1.00 38.17 C ANISOU 3478 CA TYR B 448 5667 3999 4837 -184 1154 -819 C ATOM 3479 C TYR A 448 33.868 -4.320 47.912 1.00 38.84 C ANISOU 3479 C TYR B 448 5838 4020 4898 -136 1183 -781 C ATOM 3480 O TYR A 448 34.047 -5.341 47.275 1.00 39.73 O ANISOU 3480 O TYR B 448 5950 4134 5011 -110 1183 -773 O ATOM 3481 CB TYR A 448 31.920 -2.958 47.147 1.00 35.22 C ANISOU 3481 CB TYR B 448 5241 3692 4450 -156 1060 -779 C ATOM 3482 CG TYR A 448 31.524 -1.597 46.673 1.00 34.14 C ANISOU 3482 CG TYR B 448 5031 3608 4332 -198 1036 -812 C ATOM 3483 CD1 TYR A 448 31.451 -1.319 45.314 1.00 33.31 C ANISOU 3483 CD1 TYR B 448 4848 3562 4245 -220 1015 -845 C ATOM 3484 CD2 TYR A 448 31.283 -0.552 47.585 1.00 33.06 C ANISOU 3484 CD2 TYR B 448 4908 3460 4195 -216 1040 -812 C ATOM 3485 CE1 TYR A 448 31.140 -0.051 44.863 1.00 31.80 C ANISOU 3485 CE1 TYR B 448 4592 3420 4069 -255 994 -877 C ATOM 3486 CE2 TYR A 448 30.968 0.728 47.135 1.00 31.33 C ANISOU 3486 CE2 TYR B 448 4621 3288 3994 -252 1021 -844 C ATOM 3487 CZ TYR A 448 30.913 0.969 45.780 1.00 31.11 C ANISOU 3487 CZ TYR B 448 4516 3321 3984 -269 997 -876 C ATOM 3488 OH TYR A 448 30.613 2.209 45.297 1.00 29.92 O ANISOU 3488 OH TYR B 448 4298 3218 3850 -298 976 -907 O ATOM 3489 N GLY A 449 34.023 -4.241 49.218 1.00 40.00 N ANISOU 3489 N GLY B 449 6062 4110 5024 -122 1209 -757 N ATOM 3490 CA GLY A 449 34.140 -5.425 50.028 1.00 41.56 C ANISOU 3490 CA GLY B 449 6345 4256 5191 -62 1218 -708 C ATOM 3491 C GLY A 449 33.024 -5.505 51.035 1.00 43.11 C ANISOU 3491 C GLY B 449 6562 4464 5354 -19 1152 -654 C ATOM 3492 O GLY A 449 32.091 -4.701 51.028 1.00 42.16 O ANISOU 3492 O GLY B 449 6387 4395 5236 -36 1099 -653 O ATOM 3493 N LYS A 450 33.144 -6.470 51.934 1.00 44.99 N ANISOU 3493 N LYS B 450 6883 4652 5558 37 1158 -610 N ATOM 3494 CA LYS A 450 32.125 -6.721 52.906 1.00 46.48 C ANISOU 3494 CA LYS B 450 7097 4853 5712 83 1093 -559 C ATOM 3495 C LYS A 450 32.763 -7.091 54.238 1.00 48.73 C ANISOU 3495 C LYS B 450 7502 5055 5958 117 1141 -531 C ATOM 3496 O LYS A 450 33.599 -8.003 54.285 1.00 48.68 O ANISOU 3496 O LYS B 450 7557 4997 5943 149 1188 -522 O ATOM 3497 CB LYS A 450 31.213 -7.845 52.410 1.00 45.90 C ANISOU 3497 CB LYS B 450 6978 4831 5632 137 1015 -523 C ATOM 3498 CG LYS A 450 30.350 -8.486 53.482 1.00 46.57 C ANISOU 3498 CG LYS B 450 7103 4917 5676 198 953 -469 C ATOM 3499 CD LYS A 450 29.134 -9.176 52.863 1.00 46.35 C ANISOU 3499 CD LYS B 450 6994 4963 5653 230 864 -446 C ATOM 3500 CE LYS A 450 28.430 -10.062 53.864 1.00 47.12 C ANISOU 3500 CE LYS B 450 7132 5061 5712 298 805 -395 C ATOM 3501 NZ LYS A 450 27.405 -10.865 53.156 1.00 47.45 N ANISOU 3501 NZ LYS B 450 7092 5169 5767 327 730 -379 N ATOM 3502 N LYS A 451 32.405 -6.325 55.279 1.00 50.26 N ANISOU 3502 N LYS B 451 7733 5235 6129 108 1135 -521 N ATOM 3503 CA LYS A 451 32.402 -6.754 56.703 1.00 53.13 C ANISOU 3503 CA LYS B 451 8203 5543 6440 158 1137 -477 C ATOM 3504 C LYS A 451 33.512 -6.218 57.607 1.00 54.65 C ANISOU 3504 C LYS B 451 8497 5647 6619 135 1236 -491 C ATOM 3505 O LYS A 451 34.663 -6.677 57.506 1.00 56.56 O ANISOU 3505 O LYS B 451 8797 5828 6866 137 1314 -502 O ATOM 3506 CB LYS A 451 32.225 -8.277 56.844 1.00 53.56 C ANISOU 3506 CB LYS B 451 8291 5594 6466 239 1098 -430 C ATOM 3507 CG LYS A 451 32.542 -8.854 58.208 1.00 56.12 C ANISOU 3507 CG LYS B 451 8739 5850 6734 297 1116 -387 C ATOM 3508 CD LYS A 451 33.921 -9.535 58.194 1.00 59.76 C ANISOU 3508 CD LYS B 451 9283 6231 7192 315 1208 -389 C ATOM 3509 CE LYS A 451 34.618 -9.435 59.547 1.00 63.39 C ANISOU 3509 CE LYS B 451 9879 6602 7605 335 1272 -369 C ATOM 3510 NZ LYS A 451 33.982 -10.272 60.623 1.00 66.44 N ANISOU 3510 NZ LYS B 451 10331 6984 7929 420 1207 -308 N TER 3511 LYS B 451 END