ATOM 1 N GLY A 2 54.305 41.007 -7.713 1.00 29.03 N ANISOU 1 N GLY A 2 3383 3457 4188 501 294 -471 N ATOM 2 CA GLY A 2 53.854 42.047 -6.743 1.00 27.01 C ANISOU 2 CA GLY A 2 3055 3303 3904 373 248 -319 C ATOM 3 C GLY A 2 52.666 42.829 -7.275 1.00 25.73 C ANISOU 3 C GLY A 2 2951 3245 3582 268 251 -323 C ATOM 4 O GLY A 2 52.152 42.542 -8.354 1.00 26.66 O ANISOU 4 O GLY A 2 3167 3363 3599 274 269 -423 O ATOM 5 N TYR A 3 52.246 43.837 -6.524 1.00 24.18 N ANISOU 5 N TYR A 3 2688 3137 3361 180 227 -220 N ATOM 6 CA TYR A 3 51.017 44.558 -6.823 1.00 23.31 C ANISOU 6 CA TYR A 3 2611 3110 3137 92 204 -209 C ATOM 7 C TYR A 3 51.309 45.939 -7.367 1.00 22.93 C ANISOU 7 C TYR A 3 2512 3175 3025 108 290 -179 C ATOM 8 O TYR A 3 52.321 46.542 -7.040 1.00 22.37 O ANISOU 8 O TYR A 3 2357 3133 3011 139 348 -133 O ATOM 9 CB TYR A 3 50.180 44.732 -5.567 1.00 22.05 C ANISOU 9 CB TYR A 3 2412 2967 2997 -12 116 -129 C ATOM 10 CG TYR A 3 49.673 43.439 -4.989 1.00 22.58 C ANISOU 10 CG TYR A 3 2533 2934 3111 -74 14 -120 C ATOM 11 CD1 TYR A 3 48.815 42.619 -5.714 1.00 22.33 C ANISOU 11 CD1 TYR A 3 2601 2845 3038 -114 -42 -183 C ATOM 12 CD2 TYR A 3 50.054 43.035 -3.722 1.00 21.00 C ANISOU 12 CD2 TYR A 3 2291 2696 2994 -108 -43 -36 C ATOM 13 CE1 TYR A 3 48.359 41.433 -5.187 1.00 22.56 C ANISOU 13 CE1 TYR A 3 2686 2762 3124 -193 -148 -159 C ATOM 14 CE2 TYR A 3 49.597 41.862 -3.188 1.00 20.42 C ANISOU 14 CE2 TYR A 3 2272 2522 2963 -184 -148 4 C ATOM 15 CZ TYR A 3 48.754 41.067 -3.916 1.00 21.08 C ANISOU 15 CZ TYR A 3 2455 2532 3024 -228 -199 -55 C ATOM 16 OH TYR A 3 48.299 39.907 -3.379 1.00 20.91 O ANISOU 16 OH TYR A 3 2494 2394 3059 -325 -316 -1 O ATOM 17 N THR A 4 50.392 46.427 -8.190 1.00 23.10 N ANISOU 17 N THR A 4 2585 3257 2936 73 281 -191 N ATOM 18 CA THR A 4 50.249 47.855 -8.428 1.00 22.92 C ANISOU 18 CA THR A 4 2520 3317 2870 56 310 -124 C ATOM 19 C THR A 4 49.299 48.406 -7.381 1.00 21.98 C ANISOU 19 C THR A 4 2353 3207 2792 -4 233 -78 C ATOM 20 O THR A 4 48.183 47.920 -7.245 1.00 22.23 O ANISOU 20 O THR A 4 2407 3242 2796 -50 159 -98 O ATOM 21 CB THR A 4 49.713 48.085 -9.829 1.00 23.72 C ANISOU 21 CB THR A 4 2698 3481 2834 54 319 -143 C ATOM 22 OG1 THR A 4 50.678 47.593 -10.762 1.00 25.05 O ANISOU 22 OG1 THR A 4 2907 3669 2944 112 416 -205 O ATOM 23 CG2 THR A 4 49.586 49.575 -10.146 1.00 23.27 C ANISOU 23 CG2 THR A 4 2608 3484 2748 38 330 -47 C ATOM 24 N VAL A 5 49.771 49.384 -6.611 1.00 21.46 N ANISOU 24 N VAL A 5 2214 3151 2790 -6 253 -28 N ATOM 25 CA VAL A 5 48.993 50.007 -5.550 1.00 20.79 C ANISOU 25 CA VAL A 5 2077 3085 2737 -47 202 -14 C ATOM 26 C VAL A 5 48.820 51.487 -5.878 1.00 20.98 C ANISOU 26 C VAL A 5 2083 3120 2768 -30 212 20 C ATOM 27 O VAL A 5 49.761 52.134 -6.322 1.00 20.65 O ANISOU 27 O VAL A 5 2039 3061 2745 -15 261 61 O ATOM 28 CB VAL A 5 49.714 49.870 -4.178 1.00 20.72 C ANISOU 28 CB VAL A 5 2013 3062 2799 -72 197 -2 C ATOM 29 CG1 VAL A 5 48.908 50.521 -3.057 1.00 20.12 C ANISOU 29 CG1 VAL A 5 1888 3031 2724 -115 162 -14 C ATOM 30 CG2 VAL A 5 49.989 48.404 -3.856 1.00 21.48 C ANISOU 30 CG2 VAL A 5 2132 3119 2912 -84 168 -7 C ATOM 31 N ALA A 6 47.613 52.011 -5.680 1.00 21.13 N ANISOU 31 N ALA A 6 2080 3165 2783 -32 162 9 N ATOM 32 CA ALA A 6 47.364 53.436 -5.831 1.00 21.31 C ANISOU 32 CA ALA A 6 2085 3163 2848 1 150 37 C ATOM 33 C ALA A 6 46.940 54.014 -4.499 1.00 21.31 C ANISOU 33 C ALA A 6 2019 3165 2911 1 135 -18 C ATOM 34 O ALA A 6 46.213 53.379 -3.741 1.00 21.55 O ANISOU 34 O ALA A 6 2010 3261 2917 -24 121 -65 O ATOM 35 CB ALA A 6 46.306 53.689 -6.875 1.00 22.09 C ANISOU 35 CB ALA A 6 2205 3288 2901 27 97 67 C ATOM 36 N VAL A 7 47.418 55.214 -4.209 1.00 21.46 N ANISOU 36 N VAL A 7 2033 3116 3004 19 139 -15 N ATOM 37 CA VAL A 7 46.947 55.987 -3.081 1.00 21.83 C ANISOU 37 CA VAL A 7 2033 3154 3106 37 126 -97 C ATOM 38 C VAL A 7 46.115 57.121 -3.679 1.00 23.03 C ANISOU 38 C VAL A 7 2182 3242 3324 118 82 -89 C ATOM 39 O VAL A 7 46.639 57.935 -4.449 1.00 23.21 O ANISOU 39 O VAL A 7 2256 3166 3399 128 63 -11 O ATOM 40 CB VAL A 7 48.122 56.556 -2.253 1.00 21.80 C ANISOU 40 CB VAL A 7 2036 3093 3155 -5 140 -118 C ATOM 41 CG1 VAL A 7 47.618 57.380 -1.085 1.00 22.52 C ANISOU 41 CG1 VAL A 7 2096 3176 3283 15 128 -237 C ATOM 42 CG2 VAL A 7 49.028 55.433 -1.759 1.00 21.43 C ANISOU 42 CG2 VAL A 7 1981 3104 3059 -73 163 -98 C ATOM 43 N VAL A 8 44.824 57.142 -3.356 1.00 23.49 N ANISOU 43 N VAL A 8 2173 3364 3386 171 62 -153 N ATOM 44 CA VAL A 8 43.897 58.149 -3.860 1.00 25.20 C ANISOU 44 CA VAL A 8 2363 3524 3688 273 6 -148 C ATOM 45 C VAL A 8 43.703 59.220 -2.789 1.00 26.43 C ANISOU 45 C VAL A 8 2481 3614 3946 340 14 -274 C ATOM 46 O VAL A 8 43.232 58.923 -1.702 1.00 26.77 O ANISOU 46 O VAL A 8 2453 3764 3953 340 60 -393 O ATOM 47 CB VAL A 8 42.536 57.518 -4.224 1.00 25.52 C ANISOU 47 CB VAL A 8 2322 3689 3684 302 -27 -146 C ATOM 48 CG1 VAL A 8 41.617 58.540 -4.881 1.00 26.60 C ANISOU 48 CG1 VAL A 8 2418 3766 3922 420 -107 -114 C ATOM 49 CG2 VAL A 8 42.732 56.308 -5.129 1.00 24.80 C ANISOU 49 CG2 VAL A 8 2284 3662 3477 219 -36 -61 C ATOM 50 N GLY A 9 44.056 60.463 -3.106 1.00 27.75 N ANISOU 50 N GLY A 9 2703 3606 4234 391 -33 -250 N ATOM 51 CA GLY A 9 44.158 61.525 -2.117 1.00 28.78 C ANISOU 51 CA GLY A 9 2836 3628 4471 442 -32 -387 C ATOM 52 C GLY A 9 45.551 61.557 -1.501 1.00 28.53 C ANISOU 52 C GLY A 9 2873 3550 4418 325 -4 -402 C ATOM 53 O GLY A 9 45.703 61.704 -0.286 1.00 28.38 O ANISOU 53 O GLY A 9 2841 3557 4384 307 27 -549 O ATOM 54 N ALA A 10 46.567 61.446 -2.356 1.00 28.06 N ANISOU 54 N ALA A 10 2878 3435 4349 242 -17 -249 N ATOM 55 CA ALA A 10 47.954 61.310 -1.927 1.00 27.83 C ANISOU 55 CA ALA A 10 2882 3394 4298 123 6 -230 C ATOM 56 C ALA A 10 48.547 62.573 -1.308 1.00 29.33 C ANISOU 56 C ALA A 10 3120 3412 4611 98 -39 -298 C ATOM 57 O ALA A 10 49.524 62.490 -0.564 1.00 28.72 O ANISOU 57 O ALA A 10 3049 3350 4514 -1 -31 -333 O ATOM 58 CB ALA A 10 48.817 60.866 -3.103 1.00 27.29 C ANISOU 58 CB ALA A 10 2843 3338 4189 54 22 -52 C ATOM 59 N THR A 11 47.970 63.734 -1.618 1.00 31.13 N ANISOU 59 N THR A 11 3385 3468 4975 186 -103 -315 N ATOM 60 CA THR A 11 48.518 65.017 -1.159 1.00 33.14 C ANISOU 60 CA THR A 11 3709 3508 5374 159 -168 -377 C ATOM 61 C THR A 11 48.011 65.472 0.205 1.00 34.70 C ANISOU 61 C THR A 11 3900 3687 5598 224 -164 -632 C ATOM 62 O THR A 11 48.519 66.451 0.763 1.00 35.98 O ANISOU 62 O THR A 11 4132 3676 5865 189 -220 -727 O ATOM 63 CB THR A 11 48.247 66.134 -2.192 1.00 34.69 C ANISOU 63 CB THR A 11 3970 3479 5731 216 -260 -254 C ATOM 64 OG1 THR A 11 46.842 66.238 -2.453 1.00 34.29 O ANISOU 64 OG1 THR A 11 3876 3432 5720 389 -281 -298 O ATOM 65 CG2 THR A 11 48.858 65.784 -3.537 1.00 34.31 C ANISOU 65 CG2 THR A 11 3940 3469 5627 126 -257 1 C ATOM 66 N GLY A 12 47.023 64.784 0.764 1.00 34.75 N ANISOU 66 N GLY A 12 3824 3876 5503 308 -97 -752 N ATOM 67 CA GLY A 12 46.552 65.152 2.092 1.00 36.86 C ANISOU 67 CA GLY A 12 4076 4176 5756 363 -67 -1007 C ATOM 68 C GLY A 12 47.663 65.096 3.144 1.00 37.36 C ANISOU 68 C GLY A 12 4186 4272 5738 212 -68 -1090 C ATOM 69 O GLY A 12 48.768 64.596 2.891 1.00 36.35 O ANISOU 69 O GLY A 12 4074 4172 5565 70 -83 -941 O ATOM 70 N ALA A 13 47.377 65.640 4.325 1.00 39.18 N ANISOU 70 N ALA A 13 4433 4505 5951 245 -54 -1336 N ATOM 71 CA ALA A 13 48.086 65.234 5.539 1.00 38.99 C ANISOU 71 CA ALA A 13 4422 4625 5767 106 -38 -1437 C ATOM 72 C ALA A 13 47.616 63.799 5.837 1.00 37.06 C ANISOU 72 C ALA A 13 4078 4683 5321 80 52 -1380 C ATOM 73 O ALA A 13 48.337 62.990 6.429 1.00 36.11 O ANISOU 73 O ALA A 13 3952 4711 5059 -58 53 -1328 O ATOM 74 CB ALA A 13 47.761 66.168 6.696 1.00 41.25 C ANISOU 74 CB ALA A 13 4758 4861 6054 156 -37 -1738 C ATOM 75 N VAL A 14 46.395 63.495 5.397 1.00 36.36 N ANISOU 75 N VAL A 14 3908 4673 5236 210 112 -1376 N ATOM 76 CA VAL A 14 45.849 62.136 5.454 1.00 34.46 C ANISOU 76 CA VAL A 14 3573 4684 4837 177 182 -1289 C ATOM 77 C VAL A 14 46.633 61.210 4.504 1.00 31.92 C ANISOU 77 C VAL A 14 3265 4354 4509 85 147 -1040 C ATOM 78 O VAL A 14 47.035 60.108 4.879 1.00 30.85 O ANISOU 78 O VAL A 14 3110 4369 4244 -23 163 -961 O ATOM 79 CB VAL A 14 44.352 62.127 5.071 1.00 35.13 C ANISOU 79 CB VAL A 14 3553 4839 4957 330 236 -1333 C ATOM 80 CG1 VAL A 14 43.728 60.769 5.355 1.00 34.72 C ANISOU 80 CG1 VAL A 14 3401 5058 4732 266 306 -1269 C ATOM 81 CG2 VAL A 14 43.586 63.230 5.816 1.00 37.38 C ANISOU 81 CG2 VAL A 14 3815 5090 5300 471 273 -1596 C ATOM 82 N GLY A 15 46.855 61.675 3.277 1.00 30.91 N ANISOU 82 N GLY A 15 3172 4049 4522 131 99 -918 N ATOM 83 CA GLY A 15 47.627 60.937 2.293 1.00 28.65 C ANISOU 83 CA GLY A 15 2902 3754 4230 59 82 -709 C ATOM 84 C GLY A 15 49.065 60.691 2.728 1.00 27.68 C ANISOU 84 C GLY A 15 2810 3630 4075 -78 58 -657 C ATOM 85 O GLY A 15 49.614 59.638 2.451 1.00 25.94 O ANISOU 85 O GLY A 15 2568 3496 3792 -139 72 -535 O ATOM 86 N ALA A 16 49.659 61.661 3.421 1.00 28.64 N ANISOU 86 N ALA A 16 2980 3652 4252 -122 14 -758 N ATOM 87 CA ALA A 16 51.038 61.560 3.896 1.00 28.37 C ANISOU 87 CA ALA A 16 2959 3620 4201 -262 -30 -712 C ATOM 88 C ALA A 16 51.202 60.395 4.864 1.00 27.64 C ANISOU 88 C ALA A 16 2822 3738 3945 -335 -13 -718 C ATOM 89 O ALA A 16 52.171 59.644 4.757 1.00 27.03 O ANISOU 89 O ALA A 16 2714 3709 3848 -413 -33 -586 O ATOM 90 CB ALA A 16 51.482 62.865 4.549 1.00 30.27 C ANISOU 90 CB ALA A 16 3266 3711 4523 -307 -98 -848 C ATOM 91 N GLN A 17 50.254 60.226 5.787 1.00 27.82 N ANISOU 91 N GLN A 17 2831 3889 3850 -306 25 -859 N ATOM 92 CA GLN A 17 50.305 59.110 6.741 1.00 27.79 C ANISOU 92 CA GLN A 17 2792 4094 3674 -392 34 -840 C ATOM 93 C GLN A 17 50.104 57.763 6.055 1.00 26.15 C ANISOU 93 C GLN A 17 2538 3961 3438 -383 62 -669 C ATOM 94 O GLN A 17 50.722 56.770 6.427 1.00 25.74 O ANISOU 94 O GLN A 17 2468 3995 3318 -465 31 -565 O ATOM 95 CB GLN A 17 49.262 59.283 7.861 1.00 29.38 C ANISOU 95 CB GLN A 17 2982 4445 3736 -376 87 -1028 C ATOM 96 CG GLN A 17 49.542 60.421 8.813 1.00 32.31 C ANISOU 96 CG GLN A 17 3413 4775 4088 -405 56 -1233 C ATOM 97 CD GLN A 17 50.955 60.398 9.398 1.00 33.21 C ANISOU 97 CD GLN A 17 3565 4885 4169 -558 -46 -1182 C ATOM 98 OE1 GLN A 17 51.584 61.441 9.510 1.00 37.89 O ANISOU 98 OE1 GLN A 17 4217 5328 4851 -589 -111 -1271 O ATOM 99 NE2 GLN A 17 51.443 59.223 9.770 1.00 32.47 N ANISOU 99 NE2 GLN A 17 3433 4943 3961 -657 -74 -1033 N ATOM 100 N MET A 18 49.243 57.735 5.044 1.00 25.74 N ANISOU 100 N MET A 18 2470 3863 3446 -281 106 -642 N ATOM 101 CA MET A 18 49.040 56.539 4.241 1.00 24.84 C ANISOU 101 CA MET A 18 2331 3788 3317 -273 122 -501 C ATOM 102 C MET A 18 50.325 56.136 3.524 1.00 24.02 C ANISOU 102 C MET A 18 2241 3603 3281 -304 91 -362 C ATOM 103 O MET A 18 50.709 54.965 3.514 1.00 23.15 O ANISOU 103 O MET A 18 2116 3546 3134 -341 80 -266 O ATOM 104 CB MET A 18 47.928 56.786 3.212 1.00 25.13 C ANISOU 104 CB MET A 18 2354 3784 3410 -164 154 -506 C ATOM 105 CG MET A 18 47.401 55.533 2.564 1.00 25.22 C ANISOU 105 CG MET A 18 2343 3864 3377 -168 166 -405 C ATOM 106 SD MET A 18 46.423 54.542 3.709 1.00 27.67 S ANISOU 106 SD MET A 18 2592 4380 3540 -241 192 -437 S ATOM 107 CE MET A 18 44.854 55.456 3.743 1.00 29.08 C ANISOU 107 CE MET A 18 2693 4623 3734 -136 244 -576 C ATOM 108 N ILE A 19 50.991 57.111 2.920 1.00 24.11 N ANISOU 108 N ILE A 19 2276 3483 3401 -288 77 -350 N ATOM 109 CA ILE A 19 52.255 56.855 2.248 1.00 23.77 C ANISOU 109 CA ILE A 19 2220 3389 3421 -321 66 -226 C ATOM 110 C ILE A 19 53.268 56.298 3.238 1.00 23.87 C ANISOU 110 C ILE A 19 2195 3473 3400 -411 18 -197 C ATOM 111 O ILE A 19 53.945 55.330 2.939 1.00 22.56 O ANISOU 111 O ILE A 19 1991 3336 3244 -414 18 -95 O ATOM 112 CB ILE A 19 52.792 58.144 1.564 1.00 24.69 C ANISOU 112 CB ILE A 19 2362 3366 3655 -323 55 -207 C ATOM 113 CG1 ILE A 19 51.957 58.451 0.317 1.00 24.33 C ANISOU 113 CG1 ILE A 19 2349 3255 3640 -235 88 -171 C ATOM 114 CG2 ILE A 19 54.289 58.004 1.199 1.00 24.82 C ANISOU 114 CG2 ILE A 19 2331 3370 3728 -392 49 -90 C ATOM 115 CD1 ILE A 19 52.206 59.823 -0.259 1.00 26.52 C ANISOU 115 CD1 ILE A 19 2668 3378 4031 -239 59 -145 C ATOM 116 N LYS A 20 53.345 56.895 4.425 1.00 24.96 N ANISOU 116 N LYS A 20 2345 3642 3495 -477 -29 -295 N ATOM 117 CA LYS A 20 54.326 56.484 5.430 1.00 25.79 C ANISOU 117 CA LYS A 20 2416 3825 3557 -579 -102 -260 C ATOM 118 C LYS A 20 54.140 55.013 5.834 1.00 24.89 C ANISOU 118 C LYS A 20 2276 3827 3352 -588 -112 -178 C ATOM 119 O LYS A 20 55.099 54.257 5.889 1.00 25.23 O ANISOU 119 O LYS A 20 2271 3888 3430 -614 -161 -63 O ATOM 120 CB LYS A 20 54.256 57.415 6.652 1.00 27.28 C ANISOU 120 CB LYS A 20 2644 4043 3680 -655 -153 -409 C ATOM 121 CG LYS A 20 55.311 57.151 7.721 1.00 30.36 C ANISOU 121 CG LYS A 20 3003 4520 4011 -781 -255 -374 C ATOM 122 CD LYS A 20 55.318 58.251 8.773 1.00 34.15 C ANISOU 122 CD LYS A 20 3541 5008 4426 -864 -309 -548 C ATOM 123 CE LYS A 20 56.064 57.825 10.034 1.00 37.15 C ANISOU 123 CE LYS A 20 3902 5534 4680 -1001 -420 -523 C ATOM 124 NZ LYS A 20 57.538 57.678 9.821 1.00 39.34 N ANISOU 124 NZ LYS A 20 4097 5779 5072 -1071 -517 -374 N ATOM 125 N MET A 21 52.901 54.608 6.085 1.00 24.48 N ANISOU 125 N MET A 21 2251 3849 3202 -565 -71 -227 N ATOM 126 CA MET A 21 52.595 53.227 6.469 1.00 24.09 C ANISOU 126 CA MET A 21 2190 3892 3070 -596 -90 -136 C ATOM 127 C MET A 21 52.864 52.239 5.337 1.00 23.34 C ANISOU 127 C MET A 21 2084 3716 3070 -527 -76 -20 C ATOM 128 O MET A 21 53.302 51.111 5.581 1.00 22.89 O ANISOU 128 O MET A 21 2012 3671 3014 -550 -130 87 O ATOM 129 CB MET A 21 51.135 53.103 6.931 1.00 23.92 C ANISOU 129 CB MET A 21 2182 3982 2924 -605 -38 -213 C ATOM 130 CG MET A 21 50.854 53.763 8.271 1.00 24.80 C ANISOU 130 CG MET A 21 2303 4226 2896 -681 -43 -336 C ATOM 131 SD MET A 21 51.821 53.056 9.636 1.00 24.53 S ANISOU 131 SD MET A 21 2269 4318 2735 -834 -159 -235 S ATOM 132 CE MET A 21 53.137 54.291 9.808 1.00 26.19 C ANISOU 132 CE MET A 21 2487 4438 3028 -857 -227 -309 C ATOM 133 N LEU A 22 52.604 52.670 4.104 1.00 23.00 N ANISOU 133 N LEU A 22 2053 3583 3103 -440 -12 -44 N ATOM 134 CA LEU A 22 52.827 51.831 2.926 1.00 22.79 C ANISOU 134 CA LEU A 22 2027 3488 3143 -370 16 31 C ATOM 135 C LEU A 22 54.312 51.604 2.715 1.00 22.82 C ANISOU 135 C LEU A 22 1979 3452 3241 -359 -6 108 C ATOM 136 O LEU A 22 54.733 50.509 2.355 1.00 22.27 O ANISOU 136 O LEU A 22 1895 3354 3213 -317 -14 174 O ATOM 137 CB LEU A 22 52.265 52.498 1.665 1.00 22.86 C ANISOU 137 CB LEU A 22 2064 3436 3185 -297 83 -8 C ATOM 138 CG LEU A 22 51.077 51.898 0.924 1.00 25.01 C ANISOU 138 CG LEU A 22 2372 3713 3416 -255 110 -19 C ATOM 139 CD1 LEU A 22 51.188 52.278 -0.549 1.00 25.58 C ANISOU 139 CD1 LEU A 22 2469 3719 3531 -185 157 -4 C ATOM 140 CD2 LEU A 22 50.915 50.370 1.099 1.00 25.80 C ANISOU 140 CD2 LEU A 22 2485 3828 3488 -278 77 34 C ATOM 141 N GLU A 23 55.098 52.657 2.941 1.00 23.25 N ANISOU 141 N GLU A 23 1998 3498 3339 -397 -19 94 N ATOM 142 CA GLU A 23 56.540 52.610 2.780 1.00 24.06 C ANISOU 142 CA GLU A 23 2016 3588 3538 -401 -38 170 C ATOM 143 C GLU A 23 57.146 51.608 3.755 1.00 24.38 C ANISOU 143 C GLU A 23 2007 3680 3577 -433 -132 244 C ATOM 144 O GLU A 23 58.200 51.050 3.487 1.00 25.18 O ANISOU 144 O GLU A 23 2023 3769 3774 -391 -147 322 O ATOM 145 CB GLU A 23 57.173 54.003 3.022 1.00 24.83 C ANISOU 145 CB GLU A 23 2086 3669 3678 -476 -59 143 C ATOM 146 CG GLU A 23 57.023 54.967 1.858 1.00 25.48 C ANISOU 146 CG GLU A 23 2195 3675 3811 -446 18 129 C ATOM 147 CD GLU A 23 57.487 56.381 2.177 1.00 27.73 C ANISOU 147 CD GLU A 23 2479 3907 4148 -538 -24 100 C ATOM 148 OE1 GLU A 23 57.311 56.842 3.327 1.00 28.38 O ANISOU 148 OE1 GLU A 23 2593 4001 4189 -607 -98 18 O ATOM 149 OE2 GLU A 23 58.008 57.045 1.259 1.00 28.08 O ANISOU 149 OE2 GLU A 23 2501 3897 4270 -550 17 157 O ATOM 150 N GLU A 24 56.488 51.419 4.895 1.00 24.17 N ANISOU 150 N GLU A 24 2026 3718 3439 -506 -196 224 N ATOM 151 CA GLU A 24 56.981 50.538 5.952 1.00 25.13 C ANISOU 151 CA GLU A 24 2116 3898 3534 -562 -310 318 C ATOM 152 C GLU A 24 56.300 49.159 5.890 1.00 24.31 C ANISOU 152 C GLU A 24 2059 3772 3407 -528 -323 382 C ATOM 153 O GLU A 24 56.610 48.273 6.677 1.00 24.82 O ANISOU 153 O GLU A 24 2111 3860 3459 -570 -428 489 O ATOM 154 CB GLU A 24 56.798 51.220 7.322 1.00 26.03 C ANISOU 154 CB GLU A 24 2255 4123 3512 -694 -382 267 C ATOM 155 CG GLU A 24 57.466 52.596 7.377 1.00 28.70 C ANISOU 155 CG GLU A 24 2565 4449 3890 -740 -388 190 C ATOM 156 CD GLU A 24 57.563 53.210 8.765 1.00 32.25 C ANISOU 156 CD GLU A 24 3039 5004 4210 -875 -482 128 C ATOM 157 OE1 GLU A 24 56.841 52.775 9.677 1.00 34.64 O ANISOU 157 OE1 GLU A 24 3393 5416 4354 -933 -507 114 O ATOM 158 OE2 GLU A 24 58.370 54.150 8.945 1.00 36.43 O ANISOU 158 OE2 GLU A 24 3537 5516 4788 -938 -531 89 O ATOM 159 N SER A 25 55.397 48.979 4.926 1.00 23.11 N ANISOU 159 N SER A 25 1962 3564 3255 -462 -232 328 N ATOM 160 CA SER A 25 54.660 47.725 4.760 1.00 23.00 C ANISOU 160 CA SER A 25 2003 3509 3227 -448 -248 376 C ATOM 161 C SER A 25 55.527 46.582 4.196 1.00 23.22 C ANISOU 161 C SER A 25 2006 3420 3395 -352 -284 455 C ATOM 162 O SER A 25 56.531 46.824 3.535 1.00 22.75 O ANISOU 162 O SER A 25 1878 3322 3442 -265 -245 446 O ATOM 163 CB SER A 25 53.460 47.953 3.838 1.00 22.51 C ANISOU 163 CB SER A 25 1998 3429 3126 -413 -153 286 C ATOM 164 OG SER A 25 52.587 46.840 3.846 1.00 23.67 O ANISOU 164 OG SER A 25 2199 3554 3240 -442 -183 326 O ATOM 165 N THR A 26 55.124 45.345 4.492 1.00 23.54 N ANISOU 165 N THR A 26 2098 3406 3440 -372 -358 532 N ATOM 166 CA THR A 26 55.696 44.131 3.888 1.00 24.17 C ANISOU 166 CA THR A 26 2183 3333 3666 -263 -395 579 C ATOM 167 C THR A 26 55.013 43.752 2.562 1.00 23.66 C ANISOU 167 C THR A 26 2193 3174 3621 -184 -305 480 C ATOM 168 O THR A 26 55.401 42.785 1.911 1.00 23.35 O ANISOU 168 O THR A 26 2177 2998 3696 -80 -317 473 O ATOM 169 CB THR A 26 55.525 42.941 4.832 1.00 25.30 C ANISOU 169 CB THR A 26 2370 3426 3818 -335 -541 722 C ATOM 170 OG1 THR A 26 54.132 42.758 5.121 1.00 24.70 O ANISOU 170 OG1 THR A 26 2380 3397 3608 -461 -540 722 O ATOM 171 CG2 THR A 26 56.194 43.190 6.192 1.00 27.70 C ANISOU 171 CG2 THR A 26 2609 3837 4078 -428 -656 841 C ATOM 172 N LEU A 27 53.975 44.495 2.192 1.00 22.93 N ANISOU 172 N LEU A 27 2141 3155 3416 -233 -228 397 N ATOM 173 CA LEU A 27 53.233 44.249 0.961 1.00 23.24 C ANISOU 173 CA LEU A 27 2251 3134 3444 -183 -161 307 C ATOM 174 C LEU A 27 54.204 44.285 -0.227 1.00 23.67 C ANISOU 174 C LEU A 27 2280 3128 3585 -38 -77 242 C ATOM 175 O LEU A 27 54.965 45.233 -0.367 1.00 23.09 O ANISOU 175 O LEU A 27 2127 3121 3524 -7 -15 232 O ATOM 176 CB LEU A 27 52.138 45.310 0.801 1.00 22.45 C ANISOU 176 CB LEU A 27 2161 3145 3225 -242 -97 242 C ATOM 177 CG LEU A 27 50.934 45.015 -0.089 1.00 24.04 C ANISOU 177 CG LEU A 27 2432 3327 3374 -251 -75 182 C ATOM 178 CD1 LEU A 27 50.108 43.861 0.436 1.00 24.98 C ANISOU 178 CD1 LEU A 27 2602 3411 3478 -350 -165 240 C ATOM 179 CD2 LEU A 27 50.072 46.274 -0.224 1.00 25.26 C ANISOU 179 CD2 LEU A 27 2559 3594 3443 -275 -17 127 C ATOM 180 N PRO A 28 54.206 43.251 -1.066 1.00 24.92 N ANISOU 180 N PRO A 28 2502 3165 3801 44 -74 193 N ATOM 181 CA PRO A 28 55.077 43.253 -2.245 1.00 25.69 C ANISOU 181 CA PRO A 28 2573 3236 3952 185 29 108 C ATOM 182 C PRO A 28 54.488 44.199 -3.272 1.00 25.16 C ANISOU 182 C PRO A 28 2538 3259 3763 172 134 31 C ATOM 183 O PRO A 28 53.441 43.902 -3.859 1.00 25.24 O ANISOU 183 O PRO A 28 2647 3246 3697 140 125 -25 O ATOM 184 CB PRO A 28 55.039 41.800 -2.726 1.00 27.18 C ANISOU 184 CB PRO A 28 2849 3256 4221 264 -14 53 C ATOM 185 CG PRO A 28 53.699 41.273 -2.250 1.00 26.67 C ANISOU 185 CG PRO A 28 2891 3145 4096 129 -118 90 C ATOM 186 CD PRO A 28 53.397 42.022 -0.977 1.00 25.54 C ANISOU 186 CD PRO A 28 2685 3126 3892 -1 -165 205 C ATOM 187 N ILE A 29 55.133 45.347 -3.440 1.00 24.95 N ANISOU 187 N ILE A 29 2426 3332 3724 180 212 46 N ATOM 188 CA ILE A 29 54.669 46.390 -4.343 1.00 24.73 C ANISOU 188 CA ILE A 29 2423 3383 3592 160 294 11 C ATOM 189 C ILE A 29 55.652 46.488 -5.497 1.00 26.04 C ANISOU 189 C ILE A 29 2548 3585 3762 254 416 -30 C ATOM 190 O ILE A 29 56.837 46.751 -5.281 1.00 26.54 O ANISOU 190 O ILE A 29 2494 3684 3907 288 457 11 O ATOM 191 CB ILE A 29 54.589 47.742 -3.595 1.00 23.92 C ANISOU 191 CB ILE A 29 2264 3353 3473 74 279 70 C ATOM 192 CG1 ILE A 29 53.585 47.655 -2.438 1.00 23.12 C ANISOU 192 CG1 ILE A 29 2192 3253 3341 -14 183 90 C ATOM 193 CG2 ILE A 29 54.197 48.873 -4.552 1.00 23.78 C ANISOU 193 CG2 ILE A 29 2271 3386 3377 62 347 58 C ATOM 194 CD1 ILE A 29 53.705 48.788 -1.432 1.00 23.59 C ANISOU 194 CD1 ILE A 29 2194 3371 3397 -85 159 120 C ATOM 195 N ASP A 30 55.168 46.242 -6.712 1.00 26.62 N ANISOU 195 N ASP A 30 2711 3666 3739 287 474 -110 N ATOM 196 CA ASP A 30 55.972 46.410 -7.928 1.00 28.29 C ANISOU 196 CA ASP A 30 2894 3953 3900 360 612 -156 C ATOM 197 C ASP A 30 55.846 47.809 -8.506 1.00 27.95 C ANISOU 197 C ASP A 30 2840 4021 3760 288 669 -89 C ATOM 198 O ASP A 30 56.770 48.307 -9.147 1.00 28.91 O ANISOU 198 O ASP A 30 2887 4236 3861 306 782 -64 O ATOM 199 CB ASP A 30 55.547 45.394 -8.989 1.00 29.45 C ANISOU 199 CB ASP A 30 3161 4064 3965 425 641 -290 C ATOM 200 CG ASP A 30 55.975 43.988 -8.647 1.00 31.30 C ANISOU 200 CG ASP A 30 3404 4163 4325 527 604 -367 C ATOM 201 OD1 ASP A 30 56.819 43.831 -7.736 1.00 32.53 O ANISOU 201 OD1 ASP A 30 3447 4282 4629 566 577 -304 O ATOM 202 OD2 ASP A 30 55.515 42.980 -9.230 1.00 32.56 O ANISOU 202 OD2 ASP A 30 3684 4234 4454 570 583 -489 O ATOM 203 N LYS A 31 54.696 48.434 -8.277 1.00 27.23 N ANISOU 203 N LYS A 31 2814 3918 3615 205 588 -53 N ATOM 204 CA LYS A 31 54.393 49.744 -8.846 1.00 27.37 C ANISOU 204 CA LYS A 31 2843 4001 3555 144 610 18 C ATOM 205 C LYS A 31 53.493 50.545 -7.907 1.00 26.24 C ANISOU 205 C LYS A 31 2704 3815 3451 76 507 65 C ATOM 206 O LYS A 31 52.548 50.017 -7.344 1.00 24.42 O ANISOU 206 O LYS A 31 2512 3544 3222 65 427 26 O ATOM 207 CB LYS A 31 53.718 49.571 -10.208 1.00 28.29 C ANISOU 207 CB LYS A 31 3067 4170 3513 152 638 -25 C ATOM 208 CG LYS A 31 53.540 50.867 -11.001 1.00 30.34 C ANISOU 208 CG LYS A 31 3343 4501 3684 93 659 76 C ATOM 209 CD LYS A 31 53.660 50.634 -12.519 1.00 34.08 C ANISOU 209 CD LYS A 31 3887 5085 3977 106 746 49 C ATOM 210 CE LYS A 31 52.302 50.647 -13.213 1.00 35.48 C ANISOU 210 CE LYS A 31 4182 5275 4023 73 653 41 C ATOM 211 NZ LYS A 31 52.468 50.594 -14.691 1.00 37.72 N ANISOU 211 NZ LYS A 31 4541 5691 4099 63 731 32 N ATOM 212 N ILE A 32 53.816 51.823 -7.742 1.00 26.37 N ANISOU 212 N ILE A 32 2676 3841 3504 29 513 144 N ATOM 213 CA ILE A 32 53.014 52.729 -6.943 1.00 26.27 C ANISOU 213 CA ILE A 32 2669 3781 3533 -16 428 163 C ATOM 214 C ILE A 32 52.531 53.879 -7.825 1.00 26.82 C ANISOU 214 C ILE A 32 2783 3849 3558 -36 422 230 C ATOM 215 O ILE A 32 53.276 54.376 -8.668 1.00 27.64 O ANISOU 215 O ILE A 32 2881 3988 3634 -59 485 304 O ATOM 216 CB ILE A 32 53.815 53.234 -5.713 1.00 26.24 C ANISOU 216 CB ILE A 32 2584 3748 3639 -57 406 182 C ATOM 217 CG1 ILE A 32 52.921 54.063 -4.785 1.00 26.94 C ANISOU 217 CG1 ILE A 32 2687 3791 3758 -88 326 156 C ATOM 218 CG2 ILE A 32 55.053 54.021 -6.131 1.00 28.74 C ANISOU 218 CG2 ILE A 32 2838 4082 3998 -94 466 261 C ATOM 219 CD1 ILE A 32 52.207 53.229 -3.751 1.00 26.86 C ANISOU 219 CD1 ILE A 32 2677 3797 3733 -87 275 89 C ATOM 220 N ARG A 33 51.275 54.272 -7.628 1.00 26.21 N ANISOU 220 N ARG A 33 2741 3740 3477 -30 343 213 N ATOM 221 CA ARG A 33 50.683 55.431 -8.294 1.00 26.81 C ANISOU 221 CA ARG A 33 2855 3786 3547 -34 300 287 C ATOM 222 C ARG A 33 50.006 56.334 -7.269 1.00 26.19 C ANISOU 222 C ARG A 33 2750 3624 3575 -23 226 256 C ATOM 223 O ARG A 33 49.373 55.848 -6.331 1.00 25.59 O ANISOU 223 O ARG A 33 2645 3564 3514 -6 201 167 O ATOM 224 CB ARG A 33 49.646 54.974 -9.307 1.00 27.60 C ANISOU 224 CB ARG A 33 3016 3940 3532 -9 266 288 C ATOM 225 CG ARG A 33 50.221 54.120 -10.418 1.00 29.23 C ANISOU 225 CG ARG A 33 3268 4232 3606 -15 341 287 C ATOM 226 CD ARG A 33 49.186 53.659 -11.402 1.00 31.90 C ANISOU 226 CD ARG A 33 3679 4629 3813 -9 288 274 C ATOM 227 NE ARG A 33 48.465 54.792 -11.969 1.00 33.15 N ANISOU 227 NE ARG A 33 3860 4776 3960 -17 207 384 N ATOM 228 CZ ARG A 33 47.289 54.715 -12.586 1.00 35.18 C ANISOU 228 CZ ARG A 33 4153 5071 4142 -11 111 397 C ATOM 229 NH1 ARG A 33 46.674 53.544 -12.748 1.00 35.14 N ANISOU 229 NH1 ARG A 33 4173 5121 4057 -15 84 300 N ATOM 230 NH2 ARG A 33 46.731 55.826 -13.059 1.00 36.35 N ANISOU 230 NH2 ARG A 33 4311 5194 4307 -6 24 519 N ATOM 231 N TYR A 34 50.167 57.642 -7.442 1.00 26.24 N ANISOU 231 N TYR A 34 2771 3544 3655 -38 195 328 N ATOM 232 CA TYR A 34 49.556 58.644 -6.582 1.00 26.11 C ANISOU 232 CA TYR A 34 2743 3424 3754 -9 126 279 C ATOM 233 C TYR A 34 48.497 59.425 -7.369 1.00 26.94 C ANISOU 233 C TYR A 34 2883 3472 3879 49 48 341 C ATOM 234 O TYR A 34 48.782 59.973 -8.428 1.00 28.01 O ANISOU 234 O TYR A 34 3068 3577 3996 21 31 477 O ATOM 235 CB TYR A 34 50.624 59.615 -6.060 1.00 26.73 C ANISOU 235 CB TYR A 34 2817 3399 3940 -72 125 305 C ATOM 236 CG TYR A 34 51.587 59.064 -5.014 1.00 25.60 C ANISOU 236 CG TYR A 34 2621 3300 3807 -126 165 238 C ATOM 237 CD1 TYR A 34 51.306 57.898 -4.293 1.00 23.99 C ANISOU 237 CD1 TYR A 34 2382 3193 3541 -104 185 148 C ATOM 238 CD2 TYR A 34 52.784 59.726 -4.739 1.00 26.32 C ANISOU 238 CD2 TYR A 34 2692 3334 3974 -212 166 284 C ATOM 239 CE1 TYR A 34 52.190 57.410 -3.336 1.00 23.76 C ANISOU 239 CE1 TYR A 34 2304 3201 3522 -154 199 113 C ATOM 240 CE2 TYR A 34 53.675 59.240 -3.775 1.00 25.69 C ANISOU 240 CE2 TYR A 34 2550 3305 3907 -264 181 237 C ATOM 241 CZ TYR A 34 53.366 58.082 -3.085 1.00 24.33 C ANISOU 241 CZ TYR A 34 2349 3228 3668 -228 194 155 C ATOM 242 OH TYR A 34 54.225 57.594 -2.139 1.00 24.00 O ANISOU 242 OH TYR A 34 2248 3234 3636 -278 186 131 O ATOM 243 N LEU A 35 47.281 59.467 -6.840 1.00 26.58 N ANISOU 243 N LEU A 35 2801 3428 3871 128 -2 252 N ATOM 244 CA LEU A 35 46.170 60.167 -7.475 1.00 27.80 C ANISOU 244 CA LEU A 35 2959 3533 4070 207 -93 304 C ATOM 245 C LEU A 35 45.685 61.268 -6.544 1.00 28.23 C ANISOU 245 C LEU A 35 2982 3455 4288 288 -140 213 C ATOM 246 O LEU A 35 45.611 61.071 -5.344 1.00 27.74 O ANISOU 246 O LEU A 35 2871 3423 4247 299 -99 65 O ATOM 247 CB LEU A 35 45.033 59.199 -7.789 1.00 27.48 C ANISOU 247 CB LEU A 35 2875 3630 3935 242 -114 272 C ATOM 248 CG LEU A 35 45.095 58.417 -9.106 1.00 29.09 C ANISOU 248 CG LEU A 35 3135 3934 3984 191 -117 368 C ATOM 249 CD1 LEU A 35 46.405 57.689 -9.259 1.00 29.78 C ANISOU 249 CD1 LEU A 35 3269 4063 3983 109 -15 373 C ATOM 250 CD2 LEU A 35 43.934 57.430 -9.186 1.00 29.54 C ANISOU 250 CD2 LEU A 35 3143 4113 3968 206 -154 310 C ATOM 251 N ALA A 36 45.383 62.428 -7.106 1.00 29.87 N ANISOU 251 N ALA A 36 3225 3515 4609 343 -231 301 N ATOM 252 CA ALA A 36 44.886 63.576 -6.348 1.00 31.39 C ANISOU 252 CA ALA A 36 3399 3541 4984 446 -289 204 C ATOM 253 C ALA A 36 44.120 64.508 -7.299 1.00 33.54 C ANISOU 253 C ALA A 36 3692 3685 5365 540 -419 335 C ATOM 254 O ALA A 36 43.684 64.070 -8.359 1.00 33.26 O ANISOU 254 O ALA A 36 3658 3748 5233 533 -460 468 O ATOM 255 CB ALA A 36 46.050 64.307 -5.681 1.00 31.79 C ANISOU 255 CB ALA A 36 3512 3443 5123 370 -273 168 C ATOM 256 N SER A 37 43.957 65.779 -6.931 1.00 35.70 N ANISOU 256 N SER A 37 3990 3732 5841 627 -496 299 N ATOM 257 CA SER A 37 43.257 66.748 -7.783 1.00 38.07 C ANISOU 257 CA SER A 37 4313 3870 6281 730 -644 440 C ATOM 258 C SER A 37 44.058 67.095 -9.040 1.00 38.62 C ANISOU 258 C SER A 37 4501 3871 6302 598 -706 714 C ATOM 259 O SER A 37 45.292 67.057 -9.044 1.00 37.78 O ANISOU 259 O SER A 37 4462 3755 6138 444 -640 767 O ATOM 260 CB SER A 37 42.932 68.027 -7.002 1.00 40.22 C ANISOU 260 CB SER A 37 4592 3880 6809 869 -714 311 C ATOM 261 OG SER A 37 44.078 68.854 -6.870 1.00 41.96 O ANISOU 261 OG SER A 37 4937 3884 7121 759 -739 359 O ATOM 262 N GLY A 42 50.947 66.334 -11.853 1.00 40.78 N ANISOU 262 N GLY A 42 5007 4490 5998 -354 -300 1449 N ATOM 263 CA GLY A 42 52.186 66.855 -12.396 1.00 42.44 C ANISOU 263 CA GLY A 42 5234 4698 6191 -542 -260 1644 C ATOM 264 C GLY A 42 53.243 67.109 -11.338 1.00 42.21 C ANISOU 264 C GLY A 42 5153 4590 6294 -630 -219 1553 C ATOM 265 O GLY A 42 54.437 67.009 -11.618 1.00 42.80 O ANISOU 265 O GLY A 42 5178 4773 6310 -782 -124 1653 O ATOM 266 N LYS A 43 52.801 67.458 -10.131 1.00 41.81 N ANISOU 266 N LYS A 43 5105 4366 6416 -539 -291 1361 N ATOM 267 CA LYS A 43 53.674 67.589 -8.959 1.00 41.50 C ANISOU 267 CA LYS A 43 5019 4269 6482 -611 -268 1229 C ATOM 268 C LYS A 43 54.260 66.225 -8.565 1.00 39.17 C ANISOU 268 C LYS A 43 4612 4233 6038 -611 -120 1110 C ATOM 269 O LYS A 43 53.897 65.196 -9.135 1.00 37.42 O ANISOU 269 O LYS A 43 4364 4204 5651 -541 -39 1102 O ATOM 270 CB LYS A 43 52.889 68.195 -7.779 1.00 42.01 C ANISOU 270 CB LYS A 43 5122 4117 6723 -491 -373 1018 C ATOM 271 CG LYS A 43 53.742 68.738 -6.616 1.00 43.92 C ANISOU 271 CG LYS A 43 5359 4231 7098 -592 -404 899 C ATOM 272 CD LYS A 43 53.080 69.921 -5.886 1.00 46.99 C ANISOU 272 CD LYS A 43 5842 4311 7703 -513 -545 766 C ATOM 273 CE LYS A 43 53.863 70.319 -4.621 1.00 47.91 C ANISOU 273 CE LYS A 43 5960 4330 7914 -612 -576 597 C ATOM 274 NZ LYS A 43 54.113 71.785 -4.529 1.00 51.89 N ANISOU 274 NZ LYS A 43 6580 4489 8648 -697 -728 637 N ATOM 275 N SER A 44 55.149 66.234 -7.575 1.00 38.55 N ANISOU 275 N SER A 44 4474 4142 6029 -690 -104 1018 N ATOM 276 CA SER A 44 55.915 65.065 -7.175 1.00 36.93 C ANISOU 276 CA SER A 44 4155 4154 5722 -707 12 942 C ATOM 277 C SER A 44 55.871 64.814 -5.658 1.00 35.37 C ANISOU 277 C SER A 44 3926 3930 5582 -667 -21 725 C ATOM 278 O SER A 44 56.014 65.746 -4.859 1.00 36.07 O ANISOU 278 O SER A 44 4054 3845 5806 -722 -116 661 O ATOM 279 CB SER A 44 57.365 65.273 -7.615 1.00 38.36 C ANISOU 279 CB SER A 44 4256 4410 5911 -885 71 1106 C ATOM 280 OG SER A 44 58.056 64.051 -7.682 1.00 38.63 O ANISOU 280 OG SER A 44 4169 4681 5829 -870 203 1077 O ATOM 281 N LEU A 45 55.666 63.549 -5.280 1.00 32.93 N ANISOU 281 N LEU A 45 3559 3792 5161 -580 50 615 N ATOM 282 CA LEU A 45 55.850 63.073 -3.906 1.00 31.74 C ANISOU 282 CA LEU A 45 3360 3680 5017 -573 35 451 C ATOM 283 C LEU A 45 56.681 61.803 -3.911 1.00 30.41 C ANISOU 283 C LEU A 45 3083 3710 4761 -583 125 472 C ATOM 284 O LEU A 45 56.589 61.006 -4.838 1.00 29.52 O ANISOU 284 O LEU A 45 2952 3710 4552 -528 210 531 O ATOM 285 CB LEU A 45 54.507 62.740 -3.251 1.00 30.79 C ANISOU 285 CB LEU A 45 3284 3556 4857 -437 11 285 C ATOM 286 CG LEU A 45 53.630 63.890 -2.761 1.00 32.92 C ANISOU 286 CG LEU A 45 3637 3638 5234 -387 -80 181 C ATOM 287 CD1 LEU A 45 52.277 63.329 -2.324 1.00 32.26 C ANISOU 287 CD1 LEU A 45 3552 3623 5082 -244 -65 39 C ATOM 288 CD2 LEU A 45 54.302 64.660 -1.626 1.00 34.73 C ANISOU 288 CD2 LEU A 45 3880 3760 5556 -482 -150 79 C ATOM 289 N LYS A 46 57.445 61.594 -2.845 1.00 30.11 N ANISOU 289 N LYS A 46 2975 3708 4756 -644 96 411 N ATOM 290 CA LYS A 46 58.281 60.405 -2.699 1.00 29.76 C ANISOU 290 CA LYS A 46 2814 3829 4663 -639 157 430 C ATOM 291 C LYS A 46 57.486 59.151 -2.381 1.00 27.99 C ANISOU 291 C LYS A 46 2604 3690 4341 -517 183 337 C ATOM 292 O LYS A 46 56.488 59.208 -1.656 1.00 27.40 O ANISOU 292 O LYS A 46 2597 3574 4239 -474 133 225 O ATOM 293 CB LYS A 46 59.299 60.597 -1.569 1.00 30.47 C ANISOU 293 CB LYS A 46 2822 3931 4824 -749 84 407 C ATOM 294 CG LYS A 46 60.492 61.419 -1.947 1.00 33.48 C ANISOU 294 CG LYS A 46 3126 4291 5304 -896 76 534 C ATOM 295 CD LYS A 46 61.390 60.666 -2.933 1.00 34.66 C ANISOU 295 CD LYS A 46 3138 4601 5429 -883 201 662 C ATOM 296 CE LYS A 46 62.758 61.267 -3.006 1.00 36.74 C ANISOU 296 CE LYS A 46 3264 4903 5792 -1045 193 784 C ATOM 297 NZ LYS A 46 62.810 62.543 -2.265 1.00 40.17 N ANISOU 297 NZ LYS A 46 3767 5170 6326 -1192 53 762 N ATOM 298 N PHE A 47 57.924 58.030 -2.956 1.00 27.59 N ANISOU 298 N PHE A 47 2487 3754 4241 -464 264 382 N ATOM 299 CA PHE A 47 57.697 56.708 -2.376 1.00 26.86 C ANISOU 299 CA PHE A 47 2374 3734 4098 -389 263 316 C ATOM 300 C PHE A 47 59.042 56.012 -2.173 1.00 27.15 C ANISOU 300 C PHE A 47 2274 3855 4185 -402 282 370 C ATOM 301 O PHE A 47 59.714 55.650 -3.133 1.00 27.49 O ANISOU 301 O PHE A 47 2248 3962 4234 -368 376 431 O ATOM 302 CB PHE A 47 56.797 55.826 -3.238 1.00 26.35 C ANISOU 302 CB PHE A 47 2373 3698 3942 -284 323 294 C ATOM 303 CG PHE A 47 56.431 54.535 -2.568 1.00 26.14 C ANISOU 303 CG PHE A 47 2347 3708 3879 -229 297 234 C ATOM 304 CD1 PHE A 47 55.513 54.522 -1.530 1.00 26.00 C ANISOU 304 CD1 PHE A 47 2375 3675 3828 -243 226 162 C ATOM 305 CD2 PHE A 47 57.046 53.344 -2.931 1.00 27.54 C ANISOU 305 CD2 PHE A 47 2472 3933 4059 -167 344 250 C ATOM 306 CE1 PHE A 47 55.189 53.346 -0.893 1.00 25.53 C ANISOU 306 CE1 PHE A 47 2317 3652 3730 -221 195 138 C ATOM 307 CE2 PHE A 47 56.718 52.154 -2.289 1.00 26.38 C ANISOU 307 CE2 PHE A 47 2338 3787 3898 -127 298 215 C ATOM 308 CZ PHE A 47 55.796 52.158 -1.275 1.00 25.31 C ANISOU 308 CZ PHE A 47 2255 3641 3722 -168 221 174 C ATOM 309 N LYS A 48 59.409 55.806 -0.913 1.00 27.37 N ANISOU 309 N LYS A 48 2256 3898 4244 -445 192 343 N ATOM 310 CA LYS A 48 60.750 55.361 -0.537 1.00 28.63 C ANISOU 310 CA LYS A 48 2264 4133 4481 -471 172 408 C ATOM 311 C LYS A 48 61.785 56.266 -1.215 1.00 29.83 C ANISOU 311 C LYS A 48 2317 4305 4711 -555 219 498 C ATOM 312 O LYS A 48 61.729 57.475 -1.023 1.00 29.91 O ANISOU 312 O LYS A 48 2373 4243 4750 -668 168 502 O ATOM 313 CB LYS A 48 60.938 53.875 -0.850 1.00 28.62 C ANISOU 313 CB LYS A 48 2213 4185 4478 -342 220 417 C ATOM 314 CG LYS A 48 59.953 52.974 -0.123 1.00 29.10 C ANISOU 314 CG LYS A 48 2369 4218 4470 -294 156 356 C ATOM 315 CD LYS A 48 60.219 51.503 -0.444 1.00 31.30 C ANISOU 315 CD LYS A 48 2608 4505 4777 -172 183 370 C ATOM 316 CE LYS A 48 59.111 50.597 0.088 1.00 31.88 C ANISOU 316 CE LYS A 48 2796 4536 4781 -146 124 329 C ATOM 317 NZ LYS A 48 59.653 49.529 0.978 1.00 33.41 N ANISOU 317 NZ LYS A 48 2931 4729 5034 -123 24 386 N ATOM 318 N ASP A 49 62.689 55.701 -2.017 1.00 31.10 N ANISOU 318 N ASP A 49 2346 4561 4911 -504 319 567 N ATOM 319 CA ASP A 49 63.747 56.475 -2.692 1.00 33.41 C ANISOU 319 CA ASP A 49 2512 4914 5269 -599 383 673 C ATOM 320 C ASP A 49 63.339 57.112 -4.040 1.00 33.48 C ANISOU 320 C ASP A 49 2600 4913 5210 -615 496 720 C ATOM 321 O ASP A 49 64.165 57.765 -4.687 1.00 35.39 O ANISOU 321 O ASP A 49 2742 5218 5487 -713 561 830 O ATOM 322 CB ASP A 49 64.988 55.597 -2.914 1.00 35.01 C ANISOU 322 CB ASP A 49 2499 5259 5545 -533 454 724 C ATOM 323 CG ASP A 49 64.699 54.367 -3.776 1.00 36.75 C ANISOU 323 CG ASP A 49 2735 5524 5703 -346 580 666 C ATOM 324 OD1 ASP A 49 65.608 53.919 -4.510 1.00 40.89 O ANISOU 324 OD1 ASP A 49 3101 6171 6263 -280 704 696 O ATOM 325 OD2 ASP A 49 63.600 53.766 -3.771 1.00 38.57 O ANISOU 325 OD2 ASP A 49 3125 5677 5852 -257 563 579 O ATOM 326 N GLN A 50 62.086 56.932 -4.458 1.00 31.85 N ANISOU 326 N GLN A 50 2561 4641 4902 -534 511 654 N ATOM 327 CA GLN A 50 61.639 57.353 -5.791 1.00 31.98 C ANISOU 327 CA GLN A 50 2656 4665 4828 -533 605 708 C ATOM 328 C GLN A 50 60.721 58.560 -5.768 1.00 31.02 C ANISOU 328 C GLN A 50 2684 4397 4707 -606 519 725 C ATOM 329 O GLN A 50 59.880 58.692 -4.890 1.00 29.31 O ANISOU 329 O GLN A 50 2557 4075 4506 -582 417 631 O ATOM 330 CB GLN A 50 60.870 56.227 -6.471 1.00 31.27 C ANISOU 330 CB GLN A 50 2644 4617 4621 -383 678 626 C ATOM 331 CG GLN A 50 61.593 54.907 -6.517 1.00 33.86 C ANISOU 331 CG GLN A 50 2857 5047 4963 -271 754 577 C ATOM 332 CD GLN A 50 60.693 53.792 -7.006 1.00 35.47 C ANISOU 332 CD GLN A 50 3171 5241 5065 -136 787 471 C ATOM 333 OE1 GLN A 50 59.782 53.359 -6.287 1.00 36.39 O ANISOU 333 OE1 GLN A 50 3382 5268 5178 -102 689 400 O ATOM 334 NE2 GLN A 50 60.927 53.337 -8.231 1.00 38.36 N ANISOU 334 NE2 GLN A 50 3530 5708 5339 -73 924 456 N ATOM 335 N ASP A 51 60.859 59.416 -6.769 1.00 31.53 N ANISOU 335 N ASP A 51 2770 4458 4750 -688 564 848 N ATOM 336 CA ASP A 51 59.903 60.488 -6.994 1.00 31.50 C ANISOU 336 CA ASP A 51 2917 4299 4751 -726 482 881 C ATOM 337 C ASP A 51 58.733 59.965 -7.838 1.00 30.40 C ANISOU 337 C ASP A 51 2891 4182 4476 -606 516 847 C ATOM 338 O ASP A 51 58.927 59.486 -8.954 1.00 30.94 O ANISOU 338 O ASP A 51 2946 4383 4427 -584 627 903 O ATOM 339 CB ASP A 51 60.589 61.675 -7.677 1.00 33.19 C ANISOU 339 CB ASP A 51 3113 4484 5014 -890 487 1063 C ATOM 340 CG ASP A 51 61.561 62.388 -6.754 1.00 33.94 C ANISOU 340 CG ASP A 51 3120 4514 5262 -1036 409 1089 C ATOM 341 OD1 ASP A 51 62.673 62.740 -7.199 1.00 35.74 O ANISOU 341 OD1 ASP A 51 3227 4829 5524 -1173 465 1232 O ATOM 342 OD2 ASP A 51 61.300 62.646 -5.562 1.00 33.03 O ANISOU 342 OD2 ASP A 51 3043 4275 5232 -1038 289 972 O ATOM 343 N ILE A 52 57.527 60.026 -7.284 1.00 29.07 N ANISOU 343 N ILE A 52 2825 3902 4317 -531 423 746 N ATOM 344 CA ILE A 52 56.320 59.623 -8.003 1.00 28.57 C ANISOU 344 CA ILE A 52 2859 3853 4143 -432 425 718 C ATOM 345 C ILE A 52 55.541 60.848 -8.494 1.00 29.47 C ANISOU 345 C ILE A 52 3075 3833 4289 -457 339 807 C ATOM 346 O ILE A 52 55.197 61.727 -7.710 1.00 29.74 O ANISOU 346 O ILE A 52 3144 3708 4449 -469 238 770 O ATOM 347 CB ILE A 52 55.403 58.766 -7.103 1.00 27.07 C ANISOU 347 CB ILE A 52 2689 3655 3941 -328 382 557 C ATOM 348 CG1 ILE A 52 56.160 57.569 -6.511 1.00 26.87 C ANISOU 348 CG1 ILE A 52 2574 3727 3910 -303 436 488 C ATOM 349 CG2 ILE A 52 54.161 58.321 -7.872 1.00 26.59 C ANISOU 349 CG2 ILE A 52 2711 3621 3772 -244 374 535 C ATOM 350 CD1 ILE A 52 57.033 56.792 -7.499 1.00 28.22 C ANISOU 350 CD1 ILE A 52 2684 4031 4009 -285 559 534 C ATOM 351 N THR A 53 55.234 60.878 -9.786 1.00 30.06 N ANISOU 351 N THR A 53 3204 3970 4249 -457 371 916 N ATOM 352 CA THR A 53 54.421 61.941 -10.363 1.00 31.19 C ANISOU 352 CA THR A 53 3446 3989 4418 -467 270 1026 C ATOM 353 C THR A 53 52.936 61.739 -10.048 1.00 30.58 C ANISOU 353 C THR A 53 3421 3851 4346 -335 181 912 C ATOM 354 O THR A 53 52.361 60.691 -10.348 1.00 29.35 O ANISOU 354 O THR A 53 3267 3816 4067 -262 216 839 O ATOM 355 CB THR A 53 54.657 61.985 -11.879 1.00 32.67 C ANISOU 355 CB THR A 53 3668 4299 4445 -530 330 1202 C ATOM 356 OG1 THR A 53 56.037 62.288 -12.136 1.00 33.25 O ANISOU 356 OG1 THR A 53 3667 4442 4523 -666 422 1319 O ATOM 357 CG2 THR A 53 53.886 63.120 -12.539 1.00 34.05 C ANISOU 357 CG2 THR A 53 3946 4340 4650 -552 203 1361 C ATOM 358 N ILE A 54 52.325 62.753 -9.441 1.00 31.60 N ANISOU 358 N ILE A 54 3587 3792 4627 -305 66 892 N ATOM 359 CA ILE A 54 50.902 62.741 -9.117 1.00 31.55 C ANISOU 359 CA ILE A 54 3602 3732 4652 -174 -16 789 C ATOM 360 C ILE A 54 50.065 62.858 -10.401 1.00 32.89 C ANISOU 360 C ILE A 54 3829 3934 4734 -139 -72 922 C ATOM 361 O ILE A 54 50.339 63.696 -11.262 1.00 34.64 O ANISOU 361 O ILE A 54 4107 4091 4963 -207 -117 1109 O ATOM 362 CB ILE A 54 50.549 63.881 -8.118 1.00 32.37 C ANISOU 362 CB ILE A 54 3722 3620 4956 -135 -114 710 C ATOM 363 CG1 ILE A 54 51.272 63.678 -6.777 1.00 32.22 C ANISOU 363 CG1 ILE A 54 3653 3601 4989 -175 -72 559 C ATOM 364 CG2 ILE A 54 49.044 63.941 -7.867 1.00 32.68 C ANISOU 364 CG2 ILE A 54 3755 3624 5036 17 -186 609 C ATOM 365 CD1 ILE A 54 51.492 64.965 -5.989 1.00 34.01 C ANISOU 365 CD1 ILE A 54 3918 3606 5399 -204 -158 509 C ATOM 366 N GLU A 55 49.063 61.991 -10.512 1.00 32.22 N ANISOU 366 N GLU A 55 3726 3956 4558 -51 -79 836 N ATOM 367 CA GLU A 55 48.089 62.016 -11.594 1.00 33.52 C ANISOU 367 CA GLU A 55 3933 4165 4638 -10 -160 936 C ATOM 368 C GLU A 55 46.731 62.418 -11.045 1.00 32.91 C ANISOU 368 C GLU A 55 3818 3998 4690 121 -272 857 C ATOM 369 O GLU A 55 46.468 62.279 -9.854 1.00 31.74 O ANISOU 369 O GLU A 55 3608 3819 4633 179 -250 687 O ATOM 370 CB GLU A 55 47.977 60.631 -12.235 1.00 33.15 C ANISOU 370 CB GLU A 55 3887 4327 4380 -23 -89 892 C ATOM 371 CG GLU A 55 49.306 60.036 -12.677 1.00 35.69 C ANISOU 371 CG GLU A 55 4220 4764 4577 -117 50 918 C ATOM 372 CD GLU A 55 49.210 58.540 -12.900 1.00 38.40 C ANISOU 372 CD GLU A 55 4559 5266 4766 -98 124 794 C ATOM 373 OE1 GLU A 55 48.617 58.132 -13.926 1.00 41.97 O ANISOU 373 OE1 GLU A 55 5067 5818 5061 -100 92 827 O ATOM 374 OE2 GLU A 55 49.710 57.781 -12.045 1.00 37.76 O ANISOU 374 OE2 GLU A 55 4426 5198 4724 -85 199 666 O ATOM 375 N GLU A 56 45.864 62.893 -11.928 1.00 33.76 N ANISOU 375 N GLU A 56 3953 4082 4792 166 -391 983 N ATOM 376 CA GLU A 56 44.518 63.295 -11.550 1.00 33.95 C ANISOU 376 CA GLU A 56 3914 4037 4948 309 -503 922 C ATOM 377 C GLU A 56 43.635 62.065 -11.364 1.00 32.37 C ANISOU 377 C GLU A 56 3634 4025 4642 348 -477 791 C ATOM 378 O GLU A 56 43.655 61.152 -12.187 1.00 31.43 O ANISOU 378 O GLU A 56 3546 4062 4334 281 -456 833 O ATOM 379 CB GLU A 56 43.910 64.206 -12.617 1.00 36.13 C ANISOU 379 CB GLU A 56 4237 4227 5266 344 -663 1130 C ATOM 380 CG GLU A 56 42.715 64.989 -12.106 1.00 37.95 C ANISOU 380 CG GLU A 56 4390 4317 5715 519 -788 1074 C ATOM 381 CD GLU A 56 41.905 65.638 -13.206 1.00 41.06 C ANISOU 381 CD GLU A 56 4803 4661 6138 574 -972 1284 C ATOM 382 OE1 GLU A 56 42.318 65.577 -14.386 1.00 42.07 O ANISOU 382 OE1 GLU A 56 5025 4859 6098 455 -1007 1490 O ATOM 383 OE2 GLU A 56 40.847 66.213 -12.877 1.00 43.44 O ANISOU 383 OE2 GLU A 56 5017 4862 6626 740 -1082 1243 O ATOM 384 N THR A 57 42.863 62.055 -10.279 1.00 32.07 N ANISOU 384 N THR A 57 3494 3972 4721 449 -476 629 N ATOM 385 CA THR A 57 41.890 60.997 -10.019 1.00 31.39 C ANISOU 385 CA THR A 57 3311 4056 4561 476 -465 522 C ATOM 386 C THR A 57 40.784 61.108 -11.057 1.00 32.80 C ANISOU 386 C THR A 57 3459 4289 4715 525 -606 638 C ATOM 387 O THR A 57 40.148 62.148 -11.162 1.00 34.34 O ANISOU 387 O THR A 57 3615 4369 5063 637 -716 698 O ATOM 388 CB THR A 57 41.283 61.136 -8.590 1.00 31.20 C ANISOU 388 CB THR A 57 3167 4021 4667 569 -425 334 C ATOM 389 OG1 THR A 57 42.326 61.149 -7.601 1.00 29.62 O ANISOU 389 OG1 THR A 57 3003 3768 4484 516 -319 235 O ATOM 390 CG2 THR A 57 40.451 59.921 -8.222 1.00 30.37 C ANISOU 390 CG2 THR A 57 2959 4114 4468 550 -391 238 C ATOM 391 N THR A 58 40.581 60.055 -11.845 1.00 32.66 N ANISOU 391 N THR A 58 3465 4435 4510 442 -616 672 N ATOM 392 CA THR A 58 39.460 60.005 -12.793 1.00 34.52 C ANISOU 392 CA THR A 58 3662 4758 4698 468 -765 771 C ATOM 393 C THR A 58 38.854 58.608 -12.869 1.00 34.19 C ANISOU 393 C THR A 58 3572 4904 4514 396 -757 683 C ATOM 394 O THR A 58 39.369 57.657 -12.278 1.00 32.77 O ANISOU 394 O THR A 58 3411 4772 4270 325 -637 562 O ATOM 395 CB THR A 58 39.895 60.429 -14.221 1.00 35.79 C ANISOU 395 CB THR A 58 3957 4909 4734 402 -848 980 C ATOM 396 OG1 THR A 58 40.757 59.431 -14.779 1.00 34.80 O ANISOU 396 OG1 THR A 58 3940 4899 4382 267 -748 962 O ATOM 397 CG2 THR A 58 40.732 61.697 -14.218 1.00 36.53 C ANISOU 397 CG2 THR A 58 4125 4807 4947 420 -847 1094 C ATOM 398 N GLU A 59 37.780 58.495 -13.647 1.00 36.17 N ANISOU 398 N GLU A 59 3769 5252 4721 404 -905 759 N ATOM 399 CA GLU A 59 37.063 57.240 -13.845 1.00 36.39 C ANISOU 399 CA GLU A 59 3751 5450 4625 319 -938 693 C ATOM 400 C GLU A 59 37.940 56.197 -14.527 1.00 35.80 C ANISOU 400 C GLU A 59 3844 5434 4325 177 -871 668 C ATOM 401 O GLU A 59 37.708 54.997 -14.368 1.00 35.54 O ANISOU 401 O GLU A 59 3806 5488 4211 93 -849 562 O ATOM 402 CB GLU A 59 35.809 57.457 -14.705 1.00 38.77 C ANISOU 402 CB GLU A 59 3968 5845 4919 344 -1139 807 C ATOM 403 CG GLU A 59 34.850 58.522 -14.200 1.00 40.93 C ANISOU 403 CG GLU A 59 4057 6063 5431 516 -1225 838 C ATOM 404 CD GLU A 59 35.069 59.874 -14.849 1.00 43.48 C ANISOU 404 CD GLU A 59 4444 6236 5841 611 -1331 1014 C ATOM 405 OE1 GLU A 59 34.363 60.196 -15.830 1.00 46.27 O ANISOU 405 OE1 GLU A 59 4776 6636 6167 627 -1520 1174 O ATOM 406 OE2 GLU A 59 35.951 60.617 -14.371 1.00 44.14 O ANISOU 406 OE2 GLU A 59 4601 6148 6021 657 -1238 1005 O ATOM 407 N THR A 60 38.930 56.661 -15.290 1.00 36.14 N ANISOU 407 N THR A 60 4030 5427 4274 150 -840 765 N ATOM 408 CA THR A 60 39.789 55.794 -16.100 1.00 36.11 C ANISOU 408 CA THR A 60 4180 5496 4045 38 -768 739 C ATOM 409 C THR A 60 41.216 55.660 -15.562 1.00 34.70 C ANISOU 409 C THR A 60 4064 5243 3879 25 -580 672 C ATOM 410 O THR A 60 42.075 55.088 -16.227 1.00 35.01 O ANISOU 410 O THR A 60 4216 5336 3750 -42 -497 650 O ATOM 411 CB THR A 60 39.841 56.324 -17.559 1.00 38.07 C ANISOU 411 CB THR A 60 4537 5808 4122 -7 -867 913 C ATOM 412 OG1 THR A 60 40.312 57.679 -17.580 1.00 38.57 O ANISOU 412 OG1 THR A 60 4610 5752 4293 48 -873 1069 O ATOM 413 CG2 THR A 60 38.444 56.410 -18.163 1.00 40.01 C ANISOU 413 CG2 THR A 60 4716 6142 4343 -2 -1080 995 C ATOM 414 N ALA A 61 41.468 56.154 -14.351 1.00 33.53 N ANISOU 414 N ALA A 61 3834 4984 3922 91 -513 627 N ATOM 415 CA ALA A 61 42.821 56.170 -13.797 1.00 32.22 C ANISOU 415 CA ALA A 61 3707 4747 3787 77 -361 584 C ATOM 416 C ALA A 61 43.190 54.916 -13.006 1.00 30.60 C ANISOU 416 C ALA A 61 3490 4567 3571 46 -262 425 C ATOM 417 O ALA A 61 44.243 54.886 -12.383 1.00 30.22 O ANISOU 417 O ALA A 61 3447 4464 3573 43 -151 387 O ATOM 418 CB ALA A 61 43.011 57.404 -12.921 1.00 32.02 C ANISOU 418 CB ALA A 61 3622 4581 3964 148 -356 617 C ATOM 419 N PHE A 62 42.347 53.886 -13.025 1.00 30.12 N ANISOU 419 N PHE A 62 3410 4579 3454 13 -314 347 N ATOM 420 CA PHE A 62 42.542 52.712 -12.167 1.00 28.60 C ANISOU 420 CA PHE A 62 3204 4384 3281 -22 -250 220 C ATOM 421 C PHE A 62 42.898 51.441 -12.940 1.00 29.05 C ANISOU 421 C PHE A 62 3372 4480 3186 -87 -230 148 C ATOM 422 O PHE A 62 42.976 50.362 -12.358 1.00 28.12 O ANISOU 422 O PHE A 62 3258 4337 3088 -121 -205 53 O ATOM 423 CB PHE A 62 41.287 52.479 -11.309 1.00 28.41 C ANISOU 423 CB PHE A 62 3055 4395 3345 -24 -319 179 C ATOM 424 CG PHE A 62 41.042 53.565 -10.303 1.00 27.75 C ANISOU 424 CG PHE A 62 2858 4270 3417 56 -304 190 C ATOM 425 CD1 PHE A 62 41.689 53.549 -9.079 1.00 26.10 C ANISOU 425 CD1 PHE A 62 2619 4012 3286 63 -209 126 C ATOM 426 CD2 PHE A 62 40.175 54.615 -10.586 1.00 28.61 C ANISOU 426 CD2 PHE A 62 2893 4383 3595 131 -395 258 C ATOM 427 CE1 PHE A 62 41.474 54.551 -8.156 1.00 25.79 C ANISOU 427 CE1 PHE A 62 2491 3937 3372 135 -193 106 C ATOM 428 CE2 PHE A 62 39.961 55.617 -9.666 1.00 27.59 C ANISOU 428 CE2 PHE A 62 2667 4196 3619 224 -377 237 C ATOM 429 CZ PHE A 62 40.613 55.584 -8.450 1.00 27.44 C ANISOU 429 CZ PHE A 62 2633 4136 3658 222 -270 149 C ATOM 430 N GLU A 63 43.124 51.569 -14.245 1.00 30.26 N ANISOU 430 N GLU A 63 3623 4690 3185 -105 -244 192 N ATOM 431 CA GLU A 63 43.444 50.416 -15.086 1.00 31.59 C ANISOU 431 CA GLU A 63 3911 4901 3189 -156 -221 93 C ATOM 432 C GLU A 63 44.770 49.778 -14.645 1.00 30.00 C ANISOU 432 C GLU A 63 3740 4636 3022 -126 -70 1 C ATOM 433 O GLU A 63 45.767 50.470 -14.454 1.00 29.61 O ANISOU 433 O GLU A 63 3664 4567 3018 -86 32 56 O ATOM 434 CB GLU A 63 43.485 50.813 -16.579 1.00 33.64 C ANISOU 434 CB GLU A 63 4270 5267 3243 -185 -251 161 C ATOM 435 CG GLU A 63 42.536 50.016 -17.467 1.00 37.76 C ANISOU 435 CG GLU A 63 4869 5875 3604 -260 -380 101 C ATOM 436 CD GLU A 63 41.082 50.075 -17.009 1.00 41.13 C ANISOU 436 CD GLU A 63 5186 6309 4131 -286 -544 139 C ATOM 437 OE1 GLU A 63 40.446 48.995 -16.906 1.00 43.69 O ANISOU 437 OE1 GLU A 63 5523 6635 4442 -355 -615 34 O ATOM 438 OE2 GLU A 63 40.572 51.195 -16.752 1.00 42.29 O ANISOU 438 OE2 GLU A 63 5229 6457 4382 -237 -605 272 O ATOM 439 N GLY A 64 44.753 48.464 -14.447 1.00 29.57 N ANISOU 439 N GLY A 64 3731 4537 2965 -149 -71 -130 N ATOM 440 CA GLY A 64 45.941 47.724 -14.039 1.00 28.80 C ANISOU 440 CA GLY A 64 3656 4365 2921 -104 48 -219 C ATOM 441 C GLY A 64 46.287 47.828 -12.561 1.00 26.73 C ANISOU 441 C GLY A 64 3289 4017 2850 -79 77 -190 C ATOM 442 O GLY A 64 47.310 47.307 -12.127 1.00 26.37 O ANISOU 442 O GLY A 64 3239 3909 2870 -35 160 -238 O ATOM 443 N VAL A 65 45.431 48.491 -11.783 1.00 25.42 N ANISOU 443 N VAL A 65 3032 3860 2769 -101 7 -117 N ATOM 444 CA VAL A 65 45.637 48.647 -10.350 1.00 23.32 C ANISOU 444 CA VAL A 65 2672 3541 2649 -92 29 -97 C ATOM 445 C VAL A 65 45.038 47.442 -9.612 1.00 23.25 C ANISOU 445 C VAL A 65 2660 3491 2682 -154 -33 -149 C ATOM 446 O VAL A 65 43.909 47.052 -9.870 1.00 23.10 O ANISOU 446 O VAL A 65 2645 3509 2624 -218 -126 -160 O ATOM 447 CB VAL A 65 44.990 49.959 -9.843 1.00 22.91 C ANISOU 447 CB VAL A 65 2523 3522 2659 -77 -3 -18 C ATOM 448 CG1 VAL A 65 45.063 50.064 -8.312 1.00 21.26 C ANISOU 448 CG1 VAL A 65 2225 3286 2568 -80 16 -25 C ATOM 449 CG2 VAL A 65 45.639 51.171 -10.502 1.00 22.08 C ANISOU 449 CG2 VAL A 65 2432 3421 2537 -32 42 58 C ATOM 450 N ASP A 66 45.803 46.853 -8.694 1.00 22.97 N ANISOU 450 N ASP A 66 2613 3384 2732 -147 6 -165 N ATOM 451 CA ASP A 66 45.320 45.725 -7.879 1.00 23.12 C ANISOU 451 CA ASP A 66 2633 3351 2801 -223 -61 -179 C ATOM 452 C ASP A 66 44.669 46.182 -6.584 1.00 22.39 C ANISOU 452 C ASP A 66 2425 3319 2762 -274 -81 -118 C ATOM 453 O ASP A 66 43.646 45.637 -6.166 1.00 23.12 O ANISOU 453 O ASP A 66 2487 3445 2852 -369 -151 -104 O ATOM 454 CB ASP A 66 46.470 44.779 -7.544 1.00 23.44 C ANISOU 454 CB ASP A 66 2723 3274 2910 -187 -28 -211 C ATOM 455 CG ASP A 66 47.168 44.265 -8.780 1.00 24.50 C ANISOU 455 CG ASP A 66 2960 3357 2992 -117 16 -304 C ATOM 456 OD1 ASP A 66 46.563 43.452 -9.502 1.00 24.75 O ANISOU 456 OD1 ASP A 66 3087 3352 2966 -159 -47 -378 O ATOM 457 OD2 ASP A 66 48.317 44.623 -9.109 1.00 24.53 O ANISOU 457 OD2 ASP A 66 2952 3366 3001 -25 117 -318 O ATOM 458 N ILE A 67 45.294 47.152 -5.929 1.00 21.72 N ANISOU 458 N ILE A 67 2276 3256 2719 -222 -18 -88 N ATOM 459 CA ILE A 67 44.813 47.671 -4.658 1.00 21.32 C ANISOU 459 CA ILE A 67 2125 3273 2701 -258 -18 -60 C ATOM 460 C ILE A 67 44.820 49.199 -4.695 1.00 21.01 C ANISOU 460 C ILE A 67 2030 3274 2678 -186 23 -58 C ATOM 461 O ILE A 67 45.789 49.804 -5.143 1.00 20.49 O ANISOU 461 O ILE A 67 1996 3159 2630 -126 68 -48 O ATOM 462 CB ILE A 67 45.699 47.176 -3.487 1.00 21.03 C ANISOU 462 CB ILE A 67 2082 3198 2711 -285 -3 -34 C ATOM 463 CG1 ILE A 67 45.692 45.648 -3.390 1.00 21.84 C ANISOU 463 CG1 ILE A 67 2249 3225 2826 -353 -64 -18 C ATOM 464 CG2 ILE A 67 45.212 47.773 -2.166 1.00 21.53 C ANISOU 464 CG2 ILE A 67 2049 3363 2768 -330 7 -21 C ATOM 465 CD1 ILE A 67 46.822 45.073 -2.547 1.00 22.28 C ANISOU 465 CD1 ILE A 67 2316 3206 2944 -350 -68 25 C ATOM 466 N ALA A 68 43.740 49.805 -4.214 1.00 21.34 N ANISOU 466 N ALA A 68 1982 3400 2725 -192 6 -67 N ATOM 467 CA ALA A 68 43.651 51.253 -4.056 1.00 22.04 C ANISOU 467 CA ALA A 68 2017 3498 2859 -114 31 -80 C ATOM 468 C ALA A 68 43.305 51.590 -2.616 1.00 22.43 C ANISOU 468 C ALA A 68 1977 3620 2926 -132 60 -126 C ATOM 469 O ALA A 68 42.280 51.140 -2.100 1.00 22.77 O ANISOU 469 O ALA A 68 1942 3771 2938 -184 49 -140 O ATOM 470 CB ALA A 68 42.602 51.838 -4.995 1.00 22.54 C ANISOU 470 CB ALA A 68 2049 3594 2922 -65 -21 -67 C ATOM 471 N LEU A 69 44.181 52.352 -1.965 1.00 22.66 N ANISOU 471 N LEU A 69 2159 3415 3035 -146 -118 -11 N ATOM 472 CA LEU A 69 43.916 52.896 -0.648 1.00 22.82 C ANISOU 472 CA LEU A 69 2189 3372 3110 -191 -143 -21 C ATOM 473 C LEU A 69 43.441 54.337 -0.812 1.00 23.82 C ANISOU 473 C LEU A 69 2366 3445 3238 -214 -194 3 C ATOM 474 O LEU A 69 44.218 55.212 -1.205 1.00 24.08 O ANISOU 474 O LEU A 69 2418 3488 3244 -260 -204 81 O ATOM 475 CB LEU A 69 45.183 52.875 0.205 1.00 23.29 C ANISOU 475 CB LEU A 69 2212 3463 3175 -240 -124 37 C ATOM 476 CG LEU A 69 45.908 51.535 0.296 1.00 23.93 C ANISOU 476 CG LEU A 69 2245 3606 3242 -197 -70 37 C ATOM 477 CD1 LEU A 69 47.295 51.715 0.860 1.00 25.99 C ANISOU 477 CD1 LEU A 69 2448 3935 3491 -240 -59 118 C ATOM 478 CD2 LEU A 69 45.118 50.582 1.143 1.00 24.51 C ANISOU 478 CD2 LEU A 69 2335 3625 3354 -170 -59 -41 C ATOM 479 N PHE A 70 42.171 54.577 -0.515 1.00 23.66 N ANISOU 479 N PHE A 70 2372 3371 3246 -180 -223 -59 N ATOM 480 CA PHE A 70 41.622 55.927 -0.546 1.00 24.60 C ANISOU 480 CA PHE A 70 2554 3425 3367 -175 -269 -43 C ATOM 481 C PHE A 70 41.973 56.659 0.752 1.00 25.27 C ANISOU 481 C PHE A 70 2680 3441 3481 -230 -281 -32 C ATOM 482 O PHE A 70 41.944 56.071 1.832 1.00 25.50 O ANISOU 482 O PHE A 70 2682 3467 3540 -242 -262 -72 O ATOM 483 CB PHE A 70 40.105 55.883 -0.736 1.00 24.35 C ANISOU 483 CB PHE A 70 2520 3385 3348 -98 -294 -113 C ATOM 484 CG PHE A 70 39.667 55.715 -2.171 1.00 24.20 C ANISOU 484 CG PHE A 70 2492 3421 3284 -49 -311 -111 C ATOM 485 CD1 PHE A 70 40.077 54.617 -2.915 1.00 24.16 C ANISOU 485 CD1 PHE A 70 2449 3485 3247 -53 -282 -121 C ATOM 486 CD2 PHE A 70 38.825 56.648 -2.770 1.00 24.62 C ANISOU 486 CD2 PHE A 70 2584 3455 3317 11 -359 -102 C ATOM 487 CE1 PHE A 70 39.671 54.457 -4.232 1.00 24.53 C ANISOU 487 CE1 PHE A 70 2498 3583 3239 -11 -302 -126 C ATOM 488 CE2 PHE A 70 38.413 56.490 -4.085 1.00 24.48 C ANISOU 488 CE2 PHE A 70 2557 3497 3246 56 -383 -98 C ATOM 489 CZ PHE A 70 38.830 55.390 -4.815 1.00 24.09 C ANISOU 489 CZ PHE A 70 2470 3519 3162 39 -356 -114 C ATOM 490 N SER A 71 42.293 57.942 0.638 1.00 26.24 N ANISOU 490 N SER A 71 2882 3501 3587 -266 -315 23 N ATOM 491 CA SER A 71 42.676 58.762 1.778 1.00 26.96 C ANISOU 491 CA SER A 71 3039 3514 3692 -332 -336 33 C ATOM 492 C SER A 71 42.182 60.199 1.599 1.00 27.80 C ANISOU 492 C SER A 71 3272 3508 3785 -315 -382 50 C ATOM 493 O SER A 71 42.785 61.130 2.113 1.00 28.58 O ANISOU 493 O SER A 71 3458 3527 3873 -396 -408 86 O ATOM 494 CB SER A 71 44.199 58.731 1.971 1.00 27.66 C ANISOU 494 CB SER A 71 3097 3648 3763 -448 -328 106 C ATOM 495 OG SER A 71 44.891 59.296 0.866 1.00 29.40 O ANISOU 495 OG SER A 71 3334 3893 3945 -495 -335 193 O ATOM 496 N ALA A 72 41.082 60.362 0.865 1.00 27.58 N ANISOU 496 N ALA A 72 3258 3471 3750 -208 -395 25 N ATOM 497 CA ALA A 72 40.497 61.670 0.615 1.00 28.41 C ANISOU 497 CA ALA A 72 3488 3469 3837 -155 -437 43 C ATOM 498 C ALA A 72 39.200 61.788 1.423 1.00 28.10 C ANISOU 498 C ALA A 72 3462 3392 3824 -43 -440 -43 C ATOM 499 O ALA A 72 39.150 61.343 2.578 1.00 27.74 O ANISOU 499 O ALA A 72 3384 3350 3805 -61 -417 -98 O ATOM 500 CB ALA A 72 40.265 61.865 -0.871 1.00 28.95 C ANISOU 500 CB ALA A 72 3562 3571 3866 -104 -453 93 C ATOM 501 N GLY A 73 38.173 62.400 0.841 1.00 28.54 N ANISOU 501 N GLY A 73 3560 3421 3864 78 -467 -49 N ATOM 502 CA GLY A 73 36.885 62.552 1.503 1.00 28.39 C ANISOU 502 CA GLY A 73 3534 3391 3860 205 -466 -124 C ATOM 503 C GLY A 73 35.816 61.667 0.885 1.00 27.88 C ANISOU 503 C GLY A 73 3329 3461 3803 293 -460 -165 C ATOM 504 O GLY A 73 36.059 60.954 -0.100 1.00 26.42 O ANISOU 504 O GLY A 73 3072 3362 3606 259 -461 -142 O ATOM 505 N SER A 74 34.636 61.717 1.497 1.00 27.84 N ANISOU 505 N SER A 74 3286 3481 3812 402 -452 -228 N ATOM 506 CA SER A 74 33.461 60.943 1.088 1.00 28.24 C ANISOU 506 CA SER A 74 3192 3671 3869 478 -451 -273 C ATOM 507 C SER A 74 33.091 61.104 -0.378 1.00 28.53 C ANISOU 507 C SER A 74 3209 3762 3867 538 -500 -233 C ATOM 508 O SER A 74 32.742 60.130 -1.033 1.00 27.99 O ANISOU 508 O SER A 74 3025 3815 3796 518 -504 -254 O ATOM 509 CB SER A 74 32.246 61.348 1.939 1.00 28.89 C ANISOU 509 CB SER A 74 3251 3767 3959 607 -439 -329 C ATOM 510 OG SER A 74 32.340 60.769 3.225 1.00 29.76 O ANISOU 510 OG SER A 74 3325 3883 4099 548 -386 -380 O ATOM 511 N SER A 75 33.157 62.331 -0.884 1.00 29.47 N ANISOU 511 N SER A 75 3457 3789 3951 610 -538 -174 N ATOM 512 CA SER A 75 32.754 62.604 -2.256 1.00 30.36 C ANISOU 512 CA SER A 75 3567 3952 4016 685 -589 -127 C ATOM 513 C SER A 75 33.666 61.872 -3.237 1.00 29.40 C ANISOU 513 C SER A 75 3417 3881 3872 567 -588 -89 C ATOM 514 O SER A 75 33.182 61.296 -4.208 1.00 29.14 O ANISOU 514 O SER A 75 3299 3964 3808 593 -613 -95 O ATOM 515 CB SER A 75 32.696 64.118 -2.544 1.00 31.85 C ANISOU 515 CB SER A 75 3927 4007 4166 788 -628 -62 C ATOM 516 OG SER A 75 33.981 64.723 -2.476 1.00 33.62 O ANISOU 516 OG SER A 75 4300 4090 4382 673 -621 0 O ATOM 517 N THR A 76 34.972 61.867 -2.956 1.00 28.77 N ANISOU 517 N THR A 76 3402 3729 3802 439 -557 -53 N ATOM 518 CA THR A 76 35.954 61.141 -3.774 1.00 28.32 C ANISOU 518 CA THR A 76 3312 3728 3720 334 -541 -15 C ATOM 519 C THR A 76 35.740 59.622 -3.762 1.00 27.02 C ANISOU 519 C THR A 76 3007 3686 3575 297 -512 -86 C ATOM 520 O THR A 76 35.930 58.972 -4.784 1.00 26.50 O ANISOU 520 O THR A 76 2902 3698 3470 278 -516 -78 O ATOM 521 CB THR A 76 37.405 61.467 -3.322 1.00 28.16 C ANISOU 521 CB THR A 76 3369 3623 3707 206 -511 41 C ATOM 522 OG1 THR A 76 37.694 62.847 -3.564 1.00 30.03 O ANISOU 522 OG1 THR A 76 3755 3742 3914 213 -542 118 O ATOM 523 CG2 THR A 76 38.435 60.731 -4.180 1.00 28.45 C ANISOU 523 CG2 THR A 76 3359 3739 3711 119 -485 85 C ATOM 524 N SER A 77 35.359 59.064 -2.612 1.00 26.22 N ANISOU 524 N SER A 77 2845 3592 3528 284 -483 -156 N ATOM 525 CA SER A 77 35.089 57.627 -2.500 1.00 25.70 C ANISOU 525 CA SER A 77 2665 3620 3481 241 -455 -222 C ATOM 526 C SER A 77 33.797 57.229 -3.207 1.00 25.98 C ANISOU 526 C SER A 77 2614 3761 3496 308 -494 -267 C ATOM 527 O SER A 77 33.750 56.219 -3.902 1.00 25.83 O ANISOU 527 O SER A 77 2540 3818 3454 267 -496 -295 O ATOM 528 CB SER A 77 35.008 57.194 -1.040 1.00 25.17 C ANISOU 528 CB SER A 77 2565 3528 3469 205 -412 -273 C ATOM 529 OG SER A 77 36.244 57.387 -0.378 1.00 26.66 O ANISOU 529 OG SER A 77 2818 3641 3672 129 -383 -236 O ATOM 530 N ALA A 78 32.747 58.018 -3.004 1.00 26.74 N ANISOU 530 N ALA A 78 2698 3866 3594 413 -526 -276 N ATOM 531 CA ALA A 78 31.440 57.766 -3.604 1.00 27.33 C ANISOU 531 CA ALA A 78 2672 4065 3648 484 -571 -312 C ATOM 532 C ALA A 78 31.536 57.795 -5.125 1.00 27.85 C ANISOU 532 C ALA A 78 2755 4182 3643 501 -623 -274 C ATOM 533 O ALA A 78 30.929 56.969 -5.818 1.00 28.14 O ANISOU 533 O ALA A 78 2706 4335 3653 483 -653 -315 O ATOM 534 CB ALA A 78 30.442 58.804 -3.124 1.00 28.37 C ANISOU 534 CB ALA A 78 2798 4194 3785 622 -592 -311 C ATOM 535 N LYS A 79 32.326 58.737 -5.630 1.00 27.87 N ANISOU 535 N LYS A 79 2879 4097 3612 523 -633 -194 N ATOM 536 CA LYS A 79 32.452 58.964 -7.064 1.00 28.99 C ANISOU 536 CA LYS A 79 3059 4281 3677 552 -679 -142 C ATOM 537 C LYS A 79 33.400 57.981 -7.750 1.00 28.09 C ANISOU 537 C LYS A 79 2945 4198 3529 446 -651 -144 C ATOM 538 O LYS A 79 33.103 57.517 -8.845 1.00 28.63 O ANISOU 538 O LYS A 79 2986 4358 3533 456 -687 -154 O ATOM 539 CB LYS A 79 32.891 60.414 -7.347 1.00 30.07 C ANISOU 539 CB LYS A 79 3338 4306 3783 615 -698 -45 C ATOM 540 CG LYS A 79 31.723 61.409 -7.349 1.00 32.46 C ANISOU 540 CG LYS A 79 3652 4608 4072 775 -753 -33 C ATOM 541 CD LYS A 79 32.136 62.826 -6.960 1.00 34.61 C ANISOU 541 CD LYS A 79 4090 4713 4346 827 -751 39 C ATOM 542 CE LYS A 79 30.966 63.793 -7.129 1.00 37.59 C ANISOU 542 CE LYS A 79 4494 5092 4696 1018 -807 57 C ATOM 543 NZ LYS A 79 31.089 64.995 -6.252 1.00 39.88 N ANISOU 543 NZ LYS A 79 4936 5208 5009 1083 -793 83 N ATOM 544 N TYR A 80 34.535 57.661 -7.128 1.00 26.74 N ANISOU 544 N TYR A 80 2807 3960 3394 354 -587 -134 N ATOM 545 CA TYR A 80 35.584 56.932 -7.843 1.00 26.30 C ANISOU 545 CA TYR A 80 2768 3931 3295 283 -553 -116 C ATOM 546 C TYR A 80 35.832 55.485 -7.415 1.00 25.51 C ANISOU 546 C TYR A 80 2606 3863 3224 210 -506 -190 C ATOM 547 O TYR A 80 36.345 54.700 -8.210 1.00 25.67 O ANISOU 547 O TYR A 80 2633 3930 3193 184 -488 -199 O ATOM 548 CB TYR A 80 36.881 57.737 -7.829 1.00 26.29 C ANISOU 548 CB TYR A 80 2856 3851 3283 241 -520 -20 C ATOM 549 CG TYR A 80 36.726 59.050 -8.555 1.00 27.49 C ANISOU 549 CG TYR A 80 3096 3965 3384 302 -566 63 C ATOM 550 CD1 TYR A 80 36.501 59.086 -9.930 1.00 28.76 C ANISOU 550 CD1 TYR A 80 3273 4198 3457 348 -602 95 C ATOM 551 CD2 TYR A 80 36.748 60.257 -7.863 1.00 27.59 C ANISOU 551 CD2 TYR A 80 3191 3863 3430 320 -578 109 C ATOM 552 CE1 TYR A 80 36.334 60.300 -10.596 1.00 30.35 C ANISOU 552 CE1 TYR A 80 3567 4359 3605 412 -646 181 C ATOM 553 CE2 TYR A 80 36.583 61.464 -8.518 1.00 28.86 C ANISOU 553 CE2 TYR A 80 3456 3968 3541 382 -621 190 C ATOM 554 CZ TYR A 80 36.384 61.483 -9.874 1.00 29.99 C ANISOU 554 CZ TYR A 80 3611 4185 3599 429 -653 231 C ATOM 555 OH TYR A 80 36.221 62.690 -10.501 1.00 32.85 O ANISOU 555 OH TYR A 80 4090 4485 3908 495 -696 320 O ATOM 556 N ALA A 81 35.472 55.124 -6.188 1.00 24.82 N ANISOU 556 N ALA A 81 2472 3748 3209 186 -483 -243 N ATOM 557 CA ALA A 81 35.647 53.743 -5.721 1.00 24.01 C ANISOU 557 CA ALA A 81 2327 3661 3134 119 -440 -308 C ATOM 558 C ALA A 81 34.884 52.717 -6.568 1.00 24.09 C ANISOU 558 C ALA A 81 2297 3753 3101 109 -470 -378 C ATOM 559 O ALA A 81 35.414 51.645 -6.823 1.00 23.82 O ANISOU 559 O ALA A 81 2282 3722 3046 64 -436 -409 O ATOM 560 CB ALA A 81 35.261 53.598 -4.245 1.00 23.55 C ANISOU 560 CB ALA A 81 2230 3564 3155 96 -413 -346 C ATOM 561 N PRO A 82 33.644 53.008 -6.971 1.00 24.59 N ANISOU 561 N PRO A 82 2309 3885 3147 151 -534 -404 N ATOM 562 CA PRO A 82 32.902 52.086 -7.846 1.00 25.36 C ANISOU 562 CA PRO A 82 2369 4073 3194 124 -577 -471 C ATOM 563 C PRO A 82 33.569 51.855 -9.205 1.00 25.47 C ANISOU 563 C PRO A 82 2453 4111 3113 131 -587 -453 C ATOM 564 O PRO A 82 33.545 50.731 -9.697 1.00 26.07 O ANISOU 564 O PRO A 82 2543 4214 3149 80 -587 -517 O ATOM 565 CB PRO A 82 31.538 52.766 -7.985 1.00 26.03 C ANISOU 565 CB PRO A 82 2373 4242 3274 186 -651 -477 C ATOM 566 CG PRO A 82 31.437 53.595 -6.763 1.00 25.34 C ANISOU 566 CG PRO A 82 2271 4097 3262 228 -621 -448 C ATOM 567 CD PRO A 82 32.813 54.167 -6.604 1.00 24.85 C ANISOU 567 CD PRO A 82 2314 3925 3205 229 -573 -378 C ATOM 568 N TYR A 83 34.171 52.891 -9.779 1.00 25.73 N ANISOU 568 N TYR A 83 2542 4129 3105 191 -592 -367 N ATOM 569 CA TYR A 83 34.919 52.754 -11.029 1.00 26.20 C ANISOU 569 CA TYR A 83 2669 4218 3067 202 -587 -337 C ATOM 570 C TYR A 83 36.206 51.941 -10.849 1.00 25.65 C ANISOU 570 C TYR A 83 2644 4105 2998 157 -501 -338 C ATOM 571 O TYR A 83 36.614 51.234 -11.766 1.00 25.72 O ANISOU 571 O TYR A 83 2696 4150 2926 158 -486 -361 O ATOM 572 CB TYR A 83 35.222 54.130 -11.638 1.00 26.66 C ANISOU 572 CB TYR A 83 2778 4270 3081 268 -609 -231 C ATOM 573 CG TYR A 83 33.995 54.800 -12.223 1.00 28.10 C ANISOU 573 CG TYR A 83 2934 4519 3225 341 -701 -226 C ATOM 574 CD1 TYR A 83 33.503 54.442 -13.481 1.00 28.81 C ANISOU 574 CD1 TYR A 83 3025 4708 3211 362 -761 -252 C ATOM 575 CD2 TYR A 83 33.310 55.770 -11.505 1.00 27.83 C ANISOU 575 CD2 TYR A 83 2872 4451 3249 399 -731 -200 C ATOM 576 CE1 TYR A 83 32.363 55.061 -14.014 1.00 30.10 C ANISOU 576 CE1 TYR A 83 3151 4951 3334 438 -853 -241 C ATOM 577 CE2 TYR A 83 32.176 56.392 -12.019 1.00 29.50 C ANISOU 577 CE2 TYR A 83 3050 4734 3423 490 -815 -190 C ATOM 578 CZ TYR A 83 31.700 56.035 -13.268 1.00 31.00 C ANISOU 578 CZ TYR A 83 3229 5037 3514 508 -879 -207 C ATOM 579 OH TYR A 83 30.572 56.665 -13.758 1.00 31.73 O ANISOU 579 OH TYR A 83 3277 5216 3565 608 -969 -191 O ATOM 580 N ALA A 84 36.833 52.028 -9.670 1.00 24.62 N ANISOU 580 N ALA A 84 2503 3902 2950 129 -445 -314 N ATOM 581 CA ALA A 84 37.997 51.197 -9.370 1.00 23.99 C ANISOU 581 CA ALA A 84 2447 3793 2874 100 -367 -314 C ATOM 582 C ALA A 84 37.598 49.727 -9.327 1.00 24.00 C ANISOU 582 C ALA A 84 2452 3794 2872 68 -357 -417 C ATOM 583 O ALA A 84 38.299 48.883 -9.880 1.00 24.03 O ANISOU 583 O ALA A 84 2507 3805 2819 77 -315 -436 O ATOM 584 CB ALA A 84 38.647 51.615 -8.052 1.00 23.58 C ANISOU 584 CB ALA A 84 2376 3675 2908 73 -324 -269 C ATOM 585 N VAL A 85 36.460 49.427 -8.695 1.00 24.01 N ANISOU 585 N VAL A 85 2405 3788 2927 30 -394 -482 N ATOM 586 CA VAL A 85 35.948 48.051 -8.614 1.00 24.50 C ANISOU 586 CA VAL A 85 2479 3841 2988 -26 -393 -579 C ATOM 587 C VAL A 85 35.659 47.495 -10.016 1.00 25.73 C ANISOU 587 C VAL A 85 2686 4052 3039 -23 -434 -631 C ATOM 588 O VAL A 85 35.937 46.335 -10.299 1.00 25.92 O ANISOU 588 O VAL A 85 2780 4045 3023 -48 -407 -692 O ATOM 589 CB VAL A 85 34.670 47.954 -7.722 1.00 24.60 C ANISOU 589 CB VAL A 85 2414 3861 3073 -81 -429 -628 C ATOM 590 CG1 VAL A 85 34.064 46.558 -7.771 1.00 25.25 C ANISOU 590 CG1 VAL A 85 2516 3936 3143 -166 -437 -723 C ATOM 591 CG2 VAL A 85 34.990 48.320 -6.277 1.00 23.99 C ANISOU 591 CG2 VAL A 85 2306 3723 3087 -86 -380 -589 C ATOM 592 N LYS A 86 35.104 48.332 -10.883 1.00 26.82 N ANISOU 592 N LYS A 86 2801 4267 3124 14 -501 -606 N ATOM 593 CA LYS A 86 34.784 47.942 -12.251 1.00 28.37 C ANISOU 593 CA LYS A 86 3043 4530 3206 20 -552 -651 C ATOM 594 C LYS A 86 36.046 47.655 -13.068 1.00 28.44 C ANISOU 594 C LYS A 86 3149 4530 3128 69 -490 -626 C ATOM 595 O LYS A 86 36.025 46.839 -13.985 1.00 28.83 O ANISOU 595 O LYS A 86 3271 4600 3082 64 -502 -691 O ATOM 596 CB LYS A 86 33.981 49.046 -12.923 1.00 29.10 C ANISOU 596 CB LYS A 86 3085 4713 3260 67 -638 -610 C ATOM 597 CG LYS A 86 33.441 48.679 -14.291 1.00 32.05 C ANISOU 597 CG LYS A 86 3492 5175 3509 66 -711 -661 C ATOM 598 CD LYS A 86 32.339 49.642 -14.726 1.00 35.15 C ANISOU 598 CD LYS A 86 3808 5669 3879 109 -811 -631 C ATOM 599 CE LYS A 86 32.832 50.641 -15.778 1.00 37.75 C ANISOU 599 CE LYS A 86 4192 6036 4114 202 -826 -538 C ATOM 600 NZ LYS A 86 32.602 50.143 -17.170 1.00 38.66 N ANISOU 600 NZ LYS A 86 4363 6241 4086 202 -885 -585 N ATOM 601 N ALA A 87 37.135 48.339 -12.723 1.00 27.95 N ANISOU 601 N ALA A 87 3086 4441 3093 112 -425 -531 N ATOM 602 CA ALA A 87 38.428 48.163 -13.382 1.00 28.01 C ANISOU 602 CA ALA A 87 3158 4461 3025 164 -352 -488 C ATOM 603 C ALA A 87 39.246 46.973 -12.852 1.00 27.69 C ANISOU 603 C ALA A 87 3159 4359 3001 164 -269 -529 C ATOM 604 O ALA A 87 40.336 46.702 -13.355 1.00 28.26 O ANISOU 604 O ALA A 87 3277 4454 3007 222 -200 -499 O ATOM 605 CB ALA A 87 39.237 49.442 -13.260 1.00 27.61 C ANISOU 605 CB ALA A 87 3077 4424 2991 193 -323 -360 C ATOM 606 N GLY A 88 38.733 46.273 -11.841 1.00 27.20 N ANISOU 606 N GLY A 88 3084 4228 3024 108 -273 -592 N ATOM 607 CA GLY A 88 39.380 45.078 -11.307 1.00 26.70 C ANISOU 607 CA GLY A 88 3078 4092 2975 114 -202 -633 C ATOM 608 C GLY A 88 40.133 45.282 -10.003 1.00 25.65 C ANISOU 608 C GLY A 88 2893 3915 2939 117 -144 -568 C ATOM 609 O GLY A 88 40.834 44.374 -9.553 1.00 25.66 O ANISOU 609 O GLY A 88 2937 3864 2946 145 -80 -582 O ATOM 610 N VAL A 89 39.966 46.452 -9.384 1.00 24.86 N ANISOU 610 N VAL A 89 2709 3830 2908 94 -170 -500 N ATOM 611 CA VAL A 89 40.693 46.827 -8.165 1.00 23.96 C ANISOU 611 CA VAL A 89 2546 3685 2875 87 -126 -434 C ATOM 612 C VAL A 89 39.993 46.300 -6.910 1.00 23.41 C ANISOU 612 C VAL A 89 2458 3544 2893 30 -134 -485 C ATOM 613 O VAL A 89 38.784 46.087 -6.911 1.00 23.93 O ANISOU 613 O VAL A 89 2517 3601 2974 -18 -185 -551 O ATOM 614 CB VAL A 89 40.822 48.379 -8.043 1.00 23.51 C ANISOU 614 CB VAL A 89 2431 3659 2843 80 -154 -342 C ATOM 615 CG1 VAL A 89 41.661 48.777 -6.845 1.00 23.41 C ANISOU 615 CG1 VAL A 89 2378 3619 2900 61 -116 -277 C ATOM 616 CG2 VAL A 89 41.405 48.995 -9.310 1.00 23.77 C ANISOU 616 CG2 VAL A 89 2484 3764 2785 122 -149 -280 C ATOM 617 N VAL A 90 40.762 46.083 -5.844 1.00 22.81 N ANISOU 617 N VAL A 90 2369 3430 2869 33 -83 -449 N ATOM 618 CA VAL A 90 40.208 45.965 -4.504 1.00 22.14 C ANISOU 618 CA VAL A 90 2254 3289 2868 -21 -88 -468 C ATOM 619 C VAL A 90 40.514 47.276 -3.785 1.00 21.23 C ANISOU 619 C VAL A 90 2077 3189 2801 -30 -99 -391 C ATOM 620 O VAL A 90 41.675 47.668 -3.687 1.00 21.08 O ANISOU 620 O VAL A 90 2045 3193 2772 -6 -68 -319 O ATOM 621 CB VAL A 90 40.805 44.788 -3.699 1.00 22.28 C ANISOU 621 CB VAL A 90 2315 3245 2904 -12 -30 -480 C ATOM 622 CG1 VAL A 90 40.024 44.608 -2.377 1.00 22.17 C ANISOU 622 CG1 VAL A 90 2278 3178 2966 -79 -37 -505 C ATOM 623 CG2 VAL A 90 40.768 43.511 -4.502 1.00 23.50 C ANISOU 623 CG2 VAL A 90 2566 3366 2997 12 -10 -549 C ATOM 624 N VAL A 91 39.462 47.937 -3.307 1.00 20.68 N ANISOU 624 N VAL A 91 1970 3111 2776 -65 -144 -410 N ATOM 625 CA VAL A 91 39.528 49.242 -2.661 1.00 20.18 C ANISOU 625 CA VAL A 91 1874 3043 2751 -70 -164 -355 C ATOM 626 C VAL A 91 39.476 49.071 -1.148 1.00 19.66 C ANISOU 626 C VAL A 91 1790 2930 2748 -103 -142 -362 C ATOM 627 O VAL A 91 38.633 48.337 -0.621 1.00 19.46 O ANISOU 627 O VAL A 91 1757 2887 2750 -131 -137 -421 O ATOM 628 CB VAL A 91 38.320 50.153 -3.081 1.00 20.46 C ANISOU 628 CB VAL A 91 1887 3100 2787 -58 -227 -372 C ATOM 629 CG1 VAL A 91 38.302 51.456 -2.282 1.00 19.83 C ANISOU 629 CG1 VAL A 91 1799 2988 2745 -54 -243 -326 C ATOM 630 CG2 VAL A 91 38.350 50.463 -4.558 1.00 20.58 C ANISOU 630 CG2 VAL A 91 1923 3165 2730 -23 -257 -355 C ATOM 631 N VAL A 92 40.396 49.731 -0.455 1.00 19.65 N ANISOU 631 N VAL A 92 1786 2917 2763 -110 -128 -299 N ATOM 632 CA VAL A 92 40.300 49.919 0.984 1.00 19.62 C ANISOU 632 CA VAL A 92 1772 2874 2808 -140 -120 -300 C ATOM 633 C VAL A 92 39.932 51.385 1.182 1.00 20.18 C ANISOU 633 C VAL A 92 1848 2929 2892 -139 -162 -278 C ATOM 634 O VAL A 92 40.718 52.266 0.854 1.00 20.10 O ANISOU 634 O VAL A 92 1856 2919 2861 -146 -176 -216 O ATOM 635 CB VAL A 92 41.620 49.573 1.703 1.00 19.42 C ANISOU 635 CB VAL A 92 1747 2849 2783 -151 -84 -249 C ATOM 636 CG1 VAL A 92 41.457 49.718 3.218 1.00 18.46 C ANISOU 636 CG1 VAL A 92 1623 2691 2700 -183 -80 -256 C ATOM 637 CG2 VAL A 92 42.086 48.156 1.342 1.00 19.13 C ANISOU 637 CG2 VAL A 92 1725 2823 2723 -121 -40 -264 C ATOM 638 N ASP A 93 38.721 51.648 1.665 1.00 21.26 N ANISOU 638 N ASP A 93 1971 3052 3055 -130 -179 -327 N ATOM 639 CA ASP A 93 38.229 53.022 1.782 1.00 22.42 C ANISOU 639 CA ASP A 93 2137 3174 3206 -101 -217 -314 C ATOM 640 C ASP A 93 38.368 53.533 3.196 1.00 22.64 C ANISOU 640 C ASP A 93 2189 3153 3260 -120 -206 -313 C ATOM 641 O ASP A 93 38.050 52.829 4.150 1.00 23.11 O ANISOU 641 O ASP A 93 2225 3215 3342 -137 -175 -350 O ATOM 642 CB ASP A 93 36.763 53.140 1.359 1.00 23.09 C ANISOU 642 CB ASP A 93 2185 3294 3293 -53 -245 -365 C ATOM 643 CG ASP A 93 36.290 54.592 1.301 1.00 25.13 C ANISOU 643 CG ASP A 93 2479 3523 3545 9 -284 -345 C ATOM 644 OD1 ASP A 93 37.071 55.475 0.860 1.00 26.86 O ANISOU 644 OD1 ASP A 93 2763 3700 3742 9 -305 -284 O ATOM 645 OD2 ASP A 93 35.168 54.958 1.695 1.00 27.55 O ANISOU 645 OD2 ASP A 93 2757 3844 3865 62 -295 -382 O ATOM 646 N ASN A 94 38.793 54.784 3.310 1.00 23.07 N ANISOU 646 N ASN A 94 2303 3157 3305 -120 -234 -272 N ATOM 647 CA ASN A 94 39.065 55.415 4.592 1.00 23.36 C ANISOU 647 CA ASN A 94 2387 3138 3352 -145 -234 -270 C ATOM 648 C ASN A 94 37.852 56.112 5.195 1.00 23.32 C ANISOU 648 C ASN A 94 2405 3099 3355 -80 -242 -320 C ATOM 649 O ASN A 94 37.805 56.320 6.407 1.00 23.90 O ANISOU 649 O ASN A 94 2509 3139 3433 -89 -228 -344 O ATOM 650 CB ASN A 94 40.192 56.437 4.431 1.00 24.14 C ANISOU 650 CB ASN A 94 2556 3190 3428 -197 -264 -201 C ATOM 651 CG ASN A 94 39.787 57.622 3.560 1.00 25.75 C ANISOU 651 CG ASN A 94 2825 3346 3613 -154 -305 -178 C ATOM 652 OD1 ASN A 94 39.490 57.466 2.365 1.00 27.02 O ANISOU 652 OD1 ASN A 94 2960 3548 3759 -116 -313 -165 O ATOM 653 ND2 ASN A 94 39.754 58.810 4.158 1.00 28.37 N ANISOU 653 ND2 ASN A 94 3256 3585 3938 -156 -332 -173 N ATOM 654 N THR A 95 36.879 56.476 4.360 1.00 22.90 N ANISOU 654 N THR A 95 2337 3066 3297 -5 -264 -336 N ATOM 655 CA THR A 95 35.780 57.335 4.800 1.00 22.79 C ANISOU 655 CA THR A 95 2348 3028 3283 85 -274 -372 C ATOM 656 C THR A 95 34.648 56.517 5.387 1.00 22.58 C ANISOU 656 C THR A 95 2223 3080 3276 115 -237 -435 C ATOM 657 O THR A 95 34.671 55.292 5.348 1.00 22.09 O ANISOU 657 O THR A 95 2089 3077 3228 56 -211 -450 O ATOM 658 CB THR A 95 35.240 58.222 3.635 1.00 23.35 C ANISOU 658 CB THR A 95 2448 3093 3332 171 -321 -348 C ATOM 659 OG1 THR A 95 34.481 57.436 2.698 1.00 22.49 O ANISOU 659 OG1 THR A 95 2235 3089 3222 198 -328 -367 O ATOM 660 CG2 THR A 95 36.377 58.810 2.812 1.00 23.05 C ANISOU 660 CG2 THR A 95 2491 2997 3269 120 -351 -273 C ATOM 661 N SER A 96 33.646 57.219 5.899 1.00 22.88 N ANISOU 661 N SER A 96 2265 3119 3309 208 -234 -468 N ATOM 662 CA SER A 96 32.439 56.604 6.427 1.00 23.31 C ANISOU 662 CA SER A 96 2211 3269 3375 243 -197 -521 C ATOM 663 C SER A 96 31.455 56.157 5.347 1.00 23.44 C ANISOU 663 C SER A 96 2115 3398 3394 277 -220 -533 C ATOM 664 O SER A 96 30.472 55.476 5.658 1.00 23.20 O ANISOU 664 O SER A 96 1972 3470 3374 275 -192 -571 O ATOM 665 CB SER A 96 31.718 57.600 7.333 1.00 24.46 C ANISOU 665 CB SER A 96 2397 3391 3504 352 -180 -550 C ATOM 666 OG SER A 96 31.279 58.726 6.581 1.00 25.57 O ANISOU 666 OG SER A 96 2585 3505 3625 471 -225 -535 O ATOM 667 N TYR A 97 31.708 56.544 4.095 1.00 23.06 N ANISOU 667 N TYR A 97 2094 3338 3329 300 -273 -498 N ATOM 668 CA TYR A 97 30.709 56.413 3.034 1.00 23.59 C ANISOU 668 CA TYR A 97 2069 3512 3383 355 -311 -507 C ATOM 669 C TYR A 97 30.145 55.002 2.834 1.00 23.41 C ANISOU 669 C TYR A 97 1920 3602 3373 270 -298 -546 C ATOM 670 O TYR A 97 28.929 54.841 2.678 1.00 23.88 O ANISOU 670 O TYR A 97 1864 3780 3428 309 -309 -576 O ATOM 671 CB TYR A 97 31.231 56.944 1.683 1.00 23.44 C ANISOU 671 CB TYR A 97 2113 3460 3332 377 -369 -456 C ATOM 672 CG TYR A 97 30.095 57.105 0.693 1.00 24.56 C ANISOU 672 CG TYR A 97 2172 3712 3447 466 -420 -462 C ATOM 673 CD1 TYR A 97 29.210 58.175 0.799 1.00 25.30 C ANISOU 673 CD1 TYR A 97 2265 3821 3526 615 -441 -457 C ATOM 674 CD2 TYR A 97 29.860 56.157 -0.300 1.00 24.64 C ANISOU 674 CD2 TYR A 97 2103 3819 3441 407 -448 -476 C ATOM 675 CE1 TYR A 97 28.139 58.323 -0.082 1.00 26.24 C ANISOU 675 CE1 TYR A 97 2292 4064 3616 708 -494 -457 C ATOM 676 CE2 TYR A 97 28.787 56.291 -1.186 1.00 25.52 C ANISOU 676 CE2 TYR A 97 2128 4050 3520 481 -505 -483 C ATOM 677 CZ TYR A 97 27.937 57.378 -1.071 1.00 26.70 C ANISOU 677 CZ TYR A 97 2261 4227 3656 633 -529 -469 C ATOM 678 OH TYR A 97 26.882 57.530 -1.935 1.00 30.15 O ANISOU 678 OH TYR A 97 2600 4799 4056 719 -592 -468 O ATOM 679 N PHE A 98 31.021 54.000 2.817 1.00 22.47 N ANISOU 679 N PHE A 98 1825 3447 3264 155 -275 -545 N ATOM 680 CA PHE A 98 30.623 52.619 2.547 1.00 22.79 C ANISOU 680 CA PHE A 98 1788 3561 3311 61 -266 -582 C ATOM 681 C PHE A 98 30.492 51.746 3.792 1.00 22.98 C ANISOU 681 C PHE A 98 1783 3584 3363 -17 -202 -609 C ATOM 682 O PHE A 98 30.098 50.587 3.673 1.00 23.70 O ANISOU 682 O PHE A 98 1823 3722 3459 -106 -190 -639 O ATOM 683 CB PHE A 98 31.605 51.952 1.563 1.00 22.16 C ANISOU 683 CB PHE A 98 1767 3442 3211 -1 -281 -566 C ATOM 684 CG PHE A 98 31.550 52.521 0.176 1.00 21.59 C ANISOU 684 CG PHE A 98 1706 3399 3098 56 -343 -544 C ATOM 685 CD1 PHE A 98 32.543 53.376 -0.279 1.00 21.43 C ANISOU 685 CD1 PHE A 98 1779 3308 3058 95 -357 -486 C ATOM 686 CD2 PHE A 98 30.498 52.220 -0.664 1.00 23.31 C ANISOU 686 CD2 PHE A 98 1841 3725 3291 62 -391 -576 C ATOM 687 CE1 PHE A 98 32.495 53.906 -1.554 1.00 22.61 C ANISOU 687 CE1 PHE A 98 1947 3485 3160 147 -411 -458 C ATOM 688 CE2 PHE A 98 30.440 52.750 -1.944 1.00 24.01 C ANISOU 688 CE2 PHE A 98 1944 3847 3330 120 -452 -553 C ATOM 689 CZ PHE A 98 31.452 53.595 -2.389 1.00 23.39 C ANISOU 689 CZ PHE A 98 1969 3688 3230 166 -458 -491 C ATOM 690 N ARG A 99 30.803 52.286 4.970 1.00 22.93 N ANISOU 690 N ARG A 99 1821 3522 3369 12 -162 -598 N ATOM 691 CA ARG A 99 30.887 51.477 6.200 1.00 23.04 C ANISOU 691 CA ARG A 99 1831 3523 3399 -62 -99 -612 C ATOM 692 C ARG A 99 29.634 50.669 6.550 1.00 24.27 C ANISOU 692 C ARG A 99 1871 3788 3564 -112 -69 -649 C ATOM 693 O ARG A 99 29.748 49.555 7.065 1.00 24.04 O ANISOU 693 O ARG A 99 1843 3746 3544 -213 -28 -656 O ATOM 694 CB ARG A 99 31.247 52.346 7.394 1.00 22.71 C ANISOU 694 CB ARG A 99 1853 3421 3354 -10 -70 -601 C ATOM 695 CG ARG A 99 32.655 52.897 7.356 1.00 21.83 C ANISOU 695 CG ARG A 99 1859 3201 3235 -13 -91 -560 C ATOM 696 CD ARG A 99 33.051 53.602 8.620 1.00 20.93 C ANISOU 696 CD ARG A 99 1817 3026 3110 9 -68 -557 C ATOM 697 NE ARG A 99 34.293 54.350 8.429 1.00 21.12 N ANISOU 697 NE ARG A 99 1944 2960 3123 0 -104 -515 N ATOM 698 CZ ARG A 99 34.579 55.526 8.971 1.00 20.75 C ANISOU 698 CZ ARG A 99 1987 2842 3056 40 -120 -510 C ATOM 699 NH1 ARG A 99 33.722 56.158 9.766 1.00 22.55 N ANISOU 699 NH1 ARG A 99 2228 3071 3269 116 -99 -549 N ATOM 700 NH2 ARG A 99 35.739 56.092 8.692 1.00 20.58 N ANISOU 700 NH2 ARG A 99 2048 2748 3023 0 -157 -465 N ATOM 701 N GLN A 100 28.455 51.221 6.270 1.00 25.59 N ANISOU 701 N GLN A 100 1936 4064 3724 -43 -89 -667 N ATOM 702 CA GLN A 100 27.185 50.586 6.647 1.00 27.14 C ANISOU 702 CA GLN A 100 1995 4394 3924 -92 -59 -696 C ATOM 703 C GLN A 100 26.479 49.900 5.478 1.00 27.98 C ANISOU 703 C GLN A 100 2008 4599 4024 -160 -112 -717 C ATOM 704 O GLN A 100 25.334 49.465 5.605 1.00 28.71 O ANISOU 704 O GLN A 100 1964 4828 4115 -209 -103 -738 O ATOM 705 CB GLN A 100 26.251 51.613 7.288 1.00 28.21 C ANISOU 705 CB GLN A 100 2054 4617 4047 37 -37 -703 C ATOM 706 CG GLN A 100 26.854 52.324 8.489 1.00 29.06 C ANISOU 706 CG GLN A 100 2266 4628 4148 103 13 -694 C ATOM 707 CD GLN A 100 27.227 51.383 9.619 1.00 30.52 C ANISOU 707 CD GLN A 100 2480 4778 4339 -10 82 -694 C ATOM 708 OE1 GLN A 100 28.268 51.557 10.257 1.00 31.46 O ANISOU 708 OE1 GLN A 100 2721 4779 4453 -15 97 -678 O ATOM 709 NE2 GLN A 100 26.388 50.381 9.867 1.00 31.86 N ANISOU 709 NE2 GLN A 100 2538 5052 4514 -108 120 -705 N ATOM 710 N ASN A 101 27.175 49.793 4.349 1.00 27.55 N ANISOU 710 N ASN A 101 2025 4483 3958 -171 -168 -710 N ATOM 711 CA ASN A 101 26.689 49.051 3.195 1.00 28.26 C ANISOU 711 CA ASN A 101 2062 4645 4031 -249 -224 -736 C ATOM 712 C ASN A 101 26.814 47.539 3.462 1.00 28.24 C ANISOU 712 C ASN A 101 2087 4605 4039 -418 -190 -761 C ATOM 713 O ASN A 101 27.899 47.069 3.746 1.00 27.40 O ANISOU 713 O ASN A 101 2104 4368 3940 -449 -156 -747 O ATOM 714 CB ASN A 101 27.515 49.452 1.961 1.00 27.99 C ANISOU 714 CB ASN A 101 2120 4547 3970 -196 -283 -719 C ATOM 715 CG ASN A 101 26.940 48.917 0.662 1.00 28.85 C ANISOU 715 CG ASN A 101 2177 4743 4043 -249 -354 -750 C ATOM 716 OD1 ASN A 101 26.578 47.752 0.574 1.00 28.90 O ANISOU 716 OD1 ASN A 101 2159 4775 4046 -383 -353 -788 O ATOM 717 ND2 ASN A 101 26.858 49.771 -0.351 1.00 28.91 N ANISOU 717 ND2 ASN A 101 2179 4789 4014 -148 -419 -731 N ATOM 718 N PRO A 102 25.725 46.775 3.362 1.00 29.62 N ANISOU 718 N PRO A 102 2152 4893 4209 -528 -200 -793 N ATOM 719 CA PRO A 102 25.777 45.325 3.648 1.00 29.81 C ANISOU 719 CA PRO A 102 2224 4863 4240 -702 -167 -814 C ATOM 720 C PRO A 102 26.704 44.497 2.738 1.00 29.23 C ANISOU 720 C PRO A 102 2297 4664 4146 -757 -196 -832 C ATOM 721 O PRO A 102 27.055 43.372 3.104 1.00 29.57 O ANISOU 721 O PRO A 102 2431 4611 4193 -867 -157 -841 O ATOM 722 CB PRO A 102 24.318 44.858 3.476 1.00 31.52 C ANISOU 722 CB PRO A 102 2277 5251 4447 -814 -193 -843 C ATOM 723 CG PRO A 102 23.489 46.072 3.239 1.00 32.03 C ANISOU 723 CG PRO A 102 2192 5475 4502 -678 -230 -834 C ATOM 724 CD PRO A 102 24.374 47.231 2.993 1.00 30.64 C ANISOU 724 CD PRO A 102 2107 5211 4324 -499 -244 -806 C ATOM 725 N ASP A 103 27.073 45.038 1.579 1.00 28.67 N ANISOU 725 N ASP A 103 2255 4593 4045 -676 -258 -835 N ATOM 726 CA ASP A 103 28.008 44.391 0.653 1.00 28.06 C ANISOU 726 CA ASP A 103 2317 4410 3936 -697 -279 -851 C ATOM 727 C ASP A 103 29.470 44.720 0.956 1.00 26.19 C ANISOU 727 C ASP A 103 2200 4042 3708 -603 -234 -806 C ATOM 728 O ASP A 103 30.371 44.302 0.231 1.00 25.37 O ANISOU 728 O ASP A 103 2206 3861 3574 -591 -240 -810 O ATOM 729 CB ASP A 103 27.696 44.826 -0.784 1.00 28.72 C ANISOU 729 CB ASP A 103 2369 4574 3969 -655 -366 -871 C ATOM 730 CG ASP A 103 26.298 44.430 -1.228 1.00 31.31 C ANISOU 730 CG ASP A 103 2571 5048 4276 -759 -427 -917 C ATOM 731 OD1 ASP A 103 25.858 43.301 -0.906 1.00 32.24 O ANISOU 731 OD1 ASP A 103 2695 5156 4400 -916 -411 -953 O ATOM 732 OD2 ASP A 103 25.570 45.189 -1.901 1.00 34.06 O ANISOU 732 OD2 ASP A 103 2811 5532 4599 -697 -494 -916 O ATOM 733 N VAL A 104 29.703 45.468 2.027 1.00 25.05 N ANISOU 733 N VAL A 104 2034 3885 3598 -538 -191 -765 N ATOM 734 CA VAL A 104 31.027 45.984 2.331 1.00 23.56 C ANISOU 734 CA VAL A 104 1936 3601 3416 -454 -162 -717 C ATOM 735 C VAL A 104 31.450 45.528 3.719 1.00 23.15 C ANISOU 735 C VAL A 104 1923 3481 3393 -488 -92 -697 C ATOM 736 O VAL A 104 30.814 45.887 4.710 1.00 23.15 O ANISOU 736 O VAL A 104 1858 3524 3415 -489 -65 -693 O ATOM 737 CB VAL A 104 31.058 47.516 2.257 1.00 23.30 C ANISOU 737 CB VAL A 104 1866 3604 3384 -336 -189 -683 C ATOM 738 CG1 VAL A 104 32.427 48.056 2.696 1.00 22.64 C ANISOU 738 CG1 VAL A 104 1870 3426 3305 -280 -161 -631 C ATOM 739 CG2 VAL A 104 30.714 47.988 0.850 1.00 23.24 C ANISOU 739 CG2 VAL A 104 1833 3660 3339 -291 -260 -692 C ATOM 740 N PRO A 105 32.503 44.715 3.793 1.00 22.97 N ANISOU 740 N PRO A 105 2006 3359 3363 -505 -62 -682 N ATOM 741 CA PRO A 105 33.142 44.412 5.077 1.00 22.52 C ANISOU 741 CA PRO A 105 1997 3235 3323 -511 -3 -647 C ATOM 742 C PRO A 105 33.743 45.651 5.742 1.00 21.79 C ANISOU 742 C PRO A 105 1894 3145 3241 -426 1 -603 C ATOM 743 O PRO A 105 34.417 46.434 5.081 1.00 20.79 O ANISOU 743 O PRO A 105 1782 3015 3102 -360 -31 -580 O ATOM 744 CB PRO A 105 34.237 43.410 4.702 1.00 22.33 C ANISOU 744 CB PRO A 105 2088 3117 3278 -512 15 -637 C ATOM 745 CG PRO A 105 33.827 42.858 3.393 1.00 23.55 C ANISOU 745 CG PRO A 105 2261 3282 3405 -547 -23 -686 C ATOM 746 CD PRO A 105 33.123 43.971 2.685 1.00 23.18 C ANISOU 746 CD PRO A 105 2116 3336 3354 -512 -79 -698 C ATOM 747 N LEU A 106 33.467 45.806 7.034 1.00 21.78 N ANISOU 747 N LEU A 106 1873 3148 3254 -438 39 -593 N ATOM 748 CA LEU A 106 33.986 46.870 7.878 1.00 21.58 C ANISOU 748 CA LEU A 106 1857 3112 3229 -375 45 -561 C ATOM 749 C LEU A 106 34.948 46.207 8.870 1.00 21.39 C ANISOU 749 C LEU A 106 1904 3024 3199 -397 86 -524 C ATOM 750 O LEU A 106 34.513 45.513 9.805 1.00 21.75 O ANISOU 750 O LEU A 106 1952 3065 3246 -448 131 -527 O ATOM 751 CB LEU A 106 32.818 47.539 8.610 1.00 22.01 C ANISOU 751 CB LEU A 106 1837 3234 3290 -360 60 -584 C ATOM 752 CG LEU A 106 33.087 48.684 9.583 1.00 21.72 C ANISOU 752 CG LEU A 106 1822 3185 3245 -295 68 -569 C ATOM 753 CD1 LEU A 106 33.780 49.838 8.890 1.00 21.50 C ANISOU 753 CD1 LEU A 106 1834 3124 3211 -226 15 -549 C ATOM 754 CD2 LEU A 106 31.783 49.150 10.213 1.00 22.52 C ANISOU 754 CD2 LEU A 106 1846 3367 3344 -267 94 -600 C ATOM 755 N VAL A 107 36.246 46.417 8.667 1.00 20.85 N ANISOU 755 N VAL A 107 1887 2916 3120 -358 71 -483 N ATOM 756 CA VAL A 107 37.248 45.511 9.223 1.00 20.70 C ANISOU 756 CA VAL A 107 1929 2847 3088 -367 101 -445 C ATOM 757 C VAL A 107 38.300 46.165 10.111 1.00 20.37 C ANISOU 757 C VAL A 107 1908 2800 3032 -337 96 -396 C ATOM 758 O VAL A 107 38.863 47.205 9.784 1.00 20.01 O ANISOU 758 O VAL A 107 1853 2769 2982 -308 58 -377 O ATOM 759 CB VAL A 107 37.933 44.718 8.082 1.00 20.79 C ANISOU 759 CB VAL A 107 1981 2831 3088 -350 95 -438 C ATOM 760 CG1 VAL A 107 39.074 43.846 8.607 1.00 21.17 C ANISOU 760 CG1 VAL A 107 2092 2834 3118 -325 126 -391 C ATOM 761 CG2 VAL A 107 36.887 43.857 7.358 1.00 21.91 C ANISOU 761 CG2 VAL A 107 2124 2965 3234 -403 99 -494 C ATOM 762 N VAL A 108 38.520 45.546 11.267 1.00 20.66 N ANISOU 762 N VAL A 108 1977 2815 3056 -355 130 -373 N ATOM 763 CA VAL A 108 39.718 45.743 12.067 1.00 20.36 C ANISOU 763 CA VAL A 108 1966 2776 2993 -333 122 -319 C ATOM 764 C VAL A 108 40.412 44.375 12.034 1.00 20.63 C ANISOU 764 C VAL A 108 2048 2776 3014 -317 151 -283 C ATOM 765 O VAL A 108 39.892 43.427 12.600 1.00 20.38 O ANISOU 765 O VAL A 108 2056 2707 2980 -346 191 -288 O ATOM 766 CB VAL A 108 39.373 46.098 13.521 1.00 20.72 C ANISOU 766 CB VAL A 108 2023 2830 3019 -354 138 -320 C ATOM 767 CG1 VAL A 108 40.645 46.295 14.323 1.00 20.71 C ANISOU 767 CG1 VAL A 108 2048 2838 2982 -340 117 -264 C ATOM 768 CG2 VAL A 108 38.478 47.331 13.587 1.00 20.80 C ANISOU 768 CG2 VAL A 108 2002 2863 3037 -352 122 -367 C ATOM 769 N PRO A 109 41.538 44.249 11.334 1.00 21.06 N ANISOU 769 N PRO A 109 2103 2842 3057 -267 135 -245 N ATOM 770 CA PRO A 109 42.126 42.928 11.050 1.00 21.92 C ANISOU 770 CA PRO A 109 2267 2912 3151 -223 166 -219 C ATOM 771 C PRO A 109 42.311 41.969 12.232 1.00 22.58 C ANISOU 771 C PRO A 109 2412 2955 3213 -217 201 -183 C ATOM 772 O PRO A 109 42.207 40.765 12.036 1.00 23.38 O ANISOU 772 O PRO A 109 2589 2987 3308 -202 236 -185 O ATOM 773 CB PRO A 109 43.469 43.287 10.417 1.00 21.80 C ANISOU 773 CB PRO A 109 2215 2953 3115 -157 143 -169 C ATOM 774 CG PRO A 109 43.182 44.562 9.724 1.00 21.24 C ANISOU 774 CG PRO A 109 2087 2921 3060 -188 104 -193 C ATOM 775 CD PRO A 109 42.311 45.324 10.687 1.00 20.64 C ANISOU 775 CD PRO A 109 2003 2839 3000 -246 91 -222 C ATOM 776 N GLU A 110 42.534 42.483 13.434 1.00 22.82 N ANISOU 776 N GLU A 110 2427 3018 3226 -231 190 -153 N ATOM 777 CA GLU A 110 42.722 41.626 14.603 1.00 23.24 C ANISOU 777 CA GLU A 110 2542 3041 3248 -223 220 -110 C ATOM 778 C GLU A 110 41.398 41.056 15.093 1.00 23.14 C ANISOU 778 C GLU A 110 2575 2970 3246 -296 265 -147 C ATOM 779 O GLU A 110 41.375 40.072 15.830 1.00 23.26 O ANISOU 779 O GLU A 110 2667 2934 3238 -299 302 -113 O ATOM 780 CB GLU A 110 43.389 42.407 15.733 1.00 23.38 C ANISOU 780 CB GLU A 110 2528 3124 3230 -221 186 -68 C ATOM 781 CG GLU A 110 44.777 42.925 15.378 1.00 24.45 C ANISOU 781 CG GLU A 110 2605 3335 3348 -169 139 -17 C ATOM 782 CD GLU A 110 44.782 44.340 14.814 1.00 24.97 C ANISOU 782 CD GLU A 110 2605 3448 3434 -211 92 -46 C ATOM 783 OE1 GLU A 110 43.713 44.848 14.386 1.00 24.20 O ANISOU 783 OE1 GLU A 110 2506 3319 3369 -252 98 -110 O ATOM 784 OE2 GLU A 110 45.879 44.938 14.791 1.00 25.95 O ANISOU 784 OE2 GLU A 110 2677 3645 3536 -202 48 1 O ATOM 785 N VAL A 111 40.299 41.675 14.682 1.00 22.47 N ANISOU 785 N VAL A 111 2442 2903 3193 -355 262 -211 N ATOM 786 CA VAL A 111 38.978 41.343 15.208 1.00 22.75 C ANISOU 786 CA VAL A 111 2484 2923 3235 -436 304 -244 C ATOM 787 C VAL A 111 38.139 40.480 14.256 1.00 23.03 C ANISOU 787 C VAL A 111 2542 2909 3299 -491 324 -286 C ATOM 788 O VAL A 111 37.656 39.408 14.649 1.00 23.73 O ANISOU 788 O VAL A 111 2699 2937 3379 -550 367 -277 O ATOM 789 CB VAL A 111 38.219 42.635 15.554 1.00 22.33 C ANISOU 789 CB VAL A 111 2352 2942 3190 -458 291 -284 C ATOM 790 CG1 VAL A 111 36.845 42.319 16.111 1.00 23.41 C ANISOU 790 CG1 VAL A 111 2472 3094 3329 -533 342 -313 C ATOM 791 CG2 VAL A 111 39.044 43.463 16.558 1.00 22.68 C ANISOU 791 CG2 VAL A 111 2400 3022 3197 -419 267 -250 C ATOM 792 N ASN A 112 37.958 40.955 13.021 1.00 22.35 N ANISOU 792 N ASN A 112 2407 2847 3239 -481 289 -331 N ATOM 793 CA ASN A 112 37.059 40.315 12.057 1.00 22.51 C ANISOU 793 CA ASN A 112 2435 2840 3279 -545 292 -383 C ATOM 794 C ASN A 112 37.666 40.184 10.650 1.00 22.49 C ANISOU 794 C ASN A 112 2454 2815 3276 -491 259 -401 C ATOM 795 O ASN A 112 37.021 40.488 9.645 1.00 22.08 O ANISOU 795 O ASN A 112 2356 2796 3238 -517 230 -452 O ATOM 796 CB ASN A 112 35.711 41.063 12.003 1.00 22.34 C ANISOU 796 CB ASN A 112 2309 2901 3280 -607 285 -433 C ATOM 797 CG ASN A 112 35.828 42.459 11.389 1.00 21.81 C ANISOU 797 CG ASN A 112 2159 2903 3223 -542 235 -452 C ATOM 798 OD1 ASN A 112 36.911 43.055 11.367 1.00 18.60 O ANISOU 798 OD1 ASN A 112 1765 2495 2808 -469 211 -419 O ATOM 799 ND2 ASN A 112 34.711 42.977 10.881 1.00 20.21 N ANISOU 799 ND2 ASN A 112 1873 2767 3039 -570 218 -499 N ATOM 800 N ALA A 113 38.912 39.726 10.586 1.00 22.61 N ANISOU 800 N ALA A 113 2535 2787 3268 -408 265 -356 N ATOM 801 CA ALA A 113 39.566 39.434 9.307 1.00 22.87 C ANISOU 801 CA ALA A 113 2603 2800 3288 -344 250 -369 C ATOM 802 C ALA A 113 38.746 38.465 8.438 1.00 23.72 C ANISOU 802 C ALA A 113 2783 2838 3393 -409 256 -432 C ATOM 803 O ALA A 113 38.743 38.585 7.214 1.00 23.59 O ANISOU 803 O ALA A 113 2761 2835 3366 -390 230 -471 O ATOM 804 CB ALA A 113 40.991 38.886 9.537 1.00 22.91 C ANISOU 804 CB ALA A 113 2668 2775 3260 -234 269 -304 C ATOM 805 N HIS A 114 38.032 37.529 9.066 1.00 24.78 N ANISOU 805 N HIS A 114 2989 2898 3529 -497 288 -440 N ATOM 806 CA HIS A 114 37.195 36.565 8.329 1.00 26.06 C ANISOU 806 CA HIS A 114 3231 2986 3685 -592 288 -501 C ATOM 807 C HIS A 114 36.139 37.244 7.441 1.00 25.72 C ANISOU 807 C HIS A 114 3081 3032 3659 -666 241 -567 C ATOM 808 O HIS A 114 35.745 36.689 6.419 1.00 26.24 O ANISOU 808 O HIS A 114 3200 3063 3708 -713 218 -625 O ATOM 809 CB HIS A 114 36.504 35.590 9.293 1.00 27.40 C ANISOU 809 CB HIS A 114 3480 3074 3855 -706 329 -489 C ATOM 810 CG HIS A 114 35.603 36.267 10.273 1.00 28.62 C ANISOU 810 CG HIS A 114 3514 3323 4035 -788 340 -476 C ATOM 811 ND1 HIS A 114 34.344 36.713 9.935 1.00 31.08 N ANISOU 811 ND1 HIS A 114 3715 3725 4369 -893 318 -528 N ATOM 812 CD2 HIS A 114 35.793 36.617 11.567 1.00 29.61 C ANISOU 812 CD2 HIS A 114 3610 3481 4160 -768 371 -419 C ATOM 813 CE1 HIS A 114 33.795 37.301 10.981 1.00 31.37 C ANISOU 813 CE1 HIS A 114 3658 3843 4418 -924 342 -503 C ATOM 814 NE2 HIS A 114 34.651 37.253 11.985 1.00 31.42 N ANISOU 814 NE2 HIS A 114 3719 3812 4409 -854 374 -441 N ATOM 815 N ALA A 115 35.683 38.434 7.835 1.00 24.92 N ANISOU 815 N ALA A 115 2838 3045 3584 -670 224 -560 N ATOM 816 CA ALA A 115 34.699 39.199 7.057 1.00 24.74 C ANISOU 816 CA ALA A 115 2702 3123 3575 -712 177 -611 C ATOM 817 C ALA A 115 35.240 39.688 5.703 1.00 24.34 C ANISOU 817 C ALA A 115 2646 3097 3505 -631 131 -632 C ATOM 818 O ALA A 115 34.460 40.026 4.810 1.00 24.34 O ANISOU 818 O ALA A 115 2586 3160 3501 -666 86 -679 O ATOM 819 CB ALA A 115 34.176 40.380 7.870 1.00 24.24 C ANISOU 819 CB ALA A 115 2511 3163 3538 -703 176 -593 C ATOM 820 N LEU A 116 36.562 39.728 5.560 1.00 23.70 N ANISOU 820 N LEU A 116 2619 2980 3405 -522 143 -591 N ATOM 821 CA LEU A 116 37.199 40.053 4.281 1.00 23.94 C ANISOU 821 CA LEU A 116 2658 3034 3406 -444 114 -601 C ATOM 822 C LEU A 116 36.902 39.034 3.175 1.00 25.25 C ANISOU 822 C LEU A 116 2919 3142 3533 -479 103 -665 C ATOM 823 O LEU A 116 36.879 39.394 2.007 1.00 25.23 O ANISOU 823 O LEU A 116 2900 3185 3502 -452 67 -694 O ATOM 824 CB LEU A 116 38.722 40.164 4.435 1.00 23.30 C ANISOU 824 CB LEU A 116 2606 2941 3306 -326 140 -537 C ATOM 825 CG LEU A 116 39.276 41.276 5.328 1.00 21.87 C ANISOU 825 CG LEU A 116 2341 2821 3149 -289 137 -474 C ATOM 826 CD1 LEU A 116 40.713 40.991 5.689 1.00 22.32 C ANISOU 826 CD1 LEU A 116 2432 2864 3183 -199 167 -408 C ATOM 827 CD2 LEU A 116 39.176 42.644 4.665 1.00 21.12 C ANISOU 827 CD2 LEU A 116 2156 2810 3058 -272 92 -472 C ATOM 828 N ASP A 117 36.686 37.771 3.543 1.00 26.69 N ANISOU 828 N ASP A 117 3215 3217 3707 -541 134 -685 N ATOM 829 CA ASP A 117 36.592 36.679 2.561 1.00 28.28 C ANISOU 829 CA ASP A 117 3553 3330 3861 -568 127 -748 C ATOM 830 C ASP A 117 35.472 36.849 1.545 1.00 28.67 C ANISOU 830 C ASP A 117 3556 3442 3896 -666 65 -822 C ATOM 831 O ASP A 117 35.636 36.466 0.397 1.00 29.71 O ANISOU 831 O ASP A 117 3768 3547 3974 -645 42 -873 O ATOM 832 CB ASP A 117 36.416 35.326 3.255 1.00 29.41 C ANISOU 832 CB ASP A 117 3842 3331 4002 -642 168 -754 C ATOM 833 CG ASP A 117 37.637 34.912 4.047 1.00 30.53 C ANISOU 833 CG ASP A 117 4066 3397 4137 -520 226 -683 C ATOM 834 OD1 ASP A 117 38.705 35.516 3.861 1.00 31.79 O ANISOU 834 OD1 ASP A 117 4179 3615 4286 -379 233 -639 O ATOM 835 OD2 ASP A 117 37.623 33.994 4.889 1.00 34.45 O ANISOU 835 OD2 ASP A 117 4671 3784 4636 -555 264 -660 O ATOM 836 N ALA A 118 34.349 37.423 1.967 1.00 28.51 N ANISOU 836 N ALA A 118 3405 3513 3916 -765 37 -829 N ATOM 837 CA ALA A 118 33.200 37.620 1.085 1.00 29.08 C ANISOU 837 CA ALA A 118 3405 3671 3973 -859 -30 -892 C ATOM 838 C ALA A 118 33.147 39.020 0.465 1.00 27.85 C ANISOU 838 C ALA A 118 3113 3651 3817 -774 -76 -878 C ATOM 839 O ALA A 118 32.101 39.416 -0.041 1.00 28.84 O ANISOU 839 O ALA A 118 3140 3879 3938 -835 -133 -913 O ATOM 840 CB ALA A 118 31.890 37.327 1.846 1.00 30.12 C ANISOU 840 CB ALA A 118 3463 3841 4139 -1021 -32 -907 C ATOM 841 N HIS A 119 34.260 39.758 0.459 1.00 25.86 N ANISOU 841 N HIS A 119 2857 3404 3566 -636 -55 -823 N ATOM 842 CA HIS A 119 34.244 41.127 -0.081 1.00 24.61 C ANISOU 842 CA HIS A 119 2590 3354 3406 -561 -97 -799 C ATOM 843 C HIS A 119 33.846 41.201 -1.563 1.00 24.33 C ANISOU 843 C HIS A 119 2558 3375 3313 -564 -160 -849 C ATOM 844 O HIS A 119 34.066 40.265 -2.342 1.00 24.31 O ANISOU 844 O HIS A 119 2668 3313 3257 -583 -163 -897 O ATOM 845 CB HIS A 119 35.584 41.856 0.143 1.00 23.35 C ANISOU 845 CB HIS A 119 2436 3185 3250 -438 -64 -727 C ATOM 846 CG HIS A 119 36.650 41.520 -0.859 1.00 24.09 C ANISOU 846 CG HIS A 119 2619 3250 3286 -358 -53 -723 C ATOM 847 ND1 HIS A 119 37.787 40.821 -0.518 1.00 24.25 N ANISOU 847 ND1 HIS A 119 2725 3195 3293 -298 5 -693 N ATOM 848 CD2 HIS A 119 36.761 41.785 -2.184 1.00 23.88 C ANISOU 848 CD2 HIS A 119 2604 3269 3201 -318 -87 -742 C ATOM 849 CE1 HIS A 119 38.546 40.668 -1.586 1.00 23.54 C ANISOU 849 CE1 HIS A 119 2691 3112 3142 -220 11 -695 C ATOM 850 NE2 HIS A 119 37.945 41.240 -2.612 1.00 24.12 N ANISOU 850 NE2 HIS A 119 2725 3254 3185 -236 -42 -726 N ATOM 851 N ASN A 120 33.274 42.348 -1.919 1.00 23.72 N ANISOU 851 N ASN A 120 2366 3407 3239 -536 -210 -836 N ATOM 852 CA ASN A 120 32.803 42.655 -3.272 1.00 23.95 C ANISOU 852 CA ASN A 120 2376 3515 3211 -527 -280 -870 C ATOM 853 C ASN A 120 33.593 43.819 -3.906 1.00 22.96 C ANISOU 853 C ASN A 120 2237 3426 3059 -402 -290 -812 C ATOM 854 O ASN A 120 33.089 44.532 -4.770 1.00 23.01 O ANISOU 854 O ASN A 120 2192 3519 3030 -374 -350 -813 O ATOM 855 CB ASN A 120 31.308 42.997 -3.223 1.00 24.58 C ANISOU 855 CB ASN A 120 2324 3707 3307 -599 -340 -899 C ATOM 856 CG ASN A 120 30.463 41.849 -2.695 1.00 25.67 C ANISOU 856 CG ASN A 120 2465 3827 3463 -750 -334 -953 C ATOM 857 OD1 ASN A 120 30.245 40.873 -3.396 1.00 25.87 O ANISOU 857 OD1 ASN A 120 2569 3819 3440 -837 -362 -1015 O ATOM 858 ND2 ASN A 120 29.988 41.963 -1.455 1.00 24.04 N ANISOU 858 ND2 ASN A 120 2180 3635 3318 -789 -296 -928 N ATOM 859 N GLY A 121 34.820 44.023 -3.439 1.00 22.04 N ANISOU 859 N GLY A 121 2164 3252 2959 -333 -232 -753 N ATOM 860 CA GLY A 121 35.757 44.942 -4.060 1.00 21.68 C ANISOU 860 CA GLY A 121 2124 3232 2881 -238 -230 -692 C ATOM 861 C GLY A 121 36.014 46.199 -3.238 1.00 21.13 C ANISOU 861 C GLY A 121 1990 3174 2864 -198 -223 -621 C ATOM 862 O GLY A 121 36.896 46.980 -3.585 1.00 20.60 O ANISOU 862 O GLY A 121 1934 3117 2777 -139 -215 -559 O ATOM 863 N ILE A 122 35.228 46.403 -2.178 1.00 21.00 N ANISOU 863 N ILE A 122 1912 3159 2906 -236 -224 -631 N ATOM 864 CA ILE A 122 35.421 47.509 -1.240 1.00 20.35 C ANISOU 864 CA ILE A 122 1792 3072 2870 -201 -214 -577 C ATOM 865 C ILE A 122 35.420 46.981 0.191 1.00 20.21 C ANISOU 865 C ILE A 122 1771 3006 2902 -245 -165 -582 C ATOM 866 O ILE A 122 34.479 46.321 0.624 1.00 20.25 O ANISOU 866 O ILE A 122 1746 3022 2927 -307 -161 -629 O ATOM 867 CB ILE A 122 34.311 48.572 -1.366 1.00 20.77 C ANISOU 867 CB ILE A 122 1772 3190 2932 -172 -267 -581 C ATOM 868 CG1 ILE A 122 34.234 49.110 -2.796 1.00 21.74 C ANISOU 868 CG1 ILE A 122 1902 3363 2996 -124 -321 -569 C ATOM 869 CG2 ILE A 122 34.558 49.705 -0.371 1.00 20.01 C ANISOU 869 CG2 ILE A 122 1666 3063 2872 -131 -253 -533 C ATOM 870 CD1 ILE A 122 33.158 50.200 -2.994 1.00 23.20 C ANISOU 870 CD1 ILE A 122 2021 3614 3181 -69 -378 -563 C ATOM 871 N ILE A 123 36.484 47.292 0.917 1.00 19.88 N ANISOU 871 N ILE A 123 1757 2921 2876 -221 -131 -529 N ATOM 872 CA ILE A 123 36.532 47.080 2.351 1.00 20.16 C ANISOU 872 CA ILE A 123 1788 2921 2950 -249 -92 -522 C ATOM 873 C ILE A 123 36.635 48.462 2.974 1.00 19.81 C ANISOU 873 C ILE A 123 1722 2882 2924 -214 -107 -484 C ATOM 874 O ILE A 123 37.447 49.270 2.537 1.00 20.06 O ANISOU 874 O ILE A 123 1773 2909 2938 -180 -124 -437 O ATOM 875 CB ILE A 123 37.741 46.203 2.715 1.00 20.03 C ANISOU 875 CB ILE A 123 1833 2853 2926 -247 -46 -492 C ATOM 876 CG1 ILE A 123 37.588 44.827 2.041 1.00 22.14 C ANISOU 876 CG1 ILE A 123 2154 3091 3167 -271 -32 -538 C ATOM 877 CG2 ILE A 123 37.857 46.036 4.230 1.00 19.08 C ANISOU 877 CG2 ILE A 123 1715 2700 2836 -271 -11 -475 C ATOM 878 CD1 ILE A 123 38.051 44.787 0.591 1.00 23.42 C ANISOU 878 CD1 ILE A 123 2346 3275 3276 -227 -50 -541 C ATOM 879 N ALA A 124 35.809 48.737 3.978 1.00 19.97 N ANISOU 879 N ALA A 124 1706 2909 2971 -226 -98 -505 N ATOM 880 CA ALA A 124 35.843 50.016 4.676 1.00 19.91 C ANISOU 880 CA ALA A 124 1701 2891 2974 -188 -108 -481 C ATOM 881 C ALA A 124 36.672 49.948 5.964 1.00 20.08 C ANISOU 881 C ALA A 124 1759 2867 3003 -210 -74 -454 C ATOM 882 O ALA A 124 36.497 49.048 6.788 1.00 20.40 O ANISOU 882 O ALA A 124 1797 2902 3053 -248 -35 -469 O ATOM 883 CB ALA A 124 34.455 50.459 5.003 1.00 20.61 C ANISOU 883 CB ALA A 124 1731 3026 3075 -163 -116 -521 C ATOM 884 N CYS A 125 37.554 50.926 6.126 1.00 19.56 N ANISOU 884 N CYS A 125 1734 2772 2927 -195 -94 -410 N ATOM 885 CA CYS A 125 38.234 51.180 7.376 1.00 19.61 C ANISOU 885 CA CYS A 125 1774 2747 2932 -216 -81 -387 C ATOM 886 C CYS A 125 37.237 51.864 8.322 1.00 20.03 C ANISOU 886 C CYS A 125 1828 2792 2989 -193 -75 -426 C ATOM 887 O CYS A 125 36.563 52.811 7.918 1.00 20.17 O ANISOU 887 O CYS A 125 1848 2809 3006 -143 -101 -442 O ATOM 888 CB CYS A 125 39.430 52.082 7.114 1.00 19.47 C ANISOU 888 CB CYS A 125 1795 2707 2896 -226 -114 -329 C ATOM 889 SG CYS A 125 40.399 52.518 8.562 1.00 20.33 S ANISOU 889 SG CYS A 125 1946 2788 2990 -271 -118 -298 S ATOM 890 N PRO A 126 37.093 51.379 9.555 1.00 20.12 N ANISOU 890 N PRO A 126 1842 2803 3001 -216 -37 -440 N ATOM 891 CA PRO A 126 36.185 52.034 10.503 1.00 20.81 C ANISOU 891 CA PRO A 126 1932 2893 3080 -183 -21 -477 C ATOM 892 C PRO A 126 36.687 53.382 11.008 1.00 21.15 C ANISOU 892 C PRO A 126 2056 2880 3100 -160 -53 -468 C ATOM 893 O PRO A 126 37.822 53.800 10.740 1.00 20.66 O ANISOU 893 O PRO A 126 2041 2781 3028 -192 -90 -425 O ATOM 894 CB PRO A 126 36.078 51.034 11.663 1.00 21.12 C ANISOU 894 CB PRO A 126 1963 2948 3114 -225 32 -483 C ATOM 895 CG PRO A 126 36.712 49.772 11.171 1.00 20.72 C ANISOU 895 CG PRO A 126 1903 2895 3074 -272 43 -455 C ATOM 896 CD PRO A 126 37.709 50.176 10.130 1.00 19.79 C ANISOU 896 CD PRO A 126 1805 2760 2956 -261 -2 -419 C ATOM 897 N ASN A 127 35.786 54.058 11.711 1.00 21.98 N ANISOU 897 N ASN A 127 2176 2984 3191 -104 -37 -509 N ATOM 898 CA ASN A 127 36.050 55.266 12.471 1.00 23.03 C ANISOU 898 CA ASN A 127 2410 3050 3290 -78 -58 -520 C ATOM 899 C ASN A 127 37.180 55.048 13.492 1.00 22.97 C ANISOU 899 C ASN A 127 2457 3016 3255 -155 -61 -496 C ATOM 900 O ASN A 127 37.268 53.987 14.124 1.00 22.21 O ANISOU 900 O ASN A 127 2320 2961 3157 -192 -22 -490 O ATOM 901 CB ASN A 127 34.737 55.659 13.155 1.00 24.51 C ANISOU 901 CB ASN A 127 2586 3267 3461 10 -17 -576 C ATOM 902 CG ASN A 127 34.895 56.738 14.172 1.00 27.11 C ANISOU 902 CG ASN A 127 3035 3523 3742 45 -23 -603 C ATOM 903 OD1 ASN A 127 34.992 56.458 15.374 1.00 32.57 O ANISOU 903 OD1 ASN A 127 3751 4224 4400 21 11 -620 O ATOM 904 ND2 ASN A 127 34.877 57.988 13.722 1.00 29.62 N ANISOU 904 ND2 ASN A 127 3443 3764 4048 106 -66 -609 N ATOM 905 N CYS A 128 38.058 56.042 13.625 1.00 23.15 N ANISOU 905 N CYS A 128 2574 2969 3252 -185 -112 -477 N ATOM 906 CA CYS A 128 39.243 55.933 14.483 1.00 23.59 C ANISOU 906 CA CYS A 128 2673 3015 3276 -269 -134 -448 C ATOM 907 C CYS A 128 38.917 55.598 15.939 1.00 23.18 C ANISOU 907 C CYS A 128 2643 2980 3184 -264 -95 -483 C ATOM 908 O CYS A 128 39.515 54.691 16.523 1.00 22.55 O ANISOU 908 O CYS A 128 2532 2943 3091 -313 -82 -453 O ATOM 909 CB CYS A 128 40.062 57.222 14.436 1.00 24.24 C ANISOU 909 CB CYS A 128 2862 3018 3330 -317 -201 -431 C ATOM 910 SG CYS A 128 39.097 58.732 14.587 1.00 29.18 S ANISOU 910 SG CYS A 128 3618 3539 3930 -230 -214 -494 S ATOM 911 N SER A 129 37.968 56.320 16.521 1.00 23.44 N ANISOU 911 N SER A 129 2732 2984 3189 -194 -73 -542 N ATOM 912 CA SER A 129 37.597 56.082 17.914 1.00 24.29 C ANISOU 912 CA SER A 129 2868 3116 3246 -181 -28 -578 C ATOM 913 C SER A 129 37.058 54.654 18.107 1.00 23.25 C ANISOU 913 C SER A 129 2625 3072 3135 -185 41 -565 C ATOM 914 O SER A 129 37.295 54.032 19.140 1.00 23.77 O ANISOU 914 O SER A 129 2702 3168 3163 -219 68 -555 O ATOM 915 CB SER A 129 36.594 57.135 18.392 1.00 25.33 C ANISOU 915 CB SER A 129 3077 3209 3339 -80 -6 -647 C ATOM 916 OG SER A 129 35.417 57.104 17.595 1.00 27.56 O ANISOU 916 OG SER A 129 3276 3532 3663 11 30 -666 O ATOM 917 N THR A 130 36.375 54.125 17.096 1.00 22.47 N ANISOU 917 N THR A 130 2432 3014 3093 -161 63 -561 N ATOM 918 CA THR A 130 35.830 52.766 17.145 1.00 22.19 C ANISOU 918 CA THR A 130 2304 3048 3080 -185 122 -549 C ATOM 919 C THR A 130 36.918 51.689 17.063 1.00 21.26 C ANISOU 919 C THR A 130 2178 2927 2973 -260 110 -490 C ATOM 920 O THR A 130 36.860 50.697 17.781 1.00 21.15 O ANISOU 920 O THR A 130 2153 2940 2944 -291 155 -473 O ATOM 921 CB THR A 130 34.842 52.541 15.991 1.00 22.17 C ANISOU 921 CB THR A 130 2207 3088 3128 -153 134 -564 C ATOM 922 OG1 THR A 130 33.682 53.366 16.175 1.00 24.80 O ANISOU 922 OG1 THR A 130 2525 3451 3447 -64 158 -614 O ATOM 923 CG2 THR A 130 34.306 51.116 16.007 1.00 22.31 C ANISOU 923 CG2 THR A 130 2145 3166 3168 -205 188 -553 C ATOM 924 N ILE A 131 37.893 51.884 16.182 1.00 20.15 N ANISOU 924 N ILE A 131 2044 2758 2854 -281 54 -455 N ATOM 925 CA ILE A 131 38.954 50.899 15.966 1.00 19.86 C ANISOU 925 CA ILE A 131 1991 2729 2825 -325 45 -397 C ATOM 926 C ILE A 131 39.692 50.524 17.249 1.00 19.71 C ANISOU 926 C ILE A 131 2013 2719 2756 -355 49 -367 C ATOM 927 O ILE A 131 39.875 49.351 17.536 1.00 19.41 O ANISOU 927 O ILE A 131 1962 2698 2716 -368 82 -334 O ATOM 928 CB ILE A 131 39.981 51.406 14.926 1.00 19.24 C ANISOU 928 CB ILE A 131 1912 2637 2763 -338 -14 -360 C ATOM 929 CG1 ILE A 131 39.361 51.411 13.529 1.00 19.27 C ANISOU 929 CG1 ILE A 131 1869 2641 2809 -308 -14 -377 C ATOM 930 CG2 ILE A 131 41.239 50.512 14.925 1.00 19.70 C ANISOU 930 CG2 ILE A 131 1952 2721 2813 -365 -22 -296 C ATOM 931 CD1 ILE A 131 40.116 52.289 12.508 1.00 18.83 C ANISOU 931 CD1 ILE A 131 1826 2569 2760 -313 -69 -347 C ATOM 932 N GLN A 132 40.149 51.531 17.985 1.00 20.02 N ANISOU 932 N GLN A 132 2114 2742 2750 -368 9 -376 N ATOM 933 CA GLN A 132 40.938 51.301 19.195 1.00 20.40 C ANISOU 933 CA GLN A 132 2203 2810 2738 -402 -5 -346 C ATOM 934 C GLN A 132 40.095 50.648 20.291 1.00 20.79 C ANISOU 934 C GLN A 132 2267 2879 2752 -386 63 -366 C ATOM 935 O GLN A 132 40.598 49.830 21.066 1.00 20.77 O ANISOU 935 O GLN A 132 2277 2903 2713 -403 74 -323 O ATOM 936 CB GLN A 132 41.582 52.598 19.690 1.00 20.71 C ANISOU 936 CB GLN A 132 2316 2823 2728 -437 -73 -360 C ATOM 937 CG GLN A 132 40.609 53.670 20.151 1.00 21.35 C ANISOU 937 CG GLN A 132 2473 2856 2781 -400 -61 -437 C ATOM 938 CD GLN A 132 41.331 54.923 20.602 1.00 22.33 C ANISOU 938 CD GLN A 132 2701 2932 2853 -448 -136 -453 C ATOM 939 OE1 GLN A 132 41.913 55.630 19.784 1.00 24.31 O ANISOU 939 OE1 GLN A 132 2963 3147 3127 -486 -193 -435 O ATOM 940 NE2 GLN A 132 41.324 55.181 21.902 1.00 21.44 N ANISOU 940 NE2 GLN A 132 2669 2818 2661 -458 -138 -485 N ATOM 941 N MET A 133 38.809 50.977 20.333 1.00 21.11 N ANISOU 941 N MET A 133 2303 2918 2801 -348 111 -424 N ATOM 942 CA MET A 133 37.916 50.325 21.269 1.00 21.97 C ANISOU 942 CA MET A 133 2408 3063 2877 -340 188 -437 C ATOM 943 C MET A 133 37.761 48.836 20.939 1.00 21.83 C ANISOU 943 C MET A 133 2338 3061 2897 -369 234 -392 C ATOM 944 O MET A 133 37.719 48.002 21.844 1.00 21.61 O ANISOU 944 O MET A 133 2331 3049 2829 -391 278 -361 O ATOM 945 CB MET A 133 36.552 51.000 21.304 1.00 22.50 C ANISOU 945 CB MET A 133 2457 3148 2944 -285 235 -503 C ATOM 946 CG MET A 133 35.710 50.530 22.481 1.00 24.66 C ANISOU 946 CG MET A 133 2731 3477 3163 -279 318 -515 C ATOM 947 SD MET A 133 34.308 51.585 22.782 1.00 26.08 S ANISOU 947 SD MET A 133 2899 3698 3314 -186 371 -594 S ATOM 948 CE MET A 133 33.253 51.148 21.404 1.00 26.83 C ANISOU 948 CE MET A 133 2853 3839 3501 -177 395 -599 C ATOM 949 N MET A 134 37.700 48.505 19.651 1.00 21.46 N ANISOU 949 N MET A 134 2237 3001 2918 -371 222 -387 N ATOM 950 CA MET A 134 37.535 47.107 19.221 1.00 21.30 C ANISOU 950 CA MET A 134 2189 2974 2929 -402 260 -355 C ATOM 951 C MET A 134 38.784 46.258 19.488 1.00 21.00 C ANISOU 951 C MET A 134 2195 2913 2871 -410 242 -286 C ATOM 952 O MET A 134 38.671 45.070 19.782 1.00 20.91 O ANISOU 952 O MET A 134 2207 2885 2854 -431 286 -253 O ATOM 953 CB MET A 134 37.176 47.043 17.741 1.00 20.87 C ANISOU 953 CB MET A 134 2079 2912 2940 -398 244 -377 C ATOM 954 CG MET A 134 35.818 47.624 17.415 1.00 22.04 C ANISOU 954 CG MET A 134 2166 3100 3108 -384 266 -435 C ATOM 955 SD MET A 134 34.444 46.719 18.183 1.00 23.52 S ANISOU 955 SD MET A 134 2311 3342 3283 -434 357 -447 S ATOM 956 CE MET A 134 34.098 47.789 19.592 1.00 23.79 C ANISOU 956 CE MET A 134 2372 3417 3249 -382 385 -473 C ATOM 957 N VAL A 135 39.964 46.859 19.370 1.00 20.69 N ANISOU 957 N VAL A 135 2167 2876 2819 -393 177 -261 N ATOM 958 CA VAL A 135 41.219 46.155 19.655 1.00 21.01 C ANISOU 958 CA VAL A 135 2230 2922 2832 -384 154 -190 C ATOM 959 C VAL A 135 41.303 45.809 21.150 1.00 21.66 C ANISOU 959 C VAL A 135 2365 3021 2842 -392 175 -161 C ATOM 960 O VAL A 135 41.724 44.712 21.511 1.00 22.14 O ANISOU 960 O VAL A 135 2456 3073 2883 -378 196 -103 O ATOM 961 CB VAL A 135 42.464 46.976 19.227 1.00 20.70 C ANISOU 961 CB VAL A 135 2168 2910 2788 -378 77 -164 C ATOM 962 CG1 VAL A 135 43.766 46.356 19.777 1.00 20.79 C ANISOU 962 CG1 VAL A 135 2184 2962 2755 -360 49 -85 C ATOM 963 CG2 VAL A 135 42.533 47.070 17.702 1.00 20.09 C ANISOU 963 CG2 VAL A 135 2043 2821 2771 -364 65 -173 C ATOM 964 N ALA A 136 40.888 46.740 22.003 1.00 21.92 N ANISOU 964 N ALA A 136 2424 3075 2832 -406 171 -202 N ATOM 965 CA ALA A 136 40.939 46.542 23.444 1.00 22.77 C ANISOU 965 CA ALA A 136 2589 3207 2857 -413 188 -181 C ATOM 966 C ALA A 136 39.892 45.541 23.926 1.00 23.45 C ANISOU 966 C ALA A 136 2691 3285 2936 -426 280 -175 C ATOM 967 O ALA A 136 40.157 44.771 24.855 1.00 23.82 O ANISOU 967 O ALA A 136 2788 3338 2924 -429 303 -120 O ATOM 968 CB ALA A 136 40.760 47.868 24.166 1.00 23.05 C ANISOU 968 CB ALA A 136 2661 3260 2838 -420 160 -238 C ATOM 969 N LEU A 137 38.715 45.540 23.292 1.00 23.19 N ANISOU 969 N LEU A 137 2612 3242 2955 -439 330 -223 N ATOM 970 CA LEU A 137 37.578 44.784 23.808 1.00 24.19 C ANISOU 970 CA LEU A 137 2739 3382 3070 -473 419 -223 C ATOM 971 C LEU A 137 37.424 43.380 23.222 1.00 24.61 C ANISOU 971 C LEU A 137 2797 3386 3168 -511 455 -180 C ATOM 972 O LEU A 137 36.836 42.512 23.866 1.00 25.35 O ANISOU 972 O LEU A 137 2922 3476 3233 -557 522 -149 O ATOM 973 CB LEU A 137 36.271 45.574 23.624 1.00 24.19 C ANISOU 973 CB LEU A 137 2677 3426 3089 -470 458 -297 C ATOM 974 CG LEU A 137 36.138 46.877 24.409 1.00 23.96 C ANISOU 974 CG LEU A 137 2672 3432 2998 -424 447 -348 C ATOM 975 CD1 LEU A 137 34.733 47.422 24.245 1.00 24.84 C ANISOU 975 CD1 LEU A 137 2716 3598 3124 -399 504 -410 C ATOM 976 CD2 LEU A 137 36.474 46.669 25.881 1.00 25.17 C ANISOU 976 CD2 LEU A 137 2905 3609 3051 -430 469 -315 C ATOM 977 N GLU A 138 37.938 43.142 22.018 1.00 24.14 N ANISOU 977 N GLU A 138 2718 3284 3169 -497 414 -178 N ATOM 978 CA GLU A 138 37.793 41.829 21.401 1.00 24.61 C ANISOU 978 CA GLU A 138 2806 3280 3264 -529 445 -149 C ATOM 979 C GLU A 138 38.393 40.666 22.226 1.00 25.43 C ANISOU 979 C GLU A 138 3009 3334 3318 -526 470 -68 C ATOM 980 O GLU A 138 37.748 39.623 22.331 1.00 25.96 O ANISOU 980 O GLU A 138 3124 3352 3387 -586 528 -47 O ATOM 981 CB GLU A 138 38.328 41.830 19.964 1.00 24.57 C ANISOU 981 CB GLU A 138 2775 3241 3318 -498 396 -165 C ATOM 982 CG GLU A 138 38.367 40.469 19.279 1.00 25.35 C ANISOU 982 CG GLU A 138 2931 3257 3443 -516 419 -141 C ATOM 983 CD GLU A 138 37.003 39.809 19.116 1.00 27.29 C ANISOU 983 CD GLU A 138 3174 3483 3711 -615 476 -172 C ATOM 984 OE1 GLU A 138 35.959 40.476 19.290 1.00 28.24 O ANISOU 984 OE1 GLU A 138 3215 3675 3839 -658 495 -217 O ATOM 985 OE2 GLU A 138 36.977 38.603 18.781 1.00 29.13 O ANISOU 985 OE2 GLU A 138 3487 3630 3952 -650 499 -151 O ATOM 986 N PRO A 139 39.594 40.808 22.798 1.00 25.30 N ANISOU 986 N PRO A 139 3027 3331 3253 -462 426 -17 N ATOM 987 CA PRO A 139 40.145 39.737 23.647 1.00 26.16 C ANISOU 987 CA PRO A 139 3233 3403 3306 -441 447 68 C ATOM 988 C PRO A 139 39.277 39.412 24.859 1.00 27.23 C ANISOU 988 C PRO A 139 3415 3549 3382 -502 516 88 C ATOM 989 O PRO A 139 39.247 38.253 25.288 1.00 28.39 O ANISOU 989 O PRO A 139 3654 3631 3500 -518 561 153 O ATOM 990 CB PRO A 139 41.501 40.290 24.099 1.00 26.26 C ANISOU 990 CB PRO A 139 3236 3472 3269 -366 373 109 C ATOM 991 CG PRO A 139 41.429 41.753 23.861 1.00 25.23 C ANISOU 991 CG PRO A 139 3024 3407 3154 -379 326 39 C ATOM 992 CD PRO A 139 40.538 41.934 22.668 1.00 24.62 C ANISOU 992 CD PRO A 139 2894 3301 3160 -412 348 -28 C ATOM 993 N VAL A 140 38.585 40.420 25.387 1.00 27.01 N ANISOU 993 N VAL A 140 3333 3598 3332 -530 530 34 N ATOM 994 CA VAL A 140 37.635 40.248 26.480 1.00 27.87 C ANISOU 994 CA VAL A 140 3466 3742 3380 -586 607 43 C ATOM 995 C VAL A 140 36.359 39.523 25.999 1.00 28.86 C ANISOU 995 C VAL A 140 3569 3841 3556 -680 684 28 C ATOM 996 O VAL A 140 35.897 38.580 26.635 1.00 29.03 O ANISOU 996 O VAL A 140 3654 3837 3540 -743 751 83 O ATOM 997 CB VAL A 140 37.267 41.621 27.121 1.00 27.65 C ANISOU 997 CB VAL A 140 3389 3808 3307 -567 601 -20 C ATOM 998 CG1 VAL A 140 36.307 41.441 28.283 1.00 28.24 C ANISOU 998 CG1 VAL A 140 3486 3937 3307 -611 692 -9 C ATOM 999 CG2 VAL A 140 38.534 42.366 27.578 1.00 26.83 C ANISOU 999 CG2 VAL A 140 3315 3728 3150 -502 514 -10 C ATOM 1000 N ARG A 141 35.814 39.972 24.870 1.00 28.88 N ANISOU 1000 N ARG A 141 3361 3451 4159 -1019 379 -689 N ATOM 1001 CA ARG A 141 34.591 39.418 24.291 1.00 30.07 C ANISOU 1001 CA ARG A 141 3517 3664 4243 -1120 407 -749 C ATOM 1002 C ARG A 141 34.703 37.919 23.943 1.00 31.01 C ANISOU 1002 C ARG A 141 3719 3671 4392 -1179 445 -797 C ATOM 1003 O ARG A 141 33.764 37.150 24.160 1.00 31.15 O ANISOU 1003 O ARG A 141 3772 3690 4375 -1277 455 -818 O ATOM 1004 CB ARG A 141 34.227 40.219 23.040 1.00 29.91 C ANISOU 1004 CB ARG A 141 3434 3762 4169 -1117 409 -791 C ATOM 1005 CG ARG A 141 32.948 39.783 22.313 1.00 32.58 C ANISOU 1005 CG ARG A 141 3764 4175 4441 -1225 411 -849 C ATOM 1006 CD ARG A 141 32.947 40.127 20.817 1.00 34.79 C ANISOU 1006 CD ARG A 141 4038 4514 4667 -1234 408 -900 C ATOM 1007 NE ARG A 141 32.910 38.927 19.987 1.00 39.44 N ANISOU 1007 NE ARG A 141 4712 5038 5236 -1313 446 -971 N ATOM 1008 CZ ARG A 141 33.091 38.890 18.667 1.00 42.57 C ANISOU 1008 CZ ARG A 141 5154 5443 5576 -1340 464 -1028 C ATOM 1009 NH1 ARG A 141 33.024 37.719 18.032 1.00 45.00 N ANISOU 1009 NH1 ARG A 141 5556 5678 5863 -1421 507 -1098 N ATOM 1010 NH2 ARG A 141 33.344 39.993 17.974 1.00 42.37 N ANISOU 1010 NH2 ARG A 141 5100 5490 5510 -1294 443 -1018 N ATOM 1011 N GLN A 142 35.847 37.503 23.418 1.00 31.48 N ANISOU 1011 N GLN A 142 3807 3628 4527 -1119 473 -816 N ATOM 1012 CA GLN A 142 35.992 36.128 22.955 1.00 33.06 C ANISOU 1012 CA GLN A 142 4087 3713 4762 -1166 522 -872 C ATOM 1013 C GLN A 142 36.118 35.124 24.117 1.00 33.36 C ANISOU 1013 C GLN A 142 4197 3619 4859 -1187 498 -826 C ATOM 1014 O GLN A 142 35.831 33.948 23.938 1.00 34.39 O ANISOU 1014 O GLN A 142 4403 3668 4996 -1257 530 -867 O ATOM 1015 CB GLN A 142 37.136 36.007 21.925 1.00 33.96 C ANISOU 1015 CB GLN A 142 4206 3752 4947 -1099 585 -922 C ATOM 1016 CG GLN A 142 38.549 36.143 22.456 1.00 35.31 C ANISOU 1016 CG GLN A 142 4347 3809 5259 -981 576 -869 C ATOM 1017 CD GLN A 142 39.602 36.284 21.344 1.00 37.91 C ANISOU 1017 CD GLN A 142 4653 4092 5659 -916 661 -926 C ATOM 1018 OE1 GLN A 142 39.316 36.078 20.161 1.00 39.22 O ANISOU 1018 OE1 GLN A 142 4857 4286 5757 -968 737 -1011 O ATOM 1019 NE2 GLN A 142 40.818 36.644 21.733 1.00 38.44 N ANISOU 1019 NE2 GLN A 142 4661 4083 5862 -811 649 -878 N ATOM 1020 N LYS A 143 36.499 35.595 25.306 1.00 32.71 N ANISOU 1020 N LYS A 143 4108 3513 4807 -1139 437 -739 N ATOM 1021 CA LYS A 143 36.588 34.739 26.497 1.00 33.12 C ANISOU 1021 CA LYS A 143 4250 3441 4895 -1169 396 -680 C ATOM 1022 C LYS A 143 35.377 34.861 27.436 1.00 32.56 C ANISOU 1022 C LYS A 143 4211 3444 4718 -1268 383 -650 C ATOM 1023 O LYS A 143 34.940 33.875 28.008 1.00 33.36 O ANISOU 1023 O LYS A 143 4404 3466 4805 -1351 387 -641 O ATOM 1024 CB LYS A 143 37.874 35.035 27.274 1.00 33.26 C ANISOU 1024 CB LYS A 143 4266 3355 5017 -1065 324 -597 C ATOM 1025 CG LYS A 143 39.117 34.360 26.699 1.00 34.67 C ANISOU 1025 CG LYS A 143 4437 3386 5352 -983 340 -616 C ATOM 1026 CD LYS A 143 40.369 34.761 27.472 1.00 36.00 C ANISOU 1026 CD LYS A 143 4576 3460 5643 -881 249 -526 C ATOM 1027 CE LYS A 143 41.650 34.315 26.764 1.00 37.37 C ANISOU 1027 CE LYS A 143 4695 3503 6002 -783 283 -554 C ATOM 1028 NZ LYS A 143 41.914 32.866 26.959 1.00 39.58 N ANISOU 1028 NZ LYS A 143 5053 3598 6386 -794 280 -554 N ATOM 1029 N TRP A 144 34.848 36.067 27.604 1.00 31.26 N ANISOU 1029 N TRP A 144 3973 3419 4484 -1261 377 -637 N ATOM 1030 CA TRP A 144 33.776 36.311 28.575 1.00 30.99 C ANISOU 1030 CA TRP A 144 3959 3448 4367 -1345 385 -611 C ATOM 1031 C TRP A 144 32.503 36.939 27.997 1.00 30.58 C ANISOU 1031 C TRP A 144 3808 3562 4250 -1399 429 -665 C ATOM 1032 O TRP A 144 31.505 37.039 28.697 1.00 30.85 O ANISOU 1032 O TRP A 144 3843 3646 4234 -1477 459 -659 O ATOM 1033 CB TRP A 144 34.308 37.185 29.710 1.00 30.16 C ANISOU 1033 CB TRP A 144 3876 3331 4254 -1291 333 -529 C ATOM 1034 CG TRP A 144 35.427 36.542 30.419 1.00 29.95 C ANISOU 1034 CG TRP A 144 3948 3138 4293 -1255 264 -463 C ATOM 1035 CD1 TRP A 144 35.343 35.519 31.320 1.00 30.77 C ANISOU 1035 CD1 TRP A 144 4184 3119 4388 -1329 242 -422 C ATOM 1036 CD2 TRP A 144 36.819 36.835 30.271 1.00 28.53 C ANISOU 1036 CD2 TRP A 144 3740 2883 4215 -1139 198 -425 C ATOM 1037 NE1 TRP A 144 36.597 35.169 31.756 1.00 31.08 N ANISOU 1037 NE1 TRP A 144 4280 3009 4519 -1261 151 -354 N ATOM 1038 CE2 TRP A 144 37.524 35.968 31.133 1.00 30.04 C ANISOU 1038 CE2 TRP A 144 4041 2905 4466 -1142 124 -356 C ATOM 1039 CE3 TRP A 144 37.548 37.759 29.510 1.00 27.66 C ANISOU 1039 CE3 TRP A 144 3522 2829 4158 -1036 193 -438 C ATOM 1040 CZ2 TRP A 144 38.922 35.989 31.247 1.00 30.33 C ANISOU 1040 CZ2 TRP A 144 4062 2827 4633 -1040 38 -301 C ATOM 1041 CZ3 TRP A 144 38.943 37.784 29.630 1.00 28.37 C ANISOU 1041 CZ3 TRP A 144 3599 2808 4371 -941 126 -389 C ATOM 1042 CH2 TRP A 144 39.610 36.901 30.486 1.00 28.75 C ANISOU 1042 CH2 TRP A 144 3738 2689 4496 -941 46 -322 C ATOM 1043 N GLY A 145 32.534 37.342 26.730 1.00 30.25 N ANISOU 1043 N GLY A 145 3685 3596 4213 -1362 433 -717 N ATOM 1044 CA GLY A 145 31.381 37.945 26.078 1.00 30.13 C ANISOU 1044 CA GLY A 145 3571 3728 4150 -1407 446 -760 C ATOM 1045 C GLY A 145 31.223 39.427 26.394 1.00 29.44 C ANISOU 1045 C GLY A 145 3395 3745 4047 -1342 428 -726 C ATOM 1046 O GLY A 145 31.889 39.965 27.283 1.00 28.70 O ANISOU 1046 O GLY A 145 3329 3612 3963 -1280 413 -668 O ATOM 1047 N LEU A 146 30.332 40.083 25.649 1.00 29.60 N ANISOU 1047 N LEU A 146 3311 3889 4045 -1359 422 -759 N ATOM 1048 CA LEU A 146 30.048 41.507 25.815 1.00 29.16 C ANISOU 1048 CA LEU A 146 3161 3934 3986 -1298 407 -733 C ATOM 1049 C LEU A 146 28.555 41.752 25.721 1.00 29.43 C ANISOU 1049 C LEU A 146 3090 4072 4020 -1370 419 -761 C ATOM 1050 O LEU A 146 27.938 41.427 24.710 1.00 29.85 O ANISOU 1050 O LEU A 146 3098 4175 4070 -1424 392 -804 O ATOM 1051 CB LEU A 146 30.723 42.324 24.711 1.00 29.02 C ANISOU 1051 CB LEU A 146 3104 3958 3964 -1212 363 -737 C ATOM 1052 CG LEU A 146 32.110 42.890 24.945 1.00 29.21 C ANISOU 1052 CG LEU A 146 3164 3924 4009 -1105 349 -694 C ATOM 1053 CD1 LEU A 146 32.457 43.773 23.752 1.00 30.20 C ANISOU 1053 CD1 LEU A 146 3240 4114 4121 -1046 320 -706 C ATOM 1054 CD2 LEU A 146 32.210 43.671 26.255 1.00 29.57 C ANISOU 1054 CD2 LEU A 146 3212 3965 4059 -1066 349 -637 C ATOM 1055 N ASP A 147 27.994 42.351 26.765 1.00 29.22 N ANISOU 1055 N ASP A 147 3025 4072 4003 -1372 461 -737 N ATOM 1056 CA ASP A 147 26.571 42.670 26.832 1.00 29.84 C ANISOU 1056 CA ASP A 147 2981 4242 4115 -1431 490 -763 C ATOM 1057 C ASP A 147 26.341 44.141 26.508 1.00 28.73 C ANISOU 1057 C ASP A 147 2721 4193 4002 -1342 457 -748 C ATOM 1058 O ASP A 147 25.417 44.483 25.771 1.00 28.80 O ANISOU 1058 O ASP A 147 2604 4286 4052 -1360 420 -771 O ATOM 1059 CB ASP A 147 26.023 42.376 28.233 1.00 30.85 C ANISOU 1059 CB ASP A 147 3147 4332 4244 -1499 587 -755 C ATOM 1060 CG ASP A 147 25.353 41.021 28.338 1.00 34.06 C ANISOU 1060 CG ASP A 147 3590 4700 4650 -1633 628 -788 C ATOM 1061 OD1 ASP A 147 25.104 40.359 27.295 1.00 37.98 O ANISOU 1061 OD1 ASP A 147 4060 5216 5157 -1680 580 -824 O ATOM 1062 OD2 ASP A 147 25.027 40.542 29.446 1.00 37.45 O ANISOU 1062 OD2 ASP A 147 4088 5077 5064 -1709 711 -782 O ATOM 1063 N ARG A 148 27.173 45.013 27.073 1.00 26.85 N ANISOU 1063 N ARG A 148 2525 3930 3748 -1248 461 -708 N ATOM 1064 CA ARG A 148 27.037 46.449 26.826 1.00 26.15 C ANISOU 1064 CA ARG A 148 2339 3913 3684 -1159 432 -691 C ATOM 1065 C ARG A 148 28.344 47.208 26.955 1.00 24.60 C ANISOU 1065 C ARG A 148 2214 3677 3456 -1056 401 -648 C ATOM 1066 O ARG A 148 29.328 46.704 27.494 1.00 23.95 O ANISOU 1066 O ARG A 148 2248 3508 3344 -1051 408 -625 O ATOM 1067 CB ARG A 148 25.952 47.077 27.740 1.00 26.68 C ANISOU 1067 CB ARG A 148 2319 4017 3802 -1175 512 -699 C ATOM 1068 CG ARG A 148 26.430 47.561 29.100 1.00 27.08 C ANISOU 1068 CG ARG A 148 2462 4008 3820 -1147 585 -671 C ATOM 1069 CD ARG A 148 25.323 48.180 29.963 1.00 28.41 C ANISOU 1069 CD ARG A 148 2551 4205 4038 -1169 692 -693 C ATOM 1070 NE ARG A 148 24.855 49.451 29.406 1.00 28.40 N ANISOU 1070 NE ARG A 148 2403 4277 4109 -1082 662 -695 N ATOM 1071 CZ ARG A 148 24.038 50.304 30.013 1.00 29.43 C ANISOU 1071 CZ ARG A 148 2445 4430 4306 -1063 749 -713 C ATOM 1072 NH1 ARG A 148 23.575 50.061 31.236 1.00 30.58 N ANISOU 1072 NH1 ARG A 148 2642 4533 4445 -1132 890 -737 N ATOM 1073 NH2 ARG A 148 23.681 51.423 29.393 1.00 29.16 N ANISOU 1073 NH2 ARG A 148 2278 4452 4349 -975 700 -707 N ATOM 1074 N ILE A 149 28.315 48.433 26.438 1.00 24.20 N ANISOU 1074 N ILE A 149 2085 3688 3423 -978 360 -634 N ATOM 1075 CA ILE A 149 29.440 49.360 26.439 1.00 23.18 C ANISOU 1075 CA ILE A 149 2000 3536 3273 -881 327 -595 C ATOM 1076 C ILE A 149 28.913 50.779 26.651 1.00 23.00 C ANISOU 1076 C ILE A 149 1890 3567 3282 -817 330 -580 C ATOM 1077 O ILE A 149 27.959 51.197 25.997 1.00 22.17 O ANISOU 1077 O ILE A 149 1669 3533 3221 -815 303 -595 O ATOM 1078 CB ILE A 149 30.196 49.329 25.092 1.00 22.74 C ANISOU 1078 CB ILE A 149 1956 3488 3195 -850 258 -595 C ATOM 1079 CG1 ILE A 149 30.739 47.935 24.784 1.00 23.25 C ANISOU 1079 CG1 ILE A 149 2104 3489 3242 -906 266 -618 C ATOM 1080 CG2 ILE A 149 31.332 50.359 25.098 1.00 22.78 C ANISOU 1080 CG2 ILE A 149 1994 3472 3191 -755 233 -554 C ATOM 1081 CD1 ILE A 149 31.199 47.764 23.351 1.00 24.28 C ANISOU 1081 CD1 ILE A 149 2247 3631 3346 -902 224 -640 C ATOM 1082 N ILE A 150 29.553 51.514 27.553 1.00 22.78 N ANISOU 1082 N ILE A 150 1922 3497 3238 -765 356 -550 N ATOM 1083 CA ILE A 150 29.378 52.961 27.650 1.00 23.07 C ANISOU 1083 CA ILE A 150 1901 3565 3299 -688 352 -533 C ATOM 1084 C ILE A 150 30.763 53.573 27.497 1.00 22.33 C ANISOU 1084 C ILE A 150 1882 3433 3170 -618 300 -492 C ATOM 1085 O ILE A 150 31.694 53.167 28.180 1.00 22.34 O ANISOU 1085 O ILE A 150 1988 3362 3139 -629 306 -472 O ATOM 1086 CB ILE A 150 28.749 53.356 28.997 1.00 23.81 C ANISOU 1086 CB ILE A 150 2004 3637 3406 -704 451 -544 C ATOM 1087 CG1 ILE A 150 27.333 52.789 29.105 1.00 25.21 C ANISOU 1087 CG1 ILE A 150 2084 3854 3641 -775 518 -589 C ATOM 1088 CG2 ILE A 150 28.716 54.882 29.158 1.00 23.55 C ANISOU 1088 CG2 ILE A 150 1932 3617 3399 -616 455 -529 C ATOM 1089 CD1 ILE A 150 26.813 52.727 30.508 1.00 26.44 C ANISOU 1089 CD1 ILE A 150 2287 3968 3791 -828 647 -610 C ATOM 1090 N VAL A 151 30.900 54.540 26.600 1.00 21.83 N ANISOU 1090 N VAL A 151 1765 3412 3118 -553 244 -476 N ATOM 1091 CA VAL A 151 32.197 55.145 26.340 1.00 21.42 C ANISOU 1091 CA VAL A 151 1773 3326 3040 -495 201 -440 C ATOM 1092 C VAL A 151 32.109 56.666 26.364 1.00 21.58 C ANISOU 1092 C VAL A 151 1758 3366 3075 -420 185 -416 C ATOM 1093 O VAL A 151 31.135 57.263 25.907 1.00 21.50 O ANISOU 1093 O VAL A 151 1657 3412 3102 -399 171 -424 O ATOM 1094 CB VAL A 151 32.831 54.640 25.011 1.00 21.02 C ANISOU 1094 CB VAL A 151 1732 3286 2971 -501 151 -444 C ATOM 1095 CG1 VAL A 151 31.942 54.936 23.813 1.00 21.56 C ANISOU 1095 CG1 VAL A 151 1722 3431 3041 -505 103 -457 C ATOM 1096 CG2 VAL A 151 34.240 55.222 24.824 1.00 20.59 C ANISOU 1096 CG2 VAL A 151 1732 3187 2906 -448 128 -410 C ATOM 1097 N SER A 152 33.125 57.270 26.963 1.00 20.97 N ANISOU 1097 N SER A 152 1754 3235 2979 -384 182 -385 N ATOM 1098 CA SER A 152 33.318 58.706 26.924 1.00 21.04 C ANISOU 1098 CA SER A 152 1754 3248 2995 -315 162 -358 C ATOM 1099 C SER A 152 34.718 58.934 26.353 1.00 20.25 C ANISOU 1099 C SER A 152 1703 3117 2875 -289 111 -325 C ATOM 1100 O SER A 152 35.691 58.402 26.877 1.00 19.84 O ANISOU 1100 O SER A 152 1717 3006 2815 -308 111 -312 O ATOM 1101 CB SER A 152 33.158 59.277 28.329 1.00 21.35 C ANISOU 1101 CB SER A 152 1843 3241 3029 -310 219 -358 C ATOM 1102 OG SER A 152 31.799 59.190 28.754 1.00 23.01 O ANISOU 1102 OG SER A 152 1989 3479 3273 -331 288 -396 O ATOM 1103 N THR A 153 34.808 59.683 25.254 1.00 20.32 N ANISOU 1103 N THR A 153 1678 3162 2882 -250 68 -310 N ATOM 1104 CA THR A 153 36.068 59.871 24.554 1.00 20.29 C ANISOU 1104 CA THR A 153 1714 3134 2863 -236 40 -286 C ATOM 1105 C THR A 153 36.695 61.238 24.828 1.00 20.01 C ANISOU 1105 C THR A 153 1704 3069 2829 -184 21 -248 C ATOM 1106 O THR A 153 36.026 62.200 25.227 1.00 19.85 O ANISOU 1106 O THR A 153 1667 3058 2817 -147 21 -241 O ATOM 1107 CB THR A 153 35.907 59.696 23.016 1.00 20.81 C ANISOU 1107 CB THR A 153 1756 3248 2903 -250 10 -295 C ATOM 1108 OG1 THR A 153 35.280 60.861 22.464 1.00 20.72 O ANISOU 1108 OG1 THR A 153 1712 3276 2885 -210 -35 -273 O ATOM 1109 CG2 THR A 153 34.975 58.534 22.662 1.00 20.56 C ANISOU 1109 CG2 THR A 153 1692 3255 2866 -306 16 -336 C ATOM 1110 N TYR A 154 37.998 61.278 24.594 1.00 19.94 N ANISOU 1110 N TYR A 154 1733 3019 2824 -182 12 -227 N ATOM 1111 CA TYR A 154 38.844 62.440 24.811 1.00 19.78 C ANISOU 1111 CA TYR A 154 1744 2962 2810 -147 -8 -189 C ATOM 1112 C TYR A 154 39.665 62.556 23.520 1.00 20.03 C ANISOU 1112 C TYR A 154 1775 3000 2837 -150 -12 -180 C ATOM 1113 O TYR A 154 40.782 62.053 23.425 1.00 19.94 O ANISOU 1113 O TYR A 154 1773 2945 2860 -167 4 -178 O ATOM 1114 CB TYR A 154 39.755 62.226 26.032 1.00 19.95 C ANISOU 1114 CB TYR A 154 1813 2909 2856 -161 -14 -172 C ATOM 1115 CG TYR A 154 39.040 61.990 27.355 1.00 19.02 C ANISOU 1115 CG TYR A 154 1731 2773 2722 -180 2 -183 C ATOM 1116 CD1 TYR A 154 39.190 62.884 28.415 1.00 19.13 C ANISOU 1116 CD1 TYR A 154 1806 2742 2720 -172 -7 -164 C ATOM 1117 CD2 TYR A 154 38.231 60.867 27.559 1.00 18.75 C ANISOU 1117 CD2 TYR A 154 1683 2760 2682 -217 34 -216 C ATOM 1118 CE1 TYR A 154 38.537 62.675 29.632 1.00 18.86 C ANISOU 1118 CE1 TYR A 154 1827 2684 2656 -202 26 -181 C ATOM 1119 CE2 TYR A 154 37.576 60.655 28.772 1.00 18.69 C ANISOU 1119 CE2 TYR A 154 1719 2730 2651 -247 66 -229 C ATOM 1120 CZ TYR A 154 37.742 61.555 29.808 1.00 19.21 C ANISOU 1120 CZ TYR A 154 1855 2750 2693 -241 67 -213 C ATOM 1121 OH TYR A 154 37.094 61.359 31.015 1.00 19.46 O ANISOU 1121 OH TYR A 154 1952 2753 2687 -282 116 -232 O ATOM 1122 N GLN A 155 39.087 63.195 22.510 1.00 20.83 N ANISOU 1122 N GLN A 155 1865 3147 2900 -136 -31 -174 N ATOM 1123 CA GLN A 155 39.625 63.119 21.153 1.00 20.92 C ANISOU 1123 CA GLN A 155 1897 3171 2881 -160 -23 -176 C ATOM 1124 C GLN A 155 40.504 64.306 20.755 1.00 20.86 C ANISOU 1124 C GLN A 155 1924 3136 2866 -142 -28 -137 C ATOM 1125 O GLN A 155 40.201 65.461 21.055 1.00 20.21 O ANISOU 1125 O GLN A 155 1850 3051 2779 -103 -64 -105 O ATOM 1126 CB GLN A 155 38.488 62.898 20.146 1.00 21.68 C ANISOU 1126 CB GLN A 155 1984 3331 2923 -180 -53 -191 C ATOM 1127 CG GLN A 155 37.971 61.455 20.163 1.00 22.64 C ANISOU 1127 CG GLN A 155 2083 3472 3047 -225 -31 -237 C ATOM 1128 CD GLN A 155 36.804 61.209 19.223 1.00 24.93 C ANISOU 1128 CD GLN A 155 2360 3823 3289 -257 -79 -251 C ATOM 1129 OE1 GLN A 155 35.690 60.933 19.674 1.00 25.62 O ANISOU 1129 OE1 GLN A 155 2390 3944 3402 -256 -104 -263 O ATOM 1130 NE2 GLN A 155 37.060 61.285 17.920 1.00 24.92 N ANISOU 1130 NE2 GLN A 155 2416 3834 3219 -293 -92 -250 N ATOM 1131 N ALA A 156 41.633 63.973 20.130 1.00 20.82 N ANISOU 1131 N ALA A 156 1938 3101 2872 -172 20 -144 N ATOM 1132 CA ALA A 156 42.566 64.911 19.523 1.00 21.25 C ANISOU 1132 CA ALA A 156 2027 3129 2920 -176 37 -116 C ATOM 1133 C ALA A 156 42.016 65.611 18.289 1.00 22.07 C ANISOU 1133 C ALA A 156 2185 3271 2932 -190 14 -99 C ATOM 1134 O ALA A 156 41.154 65.092 17.599 1.00 23.06 O ANISOU 1134 O ALA A 156 2322 3440 2998 -214 -6 -119 O ATOM 1135 CB ALA A 156 43.856 64.172 19.160 1.00 21.38 C ANISOU 1135 CB ALA A 156 2033 3099 2991 -211 117 -140 C ATOM 1136 N VAL A 157 42.558 66.783 17.995 1.00 22.82 N ANISOU 1136 N VAL A 157 2318 3340 3011 -183 7 -59 N ATOM 1137 CA VAL A 157 42.060 67.625 16.907 1.00 23.73 C ANISOU 1137 CA VAL A 157 2502 3477 3035 -195 -34 -28 C ATOM 1138 C VAL A 157 42.567 67.207 15.516 1.00 24.54 C ANISOU 1138 C VAL A 157 2680 3582 3061 -270 28 -47 C ATOM 1139 O VAL A 157 41.975 67.606 14.508 1.00 24.46 O ANISOU 1139 O VAL A 157 2747 3596 2952 -299 -20 -25 O ATOM 1140 CB VAL A 157 42.385 69.123 17.172 1.00 24.11 C ANISOU 1140 CB VAL A 157 2580 3488 3091 -161 -68 27 C ATOM 1141 CG1 VAL A 157 41.804 69.562 18.515 1.00 23.50 C ANISOU 1141 CG1 VAL A 157 2450 3402 3076 -93 -117 38 C ATOM 1142 CG2 VAL A 157 43.892 69.386 17.149 1.00 24.37 C ANISOU 1142 CG2 VAL A 157 2628 3468 3164 -193 9 32 C ATOM 1143 N SER A 158 43.636 66.408 15.446 1.00 24.75 N ANISOU 1143 N SER A 158 2691 3576 3135 -306 134 -89 N ATOM 1144 CA SER A 158 44.158 65.958 14.146 1.00 26.21 C ANISOU 1144 CA SER A 158 2955 3752 3250 -384 226 -122 C ATOM 1145 C SER A 158 43.162 65.098 13.371 1.00 27.22 C ANISOU 1145 C SER A 158 3134 3927 3282 -428 200 -155 C ATOM 1146 O SER A 158 43.312 64.917 12.171 1.00 28.00 O ANISOU 1146 O SER A 158 3337 4023 3280 -503 251 -175 O ATOM 1147 CB SER A 158 45.481 65.197 14.277 1.00 26.09 C ANISOU 1147 CB SER A 158 2892 3682 3339 -404 358 -168 C ATOM 1148 OG SER A 158 45.327 64.004 15.015 1.00 25.92 O ANISOU 1148 OG SER A 158 2792 3659 3396 -380 363 -207 O ATOM 1149 N GLY A 159 42.167 64.559 14.067 1.00 27.68 N ANISOU 1149 N GLY A 159 3126 4023 3370 -390 125 -163 N ATOM 1150 CA GLY A 159 41.076 63.839 13.437 1.00 29.31 C ANISOU 1150 CA GLY A 159 3364 4276 3494 -431 72 -187 C ATOM 1151 C GLY A 159 40.156 64.720 12.603 1.00 30.53 C ANISOU 1151 C GLY A 159 3593 4466 3543 -448 -45 -135 C ATOM 1152 O GLY A 159 39.469 64.222 11.715 1.00 31.54 O ANISOU 1152 O GLY A 159 3785 4623 3576 -510 -90 -150 O ATOM 1153 N ALA A 160 40.131 66.019 12.909 1.00 30.84 N ANISOU 1153 N ALA A 160 3624 4494 3600 -394 -105 -73 N ATOM 1154 CA ALA A 160 39.394 67.005 12.122 1.00 31.86 C ANISOU 1154 CA ALA A 160 3827 4636 3643 -402 -224 -11 C ATOM 1155 C ALA A 160 40.249 67.614 11.017 1.00 32.82 C ANISOU 1155 C ALA A 160 4094 4721 3656 -471 -176 12 C ATOM 1156 O ALA A 160 39.754 68.423 10.240 1.00 34.33 O ANISOU 1156 O ALA A 160 4376 4910 3756 -492 -277 70 O ATOM 1157 CB ALA A 160 38.850 68.101 13.023 1.00 31.67 C ANISOU 1157 CB ALA A 160 3725 4607 3702 -304 -310 43 C ATOM 1158 N GLY A 161 41.529 67.248 10.955 1.00 32.41 N ANISOU 1158 N GLY A 161 4062 4631 3621 -508 -22 -31 N ATOM 1159 CA GLY A 161 42.391 67.632 9.840 1.00 33.10 C ANISOU 1159 CA GLY A 161 4292 4679 3604 -594 63 -27 C ATOM 1160 C GLY A 161 43.447 68.665 10.192 1.00 32.58 C ANISOU 1160 C GLY A 161 4217 4564 3597 -570 126 6 C ATOM 1161 O GLY A 161 43.497 69.165 11.319 1.00 31.65 O ANISOU 1161 O GLY A 161 3992 4439 3594 -485 88 30 O ATOM 1162 N MET A 162 44.284 68.988 9.208 1.00 33.16 N ANISOU 1162 N MET A 162 4416 4599 3585 -656 226 4 N ATOM 1163 CA MET A 162 45.404 69.916 9.381 1.00 32.94 C ANISOU 1163 CA MET A 162 4388 4518 3609 -658 307 30 C ATOM 1164 C MET A 162 44.949 71.314 9.794 1.00 31.56 C ANISOU 1164 C MET A 162 4220 4335 3436 -597 170 117 C ATOM 1165 O MET A 162 45.583 71.942 10.624 1.00 30.64 O ANISOU 1165 O MET A 162 4029 4187 3427 -549 190 135 O ATOM 1166 CB MET A 162 46.228 69.997 8.089 1.00 34.54 C ANISOU 1166 CB MET A 162 4748 4681 3697 -779 447 10 C ATOM 1167 CG MET A 162 47.523 70.802 8.210 1.00 36.82 C ANISOU 1167 CG MET A 162 5023 4910 4057 -799 565 24 C ATOM 1168 SD MET A 162 48.729 70.036 9.332 1.00 40.01 S ANISOU 1168 SD MET A 162 5216 5286 4702 -747 699 -40 S ATOM 1169 CE MET A 162 48.832 71.203 10.577 1.00 37.58 C ANISOU 1169 CE MET A 162 4808 4964 4505 -657 583 31 C ATOM 1170 N GLY A 163 43.851 71.788 9.217 1.00 30.99 N ANISOU 1170 N GLY A 163 4237 4283 3254 -599 26 170 N ATOM 1171 CA GLY A 163 43.284 73.075 9.577 1.00 30.30 C ANISOU 1171 CA GLY A 163 4153 4179 3182 -531 -111 252 C ATOM 1172 C GLY A 163 42.917 73.165 11.048 1.00 28.61 C ANISOU 1172 C GLY A 163 3772 3977 3122 -412 -161 248 C ATOM 1173 O GLY A 163 43.137 74.188 11.682 1.00 28.03 O ANISOU 1173 O GLY A 163 3677 3865 3109 -360 -187 288 O ATOM 1174 N ALA A 164 42.359 72.090 11.592 1.00 27.58 N ANISOU 1174 N ALA A 164 3537 3894 3048 -380 -168 197 N ATOM 1175 CA ALA A 164 41.988 72.042 13.004 1.00 26.32 C ANISOU 1175 CA ALA A 164 3237 3745 3021 -283 -199 185 C ATOM 1176 C ALA A 164 43.217 72.069 13.928 1.00 25.27 C ANISOU 1176 C ALA A 164 3042 3572 2987 -271 -96 162 C ATOM 1177 O ALA A 164 43.165 72.657 15.002 1.00 24.23 O ANISOU 1177 O ALA A 164 2851 3419 2935 -206 -129 178 O ATOM 1178 CB ALA A 164 41.146 70.827 13.280 1.00 25.99 C ANISOU 1178 CB ALA A 164 3115 3758 3002 -270 -220 137 C ATOM 1179 N ILE A 165 44.304 71.425 13.503 1.00 25.43 N ANISOU 1179 N ILE A 165 3076 3578 3008 -339 27 122 N ATOM 1180 CA ILE A 165 45.581 71.467 14.217 1.00 25.32 C ANISOU 1180 CA ILE A 165 2999 3519 3104 -339 115 106 C ATOM 1181 C ILE A 165 46.129 72.894 14.253 1.00 25.72 C ANISOU 1181 C ILE A 165 3100 3519 3154 -340 101 163 C ATOM 1182 O ILE A 165 46.558 73.364 15.303 1.00 25.37 O ANISOU 1182 O ILE A 165 2995 3442 3202 -301 85 176 O ATOM 1183 CB ILE A 165 46.632 70.543 13.545 1.00 25.80 C ANISOU 1183 CB ILE A 165 3060 3563 3178 -414 262 52 C ATOM 1184 CG1 ILE A 165 46.308 69.070 13.790 1.00 25.49 C ANISOU 1184 CG1 ILE A 165 2953 3555 3177 -405 286 -10 C ATOM 1185 CG2 ILE A 165 48.049 70.866 14.047 1.00 26.04 C ANISOU 1185 CG2 ILE A 165 3028 3534 3331 -425 345 52 C ATOM 1186 CD1 ILE A 165 47.075 68.116 12.862 1.00 26.23 C ANISOU 1186 CD1 ILE A 165 3075 3630 3260 -481 434 -72 C ATOM 1187 N LEU A 166 46.124 73.569 13.108 1.00 26.46 N ANISOU 1187 N LEU A 166 3318 3600 3136 -395 104 198 N ATOM 1188 CA LEU A 166 46.701 74.909 13.014 1.00 27.18 C ANISOU 1188 CA LEU A 166 3475 3635 3218 -411 101 253 C ATOM 1189 C LEU A 166 45.888 75.904 13.822 1.00 26.34 C ANISOU 1189 C LEU A 166 3358 3515 3136 -323 -29 302 C ATOM 1190 O LEU A 166 46.440 76.840 14.403 1.00 26.45 O ANISOU 1190 O LEU A 166 3371 3476 3202 -310 -33 331 O ATOM 1191 CB LEU A 166 46.798 75.373 11.557 1.00 28.58 C ANISOU 1191 CB LEU A 166 3813 3796 3251 -499 130 283 C ATOM 1192 CG LEU A 166 47.766 74.558 10.693 1.00 30.45 C ANISOU 1192 CG LEU A 166 4082 4027 3460 -601 298 228 C ATOM 1193 CD1 LEU A 166 47.618 74.926 9.217 1.00 32.12 C ANISOU 1193 CD1 LEU A 166 4489 4226 3491 -700 316 256 C ATOM 1194 CD2 LEU A 166 49.213 74.726 11.161 1.00 31.77 C ANISOU 1194 CD2 LEU A 166 4170 4144 3757 -627 424 207 C ATOM 1195 N GLU A 167 44.579 75.685 13.861 1.00 25.86 N ANISOU 1195 N GLU A 167 3284 3495 3048 -268 -129 308 N ATOM 1196 CA GLU A 167 43.666 76.525 14.622 1.00 25.56 C ANISOU 1196 CA GLU A 167 3221 3440 3050 -176 -238 344 C ATOM 1197 C GLU A 167 43.923 76.385 16.113 1.00 24.34 C ANISOU 1197 C GLU A 167 2963 3274 3011 -123 -215 310 C ATOM 1198 O GLU A 167 43.818 77.357 16.858 1.00 24.13 O ANISOU 1198 O GLU A 167 2942 3200 3027 -73 -254 336 O ATOM 1199 CB GLU A 167 42.214 76.153 14.303 1.00 25.78 C ANISOU 1199 CB GLU A 167 3231 3516 3048 -134 -339 349 C ATOM 1200 CG GLU A 167 41.183 76.788 15.222 1.00 25.70 C ANISOU 1200 CG GLU A 167 3157 3491 3118 -29 -426 367 C ATOM 1201 CD GLU A 167 39.788 76.753 14.633 1.00 26.60 C ANISOU 1201 CD GLU A 167 3261 3635 3212 7 -544 394 C ATOM 1202 OE1 GLU A 167 38.931 76.019 15.158 1.00 28.29 O ANISOU 1202 OE1 GLU A 167 3370 3894 3484 48 -562 356 O ATOM 1203 OE2 GLU A 167 39.545 77.468 13.653 1.00 26.52 O ANISOU 1203 OE2 GLU A 167 3347 3597 3131 -11 -625 457 O ATOM 1204 N THR A 168 44.258 75.169 16.540 1.00 23.56 N ANISOU 1204 N THR A 168 2784 3209 2958 -139 -155 254 N ATOM 1205 CA THR A 168 44.469 74.869 17.947 1.00 22.70 C ANISOU 1205 CA THR A 168 2593 3089 2944 -101 -145 225 C ATOM 1206 C THR A 168 45.764 75.505 18.435 1.00 22.85 C ANISOU 1206 C THR A 168 2620 3045 3016 -132 -109 240 C ATOM 1207 O THR A 168 45.808 76.112 19.508 1.00 21.96 O ANISOU 1207 O THR A 168 2502 2892 2949 -99 -143 249 O ATOM 1208 CB THR A 168 44.483 73.338 18.161 1.00 22.22 C ANISOU 1208 CB THR A 168 2455 3073 2914 -117 -101 169 C ATOM 1209 OG1 THR A 168 43.213 72.785 17.775 1.00 22.38 O ANISOU 1209 OG1 THR A 168 2464 3150 2889 -94 -144 155 O ATOM 1210 CG2 THR A 168 44.606 72.995 19.621 1.00 21.67 C ANISOU 1210 CG2 THR A 168 2321 2987 2926 -86 -108 146 C ATOM 1211 N GLN A 169 46.808 75.377 17.621 1.00 23.44 N ANISOU 1211 N GLN A 169 2714 3108 3086 -203 -35 240 N ATOM 1212 CA GLN A 169 48.104 75.985 17.898 1.00 23.86 C ANISOU 1212 CA GLN A 169 2764 3101 3202 -246 4 257 C ATOM 1213 C GLN A 169 48.027 77.518 17.915 1.00 24.28 C ANISOU 1213 C GLN A 169 2904 3101 3220 -237 -46 311 C ATOM 1214 O GLN A 169 48.622 78.162 18.774 1.00 24.33 O ANISOU 1214 O GLN A 169 2903 3055 3287 -239 -65 325 O ATOM 1215 CB GLN A 169 49.137 75.501 16.870 1.00 24.38 C ANISOU 1215 CB GLN A 169 2825 3163 3275 -327 118 239 C ATOM 1216 CG GLN A 169 49.461 74.002 17.000 1.00 24.41 C ANISOU 1216 CG GLN A 169 2731 3194 3349 -335 180 182 C ATOM 1217 CD GLN A 169 50.406 73.492 15.923 1.00 26.15 C ANISOU 1217 CD GLN A 169 2949 3403 3583 -412 316 152 C ATOM 1218 OE1 GLN A 169 50.333 73.926 14.772 1.00 28.83 O ANISOU 1218 OE1 GLN A 169 3391 3744 3816 -463 364 164 O ATOM 1219 NE2 GLN A 169 51.292 72.569 16.293 1.00 25.55 N ANISOU 1219 NE2 GLN A 169 2761 3307 3639 -423 382 113 N ATOM 1220 N ARG A 170 47.281 78.089 16.978 1.00 27.07 N ANISOU 1220 N ARG A 170 3568 4126 2593 -1033 0 96 N ATOM 1221 CA ARG A 170 47.103 79.543 16.894 1.00 28.18 C ANISOU 1221 CA ARG A 170 3932 4126 2651 -1135 21 349 C ATOM 1222 C ARG A 170 46.380 80.078 18.120 1.00 26.96 C ANISOU 1222 C ARG A 170 3905 3649 2689 -991 -6 415 C ATOM 1223 O ARG A 170 46.795 81.069 18.684 1.00 27.37 O ANISOU 1223 O ARG A 170 4092 3531 2775 -1064 9 479 O ATOM 1224 CB ARG A 170 46.321 79.941 15.641 1.00 29.85 C ANISOU 1224 CB ARG A 170 4209 4429 2704 -1153 -53 526 C ATOM 1225 CG ARG A 170 45.900 81.413 15.633 1.00 32.58 C ANISOU 1225 CG ARG A 170 4831 4494 3054 -1197 -147 814 C ATOM 1226 CD ARG A 170 45.111 81.841 14.417 1.00 36.59 C ANISOU 1226 CD ARG A 170 5440 5054 3408 -1204 -293 1034 C ATOM 1227 NE ARG A 170 43.796 81.204 14.327 1.00 36.81 N ANISOU 1227 NE ARG A 170 5364 5078 3545 -917 -371 941 N ATOM 1228 CZ ARG A 170 42.759 81.461 15.123 1.00 36.96 C ANISOU 1228 CZ ARG A 170 5411 4833 3797 -665 -451 899 C ATOM 1229 NH1 ARG A 170 42.844 82.351 16.110 1.00 37.27 N ANISOU 1229 NH1 ARG A 170 5582 4571 4007 -622 -480 911 N ATOM 1230 NH2 ARG A 170 41.616 80.813 14.927 1.00 36.84 N ANISOU 1230 NH2 ARG A 170 5254 4904 3838 -462 -504 793 N ATOM 1231 N GLU A 171 45.288 79.424 18.507 1.00 25.98 N ANISOU 1231 N GLU A 171 3709 3482 2679 -809 -48 369 N ATOM 1232 CA GLU A 171 44.486 79.847 19.653 1.00 25.56 C ANISOU 1232 CA GLU A 171 3697 3260 2755 -686 -55 363 C ATOM 1233 C GLU A 171 45.335 79.794 20.915 1.00 25.03 C ANISOU 1233 C GLU A 171 3626 3151 2731 -752 12 279 C ATOM 1234 O GLU A 171 45.326 80.722 21.711 1.00 25.49 O ANISOU 1234 O GLU A 171 3762 3085 2838 -730 26 261 O ATOM 1235 CB GLU A 171 43.227 78.969 19.815 1.00 24.92 C ANISOU 1235 CB GLU A 171 3479 3257 2733 -562 -86 309 C ATOM 1236 CG GLU A 171 42.099 79.288 18.835 1.00 25.87 C ANISOU 1236 CG GLU A 171 3594 3400 2836 -435 -174 357 C ATOM 1237 CD GLU A 171 40.943 78.292 18.883 1.00 25.48 C ANISOU 1237 CD GLU A 171 3366 3481 2836 -362 -193 273 C ATOM 1238 OE1 GLU A 171 40.121 78.255 17.928 1.00 25.89 O ANISOU 1238 OE1 GLU A 171 3368 3607 2864 -265 -274 277 O ATOM 1239 OE2 GLU A 171 40.839 77.549 19.878 1.00 24.79 O ANISOU 1239 OE2 GLU A 171 3188 3436 2796 -431 -144 219 O ATOM 1240 N LEU A 172 46.080 78.707 21.086 1.00 24.45 N ANISOU 1240 N LEU A 172 3454 3178 2657 -813 14 199 N ATOM 1241 CA LEU A 172 46.919 78.541 22.271 1.00 24.26 C ANISOU 1241 CA LEU A 172 3425 3128 2663 -866 30 129 C ATOM 1242 C LEU A 172 48.031 79.587 22.328 1.00 24.54 C ANISOU 1242 C LEU A 172 3539 3127 2658 -971 93 99 C ATOM 1243 O LEU A 172 48.338 80.092 23.394 1.00 24.55 O ANISOU 1243 O LEU A 172 3580 3064 2683 -985 119 56 O ATOM 1244 CB LEU A 172 47.497 77.124 22.341 1.00 23.88 C ANISOU 1244 CB LEU A 172 3267 3136 2670 -874 -73 41 C ATOM 1245 CG LEU A 172 46.488 76.044 22.736 1.00 24.26 C ANISOU 1245 CG LEU A 172 3272 3154 2791 -845 -174 108 C ATOM 1246 CD1 LEU A 172 46.993 74.672 22.352 1.00 24.86 C ANISOU 1246 CD1 LEU A 172 3257 3196 2991 -826 -362 8 C ATOM 1247 CD2 LEU A 172 46.159 76.095 24.221 1.00 25.18 C ANISOU 1247 CD2 LEU A 172 3431 3266 2871 -908 -164 193 C ATOM 1248 N ARG A 173 48.611 79.929 21.182 1.00 25.93 N ANISOU 1248 N ARG A 173 3724 3381 2746 -1081 116 120 N ATOM 1249 CA ARG A 173 49.640 80.972 21.119 1.00 26.97 C ANISOU 1249 CA ARG A 173 3932 3496 2819 -1268 174 129 C ATOM 1250 C ARG A 173 49.061 82.357 21.410 1.00 28.17 C ANISOU 1250 C ARG A 173 4283 3378 3043 -1263 142 264 C ATOM 1251 O ARG A 173 49.703 83.184 22.068 1.00 28.92 O ANISOU 1251 O ARG A 173 4449 3349 3188 -1355 157 224 O ATOM 1252 CB ARG A 173 50.316 80.988 19.752 1.00 28.76 C ANISOU 1252 CB ARG A 173 4098 3962 2865 -1466 212 144 C ATOM 1253 CG ARG A 173 51.455 80.001 19.608 1.00 29.21 C ANISOU 1253 CG ARG A 173 3913 4315 2870 -1510 238 -127 C ATOM 1254 CD ARG A 173 51.956 79.893 18.200 1.00 32.83 C ANISOU 1254 CD ARG A 173 4230 5145 3099 -1698 290 -187 C ATOM 1255 NE ARG A 173 52.932 78.815 18.041 1.00 34.09 N ANISOU 1255 NE ARG A 173 4083 5620 3250 -1658 274 -568 N ATOM 1256 CZ ARG A 173 52.875 77.857 17.117 1.00 34.06 C ANISOU 1256 CZ ARG A 173 3856 5900 3188 -1580 224 -785 C ATOM 1257 NH1 ARG A 173 51.878 77.804 16.243 1.00 33.83 N ANISOU 1257 NH1 ARG A 173 3880 5906 3069 -1556 209 -630 N ATOM 1258 NH2 ARG A 173 53.826 76.935 17.070 1.00 34.56 N ANISOU 1258 NH2 ARG A 173 3616 6216 3301 -1498 157 -1211 N ATOM 1259 N GLU A 174 47.853 82.618 20.929 1.00 28.25 N ANISOU 1259 N GLU A 174 4368 3280 3087 -1134 61 384 N ATOM 1260 CA GLU A 174 47.196 83.890 21.207 1.00 30.19 C ANISOU 1260 CA GLU A 174 4781 3225 3467 -1051 -52 446 C ATOM 1261 C GLU A 174 46.940 84.050 22.710 1.00 29.34 C ANISOU 1261 C GLU A 174 4608 3053 3488 -900 -30 235 C ATOM 1262 O GLU A 174 47.103 85.135 23.248 1.00 31.19 O ANISOU 1262 O GLU A 174 4939 3064 3847 -895 -98 170 O ATOM 1263 CB GLU A 174 45.896 84.021 20.412 1.00 31.32 C ANISOU 1263 CB GLU A 174 4970 3296 3633 -886 -185 558 C ATOM 1264 CG GLU A 174 46.113 84.317 18.930 1.00 34.61 C ANISOU 1264 CG GLU A 174 5515 3741 3896 -1069 -263 814 C ATOM 1265 CD GLU A 174 44.817 84.392 18.129 1.00 37.54 C ANISOU 1265 CD GLU A 174 5926 4061 4277 -883 -429 922 C ATOM 1266 OE1 GLU A 174 43.770 83.911 18.614 1.00 37.15 O ANISOU 1266 OE1 GLU A 174 5736 4045 4335 -620 -435 755 O ATOM 1267 OE2 GLU A 174 44.847 84.934 17.001 1.00 42.48 O ANISOU 1267 OE2 GLU A 174 6715 4648 4778 -1027 -564 1181 O ATOM 1268 N VAL A 175 46.568 82.969 23.391 1.00 27.50 N ANISOU 1268 N VAL A 175 4207 3030 3213 -809 45 129 N ATOM 1269 CA VAL A 175 46.356 83.027 24.841 1.00 27.52 C ANISOU 1269 CA VAL A 175 4120 3095 3243 -732 83 -55 C ATOM 1270 C VAL A 175 47.680 83.207 25.589 1.00 27.50 C ANISOU 1270 C VAL A 175 4131 3100 3218 -868 135 -136 C ATOM 1271 O VAL A 175 47.831 84.134 26.393 1.00 28.75 O ANISOU 1271 O VAL A 175 4311 3165 3448 -842 120 -286 O ATOM 1272 CB VAL A 175 45.626 81.768 25.378 1.00 26.33 C ANISOU 1272 CB VAL A 175 3808 3196 3002 -696 128 -70 C ATOM 1273 CG1 VAL A 175 45.508 81.817 26.908 1.00 26.75 C ANISOU 1273 CG1 VAL A 175 3757 3418 2987 -699 178 -229 C ATOM 1274 CG2 VAL A 175 44.241 81.633 24.749 1.00 26.93 C ANISOU 1274 CG2 VAL A 175 3824 3305 3102 -564 86 -46 C ATOM 1275 N LEU A 176 48.644 82.335 25.306 1.00 26.54 N ANISOU 1275 N LEU A 176 3969 3097 3016 -992 171 -90 N ATOM 1276 CA LEU A 176 49.895 82.287 26.070 1.00 26.84 C ANISOU 1276 CA LEU A 176 3971 3200 3026 -1094 198 -204 C ATOM 1277 C LEU A 176 50.943 83.349 25.678 1.00 28.21 C ANISOU 1277 C LEU A 176 4226 3258 3235 -1262 220 -232 C ATOM 1278 O LEU A 176 51.738 83.780 26.517 1.00 29.06 O ANISOU 1278 O LEU A 176 4315 3368 3360 -1324 235 -374 O ATOM 1279 CB LEU A 176 50.497 80.886 25.969 1.00 26.00 C ANISOU 1279 CB LEU A 176 3758 3255 2864 -1114 162 -206 C ATOM 1280 CG LEU A 176 49.594 79.766 26.516 1.00 26.03 C ANISOU 1280 CG LEU A 176 3712 3335 2844 -1030 95 -134 C ATOM 1281 CD1 LEU A 176 50.044 78.420 25.999 1.00 26.75 C ANISOU 1281 CD1 LEU A 176 3732 3463 2970 -1025 -24 -125 C ATOM 1282 CD2 LEU A 176 49.582 79.774 28.022 1.00 27.36 C ANISOU 1282 CD2 LEU A 176 3861 3597 2936 -1044 84 -177 C ATOM 1283 N ASN A 177 50.954 83.764 24.415 1.00 29.00 N ANISOU 1283 N ASN A 177 4413 3285 3321 -1376 211 -85 N ATOM 1284 CA ASN A 177 51.940 84.738 23.933 1.00 30.81 C ANISOU 1284 CA ASN A 177 4730 3436 3540 -1641 225 -44 C ATOM 1285 C ASN A 177 51.397 86.171 23.890 1.00 33.41 C ANISOU 1285 C ASN A 177 5278 3392 4025 -1661 102 61 C ATOM 1286 O ASN A 177 52.139 87.122 24.159 1.00 35.34 O ANISOU 1286 O ASN A 177 5607 3473 4348 -1847 72 29 O ATOM 1287 CB ASN A 177 52.490 84.331 22.554 1.00 31.30 C ANISOU 1287 CB ASN A 177 4738 3728 3425 -1853 276 63 C ATOM 1288 CG ASN A 177 53.353 83.064 22.599 1.00 29.44 C ANISOU 1288 CG ASN A 177 4252 3838 3097 -1836 341 -154 C ATOM 1289 OD1 ASN A 177 53.777 82.613 23.664 1.00 28.00 O ANISOU 1289 OD1 ASN A 177 3976 3683 2979 -1723 327 -335 O ATOM 1290 ND2 ASN A 177 53.626 82.500 21.432 1.00 28.43 N ANISOU 1290 ND2 ASN A 177 4002 3983 2816 -1939 375 -161 N ATOM 1291 N ASP A 178 50.112 86.326 23.560 1.00 34.04 N ANISOU 1291 N ASP A 178 5439 3314 4180 -1461 -6 161 N ATOM 1292 CA ASP A 178 49.490 87.654 23.417 1.00 37.26 C ANISOU 1292 CA ASP A 178 6059 3305 4793 -1412 -217 239 C ATOM 1293 C ASP A 178 48.491 87.998 24.530 1.00 37.50 C ANISOU 1293 C ASP A 178 6021 3209 5020 -1072 -306 -35 C ATOM 1294 O ASP A 178 47.911 89.079 24.520 1.00 40.17 O ANISOU 1294 O ASP A 178 6493 3180 5590 -948 -536 -72 O ATOM 1295 CB ASP A 178 48.769 87.779 22.066 1.00 38.76 C ANISOU 1295 CB ASP A 178 6394 3399 4935 -1429 -352 533 C ATOM 1296 CG ASP A 178 49.649 87.407 20.886 1.00 40.25 C ANISOU 1296 CG ASP A 178 6597 3839 4855 -1785 -251 769 C ATOM 1297 OD1 ASP A 178 50.863 87.713 20.908 1.00 42.46 O ANISOU 1297 OD1 ASP A 178 6882 4190 5059 -2105 -169 778 O ATOM 1298 OD2 ASP A 178 49.200 86.811 19.881 1.00 41.72 O ANISOU 1298 OD2 ASP A 178 6756 4221 4876 -1781 -245 917 O ATOM 1299 N GLY A 179 48.267 87.075 25.465 1.00 35.25 N ANISOU 1299 N GLY A 179 5515 3245 4635 -931 -155 -236 N ATOM 1300 CA GLY A 179 47.395 87.321 26.602 1.00 35.91 C ANISOU 1300 CA GLY A 179 5460 3376 4808 -673 -188 -540 C ATOM 1301 C GLY A 179 45.907 87.412 26.305 1.00 36.86 C ANISOU 1301 C GLY A 179 5528 3465 5011 -408 -305 -596 C ATOM 1302 O GLY A 179 45.160 87.975 27.088 1.00 38.68 O ANISOU 1302 O GLY A 179 5635 3696 5365 -184 -388 -915 O ATOM 1303 N VAL A 180 45.465 86.851 25.184 1.00 36.13 N ANISOU 1303 N VAL A 180 5487 3395 4845 -421 -316 -344 N ATOM 1304 CA VAL A 180 44.042 86.834 24.837 1.00 36.98 C ANISOU 1304 CA VAL A 180 5515 3518 5017 -168 -429 -407 C ATOM 1305 C VAL A 180 43.305 85.852 25.754 1.00 35.52 C ANISOU 1305 C VAL A 180 5040 3777 4680 -86 -256 -613 C ATOM 1306 O VAL A 180 43.827 84.789 26.069 1.00 33.48 O ANISOU 1306 O VAL A 180 4715 3774 4230 -262 -80 -514 O ATOM 1307 CB VAL A 180 43.832 86.439 23.344 1.00 36.49 C ANISOU 1307 CB VAL A 180 5577 3408 4879 -234 -487 -76 C ATOM 1308 CG1 VAL A 180 42.353 86.234 23.022 1.00 36.96 C ANISOU 1308 CG1 VAL A 180 5508 3554 4980 31 -587 -168 C ATOM 1309 CG2 VAL A 180 44.442 87.501 22.420 1.00 39.07 C ANISOU 1309 CG2 VAL A 180 6205 3338 5302 -382 -689 181 C ATOM 1310 N LYS A 181 42.106 86.222 26.194 1.00 37.48 N ANISOU 1310 N LYS A 181 5105 4124 5012 164 -337 -909 N ATOM 1311 CA LYS A 181 41.257 85.333 26.990 1.00 37.01 C ANISOU 1311 CA LYS A 181 4743 4561 4760 174 -173 -1089 C ATOM 1312 C LYS A 181 40.619 84.266 26.089 1.00 35.31 C ANISOU 1312 C LYS A 181 4494 4482 4441 123 -129 -857 C ATOM 1313 O LYS A 181 40.275 84.556 24.938 1.00 35.22 O ANISOU 1313 O LYS A 181 4602 4230 4549 238 -282 -728 O ATOM 1314 CB LYS A 181 40.168 86.134 27.705 1.00 40.64 C ANISOU 1314 CB LYS A 181 4945 5171 5326 454 -269 -1569 C ATOM 1315 CG LYS A 181 40.709 87.087 28.761 1.00 43.25 C ANISOU 1315 CG LYS A 181 5235 5449 5748 516 -309 -1902 C ATOM 1316 CD LYS A 181 39.604 87.880 29.417 1.00 48.02 C ANISOU 1316 CD LYS A 181 5525 6242 6480 839 -435 -2484 C ATOM 1317 CE LYS A 181 40.173 88.936 30.349 1.00 51.76 C ANISOU 1317 CE LYS A 181 5965 6595 7108 939 -532 -2869 C ATOM 1318 NZ LYS A 181 40.520 90.197 29.626 1.00 54.32 N ANISOU 1318 NZ LYS A 181 6590 6173 7877 1131 -895 -2855 N ATOM 1319 N PRO A 182 40.488 83.032 26.583 1.00 33.58 N ANISOU 1319 N PRO A 182 4130 4626 4004 -70 43 -781 N ATOM 1320 CA PRO A 182 39.908 81.947 25.781 1.00 32.60 C ANISOU 1320 CA PRO A 182 3965 4609 3815 -141 64 -589 C ATOM 1321 C PRO A 182 38.537 82.244 25.164 1.00 34.39 C ANISOU 1321 C PRO A 182 4043 4895 4127 85 -38 -747 C ATOM 1322 O PRO A 182 38.307 81.863 24.019 1.00 33.06 O ANISOU 1322 O PRO A 182 3950 4616 3997 111 -109 -571 O ATOM 1323 CB PRO A 182 39.820 80.794 26.780 1.00 32.19 C ANISOU 1323 CB PRO A 182 3760 4930 3543 -396 209 -544 C ATOM 1324 CG PRO A 182 40.923 81.060 27.716 1.00 31.71 C ANISOU 1324 CG PRO A 182 3782 4846 3419 -498 255 -554 C ATOM 1325 CD PRO A 182 40.929 82.545 27.901 1.00 33.51 C ANISOU 1325 CD PRO A 182 4015 4920 3797 -266 189 -836 C ATOM 1326 N CYS A 183 37.656 82.909 25.905 1.00 37.55 N ANISOU 1326 N CYS A 183 4206 5507 4554 259 -58 -1122 N ATOM 1327 CA CYS A 183 36.319 83.228 25.400 1.00 40.28 C ANISOU 1327 CA CYS A 183 4355 5947 5001 519 -187 -1359 C ATOM 1328 C CYS A 183 36.311 84.357 24.354 1.00 41.26 C ANISOU 1328 C CYS A 183 4702 5572 5403 824 -490 -1338 C ATOM 1329 O CYS A 183 35.324 84.535 23.650 1.00 43.06 O ANISOU 1329 O CYS A 183 4837 5792 5731 1051 -660 -1443 O ATOM 1330 CB CYS A 183 35.372 83.562 26.558 1.00 43.69 C ANISOU 1330 CB CYS A 183 4388 6851 5360 618 -125 -1860 C ATOM 1331 SG CYS A 183 35.967 84.875 27.637 1.00 48.63 S ANISOU 1331 SG CYS A 183 5003 7370 6103 785 -194 -2230 S ATOM 1332 N ASP A 184 37.401 85.120 24.269 1.00 40.77 N ANISOU 1332 N ASP A 184 4935 5098 5457 803 -584 -1189 N ATOM 1333 CA ASP A 184 37.579 86.137 23.222 1.00 42.13 C ANISOU 1333 CA ASP A 184 5402 4748 5856 968 -898 -1028 C ATOM 1334 C ASP A 184 38.209 85.591 21.935 1.00 39.76 C ANISOU 1334 C ASP A 184 5361 4310 5434 752 -885 -547 C ATOM 1335 O ASP A 184 38.385 86.346 20.977 1.00 41.29 O ANISOU 1335 O ASP A 184 5818 4137 5733 797 -1139 -326 O ATOM 1336 CB ASP A 184 38.459 87.288 23.732 1.00 43.68 C ANISOU 1336 CB ASP A 184 5794 4564 6238 982 -1028 -1091 C ATOM 1337 CG ASP A 184 37.814 88.074 24.859 1.00 46.77 C ANISOU 1337 CG ASP A 184 5925 5040 6807 1269 -1130 -1653 C ATOM 1338 OD1 ASP A 184 36.569 88.118 24.934 1.00 48.97 O ANISOU 1338 OD1 ASP A 184 5918 5542 7147 1546 -1228 -2001 O ATOM 1339 OD2 ASP A 184 38.482 88.687 25.712 1.00 46.69 O ANISOU 1339 OD2 ASP A 184 5937 4923 6879 1245 -1126 -1834 O ATOM 1340 N LEU A 185 38.566 84.305 21.912 1.00 36.41 N ANISOU 1340 N LEU A 185 4862 4184 4789 505 -625 -394 N ATOM 1341 CA LEU A 185 39.164 83.694 20.718 1.00 34.71 C ANISOU 1341 CA LEU A 185 4810 3933 4446 320 -603 -50 C ATOM 1342 C LEU A 185 38.157 83.554 19.577 1.00 36.02 C ANISOU 1342 C LEU A 185 4943 4136 4608 473 -764 7 C ATOM 1343 O LEU A 185 36.962 83.355 19.803 1.00 36.67 O ANISOU 1343 O LEU A 185 4791 4404 4740 663 -796 -227 O ATOM 1344 CB LEU A 185 39.734 82.311 21.024 1.00 31.78 C ANISOU 1344 CB LEU A 185 4334 3832 3909 80 -358 12 C ATOM 1345 CG LEU A 185 40.886 82.202 22.029 1.00 29.97 C ANISOU 1345 CG LEU A 185 4144 3605 3640 -100 -213 3 C ATOM 1346 CD1 LEU A 185 41.058 80.748 22.431 1.00 27.33 C ANISOU 1346 CD1 LEU A 185 3676 3515 3192 -268 -71 31 C ATOM 1347 CD2 LEU A 185 42.174 82.767 21.459 1.00 30.05 C ANISOU 1347 CD2 LEU A 185 4384 3393 3639 -243 -243 184 C ATOM 1348 N HIS A 186 38.678 83.657 18.357 1.00 36.53 N ANISOU 1348 N HIS A 186 5217 4081 4579 361 -860 304 N ATOM 1349 CA HIS A 186 37.921 83.478 17.128 1.00 38.25 C ANISOU 1349 CA HIS A 186 5434 4370 4732 458 -1020 411 C ATOM 1350 C HIS A 186 38.233 82.086 16.602 1.00 35.71 C ANISOU 1350 C HIS A 186 4983 4370 4215 265 -818 464 C ATOM 1351 O HIS A 186 39.401 81.713 16.487 1.00 34.89 O ANISOU 1351 O HIS A 186 4951 4314 3994 25 -679 578 O ATOM 1352 CB HIS A 186 38.345 84.534 16.099 1.00 41.29 C ANISOU 1352 CB HIS A 186 6145 4461 5084 401 -1285 733 C ATOM 1353 CG HIS A 186 37.524 84.531 14.845 1.00 44.82 C ANISOU 1353 CG HIS A 186 6619 4970 5441 518 -1515 867 C ATOM 1354 ND1 HIS A 186 37.973 83.982 13.661 1.00 45.61 N ANISOU 1354 ND1 HIS A 186 6769 5309 5251 291 -1469 1106 N ATOM 1355 CD2 HIS A 186 36.287 85.018 14.588 1.00 49.13 C ANISOU 1355 CD2 HIS A 186 7123 5408 6136 850 -1813 760 C ATOM 1356 CE1 HIS A 186 37.045 84.126 12.732 1.00 48.89 C ANISOU 1356 CE1 HIS A 186 7195 5762 5620 460 -1722 1178 C ATOM 1357 NE2 HIS A 186 36.013 84.754 13.267 1.00 51.18 N ANISOU 1357 NE2 HIS A 186 7438 5821 6188 810 -1947 979 N ATOM 1358 N ALA A 187 37.195 81.311 16.316 1.00 35.42 N ANISOU 1358 N ALA A 187 4730 4557 4173 379 -822 330 N ATOM 1359 CA ALA A 187 37.348 79.958 15.801 1.00 33.49 C ANISOU 1359 CA ALA A 187 4343 4570 3810 232 -694 322 C ATOM 1360 C ALA A 187 36.623 79.851 14.470 1.00 35.11 C ANISOU 1360 C ALA A 187 4513 4907 3920 336 -858 366 C ATOM 1361 O ALA A 187 35.580 80.472 14.290 1.00 36.29 O ANISOU 1361 O ALA A 187 4637 5008 4144 568 -1044 310 O ATOM 1362 CB ALA A 187 36.786 78.966 16.784 1.00 32.35 C ANISOU 1362 CB ALA A 187 3957 4585 3750 201 -552 121 C ATOM 1363 N GLU A 188 37.182 79.064 13.548 1.00 34.61 N ANISOU 1363 N GLU A 188 4421 5037 3693 184 -811 418 N ATOM 1364 CA GLU A 188 36.610 78.884 12.210 1.00 36.72 C ANISOU 1364 CA GLU A 188 4636 5508 3810 249 -957 447 C ATOM 1365 C GLU A 188 36.242 77.438 11.848 1.00 35.50 C ANISOU 1365 C GLU A 188 4209 5619 3662 224 -889 222 C ATOM 1366 O GLU A 188 35.462 77.225 10.923 1.00 36.83 O ANISOU 1366 O GLU A 188 4270 5974 3751 326 -1015 167 O ATOM 1367 CB GLU A 188 37.572 79.435 11.143 1.00 38.58 C ANISOU 1367 CB GLU A 188 5071 5822 3767 68 -1016 700 C ATOM 1368 CG GLU A 188 38.154 80.801 11.477 1.00 41.11 C ANISOU 1368 CG GLU A 188 5694 5830 4095 -2 -1099 962 C ATOM 1369 CD GLU A 188 38.718 81.532 10.273 1.00 46.39 C ANISOU 1369 CD GLU A 188 6587 6588 4453 -215 -1244 1298 C ATOM 1370 OE1 GLU A 188 39.066 82.724 10.425 1.00 49.94 O ANISOU 1370 OE1 GLU A 188 7323 6725 4927 -297 -1389 1564 O ATOM 1371 OE2 GLU A 188 38.813 80.934 9.174 1.00 49.47 O ANISOU 1371 OE2 GLU A 188 6864 7372 4560 -328 -1231 1298 O ATOM 1372 N ILE A 189 36.779 76.459 12.575 1.00 29.87 N ANISOU 1372 N ILE A 189 4247 3690 3411 292 -457 -30 N ATOM 1373 CA ILE A 189 36.664 75.044 12.197 1.00 29.33 C ANISOU 1373 CA ILE A 189 4057 3723 3364 277 -430 -55 C ATOM 1374 C ILE A 189 35.993 74.191 13.281 1.00 28.38 C ANISOU 1374 C ILE A 189 3781 3690 3314 281 -433 -127 C ATOM 1375 O ILE A 189 34.947 73.581 13.053 1.00 28.32 O ANISOU 1375 O ILE A 189 3701 3753 3307 349 -471 -188 O ATOM 1376 CB ILE A 189 38.068 74.464 11.840 1.00 29.07 C ANISOU 1376 CB ILE A 189 4013 3689 3343 159 -341 10 C ATOM 1377 CG1 ILE A 189 38.659 75.198 10.623 1.00 31.16 C ANISOU 1377 CG1 ILE A 189 4431 3878 3531 152 -324 80 C ATOM 1378 CG2 ILE A 189 37.974 72.965 11.544 1.00 28.94 C ANISOU 1378 CG2 ILE A 189 3878 3768 3351 145 -310 -19 C ATOM 1379 CD1 ILE A 189 40.154 74.978 10.414 1.00 31.61 C ANISOU 1379 CD1 ILE A 189 4487 3918 3604 29 -228 150 C ATOM 1380 N LEU A 190 36.608 74.120 14.451 1.00 27.79 N ANISOU 1380 N LEU A 190 3655 3610 3293 202 -393 -119 N ATOM 1381 CA LEU A 190 36.096 73.264 15.517 1.00 27.24 C ANISOU 1381 CA LEU A 190 3452 3616 3283 192 -383 -177 C ATOM 1382 C LEU A 190 34.813 73.888 16.073 1.00 27.71 C ANISOU 1382 C LEU A 190 3506 3682 3339 293 -442 -244 C ATOM 1383 O LEU A 190 34.652 75.098 15.999 1.00 28.21 O ANISOU 1383 O LEU A 190 3677 3672 3368 348 -482 -235 O ATOM 1384 CB LEU A 190 37.153 73.082 16.612 1.00 26.44 C ANISOU 1384 CB LEU A 190 3314 3502 3230 86 -332 -146 C ATOM 1385 CG LEU A 190 38.404 72.299 16.207 1.00 26.06 C ANISOU 1385 CG LEU A 190 3236 3465 3200 -7 -270 -89 C ATOM 1386 CD1 LEU A 190 39.486 72.398 17.294 1.00 26.00 C ANISOU 1386 CD1 LEU A 190 3206 3436 3237 -103 -239 -55 C ATOM 1387 CD2 LEU A 190 38.065 70.837 15.934 1.00 25.39 C ANISOU 1387 CD2 LEU A 190 3045 3465 3135 -5 -245 -121 C ATOM 1388 N PRO A 191 33.889 73.092 16.609 1.00 27.74 N ANISOU 1388 N PRO A 191 3389 3771 3380 319 -444 -313 N ATOM 1389 CA PRO A 191 33.992 71.628 16.703 1.00 27.22 C ANISOU 1389 CA PRO A 191 3207 3784 3353 255 -398 -328 C ATOM 1390 C PRO A 191 33.836 70.868 15.378 1.00 27.66 C ANISOU 1390 C PRO A 191 3249 3877 3383 270 -407 -328 C ATOM 1391 O PRO A 191 34.362 69.772 15.274 1.00 27.08 O ANISOU 1391 O PRO A 191 3121 3837 3331 202 -358 -315 O ATOM 1392 CB PRO A 191 32.830 71.271 17.637 1.00 27.25 C ANISOU 1392 CB PRO A 191 3106 3855 3393 292 -404 -408 C ATOM 1393 CG PRO A 191 31.832 72.345 17.423 1.00 27.67 C ANISOU 1393 CG PRO A 191 3203 3893 3418 410 -470 -447 C ATOM 1394 CD PRO A 191 32.645 73.592 17.221 1.00 28.30 C ANISOU 1394 CD PRO A 191 3430 3864 3457 413 -487 -384 C ATOM 1395 N SER A 192 33.128 71.434 14.405 1.00 29.06 N ANISOU 1395 N SER A 192 3483 4047 3511 363 -471 -344 N ATOM 1396 CA SER A 192 32.879 70.770 13.125 1.00 29.85 C ANISOU 1396 CA SER A 192 3583 4183 3575 386 -492 -352 C ATOM 1397 C SER A 192 32.838 71.764 11.965 1.00 30.96 C ANISOU 1397 C SER A 192 3861 4264 3637 462 -548 -319 C ATOM 1398 O SER A 192 32.007 72.665 11.942 1.00 31.14 O ANISOU 1398 O SER A 192 3923 4271 3638 561 -618 -347 O ATOM 1399 CB SER A 192 31.568 69.989 13.185 1.00 30.33 C ANISOU 1399 CB SER A 192 3522 4339 3664 429 -529 -440 C ATOM 1400 OG SER A 192 31.256 69.426 11.924 1.00 32.05 O ANISOU 1400 OG SER A 192 3750 4589 3841 456 -565 -455 O ATOM 1401 N GLY A 193 33.749 71.585 11.008 1.00 31.68 N ANISOU 1401 N GLY A 193 4032 4322 3685 419 -514 -259 N ATOM 1402 CA GLY A 193 33.890 72.469 9.863 1.00 32.90 C ANISOU 1402 CA GLY A 193 4337 4410 3753 474 -551 -214 C ATOM 1403 C GLY A 193 32.619 72.668 9.056 1.00 34.25 C ANISOU 1403 C GLY A 193 4529 4612 3874 598 -653 -267 C ATOM 1404 O GLY A 193 32.403 73.752 8.520 1.00 36.07 O ANISOU 1404 O GLY A 193 4887 4778 4041 678 -710 -243 O ATOM 1405 N GLY A 194 31.783 71.633 8.976 1.00 34.12 N ANISOU 1405 N GLY A 194 4390 4690 3884 614 -681 -339 N ATOM 1406 CA GLY A 194 30.542 71.687 8.217 1.00 35.32 C ANISOU 1406 CA GLY A 194 4534 4888 3996 726 -787 -399 C ATOM 1407 C GLY A 194 29.299 72.132 8.985 1.00 35.52 C ANISOU 1407 C GLY A 194 4468 4959 4067 815 -856 -473 C ATOM 1408 O GLY A 194 28.204 72.118 8.420 1.00 36.98 O ANISOU 1408 O GLY A 194 4619 5199 4232 911 -950 -532 O ATOM 1409 N ASP A 195 29.457 72.517 10.253 1.00 34.43 N ANISOU 1409 N ASP A 195 4288 4803 3990 787 -810 -473 N ATOM 1410 CA ASP A 195 28.350 73.029 11.073 1.00 34.45 C ANISOU 1410 CA ASP A 195 4212 4843 4036 874 -858 -541 C ATOM 1411 C ASP A 195 28.407 74.562 11.124 1.00 34.75 C ANISOU 1411 C ASP A 195 4392 4781 4029 963 -899 -505 C ATOM 1412 O ASP A 195 29.401 75.165 10.717 1.00 34.64 O ANISOU 1412 O ASP A 195 4528 4668 3964 930 -874 -424 O ATOM 1413 CB ASP A 195 28.411 72.426 12.489 1.00 33.45 C ANISOU 1413 CB ASP A 195 3955 4760 3995 789 -778 -571 C ATOM 1414 CG ASP A 195 27.032 72.165 13.090 1.00 33.99 C ANISOU 1414 CG ASP A 195 3869 4927 4118 850 -812 -669 C ATOM 1415 OD1 ASP A 195 26.950 71.390 14.071 1.00 33.23 O ANISOU 1415 OD1 ASP A 195 3656 4884 4086 773 -745 -701 O ATOM 1416 OD2 ASP A 195 25.975 72.686 12.667 1.00 34.59 O ANISOU 1416 OD2 ASP A 195 3927 5035 4179 975 -901 -719 O ATOM 1417 N LYS A 196 27.349 75.180 11.642 1.00 35.14 N ANISOU 1417 N LYS A 196 4395 4855 4101 1074 -956 -566 N ATOM 1418 CA LYS A 196 27.132 76.625 11.518 1.00 35.91 C ANISOU 1418 CA LYS A 196 4632 4861 4150 1194 -1018 -547 C ATOM 1419 C LYS A 196 27.987 77.480 12.447 1.00 35.44 C ANISOU 1419 C LYS A 196 4671 4696 4098 1143 -957 -497 C ATOM 1420 O LYS A 196 28.467 78.541 12.054 1.00 36.25 O ANISOU 1420 O LYS A 196 4950 4683 4140 1176 -979 -438 O ATOM 1421 CB LYS A 196 25.663 76.951 11.792 1.00 37.06 C ANISOU 1421 CB LYS A 196 4680 5078 4325 1343 -1099 -639 C ATOM 1422 CG LYS A 196 24.693 76.332 10.802 1.00 37.71 C ANISOU 1422 CG LYS A 196 4674 5260 4394 1415 -1188 -695 C ATOM 1423 CD LYS A 196 23.270 76.404 11.322 1.00 39.26 C ANISOU 1423 CD LYS A 196 4711 5557 4649 1531 -1244 -798 C ATOM 1424 CE LYS A 196 22.259 75.972 10.269 1.00 40.72 C ANISOU 1424 CE LYS A 196 4818 5837 4817 1619 -1356 -856 C ATOM 1425 NZ LYS A 196 20.911 76.502 10.586 1.00 42.77 N ANISOU 1425 NZ LYS A 196 4968 6168 5116 1778 -1435 -943 N ATOM 1426 N LYS A 197 28.146 77.027 13.686 1.00 34.00 N ANISOU 1426 N LYS A 197 4383 4551 3986 1063 -884 -523 N ATOM 1427 CA LYS A 197 28.819 77.803 14.719 1.00 33.43 C ANISOU 1427 CA LYS A 197 4386 4391 3925 1018 -835 -493 C ATOM 1428 C LYS A 197 30.134 77.140 15.089 1.00 31.80 C ANISOU 1428 C LYS A 197 4172 4169 3742 848 -744 -435 C ATOM 1429 O LYS A 197 30.274 75.921 15.015 1.00 30.67 O ANISOU 1429 O LYS A 197 3915 4107 3631 772 -704 -444 O ATOM 1430 CB LYS A 197 27.924 77.953 15.952 1.00 33.57 C ANISOU 1430 CB LYS A 197 4303 4457 3995 1075 -828 -573 C ATOM 1431 CG LYS A 197 26.610 78.696 15.677 1.00 35.45 C ANISOU 1431 CG LYS A 197 4538 4713 4218 1259 -917 -637 C ATOM 1432 CD LYS A 197 25.575 78.451 16.777 1.00 36.32 C ANISOU 1432 CD LYS A 197 4490 4917 4393 1307 -896 -731 C ATOM 1433 CE LYS A 197 25.816 79.343 17.987 1.00 36.40 C ANISOU 1433 CE LYS A 197 4574 4848 4407 1314 -855 -734 C ATOM 1434 NZ LYS A 197 24.843 79.092 19.091 1.00 37.04 N ANISOU 1434 NZ LYS A 197 4507 5021 4544 1358 -819 -825 N ATOM 1435 N HIS A 198 31.099 77.967 15.472 1.00 31.27 N ANISOU 1435 N HIS A 198 4229 3994 3657 792 -716 -376 N ATOM 1436 CA HIS A 198 32.436 77.510 15.795 1.00 30.02 C ANISOU 1436 CA HIS A 198 4072 3813 3520 638 -640 -315 C ATOM 1437 C HIS A 198 32.870 78.108 17.132 1.00 29.62 C ANISOU 1437 C HIS A 198 4050 3708 3496 588 -611 -316 C ATOM 1438 O HIS A 198 32.537 79.255 17.458 1.00 30.38 O ANISOU 1438 O HIS A 198 4246 3728 3568 661 -648 -328 O ATOM 1439 CB HIS A 198 33.412 77.871 14.666 1.00 30.14 C ANISOU 1439 CB HIS A 198 4220 3751 3481 592 -633 -230 C ATOM 1440 CG HIS A 198 32.984 77.359 13.325 1.00 30.52 C ANISOU 1440 CG HIS A 198 4265 3844 3486 647 -666 -230 C ATOM 1441 ND1 HIS A 198 32.328 78.147 12.399 1.00 31.76 N ANISOU 1441 ND1 HIS A 198 4534 3958 3576 768 -743 -229 N ATOM 1442 CD2 HIS A 198 33.086 76.130 12.767 1.00 30.12 C ANISOU 1442 CD2 HIS A 198 4121 3876 3447 602 -638 -235 C ATOM 1443 CE1 HIS A 198 32.057 77.427 11.325 1.00 30.73 C ANISOU 1443 CE1 HIS A 198 4377 3885 3414 792 -764 -234 C ATOM 1444 NE2 HIS A 198 32.499 76.200 11.523 1.00 30.61 N ANISOU 1444 NE2 HIS A 198 4238 3945 3446 691 -700 -239 N ATOM 1445 N TYR A 199 33.594 77.298 17.895 1.00 27.99 N ANISOU 1445 N TYR A 199 3758 3540 3336 470 -548 -304 N ATOM 1446 CA TYR A 199 33.986 77.608 19.263 1.00 27.31 C ANISOU 1446 CA TYR A 199 3676 3424 3277 414 -522 -313 C ATOM 1447 C TYR A 199 35.474 77.339 19.469 1.00 26.44 C ANISOU 1447 C TYR A 199 3580 3283 3185 267 -473 -244 C ATOM 1448 O TYR A 199 36.045 76.459 18.817 1.00 25.43 O ANISOU 1448 O TYR A 199 3396 3197 3069 207 -441 -208 O ATOM 1449 CB TYR A 199 33.205 76.716 20.225 1.00 26.62 C ANISOU 1449 CB TYR A 199 3442 3437 3234 425 -497 -384 C ATOM 1450 CG TYR A 199 31.697 76.842 20.114 1.00 26.73 C ANISOU 1450 CG TYR A 199 3404 3506 3245 562 -536 -462 C ATOM 1451 CD1 TYR A 199 31.076 78.080 20.225 1.00 26.71 C ANISOU 1451 CD1 TYR A 199 3495 3441 3213 675 -584 -489 C ATOM 1452 CD2 TYR A 199 30.892 75.715 19.927 1.00 25.09 C ANISOU 1452 CD2 TYR A 199 3051 3414 3070 579 -525 -511 C ATOM 1453 CE1 TYR A 199 29.688 78.200 20.143 1.00 27.79 C ANISOU 1453 CE1 TYR A 199 3569 3637 3355 811 -621 -565 C ATOM 1454 CE2 TYR A 199 29.509 75.824 19.844 1.00 25.49 C ANISOU 1454 CE2 TYR A 199 3033 3525 3126 700 -562 -587 C ATOM 1455 CZ TYR A 199 28.911 77.071 19.952 1.00 26.95 C ANISOU 1455 CZ TYR A 199 3300 3655 3284 820 -610 -614 C ATOM 1456 OH TYR A 199 27.544 77.192 19.870 1.00 27.01 O ANISOU 1456 OH TYR A 199 3228 3731 3303 949 -649 -692 O ATOM 1457 N PRO A 200 36.102 78.078 20.379 1.00 26.62 N ANISOU 1457 N PRO A 200 3672 3234 3210 211 -470 -229 N ATOM 1458 CA PRO A 200 37.503 77.820 20.732 1.00 26.13 C ANISOU 1458 CA PRO A 200 3601 3153 3174 70 -432 -171 C ATOM 1459 C PRO A 200 37.679 76.446 21.367 1.00 25.27 C ANISOU 1459 C PRO A 200 3344 3143 3112 13 -391 -186 C ATOM 1460 O PRO A 200 36.814 76.018 22.131 1.00 25.28 O ANISOU 1460 O PRO A 200 3278 3200 3127 59 -390 -247 O ATOM 1461 CB PRO A 200 37.827 78.931 21.735 1.00 26.64 C ANISOU 1461 CB PRO A 200 3767 3126 3228 41 -454 -175 C ATOM 1462 CG PRO A 200 36.756 79.961 21.549 1.00 27.46 C ANISOU 1462 CG PRO A 200 3972 3173 3289 172 -501 -216 C ATOM 1463 CD PRO A 200 35.547 79.218 21.133 1.00 27.38 C ANISOU 1463 CD PRO A 200 3858 3260 3283 279 -506 -269 C ATOM 1464 N ILE A 201 38.767 75.760 21.022 1.00 24.73 N ANISOU 1464 N ILE A 201 3231 3096 3069 -81 -355 -131 N ATOM 1465 CA ILE A 201 39.160 74.509 21.684 1.00 23.76 C ANISOU 1465 CA ILE A 201 2988 3049 2991 -143 -318 -134 C ATOM 1466 C ILE A 201 40.222 74.740 22.775 1.00 23.68 C ANISOU 1466 C ILE A 201 2986 3007 3003 -241 -317 -108 C ATOM 1467 O ILE A 201 40.342 73.937 23.701 1.00 22.95 O ANISOU 1467 O ILE A 201 2820 2965 2937 -274 -304 -123 O ATOM 1468 CB ILE A 201 39.678 73.475 20.632 1.00 23.46 C ANISOU 1468 CB ILE A 201 2884 3061 2968 -173 -278 -96 C ATOM 1469 CG1 ILE A 201 39.917 72.086 21.255 1.00 22.25 C ANISOU 1469 CG1 ILE A 201 2612 2984 2858 -216 -243 -105 C ATOM 1470 CG2 ILE A 201 40.973 73.961 19.976 1.00 23.76 C ANISOU 1470 CG2 ILE A 201 2977 3046 3006 -249 -260 -23 C ATOM 1471 CD1 ILE A 201 38.744 71.529 22.068 1.00 23.54 C ANISOU 1471 CD1 ILE A 201 2718 3201 3026 -166 -246 -174 C ATOM 1472 N ALA A 202 40.985 75.829 22.670 1.00 24.37 N ANISOU 1472 N ALA A 202 3171 3011 3079 -291 -336 -69 N ATOM 1473 CA ALA A 202 42.069 76.103 23.614 1.00 24.47 C ANISOU 1473 CA ALA A 202 3192 2993 3114 -394 -346 -44 C ATOM 1474 C ALA A 202 41.532 76.245 25.030 1.00 24.77 C ANISOU 1474 C ALA A 202 3239 3029 3142 -374 -373 -99 C ATOM 1475 O ALA A 202 40.600 77.013 25.275 1.00 25.09 O ANISOU 1475 O ALA A 202 3356 3030 3147 -298 -396 -145 O ATOM 1476 CB ALA A 202 42.827 77.347 23.211 1.00 25.45 C ANISOU 1476 CB ALA A 202 3428 3018 3223 -452 -362 0 C ATOM 1477 N PHE A 203 42.128 75.495 25.957 1.00 24.63 N ANISOU 1477 N PHE A 203 3149 3056 3152 -437 -368 -95 N ATOM 1478 CA PHE A 203 41.680 75.445 27.354 1.00 24.66 C ANISOU 1478 CA PHE A 203 3161 3069 3140 -426 -385 -144 C ATOM 1479 C PHE A 203 40.180 75.159 27.502 1.00 24.42 C ANISOU 1479 C PHE A 203 3114 3079 3087 -318 -366 -209 C ATOM 1480 O PHE A 203 39.525 75.640 28.429 1.00 24.95 O ANISOU 1480 O PHE A 203 3230 3126 3123 -279 -378 -260 O ATOM 1481 CB PHE A 203 42.082 76.729 28.073 1.00 25.49 C ANISOU 1481 CB PHE A 203 3383 3082 3219 -467 -433 -150 C ATOM 1482 CG PHE A 203 43.555 76.966 28.070 1.00 26.46 C ANISOU 1482 CG PHE A 203 3507 3176 3372 -587 -454 -93 C ATOM 1483 CD1 PHE A 203 44.399 76.135 28.795 1.00 27.17 C ANISOU 1483 CD1 PHE A 203 3512 3319 3492 -658 -462 -73 C ATOM 1484 CD2 PHE A 203 44.109 77.976 27.308 1.00 28.09 C ANISOU 1484 CD2 PHE A 203 3790 3304 3576 -631 -466 -56 C ATOM 1485 CE1 PHE A 203 45.773 76.338 28.791 1.00 28.71 C ANISOU 1485 CE1 PHE A 203 3687 3498 3723 -768 -486 -24 C ATOM 1486 CE2 PHE A 203 45.489 78.183 27.299 1.00 30.04 C ANISOU 1486 CE2 PHE A 203 4021 3532 3859 -753 -480 -5 C ATOM 1487 CZ PHE A 203 46.319 77.363 28.044 1.00 28.82 C ANISOU 1487 CZ PHE A 203 3767 3441 3741 -820 -492 9 C ATOM 1488 N ASN A 204 39.663 74.321 26.607 1.00 23.71 N ANISOU 1488 N ASN A 204 2946 3050 3012 -273 -334 -210 N ATOM 1489 CA ASN A 204 38.245 73.988 26.554 1.00 23.23 C ANISOU 1489 CA ASN A 204 2846 3039 2940 -178 -316 -272 C ATOM 1490 C ASN A 204 38.031 72.494 26.346 1.00 22.50 C ANISOU 1490 C ASN A 204 2637 3035 2876 -187 -274 -274 C ATOM 1491 O ASN A 204 38.967 71.763 26.017 1.00 22.19 O ANISOU 1491 O ASN A 204 2553 3013 2863 -250 -259 -225 O ATOM 1492 CB ASN A 204 37.572 74.772 25.416 1.00 23.78 C ANISOU 1492 CB ASN A 204 2968 3078 2990 -94 -337 -282 C ATOM 1493 CG ASN A 204 36.085 74.998 25.649 1.00 24.08 C ANISOU 1493 CG ASN A 204 2996 3144 3011 17 -340 -358 C ATOM 1494 OD1 ASN A 204 35.588 74.839 26.764 1.00 25.53 O ANISOU 1494 OD1 ASN A 204 3158 3353 3190 27 -322 -404 O ATOM 1495 ND2 ASN A 204 35.375 75.398 24.601 1.00 24.71 N ANISOU 1495 ND2 ASN A 204 3092 3219 3077 104 -362 -371 N ATOM 1496 N ALA A 205 36.800 72.038 26.575 1.00 22.06 N ANISOU 1496 N ALA A 205 2529 3035 2817 -125 -251 -334 N ATOM 1497 CA ALA A 205 36.381 70.702 26.176 1.00 21.49 C ANISOU 1497 CA ALA A 205 2356 3040 2770 -127 -214 -345 C ATOM 1498 C ALA A 205 35.019 70.820 25.517 1.00 21.61 C ANISOU 1498 C ALA A 205 2338 3093 2780 -35 -217 -403 C ATOM 1499 O ALA A 205 34.070 71.317 26.124 1.00 22.26 O ANISOU 1499 O ALA A 205 2425 3185 2850 23 -218 -460 O ATOM 1500 CB ALA A 205 36.326 69.769 27.361 1.00 21.41 C ANISOU 1500 CB ALA A 205 2299 3069 2766 -171 -176 -361 C ATOM 1501 N LEU A 206 34.943 70.368 24.268 1.00 20.97 N ANISOU 1501 N LEU A 206 2222 3035 2708 -19 -222 -391 N ATOM 1502 CA LEU A 206 33.786 70.560 23.408 1.00 21.31 C ANISOU 1502 CA LEU A 206 2241 3112 2745 70 -245 -438 C ATOM 1503 C LEU A 206 33.069 69.231 23.188 1.00 21.36 C ANISOU 1503 C LEU A 206 2136 3203 2778 60 -214 -477 C ATOM 1504 O LEU A 206 33.592 68.362 22.500 1.00 20.27 O ANISOU 1504 O LEU A 206 1973 3079 2650 16 -199 -445 O ATOM 1505 CB LEU A 206 34.239 71.111 22.050 1.00 21.52 C ANISOU 1505 CB LEU A 206 2332 3095 2751 94 -283 -395 C ATOM 1506 CG LEU A 206 34.724 72.562 22.003 1.00 21.66 C ANISOU 1506 CG LEU A 206 2472 3020 2737 115 -320 -363 C ATOM 1507 CD1 LEU A 206 35.209 72.918 20.595 1.00 22.81 C ANISOU 1507 CD1 LEU A 206 2683 3126 2856 126 -343 -313 C ATOM 1508 CD2 LEU A 206 33.628 73.516 22.433 1.00 22.77 C ANISOU 1508 CD2 LEU A 206 2645 3149 2859 214 -352 -423 C ATOM 1509 N PRO A 207 31.886 69.053 23.774 1.00 22.03 N ANISOU 1509 N PRO A 207 2154 3343 2872 98 -198 -546 N ATOM 1510 CA PRO A 207 31.146 67.795 23.637 1.00 22.21 C ANISOU 1510 CA PRO A 207 2069 3445 2923 75 -164 -588 C ATOM 1511 C PRO A 207 30.372 67.719 22.319 1.00 22.87 C ANISOU 1511 C PRO A 207 2112 3569 3008 136 -208 -621 C ATOM 1512 O PRO A 207 29.174 67.442 22.322 1.00 23.42 O ANISOU 1512 O PRO A 207 2093 3708 3097 172 -208 -690 O ATOM 1513 CB PRO A 207 30.192 67.838 24.829 1.00 22.73 C ANISOU 1513 CB PRO A 207 2085 3552 2997 90 -126 -650 C ATOM 1514 CG PRO A 207 29.895 69.276 24.973 1.00 23.04 C ANISOU 1514 CG PRO A 207 2188 3554 3013 178 -167 -668 C ATOM 1515 CD PRO A 207 31.170 70.004 24.641 1.00 22.62 C ANISOU 1515 CD PRO A 207 2249 3410 2934 159 -203 -594 C ATOM 1516 N GLN A 208 31.061 67.980 21.211 1.00 22.99 N ANISOU 1516 N GLN A 208 2191 3543 3002 146 -245 -572 N ATOM 1517 CA GLN A 208 30.519 67.763 19.883 1.00 24.10 C ANISOU 1517 CA GLN A 208 2309 3715 3132 193 -289 -593 C ATOM 1518 C GLN A 208 31.637 67.372 18.914 1.00 24.17 C ANISOU 1518 C GLN A 208 2376 3685 3122 149 -286 -527 C ATOM 1519 O GLN A 208 32.610 68.106 18.735 1.00 24.49 O ANISOU 1519 O GLN A 208 2508 3657 3139 142 -291 -465 O ATOM 1520 CB GLN A 208 29.798 69.001 19.353 1.00 24.50 C ANISOU 1520 CB GLN A 208 2400 3754 3155 309 -360 -620 C ATOM 1521 CG GLN A 208 29.261 68.786 17.945 1.00 25.15 C ANISOU 1521 CG GLN A 208 2470 3869 3218 362 -418 -640 C ATOM 1522 CD GLN A 208 28.724 70.035 17.292 1.00 26.10 C ANISOU 1522 CD GLN A 208 2655 3962 3299 483 -497 -651 C ATOM 1523 OE1 GLN A 208 28.574 71.074 17.939 1.00 27.09 O ANISOU 1523 OE1 GLN A 208 2826 4049 3419 537 -508 -655 O ATOM 1524 NE2 GLN A 208 28.410 69.932 16.003 1.00 25.85 N ANISOU 1524 NE2 GLN A 208 2639 3946 3235 531 -557 -657 N ATOM 1525 N ILE A 209 31.484 66.199 18.316 1.00 24.71 N ANISOU 1525 N ILE A 209 2390 3798 3201 114 -271 -543 N ATOM 1526 CA ILE A 209 32.305 65.765 17.198 1.00 25.14 C ANISOU 1526 CA ILE A 209 2494 3828 3232 91 -269 -496 C ATOM 1527 C ILE A 209 31.331 65.363 16.089 1.00 26.27 C ANISOU 1527 C ILE A 209 2602 4020 3357 138 -317 -551 C ATOM 1528 O ILE A 209 30.353 64.642 16.329 1.00 26.11 O ANISOU 1528 O ILE A 209 2489 4066 3367 129 -318 -617 O ATOM 1529 CB ILE A 209 33.259 64.636 17.634 1.00 24.80 C ANISOU 1529 CB ILE A 209 2431 3776 3215 -1 -201 -459 C ATOM 1530 CG1 ILE A 209 34.267 65.211 18.639 1.00 24.99 C ANISOU 1530 CG1 ILE A 209 2496 3751 3250 -38 -174 -404 C ATOM 1531 CG2 ILE A 209 33.999 64.032 16.435 1.00 24.54 C ANISOU 1531 CG2 ILE A 209 2437 3728 3159 -18 -189 -424 C ATOM 1532 CD1 ILE A 209 35.268 64.234 19.179 1.00 25.29 C ANISOU 1532 CD1 ILE A 209 2517 3779 3315 -115 -118 -364 C ATOM 1533 N ASP A 210 31.571 65.896 14.891 1.00 27.27 N ANISOU 1533 N ASP A 210 2810 4117 3432 187 -361 -524 N ATOM 1534 CA ASP A 210 30.639 65.788 13.778 1.00 28.47 C ANISOU 1534 CA ASP A 210 2953 4312 3554 249 -429 -573 C ATOM 1535 C ASP A 210 29.366 66.576 14.143 1.00 29.33 C ANISOU 1535 C ASP A 210 3010 4460 3675 335 -491 -636 C ATOM 1536 O ASP A 210 29.374 67.349 15.104 1.00 29.72 O ANISOU 1536 O ASP A 210 3064 4487 3742 352 -478 -629 O ATOM 1537 CB ASP A 210 30.349 64.313 13.461 1.00 28.52 C ANISOU 1537 CB ASP A 210 2886 4370 3580 191 -408 -615 C ATOM 1538 CG ASP A 210 30.204 64.046 11.972 1.00 30.12 C ANISOU 1538 CG ASP A 210 3138 4579 3726 225 -458 -625 C ATOM 1539 OD1 ASP A 210 29.391 64.728 11.312 1.00 31.43 O ANISOU 1539 OD1 ASP A 210 3319 4765 3857 311 -543 -658 O ATOM 1540 OD2 ASP A 210 30.847 63.157 11.382 1.00 31.27 O ANISOU 1540 OD2 ASP A 210 3315 4712 3855 175 -421 -605 O ATOM 1541 N VAL A 211 28.285 66.381 13.389 1.00 29.90 N ANISOU 1541 N VAL A 211 3032 4592 3736 393 -561 -700 N ATOM 1542 CA VAL A 211 27.051 67.145 13.564 1.00 30.78 C ANISOU 1542 CA VAL A 211 3087 4749 3858 492 -630 -763 C ATOM 1543 C VAL A 211 26.008 66.316 14.311 1.00 30.73 C ANISOU 1543 C VAL A 211 2919 4837 3920 457 -609 -847 C ATOM 1544 O VAL A 211 26.165 65.112 14.476 1.00 30.23 O ANISOU 1544 O VAL A 211 2801 4799 3884 359 -555 -858 O ATOM 1545 CB VAL A 211 26.481 67.639 12.206 1.00 31.95 C ANISOU 1545 CB VAL A 211 3287 4907 3947 596 -738 -781 C ATOM 1546 CG1 VAL A 211 27.530 68.457 11.447 1.00 32.08 C ANISOU 1546 CG1 VAL A 211 3477 4824 3889 622 -747 -693 C ATOM 1547 CG2 VAL A 211 25.983 66.473 11.344 1.00 32.87 C ANISOU 1547 CG2 VAL A 211 3340 5090 4061 563 -770 -832 C ATOM 1548 N PHE A 212 24.953 66.968 14.776 1.00 31.23 N ANISOU 1548 N PHE A 212 2908 4949 4009 538 -646 -906 N ATOM 1549 CA PHE A 212 23.927 66.287 15.559 1.00 31.77 C ANISOU 1549 CA PHE A 212 2816 5112 4145 503 -614 -987 C ATOM 1550 C PHE A 212 22.956 65.496 14.677 1.00 33.09 C ANISOU 1550 C PHE A 212 2881 5367 4326 503 -677 -1060 C ATOM 1551 O PHE A 212 22.598 65.942 13.586 1.00 33.59 O ANISOU 1551 O PHE A 212 2975 5439 4348 592 -778 -1074 O ATOM 1552 CB PHE A 212 23.190 67.292 16.450 1.00 32.05 C ANISOU 1552 CB PHE A 212 2803 5169 4204 591 -618 -1026 C ATOM 1553 CG PHE A 212 24.005 67.733 17.623 1.00 30.41 C ANISOU 1553 CG PHE A 212 2664 4892 3998 554 -537 -974 C ATOM 1554 CD1 PHE A 212 24.738 68.911 17.578 1.00 29.91 C ANISOU 1554 CD1 PHE A 212 2742 4735 3889 614 -560 -913 C ATOM 1555 CD2 PHE A 212 24.088 66.941 18.754 1.00 28.73 C ANISOU 1555 CD2 PHE A 212 2387 4702 3827 452 -440 -983 C ATOM 1556 CE1 PHE A 212 25.514 69.307 18.660 1.00 28.69 C ANISOU 1556 CE1 PHE A 212 2651 4515 3733 572 -494 -869 C ATOM 1557 CE2 PHE A 212 24.870 67.326 19.831 1.00 28.11 C ANISOU 1557 CE2 PHE A 212 2380 4560 3741 417 -375 -936 C ATOM 1558 CZ PHE A 212 25.584 68.512 19.781 1.00 27.64 C ANISOU 1558 CZ PHE A 212 2450 4411 3639 476 -406 -881 C ATOM 1559 N THR A 213 22.577 64.305 15.146 1.00 33.58 N ANISOU 1559 N THR A 213 2831 5487 4440 398 -619 -1105 N ATOM 1560 CA THR A 213 21.537 63.501 14.505 1.00 35.00 C ANISOU 1560 CA THR A 213 2891 5761 4648 378 -672 -1189 C ATOM 1561 C THR A 213 20.237 63.730 15.243 1.00 36.15 C ANISOU 1561 C THR A 213 2872 6006 4858 414 -672 -1275 C ATOM 1562 O THR A 213 20.234 64.285 16.342 1.00 36.67 O ANISOU 1562 O THR A 213 2924 6063 4947 432 -608 -1267 O ATOM 1563 CB THR A 213 21.858 61.983 14.528 1.00 34.81 C ANISOU 1563 CB THR A 213 2846 5736 4644 229 -605 -1192 C ATOM 1564 OG1 THR A 213 21.583 61.437 15.827 1.00 35.41 O ANISOU 1564 OG1 THR A 213 2832 5842 4781 142 -503 -1214 O ATOM 1565 CG2 THR A 213 23.330 61.703 14.312 1.00 33.65 C ANISOU 1565 CG2 THR A 213 2851 5485 4449 179 -556 -1098 C ATOM 1566 N ASP A 214 19.141 63.262 14.653 1.00 37.13 N ANISOU 1566 N ASP A 214 2867 6227 5012 419 -739 -1361 N ATOM 1567 CA ASP A 214 17.808 63.446 15.199 1.00 38.18 C ANISOU 1567 CA ASP A 214 2819 6474 5214 457 -747 -1454 C ATOM 1568 C ASP A 214 17.545 62.950 16.612 1.00 37.75 C ANISOU 1568 C ASP A 214 2666 6454 5224 360 -614 -1477 C ATOM 1569 O ASP A 214 16.584 63.403 17.242 1.00 38.87 O ANISOU 1569 O ASP A 214 2678 6677 5416 415 -601 -1541 O ATOM 1570 N ASN A 215 18.376 62.030 17.113 1.00 36.31 N ANISOU 1570 N ASN A 215 2547 6210 5038 223 -514 -1427 N ATOM 1571 CA ASN A 215 18.220 61.491 18.477 1.00 35.59 C ANISOU 1571 CA ASN A 215 2390 6138 4994 122 -381 -1439 C ATOM 1572 C ASN A 215 19.074 62.192 19.540 1.00 34.19 C ANISOU 1572 C ASN A 215 2322 5879 4788 144 -304 -1367 C ATOM 1573 O ASN A 215 19.186 61.722 20.678 1.00 33.81 O ANISOU 1573 O ASN A 215 2261 5825 4759 57 -193 -1358 O ATOM 1574 CB ASN A 215 18.455 59.973 18.490 1.00 35.16 C ANISOU 1574 CB ASN A 215 2330 6073 4956 -45 -317 -1437 C ATOM 1575 CG ASN A 215 19.916 59.580 18.306 1.00 33.88 C ANISOU 1575 CG ASN A 215 2344 5789 4739 -94 -290 -1339 C ATOM 1576 OD1 ASN A 215 20.803 60.424 18.212 1.00 31.27 O ANISOU 1576 OD1 ASN A 215 2136 5385 4360 -19 -312 -1269 O ATOM 1577 ND2 ASN A 215 20.164 58.270 18.255 1.00 33.89 N ANISOU 1577 ND2 ASN A 215 2357 5769 4749 -225 -241 -1336 N ATOM 1578 N ASP A 216 19.668 63.315 19.146 1.00 33.23 N ANISOU 1578 N ASP A 216 2316 5694 4616 259 -369 -1316 N ATOM 1579 CA ASP A 216 20.480 64.173 20.011 1.00 31.94 C ANISOU 1579 CA ASP A 216 2266 5448 4421 294 -321 -1252 C ATOM 1580 C ASP A 216 21.866 63.636 20.377 1.00 30.19 C ANISOU 1580 C ASP A 216 2174 5128 4168 193 -256 -1162 C ATOM 1581 O ASP A 216 22.592 64.293 21.109 1.00 29.73 O ANISOU 1581 O ASP A 216 2208 5004 4085 210 -221 -1109 O ATOM 1582 CB ASP A 216 19.687 64.617 21.257 1.00 32.60 C ANISOU 1582 CB ASP A 216 2259 5586 4540 322 -252 -1304 C ATOM 1583 CG ASP A 216 18.409 65.351 20.888 1.00 34.10 C ANISOU 1583 CG ASP A 216 2327 5869 4761 452 -323 -1389 C ATOM 1584 OD1 ASP A 216 18.285 65.726 19.700 1.00 34.60 O ANISOU 1584 OD1 ASP A 216 2409 5935 4805 535 -439 -1393 O ATOM 1585 OD2 ASP A 216 17.482 65.599 21.701 1.00 34.35 O ANISOU 1585 OD2 ASP A 216 2241 5975 4834 484 -273 -1455 O ATOM 1586 N TYR A 217 22.217 62.452 19.871 1.00 29.36 N ANISOU 1586 N TYR A 217 2074 5015 4066 93 -243 -1148 N ATOM 1587 CA TYR A 217 23.605 62.009 19.778 1.00 27.64 C ANISOU 1587 CA TYR A 217 1985 4703 3812 29 -213 -1060 C ATOM 1588 C TYR A 217 24.169 62.574 18.478 1.00 27.79 C ANISOU 1588 C TYR A 217 2098 4678 3785 103 -304 -1021 C ATOM 1589 O TYR A 217 23.413 62.822 17.542 1.00 28.10 O ANISOU 1589 O TYR A 217 2092 4765 3819 170 -387 -1069 O ATOM 1590 CB TYR A 217 23.699 60.482 19.713 1.00 27.30 C ANISOU 1590 CB TYR A 217 1916 4667 3791 -98 -162 -1066 C ATOM 1591 CG TYR A 217 23.349 59.750 20.988 1.00 26.86 C ANISOU 1591 CG TYR A 217 1801 4635 3771 -193 -59 -1087 C ATOM 1592 CD1 TYR A 217 24.341 59.180 21.777 1.00 24.62 C ANISOU 1592 CD1 TYR A 217 1600 4280 3473 -270 17 -1021 C ATOM 1593 CD2 TYR A 217 22.025 59.622 21.400 1.00 26.98 C ANISOU 1593 CD2 TYR A 217 1675 4744 3833 -206 -36 -1173 C ATOM 1594 CE1 TYR A 217 24.025 58.502 22.952 1.00 26.06 C ANISOU 1594 CE1 TYR A 217 1747 4477 3677 -357 112 -1036 C ATOM 1595 CE2 TYR A 217 21.698 58.944 22.570 1.00 27.77 C ANISOU 1595 CE2 TYR A 217 1729 4864 3960 -301 70 -1190 C ATOM 1596 CZ TYR A 217 22.702 58.384 23.341 1.00 26.56 C ANISOU 1596 CZ TYR A 217 1680 4631 3781 -376 144 -1119 C ATOM 1597 OH TYR A 217 22.376 57.708 24.497 1.00 26.68 O ANISOU 1597 OH TYR A 217 1667 4659 3813 -469 249 -1131 O ATOM 1598 N THR A 218 25.486 62.769 18.415 1.00 27.17 N ANISOU 1598 N THR A 218 2145 4509 3668 89 -287 -935 N ATOM 1599 CA THR A 218 26.140 63.190 17.171 1.00 27.47 C ANISOU 1599 CA THR A 218 2281 4499 3656 140 -353 -890 C ATOM 1600 C THR A 218 26.433 61.985 16.306 1.00 27.47 C ANISOU 1600 C THR A 218 2291 4500 3648 73 -350 -888 C ATOM 1601 O THR A 218 26.302 60.850 16.752 1.00 27.48 O ANISOU 1601 O THR A 218 2238 4520 3682 -19 -293 -910 O ATOM 1602 CB THR A 218 27.467 63.932 17.432 1.00 26.30 C ANISOU 1602 CB THR A 218 2259 4258 3474 147 -331 -799 C ATOM 1603 OG1 THR A 218 28.411 63.050 18.059 1.00 25.93 O ANISOU 1603 OG1 THR A 218 2234 4177 3442 47 -252 -753 O ATOM 1604 CG2 THR A 218 27.280 65.089 18.413 1.00 26.40 C ANISOU 1604 CG2 THR A 218 2282 4257 3492 202 -327 -800 C ATOM 1605 N TYR A 219 26.864 62.247 15.078 1.00 27.91 N ANISOU 1605 N TYR A 219 2429 4524 3653 118 -407 -860 N ATOM 1606 CA TYR A 219 27.221 61.195 14.141 1.00 28.13 C ANISOU 1606 CA TYR A 219 2487 4542 3660 66 -406 -857 C ATOM 1607 C TYR A 219 28.416 60.409 14.617 1.00 26.82 C ANISOU 1607 C TYR A 219 2371 4318 3502 -19 -317 -795 C ATOM 1608 O TYR A 219 28.475 59.207 14.411 1.00 26.28 O ANISOU 1608 O TYR A 219 2290 4252 3444 -88 -286 -812 O ATOM 1609 CB TYR A 219 27.514 61.767 12.755 1.00 28.81 C ANISOU 1609 CB TYR A 219 2670 4601 3677 140 -478 -832 C ATOM 1610 CG TYR A 219 26.292 61.815 11.906 1.00 32.01 C ANISOU 1610 CG TYR A 219 3019 5074 4069 198 -576 -909 C ATOM 1611 CD1 TYR A 219 25.818 60.668 11.271 1.00 34.24 C ANISOU 1611 CD1 TYR A 219 3259 5397 4355 145 -596 -966 C ATOM 1612 CD2 TYR A 219 25.586 63.002 11.748 1.00 34.48 C ANISOU 1612 CD2 TYR A 219 3322 5410 4367 308 -656 -931 C ATOM 1613 CE1 TYR A 219 24.681 60.715 10.492 1.00 36.18 C ANISOU 1613 CE1 TYR A 219 3446 5712 4590 195 -698 -1042 C ATOM 1614 CE2 TYR A 219 24.453 63.057 10.977 1.00 36.19 C ANISOU 1614 CE2 TYR A 219 3480 5697 4574 371 -758 -1004 C ATOM 1615 CZ TYR A 219 24.005 61.916 10.352 1.00 36.81 C ANISOU 1615 CZ TYR A 219 3507 5821 4656 311 -781 -1060 C ATOM 1616 OH TYR A 219 22.879 61.987 9.594 1.00 39.09 O ANISOU 1616 OH TYR A 219 3732 6185 4937 372 -893 -1136 O ATOM 1617 N GLU A 220 29.372 61.089 15.243 1.00 25.94 N ANISOU 1617 N GLU A 220 2319 4151 3385 -13 -280 -725 N ATOM 1618 CA GLU A 220 30.539 60.415 15.785 1.00 24.92 C ANISOU 1618 CA GLU A 220 2229 3972 3269 -84 -203 -665 C ATOM 1619 C GLU A 220 30.117 59.364 16.803 1.00 24.70 C ANISOU 1619 C GLU A 220 2128 3970 3288 -162 -146 -699 C ATOM 1620 O GLU A 220 30.594 58.233 16.775 1.00 24.70 O ANISOU 1620 O GLU A 220 2141 3948 3296 -225 -101 -686 O ATOM 1621 CB GLU A 220 31.487 61.424 16.448 1.00 24.57 C ANISOU 1621 CB GLU A 220 2241 3875 3218 -67 -185 -595 C ATOM 1622 CG GLU A 220 32.780 60.808 16.941 1.00 24.12 C ANISOU 1622 CG GLU A 220 2219 3771 3173 -130 -118 -530 C ATOM 1623 CD GLU A 220 33.820 60.621 15.851 1.00 25.47 C ANISOU 1623 CD GLU A 220 2460 3904 3313 -126 -110 -480 C ATOM 1624 OE1 GLU A 220 33.507 60.759 14.639 1.00 26.50 O ANISOU 1624 OE1 GLU A 220 2621 4043 3405 -85 -150 -497 O ATOM 1625 OE2 GLU A 220 34.978 60.335 16.217 1.00 27.96 O ANISOU 1625 OE2 GLU A 220 2801 4183 3641 -163 -62 -421 O ATOM 1626 N GLU A 221 29.234 59.756 17.710 1.00 24.58 N ANISOU 1626 N GLU A 221 2043 3997 3301 -156 -144 -741 N ATOM 1627 CA GLU A 221 28.719 58.858 18.741 1.00 24.27 C ANISOU 1627 CA GLU A 221 1935 3983 3301 -233 -83 -775 C ATOM 1628 C GLU A 221 27.953 57.673 18.130 1.00 24.80 C ANISOU 1628 C GLU A 221 1947 4090 3385 -288 -85 -837 C ATOM 1629 O GLU A 221 28.171 56.518 18.507 1.00 24.19 O ANISOU 1629 O GLU A 221 1875 3991 3324 -371 -26 -832 O ATOM 1630 CB GLU A 221 27.842 59.645 19.723 1.00 24.43 C ANISOU 1630 CB GLU A 221 1891 4049 3343 -204 -78 -814 C ATOM 1631 CG GLU A 221 28.655 60.601 20.579 1.00 23.39 C ANISOU 1631 CG GLU A 221 1825 3867 3195 -176 -62 -755 C ATOM 1632 CD GLU A 221 27.876 61.778 21.127 1.00 24.55 C ANISOU 1632 CD GLU A 221 1938 4045 3344 -105 -83 -792 C ATOM 1633 OE1 GLU A 221 26.635 61.844 20.976 1.00 23.25 O ANISOU 1633 OE1 GLU A 221 1682 3952 3202 -75 -104 -867 O ATOM 1634 OE2 GLU A 221 28.532 62.653 21.722 1.00 25.77 O ANISOU 1634 OE2 GLU A 221 2159 4152 3480 -79 -81 -747 O ATOM 1635 N MET A 222 27.090 57.959 17.162 1.00 25.41 N ANISOU 1635 N MET A 222 1980 4218 3455 -240 -158 -894 N ATOM 1636 CA MET A 222 26.301 56.919 16.504 1.00 26.31 C ANISOU 1636 CA MET A 222 2039 4374 3584 -292 -176 -963 C ATOM 1637 C MET A 222 27.172 55.986 15.667 1.00 26.55 C ANISOU 1637 C MET A 222 2159 4345 3584 -330 -166 -930 C ATOM 1638 O MET A 222 26.851 54.816 15.519 1.00 27.03 O ANISOU 1638 O MET A 222 2200 4409 3660 -408 -144 -969 O ATOM 1639 CB MET A 222 25.205 57.541 15.637 1.00 26.99 C ANISOU 1639 CB MET A 222 2058 4532 3665 -220 -274 -1032 C ATOM 1640 CG MET A 222 24.106 58.244 16.434 1.00 28.05 C ANISOU 1640 CG MET A 222 2076 4740 3840 -186 -280 -1086 C ATOM 1641 SD MET A 222 23.488 57.276 17.843 1.00 28.96 S ANISOU 1641 SD MET A 222 2092 4892 4019 -308 -172 -1125 S ATOM 1642 CE MET A 222 22.830 55.809 16.989 1.00 30.18 C ANISOU 1642 CE MET A 222 2194 5080 4194 -409 -190 -1196 C ATOM 1643 N LYS A 223 28.275 56.500 15.127 1.00 26.56 N ANISOU 1643 N LYS A 223 2259 4291 3543 -277 -176 -861 N ATOM 1644 CA LYS A 223 29.217 55.669 14.386 1.00 26.66 C ANISOU 1644 CA LYS A 223 2358 4247 3525 -302 -152 -826 C ATOM 1645 C LYS A 223 29.841 54.632 15.323 1.00 26.00 C ANISOU 1645 C LYS A 223 2289 4117 3471 -382 -64 -794 C ATOM 1646 O LYS A 223 29.931 53.466 14.984 1.00 26.73 O ANISOU 1646 O LYS A 223 2407 4184 3563 -436 -38 -811 O ATOM 1647 CB LYS A 223 30.306 56.519 13.733 1.00 26.67 C ANISOU 1647 CB LYS A 223 2452 4203 3478 -232 -166 -754 C ATOM 1648 CG LYS A 223 29.911 57.127 12.398 1.00 28.01 C ANISOU 1648 CG LYS A 223 2655 4394 3595 -160 -249 -778 C ATOM 1649 CD LYS A 223 31.052 57.968 11.850 1.00 29.07 C ANISOU 1649 CD LYS A 223 2888 4475 3680 -105 -245 -699 C ATOM 1650 CE LYS A 223 30.588 58.941 10.791 1.00 31.45 C ANISOU 1650 CE LYS A 223 3231 4794 3926 -20 -331 -713 C ATOM 1651 NZ LYS A 223 31.609 59.995 10.550 1.00 33.14 N ANISOU 1651 NZ LYS A 223 3536 4955 4100 25 -318 -631 N ATOM 1652 N MET A 224 30.249 55.048 16.512 1.00 25.32 N ANISOU 1652 N MET A 224 2197 4016 3407 -388 -21 -749 N ATOM 1653 CA MET A 224 30.771 54.106 17.502 1.00 24.86 C ANISOU 1653 CA MET A 224 2158 3917 3373 -457 55 -718 C ATOM 1654 C MET A 224 29.760 52.979 17.790 1.00 25.34 C ANISOU 1654 C MET A 224 2167 3999 3462 -543 82 -785 C ATOM 1655 O MET A 224 30.142 51.806 17.908 1.00 25.52 O ANISOU 1655 O MET A 224 2234 3973 3488 -602 130 -774 O ATOM 1656 CB MET A 224 31.162 54.839 18.784 1.00 24.46 C ANISOU 1656 CB MET A 224 2102 3856 3334 -448 83 -672 C ATOM 1657 CG MET A 224 32.268 55.884 18.563 1.00 24.67 C ANISOU 1657 CG MET A 224 2183 3852 3337 -383 60 -603 C ATOM 1658 SD MET A 224 33.095 56.440 20.058 1.00 25.17 S ANISOU 1658 SD MET A 224 2267 3884 3411 -390 94 -538 S ATOM 1659 CE MET A 224 34.064 54.972 20.467 1.00 25.25 C ANISOU 1659 CE MET A 224 2323 3839 3432 -447 155 -493 C ATOM 1660 N THR A 225 28.476 53.334 17.862 1.00 25.10 N ANISOU 1660 N THR A 225 2044 4041 3452 -548 52 -856 N ATOM 1661 CA THR A 225 27.413 52.372 18.146 1.00 25.50 C ANISOU 1661 CA THR A 225 2027 4124 3535 -640 80 -926 C ATOM 1662 C THR A 225 27.235 51.370 17.008 1.00 25.98 C ANISOU 1662 C THR A 225 2113 4172 3586 -679 53 -968 C ATOM 1663 O THR A 225 27.289 50.163 17.217 1.00 26.27 O ANISOU 1663 O THR A 225 2183 4166 3634 -764 105 -976 O ATOM 1664 CB THR A 225 26.076 53.119 18.407 1.00 26.04 C ANISOU 1664 CB THR A 225 1971 4288 3633 -624 49 -996 C ATOM 1665 OG1 THR A 225 26.162 53.849 19.640 1.00 24.26 O ANISOU 1665 OG1 THR A 225 1731 4069 3418 -605 92 -965 O ATOM 1666 CG2 THR A 225 24.904 52.136 18.605 1.00 26.93 C ANISOU 1666 CG2 THR A 225 1996 4447 3787 -729 78 -1077 C ATOM 1667 N LYS A 226 27.040 51.896 15.806 1.00 25.90 N ANISOU 1667 N LYS A 226 2101 4192 3549 -613 -29 -995 N ATOM 1668 CA LYS A 226 26.693 51.099 14.642 1.00 26.44 C ANISOU 1668 CA LYS A 226 2188 4260 3598 -643 -72 -1050 C ATOM 1669 C LYS A 226 27.879 50.327 14.114 1.00 25.46 C ANISOU 1669 C LYS A 226 2190 4046 3437 -645 -39 -1000 C ATOM 1670 O LYS A 226 27.728 49.212 13.640 1.00 25.19 O ANISOU 1670 O LYS A 226 2191 3982 3398 -708 -31 -1038 O ATOM 1671 CB LYS A 226 26.136 52.001 13.540 1.00 27.15 C ANISOU 1671 CB LYS A 226 2248 4411 3659 -559 -178 -1090 C ATOM 1672 CG LYS A 226 24.748 52.558 13.855 1.00 29.61 C ANISOU 1672 CG LYS A 226 2417 4822 4012 -555 -225 -1164 C ATOM 1673 CD LYS A 226 24.184 53.304 12.653 1.00 32.52 C ANISOU 1673 CD LYS A 226 2766 5246 4346 -467 -343 -1207 C ATOM 1674 CE LYS A 226 24.849 54.669 12.483 1.00 33.76 C ANISOU 1674 CE LYS A 226 2983 5383 4461 -345 -374 -1140 C ATOM 1675 NZ LYS A 226 23.954 55.679 11.824 1.00 36.10 N ANISOU 1675 NZ LYS A 226 3223 5752 4743 -248 -485 -1187 N ATOM 1676 N GLU A 227 29.063 50.924 14.184 1.00 24.15 N ANISOU 1676 N GLU A 227 2092 3837 3246 -577 -18 -917 N ATOM 1677 CA GLU A 227 30.251 50.265 13.660 1.00 23.76 C ANISOU 1677 CA GLU A 227 2152 3711 3166 -566 18 -868 C ATOM 1678 C GLU A 227 30.665 49.124 14.584 1.00 23.17 C ANISOU 1678 C GLU A 227 2109 3575 3120 -638 100 -844 C ATOM 1679 O GLU A 227 31.095 48.066 14.119 1.00 22.85 O ANISOU 1679 O GLU A 227 2143 3474 3064 -663 127 -847 O ATOM 1680 CB GLU A 227 31.379 51.269 13.420 1.00 23.24 C ANISOU 1680 CB GLU A 227 2134 3625 3069 -477 17 -789 C ATOM 1681 CG GLU A 227 31.041 52.266 12.311 1.00 24.39 C ANISOU 1681 CG GLU A 227 2283 3813 3171 -404 -62 -809 C ATOM 1682 CD GLU A 227 32.183 53.199 11.968 1.00 25.23 C ANISOU 1682 CD GLU A 227 2451 3891 3243 -330 -55 -730 C ATOM 1683 OE1 GLU A 227 33.342 52.819 12.210 1.00 27.14 O ANISOU 1683 OE1 GLU A 227 2742 4081 3489 -334 9 -670 O ATOM 1684 OE2 GLU A 227 31.926 54.316 11.467 1.00 25.15 O ANISOU 1684 OE2 GLU A 227 2441 3911 3204 -268 -113 -729 O ATOM 1685 N THR A 228 30.498 49.320 15.888 1.00 22.60 N ANISOU 1685 N THR A 228 1990 3513 3084 -670 138 -823 N ATOM 1686 CA THR A 228 30.787 48.261 16.852 1.00 22.36 C ANISOU 1686 CA THR A 228 1997 3423 3075 -739 211 -800 C ATOM 1687 C THR A 228 29.919 47.039 16.573 1.00 23.47 C ANISOU 1687 C THR A 228 2140 3550 3226 -834 223 -872 C ATOM 1688 O THR A 228 30.436 45.926 16.478 1.00 23.52 O ANISOU 1688 O THR A 228 2234 3479 3225 -867 263 -859 O ATOM 1689 CB THR A 228 30.570 48.744 18.287 1.00 22.02 C ANISOU 1689 CB THR A 228 1904 3402 3059 -761 246 -775 C ATOM 1690 OG1 THR A 228 31.632 49.623 18.666 1.00 20.43 O ANISOU 1690 OG1 THR A 228 1728 3187 2847 -687 244 -698 O ATOM 1691 CG2 THR A 228 30.663 47.589 19.289 1.00 21.98 C ANISOU 1691 CG2 THR A 228 1945 3337 3068 -843 320 -758 C ATOM 1692 N LYS A 229 28.613 47.263 16.438 1.00 23.68 N ANISOU 1692 N LYS A 229 2072 3652 3274 -877 186 -950 N ATOM 1693 CA LYS A 229 27.665 46.198 16.107 1.00 24.99 C ANISOU 1693 CA LYS A 229 2222 3818 3455 -980 186 -1030 C ATOM 1694 C LYS A 229 28.050 45.406 14.837 1.00 25.21 C ANISOU 1694 C LYS A 229 2343 3791 3445 -975 158 -1052 C ATOM 1695 O LYS A 229 27.952 44.188 14.822 1.00 25.71 O ANISOU 1695 O LYS A 229 2465 3791 3511 -1057 194 -1078 O ATOM 1696 CB LYS A 229 26.261 46.779 15.942 1.00 25.68 C ANISOU 1696 CB LYS A 229 2173 4015 3571 -1002 130 -1113 C ATOM 1697 CG LYS A 229 25.626 47.244 17.244 1.00 26.84 C ANISOU 1697 CG LYS A 229 2223 4214 3760 -1036 176 -1114 C ATOM 1698 CD LYS A 229 24.263 47.862 16.991 1.00 28.64 C ANISOU 1698 CD LYS A 229 2304 4558 4020 -1041 117 -1200 C ATOM 1699 CE LYS A 229 23.739 48.585 18.213 1.00 28.71 C ANISOU 1699 CE LYS A 229 2218 4626 4063 -1040 162 -1197 C ATOM 1700 NZ LYS A 229 23.209 47.629 19.218 1.00 31.00 N ANISOU 1700 NZ LYS A 229 2486 4904 4387 -1173 257 -1217 N ATOM 1701 N LYS A 230 28.491 46.101 13.788 1.00 24.65 N ANISOU 1701 N LYS A 230 2297 3737 3333 -878 98 -1042 N ATOM 1702 CA LYS A 230 28.875 45.456 12.520 1.00 24.96 C ANISOU 1702 CA LYS A 230 2432 3728 3324 -861 73 -1065 C ATOM 1703 C LYS A 230 30.199 44.677 12.620 1.00 24.51 C ANISOU 1703 C LYS A 230 2499 3566 3248 -839 146 -998 C ATOM 1704 O LYS A 230 30.308 43.558 12.125 1.00 24.93 O ANISOU 1704 O LYS A 230 2637 3552 3283 -879 164 -1028 O ATOM 1705 CB LYS A 230 28.981 46.505 11.405 1.00 24.66 C ANISOU 1705 CB LYS A 230 2393 3740 3238 -761 -5 -1067 C ATOM 1706 CG LYS A 230 29.350 45.931 10.045 1.00 24.41 C ANISOU 1706 CG LYS A 230 2467 3665 3144 -737 -31 -1093 C ATOM 1707 CD LYS A 230 28.863 46.811 8.897 1.00 24.37 C ANISOU 1707 CD LYS A 230 2444 3726 3089 -671 -130 -1131 C ATOM 1708 CE LYS A 230 29.328 46.270 7.541 1.00 25.19 C ANISOU 1708 CE LYS A 230 2673 3782 3117 -641 -149 -1151 C ATOM 1709 NZ LYS A 230 28.837 47.088 6.389 1.00 25.57 N ANISOU 1709 NZ LYS A 230 2723 3889 3103 -577 -252 -1188 N ATOM 1710 N ILE A 231 31.196 45.275 13.270 1.00 23.88 N ANISOU 1710 N ILE A 231 2427 3471 3173 -774 184 -911 N ATOM 1711 CA ILE A 231 32.527 44.680 13.365 1.00 23.98 C ANISOU 1711 CA ILE A 231 2539 3399 3174 -733 245 -844 C ATOM 1712 C ILE A 231 32.472 43.390 14.177 1.00 24.72 C ANISOU 1712 C ILE A 231 2683 3416 3292 -814 305 -846 C ATOM 1713 O ILE A 231 33.012 42.368 13.761 1.00 25.14 O ANISOU 1713 O ILE A 231 2838 3388 3326 -813 337 -846 O ATOM 1714 CB ILE A 231 33.539 45.689 13.977 1.00 22.93 C ANISOU 1714 CB ILE A 231 2383 3280 3050 -655 262 -754 C ATOM 1715 CG1 ILE A 231 33.838 46.816 12.978 1.00 23.11 C ANISOU 1715 CG1 ILE A 231 2394 3350 3035 -571 215 -742 C ATOM 1716 CG2 ILE A 231 34.846 44.996 14.380 1.00 22.81 C ANISOU 1716 CG2 ILE A 231 2445 3184 3038 -622 326 -685 C ATOM 1717 CD1 ILE A 231 34.288 48.112 13.641 1.00 22.83 C ANISOU 1717 CD1 ILE A 231 2304 3353 3016 -522 208 -679 C ATOM 1718 N MET A 232 31.791 43.441 15.317 1.00 25.37 N ANISOU 1718 N MET A 232 2704 3522 3413 -884 324 -849 N ATOM 1719 CA MET A 232 31.654 42.283 16.200 1.00 26.82 C ANISOU 1719 CA MET A 232 2942 3633 3617 -970 386 -846 C ATOM 1720 C MET A 232 30.489 41.365 15.809 1.00 28.39 C ANISOU 1720 C MET A 232 3143 3821 3822 -1086 379 -938 C ATOM 1721 O MET A 232 30.272 40.337 16.444 1.00 29.01 O ANISOU 1721 O MET A 232 3277 3831 3913 -1174 433 -943 O ATOM 1722 CB MET A 232 31.504 42.751 17.651 1.00 26.57 C ANISOU 1722 CB MET A 232 2855 3628 3614 -996 419 -803 C ATOM 1723 CG MET A 232 32.753 43.452 18.180 1.00 26.31 C ANISOU 1723 CG MET A 232 2836 3585 3574 -897 428 -710 C ATOM 1724 SD MET A 232 32.704 43.768 19.948 1.00 29.06 S ANISOU 1724 SD MET A 232 3159 3941 3942 -929 470 -658 S ATOM 1725 CE MET A 232 34.502 43.804 20.353 1.00 28.60 C ANISOU 1725 CE MET A 232 3176 3819 3871 -825 482 -551 C ATOM 1726 N GLU A 233 29.753 41.753 14.767 1.00 29.44 N ANISOU 1726 N GLU A 233 3220 4021 3944 -1088 310 -1010 N ATOM 1727 CA GLU A 233 28.666 40.962 14.194 1.00 31.12 C ANISOU 1727 CA GLU A 233 3426 4235 4162 -1194 284 -1107 C ATOM 1728 C GLU A 233 27.661 40.536 15.260 1.00 32.07 C ANISOU 1728 C GLU A 233 3483 4370 4331 -1325 327 -1138 C ATOM 1729 O GLU A 233 27.373 39.359 15.451 1.00 32.61 O ANISOU 1729 O GLU A 233 3619 4364 4408 -1431 370 -1166 O ATOM 1730 CB GLU A 233 29.239 39.780 13.415 1.00 32.01 C ANISOU 1730 CB GLU A 233 3686 4238 4237 -1200 301 -1120 C ATOM 1731 CG GLU A 233 30.221 40.247 12.341 1.00 32.26 C ANISOU 1731 CG GLU A 233 3774 4265 4217 -1069 269 -1092 C ATOM 1732 CD GLU A 233 30.851 39.131 11.545 1.00 34.89 C ANISOU 1732 CD GLU A 233 4258 4492 4509 -1057 293 -1106 C ATOM 1733 OE1 GLU A 233 30.839 37.976 12.020 1.00 37.19 O ANISOU 1733 OE1 GLU A 233 4629 4689 4813 -1130 345 -1112 O ATOM 1734 OE2 GLU A 233 31.374 39.419 10.437 1.00 35.61 O ANISOU 1734 OE2 GLU A 233 4394 4587 4550 -970 262 -1110 O ATOM 1735 N ASP A 234 27.142 41.528 15.968 1.00 32.23 N ANISOU 1735 N ASP A 234 3379 4484 4382 -1318 322 -1131 N ATOM 1736 CA ASP A 234 26.193 41.288 17.039 1.00 33.21 C ANISOU 1736 CA ASP A 234 3430 4638 4551 -1433 374 -1157 C ATOM 1737 C ASP A 234 25.440 42.571 17.322 1.00 33.24 C ANISOU 1737 C ASP A 234 3275 4772 4583 -1399 337 -1180 C ATOM 1738 O ASP A 234 25.946 43.460 18.002 1.00 32.12 O ANISOU 1738 O ASP A 234 3115 4651 4437 -1320 352 -1116 O ATOM 1739 CB ASP A 234 26.922 40.793 18.293 1.00 33.10 C ANISOU 1739 CB ASP A 234 3506 4536 4535 -1450 467 -1074 C ATOM 1740 CG ASP A 234 25.971 40.380 19.405 1.00 34.36 C ANISOU 1740 CG ASP A 234 3618 4709 4729 -1583 538 -1097 C ATOM 1741 OD1 ASP A 234 24.739 40.368 19.197 1.00 35.69 O ANISOU 1741 OD1 ASP A 234 3675 4953 4933 -1674 522 -1183 O ATOM 1742 OD2 ASP A 234 26.376 40.054 20.534 1.00 36.48 O ANISOU 1742 OD2 ASP A 234 3952 4917 4990 -1606 614 -1034 O ATOM 1743 N ASP A 235 24.224 42.658 16.790 1.00 34.71 N ANISOU 1743 N ASP A 235 3347 5044 4796 -1457 285 -1274 N ATOM 1744 CA ASP A 235 23.376 43.829 16.990 1.00 35.34 C ANISOU 1744 CA ASP A 235 3266 5252 4907 -1419 244 -1309 C ATOM 1745 C ASP A 235 22.819 43.931 18.415 1.00 35.51 C ANISOU 1745 C ASP A 235 3213 5308 4970 -1488 332 -1301 C ATOM 1746 O ASP A 235 22.292 44.981 18.796 1.00 35.55 O ANISOU 1746 O ASP A 235 3099 5410 4998 -1438 316 -1314 O ATOM 1747 CB ASP A 235 22.237 43.845 15.959 1.00 36.87 C ANISOU 1747 CB ASP A 235 3355 5534 5121 -1454 152 -1417 C ATOM 1748 CG ASP A 235 22.721 44.225 14.570 1.00 38.34 C ANISOU 1748 CG ASP A 235 3596 5716 5254 -1348 51 -1422 C ATOM 1749 OD1 ASP A 235 23.495 45.202 14.452 1.00 39.27 O ANISOU 1749 OD1 ASP A 235 3744 5836 5340 -1217 28 -1357 O ATOM 1750 OD2 ASP A 235 22.390 43.607 13.537 1.00 42.29 O ANISOU 1750 OD2 ASP A 235 4123 6208 5739 -1388 -10 -1487 O ATOM 1751 N SER A 236 22.949 42.863 19.204 1.00 35.75 N ANISOU 1751 N SER A 236 3323 5255 5004 -1597 426 -1277 N ATOM 1752 CA SER A 236 22.479 42.873 20.596 1.00 36.14 C ANISOU 1752 CA SER A 236 3326 5325 5080 -1669 523 -1263 C ATOM 1753 C SER A 236 23.448 43.538 21.582 1.00 34.50 C ANISOU 1753 C SER A 236 3182 5085 4842 -1577 565 -1163 C ATOM 1754 O SER A 236 23.112 43.692 22.751 1.00 35.01 O ANISOU 1754 O SER A 236 3216 5170 4916 -1619 641 -1148 O ATOM 1755 CB SER A 236 22.138 41.449 21.075 1.00 37.26 C ANISOU 1755 CB SER A 236 3536 5388 5234 -1835 611 -1279 C ATOM 1756 OG SER A 236 23.309 40.693 21.347 1.00 37.10 O ANISOU 1756 OG SER A 236 3701 5228 5169 -1820 653 -1196 O ATOM 1757 N ILE A 237 24.638 43.937 21.130 1.00 33.33 N ANISOU 1757 N ILE A 237 3121 4888 4656 -1456 517 -1098 N ATOM 1758 CA ILE A 237 25.556 44.674 22.001 1.00 31.79 C ANISOU 1758 CA ILE A 237 2971 4672 4435 -1367 540 -1010 C ATOM 1759 C ILE A 237 25.030 46.098 22.144 1.00 31.25 C ANISOU 1759 C ILE A 237 2776 4715 4381 -1293 501 -1033 C ATOM 1760 O ILE A 237 24.930 46.836 21.160 1.00 30.89 O ANISOU 1760 O ILE A 237 2676 4723 4337 -1213 416 -1062 O ATOM 1761 CB ILE A 237 27.002 44.718 21.459 1.00 31.06 C ANISOU 1761 CB ILE A 237 2994 4504 4304 -1263 503 -937 C ATOM 1762 CG1 ILE A 237 27.557 43.313 21.201 1.00 31.59 C ANISOU 1762 CG1 ILE A 237 3192 4457 4355 -1316 535 -919 C ATOM 1763 CG2 ILE A 237 27.911 45.458 22.469 1.00 30.22 C ANISOU 1763 CG2 ILE A 237 2925 4381 4177 -1188 524 -850 C ATOM 1764 CD1 ILE A 237 28.792 43.301 20.284 1.00 31.25 C ANISOU 1764 CD1 ILE A 237 3236 4357 4282 -1211 490 -873 C ATOM 1765 N ALA A 238 24.674 46.466 23.368 1.00 30.83 N ANISOU 1765 N ALA A 238 2685 4693 4335 -1317 566 -1021 N ATOM 1766 CA ALA A 238 24.219 47.813 23.660 1.00 30.40 C ANISOU 1766 CA ALA A 238 2526 4732 4292 -1240 540 -1040 C ATOM 1767 C ALA A 238 25.436 48.733 23.750 1.00 28.89 C ANISOU 1767 C ALA A 238 2409 4505 4063 -1116 500 -959 C ATOM 1768 O ALA A 238 26.359 48.464 24.522 1.00 28.32 O ANISOU 1768 O ALA A 238 2440 4358 3962 -1116 542 -885 O ATOM 1769 CB ALA A 238 23.425 47.830 24.964 1.00 31.01 C ANISOU 1769 CB ALA A 238 2548 4850 4384 -1312 634 -1058 C ATOM 1770 N VAL A 239 25.436 49.794 22.944 1.00 28.17 N ANISOU 1770 N VAL A 239 2266 4465 3972 -1015 416 -974 N ATOM 1771 CA VAL A 239 26.527 50.767 22.904 1.00 27.18 C ANISOU 1771 CA VAL A 239 2201 4310 3815 -904 374 -904 C ATOM 1772 C VAL A 239 25.987 52.207 22.896 1.00 26.88 C ANISOU 1772 C VAL A 239 2078 4351 3784 -817 326 -933 C ATOM 1773 O VAL A 239 25.203 52.581 22.025 1.00 26.77 O ANISOU 1773 O VAL A 239 1983 4402 3787 -785 265 -995 O ATOM 1774 CB VAL A 239 27.427 50.579 21.651 1.00 26.93 C ANISOU 1774 CB VAL A 239 2239 4231 3763 -854 313 -875 C ATOM 1775 CG1 VAL A 239 28.613 51.547 21.682 1.00 26.10 C ANISOU 1775 CG1 VAL A 239 2193 4093 3629 -757 282 -799 C ATOM 1776 CG2 VAL A 239 27.924 49.140 21.536 1.00 27.91 C ANISOU 1776 CG2 VAL A 239 2450 4273 3880 -927 355 -855 C ATOM 1777 N SER A 240 26.413 52.998 23.877 1.00 26.21 N ANISOU 1777 N SER A 240 2022 4256 3682 -776 349 -889 N ATOM 1778 CA SER A 240 26.152 54.437 23.908 1.00 26.00 C ANISOU 1778 CA SER A 240 1949 4278 3651 -679 302 -902 C ATOM 1779 C SER A 240 27.454 55.183 24.150 1.00 24.88 C ANISOU 1779 C SER A 240 1905 4073 3474 -614 279 -819 C ATOM 1780 O SER A 240 28.282 54.745 24.952 1.00 24.83 O ANISOU 1780 O SER A 240 1976 4007 3450 -649 324 -760 O ATOM 1781 CB SER A 240 25.142 54.790 24.999 1.00 26.50 C ANISOU 1781 CB SER A 240 1935 4403 3732 -699 361 -949 C ATOM 1782 OG SER A 240 23.834 54.395 24.622 1.00 28.55 O ANISOU 1782 OG SER A 240 2072 4743 4034 -742 366 -1037 O ATOM 1783 N ALA A 241 27.619 56.311 23.461 1.00 24.40 N ANISOU 1783 N ALA A 241 1843 4025 3403 -520 207 -815 N ATOM 1784 CA ALA A 241 28.862 57.083 23.493 1.00 23.68 C ANISOU 1784 CA ALA A 241 1839 3875 3283 -464 178 -740 C ATOM 1785 C ALA A 241 28.633 58.582 23.690 1.00 23.51 C ANISOU 1785 C ALA A 241 1808 3874 3250 -379 137 -748 C ATOM 1786 O ALA A 241 27.616 59.136 23.269 1.00 23.24 O ANISOU 1786 O ALA A 241 1702 3898 3228 -330 103 -810 O ATOM 1787 CB ALA A 241 29.640 56.859 22.219 1.00 23.66 C ANISOU 1787 CB ALA A 241 1883 3839 3269 -441 132 -707 C ATOM 1788 N THR A 242 29.610 59.213 24.338 1.00 23.03 N ANISOU 1788 N THR A 242 1822 3761 3166 -361 138 -687 N ATOM 1789 CA THR A 242 29.747 60.660 24.397 1.00 23.09 C ANISOU 1789 CA THR A 242 1858 3760 3156 -282 92 -678 C ATOM 1790 C THR A 242 31.125 61.006 23.843 1.00 22.42 C ANISOU 1790 C THR A 242 1856 3611 3052 -266 56 -602 C ATOM 1791 O THR A 242 32.151 60.570 24.385 1.00 21.79 O ANISOU 1791 O THR A 242 1825 3487 2968 -311 82 -545 O ATOM 1792 CB THR A 242 29.627 61.140 25.854 1.00 23.33 C ANISOU 1792 CB THR A 242 1904 3786 3174 -288 133 -680 C ATOM 1793 OG1 THR A 242 28.391 60.673 26.420 1.00 24.27 O ANISOU 1793 OG1 THR A 242 1942 3968 3312 -316 187 -748 O ATOM 1794 CG2 THR A 242 29.532 62.662 25.929 1.00 23.69 C ANISOU 1794 CG2 THR A 242 1978 3822 3202 -203 87 -688 C ATOM 1795 N CYS A 243 31.155 61.785 22.769 1.00 22.51 N ANISOU 1795 N CYS A 243 1883 3618 3052 -203 -3 -601 N ATOM 1796 CA CYS A 243 32.403 62.110 22.088 1.00 22.12 C ANISOU 1796 CA CYS A 243 1905 3513 2985 -193 -29 -532 C ATOM 1797 C CYS A 243 32.772 63.584 22.285 1.00 21.52 C ANISOU 1797 C CYS A 243 1888 3400 2888 -142 -66 -506 C ATOM 1798 O CYS A 243 32.041 64.492 21.878 1.00 21.83 O ANISOU 1798 O CYS A 243 1927 3453 2915 -73 -109 -540 O ATOM 1799 CB CYS A 243 32.303 61.740 20.617 1.00 22.50 C ANISOU 1799 CB CYS A 243 1950 3574 3027 -173 -58 -541 C ATOM 1800 SG CYS A 243 32.110 59.958 20.373 1.00 25.12 S ANISOU 1800 SG CYS A 243 2239 3928 3380 -244 -13 -564 S ATOM 1801 N VAL A 244 33.902 63.807 22.949 1.00 20.66 N ANISOU 1801 N VAL A 244 1832 3244 2776 -177 -54 -447 N ATOM 1802 CA VAL A 244 34.330 65.148 23.339 1.00 20.11 C ANISOU 1802 CA VAL A 244 1826 3129 2687 -150 -85 -423 C ATOM 1803 C VAL A 244 35.695 65.462 22.725 1.00 20.05 C ANISOU 1803 C VAL A 244 1875 3070 2674 -170 -100 -350 C ATOM 1804 O VAL A 244 36.587 64.631 22.764 1.00 20.23 O ANISOU 1804 O VAL A 244 1887 3086 2712 -222 -72 -309 O ATOM 1805 CB VAL A 244 34.428 65.242 24.877 1.00 19.79 C ANISOU 1805 CB VAL A 244 1796 3078 2644 -182 -61 -425 C ATOM 1806 CG1 VAL A 244 34.723 66.667 25.329 1.00 19.64 C ANISOU 1806 CG1 VAL A 244 1849 3010 2603 -153 -97 -413 C ATOM 1807 CG2 VAL A 244 33.167 64.719 25.524 1.00 19.09 C ANISOU 1807 CG2 VAL A 244 1645 3046 2563 -179 -24 -492 C ATOM 1808 N ARG A 245 35.845 66.653 22.148 1.00 20.63 N ANISOU 1808 N ARG A 245 2007 3105 2725 -129 -139 -334 N ATOM 1809 CA ARG A 245 37.148 67.150 21.676 1.00 20.76 C ANISOU 1809 CA ARG A 245 2082 3070 2736 -159 -146 -265 C ATOM 1810 C ARG A 245 37.868 67.888 22.789 1.00 20.78 C ANISOU 1810 C ARG A 245 2127 3029 2741 -197 -156 -237 C ATOM 1811 O ARG A 245 37.263 68.717 23.472 1.00 21.23 O ANISOU 1811 O ARG A 245 2216 3070 2782 -166 -178 -270 O ATOM 1812 CB ARG A 245 36.960 68.113 20.495 1.00 21.04 C ANISOU 1812 CB ARG A 245 2179 3076 2739 -104 -183 -257 C ATOM 1813 CG ARG A 245 38.230 68.361 19.706 1.00 21.01 C ANISOU 1813 CG ARG A 245 2224 3030 2728 -142 -171 -187 C ATOM 1814 CD ARG A 245 38.547 67.259 18.713 1.00 21.15 C ANISOU 1814 CD ARG A 245 2206 3080 2750 -154 -137 -172 C ATOM 1815 NE ARG A 245 37.561 67.224 17.644 1.00 20.47 N ANISOU 1815 NE ARG A 245 2132 3016 2631 -88 -162 -210 N ATOM 1816 CZ ARG A 245 37.569 66.367 16.632 1.00 21.39 C ANISOU 1816 CZ ARG A 245 2233 3158 2735 -84 -144 -212 C ATOM 1817 NH1 ARG A 245 38.537 65.471 16.498 1.00 21.66 N ANISOU 1817 NH1 ARG A 245 2243 3198 2791 -135 -93 -177 N ATOM 1818 NH2 ARG A 245 36.603 66.429 15.733 1.00 22.64 N ANISOU 1818 NH2 ARG A 245 2406 3337 2859 -21 -183 -253 N ATOM 1819 N ILE A 246 39.153 67.592 22.967 1.00 20.70 N ANISOU 1819 N ILE A 246 2115 3001 2749 -261 -141 -180 N ATOM 1820 CA ILE A 246 39.986 68.271 23.957 1.00 20.97 C ANISOU 1820 CA ILE A 246 2186 2996 2787 -308 -161 -151 C ATOM 1821 C ILE A 246 41.272 68.805 23.294 1.00 21.37 C ANISOU 1821 C ILE A 246 2266 3007 2847 -353 -165 -87 C ATOM 1822 O ILE A 246 41.559 68.442 22.162 1.00 21.38 O ANISOU 1822 O ILE A 246 2252 3019 2852 -347 -141 -63 O ATOM 1823 CB ILE A 246 40.278 67.332 25.157 1.00 20.63 C ANISOU 1823 CB ILE A 246 2099 2978 2761 -351 -144 -151 C ATOM 1824 CG1 ILE A 246 41.023 66.071 24.717 1.00 20.20 C ANISOU 1824 CG1 ILE A 246 1986 2952 2737 -380 -111 -115 C ATOM 1825 CG2 ILE A 246 38.972 66.951 25.853 1.00 20.96 C ANISOU 1825 CG2 ILE A 246 2122 3053 2788 -316 -129 -214 C ATOM 1826 CD1 ILE A 246 41.836 65.420 25.829 1.00 20.53 C ANISOU 1826 CD1 ILE A 246 2006 2998 2795 -427 -111 -88 C ATOM 1827 N PRO A 247 42.007 69.700 23.961 1.00 21.72 N ANISOU 1827 N PRO A 247 2355 3005 2892 -399 -194 -63 N ATOM 1828 CA PRO A 247 43.218 70.309 23.384 1.00 22.26 C ANISOU 1828 CA PRO A 247 2447 3036 2973 -455 -195 -4 C ATOM 1829 C PRO A 247 44.429 69.372 23.296 1.00 22.50 C ANISOU 1829 C PRO A 247 2398 3103 3048 -510 -166 43 C ATOM 1830 O PRO A 247 45.441 69.601 23.960 1.00 23.51 O ANISOU 1830 O PRO A 247 2511 3219 3201 -574 -185 73 O ATOM 1831 CB PRO A 247 43.517 71.483 24.343 1.00 22.62 C ANISOU 1831 CB PRO A 247 2563 3024 3009 -494 -242 -5 C ATOM 1832 CG PRO A 247 42.329 71.608 25.225 1.00 22.25 C ANISOU 1832 CG PRO A 247 2542 2979 2932 -438 -260 -68 C ATOM 1833 CD PRO A 247 41.710 70.257 25.293 1.00 22.13 C ANISOU 1833 CD PRO A 247 2446 3035 2929 -405 -226 -93 C ATOM 1834 N VAL A 248 44.311 68.337 22.471 1.00 22.20 N ANISOU 1834 N VAL A 248 2310 3108 3020 -481 -123 46 N ATOM 1835 CA VAL A 248 45.361 67.363 22.232 1.00 22.28 C ANISOU 1835 CA VAL A 248 2245 3153 3070 -512 -87 85 C ATOM 1836 C VAL A 248 45.513 67.343 20.717 1.00 22.70 C ANISOU 1836 C VAL A 248 2308 3206 3111 -494 -43 106 C ATOM 1837 O VAL A 248 44.513 67.323 20.005 1.00 21.51 O ANISOU 1837 O VAL A 248 2194 3055 2924 -438 -39 75 O ATOM 1838 CB VAL A 248 44.938 65.968 22.756 1.00 21.80 C ANISOU 1838 CB VAL A 248 2128 3135 3019 -485 -72 59 C ATOM 1839 CG1 VAL A 248 45.918 64.883 22.332 1.00 21.77 C ANISOU 1839 CG1 VAL A 248 2056 3163 3053 -495 -31 95 C ATOM 1840 CG2 VAL A 248 44.793 65.988 24.277 1.00 21.91 C ANISOU 1840 CG2 VAL A 248 2145 3146 3032 -503 -111 41 C ATOM 1841 N LEU A 249 46.744 67.382 20.214 1.00 23.28 N ANISOU 1841 N LEU A 249 2352 3282 3212 -540 -10 158 N ATOM 1842 CA LEU A 249 46.952 67.376 18.766 1.00 23.85 C ANISOU 1842 CA LEU A 249 2445 3353 3266 -526 43 181 C ATOM 1843 C LEU A 249 46.773 65.984 18.179 1.00 23.46 C ANISOU 1843 C LEU A 249 2347 3348 3218 -479 87 166 C ATOM 1844 O LEU A 249 46.104 65.834 17.160 1.00 23.44 O ANISOU 1844 O LEU A 249 2387 3345 3173 -434 106 148 O ATOM 1845 CB LEU A 249 48.319 67.961 18.382 1.00 25.04 C ANISOU 1845 CB LEU A 249 2579 3491 3443 -596 76 240 C ATOM 1846 CG LEU A 249 48.541 69.429 18.772 1.00 25.99 C ANISOU 1846 CG LEU A 249 2765 3553 3556 -655 37 257 C ATOM 1847 CD1 LEU A 249 49.898 69.932 18.308 1.00 28.15 C ANISOU 1847 CD1 LEU A 249 3014 3819 3861 -738 80 315 C ATOM 1848 CD2 LEU A 249 47.427 70.324 18.234 1.00 26.87 C ANISOU 1848 CD2 LEU A 249 2996 3611 3601 -608 13 234 C ATOM 1849 N SER A 250 47.346 64.972 18.831 1.00 22.94 N ANISOU 1849 N SER A 250 2202 3317 3197 -488 98 172 N ATOM 1850 CA SER A 250 47.325 63.604 18.320 1.00 22.63 C ANISOU 1850 CA SER A 250 2124 3310 3164 -448 144 161 C ATOM 1851 C SER A 250 47.080 62.581 19.412 1.00 21.48 C ANISOU 1851 C SER A 250 1936 3183 3043 -436 123 139 C ATOM 1852 O SER A 250 47.549 62.742 20.539 1.00 20.87 O ANISOU 1852 O SER A 250 1830 3105 2994 -467 87 153 O ATOM 1853 CB SER A 250 48.646 63.262 17.629 1.00 23.23 C ANISOU 1853 CB SER A 250 2149 3405 3272 -463 206 208 C ATOM 1854 OG SER A 250 48.928 64.184 16.605 1.00 26.63 O ANISOU 1854 OG SER A 250 2627 3818 3676 -483 238 235 O ATOM 1855 N ALA A 251 46.353 61.532 19.029 1.00 20.72 N ANISOU 1855 N ALA A 251 1845 3098 2930 -393 145 104 N ATOM 1856 CA ALA A 251 45.993 60.384 19.866 1.00 20.54 C ANISOU 1856 CA ALA A 251 1799 3085 2921 -381 140 80 C ATOM 1857 C ALA A 251 44.706 60.601 20.657 1.00 20.37 C ANISOU 1857 C ALA A 251 1807 3057 2874 -381 100 32 C ATOM 1858 O ALA A 251 44.591 61.564 21.423 1.00 20.30 O ANISOU 1858 O ALA A 251 1814 3038 2862 -403 59 33 O ATOM 1859 CB ALA A 251 47.154 59.961 20.798 1.00 20.97 C ANISOU 1859 CB ALA A 251 1799 3147 3023 -400 133 121 C ATOM 1860 N HIS A 252 43.733 59.709 20.437 1.00 20.06 N ANISOU 1860 N HIS A 252 1777 3027 2820 -359 115 -13 N ATOM 1861 CA HIS A 252 42.485 59.675 21.197 1.00 19.71 C ANISOU 1861 CA HIS A 252 1743 2986 2758 -361 92 -63 C ATOM 1862 C HIS A 252 42.625 58.795 22.424 1.00 19.74 C ANISOU 1862 C HIS A 252 1734 2987 2778 -382 97 -57 C ATOM 1863 O HIS A 252 43.298 57.774 22.394 1.00 19.97 O ANISOU 1863 O HIS A 252 1750 3011 2828 -378 123 -34 O ATOM 1864 CB HIS A 252 41.339 59.121 20.336 1.00 19.88 C ANISOU 1864 CB HIS A 252 1773 3023 2757 -338 106 -117 C ATOM 1865 CG HIS A 252 41.067 59.931 19.110 1.00 20.30 C ANISOU 1865 CG HIS A 252 1852 3079 2782 -309 94 -126 C ATOM 1866 ND1 HIS A 252 40.457 59.417 17.984 1.00 21.48 N ANISOU 1866 ND1 HIS A 252 2015 3240 2908 -284 103 -161 N ATOM 1867 CD2 HIS A 252 41.315 61.231 18.844 1.00 19.00 C ANISOU 1867 CD2 HIS A 252 1716 2900 2602 -301 68 -104 C ATOM 1868 CE1 HIS A 252 40.362 60.370 17.072 1.00 20.25 C ANISOU 1868 CE1 HIS A 252 1894 3080 2720 -256 83 -157 C ATOM 1869 NE2 HIS A 252 40.872 61.481 17.571 1.00 21.09 N ANISOU 1869 NE2 HIS A 252 2013 3168 2831 -267 64 -121 N ATOM 1870 N SER A 253 41.951 59.195 23.494 1.00 19.59 N ANISOU 1870 N SER A 253 1727 2968 2747 -398 73 -81 N ATOM 1871 CA SER A 253 41.862 58.427 24.711 1.00 19.30 C ANISOU 1871 CA SER A 253 1697 2927 2711 -419 79 -81 C ATOM 1872 C SER A 253 40.398 58.152 24.976 1.00 19.57 C ANISOU 1872 C SER A 253 1737 2976 2725 -425 97 -142 C ATOM 1873 O SER A 253 39.535 58.943 24.589 1.00 19.56 O ANISOU 1873 O SER A 253 1731 2991 2710 -409 84 -182 O ATOM 1874 CB SER A 253 42.468 59.198 25.870 1.00 19.47 C ANISOU 1874 CB SER A 253 1732 2937 2730 -438 39 -52 C ATOM 1875 OG SER A 253 43.690 59.792 25.495 1.00 20.12 O ANISOU 1875 OG SER A 253 1796 3014 2834 -441 16 -4 O ATOM 1876 N GLU A 254 40.114 57.036 25.637 1.00 19.56 N ANISOU 1876 N GLU A 254 1745 2966 2720 -447 126 -149 N ATOM 1877 CA GLU A 254 38.741 56.619 25.858 1.00 19.85 C ANISOU 1877 CA GLU A 254 1777 3021 2744 -466 156 -209 C ATOM 1878 C GLU A 254 38.569 56.017 27.240 1.00 19.58 C ANISOU 1878 C GLU A 254 1774 2972 2693 -502 178 -203 C ATOM 1879 O GLU A 254 39.295 55.106 27.629 1.00 19.32 O ANISOU 1879 O GLU A 254 1771 2908 2663 -511 189 -163 O ATOM 1880 CB GLU A 254 38.310 55.606 24.800 1.00 20.34 C ANISOU 1880 CB GLU A 254 1826 3086 2817 -468 186 -237 C ATOM 1881 CG GLU A 254 38.175 56.192 23.403 1.00 22.39 C ANISOU 1881 CG GLU A 254 2065 3366 3079 -432 165 -255 C ATOM 1882 CD GLU A 254 38.028 55.138 22.318 1.00 24.94 C ANISOU 1882 CD GLU A 254 2388 3683 3405 -432 189 -275 C ATOM 1883 OE1 GLU A 254 37.737 55.518 21.157 1.00 25.64 O ANISOU 1883 OE1 GLU A 254 2468 3789 3485 -405 171 -299 O ATOM 1884 OE2 GLU A 254 38.223 53.939 22.609 1.00 27.01 O ANISOU 1884 OE2 GLU A 254 2671 3918 3675 -456 223 -267 O ATOM 1885 N SER A 255 37.608 56.552 27.979 1.00 19.13 N ANISOU 1885 N SER A 255 1717 2936 2615 -516 187 -243 N ATOM 1886 CA SER A 255 37.124 55.915 29.189 1.00 19.53 C ANISOU 1886 CA SER A 255 1801 2978 2641 -556 227 -252 C ATOM 1887 C SER A 255 36.011 54.932 28.798 1.00 19.80 C ANISOU 1887 C SER A 255 1809 3028 2685 -592 282 -302 C ATOM 1888 O SER A 255 34.922 55.349 28.390 1.00 19.52 O ANISOU 1888 O SER A 255 1722 3036 2658 -590 292 -362 O ATOM 1889 CB SER A 255 36.601 56.958 30.171 1.00 19.31 C ANISOU 1889 CB SER A 255 1786 2968 2584 -555 221 -276 C ATOM 1890 OG SER A 255 36.222 56.329 31.366 1.00 19.30 O ANISOU 1890 OG SER A 255 1828 2957 2550 -596 267 -278 O ATOM 1891 N VAL A 256 36.303 53.635 28.922 1.00 20.11 N ANISOU 1891 N VAL A 256 1886 3030 2725 -623 314 -278 N ATOM 1892 CA VAL A 256 35.402 52.577 28.482 1.00 20.75 C ANISOU 1892 CA VAL A 256 1954 3112 2817 -668 365 -322 C ATOM 1893 C VAL A 256 34.867 51.744 29.649 1.00 21.05 C ANISOU 1893 C VAL A 256 2041 3128 2829 -732 427 -325 C ATOM 1894 O VAL A 256 35.626 51.197 30.456 1.00 21.34 O ANISOU 1894 O VAL A 256 2154 3115 2841 -738 431 -270 O ATOM 1895 CB VAL A 256 36.103 51.616 27.493 1.00 20.98 C ANISOU 1895 CB VAL A 256 2002 3103 2866 -656 361 -298 C ATOM 1896 CG1 VAL A 256 35.141 50.516 27.045 1.00 21.64 C ANISOU 1896 CG1 VAL A 256 2082 3181 2960 -713 409 -349 C ATOM 1897 CG2 VAL A 256 36.645 52.380 26.294 1.00 20.94 C ANISOU 1897 CG2 VAL A 256 1958 3119 2881 -597 312 -293 C ATOM 1898 N TYR A 257 33.548 51.646 29.714 1.00 21.41 N ANISOU 1898 N TYR A 257 2042 3213 2879 -781 474 -389 N ATOM 1899 CA TYR A 257 32.873 50.769 30.645 1.00 22.16 C ANISOU 1899 CA TYR A 257 2177 3291 2952 -858 550 -400 C ATOM 1900 C TYR A 257 32.213 49.642 29.860 1.00 22.71 C ANISOU 1900 C TYR A 257 2228 3352 3050 -917 587 -441 C ATOM 1901 O TYR A 257 31.492 49.905 28.900 1.00 23.01 O ANISOU 1901 O TYR A 257 2179 3441 3121 -915 572 -500 O ATOM 1902 CB TYR A 257 31.796 51.534 31.410 1.00 22.45 C ANISOU 1902 CB TYR A 257 2167 3388 2975 -878 589 -451 C ATOM 1903 CG TYR A 257 30.974 50.646 32.311 1.00 23.54 C ANISOU 1903 CG TYR A 257 2338 3516 3091 -969 683 -468 C ATOM 1904 CD1 TYR A 257 31.504 50.173 33.498 1.00 24.49 C ANISOU 1904 CD1 TYR A 257 2571 3577 3156 -994 714 -412 C ATOM 1905 CD2 TYR A 257 29.675 50.260 31.969 1.00 25.58 C ANISOU 1905 CD2 TYR A 257 2516 3823 3381 -1035 739 -542 C ATOM 1906 CE1 TYR A 257 30.779 49.352 34.337 1.00 25.91 C ANISOU 1906 CE1 TYR A 257 2797 3741 3308 -1083 808 -422 C ATOM 1907 CE2 TYR A 257 28.929 49.428 32.810 1.00 26.67 C ANISOU 1907 CE2 TYR A 257 2685 3951 3499 -1133 837 -556 C ATOM 1908 CZ TYR A 257 29.492 48.979 33.997 1.00 26.89 C ANISOU 1908 CZ TYR A 257 2839 3911 3465 -1157 876 -494 C ATOM 1909 OH TYR A 257 28.791 48.158 34.860 1.00 28.07 O ANISOU 1909 OH TYR A 257 3038 4043 3586 -1257 979 -501 O ATOM 1910 N ILE A 258 32.445 48.401 30.273 1.00 23.06 N ANISOU 1910 N ILE A 258 2359 3327 3077 -970 632 -410 N ATOM 1911 CA ILE A 258 31.708 47.259 29.739 1.00 24.02 C ANISOU 1911 CA ILE A 258 2478 3428 3218 -1048 679 -452 C ATOM 1912 C ILE A 258 30.994 46.464 30.834 1.00 24.90 C ANISOU 1912 C ILE A 258 2646 3512 3303 -1148 770 -457 C ATOM 1913 O ILE A 258 31.278 46.596 32.028 1.00 24.77 O ANISOU 1913 O ILE A 258 2697 3473 3241 -1150 796 -413 O ATOM 1914 CB ILE A 258 32.645 46.317 28.937 1.00 23.77 C ANISOU 1914 CB ILE A 258 2515 3322 3195 -1023 653 -415 C ATOM 1915 CG1 ILE A 258 33.723 45.708 29.842 1.00 24.11 C ANISOU 1915 CG1 ILE A 258 2681 3279 3200 -1002 659 -332 C ATOM 1916 CG2 ILE A 258 33.271 47.066 27.777 1.00 24.02 C ANISOU 1916 CG2 ILE A 258 2490 3384 3251 -934 578 -415 C ATOM 1917 CD1 ILE A 258 34.607 44.692 29.146 1.00 24.33 C ANISOU 1917 CD1 ILE A 258 2780 3229 3236 -970 643 -299 C ATOM 1918 N GLU A 259 30.043 45.655 30.400 1.00 25.55 N ANISOU 1918 N GLU A 259 2700 3598 3410 -1238 819 -513 N ATOM 1919 CA GLU A 259 29.541 44.545 31.195 1.00 26.57 C ANISOU 1919 CA GLU A 259 2909 3670 3516 -1348 911 -508 C ATOM 1920 C GLU A 259 29.668 43.299 30.321 1.00 26.96 C ANISOU 1920 C GLU A 259 3013 3647 3585 -1391 912 -516 C ATOM 1921 O GLU A 259 29.184 43.274 29.189 1.00 26.20 O ANISOU 1921 O GLU A 259 2834 3589 3532 -1402 882 -577 O ATOM 1922 CB GLU A 259 28.100 44.802 31.661 1.00 27.51 C ANISOU 1922 CB GLU A 259 2934 3870 3648 -1437 986 -579 C ATOM 1923 CG GLU A 259 28.034 45.934 32.678 1.00 27.44 C ANISOU 1923 CG GLU A 259 2901 3917 3607 -1392 998 -568 C ATOM 1924 CD GLU A 259 26.634 46.243 33.178 1.00 28.93 C ANISOU 1924 CD GLU A 259 2989 4191 3809 -1466 1081 -639 C ATOM 1925 OE1 GLU A 259 25.651 45.699 32.647 1.00 30.52 O ANISOU 1925 OE1 GLU A 259 3112 4429 4058 -1553 1120 -706 O ATOM 1926 OE2 GLU A 259 26.522 47.049 34.118 1.00 29.12 O ANISOU 1926 OE2 GLU A 259 3012 4252 3799 -1437 1108 -633 O ATOM 1927 N THR A 260 30.386 42.302 30.831 1.00 27.42 N ANISOU 1927 N THR A 260 3218 3594 3605 -1403 936 -451 N ATOM 1928 CA THR A 260 30.590 41.041 30.135 1.00 28.14 C ANISOU 1928 CA THR A 260 3392 3594 3707 -1439 944 -452 C ATOM 1929 C THR A 260 29.402 40.120 30.380 1.00 29.66 C ANISOU 1929 C THR A 260 3602 3764 3904 -1593 1035 -502 C ATOM 1930 O THR A 260 28.557 40.407 31.225 1.00 29.85 O ANISOU 1930 O THR A 260 3586 3838 3918 -1666 1100 -522 O ATOM 1931 CB THR A 260 31.890 40.358 30.620 1.00 28.17 C ANISOU 1931 CB THR A 260 3554 3483 3667 -1374 929 -360 C ATOM 1932 OG1 THR A 260 31.918 40.303 32.055 1.00 28.21 O ANISOU 1932 OG1 THR A 260 3644 3457 3618 -1403 977 -308 O ATOM 1933 CG2 THR A 260 33.096 41.179 30.258 1.00 27.19 C ANISOU 1933 CG2 THR A 260 3399 3383 3549 -1232 840 -316 C ATOM 1934 N LYS A 261 29.337 39.025 29.632 1.00 30.67 N ANISOU 1934 N LYS A 261 3789 3816 4046 -1646 1043 -524 N ATOM 1935 CA LYS A 261 28.269 38.028 29.803 1.00 32.83 C ANISOU 1935 CA LYS A 261 4093 4054 4328 -1808 1129 -571 C ATOM 1936 C LYS A 261 28.580 37.074 30.956 1.00 33.86 C ANISOU 1936 C LYS A 261 4405 4060 4399 -1862 1204 -499 C ATOM 1937 O LYS A 261 27.685 36.479 31.551 1.00 35.11 O ANISOU 1937 O LYS A 261 4596 4197 4549 -2003 1298 -521 O ATOM 1938 CB LYS A 261 28.055 37.235 28.507 1.00 33.37 C ANISOU 1938 CB LYS A 261 4164 4084 4432 -1849 1101 -630 C ATOM 1939 CG LYS A 261 27.311 38.017 27.438 1.00 33.98 C ANISOU 1939 CG LYS A 261 4060 4288 4564 -1844 1044 -720 C ATOM 1940 CD LYS A 261 27.418 37.346 26.081 1.00 36.28 C ANISOU 1940 CD LYS A 261 4376 4535 4874 -1845 994 -765 C ATOM 1941 CE LYS A 261 26.364 37.867 25.125 1.00 37.60 C ANISOU 1941 CE LYS A 261 4374 4821 5091 -1884 949 -868 C ATOM 1942 NZ LYS A 261 26.628 37.387 23.744 1.00 40.13 N ANISOU 1942 NZ LYS A 261 4727 5104 5417 -1858 883 -907 N ATOM 1943 N GLU A 262 29.865 36.959 31.259 1.00 34.03 N ANISOU 1943 N GLU A 262 4545 4004 4380 -1747 1161 -414 N ATOM 1944 CA GLU A 262 30.387 36.080 32.289 1.00 35.43 C ANISOU 1944 CA GLU A 262 4914 4054 4493 -1762 1208 -333 C ATOM 1945 C GLU A 262 31.408 36.882 33.090 1.00 34.33 C ANISOU 1945 C GLU A 262 4798 3934 4313 -1631 1156 -255 C ATOM 1946 O GLU A 262 32.144 37.698 32.523 1.00 33.26 O ANISOU 1946 O GLU A 262 4579 3856 4203 -1509 1069 -249 O ATOM 1947 CB GLU A 262 31.052 34.890 31.606 1.00 36.55 C ANISOU 1947 CB GLU A 262 5189 4062 4634 -1738 1187 -313 C ATOM 1948 CG GLU A 262 31.701 33.880 32.529 1.00 39.80 C ANISOU 1948 CG GLU A 262 5818 4324 4979 -1732 1221 -226 C ATOM 1949 CD GLU A 262 31.811 32.511 31.884 1.00 43.04 C ANISOU 1949 CD GLU A 262 6366 4594 5392 -1770 1239 -235 C ATOM 1950 OE1 GLU A 262 30.820 31.752 31.942 1.00 47.35 O ANISOU 1950 OE1 GLU A 262 6959 5093 5940 -1930 1320 -277 O ATOM 1951 OE2 GLU A 262 32.880 32.198 31.318 1.00 44.11 O ANISOU 1951 OE2 GLU A 262 6562 4668 5530 -1644 1174 -202 O ATOM 1952 N VAL A 263 31.458 36.660 34.400 1.00 34.45 N ANISOU 1952 N VAL A 263 4930 3898 4260 -1662 1207 -197 N ATOM 1953 CA VAL A 263 32.396 37.393 35.250 1.00 33.86 C ANISOU 1953 CA VAL A 263 4888 3840 4139 -1548 1152 -125 C ATOM 1954 C VAL A 263 33.828 37.126 34.784 1.00 32.84 C ANISOU 1954 C VAL A 263 4819 3645 4014 -1405 1057 -67 C ATOM 1955 O VAL A 263 34.252 35.976 34.656 1.00 33.33 O ANISOU 1955 O VAL A 263 5018 3585 4059 -1401 1065 -33 O ATOM 1956 CB VAL A 263 32.236 37.038 36.746 1.00 34.98 C ANISOU 1956 CB VAL A 263 5177 3921 4193 -1606 1224 -68 C ATOM 1957 CG1 VAL A 263 33.338 37.721 37.590 1.00 35.06 C ANISOU 1957 CG1 VAL A 263 5235 3936 4149 -1479 1147 7 C ATOM 1958 CG2 VAL A 263 30.862 37.453 37.234 1.00 35.20 C ANISOU 1958 CG2 VAL A 263 5124 4032 4220 -1735 1325 -129 C ATOM 1959 N ALA A 264 34.551 38.201 34.500 1.00 31.39 N ANISOU 1959 N ALA A 264 4530 3543 3854 -1291 971 -58 N ATOM 1960 CA ALA A 264 35.893 38.114 33.952 1.00 30.50 C ANISOU 1960 CA ALA A 264 4433 3396 3758 -1155 882 -13 C ATOM 1961 C ALA A 264 36.877 38.585 35.015 1.00 30.28 C ANISOU 1961 C ALA A 264 4458 3364 3681 -1065 825 66 C ATOM 1962 O ALA A 264 36.942 39.784 35.288 1.00 29.78 O ANISOU 1962 O ALA A 264 4297 3397 3621 -1035 787 59 O ATOM 1963 CB ALA A 264 35.996 38.983 32.710 1.00 29.48 C ANISOU 1963 CB ALA A 264 4138 3365 3699 -1101 828 -65 C ATOM 1964 N PRO A 265 37.651 37.674 35.612 1.00 30.69 N ANISOU 1964 N PRO A 265 4668 3306 3686 -1018 810 138 N ATOM 1965 CA PRO A 265 38.622 38.080 36.637 1.00 30.55 C ANISOU 1965 CA PRO A 265 4704 3285 3618 -928 741 212 C ATOM 1966 C PRO A 265 39.603 39.083 36.046 1.00 29.47 C ANISOU 1966 C PRO A 265 4428 3234 3534 -813 642 215 C ATOM 1967 O PRO A 265 40.072 38.879 34.937 1.00 29.06 O ANISOU 1967 O PRO A 265 4318 3182 3542 -757 616 199 O ATOM 1968 CB PRO A 265 39.325 36.772 37.017 1.00 31.62 C ANISOU 1968 CB PRO A 265 5024 3280 3710 -880 733 281 C ATOM 1969 CG PRO A 265 38.425 35.678 36.539 1.00 32.30 C ANISOU 1969 CG PRO A 265 5186 3284 3803 -986 827 243 C ATOM 1970 CD PRO A 265 37.702 36.223 35.351 1.00 31.64 C ANISOU 1970 CD PRO A 265 4931 3294 3796 -1038 849 154 C ATOM 1971 N ILE A 266 39.878 40.160 36.767 1.00 29.14 N ANISOU 1971 N ILE A 266 4338 3264 3470 -785 592 232 N ATOM 1972 CA ILE A 266 40.683 41.256 36.243 1.00 28.46 C ANISOU 1972 CA ILE A 266 4112 3266 3435 -700 506 228 C ATOM 1973 C ILE A 266 42.102 40.819 35.855 1.00 28.77 C ANISOU 1973 C ILE A 266 4160 3267 3503 -577 428 281 C ATOM 1974 O ILE A 266 42.662 41.328 34.890 1.00 27.57 O ANISOU 1974 O ILE A 266 3888 3171 3416 -519 389 264 O ATOM 1975 CB ILE A 266 40.729 42.422 37.256 1.00 28.32 C ANISOU 1975 CB ILE A 266 4070 3315 3376 -701 466 239 C ATOM 1976 CG1 ILE A 266 39.324 43.016 37.465 1.00 28.68 C ANISOU 1976 CG1 ILE A 266 4074 3416 3407 -808 546 175 C ATOM 1977 CG2 ILE A 266 41.712 43.506 36.798 1.00 27.54 C ANISOU 1977 CG2 ILE A 266 3844 3292 3327 -616 371 245 C ATOM 1978 CD1 ILE A 266 38.678 43.629 36.223 1.00 27.62 C ANISOU 1978 CD1 ILE A 266 3787 3360 3348 -832 567 101 C ATOM 1979 N GLU A 267 42.668 39.861 36.582 1.00 29.90 N ANISOU 1979 N GLU A 267 4447 3316 3598 -534 411 344 N ATOM 1980 CA GLU A 267 44.015 39.372 36.265 1.00 30.85 C ANISOU 1980 CA GLU A 267 4574 3401 3748 -405 337 393 C ATOM 1981 C GLU A 267 44.009 38.665 34.910 1.00 30.47 C ANISOU 1981 C GLU A 267 4496 3319 3760 -385 378 358 C ATOM 1982 O GLU A 267 44.972 38.749 34.152 1.00 30.17 O ANISOU 1982 O GLU A 267 4378 3307 3779 -287 332 366 O ATOM 1983 CB GLU A 267 44.548 38.424 37.344 1.00 32.37 C ANISOU 1983 CB GLU A 267 4942 3489 3869 -355 307 467 C ATOM 1984 CG GLU A 267 44.192 38.820 38.772 1.00 34.87 C ANISOU 1984 CG GLU A 267 5346 3807 4095 -407 298 496 C ATOM 1985 CD GLU A 267 42.925 38.138 39.280 1.00 37.52 C ANISOU 1985 CD GLU A 267 5818 4072 4366 -531 410 482 C ATOM 1986 OE1 GLU A 267 42.996 36.939 39.641 1.00 41.91 O ANISOU 1986 OE1 GLU A 267 6542 4508 4874 -523 434 525 O ATOM 1987 OE2 GLU A 267 41.861 38.802 39.322 1.00 37.49 O ANISOU 1987 OE2 GLU A 267 5755 4131 4360 -637 476 427 O ATOM 1988 N GLU A 268 42.918 37.960 34.626 1.00 30.60 N ANISOU 1988 N GLU A 268 4580 3281 3764 -483 469 318 N ATOM 1989 CA GLU A 268 42.765 37.238 33.368 1.00 30.62 C ANISOU 1989 CA GLU A 268 4575 3244 3814 -481 511 276 C ATOM 1990 C GLU A 268 42.460 38.185 32.214 1.00 29.04 C ANISOU 1990 C GLU A 268 4205 3153 3677 -498 513 210 C ATOM 1991 O GLU A 268 42.883 37.933 31.088 1.00 28.75 O ANISOU 1991 O GLU A 268 4125 3113 3687 -443 511 189 O ATOM 1992 CB GLU A 268 41.676 36.166 33.489 1.00 31.45 C ANISOU 1992 CB GLU A 268 4814 3251 3882 -594 602 252 C ATOM 1993 CG GLU A 268 42.039 35.049 34.463 1.00 33.97 C ANISOU 1993 CG GLU A 268 5332 3438 4136 -568 605 321 C ATOM 1994 CD GLU A 268 41.024 33.913 34.500 1.00 36.55 C ANISOU 1994 CD GLU A 268 5803 3653 4430 -686 701 299 C ATOM 1995 OE1 GLU A 268 40.340 33.654 33.486 1.00 38.19 O ANISOU 1995 OE1 GLU A 268 5969 3862 4680 -754 751 230 O ATOM 1996 OE2 GLU A 268 40.920 33.257 35.555 1.00 39.75 O ANISOU 1996 OE2 GLU A 268 6374 3965 4763 -715 724 350 O ATOM 1997 N VAL A 269 41.718 39.259 32.495 1.00 27.86 N ANISOU 1997 N VAL A 269 3968 3094 3524 -571 520 177 N ATOM 1998 CA VAL A 269 41.400 40.276 31.492 1.00 26.52 C ANISOU 1998 CA VAL A 269 3643 3026 3405 -583 514 119 C ATOM 1999 C VAL A 269 42.701 40.973 31.077 1.00 25.81 C ANISOU 1999 C VAL A 269 3461 2990 3356 -468 439 152 C ATOM 2000 O VAL A 269 42.966 41.140 29.884 1.00 24.91 O ANISOU 2000 O VAL A 269 3270 2908 3288 -431 437 123 O ATOM 2001 CB VAL A 269 40.378 41.318 32.027 1.00 26.04 C ANISOU 2001 CB VAL A 269 3518 3047 3328 -669 532 82 C ATOM 2002 CG1 VAL A 269 40.197 42.471 31.065 1.00 25.64 C ANISOU 2002 CG1 VAL A 269 3317 3098 3326 -660 509 33 C ATOM 2003 CG2 VAL A 269 39.027 40.670 32.310 1.00 27.22 C ANISOU 2003 CG2 VAL A 269 3730 3160 3450 -792 617 41 C ATOM 2004 N LYS A 270 43.499 41.368 32.068 1.00 25.41 N ANISOU 2004 N LYS A 270 3421 2950 3283 -417 378 210 N ATOM 2005 CA LYS A 270 44.836 41.921 31.840 1.00 25.23 C ANISOU 2005 CA LYS A 270 3314 2972 3299 -313 303 247 C ATOM 2006 C LYS A 270 45.706 41.016 30.966 1.00 25.22 C ANISOU 2006 C LYS A 270 3323 2923 3335 -221 305 262 C ATOM 2007 O LYS A 270 46.330 41.488 30.023 1.00 24.75 O ANISOU 2007 O LYS A 270 3157 2918 3328 -168 291 251 O ATOM 2008 CB LYS A 270 45.566 42.166 33.169 1.00 25.64 C ANISOU 2008 CB LYS A 270 3406 3022 3313 -274 232 309 C ATOM 2009 CG LYS A 270 45.143 43.431 33.892 1.00 25.98 C ANISOU 2009 CG LYS A 270 3403 3138 3333 -332 206 297 C ATOM 2010 CD LYS A 270 45.970 43.629 35.164 1.00 27.69 C ANISOU 2010 CD LYS A 270 3666 3348 3506 -288 124 358 C ATOM 2011 CE LYS A 270 45.381 44.696 36.065 1.00 27.87 C ANISOU 2011 CE LYS A 270 3687 3420 3484 -355 111 342 C ATOM 2012 NZ LYS A 270 46.112 44.773 37.370 1.00 28.57 N ANISOU 2012 NZ LYS A 270 3848 3493 3515 -318 29 399 N ATOM 2013 N ALA A 271 45.738 39.723 31.277 1.00 25.82 N ANISOU 2013 N ALA A 271 3534 2893 3382 -201 329 286 N ATOM 2014 CA ALA A 271 46.565 38.773 30.530 1.00 26.43 C ANISOU 2014 CA ALA A 271 3640 2913 3490 -101 333 299 C ATOM 2015 C ALA A 271 46.063 38.563 29.101 1.00 25.97 C ANISOU 2015 C ALA A 271 3546 2856 3464 -127 395 234 C ATOM 2016 O ALA A 271 46.861 38.398 28.182 1.00 25.65 O ANISOU 2016 O ALA A 271 3458 2824 3465 -39 394 232 O ATOM 2017 CB ALA A 271 46.644 37.445 31.259 1.00 27.76 C ANISOU 2017 CB ALA A 271 3983 2954 3612 -75 342 340 C ATOM 2018 N ALA A 272 44.745 38.576 28.926 1.00 25.54 N ANISOU 2018 N ALA A 272 3514 2799 3390 -245 449 179 N ATOM 2019 CA ALA A 272 44.123 38.380 27.621 1.00 25.30 C ANISOU 2019 CA ALA A 272 3459 2771 3381 -283 498 111 C ATOM 2020 C ALA A 272 44.405 39.556 26.685 1.00 24.77 C ANISOU 2020 C ALA A 272 3240 2816 3356 -256 477 86 C ATOM 2021 O ALA A 272 44.712 39.362 25.508 1.00 24.87 O ANISOU 2021 O ALA A 272 3226 2830 3393 -211 495 58 O ATOM 2022 CB ALA A 272 42.621 38.193 27.786 1.00 25.28 C ANISOU 2022 CB ALA A 272 3500 2753 3351 -423 550 58 C ATOM 2023 N ILE A 273 44.297 40.774 27.209 1.00 24.30 N ANISOU 2023 N ILE A 273 3092 2842 3299 -285 440 94 N ATOM 2024 CA ILE A 273 44.608 41.971 26.431 1.00 24.18 C ANISOU 2024 CA ILE A 273 2945 2925 3318 -262 417 79 C ATOM 2025 C ILE A 273 46.097 42.016 26.077 1.00 24.39 C ANISOU 2025 C ILE A 273 2920 2965 3381 -147 387 124 C ATOM 2026 O ILE A 273 46.458 42.349 24.944 1.00 24.36 O ANISOU 2026 O ILE A 273 2848 3001 3406 -112 401 104 O ATOM 2027 CB ILE A 273 44.157 43.244 27.191 1.00 23.85 C ANISOU 2027 CB ILE A 273 2838 2957 3266 -318 383 79 C ATOM 2028 CG1 ILE A 273 42.626 43.348 27.162 1.00 23.65 C ANISOU 2028 CG1 ILE A 273 2825 2942 3219 -424 423 17 C ATOM 2029 CG2 ILE A 273 44.811 44.501 26.597 1.00 24.02 C ANISOU 2029 CG2 ILE A 273 2739 3066 3323 -280 346 84 C ATOM 2030 CD1 ILE A 273 42.053 44.307 28.175 1.00 24.99 C ANISOU 2030 CD1 ILE A 273 2967 3162 3367 -479 404 17 C ATOM 2031 N ALA A 274 46.953 41.672 27.036 1.00 24.93 N ANISOU 2031 N ALA A 274 3021 3004 3447 -88 347 184 N ATOM 2032 CA ALA A 274 48.396 41.619 26.802 1.00 25.48 C ANISOU 2032 CA ALA A 274 3033 3091 3558 26 316 227 C ATOM 2033 C ALA A 274 48.773 40.618 25.703 1.00 26.01 C ANISOU 2033 C ALA A 274 3134 3106 3643 98 367 209 C ATOM 2034 O ALA A 274 49.685 40.875 24.922 1.00 26.66 O ANISOU 2034 O ALA A 274 3129 3233 3766 171 372 215 O ATOM 2035 CB ALA A 274 49.149 41.284 28.104 1.00 26.06 C ANISOU 2035 CB ALA A 274 3150 3134 3619 81 254 292 C ATOM 2036 N ALA A 275 48.067 39.494 25.632 1.00 26.57 N ANISOU 2036 N ALA A 275 3332 3081 3681 72 411 185 N ATOM 2037 CA ALA A 275 48.339 38.473 24.614 1.00 27.31 C ANISOU 2037 CA ALA A 275 3483 3111 3784 136 462 161 C ATOM 2038 C ALA A 275 47.729 38.777 23.235 1.00 26.85 C ANISOU 2038 C ALA A 275 3387 3088 3728 92 510 93 C ATOM 2039 O ALA A 275 48.082 38.129 22.258 1.00 27.34 O ANISOU 2039 O ALA A 275 3479 3113 3797 153 551 70 O ATOM 2040 CB ALA A 275 47.858 37.113 25.090 1.00 28.18 C ANISOU 2040 CB ALA A 275 3761 3092 3854 122 486 161 C ATOM 2041 N PHE A 276 46.815 39.740 23.159 1.00 25.99 N ANISOU 2041 N PHE A 276 3220 3045 3609 -7 503 60 N ATOM 2042 CA PHE A 276 46.075 40.007 21.928 1.00 25.44 C ANISOU 2042 CA PHE A 276 3129 3003 3532 -55 537 -6 C ATOM 2043 C PHE A 276 46.896 40.833 20.923 1.00 25.00 C ANISOU 2043 C PHE A 276 2969 3027 3504 8 541 -3 C ATOM 2044 O PHE A 276 47.425 41.874 21.289 1.00 24.11 O ANISOU 2044 O PHE A 276 2759 2988 3415 19 505 33 O ATOM 2045 CB PHE A 276 44.796 40.756 22.254 1.00 24.87 C ANISOU 2045 CB PHE A 276 3030 2977 3441 -172 524 -42 C ATOM 2046 CG PHE A 276 43.788 40.750 21.142 1.00 25.09 C ANISOU 2046 CG PHE A 276 3063 3015 3453 -232 550 -117 C ATOM 2047 CD1 PHE A 276 43.028 39.613 20.885 1.00 25.19 C ANISOU 2047 CD1 PHE A 276 3180 2947 3444 -282 584 -163 C ATOM 2048 CD2 PHE A 276 43.587 41.881 20.360 1.00 24.85 C ANISOU 2048 CD2 PHE A 276 2942 3073 3428 -242 535 -142 C ATOM 2049 CE1 PHE A 276 42.091 39.602 19.862 1.00 25.27 C ANISOU 2049 CE1 PHE A 276 3192 2972 3439 -341 596 -237 C ATOM 2050 CE2 PHE A 276 42.640 41.873 19.328 1.00 24.45 C ANISOU 2050 CE2 PHE A 276 2900 3034 3357 -291 547 -212 C ATOM 2051 CZ PHE A 276 41.904 40.736 19.079 1.00 24.84 C ANISOU 2051 CZ PHE A 276 3041 3009 3386 -340 574 -261 C ATOM 2052 N PRO A 277 46.962 40.399 19.659 1.00 25.12 N ANISOU 2052 N PRO A 277 3010 3023 3511 42 586 -43 N ATOM 2053 CA PRO A 277 47.702 41.141 18.630 1.00 25.14 C ANISOU 2053 CA PRO A 277 2926 3096 3530 96 604 -41 C ATOM 2054 C PRO A 277 47.258 42.599 18.491 1.00 24.14 C ANISOU 2054 C PRO A 277 2707 3062 3403 32 575 -47 C ATOM 2055 O PRO A 277 46.062 42.875 18.414 1.00 23.90 O ANISOU 2055 O PRO A 277 2696 3039 3345 -51 561 -91 O ATOM 2056 CB PRO A 277 47.393 40.372 17.336 1.00 25.51 C ANISOU 2056 CB PRO A 277 3051 3095 3546 112 658 -100 C ATOM 2057 CG PRO A 277 46.966 39.031 17.756 1.00 26.70 C ANISOU 2057 CG PRO A 277 3327 3138 3679 102 670 -117 C ATOM 2058 CD PRO A 277 46.346 39.175 19.116 1.00 25.67 C ANISOU 2058 CD PRO A 277 3202 3001 3551 26 626 -94 C ATOM 2059 N GLY A 278 48.219 43.518 18.483 1.00 23.80 N ANISOU 2059 N GLY A 278 2565 3087 3392 72 564 -3 N ATOM 2060 CA GLY A 278 47.927 44.928 18.295 1.00 23.09 C ANISOU 2060 CA GLY A 278 2399 3074 3300 20 538 -5 C ATOM 2061 C GLY A 278 47.578 45.687 19.560 1.00 22.66 C ANISOU 2061 C GLY A 278 2309 3047 3254 -38 478 19 C ATOM 2062 O GLY A 278 47.455 46.900 19.517 1.00 21.05 O ANISOU 2062 O GLY A 278 2045 2901 3052 -72 453 24 O ATOM 2063 N ALA A 279 47.426 44.977 20.680 1.00 23.43 N ANISOU 2063 N ALA A 279 2455 3096 3351 -46 457 35 N ATOM 2064 CA ALA A 279 47.147 45.601 21.965 1.00 23.44 C ANISOU 2064 CA ALA A 279 2437 3117 3352 -94 405 59 C ATOM 2065 C ALA A 279 48.362 45.477 22.885 1.00 24.40 C ANISOU 2065 C ALA A 279 2530 3238 3504 -36 369 123 C ATOM 2066 O ALA A 279 49.056 44.456 22.887 1.00 25.52 O ANISOU 2066 O ALA A 279 2705 3334 3658 35 385 144 O ATOM 2067 CB ALA A 279 45.926 44.967 22.606 1.00 23.72 C ANISOU 2067 CB ALA A 279 2557 3103 3353 -161 409 27 C ATOM 2068 N VAL A 280 48.607 46.525 23.663 1.00 24.01 N ANISOU 2068 N VAL A 280 2421 3239 3465 -62 317 151 N ATOM 2069 CA VAL A 280 49.691 46.565 24.624 1.00 24.45 C ANISOU 2069 CA VAL A 280 2440 3304 3546 -18 264 208 C ATOM 2070 C VAL A 280 49.128 46.912 26.000 1.00 24.31 C ANISOU 2070 C VAL A 280 2461 3278 3495 -75 212 218 C ATOM 2071 O VAL A 280 48.511 47.963 26.174 1.00 23.32 O ANISOU 2071 O VAL A 280 2313 3191 3356 -139 196 199 O ATOM 2072 CB VAL A 280 50.726 47.622 24.270 1.00 24.29 C ANISOU 2072 CB VAL A 280 2302 3358 3571 0 244 234 C ATOM 2073 CG1 VAL A 280 51.731 47.780 25.420 1.00 25.36 C ANISOU 2073 CG1 VAL A 280 2393 3511 3731 30 171 287 C ATOM 2074 CG2 VAL A 280 51.437 47.268 22.961 1.00 24.89 C ANISOU 2074 CG2 VAL A 280 2335 3445 3677 63 305 230 C ATOM 2075 N LEU A 281 49.355 46.024 26.962 1.00 24.70 N ANISOU 2075 N LEU A 281 2580 3277 3529 -45 189 248 N ATOM 2076 CA LEU A 281 49.002 46.256 28.353 1.00 25.13 C ANISOU 2076 CA LEU A 281 2684 3320 3545 -87 139 266 C ATOM 2077 C LEU A 281 49.960 47.261 28.997 1.00 25.64 C ANISOU 2077 C LEU A 281 2667 3443 3632 -74 61 304 C ATOM 2078 O LEU A 281 51.151 46.994 29.167 1.00 25.61 O ANISOU 2078 O LEU A 281 2619 3448 3662 -3 20 346 O ATOM 2079 CB LEU A 281 49.024 44.938 29.131 1.00 26.10 C ANISOU 2079 CB LEU A 281 2922 3360 3636 -53 138 293 C ATOM 2080 CG LEU A 281 48.552 45.014 30.582 1.00 26.78 C ANISOU 2080 CG LEU A 281 3088 3422 3665 -100 101 312 C ATOM 2081 CD1 LEU A 281 47.059 45.333 30.636 1.00 26.53 C ANISOU 2081 CD1 LEU A 281 3095 3390 3594 -202 152 260 C ATOM 2082 CD2 LEU A 281 48.877 43.720 31.325 1.00 27.53 C ANISOU 2082 CD2 LEU A 281 3299 3432 3729 -47 89 353 C ATOM 2083 N GLU A 282 49.413 48.425 29.327 1.00 25.70 N ANISOU 2083 N GLU A 282 2652 3490 3622 -145 40 285 N ATOM 2084 CA GLU A 282 50.098 49.453 30.094 1.00 26.40 C ANISOU 2084 CA GLU A 282 2688 3625 3719 -156 -38 312 C ATOM 2085 C GLU A 282 49.278 49.642 31.364 1.00 25.83 C ANISOU 2085 C GLU A 282 2705 3530 3581 -210 -63 306 C ATOM 2086 O GLU A 282 48.414 50.512 31.436 1.00 24.80 O ANISOU 2086 O GLU A 282 2578 3418 3427 -272 -51 270 O ATOM 2087 CB GLU A 282 50.169 50.744 29.270 1.00 26.38 C ANISOU 2087 CB GLU A 282 2593 3682 3749 -192 -32 292 C ATOM 2088 CG GLU A 282 51.487 51.475 29.329 1.00 29.40 C ANISOU 2088 CG GLU A 282 2874 4116 4181 -175 -91 327 C ATOM 2089 CD GLU A 282 51.745 52.308 28.087 1.00 32.10 C ANISOU 2089 CD GLU A 282 3130 4501 4565 -191 -54 314 C ATOM 2090 OE1 GLU A 282 50.836 53.052 27.657 1.00 30.95 O ANISOU 2090 OE1 GLU A 282 3005 4358 4396 -243 -26 278 O ATOM 2091 OE2 GLU A 282 52.863 52.216 27.535 1.00 35.68 O ANISOU 2091 OE2 GLU A 282 3497 4987 5074 -149 -50 340 O ATOM 2092 N ASP A 283 49.524 48.785 32.350 1.00 23.48 N ANISOU 2092 N ASP A 283 2729 3125 3067 25 -296 191 N ATOM 2093 CA ASP A 283 48.735 48.772 33.581 1.00 23.53 C ANISOU 2093 CA ASP A 283 2837 3072 3032 -30 -284 215 C ATOM 2094 C ASP A 283 49.578 48.313 34.761 1.00 24.63 C ANISOU 2094 C ASP A 283 3033 3214 3111 30 -348 266 C ATOM 2095 O ASP A 283 49.799 47.113 34.968 1.00 25.85 O ANISOU 2095 O ASP A 283 3270 3302 3251 107 -364 296 O ATOM 2096 CB ASP A 283 47.515 47.865 33.414 1.00 23.56 C ANISOU 2096 CB ASP A 283 2934 2968 3051 -62 -219 206 C ATOM 2097 CG ASP A 283 46.334 48.294 34.263 1.00 22.82 C ANISOU 2097 CG ASP A 283 2897 2843 2932 -161 -170 203 C ATOM 2098 OD1 ASP A 283 46.511 48.837 35.383 1.00 22.89 O ANISOU 2098 OD1 ASP A 283 2934 2876 2889 -183 -191 226 O ATOM 2099 OD2 ASP A 283 45.171 48.093 33.882 1.00 22.33 O ANISOU 2099 OD2 ASP A 283 2850 2737 2897 -221 -108 172 O ATOM 2100 N ASP A 284 50.051 49.288 35.527 1.00 24.53 N ANISOU 2100 N ASP A 284 2985 3275 3060 -3 -391 275 N ATOM 2101 CA ASP A 284 50.768 49.036 36.764 1.00 25.61 C ANISOU 2101 CA ASP A 284 3176 3428 3126 39 -462 321 C ATOM 2102 C ASP A 284 50.641 50.294 37.619 1.00 25.14 C ANISOU 2102 C ASP A 284 3110 3420 3021 -54 -473 312 C ATOM 2103 O ASP A 284 51.533 51.136 37.642 1.00 24.89 O ANISOU 2103 O ASP A 284 2987 3489 2983 -64 -527 301 O ATOM 2104 CB ASP A 284 52.229 48.689 36.467 1.00 26.55 C ANISOU 2104 CB ASP A 284 3205 3630 3252 152 -543 332 C ATOM 2105 CG ASP A 284 53.014 48.317 37.710 1.00 28.50 C ANISOU 2105 CG ASP A 284 3505 3900 3424 217 -635 382 C ATOM 2106 OD1 ASP A 284 52.429 48.237 38.817 1.00 28.91 O ANISOU 2106 OD1 ASP A 284 3685 3891 3409 172 -633 415 O ATOM 2107 OD2 ASP A 284 54.242 48.090 37.657 1.00 30.32 O ANISOU 2107 OD2 ASP A 284 3651 4217 3653 316 -715 390 O ATOM 2108 N VAL A 285 49.522 50.408 38.326 1.00 25.01 N ANISOU 2108 N VAL A 285 3194 3337 2972 -127 -417 313 N ATOM 2109 CA VAL A 285 49.198 51.636 39.051 1.00 25.17 C ANISOU 2109 CA VAL A 285 3219 3390 2953 -216 -408 290 C ATOM 2110 C VAL A 285 50.132 51.898 40.238 1.00 25.79 C ANISOU 2110 C VAL A 285 3327 3527 2946 -208 -495 319 C ATOM 2111 O VAL A 285 50.239 53.035 40.702 1.00 25.33 O ANISOU 2111 O VAL A 285 3251 3517 2856 -275 -509 293 O ATOM 2112 CB VAL A 285 47.714 51.682 39.522 1.00 25.04 C ANISOU 2112 CB VAL A 285 3293 3300 2922 -291 -314 273 C ATOM 2113 CG1 VAL A 285 46.765 51.491 38.340 1.00 25.34 C ANISOU 2113 CG1 VAL A 285 3286 3297 3044 -305 -240 237 C ATOM 2114 CG2 VAL A 285 47.442 50.669 40.605 1.00 25.84 C ANISOU 2114 CG2 VAL A 285 3535 3336 2947 -286 -307 321 C ATOM 2115 N ALA A 286 50.798 50.846 40.707 1.00 26.57 N ANISOU 2115 N ALA A 286 3476 3616 3002 -123 -558 372 N ATOM 2116 CA ALA A 286 51.816 50.950 41.755 1.00 27.90 C ANISOU 2116 CA ALA A 286 3661 3852 3087 -93 -662 404 C ATOM 2117 C ALA A 286 52.994 51.825 41.325 1.00 27.83 C ANISOU 2117 C ALA A 286 3495 3976 3104 -92 -735 374 C ATOM 2118 O ALA A 286 53.659 52.430 42.166 1.00 28.31 O ANISOU 2118 O ALA A 286 3546 4113 3098 -122 -810 375 O ATOM 2119 CB ALA A 286 52.310 49.562 42.150 1.00 29.04 C ANISOU 2119 CB ALA A 286 3887 3954 3192 24 -722 468 C ATOM 2120 N HIS A 287 53.239 51.883 40.017 1.00 27.06 N ANISOU 2120 N HIS A 287 3277 3907 3096 -69 -709 345 N ATOM 2121 CA HIS A 287 54.264 52.745 39.438 1.00 27.36 C ANISOU 2121 CA HIS A 287 3160 4070 3164 -91 -753 311 C ATOM 2122 C HIS A 287 53.668 53.760 38.448 1.00 26.14 C ANISOU 2122 C HIS A 287 2956 3905 3073 -185 -673 263 C ATOM 2123 O HIS A 287 54.360 54.269 37.569 1.00 26.32 O ANISOU 2123 O HIS A 287 2857 4008 3138 -201 -680 237 O ATOM 2124 CB HIS A 287 55.326 51.883 38.766 1.00 28.14 C ANISOU 2124 CB HIS A 287 3156 4235 3302 32 -803 323 C ATOM 2125 CG HIS A 287 55.971 50.907 39.698 1.00 29.68 C ANISOU 2125 CG HIS A 287 3401 4440 3436 146 -896 373 C ATOM 2126 ND1 HIS A 287 56.820 51.299 40.711 1.00 31.37 N ANISOU 2126 ND1 HIS A 287 3590 4751 3577 140 -1000 385 N ATOM 2127 CD2 HIS A 287 55.863 49.561 39.798 1.00 30.80 C ANISOU 2127 CD2 HIS A 287 3634 4497 3573 268 -906 416 C ATOM 2128 CE1 HIS A 287 57.223 50.233 41.380 1.00 33.03 C ANISOU 2128 CE1 HIS A 287 3867 4943 3738 265 -1076 437 C ATOM 2129 NE2 HIS A 287 56.653 49.166 40.849 1.00 32.49 N ANISOU 2129 NE2 HIS A 287 3878 4757 3710 345 -1018 458 N ATOM 2130 N GLN A 288 52.385 54.054 38.624 1.00 25.12 N ANISOU 2130 N GLN A 288 2922 3680 2943 -244 -597 251 N ATOM 2131 CA GLN A 288 51.664 55.055 37.831 1.00 24.10 C ANISOU 2131 CA GLN A 288 2769 3527 2862 -321 -529 208 C ATOM 2132 C GLN A 288 51.781 54.804 36.328 1.00 23.37 C ANISOU 2132 C GLN A 288 2587 3446 2848 -286 -497 195 C ATOM 2133 O GLN A 288 52.004 55.734 35.551 1.00 22.64 O ANISOU 2133 O GLN A 288 2427 3391 2783 -340 -486 168 O ATOM 2134 CB GLN A 288 52.149 56.462 38.183 1.00 24.09 C ANISOU 2134 CB GLN A 288 2741 3583 2829 -414 -562 179 C ATOM 2135 CG GLN A 288 51.880 56.883 39.614 1.00 24.67 C ANISOU 2135 CG GLN A 288 2917 3637 2819 -462 -581 178 C ATOM 2136 CD GLN A 288 52.562 58.194 39.951 1.00 24.92 C ANISOU 2136 CD GLN A 288 2925 3730 2815 -556 -627 146 C ATOM 2137 OE1 GLN A 288 52.102 59.273 39.538 1.00 24.26 O ANISOU 2137 OE1 GLN A 288 2853 3610 2753 -626 -584 109 O ATOM 2138 NE2 GLN A 288 53.671 58.109 40.669 1.00 21.61 N ANISOU 2138 NE2 GLN A 288 2472 3400 2337 -557 -720 160 N ATOM 2139 N ILE A 289 51.639 53.539 35.936 1.00 23.52 N ANISOU 2139 N ILE A 289 2618 3425 2893 -201 -482 214 N ATOM 2140 CA ILE A 289 51.666 53.145 34.531 1.00 23.24 C ANISOU 2140 CA ILE A 289 2516 3392 2923 -162 -447 198 C ATOM 2141 C ILE A 289 50.236 52.980 34.009 1.00 22.54 C ANISOU 2141 C ILE A 289 2486 3207 2869 -188 -369 180 C ATOM 2142 O ILE A 289 49.462 52.145 34.492 1.00 22.41 O ANISOU 2142 O ILE A 289 2558 3113 2844 -172 -341 193 O ATOM 2143 CB ILE A 289 52.464 51.844 34.323 1.00 23.96 C ANISOU 2143 CB ILE A 289 2582 3499 3022 -45 -481 219 C ATOM 2144 CG1 ILE A 289 53.897 51.979 34.858 1.00 25.51 C ANISOU 2144 CG1 ILE A 289 2698 3811 3185 -6 -568 232 C ATOM 2145 CG2 ILE A 289 52.482 51.441 32.818 1.00 24.10 C ANISOU 2145 CG2 ILE A 289 2537 3518 3100 -7 -436 192 C ATOM 2146 CD1 ILE A 289 54.633 53.202 34.393 1.00 25.75 C ANISOU 2146 CD1 ILE A 289 2609 3953 3223 -84 -580 202 C ATOM 2147 N TYR A 290 49.910 53.811 33.027 1.00 21.81 N ANISOU 2147 N TYR A 290 2346 3128 2814 -235 -337 149 N ATOM 2148 CA TYR A 290 48.644 53.768 32.307 1.00 21.02 C ANISOU 2148 CA TYR A 290 2272 2963 2753 -253 -276 125 C ATOM 2149 C TYR A 290 48.879 54.372 30.926 1.00 20.49 C ANISOU 2149 C TYR A 290 2131 2934 2718 -267 -266 103 C ATOM 2150 O TYR A 290 49.886 55.062 30.711 1.00 20.62 O ANISOU 2150 O TYR A 290 2090 3023 2723 -288 -296 106 O ATOM 2151 CB TYR A 290 47.554 54.555 33.057 1.00 20.92 C ANISOU 2151 CB TYR A 290 2318 2906 2725 -314 -246 109 C ATOM 2152 CG TYR A 290 48.068 55.735 33.846 1.00 20.87 C ANISOU 2152 CG TYR A 290 2316 2935 2677 -364 -280 109 C ATOM 2153 CD1 TYR A 290 48.536 56.880 33.202 1.00 20.97 C ANISOU 2153 CD1 TYR A 290 2283 2986 2698 -405 -296 94 C ATOM 2154 CD2 TYR A 290 48.096 55.710 35.235 1.00 22.02 C ANISOU 2154 CD2 TYR A 290 2527 3073 2767 -379 -296 122 C ATOM 2155 CE1 TYR A 290 49.012 57.962 33.925 1.00 21.24 C ANISOU 2155 CE1 TYR A 290 2335 3044 2692 -464 -326 89 C ATOM 2156 CE2 TYR A 290 48.576 56.787 35.964 1.00 21.54 C ANISOU 2156 CE2 TYR A 290 2479 3044 2661 -432 -330 114 C ATOM 2157 CZ TYR A 290 49.025 57.912 35.304 1.00 21.82 C ANISOU 2157 CZ TYR A 290 2468 3111 2712 -477 -345 95 C ATOM 2158 OH TYR A 290 49.503 58.984 36.025 1.00 22.10 O ANISOU 2158 OH TYR A 290 2529 3168 2701 -542 -379 82 O ATOM 2159 N PRO A 291 47.978 54.120 29.980 1.00 20.19 N ANISOU 2159 N PRO A 291 2099 2856 2717 -263 -226 82 N ATOM 2160 CA PRO A 291 48.105 54.731 28.650 1.00 19.66 C ANISOU 2160 CA PRO A 291 1982 2822 2668 -279 -218 65 C ATOM 2161 C PRO A 291 48.040 56.266 28.686 1.00 19.44 C ANISOU 2161 C PRO A 291 1957 2804 2625 -345 -228 62 C ATOM 2162 O PRO A 291 47.265 56.834 29.459 1.00 19.16 O ANISOU 2162 O PRO A 291 1971 2726 2584 -370 -223 55 O ATOM 2163 CB PRO A 291 46.930 54.144 27.873 1.00 19.40 C ANISOU 2163 CB PRO A 291 1971 2736 2666 -265 -183 41 C ATOM 2164 CG PRO A 291 46.539 52.913 28.620 1.00 20.17 C ANISOU 2164 CG PRO A 291 2116 2782 2766 -236 -169 46 C ATOM 2165 CD PRO A 291 46.820 53.204 30.065 1.00 19.79 C ANISOU 2165 CD PRO A 291 2102 2733 2684 -250 -188 71 C ATOM 2166 N GLN A 292 48.881 56.914 27.877 1.00 18.59 N ANISOU 2166 N GLN A 292 1805 2751 2508 -373 -238 65 N ATOM 2167 CA GLN A 292 48.868 58.361 27.721 1.00 18.58 C ANISOU 2167 CA GLN A 292 1827 2743 2488 -442 -245 65 C ATOM 2168 C GLN A 292 48.941 58.744 26.254 1.00 18.52 C ANISOU 2168 C GLN A 292 1804 2751 2481 -459 -230 64 C ATOM 2169 O GLN A 292 49.773 58.223 25.533 1.00 18.53 O ANISOU 2169 O GLN A 292 1747 2815 2478 -448 -221 66 O ATOM 2170 CB GLN A 292 50.065 58.987 28.430 1.00 19.08 C ANISOU 2170 CB GLN A 292 1867 2865 2518 -498 -276 77 C ATOM 2171 CG GLN A 292 50.084 58.752 29.916 1.00 19.53 C ANISOU 2171 CG GLN A 292 1950 2913 2556 -490 -301 81 C ATOM 2172 CD GLN A 292 51.196 59.499 30.587 1.00 20.45 C ANISOU 2172 CD GLN A 292 2045 3092 2634 -558 -341 85 C ATOM 2173 OE1 GLN A 292 51.472 60.651 30.235 1.00 19.60 O ANISOU 2173 OE1 GLN A 292 1950 2986 2511 -638 -342 80 O ATOM 2174 NE2 GLN A 292 51.840 58.860 31.559 1.00 20.47 N ANISOU 2174 NE2 GLN A 292 2021 3141 2615 -530 -378 95 N ATOM 2175 N ALA A 293 48.111 59.704 25.848 1.00 18.53 N ANISOU 2175 N ALA A 293 1864 2697 2481 -482 -229 61 N ATOM 2176 CA ALA A 293 48.087 60.215 24.480 1.00 18.62 C ANISOU 2176 CA ALA A 293 1888 2710 2477 -502 -223 67 C ATOM 2177 C ALA A 293 49.487 60.544 23.966 1.00 19.66 C ANISOU 2177 C ALA A 293 1978 2918 2574 -567 -215 83 C ATOM 2178 O ALA A 293 49.886 60.091 22.893 1.00 19.88 O ANISOU 2178 O ALA A 293 1968 2994 2592 -559 -193 82 O ATOM 2179 CB ALA A 293 47.198 61.445 24.397 1.00 18.63 C ANISOU 2179 CB ALA A 293 1973 2634 2471 -518 -238 69 C ATOM 2180 N ILE A 294 50.242 61.315 24.737 1.00 20.16 N ANISOU 2180 N ILE A 294 2044 2999 2615 -636 -230 92 N ATOM 2181 CA ILE A 294 51.547 61.777 24.273 1.00 21.24 C ANISOU 2181 CA ILE A 294 2134 3218 2716 -721 -220 103 C ATOM 2182 C ILE A 294 52.526 60.621 24.064 1.00 21.80 C ANISOU 2182 C ILE A 294 2086 3401 2797 -681 -204 91 C ATOM 2183 O ILE A 294 53.420 60.728 23.244 1.00 23.25 O ANISOU 2183 O ILE A 294 2212 3665 2956 -727 -177 91 O ATOM 2184 CB ILE A 294 52.136 62.865 25.201 1.00 21.56 C ANISOU 2184 CB ILE A 294 2205 3257 2730 -819 -244 107 C ATOM 2185 CG1 ILE A 294 52.437 62.303 26.599 1.00 21.49 C ANISOU 2185 CG1 ILE A 294 2151 3281 2735 -788 -275 95 C ATOM 2186 CG2 ILE A 294 51.187 64.095 25.236 1.00 21.36 C ANISOU 2186 CG2 ILE A 294 2317 3107 2692 -850 -254 114 C ATOM 2187 CD1 ILE A 294 53.075 63.313 27.539 1.00 21.65 C ANISOU 2187 CD1 ILE A 294 2195 3311 2720 -892 -305 92 C ATOM 2188 N ASN A 295 52.337 59.519 24.788 1.00 21.82 N ANISOU 2188 N ASN A 295 2056 3404 2832 -591 -218 81 N ATOM 2189 CA ASN A 295 53.167 58.321 24.624 1.00 22.53 C ANISOU 2189 CA ASN A 295 2047 3579 2934 -522 -210 69 C ATOM 2190 C ASN A 295 52.743 57.433 23.449 1.00 22.56 C ANISOU 2190 C ASN A 295 2050 3571 2952 -454 -172 53 C ATOM 2191 O ASN A 295 53.560 56.694 22.908 1.00 22.99 O ANISOU 2191 O ASN A 295 2026 3703 3005 -411 -150 36 O ATOM 2192 CB ASN A 295 53.172 57.487 25.912 1.00 22.58 C ANISOU 2192 CB ASN A 295 2045 3576 2960 -450 -246 71 C ATOM 2193 CG ASN A 295 53.929 58.157 27.048 1.00 23.20 C ANISOU 2193 CG ASN A 295 2099 3703 3014 -510 -289 79 C ATOM 2194 OD1 ASN A 295 54.769 59.028 26.831 1.00 24.54 O ANISOU 2194 OD1 ASN A 295 2223 3943 3158 -601 -290 77 O ATOM 2195 ND2 ASN A 295 53.650 57.728 28.267 1.00 23.98 N ANISOU 2195 ND2 ASN A 295 2232 3765 3113 -467 -325 87 N ATOM 2196 N ALA A 296 51.474 57.511 23.059 1.00 21.97 N ANISOU 2196 N ALA A 296 2057 3403 2886 -442 -167 53 N ATOM 2197 CA ALA A 296 50.936 56.702 21.966 1.00 21.83 C ANISOU 2197 CA ALA A 296 2050 3368 2876 -388 -141 33 C ATOM 2198 C ALA A 296 51.247 57.241 20.577 1.00 22.38 C ANISOU 2198 C ALA A 296 2119 3479 2905 -437 -111 32 C ATOM 2199 O ALA A 296 51.233 56.475 19.602 1.00 22.48 O ANISOU 2199 O ALA A 296 2120 3512 2910 -396 -82 9 O ATOM 2200 CB ALA A 296 49.437 56.550 22.125 1.00 21.08 C ANISOU 2200 CB ALA A 296 2028 3175 2806 -362 -154 27 C ATOM 2201 N VAL A 297 51.495 58.545 20.473 1.00 22.52 N ANISOU 2201 N VAL A 297 2166 3502 2889 -529 -115 57 N ATOM 2202 CA VAL A 297 51.776 59.173 19.182 1.00 23.32 C ANISOU 2202 CA VAL A 297 2290 3633 2936 -592 -84 66 C ATOM 2203 C VAL A 297 52.978 58.506 18.516 1.00 23.72 C ANISOU 2203 C VAL A 297 2243 3803 2967 -587 -34 43 C ATOM 2204 O VAL A 297 54.037 58.375 19.132 1.00 24.25 O ANISOU 2204 O VAL A 297 2218 3954 3044 -598 -28 36 O ATOM 2205 CB VAL A 297 52.043 60.694 19.320 1.00 23.71 C ANISOU 2205 CB VAL A 297 2397 3664 2948 -706 -94 101 C ATOM 2206 CG1 VAL A 297 52.553 61.284 17.993 1.00 24.97 C ANISOU 2206 CG1 VAL A 297 2583 3865 3038 -787 -52 116 C ATOM 2207 CG2 VAL A 297 50.776 61.408 19.759 1.00 23.47 C ANISOU 2207 CG2 VAL A 297 2474 3510 2932 -692 -138 116 C ATOM 2208 N GLY A 298 52.796 58.067 17.275 1.00 23.50 N ANISOU 2208 N GLY A 298 2232 3789 2909 -565 0 27 N ATOM 2209 CA GLY A 298 53.865 57.455 16.499 1.00 24.55 C ANISOU 2209 CA GLY A 298 2278 4035 3014 -555 60 -4 C ATOM 2210 C GLY A 298 53.885 55.931 16.511 1.00 24.26 C ANISOU 2210 C GLY A 298 2192 4009 3016 -429 70 -50 C ATOM 2211 O GLY A 298 54.614 55.334 15.736 1.00 25.49 O ANISOU 2211 O GLY A 298 2290 4248 3149 -400 124 -86 O ATOM 2212 N SER A 299 53.094 55.306 17.379 1.00 23.15 N ANISOU 2212 N SER A 299 2083 3782 2931 -358 25 -51 N ATOM 2213 CA SER A 299 53.023 53.846 17.468 1.00 22.72 C ANISOU 2213 CA SER A 299 2013 3709 2912 -243 31 -90 C ATOM 2214 C SER A 299 51.731 53.296 16.840 1.00 21.85 C ANISOU 2214 C SER A 299 1994 3505 2803 -216 24 -110 C ATOM 2215 O SER A 299 50.688 53.932 16.907 1.00 20.81 O ANISOU 2215 O SER A 299 1928 3307 2672 -260 -9 -88 O ATOM 2216 CB SER A 299 53.115 53.405 18.931 1.00 22.57 C ANISOU 2216 CB SER A 299 1972 3660 2944 -190 -11 -77 C ATOM 2217 OG SER A 299 52.826 52.019 19.057 1.00 22.77 O ANISOU 2217 OG SER A 299 2021 3630 3000 -86 -11 -106 O ATOM 2218 N ARG A 300 51.828 52.108 16.248 1.00 21.78 N ANISOU 2218 N ARG A 300 1986 3495 2795 -142 53 -157 N ATOM 2219 CA ARG A 300 50.680 51.390 15.681 1.00 21.45 C ANISOU 2219 CA ARG A 300 2025 3370 2755 -119 45 -188 C ATOM 2220 C ARG A 300 49.811 50.687 16.729 1.00 20.94 C ANISOU 2220 C ARG A 300 2003 3205 2747 -83 8 -185 C ATOM 2221 O ARG A 300 48.728 50.201 16.406 1.00 20.92 O ANISOU 2221 O ARG A 300 2062 3134 2751 -88 -3 -209 O ATOM 2222 CB ARG A 300 51.161 50.307 14.724 1.00 21.99 C ANISOU 2222 CB ARG A 300 2091 3464 2798 -54 94 -247 C ATOM 2223 CG ARG A 300 51.825 50.806 13.470 1.00 22.63 C ANISOU 2223 CG ARG A 300 2148 3641 2808 -93 144 -263 C ATOM 2224 CD ARG A 300 52.487 49.685 12.708 1.00 23.88 C ANISOU 2224 CD ARG A 300 2291 3835 2945 -12 202 -330 C ATOM 2225 NE ARG A 300 53.078 50.147 11.461 1.00 24.56 N ANISOU 2225 NE ARG A 300 2360 4021 2952 -57 261 -350 N ATOM 2226 CZ ARG A 300 54.292 50.676 11.345 1.00 25.32 C ANISOU 2226 CZ ARG A 300 2360 4239 3022 -81 312 -344 C ATOM 2227 NH1 ARG A 300 55.092 50.833 12.405 1.00 24.94 N ANISOU 2227 NH1 ARG A 300 2214 4239 3024 -59 301 -322 N ATOM 2228 NH2 ARG A 300 54.710 51.061 10.158 1.00 25.45 N ANISOU 2228 NH2 ARG A 300 2376 4338 2954 -136 375 -362 N ATOM 2229 N ASP A 301 50.300 50.613 17.963 1.00 20.91 N ANISOU 2229 N ASP A 301 1967 3200 2780 -55 -8 -159 N ATOM 2230 CA ASP A 301 49.657 49.857 19.029 1.00 20.71 C ANISOU 2230 CA ASP A 301 1989 3083 2797 -22 -33 -152 C ATOM 2231 C ASP A 301 48.471 50.588 19.644 1.00 20.50 C ANISOU 2231 C ASP A 301 1999 3003 2786 -89 -64 -126 C ATOM 2232 O ASP A 301 48.361 51.823 19.582 1.00 20.19 O ANISOU 2232 O ASP A 301 1944 2996 2732 -148 -78 -101 O ATOM 2233 CB ASP A 301 50.667 49.527 20.146 1.00 21.29 C ANISOU 2233 CB ASP A 301 2020 3179 2889 39 -46 -129 C ATOM 2234 CG ASP A 301 51.775 48.579 19.695 1.00 23.02 C ANISOU 2234 CG ASP A 301 2200 3443 3103 138 -19 -163 C ATOM 2235 OD1 ASP A 301 51.487 47.550 19.072 1.00 25.50 O ANISOU 2235 OD1 ASP A 301 2569 3701 3418 189 4 -205 O ATOM 2236 OD2 ASP A 301 52.978 48.775 19.931 1.00 27.23 O ANISOU 2236 OD2 ASP A 301 2644 4071 3632 175 -20 -157 O ATOM 2237 N THR A 302 47.571 49.802 20.237 1.00 20.45 N ANISOU 2237 N THR A 302 2049 2913 2809 -80 -70 -135 N ATOM 2238 CA THR A 302 46.512 50.322 21.082 1.00 20.04 C ANISOU 2238 CA THR A 302 2020 2818 2777 -131 -90 -116 C ATOM 2239 C THR A 302 46.872 49.977 22.526 1.00 20.20 C ANISOU 2239 C THR A 302 2053 2808 2812 -107 -98 -85 C ATOM 2240 O THR A 302 47.106 48.818 22.854 1.00 20.41 O ANISOU 2240 O THR A 302 2120 2789 2847 -57 -89 -90 O ATOM 2241 CB THR A 302 45.178 49.688 20.685 1.00 20.28 C ANISOU 2241 CB THR A 302 2095 2789 2823 -157 -85 -154 C ATOM 2242 OG1 THR A 302 44.857 50.058 19.331 1.00 20.99 O ANISOU 2242 OG1 THR A 302 2174 2914 2889 -177 -90 -181 O ATOM 2243 CG2 THR A 302 44.032 50.250 21.522 1.00 20.11 C ANISOU 2243 CG2 THR A 302 2077 2741 2823 -207 -97 -144 C ATOM 2244 N PHE A 303 46.945 50.989 23.376 1.00 20.20 N ANISOU 2244 N PHE A 303 2036 2832 2809 -140 -117 -53 N ATOM 2245 CA PHE A 303 47.382 50.819 24.758 1.00 20.20 C ANISOU 2245 CA PHE A 303 2049 2818 2807 -122 -132 -20 C ATOM 2246 C PHE A 303 46.197 50.785 25.710 1.00 20.10 C ANISOU 2246 C PHE A 303 2092 2740 2805 -163 -125 -16 C ATOM 2247 O PHE A 303 45.322 51.651 25.637 1.00 19.86 O ANISOU 2247 O PHE A 303 2054 2711 2781 -212 -122 -26 O ATOM 2248 CB PHE A 303 48.326 51.957 25.134 1.00 20.36 C ANISOU 2248 CB PHE A 303 2016 2912 2808 -143 -157 6 C ATOM 2249 CG PHE A 303 49.526 52.057 24.248 1.00 20.02 C ANISOU 2249 CG PHE A 303 1903 2952 2751 -120 -153 -1 C ATOM 2250 CD1 PHE A 303 50.680 51.340 24.541 1.00 20.90 C ANISOU 2250 CD1 PHE A 303 1975 3107 2859 -49 -164 3 C ATOM 2251 CD2 PHE A 303 49.502 52.868 23.116 1.00 20.46 C ANISOU 2251 CD2 PHE A 303 1935 3047 2793 -165 -139 -13 C ATOM 2252 CE1 PHE A 303 51.799 51.421 23.711 1.00 22.04 C ANISOU 2252 CE1 PHE A 303 2035 3346 2991 -27 -151 -13 C ATOM 2253 CE2 PHE A 303 50.607 52.956 22.284 1.00 21.56 C ANISOU 2253 CE2 PHE A 303 2010 3272 2912 -157 -122 -22 C ATOM 2254 CZ PHE A 303 51.764 52.230 22.582 1.00 22.37 C ANISOU 2254 CZ PHE A 303 2053 3431 3016 -89 -124 -26 C ATOM 2255 N VAL A 304 46.170 49.790 26.600 1.00 20.39 N ANISOU 2255 N VAL A 304 2187 2721 2840 -139 -120 -2 N ATOM 2256 CA VAL A 304 45.069 49.624 27.559 1.00 20.39 C ANISOU 2256 CA VAL A 304 2244 2663 2840 -188 -99 1 C ATOM 2257 C VAL A 304 45.580 49.562 28.998 1.00 20.63 C ANISOU 2257 C VAL A 304 2317 2682 2839 -175 -117 44 C ATOM 2258 O VAL A 304 46.550 48.875 29.283 1.00 20.84 O ANISOU 2258 O VAL A 304 2365 2704 2850 -111 -142 69 O ATOM 2259 CB VAL A 304 44.250 48.352 27.290 1.00 20.51 C ANISOU 2259 CB VAL A 304 2322 2602 2870 -200 -66 -23 C ATOM 2260 CG1 VAL A 304 42.933 48.392 28.068 1.00 21.57 C ANISOU 2260 CG1 VAL A 304 2488 2700 3007 -277 -31 -32 C ATOM 2261 CG2 VAL A 304 43.995 48.184 25.807 1.00 20.57 C ANISOU 2261 CG2 VAL A 304 2295 2622 2897 -199 -60 -67 C ATOM 2262 N GLY A 305 44.901 50.290 29.885 1.00 20.59 N ANISOU 2262 N GLY A 305 2326 2676 2822 -231 -105 48 N ATOM 2263 CA GLY A 305 45.181 50.296 31.312 1.00 20.96 C ANISOU 2263 CA GLY A 305 2428 2712 2826 -235 -117 84 C ATOM 2264 C GLY A 305 44.000 50.811 32.122 1.00 20.97 C ANISOU 2264 C GLY A 305 2457 2694 2816 -305 -76 69 C ATOM 2265 O GLY A 305 42.867 50.859 31.627 1.00 20.34 O ANISOU 2265 O GLY A 305 2358 2603 2769 -344 -35 31 O ATOM 2266 N ARG A 306 44.279 51.215 33.360 1.00 21.25 N ANISOU 2266 N ARG A 306 2533 2737 2803 -318 -88 94 N ATOM 2267 CA ARG A 306 43.257 51.537 34.363 1.00 21.70 C ANISOU 2267 CA ARG A 306 2635 2776 2834 -379 -40 81 C ATOM 2268 C ARG A 306 42.165 50.448 34.425 1.00 22.36 C ANISOU 2268 C ARG A 306 2769 2802 2927 -421 25 70 C ATOM 2269 O ARG A 306 41.003 50.733 34.706 1.00 22.70 O ANISOU 2269 O ARG A 306 2801 2848 2975 -479 83 34 O ATOM 2270 CB ARG A 306 42.627 52.926 34.110 1.00 21.26 C ANISOU 2270 CB ARG A 306 2517 2759 2803 -406 -26 37 C ATOM 2271 CG ARG A 306 43.587 54.124 34.237 1.00 20.91 C ANISOU 2271 CG ARG A 306 2449 2758 2739 -394 -79 45 C ATOM 2272 CD ARG A 306 44.241 54.312 35.607 1.00 19.85 C ANISOU 2272 CD ARG A 306 2376 2632 2535 -406 -105 73 C ATOM 2273 NE ARG A 306 43.318 53.978 36.685 1.00 22.17 N ANISOU 2273 NE ARG A 306 2742 2892 2790 -444 -48 67 N ATOM 2274 CZ ARG A 306 42.378 54.791 37.177 1.00 21.67 C ANISOU 2274 CZ ARG A 306 2686 2830 2719 -480 1 25 C ATOM 2275 NH1 ARG A 306 42.231 56.039 36.744 1.00 21.18 N ANISOU 2275 NH1 ARG A 306 2578 2787 2684 -476 -8 -12 N ATOM 2276 NH2 ARG A 306 41.596 54.351 38.135 1.00 22.48 N ANISOU 2276 NH2 ARG A 306 2848 2911 2780 -519 63 19 N ATOM 2277 N ILE A 307 42.541 49.198 34.174 1.00 22.71 N ANISOU 2277 N ILE A 307 2867 2793 2970 -394 16 96 N ATOM 2278 CA ILE A 307 41.561 48.119 34.151 1.00 22.86 C ANISOU 2278 CA ILE A 307 2945 2745 2994 -449 77 84 C ATOM 2279 C ILE A 307 41.173 47.774 35.576 1.00 23.83 C ANISOU 2279 C ILE A 307 3175 2830 3051 -505 119 114 C ATOM 2280 O ILE A 307 42.030 47.475 36.412 1.00 23.37 O ANISOU 2280 O ILE A 307 3199 2746 2933 -466 79 169 O ATOM 2281 CB ILE A 307 42.096 46.864 33.463 1.00 23.21 C ANISOU 2281 CB ILE A 307 3041 2725 3052 -402 57 101 C ATOM 2282 CG1 ILE A 307 42.479 47.152 32.006 1.00 22.83 C ANISOU 2282 CG1 ILE A 307 2894 2719 3059 -351 25 67 C ATOM 2283 CG2 ILE A 307 41.042 45.756 33.523 1.00 23.66 C ANISOU 2283 CG2 ILE A 307 3180 2701 3108 -483 123 87 C ATOM 2284 CD1 ILE A 307 43.380 46.075 31.403 1.00 23.77 C ANISOU 2284 CD1 ILE A 307 3059 2789 3182 -272 -6 83 C ATOM 2285 N ARG A 308 39.873 47.798 35.838 1.00 24.12 N ANISOU 2285 N ARG A 308 3205 2869 3091 -597 198 75 N ATOM 2286 CA ARG A 308 39.370 47.514 37.162 1.00 25.42 C ANISOU 2286 CA ARG A 308 3468 3006 3186 -669 256 96 C ATOM 2287 C ARG A 308 37.890 47.206 37.138 1.00 25.98 C ANISOU 2287 C ARG A 308 3516 3080 3275 -780 355 44 C ATOM 2288 O ARG A 308 37.136 47.736 36.325 1.00 25.43 O ANISOU 2288 O ARG A 308 3322 3069 3271 -794 373 -19 O ATOM 2289 CB ARG A 308 39.619 48.691 38.098 1.00 25.27 C ANISOU 2289 CB ARG A 308 3434 3045 3121 -657 245 98 C ATOM 2290 CG ARG A 308 38.962 49.979 37.660 1.00 24.84 C ANISOU 2290 CG ARG A 308 3250 3069 3118 -660 263 30 C ATOM 2291 CD ARG A 308 39.720 51.220 38.086 1.00 24.13 C ANISOU 2291 CD ARG A 308 3141 3023 3003 -611 210 35 C ATOM 2292 NE ARG A 308 38.876 52.400 37.979 1.00 24.62 N ANISOU 2292 NE ARG A 308 3120 3138 3097 -622 246 -31 N ATOM 2293 CZ ARG A 308 38.625 53.062 36.854 1.00 23.93 C ANISOU 2293 CZ ARG A 308 2930 3081 3082 -586 224 -70 C ATOM 2294 NH1 ARG A 308 39.176 52.707 35.696 1.00 23.70 N ANISOU 2294 NH1 ARG A 308 2862 3043 3098 -546 171 -53 N ATOM 2295 NH2 ARG A 308 37.823 54.109 36.897 1.00 23.68 N ANISOU 2295 NH2 ARG A 308 2840 3087 3071 -582 255 -127 N ATOM 2296 N LYS A 309 37.503 46.350 38.068 1.00 27.16 N ANISOU 2296 N LYS A 309 3790 3170 3360 -861 417 74 N ATOM 2297 CA LYS A 309 36.121 45.961 38.291 1.00 28.15 C ANISOU 2297 CA LYS A 309 3907 3304 3485 -992 525 29 C ATOM 2298 C LYS A 309 35.282 47.169 38.693 1.00 27.50 C ANISOU 2298 C LYS A 309 3708 3330 3412 -1018 579 -34 C ATOM 2299 O LYS A 309 35.764 48.078 39.371 1.00 26.67 O ANISOU 2299 O LYS A 309 3607 3258 3268 -966 554 -22 O ATOM 2300 CB LYS A 309 36.100 44.914 39.406 1.00 29.77 C ANISOU 2300 CB LYS A 309 4300 3417 3595 -1072 577 90 C ATOM 2301 CG LYS A 309 34.811 44.146 39.560 1.00 33.43 C ANISOU 2301 CG LYS A 309 4788 3864 4050 -1231 693 56 C ATOM 2302 CD LYS A 309 35.039 42.768 40.189 1.00 35.94 C ANISOU 2302 CD LYS A 309 5328 4042 4286 -1297 718 131 C ATOM 2303 CE LYS A 309 35.249 42.834 41.692 1.00 37.89 C ANISOU 2303 CE LYS A 309 5714 4269 4412 -1325 750 192 C ATOM 2304 NZ LYS A 309 34.603 41.667 42.385 1.00 39.47 N ANISOU 2304 NZ LYS A 309 6091 4374 4532 -1480 848 227 N ATOM 2305 N ASP A 310 34.025 47.180 38.265 1.00 27.35 N ANISOU 2305 N ASP A 310 3582 3368 3442 -1096 651 -107 N ATOM 2306 CA ASP A 310 33.073 48.168 38.749 1.00 27.47 C ANISOU 2306 CA ASP A 310 3491 3486 3463 -1123 720 -175 C ATOM 2307 C ASP A 310 32.875 47.951 40.252 1.00 28.39 C ANISOU 2307 C ASP A 310 3725 3587 3474 -1205 806 -149 C ATOM 2308 O ASP A 310 33.005 46.834 40.755 1.00 28.71 O ANISOU 2308 O ASP A 310 3912 3545 3453 -1283 839 -94 O ATOM 2309 CB ASP A 310 31.740 48.045 38.005 1.00 27.81 C ANISOU 2309 CB ASP A 310 3388 3602 3577 -1194 778 -260 C ATOM 2310 CG ASP A 310 30.762 49.151 38.368 1.00 27.90 C ANISOU 2310 CG ASP A 310 3262 3731 3606 -1188 839 -341 C ATOM 2311 OD1 ASP A 310 30.803 50.222 37.739 1.00 25.31 O ANISOU 2311 OD1 ASP A 310 2826 3456 3336 -1080 778 -377 O ATOM 2312 OD2 ASP A 310 29.912 49.044 39.271 1.00 27.10 O ANISOU 2312 OD2 ASP A 310 3157 3677 3464 -1284 951 -375 O ATOM 2313 N LEU A 311 32.557 49.021 40.963 1.00 28.56 N ANISOU 2313 N LEU A 311 3698 3682 3471 -1185 844 -189 N ATOM 2314 CA LEU A 311 32.379 48.944 42.411 1.00 29.80 C ANISOU 2314 CA LEU A 311 3968 3837 3517 -1259 930 -171 C ATOM 2315 C LEU A 311 31.089 48.237 42.843 1.00 31.03 C ANISOU 2315 C LEU A 311 4114 4028 3649 -1416 1074 -213 C ATOM 2316 O LEU A 311 30.943 47.924 44.024 1.00 32.42 O ANISOU 2316 O LEU A 311 4412 4188 3719 -1501 1155 -187 O ATOM 2317 CB LEU A 311 32.444 50.347 43.031 1.00 29.70 C ANISOU 2317 CB LEU A 311 3912 3890 3481 -1188 930 -212 C ATOM 2318 CG LEU A 311 33.807 51.050 42.974 1.00 29.73 C ANISOU 2318 CG LEU A 311 3963 3858 3474 -1068 801 -164 C ATOM 2319 CD1 LEU A 311 33.703 52.460 43.534 1.00 31.11 C ANISOU 2319 CD1 LEU A 311 4098 4092 3629 -1015 813 -220 C ATOM 2320 CD2 LEU A 311 34.863 50.256 43.734 1.00 30.77 C ANISOU 2320 CD2 LEU A 311 4278 3906 3507 -1080 755 -64 C ATOM 2321 N ASP A 312 30.174 47.961 41.907 1.00 30.92 N ANISOU 2321 N ASP A 312 3961 4064 3725 -1463 1105 -277 N ATOM 2322 CA ASP A 312 28.846 47.421 42.244 1.00 32.46 C ANISOU 2322 CA ASP A 312 4103 4322 3907 -1623 1248 -336 C ATOM 2323 C ASP A 312 28.329 46.335 41.288 1.00 32.60 C ANISOU 2323 C ASP A 312 4085 4315 3985 -1722 1255 -351 C ATOM 2324 O ASP A 312 27.875 45.272 41.730 1.00 33.59 O ANISOU 2324 O ASP A 312 4308 4398 4056 -1883 1346 -333 O ATOM 2325 CB ASP A 312 27.829 48.562 42.303 1.00 32.94 C ANISOU 2325 CB ASP A 312 3966 4536 4016 -1593 1311 -448 C ATOM 2326 CG ASP A 312 28.178 49.594 43.354 1.00 33.14 C ANISOU 2326 CG ASP A 312 4039 4582 3970 -1520 1327 -449 C ATOM 2327 OD1 ASP A 312 27.807 49.383 44.520 1.00 34.61 O ANISOU 2327 OD1 ASP A 312 4306 4785 4058 -1619 1442 -450 O ATOM 2328 OD2 ASP A 312 28.837 50.635 43.112 1.00 32.63 O ANISOU 2328 OD2 ASP A 312 3948 4515 3934 -1373 1233 -449 O ATOM 2329 N ALA A 313 28.368 46.616 39.990 1.00 31.38 N ANISOU 2329 N ALA A 313 3800 4187 3935 -1636 1164 -386 N ATOM 2330 CA ALA A 313 27.949 45.656 38.967 1.00 31.60 C ANISOU 2330 CA ALA A 313 3794 4194 4021 -1718 1154 -407 C ATOM 2331 C ALA A 313 28.975 44.530 38.859 1.00 31.36 C ANISOU 2331 C ALA A 313 3973 3993 3947 -1727 1098 -310 C ATOM 2332 O ALA A 313 30.118 44.771 38.483 1.00 29.61 O ANISOU 2332 O ALA A 313 3805 3709 3735 -1587 986 -255 O ATOM 2333 CB ALA A 313 27.798 46.356 37.634 1.00 30.49 C ANISOU 2333 CB ALA A 313 3470 4127 3987 -1607 1061 -466 C ATOM 2334 N GLU A 314 28.567 43.301 39.167 1.00 32.89 N ANISOU 2334 N GLU A 314 4287 4115 4095 -1891 1176 -291 N ATOM 2335 CA GLU A 314 29.525 42.190 39.248 1.00 33.37 C ANISOU 2335 CA GLU A 314 4581 3998 4102 -1892 1131 -194 C ATOM 2336 C GLU A 314 30.269 41.900 37.941 1.00 32.08 C ANISOU 2336 C GLU A 314 4412 3769 4009 -1783 1009 -184 C ATOM 2337 O GLU A 314 31.401 41.415 37.979 1.00 31.62 O ANISOU 2337 O GLU A 314 4513 3585 3917 -1696 937 -103 O ATOM 2338 CB GLU A 314 28.877 40.909 39.793 1.00 35.65 C ANISOU 2338 CB GLU A 314 5018 4203 4323 -2100 1243 -177 C ATOM 2339 CG GLU A 314 27.715 40.362 38.990 1.00 38.16 C ANISOU 2339 CG GLU A 314 5221 4575 4705 -2257 1302 -266 C ATOM 2340 CD GLU A 314 27.406 38.916 39.326 1.00 42.63 C ANISOU 2340 CD GLU A 314 5989 5004 5204 -2453 1384 -230 C ATOM 2341 OE1 GLU A 314 27.690 38.483 40.467 1.00 45.74 O ANISOU 2341 OE1 GLU A 314 6585 5305 5488 -2509 1440 -150 O ATOM 2342 OE2 GLU A 314 26.873 38.209 38.447 1.00 44.61 O ANISOU 2342 OE2 GLU A 314 6208 5236 5505 -2558 1389 -282 O ATOM 2343 N LYS A 315 29.647 42.213 36.803 1.00 31.23 N ANISOU 2343 N LYS A 315 4119 3752 3993 -1781 985 -268 N ATOM 2344 CA LYS A 315 30.246 41.972 35.484 1.00 30.38 C ANISOU 2344 CA LYS A 315 3997 3597 3947 -1689 880 -272 C ATOM 2345 C LYS A 315 30.710 43.258 34.795 1.00 28.78 C ANISOU 2345 C LYS A 315 3641 3488 3804 -1517 785 -292 C ATOM 2346 O LYS A 315 31.057 43.242 33.621 1.00 27.87 O ANISOU 2346 O LYS A 315 3481 3367 3742 -1446 705 -309 O ATOM 2347 CB LYS A 315 29.259 41.225 34.574 1.00 31.20 C ANISOU 2347 CB LYS A 315 4035 3720 4100 -1825 910 -348 C ATOM 2348 CG LYS A 315 28.986 39.801 35.020 1.00 32.45 C ANISOU 2348 CG LYS A 315 4382 3748 4200 -1998 988 -322 C ATOM 2349 CD LYS A 315 27.677 39.281 34.465 1.00 33.73 C ANISOU 2349 CD LYS A 315 4441 3975 4400 -2185 1053 -417 C ATOM 2350 CE LYS A 315 27.394 37.885 34.982 1.00 34.69 C ANISOU 2350 CE LYS A 315 4770 3954 4455 -2379 1140 -388 C ATOM 2351 NZ LYS A 315 26.431 37.173 34.119 1.00 35.89 N ANISOU 2351 NZ LYS A 315 4857 4130 4649 -2549 1169 -477 N ATOM 2352 N GLY A 316 30.709 44.361 35.532 1.00 28.58 N ANISOU 2352 N GLY A 316 3552 3542 3764 -1458 798 -292 N ATOM 2353 CA GLY A 316 31.190 45.637 35.040 1.00 27.38 C ANISOU 2353 CA GLY A 316 3287 3460 3656 -1304 714 -303 C ATOM 2354 C GLY A 316 32.703 45.761 35.137 1.00 26.41 C ANISOU 2354 C GLY A 316 3277 3255 3502 -1178 628 -220 C ATOM 2355 O GLY A 316 33.300 45.339 36.124 1.00 26.64 O ANISOU 2355 O GLY A 316 3453 3210 3460 -1187 644 -154 O ATOM 2356 N ILE A 317 33.311 46.326 34.095 1.00 25.53 N ANISOU 2356 N ILE A 317 3096 3165 3442 -1064 536 -225 N ATOM 2357 CA ILE A 317 34.739 46.630 34.042 1.00 24.64 C ANISOU 2357 CA ILE A 317 3044 3007 3310 -942 452 -161 C ATOM 2358 C ILE A 317 34.926 48.019 33.427 1.00 23.79 C ANISOU 2358 C ILE A 317 2810 2983 3246 -845 393 -188 C ATOM 2359 O ILE A 317 34.242 48.376 32.468 1.00 23.43 O ANISOU 2359 O ILE A 317 2649 2997 3256 -842 380 -245 O ATOM 2360 CB ILE A 317 35.500 45.571 33.204 1.00 24.75 C ANISOU 2360 CB ILE A 317 3138 2932 3333 -912 403 -132 C ATOM 2361 CG1 ILE A 317 35.279 44.169 33.786 1.00 26.21 C ANISOU 2361 CG1 ILE A 317 3475 3011 3474 -1008 460 -104 C ATOM 2362 CG2 ILE A 317 37.006 45.905 33.155 1.00 23.82 C ANISOU 2362 CG2 ILE A 317 3060 2792 3200 -781 320 -73 C ATOM 2363 CD1 ILE A 317 35.685 43.038 32.869 1.00 27.50 C ANISOU 2363 CD1 ILE A 317 3716 3080 3653 -997 429 -100 C ATOM 2364 N HIS A 318 35.822 48.805 34.010 1.00 23.28 N ANISOU 2364 N HIS A 318 2774 2921 3149 -772 355 -147 N ATOM 2365 CA HIS A 318 36.256 50.083 33.453 1.00 22.82 C ANISOU 2365 CA HIS A 318 2634 2915 3120 -683 292 -158 C ATOM 2366 C HIS A 318 37.691 49.963 32.965 1.00 22.33 C ANISOU 2366 C HIS A 318 2615 2818 3051 -607 214 -105 C ATOM 2367 O HIS A 318 38.460 49.201 33.513 1.00 22.12 O ANISOU 2367 O HIS A 318 2686 2736 2983 -601 205 -54 O ATOM 2368 CB HIS A 318 36.218 51.180 34.512 1.00 22.68 C ANISOU 2368 CB HIS A 318 2617 2932 3069 -670 310 -161 C ATOM 2369 CG HIS A 318 34.862 51.430 35.076 1.00 24.45 C ANISOU 2369 CG HIS A 318 2787 3206 3297 -730 394 -221 C ATOM 2370 ND1 HIS A 318 34.209 50.513 35.872 1.00 27.10 N ANISOU 2370 ND1 HIS A 318 3174 3526 3596 -829 479 -223 N ATOM 2371 CD2 HIS A 318 34.044 52.501 34.985 1.00 25.11 C ANISOU 2371 CD2 HIS A 318 2771 3358 3412 -702 411 -282 C ATOM 2372 CE1 HIS A 318 33.044 51.010 36.241 1.00 26.57 C ANISOU 2372 CE1 HIS A 318 3024 3529 3540 -866 551 -289 C ATOM 2373 NE2 HIS A 318 32.917 52.213 35.715 1.00 26.82 N ANISOU 2373 NE2 HIS A 318 2961 3613 3617 -780 508 -327 N ATOM 2374 N MET A 319 38.041 50.739 31.943 1.00 22.29 N ANISOU 2374 N MET A 319 2536 2850 3081 -547 159 -118 N ATOM 2375 CA MET A 319 39.406 50.786 31.439 1.00 22.02 C ANISOU 2375 CA MET A 319 2519 2806 3040 -480 94 -77 C ATOM 2376 C MET A 319 39.672 52.097 30.694 1.00 20.96 C ANISOU 2376 C MET A 319 2312 2723 2927 -436 49 -90 C ATOM 2377 O MET A 319 38.774 52.890 30.468 1.00 21.23 O ANISOU 2377 O MET A 319 2291 2789 2985 -442 59 -130 O ATOM 2378 CB MET A 319 39.694 49.573 30.540 1.00 22.24 C ANISOU 2378 CB MET A 319 2572 2793 3084 -470 84 -74 C ATOM 2379 CG MET A 319 38.825 49.484 29.301 1.00 23.83 C ANISOU 2379 CG MET A 319 2705 3018 3331 -491 88 -128 C ATOM 2380 SD MET A 319 39.181 48.042 28.252 1.00 27.40 S ANISOU 2380 SD MET A 319 3205 3413 3792 -484 79 -135 S ATOM 2381 CE MET A 319 38.196 46.792 29.063 1.00 28.34 C ANISOU 2381 CE MET A 319 3407 3462 3901 -584 149 -146 C ATOM 2382 N TRP A 320 40.920 52.285 30.298 1.00 20.61 N ANISOU 2382 N TRP A 320 2272 2686 2872 -390 -1 -57 N ATOM 2383 CA TRP A 320 41.388 53.496 29.645 1.00 19.75 C ANISOU 2383 CA TRP A 320 2118 2616 2770 -363 -42 -58 C ATOM 2384 C TRP A 320 42.133 53.035 28.407 1.00 19.70 C ANISOU 2384 C TRP A 320 2090 2621 2775 -331 -70 -50 C ATOM 2385 O TRP A 320 43.086 52.255 28.507 1.00 19.81 O ANISOU 2385 O TRP A 320 2127 2626 2773 -306 -81 -24 O ATOM 2386 CB TRP A 320 42.303 54.265 30.596 1.00 19.72 C ANISOU 2386 CB TRP A 320 2142 2624 2728 -360 -66 -27 C ATOM 2387 CG TRP A 320 42.839 55.587 30.101 1.00 18.76 C ANISOU 2387 CG TRP A 320 1995 2530 2603 -354 -103 -25 C ATOM 2388 CD1 TRP A 320 44.136 55.876 29.791 1.00 19.25 C ANISOU 2388 CD1 TRP A 320 2043 2622 2646 -348 -141 3 C ATOM 2389 CD2 TRP A 320 42.105 56.802 29.892 1.00 19.16 C ANISOU 2389 CD2 TRP A 320 2036 2578 2665 -357 -103 -52 C ATOM 2390 NE1 TRP A 320 44.256 57.186 29.391 1.00 18.63 N ANISOU 2390 NE1 TRP A 320 1960 2554 2565 -364 -161 -2 N ATOM 2391 CE2 TRP A 320 43.027 57.783 29.451 1.00 19.12 C ANISOU 2391 CE2 TRP A 320 2035 2587 2644 -362 -142 -33 C ATOM 2392 CE3 TRP A 320 40.761 57.165 30.024 1.00 18.76 C ANISOU 2392 CE3 TRP A 320 1975 2517 2637 -352 -74 -93 C ATOM 2393 CZ2 TRP A 320 42.648 59.097 29.144 1.00 19.14 C ANISOU 2393 CZ2 TRP A 320 2053 2571 2647 -361 -156 -47 C ATOM 2394 CZ3 TRP A 320 40.384 58.480 29.718 1.00 19.52 C ANISOU 2394 CZ3 TRP A 320 2072 2605 2740 -332 -93 -111 C ATOM 2395 CH2 TRP A 320 41.327 59.425 29.278 1.00 18.61 C ANISOU 2395 CH2 TRP A 320 1984 2483 2604 -336 -135 -85 C ATOM 2396 N VAL A 321 41.681 53.496 27.241 1.00 19.56 N ANISOU 2396 N VAL A 321 2029 2624 2778 -326 -83 -76 N ATOM 2397 CA VAL A 321 42.194 53.037 25.955 1.00 19.68 C ANISOU 2397 CA VAL A 321 2027 2654 2796 -303 -99 -79 C ATOM 2398 C VAL A 321 42.703 54.221 25.136 1.00 19.42 C ANISOU 2398 C VAL A 321 1969 2659 2750 -294 -131 -69 C ATOM 2399 O VAL A 321 41.983 55.194 24.936 1.00 19.10 O ANISOU 2399 O VAL A 321 1920 2621 2715 -300 -144 -80 O ATOM 2400 CB VAL A 321 41.096 52.317 25.148 1.00 19.98 C ANISOU 2400 CB VAL A 321 2051 2680 2858 -319 -86 -122 C ATOM 2401 CG1 VAL A 321 41.655 51.766 23.832 1.00 20.02 C ANISOU 2401 CG1 VAL A 321 2053 2697 2856 -296 -99 -132 C ATOM 2402 CG2 VAL A 321 40.473 51.202 25.971 1.00 20.51 C ANISOU 2402 CG2 VAL A 321 2155 2704 2936 -352 -46 -134 C ATOM 2403 N VAL A 322 43.939 54.115 24.654 1.00 19.44 N ANISOU 2403 N VAL A 322 1963 2690 2733 -279 -142 -48 N ATOM 2404 CA VAL A 322 44.594 55.173 23.888 1.00 19.52 C ANISOU 2404 CA VAL A 322 1959 2739 2720 -289 -162 -33 C ATOM 2405 C VAL A 322 45.256 54.608 22.631 1.00 19.43 C ANISOU 2405 C VAL A 322 1927 2762 2693 -272 -156 -40 C ATOM 2406 O VAL A 322 45.894 53.563 22.688 1.00 19.59 O ANISOU 2406 O VAL A 322 1938 2790 2716 -241 -141 -45 O ATOM 2407 CB VAL A 322 45.694 55.873 24.749 1.00 19.49 C ANISOU 2407 CB VAL A 322 1952 2759 2693 -310 -174 -1 C ATOM 2408 CG1 VAL A 322 46.422 56.946 23.950 1.00 20.02 C ANISOU 2408 CG1 VAL A 322 2012 2864 2732 -344 -186 15 C ATOM 2409 CG2 VAL A 322 45.089 56.493 25.990 1.00 19.96 C ANISOU 2409 CG2 VAL A 322 2044 2784 2757 -328 -177 1 C ATOM 2410 N SER A 323 45.122 55.318 21.510 1.00 19.64 N ANISOU 2410 N SER A 323 1957 2808 2698 -287 -167 -42 N ATOM 2411 CA SER A 323 45.899 55.036 20.295 1.00 19.64 C ANISOU 2411 CA SER A 323 1942 2854 2666 -283 -154 -47 C ATOM 2412 C SER A 323 46.036 56.272 19.390 1.00 19.75 C ANISOU 2412 C SER A 323 1978 2889 2637 -321 -168 -26 C ATOM 2413 O SER A 323 45.228 57.191 19.440 1.00 19.04 O ANISOU 2413 O SER A 323 1923 2764 2547 -333 -197 -16 O ATOM 2414 CB SER A 323 45.267 53.888 19.502 1.00 20.26 C ANISOU 2414 CB SER A 323 2029 2917 2752 -255 -144 -88 C ATOM 2415 OG SER A 323 46.182 53.332 18.566 1.00 20.41 O ANISOU 2415 OG SER A 323 2035 2980 2741 -238 -119 -101 O ATOM 2416 N ASP A 324 47.080 56.280 18.565 1.00 20.17 N ANISOU 2416 N ASP A 324 2014 3000 2650 -338 -144 -21 N ATOM 2417 CA ASP A 324 47.306 57.354 17.606 1.00 20.55 C ANISOU 2417 CA ASP A 324 2098 3067 2642 -387 -148 3 C ATOM 2418 C ASP A 324 46.198 57.269 16.559 1.00 20.40 C ANISOU 2418 C ASP A 324 2124 3022 2604 -367 -173 -13 C ATOM 2419 O ASP A 324 46.102 56.284 15.840 1.00 20.39 O ANISOU 2419 O ASP A 324 2111 3041 2594 -340 -158 -48 O ATOM 2420 CB ASP A 324 48.702 57.194 16.973 1.00 21.42 C ANISOU 2420 CB ASP A 324 2166 3262 2711 -416 -101 4 C ATOM 2421 CG ASP A 324 49.101 58.369 16.088 1.00 23.02 C ANISOU 2421 CG ASP A 324 2415 3487 2845 -492 -93 37 C ATOM 2422 OD1 ASP A 324 48.241 58.911 15.360 1.00 22.97 O ANISOU 2422 OD1 ASP A 324 2486 3435 2807 -497 -122 50 O ATOM 2423 OD2 ASP A 324 50.264 58.803 16.033 1.00 22.60 O ANISOU 2423 OD2 ASP A 324 2329 3498 2761 -554 -58 51 O ATOM 2424 N ASN A 325 45.347 58.293 16.506 1.00 20.25 N ANISOU 2424 N ASN A 325 2159 2956 2577 -373 -217 8 N ATOM 2425 CA ASN A 325 44.203 58.325 15.584 1.00 20.55 C ANISOU 2425 CA ASN A 325 2234 2978 2597 -344 -259 -7 C ATOM 2426 C ASN A 325 44.557 58.413 14.096 1.00 21.40 C ANISOU 2426 C ASN A 325 2385 3121 2624 -366 -256 1 C ATOM 2427 O ASN A 325 43.714 58.128 13.250 1.00 21.71 O ANISOU 2427 O ASN A 325 2445 3163 2641 -340 -291 -21 O ATOM 2428 CB ASN A 325 43.248 59.479 15.932 1.00 20.67 C ANISOU 2428 CB ASN A 325 2295 2935 2623 -325 -313 14 C ATOM 2429 CG ASN A 325 43.930 60.837 15.914 1.00 20.91 C ANISOU 2429 CG ASN A 325 2398 2938 2608 -371 -316 67 C ATOM 2430 OD1 ASN A 325 44.795 61.102 16.735 1.00 20.83 O ANISOU 2430 OD1 ASN A 325 2375 2930 2610 -414 -284 82 O ATOM 2431 ND2 ASN A 325 43.540 61.701 14.985 1.00 20.13 N ANISOU 2431 ND2 ASN A 325 2384 2811 2454 -367 -358 96 N ATOM 2432 N LEU A 326 45.773 58.843 13.777 1.00 24.78 N ANISOU 2432 N LEU A 326 3080 3238 3096 -278 163 -503 N ATOM 2433 CA LEU A 326 46.222 58.879 12.384 1.00 24.82 C ANISOU 2433 CA LEU A 326 3059 3214 3155 -311 149 -449 C ATOM 2434 C LEU A 326 46.816 57.551 11.915 1.00 23.42 C ANISOU 2434 C LEU A 326 2741 3171 2985 -308 101 -387 C ATOM 2435 O LEU A 326 46.915 57.323 10.710 1.00 23.21 O ANISOU 2435 O LEU A 326 2687 3130 3003 -295 96 -331 O ATOM 2436 CB LEU A 326 47.244 59.993 12.166 1.00 26.08 C ANISOU 2436 CB LEU A 326 3299 3310 3300 -457 156 -501 C ATOM 2437 CG LEU A 326 46.812 61.437 12.447 1.00 29.35 C ANISOU 2437 CG LEU A 326 3889 3552 3712 -477 218 -565 C ATOM 2438 CD1 LEU A 326 47.919 62.396 11.997 1.00 31.81 C ANISOU 2438 CD1 LEU A 326 4268 3793 4024 -645 231 -602 C ATOM 2439 CD2 LEU A 326 45.521 61.780 11.753 1.00 29.87 C ANISOU 2439 CD2 LEU A 326 4020 3494 3834 -327 268 -506 C ATOM 2440 N LEU A 327 47.215 56.692 12.856 1.00 22.92 N ANISOU 2440 N LEU A 327 2602 3235 2873 -308 72 -395 N ATOM 2441 CA LEU A 327 47.857 55.413 12.532 1.00 21.77 C ANISOU 2441 CA LEU A 327 2335 3209 2726 -292 38 -335 C ATOM 2442 C LEU A 327 46.860 54.261 12.668 1.00 20.85 C ANISOU 2442 C LEU A 327 2175 3108 2638 -174 54 -283 C ATOM 2443 O LEU A 327 46.134 53.961 11.706 1.00 19.89 O ANISOU 2443 O LEU A 327 2047 2930 2582 -120 65 -243 O ATOM 2444 CB LEU A 327 49.126 55.213 13.377 1.00 22.39 C ANISOU 2444 CB LEU A 327 2351 3428 2727 -369 -5 -364 C ATOM 2445 CG LEU A 327 50.280 56.182 13.087 1.00 24.10 C ANISOU 2445 CG LEU A 327 2575 3656 2928 -515 -25 -412 C ATOM 2446 CD1 LEU A 327 51.518 55.855 13.936 1.00 25.45 C ANISOU 2446 CD1 LEU A 327 2646 4005 3017 -585 -83 -437 C ATOM 2447 CD2 LEU A 327 50.670 56.202 11.607 1.00 24.49 C ANISOU 2447 CD2 LEU A 327 2598 3665 3039 -537 -10 -358 C ATOM 2448 N LYS A 328 46.777 53.607 13.827 1.00 20.73 N ANISOU 2448 N LYS A 328 2133 3169 2573 -137 56 -282 N ATOM 2449 CA LYS A 328 45.763 52.551 13.982 1.00 20.22 C ANISOU 2449 CA LYS A 328 2037 3101 2546 -40 89 -231 C ATOM 2450 C LYS A 328 44.350 53.080 13.718 1.00 20.23 C ANISOU 2450 C LYS A 328 2081 2997 2607 11 129 -239 C ATOM 2451 O LYS A 328 43.498 52.355 13.215 1.00 19.92 O ANISOU 2451 O LYS A 328 2000 2938 2632 64 146 -197 O ATOM 2452 CB LYS A 328 45.820 51.891 15.366 1.00 21.01 C ANISOU 2452 CB LYS A 328 2122 3288 2573 -2 103 -221 C ATOM 2453 CG LYS A 328 44.866 50.682 15.535 1.00 19.66 C ANISOU 2453 CG LYS A 328 1918 3107 2445 83 153 -157 C ATOM 2454 CD LYS A 328 44.938 49.692 14.354 1.00 19.48 C ANISOU 2454 CD LYS A 328 1841 3064 2496 95 145 -104 C ATOM 2455 CE LYS A 328 44.325 48.326 14.701 1.00 19.83 C ANISOU 2455 CE LYS A 328 1858 3107 2568 155 197 -44 C ATOM 2456 NZ LYS A 328 44.363 47.378 13.570 1.00 18.15 N ANISOU 2456 NZ LYS A 328 1616 2859 2423 158 194 -10 N ATOM 2457 N GLY A 329 44.111 54.349 14.038 1.00 20.84 N ANISOU 2457 N GLY A 329 2243 3009 2666 -6 147 -295 N ATOM 2458 CA GLY A 329 42.810 54.961 13.838 1.00 21.25 C ANISOU 2458 CA GLY A 329 2336 2970 2769 63 190 -298 C ATOM 2459 C GLY A 329 42.452 55.234 12.385 1.00 20.85 C ANISOU 2459 C GLY A 329 2279 2854 2788 81 173 -265 C ATOM 2460 O GLY A 329 41.308 55.555 12.077 1.00 20.96 O ANISOU 2460 O GLY A 329 2298 2818 2850 159 198 -251 O ATOM 2461 N ALA A 330 43.434 55.130 11.498 1.00 20.43 N ANISOU 2461 N ALA A 330 2214 2814 2734 18 132 -251 N ATOM 2462 CA ALA A 330 43.230 55.411 10.087 1.00 20.27 C ANISOU 2462 CA ALA A 330 2202 2741 2758 34 115 -218 C ATOM 2463 C ALA A 330 44.253 54.698 9.198 1.00 19.48 C ANISOU 2463 C ALA A 330 2054 2695 2654 -18 77 -189 C ATOM 2464 O ALA A 330 44.035 53.553 8.815 1.00 19.05 O ANISOU 2464 O ALA A 330 1929 2688 2621 12 61 -158 O ATOM 2465 CB ALA A 330 43.252 56.930 9.848 1.00 21.39 C ANISOU 2465 CB ALA A 330 2461 2773 2892 20 140 -243 C ATOM 2466 N ALA A 331 45.370 55.362 8.899 1.00 19.27 N ANISOU 2466 N ALA A 331 2065 2658 2597 -100 73 -202 N ATOM 2467 CA ALA A 331 46.292 54.920 7.854 1.00 19.09 C ANISOU 2467 CA ALA A 331 2006 2676 2572 -138 55 -168 C ATOM 2468 C ALA A 331 46.869 53.526 8.072 1.00 18.48 C ANISOU 2468 C ALA A 331 1834 2706 2483 -131 37 -148 C ATOM 2469 O ALA A 331 46.958 52.748 7.129 1.00 17.78 O ANISOU 2469 O ALA A 331 1713 2635 2408 -102 29 -114 O ATOM 2470 CB ALA A 331 47.434 55.939 7.673 1.00 19.83 C ANISOU 2470 CB ALA A 331 2146 2748 2640 -245 68 -186 C ATOM 2471 N TRP A 332 47.299 53.222 9.294 1.00 18.80 N ANISOU 2471 N TRP A 332 1840 2815 2488 -149 34 -168 N ATOM 2472 CA TRP A 332 47.776 51.871 9.603 1.00 18.76 C ANISOU 2472 CA TRP A 332 1757 2904 2467 -115 27 -136 C ATOM 2473 C TRP A 332 46.657 50.810 9.544 1.00 17.90 C ANISOU 2473 C TRP A 332 1634 2767 2402 -34 42 -109 C ATOM 2474 O TRP A 332 46.900 49.723 9.068 1.00 17.79 O ANISOU 2474 O TRP A 332 1585 2777 2399 -3 46 -76 O ATOM 2475 CB TRP A 332 48.510 51.804 10.947 1.00 19.38 C ANISOU 2475 CB TRP A 332 1803 3079 2482 -141 16 -154 C ATOM 2476 CG TRP A 332 48.714 50.384 11.447 1.00 20.61 C ANISOU 2476 CG TRP A 332 1898 3314 2619 -69 21 -105 C ATOM 2477 CD1 TRP A 332 48.284 49.873 12.632 1.00 21.39 C ANISOU 2477 CD1 TRP A 332 1997 3444 2686 -20 35 -97 C ATOM 2478 CD2 TRP A 332 49.371 49.305 10.763 1.00 21.19 C ANISOU 2478 CD2 TRP A 332 1918 3432 2702 -29 26 -53 C ATOM 2479 NE1 TRP A 332 48.646 48.552 12.740 1.00 21.73 N ANISOU 2479 NE1 TRP A 332 1995 3541 2720 48 49 -36 N ATOM 2480 CE2 TRP A 332 49.303 48.173 11.603 1.00 22.18 C ANISOU 2480 CE2 TRP A 332 2020 3603 2804 47 45 -11 C ATOM 2481 CE3 TRP A 332 50.011 49.178 9.516 1.00 23.15 C ANISOU 2481 CE3 TRP A 332 2145 3681 2969 -40 28 -34 C ATOM 2482 CZ2 TRP A 332 49.855 46.935 11.249 1.00 23.97 C ANISOU 2482 CZ2 TRP A 332 2212 3863 3033 116 66 46 C ATOM 2483 CZ3 TRP A 332 50.560 47.944 9.160 1.00 22.26 C ANISOU 2483 CZ3 TRP A 332 1992 3611 2854 28 48 16 C ATOM 2484 CH2 TRP A 332 50.478 46.843 10.023 1.00 24.22 C ANISOU 2484 CH2 TRP A 332 2226 3892 3086 107 67 55 C ATOM 2485 N ASN A 333 45.451 51.094 10.024 1.00 17.98 N ANISOU 2485 N ASN A 333 1670 2725 2437 -2 59 -124 N ATOM 2486 CA ASN A 333 44.371 50.111 9.872 1.00 18.03 C ANISOU 2486 CA ASN A 333 1646 2709 2494 52 75 -102 C ATOM 2487 C ASN A 333 44.141 49.783 8.389 1.00 18.02 C ANISOU 2487 C ASN A 333 1640 2676 2532 57 51 -91 C ATOM 2488 O ASN A 333 44.013 48.621 8.039 1.00 18.33 O ANISOU 2488 O ASN A 333 1652 2720 2594 71 56 -75 O ATOM 2489 CB ASN A 333 43.071 50.563 10.548 1.00 18.30 C ANISOU 2489 CB ASN A 333 1691 2707 2556 86 103 -117 C ATOM 2490 CG ASN A 333 42.051 49.430 10.683 1.00 18.96 C ANISOU 2490 CG ASN A 333 1723 2789 2693 120 131 -93 C ATOM 2491 OD1 ASN A 333 41.021 49.415 9.985 1.00 22.35 O ANISOU 2491 OD1 ASN A 333 2124 3189 3179 135 122 -95 O ATOM 2492 ND2 ASN A 333 42.329 48.479 11.571 1.00 14.42 N ANISOU 2492 ND2 ASN A 333 1133 2248 2097 128 166 -67 N ATOM 2493 N SER A 334 44.136 50.805 7.531 1.00 18.10 N ANISOU 2493 N SER A 334 1688 2650 2540 44 30 -100 N ATOM 2494 CA SER A 334 43.963 50.637 6.088 1.00 18.37 C ANISOU 2494 CA SER A 334 1729 2665 2586 55 2 -90 C ATOM 2495 C SER A 334 45.072 49.805 5.415 1.00 18.35 C ANISOU 2495 C SER A 334 1716 2698 2557 38 2 -74 C ATOM 2496 O SER A 334 44.779 48.916 4.617 1.00 18.42 O ANISOU 2496 O SER A 334 1719 2703 2579 56 -9 -74 O ATOM 2497 CB SER A 334 43.847 52.006 5.401 1.00 19.03 C ANISOU 2497 CB SER A 334 1873 2700 2658 56 -10 -88 C ATOM 2498 OG SER A 334 42.580 52.612 5.649 1.00 20.44 O ANISOU 2498 OG SER A 334 2058 2842 2867 107 -11 -94 O ATOM 2499 N VAL A 335 46.333 50.091 5.730 1.00 18.48 N ANISOU 2499 N VAL A 335 1730 2755 2535 2 16 -66 N ATOM 2500 CA VAL A 335 47.447 49.329 5.170 1.00 18.42 C ANISOU 2500 CA VAL A 335 1700 2797 2503 2 28 -44 C ATOM 2501 C VAL A 335 47.412 47.898 5.721 1.00 18.29 C ANISOU 2501 C VAL A 335 1650 2803 2497 46 47 -31 C ATOM 2502 O VAL A 335 47.657 46.945 4.990 1.00 17.72 O ANISOU 2502 O VAL A 335 1583 2727 2424 76 62 -21 O ATOM 2503 CB VAL A 335 48.812 50.024 5.415 1.00 18.99 C ANISOU 2503 CB VAL A 335 1750 2929 2535 -53 38 -36 C ATOM 2504 CG1 VAL A 335 49.970 49.131 5.005 1.00 20.16 C ANISOU 2504 CG1 VAL A 335 1849 3151 2658 -32 60 -5 C ATOM 2505 CG2 VAL A 335 48.885 51.337 4.636 1.00 19.19 C ANISOU 2505 CG2 VAL A 335 1830 2906 2555 -103 39 -40 C ATOM 2506 N GLN A 336 47.053 47.757 6.996 1.00 18.25 N ANISOU 2506 N GLN A 336 1626 2809 2498 55 57 -31 N ATOM 2507 CA GLN A 336 46.912 46.446 7.621 1.00 18.21 C ANISOU 2507 CA GLN A 336 1607 2809 2505 101 89 -7 C ATOM 2508 C GLN A 336 45.813 45.620 6.947 1.00 18.03 C ANISOU 2508 C GLN A 336 1604 2710 2536 111 97 -21 C ATOM 2509 O GLN A 336 45.979 44.421 6.767 1.00 18.13 O ANISOU 2509 O GLN A 336 1629 2700 2558 139 129 -5 O ATOM 2510 CB GLN A 336 46.656 46.562 9.123 1.00 18.40 C ANISOU 2510 CB GLN A 336 1618 2862 2513 110 103 0 C ATOM 2511 CG GLN A 336 46.910 45.261 9.883 1.00 19.21 C ANISOU 2511 CG GLN A 336 1711 2985 2603 168 146 48 C ATOM 2512 CD GLN A 336 46.602 45.364 11.349 1.00 21.21 C ANISOU 2512 CD GLN A 336 1962 3273 2825 185 165 62 C ATOM 2513 OE1 GLN A 336 45.831 46.240 11.771 1.00 25.03 O ANISOU 2513 OE1 GLN A 336 2456 3738 3316 156 157 27 O ATOM 2514 NE2 GLN A 336 47.184 44.470 12.143 1.00 20.84 N ANISOU 2514 NE2 GLN A 336 1908 3275 2735 245 195 116 N ATOM 2515 N ILE A 337 44.718 46.261 6.550 1.00 18.18 N ANISOU 2515 N ILE A 337 1628 2692 2589 88 67 -51 N ATOM 2516 CA ILE A 337 43.673 45.592 5.767 1.00 18.87 C ANISOU 2516 CA ILE A 337 1717 2731 2723 80 55 -76 C ATOM 2517 C ILE A 337 44.217 45.090 4.430 1.00 19.18 C ANISOU 2517 C ILE A 337 1792 2759 2738 81 41 -89 C ATOM 2518 O ILE A 337 43.934 43.962 4.033 1.00 19.00 O ANISOU 2518 O ILE A 337 1787 2696 2736 76 56 -107 O ATOM 2519 CB ILE A 337 42.447 46.526 5.542 1.00 18.92 C ANISOU 2519 CB ILE A 337 1701 2729 2759 71 16 -99 C ATOM 2520 CG1 ILE A 337 41.633 46.633 6.830 1.00 19.57 C ANISOU 2520 CG1 ILE A 337 1747 2813 2877 78 50 -91 C ATOM 2521 CG2 ILE A 337 41.550 46.022 4.374 1.00 19.50 C ANISOU 2521 CG2 ILE A 337 1764 2785 2859 55 -27 -133 C ATOM 2522 CD1 ILE A 337 40.679 47.836 6.876 1.00 20.97 C ANISOU 2522 CD1 ILE A 337 1905 2992 3070 97 28 -102 C ATOM 2523 N ALA A 338 44.993 45.928 3.743 1.00 19.26 N ANISOU 2523 N ALA A 338 1821 2797 2700 83 21 -82 N ATOM 2524 CA ALA A 338 45.635 45.529 2.490 1.00 19.79 C ANISOU 2524 CA ALA A 338 1927 2865 2728 95 20 -89 C ATOM 2525 C ALA A 338 46.577 44.343 2.693 1.00 20.09 C ANISOU 2525 C ALA A 338 1974 2905 2754 129 77 -70 C ATOM 2526 O ALA A 338 46.560 43.401 1.898 1.00 20.40 O ANISOU 2526 O ALA A 338 2058 2906 2786 144 92 -94 O ATOM 2527 CB ALA A 338 46.381 46.699 1.865 1.00 19.86 C ANISOU 2527 CB ALA A 338 1951 2905 2688 88 9 -70 C ATOM 2528 N GLU A 339 47.376 44.380 3.762 1.00 20.03 N ANISOU 2528 N GLU A 339 1928 2944 2738 148 107 -29 N ATOM 2529 CA GLU A 339 48.288 43.284 4.086 1.00 19.91 C ANISOU 2529 CA GLU A 339 1913 2946 2708 207 163 6 C ATOM 2530 C GLU A 339 47.518 42.000 4.381 1.00 19.92 C ANISOU 2530 C GLU A 339 1954 2862 2752 224 199 -2 C ATOM 2531 O GLU A 339 47.963 40.913 4.027 1.00 20.12 O ANISOU 2531 O GLU A 339 2025 2848 2770 274 250 6 O ATOM 2532 CB GLU A 339 49.181 43.637 5.294 1.00 20.27 C ANISOU 2532 CB GLU A 339 1895 3081 2725 226 172 53 C ATOM 2533 CG GLU A 339 50.287 44.650 4.996 1.00 20.65 C ANISOU 2533 CG GLU A 339 1895 3219 2730 200 155 64 C ATOM 2534 CD GLU A 339 51.181 44.943 6.202 1.00 21.41 C ANISOU 2534 CD GLU A 339 1917 3425 2793 204 149 97 C ATOM 2535 OE1 GLU A 339 50.941 44.398 7.304 1.00 23.45 O ANISOU 2535 OE1 GLU A 339 2168 3693 3049 242 157 118 O ATOM 2536 OE2 GLU A 339 52.138 45.724 6.051 1.00 20.75 O ANISOU 2536 OE2 GLU A 339 1779 3425 2679 164 137 101 O ATOM 2537 N THR A 340 46.362 42.132 5.028 1.00 19.49 N ANISOU 2537 N THR A 340 1887 2774 2745 183 184 -18 N ATOM 2538 CA THR A 340 45.564 40.983 5.433 1.00 19.95 C ANISOU 2538 CA THR A 340 1975 2750 2854 177 229 -22 C ATOM 2539 C THR A 340 44.819 40.401 4.239 1.00 20.54 C ANISOU 2539 C THR A 340 2097 2749 2957 130 213 -88 C ATOM 2540 O THR A 340 44.660 39.175 4.146 1.00 21.23 O ANISOU 2540 O THR A 340 2244 2751 3073 129 267 -99 O ATOM 2541 CB THR A 340 44.583 41.368 6.559 1.00 20.00 C ANISOU 2541 CB THR A 340 1939 2761 2900 146 229 -12 C ATOM 2542 OG1 THR A 340 45.309 41.935 7.659 1.00 19.41 O ANISOU 2542 OG1 THR A 340 1832 2763 2779 186 236 36 O ATOM 2543 CG2 THR A 340 43.907 40.128 7.160 1.00 20.50 C ANISOU 2543 CG2 THR A 340 2031 2740 3016 137 299 3 C ATOM 2544 N LEU A 341 44.364 41.266 3.333 1.00 19.78 N ANISOU 2544 N LEU A 341 1984 2683 2849 91 141 -132 N ATOM 2545 CA LEU A 341 43.808 40.813 2.060 1.00 20.52 C ANISOU 2545 CA LEU A 341 2121 2735 2941 51 106 -201 C ATOM 2546 C LEU A 341 44.830 39.947 1.328 1.00 21.22 C ANISOU 2546 C LEU A 341 2294 2787 2983 98 155 -208 C ATOM 2547 O LEU A 341 44.497 38.874 0.841 1.00 21.59 O ANISOU 2547 O LEU A 341 2408 2751 3044 73 180 -259 O ATOM 2548 CB LEU A 341 43.377 41.992 1.182 1.00 20.38 C ANISOU 2548 CB LEU A 341 2076 2776 2890 34 20 -227 C ATOM 2549 CG LEU A 341 42.086 42.722 1.582 1.00 20.12 C ANISOU 2549 CG LEU A 341 1968 2771 2905 -3 -32 -236 C ATOM 2550 CD1 LEU A 341 42.006 44.087 0.910 1.00 20.76 C ANISOU 2550 CD1 LEU A 341 2037 2910 2941 20 -98 -228 C ATOM 2551 CD2 LEU A 341 40.875 41.904 1.243 1.00 22.38 C ANISOU 2551 CD2 LEU A 341 2235 3026 3242 -72 -59 -298 C ATOM 2552 N HIS A 342 46.077 40.405 1.285 1.00 21.24 N ANISOU 2552 N HIS A 342 2291 2849 2931 164 176 -159 N ATOM 2553 CA HIS A 342 47.156 39.648 0.649 1.00 22.02 C ANISOU 2553 CA HIS A 342 2455 2931 2982 231 237 -152 C ATOM 2554 C HIS A 342 47.455 38.334 1.393 1.00 22.80 C ANISOU 2554 C HIS A 342 2598 2954 3111 285 326 -122 C ATOM 2555 O HIS A 342 47.605 37.273 0.774 1.00 23.28 O ANISOU 2555 O HIS A 342 2755 2929 3163 312 380 -156 O ATOM 2556 CB HIS A 342 48.433 40.487 0.545 1.00 21.83 C ANISOU 2556 CB HIS A 342 2384 3010 2902 283 246 -97 C ATOM 2557 CG HIS A 342 49.622 39.682 0.129 1.00 22.42 C ANISOU 2557 CG HIS A 342 2498 3086 2933 375 325 -71 C ATOM 2558 ND1 HIS A 342 50.515 39.161 1.037 1.00 23.88 N ANISOU 2558 ND1 HIS A 342 2648 3303 3121 457 387 -2 N ATOM 2559 CD2 HIS A 342 50.033 39.260 -1.087 1.00 23.42 C ANISOU 2559 CD2 HIS A 342 2700 3191 3007 411 357 -104 C ATOM 2560 CE1 HIS A 342 51.429 38.459 0.396 1.00 24.24 C ANISOU 2560 CE1 HIS A 342 2738 3346 3127 546 458 11 C ATOM 2561 NE2 HIS A 342 51.163 38.506 -0.896 1.00 24.61 N ANISOU 2561 NE2 HIS A 342 2857 3355 3138 518 446 -54 N ATOM 2562 N GLU A 343 47.498 38.417 2.719 1.00 22.86 N ANISOU 2562 N GLU A 343 2550 2988 3149 303 345 -60 N ATOM 2563 CA GLU A 343 47.780 37.283 3.595 1.00 23.81 C ANISOU 2563 CA GLU A 343 2711 3047 3291 370 432 -7 C ATOM 2564 C GLU A 343 46.821 36.122 3.339 1.00 24.47 C ANISOU 2564 C GLU A 343 2893 2976 3431 317 476 -61 C ATOM 2565 O GLU A 343 47.223 34.956 3.361 1.00 25.17 O ANISOU 2565 O GLU A 343 3074 2967 3522 382 566 -42 O ATOM 2566 CB GLU A 343 47.654 37.743 5.052 1.00 23.70 C ANISOU 2566 CB GLU A 343 2621 3095 3290 375 425 57 C ATOM 2567 CG GLU A 343 48.043 36.718 6.102 1.00 26.46 C ANISOU 2567 CG GLU A 343 3006 3407 3641 465 513 137 C ATOM 2568 CD GLU A 343 47.797 37.239 7.510 1.00 29.52 C ANISOU 2568 CD GLU A 343 3328 3865 4025 463 499 190 C ATOM 2569 OE1 GLU A 343 46.658 37.119 8.007 1.00 30.98 O ANISOU 2569 OE1 GLU A 343 3522 3986 4262 396 511 176 O ATOM 2570 OE2 GLU A 343 48.730 37.802 8.112 1.00 32.81 O ANISOU 2570 OE2 GLU A 343 3676 4409 4381 523 476 242 O ATOM 2571 N ARG A 344 45.556 36.462 3.097 1.00 23.77 N ANISOU 2571 N ARG A 344 2780 2867 3387 199 414 -128 N ATOM 2572 CA ARG A 344 44.480 35.490 2.953 1.00 24.93 C ANISOU 2572 CA ARG A 344 2989 2884 3600 110 443 -190 C ATOM 2573 C ARG A 344 44.171 35.163 1.487 1.00 25.07 C ANISOU 2573 C ARG A 344 3077 2853 3596 49 403 -299 C ATOM 2574 O ARG A 344 43.256 34.404 1.208 1.00 26.03 O ANISOU 2574 O ARG A 344 3247 2876 3768 -51 411 -373 O ATOM 2575 CB ARG A 344 43.212 36.020 3.645 1.00 24.51 C ANISOU 2575 CB ARG A 344 2841 2860 3611 14 399 -196 C ATOM 2576 CG ARG A 344 43.357 36.231 5.142 1.00 25.37 C ANISOU 2576 CG ARG A 344 2901 3005 3734 65 447 -100 C ATOM 2577 CD ARG A 344 42.111 36.809 5.797 1.00 27.73 C ANISOU 2577 CD ARG A 344 3107 3338 4090 -17 416 -107 C ATOM 2578 NE ARG A 344 41.046 35.810 5.889 1.00 29.99 N ANISOU 2578 NE ARG A 344 3420 3515 4461 -116 470 -141 N ATOM 2579 CZ ARG A 344 40.785 35.063 6.962 1.00 31.77 C ANISOU 2579 CZ ARG A 344 3672 3667 4730 -117 573 -80 C ATOM 2580 NH1 ARG A 344 41.506 35.174 8.074 1.00 31.49 N ANISOU 2580 NH1 ARG A 344 3645 3669 4652 -10 626 20 N ATOM 2581 NH2 ARG A 344 39.794 34.180 6.913 1.00 32.48 N ANISOU 2581 NH2 ARG A 344 3785 3651 4906 -232 624 -120 N ATOM 2582 N GLY A 345 44.913 35.750 0.554 1.00 24.68 N ANISOU 2582 N GLY A 345 3033 2877 3468 100 362 -313 N ATOM 2583 CA GLY A 345 44.790 35.404 -0.857 1.00 25.16 C ANISOU 2583 CA GLY A 345 3180 2900 3480 67 333 -412 C ATOM 2584 C GLY A 345 43.557 36.011 -1.517 1.00 25.26 C ANISOU 2584 C GLY A 345 3138 2963 3497 -50 214 -494 C ATOM 2585 O GLY A 345 42.970 35.415 -2.419 1.00 25.61 O ANISOU 2585 O GLY A 345 3250 2954 3527 -125 184 -598 O ATOM 2586 N LEU A 346 43.215 37.225 -1.098 1.00 23.90 N ANISOU 2586 N LEU A 346 2845 2900 3334 -55 145 -449 N ATOM 2587 CA LEU A 346 41.942 37.854 -1.413 1.00 24.41 C ANISOU 2587 CA LEU A 346 2828 3025 3420 -143 39 -499 C ATOM 2588 C LEU A 346 42.052 39.077 -2.349 1.00 24.47 C ANISOU 2588 C LEU A 346 2808 3145 3344 -108 -52 -499 C ATOM 2589 O LEU A 346 41.048 39.740 -2.624 1.00 24.50 O ANISOU 2589 O LEU A 346 2738 3216 3353 -151 -144 -524 O ATOM 2590 CB LEU A 346 41.273 38.277 -0.101 1.00 23.80 C ANISOU 2590 CB LEU A 346 2643 2973 3428 -166 47 -442 C ATOM 2591 CG LEU A 346 40.991 37.175 0.924 1.00 23.99 C ANISOU 2591 CG LEU A 346 2687 2893 3536 -205 142 -427 C ATOM 2592 CD1 LEU A 346 40.336 37.774 2.166 1.00 23.99 C ANISOU 2592 CD1 LEU A 346 2576 2940 3599 -215 148 -366 C ATOM 2593 CD2 LEU A 346 40.099 36.072 0.322 1.00 26.00 C ANISOU 2593 CD2 LEU A 346 2988 3056 3833 -326 139 -530 C ATOM 2594 N VAL A 347 43.253 39.386 -2.827 1.00 24.43 N ANISOU 2594 N VAL A 347 2858 3163 3262 -25 -20 -462 N ATOM 2595 CA VAL A 347 43.422 40.465 -3.796 1.00 24.78 C ANISOU 2595 CA VAL A 347 2901 3294 3220 7 -86 -455 C ATOM 2596 C VAL A 347 43.093 39.942 -5.192 1.00 26.56 C ANISOU 2596 C VAL A 347 3212 3514 3366 -19 -135 -549 C ATOM 2597 O VAL A 347 43.914 39.280 -5.838 1.00 27.72 O ANISOU 2597 O VAL A 347 3462 3620 3450 20 -78 -575 O ATOM 2598 CB VAL A 347 44.829 41.078 -3.780 1.00 24.04 C ANISOU 2598 CB VAL A 347 2820 3237 3076 91 -26 -375 C ATOM 2599 CG1 VAL A 347 44.900 42.262 -4.766 1.00 24.46 C ANISOU 2599 CG1 VAL A 347 2881 3368 3047 113 -84 -357 C ATOM 2600 CG2 VAL A 347 45.211 41.541 -2.368 1.00 22.42 C ANISOU 2600 CG2 VAL A 347 2535 3047 2937 107 14 -296 C ATOM 2601 N ARG A 348 41.879 40.247 -5.634 1.00 27.38 N ANISOU 2601 N ARG A 348 3267 3669 3466 -79 -243 -602 N ATOM 2602 CA ARG A 348 41.315 39.703 -6.864 1.00 29.21 C ANISOU 2602 CA ARG A 348 3564 3913 3622 -128 -316 -711 C ATOM 2603 C ARG A 348 40.282 40.680 -7.422 1.00 29.42 C ANISOU 2603 C ARG A 348 3509 4061 3609 -137 -449 -717 C ATOM 2604 O ARG A 348 39.629 41.389 -6.648 1.00 29.01 O ANISOU 2604 O ARG A 348 3339 4052 3631 -140 -479 -664 O ATOM 2605 CB ARG A 348 40.627 38.360 -6.562 1.00 30.61 C ANISOU 2605 CB ARG A 348 3759 3997 3876 -238 -300 -806 C ATOM 2606 CG ARG A 348 39.250 38.519 -5.878 1.00 32.48 C ANISOU 2606 CG ARG A 348 3853 4274 4215 -330 -367 -819 C ATOM 2607 CD ARG A 348 38.791 37.362 -4.993 1.00 34.82 C ANISOU 2607 CD ARG A 348 4143 4457 4631 -432 -297 -856 C ATOM 2608 NE ARG A 348 37.719 37.807 -4.095 1.00 35.57 N ANISOU 2608 NE ARG A 348 4080 4608 4828 -483 -330 -822 N ATOM 2609 CZ ARG A 348 37.220 37.104 -3.079 1.00 37.33 C ANISOU 2609 CZ ARG A 348 4262 4755 5168 -562 -260 -818 C ATOM 2610 NH1 ARG A 348 37.670 35.882 -2.803 1.00 38.86 N ANISOU 2610 NH1 ARG A 348 4571 4798 5396 -600 -153 -844 N ATOM 2611 NH2 ARG A 348 36.248 37.626 -2.332 1.00 37.12 N ANISOU 2611 NH2 ARG A 348 4084 4800 5221 -595 -287 -783 N ATOM 2612 N PRO A 349 40.103 40.723 -8.741 1.00 30.34 N ANISOU 2612 N PRO A 349 3688 4239 3601 -130 -528 -777 N ATOM 2613 CA PRO A 349 38.975 41.475 -9.309 1.00 31.03 C ANISOU 2613 CA PRO A 349 3692 4454 3643 -135 -669 -790 C ATOM 2614 C PRO A 349 37.637 40.865 -8.895 1.00 31.74 C ANISOU 2614 C PRO A 349 3668 4565 3828 -255 -741 -871 C ATOM 2615 O PRO A 349 37.537 39.655 -8.730 1.00 31.94 O ANISOU 2615 O PRO A 349 3732 4501 3902 -356 -704 -960 O ATOM 2616 CB PRO A 349 39.183 41.365 -10.829 1.00 32.07 C ANISOU 2616 CB PRO A 349 3941 4640 3603 -107 -729 -853 C ATOM 2617 CG PRO A 349 40.097 40.212 -11.022 1.00 32.78 C ANISOU 2617 CG PRO A 349 4169 4615 3673 -128 -626 -917 C ATOM 2618 CD PRO A 349 40.928 40.089 -9.784 1.00 30.99 C ANISOU 2618 CD PRO A 349 3924 4286 3566 -103 -490 -834 C ATOM 2619 N THR A 350 36.632 41.712 -8.707 1.00 32.13 N ANISOU 2619 N THR A 350 3577 4724 3905 -240 -831 -833 N ATOM 2620 CA THR A 350 35.277 41.267 -8.406 1.00 33.52 C ANISOU 2620 CA THR A 350 3613 4958 4166 -351 -909 -902 C ATOM 2621 C THR A 350 34.486 41.190 -9.709 1.00 35.77 C ANISOU 2621 C THR A 350 3880 5379 4333 -384 -1067 -996 C ATOM 2622 O THR A 350 34.377 42.186 -10.424 1.00 35.85 O ANISOU 2622 O THR A 350 3881 5505 4235 -275 -1149 -942 O ATOM 2623 CB THR A 350 34.601 42.261 -7.442 1.00 32.91 C ANISOU 2623 CB THR A 350 3379 4942 4184 -298 -913 -803 C ATOM 2624 OG1 THR A 350 35.360 42.345 -6.224 1.00 31.29 O ANISOU 2624 OG1 THR A 350 3198 4620 4069 -269 -774 -724 O ATOM 2625 CG2 THR A 350 33.237 41.760 -7.006 1.00 33.81 C ANISOU 2625 CG2 THR A 350 3326 5119 4402 -414 -969 -864 C ATOM 2626 N ALA A 351 33.930 40.018 -10.007 1.00 37.60 N ANISOU 2626 N ALA A 351 4111 5596 4580 -537 -1109 -1137 N ATOM 2627 CA ALA A 351 33.149 39.825 -11.235 1.00 40.22 C ANISOU 2627 CA ALA A 351 4421 6069 4791 -593 -1273 -1251 C ATOM 2628 C ALA A 351 31.895 40.707 -11.281 1.00 41.26 C ANISOU 2628 C ALA A 351 4342 6404 4930 -561 -1415 -1212 C ATOM 2629 O ALA A 351 31.684 41.444 -12.248 1.00 42.46 O ANISOU 2629 O ALA A 351 4491 6705 4938 -462 -1534 -1191 O ATOM 2630 CB ALA A 351 32.761 38.350 -11.396 1.00 41.86 C ANISOU 2630 CB ALA A 351 4666 6202 5037 -794 -1280 -1422 C ATOM 2631 N GLU A 352 31.073 40.641 -10.238 1.00 41.20 N ANISOU 2631 N GLU A 352 4161 6408 5083 -630 -1395 -1192 N ATOM 2632 CA GLU A 352 29.793 41.354 -10.228 1.00 42.41 C ANISOU 2632 CA GLU A 352 4090 6764 5258 -602 -1521 -1162 C ATOM 2633 C GLU A 352 29.905 42.696 -9.511 1.00 40.46 C ANISOU 2633 C GLU A 352 3788 6534 5052 -418 -1465 -990 C ATOM 2634 O GLU A 352 30.214 42.735 -8.322 1.00 39.27 O ANISOU 2634 O GLU A 352 3630 6263 5028 -416 -1329 -925 O ATOM 2635 CB GLU A 352 28.709 40.491 -9.565 1.00 43.86 C ANISOU 2635 CB GLU A 352 4098 6971 5595 -793 -1531 -1247 C ATOM 2636 CG GLU A 352 27.445 41.259 -9.197 1.00 45.97 C ANISOU 2636 CG GLU A 352 4104 7435 5928 -748 -1614 -1186 C ATOM 2637 CD GLU A 352 26.263 40.364 -8.889 1.00 49.42 C ANISOU 2637 CD GLU A 352 4346 7947 6486 -960 -1659 -1294 C ATOM 2638 OE1 GLU A 352 25.135 40.732 -9.273 1.00 52.62 O ANISOU 2638 OE1 GLU A 352 4537 8583 6875 -960 -1805 -1309 O ATOM 2639 OE2 GLU A 352 26.454 39.301 -8.258 1.00 51.07 O ANISOU 2639 OE2 GLU A 352 4609 7988 6806 -1125 -1544 -1357 O ATOM 2640 N LEU A 353 29.649 43.791 -10.226 1.00 40.61 N ANISOU 2640 N LEU A 353 3777 6697 4955 -263 -1565 -919 N ATOM 2641 CA LEU A 353 29.668 45.123 -9.618 1.00 39.45 C ANISOU 2641 CA LEU A 353 3590 6558 4841 -85 -1513 -762 C ATOM 2642 C LEU A 353 28.371 45.379 -8.849 1.00 39.97 C ANISOU 2642 C LEU A 353 3414 6742 5031 -89 -1545 -737 C ATOM 2643 O LEU A 353 27.285 45.334 -9.420 1.00 41.63 O ANISOU 2643 O LEU A 353 3463 7146 5209 -107 -1691 -782 O ATOM 2644 CB LEU A 353 29.883 46.216 -10.675 1.00 40.18 C ANISOU 2644 CB LEU A 353 3762 6741 4762 97 -1591 -681 C ATOM 2645 CG LEU A 353 29.985 47.673 -10.174 1.00 39.97 C ANISOU 2645 CG LEU A 353 3737 6695 4754 289 -1528 -517 C ATOM 2646 CD1 LEU A 353 31.160 47.885 -9.223 1.00 37.85 C ANISOU 2646 CD1 LEU A 353 3601 6216 4563 295 -1348 -457 C ATOM 2647 CD2 LEU A 353 30.091 48.645 -11.345 1.00 42.19 C ANISOU 2647 CD2 LEU A 353 4104 7068 4857 460 -1610 -439 C ATOM 2648 N LYS A 354 28.498 45.672 -7.558 1.00 38.23 N ANISOU 2648 N LYS A 354 3165 6417 4945 -65 -1409 -663 N ATOM 2649 CA LYS A 354 27.350 45.849 -6.665 1.00 38.82 C ANISOU 2649 CA LYS A 354 3019 6582 5150 -69 -1401 -635 C ATOM 2650 C LYS A 354 27.178 47.309 -6.216 1.00 37.82 C ANISOU 2650 C LYS A 354 2861 6483 5025 145 -1364 -493 C ATOM 2651 O LYS A 354 26.303 47.614 -5.409 1.00 38.40 O ANISOU 2651 O LYS A 354 2767 6622 5202 179 -1334 -452 O ATOM 2652 CB LYS A 354 27.508 44.938 -5.438 1.00 38.27 C ANISOU 2652 CB LYS A 354 2940 6370 5232 -217 -1261 -669 C ATOM 2653 CG LYS A 354 27.022 43.506 -5.654 1.00 40.57 C ANISOU 2653 CG LYS A 354 3167 6675 5574 -444 -1301 -809 C ATOM 2654 CD LYS A 354 26.880 42.760 -4.328 1.00 41.19 C ANISOU 2654 CD LYS A 354 3197 6638 5817 -567 -1155 -813 C ATOM 2655 CE LYS A 354 26.490 41.295 -4.527 1.00 43.38 C ANISOU 2655 CE LYS A 354 3445 6886 6150 -807 -1170 -951 C ATOM 2656 NZ LYS A 354 27.678 40.396 -4.406 1.00 42.90 N ANISOU 2656 NZ LYS A 354 3616 6603 6082 -878 -1061 -990 N ATOM 2657 N PHE A 355 28.009 48.207 -6.738 1.00 36.35 N ANISOU 2657 N PHE A 355 2844 6239 4728 289 -1354 -417 N ATOM 2658 CA PHE A 355 27.972 49.611 -6.347 1.00 35.38 C ANISOU 2658 CA PHE A 355 2739 6102 4603 487 -1301 -285 C ATOM 2659 C PHE A 355 27.626 50.470 -7.552 1.00 36.69 C ANISOU 2659 C PHE A 355 2912 6403 4625 650 -1426 -226 C ATOM 2660 O PHE A 355 28.163 50.267 -8.636 1.00 36.67 O ANISOU 2660 O PHE A 355 3028 6413 4491 638 -1494 -256 O ATOM 2661 CB PHE A 355 29.317 50.019 -5.750 1.00 33.14 C ANISOU 2661 CB PHE A 355 2659 5606 4326 510 -1154 -234 C ATOM 2662 CG PHE A 355 29.839 49.041 -4.733 1.00 31.06 C ANISOU 2662 CG PHE A 355 2415 5215 4169 353 -1045 -293 C ATOM 2663 CD1 PHE A 355 30.844 48.144 -5.061 1.00 29.79 C ANISOU 2663 CD1 PHE A 355 2386 4959 3974 240 -1020 -358 C ATOM 2664 CD2 PHE A 355 29.288 48.988 -3.464 1.00 30.17 C ANISOU 2664 CD2 PHE A 355 2190 5086 4186 332 -962 -280 C ATOM 2665 CE1 PHE A 355 31.301 47.232 -4.135 1.00 28.69 C ANISOU 2665 CE1 PHE A 355 2268 4706 3926 117 -919 -399 C ATOM 2666 CE2 PHE A 355 29.745 48.074 -2.532 1.00 29.27 C ANISOU 2666 CE2 PHE A 355 2103 4861 4159 201 -861 -322 C ATOM 2667 CZ PHE A 355 30.759 47.198 -2.866 1.00 28.11 C ANISOU 2667 CZ PHE A 355 2089 4617 3976 98 -841 -378 C ATOM 2668 N GLU A 356 26.730 51.431 -7.357 1.00 37.62 N ANISOU 2668 N GLU A 356 2910 6623 4759 816 -1447 -137 N ATOM 2669 CA GLU A 356 26.274 52.280 -8.455 1.00 39.60 C ANISOU 2669 CA GLU A 356 3155 7020 4872 1000 -1567 -62 C ATOM 2670 C GLU A 356 27.381 53.229 -8.911 1.00 38.32 C ANISOU 2670 C GLU A 356 3248 6708 4602 1126 -1498 33 C ATOM 2671 O GLU A 356 28.104 53.796 -8.092 1.00 36.41 O ANISOU 2671 O GLU A 356 3131 6280 4424 1152 -1348 87 O ATOM 2672 CB GLU A 356 25.035 53.082 -8.042 1.00 41.25 C ANISOU 2672 CB GLU A 356 3169 7369 5136 1169 -1589 22 C ATOM 2673 CG GLU A 356 24.341 53.782 -9.197 1.00 44.39 C ANISOU 2673 CG GLU A 356 3510 7967 5390 1362 -1739 96 C ATOM 2674 CD GLU A 356 23.219 54.702 -8.748 1.00 47.44 C ANISOU 2674 CD GLU A 356 3723 8474 5829 1572 -1736 202 C ATOM 2675 OE1 GLU A 356 23.265 55.212 -7.606 1.00 47.20 O ANISOU 2675 OE1 GLU A 356 3709 8307 5916 1625 -1583 252 O ATOM 2676 OE2 GLU A 356 22.284 54.915 -9.547 1.00 51.04 O ANISOU 2676 OE2 GLU A 356 4022 9170 6200 1693 -1890 234 O ATOM 2677 N LEU A 357 27.490 53.398 -10.224 1.00 39.23 N ANISOU 2677 N LEU A 357 3439 6915 4551 1196 -1607 52 N ATOM 2678 CA LEU A 357 28.477 54.286 -10.824 1.00 38.73 C ANISOU 2678 CA LEU A 357 3615 6730 4372 1314 -1545 150 C ATOM 2679 C LEU A 357 27.959 55.716 -10.830 1.00 39.80 C ANISOU 2679 C LEU A 357 3762 6882 4480 1564 -1526 304 C ATOM 2680 O LEU A 357 26.786 55.950 -11.121 1.00 41.77 O ANISOU 2680 O LEU A 357 3840 7327 4703 1687 -1640 337 O ATOM 2681 CB LEU A 357 28.793 53.830 -12.251 1.00 39.58 C ANISOU 2681 CB LEU A 357 3809 6933 4298 1291 -1662 108 C ATOM 2682 CG LEU A 357 29.428 52.440 -12.370 1.00 38.74 C ANISOU 2682 CG LEU A 357 3737 6783 4199 1061 -1665 -44 C ATOM 2683 CD1 LEU A 357 29.470 51.980 -13.824 1.00 40.26 C ANISOU 2683 CD1 LEU A 357 3991 7109 4197 1053 -1802 -100 C ATOM 2684 CD2 LEU A 357 30.823 52.432 -11.759 1.00 36.88 C ANISOU 2684 CD2 LEU A 357 3681 6307 4023 987 -1488 -33 C TER 2685 LEU A 357 ATOM 2982 N GLY A 2 26.060 92.302 63.327 1.00 39.11 N ANISOU 2982 N GLY B 2 4109 5995 4756 787 -5 -1579 N ATOM 2983 CA GLY A 2 26.645 91.484 62.223 1.00 37.20 C ANISOU 2983 CA GLY B 2 3897 5585 4654 542 25 -1417 C ATOM 2984 C GLY A 2 27.769 90.576 62.694 1.00 36.93 C ANISOU 2984 C GLY B 2 3783 5611 4638 445 -31 -1461 C ATOM 2985 O GLY A 2 28.180 90.635 63.854 1.00 38.39 O ANISOU 2985 O GLY B 2 3897 5962 4728 551 -120 -1618 O ATOM 2986 N TYR A 3 28.282 89.763 61.771 1.00 35.57 N ANISOU 2986 N TYR B 3 3630 5301 4583 262 14 -1334 N ATOM 2987 CA TYR A 3 29.243 88.701 62.063 1.00 35.39 C ANISOU 2987 CA TYR B 3 3521 5323 4601 191 -28 -1320 C ATOM 2988 C TYR A 3 30.695 89.119 61.899 1.00 35.88 C ANISOU 2988 C TYR B 3 3550 5189 4895 97 -32 -1537 C ATOM 2989 O TYR A 3 31.028 89.910 61.020 1.00 36.24 O ANISOU 2989 O TYR B 3 3674 4984 5113 -10 60 -1613 O ATOM 2990 CB TYR A 3 29.032 87.515 61.106 1.00 33.95 C ANISOU 2990 CB TYR B 3 3380 5076 4442 55 37 -1090 C ATOM 2991 CG TYR A 3 27.697 86.824 61.225 1.00 34.15 C ANISOU 2991 CG TYR B 3 3396 5291 4290 86 26 -848 C ATOM 2992 CD1 TYR A 3 27.241 86.359 62.452 1.00 35.22 C ANISOU 2992 CD1 TYR B 3 3425 5708 4250 210 -35 -760 C ATOM 2993 CD2 TYR A 3 26.898 86.613 60.103 1.00 33.64 C ANISOU 2993 CD2 TYR B 3 3417 5137 4225 -21 74 -698 C ATOM 2994 CE1 TYR A 3 26.018 85.717 62.566 1.00 35.71 C ANISOU 2994 CE1 TYR B 3 3441 5948 4179 208 -21 -516 C ATOM 2995 CE2 TYR A 3 25.672 85.971 60.206 1.00 33.96 C ANISOU 2995 CE2 TYR B 3 3405 5356 4142 -24 47 -481 C ATOM 2996 CZ TYR A 3 25.239 85.524 61.441 1.00 35.04 C ANISOU 2996 CZ TYR B 3 3410 5760 4145 81 13 -385 C ATOM 2997 OH TYR A 3 24.032 84.883 61.565 1.00 36.05 O ANISOU 2997 OH TYR B 3 3450 6069 4179 51 11 -149 O ATOM 2998 N THR A 4 31.557 88.541 62.729 1.00 36.51 N ANISOU 2998 N THR B 4 3497 5392 4984 133 -138 -1608 N ATOM 2999 CA THR A 4 32.987 88.530 62.478 1.00 37.21 C ANISOU 2999 CA THR B 4 3485 5329 5325 26 -141 -1755 C ATOM 3000 C THR A 4 33.320 87.233 61.722 1.00 36.03 C ANISOU 3000 C THR B 4 3324 5113 5253 -52 -54 -1572 C ATOM 3001 O THR A 4 33.131 86.138 62.246 1.00 35.56 O ANISOU 3001 O THR B 4 3226 5208 5079 28 -125 -1420 O ATOM 3002 CB THR A 4 33.766 88.633 63.803 1.00 39.29 C ANISOU 3002 CB THR B 4 3589 5777 5561 130 -343 -1947 C ATOM 3003 OG1 THR A 4 33.472 89.887 64.438 1.00 40.90 O ANISOU 3003 OG1 THR B 4 3837 6006 5696 198 -419 -2171 O ATOM 3004 CG2 THR A 4 35.269 88.689 63.558 1.00 40.33 C ANISOU 3004 CG2 THR B 4 3554 5771 5997 14 -363 -2111 C ATOM 3005 N VAL A 5 33.781 87.376 60.482 1.00 35.35 N ANISOU 3005 N VAL B 5 3292 4786 5353 -202 113 -1582 N ATOM 3006 CA VAL A 5 34.159 86.249 59.634 1.00 34.86 C ANISOU 3006 CA VAL B 5 3248 4627 5371 -269 226 -1466 C ATOM 3007 C VAL A 5 35.676 86.199 59.426 1.00 36.34 C ANISOU 3007 C VAL B 5 3263 4711 5835 -324 288 -1615 C ATOM 3008 O VAL A 5 36.268 87.169 58.972 1.00 37.03 O ANISOU 3008 O VAL B 5 3318 4662 6091 -435 387 -1750 O ATOM 3009 CB VAL A 5 33.473 86.348 58.254 1.00 33.76 C ANISOU 3009 CB VAL B 5 3320 4327 5181 -386 396 -1356 C ATOM 3010 CG1 VAL A 5 33.760 85.105 57.426 1.00 33.67 C ANISOU 3010 CG1 VAL B 5 3362 4223 5206 -438 500 -1271 C ATOM 3011 CG2 VAL A 5 31.953 86.550 58.417 1.00 32.50 C ANISOU 3011 CG2 VAL B 5 3281 4282 4787 -334 323 -1216 C ATOM 3012 N ALA A 6 36.291 85.066 59.760 1.00 37.04 N ANISOU 3012 N ALA B 6 3227 4857 5990 -243 235 -1575 N ATOM 3013 CA ALA A 6 37.707 84.833 59.498 1.00 38.82 C ANISOU 3013 CA ALA B 6 3249 5003 6497 -264 307 -1694 C ATOM 3014 C ALA A 6 37.900 83.916 58.291 1.00 38.71 C ANISOU 3014 C ALA B 6 3330 4823 6555 -306 529 -1616 C ATOM 3015 O ALA A 6 37.142 82.962 58.098 1.00 37.93 O ANISOU 3015 O ALA B 6 3394 4708 6308 -264 521 -1462 O ATOM 3016 CB ALA A 6 38.380 84.230 60.721 1.00 40.27 C ANISOU 3016 CB ALA B 6 3207 5366 6730 -101 79 -1718 C ATOM 3017 N VAL A 7 38.902 84.235 57.477 1.00 40.18 N ANISOU 3017 N VAL B 7 3416 4883 6967 -399 735 -1732 N ATOM 3018 CA VAL A 7 39.378 83.377 56.400 1.00 40.97 C ANISOU 3018 CA VAL B 7 3562 4848 7158 -405 970 -1718 C ATOM 3019 C VAL A 7 40.768 82.859 56.775 1.00 43.48 C ANISOU 3019 C VAL B 7 3550 5197 7774 -297 969 -1821 C ATOM 3020 O VAL A 7 41.725 83.634 56.836 1.00 45.13 O ANISOU 3020 O VAL B 7 3510 5424 8213 -370 1022 -1957 O ATOM 3021 CB VAL A 7 39.472 84.151 55.069 1.00 41.30 C ANISOU 3021 CB VAL B 7 3741 4747 7205 -584 1266 -1751 C ATOM 3022 CG1 VAL A 7 40.049 83.270 53.968 1.00 42.88 C ANISOU 3022 CG1 VAL B 7 3989 4836 7467 -568 1536 -1773 C ATOM 3023 CG2 VAL A 7 38.103 84.694 54.671 1.00 39.76 C ANISOU 3023 CG2 VAL B 7 3856 4527 6723 -664 1239 -1634 C ATOM 3024 N VAL A 8 40.864 81.556 57.039 1.00 43.99 N ANISOU 3024 N VAL B 8 3599 5257 7857 -125 897 -1748 N ATOM 3025 CA VAL A 8 42.127 80.901 57.372 1.00 46.75 C ANISOU 3025 CA VAL B 8 3636 5630 8496 34 881 -1818 C ATOM 3026 C VAL A 8 42.758 80.375 56.087 1.00 48.43 C ANISOU 3026 C VAL B 8 3869 5675 8858 34 1224 -1889 C ATOM 3027 O VAL A 8 42.159 79.559 55.387 1.00 47.57 O ANISOU 3027 O VAL B 8 4041 5426 8609 57 1334 -1829 O ATOM 3028 CB VAL A 8 41.916 79.727 58.360 1.00 47.04 C ANISOU 3028 CB VAL B 8 3665 5721 8485 256 622 -1674 C ATOM 3029 CG1 VAL A 8 43.257 79.191 58.861 1.00 50.21 C ANISOU 3029 CG1 VAL B 8 3702 6178 9197 454 544 -1735 C ATOM 3030 CG2 VAL A 8 41.036 80.157 59.525 1.00 44.91 C ANISOU 3030 CG2 VAL B 8 3461 5637 7965 257 332 -1573 C ATOM 3031 N GLY A 9 43.966 80.841 55.787 1.00 51.10 N ANISOU 3031 N GLY B 9 3901 6036 9480 2 1397 -2029 N ATOM 3032 CA GLY A 9 44.624 80.556 54.520 1.00 53.22 C ANISOU 3032 CA GLY B 9 4165 6184 9873 -11 1787 -2113 C ATOM 3033 C GLY A 9 44.233 81.598 53.488 1.00 52.65 C ANISOU 3033 C GLY B 9 4307 6055 9645 -265 2046 -2120 C ATOM 3034 O GLY A 9 43.989 81.274 52.329 1.00 52.78 O ANISOU 3034 O GLY B 9 4582 5961 9511 -298 2322 -2120 O ATOM 3035 N ALA A 10 44.179 82.857 53.920 1.00 52.55 N ANISOU 3035 N ALA B 10 4200 6107 9659 -437 1947 -2128 N ATOM 3036 CA ALA A 10 43.730 83.960 53.067 1.00 52.31 C ANISOU 3036 CA ALA B 10 4390 5997 9487 -671 2149 -2092 C ATOM 3037 C ALA A 10 44.667 84.187 51.882 1.00 55.45 C ANISOU 3037 C ALA B 10 4695 6336 10037 -774 2588 -2142 C ATOM 3038 O ALA A 10 44.223 84.583 50.802 1.00 55.52 O ANISOU 3038 O ALA B 10 5001 6262 9833 -903 2836 -2070 O ATOM 3039 CB ALA A 10 43.594 85.237 53.885 1.00 51.85 C ANISOU 3039 CB ALA B 10 4228 5980 9493 -809 1938 -2114 C ATOM 3040 N THR A 11 45.957 83.935 52.092 1.00 58.63 N ANISOU 3040 N THR B 11 4675 6804 10798 -707 2683 -2252 N ATOM 3041 CA THR A 11 46.943 83.967 51.010 1.00 62.20 C ANISOU 3041 CA THR B 11 4977 7236 11419 -766 3141 -2302 C ATOM 3042 C THR A 11 46.718 82.792 50.059 1.00 62.53 C ANISOU 3042 C THR B 11 5296 7217 11245 -594 3376 -2311 C ATOM 3043 O THR A 11 47.448 82.618 49.081 1.00 65.40 O ANISOU 3043 O THR B 11 5595 7578 11675 -588 3791 -2367 O ATOM 3044 CB THR A 11 48.382 83.910 51.572 1.00 65.79 C ANISOU 3044 CB THR B 11 4842 7805 12352 -708 3153 -2425 C ATOM 3045 OG1 THR A 11 48.528 82.780 52.444 1.00 65.79 O ANISOU 3045 OG1 THR B 11 4691 7870 12435 -416 2864 -2469 O ATOM 3046 CG2 THR A 11 48.683 85.120 52.463 1.00 66.24 C ANISOU 3046 CG2 THR B 11 4617 7911 12641 -913 2914 -2463 C ATOM 3047 N GLY A 15 41.955 80.611 48.412 1.00 52.89 N ANISOU 3047 N GLY B 15 5845 5690 8561 -512 2983 -2086 N ATOM 3048 CA GLY A 15 41.964 81.714 49.358 1.00 51.41 C ANISOU 3048 CA GLY B 15 5429 5591 8515 -611 2793 -1999 C ATOM 3049 C GLY A 15 41.507 83.030 48.750 1.00 50.82 C ANISOU 3049 C GLY B 15 5530 5522 8258 -825 2899 -1897 C ATOM 3050 O GLY A 15 40.710 83.751 49.355 1.00 48.36 O ANISOU 3050 O GLY B 15 5273 5233 7868 -896 2649 -1798 O ATOM 3051 N ALA A 16 42.019 83.338 47.559 1.00 53.13 N ANISOU 3051 N ALA B 16 5915 5790 8480 -910 3283 -1912 N ATOM 3052 CA ALA A 16 41.639 84.546 46.822 1.00 53.35 C ANISOU 3052 CA ALA B 16 6152 5800 8320 -1105 3426 -1775 C ATOM 3053 C ALA A 16 40.172 84.526 46.391 1.00 51.28 C ANISOU 3053 C ALA B 16 6319 5523 7643 -1129 3234 -1659 C ATOM 3054 O ALA A 16 39.484 85.538 46.489 1.00 49.94 O ANISOU 3054 O ALA B 16 6259 5338 7377 -1232 3109 -1517 O ATOM 3055 CB ALA A 16 42.532 84.719 45.601 1.00 57.19 C ANISOU 3055 CB ALA B 16 6660 6287 8782 -1173 3912 -1793 C ATOM 3056 N GLN A 17 39.698 83.379 45.905 1.00 51.22 N ANISOU 3056 N GLN B 17 6543 5509 7409 -1033 3203 -1728 N ATOM 3057 CA GLN A 17 38.297 83.243 45.496 1.00 49.61 C ANISOU 3057 CA GLN B 17 6708 5311 6832 -1066 2985 -1636 C ATOM 3058 C GLN A 17 37.351 83.285 46.700 1.00 46.56 C ANISOU 3058 C GLN B 17 6234 4951 6504 -1040 2569 -1554 C ATOM 3059 O GLN A 17 36.229 83.774 46.598 1.00 44.84 O ANISOU 3059 O GLN B 17 6204 4765 6067 -1099 2382 -1421 O ATOM 3060 CB GLN A 17 38.078 81.953 44.695 1.00 50.83 C ANISOU 3060 CB GLN B 17 7121 5431 6762 -993 3038 -1771 C ATOM 3061 CG GLN A 17 38.936 81.823 43.430 1.00 54.28 C ANISOU 3061 CG GLN B 17 7691 5870 7064 -988 3476 -1878 C ATOM 3062 CD GLN A 17 38.804 83.009 42.482 1.00 55.81 C ANISOU 3062 CD GLN B 17 8091 6124 6990 -1132 3681 -1714 C ATOM 3063 OE1 GLN A 17 37.773 83.683 42.461 1.00 53.95 O ANISOU 3063 OE1 GLN B 17 8032 5911 6556 -1216 3451 -1541 O ATOM 3064 NE2 GLN A 17 39.848 83.260 41.693 1.00 59.15 N ANISOU 3064 NE2 GLN B 17 8484 6576 7414 -1150 4125 -1748 N ATOM 3065 N MET A 18 37.818 82.774 47.836 1.00 45.98 N ANISOU 3065 N MET B 18 5868 4884 6720 -937 2434 -1623 N ATOM 3066 CA MET A 18 37.081 82.853 49.100 1.00 43.79 C ANISOU 3066 CA MET B 18 5472 4666 6502 -898 2083 -1544 C ATOM 3067 C MET A 18 36.768 84.319 49.431 1.00 42.55 C ANISOU 3067 C MET B 18 5273 4547 6348 -984 2019 -1445 C ATOM 3068 O MET A 18 35.633 84.660 49.777 1.00 40.49 O ANISOU 3068 O MET B 18 5115 4336 5934 -990 1794 -1336 O ATOM 3069 CB MET A 18 37.917 82.212 50.221 1.00 44.33 C ANISOU 3069 CB MET B 18 5215 4752 6878 -763 1994 -1627 C ATOM 3070 CG MET A 18 37.149 81.799 51.459 1.00 44.02 C ANISOU 3070 CG MET B 18 5106 4784 6835 -685 1653 -1543 C ATOM 3071 SD MET A 18 36.091 80.388 51.191 1.00 46.47 S ANISOU 3071 SD MET B 18 5673 5025 6957 -661 1513 -1484 S ATOM 3072 CE MET A 18 37.165 79.036 51.513 1.00 47.74 C ANISOU 3072 CE MET B 18 5682 5074 7384 -487 1567 -1589 C ATOM 3073 N ILE A 19 37.785 85.174 49.295 1.00 43.93 N ANISOU 3073 N ILE B 19 5289 4682 6719 -1052 2231 -1488 N ATOM 3074 CA ILE A 19 37.667 86.610 49.550 1.00 43.71 C ANISOU 3074 CA ILE B 19 5230 4623 6757 -1149 2204 -1419 C ATOM 3075 C ILE A 19 36.676 87.268 48.592 1.00 43.65 C ANISOU 3075 C ILE B 19 5565 4571 6448 -1223 2237 -1255 C ATOM 3076 O ILE A 19 35.828 88.044 49.024 1.00 42.42 O ANISOU 3076 O ILE B 19 5467 4413 6237 -1216 2044 -1166 O ATOM 3077 CB ILE A 19 39.065 87.291 49.468 1.00 46.24 C ANISOU 3077 CB ILE B 19 5299 4879 7392 -1249 2457 -1498 C ATOM 3078 CG1 ILE A 19 39.911 86.916 50.690 1.00 46.17 C ANISOU 3078 CG1 ILE B 19 4900 4940 7700 -1165 2311 -1650 C ATOM 3079 CG2 ILE A 19 38.953 88.821 49.352 1.00 47.38 C ANISOU 3079 CG2 ILE B 19 5499 4909 7596 -1395 2502 -1408 C ATOM 3080 CD1 ILE A 19 41.407 87.019 50.449 1.00 49.40 C ANISOU 3080 CD1 ILE B 19 5006 5330 8434 -1232 2581 -1755 C ATOM 3081 N LYS A 20 36.768 86.946 47.304 1.00 45.38 N ANISOU 3081 N LYS B 20 6015 4769 6459 -1270 2472 -1220 N ATOM 3082 CA LYS A 20 35.901 87.562 46.296 1.00 46.24 C ANISOU 3082 CA LYS B 20 6464 4857 6247 -1331 2498 -1047 C ATOM 3083 C LYS A 20 34.425 87.213 46.506 1.00 44.20 C ANISOU 3083 C LYS B 20 6361 4682 5750 -1260 2161 -970 C ATOM 3084 O LYS A 20 33.557 88.080 46.399 1.00 44.33 O ANISOU 3084 O LYS B 20 6507 4691 5644 -1265 2034 -816 O ATOM 3085 CB LYS A 20 36.332 87.167 44.880 1.00 48.86 C ANISOU 3085 CB LYS B 20 7028 5191 6346 -1380 2815 -1045 C ATOM 3086 CG LYS A 20 35.858 88.143 43.800 1.00 51.14 C ANISOU 3086 CG LYS B 20 7632 5448 6349 -1464 2927 -831 C ATOM 3087 CD LYS A 20 35.219 87.443 42.598 1.00 53.24 C ANISOU 3087 CD LYS B 20 8265 5806 6158 -1447 2941 -810 C ATOM 3088 CE LYS A 20 36.219 87.180 41.475 1.00 57.18 C ANISOU 3088 CE LYS B 20 8888 6320 6516 -1491 3372 -864 C ATOM 3089 NZ LYS A 20 35.972 85.868 40.811 1.00 58.76 N ANISOU 3089 NZ LYS B 20 9301 6605 6420 -1424 3358 -1038 N ATOM 3090 N MET A 21 34.147 85.949 46.807 1.00 42.97 N ANISOU 3090 N MET B 21 6176 4593 5558 -1195 2019 -1067 N ATOM 3091 CA MET A 21 32.785 85.510 47.092 1.00 41.51 C ANISOU 3091 CA MET B 21 6076 4495 5200 -1157 1705 -995 C ATOM 3092 C MET A 21 32.262 86.173 48.365 1.00 40.05 C ANISOU 3092 C MET B 21 5687 4362 5167 -1093 1483 -934 C ATOM 3093 O MET A 21 31.080 86.465 48.466 1.00 39.55 O ANISOU 3093 O MET B 21 5692 4374 4960 -1067 1279 -814 O ATOM 3094 CB MET A 21 32.710 83.980 47.224 1.00 40.81 C ANISOU 3094 CB MET B 21 5983 4420 5104 -1126 1620 -1109 C ATOM 3095 CG MET A 21 32.954 83.208 45.929 1.00 42.48 C ANISOU 3095 CG MET B 21 6453 4582 5103 -1169 1791 -1207 C ATOM 3096 SD MET A 21 31.801 83.603 44.596 1.00 41.64 S ANISOU 3096 SD MET B 21 6726 4546 4549 -1254 1705 -1085 S ATOM 3097 CE MET A 21 32.792 84.765 43.649 1.00 44.07 C ANISOU 3097 CE MET B 21 7149 4813 4781 -1293 2090 -1024 C ATOM 3098 N LEU A 22 33.149 86.428 49.322 1.00 40.39 N ANISOU 3098 N LEU B 22 5474 4382 5492 -1058 1522 -1028 N ATOM 3099 CA LEU A 22 32.763 87.066 50.585 1.00 39.69 C ANISOU 3099 CA LEU B 22 5204 4353 5523 -982 1325 -1017 C ATOM 3100 C LEU A 22 32.482 88.563 50.415 1.00 40.59 C ANISOU 3100 C LEU B 22 5396 4385 5641 -1003 1346 -939 C ATOM 3101 O LEU A 22 31.671 89.130 51.143 1.00 40.35 O ANISOU 3101 O LEU B 22 5324 4409 5597 -917 1164 -898 O ATOM 3102 CB LEU A 22 33.847 86.840 51.645 1.00 39.83 C ANISOU 3102 CB LEU B 22 4934 4384 5815 -938 1326 -1166 C ATOM 3103 CG LEU A 22 33.420 86.658 53.099 1.00 39.37 C ANISOU 3103 CG LEU B 22 4695 4466 5798 -820 1076 -1183 C ATOM 3104 CD1 LEU A 22 32.419 85.514 53.259 1.00 38.58 C ANISOU 3104 CD1 LEU B 22 4658 4476 5525 -772 922 -1080 C ATOM 3105 CD2 LEU A 22 34.656 86.416 53.959 1.00 40.53 C ANISOU 3105 CD2 LEU B 22 4575 4631 6192 -778 1077 -1330 C ATOM 3106 N GLU A 23 33.140 89.193 49.444 1.00 42.71 N ANISOU 3106 N GLU B 23 5784 4513 5930 -1107 1586 -907 N ATOM 3107 CA GLU A 23 32.915 90.604 49.126 1.00 44.18 C ANISOU 3107 CA GLU B 23 6090 4561 6133 -1138 1631 -794 C ATOM 3108 C GLU A 23 31.541 90.843 48.488 1.00 44.20 C ANISOU 3108 C GLU B 23 6339 4610 5845 -1077 1492 -601 C ATOM 3109 O GLU A 23 31.004 91.946 48.565 1.00 44.88 O ANISOU 3109 O GLU B 23 6495 4606 5952 -1026 1426 -498 O ATOM 3110 CB GLU A 23 34.011 91.124 48.182 1.00 46.75 C ANISOU 3110 CB GLU B 23 6486 4728 6548 -1288 1960 -765 C ATOM 3111 CG GLU A 23 35.365 91.311 48.850 1.00 48.06 C ANISOU 3111 CG GLU B 23 6358 4823 7080 -1366 2086 -938 C ATOM 3112 CD GLU A 23 36.517 91.519 47.871 1.00 51.62 C ANISOU 3112 CD GLU B 23 6818 5169 7625 -1526 2457 -910 C ATOM 3113 OE1 GLU A 23 36.332 91.387 46.640 1.00 52.91 O ANISOU 3113 OE1 GLU B 23 7246 5334 7524 -1565 2643 -767 O ATOM 3114 OE2 GLU A 23 37.629 91.824 48.350 1.00 52.99 O ANISOU 3114 OE2 GLU B 23 6720 5277 8136 -1616 2566 -1035 O ATOM 3115 N GLU A 24 30.990 89.819 47.842 1.00 43.91 N ANISOU 3115 N GLU B 24 6429 4701 5553 -1079 1436 -561 N ATOM 3116 CA GLU A 24 29.697 89.927 47.169 1.00 44.50 C ANISOU 3116 CA GLU B 24 6708 4855 5344 -1035 1269 -387 C ATOM 3117 C GLU A 24 28.586 89.172 47.919 1.00 42.77 C ANISOU 3117 C GLU B 24 6357 4823 5070 -951 983 -394 C ATOM 3118 O GLU A 24 27.456 89.093 47.444 1.00 43.17 O ANISOU 3118 O GLU B 24 6512 4978 4911 -922 807 -266 O ATOM 3119 CB GLU A 24 29.828 89.420 45.725 1.00 46.53 C ANISOU 3119 CB GLU B 24 7239 5124 5315 -1127 1403 -335 C ATOM 3120 CG GLU A 24 30.773 90.266 44.875 1.00 49.33 C ANISOU 3120 CG GLU B 24 7747 5322 5673 -1212 1716 -260 C ATOM 3121 CD GLU A 24 31.094 89.651 43.520 1.00 52.16 C ANISOU 3121 CD GLU B 24 8370 5727 5723 -1291 1906 -251 C ATOM 3122 OE1 GLU A 24 32.222 89.866 43.020 1.00 54.45 O ANISOU 3122 OE1 GLU B 24 8691 5927 6070 -1376 2241 -271 O ATOM 3123 OE2 GLU A 24 30.222 88.966 42.945 1.00 52.37 O ANISOU 3123 OE2 GLU B 24 8566 5887 5444 -1273 1725 -233 O ATOM 3124 N SER A 25 28.906 88.641 49.096 1.00 41.24 N ANISOU 3124 N SER B 25 5922 4682 5067 -915 935 -526 N ATOM 3125 CA SER A 25 27.951 87.864 49.887 1.00 40.04 C ANISOU 3125 CA SER B 25 5626 4707 4878 -855 708 -508 C ATOM 3126 C SER A 25 26.831 88.724 50.469 1.00 39.99 C ANISOU 3126 C SER B 25 5541 4798 4856 -722 541 -401 C ATOM 3127 O SER A 25 27.009 89.918 50.681 1.00 40.68 O ANISOU 3127 O SER B 25 5635 4782 5041 -648 591 -401 O ATOM 3128 CB SER A 25 28.675 87.157 51.034 1.00 38.81 C ANISOU 3128 CB SER B 25 5250 4584 4914 -832 718 -645 C ATOM 3129 OG SER A 25 27.808 86.279 51.719 1.00 37.42 O ANISOU 3129 OG SER B 25 4959 4569 4691 -799 536 -591 O ATOM 3130 N THR A 26 25.681 88.101 50.719 1.00 39.66 N ANISOU 3130 N THR B 26 5417 4941 4712 -694 350 -314 N ATOM 3131 CA THR A 26 24.578 88.749 51.435 1.00 39.93 C ANISOU 3131 CA THR B 26 5307 5117 4747 -539 206 -223 C ATOM 3132 C THR A 26 24.712 88.587 52.954 1.00 38.83 C ANISOU 3132 C THR B 26 4930 5089 4735 -444 194 -313 C ATOM 3133 O THR A 26 23.897 89.107 53.706 1.00 39.34 O ANISOU 3133 O THR B 26 4858 5290 4798 -292 115 -272 O ATOM 3134 CB THR A 26 23.222 88.175 50.992 1.00 40.48 C ANISOU 3134 CB THR B 26 5349 5372 4659 -564 12 -71 C ATOM 3135 OG1 THR A 26 23.186 86.769 51.255 1.00 39.98 O ANISOU 3135 OG1 THR B 26 5203 5391 4597 -691 -37 -98 O ATOM 3136 CG2 THR A 26 23.028 88.287 49.473 1.00 42.20 C ANISOU 3136 CG2 THR B 26 5822 5522 4691 -649 -22 14 C ATOM 3137 N LEU A 27 25.715 87.834 53.393 1.00 38.07 N ANISOU 3137 N LEU B 27 4784 4951 4728 -515 270 -430 N ATOM 3138 CA LEU A 27 26.078 87.733 54.809 1.00 37.70 C ANISOU 3138 CA LEU B 27 4545 5004 4776 -420 257 -522 C ATOM 3139 C LEU A 27 26.311 89.127 55.411 1.00 38.17 C ANISOU 3139 C LEU B 27 4574 5009 4919 -282 284 -632 C ATOM 3140 O LEU A 27 27.070 89.921 54.851 1.00 38.80 O ANISOU 3140 O LEU B 27 4769 4875 5100 -328 385 -709 O ATOM 3141 CB LEU A 27 27.365 86.909 54.951 1.00 37.54 C ANISOU 3141 CB LEU B 27 4505 4894 4867 -504 339 -635 C ATOM 3142 CG LEU A 27 27.502 85.793 55.981 1.00 37.91 C ANISOU 3142 CG LEU B 27 4399 5073 4934 -479 273 -622 C ATOM 3143 CD1 LEU A 27 26.272 84.905 56.047 1.00 38.59 C ANISOU 3143 CD1 LEU B 27 4450 5308 4904 -514 166 -439 C ATOM 3144 CD2 LEU A 27 28.750 84.979 55.637 1.00 38.23 C ANISOU 3144 CD2 LEU B 27 4467 4962 5098 -559 364 -714 C ATOM 3145 N PRO A 28 25.679 89.431 56.545 1.00 38.34 N ANISOU 3145 N PRO B 28 4452 5212 4904 -120 208 -648 N ATOM 3146 CA PRO A 28 25.929 90.705 57.230 1.00 39.19 C ANISOU 3146 CA PRO B 28 4545 5253 5092 23 220 -810 C ATOM 3147 C PRO A 28 27.252 90.646 57.984 1.00 39.28 C ANISOU 3147 C PRO B 28 4489 5214 5224 -12 242 -1016 C ATOM 3148 O PRO A 28 27.315 89.996 59.024 1.00 39.08 O ANISOU 3148 O PRO B 28 4327 5393 5129 49 179 -1047 O ATOM 3149 CB PRO A 28 24.751 90.818 58.198 1.00 39.80 C ANISOU 3149 CB PRO B 28 4483 5597 5043 221 144 -764 C ATOM 3150 CG PRO A 28 24.352 89.394 58.490 1.00 38.96 C ANISOU 3150 CG PRO B 28 4257 5720 4827 149 103 -613 C ATOM 3151 CD PRO A 28 24.702 88.598 57.272 1.00 38.05 C ANISOU 3151 CD PRO B 28 4258 5452 4745 -64 122 -523 C ATOM 3152 N ILE A 29 28.282 91.312 57.465 1.00 39.79 N ANISOU 3152 N ILE B 29 4635 5021 5464 -114 327 -1135 N ATOM 3153 CA ILE A 29 29.625 91.241 58.039 1.00 40.19 C ANISOU 3153 CA ILE B 29 4580 5019 5670 -177 336 -1331 C ATOM 3154 C ILE A 29 30.066 92.576 58.646 1.00 42.03 C ANISOU 3154 C ILE B 29 4806 5113 6049 -126 308 -1558 C ATOM 3155 O ILE A 29 30.185 93.579 57.941 1.00 42.93 O ANISOU 3155 O ILE B 29 5048 4965 6298 -187 392 -1568 O ATOM 3156 CB ILE A 29 30.636 90.784 56.960 1.00 40.03 C ANISOU 3156 CB ILE B 29 4606 4824 5781 -372 478 -1304 C ATOM 3157 CG1 ILE A 29 30.268 89.388 56.446 1.00 38.68 C ANISOU 3157 CG1 ILE B 29 4459 4765 5474 -416 487 -1137 C ATOM 3158 CG2 ILE A 29 32.066 90.788 57.517 1.00 40.62 C ANISOU 3158 CG2 ILE B 29 4519 4851 6065 -435 486 -1506 C ATOM 3159 CD1 ILE A 29 30.860 89.068 55.089 1.00 39.35 C ANISOU 3159 CD1 ILE B 29 4670 4677 5604 -573 655 -1089 C ATOM 3160 N ASP A 30 30.294 92.576 59.957 1.00 42.82 N ANISOU 3160 N ASP B 30 4774 5383 6113 -17 183 -1736 N ATOM 3161 CA ASP A 30 30.862 93.730 60.654 1.00 44.97 C ANISOU 3161 CA ASP B 30 5030 5528 6530 12 119 -2019 C ATOM 3162 C ASP A 30 32.384 93.774 60.525 1.00 45.66 C ANISOU 3162 C ASP B 30 5012 5459 6880 -183 136 -2173 C ATOM 3163 O ASP A 30 32.953 94.847 60.353 1.00 47.49 O ANISOU 3163 O ASP B 30 5277 5424 7344 -283 164 -2333 O ATOM 3164 CB ASP A 30 30.506 93.698 62.143 1.00 46.05 C ANISOU 3164 CB ASP B 30 5078 5951 6469 218 -38 -2175 C ATOM 3165 CG ASP A 30 29.040 93.967 62.409 1.00 46.82 C ANISOU 3165 CG ASP B 30 5243 6196 6350 434 -31 -2080 C ATOM 3166 OD1 ASP A 30 28.314 94.405 61.489 1.00 48.00 O ANISOU 3166 OD1 ASP B 30 5509 6189 6541 439 58 -1930 O ATOM 3167 OD2 ASP A 30 28.526 93.770 63.529 1.00 48.62 O ANISOU 3167 OD2 ASP B 30 5404 6718 6351 621 -107 -2138 O ATOM 3168 N LYS A 31 33.036 92.615 60.632 1.00 44.56 N ANISOU 3168 N LYS B 31 4728 5474 6729 -233 119 -2123 N ATOM 3169 CA LYS A 31 34.503 92.551 60.667 1.00 45.72 C ANISOU 3169 CA LYS B 31 4701 5538 7132 -381 115 -2277 C ATOM 3170 C LYS A 31 35.057 91.342 59.912 1.00 44.27 C ANISOU 3170 C LYS B 31 4446 5379 6997 -468 235 -2113 C ATOM 3171 O LYS A 31 34.590 90.215 60.083 1.00 42.69 O ANISOU 3171 O LYS B 31 4245 5367 6609 -371 197 -1959 O ATOM 3172 CB LYS A 31 34.991 92.515 62.119 1.00 47.40 C ANISOU 3172 CB LYS B 31 4741 5965 7302 -276 -123 -2507 C ATOM 3173 CG LYS A 31 36.414 93.051 62.320 1.00 50.73 C ANISOU 3173 CG LYS B 31 4971 6261 8044 -434 -189 -2762 C ATOM 3174 CD LYS A 31 36.866 92.908 63.772 1.00 53.31 C ANISOU 3174 CD LYS B 31 5131 6852 8273 -313 -475 -2986 C ATOM 3175 CE LYS A 31 37.914 93.946 64.163 1.00 56.82 C ANISOU 3175 CE LYS B 31 5433 7145 9010 -461 -606 -3327 C ATOM 3176 NZ LYS A 31 37.308 95.137 64.839 1.00 59.09 N ANISOU 3176 NZ LYS B 31 5884 7358 9210 -385 -722 -3573 N ATOM 3177 N ILE A 32 36.052 91.594 59.068 1.00 44.89 N ANISOU 3177 N ILE B 32 4468 5250 7338 -652 397 -2147 N ATOM 3178 CA ILE A 32 36.755 90.546 58.343 1.00 44.23 C ANISOU 3178 CA ILE B 32 4299 5170 7334 -720 541 -2048 C ATOM 3179 C ILE A 32 38.132 90.398 58.977 1.00 45.83 C ANISOU 3179 C ILE B 32 4192 5428 7791 -756 458 -2236 C ATOM 3180 O ILE A 32 38.762 91.388 59.322 1.00 47.50 O ANISOU 3180 O ILE B 32 4287 5544 8215 -858 405 -2429 O ATOM 3181 CB ILE A 32 36.879 90.910 56.843 1.00 44.56 C ANISOU 3181 CB ILE B 32 4494 4975 7460 -888 828 -1931 C ATOM 3182 CG1 ILE A 32 35.495 90.943 56.173 1.00 43.01 C ANISOU 3182 CG1 ILE B 32 4591 4760 6990 -835 867 -1729 C ATOM 3183 CG2 ILE A 32 37.836 89.940 56.115 1.00 45.27 C ANISOU 3183 CG2 ILE B 32 4469 5064 7669 -953 1015 -1896 C ATOM 3184 CD1 ILE A 32 34.986 89.585 55.682 1.00 41.46 C ANISOU 3184 CD1 ILE B 32 4479 4686 6589 -780 895 -1568 C ATOM 3185 N ARG A 33 38.583 89.156 59.131 1.00 45.27 N ANISOU 3185 N ARG B 33 3985 5500 7716 -671 431 -2180 N ATOM 3186 CA ARG A 33 39.913 88.868 59.650 1.00 47.30 C ANISOU 3186 CA ARG B 33 3914 5833 8226 -673 345 -2328 C ATOM 3187 C ARG A 33 40.581 87.792 58.800 1.00 47.33 C ANISOU 3187 C ARG B 33 3830 5799 8354 -672 549 -2228 C ATOM 3188 O ARG A 33 40.011 86.726 58.574 1.00 45.54 O ANISOU 3188 O ARG B 33 3743 5615 7945 -558 575 -2067 O ATOM 3189 CB ARG A 33 39.832 88.386 61.095 1.00 47.65 C ANISOU 3189 CB ARG B 33 3844 6141 8118 -479 20 -2380 C ATOM 3190 CG ARG A 33 39.338 89.419 62.077 1.00 48.46 C ANISOU 3190 CG ARG B 33 4005 6319 8091 -448 -190 -2542 C ATOM 3191 CD ARG A 33 39.214 88.886 63.493 1.00 49.47 C ANISOU 3191 CD ARG B 33 4054 6753 7989 -239 -492 -2571 C ATOM 3192 NE ARG A 33 40.503 88.430 64.010 1.00 51.90 N ANISOU 3192 NE ARG B 33 4046 7177 8496 -210 -656 -2677 N ATOM 3193 CZ ARG A 33 40.661 87.566 65.011 1.00 53.27 C ANISOU 3193 CZ ARG B 33 4118 7614 8508 -12 -891 -2618 C ATOM 3194 NH1 ARG A 33 39.612 87.051 65.642 1.00 52.27 N ANISOU 3194 NH1 ARG B 33 4185 7665 8010 158 -967 -2445 N ATOM 3195 NH2 ARG A 33 41.887 87.214 65.389 1.00 55.95 N ANISOU 3195 NH2 ARG B 33 4145 8048 9065 21 -1050 -2711 N ATOM 3196 N TYR A 34 41.782 88.084 58.318 1.00 53.13 N ANISOU 3196 N TYR B 34 5206 5864 9118 -1619 2250 -2532 N ATOM 3197 CA TYR A 34 42.576 87.115 57.581 1.00 54.67 C ANISOU 3197 CA TYR B 34 5312 6103 9355 -1608 2481 -2610 C ATOM 3198 C TYR A 34 43.642 86.530 58.502 1.00 56.31 C ANISOU 3198 C TYR B 34 4965 6510 9920 -1474 2318 -2895 C ATOM 3199 O TYR A 34 44.401 87.277 59.121 1.00 58.56 O ANISOU 3199 O TYR B 34 4879 6842 10528 -1598 2299 -3131 O ATOM 3200 CB TYR A 34 43.230 87.788 56.374 1.00 57.89 C ANISOU 3200 CB TYR B 34 5838 6296 9863 -1906 3020 -2628 C ATOM 3201 CG TYR A 34 42.259 88.405 55.379 1.00 57.34 C ANISOU 3201 CG TYR B 34 6320 6050 9416 -2043 3164 -2270 C ATOM 3202 CD1 TYR A 34 40.993 87.852 55.150 1.00 53.91 C ANISOU 3202 CD1 TYR B 34 6248 5700 8537 -1905 2890 -1971 C ATOM 3203 CD2 TYR A 34 42.619 89.535 54.648 1.00 60.36 C ANISOU 3203 CD2 TYR B 34 6850 6189 9897 -2318 3570 -2206 C ATOM 3204 CE1 TYR A 34 40.118 88.419 54.231 1.00 54.14 C ANISOU 3204 CE1 TYR B 34 6726 5620 8224 -2022 2953 -1599 C ATOM 3205 CE2 TYR A 34 41.750 90.107 53.728 1.00 60.73 C ANISOU 3205 CE2 TYR B 34 7398 6086 9590 -2418 3663 -1797 C ATOM 3206 CZ TYR A 34 40.503 89.547 53.524 1.00 57.54 C ANISOU 3206 CZ TYR B 34 7305 5817 8742 -2262 3321 -1483 C ATOM 3207 OH TYR A 34 39.649 90.118 52.610 1.00 58.50 O ANISOU 3207 OH TYR B 34 7870 5840 8516 -2353 3346 -1035 O ATOM 3208 N LEU A 35 43.690 85.200 58.598 1.00 55.62 N ANISOU 3208 N LEU B 35 4808 6538 9786 -1229 2195 -2863 N ATOM 3209 CA LEU A 35 44.658 84.516 59.452 1.00 57.77 C ANISOU 3209 CA LEU B 35 4540 7002 10407 -1032 1993 -3034 C ATOM 3210 C LEU A 35 45.734 83.823 58.622 1.00 61.21 C ANISOU 3210 C LEU B 35 4729 7343 11187 -1026 2414 -3161 C ATOM 3211 O LEU A 35 45.465 83.330 57.530 1.00 61.08 O ANISOU 3211 O LEU B 35 5064 7151 10994 -1086 2782 -3088 O ATOM 3212 CB LEU A 35 43.963 83.501 60.362 1.00 55.29 C ANISOU 3212 CB LEU B 35 4285 6849 9872 -707 1545 -2871 C ATOM 3213 CG LEU A 35 42.880 84.025 61.321 1.00 52.58 C ANISOU 3213 CG LEU B 35 4164 6605 9207 -693 1148 -2774 C ATOM 3214 CD1 LEU A 35 42.537 82.958 62.354 1.00 51.87 C ANISOU 3214 CD1 LEU B 35 4032 6698 8978 -384 740 -2655 C ATOM 3215 CD2 LEU A 35 43.291 85.305 62.012 1.00 54.18 C ANISOU 3215 CD2 LEU B 35 4125 6887 9573 -912 1051 -2983 C ATOM 3216 N ASP A 49 37.849 97.086 49.374 1.00 81.39 N ANISOU 3216 N ASP B 49 12338 6926 11660 -2762 4467 1538 N ATOM 3217 CA ASP A 49 38.951 97.991 49.070 1.00 85.70 C ANISOU 3217 CA ASP B 49 12958 7075 12528 -3049 5126 1413 C ATOM 3218 C ASP A 49 39.579 98.574 50.340 1.00 84.27 C ANISOU 3218 C ASP B 49 12307 6626 13085 -3054 5343 843 C ATOM 3219 O ASP A 49 39.904 99.763 50.388 1.00 88.24 O ANISOU 3219 O ASP B 49 12846 6645 14035 -3172 5791 901 O ATOM 3220 CB ASP A 49 38.474 99.113 48.141 1.00 91.76 C ANISOU 3220 CB ASP B 49 14184 7466 13215 -3069 5340 2171 C ATOM 3221 N GLN A 50 39.760 97.726 51.354 1.00 79.24 N ANISOU 3221 N GLN B 50 11248 6309 12551 -2954 5035 295 N ATOM 3222 CA GLN A 50 40.401 98.119 52.612 1.00 78.19 C ANISOU 3222 CA GLN B 50 10650 6053 13005 -3007 5153 -302 C ATOM 3223 C GLN A 50 41.512 97.142 53.007 1.00 76.09 C ANISOU 3223 C GLN B 50 10005 6147 12758 -3134 5135 -928 C ATOM 3224 O GLN A 50 41.328 95.923 52.943 1.00 72.82 O ANISOU 3224 O GLN B 50 9561 6131 11977 -2995 4785 -967 O ATOM 3225 CB GLN A 50 39.370 98.190 53.737 1.00 74.95 C ANISOU 3225 CB GLN B 50 10054 5661 12764 -2712 4724 -309 C ATOM 3226 CG GLN A 50 39.873 98.910 54.988 1.00 75.75 C ANISOU 3226 CG GLN B 50 9781 5557 13442 -2829 4906 -854 C ATOM 3227 CD GLN A 50 38.982 98.692 56.197 1.00 72.58 C ANISOU 3227 CD GLN B 50 9183 5282 13112 -2585 4480 -994 C ATOM 3228 OE1 GLN A 50 38.530 97.575 56.451 1.00 68.84 O ANISOU 3228 OE1 GLN B 50 8648 5223 12285 -2384 4006 -1002 O ATOM 3229 NE2 GLN A 50 38.733 99.756 56.949 1.00 74.85 N ANISOU 3229 NE2 GLN B 50 9391 5182 13868 -2627 4705 -1128 N ATOM 3230 N ASP A 51 42.653 97.688 53.431 1.00 78.49 N ANISOU 3230 N ASP B 51 9991 6295 13535 -3396 5521 -1411 N ATOM 3231 CA ASP A 51 43.807 96.884 53.841 1.00 77.70 C ANISOU 3231 CA ASP B 51 9434 6514 13575 -3510 5516 -1989 C ATOM 3232 C ASP A 51 43.525 96.163 55.163 1.00 73.42 C ANISOU 3232 C ASP B 51 8506 6333 13057 -3270 4935 -2291 C ATOM 3233 O ASP A 51 43.067 96.778 56.127 1.00 72.71 O ANISOU 3233 O ASP B 51 8305 6143 13178 -3221 4780 -2394 O ATOM 3234 CB ASP A 51 45.061 97.764 53.984 1.00 82.26 C ANISOU 3234 CB ASP B 51 9717 6840 14697 -3883 6059 -2428 C ATOM 3235 CG ASP A 51 45.584 98.289 52.645 1.00 86.93 C ANISOU 3235 CG ASP B 51 10667 7105 15259 -4168 6712 -2201 C ATOM 3236 OD1 ASP A 51 45.402 97.617 51.607 1.00 85.60 O ANISOU 3236 OD1 ASP B 51 10850 7054 14619 -4133 6745 -1881 O ATOM 3237 OD2 ASP A 51 46.210 99.369 52.539 1.00 92.17 O ANISOU 3237 OD2 ASP B 51 11305 7379 16334 -4475 7256 -2344 O ATOM 3238 N ILE A 52 43.794 94.857 55.190 1.00 71.01 N ANISOU 3238 N ILE B 52 8028 6418 12533 -3131 4661 -2426 N ATOM 3239 CA ILE A 52 43.581 94.024 56.375 1.00 67.36 C ANISOU 3239 CA ILE B 52 7239 6315 12040 -2891 4114 -2654 C ATOM 3240 C ILE A 52 44.888 93.325 56.742 1.00 68.67 C ANISOU 3240 C ILE B 52 6878 6750 12462 -2956 4117 -3111 C ATOM 3241 O ILE A 52 45.477 92.621 55.912 1.00 69.85 O ANISOU 3241 O ILE B 52 7025 6957 12559 -2984 4340 -3115 O ATOM 3242 CB ILE A 52 42.482 92.959 56.107 1.00 63.37 C ANISOU 3242 CB ILE B 52 7031 6015 11032 -2586 3722 -2296 C ATOM 3243 CG1 ILE A 52 41.145 93.623 55.745 1.00 62.89 C ANISOU 3243 CG1 ILE B 52 7410 5729 10757 -2494 3657 -1808 C ATOM 3244 CG2 ILE A 52 42.320 92.018 57.312 1.00 59.84 C ANISOU 3244 CG2 ILE B 52 6277 5914 10546 -2343 3210 -2513 C ATOM 3245 CD1 ILE A 52 40.447 94.317 56.905 1.00 61.95 C ANISOU 3245 CD1 ILE B 52 7182 5502 10854 -2392 3443 -1868 C ATOM 3246 N THR A 53 45.326 93.509 57.987 1.00 68.97 N ANISOU 3246 N THR B 53 6464 6962 12778 -2987 3870 -3492 N ATOM 3247 CA THR A 53 46.541 92.867 58.488 1.00 70.84 C ANISOU 3247 CA THR B 53 6109 7509 13297 -3012 3760 -3890 C ATOM 3248 C THR A 53 46.311 91.374 58.720 1.00 67.64 C ANISOU 3248 C THR B 53 5631 7431 12637 -2648 3332 -3769 C ATOM 3249 O THR A 53 45.283 90.981 59.268 1.00 63.96 O ANISOU 3249 O THR B 53 5384 7074 11844 -2412 2928 -3571 O ATOM 3250 CB THR A 53 47.007 93.529 59.804 1.00 72.93 C ANISOU 3250 CB THR B 53 5928 7930 13852 -3187 3544 -4312 C ATOM 3251 OG1 THR A 53 47.174 94.941 59.615 1.00 76.28 O ANISOU 3251 OG1 THR B 53 6443 7988 14552 -3549 4005 -4455 O ATOM 3252 CG2 THR A 53 48.401 93.042 60.201 1.00 76.42 C ANISOU 3252 CG2 THR B 53 5680 8697 14660 -3264 3453 -4704 C ATOM 3253 N ILE A 54 47.275 90.555 58.305 1.00 69.55 N ANISOU 3253 N ILE B 54 5558 7789 13080 -2609 3473 -3898 N ATOM 3254 CA ILE A 54 47.205 89.106 58.491 1.00 67.63 C ANISOU 3254 CA ILE B 54 5207 7788 12701 -2263 3158 -3800 C ATOM 3255 C ILE A 54 47.716 88.724 59.880 1.00 68.59 C ANISOU 3255 C ILE B 54 4763 8276 13023 -2111 2637 -4013 C ATOM 3256 O ILE A 54 48.884 88.959 60.203 1.00 72.99 O ANISOU 3256 O ILE B 54 4746 8964 14024 -2252 2679 -4326 O ATOM 3257 CB ILE A 54 48.038 88.380 57.404 1.00 70.25 C ANISOU 3257 CB ILE B 54 5440 8026 13227 -2282 3618 -3851 C ATOM 3258 CG1 ILE A 54 47.422 88.598 56.015 1.00 69.77 C ANISOU 3258 CG1 ILE B 54 6032 7672 12804 -2444 4074 -3595 C ATOM 3259 CG2 ILE A 54 48.154 86.884 57.710 1.00 69.21 C ANISOU 3259 CG2 ILE B 54 5091 8095 13110 -1916 3349 -3802 C ATOM 3260 CD1 ILE A 54 48.454 88.803 54.918 1.00 74.44 C ANISOU 3260 CD1 ILE B 54 6559 8056 13669 -2733 4758 -3768 C ATOM 3261 N GLU A 55 46.839 88.137 60.692 1.00 65.06 N ANISOU 3261 N GLU B 55 4474 8011 12236 -1842 2142 -3832 N ATOM 3262 CA GLU A 55 47.207 87.608 62.005 1.00 66.19 C ANISOU 3262 CA GLU B 55 4174 8534 12440 -1665 1595 -3939 C ATOM 3263 C GLU A 55 47.629 86.142 61.899 1.00 66.65 C ANISOU 3263 C GLU B 55 4003 8714 12607 -1309 1481 -3800 C ATOM 3264 O GLU A 55 47.183 85.423 61.004 1.00 64.54 O ANISOU 3264 O GLU B 55 4083 8243 12195 -1170 1738 -3597 O ATOM 3265 CB GLU A 55 46.031 87.730 62.976 1.00 62.79 C ANISOU 3265 CB GLU B 55 4073 8207 11576 -1579 1177 -3813 C ATOM 3266 CG GLU A 55 45.563 89.159 63.207 1.00 63.24 C ANISOU 3266 CG GLU B 55 4338 8100 11591 -1902 1314 -3960 C ATOM 3267 CD GLU A 55 44.102 89.237 63.586 1.00 59.87 C ANISOU 3267 CD GLU B 55 4410 7583 10755 -1790 1144 -3740 C ATOM 3268 OE1 GLU A 55 43.253 88.933 62.726 1.00 57.82 O ANISOU 3268 OE1 GLU B 55 4565 7105 10297 -1655 1305 -3432 O ATOM 3269 OE2 GLU A 55 43.799 89.600 64.740 1.00 61.43 O ANISOU 3269 OE2 GLU B 55 4574 7942 10826 -1864 858 -3891 O ATOM 3270 N GLU A 56 48.488 85.704 62.816 1.00 70.00 N ANISOU 3270 N GLU B 56 3837 9467 13292 -1172 1099 -3905 N ATOM 3271 CA GLU A 56 48.939 84.314 62.843 1.00 71.35 C ANISOU 3271 CA GLU B 56 3727 9723 13658 -781 976 -3735 C ATOM 3272 C GLU A 56 47.797 83.403 63.279 1.00 67.25 C ANISOU 3272 C GLU B 56 3661 9221 12672 -467 666 -3404 C ATOM 3273 O GLU A 56 47.029 83.744 64.183 1.00 65.08 O ANISOU 3273 O GLU B 56 3615 9105 12006 -497 284 -3352 O ATOM 3274 CB GLU A 56 50.133 84.140 63.791 1.00 76.91 C ANISOU 3274 CB GLU B 56 3638 10813 14772 -693 563 -3864 C ATOM 3275 CG GLU A 56 50.642 82.707 63.889 1.00 79.18 C ANISOU 3275 CG GLU B 56 3574 11157 15356 -228 424 -3626 C ATOM 3276 CD GLU A 56 51.966 82.585 64.627 1.00 86.06 C ANISOU 3276 CD GLU B 56 3552 12399 16747 -136 54 -3723 C ATOM 3277 OE1 GLU A 56 52.645 81.552 64.449 1.00 89.21 O ANISOU 3277 OE1 GLU B 56 3529 12753 17613 225 104 -3566 O ATOM 3278 OE2 GLU A 56 52.329 83.511 65.386 1.00 88.11 O ANISOU 3278 OE2 GLU B 56 3510 12995 16973 -430 -282 -3961 O ATOM 3279 N THR A 57 47.689 82.245 62.631 1.00 66.55 N ANISOU 3279 N THR B 57 3705 8941 12641 -197 888 -3216 N ATOM 3280 CA THR A 57 46.714 81.237 63.030 1.00 63.47 C ANISOU 3280 CA THR B 57 3689 8540 11885 104 645 -2920 C ATOM 3281 C THR A 57 47.233 80.525 64.282 1.00 66.55 C ANISOU 3281 C THR B 57 3637 9241 12409 428 102 -2774 C ATOM 3282 O THR A 57 48.250 79.827 64.227 1.00 70.77 O ANISOU 3282 O THR B 57 3661 9793 13436 660 138 -2740 O ATOM 3283 CB THR A 57 46.465 80.215 61.887 1.00 62.55 C ANISOU 3283 CB THR B 57 3868 8091 11808 234 1124 -2815 C ATOM 3284 OG1 THR A 57 46.234 80.898 60.647 1.00 61.33 O ANISOU 3284 OG1 THR B 57 4052 7706 11545 -101 1624 -2947 O ATOM 3285 CG2 THR A 57 45.171 79.443 62.121 1.00 58.62 C ANISOU 3285 CG2 THR B 57 3901 7529 10843 408 964 -2566 C ATOM 3286 N THR A 58 46.548 80.734 65.407 1.00 64.87 N ANISOU 3286 N THR B 58 3611 9270 11767 433 -386 -2677 N ATOM 3287 CA THR A 58 46.905 80.095 66.678 1.00 68.26 C ANISOU 3287 CA THR B 58 3725 10040 12172 710 -963 -2479 C ATOM 3288 C THR A 58 45.676 79.524 67.382 1.00 64.96 C ANISOU 3288 C THR B 58 3847 9627 11207 867 -1214 -2213 C ATOM 3289 O THR A 58 44.547 79.666 66.907 1.00 60.06 O ANISOU 3289 O THR B 58 3786 8765 10271 754 -960 -2213 O ATOM 3290 CB THR A 58 47.626 81.095 67.620 1.00 72.08 C ANISOU 3290 CB THR B 58 3758 10957 12673 452 -1386 -2712 C ATOM 3291 OG1 THR A 58 46.709 82.104 68.065 1.00 68.73 O ANISOU 3291 OG1 THR B 58 3768 10582 11763 117 -1457 -2878 O ATOM 3292 CG2 THR A 58 48.719 81.868 66.891 1.00 75.05 C ANISOU 3292 CG2 THR B 58 3643 11297 13576 195 -1066 -3047 C ATOM 3293 N GLU A 59 45.908 78.893 68.531 1.00 68.29 N ANISOU 3293 N GLU B 59 4083 10343 11522 1118 -1724 -1971 N ATOM 3294 CA GLU A 59 44.848 78.225 69.291 1.00 66.27 C ANISOU 3294 CA GLU B 59 4317 10091 10771 1286 -1947 -1689 C ATOM 3295 C GLU A 59 43.941 79.208 70.043 1.00 63.73 C ANISOU 3295 C GLU B 59 4377 9943 9895 944 -2135 -1861 C ATOM 3296 O GLU A 59 42.844 78.840 70.469 1.00 60.98 O ANISOU 3296 O GLU B 59 4523 9514 9131 994 -2167 -1708 O ATOM 3297 CB GLU A 59 45.457 77.217 70.272 1.00 71.61 C ANISOU 3297 CB GLU B 59 4685 11017 11507 1675 -2421 -1315 C ATOM 3298 CG GLU A 59 46.227 76.082 69.602 1.00 74.58 C ANISOU 3298 CG GLU B 59 4713 11130 12494 2091 -2181 -1088 C ATOM 3299 CD GLU A 59 47.736 76.223 69.729 1.00 81.27 C ANISOU 3299 CD GLU B 59 4732 12249 13900 2188 -2417 -1119 C ATOM 3300 OE1 GLU A 59 48.267 77.297 69.377 1.00 81.04 O ANISOU 3300 OE1 GLU B 59 4410 12348 14034 1839 -2331 -1503 O ATOM 3301 OE2 GLU A 59 48.395 75.257 70.174 1.00 86.61 O ANISOU 3301 OE2 GLU B 59 5025 12992 14892 2620 -2675 -744 O ATOM 3302 N THR A 60 44.399 80.449 70.199 1.00 65.08 N ANISOU 3302 N THR B 60 4310 10316 10103 581 -2202 -2204 N ATOM 3303 CA THR A 60 43.632 81.488 70.888 1.00 63.48 C ANISOU 3303 CA THR B 60 4428 10228 9463 220 -2292 -2434 C ATOM 3304 C THR A 60 43.177 82.604 69.944 1.00 59.95 C ANISOU 3304 C THR B 60 4178 9461 9138 -92 -1810 -2719 C ATOM 3305 O THR A 60 42.583 83.589 70.387 1.00 59.01 O ANISOU 3305 O THR B 60 4286 9352 8785 -398 -1782 -2941 O ATOM 3306 CB THR A 60 44.471 82.086 72.039 1.00 69.02 C ANISOU 3306 CB THR B 60 4735 11443 10046 -7 -2781 -2626 C ATOM 3307 OG1 THR A 60 45.723 82.580 71.538 1.00 71.92 O ANISOU 3307 OG1 THR B 60 4499 11906 10920 -130 -2727 -2853 O ATOM 3308 CG2 THR A 60 44.865 81.005 73.035 1.00 73.47 C ANISOU 3308 CG2 THR B 60 5133 12364 10418 311 -3329 -2259 C ATOM 3309 N ALA A 61 43.426 82.434 68.646 1.00 58.50 N ANISOU 3309 N ALA B 61 3937 8975 9316 -15 -1405 -2694 N ATOM 3310 CA ALA A 61 43.148 83.478 67.656 1.00 56.13 C ANISOU 3310 CA ALA B 61 3797 8383 9148 -297 -958 -2895 C ATOM 3311 C ALA A 61 41.684 83.567 67.217 1.00 51.00 C ANISOU 3311 C ALA B 61 3730 7438 8210 -307 -732 -2767 C ATOM 3312 O ALA A 61 41.328 84.487 66.485 1.00 49.58 O ANISOU 3312 O ALA B 61 3714 7024 8100 -521 -414 -2863 O ATOM 3313 CB ALA A 61 44.042 83.290 66.427 1.00 57.31 C ANISOU 3313 CB ALA B 61 3674 8353 9746 -261 -595 -2924 C ATOM 3314 N PHE A 62 40.841 82.634 67.661 1.00 48.87 N ANISOU 3314 N PHE B 62 3752 7175 7642 -80 -893 -2534 N ATOM 3315 CA PHE A 62 39.453 82.557 67.184 1.00 44.68 C ANISOU 3315 CA PHE B 62 3704 6386 6888 -71 -692 -2403 C ATOM 3316 C PHE A 62 38.415 83.138 68.158 1.00 43.58 C ANISOU 3316 C PHE B 62 3832 6282 6444 -199 -821 -2463 C ATOM 3317 O PHE A 62 37.218 82.893 68.011 1.00 41.08 O ANISOU 3317 O PHE B 62 3861 5800 5949 -147 -727 -2331 O ATOM 3318 CB PHE A 62 39.103 81.101 66.849 1.00 43.33 C ANISOU 3318 CB PHE B 62 3700 6121 6641 223 -662 -2143 C ATOM 3319 CG PHE A 62 39.932 80.518 65.740 1.00 44.02 C ANISOU 3319 CG PHE B 62 3603 6082 7039 319 -401 -2117 C ATOM 3320 CD1 PHE A 62 39.492 80.575 64.423 1.00 42.10 C ANISOU 3320 CD1 PHE B 62 3596 5596 6803 211 -31 -2106 C ATOM 3321 CD2 PHE A 62 41.151 79.908 66.012 1.00 47.73 C ANISOU 3321 CD2 PHE B 62 3655 6683 7796 507 -516 -2098 C ATOM 3322 CE1 PHE A 62 40.254 80.033 63.394 1.00 43.32 C ANISOU 3322 CE1 PHE B 62 3626 5624 7209 247 280 -2128 C ATOM 3323 CE2 PHE A 62 41.923 79.365 64.988 1.00 48.96 C ANISOU 3323 CE2 PHE B 62 3625 6676 8303 590 -191 -2109 C ATOM 3324 CZ PHE A 62 41.474 79.429 63.678 1.00 47.45 C ANISOU 3324 CZ PHE B 62 3724 6225 8079 438 238 -2150 C ATOM 3325 N GLU A 63 38.861 83.917 69.139 1.00 46.24 N ANISOU 3325 N GLU B 63 3999 6833 6737 -397 -1007 -2694 N ATOM 3326 CA GLU A 63 37.937 84.527 70.098 1.00 45.82 C ANISOU 3326 CA GLU B 63 4206 6791 6413 -569 -1050 -2819 C ATOM 3327 C GLU A 63 37.146 85.661 69.441 1.00 43.35 C ANISOU 3327 C GLU B 63 4068 6136 6266 -753 -682 -2913 C ATOM 3328 O GLU A 63 37.726 86.548 68.813 1.00 44.41 O ANISOU 3328 O GLU B 63 4030 6153 6690 -922 -480 -3052 O ATOM 3329 CB GLU A 63 38.691 85.044 71.330 1.00 50.32 C ANISOU 3329 CB GLU B 63 4560 7714 6845 -796 -1335 -3089 C ATOM 3330 CG GLU A 63 37.835 85.094 72.589 1.00 51.87 C ANISOU 3330 CG GLU B 63 5069 8025 6616 -910 -1461 -3163 C ATOM 3331 CD GLU A 63 37.976 83.856 73.458 1.00 54.55 C ANISOU 3331 CD GLU B 63 5463 8672 6592 -687 -1855 -2916 C ATOM 3332 OE1 GLU A 63 37.895 82.730 72.919 1.00 53.81 O ANISOU 3332 OE1 GLU B 63 5406 8478 6560 -345 -1868 -2583 O ATOM 3333 OE2 GLU A 63 38.171 84.013 74.685 1.00 59.03 O ANISOU 3333 OE2 GLU B 63 6058 9574 6797 -875 -2134 -3053 O ATOM 3334 N GLY A 64 35.820 85.609 69.570 1.00 41.24 N ANISOU 3334 N GLY B 64 4366 6452 4853 372 -1080 -1479 N ATOM 3335 CA GLY A 64 34.939 86.609 68.983 1.00 40.64 C ANISOU 3335 CA GLY B 64 4391 6329 4720 352 -1114 -1491 C ATOM 3336 C GLY A 64 34.567 86.381 67.525 1.00 39.61 C ANISOU 3336 C GLY B 64 4314 6131 4605 245 -1025 -1457 C ATOM 3337 O GLY A 64 33.752 87.118 66.975 1.00 39.78 O ANISOU 3337 O GLY B 64 4443 6107 4566 251 -1064 -1477 O ATOM 3338 N VAL A 65 35.151 85.366 66.895 1.00 38.80 N ANISOU 3338 N VAL B 65 4148 6020 4576 166 -920 -1417 N ATOM 3339 CA VAL A 65 34.818 85.024 65.514 1.00 37.70 C ANISOU 3339 CA VAL B 65 4051 5819 4454 70 -828 -1378 C ATOM 3340 C VAL A 65 33.514 84.226 65.507 1.00 36.55 C ANISOU 3340 C VAL B 65 3903 5744 4241 141 -783 -1326 C ATOM 3341 O VAL A 65 33.335 83.322 66.320 1.00 36.29 O ANISOU 3341 O VAL B 65 3808 5799 4181 202 -761 -1294 O ATOM 3342 CB VAL A 65 35.950 84.195 64.848 1.00 37.90 C ANISOU 3342 CB VAL B 65 3994 5826 4579 -34 -736 -1367 C ATOM 3343 CG1 VAL A 65 35.565 83.771 63.423 1.00 36.85 C ANISOU 3343 CG1 VAL B 65 3906 5632 4462 -126 -638 -1319 C ATOM 3344 CG2 VAL A 65 37.260 84.990 64.843 1.00 38.97 C ANISOU 3344 CG2 VAL B 65 4106 5927 4775 -132 -765 -1453 C ATOM 3345 N ASP A 66 32.603 84.584 64.608 1.00 35.82 N ANISOU 3345 N ASP B 66 3891 5611 4108 127 -774 -1332 N ATOM 3346 CA ASP A 66 31.329 83.869 64.442 1.00 35.17 C ANISOU 3346 CA ASP B 66 3790 5610 3962 175 -722 -1311 C ATOM 3347 C ASP A 66 31.395 82.747 63.411 1.00 34.22 C ANISOU 3347 C ASP B 66 3647 5459 3898 89 -598 -1241 C ATOM 3348 O ASP A 66 30.796 81.694 63.611 1.00 33.65 O ANISOU 3348 O ASP B 66 3525 5469 3792 101 -530 -1200 O ATOM 3349 CB ASP A 66 30.224 84.831 64.018 1.00 35.09 C ANISOU 3349 CB ASP B 66 3873 5589 3871 240 -798 -1387 C ATOM 3350 CG ASP A 66 29.968 85.909 65.042 1.00 35.60 C ANISOU 3350 CG ASP B 66 3967 5699 3861 351 -937 -1468 C ATOM 3351 OD1 ASP A 66 29.579 85.582 66.181 1.00 34.46 O ANISOU 3351 OD1 ASP B 66 3734 5693 3665 424 -946 -1480 O ATOM 3352 OD2 ASP A 66 30.127 87.113 64.788 1.00 35.28 O ANISOU 3352 OD2 ASP B 66 4053 5556 3796 367 -1046 -1523 O ATOM 3353 N ILE A 67 32.074 83.009 62.294 1.00 34.04 N ANISOU 3353 N ILE B 67 3674 5316 3945 -7 -569 -1232 N ATOM 3354 CA ILE A 67 32.229 82.052 61.191 1.00 33.24 C ANISOU 3354 CA ILE B 67 3555 5173 3901 -88 -459 -1171 C ATOM 3355 C ILE A 67 33.681 82.055 60.717 1.00 33.64 C ANISOU 3355 C ILE B 67 3581 5155 4047 -197 -426 -1171 C ATOM 3356 O ILE A 67 34.235 83.118 60.457 1.00 33.71 O ANISOU 3356 O ILE B 67 3658 5087 4065 -264 -466 -1223 O ATOM 3357 CB ILE A 67 31.360 82.459 59.976 1.00 32.85 C ANISOU 3357 CB ILE B 67 3610 5047 3824 -103 -448 -1186 C ATOM 3358 CG1 ILE A 67 29.869 82.479 60.308 1.00 33.05 C ANISOU 3358 CG1 ILE B 67 3636 5170 3753 8 -482 -1229 C ATOM 3359 CG2 ILE A 67 31.621 81.530 58.792 1.00 32.04 C ANISOU 3359 CG2 ILE B 67 3493 4891 3789 -190 -336 -1122 C ATOM 3360 CD1 ILE A 67 29.053 83.321 59.320 1.00 33.70 C ANISOU 3360 CD1 ILE B 67 3851 5170 3785 46 -537 -1297 C ATOM 3361 N ALA A 68 34.268 80.869 60.550 1.00 33.70 N ANISOU 3361 N ALA B 68 3500 5194 4111 -221 -355 -1128 N ATOM 3362 CA ALA A 68 35.601 80.727 59.961 1.00 34.48 C ANISOU 3362 CA ALA B 68 3543 5262 4297 -320 -315 -1156 C ATOM 3363 C ALA A 68 35.550 79.842 58.708 1.00 34.47 C ANISOU 3363 C ALA B 68 3537 5225 4336 -382 -217 -1103 C ATOM 3364 O ALA A 68 35.086 78.701 58.767 1.00 34.14 O ANISOU 3364 O ALA B 68 3468 5221 4281 -322 -185 -1040 O ATOM 3365 CB ALA A 68 36.555 80.142 60.969 1.00 34.99 C ANISOU 3365 CB ALA B 68 3496 5409 4391 -260 -352 -1189 C ATOM 3366 N LEU A 69 36.002 80.385 57.581 1.00 34.87 N ANISOU 3366 N LEU B 69 3633 5194 4421 -510 -169 -1130 N ATOM 3367 CA LEU A 69 36.176 79.623 56.353 1.00 35.17 C ANISOU 3367 CA LEU B 69 3657 5198 4506 -579 -76 -1094 C ATOM 3368 C LEU A 69 37.635 79.203 56.245 1.00 36.05 C ANISOU 3368 C LEU B 69 3635 5372 4691 -646 -45 -1162 C ATOM 3369 O LEU A 69 38.518 80.055 56.136 1.00 36.65 O ANISOU 3369 O LEU B 69 3699 5442 4785 -764 -41 -1252 O ATOM 3370 CB LEU A 69 35.795 80.475 55.138 1.00 35.38 C ANISOU 3370 CB LEU B 69 3836 5096 4511 -685 -41 -1095 C ATOM 3371 CG LEU A 69 34.444 81.195 55.197 1.00 36.05 C ANISOU 3371 CG LEU B 69 4068 5119 4511 -605 -104 -1081 C ATOM 3372 CD1 LEU A 69 34.176 81.908 53.882 1.00 37.14 C ANISOU 3372 CD1 LEU B 69 4389 5104 4617 -695 -81 -1090 C ATOM 3373 CD2 LEU A 69 33.311 80.235 55.504 1.00 36.34 C ANISOU 3373 CD2 LEU B 69 4054 5229 4524 -476 -99 -1023 C ATOM 3374 N PHE A 70 37.886 77.897 56.296 1.00 36.08 N ANISOU 3374 N PHE B 70 3545 5441 4724 -572 -32 -1135 N ATOM 3375 CA PHE A 70 39.238 77.363 56.162 1.00 37.40 C ANISOU 3375 CA PHE B 70 3569 5689 4952 -597 -21 -1228 C ATOM 3376 C PHE A 70 39.525 77.089 54.683 1.00 37.85 C ANISOU 3376 C PHE B 70 3617 5714 5052 -717 79 -1228 C ATOM 3377 O PHE A 70 38.714 76.470 53.999 1.00 36.95 O ANISOU 3377 O PHE B 70 3570 5541 4928 -692 120 -1127 O ATOM 3378 CB PHE A 70 39.392 76.070 56.969 1.00 37.50 C ANISOU 3378 CB PHE B 70 3521 5773 4953 -431 -86 -1213 C ATOM 3379 CG PHE A 70 39.642 76.288 58.436 1.00 37.70 C ANISOU 3379 CG PHE B 70 3524 5853 4947 -323 -189 -1262 C ATOM 3380 CD1 PHE A 70 38.681 76.891 59.237 1.00 37.27 C ANISOU 3380 CD1 PHE B 70 3564 5766 4831 -285 -223 -1202 C ATOM 3381 CD2 PHE A 70 40.834 75.877 59.019 1.00 38.70 C ANISOU 3381 CD2 PHE B 70 3533 6073 5100 -246 -259 -1385 C ATOM 3382 CE1 PHE A 70 38.906 77.085 60.591 1.00 38.34 C ANISOU 3382 CE1 PHE B 70 3686 5950 4934 -184 -317 -1244 C ATOM 3383 CE2 PHE A 70 41.069 76.065 60.375 1.00 39.64 C ANISOU 3383 CE2 PHE B 70 3644 6232 5187 -132 -362 -1434 C ATOM 3384 CZ PHE A 70 40.108 76.674 61.163 1.00 39.30 C ANISOU 3384 CZ PHE B 70 3705 6145 5084 -107 -386 -1354 C ATOM 3385 N SER A 71 40.670 77.566 54.203 1.00 39.14 N ANISOU 3385 N SER B 71 3694 5923 5255 -858 123 -1351 N ATOM 3386 CA SER A 71 41.106 77.389 52.816 1.00 39.88 C ANISOU 3386 CA SER B 71 3768 6005 5381 -999 229 -1377 C ATOM 3387 C SER A 71 42.618 77.155 52.782 1.00 41.60 C ANISOU 3387 C SER B 71 3778 6379 5648 -1060 244 -1557 C ATOM 3388 O SER A 71 43.308 77.585 51.863 1.00 42.54 O ANISOU 3388 O SER B 71 3863 6521 5780 -1255 341 -1647 O ATOM 3389 CB SER A 71 40.750 78.618 51.978 1.00 40.08 C ANISOU 3389 CB SER B 71 3965 5895 5367 -1186 298 -1359 C ATOM 3390 OG SER A 71 41.344 79.789 52.519 1.00 42.05 O ANISOU 3390 OG SER B 71 4228 6155 5593 -1301 278 -1460 O ATOM 3391 N ALA A 72 43.117 76.490 53.817 1.00 42.29 N ANISOU 3391 N ALA B 72 3737 6581 5749 -891 143 -1624 N ATOM 3392 CA ALA A 72 44.503 76.073 53.894 1.00 44.02 C ANISOU 3392 CA ALA B 72 3739 6977 6010 -883 123 -1823 C ATOM 3393 C ALA A 72 44.536 74.588 53.508 1.00 43.79 C ANISOU 3393 C ALA B 72 3658 6987 5992 -724 90 -1798 C ATOM 3394 O ALA A 72 43.696 74.135 52.725 1.00 42.94 O ANISOU 3394 O ALA B 72 3665 6774 5875 -728 142 -1648 O ATOM 3395 CB ALA A 72 45.030 76.316 55.299 1.00 44.90 C ANISOU 3395 CB ALA B 72 3768 7174 6118 -768 7 -1930 C ATOM 3396 N GLY A 73 45.499 73.836 54.022 1.00 44.94 N ANISOU 3396 N GLY B 73 3645 7280 6150 -577 -8 -1956 N ATOM 3397 CA GLY A 73 45.536 72.402 53.792 1.00 44.70 C ANISOU 3397 CA GLY B 73 3603 7272 6107 -394 -77 -1938 C ATOM 3398 C GLY A 73 44.830 71.663 54.911 1.00 44.00 C ANISOU 3398 C GLY B 73 3665 7099 5954 -170 -209 -1817 C ATOM 3399 O GLY A 73 44.370 72.279 55.883 1.00 43.59 O ANISOU 3399 O GLY B 73 3694 6994 5873 -155 -242 -1762 O ATOM 3400 N SER A 74 44.748 70.341 54.777 1.00 43.79 N ANISOU 3400 N SER B 74 3691 7056 5890 -5 -285 -1779 N ATOM 3401 CA SER A 74 44.099 69.489 55.777 1.00 43.42 C ANISOU 3401 CA SER B 74 3830 6915 5751 187 -406 -1665 C ATOM 3402 C SER A 74 44.829 69.532 57.127 1.00 44.45 C ANISOU 3402 C SER B 74 3926 7117 5846 349 -557 -1810 C ATOM 3403 O SER A 74 44.209 69.355 58.173 1.00 44.20 O ANISOU 3403 O SER B 74 4061 6997 5734 444 -628 -1711 O ATOM 3404 CB SER A 74 44.000 68.042 55.274 1.00 43.41 C ANISOU 3404 CB SER B 74 3916 6875 5703 319 -466 -1616 C ATOM 3405 OG SER A 74 45.123 67.276 55.690 1.00 46.31 O ANISOU 3405 OG SER B 74 4209 7347 6039 525 -632 -1810 O ATOM 3406 N SER A 75 46.139 69.776 57.095 1.00 45.45 N ANISOU 3406 N SER B 75 3833 7411 6025 373 -602 -2057 N ATOM 3407 CA SER A 75 46.940 69.913 58.316 1.00 46.66 C ANISOU 3407 CA SER B 75 3922 7650 6155 531 -750 -2233 C ATOM 3408 C SER A 75 46.500 71.088 59.210 1.00 45.84 C ANISOU 3408 C SER B 75 3860 7500 6057 442 -716 -2171 C ATOM 3409 O SER A 75 46.444 70.963 60.435 1.00 46.15 O ANISOU 3409 O SER B 75 3996 7506 6034 600 -840 -2174 O ATOM 3410 CB SER A 75 48.416 70.080 57.959 1.00 48.33 C ANISOU 3410 CB SER B 75 3845 8086 6432 534 -778 -2543 C ATOM 3411 OG SER A 75 49.223 69.688 59.046 1.00 50.52 O ANISOU 3411 OG SER B 75 4083 8447 6666 782 -975 -2737 O ATOM 3412 N THR A 76 46.197 72.223 58.585 1.00 44.70 N ANISOU 3412 N THR B 76 3664 7344 5975 195 -558 -2119 N ATOM 3413 CA THR A 76 45.722 73.408 59.294 1.00 43.76 C ANISOU 3413 CA THR B 76 3598 7173 5857 103 -527 -2057 C ATOM 3414 C THR A 76 44.320 73.193 59.869 1.00 42.10 C ANISOU 3414 C THR B 76 3624 6804 5568 160 -536 -1820 C ATOM 3415 O THR A 76 44.037 73.609 60.988 1.00 41.82 O ANISOU 3415 O THR B 76 3656 6741 5492 225 -600 -1797 O ATOM 3416 CB THR A 76 45.736 74.623 58.349 1.00 43.51 C ANISOU 3416 CB THR B 76 3500 7144 5886 -176 -368 -2065 C ATOM 3417 OG1 THR A 76 47.088 74.964 58.021 1.00 44.69 O ANISOU 3417 OG1 THR B 76 3422 7467 6094 -264 -350 -2315 O ATOM 3418 CG2 THR A 76 45.196 75.885 59.032 1.00 43.43 C ANISOU 3418 CG2 THR B 76 3575 7063 5863 -262 -354 -2000 C ATOM 3419 N SER A 77 43.450 72.540 59.105 1.00 40.93 N ANISOU 3419 N SER B 77 3591 6565 5395 130 -470 -1660 N ATOM 3420 CA SER A 77 42.088 72.261 59.555 1.00 39.79 C ANISOU 3420 CA SER B 77 3650 6299 5169 159 -460 -1460 C ATOM 3421 C SER A 77 42.062 71.302 60.750 1.00 40.56 C ANISOU 3421 C SER B 77 3877 6372 5162 360 -598 -1448 C ATOM 3422 O SER A 77 41.396 71.566 61.749 1.00 40.17 O ANISOU 3422 O SER B 77 3940 6278 5044 390 -624 -1376 O ATOM 3423 CB SER A 77 41.263 71.688 58.404 1.00 38.88 C ANISOU 3423 CB SER B 77 3610 6109 5052 81 -360 -1320 C ATOM 3424 OG SER A 77 41.203 72.608 57.328 1.00 38.27 O ANISOU 3424 OG SER B 77 3461 6028 5050 -101 -239 -1323 O ATOM 3425 N ALA A 78 42.810 70.206 60.650 1.00 41.59 N ANISOU 3425 N ALA B 78 4005 6529 5269 502 -695 -1532 N ATOM 3426 CA ALA A 78 42.875 69.190 61.705 1.00 42.51 C ANISOU 3426 CA ALA B 78 4298 6594 5261 707 -848 -1532 C ATOM 3427 C ALA A 78 43.317 69.741 63.075 1.00 43.44 C ANISOU 3427 C ALA B 78 4413 6745 5349 815 -957 -1631 C ATOM 3428 O ALA A 78 42.724 69.408 64.105 1.00 43.16 O ANISOU 3428 O ALA B 78 4581 6624 5195 892 -1017 -1543 O ATOM 3429 CB ALA A 78 43.795 68.056 61.275 1.00 43.70 C ANISOU 3429 CB ALA B 78 4430 6779 5393 864 -962 -1654 C ATOM 3430 N LYS A 79 44.353 70.577 63.077 1.00 44.34 N ANISOU 3430 N LYS B 79 4301 6983 5564 807 -977 -1819 N ATOM 3431 CA LYS A 79 44.890 71.150 64.315 1.00 45.52 C ANISOU 3431 CA LYS B 79 4417 7176 5701 914 -1085 -1938 C ATOM 3432 C LYS A 79 44.010 72.265 64.900 1.00 44.50 C ANISOU 3432 C LYS B 79 4334 7002 5571 792 -1007 -1816 C ATOM 3433 O LYS A 79 43.707 72.252 66.096 1.00 44.76 O ANISOU 3433 O LYS B 79 4500 6988 5519 898 -1089 -1782 O ATOM 3434 CB LYS A 79 46.310 71.691 64.089 1.00 47.00 C ANISOU 3434 CB LYS B 79 4327 7534 5996 924 -1124 -2205 C ATOM 3435 CG LYS A 79 46.930 72.354 65.328 1.00 48.89 C ANISOU 3435 CG LYS B 79 4507 7832 6237 1032 -1236 -2350 C ATOM 3436 CD LYS A 79 48.423 72.629 65.155 1.00 51.43 C ANISOU 3436 CD LYS B 79 4548 8347 6646 1072 -1297 -2659 C ATOM 3437 CE LYS A 79 48.979 73.390 66.352 1.00 52.98 C ANISOU 3437 CE LYS B 79 4676 8601 6853 1159 -1397 -2802 C ATOM 3438 NZ LYS A 79 50.468 73.535 66.315 1.00 55.26 N ANISOU 3438 NZ LYS B 79 4684 9102 7212 1227 -1477 -3143 N ATOM 3439 N TYR A 80 43.606 73.215 64.059 1.00 43.36 N ANISOU 3439 N TYR B 80 4097 6868 5508 580 -860 -1760 N ATOM 3440 CA TYR A 80 43.004 74.472 64.525 1.00 42.88 C ANISOU 3440 CA TYR B 80 4045 6788 5459 477 -811 -1702 C ATOM 3441 C TYR A 80 41.476 74.539 64.492 1.00 41.32 C ANISOU 3441 C TYR B 80 4011 6495 5192 402 -727 -1496 C ATOM 3442 O TYR A 80 40.887 75.287 65.267 1.00 41.25 O ANISOU 3442 O TYR B 80 4053 6472 5148 396 -737 -1453 O ATOM 3443 CB TYR A 80 43.562 75.649 63.724 1.00 43.09 C ANISOU 3443 CB TYR B 80 3901 6877 5595 294 -725 -1798 C ATOM 3444 CG TYR A 80 45.029 75.911 63.970 1.00 44.84 C ANISOU 3444 CG TYR B 80 3929 7228 5880 332 -796 -2037 C ATOM 3445 CD1 TYR A 80 45.485 76.319 65.222 1.00 46.14 C ANISOU 3445 CD1 TYR B 80 4069 7433 6031 452 -912 -2137 C ATOM 3446 CD2 TYR A 80 45.961 75.768 62.947 1.00 46.30 C ANISOU 3446 CD2 TYR B 80 3943 7512 6136 244 -745 -2182 C ATOM 3447 CE1 TYR A 80 46.834 76.569 65.447 1.00 47.77 C ANISOU 3447 CE1 TYR B 80 4076 7777 6297 489 -979 -2384 C ATOM 3448 CE2 TYR A 80 47.308 76.016 63.162 1.00 47.83 C ANISOU 3448 CE2 TYR B 80 3928 7861 6383 266 -803 -2437 C ATOM 3449 CZ TYR A 80 47.737 76.412 64.412 1.00 48.54 C ANISOU 3449 CZ TYR B 80 3989 7990 6462 391 -922 -2542 C ATOM 3450 OH TYR A 80 49.068 76.656 64.620 1.00 50.92 O ANISOU 3450 OH TYR B 80 4066 8462 6818 415 -980 -2820 O ATOM 3451 N ALA A 81 40.833 73.792 63.597 1.00 40.22 N ANISOU 3451 N ALA B 81 3940 6305 5034 348 -649 -1386 N ATOM 3452 CA ALA A 81 39.370 73.792 63.524 1.00 38.77 C ANISOU 3452 CA ALA B 81 3890 6059 4784 277 -568 -1221 C ATOM 3453 C ALA A 81 38.692 73.372 64.841 1.00 38.87 C ANISOU 3453 C ALA B 81 4058 6046 4663 371 -626 -1157 C ATOM 3454 O ALA A 81 37.684 73.973 65.214 1.00 38.24 O ANISOU 3454 O ALA B 81 4024 5968 4537 317 -582 -1092 O ATOM 3455 CB ALA A 81 38.868 72.933 62.365 1.00 38.03 C ANISOU 3455 CB ALA B 81 3840 5920 4690 214 -483 -1130 C ATOM 3456 N PRO A 82 39.224 72.367 65.545 1.00 39.66 N ANISOU 3456 N PRO B 82 4255 6126 4688 512 -730 -1186 N ATOM 3457 CA PRO A 82 38.681 71.997 66.864 1.00 40.20 C ANISOU 3457 CA PRO B 82 4504 6159 4610 590 -787 -1135 C ATOM 3458 C PRO A 82 38.793 73.114 67.900 1.00 40.58 C ANISOU 3458 C PRO B 82 4496 6253 4668 627 -838 -1195 C ATOM 3459 O PRO A 82 37.951 73.186 68.794 1.00 40.31 O ANISOU 3459 O PRO B 82 4582 6211 4525 625 -831 -1130 O ATOM 3460 CB PRO A 82 39.538 70.793 67.283 1.00 41.36 C ANISOU 3460 CB PRO B 82 4775 6257 4683 757 -921 -1192 C ATOM 3461 CG PRO A 82 40.159 70.289 66.016 1.00 41.25 C ANISOU 3461 CG PRO B 82 4660 6254 4758 748 -905 -1235 C ATOM 3462 CD PRO A 82 40.354 71.498 65.163 1.00 40.42 C ANISOU 3462 CD PRO B 82 4318 6228 4813 618 -811 -1283 C ATOM 3463 N TYR A 83 39.822 73.954 67.788 1.00 41.16 N ANISOU 3463 N TYR B 83 4393 6383 4863 652 -885 -1326 N ATOM 3464 CA TYR A 83 39.981 75.105 68.677 1.00 41.75 C ANISOU 3464 CA TYR B 83 4406 6499 4959 678 -936 -1388 C ATOM 3465 C TYR A 83 39.040 76.251 68.328 1.00 40.64 C ANISOU 3465 C TYR B 83 4224 6371 4845 538 -842 -1325 C ATOM 3466 O TYR A 83 38.630 76.997 69.218 1.00 40.69 O ANISOU 3466 O TYR B 83 4253 6396 4810 565 -876 -1323 O ATOM 3467 CB TYR A 83 41.434 75.592 68.702 1.00 42.81 C ANISOU 3467 CB TYR B 83 4369 6696 5202 738 -1019 -1570 C ATOM 3468 CG TYR A 83 42.328 74.684 69.508 1.00 45.27 C ANISOU 3468 CG TYR B 83 4733 7007 5461 943 -1166 -1674 C ATOM 3469 CD1 TYR A 83 42.612 74.955 70.843 1.00 47.65 C ANISOU 3469 CD1 TYR B 83 5082 7310 5711 1084 -1285 -1737 C ATOM 3470 CD2 TYR A 83 42.868 73.536 68.940 1.00 46.82 C ANISOU 3470 CD2 TYR B 83 4951 7192 5646 1015 -1203 -1717 C ATOM 3471 CE1 TYR A 83 43.430 74.106 71.588 1.00 49.93 C ANISOU 3471 CE1 TYR B 83 5452 7584 5937 1299 -1442 -1847 C ATOM 3472 CE2 TYR A 83 43.678 72.687 69.667 1.00 49.34 C ANISOU 3472 CE2 TYR B 83 5349 7500 5897 1234 -1367 -1831 C ATOM 3473 CZ TYR A 83 43.957 72.971 70.988 1.00 50.63 C ANISOU 3473 CZ TYR B 83 5573 7657 6007 1378 -1488 -1898 C ATOM 3474 OH TYR A 83 44.766 72.114 71.700 1.00 53.52 O ANISOU 3474 OH TYR B 83 6045 7998 6292 1620 -1672 -2027 O ATOM 3475 N ALA A 84 38.701 76.398 67.047 1.00 39.77 N ANISOU 3475 N ALA B 84 4067 6249 4795 406 -738 -1283 N ATOM 3476 CA ALA A 84 37.699 77.379 66.638 1.00 38.90 C ANISOU 3476 CA ALA B 84 3959 6134 4686 298 -668 -1230 C ATOM 3477 C ALA A 84 36.346 77.022 67.249 1.00 38.71 C ANISOU 3477 C ALA B 84 4053 6119 4534 314 -640 -1135 C ATOM 3478 O ALA A 84 35.644 77.894 67.758 1.00 38.69 O ANISOU 3478 O ALA B 84 4058 6150 4492 314 -653 -1138 O ATOM 3479 CB ALA A 84 37.596 77.460 65.119 1.00 38.21 C ANISOU 3479 CB ALA B 84 3833 6015 4671 169 -571 -1207 C ATOM 3480 N VAL A 85 35.998 75.736 67.228 1.00 38.73 N ANISOU 3480 N VAL B 85 4153 6101 4462 323 -606 -1064 N ATOM 3481 CA VAL A 85 34.716 75.273 67.763 1.00 38.68 C ANISOU 3481 CA VAL B 85 4262 6118 4317 297 -555 -987 C ATOM 3482 C VAL A 85 34.658 75.496 69.272 1.00 39.65 C ANISOU 3482 C VAL B 85 4449 6275 4343 382 -630 -1011 C ATOM 3483 O VAL A 85 33.615 75.873 69.813 1.00 39.49 O ANISOU 3483 O VAL B 85 4453 6318 4233 351 -597 -997 O ATOM 3484 CB VAL A 85 34.475 73.780 67.436 1.00 38.76 C ANISOU 3484 CB VAL B 85 4396 6081 4251 268 -505 -908 C ATOM 3485 CG1 VAL A 85 33.250 73.244 68.165 1.00 39.46 C ANISOU 3485 CG1 VAL B 85 4621 6204 4170 211 -446 -846 C ATOM 3486 CG2 VAL A 85 34.317 73.587 65.942 1.00 37.69 C ANISOU 3486 CG2 VAL B 85 4198 5921 4202 180 -420 -876 C ATOM 3487 N LYS A 86 35.786 75.256 69.938 1.00 40.68 N ANISOU 3487 N LYS B 86 4600 6371 4486 498 -736 -1065 N ATOM 3488 CA LYS A 86 35.928 75.497 71.374 1.00 41.78 C ANISOU 3488 CA LYS B 86 4804 6525 4544 602 -826 -1099 C ATOM 3489 C LYS A 86 35.652 76.966 71.704 1.00 41.43 C ANISOU 3489 C LYS B 86 4648 6548 4548 599 -846 -1148 C ATOM 3490 O LYS A 86 35.017 77.275 72.708 1.00 41.90 O ANISOU 3490 O LYS B 86 4760 6653 4507 627 -864 -1143 O ATOM 3491 CB LYS A 86 37.347 75.120 71.841 1.00 42.82 C ANISOU 3491 CB LYS B 86 4946 6612 4712 751 -957 -1185 C ATOM 3492 CG LYS A 86 37.407 74.267 73.101 1.00 44.61 C ANISOU 3492 CG LYS B 86 5384 6787 4779 866 -1041 -1174 C ATOM 3493 CD LYS A 86 37.462 75.111 74.357 1.00 45.52 C ANISOU 3493 CD LYS B 86 5494 6937 4863 953 -1119 -1224 C ATOM 3494 CE LYS A 86 37.378 74.249 75.613 1.00 47.39 C ANISOU 3494 CE LYS B 86 5986 7109 4913 1049 -1189 -1201 C ATOM 3495 NZ LYS A 86 37.020 75.056 76.819 1.00 47.73 N ANISOU 3495 NZ LYS B 86 6042 7199 4894 1093 -1226 -1218 N ATOM 3496 N ALA A 87 36.138 77.855 70.839 1.00 40.92 N ANISOU 3496 N ALA B 87 4444 6484 4621 557 -846 -1199 N ATOM 3497 CA ALA A 87 36.028 79.299 71.028 1.00 40.60 C ANISOU 3497 CA ALA B 87 4325 6476 4623 554 -886 -1253 C ATOM 3498 C ALA A 87 34.650 79.863 70.669 1.00 39.86 C ANISOU 3498 C ALA B 87 4243 6426 4476 484 -823 -1216 C ATOM 3499 O ALA A 87 34.376 81.026 70.952 1.00 40.26 O ANISOU 3499 O ALA B 87 4266 6504 4527 505 -876 -1263 O ATOM 3500 CB ALA A 87 37.117 80.017 70.222 1.00 40.50 C ANISOU 3500 CB ALA B 87 4200 6434 4754 508 -906 -1330 C ATOM 3501 N GLY A 88 33.796 79.048 70.049 1.00 39.35 N ANISOU 3501 N GLY B 88 4221 6370 4359 411 -722 -1149 N ATOM 3502 CA GLY A 88 32.426 79.431 69.732 1.00 38.79 C ANISOU 3502 CA GLY B 88 4149 6367 4225 361 -665 -1144 C ATOM 3503 C GLY A 88 32.146 79.651 68.251 1.00 37.77 C ANISOU 3503 C GLY B 88 3987 6195 4168 279 -605 -1137 C ATOM 3504 O GLY A 88 31.051 80.069 67.887 1.00 37.49 O ANISOU 3504 O GLY B 88 3946 6213 4086 260 -579 -1161 O ATOM 3505 N VAL A 89 33.125 79.365 67.397 1.00 37.31 N ANISOU 3505 N VAL B 89 3908 6051 4216 238 -589 -1121 N ATOM 3506 CA VAL A 89 32.997 79.601 65.959 1.00 36.63 C ANISOU 3506 CA VAL B 89 3809 5909 4200 155 -532 -1113 C ATOM 3507 C VAL A 89 32.212 78.473 65.289 1.00 35.92 C ANISOU 3507 C VAL B 89 3747 5830 4073 101 -429 -1045 C ATOM 3508 O VAL A 89 32.154 77.350 65.809 1.00 36.29 O ANISOU 3508 O VAL B 89 3832 5898 4058 108 -399 -996 O ATOM 3509 CB VAL A 89 34.387 79.700 65.269 1.00 36.92 C ANISOU 3509 CB VAL B 89 3802 5869 4358 109 -539 -1137 C ATOM 3510 CG1 VAL A 89 34.245 80.103 63.802 1.00 36.75 C ANISOU 3510 CG1 VAL B 89 3794 5777 4392 9 -481 -1133 C ATOM 3511 CG2 VAL A 89 35.315 80.675 66.006 1.00 38.24 C ANISOU 3511 CG2 VAL B 89 3932 6036 4562 145 -634 -1217 C ATOM 3512 N VAL A 90 31.597 78.789 64.146 1.00 34.83 N ANISOU 3512 N VAL B 90 3610 5665 3960 48 -383 -1047 N ATOM 3513 CA VAL A 90 31.114 77.782 63.205 1.00 34.07 C ANISOU 3513 CA VAL B 90 3527 5553 3866 -14 -285 -988 C ATOM 3514 C VAL A 90 32.085 77.716 62.031 1.00 33.28 C ANISOU 3514 C VAL B 90 3413 5349 3881 -68 -261 -970 C ATOM 3515 O VAL A 90 32.261 78.689 61.302 1.00 33.02 O ANISOU 3515 O VAL B 90 3390 5257 3899 -99 -278 -1010 O ATOM 3516 CB VAL A 90 29.708 78.102 62.650 1.00 33.75 C ANISOU 3516 CB VAL B 90 3492 5562 3770 -25 -250 -1022 C ATOM 3517 CG1 VAL A 90 29.150 76.894 61.902 1.00 33.43 C ANISOU 3517 CG1 VAL B 90 3461 5525 3717 -91 -144 -961 C ATOM 3518 CG2 VAL A 90 28.772 78.527 63.770 1.00 35.13 C ANISOU 3518 CG2 VAL B 90 3651 5866 3830 31 -287 -1087 C ATOM 3519 N VAL A 91 32.700 76.557 61.851 1.00 32.81 N ANISOU 3519 N VAL B 91 3350 5269 3848 -82 -225 -918 N ATOM 3520 CA VAL A 91 33.716 76.356 60.830 1.00 32.49 C ANISOU 3520 CA VAL B 91 3273 5161 3910 -129 -202 -918 C ATOM 3521 C VAL A 91 33.111 75.772 59.553 1.00 31.99 C ANISOU 3521 C VAL B 91 3234 5056 3865 -188 -114 -862 C ATOM 3522 O VAL A 91 32.327 74.825 59.607 1.00 31.54 O ANISOU 3522 O VAL B 91 3215 5023 3746 -186 -70 -804 O ATOM 3523 CB VAL A 91 34.815 75.409 61.349 1.00 32.92 C ANISOU 3523 CB VAL B 91 3305 5226 3979 -75 -240 -922 C ATOM 3524 CG1 VAL A 91 35.833 75.095 60.250 1.00 32.64 C ANISOU 3524 CG1 VAL B 91 3205 5155 4042 -120 -212 -947 C ATOM 3525 CG2 VAL A 91 35.496 76.022 62.568 1.00 33.72 C ANISOU 3525 CG2 VAL B 91 3377 5364 4072 -4 -335 -994 C ATOM 3526 N VAL A 92 33.467 76.361 58.416 1.00 31.80 N ANISOU 3526 N VAL B 92 3200 4966 3916 -254 -86 -884 N ATOM 3527 CA VAL A 92 33.244 75.757 57.114 1.00 31.69 C ANISOU 3527 CA VAL B 92 3202 4899 3940 -306 -9 -837 C ATOM 3528 C VAL A 92 34.616 75.371 56.583 1.00 32.35 C ANISOU 3528 C VAL B 92 3222 4963 4107 -344 3 -857 C ATOM 3529 O VAL A 92 35.419 76.237 56.285 1.00 32.85 O ANISOU 3529 O VAL B 92 3258 5005 4219 -407 -4 -924 O ATOM 3530 CB VAL A 92 32.554 76.733 56.148 1.00 31.27 C ANISOU 3530 CB VAL B 92 3213 4779 3890 -349 10 -859 C ATOM 3531 CG1 VAL A 92 32.353 76.091 54.782 1.00 31.04 C ANISOU 3531 CG1 VAL B 92 3205 4688 3902 -396 89 -811 C ATOM 3532 CG2 VAL A 92 31.217 77.186 56.732 1.00 31.50 C ANISOU 3532 CG2 VAL B 92 3279 4859 3829 -286 -24 -884 C ATOM 3533 N ASP A 93 34.883 74.070 56.503 1.00 32.86 N ANISOU 3533 N ASP B 93 3270 5043 4173 -309 17 -813 N ATOM 3534 CA ASP A 93 36.186 73.551 56.099 1.00 33.84 C ANISOU 3534 CA ASP B 93 3314 5180 4362 -310 8 -860 C ATOM 3535 C ASP A 93 36.215 73.191 54.616 1.00 33.89 C ANISOU 3535 C ASP B 93 3315 5137 4424 -381 88 -831 C ATOM 3536 O ASP A 93 35.362 72.458 54.140 1.00 33.27 O ANISOU 3536 O ASP B 93 3297 5024 4321 -371 129 -745 O ATOM 3537 CB ASP A 93 36.534 72.307 56.920 1.00 34.29 C ANISOU 3537 CB ASP B 93 3386 5273 4370 -198 -58 -846 C ATOM 3538 CG ASP A 93 37.959 71.837 56.689 1.00 35.19 C ANISOU 3538 CG ASP B 93 3402 5430 4541 -156 -103 -941 C ATOM 3539 OD1 ASP A 93 38.855 72.702 56.629 1.00 37.30 O ANISOU 3539 OD1 ASP B 93 3560 5742 4870 -203 -109 -1053 O ATOM 3540 OD2 ASP A 93 38.277 70.638 56.557 1.00 33.77 O ANISOU 3540 OD2 ASP B 93 3244 5249 4339 -77 -140 -930 O ATOM 3541 N ASN A 94 37.221 73.686 53.901 1.00 35.02 N ANISOU 3541 N ASN B 94 3383 5285 4636 -462 116 -911 N ATOM 3542 CA ASN A 94 37.377 73.385 52.476 1.00 35.23 C ANISOU 3542 CA ASN B 94 3402 5271 4712 -539 196 -896 C ATOM 3543 C ASN A 94 37.940 71.986 52.207 1.00 35.11 C ANISOU 3543 C ASN B 94 3326 5300 4715 -463 179 -892 C ATOM 3544 O ASN A 94 37.607 71.372 51.185 1.00 35.26 O ANISOU 3544 O ASN B 94 3373 5273 4751 -480 234 -831 O ATOM 3545 CB ASN A 94 38.279 74.427 51.801 1.00 36.36 C ANISOU 3545 CB ASN B 94 3500 5412 4902 -686 245 -997 C ATOM 3546 CG ASN A 94 39.757 74.152 52.022 1.00 39.01 C ANISOU 3546 CG ASN B 94 3672 5869 5280 -691 220 -1133 C ATOM 3547 OD1 ASN A 94 40.244 74.211 53.150 1.00 42.97 O ANISOU 3547 OD1 ASN B 94 4110 6445 5771 -615 139 -1201 O ATOM 3548 ND2 ASN A 94 40.478 73.852 50.943 1.00 41.81 N ANISOU 3548 ND2 ASN B 94 3950 6255 5679 -774 287 -1190 N ATOM 3549 N THR A 95 38.766 71.484 53.127 1.00 35.24 N ANISOU 3549 N THR B 95 3274 5397 4718 -362 90 -964 N ATOM 3550 CA THR A 95 39.577 70.285 52.887 1.00 35.15 C ANISOU 3550 CA THR B 95 3201 5439 4716 -269 40 -1011 C ATOM 3551 C THR A 95 38.794 68.982 53.002 1.00 34.35 C ANISOU 3551 C THR B 95 3231 5276 4545 -167 6 -888 C ATOM 3552 O THR A 95 37.592 68.976 53.304 1.00 33.43 O ANISOU 3552 O THR B 95 3234 5094 4373 -184 35 -772 O ATOM 3553 CB THR A 95 40.789 70.208 53.869 1.00 36.68 C ANISOU 3553 CB THR B 95 3290 5742 4905 -166 -73 -1166 C ATOM 3554 OG1 THR A 95 40.344 69.796 55.169 1.00 35.81 O ANISOU 3554 OG1 THR B 95 3292 5605 4708 -39 -169 -1115 O ATOM 3555 CG2 THR A 95 41.445 71.573 54.099 1.00 37.42 C ANISOU 3555 CG2 THR B 95 3272 5898 5046 -276 -47 -1289 C ATOM 3556 N SER A 96 39.517 67.884 52.786 1.00 34.33 N ANISOU 3556 N SER B 96 3205 5306 4535 -63 -63 -933 N ATOM 3557 CA SER A 96 38.978 66.531 52.848 1.00 34.08 C ANISOU 3557 CA SER B 96 3323 5205 4420 33 -114 -830 C ATOM 3558 C SER A 96 39.015 65.906 54.247 1.00 34.59 C ANISOU 3558 C SER B 96 3519 5255 4369 168 -244 -831 C ATOM 3559 O SER A 96 38.453 64.831 54.454 1.00 34.61 O ANISOU 3559 O SER B 96 3701 5179 4270 221 -285 -735 O ATOM 3560 CB SER A 96 39.770 65.633 51.893 1.00 34.35 C ANISOU 3560 CB SER B 96 3296 5270 4487 99 -148 -888 C ATOM 3561 OG SER A 96 41.080 65.415 52.386 1.00 35.97 O ANISOU 3561 OG SER B 96 3399 5580 4690 229 -274 -1064 O ATOM 3562 N TYR A 97 39.671 66.571 55.197 1.00 34.96 N ANISOU 3562 N TYR B 97 3497 5367 4419 214 -309 -941 N ATOM 3563 CA TYR A 97 39.977 65.970 56.498 1.00 35.70 C ANISOU 3563 CA TYR B 97 3714 5449 4402 370 -457 -977 C ATOM 3564 C TYR A 97 38.758 65.519 57.316 1.00 35.42 C ANISOU 3564 C TYR B 97 3915 5312 4231 351 -449 -824 C ATOM 3565 O TYR A 97 38.797 64.456 57.938 1.00 35.78 O ANISOU 3565 O TYR B 97 4156 5291 4146 463 -558 -802 O ATOM 3566 CB TYR A 97 40.813 66.927 57.344 1.00 36.49 C ANISOU 3566 CB TYR B 97 3682 5641 4541 409 -514 -1124 C ATOM 3567 CG TYR A 97 41.333 66.289 58.613 1.00 37.37 C ANISOU 3567 CG TYR B 97 3914 5741 4542 603 -689 -1195 C ATOM 3568 CD1 TYR A 97 42.457 65.464 58.590 1.00 38.58 C ANISOU 3568 CD1 TYR B 97 4043 5940 4674 787 -840 -1346 C ATOM 3569 CD2 TYR A 97 40.686 66.490 59.831 1.00 37.18 C ANISOU 3569 CD2 TYR B 97 4041 5662 4423 613 -713 -1124 C ATOM 3570 CE1 TYR A 97 42.940 64.870 59.756 1.00 40.38 C ANISOU 3570 CE1 TYR B 97 4418 6141 4785 993 -1026 -1426 C ATOM 3571 CE2 TYR A 97 41.156 65.899 61.003 1.00 38.96 C ANISOU 3571 CE2 TYR B 97 4415 5857 4531 794 -879 -1187 C ATOM 3572 CZ TYR A 97 42.282 65.092 60.959 1.00 40.67 C ANISOU 3572 CZ TYR B 97 4628 6100 4724 990 -1042 -1338 C ATOM 3573 OH TYR A 97 42.751 64.516 62.114 1.00 44.05 O ANISOU 3573 OH TYR B 97 5235 6481 5023 1193 -1228 -1415 O ATOM 3574 N PHE A 98 37.699 66.331 57.323 1.00 34.51 N ANISOU 3574 N PHE B 98 3791 5189 4131 208 -326 -737 N ATOM 3575 CA PHE A 98 36.492 66.050 58.115 1.00 34.56 C ANISOU 3575 CA PHE B 98 3982 5143 4009 157 -294 -622 C ATOM 3576 C PHE A 98 35.311 65.473 57.310 1.00 33.85 C ANISOU 3576 C PHE B 98 3975 4999 3886 44 -183 -497 C ATOM 3577 O PHE A 98 34.259 65.189 57.876 1.00 33.84 O ANISOU 3577 O PHE B 98 4111 4976 3769 -28 -137 -420 O ATOM 3578 CB PHE A 98 36.016 67.327 58.825 1.00 34.33 C ANISOU 3578 CB PHE B 98 3882 5167 3995 94 -248 -640 C ATOM 3579 CG PHE A 98 36.909 67.780 59.951 1.00 34.99 C ANISOU 3579 CG PHE B 98 3936 5290 4068 202 -361 -743 C ATOM 3580 CD1 PHE A 98 37.627 68.962 59.850 1.00 35.00 C ANISOU 3580 CD1 PHE B 98 3750 5362 4188 193 -363 -849 C ATOM 3581 CD2 PHE A 98 37.008 67.038 61.121 1.00 36.36 C ANISOU 3581 CD2 PHE B 98 4292 5422 4100 302 -465 -738 C ATOM 3582 CE1 PHE A 98 38.446 69.384 60.891 1.00 36.23 C ANISOU 3582 CE1 PHE B 98 3868 5561 4337 292 -468 -955 C ATOM 3583 CE2 PHE A 98 37.820 67.455 62.160 1.00 37.38 C ANISOU 3583 CE2 PHE B 98 4398 5585 4220 418 -577 -842 C ATOM 3584 CZ PHE A 98 38.542 68.633 62.044 1.00 37.22 C ANISOU 3584 CZ PHE B 98 4157 5650 4335 417 -578 -954 C ATOM 3585 N ARG A 99 35.474 65.297 56.004 1.00 33.40 N ANISOU 3585 N ARG B 99 3833 4932 3924 19 -136 -488 N ATOM 3586 CA ARG A 99 34.352 64.915 55.133 1.00 32.64 C ANISOU 3586 CA ARG B 99 3786 4796 3821 -87 -25 -385 C ATOM 3587 C ARG A 99 33.639 63.601 55.469 1.00 33.39 C ANISOU 3587 C ARG B 99 4107 4819 3762 -108 -35 -288 C ATOM 3588 O ARG A 99 32.444 63.461 55.196 1.00 32.81 O ANISOU 3588 O ARG B 99 4078 4739 3648 -226 70 -218 O ATOM 3589 CB ARG A 99 34.822 64.837 53.691 1.00 31.90 C ANISOU 3589 CB ARG B 99 3580 4692 3848 -88 8 -397 C ATOM 3590 CG ARG A 99 35.129 66.170 53.092 1.00 31.27 C ANISOU 3590 CG ARG B 99 3321 4660 3899 -143 68 -466 C ATOM 3591 CD ARG A 99 35.385 66.094 51.617 1.00 29.97 C ANISOU 3591 CD ARG B 99 3079 4477 3833 -177 126 -465 C ATOM 3592 NE ARG A 99 35.865 67.365 51.104 1.00 29.82 N ANISOU 3592 NE ARG B 99 2927 4489 3912 -246 176 -545 N ATOM 3593 CZ ARG A 99 36.655 67.507 50.049 1.00 30.50 C ANISOU 3593 CZ ARG B 99 2917 4590 4083 -277 207 -601 C ATOM 3594 NH1 ARG A 99 37.077 66.452 49.356 1.00 29.39 N ANISOU 3594 NH1 ARG B 99 2769 4445 3954 -222 187 -592 N ATOM 3595 NH2 ARG A 99 37.026 68.726 49.682 1.00 31.15 N ANISOU 3595 NH2 ARG B 99 2921 4689 4227 -373 260 -672 N ATOM 3596 N GLN A 100 34.372 62.636 56.021 1.00 34.87 N ANISOU 3596 N GLN B 100 4447 4950 3853 6 -164 -298 N ATOM 3597 CA GLN A 100 33.826 61.306 56.312 1.00 36.04 C ANISOU 3597 CA GLN B 100 4868 4998 3828 -18 -191 -207 C ATOM 3598 C GLN A 100 33.706 61.057 57.817 1.00 37.01 C ANISOU 3598 C GLN B 100 5203 5087 3773 -7 -258 -203 C ATOM 3599 O GLN A 100 33.541 59.916 58.263 1.00 37.86 O ANISOU 3599 O GLN B 100 5597 5087 3701 -6 -320 -146 O ATOM 3600 CB GLN A 100 34.690 60.224 55.657 1.00 36.85 C ANISOU 3600 CB GLN B 100 5052 5028 3922 114 -309 -216 C ATOM 3601 CG GLN A 100 34.847 60.380 54.133 1.00 37.29 C ANISOU 3601 CG GLN B 100 4911 5116 4143 101 -242 -220 C ATOM 3602 CD GLN A 100 33.528 60.276 53.359 1.00 38.53 C ANISOU 3602 CD GLN B 100 5080 5251 4310 -65 -87 -112 C ATOM 3603 OE1 GLN A 100 33.357 60.934 52.328 1.00 39.52 O ANISOU 3603 OE1 GLN B 100 5018 5419 4578 -113 7 -120 O ATOM 3604 NE2 GLN A 100 32.610 59.442 53.841 1.00 40.68 N ANISOU 3604 NE2 GLN B 100 5581 5455 4419 -157 -63 -24 N ATOM 3605 N ASN A 101 33.804 62.138 58.587 1.00 36.54 N ANISOU 3605 N ASN B 101 5024 5108 3753 -1 -250 -265 N ATOM 3606 CA ASN A 101 33.540 62.128 60.018 1.00 37.37 C ANISOU 3606 CA ASN B 101 5300 5200 3700 -12 -285 -263 C ATOM 3607 C ASN A 101 32.019 62.201 60.180 1.00 36.95 C ANISOU 3607 C ASN B 101 5296 5186 3559 -223 -124 -190 C ATOM 3608 O ASN A 101 31.398 63.109 59.647 1.00 35.44 O ANISOU 3608 O ASN B 101 4891 5092 3483 -304 -11 -206 O ATOM 3609 CB ASN A 101 34.235 63.337 60.670 1.00 37.22 C ANISOU 3609 CB ASN B 101 5099 5265 3776 79 -336 -367 C ATOM 3610 CG ASN A 101 34.202 63.302 62.196 1.00 38.24 C ANISOU 3610 CG ASN B 101 5410 5372 3747 111 -404 -380 C ATOM 3611 OD1 ASN A 101 33.185 62.988 62.797 1.00 37.84 O ANISOU 3611 OD1 ASN B 101 5529 5306 3544 -21 -329 -310 O ATOM 3612 ND2 ASN A 101 35.323 63.650 62.824 1.00 38.65 N ANISOU 3612 ND2 ASN B 101 5419 5433 3833 281 -543 -482 N ATOM 3613 N PRO A 102 31.409 61.251 60.885 1.00 38.23 N ANISOU 3613 N PRO B 102 5745 5276 3507 -318 -114 -125 N ATOM 3614 CA PRO A 102 29.942 61.218 60.995 1.00 38.06 C ANISOU 3614 CA PRO B 102 5756 5320 3386 -545 54 -82 C ATOM 3615 C PRO A 102 29.339 62.368 61.818 1.00 37.74 C ANISOU 3615 C PRO B 102 5570 5421 3347 -607 127 -145 C ATOM 3616 O PRO A 102 28.138 62.580 61.711 1.00 37.63 O ANISOU 3616 O PRO B 102 5489 5513 3297 -773 269 -153 O ATOM 3617 CB PRO A 102 29.668 59.858 61.648 1.00 39.74 C ANISOU 3617 CB PRO B 102 6357 5403 3340 -636 29 -9 C ATOM 3618 CG PRO A 102 30.912 59.544 62.406 1.00 41.12 C ANISOU 3618 CG PRO B 102 6709 5461 3452 -432 -169 -34 C ATOM 3619 CD PRO A 102 32.043 60.140 61.619 1.00 39.90 C ANISOU 3619 CD PRO B 102 6287 5340 3534 -225 -263 -104 C ATOM 3620 N ASP A 103 30.150 63.084 62.604 1.00 37.74 N ANISOU 3620 N ASP B 103 5518 5434 3387 -468 25 -203 N ATOM 3621 CA ASP A 103 29.710 64.283 63.334 1.00 37.38 C ANISOU 3621 CA ASP B 103 5317 5521 3363 -492 70 -269 C ATOM 3622 C ASP A 103 29.818 65.589 62.529 1.00 35.41 C ANISOU 3622 C ASP B 103 4754 5366 3336 -435 91 -334 C ATOM 3623 O ASP A 103 29.580 66.675 63.065 1.00 34.98 O ANISOU 3623 O ASP B 103 4571 5409 3312 -423 99 -397 O ATOM 3624 CB ASP A 103 30.533 64.451 64.617 1.00 38.61 C ANISOU 3624 CB ASP B 103 5585 5637 3448 -367 -58 -303 C ATOM 3625 CG ASP A 103 30.367 63.293 65.580 1.00 41.13 C ANISOU 3625 CG ASP B 103 6266 5849 3513 -427 -88 -247 C ATOM 3626 OD1 ASP A 103 29.217 62.882 65.839 1.00 43.23 O ANISOU 3626 OD1 ASP B 103 6650 6155 3623 -633 42 -211 O ATOM 3627 OD2 ASP A 103 31.338 62.738 66.135 1.00 43.36 O ANISOU 3627 OD2 ASP B 103 6748 6005 3724 -280 -242 -250 O ATOM 3628 N VAL A 104 30.184 65.479 61.256 1.00 34.19 N ANISOU 3628 N VAL B 104 4500 5170 3319 -400 94 -318 N ATOM 3629 CA VAL A 104 30.385 66.629 60.379 1.00 32.81 C ANISOU 3629 CA VAL B 104 4085 5048 3336 -358 110 -373 C ATOM 3630 C VAL A 104 29.479 66.500 59.155 1.00 31.81 C ANISOU 3630 C VAL B 104 3890 4938 3257 -453 219 -348 C ATOM 3631 O VAL A 104 29.634 65.558 58.381 1.00 31.70 O ANISOU 3631 O VAL B 104 3945 4849 3251 -464 228 -289 O ATOM 3632 CB VAL A 104 31.849 66.707 59.906 1.00 32.44 C ANISOU 3632 CB VAL B 104 3971 4939 3417 -224 7 -402 C ATOM 3633 CG1 VAL A 104 32.041 67.844 58.898 1.00 31.25 C ANISOU 3633 CG1 VAL B 104 3611 4822 3439 -224 41 -453 C ATOM 3634 CG2 VAL A 104 32.782 66.862 61.101 1.00 33.75 C ANISOU 3634 CG2 VAL B 104 4185 5096 3540 -109 -115 -454 C ATOM 3635 N PRO A 105 28.529 67.419 58.976 1.00 31.51 N ANISOU 3635 N PRO B 105 3727 5000 3247 -506 289 -404 N ATOM 3636 CA PRO A 105 27.732 67.452 57.745 1.00 31.02 C ANISOU 3636 CA PRO B 105 3585 4953 3247 -561 373 -408 C ATOM 3637 C PRO A 105 28.570 67.801 56.507 1.00 30.26 C ANISOU 3637 C PRO B 105 3405 4774 3318 -488 342 -401 C ATOM 3638 O PRO A 105 29.406 68.702 56.560 1.00 30.25 O ANISOU 3638 O PRO B 105 3330 4760 3403 -417 281 -444 O ATOM 3639 CB PRO A 105 26.692 68.549 58.022 1.00 30.89 C ANISOU 3639 CB PRO B 105 3456 5069 3213 -583 410 -510 C ATOM 3640 CG PRO A 105 26.706 68.745 59.474 1.00 32.06 C ANISOU 3640 CG PRO B 105 3649 5281 3250 -584 377 -536 C ATOM 3641 CD PRO A 105 28.100 68.466 59.919 1.00 31.82 C ANISOU 3641 CD PRO B 105 3697 5143 3248 -498 280 -482 C ATOM 3642 N LEU A 106 28.338 67.077 55.417 1.00 30.29 N ANISOU 3642 N LEU B 106 3426 4726 3355 -522 392 -352 N ATOM 3643 CA LEU A 106 29.025 67.274 54.144 1.00 29.83 C ANISOU 3643 CA LEU B 106 3302 4594 3439 -475 382 -342 C ATOM 3644 C LEU A 106 27.990 67.819 53.172 1.00 29.44 C ANISOU 3644 C LEU B 106 3186 4565 3434 -509 452 -379 C ATOM 3645 O LEU A 106 27.120 67.079 52.719 1.00 29.44 O ANISOU 3645 O LEU B 106 3217 4575 3393 -566 517 -353 O ATOM 3646 CB LEU A 106 29.577 65.931 53.660 1.00 29.76 C ANISOU 3646 CB LEU B 106 3382 4503 3422 -465 368 -262 C ATOM 3647 CG LEU A 106 30.340 65.934 52.339 1.00 29.51 C ANISOU 3647 CG LEU B 106 3283 4405 3523 -423 363 -254 C ATOM 3648 CD1 LEU A 106 31.620 66.763 52.461 1.00 29.50 C ANISOU 3648 CD1 LEU B 106 3192 4410 3608 -360 298 -321 C ATOM 3649 CD2 LEU A 106 30.645 64.507 51.913 1.00 29.85 C ANISOU 3649 CD2 LEU B 106 3428 4381 3534 -405 342 -181 C ATOM 3650 N VAL A 107 28.076 69.113 52.864 1.00 29.50 N ANISOU 3650 N VAL B 107 3122 4574 3513 -471 430 -449 N ATOM 3651 CA VAL A 107 26.916 69.856 52.353 1.00 29.60 C ANISOU 3651 CA VAL B 107 3097 4628 3523 -471 460 -525 C ATOM 3652 C VAL A 107 27.117 70.598 51.025 1.00 29.36 C ANISOU 3652 C VAL B 107 3062 4501 3594 -438 455 -549 C ATOM 3653 O VAL A 107 28.104 71.310 50.826 1.00 28.98 O ANISOU 3653 O VAL B 107 3017 4386 3609 -424 415 -555 O ATOM 3654 CB VAL A 107 26.418 70.875 53.418 1.00 30.01 C ANISOU 3654 CB VAL B 107 3115 4779 3507 -445 419 -620 C ATOM 3655 CG1 VAL A 107 25.285 71.744 52.878 1.00 29.93 C ANISOU 3655 CG1 VAL B 107 3071 4816 3486 -405 415 -734 C ATOM 3656 CG2 VAL A 107 25.971 70.144 54.677 1.00 31.44 C ANISOU 3656 CG2 VAL B 107 3317 5067 3564 -499 444 -609 C ATOM 3657 N VAL A 108 26.157 70.384 50.126 1.00 29.42 N ANISOU 3657 N VAL B 108 3072 4504 3604 -438 498 -570 N ATOM 3658 CA VAL A 108 25.903 71.224 48.966 1.00 29.46 C ANISOU 3658 CA VAL B 108 3104 4427 3662 -392 484 -624 C ATOM 3659 C VAL A 108 24.542 71.865 49.264 1.00 30.13 C ANISOU 3659 C VAL B 108 3163 4615 3670 -340 459 -757 C ATOM 3660 O VAL A 108 23.542 71.163 49.282 1.00 30.26 O ANISOU 3660 O VAL B 108 3133 4728 3638 -361 510 -789 O ATOM 3661 CB VAL A 108 25.789 70.380 47.677 1.00 28.84 C ANISOU 3661 CB VAL B 108 3046 4271 3641 -406 541 -565 C ATOM 3662 CG1 VAL A 108 25.546 71.278 46.463 1.00 28.87 C ANISOU 3662 CG1 VAL B 108 3114 4168 3686 -353 518 -624 C ATOM 3663 CG2 VAL A 108 27.031 69.529 47.473 1.00 29.26 C ANISOU 3663 CG2 VAL B 108 3105 4261 3753 -446 559 -452 C ATOM 3664 N PRO A 109 24.494 73.169 49.531 1.00 31.03 N ANISOU 3664 N PRO B 109 3306 4722 3761 -274 377 -851 N ATOM 3665 CA PRO A 109 23.268 73.823 50.032 1.00 31.91 C ANISOU 3665 CA PRO B 109 3379 4964 3783 -199 328 -1006 C ATOM 3666 C PRO A 109 21.958 73.538 49.288 1.00 32.10 C ANISOU 3666 C PRO B 109 3366 5053 3778 -151 349 -1111 C ATOM 3667 O PRO A 109 20.902 73.492 49.922 1.00 32.98 O ANISOU 3667 O PRO B 109 3382 5345 3803 -135 353 -1236 O ATOM 3668 CB PRO A 109 23.615 75.308 49.928 1.00 32.20 C ANISOU 3668 CB PRO B 109 3515 4904 3817 -117 215 -1075 C ATOM 3669 CG PRO A 109 25.086 75.334 50.142 1.00 31.97 C ANISOU 3669 CG PRO B 109 3520 4775 3850 -195 227 -954 C ATOM 3670 CD PRO A 109 25.605 74.131 49.416 1.00 30.79 C ANISOU 3670 CD PRO B 109 3352 4571 3776 -271 321 -832 C ATOM 3671 N GLU A 110 22.026 73.363 47.974 1.00 31.80 N ANISOU 3671 N GLU B 110 3395 4883 3807 -130 363 -1078 N ATOM 3672 CA GLU A 110 20.836 73.100 47.158 1.00 32.07 C ANISOU 3672 CA GLU B 110 3398 4964 3823 -69 374 -1188 C ATOM 3673 C GLU A 110 20.308 71.677 47.318 1.00 31.79 C ANISOU 3673 C GLU B 110 3253 5051 3774 -177 492 -1146 C ATOM 3674 O GLU A 110 19.135 71.415 47.052 1.00 32.14 O ANISOU 3674 O GLU B 110 3221 5217 3776 -152 513 -1277 O ATOM 3675 CB GLU A 110 21.143 73.361 45.676 1.00 31.79 C ANISOU 3675 CB GLU B 110 3495 4724 3858 -12 349 -1157 C ATOM 3676 CG GLU A 110 21.451 74.819 45.367 1.00 33.21 C ANISOU 3676 CG GLU B 110 3837 4764 4016 86 227 -1225 C ATOM 3677 CD GLU A 110 22.932 75.112 45.187 1.00 33.72 C ANISOU 3677 CD GLU B 110 4010 4662 4142 -6 241 -1081 C ATOM 3678 OE1 GLU A 110 23.781 74.390 45.758 1.00 32.74 O ANISOU 3678 OE1 GLU B 110 3800 4575 4063 -118 316 -955 O ATOM 3679 OE2 GLU A 110 23.241 76.091 44.472 1.00 34.48 O ANISOU 3679 OE2 GLU B 110 4288 4588 4225 34 172 -1111 O ATOM 3680 N VAL A 111 21.174 70.763 47.751 1.00 31.29 N ANISOU 3680 N VAL B 111 3197 4957 3736 -297 561 -978 N ATOM 3681 CA VAL A 111 20.844 69.338 47.824 1.00 31.15 C ANISOU 3681 CA VAL B 111 3140 5003 3692 -415 664 -908 C ATOM 3682 C VAL A 111 20.427 68.900 49.224 1.00 31.92 C ANISOU 3682 C VAL B 111 3181 5274 3672 -520 711 -935 C ATOM 3683 O VAL A 111 19.369 68.298 49.393 1.00 33.20 O ANISOU 3683 O VAL B 111 3278 5583 3755 -599 783 -1018 O ATOM 3684 CB VAL A 111 22.043 68.477 47.350 1.00 30.23 C ANISOU 3684 CB VAL B 111 3102 4730 3655 -466 693 -715 C ATOM 3685 CG1 VAL A 111 21.694 66.980 47.377 1.00 30.75 C ANISOU 3685 CG1 VAL B 111 3173 4833 3677 -581 780 -639 C ATOM 3686 CG2 VAL A 111 22.472 68.908 45.948 1.00 29.13 C ANISOU 3686 CG2 VAL B 111 3021 4427 3621 -385 662 -693 C ATOM 3687 N ASN A 112 21.252 69.210 50.221 1.00 31.79 N ANISOU 3687 N ASN B 112 3197 5245 3637 -531 674 -876 N ATOM 3688 CA ASN A 112 21.063 68.693 51.579 1.00 32.37 C ANISOU 3688 CA ASN B 112 3261 5445 3591 -640 719 -869 C ATOM 3689 C ASN A 112 21.290 69.749 52.665 1.00 32.61 C ANISOU 3689 C ASN B 112 3267 5541 3583 -584 647 -935 C ATOM 3690 O ASN A 112 22.026 69.518 53.625 1.00 32.92 O ANISOU 3690 O ASN B 112 3359 5562 3587 -625 637 -851 O ATOM 3691 CB ASN A 112 21.975 67.468 51.805 1.00 32.15 C ANISOU 3691 CB ASN B 112 3346 5311 3557 -731 753 -689 C ATOM 3692 CG ASN A 112 23.461 67.823 51.794 1.00 31.44 C ANISOU 3692 CG ASN B 112 3312 5073 3560 -652 672 -587 C ATOM 3693 OD1 ASN A 112 23.856 68.823 51.205 1.00 31.33 O ANISOU 3693 OD1 ASN B 112 3271 4995 3638 -557 616 -621 O ATOM 3694 ND2 ASN A 112 24.283 67.008 52.456 1.00 30.16 N ANISOU 3694 ND2 ASN B 112 3241 4861 3359 -694 663 -480 N ATOM 3695 N ALA A 113 20.645 70.905 52.523 1.00 32.91 N ANISOU 3695 N ALA B 113 3237 5651 3618 -475 583 -1094 N ATOM 3696 CA ALA A 113 20.733 71.965 53.544 1.00 33.60 C ANISOU 3696 CA ALA B 113 3298 5811 3657 -410 503 -1174 C ATOM 3697 C ALA A 113 20.275 71.508 54.931 1.00 34.62 C ANISOU 3697 C ALA B 113 3382 6120 3653 -517 562 -1207 C ATOM 3698 O ALA A 113 20.756 72.026 55.939 1.00 35.40 O ANISOU 3698 O ALA B 113 3494 6235 3720 -493 510 -1198 O ATOM 3699 CB ALA A 113 19.934 73.201 53.111 1.00 33.98 C ANISOU 3699 CB ALA B 113 3300 5915 3696 -259 407 -1367 C ATOM 3700 N HIS A 114 19.342 70.554 54.978 1.00 35.31 N ANISOU 3700 N HIS B 114 3423 6339 3653 -646 673 -1252 N ATOM 3701 CA HIS A 114 18.781 70.043 56.238 1.00 36.60 C ANISOU 3701 CA HIS B 114 3563 6684 3660 -792 755 -1298 C ATOM 3702 C HIS A 114 19.831 69.398 57.145 1.00 36.36 C ANISOU 3702 C HIS B 114 3679 6541 3594 -872 765 -1117 C ATOM 3703 O HIS A 114 19.661 69.380 58.361 1.00 37.27 O ANISOU 3703 O HIS B 114 3807 6766 3587 -943 787 -1147 O ATOM 3704 CB HIS A 114 17.645 69.033 55.976 1.00 37.62 C ANISOU 3704 CB HIS B 114 3641 6959 3696 -958 892 -1375 C ATOM 3705 CG HIS A 114 18.045 67.887 55.093 1.00 38.20 C ANISOU 3705 CG HIS B 114 3824 6866 3826 -1036 949 -1213 C ATOM 3706 ND1 HIS A 114 18.802 66.826 55.543 1.00 39.21 N ANISOU 3706 ND1 HIS B 114 4123 6868 3906 -1156 988 -1026 N ATOM 3707 CD2 HIS A 114 17.801 67.645 53.783 1.00 39.12 C ANISOU 3707 CD2 HIS B 114 3914 6915 4034 -994 958 -1216 C ATOM 3708 CE1 HIS A 114 19.008 65.982 54.548 1.00 39.38 C ANISOU 3708 CE1 HIS B 114 4214 6759 3990 -1184 1017 -923 C ATOM 3709 NE2 HIS A 114 18.412 66.455 53.469 1.00 39.13 N ANISOU 3709 NE2 HIS B 114 4058 6761 4048 -1093 1007 -1029 N ATOM 3710 N ALA A 115 20.896 68.859 56.547 1.00 35.22 N ANISOU 3710 N ALA B 115 3648 6186 3547 -851 741 -945 N ATOM 3711 CA ALA A 115 21.995 68.251 57.300 1.00 35.14 C ANISOU 3711 CA ALA B 115 3785 6056 3510 -882 716 -794 C ATOM 3712 C ALA A 115 22.781 69.263 58.132 1.00 34.79 C ANISOU 3712 C ALA B 115 3729 5994 3496 -769 613 -804 C ATOM 3713 O ALA A 115 23.520 68.876 59.032 1.00 35.31 O ANISOU 3713 O ALA B 115 3902 6005 3509 -784 585 -725 O ATOM 3714 CB ALA A 115 22.940 67.502 56.351 1.00 34.27 C ANISOU 3714 CB ALA B 115 3768 5750 3503 -856 697 -648 C ATOM 3715 N LEU A 116 22.634 70.548 57.821 1.00 34.16 N ANISOU 3715 N LEU B 116 3540 5948 3492 -648 544 -907 N ATOM 3716 CA LEU A 116 23.248 71.618 58.614 1.00 33.97 C ANISOU 3716 CA LEU B 116 3501 5920 3485 -548 444 -936 C ATOM 3717 C LEU A 116 22.651 71.744 60.021 1.00 35.04 C ANISOU 3717 C LEU B 116 3616 6223 3474 -593 460 -1013 C ATOM 3718 O LEU A 116 23.347 72.143 60.953 1.00 34.98 O ANISOU 3718 O LEU B 116 3644 6191 3455 -545 394 -987 O ATOM 3719 CB LEU A 116 23.128 72.969 57.893 1.00 33.37 C ANISOU 3719 CB LEU B 116 3357 5826 3498 -417 359 -1036 C ATOM 3720 CG LEU A 116 23.850 73.092 56.545 1.00 32.16 C ANISOU 3720 CG LEU B 116 3243 5493 3483 -373 335 -967 C ATOM 3721 CD1 LEU A 116 23.440 74.358 55.822 1.00 31.58 C ANISOU 3721 CD1 LEU B 116 3152 5401 3447 -263 256 -1084 C ATOM 3722 CD2 LEU A 116 25.349 73.079 56.744 1.00 31.87 C ANISOU 3722 CD2 LEU B 116 3266 5322 3524 -361 290 -856 C ATOM 3723 N ASP A 117 21.373 71.408 60.173 1.00 35.80 N ANISOU 3723 N ASP B 117 3649 6498 3455 -691 550 -1120 N ATOM 3724 CA ASP A 117 20.675 71.585 61.455 1.00 37.23 C ANISOU 3724 CA ASP B 117 3790 6875 3482 -752 581 -1226 C ATOM 3725 C ASP A 117 21.346 70.880 62.626 1.00 37.61 C ANISOU 3725 C ASP B 117 3990 6865 3434 -837 599 -1106 C ATOM 3726 O ASP A 117 21.303 71.372 63.749 1.00 38.09 O ANISOU 3726 O ASP B 117 4043 7017 3414 -820 569 -1159 O ATOM 3727 CB ASP A 117 19.227 71.112 61.360 1.00 38.48 C ANISOU 3727 CB ASP B 117 3852 7252 3519 -889 704 -1370 C ATOM 3728 CG ASP A 117 18.449 71.840 60.295 1.00 38.86 C ANISOU 3728 CG ASP B 117 3747 7379 3640 -777 667 -1530 C ATOM 3729 OD1 ASP A 117 18.837 72.970 59.942 1.00 38.37 O ANISOU 3729 OD1 ASP B 117 3658 7243 3679 -589 534 -1563 O ATOM 3730 OD2 ASP A 117 17.442 71.352 59.752 1.00 41.00 O ANISOU 3730 OD2 ASP B 117 3935 7780 3864 -863 757 -1636 O ATOM 3731 N ALA A 118 21.986 69.746 62.356 1.00 37.26 N ANISOU 3731 N ALA B 118 4102 6662 3394 -911 633 -953 N ATOM 3732 CA ALA A 118 22.548 68.914 63.415 1.00 38.17 C ANISOU 3732 CA ALA B 118 4412 6703 3386 -988 640 -849 C ATOM 3733 C ALA A 118 24.060 69.095 63.573 1.00 37.23 C ANISOU 3733 C ALA B 118 4377 6395 3374 -836 507 -743 C ATOM 3734 O ALA A 118 24.716 68.256 64.185 1.00 38.06 O ANISOU 3734 O ALA B 118 4673 6390 3398 -860 484 -648 O ATOM 3735 CB ALA A 118 22.213 67.448 63.143 1.00 39.00 C ANISOU 3735 CB ALA B 118 4679 6759 3381 -1171 747 -769 C ATOM 3736 N HIS A 119 24.611 70.191 63.052 1.00 35.78 N ANISOU 3736 N HIS B 119 4063 6176 3355 -681 416 -775 N ATOM 3737 CA HIS A 119 26.065 70.380 63.054 1.00 34.91 C ANISOU 3737 CA HIS B 119 3996 5910 3357 -555 303 -703 C ATOM 3738 C HIS A 119 26.622 70.534 64.466 1.00 35.31 C ANISOU 3738 C HIS B 119 4127 5960 3327 -507 233 -701 C ATOM 3739 O HIS A 119 25.913 70.930 65.384 1.00 36.13 O ANISOU 3739 O HIS B 119 4212 6193 3324 -541 255 -769 O ATOM 3740 CB HIS A 119 26.490 71.562 62.170 1.00 33.71 C ANISOU 3740 CB HIS B 119 3706 5723 3378 -442 238 -748 C ATOM 3741 CG HIS A 119 26.308 72.909 62.803 1.00 34.16 C ANISOU 3741 CG HIS B 119 3674 5866 3438 -363 170 -849 C ATOM 3742 ND1 HIS A 119 25.420 73.842 62.311 1.00 34.91 N ANISOU 3742 ND1 HIS B 119 3664 6050 3550 -332 168 -957 N ATOM 3743 CD2 HIS A 119 26.921 73.498 63.857 1.00 34.24 C ANISOU 3743 CD2 HIS B 119 3694 5880 3435 -290 87 -866 C ATOM 3744 CE1 HIS A 119 25.481 74.936 63.049 1.00 33.83 C ANISOU 3744 CE1 HIS B 119 3485 5965 3402 -247 83 -1033 C ATOM 3745 NE2 HIS A 119 26.386 74.755 63.991 1.00 34.66 N ANISOU 3745 NE2 HIS B 119 3653 6023 3495 -227 39 -974 N ATOM 3746 N ASN A 120 27.904 70.207 64.590 1.00 34.86 N ANISOU 3746 N ASN B 120 4155 5767 3325 -420 144 -637 N ATOM 3747 CA ASN A 120 28.665 70.249 65.826 1.00 35.35 C ANISOU 3747 CA ASN B 120 4309 5794 3327 -341 53 -635 C ATOM 3748 C ASN A 120 29.838 71.228 65.717 1.00 34.75 C ANISOU 3748 C ASN B 120 4119 5673 3412 -193 -62 -675 C ATOM 3749 O ASN A 120 30.838 71.096 66.420 1.00 35.28 O ANISOU 3749 O ASN B 120 4252 5677 3475 -97 -159 -676 O ATOM 3750 CB ASN A 120 29.197 68.847 66.150 1.00 36.04 C ANISOU 3750 CB ASN B 120 4631 5757 3306 -354 28 -551 C ATOM 3751 CG ASN A 120 28.086 67.830 66.343 1.00 36.39 C ANISOU 3751 CG ASN B 120 4834 5830 3161 -536 147 -509 C ATOM 3752 OD1 ASN A 120 27.465 67.775 67.399 1.00 35.80 O ANISOU 3752 OD1 ASN B 120 4852 5827 2924 -619 188 -530 O ATOM 3753 ND2 ASN A 120 27.834 67.015 65.317 1.00 35.95 N ANISOU 3753 ND2 ASN B 120 4814 5724 3120 -612 208 -455 N ATOM 3754 N GLY A 121 29.734 72.185 64.803 1.00 33.96 N ANISOU 3754 N GLY B 121 3862 5598 3444 -181 -53 -719 N ATOM 3755 CA GLY A 121 30.687 73.276 64.721 1.00 33.68 C ANISOU 3755 CA GLY B 121 3726 5535 3538 -86 -143 -772 C ATOM 3756 C GLY A 121 31.531 73.225 63.466 1.00 33.06 C ANISOU 3756 C GLY B 121 3591 5370 3601 -81 -145 -759 C ATOM 3757 O GLY A 121 32.170 74.207 63.129 1.00 32.73 O ANISOU 3757 O GLY B 121 3462 5309 3663 -52 -189 -812 O ATOM 3758 N ILE A 122 31.543 72.081 62.784 1.00 33.02 N ANISOU 3758 N ILE B 122 3646 5312 3588 -121 -97 -694 N ATOM 3759 CA ILE A 122 32.237 71.954 61.509 1.00 32.68 C ANISOU 3759 CA ILE B 122 3546 5203 3670 -126 -85 -685 C ATOM 3760 C ILE A 122 31.275 71.462 60.425 1.00 32.04 C ANISOU 3760 C ILE B 122 3475 5111 3586 -211 15 -634 C ATOM 3761 O ILE A 122 30.568 70.470 60.602 1.00 32.16 O ANISOU 3761 O ILE B 122 3586 5135 3498 -261 65 -580 O ATOM 3762 CB ILE A 122 33.450 71.003 61.626 1.00 33.32 C ANISOU 3762 CB ILE B 122 3675 5225 3762 -54 -154 -677 C ATOM 3763 CG1 ILE A 122 34.477 71.547 62.630 1.00 33.76 C ANISOU 3763 CG1 ILE B 122 3697 5299 3834 46 -264 -757 C ATOM 3764 CG2 ILE A 122 34.110 70.812 60.265 1.00 33.08 C ANISOU 3764 CG2 ILE B 122 3569 5151 3851 -69 -132 -682 C ATOM 3765 CD1 ILE A 122 35.457 70.506 63.130 1.00 34.36 C ANISOU 3765 CD1 ILE B 122 3860 5332 3864 155 -362 -774 C ATOM 3766 N ILE A 123 31.239 72.192 59.317 1.00 31.31 N ANISOU 3766 N ILE B 123 3302 4997 3596 -234 43 -659 N ATOM 3767 CA ILE A 123 30.571 71.755 58.100 1.00 30.79 C ANISOU 3767 CA ILE B 123 3240 4902 3556 -292 124 -621 C ATOM 3768 C ILE A 123 31.656 71.601 57.043 1.00 30.31 C ANISOU 3768 C ILE B 123 3144 4762 3612 -287 119 -609 C ATOM 3769 O ILE A 123 32.447 72.514 56.826 1.00 30.39 O ANISOU 3769 O ILE B 123 3095 4753 3700 -281 86 -665 O ATOM 3770 CB ILE A 123 29.493 72.777 57.673 1.00 30.55 C ANISOU 3770 CB ILE B 123 3170 4912 3526 -308 151 -679 C ATOM 3771 CG1 ILE A 123 28.387 72.850 58.735 1.00 31.63 C ANISOU 3771 CG1 ILE B 123 3313 5167 3537 -314 160 -718 C ATOM 3772 CG2 ILE A 123 28.867 72.379 56.326 1.00 29.87 C ANISOU 3772 CG2 ILE B 123 3087 4787 3477 -350 223 -654 C ATOM 3773 CD1 ILE A 123 28.616 73.887 59.808 1.00 33.09 C ANISOU 3773 CD1 ILE B 123 3474 5401 3697 -256 81 -783 C ATOM 3774 N ALA A 124 31.725 70.424 56.429 1.00 30.38 N ANISOU 3774 N ALA B 124 3193 4729 3619 -300 152 -546 N ATOM 3775 CA ALA A 124 32.696 70.153 55.370 1.00 30.26 C ANISOU 3775 CA ALA B 124 3135 4659 3705 -295 153 -544 C ATOM 3776 C ALA A 124 32.141 70.540 54.000 1.00 29.72 C ANISOU 3776 C ALA B 124 3045 4547 3702 -354 228 -533 C ATOM 3777 O ALA A 124 30.997 70.243 53.671 1.00 29.04 O ANISOU 3777 O ALA B 124 2997 4462 3574 -382 282 -497 O ATOM 3778 CB ALA A 124 33.096 68.674 55.376 1.00 30.40 C ANISOU 3778 CB ALA B 124 3224 4646 3680 -255 127 -490 C ATOM 3779 N CYS A 125 32.966 71.220 53.212 1.00 30.20 N ANISOU 3779 N CYS B 125 3048 4571 3854 -379 232 -578 N ATOM 3780 CA CYS A 125 32.669 71.470 51.813 1.00 30.08 C ANISOU 3780 CA CYS B 125 3044 4490 3896 -432 296 -566 C ATOM 3781 C CYS A 125 33.081 70.218 51.045 1.00 29.84 C ANISOU 3781 C CYS B 125 3005 4435 3897 -423 322 -513 C ATOM 3782 O CYS A 125 34.176 69.721 51.254 1.00 30.12 O ANISOU 3782 O CYS B 125 2993 4498 3954 -391 280 -538 O ATOM 3783 CB CYS A 125 33.466 72.673 51.315 1.00 30.64 C ANISOU 3783 CB CYS B 125 3091 4525 4027 -492 297 -639 C ATOM 3784 SG CYS A 125 33.241 73.032 49.562 1.00 32.52 S ANISOU 3784 SG CYS B 125 3388 4653 4315 -567 372 -628 S ATOM 3785 N PRO A 126 32.235 69.690 50.164 1.00 29.64 N ANISOU 3785 N PRO B 126 3024 4366 3873 -438 378 -454 N ATOM 3786 CA PRO A 126 32.615 68.486 49.411 1.00 29.72 C ANISOU 3786 CA PRO B 126 3036 4347 3910 -422 393 -400 C ATOM 3787 C PRO A 126 33.646 68.743 48.309 1.00 30.35 C ANISOU 3787 C PRO B 126 3053 4397 4080 -454 417 -439 C ATOM 3788 O PRO A 126 33.966 69.878 47.984 1.00 29.98 O ANISOU 3788 O PRO B 126 2987 4334 4071 -515 439 -499 O ATOM 3789 CB PRO A 126 31.286 67.999 48.811 1.00 28.97 C ANISOU 3789 CB PRO B 126 3002 4218 3787 -439 451 -337 C ATOM 3790 CG PRO A 126 30.239 68.897 49.331 1.00 28.55 C ANISOU 3790 CG PRO B 126 2963 4199 3686 -453 460 -378 C ATOM 3791 CD PRO A 126 30.886 70.150 49.804 1.00 28.82 C ANISOU 3791 CD PRO B 126 2965 4244 3742 -455 418 -451 C ATOM 3792 N ASN A 127 34.162 67.651 47.760 1.00 31.45 N ANISOU 3792 N ASN B 127 3177 4533 4241 -418 409 -411 N ATOM 3793 CA ASN A 127 35.102 67.657 46.631 1.00 32.42 C ANISOU 3793 CA ASN B 127 3229 4650 4440 -449 441 -454 C ATOM 3794 C ASN A 127 34.498 68.368 45.408 1.00 31.95 C ANISOU 3794 C ASN B 127 3215 4505 4421 -532 530 -434 C ATOM 3795 O ASN A 127 33.296 68.272 45.162 1.00 30.91 O ANISOU 3795 O ASN B 127 3164 4316 4266 -521 555 -370 O ATOM 3796 CB ASN A 127 35.494 66.191 46.346 1.00 32.93 C ANISOU 3796 CB ASN B 127 3291 4725 4496 -364 397 -420 C ATOM 3797 CG ASN A 127 35.991 65.957 44.951 1.00 34.23 C ANISOU 3797 CG ASN B 127 3404 4873 4730 -391 447 -434 C ATOM 3798 OD1 ASN A 127 35.205 65.667 44.046 1.00 36.22 O ANISOU 3798 OD1 ASN B 127 3718 5047 4996 -408 502 -354 O ATOM 3799 ND2 ASN A 127 37.306 66.014 44.772 1.00 36.23 N ANISOU 3799 ND2 ASN B 127 3535 5213 5019 -390 426 -548 N ATOM 3800 N CYS A 128 35.324 69.102 44.664 1.00 32.87 N ANISOU 3800 N CYS B 128 3290 4613 4584 -619 575 -504 N ATOM 3801 CA CYS A 128 34.838 69.950 43.564 1.00 33.29 C ANISOU 3801 CA CYS B 128 3438 4559 4653 -705 647 -497 C ATOM 3802 C CYS A 128 34.033 69.205 42.482 1.00 32.55 C ANISOU 3802 C CYS B 128 3405 4385 4575 -667 685 -413 C ATOM 3803 O CYS A 128 32.934 69.634 42.109 1.00 31.97 O ANISOU 3803 O CYS B 128 3439 4227 4482 -657 700 -384 O ATOM 3804 CB CYS A 128 35.994 70.721 42.912 1.00 34.27 C ANISOU 3804 CB CYS B 128 3529 4690 4804 -840 702 -589 C ATOM 3805 SG CYS A 128 37.461 69.742 42.520 1.00 38.21 S ANISOU 3805 SG CYS B 128 3848 5318 5352 -843 712 -663 S ATOM 3806 N SER A 129 34.574 68.091 41.993 1.00 32.45 N ANISOU 3806 N SER B 129 3326 4407 4596 -630 688 -389 N ATOM 3807 CA SER A 129 33.906 67.310 40.951 1.00 31.84 C ANISOU 3807 CA SER B 129 3301 4257 4539 -591 720 -310 C ATOM 3808 C SER A 129 32.579 66.726 41.448 1.00 30.63 C ANISOU 3808 C SER B 129 3210 4085 4344 -517 693 -233 C ATOM 3809 O SER A 129 31.630 66.589 40.680 1.00 30.32 O ANISOU 3809 O SER B 129 3238 3972 4311 -503 727 -191 O ATOM 3810 CB SER A 129 34.830 66.201 40.427 1.00 32.31 C ANISOU 3810 CB SER B 129 3274 4370 4633 -552 708 -311 C ATOM 3811 OG SER A 129 35.440 65.487 41.493 1.00 34.53 O ANISOU 3811 OG SER B 129 3485 4750 4884 -474 620 -336 O ATOM 3812 N THR A 130 32.513 66.409 42.739 1.00 30.17 N ANISOU 3812 N THR B 130 3133 4099 4234 -480 636 -230 N ATOM 3813 CA THR A 130 31.302 65.873 43.351 1.00 29.48 C ANISOU 3813 CA THR B 130 3101 4017 4082 -449 625 -176 C ATOM 3814 C THR A 130 30.201 66.920 43.414 1.00 28.69 C ANISOU 3814 C THR B 130 3041 3898 3961 -471 651 -214 C ATOM 3815 O THR A 130 29.049 66.619 43.119 1.00 27.97 O ANISOU 3815 O THR B 130 2986 3793 3847 -458 677 -195 O ATOM 3816 CB THR A 130 31.605 65.350 44.768 1.00 29.99 C ANISOU 3816 CB THR B 130 3163 4156 4075 -419 558 -173 C ATOM 3817 OG1 THR A 130 32.517 64.248 44.689 1.00 31.43 O ANISOU 3817 OG1 THR B 130 3339 4347 4257 -363 505 -151 O ATOM 3818 CG2 THR A 130 30.371 64.762 45.419 1.00 30.40 C ANISOU 3818 CG2 THR B 130 3288 4224 4039 -428 566 -124 C ATOM 3819 N ILE A 131 30.557 68.146 43.789 1.00 28.57 N ANISOU 3819 N ILE B 131 3020 3889 3945 -499 636 -283 N ATOM 3820 CA ILE A 131 29.561 69.194 44.006 1.00 28.65 C ANISOU 3820 CA ILE B 131 3081 3888 3916 -492 627 -340 C ATOM 3821 C ILE A 131 28.721 69.440 42.754 1.00 27.97 C ANISOU 3821 C ILE B 131 3070 3708 3847 -471 657 -352 C ATOM 3822 O ILE A 131 27.492 69.401 42.824 1.00 27.42 O ANISOU 3822 O ILE B 131 3015 3664 3738 -425 652 -381 O ATOM 3823 CB ILE A 131 30.212 70.521 44.478 1.00 29.22 C ANISOU 3823 CB ILE B 131 3166 3954 3980 -528 594 -412 C ATOM 3824 CG1 ILE A 131 30.776 70.379 45.894 1.00 29.38 C ANISOU 3824 CG1 ILE B 131 3114 4076 3971 -523 550 -420 C ATOM 3825 CG2 ILE A 131 29.179 71.652 44.466 1.00 30.01 C ANISOU 3825 CG2 ILE B 131 3355 4017 4032 -496 563 -483 C ATOM 3826 CD1 ILE A 131 31.802 71.435 46.247 1.00 30.10 C ANISOU 3826 CD1 ILE B 131 3192 4169 4076 -574 525 -486 C ATOM 3827 N GLN A 132 29.377 69.698 41.620 1.00 27.54 N ANISOU 3827 N GLN B 132 3064 3556 3845 -505 687 -344 N ATOM 3828 CA GLN A 132 28.650 70.024 40.390 1.00 27.14 C ANISOU 3828 CA GLN B 132 3119 3390 3801 -475 705 -361 C ATOM 3829 C GLN A 132 27.760 68.870 39.918 1.00 26.69 C ANISOU 3829 C GLN B 132 3032 3347 3760 -417 729 -313 C ATOM 3830 O GLN A 132 26.650 69.099 39.452 1.00 26.10 O ANISOU 3830 O GLN B 132 3012 3239 3666 -354 718 -362 O ATOM 3831 CB GLN A 132 29.589 70.507 39.275 1.00 27.30 C ANISOU 3831 CB GLN B 132 3220 3297 3857 -548 744 -361 C ATOM 3832 CG GLN A 132 30.542 69.469 38.700 1.00 26.48 C ANISOU 3832 CG GLN B 132 3029 3215 3816 -586 796 -298 C ATOM 3833 CD GLN A 132 31.529 70.074 37.716 1.00 26.85 C ANISOU 3833 CD GLN B 132 3140 3180 3880 -693 849 -325 C ATOM 3834 OE1 GLN A 132 32.361 70.892 38.099 1.00 28.01 O ANISOU 3834 OE1 GLN B 132 3291 3346 4007 -791 855 -383 O ATOM 3835 NE2 GLN A 132 31.448 69.663 36.444 1.00 25.16 N ANISOU 3835 NE2 GLN B 132 2981 2882 3697 -689 895 -291 N ATOM 3836 N MET A 133 28.236 67.636 40.072 1.00 27.01 N ANISOU 3836 N MET B 133 2994 3440 3827 -431 750 -233 N ATOM 3837 CA MET A 133 27.435 66.452 39.745 1.00 26.77 C ANISOU 3837 CA MET B 133 2950 3424 3797 -397 771 -180 C ATOM 3838 C MET A 133 26.181 66.365 40.617 1.00 27.10 C ANISOU 3838 C MET B 133 2969 3561 3767 -385 762 -226 C ATOM 3839 O MET A 133 25.114 65.979 40.143 1.00 27.13 O ANISOU 3839 O MET B 133 2977 3570 3761 -359 784 -247 O ATOM 3840 CB MET A 133 28.262 65.175 39.914 1.00 27.03 C ANISOU 3840 CB MET B 133 2938 3487 3844 -409 768 -92 C ATOM 3841 CG MET A 133 27.550 63.906 39.444 1.00 27.27 C ANISOU 3841 CG MET B 133 2988 3506 3869 -388 787 -26 C ATOM 3842 SD MET A 133 28.636 62.477 39.394 1.00 30.51 S ANISOU 3842 SD MET B 133 3394 3914 4286 -371 752 67 S ATOM 3843 CE MET A 133 28.708 62.031 41.115 1.00 30.34 C ANISOU 3843 CE MET B 133 3390 3982 4156 -395 701 76 C ATOM 3844 N MET A 134 26.316 66.708 41.896 1.00 27.49 N ANISOU 3844 N MET B 134 2986 3698 3761 -411 735 -254 N ATOM 3845 CA MET A 134 25.186 66.687 42.815 1.00 27.78 C ANISOU 3845 CA MET B 134 2991 3849 3715 -419 736 -314 C ATOM 3846 C MET A 134 24.154 67.751 42.461 1.00 27.64 C ANISOU 3846 C MET B 134 2984 3837 3680 -355 715 -445 C ATOM 3847 O MET A 134 22.964 67.522 42.617 1.00 27.86 O ANISOU 3847 O MET B 134 2970 3959 3658 -346 731 -521 O ATOM 3848 CB MET A 134 25.657 66.853 44.269 1.00 28.35 C ANISOU 3848 CB MET B 134 3038 4007 3728 -454 707 -315 C ATOM 3849 CG MET A 134 26.464 65.675 44.788 1.00 28.80 C ANISOU 3849 CG MET B 134 3109 4068 3766 -491 704 -212 C ATOM 3850 SD MET A 134 25.506 64.161 44.895 1.00 31.20 S ANISOU 3850 SD MET B 134 3456 4411 3989 -553 753 -156 S ATOM 3851 CE MET A 134 26.030 63.307 43.343 1.00 30.10 C ANISOU 3851 CE MET B 134 3348 4145 3945 -514 761 -67 C ATOM 3852 N VAL A 135 24.599 68.910 41.988 1.00 27.56 N ANISOU 3852 N VAL B 135 3041 3731 3699 -314 672 -487 N ATOM 3853 CA VAL A 135 23.669 69.981 41.628 1.00 27.82 C ANISOU 3853 CA VAL B 135 3131 3744 3696 -223 618 -624 C ATOM 3854 C VAL A 135 22.841 69.552 40.415 1.00 27.63 C ANISOU 3854 C VAL B 135 3134 3667 3699 -161 636 -653 C ATOM 3855 O VAL A 135 21.650 69.839 40.343 1.00 27.84 O ANISOU 3855 O VAL B 135 3142 3757 3679 -78 602 -789 O ATOM 3856 CB VAL A 135 24.408 71.314 41.341 1.00 28.20 C ANISOU 3856 CB VAL B 135 3306 3662 3745 -209 561 -653 C ATOM 3857 CG1 VAL A 135 23.489 72.329 40.638 1.00 28.63 C ANISOU 3857 CG1 VAL B 135 3489 3637 3754 -89 483 -790 C ATOM 3858 CG2 VAL A 135 24.964 71.910 42.642 1.00 28.05 C ANISOU 3858 CG2 VAL B 135 3252 3717 3689 -249 527 -664 C ATOM 3859 N ALA A 136 23.489 68.861 39.476 1.00 27.18 N ANISOU 3859 N ALA B 136 3109 3505 3714 -192 683 -541 N ATOM 3860 CA ALA A 136 22.854 68.388 38.249 1.00 27.08 C ANISOU 3860 CA ALA B 136 3129 3422 3737 -133 702 -550 C ATOM 3861 C ALA A 136 21.877 67.238 38.484 1.00 27.19 C ANISOU 3861 C ALA B 136 3032 3565 3734 -149 747 -560 C ATOM 3862 O ALA A 136 20.843 67.157 37.824 1.00 27.38 O ANISOU 3862 O ALA B 136 3050 3597 3754 -76 740 -654 O ATOM 3863 CB ALA A 136 23.932 67.932 37.245 1.00 26.48 C ANISOU 3863 CB ALA B 136 3111 3211 3739 -172 743 -423 C ATOM 3864 N LEU A 137 22.229 66.337 39.401 1.00 27.59 N ANISOU 3864 N LEU B 137 3013 3708 3764 -251 790 -471 N ATOM 3865 CA LEU A 137 21.530 65.062 39.547 1.00 27.65 C ANISOU 3865 CA LEU B 137 2961 3802 3741 -313 847 -444 C ATOM 3866 C LEU A 137 20.416 65.075 40.589 1.00 28.74 C ANISOU 3866 C LEU B 137 3012 4127 3779 -361 866 -567 C ATOM 3867 O LEU A 137 19.496 64.270 40.499 1.00 28.85 O ANISOU 3867 O LEU B 137 2978 4228 3758 -413 919 -608 O ATOM 3868 CB LEU A 137 22.521 63.948 39.879 1.00 27.38 C ANISOU 3868 CB LEU B 137 2950 3740 3714 -396 871 -280 C ATOM 3869 CG LEU A 137 23.486 63.548 38.760 1.00 26.78 C ANISOU 3869 CG LEU B 137 2927 3520 3729 -360 867 -172 C ATOM 3870 CD1 LEU A 137 24.267 62.322 39.202 1.00 26.51 C ANISOU 3870 CD1 LEU B 137 2914 3485 3672 -417 866 -45 C ATOM 3871 CD2 LEU A 137 22.765 63.283 37.432 1.00 26.48 C ANISOU 3871 CD2 LEU B 137 2907 3412 3741 -300 887 -193 C ATOM 3872 N GLU A 138 20.502 65.967 41.574 1.00 29.32 N ANISOU 3872 N GLU B 138 3063 4274 3802 -355 828 -634 N ATOM 3873 CA GLU A 138 19.501 66.034 42.643 1.00 30.45 C ANISOU 3873 CA GLU B 138 3114 4616 3839 -408 849 -764 C ATOM 3874 C GLU A 138 18.072 66.306 42.141 1.00 31.17 C ANISOU 3874 C GLU B 138 3122 4818 3903 -338 846 -968 C ATOM 3875 O GLU A 138 17.151 65.627 42.583 1.00 31.43 O ANISOU 3875 O GLU B 138 3063 5018 3860 -437 916 -1047 O ATOM 3876 CB GLU A 138 19.895 67.067 43.709 1.00 30.71 C ANISOU 3876 CB GLU B 138 3141 4697 3830 -387 793 -807 C ATOM 3877 CG GLU A 138 18.831 67.340 44.783 1.00 32.36 C ANISOU 3877 CG GLU B 138 3245 5127 3925 -421 805 -971 C ATOM 3878 CD GLU A 138 18.459 66.115 45.616 1.00 33.81 C ANISOU 3878 CD GLU B 138 3392 5437 4015 -601 907 -929 C ATOM 3879 OE1 GLU A 138 19.209 65.126 45.595 1.00 33.72 O ANISOU 3879 OE1 GLU B 138 3468 5326 4020 -685 943 -753 O ATOM 3880 OE2 GLU A 138 17.414 66.141 46.314 1.00 36.28 O ANISOU 3880 OE2 GLU B 138 3605 5955 4224 -664 948 -1083 O ATOM 3881 N PRO A 139 17.873 67.284 41.249 1.00 31.37 N ANISOU 3881 N PRO B 139 3188 4757 3973 -175 764 -1069 N ATOM 3882 CA PRO A 139 16.535 67.522 40.674 1.00 32.29 C ANISOU 3882 CA PRO B 139 3233 4973 4064 -69 736 -1288 C ATOM 3883 C PRO A 139 15.958 66.307 39.942 1.00 32.49 C ANISOU 3883 C PRO B 139 3207 5021 4115 -130 819 -1271 C ATOM 3884 O PRO A 139 14.739 66.132 39.902 1.00 33.27 O ANISOU 3884 O PRO B 139 3184 5292 4164 -120 838 -1465 O ATOM 3885 CB PRO A 139 16.762 68.679 39.693 1.00 32.07 C ANISOU 3885 CB PRO B 139 3342 4762 4080 122 617 -1342 C ATOM 3886 CG PRO A 139 18.235 68.782 39.508 1.00 31.20 C ANISOU 3886 CG PRO B 139 3367 4452 4036 71 623 -1125 C ATOM 3887 CD PRO A 139 18.866 68.249 40.740 1.00 30.88 C ANISOU 3887 CD PRO B 139 3261 4501 3971 -83 686 -1004 C ATOM 3888 N VAL A 140 16.830 65.482 39.375 1.00 31.68 N ANISOU 3888 N VAL B 140 3191 4757 4087 -192 863 -1057 N ATOM 3889 CA VAL A 140 16.415 64.230 38.752 1.00 31.95 C ANISOU 3889 CA VAL B 140 3201 4795 4142 -265 939 -1008 C ATOM 3890 C VAL A 140 16.071 63.177 39.814 1.00 33.01 C ANISOU 3890 C VAL B 140 3272 5092 4179 -476 1039 -979 C ATOM 3891 O VAL A 140 15.061 62.489 39.698 1.00 33.80 O ANISOU 3891 O VAL B 140 3290 5320 4233 -557 1106 -1080 O ATOM 3892 CB VAL A 140 17.495 63.710 37.767 1.00 30.64 C ANISOU 3892 CB VAL B 140 3159 4404 4080 -244 937 -797 C ATOM 3893 CG1 VAL A 140 17.033 62.440 37.068 1.00 30.50 C ANISOU 3893 CG1 VAL B 140 3127 4379 4082 -302 1000 -750 C ATOM 3894 CG2 VAL A 140 17.829 64.793 36.744 1.00 30.42 C ANISOU 3894 CG2 VAL B 140 3224 4211 4122 -70 852 -832 C ATOM 3895 N ARG A 141 16.895 63.068 40.852 1.00 37.82 N ANISOU 3895 N ARG B 141 2898 6288 5185 -794 862 -1463 N ATOM 3896 CA ARG A 141 16.679 62.105 41.936 1.00 38.92 C ANISOU 3896 CA ARG B 141 3002 6551 5235 -973 956 -1398 C ATOM 3897 C ARG A 141 15.345 62.309 42.658 1.00 40.56 C ANISOU 3897 C ARG B 141 3037 6933 5441 -1017 1071 -1525 C ATOM 3898 O ARG A 141 14.654 61.342 42.975 1.00 41.08 O ANISOU 3898 O ARG B 141 3020 7087 5503 -1147 1122 -1486 O ATOM 3899 CB ARG A 141 17.826 62.209 42.952 1.00 39.02 C ANISOU 3899 CB ARG B 141 3136 6585 5105 -1045 992 -1320 C ATOM 3900 CG ARG A 141 17.775 61.234 44.136 1.00 40.79 C ANISOU 3900 CG ARG B 141 3350 6936 5214 -1238 1079 -1222 C ATOM 3901 CD ARG A 141 18.687 61.653 45.288 1.00 42.98 C ANISOU 3901 CD ARG B 141 3716 7282 5334 -1298 1125 -1189 C ATOM 3902 NE ARG A 141 18.221 61.163 46.583 1.00 47.18 N ANISOU 3902 NE ARG B 141 4192 7997 5739 -1468 1240 -1166 N ATOM 3903 CZ ARG A 141 18.503 61.716 47.761 1.00 49.32 C ANISOU 3903 CZ ARG B 141 4484 8399 5857 -1533 1320 -1205 C ATOM 3904 NH1 ARG A 141 18.020 61.175 48.872 1.00 52.58 N ANISOU 3904 NH1 ARG B 141 4844 8987 6148 -1700 1425 -1173 N ATOM 3905 NH2 ARG A 141 19.248 62.812 47.844 1.00 49.88 N ANISOU 3905 NH2 ARG B 141 4630 8433 5890 -1442 1297 -1278 N ATOM 3906 N GLN A 142 14.979 63.561 42.912 1.00 41.09 N ANISOU 3906 N GLN B 142 3047 7047 5519 -909 1114 -1681 N ATOM 3907 CA GLN A 142 13.796 63.846 43.723 1.00 43.13 C ANISOU 3907 CA GLN B 142 3137 7483 5766 -945 1242 -1819 C ATOM 3908 C GLN A 142 12.478 63.595 42.967 1.00 43.63 C ANISOU 3908 C GLN B 142 3028 7579 5972 -903 1224 -1889 C ATOM 3909 O GLN A 142 11.436 63.422 43.593 1.00 44.92 O ANISOU 3909 O GLN B 142 3033 7902 6131 -975 1331 -1968 O ATOM 3910 CB GLN A 142 13.860 65.256 44.349 1.00 44.04 C ANISOU 3910 CB GLN B 142 3248 7637 5848 -848 1308 -1976 C ATOM 3911 CG GLN A 142 14.019 66.430 43.386 1.00 44.10 C ANISOU 3911 CG GLN B 142 3286 7496 5976 -638 1212 -2060 C ATOM 3912 CD GLN A 142 14.196 67.782 44.097 1.00 46.02 C ANISOU 3912 CD GLN B 142 3545 7757 6184 -558 1282 -2210 C ATOM 3913 OE1 GLN A 142 14.513 67.841 45.290 1.00 47.71 O ANISOU 3913 OE1 GLN B 142 3790 8081 6256 -667 1387 -2235 O ATOM 3914 NE2 GLN A 142 13.991 68.866 43.358 1.00 45.72 N ANISOU 3914 NE2 GLN B 142 3490 7607 6275 -373 1220 -2310 N ATOM 3915 N LYS A 143 12.535 63.529 41.635 1.00 42.24 N ANISOU 3915 N LYS B 143 2876 7262 5912 -799 1088 -1854 N ATOM 3916 CA LYS A 143 11.352 63.192 40.827 1.00 43.12 C ANISOU 3916 CA LYS B 143 2830 7402 6153 -770 1048 -1904 C ATOM 3917 C LYS A 143 11.310 61.718 40.372 1.00 42.22 C ANISOU 3917 C LYS B 143 2731 7260 6050 -909 1002 -1772 C ATOM 3918 O LYS A 143 10.236 61.129 40.306 1.00 42.87 O ANISOU 3918 O LYS B 143 2662 7437 6189 -981 1030 -1804 O ATOM 3919 CB LYS A 143 11.244 64.126 39.608 1.00 42.82 C ANISOU 3919 CB LYS B 143 2786 7244 6238 -565 923 -1967 C ATOM 3920 CG LYS A 143 10.417 65.383 39.876 1.00 44.99 C ANISOU 3920 CG LYS B 143 2923 7588 6584 -427 974 -2143 C ATOM 3921 CD LYS A 143 10.747 66.520 38.909 1.00 44.90 C ANISOU 3921 CD LYS B 143 2973 7425 6661 -222 854 -2177 C ATOM 3922 CE LYS A 143 9.894 67.765 39.181 1.00 47.66 C ANISOU 3922 CE LYS B 143 3181 7824 7103 -73 902 -2352 C ATOM 3923 NZ LYS A 143 10.707 68.931 39.656 1.00 47.51 N ANISOU 3923 NZ LYS B 143 3283 7723 7047 15 930 -2406 N ATOM 3924 N TRP A 144 12.467 61.132 40.057 1.00 40.01 N ANISOU 3924 N TRP B 144 2628 6849 5725 -947 934 -1630 N ATOM 3925 CA TRP A 144 12.512 59.774 39.481 1.00 39.53 C ANISOU 3925 CA TRP B 144 2599 6724 5696 -1057 879 -1514 C ATOM 3926 C TRP A 144 13.487 58.798 40.142 1.00 38.65 C ANISOU 3926 C TRP B 144 2624 6572 5488 -1202 908 -1355 C ATOM 3927 O TRP A 144 13.593 57.660 39.712 1.00 38.60 O ANISOU 3927 O TRP B 144 2655 6494 5517 -1292 866 -1257 O ATOM 3928 CB TRP A 144 12.818 59.846 37.984 1.00 38.15 C ANISOU 3928 CB TRP B 144 2489 6397 5611 -937 731 -1502 C ATOM 3929 CG TRP A 144 11.826 60.654 37.231 1.00 38.42 C ANISOU 3929 CG TRP B 144 2387 6464 5747 -802 679 -1631 C ATOM 3930 CD1 TRP A 144 10.572 60.269 36.847 1.00 39.28 C ANISOU 3930 CD1 TRP B 144 2326 6657 5942 -833 669 -1695 C ATOM 3931 CD2 TRP A 144 11.988 62.000 36.780 1.00 37.61 C ANISOU 3931 CD2 TRP B 144 2301 6311 5678 -616 624 -1708 C ATOM 3932 NE1 TRP A 144 9.951 61.290 36.170 1.00 39.42 N ANISOU 3932 NE1 TRP B 144 2249 6683 6046 -668 604 -1802 N ATOM 3933 CE2 TRP A 144 10.799 62.365 36.113 1.00 38.99 C ANISOU 3933 CE2 TRP B 144 2311 6539 5963 -531 576 -1809 C ATOM 3934 CE3 TRP A 144 13.027 62.937 36.857 1.00 36.84 C ANISOU 3934 CE3 TRP B 144 2341 6124 5534 -515 606 -1697 C ATOM 3935 CZ2 TRP A 144 10.617 63.626 35.540 1.00 38.97 C ANISOU 3935 CZ2 TRP B 144 2283 6496 6029 -343 508 -1889 C ATOM 3936 CZ3 TRP A 144 12.844 64.188 36.287 1.00 36.72 C ANISOU 3936 CZ3 TRP B 144 2305 6064 5585 -338 546 -1782 C ATOM 3937 CH2 TRP A 144 11.646 64.520 35.637 1.00 37.25 C ANISOU 3937 CH2 TRP B 144 2211 6178 5765 -250 496 -1873 C ATOM 3938 N GLY A 145 14.180 59.232 41.186 1.00 38.44 N ANISOU 3938 N GLY B 145 2668 6591 5345 -1227 976 -1329 N ATOM 3939 CA GLY A 145 15.091 58.370 41.917 1.00 37.93 C ANISOU 3939 CA GLY B 145 2723 6506 5184 -1362 1000 -1170 C ATOM 3940 C GLY A 145 16.420 58.197 41.206 1.00 36.19 C ANISOU 3940 C GLY B 145 2671 6105 4976 -1296 893 -1064 C ATOM 3941 O GLY A 145 16.602 58.656 40.081 1.00 34.35 O ANISOU 3941 O GLY B 145 2467 5763 4822 -1161 802 -1109 O ATOM 3942 N LEU A 146 17.341 57.523 41.887 1.00 36.29 N ANISOU 3942 N LEU B 146 2790 6093 4907 -1397 905 -917 N ATOM 3943 CA LEU A 146 18.692 57.308 41.397 1.00 35.24 C ANISOU 3943 CA LEU B 146 2809 5804 4777 -1347 819 -807 C ATOM 3944 C LEU A 146 19.189 55.958 41.888 1.00 35.63 C ANISOU 3944 C LEU B 146 2921 5812 4803 -1491 823 -630 C ATOM 3945 O LEU A 146 19.246 55.708 43.097 1.00 36.44 O ANISOU 3945 O LEU B 146 3023 6023 4800 -1613 894 -558 O ATOM 3946 CB LEU A 146 19.628 58.405 41.908 1.00 35.00 C ANISOU 3946 CB LEU B 146 2856 5790 4653 -1274 822 -825 C ATOM 3947 CG LEU A 146 19.837 59.657 41.057 1.00 35.23 C ANISOU 3947 CG LEU B 146 2905 5751 4729 -1098 765 -940 C ATOM 3948 CD1 LEU A 146 20.869 60.529 41.735 1.00 35.71 C ANISOU 3948 CD1 LEU B 146 3055 5826 4688 -1069 775 -931 C ATOM 3949 CD2 LEU A 146 20.299 59.314 39.634 1.00 35.11 C ANISOU 3949 CD2 LEU B 146 2956 5569 4816 -1012 656 -902 C ATOM 3950 N ASP A 147 19.558 55.099 40.945 1.00 35.05 N ANISOU 3950 N ASP B 147 2906 5583 4828 -1478 747 -560 N ATOM 3951 CA ASP A 147 20.079 53.777 41.256 1.00 35.56 C ANISOU 3951 CA ASP B 147 3038 5570 4904 -1595 738 -390 C ATOM 3952 C ASP A 147 21.586 53.666 41.035 1.00 33.83 C ANISOU 3952 C ASP B 147 2955 5217 4681 -1529 669 -281 C ATOM 3953 O ASP A 147 22.292 53.081 41.849 1.00 33.83 O ANISOU 3953 O ASP B 147 3016 5211 4628 -1611 677 -133 O ATOM 3954 CB ASP A 147 19.354 52.720 40.430 1.00 36.46 C ANISOU 3954 CB ASP B 147 3112 5597 5144 -1647 712 -393 C ATOM 3955 CG ASP A 147 19.143 51.451 41.204 1.00 39.92 C ANISOU 3955 CG ASP B 147 3550 6038 5581 -1826 756 -253 C ATOM 3956 OD1 ASP A 147 20.066 50.605 41.215 1.00 43.93 O ANISOU 3956 OD1 ASP B 147 4162 6413 6118 -1853 715 -109 O ATOM 3957 OD2 ASP A 147 18.110 51.231 41.866 1.00 43.85 O ANISOU 3957 OD2 ASP B 147 3947 6665 6048 -1948 833 -270 O ATOM 3958 N ARG A 148 22.077 54.203 39.926 1.00 32.39 N ANISOU 3958 N ARG B 148 2817 4932 4556 -1386 600 -348 N ATOM 3959 CA ARG A 148 23.510 54.170 39.659 1.00 31.05 C ANISOU 3959 CA ARG B 148 2762 4646 4388 -1318 541 -259 C ATOM 3960 C ARG A 148 24.025 55.396 38.906 1.00 29.76 C ANISOU 3960 C ARG B 148 2633 4456 4218 -1165 497 -357 C ATOM 3961 O ARG A 148 23.280 56.079 38.207 1.00 28.99 O ANISOU 3961 O ARG B 148 2483 4379 4154 -1092 486 -489 O ATOM 3962 CB ARG A 148 23.903 52.866 38.944 1.00 31.09 C ANISOU 3962 CB ARG B 148 2821 4485 4505 -1339 494 -170 C ATOM 3963 CG ARG A 148 23.783 52.873 37.424 1.00 30.72 C ANISOU 3963 CG ARG B 148 2784 4327 4560 -1239 436 -270 C ATOM 3964 CD ARG A 148 24.246 51.577 36.774 1.00 31.63 C ANISOU 3964 CD ARG B 148 2960 4275 4784 -1261 399 -195 C ATOM 3965 NE ARG A 148 25.661 51.314 37.038 1.00 32.01 N ANISOU 3965 NE ARG B 148 3099 4238 4828 -1230 376 -70 N ATOM 3966 CZ ARG A 148 26.344 50.276 36.553 1.00 32.18 C ANISOU 3966 CZ ARG B 148 3180 4099 4946 -1225 345 4 C ATOM 3967 NH1 ARG A 148 25.760 49.393 35.761 1.00 33.23 N ANISOU 3967 NH1 ARG B 148 3306 4135 5186 -1257 335 -42 N ATOM 3968 NH2 ARG A 148 27.628 50.123 36.855 1.00 32.09 N ANISOU 3968 NH2 ARG B 148 3233 4026 4932 -1187 324 117 N ATOM 3969 N ILE A 149 25.319 55.651 39.088 1.00 28.71 N ANISOU 3969 N ILE B 149 2587 4279 4044 -1124 467 -280 N ATOM 3970 CA ILE A 149 26.036 56.706 38.394 1.00 27.77 C ANISOU 3970 CA ILE B 149 2517 4116 3918 -994 423 -343 C ATOM 3971 C ILE A 149 27.342 56.143 37.867 1.00 26.55 C ANISOU 3971 C ILE B 149 2450 3829 3807 -956 369 -241 C ATOM 3972 O ILE A 149 28.074 55.451 38.582 1.00 26.54 O ANISOU 3972 O ILE B 149 2482 3814 3787 -1019 371 -107 O ATOM 3973 CB ILE A 149 26.341 57.902 39.327 1.00 27.66 C ANISOU 3973 CB ILE B 149 2506 4212 3789 -985 454 -376 C ATOM 3974 CG1 ILE A 149 25.063 58.454 39.956 1.00 29.48 C ANISOU 3974 CG1 ILE B 149 2642 4581 3978 -1022 522 -487 C ATOM 3975 CG2 ILE A 149 27.056 59.012 38.549 1.00 27.13 C ANISOU 3975 CG2 ILE B 149 2495 4087 3728 -858 406 -439 C ATOM 3976 CD1 ILE A 149 25.318 59.514 41.010 1.00 30.95 C ANISOU 3976 CD1 ILE B 149 2832 4881 4046 -1032 566 -528 C ATOM 3977 N ILE A 150 27.626 56.431 36.606 1.00 25.89 N ANISOU 3977 N ILE B 150 2400 3654 3783 -853 322 -302 N ATOM 3978 CA ILE A 150 28.963 56.239 36.062 1.00 24.89 C ANISOU 3978 CA ILE B 150 2351 3421 3684 -795 280 -234 C ATOM 3979 C ILE A 150 29.409 57.567 35.507 1.00 23.89 C ANISOU 3979 C ILE B 150 2256 3302 3520 -694 255 -311 C ATOM 3980 O ILE A 150 28.740 58.136 34.640 1.00 23.49 O ANISOU 3980 O ILE B 150 2188 3245 3490 -633 238 -418 O ATOM 3981 CB ILE A 150 28.970 55.184 34.946 1.00 24.95 C ANISOU 3981 CB ILE B 150 2379 3300 3802 -777 253 -233 C ATOM 3982 CG1 ILE A 150 28.597 53.816 35.505 1.00 26.25 C ANISOU 3982 CG1 ILE B 150 2523 3432 4020 -884 275 -146 C ATOM 3983 CG2 ILE A 150 30.350 55.145 34.264 1.00 24.83 C ANISOU 3983 CG2 ILE B 150 2435 3185 3814 -700 219 -190 C ATOM 3984 CD1 ILE A 150 28.270 52.796 34.447 1.00 27.46 C ANISOU 3984 CD1 ILE B 150 2685 3465 4285 -884 256 -179 C ATOM 3985 N VAL A 151 30.557 58.054 35.967 1.00 23.18 N ANISOU 3985 N VAL B 151 2211 3221 3376 -679 247 -250 N ATOM 3986 CA VAL A 151 31.038 59.350 35.515 1.00 22.24 C ANISOU 3986 CA VAL B 151 2126 3104 3220 -598 226 -315 C ATOM 3987 C VAL A 151 32.494 59.259 35.052 1.00 21.35 C ANISOU 3987 C VAL B 151 2075 2916 3123 -556 195 -242 C ATOM 3988 O VAL A 151 33.312 58.538 35.632 1.00 21.24 O ANISOU 3988 O VAL B 151 2069 2889 3111 -597 194 -130 O ATOM 3989 CB VAL A 151 30.815 60.434 36.607 1.00 22.51 C ANISOU 3989 CB VAL B 151 2141 3250 3160 -624 257 -357 C ATOM 3990 CG1 VAL A 151 31.491 60.045 37.916 1.00 24.24 C ANISOU 3990 CG1 VAL B 151 2365 3535 3309 -714 276 -247 C ATOM 3991 CG2 VAL A 151 31.278 61.809 36.142 1.00 21.87 C ANISOU 3991 CG2 VAL B 151 2102 3153 3054 -544 234 -425 C ATOM 3992 N SER A 152 32.780 59.961 33.962 1.00 20.63 N ANISOU 3992 N SER B 152 2020 2774 3045 -474 168 -303 N ATOM 3993 CA SER A 152 34.138 60.168 33.468 1.00 19.99 C ANISOU 3993 CA SER B 152 1989 2640 2965 -431 147 -256 C ATOM 3994 C SER A 152 34.348 61.670 33.463 1.00 19.83 C ANISOU 3994 C SER B 152 1996 2654 2883 -396 137 -312 C ATOM 3995 O SER A 152 33.555 62.400 32.875 1.00 20.27 O ANISOU 3995 O SER B 152 2055 2708 2940 -351 127 -403 O ATOM 3996 CB SER A 152 34.291 59.602 32.052 1.00 19.72 C ANISOU 3996 CB SER B 152 1981 2512 3000 -376 130 -280 C ATOM 3997 OG SER A 152 34.144 58.192 32.029 1.00 18.78 O ANISOU 3997 OG SER B 152 1843 2340 2953 -409 140 -236 O ATOM 3998 N THR A 153 35.397 62.141 34.128 1.00 20.26 N ANISOU 3998 N THR B 153 2070 2739 2889 -418 136 -258 N ATOM 3999 CA THR A 153 35.617 63.576 34.279 1.00 20.20 C ANISOU 3999 CA THR B 153 2092 2759 2824 -401 130 -312 C ATOM 4000 C THR A 153 36.722 64.089 33.377 1.00 19.90 C ANISOU 4000 C THR B 153 2104 2663 2793 -356 106 -294 C ATOM 4001 O THR A 153 37.588 63.344 32.917 1.00 19.96 O ANISOU 4001 O THR B 153 2116 2631 2836 -347 101 -227 O ATOM 4002 CB THR A 153 35.947 63.947 35.729 1.00 20.40 C ANISOU 4002 CB THR B 153 2104 2874 2771 -474 146 -283 C ATOM 4003 OG1 THR A 153 37.276 63.497 36.067 1.00 20.73 O ANISOU 4003 OG1 THR B 153 2153 2922 2803 -506 130 -173 O ATOM 4004 CG2 THR A 153 35.022 63.247 36.711 1.00 21.11 C ANISOU 4004 CG2 THR B 153 2142 3036 2840 -539 178 -275 C ATOM 4005 N TYR A 154 36.668 65.398 33.177 1.00 20.38 N ANISOU 4005 N TYR B 154 2201 2719 2824 -330 96 -357 N ATOM 4006 CA TYR A 154 37.547 66.153 32.304 1.00 20.10 C ANISOU 4006 CA TYR B 154 2219 2632 2786 -295 76 -352 C ATOM 4007 C TYR A 154 37.917 67.355 33.159 1.00 20.09 C ANISOU 4007 C TYR B 154 2239 2665 2729 -331 76 -375 C ATOM 4008 O TYR A 154 37.288 68.402 33.078 1.00 20.51 O ANISOU 4008 O TYR B 154 2317 2699 2776 -304 70 -453 O ATOM 4009 CB TYR A 154 36.802 66.606 31.035 1.00 19.91 C ANISOU 4009 CB TYR B 154 2226 2549 2789 -225 53 -416 C ATOM 4010 CG TYR A 154 36.264 65.493 30.143 1.00 20.41 C ANISOU 4010 CG TYR B 154 2271 2584 2899 -196 49 -418 C ATOM 4011 CD1 TYR A 154 36.728 65.329 28.845 1.00 20.71 C ANISOU 4011 CD1 TYR B 154 2348 2572 2949 -160 36 -409 C ATOM 4012 CD2 TYR A 154 35.245 64.645 30.581 1.00 21.25 C ANISOU 4012 CD2 TYR B 154 2323 2718 3034 -214 61 -439 C ATOM 4013 CE1 TYR A 154 36.218 64.327 28.020 1.00 21.54 C ANISOU 4013 CE1 TYR B 154 2440 2653 3091 -141 32 -428 C ATOM 4014 CE2 TYR A 154 34.749 63.639 29.780 1.00 20.88 C ANISOU 4014 CE2 TYR B 154 2262 2640 3033 -199 56 -450 C ATOM 4015 CZ TYR A 154 35.234 63.479 28.498 1.00 21.36 C ANISOU 4015 CZ TYR B 154 2364 2649 3103 -161 40 -449 C ATOM 4016 OH TYR A 154 34.713 62.487 27.697 1.00 19.99 O ANISOU 4016 OH TYR B 154 2180 2447 2970 -153 35 -476 O ATOM 4017 N GLN A 155 38.915 67.189 34.018 1.00 20.40 N ANISOU 4017 N GLN B 155 2266 2754 2731 -393 80 -309 N ATOM 4018 CA GLN A 155 39.154 68.149 35.093 1.00 21.16 C ANISOU 4018 CA GLN B 155 2373 2905 2763 -450 84 -340 C ATOM 4019 C GLN A 155 40.312 69.098 34.782 1.00 21.25 C ANISOU 4019 C GLN B 155 2429 2887 2757 -464 65 -326 C ATOM 4020 O GLN A 155 41.320 68.704 34.195 1.00 21.29 O ANISOU 4020 O GLN B 155 2433 2873 2783 -460 55 -252 O ATOM 4021 CB GLN A 155 39.384 67.414 36.421 1.00 21.48 C ANISOU 4021 CB GLN B 155 2366 3043 2752 -529 94 -280 C ATOM 4022 CG GLN A 155 38.095 66.882 37.045 1.00 22.07 C ANISOU 4022 CG GLN B 155 2402 3166 2818 -542 123 -318 C ATOM 4023 CD GLN A 155 38.332 66.046 38.278 1.00 22.75 C ANISOU 4023 CD GLN B 155 2446 3348 2848 -627 130 -235 C ATOM 4024 OE1 GLN A 155 38.155 64.824 38.238 1.00 25.60 O ANISOU 4024 OE1 GLN B 155 2775 3704 3248 -631 131 -160 O ATOM 4025 NE2 GLN A 155 38.733 66.690 39.380 1.00 20.76 N ANISOU 4025 NE2 GLN B 155 2200 3183 2504 -702 132 -246 N ATOM 4026 N ALA A 156 40.123 70.355 35.157 1.00 21.56 N ANISOU 4026 N ALA B 156 2507 2919 2766 -480 65 -404 N ATOM 4027 CA ALA A 156 41.103 71.412 35.004 1.00 22.24 C ANISOU 4027 CA ALA B 156 2642 2973 2834 -510 49 -404 C ATOM 4028 C ALA A 156 42.230 71.330 36.032 1.00 22.87 C ANISOU 4028 C ALA B 156 2696 3140 2855 -605 41 -348 C ATOM 4029 O ALA A 156 42.060 70.803 37.134 1.00 22.85 O ANISOU 4029 O ALA B 156 2652 3228 2803 -656 49 -336 O ATOM 4030 CB ALA A 156 40.403 72.751 35.101 1.00 22.94 C ANISOU 4030 CB ALA B 156 2783 3009 2926 -493 51 -515 C ATOM 4031 N VAL A 157 43.375 71.896 35.665 1.00 23.34 N ANISOU 4031 N VAL B 157 2779 3176 2912 -636 24 -313 N ATOM 4032 CA VAL A 157 44.594 71.790 36.464 1.00 23.81 C ANISOU 4032 CA VAL B 157 2802 3320 2923 -725 5 -247 C ATOM 4033 C VAL A 157 44.591 72.650 37.723 1.00 24.41 C ANISOU 4033 C VAL B 157 2895 3458 2921 -813 1 -316 C ATOM 4034 O VAL A 157 45.336 72.360 38.655 1.00 24.89 O ANISOU 4034 O VAL B 157 2914 3621 2923 -894 -20 -264 O ATOM 4035 CB VAL A 157 45.860 72.087 35.613 1.00 23.84 C ANISOU 4035 CB VAL B 157 2813 3291 2955 -736 -8 -188 C ATOM 4036 CG1 VAL A 157 46.007 71.036 34.515 1.00 23.84 C ANISOU 4036 CG1 VAL B 157 2782 3257 3019 -660 4 -120 C ATOM 4037 CG2 VAL A 157 45.838 73.490 35.020 1.00 24.40 C ANISOU 4037 CG2 VAL B 157 2966 3272 3035 -740 -7 -257 C ATOM 4038 N SER A 158 43.767 73.698 37.752 1.00 24.51 N ANISOU 4038 N SER B 158 2966 3411 2935 -797 18 -435 N ATOM 4039 CA SER A 158 43.667 74.571 38.933 1.00 25.35 C ANISOU 4039 CA SER B 158 3095 3567 2969 -878 25 -530 C ATOM 4040 C SER A 158 43.122 73.833 40.153 1.00 26.06 C ANISOU 4040 C SER B 158 3134 3785 2984 -921 42 -536 C ATOM 4041 O SER A 158 43.274 74.301 41.274 1.00 26.44 O ANISOU 4041 O SER B 158 3186 3915 2944 -1012 45 -592 O ATOM 4042 CB SER A 158 42.806 75.812 38.655 1.00 25.75 C ANISOU 4042 CB SER B 158 3216 3508 3060 -834 45 -664 C ATOM 4043 OG SER A 158 41.458 75.463 38.350 1.00 24.89 O ANISOU 4043 OG SER B 158 3094 3368 2995 -739 71 -711 O ATOM 4044 N GLY A 159 42.488 72.684 39.928 1.00 26.19 N ANISOU 4044 N GLY B 159 3105 3817 3028 -865 54 -480 N ATOM 4045 CA GLY A 159 42.148 71.768 41.007 1.00 27.01 C ANISOU 4045 CA GLY B 159 3156 4046 3062 -916 65 -443 C ATOM 4046 C GLY A 159 43.364 71.299 41.787 1.00 27.69 C ANISOU 4046 C GLY B 159 3204 4239 3076 -1011 23 -331 C ATOM 4047 O GLY A 159 43.293 71.143 43.006 1.00 28.72 O ANISOU 4047 O GLY B 159 3315 4493 3104 -1098 23 -331 O ATOM 4048 N ALA A 160 44.474 71.074 41.084 1.00 27.41 N ANISOU 4048 N ALA B 160 3155 4167 3093 -995 -15 -235 N ATOM 4049 CA ALA A 160 45.755 70.717 41.715 1.00 28.30 C ANISOU 4049 CA ALA B 160 3219 4376 3155 -1076 -66 -125 C ATOM 4050 C ALA A 160 46.567 71.918 42.241 1.00 29.33 C ANISOU 4050 C ALA B 160 3378 4549 3218 -1173 -90 -183 C ATOM 4051 O ALA A 160 47.694 71.739 42.717 1.00 30.06 O ANISOU 4051 O ALA B 160 3424 4726 3270 -1245 -141 -96 O ATOM 4052 CB ALA A 160 46.604 69.905 40.747 1.00 27.69 C ANISOU 4052 CB ALA B 160 3099 4249 3174 -1013 -89 -4 C ATOM 4053 N GLY A 161 46.011 73.126 42.142 1.00 29.46 N ANISOU 4053 N GLY B 161 3465 4500 3230 -1175 -58 -327 N ATOM 4054 CA GLY A 161 46.602 74.313 42.744 1.00 30.60 C ANISOU 4054 CA GLY B 161 3647 4672 3309 -1277 -74 -409 C ATOM 4055 C GLY A 161 47.390 75.179 41.767 1.00 30.35 C ANISOU 4055 C GLY B 161 3653 4531 3349 -1270 -87 -416 C ATOM 4056 O GLY A 161 47.555 74.832 40.596 1.00 29.42 O ANISOU 4056 O GLY B 161 3529 4327 3323 -1186 -84 -351 O ATOM 4057 N MET A 162 47.897 76.303 42.266 1.00 31.51 N ANISOU 4057 N MET B 162 3841 4685 3448 -1368 -100 -497 N ATOM 4058 CA MET A 162 48.589 77.292 41.432 1.00 31.69 C ANISOU 4058 CA MET B 162 3911 4597 3533 -1383 -109 -516 C ATOM 4059 C MET A 162 49.828 76.722 40.730 1.00 30.39 C ANISOU 4059 C MET B 162 3681 4454 3411 -1386 -143 -370 C ATOM 4060 O MET A 162 50.044 76.984 39.553 1.00 29.80 O ANISOU 4060 O MET B 162 3632 4272 3418 -1333 -129 -345 O ATOM 4061 CB MET A 162 48.963 78.520 42.272 1.00 33.68 C ANISOU 4061 CB MET B 162 4213 4865 3718 -1510 -121 -631 C ATOM 4062 CG MET A 162 49.543 79.696 41.483 1.00 36.74 C ANISOU 4062 CG MET B 162 4666 5117 4174 -1539 -125 -666 C ATOM 4063 SD MET A 162 48.465 80.323 40.153 1.00 42.43 S ANISOU 4063 SD MET B 162 5481 5619 5021 -1396 -81 -723 S ATOM 4064 CE MET A 162 49.097 82.048 40.012 1.00 43.84 C ANISOU 4064 CE MET B 162 5760 5665 5233 -1499 -91 -813 C ATOM 4065 N GLY A 163 50.634 75.945 41.444 1.00 29.84 N ANISOU 4065 N GLY B 163 3524 4528 3285 -1447 -186 -273 N ATOM 4066 CA GLY A 163 51.808 75.315 40.856 1.00 29.22 C ANISOU 4066 CA GLY B 163 3363 4483 3258 -1440 -215 -137 C ATOM 4067 C GLY A 163 51.491 74.521 39.596 1.00 27.71 C ANISOU 4067 C GLY B 163 3160 4201 3169 -1304 -179 -75 C ATOM 4068 O GLY A 163 52.234 74.574 38.617 1.00 27.05 O ANISOU 4068 O GLY B 163 3058 4072 3149 -1283 -172 -25 O ATOM 4069 N ALA A 164 50.381 73.787 39.624 1.00 26.59 N ANISOU 4069 N ALA B 164 3027 4039 3035 -1219 -154 -84 N ATOM 4070 CA ALA A 164 49.943 72.996 38.478 1.00 25.50 C ANISOU 4070 CA ALA B 164 2884 3818 2986 -1095 -122 -41 C ATOM 4071 C ALA A 164 49.572 73.887 37.299 1.00 24.74 C ANISOU 4071 C ALA B 164 2872 3585 2944 -1047 -88 -110 C ATOM 4072 O ALA A 164 49.931 73.591 36.167 1.00 24.19 O ANISOU 4072 O ALA B 164 2792 3463 2936 -990 -72 -61 O ATOM 4073 CB ALA A 164 48.762 72.124 38.862 1.00 25.02 C ANISOU 4073 CB ALA B 164 2819 3768 2918 -1036 -105 -49 C ATOM 4074 N ILE A 165 48.853 74.973 37.577 1.00 24.74 N ANISOU 4074 N ILE B 165 2953 3530 2918 -1069 -78 -225 N ATOM 4075 CA ILE A 165 48.492 75.952 36.555 1.00 24.57 C ANISOU 4075 CA ILE B 165 3019 3370 2947 -1030 -59 -283 C ATOM 4076 C ILE A 165 49.751 76.482 35.855 1.00 24.72 C ANISOU 4076 C ILE B 165 3040 3367 2988 -1085 -68 -228 C ATOM 4077 O ILE A 165 49.809 76.560 34.626 1.00 24.14 O ANISOU 4077 O ILE B 165 2995 3214 2964 -1032 -50 -197 O ATOM 4078 CB ILE A 165 47.707 77.153 37.165 1.00 25.11 C ANISOU 4078 CB ILE B 165 3167 3381 2993 -1058 -53 -418 C ATOM 4079 CG1 ILE A 165 46.352 76.716 37.731 1.00 25.07 C ANISOU 4079 CG1 ILE B 165 3157 3396 2973 -997 -31 -486 C ATOM 4080 CG2 ILE A 165 47.494 78.238 36.102 1.00 26.01 C ANISOU 4080 CG2 ILE B 165 3373 3339 3169 -1023 -46 -457 C ATOM 4081 CD1 ILE A 165 45.632 77.819 38.518 1.00 25.89 C ANISOU 4081 CD1 ILE B 165 3321 3465 3051 -1027 -16 -632 C ATOM 4082 N LEU A 166 50.749 76.849 36.646 1.00 25.46 N ANISOU 4082 N LEU B 166 3099 3540 3035 -1201 -95 -217 N ATOM 4083 CA LEU A 166 51.949 77.486 36.111 1.00 25.91 C ANISOU 4083 CA LEU B 166 3153 3583 3109 -1276 -102 -176 C ATOM 4084 C LEU A 166 52.753 76.477 35.293 1.00 25.47 C ANISOU 4084 C LEU B 166 3009 3574 3094 -1232 -89 -60 C ATOM 4085 O LEU A 166 53.278 76.820 34.243 1.00 25.68 O ANISOU 4085 O LEU B 166 3052 3549 3158 -1233 -67 -29 O ATOM 4086 CB LEU A 166 52.798 78.096 37.235 1.00 27.00 C ANISOU 4086 CB LEU B 166 3266 3809 3185 -1421 -140 -200 C ATOM 4087 CG LEU A 166 52.140 79.197 38.077 1.00 28.12 C ANISOU 4087 CG LEU B 166 3497 3903 3283 -1482 -145 -336 C ATOM 4088 CD1 LEU A 166 53.041 79.580 39.247 1.00 30.00 C ANISOU 4088 CD1 LEU B 166 3696 4258 3444 -1633 -188 -356 C ATOM 4089 CD2 LEU A 166 51.784 80.432 37.251 1.00 28.81 C ANISOU 4089 CD2 LEU B 166 3702 3817 3429 -1472 -123 -403 C ATOM 4090 N GLU A 167 52.804 75.233 35.764 1.00 25.09 N ANISOU 4090 N GLU B 167 2871 3620 3043 -1191 -101 1 N ATOM 4091 CA GLU A 167 53.457 74.134 35.055 1.00 25.05 C ANISOU 4091 CA GLU B 167 2775 3649 3092 -1128 -85 99 C ATOM 4092 C GLU A 167 52.817 73.868 33.689 1.00 24.15 C ANISOU 4092 C GLU B 167 2713 3433 3031 -1021 -36 90 C ATOM 4093 O GLU A 167 53.514 73.629 32.705 1.00 24.41 O ANISOU 4093 O GLU B 167 2713 3460 3103 -1000 -5 137 O ATOM 4094 CB GLU A 167 53.401 72.857 35.907 1.00 25.19 C ANISOU 4094 CB GLU B 167 2705 3760 3106 -1095 -112 161 C ATOM 4095 CG GLU A 167 53.800 71.582 35.181 1.00 25.61 C ANISOU 4095 CG GLU B 167 2675 3819 3236 -1003 -90 246 C ATOM 4096 CD GLU A 167 54.124 70.458 36.142 1.00 27.12 C ANISOU 4096 CD GLU B 167 2765 4107 3432 -996 -133 333 C ATOM 4097 OE1 GLU A 167 53.352 69.468 36.214 1.00 25.11 O ANISOU 4097 OE1 GLU B 167 2508 3828 3204 -918 -125 352 O ATOM 4098 OE2 GLU A 167 55.155 70.583 36.836 1.00 28.63 O ANISOU 4098 OE2 GLU B 167 2880 4398 3601 -1074 -179 388 O ATOM 4099 N THR A 168 51.491 73.905 33.642 1.00 23.11 N ANISOU 4099 N THR B 168 2655 3231 2896 -957 -28 26 N ATOM 4100 CA THR A 168 50.743 73.644 32.415 1.00 22.59 C ANISOU 4100 CA THR B 168 2638 3076 2868 -859 5 12 C ATOM 4101 C THR A 168 51.073 74.674 31.347 1.00 22.55 C ANISOU 4101 C THR B 168 2705 2995 2868 -883 23 4 C ATOM 4102 O THR A 168 51.308 74.335 30.199 1.00 21.99 O ANISOU 4102 O THR B 168 2633 2903 2819 -840 55 38 O ATOM 4103 CB THR A 168 49.231 73.674 32.708 1.00 22.26 C ANISOU 4103 CB THR B 168 2655 2982 2820 -800 0 -63 C ATOM 4104 OG1 THR A 168 48.888 72.586 33.582 1.00 21.21 O ANISOU 4104 OG1 THR B 168 2457 2921 2682 -779 -8 -42 O ATOM 4105 CG2 THR A 168 48.414 73.440 31.431 1.00 22.34 C ANISOU 4105 CG2 THR B 168 2714 2909 2865 -703 23 -78 C ATOM 4106 N GLN A 169 51.083 75.935 31.754 1.00 23.11 N ANISOU 4106 N GLN B 169 2841 3024 2914 -958 3 -43 N ATOM 4107 CA GLN A 169 51.405 77.045 30.863 1.00 23.68 C ANISOU 4107 CA GLN B 169 2993 3012 2991 -1000 13 -42 C ATOM 4108 C GLN A 169 52.854 76.993 30.400 1.00 23.50 C ANISOU 4108 C GLN B 169 2907 3052 2969 -1071 34 33 C ATOM 4109 O GLN A 169 53.138 77.292 29.252 1.00 23.10 O ANISOU 4109 O GLN B 169 2894 2959 2925 -1072 64 66 O ATOM 4110 CB GLN A 169 51.117 78.379 31.551 1.00 24.36 C ANISOU 4110 CB GLN B 169 3161 3030 3065 -1069 -15 -115 C ATOM 4111 CG GLN A 169 49.637 78.578 31.844 1.00 24.92 C ANISOU 4111 CG GLN B 169 3295 3026 3146 -989 -26 -200 C ATOM 4112 CD GLN A 169 49.379 79.822 32.643 1.00 26.99 C ANISOU 4112 CD GLN B 169 3628 3223 3405 -1052 -45 -290 C ATOM 4113 OE1 GLN A 169 49.882 79.956 33.757 1.00 27.61 O ANISOU 4113 OE1 GLN B 169 3670 3376 3445 -1141 -57 -321 O ATOM 4114 NE2 GLN A 169 48.609 80.749 32.078 1.00 27.42 N ANISOU 4114 NE2 GLN B 169 3783 3137 3500 -1009 -52 -334 N ATOM 4115 N ARG A 170 53.760 76.602 31.293 1.00 23.74 N ANISOU 4115 N ARG B 170 2837 3193 2991 -1133 19 63 N ATOM 4116 CA ARG A 170 55.181 76.475 30.948 1.00 24.71 C ANISOU 4116 CA ARG B 170 2871 3394 3124 -1199 39 134 C ATOM 4117 C ARG A 170 55.406 75.393 29.892 1.00 24.09 C ANISOU 4117 C ARG B 170 2732 3340 3080 -1108 89 185 C ATOM 4118 O ARG A 170 56.137 75.594 28.923 1.00 24.63 O ANISOU 4118 O ARG B 170 2790 3414 3156 -1135 133 219 O ATOM 4119 CB ARG A 170 55.990 76.143 32.201 1.00 25.21 C ANISOU 4119 CB ARG B 170 2824 3581 3175 -1268 -2 159 C ATOM 4120 CG ARG A 170 57.477 76.372 32.069 1.00 28.15 C ANISOU 4120 CG ARG B 170 3105 4036 3557 -1366 4 217 C ATOM 4121 CD ARG A 170 58.290 75.107 31.879 1.00 30.24 C ANISOU 4121 CD ARG B 170 3219 4402 3867 -1309 22 295 C ATOM 4122 NE ARG A 170 58.051 74.133 32.946 1.00 30.16 N ANISOU 4122 NE ARG B 170 3139 4460 3859 -1262 -26 318 N ATOM 4123 CZ ARG A 170 57.949 72.817 32.758 1.00 31.67 C ANISOU 4123 CZ ARG B 170 3258 4672 4102 -1150 -11 363 C ATOM 4124 NH1 ARG A 170 58.101 72.275 31.538 1.00 29.30 N ANISOU 4124 NH1 ARG B 170 2939 4338 3854 -1070 56 376 N ATOM 4125 NH2 ARG A 170 57.714 72.029 33.809 1.00 32.49 N ANISOU 4125 NH2 ARG B 170 3310 4832 4203 -1123 -62 394 N ATOM 4126 N GLU A 171 54.769 74.249 30.096 1.00 23.40 N ANISOU 4126 N GLU B 171 2608 3267 3014 -1007 87 184 N ATOM 4127 CA GLU A 171 54.848 73.120 29.173 1.00 23.43 C ANISOU 4127 CA GLU B 171 2561 3281 3058 -913 135 213 C ATOM 4128 C GLU A 171 54.307 73.484 27.793 1.00 23.08 C ANISOU 4128 C GLU B 171 2616 3156 3000 -875 176 188 C ATOM 4129 O GLU A 171 54.931 73.185 26.790 1.00 22.79 O ANISOU 4129 O GLU B 171 2547 3141 2970 -865 230 213 O ATOM 4130 CB GLU A 171 54.069 71.931 29.739 1.00 22.89 C ANISOU 4130 CB GLU B 171 2459 3220 3019 -822 117 208 C ATOM 4131 CG GLU A 171 54.840 71.188 30.820 1.00 23.64 C ANISOU 4131 CG GLU B 171 2430 3413 3139 -840 85 267 C ATOM 4132 CD GLU A 171 54.013 70.124 31.516 1.00 23.97 C ANISOU 4132 CD GLU B 171 2452 3455 3201 -770 60 273 C ATOM 4133 OE1 GLU A 171 54.393 69.734 32.641 1.00 25.35 O ANISOU 4133 OE1 GLU B 171 2554 3705 3373 -801 15 322 O ATOM 4134 OE2 GLU A 171 52.993 69.671 30.945 1.00 23.18 O ANISOU 4134 OE2 GLU B 171 2408 3284 3115 -691 83 234 O ATOM 4135 N LEU A 172 53.150 74.136 27.762 1.00 23.09 N ANISOU 4135 N LEU B 172 2730 3068 2976 -856 149 138 N ATOM 4136 CA LEU A 172 52.506 74.524 26.503 1.00 23.43 C ANISOU 4136 CA LEU B 172 2873 3032 2999 -818 168 123 C ATOM 4137 C LEU A 172 53.381 75.513 25.737 1.00 24.33 C ANISOU 4137 C LEU B 172 3025 3136 3084 -908 194 161 C ATOM 4138 O LEU A 172 53.558 75.377 24.534 1.00 24.53 O ANISOU 4138 O LEU B 172 3070 3161 3087 -893 238 184 O ATOM 4139 CB LEU A 172 51.115 75.131 26.760 1.00 23.24 C ANISOU 4139 CB LEU B 172 2950 2915 2967 -779 122 67 C ATOM 4140 CG LEU A 172 50.008 74.140 27.134 1.00 22.91 C ANISOU 4140 CG LEU B 172 2886 2874 2947 -683 108 27 C ATOM 4141 CD1 LEU A 172 48.789 74.861 27.696 1.00 24.62 C ANISOU 4141 CD1 LEU B 172 3175 3018 3162 -662 65 -36 C ATOM 4142 CD2 LEU A 172 49.607 73.305 25.931 1.00 23.33 C ANISOU 4142 CD2 LEU B 172 2945 2918 3002 -604 138 29 C ATOM 4143 N ARG A 173 53.940 76.500 26.437 1.00 24.91 N ANISOU 4143 N ARG B 173 3108 3204 3151 -1011 169 167 N ATOM 4144 CA ARG A 173 54.867 77.446 25.808 1.00 25.91 C ANISOU 4144 CA ARG B 173 3264 3325 3257 -1117 194 210 C ATOM 4145 C ARG A 173 56.110 76.750 25.244 1.00 26.26 C ANISOU 4145 C ARG B 173 3192 3480 3304 -1141 259 261 C ATOM 4146 O ARG A 173 56.563 77.091 24.160 1.00 27.26 O ANISOU 4146 O ARG B 173 3348 3608 3402 -1181 307 296 O ATOM 4147 CB ARG A 173 55.271 78.553 26.788 1.00 26.55 C ANISOU 4147 CB ARG B 173 3366 3382 3339 -1232 153 196 C ATOM 4148 CG ARG A 173 54.163 79.569 27.032 1.00 26.37 C ANISOU 4148 CG ARG B 173 3479 3223 3318 -1223 106 143 C ATOM 4149 CD ARG A 173 54.453 80.545 28.148 1.00 27.06 C ANISOU 4149 CD ARG B 173 3587 3285 3411 -1328 67 102 C ATOM 4150 NE ARG A 173 53.424 81.574 28.237 1.00 26.61 N ANISOU 4150 NE ARG B 173 3662 3079 3369 -1310 32 45 N ATOM 4151 CZ ARG A 173 52.753 81.910 29.340 1.00 27.34 C ANISOU 4151 CZ ARG B 173 3779 3136 3474 -1303 -4 -42 C ATOM 4152 NH1 ARG A 173 52.978 81.306 30.498 1.00 27.01 N ANISOU 4152 NH1 ARG B 173 3646 3204 3413 -1321 -15 -75 N ATOM 4153 NH2 ARG A 173 51.834 82.868 29.282 1.00 28.34 N ANISOU 4153 NH2 ARG B 173 4022 3117 3630 -1274 -29 -96 N ATOM 4154 N GLU A 174 56.643 75.766 25.963 1.00 26.05 N ANISOU 4154 N GLU B 174 3034 3549 3316 -1114 261 267 N ATOM 4155 CA GLU A 174 57.811 75.012 25.499 1.00 26.91 C ANISOU 4155 CA GLU B 174 3013 3763 3449 -1117 323 307 C ATOM 4156 C GLU A 174 57.517 74.312 24.176 1.00 26.27 C ANISOU 4156 C GLU B 174 2951 3673 3356 -1032 390 298 C ATOM 4157 O GLU A 174 58.315 74.370 23.253 1.00 26.21 O ANISOU 4157 O GLU B 174 2913 3715 3332 -1071 459 321 O ATOM 4158 CB GLU A 174 58.257 73.971 26.534 1.00 27.03 C ANISOU 4158 CB GLU B 174 2886 3863 3520 -1077 299 320 C ATOM 4159 CG GLU A 174 59.245 74.484 27.567 1.00 29.40 C ANISOU 4159 CG GLU B 174 3103 4239 3827 -1188 257 351 C ATOM 4160 CD GLU A 174 60.196 73.406 28.068 1.00 30.76 C ANISOU 4160 CD GLU B 174 3098 4528 4062 -1156 258 397 C ATOM 4161 OE1 GLU A 174 59.824 72.655 28.969 1.00 29.75 O ANISOU 4161 OE1 GLU B 174 2930 4415 3959 -1097 208 403 O ATOM 4162 OE2 GLU A 174 61.328 73.319 27.565 1.00 35.63 O ANISOU 4162 OE2 GLU B 174 3611 5221 4706 -1191 309 430 O ATOM 4163 N VAL A 175 56.363 73.653 24.098 1.00 25.50 N ANISOU 4163 N VAL B 175 2904 3521 3266 -925 371 258 N ATOM 4164 CA VAL A 175 55.952 72.954 22.879 1.00 25.41 C ANISOU 4164 CA VAL B 175 2919 3499 3236 -846 426 235 C ATOM 4165 C VAL A 175 55.751 73.946 21.735 1.00 25.96 C ANISOU 4165 C VAL B 175 3110 3526 3228 -900 445 248 C ATOM 4166 O VAL A 175 56.297 73.776 20.647 1.00 26.08 O ANISOU 4166 O VAL B 175 3113 3589 3205 -915 518 258 O ATOM 4167 CB VAL A 175 54.637 72.146 23.087 1.00 24.49 C ANISOU 4167 CB VAL B 175 2839 3326 3141 -735 389 186 C ATOM 4168 CG1 VAL A 175 54.171 71.514 21.782 1.00 24.39 C ANISOU 4168 CG1 VAL B 175 2865 3302 3099 -669 438 153 C ATOM 4169 CG2 VAL A 175 54.821 71.074 24.153 1.00 24.23 C ANISOU 4169 CG2 VAL B 175 2692 3332 3183 -684 372 188 C ATOM 4170 N LEU A 176 54.981 74.993 22.002 1.00 25.96 N ANISOU 4170 N LEU B 176 3225 3436 3203 -929 380 249 N ATOM 4171 CA LEU A 176 54.546 75.917 20.958 1.00 26.82 C ANISOU 4171 CA LEU B 176 3467 3480 3245 -962 377 272 C ATOM 4172 C LEU A 176 55.633 76.897 20.481 1.00 28.07 C ANISOU 4172 C LEU B 176 3640 3661 3365 -1094 415 334 C ATOM 4173 O LEU A 176 55.693 77.214 19.304 1.00 28.18 O ANISOU 4173 O LEU B 176 3720 3675 3311 -1125 452 368 O ATOM 4174 CB LEU A 176 53.303 76.674 21.423 1.00 26.62 C ANISOU 4174 CB LEU B 176 3551 3336 3226 -932 292 250 C ATOM 4175 CG LEU A 176 52.050 75.802 21.588 1.00 26.79 C ANISOU 4175 CG LEU B 176 3576 3333 3270 -808 259 192 C ATOM 4176 CD1 LEU A 176 51.033 76.491 22.466 1.00 27.87 C ANISOU 4176 CD1 LEU B 176 3775 3378 3437 -785 183 159 C ATOM 4177 CD2 LEU A 176 51.437 75.473 20.240 1.00 26.94 C ANISOU 4177 CD2 LEU B 176 3657 3346 3234 -755 274 192 C ATOM 4178 N ASN A 177 56.490 77.368 21.382 1.00 28.70 N ANISOU 4178 N ASN B 177 3658 3766 3481 -1182 406 351 N ATOM 4179 CA ASN A 177 57.503 78.370 21.029 1.00 30.16 C ANISOU 4179 CA ASN B 177 3856 3966 3637 -1324 437 409 C ATOM 4180 C ASN A 177 58.901 77.785 20.813 1.00 31.55 C ANISOU 4180 C ASN B 177 3881 4284 3821 -1374 522 430 C ATOM 4181 O ASN A 177 59.680 78.309 20.010 1.00 32.27 O ANISOU 4181 O ASN B 177 3978 4415 3868 -1474 581 479 O ATOM 4182 CB ASN A 177 57.569 79.464 22.102 1.00 30.18 C ANISOU 4182 CB ASN B 177 3898 3898 3672 -1412 371 408 C ATOM 4183 CG ASN A 177 56.231 80.171 22.315 1.00 28.73 C ANISOU 4183 CG ASN B 177 3859 3564 3493 -1363 294 380 C ATOM 4184 OD1 ASN A 177 55.435 80.316 21.390 1.00 26.75 O ANISOU 4184 OD1 ASN B 177 3709 3249 3206 -1310 288 395 O ATOM 4185 ND2 ASN A 177 55.991 80.627 23.544 1.00 25.83 N ANISOU 4185 ND2 ASN B 177 3498 3148 3168 -1383 236 335 N ATOM 4186 N ASP A 178 59.214 76.705 21.531 1.00 31.83 N ANISOU 4186 N ASP B 178 3779 4397 3918 -1305 527 399 N ATOM 4187 CA ASP A 178 60.560 76.122 21.532 1.00 33.29 C ANISOU 4187 CA ASP B 178 3796 4715 4138 -1338 594 417 C ATOM 4188 C ASP A 178 60.659 74.784 20.792 1.00 33.86 C ANISOU 4188 C ASP B 178 3785 4854 4226 -1226 672 385 C ATOM 4189 O ASP A 178 61.752 74.226 20.667 1.00 34.89 O ANISOU 4189 O ASP B 178 3769 5094 4395 -1235 740 392 O ATOM 4190 CB ASP A 178 61.057 75.954 22.975 1.00 33.55 C ANISOU 4190 CB ASP B 178 3714 4792 4239 -1356 535 418 C ATOM 4191 CG ASP A 178 61.054 77.263 23.753 1.00 34.30 C ANISOU 4191 CG ASP B 178 3883 4829 4319 -1479 465 431 C ATOM 4192 OD1 ASP A 178 61.300 78.320 23.142 1.00 35.56 O ANISOU 4192 OD1 ASP B 178 4125 4950 4435 -1587 485 461 O ATOM 4193 OD2 ASP A 178 60.827 77.337 24.978 1.00 36.15 O ANISOU 4193 OD2 ASP B 178 4104 5051 4581 -1482 390 411 O ATOM 4194 N GLY A 179 59.524 74.266 20.319 1.00 33.71 N ANISOU 4194 N GLY B 179 3854 4770 4183 -1122 662 345 N ATOM 4195 CA GLY A 179 59.497 73.073 19.488 1.00 34.03 C ANISOU 4195 CA GLY B 179 3844 4856 4229 -1024 737 300 C ATOM 4196 C GLY A 179 59.767 71.764 20.209 1.00 33.89 C ANISOU 4196 C GLY B 179 3683 4876 4317 -922 740 271 C ATOM 4197 O GLY A 179 60.190 70.790 19.585 1.00 34.56 O ANISOU 4197 O GLY B 179 3685 5015 4432 -858 822 235 O ATOM 4198 N VAL A 180 59.518 71.731 21.515 1.00 33.30 N ANISOU 4198 N VAL B 180 3582 4771 4298 -907 653 286 N ATOM 4199 CA VAL A 180 59.715 70.517 22.307 1.00 32.99 C ANISOU 4199 CA VAL B 180 3416 4759 4360 -814 639 279 C ATOM 4200 C VAL A 180 58.530 69.572 22.085 1.00 32.26 C ANISOU 4200 C VAL B 180 3384 4591 4282 -694 628 226 C ATOM 4201 O VAL A 180 57.381 70.007 22.112 1.00 31.17 O ANISOU 4201 O VAL B 180 3375 4375 4094 -689 576 207 O ATOM 4202 CB VAL A 180 59.874 70.853 23.814 1.00 32.85 C ANISOU 4202 CB VAL B 180 3354 4751 4377 -858 544 323 C ATOM 4203 CG1 VAL A 180 60.165 69.601 24.627 1.00 32.77 C ANISOU 4203 CG1 VAL B 180 3209 4775 4468 -769 523 339 C ATOM 4204 CG2 VAL A 180 60.992 71.902 24.020 1.00 33.93 C ANISOU 4204 CG2 VAL B 180 3442 4958 4493 -996 547 368 C ATOM 4205 N LYS A 181 58.803 68.290 21.837 1.00 32.51 N ANISOU 4205 N LYS B 181 3320 4642 4389 -599 680 197 N ATOM 4206 CA LYS A 181 57.731 67.299 21.734 1.00 32.09 C ANISOU 4206 CA LYS B 181 3313 4515 4366 -493 667 146 C ATOM 4207 C LYS A 181 57.119 67.067 23.118 1.00 30.89 C ANISOU 4207 C LYS B 181 3156 4319 4261 -468 569 178 C ATOM 4208 O LYS A 181 57.847 67.000 24.110 1.00 30.80 O ANISOU 4208 O LYS B 181 3044 4355 4303 -489 533 235 O ATOM 4209 CB LYS A 181 58.241 65.981 21.144 1.00 33.12 C ANISOU 4209 CB LYS B 181 3343 4663 4579 -400 751 101 C ATOM 4210 CG LYS A 181 58.620 66.092 19.666 1.00 35.94 C ANISOU 4210 CG LYS B 181 3722 5063 4869 -418 859 44 C ATOM 4211 CD LYS A 181 58.572 64.742 18.931 1.00 38.94 C ANISOU 4211 CD LYS B 181 4059 5424 5311 -313 938 -42 C ATOM 4212 CE LYS A 181 57.710 64.814 17.666 1.00 39.78 C ANISOU 4212 CE LYS B 181 4301 5509 5306 -317 977 -120 C ATOM 4213 NZ LYS A 181 58.352 65.608 16.569 1.00 41.79 N ANISOU 4213 NZ LYS B 181 4580 5851 5445 -403 1060 -126 N ATOM 4214 N PRO A 182 55.793 66.991 23.201 1.00 30.02 N ANISOU 4214 N PRO B 182 3151 4132 4123 -434 523 145 N ATOM 4215 CA PRO A 182 55.122 66.785 24.491 1.00 29.37 C ANISOU 4215 CA PRO B 182 3071 4018 4071 -420 440 170 C ATOM 4216 C PRO A 182 55.732 65.671 25.344 1.00 30.16 C ANISOU 4216 C PRO B 182 3038 4143 4276 -369 428 217 C ATOM 4217 O PRO A 182 55.930 65.883 26.541 1.00 29.43 O ANISOU 4217 O PRO B 182 2907 4084 4193 -408 363 274 O ATOM 4218 CB PRO A 182 53.691 66.466 24.080 1.00 28.74 C ANISOU 4218 CB PRO B 182 3093 3859 3967 -366 426 111 C ATOM 4219 CG PRO A 182 53.506 67.259 22.838 1.00 28.71 C ANISOU 4219 CG PRO B 182 3183 3849 3878 -396 462 74 C ATOM 4220 CD PRO A 182 54.816 67.144 22.106 1.00 29.67 C ANISOU 4220 CD PRO B 182 3228 4037 4008 -415 544 84 C ATOM 4221 N CYS A 183 56.066 64.534 24.733 1.00 31.01 N ANISOU 4221 N CYS B 183 3081 4238 4464 -287 488 193 N ATOM 4222 CA CYS A 183 56.616 63.393 25.479 1.00 32.11 C ANISOU 4222 CA CYS B 183 3096 4380 4724 -223 472 245 C ATOM 4223 C CYS A 183 58.012 63.641 26.071 1.00 32.65 C ANISOU 4223 C CYS B 183 3031 4544 4833 -261 461 321 C ATOM 4224 O CYS A 183 58.414 62.927 26.982 1.00 33.65 O ANISOU 4224 O CYS B 183 3058 4682 5044 -225 414 391 O ATOM 4225 CB CYS A 183 56.623 62.114 24.620 1.00 32.68 C ANISOU 4225 CB CYS B 183 3134 4397 4888 -119 545 187 C ATOM 4226 SG CYS A 183 57.565 62.249 23.081 1.00 35.00 S ANISOU 4226 SG CYS B 183 3392 4741 5166 -114 671 114 S ATOM 4227 N ASP A 184 58.734 64.643 25.563 1.00 32.92 N ANISOU 4227 N ASP B 184 3059 4645 4805 -338 498 314 N ATOM 4228 CA ASP A 184 60.046 65.038 26.103 1.00 33.51 C ANISOU 4228 CA ASP B 184 3005 4821 4906 -396 483 382 C ATOM 4229 C ASP A 184 60.015 66.131 27.183 1.00 32.90 C ANISOU 4229 C ASP B 184 2960 4786 4752 -509 393 432 C ATOM 4230 O ASP A 184 61.069 66.529 27.692 1.00 33.37 O ANISOU 4230 O ASP B 184 2918 4938 4825 -574 369 486 O ATOM 4231 CB ASP A 184 60.958 65.529 24.974 1.00 34.47 C ANISOU 4231 CB ASP B 184 3088 5004 5005 -435 580 349 C ATOM 4232 CG ASP A 184 61.198 64.483 23.906 1.00 36.20 C ANISOU 4232 CG ASP B 184 3255 5203 5296 -332 683 287 C ATOM 4233 OD1 ASP A 184 60.961 63.280 24.157 1.00 36.65 O ANISOU 4233 OD1 ASP B 184 3266 5202 5455 -224 675 283 O ATOM 4234 OD2 ASP A 184 61.633 64.784 22.773 1.00 37.96 O ANISOU 4234 OD2 ASP B 184 3481 5465 5478 -356 780 235 O ATOM 4235 N LEU A 185 58.832 66.631 27.524 1.00 31.37 N ANISOU 4235 N LEU B 185 2904 4532 4484 -536 345 406 N ATOM 4236 CA LEU A 185 58.709 67.699 28.517 1.00 31.16 C ANISOU 4236 CA LEU B 185 2922 4535 4382 -642 270 429 C ATOM 4237 C LEU A 185 59.068 67.204 29.920 1.00 31.63 C ANISOU 4237 C LEU B 185 2884 4655 4478 -649 188 505 C ATOM 4238 O LEU A 185 58.745 66.078 30.287 1.00 31.59 O ANISOU 4238 O LEU B 185 2841 4624 4537 -564 169 535 O ATOM 4239 CB LEU A 185 57.283 68.264 28.525 1.00 30.09 C ANISOU 4239 CB LEU B 185 2948 4315 4171 -650 246 372 C ATOM 4240 CG LEU A 185 56.844 69.111 27.330 1.00 29.38 C ANISOU 4240 CG LEU B 185 2976 4169 4019 -672 296 312 C ATOM 4241 CD1 LEU A 185 55.340 69.292 27.346 1.00 28.92 C ANISOU 4241 CD1 LEU B 185 3047 4023 3919 -639 267 260 C ATOM 4242 CD2 LEU A 185 57.551 70.467 27.343 1.00 30.55 C ANISOU 4242 CD2 LEU B 185 3144 4353 4112 -794 291 326 C ATOM 4243 N HIS A 186 59.757 68.044 30.693 1.00 32.50 N ANISOU 4243 N HIS B 186 2955 4847 4545 -758 136 541 N ATOM 4244 CA HIS A 186 60.000 67.766 32.111 1.00 33.07 C ANISOU 4244 CA HIS B 186 2956 4991 4617 -789 43 612 C ATOM 4245 C HIS A 186 58.817 68.289 32.923 1.00 31.71 C ANISOU 4245 C HIS B 186 2912 4784 4354 -835 -9 574 C ATOM 4246 O HIS A 186 58.332 69.388 32.687 1.00 31.36 O ANISOU 4246 O HIS B 186 2979 4699 4237 -898 4 505 O ATOM 4247 CB HIS A 186 61.353 68.343 32.590 1.00 34.64 C ANISOU 4247 CB HIS B 186 3037 5312 4813 -890 6 664 C ATOM 4248 CG HIS A 186 61.417 69.844 32.653 1.00 36.56 C ANISOU 4248 CG HIS B 186 3363 5569 4961 -1029 -2 615 C ATOM 4249 ND1 HIS A 186 60.809 70.579 33.649 1.00 38.44 N ANISOU 4249 ND1 HIS B 186 3689 5809 5108 -1114 -68 588 N ATOM 4250 CD2 HIS A 186 62.067 70.742 31.872 1.00 38.85 C ANISOU 4250 CD2 HIS B 186 3656 5869 5235 -1105 49 588 C ATOM 4251 CE1 HIS A 186 61.056 71.865 33.463 1.00 38.26 C ANISOU 4251 CE1 HIS B 186 3726 5781 5029 -1229 -59 541 C ATOM 4252 NE2 HIS A 186 61.815 71.990 32.389 1.00 39.60 N ANISOU 4252 NE2 HIS B 186 3848 5955 5242 -1229 9 548 N ATOM 4253 N ALA A 187 58.311 67.466 33.831 1.00 31.32 N ANISOU 4253 N ALA B 187 2846 4741 4312 -796 -61 619 N ATOM 4254 CA ALA A 187 57.217 67.862 34.717 1.00 30.28 C ANISOU 4254 CA ALA B 187 2816 4597 4092 -841 -104 584 C ATOM 4255 C ALA A 187 57.622 67.559 36.147 1.00 30.86 C ANISOU 4255 C ALA B 187 2814 4779 4134 -898 -193 668 C ATOM 4256 O ALA A 187 58.396 66.636 36.384 1.00 31.44 O ANISOU 4256 O ALA B 187 2764 4901 4279 -855 -223 767 O ATOM 4257 CB ALA A 187 55.943 67.108 34.359 1.00 29.38 C ANISOU 4257 CB ALA B 187 2776 4383 4002 -745 -72 549 C ATOM 4258 N GLU A 188 57.089 68.334 37.091 1.00 30.58 N ANISOU 4258 N GLU B 188 2849 4781 3989 -992 -235 628 N ATOM 4259 CA GLU A 188 57.408 68.173 38.511 1.00 31.47 C ANISOU 4259 CA GLU B 188 2905 5014 4038 -1068 -323 700 C ATOM 4260 C GLU A 188 56.195 68.053 39.455 1.00 30.65 C ANISOU 4260 C GLU B 188 2884 4915 3847 -1089 -344 674 C ATOM 4261 O GLU A 188 56.374 67.677 40.606 1.00 31.14 O ANISOU 4261 O GLU B 188 2899 5080 3852 -1141 -415 750 O ATOM 4262 CB GLU A 188 58.287 69.338 38.983 1.00 32.63 C ANISOU 4262 CB GLU B 188 3031 5255 4113 -1205 -363 678 C ATOM 4263 CG GLU A 188 59.725 69.292 38.473 1.00 35.05 C ANISOU 4263 CG GLU B 188 3207 5615 4495 -1211 -368 741 C ATOM 4264 CD GLU A 188 59.863 69.816 37.055 1.00 37.48 C ANISOU 4264 CD GLU B 188 3553 5829 4858 -1179 -278 673 C ATOM 4265 OE1 GLU A 188 59.184 70.810 36.720 1.00 38.15 O ANISOU 4265 OE1 GLU B 188 3767 5840 4888 -1221 -241 572 O ATOM 4266 OE2 GLU A 188 60.651 69.233 36.267 1.00 40.54 O ANISOU 4266 OE2 GLU B 188 3840 6219 5343 -1112 -242 721 O ATOM 4267 N ILE A 189 54.984 68.361 38.990 1.00 27.44 N ANISOU 4267 N ILE B 189 2967 4349 3109 -1104 -218 -501 N ATOM 4268 CA ILE A 189 53.801 68.366 39.861 1.00 27.46 C ANISOU 4268 CA ILE B 189 3040 4288 3107 -1108 -173 -530 C ATOM 4269 C ILE A 189 52.733 67.363 39.410 1.00 26.03 C ANISOU 4269 C ILE B 189 2900 4007 2982 -957 -200 -413 C ATOM 4270 O ILE A 189 52.405 66.437 40.144 1.00 26.23 O ANISOU 4270 O ILE B 189 2929 4102 2936 -913 -246 -365 O ATOM 4271 CB ILE A 189 53.198 69.798 39.971 1.00 28.23 C ANISOU 4271 CB ILE B 189 3204 4223 3298 -1211 -29 -650 C ATOM 4272 CG1 ILE A 189 54.220 70.762 40.589 1.00 30.88 C ANISOU 4272 CG1 ILE B 189 3507 4661 3565 -1400 20 -802 C ATOM 4273 CG2 ILE A 189 51.919 69.792 40.807 1.00 28.33 C ANISOU 4273 CG2 ILE B 189 3282 4163 3319 -1203 31 -681 C ATOM 4274 CD1 ILE A 189 53.841 72.225 40.463 1.00 32.45 C ANISOU 4274 CD1 ILE B 189 3775 4657 3899 -1502 193 -921 C ATOM 4275 N LEU A 190 52.171 67.555 38.223 1.00 25.03 N ANISOU 4275 N LEU B 190 2801 3733 2976 -891 -167 -365 N ATOM 4276 CA LEU A 190 51.118 66.658 37.730 1.00 24.12 C ANISOU 4276 CA LEU B 190 2716 3546 2903 -779 -184 -275 C ATOM 4277 C LEU A 190 51.670 65.257 37.417 1.00 23.68 C ANISOU 4277 C LEU B 190 2623 3570 2802 -696 -268 -196 C ATOM 4278 O LEU A 190 52.840 65.131 37.051 1.00 23.92 O ANISOU 4278 O LEU B 190 2597 3683 2809 -696 -307 -189 O ATOM 4279 CB LEU A 190 50.439 67.261 36.499 1.00 23.54 C ANISOU 4279 CB LEU B 190 2656 3344 2946 -746 -132 -233 C ATOM 4280 CG LEU A 190 49.592 68.493 36.829 1.00 25.05 C ANISOU 4280 CG LEU B 190 2885 3412 3220 -785 -22 -276 C ATOM 4281 CD1 LEU A 190 49.248 69.256 35.565 1.00 25.94 C ANISOU 4281 CD1 LEU B 190 2985 3425 3447 -750 30 -201 C ATOM 4282 CD2 LEU A 190 48.323 68.106 37.581 1.00 25.11 C ANISOU 4282 CD2 LEU B 190 2930 3388 3224 -752 1 -273 C ATOM 4283 N PRO A 191 50.857 64.201 37.541 1.00 23.37 N ANISOU 4283 N PRO B 191 2616 3501 2762 -626 -281 -139 N ATOM 4284 CA PRO A 191 49.439 64.270 37.923 1.00 23.27 C ANISOU 4284 CA PRO B 191 2659 3408 2774 -625 -236 -143 C ATOM 4285 C PRO A 191 49.163 64.581 39.390 1.00 24.14 C ANISOU 4285 C PRO B 191 2793 3564 2816 -685 -215 -194 C ATOM 4286 O PRO A 191 48.072 65.074 39.671 1.00 24.48 O ANISOU 4286 O PRO B 191 2874 3531 2896 -703 -152 -225 O ATOM 4287 CB PRO A 191 48.934 62.856 37.600 1.00 22.82 C ANISOU 4287 CB PRO B 191 2618 3329 2722 -550 -257 -74 C ATOM 4288 CG PRO A 191 50.125 62.000 37.795 1.00 23.06 C ANISOU 4288 CG PRO B 191 2612 3439 2709 -510 -307 -33 C ATOM 4289 CD PRO A 191 51.282 62.814 37.285 1.00 23.00 C ANISOU 4289 CD PRO B 191 2549 3488 2702 -543 -325 -68 C ATOM 4290 N SER A 192 50.117 64.315 40.284 1.00 25.28 N ANISOU 4290 N SER B 192 2902 3846 2856 -719 -262 -199 N ATOM 4291 CA SER A 192 49.957 64.552 41.724 1.00 26.49 C ANISOU 4291 CA SER B 192 3064 4095 2905 -799 -248 -251 C ATOM 4292 C SER A 192 51.268 64.919 42.418 1.00 27.89 C ANISOU 4292 C SER B 192 3172 4460 2964 -889 -288 -295 C ATOM 4293 O SER A 192 52.268 64.211 42.282 1.00 28.06 O ANISOU 4293 O SER B 192 3127 4596 2941 -837 -365 -211 O ATOM 4294 CB SER A 192 49.397 63.307 42.407 1.00 26.72 C ANISOU 4294 CB SER B 192 3114 4161 2879 -739 -278 -157 C ATOM 4295 OG SER A 192 49.336 63.497 43.812 1.00 28.19 O ANISOU 4295 OG SER B 192 3295 4479 2936 -826 -272 -196 O ATOM 4296 N GLY A 193 51.244 66.013 43.177 1.00 28.95 N ANISOU 4296 N GLY B 193 3316 4635 3049 -1028 -226 -431 N ATOM 4297 CA GLY A 193 52.374 66.454 43.977 1.00 30.68 C ANISOU 4297 CA GLY B 193 3462 5069 3126 -1160 -253 -504 C ATOM 4298 C GLY A 193 52.722 65.550 45.150 1.00 31.88 C ANISOU 4298 C GLY B 193 3552 5463 3097 -1167 -336 -422 C ATOM 4299 O GLY A 193 53.809 65.679 45.730 1.00 33.58 O ANISOU 4299 O GLY B 193 3671 5919 3170 -1258 -389 -438 O ATOM 4300 N GLY A 194 51.807 64.651 45.509 1.00 31.57 N ANISOU 4300 N GLY B 194 3558 5380 3056 -1079 -344 -324 N ATOM 4301 CA GLY A 194 52.063 63.635 46.520 1.00 32.78 C ANISOU 4301 CA GLY B 194 3656 5741 3058 -1052 -420 -192 C ATOM 4302 C GLY A 194 52.411 62.243 45.993 1.00 32.38 C ANISOU 4302 C GLY B 194 3574 5666 3062 -868 -490 18 C ATOM 4303 O GLY A 194 52.400 61.275 46.759 1.00 33.58 O ANISOU 4303 O GLY B 194 3697 5933 3129 -811 -531 165 O ATOM 4304 N ASP A 195 52.730 62.128 44.703 1.00 31.17 N ANISOU 4304 N ASP B 195 3425 5364 3052 -776 -490 34 N ATOM 4305 CA ASP A 195 53.172 60.852 44.140 1.00 30.62 C ANISOU 4305 CA ASP B 195 3325 5258 3051 -612 -528 204 C ATOM 4306 C ASP A 195 54.572 60.921 43.547 1.00 30.84 C ANISOU 4306 C ASP B 195 3247 5386 3086 -580 -576 230 C ATOM 4307 O ASP A 195 55.118 62.004 43.343 1.00 31.27 O ANISOU 4307 O ASP B 195 3266 5502 3111 -690 -577 106 O ATOM 4308 CB ASP A 195 52.181 60.348 43.096 1.00 29.10 C ANISOU 4308 CB ASP B 195 3231 4802 3023 -524 -470 207 C ATOM 4309 CG ASP A 195 51.934 58.849 43.202 1.00 29.34 C ANISOU 4309 CG ASP B 195 3282 4771 3096 -395 -463 368 C ATOM 4310 OD1 ASP A 195 50.949 58.372 42.591 1.00 25.90 O ANISOU 4310 OD1 ASP B 195 2931 4146 2764 -359 -407 356 O ATOM 4311 OD2 ASP A 195 52.673 58.077 43.867 1.00 28.95 O ANISOU 4311 OD2 ASP B 195 3162 4854 2985 -325 -503 518 O ATOM 4312 N LYS A 196 55.136 59.752 43.248 1.00 30.96 N ANISOU 4312 N LYS B 196 3212 5401 3152 -428 -599 391 N ATOM 4313 CA LYS A 196 56.558 59.616 42.934 1.00 31.92 C ANISOU 4313 CA LYS B 196 3201 5667 3260 -376 -648 456 C ATOM 4314 C LYS A 196 56.939 60.074 41.539 1.00 30.44 C ANISOU 4314 C LYS B 196 3021 5355 3191 -373 -619 357 C ATOM 4315 O LYS A 196 58.052 60.533 41.316 1.00 31.19 O ANISOU 4315 O LYS B 196 3011 5591 3248 -406 -654 335 O ATOM 4316 CB LYS A 196 57.002 58.158 43.083 1.00 33.24 C ANISOU 4316 CB LYS B 196 3309 5849 3471 -190 -655 679 C ATOM 4317 CG LYS A 196 56.611 57.505 44.397 1.00 35.48 C ANISOU 4317 CG LYS B 196 3584 6246 3651 -165 -677 830 C ATOM 4318 CD LYS A 196 57.640 56.476 44.837 1.00 38.89 C ANISOU 4318 CD LYS B 196 3874 6838 4064 -7 -713 1079 C ATOM 4319 CE LYS A 196 57.000 55.377 45.673 1.00 41.00 C ANISOU 4319 CE LYS B 196 4180 7068 4331 90 -686 1276 C ATOM 4320 NZ LYS A 196 57.959 54.276 45.963 1.00 43.91 N ANISOU 4320 NZ LYS B 196 4414 7540 4731 284 -694 1557 N ATOM 4321 N LYS A 197 56.030 59.922 40.592 1.00 28.67 N ANISOU 4321 N LYS B 197 2908 4887 3096 -341 -556 304 N ATOM 4322 CA LYS A 197 56.353 60.184 39.198 1.00 27.79 C ANISOU 4322 CA LYS B 197 2800 4671 3088 -329 -526 235 C ATOM 4323 C LYS A 197 55.468 61.292 38.661 1.00 26.28 C ANISOU 4323 C LYS B 197 2696 4360 2930 -437 -488 98 C ATOM 4324 O LYS A 197 54.315 61.430 39.058 1.00 25.47 O ANISOU 4324 O LYS B 197 2677 4173 2829 -469 -460 71 O ATOM 4325 CB LYS A 197 56.208 58.906 38.368 1.00 27.57 C ANISOU 4325 CB LYS B 197 2800 4490 3184 -190 -475 308 C ATOM 4326 CG LYS A 197 57.329 57.893 38.618 1.00 29.84 C ANISOU 4326 CG LYS B 197 2981 4870 3486 -55 -487 454 C ATOM 4327 CD LYS A 197 56.928 56.478 38.207 1.00 31.01 C ANISOU 4327 CD LYS B 197 3186 4831 3765 80 -402 534 C ATOM 4328 CE LYS A 197 57.043 56.264 36.702 1.00 30.06 C ANISOU 4328 CE LYS B 197 3090 4570 3762 97 -329 441 C ATOM 4329 NZ LYS A 197 56.780 54.844 36.332 1.00 30.25 N ANISOU 4329 NZ LYS B 197 3163 4411 3920 211 -220 496 N ATOM 4330 N HIS A 198 56.032 62.081 37.754 1.00 25.86 N ANISOU 4330 N HIS B 198 2614 4303 2909 -487 -479 27 N ATOM 4331 CA HIS A 198 55.346 63.221 37.178 1.00 24.46 C ANISOU 4331 CA HIS B 198 2500 4018 2776 -577 -434 -71 C ATOM 4332 C HIS A 198 55.414 63.161 35.655 1.00 23.46 C ANISOU 4332 C HIS B 198 2376 3801 2737 -542 -407 -74 C ATOM 4333 O HIS A 198 56.431 62.786 35.074 1.00 24.05 O ANISOU 4333 O HIS B 198 2381 3937 2819 -503 -422 -53 O ATOM 4334 CB HIS A 198 55.945 64.517 37.729 1.00 25.21 C ANISOU 4334 CB HIS B 198 2560 4211 2808 -714 -432 -161 C ATOM 4335 CG HIS A 198 55.952 64.567 39.226 1.00 26.31 C ANISOU 4335 CG HIS B 198 2682 4484 2829 -776 -457 -176 C ATOM 4336 ND1 HIS A 198 57.102 64.423 39.974 1.00 27.44 N ANISOU 4336 ND1 HIS B 198 2715 4858 2853 -811 -518 -154 N ATOM 4337 CD2 HIS A 198 54.938 64.679 40.116 1.00 26.66 C ANISOU 4337 CD2 HIS B 198 2794 4493 2842 -812 -429 -203 C ATOM 4338 CE1 HIS A 198 56.798 64.469 41.259 1.00 28.52 C ANISOU 4338 CE1 HIS B 198 2852 5106 2877 -877 -530 -167 C ATOM 4339 NE2 HIS A 198 55.491 64.625 41.374 1.00 28.75 N ANISOU 4339 NE2 HIS B 198 2995 4968 2960 -879 -472 -205 N ATOM 4340 N TYR A 199 54.303 63.524 35.029 1.00 21.79 N ANISOU 4340 N TYR B 199 2234 3463 2583 -557 -364 -93 N ATOM 4341 CA TYR A 199 54.138 63.445 33.585 1.00 20.91 C ANISOU 4341 CA TYR B 199 2123 3294 2529 -540 -339 -88 C ATOM 4342 C TYR A 199 53.627 64.771 33.049 1.00 20.32 C ANISOU 4342 C TYR B 199 2069 3163 2491 -610 -301 -109 C ATOM 4343 O TYR A 199 52.938 65.490 33.754 1.00 19.90 O ANISOU 4343 O TYR B 199 2056 3058 2447 -647 -274 -128 O ATOM 4344 CB TYR A 199 53.107 62.375 33.242 1.00 20.26 C ANISOU 4344 CB TYR B 199 2088 3136 2474 -483 -319 -60 C ATOM 4345 CG TYR A 199 53.419 61.008 33.799 1.00 19.40 C ANISOU 4345 CG TYR B 199 1978 3033 2362 -403 -325 -22 C ATOM 4346 CD1 TYR A 199 54.644 60.397 33.552 1.00 18.57 C ANISOU 4346 CD1 TYR B 199 1808 2983 2266 -346 -330 -2 C ATOM 4347 CD2 TYR A 199 52.489 60.330 34.581 1.00 19.70 C ANISOU 4347 CD2 TYR B 199 2073 3015 2397 -377 -314 7 C ATOM 4348 CE1 TYR A 199 54.928 59.140 34.055 1.00 20.05 C ANISOU 4348 CE1 TYR B 199 1987 3154 2475 -250 -316 61 C ATOM 4349 CE2 TYR A 199 52.759 59.070 35.084 1.00 20.95 C ANISOU 4349 CE2 TYR B 199 2234 3158 2569 -296 -302 67 C ATOM 4350 CZ TYR A 199 53.978 58.484 34.822 1.00 20.66 C ANISOU 4350 CZ TYR B 199 2132 3161 2556 -225 -300 101 C ATOM 4351 OH TYR A 199 54.233 57.245 35.320 1.00 22.15 O ANISOU 4351 OH TYR B 199 2319 3314 2782 -125 -270 186 O ATOM 4352 N PRO A 200 53.951 65.098 31.804 1.00 20.47 N ANISOU 4352 N PRO B 200 2056 3188 2534 -625 -287 -98 N ATOM 4353 CA PRO A 200 53.375 66.289 31.170 1.00 20.54 C ANISOU 4353 CA PRO B 200 2078 3135 2590 -670 -242 -74 C ATOM 4354 C PRO A 200 51.848 66.218 31.029 1.00 20.11 C ANISOU 4354 C PRO B 200 2062 3013 2565 -638 -220 -25 C ATOM 4355 O PRO A 200 51.287 65.143 30.826 1.00 19.82 O ANISOU 4355 O PRO B 200 2034 2994 2505 -599 -239 -16 O ATOM 4356 CB PRO A 200 54.052 66.316 29.787 1.00 20.68 C ANISOU 4356 CB PRO B 200 2042 3211 2603 -683 -242 -50 C ATOM 4357 CG PRO A 200 55.275 65.464 29.931 1.00 20.80 C ANISOU 4357 CG PRO B 200 2011 3312 2578 -662 -277 -93 C ATOM 4358 CD PRO A 200 54.904 64.409 30.918 1.00 20.62 C ANISOU 4358 CD PRO B 200 2019 3276 2541 -598 -301 -98 C ATOM 4359 N ILE A 201 51.203 67.371 31.157 1.00 20.21 N ANISOU 4359 N ILE B 201 2094 2948 2638 -659 -166 3 N ATOM 4360 CA ILE A 201 49.787 67.534 30.848 1.00 20.28 C ANISOU 4360 CA ILE B 201 2109 2912 2685 -622 -136 76 C ATOM 4361 C ILE A 201 49.568 68.171 29.466 1.00 20.63 C ANISOU 4361 C ILE B 201 2100 2980 2757 -621 -115 183 C ATOM 4362 O ILE A 201 48.513 67.984 28.862 1.00 20.88 O ANISOU 4362 O ILE B 201 2100 3050 2783 -590 -117 265 O ATOM 4363 CB ILE A 201 49.081 68.347 31.974 1.00 20.27 C ANISOU 4363 CB ILE B 201 2153 2803 2747 -625 -71 54 C ATOM 4364 CG1 ILE A 201 47.577 68.465 31.736 1.00 20.54 C ANISOU 4364 CG1 ILE B 201 2176 2802 2828 -571 -38 140 C ATOM 4365 CG2 ILE A 201 49.693 69.730 32.131 1.00 21.90 C ANISOU 4365 CG2 ILE B 201 2369 2924 3026 -678 6 30 C ATOM 4366 CD1 ILE A 201 46.846 67.136 31.618 1.00 20.42 C ANISOU 4366 CD1 ILE B 201 2152 2866 2741 -545 -96 146 C ATOM 4367 N ALA A 202 50.552 68.920 28.972 1.00 21.19 N ANISOU 4367 N ALA B 202 2152 3051 2848 -661 -94 192 N ATOM 4368 CA ALA A 202 50.424 69.589 27.681 1.00 21.68 C ANISOU 4368 CA ALA B 202 2160 3146 2930 -662 -70 317 C ATOM 4369 C ALA A 202 50.056 68.586 26.603 1.00 21.42 C ANISOU 4369 C ALA B 202 2073 3265 2802 -657 -128 355 C ATOM 4370 O ALA A 202 50.724 67.556 26.448 1.00 20.59 O ANISOU 4370 O ALA B 202 1965 3234 2625 -678 -172 265 O ATOM 4371 CB ALA A 202 51.710 70.308 27.311 1.00 22.10 C ANISOU 4371 CB ALA B 202 2202 3195 2999 -723 -44 302 C ATOM 4372 N PHE A 203 48.985 68.890 25.871 1.00 22.08 N ANISOU 4372 N PHE B 203 2103 3400 2885 -632 -117 489 N ATOM 4373 CA PHE A 203 48.499 68.041 24.773 1.00 22.64 C ANISOU 4373 CA PHE B 203 2107 3653 2844 -658 -164 523 C ATOM 4374 C PHE A 203 48.301 66.577 25.184 1.00 22.06 C ANISOU 4374 C PHE B 203 2067 3610 2705 -673 -201 387 C ATOM 4375 O PHE A 203 48.463 65.658 24.374 1.00 22.47 O ANISOU 4375 O PHE B 203 2088 3787 2664 -726 -222 333 O ATOM 4376 CB PHE A 203 49.435 68.155 23.567 1.00 23.15 C ANISOU 4376 CB PHE B 203 2118 3835 2841 -716 -173 548 C ATOM 4377 CG PHE A 203 49.526 69.546 23.019 1.00 24.77 C ANISOU 4377 CG PHE B 203 2284 4019 3108 -704 -126 714 C ATOM 4378 CD1 PHE A 203 48.472 70.089 22.309 1.00 25.22 C ANISOU 4378 CD1 PHE B 203 2261 4162 3160 -672 -116 908 C ATOM 4379 CD2 PHE A 203 50.660 70.329 23.242 1.00 26.88 C ANISOU 4379 CD2 PHE B 203 2589 4180 3445 -726 -85 689 C ATOM 4380 CE1 PHE A 203 48.539 71.371 21.811 1.00 27.09 C ANISOU 4380 CE1 PHE B 203 2460 4360 3473 -645 -57 1093 C ATOM 4381 CE2 PHE A 203 50.731 71.625 22.744 1.00 27.83 C ANISOU 4381 CE2 PHE B 203 2682 4249 3641 -720 -19 848 C ATOM 4382 CZ PHE A 203 49.669 72.144 22.030 1.00 28.00 C ANISOU 4382 CZ PHE B 203 2630 4335 3673 -670 -1 1059 C ATOM 4383 N ASN A 204 47.888 66.381 26.435 1.00 21.55 N ANISOU 4383 N ASN B 204 2066 3429 2693 -633 -194 333 N ATOM 4384 CA ASN A 204 47.761 65.056 27.033 1.00 20.99 C ANISOU 4384 CA ASN B 204 2042 3348 2586 -637 -213 220 C ATOM 4385 C ASN A 204 46.461 64.920 27.829 1.00 21.27 C ANISOU 4385 C ASN B 204 2097 3339 2644 -609 -203 238 C ATOM 4386 O ASN A 204 45.776 65.916 28.115 1.00 21.19 O ANISOU 4386 O ASN B 204 2071 3283 2696 -571 -175 324 O ATOM 4387 CB ASN A 204 48.971 64.803 27.948 1.00 20.52 C ANISOU 4387 CB ASN B 204 2040 3204 2553 -622 -219 126 C ATOM 4388 CG ASN A 204 49.242 63.314 28.186 1.00 20.85 C ANISOU 4388 CG ASN B 204 2113 3250 2560 -618 -228 35 C ATOM 4389 OD1 ASN A 204 48.756 62.462 27.452 1.00 20.11 O ANISOU 4389 OD1 ASN B 204 2003 3216 2422 -651 -217 10 O ATOM 4390 ND2 ASN A 204 50.029 63.006 29.220 1.00 19.85 N ANISOU 4390 ND2 ASN B 204 2024 3063 2455 -582 -237 -10 N ATOM 4391 N ALA A 205 46.110 63.678 28.159 1.00 21.17 N ANISOU 4391 N ALA B 205 2117 3332 2592 -625 -211 159 N ATOM 4392 CA ALA A 205 45.038 63.390 29.104 1.00 20.91 C ANISOU 4392 CA ALA B 205 2118 3250 2579 -606 -198 155 C ATOM 4393 C ALA A 205 45.558 62.359 30.100 1.00 20.76 C ANISOU 4393 C ALA B 205 2179 3148 2561 -596 -198 62 C ATOM 4394 O ALA A 205 45.852 61.223 29.728 1.00 21.39 O ANISOU 4394 O ALA B 205 2273 3244 2609 -623 -191 1 O ATOM 4395 CB ALA A 205 43.796 62.879 28.370 1.00 21.43 C ANISOU 4395 CB ALA B 205 2121 3436 2583 -654 -198 183 C ATOM 4396 N LEU A 206 45.713 62.766 31.356 1.00 20.34 N ANISOU 4396 N LEU B 206 2173 3010 2545 -559 -193 55 N ATOM 4397 CA LEU A 206 46.260 61.890 32.384 1.00 20.22 C ANISOU 4397 CA LEU B 206 2218 2944 2521 -540 -200 5 C ATOM 4398 C LEU A 206 45.131 61.279 33.213 1.00 20.06 C ANISOU 4398 C LEU B 206 2237 2892 2493 -542 -179 2 C ATOM 4399 O LEU A 206 44.460 61.993 33.950 1.00 19.43 O ANISOU 4399 O LEU B 206 2163 2789 2428 -536 -163 18 O ATOM 4400 CB LEU A 206 47.199 62.670 33.309 1.00 20.47 C ANISOU 4400 CB LEU B 206 2264 2951 2563 -525 -212 -7 C ATOM 4401 CG LEU A 206 48.519 63.143 32.717 1.00 21.30 C ANISOU 4401 CG LEU B 206 2333 3089 2670 -531 -231 -16 C ATOM 4402 CD1 LEU A 206 49.165 64.176 33.630 1.00 22.47 C ANISOU 4402 CD1 LEU B 206 2487 3226 2824 -553 -228 -41 C ATOM 4403 CD2 LEU A 206 49.456 61.965 32.486 1.00 22.12 C ANISOU 4403 CD2 LEU B 206 2431 3220 2753 -505 -249 -36 C ATOM 4404 N PRO A 207 44.934 59.965 33.125 1.00 20.34 N ANISOU 4404 N PRO B 207 2301 2915 2513 -555 -162 -24 N ATOM 4405 CA PRO A 207 43.879 59.300 33.892 1.00 20.55 C ANISOU 4405 CA PRO B 207 2367 2909 2532 -570 -133 -25 C ATOM 4406 C PRO A 207 44.292 59.050 35.350 1.00 20.77 C ANISOU 4406 C PRO B 207 2451 2887 2555 -530 -138 -9 C ATOM 4407 O PRO A 207 44.177 57.920 35.828 1.00 21.21 O ANISOU 4407 O PRO B 207 2553 2896 2610 -525 -110 -2 O ATOM 4408 CB PRO A 207 43.716 57.983 33.139 1.00 21.32 C ANISOU 4408 CB PRO B 207 2479 2997 2625 -614 -94 -69 C ATOM 4409 CG PRO A 207 45.100 57.667 32.714 1.00 20.73 C ANISOU 4409 CG PRO B 207 2405 2901 2570 -579 -97 -87 C ATOM 4410 CD PRO A 207 45.696 58.996 32.312 1.00 20.54 C ANISOU 4410 CD PRO B 207 2327 2940 2539 -563 -147 -62 C ATOM 4411 N GLN A 208 44.788 60.085 36.030 1.00 20.78 N ANISOU 4411 N GLN B 208 2443 2904 2548 -513 -163 -3 N ATOM 4412 CA GLN A 208 45.126 60.028 37.452 1.00 21.03 C ANISOU 4412 CA GLN B 208 2508 2943 2542 -501 -172 8 C ATOM 4413 C GLN A 208 44.924 61.395 38.083 1.00 21.40 C ANISOU 4413 C GLN B 208 2544 3006 2580 -530 -161 -25 C ATOM 4414 O GLN A 208 45.548 62.382 37.677 1.00 21.42 O ANISOU 4414 O GLN B 208 2517 3016 2606 -539 -167 -48 O ATOM 4415 CB GLN A 208 46.578 59.579 37.706 1.00 21.12 C ANISOU 4415 CB GLN B 208 2508 2986 2532 -462 -209 34 C ATOM 4416 CG GLN A 208 46.874 59.392 39.223 1.00 21.78 C ANISOU 4416 CG GLN B 208 2607 3126 2545 -457 -226 71 C ATOM 4417 CD GLN A 208 48.341 59.208 39.575 1.00 21.01 C ANISOU 4417 CD GLN B 208 2462 3113 2407 -420 -274 116 C ATOM 4418 OE1 GLN A 208 49.156 58.879 38.719 1.00 21.20 O ANISOU 4418 OE1 GLN B 208 2454 3126 2475 -376 -283 128 O ATOM 4419 NE2 GLN A 208 48.670 59.398 40.852 1.00 20.28 N ANISOU 4419 NE2 GLN B 208 2355 3130 2222 -443 -302 141 N ATOM 4420 N ILE A 209 44.035 61.444 39.069 1.00 21.83 N ANISOU 4420 N ILE B 209 2627 3057 2612 -551 -129 -35 N ATOM 4421 CA ILE A 209 43.909 62.594 39.957 1.00 22.38 C ANISOU 4421 CA ILE B 209 2698 3136 2668 -590 -93 -90 C ATOM 4422 C ILE A 209 44.015 62.057 41.383 1.00 23.25 C ANISOU 4422 C ILE B 209 2840 3312 2682 -618 -101 -91 C ATOM 4423 O ILE A 209 43.356 61.070 41.739 1.00 22.56 O ANISOU 4423 O ILE B 209 2781 3221 2571 -607 -96 -45 O ATOM 4424 CB ILE A 209 42.586 63.336 39.701 1.00 22.73 C ANISOU 4424 CB ILE B 209 2729 3124 2782 -588 -25 -102 C ATOM 4425 CG1 ILE A 209 42.579 63.849 38.251 1.00 22.96 C ANISOU 4425 CG1 ILE B 209 2708 3125 2889 -556 -28 -63 C ATOM 4426 CG2 ILE A 209 42.400 64.485 40.721 1.00 23.56 C ANISOU 4426 CG2 ILE B 209 2847 3211 2894 -631 49 -180 C ATOM 4427 CD1 ILE A 209 41.505 64.829 37.924 1.00 24.32 C ANISOU 4427 CD1 ILE B 209 2841 3254 3146 -533 42 -40 C ATOM 4428 N ASP A 210 44.859 62.710 42.184 1.00 24.38 N ANISOU 4428 N ASP B 210 2974 3530 2760 -669 -109 -142 N ATOM 4429 CA ASP A 210 45.248 62.218 43.504 1.00 25.52 C ANISOU 4429 CA ASP B 210 3122 3796 2777 -705 -135 -124 C ATOM 4430 C ASP A 210 46.015 60.898 43.335 1.00 25.46 C ANISOU 4430 C ASP B 210 3101 3828 2744 -633 -204 -2 C ATOM 4431 O ASP A 210 46.382 60.520 42.219 1.00 25.01 O ANISOU 4431 O ASP B 210 3033 3703 2765 -572 -223 31 O ATOM 4432 CB ASP A 210 44.021 62.053 44.411 1.00 26.26 C ANISOU 4432 CB ASP B 210 3253 3888 2835 -738 -79 -139 C ATOM 4433 CG ASP A 210 44.299 62.442 45.859 1.00 28.71 C ANISOU 4433 CG ASP B 210 3560 4344 3006 -834 -67 -196 C ATOM 4434 OD1 ASP A 210 45.372 62.093 46.394 1.00 30.87 O ANISOU 4434 OD1 ASP B 210 3798 4762 3170 -852 -134 -148 O ATOM 4435 OD2 ASP A 210 43.493 63.090 46.550 1.00 32.97 O ANISOU 4435 OD2 ASP B 210 4119 4881 3528 -902 13 -289 O ATOM 4436 N VAL A 211 46.269 60.200 44.433 1.00 26.25 N ANISOU 4436 N VAL B 211 3198 4038 2739 -637 -230 72 N ATOM 4437 CA VAL A 211 47.029 58.955 44.380 1.00 26.40 C ANISOU 4437 CA VAL B 211 3196 4082 2752 -548 -275 214 C ATOM 4438 C VAL A 211 46.089 57.753 44.403 1.00 26.17 C ANISOU 4438 C VAL B 211 3228 3946 2771 -500 -232 298 C ATOM 4439 O VAL A 211 44.892 57.892 44.657 1.00 25.29 O ANISOU 4439 O VAL B 211 3161 3787 2661 -549 -183 250 O ATOM 4440 CB VAL A 211 48.067 58.882 45.529 1.00 27.93 C ANISOU 4440 CB VAL B 211 3323 4492 2798 -567 -335 288 C ATOM 4441 CG1 VAL A 211 48.982 60.109 45.486 1.00 28.19 C ANISOU 4441 CG1 VAL B 211 3294 4639 2778 -647 -366 176 C ATOM 4442 CG2 VAL A 211 47.402 58.757 46.877 1.00 28.97 C ANISOU 4442 CG2 VAL B 211 3474 4731 2805 -633 -319 312 C ATOM 4443 N PHE A 212 46.641 56.577 44.123 1.00 26.47 N ANISOU 4443 N PHE B 212 3263 3938 2858 -408 -234 421 N ATOM 4444 CA PHE A 212 45.852 55.354 44.064 1.00 26.56 C ANISOU 4444 CA PHE B 212 3339 3817 2935 -371 -169 495 C ATOM 4445 C PHE A 212 45.597 54.791 45.454 1.00 27.66 C ANISOU 4445 C PHE B 212 3491 4042 2976 -377 -164 617 C ATOM 4446 O PHE A 212 46.416 54.944 46.362 1.00 28.33 O ANISOU 4446 O PHE B 212 3516 4303 2947 -369 -221 701 O ATOM 4447 CB PHE A 212 46.528 54.297 43.186 1.00 26.53 C ANISOU 4447 CB PHE B 212 3336 3694 3049 -272 -138 567 C ATOM 4448 CG PHE A 212 46.461 54.617 41.731 1.00 25.34 C ANISOU 4448 CG PHE B 212 3189 3449 2991 -287 -120 443 C ATOM 4449 CD1 PHE A 212 47.495 55.306 41.112 1.00 22.66 C ANISOU 4449 CD1 PHE B 212 2785 3169 2654 -267 -172 402 C ATOM 4450 CD2 PHE A 212 45.340 54.273 40.986 1.00 23.61 C ANISOU 4450 CD2 PHE B 212 3023 3109 2837 -338 -54 367 C ATOM 4451 CE1 PHE A 212 47.429 55.621 39.779 1.00 21.77 C ANISOU 4451 CE1 PHE B 212 2669 2992 2610 -289 -156 301 C ATOM 4452 CE2 PHE A 212 45.265 54.593 39.642 1.00 24.13 C ANISOU 4452 CE2 PHE B 212 3076 3134 2960 -366 -45 263 C ATOM 4453 CZ PHE A 212 46.314 55.268 39.038 1.00 22.88 C ANISOU 4453 CZ PHE B 212 2858 3031 2803 -338 -96 236 C ATOM 4454 N THR A 213 44.444 54.142 45.588 1.00 27.51 N ANISOU 4454 N THR B 213 3542 3918 2992 -403 -94 628 N ATOM 4455 CA THR A 213 44.086 53.386 46.779 1.00 28.88 C ANISOU 4455 CA THR B 213 3742 4139 3092 -406 -67 765 C ATOM 4456 C THR A 213 44.355 51.923 46.454 1.00 30.51 C ANISOU 4456 C THR B 213 3986 4188 3420 -305 0 914 C ATOM 4457 O THR A 213 44.780 51.599 45.337 1.00 30.13 O ANISOU 4457 O THR B 213 3942 4007 3498 -251 27 879 O ATOM 4458 CB THR A 213 42.592 53.617 47.174 1.00 28.42 C ANISOU 4458 CB THR B 213 3736 4061 3002 -509 -14 677 C ATOM 4459 OG1 THR A 213 41.716 52.875 46.313 1.00 26.51 O ANISOU 4459 OG1 THR B 213 3555 3631 2887 -517 66 643 O ATOM 4460 CG2 THR A 213 42.170 55.066 46.955 1.00 26.85 C ANISOU 4460 CG2 THR B 213 3510 3921 2773 -587 -36 493 C ATOM 4461 N ASP A 214 44.109 51.039 47.417 1.00 32.62 N ANISOU 4461 N ASP B 214 4281 4460 3652 -285 41 1080 N ATOM 4462 CA ASP A 214 44.410 49.616 47.234 1.00 34.45 C ANISOU 4462 CA ASP B 214 4553 4517 4019 -178 133 1249 C ATOM 4463 C ASP A 214 43.378 48.840 46.383 1.00 33.88 C ANISOU 4463 C ASP B 214 4583 4192 4098 -228 263 1155 C ATOM 4464 O ASP A 214 43.598 47.661 46.095 1.00 35.55 O ANISOU 4464 O ASP B 214 4843 4214 4451 -155 372 1257 O ATOM 4465 CB ASP A 214 44.655 48.927 48.591 1.00 36.89 C ANISOU 4465 CB ASP B 214 4844 4931 4241 -123 136 1505 C ATOM 4466 CG ASP A 214 43.392 48.755 49.415 1.00 38.86 C ANISOU 4466 CG ASP B 214 5159 5193 4414 -230 184 1509 C ATOM 4467 OD1 ASP A 214 42.408 49.488 49.185 1.00 39.45 O ANISOU 4467 OD1 ASP B 214 5263 5273 4455 -353 182 1305 O ATOM 4468 OD2 ASP A 214 43.293 47.900 50.334 1.00 44.87 O ANISOU 4468 OD2 ASP B 214 5938 5965 5146 -196 232 1724 O ATOM 4469 N ASN A 215 42.277 49.485 45.979 1.00 31.95 N ANISOU 4469 N ASN B 215 4364 3947 3827 -354 263 963 N ATOM 4470 CA ASN A 215 41.316 48.882 45.029 1.00 31.03 C ANISOU 4470 CA ASN B 215 4316 3644 3828 -429 371 844 C ATOM 4471 C ASN A 215 41.496 49.342 43.557 1.00 29.43 C ANISOU 4471 C ASN B 215 4088 3399 3695 -449 357 670 C ATOM 4472 O ASN A 215 40.641 49.071 42.713 1.00 28.77 O ANISOU 4472 O ASN B 215 4036 3229 3667 -543 426 542 O ATOM 4473 CB ASN A 215 39.865 49.108 45.498 1.00 30.67 C ANISOU 4473 CB ASN B 215 4299 3643 3711 -558 396 771 C ATOM 4474 CG ASN A 215 39.370 50.537 45.266 1.00 28.60 C ANISOU 4474 CG ASN B 215 3975 3527 3364 -623 310 612 C ATOM 4475 OD1 ASN A 215 40.094 51.385 44.760 1.00 24.78 O ANISOU 4475 OD1 ASN B 215 3436 3105 2873 -583 232 555 O ATOM 4476 ND2 ASN A 215 38.124 50.797 45.640 1.00 28.13 N ANISOU 4476 ND2 ASN B 215 3921 3514 3254 -720 337 549 N ATOM 4477 N ASP A 216 42.595 50.049 43.283 1.00 28.29 N ANISOU 4477 N ASP B 216 3877 3343 3530 -376 267 668 N ATOM 4478 CA ASP A 216 42.996 50.499 41.935 1.00 27.37 C ANISOU 4478 CA ASP B 216 3726 3205 3469 -380 248 535 C ATOM 4479 C ASP A 216 42.191 51.674 41.349 1.00 25.63 C ANISOU 4479 C ASP B 216 3469 3079 3191 -477 192 379 C ATOM 4480 O ASP A 216 42.433 52.088 40.210 1.00 25.23 O ANISOU 4480 O ASP B 216 3383 3030 3171 -490 175 283 O ATOM 4481 CB ASP A 216 43.075 49.336 40.941 1.00 28.00 C ANISOU 4481 CB ASP B 216 3856 3091 3691 -378 373 498 C ATOM 4482 CG ASP A 216 44.092 48.288 41.350 1.00 29.90 C ANISOU 4482 CG ASP B 216 4116 3217 4027 -244 442 665 C ATOM 4483 OD1 ASP A 216 44.990 48.601 42.172 1.00 29.41 O ANISOU 4483 OD1 ASP B 216 3996 3272 3906 -140 358 809 O ATOM 4484 OD2 ASP A 216 44.070 47.126 40.889 1.00 29.66 O ANISOU 4484 OD2 ASP B 216 4149 2985 4136 -234 588 667 O ATOM 4485 N TYR A 217 41.263 52.209 42.136 1.00 24.93 N ANISOU 4485 N TYR B 217 3380 3071 3021 -537 173 369 N ATOM 4486 CA TYR A 217 40.706 53.542 41.910 1.00 23.52 C ANISOU 4486 CA TYR B 217 3148 2997 2789 -587 117 267 C ATOM 4487 C TYR A 217 41.557 54.559 42.676 1.00 23.37 C ANISOU 4487 C TYR B 217 3088 3096 2694 -546 36 293 C ATOM 4488 O TYR A 217 42.113 54.237 43.727 1.00 24.22 O ANISOU 4488 O TYR B 217 3204 3254 2743 -512 20 393 O ATOM 4489 CB TYR A 217 39.272 53.630 42.436 1.00 23.56 C ANISOU 4489 CB TYR B 217 3166 3030 2757 -669 157 236 C ATOM 4490 CG TYR A 217 38.255 52.875 41.631 1.00 23.45 C ANISOU 4490 CG TYR B 217 3168 2947 2794 -749 231 178 C ATOM 4491 CD1 TYR A 217 37.306 53.549 40.862 1.00 22.40 C ANISOU 4491 CD1 TYR B 217 2972 2881 2656 -811 225 88 C ATOM 4492 CD2 TYR A 217 38.219 51.487 41.645 1.00 25.06 C ANISOU 4492 CD2 TYR B 217 3443 3026 3053 -769 318 218 C ATOM 4493 CE1 TYR A 217 36.363 52.854 40.120 1.00 22.43 C ANISOU 4493 CE1 TYR B 217 2971 2869 2681 -909 288 28 C ATOM 4494 CE2 TYR A 217 37.279 50.785 40.903 1.00 24.66 C ANISOU 4494 CE2 TYR B 217 3407 2921 3041 -876 401 137 C ATOM 4495 CZ TYR A 217 36.356 51.476 40.141 1.00 23.34 C ANISOU 4495 CZ TYR B 217 3165 2863 2842 -955 378 37 C ATOM 4496 OH TYR A 217 35.416 50.778 39.416 1.00 23.60 O ANISOU 4496 OH TYR B 217 3193 2888 2887 -1084 454 -49 O ATOM 4497 N THR A 218 41.653 55.783 42.166 1.00 22.14 N ANISOU 4497 N THR B 218 2883 2995 2534 -559 -6 208 N ATOM 4498 CA THR A 218 42.331 56.845 42.888 1.00 22.27 C ANISOU 4498 CA THR B 218 2865 3116 2479 -556 -58 194 C ATOM 4499 C THR A 218 41.435 57.398 43.992 1.00 23.11 C ANISOU 4499 C THR B 218 2980 3286 2514 -617 -31 162 C ATOM 4500 O THR A 218 40.232 57.123 44.035 1.00 22.80 O ANISOU 4500 O THR B 218 2961 3210 2491 -653 21 146 O ATOM 4501 CB THR A 218 42.722 58.001 41.960 1.00 21.29 C ANISOU 4501 CB THR B 218 2694 3000 2396 -555 -87 114 C ATOM 4502 OG1 THR A 218 41.537 58.619 41.443 1.00 20.96 O ANISOU 4502 OG1 THR B 218 2638 2929 2395 -590 -49 52 O ATOM 4503 CG2 THR A 218 43.489 57.510 40.725 1.00 20.28 C ANISOU 4503 CG2 THR B 218 2552 2820 2336 -510 -104 127 C ATOM 4504 N TYR A 219 42.029 58.207 44.858 1.00 23.79 N ANISOU 4504 N TYR B 219 3044 3479 2515 -643 -58 136 N ATOM 4505 CA TYR A 219 41.299 58.831 45.950 1.00 25.22 C ANISOU 4505 CA TYR B 219 3231 3731 2619 -715 -16 78 C ATOM 4506 C TYR A 219 40.238 59.793 45.427 1.00 24.63 C ANISOU 4506 C TYR B 219 3144 3589 2627 -736 45 -26 C ATOM 4507 O TYR A 219 39.199 59.946 46.051 1.00 25.38 O ANISOU 4507 O TYR B 219 3247 3695 2702 -778 106 -62 O ATOM 4508 CB TYR A 219 42.251 59.551 46.924 1.00 26.00 C ANISOU 4508 CB TYR B 219 3301 3979 2598 -767 -47 43 C ATOM 4509 CG TYR A 219 42.838 58.648 47.992 1.00 28.93 C ANISOU 4509 CG TYR B 219 3667 4488 2837 -769 -90 169 C ATOM 4510 CD1 TYR A 219 42.116 58.319 49.136 1.00 32.54 C ANISOU 4510 CD1 TYR B 219 4146 5028 3190 -827 -54 197 C ATOM 4511 CD2 TYR A 219 44.123 58.131 47.861 1.00 31.57 C ANISOU 4511 CD2 TYR B 219 3962 4886 3148 -707 -163 277 C ATOM 4512 CE1 TYR A 219 42.666 57.479 50.131 1.00 34.75 C ANISOU 4512 CE1 TYR B 219 4410 5457 3338 -823 -95 350 C ATOM 4513 CE2 TYR A 219 44.679 57.302 48.837 1.00 34.39 C ANISOU 4513 CE2 TYR B 219 4294 5387 3387 -689 -202 434 C ATOM 4514 CZ TYR A 219 43.948 56.978 49.967 1.00 35.28 C ANISOU 4514 CZ TYR B 219 4429 5585 3389 -747 -170 478 C ATOM 4515 OH TYR A 219 44.514 56.161 50.923 1.00 37.93 O ANISOU 4515 OH TYR B 219 4729 6083 3601 -723 -210 666 O ATOM 4516 N GLU A 220 40.492 60.434 44.289 1.00 24.15 N ANISOU 4516 N GLU B 220 3053 3464 2659 -702 34 -60 N ATOM 4517 CA GLU A 220 39.518 61.344 43.695 1.00 24.10 C ANISOU 4517 CA GLU B 220 3015 3398 2743 -697 94 -116 C ATOM 4518 C GLU A 220 38.256 60.588 43.280 1.00 24.10 C ANISOU 4518 C GLU B 220 3007 3372 2776 -692 120 -77 C ATOM 4519 O GLU A 220 37.131 61.018 43.573 1.00 24.26 O ANISOU 4519 O GLU B 220 3004 3394 2819 -706 186 -106 O ATOM 4520 CB GLU A 220 40.117 62.065 42.487 1.00 23.99 C ANISOU 4520 CB GLU B 220 2965 3337 2814 -657 70 -122 C ATOM 4521 CG GLU A 220 39.178 63.078 41.844 1.00 25.12 C ANISOU 4521 CG GLU B 220 3058 3425 3060 -632 135 -139 C ATOM 4522 CD GLU A 220 39.174 64.424 42.532 1.00 27.88 C ANISOU 4522 CD GLU B 220 3408 3740 3444 -655 221 -223 C ATOM 4523 OE1 GLU A 220 39.676 64.537 43.676 1.00 30.30 O ANISOU 4523 OE1 GLU B 220 3754 4093 3667 -719 234 -295 O ATOM 4524 OE2 GLU A 220 38.671 65.384 41.915 1.00 30.24 O ANISOU 4524 OE2 GLU B 220 3664 3970 3857 -612 284 -216 O ATOM 4525 N GLU A 221 38.463 59.462 42.603 1.00 23.44 N ANISOU 4525 N GLU B 221 2939 3267 2699 -678 81 -19 N ATOM 4526 CA GLU A 221 37.383 58.602 42.149 1.00 23.23 C ANISOU 4526 CA GLU B 221 2907 3226 2692 -704 111 2 C ATOM 4527 C GLU A 221 36.579 58.073 43.328 1.00 24.25 C ANISOU 4527 C GLU B 221 3072 3378 2764 -750 159 11 C ATOM 4528 O GLU A 221 35.344 58.116 43.311 1.00 24.16 O ANISOU 4528 O GLU B 221 3028 3387 2766 -783 209 -7 O ATOM 4529 CB GLU A 221 37.949 57.453 41.311 1.00 23.03 C ANISOU 4529 CB GLU B 221 2908 3155 2686 -700 85 35 C ATOM 4530 CG GLU A 221 38.484 57.932 39.965 1.00 22.15 C ANISOU 4530 CG GLU B 221 2748 3043 2624 -673 48 17 C ATOM 4531 CD GLU A 221 39.478 56.996 39.303 1.00 23.16 C ANISOU 4531 CD GLU B 221 2906 3123 2769 -657 30 31 C ATOM 4532 OE1 GLU A 221 39.816 55.929 39.871 1.00 23.39 O ANISOU 4532 OE1 GLU B 221 2996 3100 2792 -651 51 70 O ATOM 4533 OE2 GLU A 221 39.933 57.342 38.193 1.00 21.30 O ANISOU 4533 OE2 GLU B 221 2630 2902 2562 -647 4 12 O ATOM 4534 N MET A 222 37.281 57.600 44.357 1.00 24.91 N ANISOU 4534 N MET B 222 3210 3479 2775 -754 145 51 N ATOM 4535 CA MET A 222 36.623 57.071 45.555 1.00 25.91 C ANISOU 4535 CA MET B 222 3372 3645 2828 -804 190 78 C ATOM 4536 C MET A 222 35.901 58.158 46.345 1.00 26.43 C ANISOU 4536 C MET B 222 3408 3776 2860 -840 240 -1 C ATOM 4537 O MET A 222 34.888 57.882 46.977 1.00 27.11 O ANISOU 4537 O MET B 222 3499 3890 2913 -888 299 -6 O ATOM 4538 CB MET A 222 37.617 56.336 46.462 1.00 26.51 C ANISOU 4538 CB MET B 222 3495 3756 2822 -791 158 174 C ATOM 4539 CG MET A 222 38.060 54.968 45.943 1.00 26.78 C ANISOU 4539 CG MET B 222 3572 3695 2908 -753 156 273 C ATOM 4540 SD MET A 222 36.761 53.996 45.156 1.00 25.67 S ANISOU 4540 SD MET B 222 3456 3447 2849 -809 236 252 S ATOM 4541 CE MET A 222 35.732 53.585 46.564 1.00 26.96 C ANISOU 4541 CE MET B 222 3654 3664 2927 -881 300 296 C ATOM 4542 N LYS A 223 36.410 59.387 46.298 1.00 26.67 N ANISOU 4542 N LYS B 223 3408 3818 2907 -822 235 -72 N ATOM 4543 CA LYS A 223 35.724 60.526 46.911 1.00 27.66 C ANISOU 4543 CA LYS B 223 3506 3967 3038 -852 316 -169 C ATOM 4544 C LYS A 223 34.373 60.781 46.223 1.00 27.55 C ANISOU 4544 C LYS B 223 3432 3912 3124 -826 376 -178 C ATOM 4545 O LYS A 223 33.372 61.020 46.897 1.00 27.63 O ANISOU 4545 O LYS B 223 3422 3951 3124 -857 458 -218 O ATOM 4546 CB LYS A 223 36.592 61.795 46.877 1.00 28.18 C ANISOU 4546 CB LYS B 223 3558 4021 3129 -845 322 -251 C ATOM 4547 CG LYS A 223 37.634 61.887 47.993 1.00 30.54 C ANISOU 4547 CG LYS B 223 3888 4425 3291 -913 298 -285 C ATOM 4548 CD LYS A 223 38.420 63.202 47.901 1.00 32.86 C ANISOU 4548 CD LYS B 223 4167 4701 3618 -935 324 -394 C ATOM 4549 CE LYS A 223 39.826 63.102 48.520 1.00 34.43 C ANISOU 4549 CE LYS B 223 4372 5030 3680 -994 251 -397 C ATOM 4550 NZ LYS A 223 39.866 62.306 49.780 1.00 36.46 N ANISOU 4550 NZ LYS B 223 4643 5450 3761 -1060 227 -351 N ATOM 4551 N MET A 224 34.329 60.700 44.892 1.00 26.65 N ANISOU 4551 N MET B 224 3276 3755 3094 -776 337 -135 N ATOM 4552 CA MET A 224 33.057 60.876 44.176 1.00 26.93 C ANISOU 4552 CA MET B 224 3228 3802 3204 -756 379 -117 C ATOM 4553 C MET A 224 32.037 59.800 44.604 1.00 27.35 C ANISOU 4553 C MET B 224 3287 3905 3202 -822 407 -99 C ATOM 4554 O MET A 224 30.843 60.076 44.718 1.00 28.35 O ANISOU 4554 O MET B 224 3343 4074 3354 -828 473 -109 O ATOM 4555 CB MET A 224 33.268 60.856 42.658 1.00 26.37 C ANISOU 4555 CB MET B 224 3102 3723 3194 -715 320 -66 C ATOM 4556 CG MET A 224 34.126 62.007 42.147 1.00 26.73 C ANISOU 4556 CG MET B 224 3130 3718 3307 -651 307 -72 C ATOM 4557 SD MET A 224 34.183 62.180 40.358 1.00 27.83 S ANISOU 4557 SD MET B 224 3182 3883 3509 -605 252 5 S ATOM 4558 CE MET A 224 32.555 62.960 40.038 1.00 29.24 C ANISOU 4558 CE MET B 224 3220 4124 3766 -556 329 63 C ATOM 4559 N THR A 225 32.524 58.585 44.852 1.00 27.02 N ANISOU 4559 N THR B 225 3323 3851 3093 -868 369 -64 N ATOM 4560 CA THR A 225 31.687 57.475 45.300 1.00 27.36 C ANISOU 4560 CA THR B 225 3391 3917 3088 -943 408 -40 C ATOM 4561 C THR A 225 31.165 57.734 46.714 1.00 27.82 C ANISOU 4561 C THR B 225 3466 4027 3078 -981 474 -68 C ATOM 4562 O THR A 225 29.954 57.795 46.936 1.00 28.03 O ANISOU 4562 O THR B 225 3440 4103 3109 -1017 541 -91 O ATOM 4563 CB THR A 225 32.496 56.151 45.271 1.00 27.34 C ANISOU 4563 CB THR B 225 3480 3853 3056 -965 373 21 C ATOM 4564 OG1 THR A 225 32.851 55.819 43.919 1.00 26.99 O ANISOU 4564 OG1 THR B 225 3418 3763 3073 -951 335 22 O ATOM 4565 CG2 THR A 225 31.654 54.964 45.746 1.00 28.00 C ANISOU 4565 CG2 THR B 225 3603 3930 3105 -1052 435 52 C ATOM 4566 N LYS A 226 32.098 57.903 47.651 1.00 27.78 N ANISOU 4566 N LYS B 226 3522 4034 2999 -981 456 -68 N ATOM 4567 CA LYS A 226 31.792 58.019 49.076 1.00 28.76 C ANISOU 4567 CA LYS B 226 3670 4236 3019 -1041 514 -95 C ATOM 4568 C LYS A 226 31.029 59.306 49.405 1.00 28.90 C ANISOU 4568 C LYS B 226 3625 4283 3075 -1039 603 -207 C ATOM 4569 O LYS A 226 30.084 59.281 50.194 1.00 29.24 O ANISOU 4569 O LYS B 226 3652 4384 3074 -1093 685 -240 O ATOM 4570 CB LYS A 226 33.075 57.903 49.921 1.00 29.55 C ANISOU 4570 CB LYS B 226 3830 4389 3010 -1052 461 -61 C ATOM 4571 CG LYS A 226 33.582 56.465 50.081 1.00 31.27 C ANISOU 4571 CG LYS B 226 4110 4593 3177 -1056 416 82 C ATOM 4572 CD LYS A 226 34.967 56.417 50.742 1.00 34.95 C ANISOU 4572 CD LYS B 226 4601 5137 3542 -1040 347 148 C ATOM 4573 CE LYS A 226 35.357 55.007 51.221 1.00 37.18 C ANISOU 4573 CE LYS B 226 4936 5422 3769 -1033 329 327 C ATOM 4574 NZ LYS A 226 34.639 53.910 50.498 1.00 38.48 N ANISOU 4574 NZ LYS B 226 5138 5442 4042 -1028 376 381 N ATOM 4575 N GLU A 227 31.401 60.416 48.772 1.00 28.06 N ANISOU 4575 N GLU B 227 3478 4123 3062 -974 604 -260 N ATOM 4576 CA GLU A 227 30.786 61.709 49.080 1.00 28.94 C ANISOU 4576 CA GLU B 227 3533 4222 3240 -956 717 -362 C ATOM 4577 C GLU A 227 29.365 61.827 48.522 1.00 28.90 C ANISOU 4577 C GLU B 227 3430 4216 3336 -914 782 -340 C ATOM 4578 O GLU A 227 28.496 62.395 49.177 1.00 29.12 O ANISOU 4578 O GLU B 227 3415 4265 3385 -923 900 -407 O ATOM 4579 CB GLU A 227 31.670 62.869 48.620 1.00 28.95 C ANISOU 4579 CB GLU B 227 3529 4145 3324 -902 718 -415 C ATOM 4580 CG GLU A 227 32.989 62.927 49.384 1.00 30.29 C ANISOU 4580 CG GLU B 227 3774 4360 3377 -968 674 -463 C ATOM 4581 CD GLU A 227 33.871 64.080 48.965 1.00 33.74 C ANISOU 4581 CD GLU B 227 4207 4722 3892 -940 688 -532 C ATOM 4582 OE1 GLU A 227 33.340 65.047 48.385 1.00 35.70 O ANISOU 4582 OE1 GLU B 227 4404 4867 4292 -874 775 -562 O ATOM 4583 OE2 GLU A 227 35.099 64.022 49.220 1.00 34.56 O ANISOU 4583 OE2 GLU B 227 4351 4872 3907 -984 618 -546 O ATOM 4584 N THR A 228 29.133 61.263 47.338 1.00 28.03 N ANISOU 4584 N THR B 228 3274 4101 3275 -879 711 -251 N ATOM 4585 CA THR A 228 27.791 61.187 46.763 1.00 28.61 C ANISOU 4585 CA THR B 228 3232 4228 3410 -860 752 -212 C ATOM 4586 C THR A 228 26.848 60.484 47.726 1.00 29.40 C ANISOU 4586 C THR B 228 3338 4405 3427 -949 815 -233 C ATOM 4587 O THR A 228 25.769 60.988 48.027 1.00 30.53 O ANISOU 4587 O THR B 228 3392 4594 3613 -933 914 -260 O ATOM 4588 CB THR A 228 27.812 60.423 45.424 1.00 28.22 C ANISOU 4588 CB THR B 228 3146 4204 3373 -861 656 -130 C ATOM 4589 OG1 THR A 228 28.490 61.201 44.423 1.00 27.76 O ANISOU 4589 OG1 THR B 228 3053 4098 3397 -773 610 -99 O ATOM 4590 CG2 THR A 228 26.395 60.223 44.874 1.00 29.06 C ANISOU 4590 CG2 THR B 228 3116 4421 3505 -874 690 -90 C ATOM 4591 N LYS A 229 27.271 59.323 48.215 1.00 28.96 N ANISOU 4591 N LYS B 229 3385 4360 3260 -1035 768 -210 N ATOM 4592 CA LYS A 229 26.464 58.528 49.132 1.00 29.48 C ANISOU 4592 CA LYS B 229 3470 4493 3237 -1133 826 -211 C ATOM 4593 C LYS A 229 26.092 59.290 50.403 1.00 30.09 C ANISOU 4593 C LYS B 229 3543 4616 3272 -1153 933 -297 C ATOM 4594 O LYS A 229 24.954 59.204 50.868 1.00 30.89 O ANISOU 4594 O LYS B 229 3588 4789 3361 -1197 1020 -320 O ATOM 4595 CB LYS A 229 27.178 57.223 49.489 1.00 29.50 C ANISOU 4595 CB LYS B 229 3594 4471 3143 -1203 768 -144 C ATOM 4596 CG LYS A 229 27.206 56.205 48.343 1.00 29.22 C ANISOU 4596 CG LYS B 229 3565 4388 3150 -1223 712 -84 C ATOM 4597 CD LYS A 229 28.105 55.016 48.672 1.00 29.73 C ANISOU 4597 CD LYS B 229 3755 4382 3158 -1259 676 -6 C ATOM 4598 CE LYS A 229 28.292 54.110 47.472 1.00 30.57 C ANISOU 4598 CE LYS B 229 3877 4411 3328 -1277 644 22 C ATOM 4599 NZ LYS A 229 27.070 53.286 47.230 1.00 33.16 N ANISOU 4599 NZ LYS B 229 4174 4769 3658 -1390 713 8 N ATOM 4600 N LYS A 230 27.037 60.042 50.952 1.00 29.41 N ANISOU 4600 N LYS B 230 3511 4503 3161 -1136 935 -358 N ATOM 4601 CA LYS A 230 26.793 60.818 52.165 1.00 30.14 C ANISOU 4601 CA LYS B 230 3606 4644 3202 -1180 1052 -473 C ATOM 4602 C LYS A 230 25.883 62.030 51.918 1.00 30.52 C ANISOU 4602 C LYS B 230 3545 4652 3400 -1102 1182 -552 C ATOM 4603 O LYS A 230 24.977 62.296 52.705 1.00 31.36 O ANISOU 4603 O LYS B 230 3610 4813 3492 -1139 1308 -624 O ATOM 4604 CB LYS A 230 28.118 61.270 52.781 1.00 30.15 C ANISOU 4604 CB LYS B 230 3688 4649 3119 -1211 1022 -532 C ATOM 4605 CG LYS A 230 27.968 62.173 53.993 1.00 31.33 C ANISOU 4605 CG LYS B 230 3841 4858 3205 -1284 1156 -689 C ATOM 4606 CD LYS A 230 29.236 62.204 54.847 1.00 31.36 C ANISOU 4606 CD LYS B 230 3922 4951 3042 -1375 1107 -730 C ATOM 4607 CE LYS A 230 29.045 63.083 56.071 1.00 33.12 C ANISOU 4607 CE LYS B 230 4145 5260 3179 -1484 1256 -916 C ATOM 4608 NZ LYS A 230 30.236 63.062 56.963 1.00 34.48 N ANISOU 4608 NZ LYS B 230 4372 5582 3147 -1603 1202 -955 N ATOM 4609 N ILE A 231 26.134 62.756 50.832 1.00 29.87 N ANISOU 4609 N ILE B 231 3410 4475 3465 -990 1159 -526 N ATOM 4610 CA ILE A 231 25.377 63.967 50.485 1.00 30.86 C ANISOU 4610 CA ILE B 231 3423 4539 3764 -883 1288 -560 C ATOM 4611 C ILE A 231 23.902 63.651 50.207 1.00 31.83 C ANISOU 4611 C ILE B 231 3413 4746 3934 -855 1338 -497 C ATOM 4612 O ILE A 231 23.018 64.328 50.715 1.00 32.79 O ANISOU 4612 O ILE B 231 3458 4873 4127 -823 1490 -557 O ATOM 4613 CB ILE A 231 26.022 64.689 49.270 1.00 30.05 C ANISOU 4613 CB ILE B 231 3289 4326 3801 -765 1237 -499 C ATOM 4614 CG1 ILE A 231 27.350 65.338 49.677 1.00 29.99 C ANISOU 4614 CG1 ILE B 231 3390 4232 3774 -795 1240 -597 C ATOM 4615 CG2 ILE A 231 25.081 65.754 48.677 1.00 31.02 C ANISOU 4615 CG2 ILE B 231 3267 4395 4123 -625 1360 -460 C ATOM 4616 CD1 ILE A 231 28.296 65.596 48.513 1.00 28.11 C ANISOU 4616 CD1 ILE B 231 3159 3914 3609 -723 1137 -520 C ATOM 4617 N MET A 232 23.649 62.624 49.402 1.00 31.63 N ANISOU 4617 N MET B 232 3357 4793 3869 -877 1220 -385 N ATOM 4618 CA MET A 232 22.277 62.168 49.125 1.00 32.97 C ANISOU 4618 CA MET B 232 3394 5083 4050 -888 1251 -329 C ATOM 4619 C MET A 232 21.737 61.185 50.183 1.00 33.73 C ANISOU 4619 C MET B 232 3543 5270 4004 -1030 1286 -370 C ATOM 4620 O MET A 232 20.611 60.710 50.071 1.00 34.63 O ANISOU 4620 O MET B 232 3554 5494 4108 -1069 1317 -338 O ATOM 4621 CB MET A 232 22.213 61.550 47.724 1.00 32.37 C ANISOU 4621 CB MET B 232 3249 5062 3986 -876 1125 -212 C ATOM 4622 CG MET A 232 22.472 62.567 46.621 1.00 32.71 C ANISOU 4622 CG MET B 232 3200 5058 4170 -729 1105 -140 C ATOM 4623 SD MET A 232 22.581 61.853 44.979 1.00 34.46 S ANISOU 4623 SD MET B 232 3350 5376 4368 -744 950 -20 S ATOM 4624 CE MET A 232 22.037 63.248 43.976 1.00 34.62 C ANISOU 4624 CE MET B 232 3162 5431 4559 -555 995 105 C ATOM 4625 N GLU A 233 22.548 60.885 51.201 1.00 35.84 N ANISOU 4625 N GLU B 233 3919 5989 3709 -997 1263 -628 N ATOM 4626 CA GLU A 233 22.147 60.054 52.337 1.00 37.48 C ANISOU 4626 CA GLU B 233 4161 6254 3825 -1055 1408 -557 C ATOM 4627 C GLU A 233 21.567 58.703 51.897 1.00 38.06 C ANISOU 4627 C GLU B 233 4234 6244 3983 -1148 1522 -497 C ATOM 4628 O GLU A 233 20.508 58.283 52.358 1.00 38.34 O ANISOU 4628 O GLU B 233 4222 6318 4025 -1220 1654 -529 O ATOM 4629 CB GLU A 233 21.156 60.821 53.224 1.00 38.81 C ANISOU 4629 CB GLU B 233 4253 6553 3940 -1061 1466 -675 C ATOM 4630 CG GLU A 233 21.612 62.246 53.527 1.00 39.26 C ANISOU 4630 CG GLU B 233 4290 6680 3948 -973 1355 -768 C ATOM 4631 CD GLU A 233 21.020 62.830 54.789 1.00 41.64 C ANISOU 4631 CD GLU B 233 4552 7126 4142 -972 1423 -847 C ATOM 4632 OE1 GLU A 233 20.009 62.296 55.290 1.00 44.65 O ANISOU 4632 OE1 GLU B 233 4897 7559 4509 -1040 1554 -858 O ATOM 4633 OE2 GLU A 233 21.569 63.841 55.281 1.00 42.40 O ANISOU 4633 OE2 GLU B 233 4649 7286 4173 -905 1349 -907 O ATOM 4634 N ASP A 234 22.286 58.028 51.007 1.00 37.39 N ANISOU 4634 N ASP B 234 4197 6042 3968 -1150 1476 -419 N ATOM 4635 CA ASP A 234 21.825 56.771 50.440 1.00 38.29 C ANISOU 4635 CA ASP B 234 4304 6058 4185 -1237 1575 -378 C ATOM 4636 C ASP A 234 23.019 55.925 49.996 1.00 37.99 C ANISOU 4636 C ASP B 234 4367 5905 4162 -1221 1539 -239 C ATOM 4637 O ASP A 234 23.559 56.118 48.906 1.00 36.68 O ANISOU 4637 O ASP B 234 4191 5676 4070 -1190 1426 -264 O ATOM 4638 CB ASP A 234 20.875 57.059 49.267 1.00 37.89 C ANISOU 4638 CB ASP B 234 4127 5994 4277 -1268 1543 -531 C ATOM 4639 CG ASP A 234 20.157 55.816 48.759 1.00 39.16 C ANISOU 4639 CG ASP B 234 4248 6078 4552 -1374 1664 -534 C ATOM 4640 OD1 ASP A 234 20.473 54.695 49.200 1.00 40.58 O ANISOU 4640 OD1 ASP B 234 4511 6186 4721 -1425 1772 -406 O ATOM 4641 OD2 ASP A 234 19.253 55.869 47.904 1.00 40.66 O ANISOU 4641 OD2 ASP B 234 4323 6273 4852 -1412 1662 -665 O ATOM 4642 N ASP A 235 23.415 54.985 50.855 1.00 39.45 N ANISOU 4642 N ASP B 235 4651 6066 4274 -1239 1640 -90 N ATOM 4643 CA ASP A 235 24.507 54.052 50.568 1.00 39.65 C ANISOU 4643 CA ASP B 235 4775 5978 4312 -1221 1627 54 C ATOM 4644 C ASP A 235 24.189 53.095 49.414 1.00 39.48 C ANISOU 4644 C ASP B 235 4720 5821 4459 -1297 1670 37 C ATOM 4645 O ASP A 235 25.098 52.483 48.864 1.00 39.15 O ANISOU 4645 O ASP B 235 4738 5679 4459 -1277 1628 119 O ATOM 4646 CB ASP A 235 24.869 53.228 51.821 1.00 41.44 C ANISOU 4646 CB ASP B 235 5114 6214 4418 -1215 1742 227 C ATOM 4647 CG ASP A 235 25.673 54.023 52.853 1.00 42.50 C ANISOU 4647 CG ASP B 235 5303 6477 4369 -1114 1665 269 C ATOM 4648 OD1 ASP A 235 26.377 54.984 52.476 1.00 42.59 O ANISOU 4648 OD1 ASP B 235 5296 6524 4363 -1044 1511 203 O ATOM 4649 OD2 ASP A 235 25.669 53.745 54.076 1.00 45.90 O ANISOU 4649 OD2 ASP B 235 5794 6983 4662 -1099 1755 366 O ATOM 4650 N SER A 236 22.911 52.965 49.056 1.00 40.04 N ANISOU 4650 N SER B 236 4688 5897 4629 -1383 1752 -80 N ATOM 4651 CA SER A 236 22.492 52.070 47.972 1.00 39.99 C ANISOU 4651 CA SER B 236 4628 5780 4787 -1464 1800 -127 C ATOM 4652 C SER A 236 22.753 52.600 46.551 1.00 38.34 C ANISOU 4652 C SER B 236 4351 5554 4663 -1428 1646 -233 C ATOM 4653 O SER A 236 22.686 51.826 45.592 1.00 38.09 O ANISOU 4653 O SER B 236 4288 5432 4754 -1480 1664 -262 O ATOM 4654 CB SER A 236 21.013 51.672 48.134 1.00 41.34 C ANISOU 4654 CB SER B 236 4702 5971 5034 -1576 1955 -226 C ATOM 4655 OG SER A 236 20.150 52.545 47.430 1.00 41.47 O ANISOU 4655 OG SER B 236 4580 6072 5106 -1576 1883 -412 O ATOM 4656 N ILE A 237 23.052 53.894 46.404 1.00 37.00 N ANISOU 4656 N ILE B 237 4160 5470 4431 -1340 1501 -292 N ATOM 4657 CA ILE A 237 23.392 54.442 45.084 1.00 35.90 C ANISOU 4657 CA ILE B 237 3971 5314 4356 -1294 1357 -370 C ATOM 4658 C ILE A 237 24.774 53.953 44.669 1.00 34.57 C ANISOU 4658 C ILE B 237 3898 5049 4186 -1256 1292 -255 C ATOM 4659 O ILE A 237 25.767 54.253 45.330 1.00 34.60 O ANISOU 4659 O ILE B 237 3993 5064 4090 -1191 1243 -159 O ATOM 4660 CB ILE A 237 23.374 55.992 45.054 1.00 35.14 C ANISOU 4660 CB ILE B 237 3835 5317 4201 -1206 1232 -453 C ATOM 4661 CG1 ILE A 237 21.977 56.538 45.350 1.00 36.65 C ANISOU 4661 CG1 ILE B 237 3917 5606 4405 -1233 1285 -582 C ATOM 4662 CG2 ILE A 237 23.814 56.494 43.682 1.00 34.41 C ANISOU 4662 CG2 ILE B 237 3709 5197 4169 -1154 1094 -505 C ATOM 4663 CD1 ILE A 237 21.983 57.997 45.793 1.00 36.89 C ANISOU 4663 CD1 ILE B 237 3929 5728 4358 -1148 1199 -639 C ATOM 4664 N ALA A 238 24.820 53.196 43.579 1.00 33.89 N ANISOU 4664 N ALA B 238 3783 4879 4212 -1298 1291 -279 N ATOM 4665 CA ALA A 238 26.066 52.691 43.018 1.00 32.79 C ANISOU 4665 CA ALA B 238 3719 4647 4093 -1267 1230 -192 C ATOM 4666 C ALA A 238 26.776 53.818 42.285 1.00 30.93 C ANISOU 4666 C ALA B 238 3475 4451 3827 -1179 1062 -231 C ATOM 4667 O ALA A 238 26.170 54.486 41.454 1.00 30.43 O ANISOU 4667 O ALA B 238 3321 4437 3804 -1169 1002 -349 O ATOM 4668 CB ALA A 238 25.782 51.540 42.068 1.00 33.14 C ANISOU 4668 CB ALA B 238 3721 4596 4275 -1346 1292 -228 C ATOM 4669 N VAL A 239 28.048 54.044 42.614 1.00 29.75 N ANISOU 4669 N VAL B 239 3418 4283 3604 -1111 992 -133 N ATOM 4670 CA VAL A 239 28.838 55.109 41.988 1.00 28.04 C ANISOU 4670 CA VAL B 239 3203 4091 3361 -1033 847 -162 C ATOM 4671 C VAL A 239 30.248 54.625 41.653 1.00 27.14 C ANISOU 4671 C VAL B 239 3167 3899 3246 -1001 792 -70 C ATOM 4672 O VAL A 239 30.979 54.152 42.522 1.00 27.20 O ANISOU 4672 O VAL B 239 3257 3886 3192 -982 821 38 O ATOM 4673 CB VAL A 239 28.954 56.351 42.896 1.00 27.88 C ANISOU 4673 CB VAL B 239 3197 4160 3235 -971 800 -174 C ATOM 4674 CG1 VAL A 239 29.597 57.512 42.136 1.00 26.71 C ANISOU 4674 CG1 VAL B 239 3037 4024 3087 -901 667 -221 C ATOM 4675 CG2 VAL A 239 27.599 56.762 43.447 1.00 28.94 C ANISOU 4675 CG2 VAL B 239 3261 4375 3361 -1000 868 -256 C ATOM 4676 N SER A 240 30.620 54.760 40.387 1.00 26.05 N ANISOU 4676 N SER B 240 2999 3729 3170 -989 712 -115 N ATOM 4677 CA SER A 240 31.953 54.426 39.921 1.00 25.44 C ANISOU 4677 CA SER B 240 2981 3586 3099 -957 651 -49 C ATOM 4678 C SER A 240 32.419 55.514 38.973 1.00 24.91 C ANISOU 4678 C SER B 240 2887 3545 3032 -904 530 -108 C ATOM 4679 O SER A 240 31.686 55.910 38.071 1.00 24.62 O ANISOU 4679 O SER B 240 2776 3536 3042 -912 506 -197 O ATOM 4680 CB SER A 240 31.956 53.080 39.209 1.00 25.64 C ANISOU 4680 CB SER B 240 3000 3519 3224 -1015 708 -36 C ATOM 4681 OG SER A 240 31.905 52.021 40.137 1.00 26.38 O ANISOU 4681 OG SER B 240 3148 3558 3316 -1050 820 56 O ATOM 4682 N ALA A 241 33.648 55.977 39.172 1.00 24.55 N ANISOU 4682 N ALA B 241 2900 3493 2934 -848 459 -58 N ATOM 4683 CA ALA A 241 34.160 57.144 38.470 1.00 24.20 C ANISOU 4683 CA ALA B 241 2842 3470 2884 -798 358 -104 C ATOM 4684 C ALA A 241 35.530 56.888 37.848 1.00 23.89 C ANISOU 4684 C ALA B 241 2844 3374 2857 -775 298 -61 C ATOM 4685 O ALA A 241 36.323 56.098 38.368 1.00 24.59 O ANISOU 4685 O ALA B 241 2988 3427 2927 -774 316 15 O ATOM 4686 CB ALA A 241 34.244 58.312 39.427 1.00 24.36 C ANISOU 4686 CB ALA B 241 2876 3553 2827 -752 332 -118 C ATOM 4687 N THR A 242 35.783 57.556 36.726 1.00 23.58 N ANISOU 4687 N THR B 242 2779 3332 2849 -754 230 -106 N ATOM 4688 CA THR A 242 37.107 57.673 36.125 1.00 23.32 C ANISOU 4688 CA THR B 242 2779 3262 2821 -728 166 -81 C ATOM 4689 C THR A 242 37.429 59.164 36.120 1.00 23.06 C ANISOU 4689 C THR B 242 2747 3259 2757 -679 107 -115 C ATOM 4690 O THR A 242 36.687 59.956 35.535 1.00 22.79 O ANISOU 4690 O THR B 242 2671 3249 2740 -665 92 -166 O ATOM 4691 CB THR A 242 37.097 57.143 34.675 1.00 23.32 C ANISOU 4691 CB THR B 242 2744 3229 2889 -750 151 -109 C ATOM 4692 OG1 THR A 242 36.679 55.774 34.645 1.00 23.79 O ANISOU 4692 OG1 THR B 242 2792 3252 2996 -803 217 -97 O ATOM 4693 CG2 THR A 242 38.512 57.120 34.079 1.00 23.52 C ANISOU 4693 CG2 THR B 242 2803 3214 2919 -729 96 -82 C ATOM 4694 N CYS A 243 38.509 59.559 36.782 1.00 23.08 N ANISOU 4694 N CYS B 243 2792 3261 2717 -651 76 -90 N ATOM 4695 CA CYS A 243 38.841 60.972 36.891 1.00 23.10 C ANISOU 4695 CA CYS B 243 2793 3282 2702 -614 34 -132 C ATOM 4696 C CYS A 243 40.092 61.268 36.079 1.00 22.35 C ANISOU 4696 C CYS B 243 2716 3144 2631 -601 -18 -128 C ATOM 4697 O CYS A 243 41.142 60.668 36.307 1.00 22.36 O ANISOU 4697 O CYS B 243 2747 3131 2619 -602 -32 -94 O ATOM 4698 CB CYS A 243 39.003 61.380 38.353 1.00 23.72 C ANISOU 4698 CB CYS B 243 2891 3411 2712 -597 45 -137 C ATOM 4699 SG CYS A 243 37.467 61.217 39.303 1.00 25.58 S ANISOU 4699 SG CYS B 243 3101 3705 2915 -614 114 -151 S ATOM 4700 N VAL A 244 39.955 62.175 35.116 1.00 21.85 N ANISOU 4700 N VAL B 244 2635 3064 2605 -585 -42 -159 N ATOM 4701 CA VAL A 244 41.011 62.464 34.147 1.00 21.48 C ANISOU 4701 CA VAL B 244 2602 2974 2587 -579 -78 -154 C ATOM 4702 C VAL A 244 41.346 63.947 34.133 1.00 21.22 C ANISOU 4702 C VAL B 244 2573 2924 2564 -551 -93 -188 C ATOM 4703 O VAL A 244 40.454 64.785 34.079 1.00 21.10 O ANISOU 4703 O VAL B 244 2541 2916 2560 -527 -83 -213 O ATOM 4704 CB VAL A 244 40.592 62.048 32.715 1.00 21.18 C ANISOU 4704 CB VAL B 244 2540 2924 2585 -587 -83 -147 C ATOM 4705 CG1 VAL A 244 41.785 62.127 31.763 1.00 20.91 C ANISOU 4705 CG1 VAL B 244 2523 2852 2571 -587 -112 -135 C ATOM 4706 CG2 VAL A 244 39.994 60.651 32.720 1.00 21.93 C ANISOU 4706 CG2 VAL B 244 2616 3031 2687 -622 -53 -134 C ATOM 4707 N ARG A 245 42.637 64.253 34.171 1.00 20.82 N ANISOU 4707 N ARG B 245 2544 2847 2520 -553 -114 -194 N ATOM 4708 CA ARG A 245 43.125 65.613 34.007 1.00 21.06 C ANISOU 4708 CA ARG B 245 2580 2841 2582 -537 -117 -231 C ATOM 4709 C ARG A 245 43.336 65.915 32.533 1.00 20.66 C ANISOU 4709 C ARG B 245 2535 2742 2572 -532 -121 -206 C ATOM 4710 O ARG A 245 43.917 65.110 31.817 1.00 20.20 O ANISOU 4710 O ARG B 245 2481 2678 2516 -551 -134 -178 O ATOM 4711 CB ARG A 245 44.447 65.789 34.755 1.00 21.30 C ANISOU 4711 CB ARG B 245 2619 2873 2601 -548 -132 -264 C ATOM 4712 CG ARG A 245 44.813 67.230 34.983 1.00 22.19 C ANISOU 4712 CG ARG B 245 2727 2952 2751 -541 -120 -326 C ATOM 4713 CD ARG A 245 44.037 67.849 36.117 1.00 23.14 C ANISOU 4713 CD ARG B 245 2832 3110 2850 -525 -104 -375 C ATOM 4714 NE ARG A 245 44.499 67.330 37.400 1.00 23.92 N ANISOU 4714 NE ARG B 245 2922 3284 2881 -529 -119 -402 N ATOM 4715 CZ ARG A 245 43.947 67.627 38.567 1.00 23.39 C ANISOU 4715 CZ ARG B 245 2839 3277 2770 -517 -107 -446 C ATOM 4716 NH1 ARG A 245 42.933 68.476 38.633 1.00 23.31 N ANISOU 4716 NH1 ARG B 245 2815 3252 2788 -504 -80 -478 N ATOM 4717 NH2 ARG A 245 44.438 67.095 39.682 1.00 23.36 N ANISOU 4717 NH2 ARG B 245 2831 3356 2690 -513 -124 -460 N ATOM 4718 N ILE A 246 42.842 67.065 32.081 1.00 21.12 N ANISOU 4718 N ILE B 246 2595 2768 2661 -501 -106 -213 N ATOM 4719 CA ILE A 246 43.055 67.522 30.710 1.00 21.28 C ANISOU 4719 CA ILE B 246 2629 2746 2711 -485 -103 -178 C ATOM 4720 C ILE A 246 43.660 68.929 30.714 1.00 22.10 C ANISOU 4720 C ILE B 246 2755 2776 2864 -474 -76 -198 C ATOM 4721 O ILE A 246 43.721 69.554 31.767 1.00 22.77 O ANISOU 4721 O ILE B 246 2835 2852 2965 -477 -64 -251 O ATOM 4722 CB ILE A 246 41.745 67.460 29.898 1.00 21.33 C ANISOU 4722 CB ILE B 246 2615 2785 2704 -444 -106 -150 C ATOM 4723 CG1 ILE A 246 40.656 68.364 30.487 1.00 21.74 C ANISOU 4723 CG1 ILE B 246 2653 2840 2766 -401 -91 -174 C ATOM 4724 CG2 ILE A 246 41.260 66.013 29.790 1.00 20.78 C ANISOU 4724 CG2 ILE B 246 2516 2777 2601 -470 -122 -145 C ATOM 4725 CD1 ILE A 246 39.549 68.657 29.481 1.00 21.79 C ANISOU 4725 CD1 ILE B 246 2641 2872 2768 -342 -97 -146 C ATOM 4726 N PRO A 247 44.148 69.409 29.569 1.00 22.29 N ANISOU 4726 N PRO B 247 2803 2750 2917 -465 -61 -160 N ATOM 4727 CA PRO A 247 44.786 70.732 29.484 1.00 22.84 C ANISOU 4727 CA PRO B 247 2898 2731 3050 -462 -18 -174 C ATOM 4728 C PRO A 247 43.827 71.940 29.471 1.00 23.17 C ANISOU 4728 C PRO B 247 2950 2725 3128 -403 13 -164 C ATOM 4729 O PRO A 247 43.746 72.694 28.501 1.00 23.16 O ANISOU 4729 O PRO B 247 2978 2665 3155 -364 43 -109 O ATOM 4730 CB PRO A 247 45.583 70.642 28.171 1.00 22.84 C ANISOU 4730 CB PRO B 247 2922 2701 3057 -473 -5 -121 C ATOM 4731 CG PRO A 247 45.503 69.215 27.761 1.00 22.35 C ANISOU 4731 CG PRO B 247 2840 2718 2936 -488 -49 -101 C ATOM 4732 CD PRO A 247 44.217 68.713 28.277 1.00 22.19 C ANISOU 4732 CD PRO B 247 2793 2760 2880 -462 -75 -106 C ATOM 4733 N VAL A 248 43.129 72.111 30.583 1.00 23.46 N ANISOU 4733 N VAL B 248 2962 2789 3163 -393 8 -218 N ATOM 4734 CA VAL A 248 42.221 73.227 30.829 1.00 24.37 C ANISOU 4734 CA VAL B 248 3077 2862 3320 -339 36 -231 C ATOM 4735 C VAL A 248 42.680 73.828 32.150 1.00 24.69 C ANISOU 4735 C VAL B 248 3103 2879 3400 -373 58 -329 C ATOM 4736 O VAL A 248 43.010 73.082 33.069 1.00 23.91 O ANISOU 4736 O VAL B 248 2980 2851 3255 -415 31 -378 O ATOM 4737 CB VAL A 248 40.780 72.699 30.970 1.00 24.42 C ANISOU 4737 CB VAL B 248 3049 2953 3275 -297 5 -222 C ATOM 4738 CG1 VAL A 248 39.815 73.809 31.409 1.00 25.84 C ANISOU 4738 CG1 VAL B 248 3219 3101 3500 -237 31 -252 C ATOM 4739 CG2 VAL A 248 40.327 72.039 29.667 1.00 24.19 C ANISOU 4739 CG2 VAL B 248 3020 2969 3203 -265 -21 -146 C ATOM 4740 N LEU A 249 42.743 75.154 32.248 1.00 25.48 N ANISOU 4740 N LEU B 249 3216 2881 3583 -353 109 -360 N ATOM 4741 CA LEU A 249 43.184 75.793 33.487 1.00 26.05 C ANISOU 4741 CA LEU B 249 3263 2935 3698 -388 133 -474 C ATOM 4742 C LEU A 249 42.066 75.846 34.525 1.00 26.24 C ANISOU 4742 C LEU B 249 3251 3025 3695 -360 121 -530 C ATOM 4743 O LEU A 249 42.305 75.535 35.683 1.00 26.01 O ANISOU 4743 O LEU B 249 3189 3068 3626 -396 105 -612 O ATOM 4744 CB LEU A 249 43.740 77.200 33.236 1.00 27.29 C ANISOU 4744 CB LEU B 249 3443 2950 3975 -389 206 -503 C ATOM 4745 CG LEU A 249 44.960 77.297 32.318 1.00 27.71 C ANISOU 4745 CG LEU B 249 3530 2929 4068 -430 237 -464 C ATOM 4746 CD1 LEU A 249 45.508 78.713 32.327 1.00 29.29 C ANISOU 4746 CD1 LEU B 249 3746 2983 4401 -445 325 -515 C ATOM 4747 CD2 LEU A 249 46.038 76.299 32.728 1.00 28.22 C ANISOU 4747 CD2 LEU B 249 3569 3078 4077 -500 194 -510 C ATOM 4748 N SER A 250 40.859 76.223 34.098 1.00 26.55 N ANISOU 4748 N SER B 250 3292 3049 3746 -291 127 -487 N ATOM 4749 CA SER A 250 39.702 76.370 34.987 1.00 27.04 C ANISOU 4749 CA SER B 250 3314 3169 3792 -259 123 -543 C ATOM 4750 C SER A 250 38.430 75.758 34.403 1.00 26.11 C ANISOU 4750 C SER B 250 3182 3118 3620 -205 92 -475 C ATOM 4751 O SER A 250 38.189 75.854 33.205 1.00 26.34 O ANISOU 4751 O SER B 250 3235 3113 3660 -156 87 -390 O ATOM 4752 CB SER A 250 39.412 77.851 35.262 1.00 28.49 C ANISOU 4752 CB SER B 250 3496 3250 4080 -218 179 -602 C ATOM 4753 OG SER A 250 40.597 78.608 35.357 1.00 30.86 O ANISOU 4753 OG SER B 250 3814 3451 4461 -262 223 -651 O ATOM 4754 N ALA A 251 37.619 75.179 35.295 1.00 25.36 N ANISOU 4754 N ALA B 251 3044 3124 3467 -212 75 -521 N ATOM 4755 CA ALA A 251 36.293 74.616 35.036 1.00 24.82 C ANISOU 4755 CA ALA B 251 2942 3135 3355 -173 53 -494 C ATOM 4756 C ALA A 251 36.356 73.111 34.754 1.00 23.75 C ANISOU 4756 C ALA B 251 2802 3084 3139 -218 19 -446 C ATOM 4757 O ALA A 251 37.027 72.672 33.819 1.00 23.34 O ANISOU 4757 O ALA B 251 2779 3009 3081 -231 1 -382 O ATOM 4758 CB ALA A 251 35.550 75.370 33.921 1.00 25.24 C ANISOU 4758 CB ALA B 251 3000 3136 3455 -81 56 -439 C ATOM 4759 N HIS A 252 35.687 72.323 35.595 1.00 23.48 N ANISOU 4759 N HIS B 252 2730 3142 3048 -246 17 -480 N ATOM 4760 CA HIS A 252 35.581 70.878 35.385 1.00 22.92 C ANISOU 4760 CA HIS B 252 2652 3141 2918 -289 -2 -440 C ATOM 4761 C HIS A 252 34.393 70.544 34.498 1.00 22.90 C ANISOU 4761 C HIS B 252 2608 3180 2911 -250 -14 -418 C ATOM 4762 O HIS A 252 33.330 71.131 34.640 1.00 23.35 O ANISOU 4762 O HIS B 252 2626 3261 2985 -201 -5 -455 O ATOM 4763 CB HIS A 252 35.437 70.140 36.720 1.00 23.10 C ANISOU 4763 CB HIS B 252 2658 3238 2882 -339 16 -478 C ATOM 4764 CG HIS A 252 36.669 70.186 37.563 1.00 23.78 C ANISOU 4764 CG HIS B 252 2774 3313 2947 -376 16 -497 C ATOM 4765 ND1 HIS A 252 36.661 69.995 38.930 1.00 25.78 N ANISOU 4765 ND1 HIS B 252 3016 3633 3145 -400 33 -544 N ATOM 4766 CD2 HIS A 252 37.955 70.417 37.225 1.00 23.18 C ANISOU 4766 CD2 HIS B 252 2734 3180 2894 -389 0 -483 C ATOM 4767 CE1 HIS A 252 37.896 70.103 39.391 1.00 24.26 C ANISOU 4767 CE1 HIS B 252 2848 3432 2939 -421 21 -560 C ATOM 4768 NE2 HIS A 252 38.701 70.359 38.376 1.00 24.72 N ANISOU 4768 NE2 HIS B 252 2933 3412 3050 -418 2 -528 N ATOM 4769 N SER A 253 34.593 69.598 33.584 1.00 22.27 N ANISOU 4769 N SER B 253 2533 3119 2811 -270 -36 -367 N ATOM 4770 CA SER A 253 33.521 69.024 32.782 1.00 22.31 C ANISOU 4770 CA SER B 253 2487 3189 2802 -248 -50 -364 C ATOM 4771 C SER A 253 33.394 67.527 33.095 1.00 21.81 C ANISOU 4771 C SER B 253 2402 3181 2704 -323 -38 -369 C ATOM 4772 O SER A 253 34.391 66.859 33.387 1.00 21.06 O ANISOU 4772 O SER B 253 2348 3060 2595 -377 -35 -340 O ATOM 4773 CB SER A 253 33.798 69.217 31.289 1.00 22.45 C ANISOU 4773 CB SER B 253 2518 3185 2826 -201 -81 -308 C ATOM 4774 OG SER A 253 34.248 70.529 30.995 1.00 22.99 O ANISOU 4774 OG SER B 253 2628 3173 2933 -143 -78 -281 O ATOM 4775 N GLU A 254 32.177 67.001 33.009 1.00 21.66 N ANISOU 4775 N GLU B 254 2318 3233 2678 -324 -28 -406 N ATOM 4776 CA GLU A 254 31.899 65.616 33.383 1.00 21.65 C ANISOU 4776 CA GLU B 254 2293 3273 2659 -400 3 -417 C ATOM 4777 C GLU A 254 30.878 64.985 32.449 1.00 21.80 C ANISOU 4777 C GLU B 254 2236 3358 2687 -397 -3 -452 C ATOM 4778 O GLU A 254 29.805 65.545 32.214 1.00 22.18 O ANISOU 4778 O GLU B 254 2224 3461 2742 -344 -11 -500 O ATOM 4779 CB GLU A 254 31.375 65.548 34.820 1.00 22.35 C ANISOU 4779 CB GLU B 254 2370 3391 2731 -432 52 -454 C ATOM 4780 CG GLU A 254 32.335 66.075 35.878 1.00 22.82 C ANISOU 4780 CG GLU B 254 2491 3412 2770 -438 59 -438 C ATOM 4781 CD GLU A 254 31.703 66.189 37.257 1.00 26.17 C ANISOU 4781 CD GLU B 254 2895 3883 3164 -455 106 -483 C ATOM 4782 OE1 GLU A 254 30.454 66.298 37.361 1.00 26.35 O ANISOU 4782 OE1 GLU B 254 2856 3960 3196 -444 130 -536 O ATOM 4783 OE2 GLU A 254 32.464 66.175 38.248 1.00 27.31 O ANISOU 4783 OE2 GLU B 254 3082 4023 3270 -476 118 -471 O ATOM 4784 N SER A 255 31.237 63.831 31.895 1.00 21.53 N ANISOU 4784 N SER B 255 2201 3323 2656 -450 0 -437 N ATOM 4785 CA SER A 255 30.306 62.977 31.174 1.00 21.77 C ANISOU 4785 CA SER B 255 2150 3421 2699 -473 7 -491 C ATOM 4786 C SER A 255 29.643 62.068 32.200 1.00 22.33 C ANISOU 4786 C SER B 255 2192 3509 2784 -550 78 -528 C ATOM 4787 O SER A 255 30.292 61.202 32.785 1.00 22.41 O ANISOU 4787 O SER B 255 2249 3468 2796 -615 117 -488 O ATOM 4788 CB SER A 255 31.040 62.150 30.125 1.00 21.32 C ANISOU 4788 CB SER B 255 2103 3348 2648 -500 -15 -469 C ATOM 4789 OG SER A 255 30.146 61.312 29.413 1.00 21.64 O ANISOU 4789 OG SER B 255 2054 3461 2706 -526 -6 -541 O ATOM 4790 N VAL A 256 28.356 62.281 32.434 1.00 22.99 N ANISOU 4790 N VAL B 256 2198 3663 2875 -538 100 -600 N ATOM 4791 CA VAL A 256 27.651 61.628 33.529 1.00 23.53 C ANISOU 4791 CA VAL B 256 2239 3748 2952 -608 180 -635 C ATOM 4792 C VAL A 256 26.590 60.700 32.965 1.00 24.13 C ANISOU 4792 C VAL B 256 2214 3887 3068 -657 214 -720 C ATOM 4793 O VAL A 256 25.790 61.096 32.125 1.00 24.73 O ANISOU 4793 O VAL B 256 2206 4041 3150 -605 174 -790 O ATOM 4794 CB VAL A 256 26.985 62.667 34.459 1.00 24.01 C ANISOU 4794 CB VAL B 256 2285 3843 2995 -566 192 -667 C ATOM 4795 CG1 VAL A 256 26.212 61.983 35.586 1.00 25.52 C ANISOU 4795 CG1 VAL B 256 2446 4062 3188 -641 284 -703 C ATOM 4796 CG2 VAL A 256 28.017 63.635 35.012 1.00 23.61 C ANISOU 4796 CG2 VAL B 256 2324 3733 2915 -522 162 -604 C ATOM 4797 N TYR A 257 26.596 59.462 33.432 1.00 24.35 N ANISOU 4797 N TYR B 257 2247 3881 3125 -752 292 -716 N ATOM 4798 CA TYR A 257 25.560 58.500 33.089 1.00 25.03 C ANISOU 4798 CA TYR B 257 2232 4014 3264 -820 350 -811 C ATOM 4799 C TYR A 257 24.840 58.098 34.364 1.00 25.66 C ANISOU 4799 C TYR B 257 2301 4095 3355 -888 455 -828 C ATOM 4800 O TYR A 257 25.480 57.829 35.375 1.00 26.05 O ANISOU 4800 O TYR B 257 2439 4077 3381 -919 502 -741 O ATOM 4801 CB TYR A 257 26.165 57.266 32.420 1.00 24.48 C ANISOU 4801 CB TYR B 257 2174 3889 3240 -885 369 -799 C ATOM 4802 CG TYR A 257 25.156 56.154 32.226 1.00 25.19 C ANISOU 4802 CG TYR B 257 2162 4007 3402 -975 451 -903 C ATOM 4803 CD1 TYR A 257 24.175 56.253 31.247 1.00 25.40 C ANISOU 4803 CD1 TYR B 257 2061 4143 3449 -957 419 -1032 C ATOM 4804 CD2 TYR A 257 25.170 55.016 33.025 1.00 25.08 C ANISOU 4804 CD2 TYR B 257 2178 3914 3438 -1075 566 -877 C ATOM 4805 CE1 TYR A 257 23.247 55.253 31.057 1.00 25.75 C ANISOU 4805 CE1 TYR B 257 1998 4218 3567 -1046 497 -1149 C ATOM 4806 CE2 TYR A 257 24.234 54.005 32.842 1.00 26.49 C ANISOU 4806 CE2 TYR B 257 2261 4107 3699 -1168 656 -981 C ATOM 4807 CZ TYR A 257 23.275 54.135 31.849 1.00 26.04 C ANISOU 4807 CZ TYR B 257 2066 4161 3667 -1157 620 -1127 C ATOM 4808 OH TYR A 257 22.338 53.151 31.637 1.00 27.23 O ANISOU 4808 OH TYR B 257 2106 4333 3907 -1254 710 -1253 O ATOM 4809 N ILE A 258 23.515 58.081 34.323 1.00 26.79 N ANISOU 4809 N ILE B 258 2331 4322 3527 -906 491 -940 N ATOM 4810 CA ILE A 258 22.705 57.614 35.452 1.00 27.88 C ANISOU 4810 CA ILE B 258 2443 4468 3683 -983 606 -970 C ATOM 4811 C ILE A 258 21.666 56.616 34.986 1.00 28.94 C ANISOU 4811 C ILE B 258 2458 4641 3896 -1069 679 -1089 C ATOM 4812 O ILE A 258 21.271 56.619 33.835 1.00 29.50 O ANISOU 4812 O ILE B 258 2438 4778 3995 -1044 622 -1180 O ATOM 4813 CB ILE A 258 21.979 58.794 36.155 1.00 28.12 C ANISOU 4813 CB ILE B 258 2441 4572 3670 -923 594 -1009 C ATOM 4814 CG1 ILE A 258 20.973 59.472 35.206 1.00 28.59 C ANISOU 4814 CG1 ILE B 258 2373 4741 3747 -854 526 -1131 C ATOM 4815 CG2 ILE A 258 22.978 59.787 36.686 1.00 26.85 C ANISOU 4815 CG2 ILE B 258 2389 4370 3443 -848 533 -910 C ATOM 4816 CD1 ILE A 258 20.124 60.530 35.871 1.00 30.39 C ANISOU 4816 CD1 ILE B 258 2553 5042 3952 -797 524 -1187 C ATOM 4817 N GLU A 259 21.233 55.751 35.885 1.00 29.91 N ANISOU 4817 N GLU B 259 2581 4729 4056 -1170 811 -1090 N ATOM 4818 CA GLU A 259 19.994 55.032 35.694 1.00 31.39 C ANISOU 4818 CA GLU B 259 2638 4968 4323 -1256 899 -1228 C ATOM 4819 C GLU A 259 19.086 55.418 36.848 1.00 32.26 C ANISOU 4819 C GLU B 259 2716 5129 4411 -1277 979 -1259 C ATOM 4820 O GLU A 259 19.503 55.373 38.007 1.00 32.16 O ANISOU 4820 O GLU B 259 2805 5060 4353 -1297 1042 -1152 O ATOM 4821 CB GLU A 259 20.232 53.525 35.629 1.00 31.96 C ANISOU 4821 CB GLU B 259 2726 4936 4480 -1374 1009 -1213 C ATOM 4822 CG GLU A 259 20.931 53.117 34.346 1.00 30.94 C ANISOU 4822 CG GLU B 259 2592 4779 4383 -1359 932 -1225 C ATOM 4823 CD GLU A 259 21.342 51.659 34.304 1.00 31.73 C ANISOU 4823 CD GLU B 259 2726 4756 4576 -1466 1037 -1198 C ATOM 4824 OE1 GLU A 259 21.103 50.920 35.276 1.00 32.76 O ANISOU 4824 OE1 GLU B 259 2891 4810 4746 -1553 1177 -1156 O ATOM 4825 OE2 GLU A 259 21.910 51.248 33.276 1.00 31.66 O ANISOU 4825 OE2 GLU B 259 2708 4722 4600 -1461 984 -1218 O ATOM 4826 N THR A 260 17.872 55.844 36.522 1.00 32.91 N ANISOU 4826 N THR B 260 2658 5331 4517 -1262 969 -1408 N ATOM 4827 CA THR A 260 16.897 56.251 37.534 1.00 34.29 C ANISOU 4827 CA THR B 260 2781 5570 4677 -1281 1043 -1462 C ATOM 4828 C THR A 260 16.130 55.040 38.043 1.00 35.96 C ANISOU 4828 C THR B 260 2937 5757 4968 -1428 1215 -1522 C ATOM 4829 O THR A 260 16.257 53.948 37.503 1.00 36.29 O ANISOU 4829 O THR B 260 2963 5736 5088 -1511 1268 -1541 O ATOM 4830 CB THR A 260 15.924 57.313 36.967 1.00 34.60 C ANISOU 4830 CB THR B 260 2686 5751 4708 -1186 952 -1599 C ATOM 4831 OG1 THR A 260 15.337 56.855 35.741 1.00 33.66 O ANISOU 4831 OG1 THR B 260 2436 5702 4653 -1198 920 -1732 O ATOM 4832 CG2 THR A 260 16.684 58.576 36.560 1.00 33.54 C ANISOU 4832 CG2 THR B 260 2621 5623 4500 -1038 800 -1525 C ATOM 4833 N LYS A 261 15.353 55.233 39.100 1.00 37.71 N ANISOU 4833 N LYS B 261 3131 6023 5175 -1465 1310 -1552 N ATOM 4834 CA LYS A 261 14.485 54.172 39.618 1.00 39.84 C ANISOU 4834 CA LYS B 261 3337 6277 5525 -1610 1489 -1619 C ATOM 4835 C LYS A 261 13.236 53.987 38.748 1.00 40.90 C ANISOU 4835 C LYS B 261 3271 6518 5750 -1647 1497 -1836 C ATOM 4836 O LYS A 261 12.780 52.863 38.541 1.00 42.20 O ANISOU 4836 O LYS B 261 3370 6646 6019 -1772 1615 -1912 O ATOM 4837 CB LYS A 261 14.100 54.462 41.071 1.00 40.75 C ANISOU 4837 CB LYS B 261 3490 6412 5580 -1636 1593 -1576 C ATOM 4838 CG LYS A 261 15.269 54.351 42.038 1.00 40.97 C ANISOU 4838 CG LYS B 261 3706 6340 5520 -1623 1618 -1370 C ATOM 4839 CD LYS A 261 14.833 54.592 43.483 1.00 43.70 C ANISOU 4839 CD LYS B 261 4081 6727 5795 -1651 1729 -1336 C ATOM 4840 CE LYS A 261 15.905 54.137 44.464 1.00 44.46 C ANISOU 4840 CE LYS B 261 4355 6728 5811 -1659 1786 -1134 C ATOM 4841 NZ LYS A 261 16.171 52.673 44.319 1.00 46.41 N ANISOU 4841 NZ LYS B 261 4649 6844 6141 -1764 1907 -1062 N ATOM 4842 N GLU A 262 12.692 55.096 38.251 1.00 41.05 N ANISOU 4842 N GLU B 262 3193 6671 5735 -1536 1372 -1937 N ATOM 4843 CA GLU A 262 11.564 55.094 37.316 1.00 42.23 C ANISOU 4843 CA GLU B 262 3144 6952 5950 -1535 1343 -2147 C ATOM 4844 C GLU A 262 11.958 55.876 36.062 1.00 41.30 C ANISOU 4844 C GLU B 262 3005 6900 5788 -1388 1149 -2159 C ATOM 4845 O GLU A 262 12.854 56.721 36.104 1.00 40.15 O ANISOU 4845 O GLU B 262 2981 6716 5560 -1279 1045 -2025 O ATOM 4846 CB GLU A 262 10.327 55.740 37.949 1.00 43.64 C ANISOU 4846 CB GLU B 262 3203 7255 6124 -1526 1384 -2272 C ATOM 4847 CG GLU A 262 9.871 55.120 39.266 1.00 46.07 C ANISOU 4847 CG GLU B 262 3532 7516 6458 -1661 1579 -2258 C ATOM 4848 CD GLU A 262 8.991 53.900 39.077 1.00 50.30 C ANISOU 4848 CD GLU B 262 3939 8054 7120 -1821 1732 -2404 C ATOM 4849 OE1 GLU A 262 7.773 54.069 38.851 1.00 54.13 O ANISOU 4849 OE1 GLU B 262 4240 8674 7654 -1836 1749 -2601 O ATOM 4850 OE2 GLU A 262 9.512 52.765 39.156 1.00 52.76 O ANISOU 4850 OE2 GLU B 262 4327 8230 7490 -1932 1838 -2327 O ATOM 4851 N VAL A 263 11.280 55.605 34.950 1.00 41.81 N ANISOU 4851 N VAL B 263 2912 7069 5906 -1386 1106 -2324 N ATOM 4852 CA VAL A 263 11.608 56.252 33.679 1.00 41.03 C ANISOU 4852 CA VAL B 263 2786 7045 5758 -1246 931 -2336 C ATOM 4853 C VAL A 263 11.294 57.752 33.732 1.00 40.61 C ANISOU 4853 C VAL B 263 2716 7089 5624 -1081 813 -2331 C ATOM 4854 O VAL A 263 10.161 58.153 33.989 1.00 41.40 O ANISOU 4854 O VAL B 263 2686 7305 5740 -1063 831 -2463 O ATOM 4855 CB VAL A 263 10.866 55.605 32.493 1.00 42.13 C ANISOU 4855 CB VAL B 263 2743 7302 5962 -1277 912 -2532 C ATOM 4856 CG1 VAL A 263 11.192 56.326 31.182 1.00 41.80 C ANISOU 4856 CG1 VAL B 263 2677 7358 5849 -1118 728 -2534 C ATOM 4857 CG2 VAL A 263 11.218 54.126 32.394 1.00 42.84 C ANISOU 4857 CG2 VAL B 263 2850 7280 6147 -1441 1034 -2544 C ATOM 4858 N ALA A 264 12.314 58.563 33.478 1.00 38.94 N ANISOU 4858 N ALA B 264 2635 6823 5337 -964 699 -2182 N ATOM 4859 CA ALA A 264 12.210 60.014 33.521 1.00 38.84 C ANISOU 4859 CA ALA B 264 2635 6865 5258 -803 592 -2151 C ATOM 4860 C ALA A 264 12.184 60.566 32.098 1.00 38.93 C ANISOU 4860 C ALA B 264 2582 6976 5232 -661 442 -2186 C ATOM 4861 O ALA A 264 13.211 60.533 31.411 1.00 37.91 O ANISOU 4861 O ALA B 264 2549 6784 5069 -625 374 -2079 O ATOM 4862 CB ALA A 264 13.399 60.586 34.272 1.00 37.45 C ANISOU 4862 CB ALA B 264 2651 6551 5026 -772 580 -1961 C ATOM 4863 N PRO A 265 11.040 61.073 31.641 1.00 40.16 N ANISOU 4863 N PRO B 265 2578 7293 5389 -574 389 -2331 N ATOM 4864 CA PRO A 265 10.972 61.660 30.295 1.00 40.57 C ANISOU 4864 CA PRO B 265 2568 7456 5389 -418 242 -2354 C ATOM 4865 C PRO A 265 12.003 62.779 30.129 1.00 39.42 C ANISOU 4865 C PRO B 265 2582 7223 5173 -279 145 -2169 C ATOM 4866 O PRO A 265 12.120 63.611 31.022 1.00 39.55 O ANISOU 4866 O PRO B 265 2674 7171 5181 -240 160 -2098 O ATOM 4867 CB PRO A 265 9.535 62.202 30.214 1.00 42.07 C ANISOU 4867 CB PRO B 265 2573 7823 5588 -335 214 -2524 C ATOM 4868 CG PRO A 265 8.763 61.418 31.224 1.00 42.79 C ANISOU 4868 CG PRO B 265 2586 7915 5759 -500 364 -2642 C ATOM 4869 CD PRO A 265 9.736 61.124 32.331 1.00 41.62 C ANISOU 4869 CD PRO B 265 2622 7575 5618 -610 463 -2483 C ATOM 4870 N ILE A 266 12.730 62.793 29.016 1.00 38.89 N ANISOU 4870 N ILE B 266 2561 7157 5059 -213 55 -2100 N ATOM 4871 CA ILE A 266 13.830 63.738 28.806 1.00 37.85 C ANISOU 4871 CA ILE B 266 2588 6924 4870 -102 -20 -1918 C ATOM 4872 C ILE A 266 13.362 65.193 28.841 1.00 38.58 C ANISOU 4872 C ILE B 266 2669 7059 4932 74 -93 -1898 C ATOM 4873 O ILE A 266 14.069 66.053 29.368 1.00 38.13 O ANISOU 4873 O ILE B 266 2744 6880 4863 123 -99 -1769 O ATOM 4874 CB ILE A 266 14.588 63.452 27.472 1.00 37.24 C ANISOU 4874 CB ILE B 266 2542 6865 4744 -60 -101 -1864 C ATOM 4875 CG1 ILE A 266 15.180 62.038 27.456 1.00 36.82 C ANISOU 4875 CG1 ILE B 266 2513 6745 4731 -231 -27 -1875 C ATOM 4876 CG2 ILE A 266 15.687 64.495 27.238 1.00 36.42 C ANISOU 4876 CG2 ILE B 266 2597 6657 4586 54 -169 -1680 C ATOM 4877 CD1 ILE A 266 16.136 61.729 28.605 1.00 36.38 C ANISOU 4877 CD1 ILE B 266 2613 6502 4707 -345 63 -1753 C ATOM 4878 N GLU A 267 12.184 65.468 28.285 1.00 40.11 N ANISOU 4878 N GLU B 267 2700 7424 5117 171 -146 -2030 N ATOM 4879 CA GLU A 267 11.606 66.815 28.355 1.00 40.97 C ANISOU 4879 CA GLU B 267 2782 7576 5207 345 -208 -2023 C ATOM 4880 C GLU A 267 11.424 67.261 29.805 1.00 40.22 C ANISOU 4880 C GLU B 267 2729 7391 5163 295 -124 -2022 C ATOM 4881 O GLU A 267 11.712 68.409 30.144 1.00 39.33 O ANISOU 4881 O GLU B 267 2700 7200 5045 402 -151 -1932 O ATOM 4882 CB GLU A 267 10.271 66.906 27.590 1.00 43.08 C ANISOU 4882 CB GLU B 267 2847 8063 5460 453 -274 -2188 C ATOM 4883 CG GLU A 267 9.019 66.698 28.442 1.00 45.64 C ANISOU 4883 CG GLU B 267 3021 8474 5846 390 -202 -2364 C ATOM 4884 CD GLU A 267 7.723 66.814 27.665 1.00 49.58 C ANISOU 4884 CD GLU B 267 3309 9202 6329 505 -275 -2537 C ATOM 4885 OE1 GLU A 267 6.695 67.167 28.297 1.00 51.25 O ANISOU 4885 OE1 GLU B 267 3408 9486 6581 527 -247 -2656 O ATOM 4886 OE2 GLU A 267 7.722 66.555 26.439 1.00 52.07 O ANISOU 4886 OE2 GLU B 267 3563 9635 6587 575 -361 -2562 O ATOM 4887 N GLU A 268 10.942 66.348 30.647 1.00 40.02 N ANISOU 4887 N GLU B 268 2641 7376 5187 132 -15 -2126 N ATOM 4888 CA GLU A 268 10.715 66.640 32.062 1.00 39.95 C ANISOU 4888 CA GLU B 268 2661 7304 5216 70 76 -2137 C ATOM 4889 C GLU A 268 12.038 66.721 32.843 1.00 38.29 C ANISOU 4889 C GLU B 268 2648 6908 4994 3 121 -1972 C ATOM 4890 O GLU A 268 12.132 67.452 33.822 1.00 37.81 O ANISOU 4890 O GLU B 268 2645 6783 4940 19 153 -1939 O ATOM 4891 CB GLU A 268 9.745 65.608 32.678 1.00 40.98 C ANISOU 4891 CB GLU B 268 2659 7512 5397 -83 189 -2297 C ATOM 4892 CG GLU A 268 8.328 65.707 32.117 1.00 42.87 C ANISOU 4892 CG GLU B 268 2687 7947 5655 -10 150 -2486 C ATOM 4893 CD GLU A 268 7.385 64.609 32.602 1.00 45.06 C ANISOU 4893 CD GLU B 268 2822 8303 5995 -175 270 -2658 C ATOM 4894 OE1 GLU A 268 7.493 64.166 33.763 1.00 46.44 O ANISOU 4894 OE1 GLU B 268 3054 8391 6201 -316 397 -2640 O ATOM 4895 OE2 GLU A 268 6.514 64.188 31.818 1.00 46.85 O ANISOU 4895 OE2 GLU B 268 2877 8685 6238 -163 241 -2816 O ATOM 4896 N VAL A 269 13.061 65.993 32.395 1.00 37.19 N ANISOU 4896 N VAL B 269 2602 6691 4837 -67 118 -1878 N ATOM 4897 CA VAL A 269 14.383 66.049 33.026 1.00 35.89 C ANISOU 4897 CA VAL B 269 2616 6363 4656 -120 147 -1725 C ATOM 4898 C VAL A 269 14.991 67.433 32.785 1.00 35.38 C ANISOU 4898 C VAL B 269 2643 6232 4565 32 64 -1620 C ATOM 4899 O VAL A 269 15.527 68.046 33.703 1.00 34.60 O ANISOU 4899 O VAL B 269 2642 6037 4469 29 94 -1555 O ATOM 4900 CB VAL A 269 15.337 64.947 32.490 1.00 35.04 C ANISOU 4900 CB VAL B 269 2578 6193 4541 -217 157 -1656 C ATOM 4901 CG1 VAL A 269 16.756 65.111 33.076 1.00 33.62 C ANISOU 4901 CG1 VAL B 269 2578 5855 4339 -249 172 -1498 C ATOM 4902 CG2 VAL A 269 14.787 63.563 32.818 1.00 35.46 C ANISOU 4902 CG2 VAL B 269 2553 6283 4638 -377 260 -1753 C ATOM 4903 N LYS A 270 14.877 67.914 31.549 1.00 35.67 N ANISOU 4903 N LYS B 270 2646 6329 4579 165 -35 -1608 N ATOM 4904 CA LYS A 270 15.355 69.240 31.167 1.00 35.61 C ANISOU 4904 CA LYS B 270 2717 6257 4554 321 -109 -1506 C ATOM 4905 C LYS A 270 14.648 70.336 31.961 1.00 36.34 C ANISOU 4905 C LYS B 270 2776 6351 4680 405 -97 -1554 C ATOM 4906 O LYS A 270 15.291 71.273 32.430 1.00 35.74 O ANISOU 4906 O LYS B 270 2805 6157 4618 452 -94 -1470 O ATOM 4907 CB LYS A 270 15.132 69.479 29.667 1.00 36.24 C ANISOU 4907 CB LYS B 270 2745 6432 4593 459 -211 -1494 C ATOM 4908 CG LYS A 270 16.121 68.779 28.749 1.00 35.16 C ANISOU 4908 CG LYS B 270 2677 6267 4416 416 -240 -1411 C ATOM 4909 CD LYS A 270 15.816 69.132 27.287 1.00 36.20 C ANISOU 4909 CD LYS B 270 2750 6514 4490 571 -342 -1403 C ATOM 4910 CE LYS A 270 16.536 68.223 26.307 1.00 35.72 C ANISOU 4910 CE LYS B 270 2713 6474 4384 515 -367 -1368 C ATOM 4911 NZ LYS A 270 16.225 68.602 24.894 1.00 36.43 N ANISOU 4911 NZ LYS B 270 2745 6697 4401 675 -468 -1359 N ATOM 4912 N ALA A 271 13.328 70.217 32.106 1.00 37.25 N ANISOU 4912 N ALA B 271 2738 6601 4814 421 -85 -1699 N ATOM 4913 CA ALA A 271 12.536 71.204 32.846 1.00 38.11 C ANISOU 4913 CA ALA B 271 2794 6727 4960 502 -72 -1766 C ATOM 4914 C ALA A 271 12.905 71.236 34.328 1.00 37.51 C ANISOU 4914 C ALA B 271 2790 6554 4906 387 26 -1761 C ATOM 4915 O ALA A 271 12.965 72.305 34.928 1.00 37.92 O ANISOU 4915 O ALA B 271 2882 6542 4984 459 30 -1747 O ATOM 4916 CB ALA A 271 11.040 70.930 32.680 1.00 39.48 C ANISOU 4916 CB ALA B 271 2773 7080 5148 528 -75 -1939 C ATOM 4917 N ALA A 272 13.155 70.062 34.903 1.00 36.90 N ANISOU 4917 N ALA B 272 2730 6471 4820 214 106 -1773 N ATOM 4918 CA ALA A 272 13.505 69.928 36.319 1.00 36.44 C ANISOU 4918 CA ALA B 272 2738 6343 4763 99 202 -1764 C ATOM 4919 C ALA A 272 14.855 70.554 36.620 1.00 35.31 C ANISOU 4919 C ALA B 272 2759 6052 4605 116 186 -1628 C ATOM 4920 O ALA A 272 15.022 71.228 37.628 1.00 35.11 O ANISOU 4920 O ALA B 272 2775 5978 4586 117 224 -1633 O ATOM 4921 CB ALA A 272 13.520 68.469 36.719 1.00 36.30 C ANISOU 4921 CB ALA B 272 2712 6346 4736 -77 291 -1785 C ATOM 4922 N ILE A 273 15.823 70.322 35.737 1.00 34.77 N ANISOU 4922 N ILE B 273 2775 5919 4516 126 133 -1519 N ATOM 4923 CA ILE A 273 17.158 70.881 35.901 1.00 33.93 C ANISOU 4923 CA ILE B 273 2817 5675 4400 139 117 -1396 C ATOM 4924 C ILE A 273 17.107 72.401 35.732 1.00 34.44 C ANISOU 4924 C ILE B 273 2897 5689 4499 292 68 -1382 C ATOM 4925 O ILE A 273 17.745 73.131 36.485 1.00 34.42 O ANISOU 4925 O ILE B 273 2974 5592 4513 294 91 -1352 O ATOM 4926 CB ILE A 273 18.164 70.215 34.915 1.00 33.19 C ANISOU 4926 CB ILE B 273 2798 5533 4279 111 75 -1291 C ATOM 4927 CG1 ILE A 273 18.418 68.756 35.330 1.00 32.38 C ANISOU 4927 CG1 ILE B 273 2705 5440 4156 -50 141 -1293 C ATOM 4928 CG2 ILE A 273 19.477 70.993 34.873 1.00 32.52 C ANISOU 4928 CG2 ILE B 273 2851 5313 4194 150 47 -1174 C ATOM 4929 CD1 ILE A 273 19.089 67.894 34.269 1.00 31.78 C ANISOU 4929 CD1 ILE B 273 2662 5350 4064 -84 106 -1230 C ATOM 4930 N ALA A 274 16.314 72.872 34.773 1.00 35.20 N ANISOU 4930 N ALA B 274 2913 5853 4609 423 4 -1412 N ATOM 4931 CA ALA A 274 16.197 74.305 34.499 1.00 35.70 C ANISOU 4931 CA ALA B 274 2990 5861 4712 586 -40 -1387 C ATOM 4932 C ALA A 274 15.628 75.075 35.691 1.00 36.23 C ANISOU 4932 C ALA B 274 3021 5919 4826 601 12 -1479 C ATOM 4933 O ALA A 274 16.037 76.206 35.948 1.00 36.43 O ANISOU 4933 O ALA B 274 3110 5836 4897 677 11 -1444 O ATOM 4934 CB ALA A 274 15.342 74.539 33.264 1.00 36.71 C ANISOU 4934 CB ALA B 274 3026 6091 4832 732 -119 -1404 C ATOM 4935 N ALA A 275 14.695 74.454 36.415 1.00 36.21 N ANISOU 4935 N ALA B 275 2913 6027 4817 522 64 -1601 N ATOM 4936 CA ALA A 275 14.072 75.069 37.582 1.00 36.99 C ANISOU 4936 CA ALA B 275 2963 6141 4951 524 120 -1704 C ATOM 4937 C ALA A 275 14.904 74.935 38.869 1.00 36.06 C ANISOU 4937 C ALA B 275 2935 5950 4815 398 196 -1689 C ATOM 4938 O ALA A 275 14.645 75.639 39.840 1.00 36.60 O ANISOU 4938 O ALA B 275 2987 6009 4910 409 239 -1761 O ATOM 4939 CB ALA A 275 12.667 74.485 37.804 1.00 37.72 C ANISOU 4939 CB ALA B 275 2895 6394 5043 495 151 -1849 C ATOM 4940 N PHE A 276 15.883 74.033 38.884 1.00 34.95 N ANISOU 4940 N PHE B 276 2884 5769 4625 284 212 -1602 N ATOM 4941 CA PHE A 276 16.640 73.750 40.104 1.00 34.26 C ANISOU 4941 CA PHE B 276 2874 5641 4502 166 281 -1587 C ATOM 4942 C PHE A 276 17.626 74.872 40.416 1.00 33.75 C ANISOU 4942 C PHE B 276 2907 5451 4465 219 265 -1541 C ATOM 4943 O PHE A 276 18.422 75.252 39.550 1.00 33.05 O ANISOU 4943 O PHE B 276 2892 5268 4396 277 210 -1446 O ATOM 4944 CB PHE A 276 17.384 72.429 39.977 1.00 33.51 C ANISOU 4944 CB PHE B 276 2842 5539 4351 43 299 -1505 C ATOM 4945 CG PHE A 276 17.869 71.872 41.286 1.00 33.82 C ANISOU 4945 CG PHE B 276 2933 5580 4336 -80 379 -1500 C ATOM 4946 CD1 PHE A 276 16.984 71.246 42.156 1.00 35.35 C ANISOU 4946 CD1 PHE B 276 3053 5873 4504 -161 462 -1582 C ATOM 4947 CD2 PHE A 276 19.210 71.956 41.636 1.00 33.45 C ANISOU 4947 CD2 PHE B 276 3006 5445 4260 -111 373 -1413 C ATOM 4948 CE1 PHE A 276 17.428 70.717 43.362 1.00 35.89 C ANISOU 4948 CE1 PHE B 276 3176 5952 4508 -264 539 -1563 C ATOM 4949 CE2 PHE A 276 19.663 71.434 42.839 1.00 33.89 C ANISOU 4949 CE2 PHE B 276 3108 5519 4251 -209 439 -1404 C ATOM 4950 CZ PHE A 276 18.771 70.811 43.704 1.00 34.68 C ANISOU 4950 CZ PHE B 276 3143 5719 4316 -282 523 -1472 C ATOM 4951 N PRO A 277 17.593 75.391 41.647 1.00 33.81 N ANISOU 4951 N PRO B 277 2912 5460 4474 194 320 -1614 N ATOM 4952 CA PRO A 277 18.514 76.464 42.054 1.00 33.57 C ANISOU 4952 CA PRO B 277 2962 5316 4479 231 316 -1599 C ATOM 4953 C PRO A 277 19.963 76.067 41.830 1.00 31.84 C ANISOU 4953 C PRO B 277 2861 5010 4225 171 298 -1482 C ATOM 4954 O PRO A 277 20.328 74.941 42.152 1.00 31.34 O ANISOU 4954 O PRO B 277 2827 4994 4089 63 322 -1444 O ATOM 4955 CB PRO A 277 18.259 76.620 43.565 1.00 34.24 C ANISOU 4955 CB PRO B 277 3014 5460 4535 169 391 -1707 C ATOM 4956 CG PRO A 277 16.971 75.962 43.848 1.00 34.91 C ANISOU 4956 CG PRO B 277 2989 5681 4594 135 432 -1789 C ATOM 4957 CD PRO A 277 16.712 74.971 42.749 1.00 34.63 C ANISOU 4957 CD PRO B 277 2936 5679 4545 121 397 -1723 C ATOM 4958 N GLY A 278 20.765 76.968 41.272 1.00 31.40 N ANISOU 4958 N GLY B 278 2875 4830 4227 241 260 -1426 N ATOM 4959 CA GLY A 278 22.188 76.729 41.088 1.00 30.23 C ANISOU 4959 CA GLY B 278 2833 4597 4055 188 245 -1330 C ATOM 4960 C GLY A 278 22.568 76.026 39.796 1.00 29.38 C ANISOU 4960 C GLY B 278 2764 4470 3931 192 194 -1215 C ATOM 4961 O GLY A 278 23.755 75.911 39.476 1.00 27.90 O ANISOU 4961 O GLY B 278 2663 4204 3735 161 176 -1133 O ATOM 4962 N ALA A 279 21.566 75.559 39.056 1.00 29.75 N ANISOU 4962 N ALA B 279 2738 4594 3970 229 169 -1220 N ATOM 4963 CA ALA A 279 21.778 74.872 37.787 1.00 29.56 C ANISOU 4963 CA ALA B 279 2732 4575 3925 238 119 -1131 C ATOM 4964 C ALA A 279 21.200 75.697 36.639 1.00 30.36 C ANISOU 4964 C ALA B 279 2801 4661 4074 386 66 -1110 C ATOM 4965 O ALA A 279 20.148 76.313 36.777 1.00 31.22 O ANISOU 4965 O ALA B 279 2830 4813 4218 468 66 -1187 O ATOM 4966 CB ALA A 279 21.134 73.498 37.825 1.00 29.35 C ANISOU 4966 CB ALA B 279 2642 4667 3844 151 138 -1160 C ATOM 4967 N VAL A 280 21.905 75.708 35.511 1.00 30.36 N ANISOU 4967 N VAL B 280 2863 4603 4070 425 20 -1004 N ATOM 4968 CA VAL A 280 21.426 76.352 34.292 1.00 31.07 C ANISOU 4968 CA VAL B 280 2931 4691 4181 571 -34 -960 C ATOM 4969 C VAL A 280 21.437 75.320 33.169 1.00 30.94 C ANISOU 4969 C VAL B 280 2898 4755 4102 555 -81 -909 C ATOM 4970 O VAL A 280 22.475 74.740 32.859 1.00 30.59 O ANISOU 4970 O VAL B 280 2929 4667 4029 482 -84 -835 O ATOM 4971 CB VAL A 280 22.297 77.573 33.911 1.00 31.15 C ANISOU 4971 CB VAL B 280 3040 4544 4251 654 -36 -872 C ATOM 4972 CG1 VAL A 280 21.938 78.098 32.522 1.00 31.91 C ANISOU 4972 CG1 VAL B 280 3133 4642 4350 807 -91 -792 C ATOM 4973 CG2 VAL A 280 22.142 78.688 34.953 1.00 31.64 C ANISOU 4973 CG2 VAL B 280 3101 4529 4392 683 12 -945 C ATOM 4974 N LEU A 281 20.265 75.074 32.597 1.00 31.90 N ANISOU 4974 N LEU B 281 2912 5003 4204 622 -117 -963 N ATOM 4975 CA LEU A 281 20.118 74.264 31.401 1.00 32.10 C ANISOU 4975 CA LEU B 281 2901 5122 4174 634 -169 -934 C ATOM 4976 C LEU A 281 20.671 75.029 30.197 1.00 32.43 C ANISOU 4976 C LEU B 281 3013 5102 4209 761 -221 -812 C ATOM 4977 O LEU A 281 20.127 76.055 29.802 1.00 32.97 O ANISOU 4977 O LEU B 281 3062 5163 4301 913 -248 -795 O ATOM 4978 CB LEU A 281 18.633 73.907 31.168 1.00 32.98 C ANISOU 4978 CB LEU B 281 2860 5400 4271 681 -193 -1048 C ATOM 4979 CG LEU A 281 18.340 72.916 30.030 1.00 33.11 C ANISOU 4979 CG LEU B 281 2808 5543 4228 676 -243 -1060 C ATOM 4980 CD1 LEU A 281 18.836 71.514 30.383 1.00 32.56 C ANISOU 4980 CD1 LEU B 281 2752 5480 4141 494 -197 -1081 C ATOM 4981 CD2 LEU A 281 16.863 72.886 29.672 1.00 33.65 C ANISOU 4981 CD2 LEU B 281 2718 5778 4289 761 -279 -1178 C ATOM 4982 N GLU A 282 21.772 74.523 29.648 1.00 31.96 N ANISOU 4982 N GLU B 282 3035 4993 4115 700 -227 -724 N ATOM 4983 CA GLU A 282 22.345 75.005 28.400 1.00 32.54 C ANISOU 4983 CA GLU B 282 3173 5027 4163 800 -269 -604 C ATOM 4984 C GLU A 282 22.306 73.819 27.448 1.00 31.99 C ANISOU 4984 C GLU B 282 3057 5082 4017 760 -311 -609 C ATOM 4985 O GLU A 282 23.272 73.070 27.326 1.00 30.84 O ANISOU 4985 O GLU B 282 2969 4899 3851 654 -298 -570 O ATOM 4986 CB GLU A 282 23.786 75.478 28.620 1.00 32.22 C ANISOU 4986 CB GLU B 282 3270 4815 4157 751 -230 -508 C ATOM 4987 CG GLU A 282 23.899 76.879 29.202 1.00 34.55 C ANISOU 4987 CG GLU B 282 3617 4974 4536 823 -193 -489 C ATOM 4988 CD GLU A 282 25.300 77.461 29.086 1.00 36.72 C ANISOU 4988 CD GLU B 282 4020 5084 4848 798 -158 -389 C ATOM 4989 OE1 GLU A 282 25.431 78.704 29.039 1.00 39.92 O ANISOU 4989 OE1 GLU B 282 4476 5370 5322 892 -132 -342 O ATOM 4990 OE2 GLU A 282 26.274 76.681 29.051 1.00 37.74 O ANISOU 4990 OE2 GLU B 282 4196 5198 4946 684 -151 -363 O ATOM 4991 N ASP A 283 21.164 73.636 26.799 1.00 32.77 N ANISOU 4991 N ASP B 283 3040 5334 4076 846 -362 -671 N ATOM 4992 CA ASP A 283 20.893 72.429 26.034 1.00 32.62 C ANISOU 4992 CA ASP B 283 2942 5459 3995 797 -396 -723 C ATOM 4993 C ASP A 283 19.977 72.759 24.868 1.00 34.11 C ANISOU 4993 C ASP B 283 3041 5796 4124 963 -473 -733 C ATOM 4994 O ASP A 283 18.750 72.791 25.002 1.00 34.73 O ANISOU 4994 O ASP B 283 2995 5995 4206 1020 -494 -841 O ATOM 4995 CB ASP A 283 20.267 71.368 26.944 1.00 32.32 C ANISOU 4995 CB ASP B 283 2812 5486 3980 657 -353 -860 C ATOM 4996 CG ASP A 283 20.448 69.953 26.422 1.00 31.28 C ANISOU 4996 CG ASP B 283 2639 5433 3813 544 -355 -904 C ATOM 4997 OD1 ASP A 283 20.654 69.750 25.200 1.00 30.52 O ANISOU 4997 OD1 ASP B 283 2534 5405 3659 600 -410 -869 O ATOM 4998 OD2 ASP A 283 20.385 68.970 27.187 1.00 29.41 O ANISOU 4998 OD2 ASP B 283 2375 5195 3605 399 -299 -976 O ATOM 4999 N ASP A 284 20.599 73.027 23.724 1.00 31.05 N ANISOU 4999 N ASP B 284 2881 5231 3685 1083 -444 -1003 N ATOM 5000 CA ASP A 284 19.884 73.336 22.498 1.00 32.38 C ANISOU 5000 CA ASP B 284 3033 5523 3745 1285 -523 -1066 C ATOM 5001 C ASP A 284 20.771 72.945 21.325 1.00 31.98 C ANISOU 5001 C ASP B 284 3052 5409 3689 1237 -524 -995 C ATOM 5002 O ASP A 284 21.421 73.790 20.712 1.00 32.22 O ANISOU 5002 O ASP B 284 3287 5309 3648 1321 -536 -894 O ATOM 5003 CB ASP A 284 19.536 74.824 22.454 1.00 33.62 C ANISOU 5003 CB ASP B 284 3363 5631 3782 1523 -574 -1037 C ATOM 5004 CG ASP A 284 18.727 75.201 21.237 1.00 35.37 C ANISOU 5004 CG ASP B 284 3581 5990 3866 1774 -667 -1106 C ATOM 5005 OD1 ASP A 284 18.371 74.302 20.448 1.00 36.55 O ANISOU 5005 OD1 ASP B 284 3568 6299 4020 1757 -693 -1192 O ATOM 5006 OD2 ASP A 284 18.398 76.378 20.991 1.00 37.34 O ANISOU 5006 OD2 ASP B 284 3993 6202 3991 2008 -718 -1083 O ATOM 5007 N VAL A 285 20.777 71.651 21.021 1.00 31.42 N ANISOU 5007 N VAL B 285 2818 5428 3692 1096 -501 -1054 N ATOM 5008 CA VAL A 285 21.692 71.086 20.037 1.00 31.03 C ANISOU 5008 CA VAL B 285 2809 5320 3659 1015 -490 -993 C ATOM 5009 C VAL A 285 21.425 71.537 18.596 1.00 31.97 C ANISOU 5009 C VAL B 285 2984 5506 3656 1202 -563 -1005 C ATOM 5010 O VAL A 285 22.330 71.477 17.770 1.00 31.32 O ANISOU 5010 O VAL B 285 3006 5332 3560 1163 -553 -924 O ATOM 5011 CB VAL A 285 21.733 69.534 20.107 1.00 30.70 C ANISOU 5011 CB VAL B 285 2589 5350 3726 819 -440 -1060 C ATOM 5012 CG1 VAL A 285 22.271 69.077 21.466 1.00 29.70 C ANISOU 5012 CG1 VAL B 285 2464 5116 3706 637 -363 -1014 C ATOM 5013 CG2 VAL A 285 20.362 68.911 19.799 1.00 31.59 C ANISOU 5013 CG2 VAL B 285 2485 5700 3817 866 -466 -1239 C ATOM 5014 N ALA A 286 20.201 71.985 18.307 1.00 33.62 N ANISOU 5014 N ALA B 286 3124 5882 3766 1409 -635 -1112 N ATOM 5015 CA ALA A 286 19.864 72.599 17.011 1.00 34.96 C ANISOU 5015 CA ALA B 286 3376 6118 3787 1641 -717 -1121 C ATOM 5016 C ALA A 286 20.676 73.877 16.767 1.00 35.28 C ANISOU 5016 C ALA B 286 3728 5937 3739 1741 -712 -963 C ATOM 5017 O ALA A 286 20.899 74.261 15.624 1.00 35.88 O ANISOU 5017 O ALA B 286 3938 5987 3706 1863 -746 -918 O ATOM 5018 CB ALA A 286 18.368 72.914 16.937 1.00 36.79 C ANISOU 5018 CB ALA B 286 3472 6586 3922 1869 -801 -1278 C ATOM 5019 N HIS A 287 21.095 74.534 17.850 1.00 35.02 N ANISOU 5019 N HIS B 287 3816 5744 3746 1683 -661 -886 N ATOM 5020 CA HIS A 287 21.978 75.701 17.779 1.00 35.42 C ANISOU 5020 CA HIS B 287 4168 5562 3730 1720 -625 -744 C ATOM 5021 C HIS A 287 23.353 75.448 18.437 1.00 33.44 C ANISOU 5021 C HIS B 287 3978 5129 3599 1452 -527 -647 C ATOM 5022 O HIS A 287 24.053 76.385 18.814 1.00 33.31 O ANISOU 5022 O HIS B 287 4172 4927 3556 1429 -475 -555 O ATOM 5023 CB HIS A 287 21.264 76.912 18.396 1.00 36.81 C ANISOU 5023 CB HIS B 287 4464 5705 3816 1921 -654 -751 C ATOM 5024 CG HIS A 287 19.987 77.272 17.692 1.00 39.98 C ANISOU 5024 CG HIS B 287 4826 6289 4075 2222 -760 -849 C ATOM 5025 ND1 HIS A 287 19.946 78.143 16.624 1.00 43.30 N ANISOU 5025 ND1 HIS B 287 5476 6651 4323 2453 -804 -796 N ATOM 5026 CD2 HIS A 287 18.712 76.853 17.882 1.00 41.77 C ANISOU 5026 CD2 HIS B 287 4808 6767 4295 2333 -830 -1009 C ATOM 5027 CE1 HIS A 287 18.698 78.258 16.197 1.00 45.38 C ANISOU 5027 CE1 HIS B 287 5635 7132 4477 2718 -909 -916 C ATOM 5028 NE2 HIS A 287 17.930 77.483 16.941 1.00 43.92 N ANISOU 5028 NE2 HIS B 287 5148 7146 4391 2643 -926 -1056 N ATOM 5029 N GLN A 288 23.736 74.176 18.543 1.00 32.12 N ANISOU 5029 N GLN B 288 3628 5022 3553 1256 -500 -676 N ATOM 5030 CA GLN A 288 25.001 73.759 19.169 1.00 30.38 C ANISOU 5030 CA GLN B 288 3428 4672 3444 1020 -420 -605 C ATOM 5031 C GLN A 288 25.254 74.413 20.528 1.00 29.86 C ANISOU 5031 C GLN B 288 3433 4497 3416 965 -375 -567 C ATOM 5032 O GLN A 288 26.339 74.940 20.781 1.00 29.27 O ANISOU 5032 O GLN B 288 3509 4266 3347 867 -317 -487 O ATOM 5033 CB GLN A 288 26.174 74.064 18.251 1.00 30.25 C ANISOU 5033 CB GLN B 288 3584 4525 3384 967 -384 -516 C ATOM 5034 CG GLN A 288 26.142 73.357 16.925 1.00 30.60 C ANISOU 5034 CG GLN B 288 3565 4663 3400 990 -418 -544 C ATOM 5035 CD GLN A 288 27.229 73.866 16.019 1.00 31.23 C ANISOU 5035 CD GLN B 288 3845 4608 3413 954 -376 -457 C ATOM 5036 OE1 GLN A 288 28.398 73.461 16.143 1.00 31.50 O ANISOU 5036 OE1 GLN B 288 3881 4567 3520 765 -315 -420 O ATOM 5037 NE2 GLN A 288 26.870 74.776 15.130 1.00 29.01 N ANISOU 5037 NE2 GLN B 288 3741 4297 2984 1137 -404 -430 N ATOM 5038 N ILE A 289 24.241 74.377 21.385 1.00 30.07 N ANISOU 5038 N ILE B 289 3344 4619 3463 1022 -399 -639 N ATOM 5039 CA ILE A 289 24.332 74.913 22.733 1.00 29.69 C ANISOU 5039 CA ILE B 289 3336 4492 3451 975 -361 -619 C ATOM 5040 C ILE A 289 24.505 73.744 23.699 1.00 28.44 C ANISOU 5040 C ILE B 289 3003 4383 3421 789 -323 -650 C ATOM 5041 O ILE A 289 23.654 72.851 23.785 1.00 28.67 O ANISOU 5041 O ILE B 289 2849 4558 3487 780 -340 -741 O ATOM 5042 CB ILE A 289 23.078 75.724 23.105 1.00 30.97 C ANISOU 5042 CB ILE B 289 3501 4725 3540 1174 -409 -682 C ATOM 5043 CG1 ILE A 289 22.827 76.858 22.097 1.00 32.99 C ANISOU 5043 CG1 ILE B 289 3956 4931 3647 1398 -452 -651 C ATOM 5044 CG2 ILE A 289 23.202 76.299 24.520 1.00 31.01 C ANISOU 5044 CG2 ILE B 289 3554 4646 3585 1119 -365 -662 C ATOM 5045 CD1 ILE A 289 23.906 77.948 22.080 1.00 33.34 C ANISOU 5045 CD1 ILE B 289 4283 4742 3642 1367 -390 -533 C ATOM 5046 N TYR A 290 25.635 73.763 24.393 1.00 27.13 N ANISOU 5046 N TYR B 290 2904 4093 3310 641 -267 -581 N ATOM 5047 CA TYR A 290 25.962 72.825 25.462 1.00 25.99 C ANISOU 5047 CA TYR B 290 2646 3961 3267 483 -227 -590 C ATOM 5048 C TYR A 290 26.925 73.540 26.420 1.00 25.57 C ANISOU 5048 C TYR B 290 2712 3778 3225 406 -182 -526 C ATOM 5049 O TYR A 290 27.567 74.515 26.029 1.00 26.08 O ANISOU 5049 O TYR B 290 2936 3738 3234 427 -167 -475 O ATOM 5050 CB TYR A 290 26.614 71.562 24.892 1.00 25.35 C ANISOU 5050 CB TYR B 290 2483 3903 3245 366 -214 -585 C ATOM 5051 CG TYR A 290 27.392 71.778 23.608 1.00 25.00 C ANISOU 5051 CG TYR B 290 2530 3809 3158 378 -223 -540 C ATOM 5052 CD1 TYR A 290 28.673 72.331 23.628 1.00 24.72 C ANISOU 5052 CD1 TYR B 290 2625 3652 3113 302 -185 -471 C ATOM 5053 CD2 TYR A 290 26.853 71.421 22.376 1.00 25.11 C ANISOU 5053 CD2 TYR B 290 2496 3910 3136 455 -263 -579 C ATOM 5054 CE1 TYR A 290 29.390 72.526 22.452 1.00 24.79 C ANISOU 5054 CE1 TYR B 290 2723 3619 3079 296 -180 -439 C ATOM 5055 CE2 TYR A 290 27.557 71.616 21.200 1.00 24.83 C ANISOU 5055 CE2 TYR B 290 2552 3829 3054 463 -267 -537 C ATOM 5056 CZ TYR A 290 28.824 72.167 21.242 1.00 25.17 C ANISOU 5056 CZ TYR B 290 2733 3742 3089 380 -222 -465 C ATOM 5057 OH TYR A 290 29.523 72.355 20.076 1.00 25.47 O ANISOU 5057 OH TYR B 290 2864 3737 3075 372 -213 -432 O ATOM 5058 N PRO A 291 27.033 73.079 27.664 1.00 24.80 N ANISOU 5058 N PRO B 291 2545 3688 3190 312 -153 -534 N ATOM 5059 CA PRO A 291 28.036 73.629 28.581 1.00 24.29 C ANISOU 5059 CA PRO B 291 2569 3523 3135 228 -112 -487 C ATOM 5060 C PRO A 291 29.467 73.524 28.033 1.00 23.65 C ANISOU 5060 C PRO B 291 2550 3377 3061 130 -88 -442 C ATOM 5061 O PRO A 291 29.823 72.524 27.403 1.00 23.46 O ANISOU 5061 O PRO B 291 2453 3392 3070 83 -96 -443 O ATOM 5062 CB PRO A 291 27.879 72.758 29.834 1.00 23.80 C ANISOU 5062 CB PRO B 291 2397 3509 3137 148 -93 -509 C ATOM 5063 CG PRO A 291 26.488 72.274 29.785 1.00 24.51 C ANISOU 5063 CG PRO B 291 2375 3706 3231 211 -112 -576 C ATOM 5064 CD PRO A 291 26.211 72.043 28.316 1.00 24.64 C ANISOU 5064 CD PRO B 291 2370 3769 3222 275 -148 -595 C ATOM 5065 N GLN A 292 30.254 74.567 28.268 1.00 23.34 N ANISOU 5065 N GLN B 292 2641 3242 2986 97 -53 -415 N ATOM 5066 CA GLN A 292 31.664 74.613 27.922 1.00 23.21 C ANISOU 5066 CA GLN B 292 2676 3174 2967 -15 -16 -395 C ATOM 5067 C GLN A 292 32.457 75.213 29.074 1.00 23.22 C ANISOU 5067 C GLN B 292 2721 3132 2971 -104 28 -402 C ATOM 5068 O GLN A 292 32.037 76.193 29.695 1.00 23.70 O ANISOU 5068 O GLN B 292 2864 3140 3000 -65 46 -405 O ATOM 5069 CB GLN A 292 31.894 75.478 26.688 1.00 23.92 C ANISOU 5069 CB GLN B 292 2918 3187 2982 19 3 -373 C ATOM 5070 CG GLN A 292 31.374 74.888 25.404 1.00 23.51 C ANISOU 5070 CG GLN B 292 2829 3187 2916 95 -39 -370 C ATOM 5071 CD GLN A 292 31.540 75.840 24.247 1.00 24.66 C ANISOU 5071 CD GLN B 292 3157 3246 2967 147 -17 -341 C ATOM 5072 OE1 GLN A 292 32.599 76.472 24.104 1.00 23.42 O ANISOU 5072 OE1 GLN B 292 3122 2998 2778 46 49 -326 O ATOM 5073 NE2 GLN A 292 30.497 75.967 23.419 1.00 24.49 N ANISOU 5073 NE2 GLN B 292 3160 3256 2889 304 -67 -340 N ATOM 5074 N ALA A 293 33.621 74.634 29.324 1.00 23.14 N ANISOU 5074 N ALA B 293 2651 3151 2992 -215 44 -414 N ATOM 5075 CA ALA A 293 34.531 75.081 30.365 1.00 23.29 C ANISOU 5075 CA ALA B 293 2682 3161 3007 -307 82 -440 C ATOM 5076 C ALA A 293 34.793 76.580 30.288 1.00 24.70 C ANISOU 5076 C ALA B 293 3026 3237 3124 -338 144 -450 C ATOM 5077 O ALA A 293 34.683 77.285 31.297 1.00 24.62 O ANISOU 5077 O ALA B 293 3055 3198 3102 -348 168 -467 O ATOM 5078 CB ALA A 293 35.844 74.304 30.258 1.00 22.89 C ANISOU 5078 CB ALA B 293 2548 3172 2977 -402 85 -468 C ATOM 5079 N ILE A 294 35.135 77.068 29.093 1.00 25.96 N ANISOU 5079 N ILE B 294 3297 3331 3237 -356 178 -440 N ATOM 5080 CA ILE A 294 35.532 78.469 28.931 1.00 27.78 C ANISOU 5080 CA ILE B 294 3720 3440 3396 -409 261 -451 C ATOM 5081 C ILE A 294 34.386 79.436 29.264 1.00 28.58 C ANISOU 5081 C ILE B 294 3950 3454 3456 -285 261 -424 C ATOM 5082 O ILE A 294 34.625 80.537 29.770 1.00 29.49 O ANISOU 5082 O ILE B 294 4201 3475 3528 -331 329 -444 O ATOM 5083 CB ILE A 294 36.118 78.749 27.512 1.00 28.53 C ANISOU 5083 CB ILE B 294 3933 3473 3436 -456 310 -441 C ATOM 5084 CG1 ILE A 294 35.097 78.465 26.409 1.00 29.82 C ANISOU 5084 CG1 ILE B 294 4127 3627 3576 -303 252 -385 C ATOM 5085 CG2 ILE A 294 37.388 77.936 27.287 1.00 29.07 C ANISOU 5085 CG2 ILE B 294 3873 3634 3538 -593 322 -489 C ATOM 5086 CD1 ILE A 294 35.602 78.795 25.007 1.00 31.48 C ANISOU 5086 CD1 ILE B 294 4475 3769 3717 -336 301 -368 C ATOM 5087 N ASN A 295 33.155 79.006 28.994 1.00 28.43 N ANISOU 5087 N ASN B 295 3880 3476 3447 -130 187 -393 N ATOM 5088 CA ASN A 295 31.957 79.790 29.304 1.00 29.27 C ANISOU 5088 CA ASN B 295 4073 3534 3513 19 169 -383 C ATOM 5089 C ASN A 295 31.556 79.776 30.786 1.00 29.04 C ANISOU 5089 C ASN B 295 3954 3551 3528 17 156 -411 C ATOM 5090 O ASN A 295 30.897 80.701 31.264 1.00 29.85 O ANISOU 5090 O ASN B 295 4157 3594 3592 100 167 -417 O ATOM 5091 CB ASN A 295 30.772 79.294 28.461 1.00 29.33 C ANISOU 5091 CB ASN B 295 4030 3606 3508 187 91 -366 C ATOM 5092 CG ASN A 295 30.914 79.636 26.987 1.00 30.42 C ANISOU 5092 CG ASN B 295 4309 3678 3569 239 101 -333 C ATOM 5093 OD1 ASN A 295 31.647 80.553 26.621 1.00 31.63 O ANISOU 5093 OD1 ASN B 295 4658 3701 3659 179 178 -315 O ATOM 5094 ND2 ASN A 295 30.209 78.896 26.131 1.00 30.74 N ANISOU 5094 ND2 ASN B 295 4259 3811 3611 343 32 -331 N ATOM 5095 N ALA A 296 31.936 78.724 31.502 1.00 28.02 N ANISOU 5095 N ALA B 296 3647 3526 3471 -66 134 -429 N ATOM 5096 CA ALA A 296 31.571 78.572 32.906 1.00 27.76 C ANISOU 5096 CA ALA B 296 3527 3546 3475 -71 123 -453 C ATOM 5097 C ALA A 296 32.512 79.317 33.858 1.00 28.10 C ANISOU 5097 C ALA B 296 3627 3545 3505 -186 184 -484 C ATOM 5098 O ALA A 296 32.163 79.547 35.020 1.00 28.51 O ANISOU 5098 O ALA B 296 3651 3615 3566 -178 185 -505 O ATOM 5099 CB ALA A 296 31.519 77.101 33.266 1.00 26.77 C ANISOU 5099 CB ALA B 296 3217 3539 3416 -96 79 -454 C ATOM 5100 N VAL A 297 33.696 79.696 33.377 1.00 28.30 N ANISOU 5100 N VAL B 297 3724 3522 3504 -300 239 -499 N ATOM 5101 CA VAL A 297 34.671 80.396 34.211 1.00 28.73 C ANISOU 5101 CA VAL B 297 3820 3556 3542 -430 306 -554 C ATOM 5102 C VAL A 297 34.098 81.736 34.673 1.00 29.45 C ANISOU 5102 C VAL B 297 4073 3531 3585 -389 354 -563 C ATOM 5103 O VAL A 297 33.560 82.493 33.871 1.00 30.18 O ANISOU 5103 O VAL B 297 4331 3509 3626 -307 376 -531 O ATOM 5104 CB VAL A 297 36.020 80.614 33.464 1.00 29.25 C ANISOU 5104 CB VAL B 297 3935 3599 3580 -575 372 -591 C ATOM 5105 CG1 VAL A 297 36.991 81.457 34.298 1.00 30.09 C ANISOU 5105 CG1 VAL B 297 4083 3692 3657 -723 455 -675 C ATOM 5106 CG2 VAL A 297 36.644 79.279 33.114 1.00 28.45 C ANISOU 5106 CG2 VAL B 297 3664 3622 3523 -606 320 -594 C ATOM 5107 N GLY A 298 34.190 82.001 35.975 1.00 29.16 N ANISOU 5107 N GLY B 298 3994 3526 3559 -431 368 -605 N ATOM 5108 CA GLY A 298 33.715 83.249 36.556 1.00 30.11 C ANISOU 5108 CA GLY B 298 4261 3542 3638 -401 418 -624 C ATOM 5109 C GLY A 298 32.287 83.199 37.073 1.00 29.87 C ANISOU 5109 C GLY B 298 4197 3531 3620 -238 357 -598 C ATOM 5110 O GLY A 298 31.848 84.114 37.767 1.00 30.31 O ANISOU 5110 O GLY B 298 4343 3525 3648 -203 387 -621 O ATOM 5111 N SER A 299 31.561 82.134 36.738 1.00 29.13 N ANISOU 5111 N SER B 299 3971 3531 3565 -145 277 -562 N ATOM 5112 CA SER A 299 30.159 81.995 37.121 1.00 28.97 C ANISOU 5112 CA SER B 299 3896 3555 3554 1 224 -557 C ATOM 5113 C SER A 299 29.987 80.992 38.266 1.00 28.31 C ANISOU 5113 C SER B 299 3628 3601 3526 -36 190 -574 C ATOM 5114 O SER A 299 30.683 79.968 38.327 1.00 27.28 O ANISOU 5114 O SER B 299 3389 3543 3431 -118 175 -565 O ATOM 5115 CB SER A 299 29.316 81.567 35.909 1.00 28.89 C ANISOU 5115 CB SER B 299 3874 3566 3536 132 169 -525 C ATOM 5116 OG SER A 299 27.997 81.202 36.300 1.00 28.45 O ANISOU 5116 OG SER B 299 3714 3601 3496 251 116 -546 O ATOM 5117 N ARG A 300 29.038 81.299 39.151 1.00 28.53 N ANISOU 5117 N ARG B 300 3636 3653 3551 35 182 -599 N ATOM 5118 CA ARG A 300 28.659 80.434 40.271 1.00 28.37 C ANISOU 5118 CA ARG B 300 3468 3744 3567 12 161 -615 C ATOM 5119 C ARG A 300 27.782 79.245 39.880 1.00 28.00 C ANISOU 5119 C ARG B 300 3293 3791 3554 66 116 -606 C ATOM 5120 O ARG A 300 27.598 78.323 40.679 1.00 27.65 O ANISOU 5120 O ARG B 300 3141 3827 3536 24 113 -612 O ATOM 5121 CB ARG A 300 27.881 81.241 41.312 1.00 29.01 C ANISOU 5121 CB ARG B 300 3575 3819 3627 65 176 -656 C ATOM 5122 CG ARG A 300 28.655 82.349 41.975 1.00 29.65 C ANISOU 5122 CG ARG B 300 3768 3819 3677 -4 231 -682 C ATOM 5123 CD ARG A 300 27.808 83.148 42.952 1.00 31.04 C ANISOU 5123 CD ARG B 300 3974 3988 3833 61 245 -725 C ATOM 5124 NE ARG A 300 28.578 84.195 43.613 1.00 33.21 N ANISOU 5124 NE ARG B 300 4356 4183 4077 -20 306 -760 N ATOM 5125 CZ ARG A 300 28.893 85.373 43.075 1.00 35.85 C ANISOU 5125 CZ ARG B 300 4875 4377 4368 -15 358 -768 C ATOM 5126 NH1 ARG A 300 28.509 85.695 41.841 1.00 35.41 N ANISOU 5126 NH1 ARG B 300 4931 4237 4285 87 349 -734 N ATOM 5127 NH2 ARG A 300 29.601 86.245 43.784 1.00 37.82 N ANISOU 5127 NH2 ARG B 300 5210 4566 4593 -115 426 -817 N ATOM 5128 N ASP A 301 27.217 79.282 38.677 1.00 28.18 N ANISOU 5128 N ASP B 301 3337 3804 3566 157 88 -598 N ATOM 5129 CA ASP A 301 26.270 78.264 38.236 1.00 28.13 C ANISOU 5129 CA ASP B 301 3206 3897 3585 208 52 -613 C ATOM 5130 C ASP A 301 26.929 76.952 37.825 1.00 27.20 C ANISOU 5130 C ASP B 301 3008 3816 3509 117 46 -581 C ATOM 5131 O ASP A 301 28.135 76.876 37.572 1.00 26.44 O ANISOU 5131 O ASP B 301 2954 3673 3418 40 57 -545 O ATOM 5132 CB ASP A 301 25.426 78.780 37.065 1.00 28.93 C ANISOU 5132 CB ASP B 301 3350 3995 3647 356 16 -629 C ATOM 5133 CG ASP A 301 24.614 80.006 37.427 1.00 31.06 C ANISOU 5133 CG ASP B 301 3701 4236 3864 484 14 -668 C ATOM 5134 OD1 ASP A 301 23.980 80.005 38.501 1.00 32.44 O ANISOU 5134 OD1 ASP B 301 3805 4472 4049 486 22 -714 O ATOM 5135 OD2 ASP A 301 24.546 81.015 36.696 1.00 33.49 O ANISOU 5135 OD2 ASP B 301 4156 4457 4111 594 7 -656 O ATOM 5136 N THR A 302 26.094 75.920 37.766 1.00 26.75 N ANISOU 5136 N THR B 302 2834 3851 3480 126 35 -607 N ATOM 5137 CA THR A 302 26.467 74.620 37.253 1.00 26.15 C ANISOU 5137 CA THR B 302 2690 3806 3439 61 32 -586 C ATOM 5138 C THR A 302 25.677 74.413 35.974 1.00 26.27 C ANISOU 5138 C THR B 302 2663 3868 3452 139 0 -614 C ATOM 5139 O THR A 302 24.461 74.456 35.987 1.00 27.11 O ANISOU 5139 O THR B 302 2702 4052 3546 208 -9 -678 O ATOM 5140 CB THR A 302 26.127 73.554 38.284 1.00 25.97 C ANISOU 5140 CB THR B 302 2586 3841 3441 -9 63 -602 C ATOM 5141 OG1 THR A 302 26.954 73.736 39.442 1.00 27.58 O ANISOU 5141 OG1 THR B 302 2835 4010 3635 -67 84 -573 O ATOM 5142 CG2 THR A 302 26.479 72.158 37.778 1.00 25.29 C ANISOU 5142 CG2 THR B 302 2453 3770 3386 -72 70 -580 C ATOM 5143 N PHE A 303 26.375 74.216 34.866 1.00 25.94 N ANISOU 5143 N PHE B 303 2653 3792 3412 131 -17 -577 N ATOM 5144 CA PHE A 303 25.749 74.168 33.557 1.00 26.32 C ANISOU 5144 CA PHE B 303 2678 3881 3442 218 -53 -601 C ATOM 5145 C PHE A 303 25.591 72.728 33.082 1.00 25.82 C ANISOU 5145 C PHE B 303 2501 3888 3422 158 -50 -620 C ATOM 5146 O PHE A 303 26.532 71.950 33.129 1.00 24.98 O ANISOU 5146 O PHE B 303 2395 3747 3348 64 -32 -578 O ATOM 5147 CB PHE A 303 26.572 74.988 32.569 1.00 26.48 C ANISOU 5147 CB PHE B 303 2829 3809 3424 251 -65 -551 C ATOM 5148 CG PHE A 303 26.723 76.429 32.967 1.00 27.08 C ANISOU 5148 CG PHE B 303 3046 3794 3450 302 -50 -538 C ATOM 5149 CD1 PHE A 303 25.814 77.383 32.532 1.00 28.27 C ANISOU 5149 CD1 PHE B 303 3266 3938 3536 458 -76 -562 C ATOM 5150 CD2 PHE A 303 27.773 76.831 33.776 1.00 27.23 C ANISOU 5150 CD2 PHE B 303 3131 3738 3476 200 -9 -510 C ATOM 5151 CE1 PHE A 303 25.942 78.711 32.903 1.00 28.50 C ANISOU 5151 CE1 PHE B 303 3452 3863 3514 508 -53 -549 C ATOM 5152 CE2 PHE A 303 27.909 78.171 34.147 1.00 28.15 C ANISOU 5152 CE2 PHE B 303 3387 3763 3545 231 18 -508 C ATOM 5153 CZ PHE A 303 26.997 79.103 33.709 1.00 28.96 C ANISOU 5153 CZ PHE B 303 3581 3835 3588 382 0 -522 C ATOM 5154 N VAL A 304 24.385 72.386 32.638 1.00 26.60 N ANISOU 5154 N VAL B 304 2502 4092 3514 216 -65 -695 N ATOM 5155 CA VAL A 304 24.028 71.017 32.291 1.00 26.34 C ANISOU 5155 CA VAL B 304 2356 4133 3520 145 -45 -739 C ATOM 5156 C VAL A 304 23.415 70.963 30.892 1.00 27.03 C ANISOU 5156 C VAL B 304 2387 4301 3581 233 -89 -791 C ATOM 5157 O VAL A 304 22.586 71.796 30.532 1.00 27.44 O ANISOU 5157 O VAL B 304 2432 4415 3580 368 -131 -841 O ATOM 5158 CB VAL A 304 23.020 70.430 33.306 1.00 26.93 C ANISOU 5158 CB VAL B 304 2332 4289 3610 90 3 -817 C ATOM 5159 CG1 VAL A 304 22.768 68.946 33.024 1.00 26.87 C ANISOU 5159 CG1 VAL B 304 2238 4329 3641 -16 49 -861 C ATOM 5160 CG2 VAL A 304 23.525 70.628 34.726 1.00 26.95 C ANISOU 5160 CG2 VAL B 304 2399 4220 3622 28 40 -768 C ATOM 5161 N GLY A 305 23.819 69.959 30.117 1.00 26.59 N ANISOU 5161 N GLY B 305 2296 4252 3557 167 -82 -783 N ATOM 5162 CA GLY A 305 23.338 69.794 28.760 1.00 27.07 C ANISOU 5162 CA GLY B 305 2299 4394 3591 238 -123 -834 C ATOM 5163 C GLY A 305 23.657 68.428 28.192 1.00 26.88 C ANISOU 5163 C GLY B 305 2213 4385 3616 130 -94 -845 C ATOM 5164 O GLY A 305 23.965 67.485 28.925 1.00 26.47 O ANISOU 5164 O GLY B 305 2149 4295 3613 6 -35 -833 O ATOM 5165 N ARG A 306 23.593 68.333 26.870 1.00 27.39 N ANISOU 5165 N ARG B 306 2252 4498 3656 187 -134 -866 N ATOM 5166 CA ARG A 306 23.727 67.063 26.149 1.00 27.26 C ANISOU 5166 CA ARG B 306 2164 4515 3678 99 -110 -899 C ATOM 5167 C ARG A 306 22.831 65.980 26.760 1.00 27.68 C ANISOU 5167 C ARG B 306 2101 4648 3770 -7 -42 -1001 C ATOM 5168 O ARG A 306 23.159 64.804 26.711 1.00 28.03 O ANISOU 5168 O ARG B 306 2131 4659 3859 -125 12 -1004 O ATOM 5169 CB ARG A 306 25.187 66.587 26.117 1.00 26.33 C ANISOU 5169 CB ARG B 306 2137 4267 3601 13 -91 -795 C ATOM 5170 CG ARG A 306 26.156 67.462 25.305 1.00 26.04 C ANISOU 5170 CG ARG B 306 2206 4160 3526 78 -137 -714 C ATOM 5171 CD ARG A 306 25.873 67.541 23.812 1.00 24.71 C ANISOU 5171 CD ARG B 306 2013 4060 3315 157 -183 -747 C ATOM 5172 NE ARG A 306 25.349 66.295 23.249 1.00 23.70 N ANISOU 5172 NE ARG B 306 1760 4024 3219 101 -166 -830 N ATOM 5173 CZ ARG A 306 26.084 65.246 22.870 1.00 24.77 C ANISOU 5173 CZ ARG B 306 1886 4123 3403 4 -137 -813 C ATOM 5174 NH1 ARG A 306 27.419 65.245 22.954 1.00 23.68 N ANISOU 5174 NH1 ARG B 306 1838 3874 3284 -41 -130 -722 N ATOM 5175 NH2 ARG A 306 25.468 64.185 22.377 1.00 26.26 N ANISOU 5175 NH2 ARG B 306 1967 4396 3615 -47 -113 -903 N ATOM 5176 N ILE A 307 21.703 66.381 27.338 1.00 28.27 N ANISOU 5176 N ILE B 307 2100 4822 3819 31 -37 -1091 N ATOM 5177 CA ILE A 307 20.808 65.443 28.013 1.00 28.93 C ANISOU 5177 CA ILE B 307 2080 4984 3930 -90 47 -1202 C ATOM 5178 C ILE A 307 20.066 64.602 26.973 1.00 29.89 C ANISOU 5178 C ILE B 307 2063 5245 4049 -123 60 -1335 C ATOM 5179 O ILE A 307 19.468 65.134 26.035 1.00 30.47 O ANISOU 5179 O ILE B 307 2056 5449 4071 5 -12 -1408 O ATOM 5180 CB ILE A 307 19.799 66.177 28.925 1.00 29.51 C ANISOU 5180 CB ILE B 307 2097 5145 3972 -40 50 -1277 C ATOM 5181 CG1 ILE A 307 20.523 66.936 30.040 1.00 28.35 C ANISOU 5181 CG1 ILE B 307 2083 4860 3829 -25 48 -1156 C ATOM 5182 CG2 ILE A 307 18.804 65.181 29.534 1.00 30.89 C ANISOU 5182 CG2 ILE B 307 2154 5416 4166 -186 152 -1416 C ATOM 5183 CD1 ILE A 307 19.646 67.982 30.745 1.00 28.80 C ANISOU 5183 CD1 ILE B 307 2105 4994 3842 72 26 -1215 C ATOM 5184 N ARG A 308 20.121 63.289 27.148 1.00 30.27 N ANISOU 5184 N ARG B 308 2096 5260 4145 -291 155 -1368 N ATOM 5185 CA ARG A 308 19.504 62.348 26.218 1.00 31.10 C ANISOU 5185 CA ARG B 308 2078 5483 4255 -360 189 -1502 C ATOM 5186 C ARG A 308 19.432 60.943 26.819 1.00 31.37 C ANISOU 5186 C ARG B 308 2131 5452 4336 -569 329 -1544 C ATOM 5187 O ARG A 308 20.232 60.578 27.683 1.00 30.05 O ANISOU 5187 O ARG B 308 2105 5114 4197 -637 379 -1428 O ATOM 5188 CB ARG A 308 20.277 62.317 24.893 1.00 30.53 C ANISOU 5188 CB ARG B 308 2035 5383 4180 -291 118 -1441 C ATOM 5189 CG ARG A 308 21.680 61.770 24.999 1.00 29.94 C ANISOU 5189 CG ARG B 308 2108 5114 4153 -357 141 -1292 C ATOM 5190 CD ARG A 308 22.705 62.503 24.143 1.00 29.37 C ANISOU 5190 CD ARG B 308 2115 4982 4061 -239 47 -1177 C ATOM 5191 NE ARG A 308 23.952 61.757 24.085 1.00 28.35 N ANISOU 5191 NE ARG B 308 2085 4711 3977 -313 74 -1079 N ATOM 5192 CZ ARG A 308 24.975 61.901 24.924 1.00 26.86 C ANISOU 5192 CZ ARG B 308 2015 4384 3805 -327 81 -961 C ATOM 5193 NH1 ARG A 308 24.958 62.805 25.900 1.00 25.60 N ANISOU 5193 NH1 ARG B 308 1902 4197 3628 -284 67 -915 N ATOM 5194 NH2 ARG A 308 26.041 61.136 24.762 1.00 25.79 N ANISOU 5194 NH2 ARG B 308 1947 4150 3700 -377 100 -897 N ATOM 5195 N LYS A 309 18.466 60.164 26.347 1.00 32.49 N ANISOU 5195 N LYS B 309 2135 5733 4475 -667 394 -1719 N ATOM 5196 CA LYS A 309 18.268 58.800 26.799 1.00 33.67 C ANISOU 5196 CA LYS B 309 2312 5822 4658 -881 548 -1784 C ATOM 5197 C LYS A 309 19.382 57.902 26.286 1.00 32.72 C ANISOU 5197 C LYS B 309 2319 5536 4577 -931 569 -1679 C ATOM 5198 O LYS A 309 19.945 58.153 25.217 1.00 32.27 O ANISOU 5198 O LYS B 309 2248 5492 4520 -829 474 -1632 O ATOM 5199 CB LYS A 309 16.911 58.284 26.298 1.00 35.90 C ANISOU 5199 CB LYS B 309 2396 6323 4922 -978 614 -2028 C ATOM 5200 CG LYS A 309 16.422 56.994 26.955 1.00 38.94 C ANISOU 5200 CG LYS B 309 2807 6662 5327 -1229 805 -2134 C ATOM 5201 CD LYS A 309 14.878 56.889 26.955 1.00 42.77 C ANISOU 5201 CD LYS B 309 3073 7400 5779 -1326 878 -2400 C ATOM 5202 CE LYS A 309 14.345 56.183 25.720 1.00 45.14 C ANISOU 5202 CE LYS B 309 3218 7859 6075 -1397 903 -2581 C ATOM 5203 NZ LYS A 309 15.144 56.465 24.498 1.00 45.12 N ANISOU 5203 NZ LYS B 309 3228 7839 6078 -1234 763 -2478 N ATOM 5204 N ASP A 310 19.716 56.879 27.073 1.00 32.65 N ANISOU 5204 N ASP B 310 2445 5368 4591 -1077 693 -1639 N ATOM 5205 CA ASP A 310 20.609 55.807 26.645 1.00 32.18 C ANISOU 5205 CA ASP B 310 2507 5158 4563 -1138 739 -1572 C ATOM 5206 C ASP A 310 19.899 55.097 25.507 1.00 33.10 C ANISOU 5206 C ASP B 310 2488 5403 4686 -1226 783 -1742 C ATOM 5207 O ASP A 310 18.677 55.043 25.485 1.00 34.25 O ANISOU 5207 O ASP B 310 2486 5714 4813 -1307 840 -1922 O ATOM 5208 CB ASP A 310 20.886 54.833 27.798 1.00 32.54 C ANISOU 5208 CB ASP B 310 2738 5015 4610 -1269 879 -1519 C ATOM 5209 CG ASP A 310 21.884 53.733 27.432 1.00 31.88 C ANISOU 5209 CG ASP B 310 2807 4758 4547 -1302 921 -1439 C ATOM 5210 OD1 ASP A 310 23.103 53.945 27.557 1.00 28.93 O ANISOU 5210 OD1 ASP B 310 2547 4269 4177 -1186 841 -1281 O ATOM 5211 OD2 ASP A 310 21.538 52.603 27.036 1.00 32.55 O ANISOU 5211 OD2 ASP B 310 2913 4814 4642 -1441 1038 -1536 O ATOM 5212 N LEU A 311 20.660 54.571 24.554 1.00 32.44 N ANISOU 5212 N LEU B 311 2443 5259 4625 -1208 755 -1697 N ATOM 5213 CA LEU A 311 20.066 53.942 23.379 1.00 33.46 C ANISOU 5213 CA LEU B 311 2438 5517 4757 -1279 784 -1857 C ATOM 5214 C LEU A 311 19.408 52.582 23.666 1.00 34.97 C ANISOU 5214 C LEU B 311 2656 5669 4960 -1513 977 -1998 C ATOM 5215 O LEU A 311 18.612 52.101 22.853 1.00 36.18 O ANISOU 5215 O LEU B 311 2664 5972 5110 -1606 1025 -2182 O ATOM 5216 CB LEU A 311 21.115 53.799 22.267 1.00 32.65 C ANISOU 5216 CB LEU B 311 2374 5359 4674 -1192 699 -1767 C ATOM 5217 CG LEU A 311 21.642 55.109 21.671 1.00 31.69 C ANISOU 5217 CG LEU B 311 2210 5302 4529 -985 525 -1668 C ATOM 5218 CD1 LEU A 311 22.829 54.839 20.756 1.00 31.57 C ANISOU 5218 CD1 LEU B 311 2265 5198 4533 -930 469 -1568 C ATOM 5219 CD2 LEU A 311 20.543 55.863 20.922 1.00 32.84 C ANISOU 5219 CD2 LEU B 311 2155 5695 4628 -908 453 -1811 C ATOM 5220 N ASP A 312 19.719 51.971 24.812 1.00 34.97 N ANISOU 5220 N ASP B 312 2850 5473 4965 -1608 1093 -1920 N ATOM 5221 CA ASP A 312 19.234 50.613 25.126 1.00 36.18 C ANISOU 5221 CA ASP B 312 3093 5534 5119 -1838 1299 -2031 C ATOM 5222 C ASP A 312 18.555 50.461 26.488 1.00 36.98 C ANISOU 5222 C ASP B 312 3271 5588 5193 -1971 1438 -2071 C ATOM 5223 O ASP A 312 17.510 49.825 26.585 1.00 38.75 O ANISOU 5223 O ASP B 312 3435 5884 5403 -2174 1595 -2262 O ATOM 5224 CB ASP A 312 20.396 49.625 25.044 1.00 35.73 C ANISOU 5224 CB ASP B 312 3265 5230 5080 -1844 1343 -1898 C ATOM 5225 CG ASP A 312 21.032 49.599 23.675 1.00 34.84 C ANISOU 5225 CG ASP B 312 3081 5162 4995 -1747 1233 -1880 C ATOM 5226 OD1 ASP A 312 20.535 48.853 22.804 1.00 37.41 O ANISOU 5226 OD1 ASP B 312 3327 5556 5332 -1865 1307 -2032 O ATOM 5227 OD2 ASP A 312 22.012 50.306 23.377 1.00 31.40 O ANISOU 5227 OD2 ASP B 312 2658 4706 4567 -1563 1080 -1733 O ATOM 5228 N ALA A 313 19.176 50.997 27.538 1.00 36.07 N ANISOU 5228 N ALA B 313 3294 5349 5064 -1870 1392 -1898 N ATOM 5229 CA ALA A 313 18.624 50.932 28.893 1.00 36.88 C ANISOU 5229 CA ALA B 313 3485 5397 5131 -1978 1514 -1915 C ATOM 5230 C ALA A 313 17.520 51.971 29.045 1.00 37.08 C ANISOU 5230 C ALA B 313 3276 5670 5142 -1961 1464 -2048 C ATOM 5231 O ALA A 313 17.757 53.167 28.879 1.00 35.25 O ANISOU 5231 O ALA B 313 2944 5535 4914 -1769 1292 -1977 O ATOM 5232 CB ALA A 313 19.716 51.158 29.924 1.00 35.71 C ANISOU 5232 CB ALA B 313 3557 5046 4964 -1858 1468 -1689 C ATOM 5233 N GLU A 314 16.314 51.505 29.360 1.00 39.38 N ANISOU 5233 N GLU B 314 3488 6063 5413 -2165 1624 -2251 N ATOM 5234 CA GLU A 314 15.128 52.359 29.378 1.00 40.33 C ANISOU 5234 CA GLU B 314 3352 6459 5514 -2159 1588 -2428 C ATOM 5235 C GLU A 314 15.230 53.497 30.393 1.00 39.30 C ANISOU 5235 C GLU B 314 3237 6330 5363 -2020 1497 -2316 C ATOM 5236 O GLU A 314 14.721 54.591 30.147 1.00 39.01 O ANISOU 5236 O GLU B 314 3006 6500 5316 -1883 1370 -2378 O ATOM 5237 CB GLU A 314 13.862 51.519 29.613 1.00 43.34 C ANISOU 5237 CB GLU B 314 3653 6944 5871 -2436 1803 -2685 C ATOM 5238 CG GLU A 314 13.778 50.826 30.969 1.00 46.33 C ANISOU 5238 CG GLU B 314 4260 7125 6218 -2625 2005 -2652 C ATOM 5239 CD GLU A 314 12.429 50.185 31.203 1.00 51.41 C ANISOU 5239 CD GLU B 314 4795 7908 6831 -2908 2220 -2933 C ATOM 5240 OE1 GLU A 314 12.077 49.238 30.463 1.00 54.45 O ANISOU 5240 OE1 GLU B 314 5146 8319 7223 -3083 2342 -3089 O ATOM 5241 OE2 GLU A 314 11.713 50.639 32.121 1.00 55.08 O ANISOU 5241 OE2 GLU B 314 5201 8466 7262 -2964 2273 -3009 O ATOM 5242 N LYS A 315 15.926 53.247 31.505 1.00 38.55 N ANISOU 5242 N LYS B 315 3386 6005 5257 -2038 1556 -2148 N ATOM 5243 CA LYS A 315 16.051 54.214 32.595 1.00 37.57 C ANISOU 5243 CA LYS B 315 3299 5866 5111 -1932 1492 -2044 C ATOM 5244 C LYS A 315 17.395 54.959 32.609 1.00 35.41 C ANISOU 5244 C LYS B 315 3133 5470 4853 -1705 1318 -1806 C ATOM 5245 O LYS A 315 17.623 55.811 33.470 1.00 34.38 O ANISOU 5245 O LYS B 315 3039 5320 4706 -1607 1255 -1712 O ATOM 5246 CB LYS A 315 15.822 53.511 33.944 1.00 38.74 C ANISOU 5246 CB LYS B 315 3636 5865 5218 -2110 1682 -2037 C ATOM 5247 CG LYS A 315 14.368 53.108 34.177 1.00 41.13 C ANISOU 5247 CG LYS B 315 3806 6327 5495 -2339 1856 -2293 C ATOM 5248 CD LYS A 315 14.241 51.991 35.201 1.00 43.31 C ANISOU 5248 CD LYS B 315 4325 6405 5726 -2568 2092 -2294 C ATOM 5249 CE LYS A 315 12.806 51.514 35.331 1.00 46.05 C ANISOU 5249 CE LYS B 315 4535 6916 6046 -2832 2287 -2574 C ATOM 5250 NZ LYS A 315 12.572 50.815 36.628 1.00 47.96 N ANISOU 5250 NZ LYS B 315 5012 6985 6226 -3034 2509 -2566 N ATOM 5251 N GLY A 316 18.270 54.646 31.657 1.00 33.93 N ANISOU 5251 N GLY B 316 2987 5210 4696 -1631 1247 -1723 N ATOM 5252 CA GLY A 316 19.542 55.330 31.526 1.00 32.13 C ANISOU 5252 CA GLY B 316 2835 4892 4480 -1434 1089 -1528 C ATOM 5253 C GLY A 316 19.428 56.702 30.883 1.00 31.08 C ANISOU 5253 C GLY B 316 2530 4926 4355 -1261 919 -1535 C ATOM 5254 O GLY A 316 18.643 56.899 29.954 1.00 31.35 O ANISOU 5254 O GLY B 316 2382 5138 4390 -1254 888 -1676 O ATOM 5255 N ILE A 317 20.218 57.648 31.388 1.00 29.71 N ANISOU 5255 N ILE B 317 2424 4691 4174 -1117 813 -1388 N ATOM 5256 CA ILE A 317 20.297 59.002 30.848 1.00 29.00 C ANISOU 5256 CA ILE B 317 2229 4709 4080 -944 660 -1364 C ATOM 5257 C ILE A 317 21.755 59.478 30.864 1.00 27.58 C ANISOU 5257 C ILE B 317 2176 4395 3908 -823 562 -1179 C ATOM 5258 O ILE A 317 22.446 59.316 31.871 1.00 27.39 O ANISOU 5258 O ILE B 317 2290 4240 3875 -834 590 -1074 O ATOM 5259 CB ILE A 317 19.411 59.995 31.679 1.00 29.17 C ANISOU 5259 CB ILE B 317 2171 4841 4073 -907 647 -1425 C ATOM 5260 CG1 ILE A 317 17.938 59.581 31.669 1.00 31.21 C ANISOU 5260 CG1 ILE B 317 2274 5267 4316 -1027 744 -1637 C ATOM 5261 CG2 ILE A 317 19.547 61.410 31.130 1.00 28.64 C ANISOU 5261 CG2 ILE B 317 2037 4853 3990 -713 495 -1389 C ATOM 5262 CD1 ILE A 317 17.099 60.246 32.735 1.00 32.02 C ANISOU 5262 CD1 ILE B 317 2323 5455 4389 -1032 771 -1704 C ATOM 5263 N HIS A 318 22.217 60.048 29.752 1.00 26.79 N ANISOU 5263 N HIS B 318 2028 4336 3816 -711 452 -1149 N ATOM 5264 CA HIS A 318 23.531 60.682 29.677 1.00 25.90 C ANISOU 5264 CA HIS B 318 2009 4128 3704 -604 361 -1002 C ATOM 5265 C HIS A 318 23.396 62.190 29.722 1.00 25.56 C ANISOU 5265 C HIS B 318 1929 4147 3633 -478 268 -982 C ATOM 5266 O HIS A 318 22.369 62.741 29.337 1.00 26.02 O ANISOU 5266 O HIS B 318 1876 4339 3671 -431 242 -1080 O ATOM 5267 CB HIS A 318 24.273 60.299 28.392 1.00 25.46 C ANISOU 5267 CB HIS B 318 1952 4055 3667 -577 315 -975 C ATOM 5268 CG HIS A 318 24.585 58.843 28.296 1.00 26.07 C ANISOU 5268 CG HIS B 318 2091 4047 3768 -683 401 -981 C ATOM 5269 ND1 HIS A 318 23.636 57.904 27.949 1.00 27.63 N ANISOU 5269 ND1 HIS B 318 2224 4298 3976 -797 491 -1107 N ATOM 5270 CD2 HIS A 318 25.728 58.160 28.519 1.00 25.28 C ANISOU 5270 CD2 HIS B 318 2117 3813 3677 -687 414 -885 C ATOM 5271 CE1 HIS A 318 24.188 56.706 27.953 1.00 28.13 C ANISOU 5271 CE1 HIS B 318 2391 4241 4054 -872 564 -1079 C ATOM 5272 NE2 HIS A 318 25.459 56.833 28.293 1.00 28.78 N ANISOU 5272 NE2 HIS B 318 2591 4210 4134 -794 512 -942 N ATOM 5273 N MET A 319 24.455 62.845 30.183 1.00 24.74 N ANISOU 5273 N MET B 319 1925 3951 3524 -418 219 -863 N ATOM 5274 CA MET A 319 24.520 64.301 30.219 1.00 24.48 C ANISOU 5274 CA MET B 319 1897 3943 3463 -305 142 -831 C ATOM 5275 C MET A 319 25.954 64.820 30.360 1.00 23.07 C ANISOU 5275 C MET B 319 1826 3660 3281 -268 97 -712 C ATOM 5276 O MET A 319 26.895 64.057 30.608 1.00 22.61 O ANISOU 5276 O MET B 319 1828 3524 3240 -316 119 -656 O ATOM 5277 CB MET A 319 23.651 64.845 31.355 1.00 25.13 C ANISOU 5277 CB MET B 319 1957 4065 3525 -304 169 -874 C ATOM 5278 CG MET A 319 24.114 64.458 32.741 1.00 25.87 C ANISOU 5278 CG MET B 319 2139 4066 3622 -375 228 -815 C ATOM 5279 SD MET A 319 23.027 65.086 34.012 1.00 28.65 S ANISOU 5279 SD MET B 319 2458 4479 3950 -381 265 -877 S ATOM 5280 CE MET A 319 21.564 64.122 33.695 1.00 29.58 C ANISOU 5280 CE MET B 319 2446 4719 4073 -479 349 -1037 C ATOM 5281 N TRP A 320 26.092 66.133 30.214 1.00 22.69 N ANISOU 5281 N TRP B 320 1803 3616 3203 -179 40 -686 N ATOM 5282 CA TRP A 320 27.375 66.821 30.253 1.00 22.19 C ANISOU 5282 CA TRP B 320 1831 3473 3130 -156 6 -600 C ATOM 5283 C TRP A 320 27.290 67.977 31.249 1.00 21.97 C ANISOU 5283 C TRP B 320 1851 3423 3074 -118 -1 -582 C ATOM 5284 O TRP A 320 26.456 68.866 31.089 1.00 22.53 O ANISOU 5284 O TRP B 320 1909 3536 3116 -43 -23 -619 O ATOM 5285 CB TRP A 320 27.686 67.337 28.854 1.00 22.16 C ANISOU 5285 CB TRP B 320 1837 3477 3105 -97 -43 -591 C ATOM 5286 CG TRP A 320 28.990 68.030 28.690 1.00 21.99 C ANISOU 5286 CG TRP B 320 1906 3382 3067 -96 -62 -524 C ATOM 5287 CD1 TRP A 320 29.182 69.360 28.457 1.00 22.39 C ANISOU 5287 CD1 TRP B 320 2035 3399 3073 -40 -83 -502 C ATOM 5288 CD2 TRP A 320 30.297 67.433 28.680 1.00 22.53 C ANISOU 5288 CD2 TRP B 320 1997 3408 3156 -157 -54 -485 C ATOM 5289 NE1 TRP A 320 30.524 69.632 28.321 1.00 21.90 N ANISOU 5289 NE1 TRP B 320 2038 3279 3005 -87 -77 -459 N ATOM 5290 CE2 TRP A 320 31.232 68.467 28.454 1.00 21.71 C ANISOU 5290 CE2 TRP B 320 1968 3262 3021 -152 -67 -453 C ATOM 5291 CE3 TRP A 320 30.775 66.127 28.843 1.00 22.04 C ANISOU 5291 CE3 TRP B 320 1907 3339 3127 -210 -34 -480 C ATOM 5292 CZ2 TRP A 320 32.607 68.237 28.389 1.00 21.18 C ANISOU 5292 CZ2 TRP B 320 1917 3172 2956 -205 -64 -433 C ATOM 5293 CZ3 TRP A 320 32.139 65.903 28.791 1.00 21.43 C ANISOU 5293 CZ3 TRP B 320 1858 3234 3050 -235 -43 -450 C ATOM 5294 CH2 TRP A 320 33.042 66.954 28.562 1.00 20.87 C ANISOU 5294 CH2 TRP B 320 1832 3148 2950 -235 -60 -433 C ATOM 5295 N VAL A 321 28.139 67.959 32.278 1.00 21.65 N ANISOU 5295 N VAL B 321 1865 3324 3035 -160 17 -533 N ATOM 5296 CA VAL A 321 28.023 68.901 33.403 1.00 21.79 C ANISOU 5296 CA VAL B 321 1922 3326 3029 -142 22 -526 C ATOM 5297 C VAL A 321 29.308 69.688 33.578 1.00 21.54 C ANISOU 5297 C VAL B 321 1966 3237 2979 -146 4 -477 C ATOM 5298 O VAL A 321 30.375 69.102 33.645 1.00 21.15 O ANISOU 5298 O VAL B 321 1930 3169 2938 -188 4 -448 O ATOM 5299 CB VAL A 321 27.709 68.178 34.745 1.00 21.94 C ANISOU 5299 CB VAL B 321 1932 3348 3054 -197 71 -532 C ATOM 5300 CG1 VAL A 321 27.525 69.199 35.879 1.00 21.97 C ANISOU 5300 CG1 VAL B 321 1969 3347 3032 -176 74 -533 C ATOM 5301 CG2 VAL A 321 26.478 67.292 34.618 1.00 22.18 C ANISOU 5301 CG2 VAL B 321 1889 3436 3101 -229 113 -599 C ATOM 5302 N VAL A 322 29.195 71.012 33.667 1.00 22.17 N ANISOU 5302 N VAL B 322 2100 3295 3029 -102 -6 -480 N ATOM 5303 CA VAL A 322 30.353 71.905 33.740 1.00 22.50 C ANISOU 5303 CA VAL B 322 2221 3282 3047 -125 -6 -454 C ATOM 5304 C VAL A 322 30.155 72.986 34.797 1.00 22.81 C ANISOU 5304 C VAL B 322 2311 3296 3058 -113 9 -464 C ATOM 5305 O VAL A 322 29.073 73.550 34.914 1.00 23.15 O ANISOU 5305 O VAL B 322 2360 3348 3088 -46 7 -488 O ATOM 5306 CB VAL A 322 30.603 72.620 32.382 1.00 22.71 C ANISOU 5306 CB VAL B 322 2311 3271 3048 -94 -19 -446 C ATOM 5307 CG1 VAL A 322 31.764 73.593 32.486 1.00 23.36 C ANISOU 5307 CG1 VAL B 322 2485 3292 3099 -146 5 -436 C ATOM 5308 CG2 VAL A 322 30.855 71.609 31.274 1.00 23.48 C ANISOU 5308 CG2 VAL B 322 2356 3396 3168 -108 -35 -440 C ATOM 5309 N SER A 323 31.209 73.273 35.552 1.00 22.88 N ANISOU 5309 N SER B 323 2349 3287 3055 -172 24 -458 N ATOM 5310 CA SER A 323 31.200 74.362 36.521 1.00 23.39 C ANISOU 5310 CA SER B 323 2470 3326 3093 -174 45 -475 C ATOM 5311 C SER A 323 32.619 74.834 36.854 1.00 23.82 C ANISOU 5311 C SER B 323 2560 3365 3125 -253 64 -487 C ATOM 5312 O SER A 323 33.592 74.086 36.721 1.00 23.12 O ANISOU 5312 O SER B 323 2425 3315 3043 -298 54 -486 O ATOM 5313 CB SER A 323 30.510 73.914 37.810 1.00 23.63 C ANISOU 5313 CB SER B 323 2449 3399 3131 -167 52 -484 C ATOM 5314 OG SER A 323 30.215 75.019 38.641 1.00 24.50 O ANISOU 5314 OG SER B 323 2609 3487 3215 -153 70 -507 O ATOM 5315 N ASP A 324 32.719 76.073 37.314 1.00 24.44 N ANISOU 5315 N ASP B 324 2716 3397 3171 -269 95 -511 N ATOM 5316 CA ASP A 324 33.986 76.633 37.741 1.00 25.16 C ANISOU 5316 CA ASP B 324 2834 3490 3236 -360 126 -549 C ATOM 5317 C ASP A 324 34.396 75.893 39.019 1.00 25.28 C ANISOU 5317 C ASP B 324 2760 3594 3252 -379 107 -564 C ATOM 5318 O ASP A 324 33.711 75.988 40.037 1.00 25.33 O ANISOU 5318 O ASP B 324 2760 3611 3254 -348 107 -564 O ATOM 5319 CB ASP A 324 33.848 78.140 37.980 1.00 25.76 C ANISOU 5319 CB ASP B 324 3031 3482 3276 -375 176 -578 C ATOM 5320 CG ASP A 324 35.184 78.829 38.172 1.00 26.64 C ANISOU 5320 CG ASP B 324 3180 3589 3355 -498 228 -638 C ATOM 5321 OD1 ASP A 324 36.110 78.215 38.737 1.00 26.26 O ANISOU 5321 OD1 ASP B 324 3032 3640 3307 -555 213 -674 O ATOM 5322 OD2 ASP A 324 35.405 79.988 37.788 1.00 27.62 O ANISOU 5322 OD2 ASP B 324 3434 3617 3443 -545 290 -663 O ATOM 5323 N ASN A 325 35.493 75.139 38.932 1.00 25.25 N ANISOU 5323 N ASN B 325 2693 3657 3245 -417 89 -578 N ATOM 5324 CA ASN A 325 35.979 74.306 40.039 1.00 25.46 C ANISOU 5324 CA ASN B 325 2648 3773 3253 -404 61 -588 C ATOM 5325 C ASN A 325 36.459 75.068 41.271 1.00 26.22 C ANISOU 5325 C ASN B 325 2744 3912 3305 -442 78 -645 C ATOM 5326 O ASN A 325 36.558 74.495 42.351 1.00 26.04 O ANISOU 5326 O ASN B 325 2683 3956 3256 -407 55 -646 O ATOM 5327 CB ASN A 325 37.088 73.344 39.569 1.00 25.35 C ANISOU 5327 CB ASN B 325 2570 3829 3233 -410 30 -600 C ATOM 5328 CG ASN A 325 38.322 74.064 39.048 1.00 25.81 C ANISOU 5328 CG ASN B 325 2619 3921 3268 -497 53 -675 C ATOM 5329 OD1 ASN A 325 38.268 74.731 38.027 1.00 25.85 O ANISOU 5329 OD1 ASN B 325 2680 3857 3285 -544 88 -677 O ATOM 5330 ND2 ASN A 325 39.436 73.929 39.753 1.00 24.50 N ANISOU 5330 ND2 ASN B 325 2384 3867 3057 -518 37 -745 N ATOM 5331 N LEU A 326 36.769 76.349 41.101 1.00 26.85 N ANISOU 5331 N LEU B 326 2881 3950 3369 -513 125 -697 N ATOM 5332 CA LEU A 326 37.176 77.189 42.213 1.00 27.84 C ANISOU 5332 CA LEU B 326 3012 4111 3455 -564 153 -765 C ATOM 5333 C LEU A 326 36.022 77.965 42.835 1.00 27.67 C ANISOU 5333 C LEU B 326 3061 4015 3438 -532 178 -746 C ATOM 5334 O LEU A 326 36.123 78.373 43.988 1.00 27.84 O ANISOU 5334 O LEU B 326 3071 4077 3429 -549 189 -789 O ATOM 5335 CB LEU A 326 38.277 78.148 41.765 1.00 28.98 C ANISOU 5335 CB LEU B 326 3183 4255 3572 -685 209 -854 C ATOM 5336 CG LEU A 326 39.536 77.450 41.251 1.00 30.04 C ANISOU 5336 CG LEU B 326 3224 4496 3692 -725 187 -903 C ATOM 5337 CD1 LEU A 326 40.665 78.455 41.077 1.00 32.05 C ANISOU 5337 CD1 LEU B 326 3489 4780 3908 -872 258 -1025 C ATOM 5338 CD2 LEU A 326 39.960 76.321 42.195 1.00 31.47 C ANISOU 5338 CD2 LEU B 326 3291 4818 3848 -648 115 -910 C ATOM 5339 N LEU A 327 34.941 78.168 42.082 1.00 27.18 N ANISOU 5339 N LEU B 327 3063 3857 3407 -477 183 -692 N ATOM 5340 CA LEU A 327 33.745 78.821 42.615 1.00 27.31 C ANISOU 5340 CA LEU B 327 3134 3819 3425 -421 198 -682 C ATOM 5341 C LEU A 327 32.801 77.779 43.217 1.00 26.87 C ANISOU 5341 C LEU B 327 3005 3817 3389 -349 160 -640 C ATOM 5342 O LEU A 327 32.984 77.399 44.373 1.00 26.50 O ANISOU 5342 O LEU B 327 2912 3837 3321 -357 153 -652 O ATOM 5343 CB LEU A 327 33.066 79.697 41.553 1.00 27.56 C ANISOU 5343 CB LEU B 327 3279 3733 3460 -380 222 -664 C ATOM 5344 CG LEU A 327 33.903 80.869 41.021 1.00 28.24 C ANISOU 5344 CG LEU B 327 3486 3733 3513 -464 286 -706 C ATOM 5345 CD1 LEU A 327 33.101 81.715 40.046 1.00 29.03 C ANISOU 5345 CD1 LEU B 327 3732 3703 3596 -389 309 -675 C ATOM 5346 CD2 LEU A 327 34.451 81.741 42.154 1.00 29.45 C ANISOU 5346 CD2 LEU B 327 3665 3893 3633 -547 336 -780 C ATOM 5347 N LYS A 328 31.803 77.306 42.473 1.00 26.94 N ANISOU 5347 N LYS B 328 3005 3801 3429 -283 143 -599 N ATOM 5348 CA LYS A 328 30.870 76.309 43.025 1.00 26.86 C ANISOU 5348 CA LYS B 328 2930 3841 3434 -241 129 -577 C ATOM 5349 C LYS A 328 31.606 75.059 43.507 1.00 26.85 C ANISOU 5349 C LYS B 328 2875 3901 3424 -268 112 -554 C ATOM 5350 O LYS A 328 31.174 74.414 44.458 1.00 27.44 O ANISOU 5350 O LYS B 328 2930 4013 3485 -257 119 -544 O ATOM 5351 CB LYS A 328 29.794 75.912 42.011 1.00 26.81 C ANISOU 5351 CB LYS B 328 2905 3822 3460 -182 116 -559 C ATOM 5352 CG LYS A 328 28.738 74.936 42.550 1.00 26.48 C ANISOU 5352 CG LYS B 328 2796 3834 3431 -165 123 -559 C ATOM 5353 CD LYS A 328 28.032 75.474 43.804 1.00 26.56 C ANISOU 5353 CD LYS B 328 2808 3866 3419 -156 148 -594 C ATOM 5354 CE LYS A 328 26.909 74.558 44.270 1.00 26.69 C ANISOU 5354 CE LYS B 328 2763 3938 3442 -158 173 -610 C ATOM 5355 NZ LYS A 328 26.416 74.925 45.643 1.00 26.23 N ANISOU 5355 NZ LYS B 328 2704 3909 3354 -167 204 -642 N ATOM 5356 N GLY A 329 32.715 74.731 42.854 1.00 26.53 N ANISOU 5356 N GLY B 329 2825 3872 3384 -295 93 -549 N ATOM 5357 CA GLY A 329 33.537 73.605 43.247 1.00 26.79 C ANISOU 5357 CA GLY B 329 2818 3966 3395 -294 69 -534 C ATOM 5358 C GLY A 329 34.330 73.795 44.527 1.00 27.41 C ANISOU 5358 C GLY B 329 2886 4112 3416 -305 64 -569 C ATOM 5359 O GLY A 329 34.801 72.812 45.098 1.00 27.54 O ANISOU 5359 O GLY B 329 2885 4183 3396 -270 40 -552 O ATOM 5360 N ALA A 330 34.509 75.043 44.969 1.00 28.01 N ANISOU 5360 N ALA B 330 2981 4186 3475 -345 86 -622 N ATOM 5361 CA ALA A 330 35.180 75.315 46.240 1.00 28.47 C ANISOU 5361 CA ALA B 330 3020 4324 3474 -359 82 -672 C ATOM 5362 C ALA A 330 34.661 76.566 46.965 1.00 28.88 C ANISOU 5362 C ALA B 330 3110 4347 3517 -389 121 -713 C ATOM 5363 O ALA A 330 33.818 76.467 47.859 1.00 28.68 O ANISOU 5363 O ALA B 330 3094 4323 3480 -357 130 -696 O ATOM 5364 CB ALA A 330 36.702 75.407 46.021 1.00 29.33 C ANISOU 5364 CB ALA B 330 3080 4515 3549 -401 64 -738 C ATOM 5365 N ALA A 331 35.162 77.734 46.570 1.00 29.16 N ANISOU 5365 N ALA B 331 3177 4349 3552 -458 154 -773 N ATOM 5366 CA ALA A 331 34.993 78.967 47.345 1.00 29.84 C ANISOU 5366 CA ALA B 331 3307 4413 3616 -498 196 -832 C ATOM 5367 C ALA A 331 33.541 79.409 47.479 1.00 29.46 C ANISOU 5367 C ALA B 331 3316 4282 3595 -443 216 -797 C ATOM 5368 O ALA A 331 33.106 79.785 48.568 1.00 29.86 O ANISOU 5368 O ALA B 331 3370 4354 3623 -435 229 -822 O ATOM 5369 CB ALA A 331 35.833 80.099 46.739 1.00 30.37 C ANISOU 5369 CB ALA B 331 3425 4438 3676 -598 247 -905 C ATOM 5370 N TRP A 332 32.809 79.398 46.371 1.00 29.09 N ANISOU 5370 N TRP B 332 3308 4154 3589 -401 215 -752 N ATOM 5371 CA TRP A 332 31.392 79.748 46.386 1.00 28.98 C ANISOU 5371 CA TRP B 332 3328 4087 3594 -328 223 -734 C ATOM 5372 C TRP A 332 30.586 78.752 47.215 1.00 28.77 C ANISOU 5372 C TRP B 332 3230 4131 3569 -287 205 -708 C ATOM 5373 O TRP A 332 29.719 79.162 47.966 1.00 29.09 O ANISOU 5373 O TRP B 332 3276 4176 3601 -259 223 -731 O ATOM 5374 CB TRP A 332 30.815 79.866 44.970 1.00 28.78 C ANISOU 5374 CB TRP B 332 3348 3987 3599 -273 216 -701 C ATOM 5375 CG TRP A 332 29.292 79.868 44.925 1.00 29.10 C ANISOU 5375 CG TRP B 332 3380 4023 3654 -175 206 -693 C ATOM 5376 CD1 TRP A 332 28.495 79.041 44.187 1.00 28.00 C ANISOU 5376 CD1 TRP B 332 3186 3910 3543 -118 178 -665 C ATOM 5377 CD2 TRP A 332 28.406 80.720 45.663 1.00 30.51 C ANISOU 5377 CD2 TRP B 332 3589 4188 3815 -125 225 -733 C ATOM 5378 NE1 TRP A 332 27.171 79.333 44.408 1.00 29.25 N ANISOU 5378 NE1 TRP B 332 3329 4086 3699 -37 178 -695 N ATOM 5379 CE2 TRP A 332 27.085 80.356 45.314 1.00 30.39 C ANISOU 5379 CE2 TRP B 332 3525 4205 3816 -33 204 -734 C ATOM 5380 CE3 TRP A 332 28.592 81.760 46.588 1.00 31.49 C ANISOU 5380 CE3 TRP B 332 3772 4283 3909 -149 260 -779 C ATOM 5381 CZ2 TRP A 332 25.962 80.994 45.849 1.00 32.36 C ANISOU 5381 CZ2 TRP B 332 3777 4468 4051 45 212 -782 C ATOM 5382 CZ3 TRP A 332 27.476 82.393 47.123 1.00 32.37 C ANISOU 5382 CZ3 TRP B 332 3899 4389 4008 -72 270 -815 C ATOM 5383 CH2 TRP A 332 26.177 82.007 46.753 1.00 32.96 C ANISOU 5383 CH2 TRP B 332 3919 4506 4098 29 243 -817 C ATOM 5384 N ASN A 333 30.867 77.455 47.098 1.00 28.40 N ANISOU 5384 N ASN B 333 3129 4134 3528 -288 179 -666 N ATOM 5385 CA ASN A 333 30.121 76.473 47.892 1.00 28.61 C ANISOU 5385 CA ASN B 333 3118 4207 3545 -266 183 -642 C ATOM 5386 C ASN A 333 30.330 76.695 49.384 1.00 29.06 C ANISOU 5386 C ASN B 333 3177 4315 3548 -282 197 -669 C ATOM 5387 O ASN A 333 29.393 76.538 50.163 1.00 29.81 O ANISOU 5387 O ASN B 333 3267 4429 3631 -270 222 -673 O ATOM 5388 CB ASN A 333 30.467 75.027 47.517 1.00 28.18 C ANISOU 5388 CB ASN B 333 3038 4174 3494 -263 164 -590 C ATOM 5389 CG ASN A 333 29.471 74.026 48.085 1.00 28.85 C ANISOU 5389 CG ASN B 333 3115 4276 3572 -254 193 -567 C ATOM 5390 OD1 ASN A 333 29.792 73.248 48.989 1.00 30.95 O ANISOU 5390 OD1 ASN B 333 3400 4572 3789 -256 201 -543 O ATOM 5391 ND2 ASN A 333 28.252 74.058 47.573 1.00 26.69 N ANISOU 5391 ND2 ASN B 333 2817 3987 3336 -244 214 -583 N ATOM 5392 N SER A 334 31.543 77.086 49.776 1.00 29.15 N ANISOU 5392 N SER B 334 3191 4363 3523 -315 184 -700 N ATOM 5393 CA SER A 334 31.850 77.346 51.183 1.00 29.55 C ANISOU 5393 CA SER B 334 3237 4480 3512 -327 191 -738 C ATOM 5394 C SER A 334 31.131 78.595 51.695 1.00 29.50 C ANISOU 5394 C SER B 334 3259 4440 3510 -338 228 -789 C ATOM 5395 O SER A 334 30.593 78.599 52.802 1.00 29.62 O ANISOU 5395 O SER B 334 3271 4492 3492 -329 245 -802 O ATOM 5396 CB SER A 334 33.358 77.486 51.405 1.00 29.87 C ANISOU 5396 CB SER B 334 3250 4594 3506 -358 165 -784 C ATOM 5397 OG SER A 334 34.046 76.294 51.048 1.00 30.33 O ANISOU 5397 OG SER B 334 3281 4696 3547 -324 124 -743 O ATOM 5398 N VAL A 335 31.120 79.651 50.889 1.00 29.17 N ANISOU 5398 N VAL B 335 3259 4322 3502 -354 245 -818 N ATOM 5399 CA VAL A 335 30.468 80.889 51.289 1.00 29.31 C ANISOU 5399 CA VAL B 335 3327 4290 3518 -349 282 -868 C ATOM 5400 C VAL A 335 28.949 80.710 51.292 1.00 29.00 C ANISOU 5400 C VAL B 335 3279 4236 3504 -277 287 -849 C ATOM 5401 O VAL A 335 28.276 81.227 52.173 1.00 29.56 O ANISOU 5401 O VAL B 335 3354 4321 3557 -262 310 -888 O ATOM 5402 CB VAL A 335 30.900 82.082 50.410 1.00 29.67 C ANISOU 5402 CB VAL B 335 3459 4237 3577 -380 311 -903 C ATOM 5403 CG1 VAL A 335 30.050 83.312 50.701 1.00 30.23 C ANISOU 5403 CG1 VAL B 335 3609 4232 3644 -344 349 -945 C ATOM 5404 CG2 VAL A 335 32.378 82.398 50.636 1.00 30.12 C ANISOU 5404 CG2 VAL B 335 3511 4334 3601 -480 325 -960 C ATOM 5405 N GLN A 336 28.421 79.964 50.325 1.00 28.34 N ANISOU 5405 N GLN B 336 3172 4139 3458 -238 267 -803 N ATOM 5406 CA GLN A 336 26.985 79.685 50.251 1.00 28.20 C ANISOU 5406 CA GLN B 336 3118 4137 3459 -179 274 -807 C ATOM 5407 C GLN A 336 26.524 78.870 51.461 1.00 28.21 C ANISOU 5407 C GLN B 336 3069 4216 3431 -205 296 -809 C ATOM 5408 O GLN A 336 25.419 79.070 51.947 1.00 28.45 O ANISOU 5408 O GLN B 336 3075 4278 3459 -179 320 -851 O ATOM 5409 CB GLN A 336 26.635 78.953 48.953 1.00 27.85 C ANISOU 5409 CB GLN B 336 3047 4081 3455 -147 251 -771 C ATOM 5410 CG GLN A 336 25.129 78.834 48.666 1.00 28.71 C ANISOU 5410 CG GLN B 336 3105 4224 3581 -81 256 -805 C ATOM 5411 CD GLN A 336 24.815 77.918 47.494 1.00 29.14 C ANISOU 5411 CD GLN B 336 3113 4291 3668 -65 237 -780 C ATOM 5412 OE1 GLN A 336 25.594 77.014 47.177 1.00 30.82 O ANISOU 5412 OE1 GLN B 336 3322 4497 3892 -117 229 -728 O ATOM 5413 NE2 GLN A 336 23.675 78.145 46.852 1.00 28.02 N ANISOU 5413 NE2 GLN B 336 2931 4178 3537 14 227 -827 N ATOM 5414 N ILE A 337 27.374 77.965 51.943 1.00 27.73 N ANISOU 5414 N ILE B 337 3004 4190 3341 -248 289 -769 N ATOM 5415 CA ILE A 337 27.102 77.228 53.173 1.00 27.89 C ANISOU 5415 CA ILE B 337 3016 4270 3312 -270 317 -761 C ATOM 5416 C ILE A 337 26.968 78.212 54.337 1.00 28.09 C ANISOU 5416 C ILE B 337 3052 4322 3299 -276 337 -818 C ATOM 5417 O ILE A 337 26.040 78.112 55.127 1.00 27.89 O ANISOU 5417 O ILE B 337 3012 4332 3253 -280 375 -844 O ATOM 5418 CB ILE A 337 28.220 76.189 53.455 1.00 27.98 C ANISOU 5418 CB ILE B 337 3047 4307 3278 -285 296 -706 C ATOM 5419 CG1 ILE A 337 28.027 74.946 52.574 1.00 27.49 C ANISOU 5419 CG1 ILE B 337 2983 4219 3244 -282 296 -650 C ATOM 5420 CG2 ILE A 337 28.249 75.794 54.940 1.00 28.77 C ANISOU 5420 CG2 ILE B 337 3173 4463 3296 -292 320 -703 C ATOM 5421 CD1 ILE A 337 29.277 74.146 52.363 1.00 27.89 C ANISOU 5421 CD1 ILE B 337 3055 4276 3265 -268 258 -601 C ATOM 5422 N ALA A 338 27.896 79.163 54.423 1.00 28.05 N ANISOU 5422 N ALA B 338 3071 4304 3283 -289 320 -848 N ATOM 5423 CA ALA A 338 27.861 80.194 55.458 1.00 28.40 C ANISOU 5423 CA ALA B 338 3131 4368 3293 -301 343 -913 C ATOM 5424 C ALA A 338 26.581 81.031 55.377 1.00 28.61 C ANISOU 5424 C ALA B 338 3162 4359 3350 -259 370 -960 C ATOM 5425 O ALA A 338 25.989 81.359 56.401 1.00 28.56 O ANISOU 5425 O ALA B 338 3147 4392 3314 -259 398 -1004 O ATOM 5426 CB ALA A 338 29.099 81.087 55.371 1.00 28.65 C ANISOU 5426 CB ALA B 338 3190 4384 3312 -341 333 -954 C ATOM 5427 N GLU A 339 26.150 81.347 54.157 1.00 28.47 N ANISOU 5427 N GLU B 339 3159 4276 3383 -212 358 -955 N ATOM 5428 CA GLU A 339 24.915 82.103 53.942 1.00 29.16 C ANISOU 5428 CA GLU B 339 3250 4342 3489 -137 370 -1005 C ATOM 5429 C GLU A 339 23.705 81.284 54.382 1.00 29.24 C ANISOU 5429 C GLU B 339 3177 4437 3496 -125 390 -1022 C ATOM 5430 O GLU A 339 22.774 81.825 54.960 1.00 29.56 O ANISOU 5430 O GLU B 339 3196 4512 3524 -88 412 -1088 O ATOM 5431 CB GLU A 339 24.767 82.523 52.468 1.00 29.13 C ANISOU 5431 CB GLU B 339 3288 4258 3521 -68 345 -991 C ATOM 5432 CG GLU A 339 25.759 83.600 52.038 1.00 29.32 C ANISOU 5432 CG GLU B 339 3423 4178 3540 -85 352 -995 C ATOM 5433 CD GLU A 339 25.650 83.992 50.570 1.00 30.22 C ANISOU 5433 CD GLU B 339 3607 4200 3674 -15 334 -971 C ATOM 5434 OE1 GLU A 339 24.908 83.347 49.801 1.00 30.07 O ANISOU 5434 OE1 GLU B 339 3534 4213 3677 50 304 -950 O ATOM 5435 OE2 GLU A 339 26.323 84.963 50.178 1.00 32.24 O ANISOU 5435 OE2 GLU B 339 3981 4352 3916 -30 358 -980 O ATOM 5436 N THR A 340 23.748 79.978 54.127 1.00 28.69 N ANISOU 5436 N THR B 340 3068 4401 3434 -165 389 -971 N ATOM 5437 CA THR A 340 22.655 79.072 54.475 1.00 29.14 C ANISOU 5437 CA THR B 340 3057 4532 3484 -186 429 -994 C ATOM 5438 C THR A 340 22.580 78.873 55.989 1.00 29.53 C ANISOU 5438 C THR B 340 3111 4633 3474 -242 475 -1010 C ATOM 5439 O THR A 340 21.494 78.898 56.564 1.00 29.80 O ANISOU 5439 O THR B 340 3099 4730 3495 -248 520 -1075 O ATOM 5440 CB THR A 340 22.832 77.716 53.775 1.00 28.82 C ANISOU 5440 CB THR B 340 3001 4489 3461 -226 430 -933 C ATOM 5441 OG1 THR A 340 23.139 77.918 52.391 1.00 28.34 O ANISOU 5441 OG1 THR B 340 2944 4376 3447 -177 381 -910 O ATOM 5442 CG2 THR A 340 21.513 76.931 53.760 1.00 29.73 C ANISOU 5442 CG2 THR B 340 3042 4672 3580 -253 482 -985 C ATOM 5443 N LEU A 341 23.738 78.678 56.616 1.00 29.60 N ANISOU 5443 N LEU B 341 3174 4630 3442 -279 464 -959 N ATOM 5444 CA LEU A 341 23.864 78.682 58.074 1.00 30.37 C ANISOU 5444 CA LEU B 341 3293 4776 3468 -314 497 -973 C ATOM 5445 C LEU A 341 23.187 79.917 58.662 1.00 30.97 C ANISOU 5445 C LEU B 341 3350 4874 3544 -289 514 -1061 C ATOM 5446 O LEU A 341 22.417 79.804 59.598 1.00 31.57 O ANISOU 5446 O LEU B 341 3404 5008 3583 -313 563 -1103 O ATOM 5447 CB LEU A 341 25.341 78.654 58.496 1.00 29.99 C ANISOU 5447 CB LEU B 341 3293 4728 3374 -325 459 -930 C ATOM 5448 CG LEU A 341 26.085 77.324 58.305 1.00 30.45 C ANISOU 5448 CG LEU B 341 3383 4784 3401 -334 444 -847 C ATOM 5449 CD1 LEU A 341 27.590 77.520 58.381 1.00 31.03 C ANISOU 5449 CD1 LEU B 341 3474 4875 3441 -320 388 -833 C ATOM 5450 CD2 LEU A 341 25.629 76.292 59.335 1.00 31.58 C ANISOU 5450 CD2 LEU B 341 3568 4962 3468 -361 499 -818 C ATOM 5451 N HIS A 342 23.458 81.088 58.091 1.00 31.13 N ANISOU 5451 N HIS B 342 3390 4839 3600 -241 481 -1091 N ATOM 5452 CA HIS A 342 22.853 82.333 58.560 1.00 32.33 C ANISOU 5452 CA HIS B 342 3545 4990 3749 -200 498 -1175 C ATOM 5453 C HIS A 342 21.327 82.327 58.339 1.00 33.29 C ANISOU 5453 C HIS B 342 3599 5158 3891 -146 519 -1238 C ATOM 5454 O HIS A 342 20.564 82.698 59.222 1.00 33.94 O ANISOU 5454 O HIS B 342 3650 5298 3946 -140 554 -1310 O ATOM 5455 CB HIS A 342 23.509 83.537 57.868 1.00 32.19 C ANISOU 5455 CB HIS B 342 3599 4875 3758 -162 471 -1188 C ATOM 5456 CG HIS A 342 22.737 84.813 58.001 1.00 33.28 C ANISOU 5456 CG HIS B 342 3767 4981 3898 -88 487 -1270 C ATOM 5457 ND1 HIS A 342 22.148 85.437 56.924 1.00 34.39 N ANISOU 5457 ND1 HIS B 342 3941 5055 4070 16 468 -1287 N ATOM 5458 CD2 HIS A 342 22.452 85.580 59.080 1.00 34.24 C ANISOU 5458 CD2 HIS B 342 3898 5126 3986 -88 518 -1340 C ATOM 5459 CE1 HIS A 342 21.539 86.535 57.332 1.00 34.49 C ANISOU 5459 CE1 HIS B 342 3992 5047 4067 87 485 -1364 C ATOM 5460 NE2 HIS A 342 21.709 86.647 58.636 1.00 34.82 N ANISOU 5460 NE2 HIS B 342 4015 5141 4074 19 518 -1399 N ATOM 5461 N GLU A 343 20.894 81.877 57.168 1.00 33.99 N ANISOU 5461 N GLU B 343 3654 5238 4023 -106 498 -1223 N ATOM 5462 CA GLU A 343 19.468 81.838 56.829 1.00 35.48 C ANISOU 5462 CA GLU B 343 3756 5499 4226 -47 510 -1303 C ATOM 5463 C GLU A 343 18.682 80.895 57.750 1.00 35.61 C ANISOU 5463 C GLU B 343 3697 5622 4210 -134 578 -1343 C ATOM 5464 O GLU A 343 17.520 81.155 58.061 1.00 36.56 O ANISOU 5464 O GLU B 343 3738 5831 4320 -104 608 -1447 O ATOM 5465 CB GLU A 343 19.295 81.414 55.368 1.00 35.65 C ANISOU 5465 CB GLU B 343 3751 5502 4291 3 472 -1279 C ATOM 5466 CG GLU A 343 17.859 81.450 54.855 1.00 39.19 C ANISOU 5466 CG GLU B 343 4094 6048 4749 85 471 -1381 C ATOM 5467 CD GLU A 343 17.386 80.121 54.283 1.00 42.37 C ANISOU 5467 CD GLU B 343 4408 6521 5170 21 494 -1384 C ATOM 5468 OE1 GLU A 343 18.005 79.631 53.309 1.00 43.59 O ANISOU 5468 OE1 GLU B 343 4592 6616 5354 15 462 -1309 O ATOM 5469 OE2 GLU A 343 16.379 79.578 54.801 1.00 45.55 O ANISOU 5469 OE2 GLU B 343 4711 7040 5554 -33 553 -1472 O ATOM 5470 N ARG A 344 19.331 79.824 58.205 1.00 35.06 N ANISOU 5470 N ARG B 344 3662 5544 4114 -237 608 -1266 N ATOM 5471 CA ARG A 344 18.665 78.780 58.983 1.00 35.55 C ANISOU 5471 CA ARG B 344 3693 5681 4135 -335 690 -1288 C ATOM 5472 C ARG A 344 18.797 78.978 60.500 1.00 35.89 C ANISOU 5472 C ARG B 344 3776 5753 4107 -384 735 -1300 C ATOM 5473 O ARG A 344 18.313 78.155 61.266 1.00 36.57 O ANISOU 5473 O ARG B 344 3864 5888 4142 -472 814 -1312 O ATOM 5474 CB ARG A 344 19.203 77.405 58.580 1.00 34.96 C ANISOU 5474 CB ARG B 344 3663 5565 4056 -406 707 -1195 C ATOM 5475 CG ARG A 344 18.806 76.996 57.170 1.00 35.12 C ANISOU 5475 CG ARG B 344 3624 5582 4138 -382 685 -1204 C ATOM 5476 CD ARG A 344 19.306 75.623 56.754 1.00 34.42 C ANISOU 5476 CD ARG B 344 3586 5446 4047 -453 709 -1119 C ATOM 5477 NE ARG A 344 18.479 74.559 57.314 1.00 35.78 N ANISOU 5477 NE ARG B 344 3751 5664 4178 -567 818 -1158 N ATOM 5478 CZ ARG A 344 17.424 74.004 56.707 1.00 36.66 C ANISOU 5478 CZ ARG B 344 3775 5839 4316 -618 871 -1242 C ATOM 5479 NH1 ARG A 344 17.023 74.404 55.505 1.00 36.24 N ANISOU 5479 NH1 ARG B 344 3622 5821 4325 -543 812 -1295 N ATOM 5480 NH2 ARG A 344 16.758 73.036 57.322 1.00 37.47 N ANISOU 5480 NH2 ARG B 344 3892 5973 4371 -748 992 -1281 N ATOM 5481 N GLY A 345 19.454 80.058 60.921 1.00 35.35 N ANISOU 5481 N GLY B 345 3748 5652 4030 -334 692 -1300 N ATOM 5482 CA GLY A 345 19.609 80.375 62.331 1.00 36.08 C ANISOU 5482 CA GLY B 345 3871 5782 4055 -370 726 -1322 C ATOM 5483 C GLY A 345 20.621 79.484 63.025 1.00 35.87 C ANISOU 5483 C GLY B 345 3928 5741 3958 -431 736 -1227 C ATOM 5484 O GLY A 345 20.502 79.208 64.216 1.00 36.28 O ANISOU 5484 O GLY B 345 4010 5842 3933 -479 787 -1235 O ATOM 5485 N LEU A 346 21.632 79.055 62.274 1.00 35.03 N ANISOU 5485 N LEU B 346 3862 5574 3871 -416 683 -1142 N ATOM 5486 CA LEU A 346 22.580 78.049 62.732 1.00 35.06 C ANISOU 5486 CA LEU B 346 3946 5570 3805 -443 682 -1051 C ATOM 5487 C LEU A 346 23.972 78.617 63.034 1.00 35.35 C ANISOU 5487 C LEU B 346 4015 5605 3810 -408 615 -1030 C ATOM 5488 O LEU A 346 24.884 77.860 63.348 1.00 35.50 O ANISOU 5488 O LEU B 346 4092 5634 3764 -402 594 -964 O ATOM 5489 CB LEU A 346 22.672 76.925 61.694 1.00 34.49 C ANISOU 5489 CB LEU B 346 3891 5448 3766 -453 679 -981 C ATOM 5490 CG LEU A 346 21.353 76.215 61.367 1.00 34.03 C ANISOU 5490 CG LEU B 346 3794 5403 3731 -509 756 -1017 C ATOM 5491 CD1 LEU A 346 21.546 75.265 60.201 1.00 32.80 C ANISOU 5491 CD1 LEU B 346 3650 5194 3620 -516 745 -957 C ATOM 5492 CD2 LEU A 346 20.813 75.468 62.582 1.00 34.49 C ANISOU 5492 CD2 LEU B 346 3911 5497 3696 -587 855 -1021 C ATOM 5493 N VAL A 347 24.134 79.937 62.958 1.00 35.82 N ANISOU 5493 N VAL B 347 4043 5659 3907 -385 586 -1096 N ATOM 5494 CA VAL A 347 25.401 80.572 63.315 1.00 36.34 C ANISOU 5494 CA VAL B 347 4129 5740 3940 -378 540 -1107 C ATOM 5495 C VAL A 347 25.437 80.867 64.803 1.00 38.06 C ANISOU 5495 C VAL B 347 4357 6036 4067 -395 566 -1152 C ATOM 5496 O VAL A 347 25.002 81.930 65.258 1.00 38.46 O ANISOU 5496 O VAL B 347 4388 6096 4129 -400 587 -1234 O ATOM 5497 CB VAL A 347 25.654 81.864 62.527 1.00 35.97 C ANISOU 5497 CB VAL B 347 4069 5632 3965 -363 515 -1162 C ATOM 5498 CG1 VAL A 347 26.989 82.490 62.951 1.00 35.93 C ANISOU 5498 CG1 VAL B 347 4077 5656 3918 -387 486 -1198 C ATOM 5499 CG2 VAL A 347 25.619 81.578 61.023 1.00 35.08 C ANISOU 5499 CG2 VAL B 347 3954 5444 3932 -340 488 -1115 C ATOM 5500 N ARG A 348 25.957 79.908 65.559 1.00 39.44 N ANISOU 5500 N ARG B 348 4576 6265 4145 -393 563 -1098 N ATOM 5501 CA ARG A 348 26.060 80.041 67.004 1.00 41.21 C ANISOU 5501 CA ARG B 348 4823 6573 4263 -399 584 -1130 C ATOM 5502 C ARG A 348 27.039 79.018 67.585 1.00 41.95 C ANISOU 5502 C ARG B 348 4980 6723 4237 -358 551 -1062 C ATOM 5503 O ARG A 348 27.370 78.027 66.927 1.00 41.29 O ANISOU 5503 O ARG B 348 4935 6599 4153 -331 532 -980 O ATOM 5504 CB ARG A 348 24.675 79.904 67.661 1.00 42.18 C ANISOU 5504 CB ARG B 348 4951 6707 4370 -436 667 -1155 C ATOM 5505 CG ARG A 348 24.196 78.477 67.902 1.00 43.72 C ANISOU 5505 CG ARG B 348 5220 6892 4501 -456 723 -1076 C ATOM 5506 CD ARG A 348 23.450 77.886 66.735 1.00 45.24 C ANISOU 5506 CD ARG B 348 5392 7014 4783 -480 750 -1049 C ATOM 5507 NE ARG A 348 23.600 76.430 66.674 1.00 47.40 N ANISOU 5507 NE ARG B 348 5762 7251 4996 -491 782 -953 N ATOM 5508 CZ ARG A 348 22.609 75.567 66.455 1.00 49.47 C ANISOU 5508 CZ ARG B 348 6051 7481 5265 -556 868 -942 C ATOM 5509 NH1 ARG A 348 21.356 75.983 66.272 1.00 51.25 N ANISOU 5509 NH1 ARG B 348 6189 7730 5555 -611 926 -1031 N ATOM 5510 NH2 ARG A 348 22.869 74.268 66.421 1.00 50.12 N ANISOU 5510 NH2 ARG B 348 6250 7510 5283 -565 902 -852 N ATOM 5511 N PRO A 349 27.508 79.264 68.809 1.00 43.35 N ANISOU 5511 N PRO B 349 5172 6995 4305 -342 543 -1098 N ATOM 5512 CA PRO A 349 28.358 78.302 69.521 1.00 44.47 C ANISOU 5512 CA PRO B 349 5388 7206 4303 -273 509 -1039 C ATOM 5513 C PRO A 349 27.752 76.903 69.659 1.00 45.09 C ANISOU 5513 C PRO B 349 5588 7226 4318 -260 566 -932 C ATOM 5514 O PRO A 349 26.549 76.759 69.847 1.00 45.18 O ANISOU 5514 O PRO B 349 5624 7191 4351 -326 654 -931 O ATOM 5515 CB PRO A 349 28.510 78.938 70.911 1.00 45.33 C ANISOU 5515 CB PRO B 349 5490 7426 4308 -270 514 -1113 C ATOM 5516 CG PRO A 349 28.342 80.390 70.674 1.00 45.07 C ANISOU 5516 CG PRO B 349 5358 7389 4378 -332 518 -1224 C ATOM 5517 CD PRO A 349 27.309 80.497 69.595 1.00 43.87 C ANISOU 5517 CD PRO B 349 5189 7114 4365 -375 560 -1205 C ATOM 5518 N THR A 350 28.608 75.891 69.571 1.00 45.96 N ANISOU 5518 N THR B 350 5776 7341 4345 -176 521 -852 N ATOM 5519 CA THR A 350 28.229 74.503 69.813 1.00 47.16 C ANISOU 5519 CA THR B 350 6087 7427 4407 -152 580 -746 C ATOM 5520 C THR A 350 28.410 74.188 71.290 1.00 49.00 C ANISOU 5520 C THR B 350 6432 7733 4454 -94 597 -730 C ATOM 5521 O THR A 350 29.368 74.648 71.909 1.00 49.69 O ANISOU 5521 O THR B 350 6481 7943 4458 -14 517 -776 O ATOM 5522 CB THR A 350 29.112 73.567 68.968 1.00 46.89 C ANISOU 5522 CB THR B 350 6101 7352 4362 -66 518 -667 C ATOM 5523 OG1 THR A 350 28.903 73.833 67.576 1.00 45.99 O ANISOU 5523 OG1 THR B 350 5890 7169 4416 -123 508 -679 O ATOM 5524 CG2 THR A 350 28.699 72.112 69.139 1.00 47.78 C ANISOU 5524 CG2 THR B 350 6406 7366 4383 -45 594 -555 C ATOM 5525 N ALA A 351 27.497 73.398 71.849 1.00 50.23 N ANISOU 5525 N ALA B 351 6729 7821 4536 -138 706 -673 N ATOM 5526 CA ALA A 351 27.569 73.028 73.261 1.00 52.13 C ANISOU 5526 CA ALA B 351 7109 8113 4584 -85 739 -646 C ATOM 5527 C ALA A 351 28.670 71.997 73.510 1.00 53.28 C ANISOU 5527 C ALA B 351 7409 8269 4567 83 675 -552 C ATOM 5528 O ALA A 351 29.636 72.270 74.228 1.00 54.34 O ANISOU 5528 O ALA B 351 7530 8535 4582 204 584 -581 O ATOM 5529 CB ALA A 351 26.218 72.494 73.743 1.00 52.90 C ANISOU 5529 CB ALA B 351 7324 8125 4650 -203 896 -622 C ATOM 5530 N GLU A 352 28.522 70.822 72.904 1.00 53.46 N ANISOU 5530 N GLU B 352 7573 8159 4580 95 721 -451 N ATOM 5531 CA GLU A 352 29.405 69.689 73.169 1.00 54.67 C ANISOU 5531 CA GLU B 352 7920 8291 4560 267 681 -349 C ATOM 5532 C GLU A 352 30.531 69.616 72.137 1.00 53.59 C ANISOU 5532 C GLU B 352 7687 8190 4487 375 550 -349 C ATOM 5533 O GLU A 352 30.280 69.628 70.932 1.00 52.19 O ANISOU 5533 O GLU B 352 7421 7935 4475 294 557 -352 O ATOM 5534 CB GLU A 352 28.597 68.386 73.168 1.00 55.74 C ANISOU 5534 CB GLU B 352 8304 8245 4631 216 825 -240 C ATOM 5535 CG GLU A 352 29.418 67.136 73.459 1.00 58.25 C ANISOU 5535 CG GLU B 352 8873 8506 4752 407 800 -122 C ATOM 5536 CD GLU A 352 28.565 65.947 73.868 1.00 60.59 C ANISOU 5536 CD GLU B 352 9469 8619 4932 345 975 -21 C ATOM 5537 OE1 GLU A 352 28.563 64.930 73.137 1.00 61.60 O ANISOU 5537 OE1 GLU B 352 9739 8599 5067 355 1020 58 O ATOM 5538 OE2 GLU A 352 27.901 66.029 74.925 1.00 63.03 O ANISOU 5538 OE2 GLU B 352 9880 8929 5139 277 1075 -26 O ATOM 5539 N LEU A 353 31.767 69.538 72.627 1.00 54.07 N ANISOU 5539 N LEU B 353 7759 8381 4406 562 431 -356 N ATOM 5540 CA LEU A 353 32.952 69.462 71.780 1.00 53.34 C ANISOU 5540 CA LEU B 353 7566 8356 4345 678 303 -376 C ATOM 5541 C LEU A 353 33.248 68.007 71.418 1.00 53.68 C ANISOU 5541 C LEU B 353 7822 8280 4293 808 309 -251 C ATOM 5542 O LEU A 353 33.526 67.189 72.299 1.00 55.13 O ANISOU 5542 O LEU B 353 8221 8459 4268 963 312 -177 O ATOM 5543 CB LEU A 353 34.153 70.081 72.502 1.00 54.30 C ANISOU 5543 CB LEU B 353 7576 8706 4350 819 171 -472 C ATOM 5544 CG LEU A 353 35.428 70.287 71.676 1.00 54.48 C ANISOU 5544 CG LEU B 353 7433 8852 4416 909 37 -544 C ATOM 5545 CD1 LEU A 353 35.241 71.416 70.665 1.00 53.19 C ANISOU 5545 CD1 LEU B 353 7043 8683 4484 724 42 -640 C ATOM 5546 CD2 LEU A 353 36.613 70.578 72.588 1.00 56.41 C ANISOU 5546 CD2 LEU B 353 7610 9338 4484 1080 -84 -638 C ATOM 5547 N LYS A 354 33.200 67.701 70.120 1.00 52.17 N ANISOU 5547 N LYS B 354 7582 7990 4249 754 312 -228 N ATOM 5548 CA LYS A 354 33.382 66.339 69.613 1.00 52.55 C ANISOU 5548 CA LYS B 354 7829 7900 4236 853 333 -114 C ATOM 5549 C LYS A 354 34.684 66.184 68.820 1.00 52.01 C ANISOU 5549 C LYS B 354 7660 7925 4177 1005 190 -141 C ATOM 5550 O LYS A 354 34.880 65.187 68.125 1.00 52.09 O ANISOU 5550 O LYS B 354 7788 7823 4180 1074 196 -64 O ATOM 5551 CB LYS A 354 32.192 65.956 68.725 1.00 51.64 C ANISOU 5551 CB LYS B 354 7753 7592 4277 659 467 -70 C ATOM 5552 CG LYS A 354 30.863 65.859 69.463 1.00 52.39 C ANISOU 5552 CG LYS B 354 7972 7588 4345 507 628 -47 C ATOM 5553 CD LYS A 354 29.763 65.332 68.551 1.00 52.04 C ANISOU 5553 CD LYS B 354 7964 7373 4435 328 760 -21 C ATOM 5554 CE LYS A 354 28.419 65.273 69.260 1.00 53.04 C ANISOU 5554 CE LYS B 354 8186 7428 4539 156 928 -27 C ATOM 5555 NZ LYS A 354 28.024 66.599 69.807 1.00 53.24 N ANISOU 5555 NZ LYS B 354 8016 7589 4625 76 909 -131 N ATOM 5556 N PHE A 355 35.564 67.175 68.917 1.00 51.38 N ANISOU 5556 N PHE B 355 7360 8050 4112 1047 71 -260 N ATOM 5557 CA PHE A 355 36.836 67.153 68.200 1.00 51.10 C ANISOU 5557 CA PHE B 355 7193 8137 4083 1173 -61 -318 C ATOM 5558 C PHE A 355 37.986 67.453 69.169 1.00 52.86 C ANISOU 5558 C PHE B 355 7355 8604 4126 1362 -185 -407 C ATOM 5559 O PHE A 355 37.894 68.364 69.992 1.00 53.22 O ANISOU 5559 O PHE B 355 7308 8767 4147 1307 -188 -489 O ATOM 5560 CB PHE A 355 36.794 68.160 67.044 1.00 48.91 C ANISOU 5560 CB PHE B 355 6669 7878 4037 994 -72 -410 C ATOM 5561 CG PHE A 355 35.526 68.090 66.229 1.00 46.12 C ANISOU 5561 CG PHE B 355 6347 7321 3856 802 49 -348 C ATOM 5562 CD1 PHE A 355 35.314 67.043 65.340 1.00 44.88 C ANISOU 5562 CD1 PHE B 355 6302 7010 3739 813 86 -256 C ATOM 5563 CD2 PHE A 355 34.537 69.056 66.367 1.00 43.21 C ANISOU 5563 CD2 PHE B 355 5894 6924 3601 619 124 -393 C ATOM 5564 CE1 PHE A 355 34.140 66.966 64.594 1.00 42.92 C ANISOU 5564 CE1 PHE B 355 6068 6600 3641 637 195 -218 C ATOM 5565 CE2 PHE A 355 33.367 68.983 65.625 1.00 41.80 C ANISOU 5565 CE2 PHE B 355 5729 6587 3568 461 225 -354 C ATOM 5566 CZ PHE A 355 33.165 67.937 64.740 1.00 41.52 C ANISOU 5566 CZ PHE B 355 5792 6415 3570 466 261 -271 C ATOM 5567 N GLU A 356 39.061 66.676 69.092 1.00 54.47 N ANISOU 5567 N GLU B 356 7607 8894 4194 1593 -289 -399 N ATOM 5568 CA GLU A 356 40.178 66.842 70.026 1.00 56.51 C ANISOU 5568 CA GLU B 356 7808 9408 4255 1805 -417 -494 C ATOM 5569 C GLU A 356 41.178 67.869 69.500 1.00 55.82 C ANISOU 5569 C GLU B 356 7399 9552 4257 1760 -520 -682 C ATOM 5570 O GLU A 356 41.359 68.005 68.291 1.00 54.36 O ANISOU 5570 O GLU B 356 7093 9328 4235 1663 -524 -709 O ATOM 5571 CB GLU A 356 40.855 65.495 70.317 1.00 58.63 C ANISOU 5571 CB GLU B 356 8299 9677 4300 2111 -484 -406 C ATOM 5572 CG GLU A 356 42.010 65.114 69.394 1.00 59.63 C ANISOU 5572 CG GLU B 356 8312 9914 4432 2259 -603 -467 C ATOM 5573 CD GLU A 356 42.724 63.847 69.840 1.00 62.64 C ANISOU 5573 CD GLU B 356 8920 10319 4561 2603 -683 -393 C ATOM 5574 OE1 GLU A 356 42.919 63.662 71.064 1.00 65.45 O ANISOU 5574 OE1 GLU B 356 9404 10769 4692 2788 -720 -383 O ATOM 5575 OE2 GLU A 356 43.098 63.037 68.963 1.00 63.02 O ANISOU 5575 OE2 GLU B 356 9026 10291 4627 2702 -710 -347 O TER 5576 GLU B 356 END