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*** 3CM3_S112C_apo ***elNémo ID: 2405281028003778489Job options:ID = 2405281028003778489 JOBID = 3CM3_S112C_apo USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 3CM3_S112C_apo CRYST1 63.816 38.690 134.987 90.00 90.00 90.00 C 2 2 21 0 ATOM 1 N SER A 7 23.183 -12.243 7.340 1.00 44.49 A N ANISOU 1 N SER A 7 8216 3592 5095 1023 1280 164 A N ATOM 2 CA SER A 7 21.716 -12.220 7.558 1.00 43.59 A C ANISOU 2 CA SER A 7 8036 3596 4931 834 1225 87 A C ATOM 3 C SER A 7 21.163 -10.798 7.556 1.00 42.26 A C ANISOU 3 C SER A 7 7731 3589 4738 820 900 -142 A C ATOM 4 O SER A 7 20.211 -10.492 6.830 1.00 41.39 A O ANISOU 4 O SER A 7 7764 3474 4487 658 806 -126 A O ATOM 5 CB SER A 7 21.378 -12.924 8.872 1.00 44.08 A C ANISOU 5 CB SER A 7 8223 3643 4881 833 1322 81 A C ATOM 6 OG SER A 7 21.891 -14.249 8.855 1.00 44.41 A O ANISOU 6 OG SER A 7 7896 3876 5102 678 1747 337 A O ATOM 7 N LEU A 8 21.763 -9.925 8.369 1.00 42.33 A N ANISOU 7 N LEU A 8 7350 3720 5012 759 406 -263 A N ATOM 8 CA LEU A 8 21.334 -8.523 8.461 1.00 41.98 A C ANISOU 8 CA LEU A 8 6830 3948 5173 513 240 -274 A C ATOM 9 C LEU A 8 21.441 -7.823 7.107 1.00 39.42 A C ANISOU 9 C LEU A 8 5795 3722 5461 59 181 -5 A C ATOM 10 O LEU A 8 20.696 -6.897 6.781 1.00 38.54 A O ANISOU 10 O LEU A 8 5314 3657 5673 -135 164 153 A O ATOM 11 CB LEU A 8 22.160 -7.770 9.514 1.00 44.48 A C ANISOU 11 CB LEU A 8 7426 4363 5113 635 125 -485 A C ATOM 12 CG LEU A 8 21.858 -8.020 10.999 1.00 50.00 A C ANISOU 12 CG LEU A 8 8524 5324 5149 551 6 -427 A C ATOM 13 CD1 LEU A 8 22.859 -7.267 11.891 1.00 54.59 A C ANISOU 13 CD1 LEU A 8 9429 6126 5188 560 -313 -527 A C ATOM 14 CD2 LEU A 8 20.410 -7.636 11.363 1.00 53.72 A C ANISOU 14 CD2 LEU A 8 9136 5931 5345 395 93 -153 A C ATOM 15 N TYR A 9 22.388 -8.300 6.305 1.00 37.60 A N ANISOU 15 N TYR A 9 4841 3722 5722 -395 273 436 A N ATOM 16 CA TYR A 9 22.604 -7.778 4.968 1.00 36.44 A C ANISOU 16 CA TYR A 9 4217 3923 5705 -489 399 785 A C ATOM 17 C TYR A 9 21.475 -8.159 3.995 1.00 34.46 A C ANISOU 17 C TYR A 9 3806 3657 5630 -487 679 891 A C ATOM 18 O TYR A 9 20.937 -7.287 3.301 1.00 34.03 A O ANISOU 18 O TYR A 9 3440 3614 5874 -467 876 1000 A O ATOM 19 CB TYR A 9 23.987 -8.247 4.515 1.00 37.35 A C ANISOU 19 CB TYR A 9 4318 4250 5625 -478 186 957 A C ATOM 20 CG TYR A 9 24.576 -7.492 3.353 1.00 37.20 A C ANISOU 20 CG TYR A 9 4244 4611 5278 -421 -137 1150 A C ATOM 21 CD1 TYR A 9 24.371 -6.124 3.190 1.00 37.62 A C ANISOU 21 CD1 TYR A 9 4332 4863 5098 -496 -450 1194 A C ATOM 22 CD2 TYR A 9 25.360 -8.165 2.425 1.00 36.76 A C ANISOU 22 CD2 TYR A 9 4153 4863 4949 -467 -390 1333 A C ATOM 23 CE1 TYR A 9 24.921 -5.445 2.108 1.00 37.68 A C ANISOU 23 CE1 TYR A 9 4419 4971 4924 -744 -702 1314 A C ATOM 24 CE2 TYR A 9 25.913 -7.500 1.347 1.00 37.22 A C ANISOU 24 CE2 TYR A 9 4499 5036 4607 -658 -661 1412 A C ATOM 25 CZ TYR A 9 25.691 -6.147 1.197 1.00 37.60 A C ANISOU 25 CZ TYR A 9 4544 5052 4690 -912 -772 1342 A C ATOM 26 OH TYR A 9 26.249 -5.509 0.122 1.00 39.04 A O ANISOU 26 OH TYR A 9 4874 5281 4679 -1133 -732 1421 A O ATOM 27 N LYS A 10 21.090 -9.440 3.972 1.00 30.45 A N ANISOU 27 N LYS A 10 3280 3388 4902 -186 1049 601 A N ATOM 28 CA LYS A 10 19.977 -9.930 3.157 1.00 27.79 A C ANISOU 28 CA LYS A 10 3384 3183 3991 31 991 153 A C ATOM 29 C LYS A 10 18.679 -9.227 3.576 1.00 24.44 A C ANISOU 29 C LYS A 10 2779 3140 3366 -93 1054 -27 A C ATOM 30 O LYS A 10 17.820 -8.854 2.764 1.00 24.09 A O ANISOU 30 O LYS A 10 2867 3145 3143 -49 1093 -173 A O ATOM 31 CB LYS A 10 19.820 -11.439 3.344 1.00 28.79 A C ANISOU 31 CB LYS A 10 3743 3167 4029 137 829 120 A C ATOM 32 CG LYS A 10 19.274 -12.183 2.133 1.00 33.33 A C ANISOU 32 CG LYS A 10 4706 3370 4589 285 74 -104 A C ATOM 33 CD LYS A 10 18.705 -13.550 2.516 1.00 38.32 A C ANISOU 33 CD LYS A 10 5404 3574 5580 357 -723 -285 A C ATOM 34 CE LYS A 10 19.780 -14.482 3.067 1.00 40.07 A C ANISOU 34 CE LYS A 10 5457 3634 6132 395 -873 -208 A C ATOM 35 NZ LYS A 10 19.278 -15.893 3.007 1.00 41.44 A N ANISOU 35 NZ LYS A 10 5435 3720 6589 315 -1045 -153 A N ATOM 36 N TYR A 11 18.542 -9.040 4.879 1.00 22.01 A N ANISOU 36 N TYR A 11 2266 3070 3027 -346 794 -263 A N ATOM 37 CA TYR A 11 17.431 -8.298 5.473 1.00 20.62 A C ANISOU 37 CA TYR A 11 1912 3201 2723 -496 496 -339 A C ATOM 38 C TYR A 11 17.342 -6.888 4.890 1.00 20.56 A C ANISOU 38 C TYR A 11 1852 3127 2831 -461 249 -340 A C ATOM 39 O TYR A 11 16.295 -6.441 4.426 1.00 21.05 A O ANISOU 39 O TYR A 11 1817 3364 2815 -432 217 -419 A O ATOM 40 CB TYR A 11 17.612 -8.268 6.997 1.00 21.04 A C ANISOU 40 CB TYR A 11 1946 3316 2734 -489 342 -445 A C ATOM 41 CG TYR A 11 16.783 -7.222 7.718 1.00 21.17 A C ANISOU 41 CG TYR A 11 2008 3431 2606 -540 417 -522 A C ATOM 42 CD1 TYR A 11 15.425 -7.417 7.966 1.00 22.32 A C ANISOU 42 CD1 TYR A 11 2313 3424 2741 -766 684 -718 A C ATOM 43 CD2 TYR A 11 17.361 -6.043 8.183 1.00 22.45 A C ANISOU 43 CD2 TYR A 11 2213 3592 2725 -529 93 -640 A C ATOM 44 CE1 TYR A 11 14.674 -6.447 8.644 1.00 23.41 A C ANISOU 44 CE1 TYR A 11 2655 3289 2949 -775 891 -785 A C ATOM 45 CE2 TYR A 11 16.626 -5.070 8.849 1.00 23.11 A C ANISOU 45 CE2 TYR A 11 2426 3388 2967 -715 392 -644 A C ATOM 46 CZ TYR A 11 15.276 -5.275 9.082 1.00 23.60 A C ANISOU 46 CZ TYR A 11 2572 3228 3167 -744 692 -776 A C ATOM 47 OH TYR A 11 14.553 -4.304 9.753 1.00 25.16 A O ANISOU 47 OH TYR A 11 3032 3334 3194 -709 869 -662 A O ATOM 48 N LEU A 12 18.464 -6.178 4.897 1.00 20.33 A N ANISOU 48 N LEU A 12 1800 3034 2890 -599 43 -87 A N ATOM 49 CA LEU A 12 18.478 -4.801 4.399 1.00 21.01 A C ANISOU 49 CA LEU A 12 1658 3136 3188 -485 -82 107 A C ATOM 50 C LEU A 12 18.076 -4.684 2.934 1.00 20.09 A C ANISOU 50 C LEU A 12 1641 2908 3084 -438 153 17 A C ATOM 51 O LEU A 12 17.345 -3.764 2.549 1.00 19.44 A O ANISOU 51 O LEU A 12 1448 3059 2879 -375 -20 -109 A O ATOM 52 CB LEU A 12 19.873 -4.173 4.578 1.00 22.64 A C ANISOU 52 CB LEU A 12 1886 3160 3555 -597 -284 274 A C ATOM 53 CG LEU A 12 20.184 -3.318 5.801 1.00 27.44 A C ANISOU 53 CG LEU A 12 2307 4129 3991 -688 -780 368 A C ATOM 54 CD1 LEU A 12 19.322 -3.659 6.999 1.00 30.89 A C ANISOU 54 CD1 LEU A 12 3131 4598 4007 -939 -1062 485 A C ATOM 55 CD2 LEU A 12 21.682 -3.373 6.124 1.00 28.98 A C ANISOU 55 CD2 LEU A 12 2318 4038 4654 -662 -1368 465 A C ATOM 56 N LEU A 13 18.561 -5.620 2.120 1.00 20.25 A N ANISOU 56 N LEU A 13 1430 2964 3300 -434 394 -164 A N ATOM 57 CA LEU A 13 18.340 -5.547 0.673 1.00 19.43 A C ANISOU 57 CA LEU A 13 1221 2836 3327 -434 631 -296 A C ATOM 58 C LEU A 13 16.918 -5.903 0.275 1.00 18.78 A C ANISOU 58 C LEU A 13 1269 2745 3120 -412 653 -225 A C ATOM 59 O LEU A 13 16.395 -5.315 -0.681 1.00 18.98 A O ANISOU 59 O LEU A 13 1171 2971 3070 -344 675 -91 A O ATOM 60 CB LEU A 13 19.375 -6.396 -0.075 1.00 20.50 A C ANISOU 60 CB LEU A 13 1141 2933 3716 -386 666 -388 A C ATOM 61 CG LEU A 13 20.809 -5.863 0.013 1.00 22.36 A C ANISOU 61 CG LEU A 13 1208 3314 3973 -509 710 -573 A C ATOM 62 CD1 LEU A 13 21.757 -6.870 -0.607 1.00 25.73 A C ANISOU 62 CD1 LEU A 13 1194 3819 4765 -421 754 -952 A C ATOM 63 CD2 LEU A 13 20.918 -4.517 -0.676 1.00 23.69 A C ANISOU 63 CD2 LEU A 13 1316 3718 3968 -675 570 -463 A C ATOM 64 N LEU A 14 16.304 -6.830 1.022 1.00 18.27 A N ANISOU 64 N LEU A 14 1307 2933 2702 -630 693 -348 A N ATOM 65 CA LEU A 14 14.889 -7.151 0.792 1.00 18.82 A C ANISOU 65 CA LEU A 14 1499 2975 2678 -678 631 -505 A C ATOM 66 C LEU A 14 14.012 -5.994 1.233 1.00 18.60 A C ANISOU 66 C LEU A 14 1488 3088 2493 -631 395 -688 A C ATOM 67 O LEU A 14 13.097 -5.589 0.511 1.00 19.82 A O ANISOU 67 O LEU A 14 1445 3440 2644 -537 226 -736 A O ATOM 68 CB LEU A 14 14.473 -8.446 1.490 1.00 19.45 A C ANISOU 68 CB LEU A 14 1703 2973 2716 -724 728 -524 A C ATOM 69 CG LEU A 14 15.042 -9.718 0.855 1.00 20.59 A C ANISOU 69 CG LEU A 14 1852 3086 2885 -586 715 -496 A C ATOM 70 CD1 LEU A 14 14.845 -10.925 1.761 1.00 23.30 A C ANISOU 70 CD1 LEU A 14 2630 3127 3097 -684 702 -450 A C ATOM 71 CD2 LEU A 14 14.391 -9.961 -0.499 1.00 21.37 A C ANISOU 71 CD2 LEU A 14 1562 3574 2985 -741 666 -617 A C ATOM 72 N ARG A 15 14.295 -5.441 2.414 1.00 18.33 A N ANISOU 72 N ARG A 15 1439 3199 2328 -595 405 -746 A N ATOM 73 CA ARG A 15 13.552 -4.267 2.876 1.00 19.23 A C ANISOU 73 CA ARG A 15 1518 3366 2423 -395 364 -851 A C ATOM 74 C ARG A 15 13.692 -3.112 1.887 1.00 19.25 A C ANISOU 74 C ARG A 15 1509 3330 2477 -208 219 -878 A C ATOM 75 O ARG A 15 12.766 -2.317 1.713 1.00 20.80 A O ANISOU 75 O ARG A 15 1365 3637 2901 -93 74 -907 A O ATOM 76 CB ARG A 15 14.033 -3.804 4.254 1.00 19.86 A C ANISOU 76 CB ARG A 15 1623 3546 2377 -333 483 -829 A C ATOM 77 CG ARG A 15 13.618 -4.681 5.409 1.00 19.49 A C ANISOU 77 CG ARG A 15 1315 3382 2707 -230 496 -586 A C ATOM 78 CD ARG A 15 12.189 -4.338 5.822 1.00 21.63 A C ANISOU 78 CD ARG A 15 1474 3531 3215 -140 746 -293 A C ATOM 79 NE ARG A 15 11.763 -5.069 7.013 1.00 24.10 A N ANISOU 79 NE ARG A 15 1974 3650 3533 -240 590 -175 A N ATOM 80 CZ ARG A 15 11.262 -6.306 6.998 1.00 25.97 A C ANISOU 80 CZ ARG A 15 2433 3679 3756 -163 829 -228 A C ATOM 81 NH1 ARG A 15 11.123 -6.966 5.849 1.00 26.45 A N ANISOU 81 NH1 ARG A 15 2220 3882 3946 -54 560 -491 A N ATOM 82 NH2 ARG A 15 10.915 -6.890 8.139 1.00 28.74 A N ANISOU 82 NH2 ARG A 15 2836 3989 4095 -333 816 5 A N ATOM 83 N SER A 16 14.861 -3.017 1.259 1.00 18.28 A N ANISOU 83 N SER A 16 1412 3192 2338 -208 52 -772 A N ATOM 84 CA SER A 16 15.174 -1.901 0.381 1.00 18.14 A C ANISOU 84 CA SER A 16 1474 3041 2378 -229 -153 -714 A C ATOM 85 C SER A 16 14.520 -2.030 -0.993 1.00 18.62 A C ANISOU 85 C SER A 16 1612 3129 2333 -240 -98 -693 A C ATOM 86 O SER A 16 14.470 -1.063 -1.759 1.00 20.16 A O ANISOU 86 O SER A 16 2044 3194 2421 -219 -229 -627 A O ATOM 87 CB SER A 16 16.690 -1.765 0.229 1.00 18.16 A C ANISOU 87 CB SER A 16 1474 3064 2363 -259 -73 -649 A C ATOM 88 OG SER A 16 17.258 -1.282 1.429 1.00 19.88 A O ANISOU 88 OG SER A 16 1473 3255 2824 -333 -518 -548 A O ATOM 89 N THR A 17 14.017 -3.222 -1.304 1.00 18.90 A N ANISOU 89 N THR A 17 1479 3294 2407 -205 -252 -772 A N ATOM 90 CA THR A 17 13.371 -3.432 -2.604 1.00 19.63 A C ANISOU 90 CA THR A 17 1250 3639 2569 -37 -186 -798 A C ATOM 91 C THR A 17 11.878 -3.734 -2.488 1.00 22.21 A C ANISOU 91 C THR A 17 1280 4275 2883 126 -34 -886 A C ATOM 92 O THR A 17 11.291 -4.458 -3.310 1.00 22.54 A O ANISOU 92 O THR A 17 1132 4429 3003 -93 -46 -900 A O ATOM 93 CB THR A 17 14.118 -4.494 -3.420 1.00 19.24 A C ANISOU 93 CB THR A 17 1191 3569 2549 27 -230 -697 A C ATOM 94 CG2 THR A 17 15.484 -3.953 -3.845 1.00 19.98 A C ANISOU 94 CG2 THR A 17 982 3973 2637 -54 -194 -614 A C ATOM 95 OG1 THR A 17 14.310 -5.664 -2.631 1.00 20.92 A O ANISOU 95 OG1 THR A 17 1852 3447 2648 57 -318 -627 A O ATOM 96 N GLY A 18 11.267 -3.160 -1.460 1.00 25.57 A N ANISOU 96 N GLY A 18 1349 4981 3384 450 109 -895 A N ATOM 97 CA GLY A 18 9.812 -3.133 -1.365 1.00 29.05 A C ANISOU 97 CA GLY A 18 1509 5475 4052 617 186 -749 A C ATOM 98 C GLY A 18 9.203 -4.108 -0.388 1.00 30.47 A C ANISOU 98 C GLY A 18 1703 5519 4356 489 -31 -741 A C ATOM 99 O GLY A 18 7.992 -4.157 -0.233 1.00 31.07 A O ANISOU 99 O GLY A 18 1683 5792 4329 549 35 -627 A O ATOM 100 N ASP A 19 10.049 -4.871 0.291 1.00 30.58 A N ANISOU 100 N ASP A 19 1834 5177 4609 366 -302 -891 A N ATOM 101 CA ASP A 19 9.591 -5.824 1.293 1.00 31.86 A C ANISOU 101 CA ASP A 19 2125 5120 4859 208 -513 -882 A C ATOM 102 C ASP A 19 9.420 -5.129 2.645 1.00 32.65 A C ANISOU 102 C ASP A 19 2298 5309 4798 -41 -284 -898 A C ATOM 103 O ASP A 19 10.106 -5.462 3.617 1.00 33.37 A O ANISOU 103 O ASP A 19 2475 5364 4838 -81 -403 -776 A O ATOM 104 CB ASP A 19 10.589 -6.977 1.399 1.00 32.67 A C ANISOU 104 CB ASP A 19 2266 5044 5102 353 -754 -847 A C ATOM 105 CG ASP A 19 9.922 -8.315 1.620 1.00 35.72 A C ANISOU 105 CG ASP A 19 2606 5149 5817 408 -935 -520 A C ATOM 106 OD1 ASP A 19 8.675 -8.381 1.625 1.00 40.17 A O ANISOU 106 OD1 ASP A 19 2883 5475 6904 359 -930 52 A O ATOM 107 OD2 ASP A 19 10.655 -9.309 1.788 1.00 37.19 A O ANISOU 107 OD2 ASP A 19 2639 5320 6172 533 -472 -293 A O ATOM 108 N MET A 20 8.515 -4.150 2.686 1.00 33.80 A N ANISOU 108 N MET A 20 2196 5766 4881 -379 324 -1062 A N ATOM 109 CA MET A 20 8.201 -3.408 3.907 1.00 36.03 A C ANISOU 109 CA MET A 20 2398 6219 5073 -662 900 -1193 A C ATOM 110 C MET A 20 6.725 -3.584 4.233 1.00 35.57 A C ANISOU 110 C MET A 20 2257 6348 4910 -538 842 -1436 A C ATOM 111 O MET A 20 5.913 -3.787 3.331 1.00 36.84 A O ANISOU 111 O MET A 20 2451 6736 4809 -241 828 -1500 A O ATOM 112 CB MET A 20 8.497 -1.915 3.724 1.00 36.98 A C ANISOU 112 CB MET A 20 2511 6190 5349 -807 944 -1181 A C ATOM 113 CG MET A 20 9.956 -1.574 3.451 1.00 39.78 A C ANISOU 113 CG MET A 20 2730 6657 5727 -1058 1102 -560 A C ATOM 114 SD MET A 20 10.187 0.131 2.896 1.00 37.05 A S ANISOU 114 SD MET A 20 2205 6790 5083 -966 445 -394 A S ATOM 115 CE MET A 20 9.710 1.045 4.359 1.00 38.64 A C ANISOU 115 CE MET A 20 2572 7181 4928 -581 680 -186 A C ATOM 116 N HIS A 21 6.377 -3.495 5.514 1.00 34.13 A N ANISOU 116 N HIS A 21 1897 6115 4956 -767 781 -1594 A N ATOM 117 CA HIS A 21 4.967 -3.519 5.914 1.00 33.82 A C ANISOU 117 CA HIS A 21 1606 5917 5328 -960 579 -1536 A C ATOM 118 C HIS A 21 4.347 -2.137 5.753 1.00 33.67 A C ANISOU 118 C HIS A 21 1473 5957 5363 -1036 214 -1712 A C ATOM 119 O HIS A 21 5.060 -1.133 5.768 1.00 34.06 A O ANISOU 119 O HIS A 21 1474 5896 5572 -1141 331 -1773 A O ATOM 120 CB HIS A 21 4.812 -3.980 7.368 1.00 33.83 A C ANISOU 120 CB HIS A 21 1615 5806 5432 -1061 649 -1500 A C ATOM 121 CG HIS A 21 5.461 -3.073 8.371 1.00 35.75 A C ANISOU 121 CG HIS A 21 1923 5565 6097 -732 397 -1674 A C ATOM 122 CD2 HIS A 21 6.728 -3.039 8.850 1.00 36.72 A C ANISOU 122 CD2 HIS A 21 2071 5188 6692 -636 131 -1921 A C ATOM 123 ND1 HIS A 21 4.796 -2.045 9.006 1.00 38.16 A N ANISOU 123 ND1 HIS A 21 2213 5400 6887 -537 219 -1852 A N ATOM 124 CE1 HIS A 21 5.617 -1.420 9.830 1.00 39.04 A C ANISOU 124 CE1 HIS A 21 2560 5070 7203 -410 104 -1993 A C ATOM 125 NE2 HIS A 21 6.802 -2.003 9.752 1.00 38.17 A N ANISOU 125 NE2 HIS A 21 2383 5004 7116 -463 109 -2020 A N ATOM 126 N LYS A 22 3.023 -2.075 5.607 1.00 34.26 A N ANISOU 126 N LYS A 22 1483 6291 5245 -864 -270 -1817 A N ATOM 127 CA LYS A 22 2.320 -0.795 5.610 1.00 35.95 A C ANISOU 127 CA LYS A 22 1867 6751 5040 -485 -732 -1791 A C ATOM 128 C LYS A 22 2.526 -0.107 6.958 1.00 33.73 A C ANISOU 128 C LYS A 22 1903 6377 4535 -562 -560 -1665 A C ATOM 129 O LYS A 22 2.576 -0.773 7.994 1.00 34.00 A O ANISOU 129 O LYS A 22 2072 6352 4496 -671 -252 -1615 A O ATOM 130 CB LYS A 22 0.820 -0.983 5.369 1.00 38.34 A C ANISOU 130 CB LYS A 22 1941 7225 5400 -322 -1084 -1744 A C ATOM 131 CG LYS A 22 0.027 0.324 5.298 1.00 44.81 A C ANISOU 131 CG LYS A 22 2319 8553 6154 401 -1289 -1263 A C ATOM 132 CD LYS A 22 -1.190 0.306 6.219 1.00 52.86 A C ANISOU 132 CD LYS A 22 2624 10339 7120 1162 -1418 -544 A C ATOM 133 CE LYS A 22 -2.291 -0.594 5.668 1.00 54.96 A C ANISOU 133 CE LYS A 22 2361 11181 7342 1571 -1410 -333 A C ATOM 134 NZ LYS A 22 -2.980 0.029 4.467 1.00 57.76 A N ANISOU 134 NZ LYS A 22 2858 11706 7383 1764 -1289 -259 A N ATOM 135 N ALA A 23 2.655 1.215 6.943 1.00 31.62 A N ANISOU 135 N ALA A 23 1808 6129 4077 -610 -348 -1453 A N ATOM 136 CA ALA A 23 2.866 1.979 8.169 1.00 29.59 A C ANISOU 136 CA ALA A 23 1474 5921 3849 -793 -98 -1263 A C ATOM 137 C ALA A 23 1.743 1.778 9.181 1.00 28.94 A C ANISOU 137 C ALA A 23 1233 5787 3977 -908 -20 -1162 A C ATOM 138 O ALA A 23 0.552 1.746 8.820 1.00 29.53 A O ANISOU 138 O ALA A 23 1146 5981 4092 -913 -148 -1079 A O ATOM 139 CB ALA A 23 3.046 3.459 7.856 1.00 29.89 A C ANISOU 139 CB ALA A 23 1747 5956 3652 -856 24 -1177 A C ATOM 140 N LYS A 24 2.140 1.618 10.441 1.00 28.48 A N ANISOU 140 N LYS A 24 1054 5655 4113 -842 175 -1307 A N ATOM 141 CA LYS A 24 1.193 1.603 11.551 1.00 29.17 A C ANISOU 141 CA LYS A 24 1189 5521 4372 -763 313 -1342 A C ATOM 142 C LYS A 24 1.667 2.519 12.684 1.00 27.80 A C ANISOU 142 C LYS A 24 961 5350 4253 -612 394 -1421 A C ATOM 143 O LYS A 24 2.868 2.626 12.959 1.00 27.14 A O ANISOU 143 O LYS A 24 724 5170 4417 -727 498 -1483 A O ATOM 144 CB LYS A 24 0.877 0.178 12.026 1.00 30.86 A C ANISOU 144 CB LYS A 24 1527 5687 4510 -790 230 -1216 A C ATOM 145 CG LYS A 24 1.951 -0.563 12.789 1.00 37.50 A C ANISOU 145 CG LYS A 24 2867 6258 5123 -772 -379 -815 A C ATOM 146 CD LYS A 24 1.691 -0.548 14.304 1.00 44.81 A C ANISOU 146 CD LYS A 24 4266 6941 5820 -674 -926 -226 A C ATOM 147 CE LYS A 24 2.874 -1.170 15.046 1.00 46.58 A C ANISOU 147 CE LYS A 24 4541 7045 6111 -573 -1155 -31 A C ATOM 148 NZ LYS A 24 3.055 -0.630 16.423 1.00 46.50 A N ANISOU 148 NZ LYS A 24 4343 7031 6294 -434 -1137 -62 A N ATOM 149 N SER A 25 0.722 3.211 13.310 1.00 27.12 A N ANISOU 149 N SER A 25 1017 4992 4293 -474 478 -1342 A N ATOM 150 CA SER A 25 1.045 4.230 14.309 1.00 27.36 A C ANISOU 150 CA SER A 25 1298 4809 4287 -542 571 -988 A C ATOM 151 C SER A 25 1.682 3.638 15.557 1.00 25.25 A C ANISOU 151 C SER A 25 1263 4499 3831 -766 736 -886 A C ATOM 152 O SER A 25 1.158 2.679 16.134 1.00 27.10 A O ANISOU 152 O SER A 25 1559 4702 4034 -1027 700 -793 A O ATOM 153 CB SER A 25 -0.231 4.973 14.714 1.00 28.47 A C ANISOU 153 CB SER A 25 1474 4798 4544 -317 619 -1022 A C ATOM 154 OG SER A 25 -0.814 5.648 13.606 1.00 33.15 A O ANISOU 154 OG SER A 25 2011 5174 5411 -197 507 -493 A O ATOM 155 N PRO A 26 2.805 4.205 16.000 1.00 24.05 A N ANISOU 155 N PRO A 26 1393 4379 3366 -929 785 -640 A N ATOM 156 CA PRO A 26 3.391 3.754 17.253 1.00 24.50 A C ANISOU 156 CA PRO A 26 1728 4345 3235 -948 878 -559 A C ATOM 157 C PRO A 26 2.484 4.093 18.435 1.00 25.82 A C ANISOU 157 C PRO A 26 2157 4347 3307 -1171 1032 -553 A C ATOM 158 O PRO A 26 1.745 5.076 18.404 1.00 27.09 A O ANISOU 158 O PRO A 26 2301 4616 3375 -1001 1096 -553 A O ATOM 159 CB PRO A 26 4.703 4.546 17.342 1.00 23.89 A C ANISOU 159 CB PRO A 26 1492 4460 3127 -930 772 -551 A C ATOM 160 CG PRO A 26 4.945 5.078 15.983 1.00 23.76 A C ANISOU 160 CG PRO A 26 1315 4372 3339 -798 652 -403 A C ATOM 161 CD PRO A 26 3.614 5.245 15.344 1.00 22.80 A C ANISOU 161 CD PRO A 26 1132 4282 3249 -833 776 -582 A C ATOM 162 N THR A 27 2.570 3.296 19.486 1.00 28.48 A N ANISOU 162 N THR A 27 2856 4415 3551 -1456 1150 -406 A N ATOM 163 CA THR A 27 1.749 3.516 20.668 1.00 31.11 A C ANISOU 163 CA THR A 27 3355 4541 3925 -1650 1132 -307 A C ATOM 164 C THR A 27 2.619 3.709 21.898 1.00 30.14 A C ANISOU 164 C THR A 27 3436 4230 3785 -1404 1186 -351 A C ATOM 165 O THR A 27 2.490 4.698 22.630 1.00 31.69 A O ANISOU 165 O THR A 27 3740 4244 4056 -1229 876 -531 A O ATOM 166 CB THR A 27 0.766 2.328 20.904 1.00 32.58 A C ANISOU 166 CB THR A 27 3479 4731 4169 -1833 1096 -197 A C ATOM 167 CG2 THR A 27 -0.269 2.256 19.794 1.00 34.64 A C ANISOU 167 CG2 THR A 27 3528 5169 4465 -2010 1049 -274 A C ATOM 168 OG1 THR A 27 1.489 1.091 20.919 1.00 36.29 A O ANISOU 168 OG1 THR A 27 4320 4763 4706 -1914 820 -87 A O ATOM 169 N ILE A 28 3.504 2.744 22.127 1.00 29.61 A N ANISOU 169 N ILE A 28 3463 4086 3702 -1272 1333 -260 A N ATOM 170 CA ILE A 28 4.366 2.773 23.294 1.00 29.34 A C ANISOU 170 CA ILE A 28 3497 3914 3736 -1172 1447 59 A C ATOM 171 C ILE A 28 5.685 3.471 22.992 1.00 27.43 A C ANISOU 171 C ILE A 28 3384 3855 3185 -1075 1324 -15 A C ATOM 172 O ILE A 28 6.198 3.447 21.872 1.00 27.83 A O ANISOU 172 O ILE A 28 3422 4117 3034 -1127 1412 -41 A O ATOM 173 CB ILE A 28 4.623 1.359 23.883 1.00 30.74 A C ANISOU 173 CB ILE A 28 3643 3932 4104 -1158 1465 131 A C ATOM 174 CG1 ILE A 28 5.357 0.456 22.886 1.00 33.34 A C ANISOU 174 CG1 ILE A 28 3867 4151 4650 -842 1393 326 A C ATOM 175 CG2 ILE A 28 3.308 0.737 24.355 1.00 32.45 A C ANISOU 175 CG2 ILE A 28 3772 3995 4564 -1163 1562 472 A C ATOM 176 CD1 ILE A 28 5.969 -0.795 23.507 1.00 35.77 A C ANISOU 176 CD1 ILE A 28 3946 4587 5059 -383 1220 553 A C ATOM 177 N MET A 29 6.197 4.136 24.020 1.00 25.83 A N ANISOU 177 N MET A 29 3185 3662 2969 -636 925 46 A N ATOM 178 CA MET A 29 7.531 4.715 24.016 1.00 24.73 A C ANISOU 178 CA MET A 29 3120 3386 2890 -292 599 76 A C ATOM 179 C MET A 29 8.556 3.657 23.634 1.00 23.67 A C ANISOU 179 C MET A 29 2921 3217 2856 -93 412 193 A C ATOM 180 O MET A 29 8.382 2.480 23.942 1.00 24.72 A O ANISOU 180 O MET A 29 2890 3208 3294 -74 496 322 A O ATOM 181 CB MET A 29 7.834 5.225 25.421 1.00 26.43 A C ANISOU 181 CB MET A 29 3388 3610 3046 -251 412 -126 A C ATOM 182 CG MET A 29 8.792 6.386 25.489 1.00 27.62 A C ANISOU 182 CG MET A 29 3680 3819 2996 -263 472 -151 A C ATOM 183 SD MET A 29 8.811 7.070 27.157 1.00 24.41 A S ANISOU 183 SD MET A 29 2524 4205 2545 51 476 -164 A S ATOM 184 CE MET A 29 8.728 5.599 28.178 1.00 27.97 A C ANISOU 184 CE MET A 29 3824 3871 2933 -82 342 -346 A C ATOM 185 N THR A 30 9.627 4.077 22.969 1.00 22.04 A N ANISOU 185 N THR A 30 2903 2962 2511 87 285 98 A N ATOM 186 CA THR A 30 10.718 3.164 22.660 1.00 22.32 A C ANISOU 186 CA THR A 30 3181 2937 2362 285 172 -20 A C ATOM 187 C THR A 30 12.021 3.691 23.253 1.00 21.34 A C ANISOU 187 C THR A 30 3057 2872 2178 405 208 98 A C ATOM 188 O THR A 30 12.376 4.852 23.035 1.00 21.73 A O ANISOU 188 O THR A 30 3097 2870 2289 329 186 151 A O ATOM 189 CB THR A 30 10.868 3.013 21.130 1.00 22.88 A C ANISOU 189 CB THR A 30 3364 2955 2372 285 173 -172 A C ATOM 190 CG2 THR A 30 12.076 2.156 20.777 1.00 24.61 A C ANISOU 190 CG2 THR A 30 3689 3170 2492 476 252 -98 A C ATOM 191 OG1 THR A 30 9.693 2.409 20.575 1.00 24.99 A O ANISOU 191 OG1 THR A 30 3808 3129 2558 120 -30 -114 A O ATOM 192 N ARG A 31 12.725 2.841 23.995 1.00 22.39 A N ANISOU 192 N ARG A 31 3253 3086 2169 601 115 173 A N ATOM 193 CA ARG A 31 14.070 3.151 24.456 1.00 23.26 A C ANISOU 193 CA ARG A 31 3425 3262 2149 750 97 228 A C ATOM 194 C ARG A 31 15.027 2.913 23.294 1.00 23.42 A C ANISOU 194 C ARG A 31 3474 3176 2249 696 219 148 A C ATOM 195 O ARG A 31 15.159 1.796 22.799 1.00 24.53 A O ANISOU 195 O ARG A 31 3533 3224 2563 693 270 87 A O ATOM 196 CB ARG A 31 14.467 2.278 25.643 1.00 23.78 A C ANISOU 196 CB ARG A 31 3560 3359 2117 908 41 285 A C ATOM 197 CG ARG A 31 15.796 2.664 26.277 1.00 25.82 A C ANISOU 197 CG ARG A 31 4065 3607 2140 1018 -230 357 A C ATOM 198 CD ARG A 31 16.122 1.771 27.464 1.00 28.55 A C ANISOU 198 CD ARG A 31 4659 4029 2158 1544 -263 509 A C ATOM 199 NE ARG A 31 17.212 2.303 28.276 1.00 30.12 A N ANISOU 199 NE ARG A 31 4778 4629 2037 1902 -208 518 A N ATOM 200 CZ ARG A 31 17.817 1.627 29.259 1.00 31.37 A C ANISOU 200 CZ ARG A 31 4938 4863 2117 2178 -142 639 A C ATOM 201 NH1 ARG A 31 17.452 0.383 29.555 1.00 33.10 A N ANISOU 201 NH1 ARG A 31 5260 4902 2416 2274 -49 640 A N ATOM 202 NH2 ARG A 31 18.796 2.192 29.957 1.00 32.35 A N ANISOU 202 NH2 ARG A 31 4946 5156 2187 2318 -320 595 A N ATOM 203 N VAL A 32 15.695 3.970 22.848 1.00 23.60 A N ANISOU 203 N VAL A 32 3517 3237 2213 732 377 230 A N ATOM 204 CA VAL A 32 16.581 3.864 21.695 1.00 25.03 A C ANISOU 204 CA VAL A 32 3722 3420 2368 872 533 296 A C ATOM 205 C VAL A 32 18.026 3.629 22.123 1.00 24.78 A C ANISOU 205 C VAL A 32 3777 3407 2230 1115 467 228 A C ATOM 206 O VAL A 32 18.724 2.792 21.554 1.00 25.88 A O ANISOU 206 O VAL A 32 3989 3537 2308 1238 230 92 A O ATOM 207 CB VAL A 32 16.502 5.112 20.797 1.00 25.43 A C ANISOU 207 CB VAL A 32 3655 3522 2486 860 640 447 A C ATOM 208 CG1 VAL A 32 15.056 5.414 20.435 1.00 25.75 A C ANISOU 208 CG1 VAL A 32 3666 3571 2545 794 584 386 A C ATOM 209 CG2 VAL A 32 17.148 6.303 21.485 1.00 26.23 A C ANISOU 209 CG2 VAL A 32 3623 3736 2606 776 850 485 A C ATOM 210 N THR A 33 18.463 4.373 23.132 1.00 24.78 A N ANISOU 210 N THR A 33 3675 3578 2161 1400 406 261 A N ATOM 211 CA THR A 33 19.783 4.176 23.732 1.00 24.79 A C ANISOU 211 CA THR A 33 3512 3799 2108 1544 458 373 A C ATOM 212 C THR A 33 19.611 4.058 25.247 1.00 24.89 A C ANISOU 212 C THR A 33 3264 4070 2124 1597 443 329 A C ATOM 213 O THR A 33 18.477 3.965 25.743 1.00 25.48 A O ANISOU 213 O THR A 33 3194 4334 2152 1649 491 392 A O ATOM 214 CB THR A 33 20.755 5.333 23.401 1.00 24.72 A C ANISOU 214 CB THR A 33 3564 3747 2081 1532 472 331 A C ATOM 215 CG2 THR A 33 20.879 5.541 21.883 1.00 25.07 A C ANISOU 215 CG2 THR A 33 3542 3883 2099 1524 643 388 A C ATOM 216 OG1 THR A 33 20.293 6.536 24.029 1.00 24.91 A O ANISOU 216 OG1 THR A 33 3370 3901 2194 1562 427 170 A O ATOM 217 N ASN A 34 20.712 4.067 25.993 1.00 25.29 A N ANISOU 217 N ASN A 34 3079 4284 2247 1699 355 215 A N ATOM 218 CA ASN A 34 20.618 3.994 27.448 1.00 25.21 A C ANISOU 218 CA ASN A 34 2951 4323 2304 1676 161 137 A C ATOM 219 C ASN A 34 19.669 5.052 28.017 1.00 25.21 A C ANISOU 219 C ASN A 34 3032 4440 2107 1817 208 164 A C ATOM 220 O ASN A 34 18.836 4.745 28.875 1.00 25.96 A O ANISOU 220 O ASN A 34 3088 4571 2205 1875 315 219 A O ATOM 221 CB ASN A 34 21.984 4.106 28.120 1.00 25.64 A C ANISOU 221 CB ASN A 34 2854 4356 2531 1544 73 137 A C ATOM 222 CG ASN A 34 22.691 2.771 28.236 1.00 27.43 A C ANISOU 222 CG ASN A 34 2996 4313 3113 1221 -381 -10 A C ATOM 223 ND2 ASN A 34 23.714 2.724 29.077 1.00 29.63 A N ANISOU 223 ND2 ASN A 34 2912 4584 3763 939 -670 76 A N ATOM 224 OD1 ASN A 34 22.328 1.788 27.591 1.00 28.98 A O ANISOU 224 OD1 ASN A 34 2736 4383 3892 878 -461 -82 A O ATOM 225 N ASN A 35 19.790 6.287 27.531 1.00 24.07 A N ANISOU 225 N ASN A 35 2840 4383 1923 1858 -3 62 A N ATOM 226 CA ASN A 35 19.006 7.393 28.098 1.00 23.48 A C ANISOU 226 CA ASN A 35 2705 4408 1808 1771 -185 -35 A C ATOM 227 C ASN A 35 18.076 8.130 27.142 1.00 21.79 A C ANISOU 227 C ASN A 35 2462 4086 1729 1518 -203 -62 A C ATOM 228 O ASN A 35 17.318 9.001 27.590 1.00 22.34 A O ANISOU 228 O ASN A 35 2508 4189 1791 1562 -153 -76 A O ATOM 229 CB ASN A 35 19.922 8.419 28.761 1.00 24.36 A C ANISOU 229 CB ASN A 35 2752 4634 1869 1861 -307 -93 A C ATOM 230 CG ASN A 35 20.632 7.841 29.956 1.00 26.85 A C ANISOU 230 CG ASN A 35 2924 5213 2064 1973 -417 109 A C ATOM 231 ND2 ASN A 35 21.854 7.378 29.733 1.00 29.77 A N ANISOU 231 ND2 ASN A 35 3023 5651 2639 2073 -443 82 A N ATOM 232 OD1 ASN A 35 20.079 7.797 31.046 1.00 29.45 A O ANISOU 232 OD1 ASN A 35 3355 5658 2176 1976 -333 219 A O ATOM 233 N VAL A 36 18.146 7.795 25.858 1.00 19.70 A N ANISOU 233 N VAL A 36 2060 3756 1668 1216 -54 87 A N ATOM 234 CA VAL A 36 17.313 8.479 24.867 1.00 17.87 A C ANISOU 234 CA VAL A 36 1693 3416 1682 882 -17 159 A C ATOM 235 C VAL A 36 16.114 7.628 24.451 1.00 18.05 A C ANISOU 235 C VAL A 36 1764 3197 1897 803 136 152 A C ATOM 236 O VAL A 36 16.246 6.470 24.046 1.00 18.78 A O ANISOU 236 O VAL A 36 1932 3219 1985 877 137 148 A O ATOM 237 CB VAL A 36 18.128 8.923 23.629 1.00 17.75 A C ANISOU 237 CB VAL A 36 1579 3461 1703 772 -20 186 A C ATOM 238 CG1 VAL A 36 17.259 9.671 22.633 1.00 17.13 A C ANISOU 238 CG1 VAL A 36 1588 3323 1597 649 -193 197 A C ATOM 239 CG2 VAL A 36 19.300 9.803 24.049 1.00 17.65 A C ANISOU 239 CG2 VAL A 36 1172 3596 1939 758 -92 -31 A C ATOM 240 N TYR A 37 14.932 8.245 24.558 1.00 17.40 A N ANISOU 240 N TYR A 37 1588 3192 1832 736 120 68 A N ATOM 241 CA TYR A 37 13.660 7.583 24.264 1.00 17.61 A C ANISOU 241 CA TYR A 37 1747 3125 1817 522 186 6 A C ATOM 242 C TYR A 37 12.937 8.320 23.134 1.00 15.89 A C ANISOU 242 C TYR A 37 1488 2842 1708 408 175 -137 A C ATOM 243 O TYR A 37 13.147 9.522 22.934 1.00 15.68 A O ANISOU 243 O TYR A 37 1154 2854 1949 252 120 -109 A O ATOM 244 CB TYR A 37 12.766 7.535 25.518 1.00 18.45 A C ANISOU 244 CB TYR A 37 1939 3321 1752 524 229 76 A C ATOM 245 CG TYR A 37 13.310 6.665 26.635 1.00 20.62 A C ANISOU 245 CG TYR A 37 2468 3517 1851 680 401 197 A C ATOM 246 CD1 TYR A 37 12.720 5.447 26.961 1.00 22.65 A C ANISOU 246 CD1 TYR A 37 2946 3684 1975 706 489 337 A C ATOM 247 CD2 TYR A 37 14.425 7.060 27.375 1.00 21.91 A C ANISOU 247 CD2 TYR A 37 2655 3759 1912 847 344 241 A C ATOM 248 CE1 TYR A 37 13.225 4.643 27.987 1.00 24.00 A C ANISOU 248 CE1 TYR A 37 3248 3939 1932 847 471 417 A C ATOM 249 CE2 TYR A 37 14.944 6.269 28.395 1.00 23.67 A C ANISOU 249 CE2 TYR A 37 3129 3941 1923 957 535 476 A C ATOM 250 CZ TYR A 37 14.335 5.057 28.708 1.00 24.23 A C ANISOU 250 CZ TYR A 37 3336 3939 1932 970 482 480 A C ATOM 251 OH TYR A 37 14.843 4.257 29.721 1.00 26.78 A O ANISOU 251 OH TYR A 37 3729 4147 2298 1018 502 644 A O ATOM 252 N LEU A 38 12.106 7.575 22.398 1.00 15.76 A N ANISOU 252 N LEU A 38 1464 2698 1826 197 164 -98 A N ATOM 253 CA LEU A 38 11.323 8.114 21.275 1.00 15.83 A C ANISOU 253 CA LEU A 38 1333 2741 1941 164 172 -82 A C ATOM 254 C LEU A 38 9.834 7.890 21.541 1.00 15.88 A C ANISOU 254 C LEU A 38 1386 2583 2064 57 241 -108 A C ATOM 255 O LEU A 38 9.450 6.782 21.916 1.00 17.25 A O ANISOU 255 O LEU A 38 1630 2669 2257 98 388 -17 A O ATOM 256 CB LEU A 38 11.727 7.420 19.966 1.00 15.99 A C ANISOU 256 CB LEU A 38 1324 2777 1976 295 74 -82 A C ATOM 257 CG LEU A 38 10.886 7.673 18.702 1.00 14.71 A C ANISOU 257 CG LEU A 38 891 2791 1905 81 175 -71 A C ATOM 258 CD1 LEU A 38 10.781 9.143 18.343 1.00 15.69 A C ANISOU 258 CD1 LEU A 38 1080 2851 2029 195 395 49 A C ATOM 259 CD2 LEU A 38 11.474 6.877 17.540 1.00 15.78 A C ANISOU 259 CD2 LEU A 38 1221 2748 2027 175 436 -131 A C ATOM 260 N GLY A 39 9.018 8.924 21.343 1.00 15.65 A N ANISOU 260 N GLY A 39 1158 2671 2116 -31 331 -73 A N ATOM 261 CA GLY A 39 7.616 8.850 21.725 1.00 16.64 A C ANISOU 261 CA GLY A 39 1208 2867 2247 -115 461 -68 A C ATOM 262 C GLY A 39 6.701 9.784 20.963 1.00 15.71 A C ANISOU 262 C GLY A 39 1009 2842 2117 -296 505 -175 A C ATOM 263 O GLY A 39 7.149 10.631 20.186 1.00 15.60 A O ANISOU 263 O GLY A 39 956 2973 2000 -175 529 -162 A O ATOM 264 N ASN A 40 5.401 9.613 21.201 1.00 16.29 A N ANISOU 264 N ASN A 40 895 3111 2185 -355 612 -388 A N ATOM 265 CA ASN A 40 4.389 10.498 20.658 1.00 16.59 A C ANISOU 265 CA ASN A 40 781 3312 2212 -472 706 -458 A C ATOM 266 C ASN A 40 3.883 11.458 21.745 1.00 16.94 A C ANISOU 266 C ASN A 40 787 3429 2222 -307 723 -408 A C ATOM 267 O ASN A 40 4.439 11.541 22.852 1.00 17.08 A O ANISOU 267 O ASN A 40 876 3470 2143 -359 710 -458 A O ATOM 268 CB ASN A 40 3.257 9.672 20.040 1.00 17.02 A C ANISOU 268 CB ASN A 40 856 3422 2187 -599 709 -419 A C ATOM 269 CG ASN A 40 2.533 8.825 21.069 1.00 18.37 A C ANISOU 269 CG ASN A 40 1061 3679 2240 -788 863 -375 A C ATOM 270 ND2 ASN A 40 1.724 7.897 20.571 1.00 21.96 A N ANISOU 270 ND2 ASN A 40 1622 3964 2759 -1168 710 -203 A N ATOM 271 OD1 ASN A 40 2.685 9.005 22.284 1.00 20.29 A O ANISOU 271 OD1 ASN A 40 1365 4065 2280 -710 798 -193 A O ATOM 272 N TYR A 41 2.829 12.203 21.432 1.00 17.21 A N ANISOU 272 N TYR A 41 619 3558 2362 -237 842 -274 A N ATOM 273 CA ATYR A 41 2.318 13.197 22.369 0.50 18.26 A C ANISOU 273 CA ATYR A 41 867 3698 2372 -60 812 -186 A C ATOM 274 CA BTYR A 41 2.309 13.199 22.361 0.50 18.24 A C ANISOU 274 CA BTYR A 41 900 3677 2354 -62 790 -197 A C ATOM 275 C TYR A 41 1.783 12.576 23.659 1.00 18.55 A C ANISOU 275 C TYR A 41 996 3698 2354 -241 834 -208 A C ATOM 276 O TYR A 41 2.062 13.069 24.758 1.00 18.17 A O ANISOU 276 O TYR A 41 725 3799 2380 -285 834 -258 A O ATOM 277 CB ATYR A 41 1.249 14.085 21.720 0.50 19.19 A C ANISOU 277 CB ATYR A 41 970 3873 2449 91 768 -174 A C ATOM 278 CB BTYR A 41 1.225 14.032 21.676 0.50 19.14 A C ANISOU 278 CB BTYR A 41 1014 3817 2442 97 715 -215 A C ATOM 279 CG ATYR A 41 1.065 15.382 22.469 0.50 20.88 A C ANISOU 279 CG ATYR A 41 1217 4124 2594 421 516 -241 A C ATOM 280 CG BTYR A 41 0.408 14.879 22.612 0.50 20.72 A C ANISOU 280 CG BTYR A 41 1243 4174 2453 460 597 -296 A C ATOM 281 CD1ATYR A 41 2.043 16.372 22.427 0.50 24.43 A C ANISOU 281 CD1ATYR A 41 1956 4415 2910 252 524 -381 A C ATOM 282 CD1BTYR A 41 0.869 16.118 23.045 0.50 23.02 A C ANISOU 282 CD1BTYR A 41 1588 4359 2799 649 644 -428 A C ATOM 283 CD2ATYR A 41 -0.070 15.613 23.237 0.50 23.74 A C ANISOU 283 CD2ATYR A 41 1720 4458 2842 533 544 -421 A C ATOM 284 CD2BTYR A 41 -0.841 14.448 23.051 0.50 22.46 A C ANISOU 284 CD2BTYR A 41 1377 4487 2671 595 737 -386 A C ATOM 285 CE1ATYR A 41 1.887 17.558 23.122 0.50 26.41 A C ANISOU 285 CE1ATYR A 41 2152 4620 3264 182 671 -597 A C ATOM 286 CE1BTYR A 41 0.110 16.906 23.902 0.50 24.32 A C ANISOU 286 CE1BTYR A 41 1641 4386 3212 816 929 -467 A C ATOM 287 CE2ATYR A 41 -0.234 16.800 23.934 0.50 25.83 A C ANISOU 287 CE2ATYR A 41 1941 4566 3307 450 608 -601 A C ATOM 288 CE2BTYR A 41 -1.601 15.225 23.912 0.50 23.59 A C ANISOU 288 CE2BTYR A 41 1492 4426 3046 864 983 -403 A C ATOM 289 CZ ATYR A 41 0.748 17.770 23.870 0.50 27.41 A C ANISOU 289 CZ ATYR A 41 2202 4706 3508 280 723 -684 A C ATOM 290 CZ BTYR A 41 -1.127 16.453 24.334 0.50 25.09 A C ANISOU 290 CZ BTYR A 41 1791 4347 3395 900 1093 -381 A C ATOM 291 OH ATYR A 41 0.591 18.944 24.564 0.50 29.19 A O ANISOU 291 OH ATYR A 41 2313 4813 3962 118 728 -829 A O ATOM 292 OH BTYR A 41 -1.887 17.223 25.190 0.50 25.88 A O ANISOU 292 OH BTYR A 41 1993 4142 3698 988 1421 -318 A O ATOM 293 N LYS A 42 1.020 11.495 23.541 1.00 19.06 A N ANISOU 293 N LYS A 42 1042 3758 2442 -489 806 -247 A N ATOM 294 CA LYS A 42 0.528 10.800 24.734 1.00 20.22 A C ANISOU 294 CA LYS A 42 1386 3831 2467 -790 891 -386 A C ATOM 295 C LYS A 42 1.678 10.362 25.634 1.00 19.20 A C ANISOU 295 C LYS A 42 1500 3607 2187 -652 926 -364 A C ATOM 296 O LYS A 42 1.616 10.499 26.857 1.00 20.16 A O ANISOU 296 O LYS A 42 1404 4027 2228 -740 961 -392 A O ATOM 297 CB LYS A 42 -0.330 9.591 24.334 1.00 21.89 A C ANISOU 297 CB LYS A 42 1571 3894 2854 -929 850 -401 A C ATOM 298 CG LYS A 42 -0.797 8.743 25.523 1.00 26.76 A C ANISOU 298 CG LYS A 42 2311 4259 3596 -1500 1032 -427 A C ATOM 299 CD LYS A 42 -2.112 8.040 25.246 1.00 34.34 A C ANISOU 299 CD LYS A 42 3316 5109 4623 -2166 1190 -491 A C ATOM 300 CE LYS A 42 -2.525 7.166 26.421 1.00 36.89 A C ANISOU 300 CE LYS A 42 3702 5353 4960 -2483 1238 -489 A C ATOM 301 NZ LYS A 42 -2.532 7.883 27.734 1.00 37.59 A N ANISOU 301 NZ LYS A 42 3603 5648 5030 -2469 1360 -511 A N ATOM 302 N ASN A 43 2.755 9.855 25.023 1.00 18.59 A N ANISOU 302 N ASN A 43 1623 3425 2017 -467 930 -230 A N ATOM 303 CA ASN A 43 3.910 9.452 25.807 1.00 18.14 A C ANISOU 303 CA ASN A 43 1788 3095 2010 -348 873 -219 A C ATOM 304 C ASN A 43 4.485 10.651 26.576 1.00 17.43 A C ANISOU 304 C ASN A 43 1743 3000 1879 -320 860 -164 A C ATOM 305 O ASN A 43 4.966 10.500 27.711 1.00 18.63 A O ANISOU 305 O ASN A 43 1851 3233 1993 -353 715 -63 A O ATOM 306 CB ASN A 43 5.006 8.845 24.918 1.00 18.46 A C ANISOU 306 CB ASN A 43 1949 3088 1976 -320 921 -263 A C ATOM 307 CG ASN A 43 4.577 7.588 24.166 1.00 19.82 A C ANISOU 307 CG ASN A 43 2132 3059 2338 -471 1076 -241 A C ATOM 308 ND2 ASN A 43 5.230 7.357 23.043 1.00 21.05 A N ANISOU 308 ND2 ASN A 43 2806 3032 2161 -509 1216 -317 A N ATOM 309 OD1 ASN A 43 3.698 6.814 24.590 1.00 23.49 A O ANISOU 309 OD1 ASN A 43 2721 3422 2782 -834 1289 -175 A O ATOM 310 N ALA A 44 4.440 11.841 25.959 1.00 16.59 A N ANISOU 310 N ALA A 44 1263 2978 2064 -206 854 -203 A N ATOM 311 CA ALA A 44 4.961 13.040 26.648 1.00 16.89 A C ANISOU 311 CA ALA A 44 1262 2996 2161 -161 876 -274 A C ATOM 312 C ALA A 44 4.076 13.386 27.849 1.00 17.61 A C ANISOU 312 C ALA A 44 1084 3368 2240 -274 886 -467 A C ATOM 313 O ALA A 44 4.560 13.723 28.939 1.00 18.47 A O ANISOU 313 O ALA A 44 1168 3576 2273 -322 820 -469 A O ATOM 314 CB ALA A 44 5.056 14.211 25.693 1.00 16.99 A C ANISOU 314 CB ALA A 44 1206 2935 2316 -35 693 -184 A C ATOM 315 N MET A 45 2.765 13.301 27.647 1.00 18.92 A N ANISOU 315 N MET A 45 1124 3740 2325 -372 1032 -568 A N ATOM 316 CA MET A 45 1.820 13.582 28.734 1.00 20.47 A C ANISOU 316 CA MET A 45 1253 4149 2374 -366 1039 -610 A C ATOM 317 C MET A 45 1.975 12.598 29.893 1.00 21.18 A C ANISOU 317 C MET A 45 1553 4129 2365 -493 1128 -577 A C ATOM 318 O MET A 45 1.778 12.966 31.048 1.00 22.17 A O ANISOU 318 O MET A 45 1712 4262 2450 -564 1212 -630 A O ATOM 319 CB MET A 45 0.385 13.598 28.201 1.00 21.53 A C ANISOU 319 CB MET A 45 1289 4415 2477 -348 951 -666 A C ATOM 320 CG MET A 45 0.104 14.683 27.167 1.00 21.67 A C ANISOU 320 CG MET A 45 775 4620 2838 -388 693 -612 A C ATOM 321 SD MET A 45 0.587 16.361 27.598 1.00 26.38 A S ANISOU 321 SD MET A 45 1492 4747 3783 282 597 -934 A S ATOM 322 CE MET A 45 2.169 16.532 26.750 1.00 25.37 A C ANISOU 322 CE MET A 45 1133 4424 4083 -140 432 -671 A C ATOM 323 N ASP A 46 2.352 11.361 29.570 1.00 21.77 A N ANISOU 323 N ASP A 46 1897 3968 2406 -749 1186 -452 A N ATOM 324 CA ASP A 46 2.556 10.312 30.567 1.00 22.83 A C ANISOU 324 CA ASP A 46 2150 4054 2469 -869 1199 -274 A C ATOM 325 C ASP A 46 3.967 10.279 31.139 1.00 23.32 A C ANISOU 325 C ASP A 46 2293 3973 2592 -842 1067 -182 A C ATOM 326 O ASP A 46 4.257 9.492 32.050 1.00 24.36 A O ANISOU 326 O ASP A 46 2329 4241 2685 -903 1023 -113 A O ATOM 327 CB ASP A 46 2.222 8.940 29.969 1.00 23.87 A C ANISOU 327 CB ASP A 46 2398 4072 2599 -948 1186 -197 A C ATOM 328 CG ASP A 46 0.752 8.796 29.631 1.00 25.17 A C ANISOU 328 CG ASP A 46 2381 4645 2538 -1164 1412 -342 A C ATOM 329 OD1 ASP A 46 -0.068 9.513 30.247 1.00 29.86 A O ANISOU 329 OD1 ASP A 46 2763 5508 3075 -1127 1576 -505 A O ATOM 330 OD2 ASP A 46 0.415 7.978 28.743 1.00 26.57 A O ANISOU 330 OD2 ASP A 46 2529 4702 2865 -1286 1324 -355 A O ATOM 331 N ALA A 47 4.831 11.146 30.622 1.00 22.61 A N ANISOU 331 N ALA A 47 2221 3984 2386 -781 986 -197 A N ATOM 332 CA ALA A 47 6.226 11.200 31.042 1.00 22.15 A C ANISOU 332 CA ALA A 47 2310 3885 2222 -595 913 -109 A C ATOM 333 C ALA A 47 6.403 11.304 32.559 1.00 23.00 A C ANISOU 333 C ALA A 47 2698 3880 2161 -502 850 -118 A C ATOM 334 O ALA A 47 7.154 10.526 33.142 1.00 23.48 A O ANISOU 334 O ALA A 47 2718 4002 2203 -392 878 -82 A O ATOM 335 CB ALA A 47 6.971 12.326 30.330 1.00 22.10 A C ANISOU 335 CB ALA A 47 2230 3901 2266 -615 776 10 A C ATOM 336 N PRO A 48 5.718 12.257 33.207 1.00 24.16 A N ANISOU 336 N PRO A 48 2971 4065 2143 -375 860 -227 A N ATOM 337 CA PRO A 48 5.928 12.421 34.655 1.00 25.88 A C ANISOU 337 CA PRO A 48 3431 4237 2167 -163 882 -230 A C ATOM 338 C PRO A 48 5.686 11.160 35.496 1.00 27.51 A C ANISOU 338 C PRO A 48 3795 4402 2257 120 996 -38 A C ATOM 339 O PRO A 48 6.316 10.990 36.547 1.00 28.55 A O ANISOU 339 O PRO A 48 3943 4666 2240 204 974 -35 A O ATOM 340 CB PRO A 48 4.924 13.524 35.024 1.00 25.82 A C ANISOU 340 CB PRO A 48 3433 4203 2175 -197 895 -274 A C ATOM 341 CG PRO A 48 4.807 14.326 33.746 1.00 25.01 A C ANISOU 341 CG PRO A 48 3249 4144 2108 -351 763 -359 A C ATOM 342 CD PRO A 48 4.773 13.264 32.685 1.00 24.06 A C ANISOU 342 CD PRO A 48 3009 3930 2201 -436 776 -285 A C ATOM 343 N SER A 49 4.813 10.266 35.034 1.00 27.83 A N ANISOU 343 N SER A 49 3759 4327 2489 263 1190 216 A N ATOM 344 CA ASER A 49 4.483 9.049 35.777 0.50 28.62 A C ANISOU 344 CA ASER A 49 3957 4347 2572 285 1305 320 A C ATOM 345 CA BSER A 49 4.461 9.048 35.763 0.50 28.79 A C ANISOU 345 CA BSER A 49 3905 4347 2685 305 1208 438 A C ATOM 346 C SER A 49 5.167 7.794 35.242 1.00 28.90 A C ANISOU 346 C SER A 49 4117 4298 2567 302 1342 436 A C ATOM 347 O SER A 49 4.951 6.686 35.759 1.00 28.92 A O ANISOU 347 O SER A 49 4052 4287 2651 261 1404 449 A O ATOM 348 CB ASER A 49 2.971 8.824 35.803 0.50 28.69 A C ANISOU 348 CB ASER A 49 3901 4314 2687 263 1324 361 A C ATOM 349 CB BSER A 49 2.945 8.853 35.708 0.50 29.08 A C ANISOU 349 CB BSER A 49 3822 4379 2849 274 1208 511 A C ATOM 350 OG ASER A 49 2.346 9.783 36.633 0.50 29.61 A O ANISOU 350 OG ASER A 49 3853 4623 2773 219 1366 205 A O ATOM 351 OG BSER A 49 2.565 7.633 36.313 0.50 30.66 A O ANISOU 351 OG BSER A 49 3919 4474 3257 247 917 700 A O ATOM 352 N SER A 50 5.994 7.983 34.215 1.00 29.64 A N ANISOU 352 N SER A 50 4462 4329 2469 206 1491 368 A N ATOM 353 CA SER A 50 6.733 6.889 33.599 1.00 30.90 A C ANISOU 353 CA SER A 50 4708 4462 2569 208 1289 386 A C ATOM 354 C SER A 50 7.679 6.160 34.547 1.00 32.23 A C ANISOU 354 C SER A 50 4942 4535 2768 54 1171 592 A C ATOM 355 O SER A 50 8.201 6.747 35.494 1.00 32.55 A O ANISOU 355 O SER A 50 4787 4738 2842 73 1168 568 A O ATOM 356 CB SER A 50 7.592 7.432 32.447 1.00 29.90 A C ANISOU 356 CB SER A 50 4625 4417 2319 296 1365 313 A C ATOM 357 OG SER A 50 8.520 6.459 32.001 1.00 31.06 A O ANISOU 357 OG SER A 50 4539 4674 2590 434 1111 370 A O ATOM 358 N GLU A 51 7.907 4.878 34.262 1.00 34.10 A N ANISOU 358 N GLU A 51 5278 4375 3303 -171 744 882 A N ATOM 359 CA GLU A 51 8.893 4.072 34.983 1.00 35.15 A C ANISOU 359 CA GLU A 51 5605 4329 3420 -241 548 1096 A C ATOM 360 C GLU A 51 10.280 4.721 34.903 1.00 33.70 A C ANISOU 360 C GLU A 51 5375 4401 3030 -65 509 1146 A C ATOM 361 O GLU A 51 11.125 4.517 35.782 1.00 34.43 A O ANISOU 361 O GLU A 51 5493 4638 2949 -93 423 1199 A O ATOM 362 CB GLU A 51 8.938 2.649 34.423 1.00 36.14 A C ANISOU 362 CB GLU A 51 5849 4223 3659 -353 540 1168 A C ATOM 363 CG GLU A 51 7.623 1.888 34.559 1.00 39.64 A C ANISOU 363 CG GLU A 51 6452 4426 4185 -555 623 1031 A C ATOM 364 CD GLU A 51 7.346 1.498 35.995 1.00 43.57 A C ANISOU 364 CD GLU A 51 7099 4767 4690 -754 1014 979 A C ATOM 365 OE1 GLU A 51 6.515 2.162 36.653 1.00 45.67 A O ANISOU 365 OE1 GLU A 51 7257 5077 5019 -768 1074 803 A O ATOM 366 OE2 GLU A 51 7.977 0.524 36.468 1.00 45.62 A O ANISOU 366 OE2 GLU A 51 7529 5041 4765 -619 1092 1053 A O ATOM 367 N VAL A 52 10.486 5.496 33.846 1.00 31.35 A N ANISOU 367 N VAL A 52 4924 4345 2642 337 653 925 A N ATOM 368 CA VAL A 52 11.722 6.227 33.593 1.00 30.26 A C ANISOU 368 CA VAL A 52 4706 4305 2486 529 610 767 A C ATOM 369 C VAL A 52 11.668 7.595 34.259 1.00 31.01 A C ANISOU 369 C VAL A 52 4881 4541 2361 494 384 666 A C ATOM 370 O VAL A 52 10.680 8.317 34.106 1.00 31.45 A O ANISOU 370 O VAL A 52 4913 4553 2484 540 399 571 A O ATOM 371 CB VAL A 52 11.942 6.416 32.071 1.00 29.32 A C ANISOU 371 CB VAL A 52 4474 4277 2390 606 759 662 A C ATOM 372 CG1 VAL A 52 13.241 7.160 31.777 1.00 28.96 A C ANISOU 372 CG1 VAL A 52 4248 4239 2515 644 825 696 A C ATOM 373 CG2 VAL A 52 11.917 5.070 31.360 1.00 30.35 A C ANISOU 373 CG2 VAL A 52 4596 4239 2696 662 623 584 A C ATOM 374 N LYS A 53 12.720 7.952 34.991 1.00 32.74 A N ANISOU 374 N LYS A 53 5141 4845 2453 350 -54 772 A N ATOM 375 CA LYS A 53 12.800 9.283 35.610 1.00 33.63 A C ANISOU 375 CA LYS A 53 5138 5134 2504 261 -450 758 A C ATOM 376 C LYS A 53 13.408 10.310 34.651 1.00 29.46 A C ANISOU 376 C LYS A 53 4250 4758 2187 423 -230 505 A C ATOM 377 O LYS A 53 14.600 10.606 34.707 1.00 29.49 A O ANISOU 377 O LYS A 53 4099 4917 2187 573 -274 425 A O ATOM 378 CB LYS A 53 13.576 9.244 36.940 1.00 36.36 A C ANISOU 378 CB LYS A 53 5647 5483 2685 186 -658 908 A C ATOM 379 CG LYS A 53 14.676 8.177 37.070 1.00 42.95 A C ANISOU 379 CG LYS A 53 6121 6704 3495 227 -1058 895 A C ATOM 380 CD LYS A 53 15.928 8.465 36.240 1.00 49.58 A C ANISOU 380 CD LYS A 53 6603 8191 4045 428 -1154 732 A C ATOM 381 CE LYS A 53 17.036 7.462 36.528 1.00 51.67 A C ANISOU 381 CE LYS A 53 6664 8790 4178 516 -1181 544 A C ATOM 382 NZ LYS A 53 18.236 7.688 35.670 1.00 52.59 A N ANISOU 382 NZ LYS A 53 6751 9114 4117 507 -1212 509 A N ATOM 383 N PHE A 54 12.587 10.870 33.768 1.00 24.67 A N ANISOU 383 N PHE A 54 3258 4237 1878 379 -10 137 A N ATOM 384 CA PHE A 54 13.109 11.819 32.777 1.00 21.19 A C ANISOU 384 CA PHE A 54 2381 3941 1728 328 76 -120 A C ATOM 385 C PHE A 54 13.603 13.106 33.417 1.00 20.72 A C ANISOU 385 C PHE A 54 2034 4041 1797 340 107 -304 A C ATOM 386 O PHE A 54 12.924 13.681 34.286 1.00 21.90 A O ANISOU 386 O PHE A 54 2117 4131 2073 406 153 -410 A O ATOM 387 CB PHE A 54 12.036 12.167 31.737 1.00 19.93 A C ANISOU 387 CB PHE A 54 2148 3740 1684 346 153 -141 A C ATOM 388 CG PHE A 54 11.725 11.013 30.836 1.00 19.62 A C ANISOU 388 CG PHE A 54 2184 3537 1735 285 153 -87 A C ATOM 389 CD1 PHE A 54 12.622 10.648 29.841 1.00 19.09 A C ANISOU 389 CD1 PHE A 54 2336 3269 1648 482 305 40 A C ATOM 390 CD2 PHE A 54 10.553 10.285 30.979 1.00 20.12 A C ANISOU 390 CD2 PHE A 54 2380 3404 1861 207 419 -31 A C ATOM 391 CE1 PHE A 54 12.347 9.570 29.006 1.00 20.27 A C ANISOU 391 CE1 PHE A 54 2354 3400 1949 399 366 -62 A C ATOM 392 CE2 PHE A 54 10.263 9.212 30.150 1.00 20.71 A C ANISOU 392 CE2 PHE A 54 2511 3366 1993 63 507 -37 A C ATOM 393 CZ PHE A 54 11.164 8.850 29.150 1.00 21.72 A C ANISOU 393 CZ PHE A 54 2842 3355 2055 137 562 0 A C ATOM 394 N LYS A 55 14.773 13.557 32.970 1.00 20.09 A N ANISOU 394 N LYS A 55 1738 4126 1770 370 -70 -282 A N ATOM 395 CA LYS A 55 15.242 14.898 33.297 1.00 19.99 A C ANISOU 395 CA LYS A 55 1500 4235 1861 272 -252 -296 A C ATOM 396 C LYS A 55 14.719 15.891 32.261 1.00 18.40 A C ANISOU 396 C LYS A 55 1189 4038 1764 293 -197 -333 A C ATOM 397 O LYS A 55 14.354 17.030 32.598 1.00 18.95 A O ANISOU 397 O LYS A 55 1164 4104 1932 241 -31 -438 A O ATOM 398 CB LYS A 55 16.772 14.965 33.378 1.00 20.97 A C ANISOU 398 CB LYS A 55 1527 4336 2106 315 -326 -285 A C ATOM 399 CG LYS A 55 17.284 16.355 33.729 1.00 23.84 A C ANISOU 399 CG LYS A 55 1737 4717 2606 109 -582 -417 A C ATOM 400 CD LYS A 55 18.752 16.374 34.121 1.00 27.22 A C ANISOU 400 CD LYS A 55 1773 5044 3524 31 -678 -662 A C ATOM 401 CE LYS A 55 19.153 17.785 34.533 1.00 29.92 A C ANISOU 401 CE LYS A 55 1817 5292 4259 -285 -684 -794 A C ATOM 402 NZ LYS A 55 20.544 17.822 35.076 1.00 33.20 A N ANISOU 402 NZ LYS A 55 2319 5572 4722 -197 -750 -974 A N ATOM 403 N TYR A 56 14.669 15.444 31.008 1.00 17.19 A N ANISOU 403 N TYR A 56 981 3874 1676 148 -141 -230 A N ATOM 404 CA TYR A 56 14.303 16.300 29.890 1.00 16.24 A C ANISOU 404 CA TYR A 56 770 3664 1738 131 -71 -262 A C ATOM 405 C TYR A 56 13.226 15.666 29.028 1.00 15.16 A C ANISOU 405 C TYR A 56 664 3334 1761 219 -98 -259 A C ATOM 406 O TYR A 56 13.153 14.442 28.909 1.00 16.05 A O ANISOU 406 O TYR A 56 847 3258 1993 263 -125 -175 A O ATOM 407 CB TYR A 56 15.520 16.540 28.995 1.00 16.38 A C ANISOU 407 CB TYR A 56 585 3869 1770 92 6 -285 A C ATOM 408 CG TYR A 56 16.623 17.357 29.625 1.00 17.51 A C ANISOU 408 CG TYR A 56 675 4110 1867 70 -6 -511 A C ATOM 409 CD1 TYR A 56 16.473 18.727 29.822 1.00 18.87 A C ANISOU 409 CD1 TYR A 56 833 4320 2017 97 57 -820 A C ATOM 410 CD2 TYR A 56 17.820 16.767 29.998 1.00 19.48 A C ANISOU 410 CD2 TYR A 56 1084 4316 2002 195 -207 -544 A C ATOM 411 CE1 TYR A 56 17.471 19.485 30.395 1.00 20.50 A C ANISOU 411 CE1 TYR A 56 1075 4435 2280 109 -65 -750 A C ATOM 412 CE2 TYR A 56 18.826 17.516 30.564 1.00 20.02 A C ANISOU 412 CE2 TYR A 56 971 4528 2108 -35 -131 -820 A C ATOM 413 CZ TYR A 56 18.653 18.874 30.753 1.00 20.72 A C ANISOU 413 CZ TYR A 56 863 4623 2386 107 -141 -825 A C ATOM 414 OH TYR A 56 19.667 19.617 31.315 1.00 23.83 A O ANISOU 414 OH TYR A 56 1324 4949 2779 -252 -307 -746 A O ATOM 415 N VAL A 57 12.400 16.517 28.422 1.00 15.04 A N ANISOU 415 N VAL A 57 604 3269 1843 263 -93 -344 A N ATOM 416 CA VAL A 57 11.561 16.144 27.281 1.00 14.89 A C ANISOU 416 CA VAL A 57 623 3264 1771 109 -5 -302 A C ATOM 417 C VAL A 57 11.859 17.145 26.157 1.00 14.16 A C ANISOU 417 C VAL A 57 482 3125 1773 -23 43 -370 A C ATOM 418 O VAL A 57 11.823 18.373 26.398 1.00 15.59 A O ANISOU 418 O VAL A 57 759 3190 1976 -87 35 -395 A O ATOM 419 CB VAL A 57 10.062 16.165 27.662 1.00 15.50 A C ANISOU 419 CB VAL A 57 705 3336 1849 -3 31 -274 A C ATOM 420 CG1 VAL A 57 9.175 16.008 26.421 1.00 16.66 A C ANISOU 420 CG1 VAL A 57 498 3804 2029 313 49 -392 A C ATOM 421 CG2 VAL A 57 9.749 15.047 28.638 1.00 16.87 A C ANISOU 421 CG2 VAL A 57 1123 3289 1999 -70 219 -205 A C ATOM 422 N LEU A 58 12.158 16.612 24.966 1.00 13.51 A N ANISOU 422 N LEU A 58 426 2969 1738 -15 6 -280 A N ATOM 423 CA LEU A 58 12.355 17.447 23.801 1.00 13.34 A C ANISOU 423 CA LEU A 58 260 2998 1808 88 65 -230 A C ATOM 424 C LEU A 58 11.042 17.431 22.993 1.00 12.88 A C ANISOU 424 C LEU A 58 263 2883 1747 52 112 -210 A C ATOM 425 O LEU A 58 10.702 16.444 22.356 1.00 13.17 A O ANISOU 425 O LEU A 58 269 2880 1853 0 160 -240 A O ATOM 426 CB LEU A 58 13.550 16.932 22.981 1.00 14.47 A C ANISOU 426 CB LEU A 58 306 3172 2020 113 162 -283 A C ATOM 427 CG LEU A 58 13.865 17.721 21.731 1.00 16.30 A C ANISOU 427 CG LEU A 58 307 3503 2381 194 295 -60 A C ATOM 428 CD1 LEU A 58 14.176 19.165 22.074 1.00 20.08 A C ANISOU 428 CD1 LEU A 58 1246 3709 2673 252 599 -97 A C ATOM 429 CD2 LEU A 58 15.092 17.060 21.074 1.00 19.02 A C ANISOU 429 CD2 LEU A 58 421 4025 2779 296 606 38 A C ATOM 430 N ASN A 59 10.344 18.555 23.078 1.00 13.42 A N ANISOU 430 N ASN A 59 269 2935 1896 74 148 -54 A N ATOM 431 CA ASN A 59 9.053 18.750 22.429 1.00 13.06 A C ANISOU 431 CA ASN A 59 281 2944 1738 92 186 -118 A C ATOM 432 C ASN A 59 9.293 19.376 21.052 1.00 12.83 A C ANISOU 432 C ASN A 59 286 2754 1835 105 210 -74 A C ATOM 433 O ASN A 59 9.641 20.548 20.957 1.00 13.51 A O ANISOU 433 O ASN A 59 306 2795 2034 93 294 -43 A O ATOM 434 CB ASN A 59 8.207 19.687 23.289 1.00 13.61 A C ANISOU 434 CB ASN A 59 281 3025 1863 172 148 -215 A C ATOM 435 CG ASN A 59 6.924 20.139 22.593 1.00 13.59 A C ANISOU 435 CG ASN A 59 346 3124 1692 252 306 -125 A C ATOM 436 ND2 ASN A 59 6.388 21.267 23.040 1.00 15.20 A N ANISOU 436 ND2 ASN A 59 410 3055 2310 76 555 -204 A N ATOM 437 OD1 ASN A 59 6.456 19.491 21.650 1.00 14.91 A O ANISOU 437 OD1 ASN A 59 377 3402 1888 217 401 -249 A O ATOM 438 N LEU A 60 9.076 18.578 20.012 1.00 13.22 A N ANISOU 438 N LEU A 60 276 2991 1755 57 175 -126 A N ATOM 439 CA LEU A 60 9.279 19.005 18.636 1.00 14.22 A C ANISOU 439 CA LEU A 60 284 3124 1995 283 48 -206 A C ATOM 440 C LEU A 60 7.978 19.475 17.990 1.00 14.55 A C ANISOU 440 C LEU A 60 302 3269 1958 353 98 -92 A C ATOM 441 O LEU A 60 7.965 19.838 16.815 1.00 14.86 A O ANISOU 441 O LEU A 60 289 3346 2011 285 109 -118 A O ATOM 442 CB LEU A 60 9.864 17.858 17.807 1.00 14.16 A C ANISOU 442 CB LEU A 60 298 3025 2055 349 26 -170 A C ATOM 443 CG LEU A 60 11.384 17.697 17.741 1.00 20.88 A C ANISOU 443 CG LEU A 60 593 3483 3858 417 -31 -715 A C ATOM 444 CD1 LEU A 60 12.085 18.546 18.787 1.00 19.64 A C ANISOU 444 CD1 LEU A 60 483 3379 3600 571 -206 -586 A C ATOM 445 CD2 LEU A 60 11.767 16.233 17.879 1.00 19.00 A C ANISOU 445 CD2 LEU A 60 408 3424 3388 623 -54 -803 A C ATOM 446 N THR A 61 6.882 19.463 18.745 1.00 15.20 A N ANISOU 446 N THR A 61 344 3194 2238 423 219 -142 A N ATOM 447 CA THR A 61 5.604 19.940 18.191 1.00 16.25 A C ANISOU 447 CA THR A 61 357 3416 2401 502 226 0 A C ATOM 448 C THR A 61 5.564 21.461 18.216 1.00 16.50 A C ANISOU 448 C THR A 61 386 3418 2465 582 238 15 A C ATOM 449 O THR A 61 6.392 22.110 18.869 1.00 17.13 A O ANISOU 449 O THR A 61 337 3452 2720 493 148 68 A O ATOM 450 CB THR A 61 4.365 19.400 18.955 1.00 16.31 A C ANISOU 450 CB THR A 61 313 3459 2423 393 149 -63 A C ATOM 451 CG2 THR A 61 4.439 17.899 19.121 1.00 16.82 A C ANISOU 451 CG2 THR A 61 315 3479 2596 446 23 -11 A C ATOM 452 OG1 THR A 61 4.255 20.051 20.229 1.00 17.05 A O ANISOU 452 OG1 THR A 61 296 3612 2569 266 216 -119 A O ATOM 453 N MET A 62 4.550 22.048 17.572 1.00 17.17 A N ANISOU 453 N MET A 62 456 3503 2565 762 263 109 A N ATOM 454 CA MET A 62 4.501 23.505 17.496 1.00 18.33 A C ANISOU 454 CA MET A 62 611 3671 2682 854 284 68 A C ATOM 455 C MET A 62 4.006 24.157 18.790 1.00 19.51 A C ANISOU 455 C MET A 62 886 3731 2795 917 377 31 A C ATOM 456 O MET A 62 4.286 25.331 19.035 1.00 21.58 A O ANISOU 456 O MET A 62 1360 3770 3070 816 524 -65 A O ATOM 457 CB MET A 62 3.626 23.964 16.318 1.00 18.54 A C ANISOU 457 CB MET A 62 531 3797 2718 974 186 126 A C ATOM 458 CG MET A 62 4.263 23.666 14.975 1.00 19.83 A C ANISOU 458 CG MET A 62 746 3955 2833 833 119 37 A C ATOM 459 SD MET A 62 5.766 24.624 14.686 1.00 21.54 A S ANISOU 459 SD MET A 62 741 4246 3197 680 153 260 A S ATOM 460 CE MET A 62 5.055 26.247 14.367 1.00 24.35 A C ANISOU 460 CE MET A 62 855 4336 4059 675 417 163 A C ATOM 461 N AASP A 63 3.285 23.403 19.620 0.50 19.66 A N ANISOU 461 N AASP A 63 759 3975 2736 834 472 38 A N ATOM 462 N BASP A 63 3.327 23.402 19.639 0.50 19.66 A N ANISOU 462 N BASP A 63 758 3975 2736 834 472 38 A N ATOM 463 CA AASP A 63 2.675 23.958 20.839 0.50 20.18 A C ANISOU 463 CA AASP A 63 921 3982 2763 737 586 6 A C ATOM 464 CA BASP A 63 2.711 24.021 20.802 0.50 20.17 A C ANISOU 464 CA BASP A 63 919 3982 2763 737 586 6 A C ATOM 465 C AASP A 63 3.593 23.854 22.058 0.50 19.32 A C ANISOU 465 C AASP A 63 876 3743 2723 706 749 6 A C ATOM 466 C BASP A 63 3.489 23.844 22.108 0.50 19.33 A C ANISOU 466 C BASP A 63 878 3745 2723 706 746 6 A C ATOM 467 O AASP A 63 4.143 22.787 22.343 0.50 19.24 A O ANISOU 467 O AASP A 63 816 3720 2773 706 789 -17 A O ATOM 468 O BASP A 63 3.861 22.731 22.482 0.50 19.36 A O ANISOU 468 O BASP A 63 847 3727 2781 706 771 -19 A O ATOM 469 CB AASP A 63 1.322 23.286 21.135 0.50 20.71 A C ANISOU 469 CB AASP A 63 974 4151 2745 680 579 31 A C ATOM 470 CB BASP A 63 1.241 23.622 20.908 0.50 20.69 A C ANISOU 470 CB BASP A 63 962 4156 2743 680 575 31 A C ATOM 471 CG AASP A 63 0.621 23.877 22.360 0.50 20.44 A C ANISOU 471 CG AASP A 63 988 4038 2739 324 502 96 A C ATOM 472 CG BASP A 63 0.425 24.144 19.737 0.50 20.97 A C ANISOU 472 CG BASP A 63 1067 4088 2811 351 496 54 A C ATOM 473 OD1AASP A 63 0.327 25.092 22.362 0.50 21.35 A O ANISOU 473 OD1AASP A 63 991 4201 2921 296 423 230 A O ATOM 474 OD1BASP A 63 -0.007 25.316 19.798 0.50 21.49 A O ANISOU 474 OD1BASP A 63 1115 4111 2939 513 181 228 A O ATOM 475 OD2AASP A 63 0.346 23.121 23.319 0.50 22.12 A O ANISOU 475 OD2AASP A 63 1333 4162 2908 87 425 109 A O ATOM 476 OD2BASP A 63 0.238 23.397 18.749 0.50 21.25 A O ANISOU 476 OD2BASP A 63 935 4158 2980 205 366 65 A O ATOM 477 N LYS A 64 3.742 24.967 22.776 1.00 19.06 A N ANISOU 477 N LYS A 64 943 3521 2777 449 917 71 A N ATOM 478 CA LYS A 64 4.563 25.007 23.985 1.00 20.33 A C ANISOU 478 CA LYS A 64 1429 3393 2903 31 987 147 A C ATOM 479 C LYS A 64 3.780 24.632 25.242 1.00 20.33 A C ANISOU 479 C LYS A 64 1630 3192 2901 20 1120 175 A C ATOM 480 O LYS A 64 3.382 25.498 26.032 1.00 22.68 A O ANISOU 480 O LYS A 64 2185 3298 3136 52 1251 124 A O ATOM 481 CB LYS A 64 5.193 26.403 24.141 1.00 21.33 A C ANISOU 481 CB LYS A 64 1479 3470 3156 -126 992 87 A C ATOM 482 CG LYS A 64 6.323 26.480 25.168 1.00 24.80 A C ANISOU 482 CG LYS A 64 1967 3826 3630 -186 803 -186 A C ATOM 483 CD LYS A 64 6.808 27.906 25.352 1.00 28.42 A C ANISOU 483 CD LYS A 64 2335 4097 4368 -350 736 -307 A C ATOM 484 CE LYS A 64 7.377 28.511 24.061 1.00 31.73 A C ANISOU 484 CE LYS A 64 2847 4338 4870 -272 798 -284 A C ATOM 485 NZ LYS A 64 8.621 27.833 23.592 1.00 32.14 A N ANISOU 485 NZ LYS A 64 2784 4314 5113 -339 768 -498 A N ATOM 486 N TYR A 65 3.587 23.344 25.450 1.00 18.35 A N ANISOU 486 N TYR A 65 1061 3082 2829 -15 1000 247 A N ATOM 487 CA TYR A 65 2.849 22.870 26.617 1.00 17.78 A C ANISOU 487 CA TYR A 65 1034 3039 2682 68 939 192 A C ATOM 488 C TYR A 65 3.729 22.921 27.867 1.00 18.03 A C ANISOU 488 C TYR A 65 1042 3115 2694 12 988 137 A C ATOM 489 O TYR A 65 4.970 23.048 27.780 1.00 18.69 A O ANISOU 489 O TYR A 65 972 3282 2847 -40 872 82 A O ATOM 490 CB TYR A 65 2.283 21.452 26.367 1.00 17.17 A C ANISOU 490 CB TYR A 65 681 3027 2815 87 803 228 A C ATOM 491 CG TYR A 65 3.354 20.395 26.276 1.00 16.69 A C ANISOU 491 CG TYR A 65 723 3104 2515 181 627 175 A C ATOM 492 CD1 TYR A 65 3.901 19.788 27.413 1.00 16.44 A C ANISOU 492 CD1 TYR A 65 462 3395 2388 317 625 131 A C ATOM 493 CD2 TYR A 65 3.848 20.001 25.039 1.00 15.81 A C ANISOU 493 CD2 TYR A 65 377 3294 2337 186 493 194 A C ATOM 494 CE1 TYR A 65 4.900 18.831 27.323 1.00 16.82 A C ANISOU 494 CE1 TYR A 65 482 3583 2327 296 577 63 A C ATOM 495 CE2 TYR A 65 4.845 19.041 24.940 1.00 15.58 A C ANISOU 495 CE2 TYR A 65 308 3292 2318 96 333 131 A C ATOM 496 CZ TYR A 65 5.355 18.457 26.073 1.00 16.68 A C ANISOU 496 CZ TYR A 65 620 3443 2275 247 599 173 A C ATOM 497 OH TYR A 65 6.364 17.524 25.985 1.00 15.76 A O ANISOU 497 OH TYR A 65 329 3420 2240 229 236 17 A O ATOM 498 N THR A 66 3.095 22.781 29.025 1.00 18.93 A N ANISOU 498 N THR A 66 1421 3167 2606 68 1062 118 A N ATOM 499 CA THR A 66 3.788 22.629 30.289 1.00 19.73 A C ANISOU 499 CA THR A 66 1527 3282 2687 141 1180 82 A C ATOM 500 C THR A 66 3.369 21.325 30.965 1.00 18.67 A C ANISOU 500 C THR A 66 1322 3303 2469 5 1005 103 A C ATOM 501 O THR A 66 2.313 20.746 30.639 1.00 19.44 A O ANISOU 501 O THR A 66 1384 3434 2569 -102 952 57 A O ATOM 502 CB THR A 66 3.508 23.811 31.243 1.00 20.54 A C ANISOU 502 CB THR A 66 1720 3346 2739 109 1185 37 A C ATOM 503 CG2 THR A 66 3.923 25.135 30.622 1.00 22.66 A C ANISOU 503 CG2 THR A 66 2099 3373 3138 153 1456 35 A C ATOM 504 OG1 THR A 66 2.105 23.854 31.531 1.00 23.21 A O ANISOU 504 OG1 THR A 66 2017 3585 3215 377 1420 31 A O ATOM 505 N LEU A 67 4.212 20.864 31.881 1.00 18.09 A N ANISOU 505 N LEU A 67 1351 3240 2284 81 850 -13 A N ATOM 506 CA LEU A 67 3.894 19.777 32.794 1.00 17.24 A C ANISOU 506 CA LEU A 67 1098 3188 2266 65 631 -197 A C ATOM 507 C LEU A 67 4.128 20.305 34.208 1.00 17.92 A C ANISOU 507 C LEU A 67 1305 3237 2266 63 658 -197 A C ATOM 508 O LEU A 67 5.129 19.968 34.852 1.00 19.03 A O ANISOU 508 O LEU A 67 1263 3630 2336 -43 590 -258 A O ATOM 509 CB LEU A 67 4.787 18.558 32.509 1.00 17.21 A C ANISOU 509 CB LEU A 67 1150 3203 2187 120 584 -252 A C ATOM 510 CG LEU A 67 4.658 17.945 31.111 1.00 17.52 A C ANISOU 510 CG LEU A 67 935 3348 2374 35 438 -294 A C ATOM 511 CD1 LEU A 67 5.829 17.004 30.836 1.00 19.69 A C ANISOU 511 CD1 LEU A 67 1342 3463 2675 357 438 -388 A C ATOM 512 CD2 LEU A 67 3.318 17.227 30.924 1.00 20.43 A C ANISOU 512 CD2 LEU A 67 1331 3495 2937 -109 186 -318 A C ATOM 513 N PRO A 68 3.201 21.148 34.688 1.00 18.93 A N ANISOU 513 N PRO A 68 1342 3357 2495 49 838 -271 A N ATOM 514 CA PRO A 68 3.458 21.994 35.860 1.00 19.50 A C ANISOU 514 CA PRO A 68 1418 3294 2698 -103 934 -296 A C ATOM 515 C PRO A 68 3.580 21.232 37.172 1.00 19.79 A C ANISOU 515 C PRO A 68 1392 3499 2628 -230 942 -315 A C ATOM 516 O PRO A 68 4.112 21.788 38.147 1.00 21.01 A O ANISOU 516 O PRO A 68 1428 3716 2840 -342 776 -333 A O ATOM 517 CB PRO A 68 2.237 22.924 35.907 1.00 20.58 A C ANISOU 517 CB PRO A 68 1523 3388 2908 -30 1018 -401 A C ATOM 518 CG PRO A 68 1.151 22.127 35.259 1.00 20.13 A C ANISOU 518 CG PRO A 68 1525 3495 2628 -6 926 -313 A C ATOM 519 CD PRO A 68 1.834 21.345 34.167 1.00 19.31 A C ANISOU 519 CD PRO A 68 1287 3474 2576 70 895 -219 A C ATOM 520 N ASN A 69 3.110 19.987 37.194 1.00 18.75 A N ANISOU 520 N ASN A 69 1052 3481 2592 -197 876 -63 A N ATOM 521 CA ASN A 69 3.225 19.168 38.403 1.00 19.53 A C ANISOU 521 CA ASN A 69 1186 3655 2581 -183 741 76 A C ATOM 522 C ASN A 69 4.465 18.281 38.421 1.00 19.72 A C ANISOU 522 C ASN A 69 1272 3621 2599 -185 634 104 A C ATOM 523 O ASN A 69 4.653 17.484 39.327 1.00 21.60 A O ANISOU 523 O ASN A 69 1659 3865 2682 -140 619 219 A O ATOM 524 CB ASN A 69 1.940 18.360 38.556 1.00 19.24 A C ANISOU 524 CB ASN A 69 1076 3562 2671 -120 842 153 A C ATOM 525 CG ASN A 69 0.724 19.271 38.472 1.00 19.35 A C ANISOU 525 CG ASN A 69 1115 3601 2635 -62 793 68 A C ATOM 526 ND2 ASN A 69 -0.148 19.023 37.496 1.00 20.12 A N ANISOU 526 ND2 ASN A 69 734 3711 3201 -71 652 -218 A N ATOM 527 OD1 ASN A 69 0.606 20.199 39.262 1.00 20.67 A O ANISOU 527 OD1 ASN A 69 1168 4077 2610 35 665 -119 A O ATOM 528 N SER A 70 5.340 18.456 37.431 1.00 19.56 A N ANISOU 528 N SER A 70 1106 3734 2592 -230 403 -160 A N ATOM 529 CA SER A 70 6.534 17.640 37.251 1.00 19.89 A C ANISOU 529 CA SER A 70 1036 3840 2682 -274 237 -410 A C ATOM 530 C SER A 70 7.772 18.520 37.305 1.00 20.04 A C ANISOU 530 C SER A 70 1036 3986 2594 -263 6 -467 A C ATOM 531 O SER A 70 7.683 19.712 37.021 1.00 21.05 A O ANISOU 531 O SER A 70 1069 3858 3070 -386 219 -463 A O ATOM 532 CB SER A 70 6.454 17.000 35.874 1.00 20.59 A C ANISOU 532 CB SER A 70 1186 3810 2829 -130 -6 -595 A C ATOM 533 OG SER A 70 7.605 16.285 35.544 1.00 23.24 A O ANISOU 533 OG SER A 70 1421 4413 2996 -252 307 -675 A O ATOM 534 N ASN A 71 8.918 17.931 37.632 1.00 19.97 A N ANISOU 534 N ASN A 71 921 4453 2213 -170 -51 -560 A N ATOM 535 CA ASN A 71 10.172 18.683 37.614 1.00 20.71 A C ANISOU 535 CA ASN A 71 1054 4805 2011 -3 -120 -579 A C ATOM 536 C ASN A 71 10.912 18.495 36.294 1.00 19.30 A C ANISOU 536 C ASN A 71 1097 4352 1884 -38 0 -582 A C ATOM 537 O ASN A 71 12.077 18.860 36.186 1.00 19.63 A O ANISOU 537 O ASN A 71 945 4557 1958 -57 -20 -634 A O ATOM 538 CB ASN A 71 11.065 18.313 38.808 1.00 23.16 A C ANISOU 538 CB ASN A 71 1368 5307 2124 -10 -170 -386 A C ATOM 539 CG ASN A 71 11.522 16.853 38.787 1.00 28.00 A C ANISOU 539 CG ASN A 71 2020 6211 2407 658 -392 -185 A C ATOM 540 ND2 ASN A 71 12.188 16.439 39.861 1.00 34.74 A N ANISOU 540 ND2 ASN A 71 3160 7171 2870 1027 -652 80 A N ATOM 541 OD1 ASN A 71 11.282 16.106 37.835 1.00 31.09 A O ANISOU 541 OD1 ASN A 71 2533 6521 2757 903 -581 -26 A O ATOM 542 N ILE A 72 10.237 17.948 35.287 1.00 18.58 A N ANISOU 542 N ILE A 72 1162 4117 1779 -109 208 -631 A N ATOM 543 CA ILE A 72 10.858 17.738 33.971 1.00 18.45 A C ANISOU 543 CA ILE A 72 1186 3986 1840 -208 263 -604 A C ATOM 544 C ILE A 72 11.157 19.082 33.313 1.00 18.09 A C ANISOU 544 C ILE A 72 1000 3984 1888 -173 370 -640 A C ATOM 545 O ILE A 72 10.345 20.009 33.408 1.00 18.64 A O ANISOU 545 O ILE A 72 918 3925 2239 -250 412 -627 A O ATOM 546 CB ILE A 72 9.946 16.887 33.045 1.00 18.39 A C ANISOU 546 CB ILE A 72 1221 3887 1878 -153 216 -590 A C ATOM 547 CG1 ILE A 72 9.886 15.440 33.545 1.00 19.83 A C ANISOU 547 CG1 ILE A 72 1474 3921 2140 -252 241 -474 A C ATOM 548 CG2 ILE A 72 10.395 16.977 31.586 1.00 19.49 A C ANISOU 548 CG2 ILE A 72 1315 4266 1826 -370 250 -553 A C ATOM 549 CD1 ILE A 72 8.786 14.599 32.902 1.00 20.79 A C ANISOU 549 CD1 ILE A 72 1588 3790 2520 -229 27 -335 A C ATOM 550 N ASN A 73 12.334 19.197 32.684 1.00 18.03 A N ANISOU 550 N ASN A 73 798 4140 1914 -184 285 -606 A N ATOM 551 CA ASN A 73 12.642 20.377 31.885 1.00 18.87 A C ANISOU 551 CA ASN A 73 961 4047 2161 -230 250 -595 A C ATOM 552 C ASN A 73 12.234 20.088 30.456 1.00 17.25 A C ANISOU 552 C ASN A 73 1080 3395 2081 -93 238 -516 A C ATOM 553 O ASN A 73 12.747 19.141 29.855 1.00 16.70 A O ANISOU 553 O ASN A 73 890 3341 2116 -38 119 -533 A O ATOM 554 CB ASN A 73 14.135 20.705 31.938 1.00 20.97 A C ANISOU 554 CB ASN A 73 1025 4481 2460 -487 241 -648 A C ATOM 555 CG ASN A 73 14.515 22.007 31.235 1.00 27.48 A C ANISOU 555 CG ASN A 73 1764 5284 3395 -991 0 -362 A C ATOM 556 ND2 ASN A 73 15.531 22.680 31.771 1.00 34.28 A N ANISOU 556 ND2 ASN A 73 2603 5866 4557 -1357 -197 -282 A N ATOM 557 OD1 ASN A 73 13.932 22.404 30.227 1.00 33.59 A O ANISOU 557 OD1 ASN A 73 2476 6118 4169 -1377 -10 -62 A O ATOM 558 N ILE A 74 11.289 20.891 29.946 1.00 16.39 A N ANISOU 558 N ILE A 74 986 3176 2064 52 381 -390 A N ATOM 559 CA ILE A 74 10.748 20.698 28.598 1.00 16.22 A C ANISOU 559 CA ILE A 74 830 3097 2237 48 460 -359 A C ATOM 560 C ILE A 74 11.443 21.684 27.647 1.00 15.84 A C ANISOU 560 C ILE A 74 938 2980 2099 -5 439 -445 A C ATOM 561 O ILE A 74 11.278 22.905 27.773 1.00 17.92 A O ANISOU 561 O ILE A 74 1288 3018 2504 -24 644 -458 A O ATOM 562 CB ILE A 74 9.212 20.889 28.528 1.00 16.35 A C ANISOU 562 CB ILE A 74 761 3106 2345 103 518 -403 A C ATOM 563 CG1 ILE A 74 8.504 20.010 29.556 1.00 19.34 A C ANISOU 563 CG1 ILE A 74 1102 3515 2732 107 520 -252 A C ATOM 564 CG2 ILE A 74 8.705 20.596 27.116 1.00 17.44 A C ANISOU 564 CG2 ILE A 74 786 3231 2608 -41 296 -296 A C ATOM 565 CD1 ILE A 74 7.134 20.499 29.937 1.00 20.62 A C ANISOU 565 CD1 ILE A 74 805 3980 3048 65 571 -489 A C ATOM 566 N ILE A 75 12.226 21.138 26.724 1.00 15.47 A N ANISOU 566 N ILE A 75 761 3088 2029 -120 307 -419 A N ATOM 567 CA ILE A 75 12.890 21.944 25.714 1.00 16.32 A C ANISOU 567 CA ILE A 75 636 3404 2161 -225 208 -284 A C ATOM 568 C ILE A 75 12.022 21.974 24.468 1.00 15.17 A C ANISOU 568 C ILE A 75 474 3106 2184 -195 272 -208 A C ATOM 569 O ILE A 75 11.664 20.929 23.926 1.00 15.96 A O ANISOU 569 O ILE A 75 505 3199 2361 -147 98 -252 A O ATOM 570 CB ILE A 75 14.263 21.359 25.362 1.00 17.27 A C ANISOU 570 CB ILE A 75 588 3688 2284 -227 217 -216 A C ATOM 571 CG1 ILE A 75 15.135 21.280 26.617 1.00 21.44 A C ANISOU 571 CG1 ILE A 75 1316 4140 2689 -432 -130 -248 A C ATOM 572 CG2 ILE A 75 14.939 22.197 24.279 1.00 18.95 A C ANISOU 572 CG2 ILE A 75 780 4023 2398 -366 326 -164 A C ATOM 573 CD1 ILE A 75 16.016 20.067 26.649 1.00 28.66 A C ANISOU 573 CD1 ILE A 75 2682 4753 3454 -719 -307 -230 A C ATOM 574 N HIS A 76 11.676 23.178 24.029 1.00 15.63 A N ANISOU 574 N HIS A 76 514 3106 2319 -159 318 -120 A N ATOM 575 CA HIS A 76 10.763 23.335 22.910 1.00 15.70 A C ANISOU 575 CA HIS A 76 549 3046 2370 17 474 -68 A C ATOM 576 C HIS A 76 11.518 23.741 21.653 1.00 15.26 A C ANISOU 576 C HIS A 76 443 2921 2435 10 474 -98 A C ATOM 577 O HIS A 76 12.110 24.825 21.595 1.00 16.59 A O ANISOU 577 O HIS A 76 691 2926 2685 -193 500 -46 A O ATOM 578 CB HIS A 76 9.696 24.374 23.237 1.00 15.76 A C ANISOU 578 CB HIS A 76 357 3138 2492 3 480 -173 A C ATOM 579 CG HIS A 76 8.581 24.421 22.242 1.00 16.39 A C ANISOU 579 CG HIS A 76 500 3222 2506 74 476 -81 A C ATOM 580 CD2 HIS A 76 8.119 23.487 21.377 1.00 16.39 A C ANISOU 580 CD2 HIS A 76 406 3291 2529 85 397 -13 A C ATOM 581 ND1 HIS A 76 7.802 25.542 22.048 1.00 17.73 A N ANISOU 581 ND1 HIS A 76 741 3321 2675 151 588 -3 A N ATOM 582 CE1 HIS A 76 6.896 25.292 21.119 1.00 17.83 A C ANISOU 582 CE1 HIS A 76 744 3413 2617 474 408 31 A C ATOM 583 NE2 HIS A 76 7.059 24.049 20.703 1.00 17.25 A N ANISOU 583 NE2 HIS A 76 535 3312 2707 346 392 82 A N ATOM 584 N ILE A 77 11.493 22.863 20.655 1.00 14.82 A N ANISOU 584 N ILE A 77 359 2980 2293 49 460 -81 A N ATOM 585 CA ILE A 77 11.993 23.202 19.323 1.00 16.72 A C ANISOU 585 CA ILE A 77 802 3091 2458 183 570 -118 A C ATOM 586 C ILE A 77 10.830 23.020 18.348 1.00 15.59 A C ANISOU 586 C ILE A 77 834 2754 2335 152 597 -43 A C ATOM 587 O ILE A 77 10.599 21.919 17.855 1.00 15.56 A O ANISOU 587 O ILE A 77 697 2732 2484 114 603 24 A O ATOM 588 CB ILE A 77 13.187 22.317 18.901 1.00 18.44 A C ANISOU 588 CB ILE A 77 1005 3370 2632 239 538 -125 A C ATOM 589 CG1 ILE A 77 14.331 22.416 19.921 1.00 21.16 A C ANISOU 589 CG1 ILE A 77 878 4097 3064 627 546 -324 A C ATOM 590 CG2 ILE A 77 13.669 22.724 17.520 1.00 20.81 A C ANISOU 590 CG2 ILE A 77 1226 3828 2851 204 776 -263 A C ATOM 591 CD1 ILE A 77 15.527 21.532 19.603 1.00 24.35 A C ANISOU 591 CD1 ILE A 77 1103 4535 3614 798 630 -317 A C ATOM 592 N PRO A 78 10.082 24.097 18.092 1.00 16.61 A N ANISOU 592 N PRO A 78 846 2809 2655 197 498 -129 A N ATOM 593 CA PRO A 78 8.858 23.954 17.294 1.00 17.29 A C ANISOU 593 CA PRO A 78 980 2969 2619 241 412 -230 A C ATOM 594 C PRO A 78 9.158 23.680 15.827 1.00 17.59 A C ANISOU 594 C PRO A 78 1018 3068 2599 252 454 -208 A C ATOM 595 O PRO A 78 9.865 24.470 15.185 1.00 19.28 A O ANISOU 595 O PRO A 78 1412 3188 2725 49 494 -76 A O ATOM 596 CB PRO A 78 8.152 25.297 17.468 1.00 17.97 A C ANISOU 596 CB PRO A 78 1084 2991 2754 252 392 -247 A C ATOM 597 CG PRO A 78 9.180 26.247 17.960 1.00 17.19 A C ANISOU 597 CG PRO A 78 842 2860 2831 270 405 -181 A C ATOM 598 CD PRO A 78 10.226 25.437 18.670 1.00 17.06 A C ANISOU 598 CD PRO A 78 922 2791 2768 175 458 -93 A C ATOM 599 N LEU A 79 8.650 22.554 15.332 1.00 15.63 A N ANISOU 599 N LEU A 79 368 3242 2328 329 348 -205 A N ATOM 600 CA LEU A 79 8.786 22.173 13.933 1.00 16.17 A C ANISOU 600 CA LEU A 79 359 3440 2345 452 208 -152 A C ATOM 601 C LEU A 79 7.425 21.774 13.397 1.00 15.33 A C ANISOU 601 C LEU A 79 370 3398 2056 472 266 -114 A C ATOM 602 O LEU A 79 6.560 21.348 14.157 1.00 16.02 A O ANISOU 602 O LEU A 79 326 3720 2039 432 195 97 A O ATOM 603 CB LEU A 79 9.734 20.984 13.794 1.00 16.49 A C ANISOU 603 CB LEU A 79 355 3384 2527 410 131 -160 A C ATOM 604 CG LEU A 79 11.161 21.187 14.290 1.00 18.33 A C ANISOU 604 CG LEU A 79 322 3797 2845 419 228 57 A C ATOM 605 CD1 LEU A 79 11.847 19.837 14.402 1.00 19.45 A C ANISOU 605 CD1 LEU A 79 293 3851 3246 320 207 296 A C ATOM 606 CD2 LEU A 79 11.901 22.100 13.329 1.00 21.85 A C ANISOU 606 CD2 LEU A 79 893 3914 3495 230 348 249 A C ATOM 607 N VAL A 80 7.263 21.904 12.085 1.00 15.82 A N ANISOU 607 N VAL A 80 395 3596 2018 383 219 -63 A N ATOM 608 CA VAL A 80 6.085 21.383 11.388 1.00 16.27 A C ANISOU 608 CA VAL A 80 518 3574 2090 511 109 -38 A C ATOM 609 C VAL A 80 6.434 20.090 10.640 1.00 15.97 A C ANISOU 609 C VAL A 80 392 3560 2116 535 74 -12 A C ATOM 610 O VAL A 80 7.499 19.969 10.028 1.00 17.00 A O ANISOU 610 O VAL A 80 436 3759 2265 573 196 -63 A O ATOM 611 CB VAL A 80 5.481 22.418 10.409 1.00 17.46 A C ANISOU 611 CB VAL A 80 821 3564 2249 524 31 -3 A C ATOM 612 CG1 VAL A 80 4.240 21.846 9.737 1.00 19.03 A C ANISOU 612 CG1 VAL A 80 766 3907 2558 584 -120 5 A C ATOM 613 CG2 VAL A 80 5.111 23.710 11.135 1.00 19.43 A C ANISOU 613 CG2 VAL A 80 1280 3583 2520 581 186 12 A C ATOM 614 N ASP A 81 5.539 19.107 10.674 1.00 15.65 A N ANISOU 614 N ASP A 81 331 3630 1985 509 31 -5 A N ATOM 615 CA ASP A 81 5.693 17.888 9.883 1.00 15.85 A C ANISOU 615 CA ASP A 81 443 3763 1817 571 54 43 A C ATOM 616 C ASP A 81 5.130 18.142 8.492 1.00 17.12 A C ANISOU 616 C ASP A 81 571 4142 1791 798 73 65 A C ATOM 617 O ASP A 81 3.948 17.885 8.230 1.00 18.48 A O ANISOU 617 O ASP A 81 434 4481 2108 863 -68 98 A O ATOM 618 CB ASP A 81 5.002 16.702 10.554 1.00 15.96 A C ANISOU 618 CB ASP A 81 331 3689 2043 516 24 41 A C ATOM 619 CG ASP A 81 5.144 15.409 9.770 1.00 15.78 A C ANISOU 619 CG ASP A 81 309 3765 1921 443 -24 41 A C ATOM 620 OD1 ASP A 81 6.001 15.325 8.835 1.00 17.87 A O ANISOU 620 OD1 ASP A 81 557 4205 2027 551 274 -31 A O ATOM 621 OD2 ASP A 81 4.441 14.435 10.120 1.00 17.70 A O ANISOU 621 OD2 ASP A 81 308 3772 2646 421 105 0 A O ATOM 622 N ASP A 82 5.949 18.697 7.611 1.00 18.82 A N ANISOU 622 N ASP A 82 930 4431 1788 1164 129 159 A N ATOM 623 CA ASP A 82 5.527 18.915 6.236 1.00 22.20 A C ANISOU 623 CA ASP A 82 1356 5156 1923 1824 241 373 A C ATOM 624 C ASP A 82 6.715 18.741 5.312 1.00 23.91 A C ANISOU 624 C ASP A 82 1570 5697 1817 2011 252 487 A C ATOM 625 O ASP A 82 7.840 18.548 5.771 1.00 22.05 A O ANISOU 625 O ASP A 82 1212 5281 1885 1629 91 368 A O ATOM 626 CB ASP A 82 4.906 20.304 6.064 1.00 24.70 A C ANISOU 626 CB ASP A 82 1914 5144 2328 1905 285 469 A C ATOM 627 CG ASP A 82 5.907 21.423 6.272 1.00 28.61 A C ANISOU 627 CG ASP A 82 2433 5120 3316 2046 529 612 A C ATOM 628 OD1 ASP A 82 7.116 21.187 6.077 1.00 32.19 A O ANISOU 628 OD1 ASP A 82 2772 5008 4449 1985 930 815 A O ATOM 629 OD2 ASP A 82 5.484 22.542 6.630 1.00 32.66 A O ANISOU 629 OD2 ASP A 82 2813 5310 4286 2081 842 724 A O ATOM 630 N THR A 83 6.470 18.787 4.010 1.00 28.33 A N ANISOU 630 N THR A 83 1967 7041 1756 2388 252 540 A N ATOM 631 CA THR A 83 7.529 18.440 3.066 1.00 32.64 A C ANISOU 631 CA THR A 83 2610 7911 1879 2691 417 617 A C ATOM 632 C THR A 83 8.364 19.672 2.674 1.00 33.91 A C ANISOU 632 C THR A 83 2694 8093 2097 2930 520 908 A C ATOM 633 O THR A 83 9.265 19.568 1.836 1.00 34.76 A O ANISOU 633 O THR A 83 2554 8403 2249 3064 617 986 A O ATOM 634 CB THR A 83 6.991 17.650 1.846 1.00 33.50 A C ANISOU 634 CB THR A 83 2775 8011 1941 2709 296 502 A C ATOM 635 CG2 THR A 83 6.532 16.253 2.278 1.00 35.03 A C ANISOU 635 CG2 THR A 83 3152 8008 2149 2748 337 386 A C ATOM 636 OG1 THR A 83 5.870 18.328 1.284 1.00 34.07 A O ANISOU 636 OG1 THR A 83 2894 7997 2055 2608 285 456 A O ATOM 637 N THR A 84 8.108 20.804 3.339 1.00 36.15 A N ANISOU 637 N THR A 84 3251 7713 2772 3237 850 1280 A N ATOM 638 CA THR A 84 8.807 22.071 3.073 1.00 38.29 A C ANISOU 638 CA THR A 84 3943 7135 3472 3337 1168 1551 A C ATOM 639 C THR A 84 9.799 22.536 4.169 1.00 36.95 A C ANISOU 639 C THR A 84 3847 6420 3772 3000 1448 1578 A C ATOM 640 O THR A 84 10.773 23.229 3.871 1.00 38.69 A O ANISOU 640 O THR A 84 4122 6402 4176 2937 1553 1805 A O ATOM 641 CB THR A 84 7.802 23.206 2.702 1.00 39.78 A C ANISOU 641 CB THR A 84 4194 7322 3598 3452 1133 1597 A C ATOM 642 CG2 THR A 84 7.408 24.039 3.927 1.00 39.99 A C ANISOU 642 CG2 THR A 84 4259 7206 3731 3646 930 1518 A C ATOM 643 OG1 THR A 84 8.376 24.055 1.699 1.00 41.75 A O ANISOU 643 OG1 THR A 84 4629 7336 3898 3330 1023 1624 A O ATOM 644 N THR A 85 9.582 22.110 5.411 1.00 33.95 A N ANISOU 644 N THR A 85 3583 5618 3700 2583 1462 1230 A N ATOM 645 CA THR A 85 10.409 22.547 6.541 1.00 30.96 A C ANISOU 645 CA THR A 85 3253 4884 3625 1967 1456 811 A C ATOM 646 C THR A 85 11.836 21.992 6.512 1.00 27.45 A C ANISOU 646 C THR A 85 3097 4004 3330 1553 1401 570 A C ATOM 647 O THR A 85 12.042 20.815 6.228 1.00 26.52 A O ANISOU 647 O THR A 85 2989 3819 3269 1473 1368 586 A O ATOM 648 CB THR A 85 9.769 22.156 7.889 1.00 32.57 A C ANISOU 648 CB THR A 85 3337 5464 3576 2108 1490 780 A C ATOM 649 CG2 THR A 85 10.799 22.206 9.009 1.00 33.37 A C ANISOU 649 CG2 THR A 85 3307 5539 3833 1958 1532 789 A C ATOM 650 OG1 THR A 85 8.697 23.056 8.191 1.00 34.81 A O ANISOU 650 OG1 THR A 85 3576 5727 3925 2117 1395 701 A O ATOM 651 N AASP A 86 12.783 22.838 6.500 0.50 26.21 A N ANISOU 651 N AASP A 86 3125 3614 3219 1324 1230 526 A N ATOM 652 N BASP A 86 12.812 22.844 6.827 0.50 26.36 A N ANISOU 652 N BASP A 86 3140 3580 3294 1254 1411 485 A N ATOM 653 CA AASP A 86 14.099 22.434 6.969 0.50 24.01 A C ANISOU 653 CA AASP A 86 2858 3264 3000 1026 1168 474 A C ATOM 654 CA BASP A 86 14.211 22.424 6.927 0.50 24.42 A C ANISOU 654 CA BASP A 86 3034 3143 3102 864 1303 460 A C ATOM 655 C AASP A 86 14.021 21.979 8.419 0.50 21.54 A C ANISOU 655 C AASP A 86 2405 3082 2696 719 838 274 A C ATOM 656 C BASP A 86 14.615 22.031 8.345 0.50 22.57 A C ANISOU 656 C BASP A 86 2694 3041 2842 476 1026 241 A C ATOM 657 O AASP A 86 13.553 22.715 9.288 0.50 19.63 A O ANISOU 657 O AASP A 86 1693 3023 2743 700 785 296 A O ATOM 658 O BASP A 86 15.071 22.866 9.127 0.50 22.27 A O ANISOU 658 O BASP A 86 2560 2975 2926 153 1062 230 A O ATOM 659 CB AASP A 86 15.106 23.575 6.822 0.50 25.56 A C ANISOU 659 CB AASP A 86 3161 3366 3185 1076 1386 489 A C ATOM 660 CB BASP A 86 15.152 23.521 6.427 0.50 25.52 A C ANISOU 660 CB BASP A 86 3264 3143 3289 952 1500 540 A C ATOM 661 CG AASP A 86 16.498 23.182 7.267 0.50 27.04 A C ANISOU 661 CG AASP A 86 3316 3528 3429 939 1518 597 A C ATOM 662 CG BASP A 86 16.612 23.218 6.730 0.50 25.97 A C ANISOU 662 CG BASP A 86 3472 2842 3555 847 1430 768 A C ATOM 663 OD1AASP A 86 17.026 23.821 8.198 0.50 29.52 A O ANISOU 663 OD1AASP A 86 3576 4056 3585 829 1676 579 A O ATOM 664 OD1BASP A 86 16.981 22.027 6.745 0.50 27.24 A O ANISOU 664 OD1BASP A 86 3576 2888 3885 762 1656 847 A O ATOM 665 OD2AASP A 86 17.061 22.229 6.691 0.50 29.27 A O ANISOU 665 OD2AASP A 86 3431 3984 3707 1098 1553 533 A O ATOM 666 OD2BASP A 86 17.392 24.168 6.950 0.50 26.62 A O ANISOU 666 OD2BASP A 86 3562 2833 3720 684 1518 855 A O ATOM 667 N ILE A 87 14.467 20.754 8.667 1.00 18.79 A N ANISOU 667 N ILE A 87 1720 3000 2421 373 533 153 A N ATOM 668 CA ILE A 87 14.739 20.281 10.026 1.00 17.74 A C ANISOU 668 CA ILE A 87 1166 3228 2347 -12 131 43 A C ATOM 669 C ILE A 87 16.247 20.152 10.237 1.00 16.48 A C ANISOU 669 C ILE A 87 900 3176 2187 -35 192 -147 A C ATOM 670 O ILE A 87 16.716 20.108 11.374 1.00 16.21 A O ANISOU 670 O ILE A 87 719 3226 2213 -208 80 -184 A O ATOM 671 CB ILE A 87 14.003 18.962 10.338 1.00 18.11 A C ANISOU 671 CB ILE A 87 1150 3361 2370 -135 -142 175 A C ATOM 672 CG1 ILE A 87 14.447 17.827 9.405 1.00 18.88 A C ANISOU 672 CG1 ILE A 87 1230 3289 2655 -269 -522 318 A C ATOM 673 CG2 ILE A 87 12.491 19.197 10.325 1.00 20.90 A C ANISOU 673 CG2 ILE A 87 1321 3786 2833 -196 -164 148 A C ATOM 674 CD1 ILE A 87 14.136 16.452 9.960 1.00 22.96 A C ANISOU 674 CD1 ILE A 87 1967 3598 3160 -482 -785 553 A C ATOM 675 N SER A 88 17.000 20.104 9.135 1.00 17.09 A N ANISOU 675 N SER A 88 891 3251 2352 -76 318 -294 A N ATOM 676 CA SER A 88 18.441 19.878 9.226 1.00 18.12 A C ANISOU 676 CA SER A 88 973 3388 2524 -102 478 -388 A C ATOM 677 C SER A 88 19.154 21.004 9.972 1.00 17.58 A C ANISOU 677 C SER A 88 988 3192 2500 -142 414 -252 A C ATOM 678 O SER A 88 20.217 20.756 10.538 1.00 17.77 A O ANISOU 678 O SER A 88 833 3409 2511 -80 441 -270 A O ATOM 679 CB SER A 88 19.043 19.685 7.830 1.00 18.83 A C ANISOU 679 CB SER A 88 986 3535 2633 -20 494 -408 A C ATOM 680 OG SER A 88 19.201 20.918 7.159 1.00 23.03 A O ANISOU 680 OG SER A 88 1824 3939 2987 17 899 -329 A O ATOM 681 N LYS A 89 18.577 22.211 10.002 1.00 17.93 A N ANISOU 681 N LYS A 89 1104 3055 2655 -136 357 -147 A N ATOM 682 CA LYS A 89 19.216 23.331 10.719 1.00 19.03 A C ANISOU 682 CA LYS A 89 1518 2978 2736 -164 263 -46 A C ATOM 683 C LYS A 89 19.460 23.020 12.200 1.00 17.34 A C ANISOU 683 C LYS A 89 1092 2867 2628 -260 344 -87 A C ATOM 684 O LYS A 89 20.329 23.640 12.827 1.00 18.54 A O ANISOU 684 O LYS A 89 1194 3097 2752 -522 417 -97 A O ATOM 685 CB LYS A 89 18.421 24.643 10.570 1.00 20.47 A C ANISOU 685 CB LYS A 89 1850 3084 2845 6 124 -74 A C ATOM 686 CG LYS A 89 17.061 24.659 11.240 1.00 25.29 A C ANISOU 686 CG LYS A 89 2542 3919 3147 447 -13 -285 A C ATOM 687 CD LYS A 89 16.360 26.017 11.138 1.00 32.49 A C ANISOU 687 CD LYS A 89 3542 5194 3607 1357 -152 -241 A C ATOM 688 CE LYS A 89 15.317 26.050 10.037 1.00 36.94 A C ANISOU 688 CE LYS A 89 4210 6003 3824 1720 -125 -326 A C ATOM 689 NZ LYS A 89 15.813 26.660 8.765 1.00 38.74 A N ANISOU 689 NZ LYS A 89 4350 6621 3747 1964 76 -285 A N ATOM 690 N TYR A 90 18.706 22.074 12.759 1.00 16.07 A N ANISOU 690 N TYR A 90 629 2949 2529 -322 324 -104 A N ATOM 691 CA TYR A 90 18.829 21.728 14.176 1.00 15.20 A C ANISOU 691 CA TYR A 90 346 2951 2477 -328 372 -263 A C ATOM 692 C TYR A 90 19.570 20.429 14.448 1.00 14.36 A C ANISOU 692 C TYR A 90 318 2928 2210 -344 239 -329 A C ATOM 693 O TYR A 90 19.777 20.088 15.608 1.00 15.13 A O ANISOU 693 O TYR A 90 350 3203 2196 -240 206 -271 A O ATOM 694 CB TYR A 90 17.428 21.612 14.808 1.00 16.74 A C ANISOU 694 CB TYR A 90 410 3176 2773 -342 526 -285 A C ATOM 695 CG TYR A 90 16.603 22.867 14.683 1.00 20.77 A C ANISOU 695 CG TYR A 90 858 3400 3634 -142 832 -186 A C ATOM 696 CD1 TYR A 90 16.870 23.985 15.465 1.00 26.44 A C ANISOU 696 CD1 TYR A 90 2117 3750 4178 386 930 -361 A C ATOM 697 CD2 TYR A 90 15.531 22.934 13.783 1.00 24.91 A C ANISOU 697 CD2 TYR A 90 1149 3734 4582 175 922 76 A C ATOM 698 CE1 TYR A 90 16.095 25.148 15.356 1.00 29.65 A C ANISOU 698 CE1 TYR A 90 2484 3966 4816 612 1203 -272 A C ATOM 699 CE2 TYR A 90 14.758 24.087 13.666 1.00 27.88 A C ANISOU 699 CE2 TYR A 90 1392 3905 5296 185 1115 282 A C ATOM 700 CZ TYR A 90 15.038 25.184 14.458 1.00 29.45 A C ANISOU 700 CZ TYR A 90 1835 4029 5324 560 1500 -12 A C ATOM 701 OH TYR A 90 14.291 26.325 14.330 1.00 33.81 A O ANISOU 701 OH TYR A 90 2356 4329 6161 588 1465 38 A O ATOM 702 N PHE A 91 19.977 19.687 13.409 1.00 14.51 A N ANISOU 702 N PHE A 91 306 2969 2238 -186 252 -324 A N ATOM 703 CA PHE A 91 20.632 18.396 13.637 1.00 15.09 A C ANISOU 703 CA PHE A 91 421 2994 2319 -98 142 -397 A C ATOM 704 C PHE A 91 21.870 18.495 14.548 1.00 16.11 A C ANISOU 704 C PHE A 91 509 3156 2457 -114 136 -436 A C ATOM 705 O PHE A 91 22.010 17.716 15.488 1.00 16.38 A O ANISOU 705 O PHE A 91 375 3393 2457 -146 87 -383 A O ATOM 706 CB PHE A 91 21.050 17.745 12.320 1.00 15.88 A C ANISOU 706 CB PHE A 91 487 3088 2458 -109 120 -460 A C ATOM 707 CG PHE A 91 19.915 17.161 11.496 1.00 15.26 A C ANISOU 707 CG PHE A 91 388 2910 2500 120 -164 -456 A C ATOM 708 CD1 PHE A 91 18.665 16.863 12.038 1.00 16.77 A C ANISOU 708 CD1 PHE A 91 377 2896 3097 98 -307 -269 A C ATOM 709 CD2 PHE A 91 20.139 16.892 10.139 1.00 18.25 A C ANISOU 709 CD2 PHE A 91 649 3558 2727 417 -197 -736 A C ATOM 710 CE1 PHE A 91 17.653 16.300 11.234 1.00 16.67 A C ANISOU 710 CE1 PHE A 91 294 2966 3073 131 -324 -366 A C ATOM 711 CE2 PHE A 91 19.148 16.342 9.331 1.00 19.29 A C ANISOU 711 CE2 PHE A 91 995 3546 2788 509 -482 -630 A C ATOM 712 CZ PHE A 91 17.894 16.049 9.883 1.00 19.54 A C ANISOU 712 CZ PHE A 91 865 3321 3237 184 -344 -535 A C ATOM 713 N ASP A 92 22.770 19.437 14.269 1.00 17.24 A N ANISOU 713 N ASP A 92 491 3467 2594 -152 184 -454 A N ATOM 714 CA ASP A 92 23.997 19.491 15.066 1.00 18.86 A C ANISOU 714 CA ASP A 92 593 3903 2669 -285 197 -518 A C ATOM 715 C ASP A 92 23.732 19.721 16.553 1.00 18.20 A C ANISOU 715 C ASP A 92 571 3725 2619 -293 273 -465 A C ATOM 716 O ASP A 92 24.244 18.996 17.418 1.00 18.52 A O ANISOU 716 O ASP A 92 412 3869 2754 -293 357 -456 A O ATOM 717 CB ASP A 92 24.938 20.556 14.514 1.00 19.74 A C ANISOU 717 CB ASP A 92 634 4120 2748 -384 197 -494 A C ATOM 718 CG ASP A 92 25.602 20.148 13.215 1.00 23.75 A C ANISOU 718 CG ASP A 92 763 5188 3072 -549 381 -670 A C ATOM 719 OD1 ASP A 92 25.514 18.966 12.822 1.00 28.53 A O ANISOU 719 OD1 ASP A 92 1278 5924 3637 -241 520 -996 A O ATOM 720 OD2 ASP A 92 26.223 21.021 12.571 1.00 29.05 A O ANISOU 720 OD2 ASP A 92 1148 6503 3388 -1133 653 -702 A O ATOM 721 N ASP A 93 22.912 20.717 16.879 1.00 17.96 A N ANISOU 721 N ASP A 93 480 3704 2639 -307 357 -423 A N ATOM 722 CA ASP A 93 22.655 21.023 18.285 1.00 18.55 A C ANISOU 722 CA ASP A 93 794 3495 2759 -357 241 -447 A C ATOM 723 C ASP A 93 21.803 19.958 18.970 1.00 16.11 A C ANISOU 723 C ASP A 93 295 3467 2360 -219 160 -408 A C ATOM 724 O ASP A 93 21.999 19.655 20.143 1.00 16.72 A O ANISOU 724 O ASP A 93 350 3639 2362 -346 26 -368 A O ATOM 725 CB ASP A 93 22.037 22.413 18.442 1.00 21.11 A C ANISOU 725 CB ASP A 93 1272 3501 3249 -377 410 -527 A C ATOM 726 CG ASP A 93 23.070 23.530 18.276 1.00 26.65 A C ANISOU 726 CG ASP A 93 2099 3564 4462 -614 428 -571 A C ATOM 727 OD1 ASP A 93 24.271 23.243 18.064 1.00 30.59 A O ANISOU 727 OD1 ASP A 93 2453 3878 5289 -921 388 -768 A O ATOM 728 OD2 ASP A 93 22.672 24.707 18.364 1.00 32.41 A O ANISOU 728 OD2 ASP A 93 3075 3713 5526 -706 732 -507 A O ATOM 729 N VAL A 94 20.841 19.377 18.252 1.00 15.26 A N ANISOU 729 N VAL A 94 276 3300 2221 -140 0 -366 A N ATOM 730 CA VAL A 94 20.019 18.331 18.869 1.00 15.15 A C ANISOU 730 CA VAL A 94 253 3368 2133 -7 0 -274 A C ATOM 731 C VAL A 94 20.870 17.093 19.164 1.00 14.88 A C ANISOU 731 C VAL A 94 253 3433 1967 -31 17 -406 A C ATOM 732 O VAL A 94 20.816 16.544 20.260 1.00 15.72 A O ANISOU 732 O VAL A 94 265 3806 1903 194 28 -287 A O ATOM 733 CB VAL A 94 18.769 17.970 18.036 1.00 15.00 A C ANISOU 733 CB VAL A 94 258 3197 2243 6 -97 -213 A C ATOM 734 CG1 VAL A 94 18.101 16.693 18.567 1.00 15.18 A C ANISOU 734 CG1 VAL A 94 263 3167 2338 80 -126 -86 A C ATOM 735 CG2 VAL A 94 17.785 19.140 18.053 1.00 15.64 A C ANISOU 735 CG2 VAL A 94 285 3181 2474 295 61 -155 A C ATOM 736 N THR A 95 21.669 16.659 18.189 1.00 15.56 A N ANISOU 736 N THR A 95 253 3638 2020 26 0 -562 A N ATOM 737 CA THR A 95 22.445 15.446 18.403 1.00 16.87 A C ANISOU 737 CA THR A 95 255 3817 2335 77 -19 -644 A C ATOM 738 C THR A 95 23.516 15.664 19.492 1.00 17.67 A C ANISOU 738 C THR A 95 258 3977 2477 131 -35 -719 A C ATOM 739 O THR A 95 23.776 14.753 20.276 1.00 18.54 A O ANISOU 739 O THR A 95 271 4158 2617 219 -142 -658 A O ATOM 740 CB THR A 95 23.109 14.920 17.100 1.00 16.88 A C ANISOU 740 CB THR A 95 263 3822 2328 103 17 -610 A C ATOM 741 CG2 THR A 95 22.027 14.618 16.059 1.00 17.33 A C ANISOU 741 CG2 THR A 95 258 3982 2345 132 -56 -665 A C ATOM 742 OG1 THR A 95 24.003 15.902 16.564 1.00 18.21 A O ANISOU 742 OG1 THR A 95 263 4144 2511 18 146 -615 A O ATOM 743 N ALA A 96 24.074 16.866 19.593 1.00 18.34 A N ANISOU 743 N ALA A 96 256 4235 2476 27 -82 -697 A N ATOM 744 CA ALA A 96 25.042 17.155 20.665 1.00 19.03 A C ANISOU 744 CA ALA A 96 291 4426 2515 -109 -172 -640 A C ATOM 745 C ALA A 96 24.346 17.106 22.029 1.00 19.09 A C ANISOU 745 C ALA A 96 282 4469 2502 76 -184 -577 A C ATOM 746 O ALA A 96 24.883 16.601 23.013 1.00 20.48 A O ANISOU 746 O ALA A 96 527 4724 2529 82 -238 -573 A O ATOM 747 CB ALA A 96 25.683 18.506 20.441 1.00 19.92 A C ANISOU 747 CB ALA A 96 304 4575 2691 -263 -252 -538 A C ATOM 748 N PHE A 97 23.109 17.603 22.086 1.00 18.08 A N ANISOU 748 N PHE A 97 263 4198 2410 102 -136 -635 A N ATOM 749 CA PHE A 97 22.359 17.580 23.330 1.00 17.92 A C ANISOU 749 CA PHE A 97 373 4061 2372 285 -93 -586 A C ATOM 750 C PHE A 97 21.999 16.149 23.740 1.00 17.23 A C ANISOU 750 C PHE A 97 355 3977 2213 425 -159 -538 A C ATOM 751 O PHE A 97 22.147 15.763 24.910 1.00 17.79 A O ANISOU 751 O PHE A 97 339 4226 2195 489 -285 -555 A O ATOM 752 CB PHE A 97 21.102 18.451 23.205 1.00 17.87 A C ANISOU 752 CB PHE A 97 282 4056 2450 252 125 -496 A C ATOM 753 CG PHE A 97 20.082 18.217 24.299 1.00 20.56 A C ANISOU 753 CG PHE A 97 754 4399 2657 353 520 -397 A C ATOM 754 CD1 PHE A 97 20.363 18.555 25.618 1.00 25.57 A C ANISOU 754 CD1 PHE A 97 1729 5062 2924 557 819 -269 A C ATOM 755 CD2 PHE A 97 18.835 17.662 23.984 1.00 22.53 A C ANISOU 755 CD2 PHE A 97 749 4666 3147 342 988 -120 A C ATOM 756 CE1 PHE A 97 19.405 18.341 26.623 1.00 27.35 A C ANISOU 756 CE1 PHE A 97 2063 5296 3034 995 948 12 A C ATOM 757 CE2 PHE A 97 17.888 17.435 24.986 1.00 26.57 A C ANISOU 757 CE2 PHE A 97 1692 5012 3393 763 1216 60 A C ATOM 758 CZ PHE A 97 18.181 17.768 26.304 1.00 27.36 A C ANISOU 758 CZ PHE A 97 2046 5249 3102 868 1429 120 A C ATOM 759 N LEU A 98 21.533 15.359 22.776 1.00 16.50 A N ANISOU 759 N LEU A 98 366 3777 2125 610 -186 -461 A N ATOM 760 CA LEU A 98 21.228 13.955 23.080 1.00 16.83 A C ANISOU 760 CA LEU A 98 388 3889 2117 666 -217 -368 A C ATOM 761 C LEU A 98 22.488 13.177 23.527 1.00 18.22 A C ANISOU 761 C LEU A 98 416 4250 2257 768 -241 -388 A C ATOM 762 O LEU A 98 22.408 12.380 24.456 1.00 19.00 A O ANISOU 762 O LEU A 98 483 4420 2318 872 -361 -241 A O ATOM 763 CB LEU A 98 20.547 13.305 21.889 1.00 16.18 A C ANISOU 763 CB LEU A 98 386 3679 2081 658 -173 -368 A C ATOM 764 CG LEU A 98 19.162 13.897 21.579 1.00 15.12 A C ANISOU 764 CG LEU A 98 307 3531 1906 422 -21 -192 A C ATOM 765 CD1 LEU A 98 18.617 13.198 20.353 1.00 15.30 A C ANISOU 765 CD1 LEU A 98 340 3472 2000 513 47 -260 A C ATOM 766 CD2 LEU A 98 18.193 13.795 22.779 1.00 15.28 A C ANISOU 766 CD2 LEU A 98 280 3513 2011 287 -52 -154 A C ATOM 767 N ASER A 99 23.627 13.424 22.880 0.50 19.83 A N ANISOU 767 N ASER A 99 405 4708 2422 741 -313 -425 A N ATOM 768 N BSER A 99 23.621 13.422 22.870 0.50 19.58 A N ANISOU 768 N BSER A 99 408 4668 2362 754 -305 -447 A N ATOM 769 CA ASER A 99 24.885 12.804 23.277 0.50 21.42 A C ANISOU 769 CA ASER A 99 406 5148 2585 688 -344 -487 A C ATOM 770 CA BSER A 99 24.877 12.809 23.267 0.50 20.62 A C ANISOU 770 CA BSER A 99 405 4953 2477 749 -315 -520 A C ATOM 771 C ASER A 99 25.260 13.144 24.714 0.50 21.63 A C ANISOU 771 C ASER A 99 444 5152 2623 674 -430 -507 A C ATOM 772 C BSER A 99 25.208 13.129 24.723 0.50 21.26 A C ANISOU 772 C BSER A 99 439 5119 2518 687 -390 -502 A C ATOM 773 O ASER A 99 25.777 12.300 25.446 0.50 22.48 A O ANISOU 773 O ASER A 99 726 5141 2675 649 -505 -522 A O ATOM 774 O BSER A 99 25.634 12.256 25.479 0.50 22.31 A O ANISOU 774 O BSER A 99 728 5145 2603 675 -467 -496 A O ATOM 775 CB ASER A 99 25.970 13.256 22.315 0.50 21.97 A C ANISOU 775 CB ASER A 99 372 5296 2680 697 -287 -463 A C ATOM 776 CB BSER A 99 25.975 13.310 22.341 0.50 20.68 A C ANISOU 776 CB BSER A 99 388 4992 2476 722 -313 -549 A C ATOM 777 OG ASER A 99 25.861 12.537 21.101 0.50 24.89 A O ANISOU 777 OG ASER A 99 592 6014 2851 658 -274 -493 A O ATOM 778 OG BSER A 99 27.217 12.741 22.718 0.50 20.67 A O ANISOU 778 OG BSER A 99 421 4834 2599 842 -274 -579 A O ATOM 779 N LYS A 100 24.994 14.382 25.117 1.00 21.75 A N ANISOU 779 N LYS A 100 531 5223 2509 723 -485 -509 A N ATOM 780 CA LYS A 100 25.268 14.835 26.479 1.00 23.27 A C ANISOU 780 CA LYS A 100 841 5457 2545 807 -498 -568 A C ATOM 781 C LYS A 100 24.335 14.143 27.474 1.00 22.89 A C ANISOU 781 C LYS A 100 802 5483 2413 988 -500 -520 A C ATOM 782 O LYS A 100 24.761 13.751 28.564 1.00 24.04 A O ANISOU 782 O LYS A 100 986 5702 2444 851 -542 -480 A O ATOM 783 CB LYS A 100 25.190 16.361 26.550 1.00 24.45 A C ANISOU 783 CB LYS A 100 1087 5522 2680 781 -546 -693 A C ATOM 784 CG LYS A 100 25.571 16.991 27.882 1.00 29.27 A C ANISOU 784 CG LYS A 100 1958 5946 3219 487 -515 -878 A C ATOM 785 CD LYS A 100 25.968 18.456 27.705 1.00 36.42 A C ANISOU 785 CD LYS A 100 3023 6560 4255 142 -562 -763 A C ATOM 786 CE LYS A 100 24.790 19.421 27.798 1.00 40.63 A C ANISOU 786 CE LYS A 100 3616 7031 4791 -6 -680 -315 A C ATOM 787 NZ LYS A 100 23.813 19.245 26.686 1.00 44.34 A N ANISOU 787 NZ LYS A 100 3847 7562 5440 -197 -856 -19 A N ATOM 788 N CYS A 101 23.062 13.965 27.101 1.00 22.32 A N ANISOU 788 N CYS A 101 886 5256 2337 1040 -476 -531 A N ATOM 789 CA CYS A 101 22.146 13.223 27.965 1.00 21.76 A C ANISOU 789 CA CYS A 101 1085 4924 2257 1186 -522 -612 A C ATOM 790 C CYS A 101 22.649 11.795 28.202 1.00 23.32 A C ANISOU 790 C CYS A 101 1562 5088 2211 1553 -535 -670 A C ATOM 791 O CYS A 101 22.616 11.296 29.331 1.00 24.32 A O ANISOU 791 O CYS A 101 1736 5278 2228 1595 -627 -597 A O ATOM 792 CB CYS A 101 20.750 13.209 27.368 1.00 21.30 A C ANISOU 792 CB CYS A 101 917 4841 2334 1023 -527 -529 A C ATOM 793 SG CYS A 101 19.951 14.828 27.403 1.00 20.73 A S ANISOU 793 SG CYS A 101 797 4596 2484 688 -296 -463 A S ATOM 794 N ASP A 102 23.143 11.152 27.146 1.00 25.12 A N ANISOU 794 N ASP A 102 2026 5289 2231 1888 -737 -869 A N ATOM 795 CA ASP A 102 23.702 9.807 27.299 1.00 26.89 A C ANISOU 795 CA ASP A 102 2249 5594 2372 2152 -973 -986 A C ATOM 796 C ASP A 102 24.986 9.774 28.138 1.00 28.63 A C ANISOU 796 C ASP A 102 2345 5942 2590 2248 -1208 -1022 A C ATOM 797 O ASP A 102 25.195 8.847 28.919 1.00 29.89 A O ANISOU 797 O ASP A 102 2368 6140 2847 2275 -1181 -930 A O ATOM 798 CB ASP A 102 23.899 9.138 25.926 1.00 26.74 A C ANISOU 798 CB ASP A 102 2333 5493 2334 2150 -961 -996 A C ATOM 799 CG ASP A 102 22.729 8.239 25.535 1.00 27.50 A C ANISOU 799 CG ASP A 102 2487 5615 2345 2073 -767 -1049 A C ATOM 800 OD1 ASP A 102 22.398 8.148 24.330 1.00 26.64 A O ANISOU 800 OD1 ASP A 102 2222 5442 2459 1985 -979 -913 A O ATOM 801 OD2 ASP A 102 22.150 7.594 26.442 1.00 28.08 A O ANISOU 801 OD2 ASP A 102 2347 5895 2426 1985 -780 -860 A O ATOM 802 N GLN A 103 25.827 10.795 27.992 1.00 29.62 A N ANISOU 802 N GLN A 103 2203 6248 2802 2328 -1404 -1080 A N ATOM 803 CA GLN A 103 27.069 10.883 28.771 1.00 32.70 A C ANISOU 803 CA GLN A 103 2585 6657 3183 2213 -1597 -1089 A C ATOM 804 C GLN A 103 26.765 11.063 30.259 1.00 32.82 A C ANISOU 804 C GLN A 103 2542 6998 2930 2291 -1597 -1133 A C ATOM 805 O GLN A 103 27.431 10.483 31.115 1.00 33.98 A O ANISOU 805 O GLN A 103 2711 7185 3016 2372 -1497 -1052 A O ATOM 806 CB GLN A 103 27.926 12.054 28.285 1.00 33.30 A C ANISOU 806 CB GLN A 103 2495 6664 3494 2099 -1718 -1080 A C ATOM 807 CG GLN A 103 28.528 11.886 26.902 1.00 40.41 A C ANISOU 807 CG GLN A 103 3542 6674 5138 1779 -2055 -964 A C ATOM 808 CD GLN A 103 29.079 13.191 26.346 1.00 46.96 A C ANISOU 808 CD GLN A 103 4304 6765 6772 1492 -2414 -790 A C ATOM 809 NE2 GLN A 103 28.442 13.705 25.297 1.00 49.86 A N ANISOU 809 NE2 GLN A 103 4343 7024 7577 1535 -2460 -661 A N ATOM 810 OE1 GLN A 103 30.064 13.729 26.855 1.00 49.68 A O ANISOU 810 OE1 GLN A 103 4745 6966 7164 1445 -2186 -1075 A O ATOM 811 N ARG A 104 25.754 11.877 30.547 1.00 33.01 A N ANISOU 811 N ARG A 104 2707 7092 2745 2283 -1541 -986 A N ATOM 812 CA ARG A 104 25.420 12.254 31.916 1.00 32.86 A C ANISOU 812 CA ARG A 104 2842 6987 2657 2117 -1497 -913 A C ATOM 813 C ARG A 104 24.373 11.354 32.577 1.00 32.77 A C ANISOU 813 C ARG A 104 3230 6638 2585 2301 -1324 -728 A C ATOM 814 O ARG A 104 24.023 11.562 33.745 1.00 33.11 A O ANISOU 814 O ARG A 104 3296 6771 2515 2292 -1358 -781 A O ATOM 815 CB ARG A 104 24.952 13.718 31.964 1.00 32.85 A C ANISOU 815 CB ARG A 104 2766 6998 2716 1923 -1483 -935 A C ATOM 816 CG ARG A 104 25.995 14.730 31.517 1.00 34.68 A C ANISOU 816 CG ARG A 104 2851 7415 2910 1348 -1368 -895 A C ATOM 817 CD ARG A 104 25.432 16.142 31.417 1.00 36.46 A C ANISOU 817 CD ARG A 104 3027 7710 3115 571 -1014 -1014 A C ATOM 818 NE ARG A 104 24.868 16.630 32.674 1.00 40.66 A N ANISOU 818 NE ARG A 104 3671 8177 3601 175 -719 -1289 A N ATOM 819 CZ ARG A 104 25.492 17.416 33.547 1.00 43.53 A C ANISOU 819 CZ ARG A 104 4282 8467 3790 76 -640 -1465 A C ATOM 820 NH1 ARG A 104 26.736 17.827 33.321 1.00 45.80 A N ANISOU 820 NH1 ARG A 104 4557 8827 4018 -370 -732 -1489 A N ATOM 821 NH2 ARG A 104 24.880 17.802 34.664 1.00 45.42 A N ANISOU 821 NH2 ARG A 104 4785 8564 3907 421 -555 -1500 A N ATOM 822 N ASN A 105 23.879 10.349 31.851 1.00 32.21 A N ANISOU 822 N ASN A 105 3452 6291 2495 2431 -1145 -430 A N ATOM 823 CA ASN A 105 22.814 9.469 32.359 1.00 32.57 A C ANISOU 823 CA ASN A 105 3761 6147 2467 2441 -957 -124 A C ATOM 824 C ASN A 105 21.582 10.270 32.782 1.00 30.66 A C ANISOU 824 C ASN A 105 3508 5867 2275 2090 -850 -216 A C ATOM 825 O ASN A 105 21.035 10.076 33.876 1.00 31.30 A O ANISOU 825 O ASN A 105 3689 5964 2238 2061 -877 -185 A O ATOM 826 CB ASN A 105 23.284 8.559 33.503 1.00 34.23 A C ANISOU 826 CB ASN A 105 4065 6438 2502 2662 -851 -15 A C ATOM 827 CG ASN A 105 23.890 7.257 33.004 1.00 36.90 A C ANISOU 827 CG ASN A 105 4526 6832 2662 3079 -754 262 A C ATOM 828 ND2 ASN A 105 24.821 6.720 33.784 1.00 40.39 A N ANISOU 828 ND2 ASN A 105 4798 7368 3181 3402 -727 270 A N ATOM 829 OD1 ASN A 105 23.533 6.733 31.941 1.00 39.10 A O ANISOU 829 OD1 ASN A 105 4498 7368 2989 3497 -727 252 A O ATOM 830 N GLU A 106 21.161 11.166 31.893 1.00 27.37 A N ANISOU 830 N GLU A 106 2818 5422 2159 1685 -724 -331 A N ATOM 831 CA GLU A 106 19.993 11.999 32.128 1.00 24.21 A C ANISOU 831 CA GLU A 106 2132 4949 2117 1119 -584 -405 A C ATOM 832 C GLU A 106 18.941 11.619 31.100 1.00 22.55 A C ANISOU 832 C GLU A 106 2098 4539 1932 917 -434 -142 A C ATOM 833 O GLU A 106 19.070 11.999 29.942 1.00 22.81 A O ANISOU 833 O GLU A 106 2035 4690 1941 820 -320 -131 A O ATOM 834 CB GLU A 106 20.357 13.483 32.037 1.00 23.59 A C ANISOU 834 CB GLU A 106 1870 4978 2113 1014 -592 -480 A C ATOM 835 CG GLU A 106 21.342 13.892 33.127 1.00 24.78 A C ANISOU 835 CG GLU A 106 1587 5440 2387 671 -626 -631 A C ATOM 836 CD GLU A 106 21.872 15.308 33.009 1.00 26.12 A C ANISOU 836 CD GLU A 106 1553 5655 2714 529 -604 -697 A C ATOM 837 OE1 GLU A 106 21.783 15.901 31.906 1.00 26.04 A O ANISOU 837 OE1 GLU A 106 1448 5619 2827 590 -627 -737 A O ATOM 838 OE2 GLU A 106 22.401 15.807 34.035 1.00 27.49 A O ANISOU 838 OE2 GLU A 106 1605 5989 2851 518 -898 -688 A O ATOM 839 N PRO A 107 17.948 10.816 31.508 1.00 22.19 A N ANISOU 839 N PRO A 107 2125 4347 1958 856 -335 135 A N ATOM 840 CA PRO A 107 16.952 10.343 30.544 1.00 20.80 A C ANISOU 840 CA PRO A 107 2046 4034 1823 790 -241 164 A C ATOM 841 C PRO A 107 16.202 11.481 29.858 1.00 18.92 A C ANISOU 841 C PRO A 107 1676 3837 1676 772 -135 -35 A C ATOM 842 O PRO A 107 15.828 12.472 30.500 1.00 18.98 A O ANISOU 842 O PRO A 107 1711 3774 1726 697 -98 -118 A O ATOM 843 CB PRO A 107 16.010 9.484 31.386 1.00 21.48 A C ANISOU 843 CB PRO A 107 1982 4169 2011 825 -164 218 A C ATOM 844 CG PRO A 107 16.834 9.062 32.554 1.00 23.65 A C ANISOU 844 CG PRO A 107 2441 4489 2055 790 -241 421 A C ATOM 845 CD PRO A 107 17.716 10.250 32.849 1.00 23.00 A C ANISOU 845 CD PRO A 107 2275 4462 2002 850 -388 294 A C ATOM 846 N VAL A 108 16.008 11.330 28.552 1.00 17.43 A N ANISOU 846 N VAL A 108 1472 3555 1597 631 -131 -54 A N ATOM 847 CA VAL A 108 15.337 12.347 27.748 1.00 16.24 A C ANISOU 847 CA VAL A 108 1118 3388 1664 540 -93 -120 A C ATOM 848 C VAL A 108 14.373 11.663 26.789 1.00 15.32 A C ANISOU 848 C VAL A 108 1080 3197 1544 469 20 -131 A C ATOM 849 O VAL A 108 14.706 10.665 26.149 1.00 16.43 A O ANISOU 849 O VAL A 108 1286 3262 1693 498 19 -137 A O ATOM 850 CB VAL A 108 16.349 13.217 26.953 1.00 15.93 A C ANISOU 850 CB VAL A 108 1023 3294 1737 504 -24 -120 A C ATOM 851 CG1 VAL A 108 17.301 12.348 26.147 1.00 17.57 A C ANISOU 851 CG1 VAL A 108 885 3932 1860 678 -49 -285 A C ATOM 852 CG2 VAL A 108 15.656 14.220 26.015 1.00 16.51 A C ANISOU 852 CG2 VAL A 108 865 3488 1921 386 -215 -54 A C ATOM 853 N LEU A 109 13.157 12.205 26.729 1.00 15.12 A N ANISOU 853 N LEU A 109 913 3068 1763 329 57 -73 A N ATOM 854 CA LEU A 109 12.159 11.726 25.778 1.00 14.14 A C ANISOU 854 CA LEU A 109 925 2912 1536 164 230 -115 A C ATOM 855 C LEU A 109 12.076 12.694 24.598 1.00 13.40 A C ANISOU 855 C LEU A 109 733 2822 1536 146 285 -115 A C ATOM 856 O LEU A 109 11.778 13.877 24.815 1.00 14.04 A O ANISOU 856 O LEU A 109 753 2739 1841 120 307 -137 A O ATOM 857 CB LEU A 109 10.783 11.608 26.455 1.00 15.12 A C ANISOU 857 CB LEU A 109 979 2930 1835 15 274 -87 A C ATOM 858 CG LEU A 109 9.603 11.315 25.508 1.00 15.87 A C ANISOU 858 CG LEU A 109 957 3169 1902 -17 383 -283 A C ATOM 859 CD1 LEU A 109 9.735 9.965 24.822 1.00 17.43 A C ANISOU 859 CD1 LEU A 109 1482 3235 1905 -74 331 -203 A C ATOM 860 CD2 LEU A 109 8.278 11.381 26.259 1.00 16.99 A C ANISOU 860 CD2 LEU A 109 913 3425 2117 -6 522 -208 A C ATOM 861 N VAL A 110 12.361 12.194 23.388 1.00 12.93 A N ANISOU 861 N VAL A 110 509 2973 1430 148 252 -59 A N ATOM 862 CA VAL A 110 12.215 12.977 22.169 1.00 13.05 A C ANISOU 862 CA VAL A 110 287 3142 1528 171 172 -28 A C ATOM 863 C VAL A 110 10.844 12.649 21.576 1.00 12.29 A C ANISOU 863 C VAL A 110 299 2739 1632 161 217 -83 A C ATOM 864 O VAL A 110 10.566 11.487 21.287 1.00 13.30 A O ANISOU 864 O VAL A 110 289 2759 2004 153 199 -170 A O ATOM 865 CB VAL A 110 13.339 12.629 21.147 1.00 13.55 A C ANISOU 865 CB VAL A 110 293 3415 1439 225 164 -24 A C ATOM 866 CG1 VAL A 110 13.184 13.504 19.903 1.00 14.43 A C ANISOU 866 CG1 VAL A 110 282 3614 1585 31 195 153 A C ATOM 867 CG2 VAL A 110 14.718 12.835 21.794 1.00 15.29 A C ANISOU 867 CG2 VAL A 110 255 3621 1932 89 8 59 A C ATOM 868 N HIS A 111 9.994 13.654 21.409 1.00 12.41 A N ANISOU 868 N HIS A 111 271 2716 1729 85 142 -86 A N ATOM 869 CA HIS A 111 8.645 13.364 20.929 1.00 12.61 A C ANISOU 869 CA HIS A 111 282 2806 1703 -54 200 -15 A C ATOM 870 C HIS A 111 8.125 14.365 19.923 1.00 11.93 A C ANISOU 870 C HIS A 111 299 2620 1614 40 244 -118 A C ATOM 871 O HIS A 111 8.560 15.512 19.864 1.00 12.80 A O ANISOU 871 O HIS A 111 269 2635 1958 115 128 -39 A O ATOM 872 CB HIS A 111 7.643 13.211 22.091 1.00 12.84 A C ANISOU 872 CB HIS A 111 337 2840 1703 -38 346 -74 A C ATOM 873 CG HIS A 111 7.092 14.511 22.588 1.00 13.20 A C ANISOU 873 CG HIS A 111 339 2903 1773 27 357 -124 A C ATOM 874 CD2 HIS A 111 7.543 15.360 23.540 1.00 13.83 A C ANISOU 874 CD2 HIS A 111 370 2930 1955 0 439 -304 A C ATOM 875 ND1 HIS A 111 5.947 15.084 22.072 1.00 13.68 A N ANISOU 875 ND1 HIS A 111 390 3000 1808 -49 460 -54 A N ATOM 876 CE1 HIS A 111 5.720 16.230 22.686 1.00 14.00 A C ANISOU 876 CE1 HIS A 111 340 3199 1781 10 359 -175 A C ATOM 877 NE2 HIS A 111 6.665 16.417 23.590 1.00 13.86 A N ANISOU 877 NE2 HIS A 111 368 3055 1844 0 425 -185 A N ATOM 878 N CYS A 112 7.156 13.908 19.154 1.00 0.00 A N ATOM 879 CA CYS A 112 6.321 14.766 18.318 1.00 0.00 A C ATOM 880 C CYS A 112 4.855 14.526 18.591 1.00 0.00 A C ATOM 881 O CYS A 112 4.536 14.112 19.708 1.00 0.00 A O ATOM 882 CB CYS A 112 6.692 14.523 16.842 1.00 0.00 A C ATOM 883 SG CYS A 112 6.467 12.785 16.403 1.00 0.00 A S ATOM 884 N ALA A 113 4.004 14.721 17.617 1.00 16.37 A N ANISOU 884 N ALA A 113 302 3907 2011 -97 286 -238 A N ATOM 885 CA ALA A 113 2.583 14.404 17.811 1.00 17.29 A C ANISOU 885 CA ALA A 113 294 3923 2352 -74 291 -335 A C ATOM 886 C ALA A 113 2.363 12.903 17.637 1.00 17.43 A C ANISOU 886 C ALA A 113 286 3998 2339 -135 252 -368 A C ATOM 887 O ALA A 113 1.832 12.227 18.530 1.00 17.63 A O ANISOU 887 O ALA A 113 329 4007 2363 -92 399 -373 A O ATOM 888 CB ALA A 113 1.735 15.193 16.839 1.00 17.76 A C ANISOU 888 CB ALA A 113 285 4101 2363 -108 252 -320 A C ATOM 889 N ALA A 114 2.778 12.383 16.484 1.00 16.78 A N ANISOU 889 N ALA A 114 311 3819 2247 -209 320 -394 A N ATOM 890 CA ALA A 114 2.620 10.971 16.175 1.00 16.95 A C ANISOU 890 CA ALA A 114 329 3810 2300 -305 349 -417 A C ATOM 891 C ALA A 114 3.785 10.090 16.616 1.00 16.02 A C ANISOU 891 C ALA A 114 337 3564 2187 -384 322 -450 A C ATOM 892 O ALA A 114 3.663 8.862 16.613 1.00 16.87 A O ANISOU 892 O ALA A 114 435 3540 2433 -520 531 -467 A O ATOM 893 CB ALA A 114 2.353 10.781 14.689 1.00 16.95 A C ANISOU 893 CB ALA A 114 340 3804 2297 -406 320 -306 A C ATOM 894 N GLY A 115 4.918 10.695 16.971 1.00 15.16 A N ANISOU 894 N GLY A 115 324 3355 2081 -296 310 -379 A N ATOM 895 CA GLY A 115 6.106 9.918 17.296 1.00 14.90 A C ANISOU 895 CA GLY A 115 306 3379 1976 -86 296 -351 A C ATOM 896 C GLY A 115 6.717 9.197 16.100 1.00 13.89 A C ANISOU 896 C GLY A 115 328 3025 1923 -207 329 -225 A C ATOM 897 O GLY A 115 7.319 8.128 16.245 1.00 14.66 A O ANISOU 897 O GLY A 115 447 3052 2072 -208 348 -160 A O ATOM 898 N VAL A 116 6.560 9.793 14.919 1.00 14.05 A N ANISOU 898 N VAL A 116 284 3253 1800 -161 195 -216 A N ATOM 899 CA VAL A 116 6.996 9.176 13.670 1.00 14.16 A C ANISOU 899 CA VAL A 116 428 3093 1861 -250 175 -186 A C ATOM 900 C VAL A 116 8.018 10.032 12.913 1.00 13.47 A C ANISOU 900 C VAL A 116 291 2967 1860 -49 225 -120 A C ATOM 901 O VAL A 116 9.107 9.550 12.555 1.00 13.92 A O ANISOU 901 O VAL A 116 284 3055 1949 87 217 -23 A O ATOM 902 CB VAL A 116 5.776 8.881 12.752 1.00 14.06 A C ANISOU 902 CB VAL A 116 320 3100 1923 -274 175 -270 A C ATOM 903 CG1 VAL A 116 6.225 8.426 11.376 1.00 14.88 A C ANISOU 903 CG1 VAL A 116 397 3264 1993 -313 285 -307 A C ATOM 904 CG2 VAL A 116 4.884 7.828 13.383 1.00 16.56 A C ANISOU 904 CG2 VAL A 116 577 3537 2178 -460 295 -219 A C ATOM 905 N ASN A 117 7.660 11.289 12.656 1.00 13.24 A N ANISOU 905 N ASN A 117 364 2991 1676 6 76 3 A N ATOM 906 CA ASN A 117 8.381 12.093 11.674 1.00 12.59 A C ANISOU 906 CA ASN A 117 263 2882 1638 162 -6 -106 A C ATOM 907 C ASN A 117 9.349 13.081 12.278 1.00 12.84 A C ANISOU 907 C ASN A 117 259 2910 1709 120 -20 -227 A C ATOM 908 O ASN A 117 10.562 12.911 12.112 1.00 13.12 A O ANISOU 908 O ASN A 117 281 2982 1721 272 10 -120 A O ATOM 909 CB ASN A 117 7.435 12.787 10.698 1.00 13.08 A C ANISOU 909 CB ASN A 117 262 3089 1615 156 -5 -60 A C ATOM 910 CG ASN A 117 6.878 11.841 9.664 1.00 13.98 A C ANISOU 910 CG ASN A 117 315 3181 1817 375 70 -342 A C ATOM 911 ND2 ASN A 117 5.628 12.089 9.253 1.00 16.78 A N ANISOU 911 ND2 ASN A 117 299 3840 2237 305 -225 -276 A N ATOM 912 OD1 ASN A 117 7.531 10.896 9.243 1.00 14.87 A O ANISOU 912 OD1 ASN A 117 271 3364 2014 227 23 -254 A O ATOM 913 N ARG A 118 8.889 14.107 12.980 1.00 12.34 A N ANISOU 913 N ARG A 118 259 2799 1632 107 31 -186 A N ATOM 914 CA ARG A 118 9.831 15.103 13.527 1.00 11.82 A C ANISOU 914 CA ARG A 118 267 2594 1629 103 109 -38 A C ATOM 915 C ARG A 118 10.729 14.424 14.542 1.00 11.50 A C ANISOU 915 C ARG A 118 273 2554 1544 98 85 19 A C ATOM 916 O ARG A 118 11.985 14.620 14.525 1.00 12.70 A O ANISOU 916 O ARG A 118 260 2824 1743 56 92 61 A O ATOM 917 CB ARG A 118 9.085 16.270 14.170 1.00 12.41 A C ANISOU 917 CB ARG A 118 291 2671 1755 226 152 -49 A C ATOM 918 CG ARG A 118 8.391 17.142 13.130 1.00 13.79 A C ANISOU 918 CG ARG A 118 318 3057 1862 408 94 37 A C ATOM 919 CD ARG A 118 7.344 18.039 13.758 1.00 14.75 A C ANISOU 919 CD ARG A 118 335 2939 2329 230 364 71 A C ATOM 920 NE ARG A 118 6.150 17.256 14.113 1.00 14.64 A N ANISOU 920 NE ARG A 118 289 3224 2047 309 71 10 A N ATOM 921 CZ ARG A 118 5.031 17.806 14.599 1.00 15.22 A C ANISOU 921 CZ ARG A 118 322 3240 2222 443 74 125 A C ATOM 922 NH1 ARG A 118 4.963 19.116 14.800 1.00 15.41 A N ANISOU 922 NH1 ARG A 118 291 3323 2241 328 -77 0 A N ATOM 923 NH2 ARG A 118 4.005 17.005 14.898 1.00 15.72 A N ANISOU 923 NH2 ARG A 118 282 3528 2161 231 151 20 A N ATOM 924 N SER A 119 10.156 13.633 15.434 1.00 11.45 A N ANISOU 924 N SER A 119 265 2585 1499 145 71 125 A N ATOM 925 CA SER A 119 10.934 12.938 16.469 1.00 11.91 A C ANISOU 925 CA SER A 119 395 2560 1571 85 219 87 A C ATOM 926 C SER A 119 11.746 11.812 15.867 1.00 11.82 A C ANISOU 926 C SER A 119 267 2563 1660 131 93 -6 A C ATOM 927 O SER A 119 12.937 11.641 16.210 1.00 12.43 A O ANISOU 927 O SER A 119 267 2777 1676 164 57 -6 A O ATOM 928 CB SER A 119 9.971 12.429 17.552 1.00 12.27 A C ANISOU 928 CB SER A 119 412 2590 1659 -20 260 43 A C ATOM 929 OG SER A 119 8.938 11.641 16.963 1.00 13.78 A O ANISOU 929 OG SER A 119 342 2858 2037 -193 366 -38 A O ATOM 930 N GLY A 120 11.152 11.004 14.989 1.00 11.82 A N ANISOU 930 N GLY A 120 260 2603 1626 40 92 -39 A N ATOM 931 CA GLY A 120 11.886 9.920 14.345 1.00 11.99 A C ANISOU 931 CA GLY A 120 465 2442 1648 -113 263 52 A C ATOM 932 C GLY A 120 13.092 10.479 13.621 1.00 11.38 A C ANISOU 932 C GLY A 120 276 2493 1553 -74 163 81 A C ATOM 933 O GLY A 120 14.188 9.884 13.680 1.00 12.31 A O ANISOU 933 O GLY A 120 264 2655 1756 108 99 44 A O ATOM 934 N ALA A 121 12.954 11.606 12.950 1.00 11.12 A N ANISOU 934 N ALA A 121 295 2474 1456 -104 197 164 A N ATOM 935 CA ALA A 121 14.095 12.179 12.199 1.00 11.08 A C ANISOU 935 CA ALA A 121 274 2477 1460 -151 103 135 A C ATOM 936 C ALA A 121 15.212 12.605 13.140 1.00 11.54 A C ANISOU 936 C ALA A 121 253 2526 1604 15 14 -52 A C ATOM 937 O ALA A 121 16.399 12.400 12.813 1.00 12.42 A O ANISOU 937 O ALA A 121 287 2703 1729 276 64 -20 A O ATOM 938 CB ALA A 121 13.644 13.347 11.355 1.00 11.84 A C ANISOU 938 CB ALA A 121 289 2732 1476 -8 204 311 A C ATOM 939 N MET A 122 14.917 13.200 14.285 1.00 11.24 A N ANISOU 939 N MET A 122 260 2472 1536 121 -40 -153 A N ATOM 940 CA MET A 122 15.965 13.604 15.234 1.00 11.44 A C ANISOU 940 CA MET A 122 256 2486 1605 -50 58 -99 A C ATOM 941 C MET A 122 16.610 12.395 15.832 1.00 11.75 A C ANISOU 941 C MET A 122 258 2538 1668 30 76 -20 A C ATOM 942 O MET A 122 17.847 12.420 16.058 1.00 13.24 A O ANISOU 942 O MET A 122 260 2964 1807 123 41 -117 A O ATOM 943 CB MET A 122 15.404 14.526 16.324 1.00 12.27 A C ANISOU 943 CB MET A 122 263 2612 1787 -40 74 -186 A C ATOM 944 CG MET A 122 14.919 15.862 15.774 1.00 13.75 A C ANISOU 944 CG MET A 122 273 2624 2329 -100 182 -93 A C ATOM 945 SD MET A 122 16.263 16.729 14.907 1.00 15.59 A S ANISOU 945 SD MET A 122 255 3012 2654 38 65 95 A S ATOM 946 CE MET A 122 15.391 18.232 14.405 1.00 20.03 A C ANISOU 946 CE MET A 122 522 3023 4065 15 -208 463 A C ATOM 947 N ILE A 123 15.878 11.314 16.068 1.00 11.60 A N ANISOU 947 N ILE A 123 273 2476 1659 164 104 108 A N ATOM 948 CA ILE A 123 16.482 10.081 16.570 1.00 11.88 A C ANISOU 948 CA ILE A 123 430 2486 1597 93 142 -13 A C ATOM 949 C ILE A 123 17.366 9.450 15.505 1.00 11.83 A C ANISOU 949 C ILE A 123 265 2651 1580 145 59 -79 A C ATOM 950 O ILE A 123 18.488 8.978 15.797 1.00 12.75 A O ANISOU 950 O ILE A 123 275 2794 1775 235 0 0 A O ATOM 951 CB ILE A 123 15.387 9.069 17.012 1.00 12.79 A C ANISOU 951 CB ILE A 123 544 2517 1800 74 263 93 A C ATOM 952 CG1 ILE A 123 14.682 9.552 18.287 1.00 15.14 A C ANISOU 952 CG1 ILE A 123 934 3079 1738 175 240 -34 A C ATOM 953 CG2 ILE A 123 15.937 7.664 17.147 1.00 14.38 A C ANISOU 953 CG2 ILE A 123 780 2592 2090 192 263 131 A C ATOM 954 CD1 ILE A 123 15.587 9.710 19.505 1.00 15.91 A C ANISOU 954 CD1 ILE A 123 1001 3212 1831 372 6 172 A C ATOM 955 N LEU A 124 16.929 9.438 14.254 1.00 11.85 A N ANISOU 955 N LEU A 124 273 2707 1521 201 48 -174 A N ATOM 956 CA LEU A 124 17.764 8.899 13.172 1.00 12.19 A C ANISOU 956 CA LEU A 124 412 2666 1553 130 43 -151 A C ATOM 957 C LEU A 124 19.036 9.725 13.049 1.00 12.01 A C ANISOU 957 C LEU A 124 276 2547 1738 227 18 -97 A C ATOM 958 O LEU A 124 20.155 9.163 12.895 1.00 13.29 A O ANISOU 958 O LEU A 124 348 2790 1911 461 115 -87 A O ATOM 959 CB LEU A 124 16.971 8.891 11.865 1.00 11.72 A C ANISOU 959 CB LEU A 124 260 2725 1468 134 -5 -158 A C ATOM 960 CG LEU A 124 17.572 8.208 10.652 1.00 15.17 A C ANISOU 960 CG LEU A 124 579 3508 1676 562 -186 -322 A C ATOM 961 CD1 LEU A 124 18.275 6.891 10.947 1.00 18.57 A C ANISOU 961 CD1 LEU A 124 1288 3528 2240 612 -230 -216 A C ATOM 962 CD2 LEU A 124 16.574 8.036 9.516 1.00 14.35 A C ANISOU 962 CD2 LEU A 124 265 3607 1580 196 -57 -434 A C ATOM 963 N ALA A 125 18.926 11.044 13.103 1.00 12.04 A N ANISOU 963 N ALA A 125 260 2514 1800 123 8 -65 A N ATOM 964 CA ALA A 125 20.114 11.918 13.069 1.00 12.17 A C ANISOU 964 CA ALA A 125 256 2657 1710 93 3 20 A C ATOM 965 C ALA A 125 21.047 11.590 14.229 1.00 12.85 A C ANISOU 965 C ALA A 125 276 2946 1659 247 -5 -7 A C ATOM 966 O ALA A 125 22.278 11.475 14.042 1.00 14.23 A O ANISOU 966 O ALA A 125 311 3140 1957 388 91 -27 A O ATOM 967 CB ALA A 125 19.714 13.372 13.172 1.00 12.67 A C ANISOU 967 CB ALA A 125 254 2576 1982 43 -21 -38 A C ATOM 968 N TYR A 126 20.511 11.391 15.416 1.00 12.97 A N ANISOU 968 N TYR A 126 311 3084 1532 401 -6 107 A N ATOM 969 CA TYR A 126 21.338 11.075 16.584 1.00 13.85 A C ANISOU 969 CA TYR A 126 434 3215 1615 553 -5 0 A C ATOM 970 C TYR A 126 22.086 9.791 16.323 1.00 14.71 A C ANISOU 970 C TYR A 126 434 3305 1852 636 -31 -137 A C ATOM 971 O TYR A 126 23.318 9.728 16.511 1.00 16.15 A O ANISOU 971 O TYR A 126 408 3718 2011 727 -119 -304 A O ATOM 972 CB TYR A 126 20.478 10.957 17.838 1.00 14.61 A C ANISOU 972 CB TYR A 126 663 3395 1492 697 6 46 A C ATOM 973 CG TYR A 126 21.262 10.603 19.091 1.00 14.93 A C ANISOU 973 CG TYR A 126 692 3339 1640 916 -197 19 A C ATOM 974 CD1 TYR A 126 22.457 11.257 19.403 1.00 17.35 A C ANISOU 974 CD1 TYR A 126 944 3734 1914 856 -362 -186 A C ATOM 975 CD2 TYR A 126 20.819 9.622 19.967 1.00 16.21 A C ANISOU 975 CD2 TYR A 126 974 3501 1685 1115 -109 120 A C ATOM 976 CE1 TYR A 126 23.173 10.933 20.555 1.00 18.35 A C ANISOU 976 CE1 TYR A 126 1316 4007 1650 1067 -394 -82 A C ATOM 977 CE2 TYR A 126 21.529 9.294 21.124 1.00 18.23 A C ANISOU 977 CE2 TYR A 126 1360 3783 1782 1120 -115 115 A C ATOM 978 CZ TYR A 126 22.709 9.953 21.421 1.00 18.75 A C ANISOU 978 CZ TYR A 126 1421 4011 1692 1111 -292 -142 A C ATOM 979 OH TYR A 126 23.425 9.622 22.559 1.00 22.28 A O ANISOU 979 OH TYR A 126 1624 4874 1967 1216 -337 6 A O ATOM 980 N LEU A 127 21.388 8.746 15.890 1.00 14.44 A N ANISOU 980 N LEU A 127 419 3224 1844 701 -41 -129 A N ATOM 981 CA LEU A 127 22.063 7.468 15.662 1.00 15.89 A C ANISOU 981 CA LEU A 127 832 3185 2020 706 31 -93 A C ATOM 982 C LEU A 127 23.111 7.561 14.560 1.00 14.84 A C ANISOU 982 C LEU A 127 518 3046 2073 744 -48 -153 A C ATOM 983 O LEU A 127 24.214 6.999 14.710 1.00 16.30 A O ANISOU 983 O LEU A 127 553 3287 2354 922 -219 -74 A O ATOM 984 CB LEU A 127 21.048 6.365 15.381 1.00 16.30 A C ANISOU 984 CB LEU A 127 848 3192 2152 700 91 -34 A C ATOM 985 CG LEU A 127 20.119 6.037 16.561 1.00 19.19 A C ANISOU 985 CG LEU A 127 1324 3650 2317 731 348 98 A C ATOM 986 CD1 LEU A 127 19.009 5.105 16.128 1.00 22.03 A C ANISOU 986 CD1 LEU A 127 1659 3670 3041 627 553 6 A C ATOM 987 CD2 LEU A 127 20.897 5.437 17.738 1.00 23.27 A C ANISOU 987 CD2 LEU A 127 1993 4192 2657 832 485 390 A C ATOM 988 N MET A 128 22.831 8.288 13.484 1.00 14.87 A N ANISOU 988 N MET A 128 394 3255 2000 649 -46 -227 A N ATOM 989 CA MET A 128 23.828 8.464 12.435 1.00 15.33 A C ANISOU 989 CA MET A 128 497 3300 2029 465 -49 -373 A C ATOM 990 C MET A 128 25.027 9.207 13.017 1.00 15.53 A C ANISOU 990 C MET A 128 342 3418 2140 527 -51 -516 A C ATOM 991 O MET A 128 26.198 8.886 12.671 1.00 17.14 A O ANISOU 991 O MET A 128 390 3842 2280 684 -26 -684 A O ATOM 992 CB MET A 128 23.271 9.259 11.254 1.00 14.71 A C ANISOU 992 CB MET A 128 311 3258 2020 417 -35 -285 A C ATOM 993 CG MET A 128 22.174 8.552 10.453 1.00 15.33 A C ANISOU 993 CG MET A 128 260 3425 2140 116 -77 -254 A C ATOM 994 SD MET A 128 22.579 6.918 9.816 1.00 15.80 A S ANISOU 994 SD MET A 128 304 3413 2286 263 43 -215 A S ATOM 995 CE MET A 128 23.885 7.300 8.613 1.00 17.51 A C ANISOU 995 CE MET A 128 399 3573 2682 148 274 -162 A C ATOM 996 N SER A 129 24.796 10.180 13.884 1.00 16.25 A N ANISOU 996 N SER A 129 348 3594 2231 555 -164 -658 A N ATOM 997 CA SER A 129 25.874 11.029 14.410 1.00 18.04 A C ANISOU 997 CA SER A 129 456 3968 2430 604 -285 -797 A C ATOM 998 C SER A 129 26.783 10.204 15.299 1.00 19.20 A C ANISOU 998 C SER A 129 427 4280 2587 798 -324 -744 A C ATOM 999 O SER A 129 27.987 10.494 15.396 1.00 21.59 A O ANISOU 999 O SER A 129 375 4781 3048 666 -366 -794 A O ATOM 1000 CB SER A 129 25.347 12.239 15.192 1.00 17.67 A C ANISOU 1000 CB SER A 129 359 3925 2428 563 -326 -864 A C ATOM 1001 OG SER A 129 24.861 11.875 16.477 1.00 20.04 A O ANISOU 1001 OG SER A 129 353 4695 2567 656 -195 -807 A O ATOM 1002 N LYS A 130 26.229 9.181 15.942 1.00 20.20 A N ANISOU 1002 N LYS A 130 568 4514 2592 1110 -395 -606 A N ATOM 1003 CA LYS A 130 26.978 8.364 16.895 1.00 22.76 A C ANISOU 1003 CA LYS A 130 1168 4820 2657 1421 -386 -640 A C ATOM 1004 C LYS A 130 27.735 7.264 16.173 1.00 22.13 A C ANISOU 1004 C LYS A 130 864 4760 2786 1359 -315 -653 A C ATOM 1005 O LYS A 130 28.651 6.665 16.747 1.00 22.88 A O ANISOU 1005 O LYS A 130 752 4935 3007 1492 -414 -557 A O ATOM 1006 CB LYS A 130 26.025 7.767 17.935 1.00 24.04 A C ANISOU 1006 CB LYS A 130 1544 5095 2495 1544 -361 -568 A C ATOM 1007 CG LYS A 130 25.729 8.687 19.102 1.00 29.75 A C ANISOU 1007 CG LYS A 130 2416 6050 2836 2002 -487 -913 A C ATOM 1008 CD LYS A 130 26.651 8.383 20.288 1.00 38.03 A C ANISOU 1008 CD LYS A 130 3700 7458 3291 2257 -631 -1482 A C ATOM 1009 CE LYS A 130 26.523 9.404 21.408 1.00 41.31 A C ANISOU 1009 CE LYS A 130 4099 7746 3851 2404 -608 -1826 A C ATOM 1010 NZ LYS A 130 27.609 10.435 21.343 1.00 44.20 A N ANISOU 1010 NZ LYS A 130 4663 7846 4284 2345 -326 -2016 A N ATOM 1011 N ASN A 131 27.379 6.998 14.920 1.00 21.56 A N ANISOU 1011 N ASN A 131 640 4726 2827 1315 -229 -750 A N ATOM 1012 CA ASN A 131 28.062 5.957 14.152 1.00 21.38 A C ANISOU 1012 CA ASN A 131 661 4650 2811 1132 -153 -719 A C ATOM 1013 C ASN A 131 29.427 6.410 13.661 1.00 20.85 A C ANISOU 1013 C ASN A 131 601 4508 2813 1115 -274 -590 A C ATOM 1014 O ASN A 131 29.512 7.325 12.842 1.00 21.40 A O ANISOU 1014 O ASN A 131 562 4591 2976 1055 -472 -403 A O ATOM 1015 CB ASN A 131 27.216 5.516 12.954 1.00 20.91 A C ANISOU 1015 CB ASN A 131 544 4627 2775 1111 -54 -762 A C ATOM 1016 CG ASN A 131 28.009 4.668 11.969 1.00 20.44 A C ANISOU 1016 CG ASN A 131 493 4318 2953 955 25 -736 A C ATOM 1017 ND2 ASN A 131 27.997 5.062 10.700 1.00 20.89 A N ANISOU 1017 ND2 ASN A 131 368 4672 2899 649 120 -671 A N ATOM 1018 OD1 ASN A 131 28.637 3.679 12.354 1.00 22.84 A O ANISOU 1018 OD1 ASN A 131 1129 4140 3409 715 38 -825 A O ATOM 1019 N LYS A 132 30.484 5.754 14.159 1.00 20.37 A N ANISOU 1019 N LYS A 132 500 4329 2910 983 -272 -483 A N ATOM 1020 CA LYS A 132 31.873 6.003 13.735 1.00 20.99 A C ANISOU 1020 CA LYS A 132 527 4286 3163 908 -274 -604 A C ATOM 1021 C LYS A 132 32.470 4.767 13.052 1.00 20.29 A C ANISOU 1021 C LYS A 132 518 4158 3034 1000 -262 -439 A C ATOM 1022 O LYS A 132 33.600 4.807 12.531 1.00 22.30 A O ANISOU 1022 O LYS A 132 848 4350 3276 974 -19 -377 A O ATOM 1023 CB LYS A 132 32.731 6.401 14.940 1.00 22.10 A C ANISOU 1023 CB LYS A 132 706 4370 3321 832 -322 -662 A C ATOM 1024 CG LYS A 132 32.185 7.560 15.761 1.00 26.75 A C ANISOU 1024 CG LYS A 132 1412 4798 3953 498 -450 -1212 A C ATOM 1025 CD LYS A 132 33.124 7.939 16.890 1.00 34.43 A C ANISOU 1025 CD LYS A 132 2791 5482 4809 153 -441 -1534 A C ATOM 1026 CE LYS A 132 33.815 9.268 16.603 1.00 38.65 A C ANISOU 1026 CE LYS A 132 3495 5881 5310 23 -208 -1586 A C ATOM 1027 NZ LYS A 132 34.854 9.568 17.634 1.00 41.36 A N ANISOU 1027 NZ LYS A 132 3948 6168 5598 31 -52 -1430 A N ATOM 1028 N GLU A 133 31.713 3.670 13.068 1.00 21.01 A N ANISOU 1028 N GLU A 133 743 4214 3025 1067 -337 -571 A N ATOM 1029 CA GLU A 133 32.227 2.344 12.714 1.00 21.55 A C ANISOU 1029 CA GLU A 133 864 4280 3043 1180 -505 -627 A C ATOM 1030 C GLU A 133 31.814 1.881 11.319 1.00 21.18 A C ANISOU 1030 C GLU A 133 719 4311 3018 1312 -456 -675 A C ATOM 1031 O GLU A 133 32.641 1.338 10.570 1.00 22.64 A O ANISOU 1031 O GLU A 133 898 4487 3219 1303 -373 -768 A O ATOM 1032 CB GLU A 133 31.763 1.299 13.737 1.00 22.57 A C ANISOU 1032 CB GLU A 133 1112 4435 3030 1221 -493 -549 A C ATOM 1033 CG GLU A 133 32.320 1.477 15.141 1.00 23.21 A C ANISOU 1033 CG GLU A 133 903 4758 3156 1348 -603 -640 A C ATOM 1034 CD GLU A 133 33.593 0.682 15.369 1.00 23.54 A C ANISOU 1034 CD GLU A 133 798 5120 3027 1316 -230 -913 A C ATOM 1035 OE1 GLU A 133 33.731 -0.408 14.781 1.00 26.77 A O ANISOU 1035 OE1 GLU A 133 1225 5303 3643 1588 -542 -970 A O ATOM 1036 OE2 GLU A 133 34.435 1.145 16.159 1.00 22.31 A O ANISOU 1036 OE2 GLU A 133 439 4586 3452 831 -393 -568 A O ATOM 1037 N SER A 134 30.537 2.075 10.986 1.00 20.85 A N ANISOU 1037 N SER A 134 588 4257 3077 1054 -390 -688 A N ATOM 1038 CA SER A 134 29.943 1.431 9.817 1.00 21.39 A C ANISOU 1038 CA SER A 134 621 4508 3000 864 -164 -630 A C ATOM 1039 C SER A 134 29.787 2.371 8.627 1.00 20.53 A C ANISOU 1039 C SER A 134 427 4494 2881 841 -10 -709 A C ATOM 1040 O SER A 134 29.643 3.576 8.810 1.00 20.50 A O ANISOU 1040 O SER A 134 428 4582 2779 858 -28 -696 A O ATOM 1041 CB SER A 134 28.569 0.864 10.215 1.00 21.71 A C ANISOU 1041 CB SER A 134 688 4539 3021 702 -204 -535 A C ATOM 1042 OG SER A 134 28.680 -0.130 11.229 1.00 26.07 A O ANISOU 1042 OG SER A 134 1191 5216 3497 640 -87 -197 A O ATOM 1043 N LEU A 135 29.814 1.826 7.412 1.00 20.77 A N ANISOU 1043 N LEU A 135 456 4519 2915 784 49 -749 A N ATOM 1044 CA LEU A 135 29.584 2.638 6.214 1.00 20.53 A C ANISOU 1044 CA LEU A 135 456 4503 2842 680 219 -719 A C ATOM 1045 C LEU A 135 28.234 3.331 6.363 1.00 18.80 A C ANISOU 1045 C LEU A 135 306 4106 2730 386 135 -487 A C ATOM 1046 O LEU A 135 27.245 2.658 6.610 1.00 18.79 A O ANISOU 1046 O LEU A 135 480 3937 2721 274 108 -361 A O ATOM 1047 CB LEU A 135 29.598 1.776 4.943 1.00 22.63 A C ANISOU 1047 CB LEU A 135 776 4798 3025 658 193 -872 A C ATOM 1048 CG LEU A 135 30.868 0.957 4.693 1.00 27.13 A C ANISOU 1048 CG LEU A 135 1298 5403 3607 702 384 -1230 A C ATOM 1049 CD1 LEU A 135 30.627 -0.114 3.643 1.00 30.37 A C ANISOU 1049 CD1 LEU A 135 1949 5752 3837 803 293 -1419 A C ATOM 1050 CD2 LEU A 135 32.035 1.858 4.284 1.00 31.32 A C ANISOU 1050 CD2 LEU A 135 1527 6165 4208 496 397 -1474 A C ATOM 1051 N PRO A 136 28.205 4.660 6.233 1.00 17.99 A N ANISOU 1051 N PRO A 136 285 3935 2614 217 189 -310 A N ATOM 1052 CA PRO A 136 26.963 5.409 6.468 1.00 17.65 A C ANISOU 1052 CA PRO A 136 264 3844 2597 180 57 -245 A C ATOM 1053 C PRO A 136 25.777 4.871 5.677 1.00 17.43 A C ANISOU 1053 C PRO A 136 284 3896 2441 98 0 -164 A C ATOM 1054 O PRO A 136 24.676 4.794 6.234 1.00 17.20 A O ANISOU 1054 O PRO A 136 264 3727 2545 161 80 -208 A O ATOM 1055 CB PRO A 136 27.326 6.823 6.026 1.00 18.11 A C ANISOU 1055 CB PRO A 136 259 3856 2766 136 -41 -186 A C ATOM 1056 CG PRO A 136 28.777 6.924 6.339 1.00 18.68 A C ANISOU 1056 CG PRO A 136 260 3932 2906 0 138 -170 A C ATOM 1057 CD PRO A 136 29.357 5.561 6.024 1.00 18.65 A C ANISOU 1057 CD PRO A 136 276 4029 2781 90 220 -331 A C ATOM 1058 N MET A 137 25.964 4.503 4.413 1.00 17.90 A N ANISOU 1058 N MET A 137 331 4077 2395 -15 -43 -170 A N ATOM 1059 CA MET A 137 24.809 4.032 3.613 1.00 19.83 A C ANISOU 1059 CA MET A 137 734 4419 2381 -142 -57 -153 A C ATOM 1060 C MET A 137 24.192 2.783 4.245 1.00 18.70 A C ANISOU 1060 C MET A 137 579 4018 2509 57 148 -296 A C ATOM 1061 O MET A 137 22.962 2.652 4.356 1.00 18.80 A O ANISOU 1061 O MET A 137 460 3971 2712 109 208 -384 A O ATOM 1062 CB MET A 137 25.214 3.765 2.159 1.00 22.36 A C ANISOU 1062 CB MET A 137 1307 4888 2301 -340 -174 -120 A C ATOM 1063 CG MET A 137 24.155 2.988 1.399 1.00 27.32 A C ANISOU 1063 CG MET A 137 2117 5799 2465 -706 -230 -153 A C ATOM 1064 SD MET A 137 24.675 2.420 -0.217 0.50 31.00 A S ANISOU 1064 SD MET A 137 3253 5971 2554 -856 -107 -315 A S ATOM 1065 CE MET A 137 26.432 2.167 0.041 1.00 34.11 A C ANISOU 1065 CE MET A 137 3634 6610 2718 -837 -142 -401 A C ATOM 1066 N LEU A 138 25.037 1.857 4.686 1.00 19.23 A N ANISOU 1066 N LEU A 138 708 3822 2775 195 225 -359 A N ATOM 1067 CA LEU A 138 24.575 0.610 5.278 1.00 19.86 A C ANISOU 1067 CA LEU A 138 939 3625 2982 410 357 -467 A C ATOM 1068 C LEU A 138 23.963 0.875 6.640 1.00 18.00 A C ANISOU 1068 C LEU A 138 601 3395 2845 410 271 -364 A C ATOM 1069 O LEU A 138 22.923 0.316 6.982 1.00 18.87 A O ANISOU 1069 O LEU A 138 697 3476 2996 263 324 -322 A O ATOM 1070 CB LEU A 138 25.727 -0.387 5.430 1.00 22.00 A C ANISOU 1070 CB LEU A 138 1254 3704 3400 540 518 -627 A C ATOM 1071 CG LEU A 138 26.264 -1.026 4.151 1.00 27.00 A C ANISOU 1071 CG LEU A 138 2184 4079 3995 688 925 -860 A C ATOM 1072 CD1 LEU A 138 27.491 -1.871 4.474 1.00 31.02 A C ANISOU 1072 CD1 LEU A 138 2657 4307 4823 961 1347 -1080 A C ATOM 1073 CD2 LEU A 138 25.191 -1.887 3.498 1.00 31.25 A C ANISOU 1073 CD2 LEU A 138 2985 4438 4449 649 952 -1132 A C ATOM 1074 N TYR A 139 24.602 1.735 7.432 1.00 17.45 A N ANISOU 1074 N TYR A 139 627 3343 2660 471 87 -219 A N ATOM 1075 CA TYR A 139 24.096 2.031 8.770 1.00 17.16 A C ANISOU 1075 CA TYR A 139 557 3433 2529 557 -63 -65 A C ATOM 1076 C TYR A 139 22.729 2.725 8.683 1.00 16.16 A C ANISOU 1076 C TYR A 139 460 3233 2448 434 -93 0 A C ATOM 1077 O TYR A 139 21.816 2.433 9.483 1.00 17.41 A O ANISOU 1077 O TYR A 139 571 3370 2675 386 -38 98 A O ATOM 1078 CB TYR A 139 25.103 2.868 9.579 1.00 18.01 A C ANISOU 1078 CB TYR A 139 719 3713 2412 584 -152 19 A C ATOM 1079 CG TYR A 139 24.776 2.836 11.054 1.00 18.44 A C ANISOU 1079 CG TYR A 139 597 4065 2345 610 -175 109 A C ATOM 1080 CD1 TYR A 139 24.939 1.656 11.787 1.00 20.16 A C ANISOU 1080 CD1 TYR A 139 864 4352 2442 538 -174 322 A C ATOM 1081 CD2 TYR A 139 24.296 3.959 11.716 1.00 18.37 A C ANISOU 1081 CD2 TYR A 139 329 4244 2406 511 -150 0 A C ATOM 1082 CE1 TYR A 139 24.621 1.608 13.133 1.00 22.71 A C ANISOU 1082 CE1 TYR A 139 1747 4415 2465 531 -219 197 A C ATOM 1083 CE2 TYR A 139 23.987 3.925 13.078 1.00 20.44 A C ANISOU 1083 CE2 TYR A 139 900 4345 2522 522 -59 -15 A C ATOM 1084 CZ TYR A 139 24.141 2.743 13.775 1.00 21.59 A C ANISOU 1084 CZ TYR A 139 1421 4377 2407 384 -241 40 A C ATOM 1085 OH TYR A 139 23.835 2.684 15.109 1.00 24.93 A O ANISOU 1085 OH TYR A 139 2108 4634 2730 269 -82 43 A O ATOM 1086 N PHE A 140 22.583 3.646 7.737 1.00 15.12 A N ANISOU 1086 N PHE A 140 291 2996 2458 252 -126 31 A N ATOM 1087 CA PHE A 140 21.316 4.355 7.511 1.00 13.71 A C ANISOU 1087 CA PHE A 140 285 2739 2187 76 -153 10 A C ATOM 1088 C PHE A 140 20.213 3.358 7.200 1.00 13.51 A C ANISOU 1088 C PHE A 140 346 2750 2037 0 -76 -26 A C ATOM 1089 O PHE A 140 19.125 3.416 7.789 1.00 14.09 A O ANISOU 1089 O PHE A 140 262 2949 2142 96 98 6 A O ATOM 1090 CB PHE A 140 21.468 5.343 6.349 1.00 14.06 A C ANISOU 1090 CB PHE A 140 269 2829 2242 27 -173 99 A C ATOM 1091 CG PHE A 140 20.162 5.931 5.859 1.00 13.37 A C ANISOU 1091 CG PHE A 140 256 2838 1987 14 -71 -17 A C ATOM 1092 CD1 PHE A 140 19.494 6.919 6.589 1.00 13.62 A C ANISOU 1092 CD1 PHE A 140 260 2842 2071 14 -110 -89 A C ATOM 1093 CD2 PHE A 140 19.632 5.489 4.648 1.00 14.76 A C ANISOU 1093 CD2 PHE A 140 408 3165 2037 -74 -96 -130 A C ATOM 1094 CE1 PHE A 140 18.279 7.465 6.105 1.00 14.25 A C ANISOU 1094 CE1 PHE A 140 322 3106 1985 65 82 24 A C ATOM 1095 CE2 PHE A 140 18.435 6.006 4.173 1.00 16.06 A C ANISOU 1095 CE2 PHE A 140 900 3041 2161 46 -259 -35 A C ATOM 1096 CZ PHE A 140 17.766 6.991 4.909 1.00 15.32 A C ANISOU 1096 CZ PHE A 140 719 2985 2117 -27 65 20 A C ATOM 1097 N LEU A 141 20.451 2.436 6.279 1.00 13.80 A N ANISOU 1097 N LEU A 141 460 2621 2161 -49 -43 -62 A N ATOM 1098 CA LEU A 141 19.422 1.449 5.940 1.00 14.71 A C ANISOU 1098 CA LEU A 141 597 2569 2425 -60 20 -65 A C ATOM 1099 C LEU A 141 19.090 0.554 7.131 1.00 15.68 A C ANISOU 1099 C LEU A 141 577 2736 2644 0 86 86 A C ATOM 1100 O LEU A 141 17.926 0.233 7.387 1.00 16.70 A O ANISOU 1100 O LEU A 141 483 2858 3005 -114 219 5 A O ATOM 1101 CB LEU A 141 19.823 0.601 4.731 1.00 15.68 A C ANISOU 1101 CB LEU A 141 776 2648 2533 -137 104 -175 A C ATOM 1102 CG LEU A 141 19.924 1.383 3.411 1.00 17.12 A C ANISOU 1102 CG LEU A 141 912 2912 2680 109 175 -175 A C ATOM 1103 CD1 LEU A 141 20.446 0.468 2.325 1.00 19.02 A C ANISOU 1103 CD1 LEU A 141 926 3370 2930 35 461 -467 A C ATOM 1104 CD2 LEU A 141 18.568 1.985 3.011 1.00 19.10 A C ANISOU 1104 CD2 LEU A 141 802 3179 3276 -38 31 -109 A C ATOM 1105 N TYR A 142 20.119 0.141 7.871 1.00 16.82 A N ANISOU 1105 N TYR A 142 716 2890 2786 225 86 284 A N ATOM 1106 CA TYR A 142 19.924 -0.708 9.033 1.00 18.61 A C ANISOU 1106 CA TYR A 142 1035 3115 2921 410 175 397 A C ATOM 1107 C TYR A 142 19.088 -0.011 10.102 1.00 18.24 A C ANISOU 1107 C TYR A 142 1057 3037 2836 313 164 320 A C ATOM 1108 O TYR A 142 18.099 -0.594 10.595 1.00 19.04 A O ANISOU 1108 O TYR A 142 986 3059 3188 173 322 296 A O ATOM 1109 CB TYR A 142 21.268 -1.174 9.631 1.00 20.94 A C ANISOU 1109 CB TYR A 142 1366 3431 3158 688 186 644 A C ATOM 1110 CG TYR A 142 21.042 -1.905 10.940 1.00 25.78 A C ANISOU 1110 CG TYR A 142 2002 4178 3616 1194 450 1118 A C ATOM 1111 CD1 TYR A 142 20.528 -3.201 10.929 1.00 31.30 A C ANISOU 1111 CD1 TYR A 142 3003 4584 4307 1439 847 1571 A C ATOM 1112 CD2 TYR A 142 21.289 -1.307 12.173 1.00 31.06 A C ANISOU 1112 CD2 TYR A 142 2973 4989 3840 1606 595 1473 A C ATOM 1113 CE1 TYR A 142 20.287 -3.890 12.110 1.00 35.87 A C ANISOU 1113 CE1 TYR A 142 3901 5113 4616 1500 1124 1825 A C ATOM 1114 CE2 TYR A 142 21.049 -1.990 13.365 1.00 35.28 A C ANISOU 1114 CE2 TYR A 142 3828 5414 4162 1694 1000 1720 A C ATOM 1115 CZ TYR A 142 20.550 -3.282 13.323 1.00 37.19 A C ANISOU 1115 CZ TYR A 142 4147 5478 4505 1648 1313 1869 A C ATOM 1116 OH TYR A 142 20.309 -3.976 14.488 1.00 40.20 A O ANISOU 1116 OH TYR A 142 4623 5849 4802 1756 1553 1897 A O ATOM 1117 N VAL A 143 19.474 1.204 10.472 1.00 17.65 A N ANISOU 1117 N VAL A 143 794 3113 2800 270 164 120 A N ATOM 1118 CA VAL A 143 18.756 1.932 11.523 1.00 17.14 A C ANISOU 1118 CA VAL A 143 684 3359 2469 153 71 43 A C ATOM 1119 C VAL A 143 17.327 2.216 11.051 1.00 15.15 A C ANISOU 1119 C VAL A 143 522 3021 2213 6 142 74 A C ATOM 1120 O VAL A 143 16.380 2.042 11.824 1.00 15.53 A O ANISOU 1120 O VAL A 143 666 3086 2150 6 185 31 A O ATOM 1121 CB VAL A 143 19.453 3.249 11.969 1.00 18.19 A C ANISOU 1121 CB VAL A 143 689 3625 2596 193 -31 -173 A C ATOM 1122 CG1 VAL A 143 18.501 4.073 12.869 1.00 19.56 A C ANISOU 1122 CG1 VAL A 143 850 3935 2646 196 17 -252 A C ATOM 1123 CG2 VAL A 143 20.772 2.943 12.678 1.00 21.82 A C ANISOU 1123 CG2 VAL A 143 948 4528 2813 241 -109 -109 A C ATOM 1124 N TYR A 144 17.185 2.656 9.796 1.00 14.00 A N ANISOU 1124 N TYR A 144 406 2845 2069 59 91 49 A N ATOM 1125 CA TYR A 144 15.871 2.990 9.271 1.00 13.74 A C ANISOU 1125 CA TYR A 144 479 2651 2090 -24 148 -74 A C ATOM 1126 C TYR A 144 14.945 1.790 9.412 1.00 13.79 A C ANISOU 1126 C TYR A 144 666 2624 1949 -71 340 -164 A C ATOM 1127 O TYR A 144 13.857 1.878 10.008 1.00 14.34 A O ANISOU 1127 O TYR A 144 392 2879 2178 -71 386 -237 A O ATOM 1128 CB TYR A 144 15.936 3.480 7.800 1.00 13.42 A C ANISOU 1128 CB TYR A 144 269 2770 2060 -1 171 -18 A C ATOM 1129 CG TYR A 144 14.523 3.844 7.396 1.00 13.58 A C ANISOU 1129 CG TYR A 144 269 2969 1920 45 156 -174 A C ATOM 1130 CD1 TYR A 144 14.017 5.083 7.783 1.00 13.87 A C ANISOU 1130 CD1 TYR A 144 333 2944 1992 250 82 -129 A C ATOM 1131 CD2 TYR A 144 13.695 2.960 6.714 1.00 15.46 A C ANISOU 1131 CD2 TYR A 144 300 3373 2201 375 0 -496 A C ATOM 1132 CE1 TYR A 144 12.713 5.435 7.488 1.00 15.53 A C ANISOU 1132 CE1 TYR A 144 593 3359 1949 450 -68 -241 A C ATOM 1133 CE2 TYR A 144 12.370 3.310 6.411 1.00 16.21 A C ANISOU 1133 CE2 TYR A 144 291 3607 2258 355 -63 -688 A C ATOM 1134 CZ TYR A 144 11.901 4.549 6.804 1.00 14.83 A C ANISOU 1134 CZ TYR A 144 405 3328 1903 296 -93 -335 A C ATOM 1135 OH TYR A 144 10.597 4.909 6.522 1.00 18.25 A O ANISOU 1135 OH TYR A 144 304 4056 2574 362 -241 -564 A O ATOM 1136 N HIS A 145 15.340 0.671 8.824 1.00 14.69 A N ANISOU 1136 N HIS A 145 917 2502 2161 -175 480 -228 A N ATOM 1137 CA HIS A 145 14.439 -0.485 8.772 1.00 16.21 A C ANISOU 1137 CA HIS A 145 1254 2517 2389 -184 653 -230 A C ATOM 1138 C HIS A 145 14.230 -1.155 10.117 1.00 17.03 A C ANISOU 1138 C HIS A 145 1316 2687 2469 -184 772 -151 A C ATOM 1139 O HIS A 145 13.114 -1.596 10.417 1.00 18.52 A O ANISOU 1139 O HIS A 145 1360 2908 2768 -362 913 -219 A O ATOM 1140 CB HIS A 145 14.882 -1.466 7.688 1.00 16.78 A C ANISOU 1140 CB HIS A 145 1392 2560 2422 -305 631 -335 A C ATOM 1141 CG HIS A 145 14.593 -0.951 6.318 1.00 18.16 A C ANISOU 1141 CG HIS A 145 1509 2869 2522 -318 489 -377 A C ATOM 1142 CD2 HIS A 145 15.420 -0.580 5.306 1.00 18.79 A C ANISOU 1142 CD2 HIS A 145 1576 3088 2477 -511 355 -296 A C ATOM 1143 ND1 HIS A 145 13.314 -0.734 5.858 1.00 19.58 A N ANISOU 1143 ND1 HIS A 145 1420 3217 2804 -405 386 -549 A N ATOM 1144 CE1 HIS A 145 13.362 -0.258 4.621 1.00 20.03 A C ANISOU 1144 CE1 HIS A 145 1594 3298 2718 -390 294 -548 A C ATOM 1145 NE2 HIS A 145 14.632 -0.158 4.260 1.00 19.34 A N ANISOU 1145 NE2 HIS A 145 1527 3402 2417 -463 229 -465 A N ATOM 1146 N SER A 146 15.269 -1.220 10.941 1.00 17.75 A N ANISOU 1146 N SER A 146 1473 2768 2504 73 776 -54 A N ATOM 1147 CA SER A 146 15.132 -1.851 12.246 1.00 18.58 A C ANISOU 1147 CA SER A 146 1615 2763 2680 296 829 60 A C ATOM 1148 C SER A 146 14.224 -1.016 13.157 1.00 17.62 A C ANISOU 1148 C SER A 146 1532 2644 2520 102 939 0 A C ATOM 1149 O SER A 146 13.400 -1.583 13.884 1.00 18.70 A O ANISOU 1149 O SER A 146 1597 2815 2694 -48 1089 46 A O ATOM 1150 CB SER A 146 16.487 -2.131 12.901 1.00 20.01 A C ANISOU 1150 CB SER A 146 1835 2964 2802 428 715 87 A C ATOM 1151 OG SER A 146 17.208 -0.939 13.151 1.00 22.64 A O ANISOU 1151 OG SER A 146 1851 3357 3393 511 478 98 A O ATOM 1152 N MET A 147 14.351 0.311 13.104 1.00 16.66 A N ANISOU 1152 N MET A 147 1177 2612 2540 74 763 -164 A N ATOM 1153 CA MET A 147 13.469 1.186 13.884 1.00 16.08 A C ANISOU 1153 CA MET A 147 873 2725 2513 -26 564 -252 A C ATOM 1154 C MET A 147 12.029 1.120 13.385 1.00 16.41 A C ANISOU 1154 C MET A 147 840 2933 2460 -153 599 -307 A C ATOM 1155 O MET A 147 11.078 1.118 14.172 1.00 17.64 A O ANISOU 1155 O MET A 147 891 3271 2542 -197 619 -357 A O ATOM 1156 CB MET A 147 13.964 2.638 13.845 1.00 16.00 A C ANISOU 1156 CB MET A 147 812 2716 2551 0 447 -237 A C ATOM 1157 CG MET A 147 15.200 2.944 14.702 1.00 18.11 A C ANISOU 1157 CG MET A 147 969 3260 2651 104 162 -184 A C ATOM 1158 SD MET A 147 14.935 2.658 16.481 1.00 24.07 A S ANISOU 1158 SD MET A 147 2442 4047 2655 31 119 -31 A S ATOM 1159 CE MET A 147 13.679 3.863 16.862 1.00 25.03 A C ANISOU 1159 CE MET A 147 1360 5788 2363 781 357 -293 A C ATOM 1160 N ARG A 148 11.863 1.082 12.074 1.00 16.68 A N ANISOU 1160 N ARG A 148 867 2975 2496 -219 568 -390 A N ATOM 1161 CA ARG A 148 10.523 1.031 11.499 1.00 17.53 A C ANISOU 1161 CA ARG A 148 1044 2978 2639 -271 560 -320 A C ATOM 1162 C ARG A 148 9.817 -0.274 11.854 1.00 18.40 A C ANISOU 1162 C ARG A 148 1224 2933 2833 -443 846 -480 A C ATOM 1163 O ARG A 148 8.603 -0.291 12.147 1.00 19.26 A O ANISOU 1163 O ARG A 148 1025 3296 2998 -489 979 -482 A O ATOM 1164 CB ARG A 148 10.582 1.214 9.982 1.00 17.34 A C ANISOU 1164 CB ARG A 148 943 3084 2560 -109 516 -322 A C ATOM 1165 CG ARG A 148 9.200 1.483 9.396 1.00 19.17 A C ANISOU 1165 CG ARG A 148 1000 3391 2894 -98 130 -241 A C ATOM 1166 CD ARG A 148 9.312 1.750 7.923 1.00 20.36 A C ANISOU 1166 CD ARG A 148 1071 3731 2935 76 -81 -428 A C ATOM 1167 NE ARG A 148 8.051 2.218 7.363 1.00 21.34 A N ANISOU 1167 NE ARG A 148 991 3973 3143 -153 -296 -500 A N ATOM 1168 CZ ARG A 148 7.118 1.429 6.852 1.00 23.26 A C ANISOU 1168 CZ ARG A 148 1604 4138 3095 -606 -63 -416 A C ATOM 1169 NH1 ARG A 148 7.275 0.112 6.809 1.00 25.20 A N ANISOU 1169 NH1 ARG A 148 1976 4135 3463 -723 241 -340 A N ATOM 1170 NH2 ARG A 148 6.018 1.971 6.366 1.00 23.35 A N ANISOU 1170 NH2 ARG A 148 1000 4888 2984 -588 -30 -353 A N ATOM 1171 N ASP A 149 10.565 -1.377 11.829 1.00 20.64 A N ANISOU 1171 N ASP A 149 1756 2851 3237 -606 1049 -568 A N ATOM 1172 CA ASP A 149 10.003 -2.677 12.192 1.00 23.37 A C ANISOU 1172 CA ASP A 149 2425 2930 3526 -653 1092 -540 A C ATOM 1173 C ASP A 149 9.552 -2.697 13.654 1.00 24.16 A C ANISOU 1173 C ASP A 149 2635 3109 3436 -656 1067 -294 A C ATOM 1174 O ASP A 149 8.533 -3.300 14.000 1.00 24.97 A O ANISOU 1174 O ASP A 149 2536 3458 3494 -696 1067 -186 A O ATOM 1175 CB ASP A 149 11.026 -3.788 11.927 1.00 24.80 A C ANISOU 1175 CB ASP A 149 2660 2874 3887 -706 1119 -627 A C ATOM 1176 CG ASP A 149 11.193 -4.102 10.447 1.00 27.73 A C ANISOU 1176 CG ASP A 149 2960 3143 4433 -702 1251 -900 A C ATOM 1177 OD1 ASP A 149 10.468 -3.520 9.603 1.00 31.16 A O ANISOU 1177 OD1 ASP A 149 3576 3734 4528 -741 1392 -806 A O ATOM 1178 OD2 ASP A 149 12.064 -4.932 10.111 1.00 31.22 A O ANISOU 1178 OD2 ASP A 149 3100 3411 5353 -675 1579 -1225 A O ATOM 1179 N LEU A 150 10.318 -2.014 14.500 1.00 23.53 A N ANISOU 1179 N LEU A 150 2533 3172 3237 -379 1000 -108 A N ATOM 1180 CA LEU A 150 10.049 -1.943 15.934 1.00 24.05 A C ANISOU 1180 CA LEU A 150 2691 3249 3197 -170 904 82 A C ATOM 1181 C LEU A 150 8.884 -1.018 16.269 1.00 23.69 A C ANISOU 1181 C LEU A 150 2508 3203 3289 -142 1058 24 A C ATOM 1182 O LEU A 150 8.024 -1.367 17.097 1.00 24.94 A O ANISOU 1182 O LEU A 150 2606 3486 3384 -114 1238 208 A O ATOM 1183 CB LEU A 150 11.308 -1.481 16.685 1.00 24.92 A C ANISOU 1183 CB LEU A 150 2942 3321 3206 -131 776 15 A C ATOM 1184 CG LEU A 150 11.201 -1.342 18.209 1.00 28.06 A C ANISOU 1184 CG LEU A 150 3790 3659 3212 -87 467 142 A C ATOM 1185 CD1 LEU A 150 10.763 -2.651 18.860 1.00 30.46 A C ANISOU 1185 CD1 LEU A 150 4370 3937 3267 -34 280 197 A C ATOM 1186 CD2 LEU A 150 12.525 -0.851 18.774 1.00 30.45 A C ANISOU 1186 CD2 LEU A 150 4359 3952 3257 -31 -10 204 A C ATOM 1187 N ARG A 151 8.844 0.146 15.629 1.00 21.55 A N ANISOU 1187 N ARG A 151 1949 3122 3118 -208 820 -259 A N ATOM 1188 CA ARG A 151 7.869 1.193 15.929 1.00 20.98 A C ANISOU 1188 CA ARG A 151 1641 3312 3018 -208 684 -571 A C ATOM 1189 C ARG A 151 6.575 1.066 15.132 1.00 20.63 A C ANISOU 1189 C ARG A 151 1351 3504 2985 -401 798 -688 A C ATOM 1190 O ARG A 151 5.533 1.491 15.625 1.00 22.41 A O ANISOU 1190 O ARG A 151 1339 3968 3206 -230 886 -851 A O ATOM 1191 CB ARG A 151 8.468 2.577 15.647 1.00 20.95 A C ANISOU 1191 CB ARG A 151 1483 3185 3291 -195 469 -643 A C ATOM 1192 CG ARG A 151 9.780 2.900 16.356 1.00 22.57 A C ANISOU 1192 CG ARG A 151 1606 3576 3395 51 324 -714 A C ATOM 1193 CD ARG A 151 9.551 3.568 17.691 1.00 21.03 A C ANISOU 1193 CD ARG A 151 1439 3677 2876 388 313 -390 A C ATOM 1194 NE ARG A 151 8.734 4.787 17.638 1.00 17.77 A N ANISOU 1194 NE ARG A 151 1050 3355 2347 208 472 -195 A N ATOM 1195 CZ ARG A 151 7.951 5.172 18.651 1.00 18.11 A C ANISOU 1195 CZ ARG A 151 1430 2991 2460 -208 571 -160 A C ATOM 1196 NH1 ARG A 151 7.881 4.417 19.755 1.00 20.47 A N ANISOU 1196 NH1 ARG A 151 2178 3244 2356 -109 573 -120 A N ATOM 1197 NH2 ARG A 151 7.238 6.293 18.554 1.00 16.43 A N ANISOU 1197 NH2 ARG A 151 1008 2980 2255 -175 573 -329 A N ATOM 1198 N GLY A 152 6.648 0.516 13.924 1.00 19.38 A N ANISOU 1198 N GLY A 152 992 3553 2818 -498 828 -635 A N ATOM 1199 CA GLY A 152 5.479 0.429 13.031 1.00 19.57 A C ANISOU 1199 CA GLY A 152 894 3698 2842 -636 675 -568 A C ATOM 1200 C GLY A 152 5.498 1.486 11.935 1.00 18.31 A C ANISOU 1200 C GLY A 152 612 3625 2720 -546 557 -621 A C ATOM 1201 O GLY A 152 5.059 1.234 10.807 1.00 19.75 A O ANISOU 1201 O GLY A 152 663 3984 2858 -679 460 -652 A O ATOM 1202 N ALA A 153 6.002 2.667 12.280 1.00 18.39 A N ANISOU 1202 N ALA A 153 571 3684 2732 -582 377 -498 A N ATOM 1203 CA ALA A 153 6.195 3.756 11.334 1.00 17.22 A C ANISOU 1203 CA ALA A 153 379 3562 2603 -445 208 -460 A C ATOM 1204 C ALA A 153 7.353 4.613 11.840 1.00 16.22 A C ANISOU 1204 C ALA A 153 439 3357 2365 -416 164 -430 A C ATOM 1205 O ALA A 153 7.494 4.820 13.042 1.00 17.23 A O ANISOU 1205 O ALA A 153 693 3553 2299 -505 262 -390 A O ATOM 1206 CB ALA A 153 4.921 4.591 11.201 1.00 18.59 A C ANISOU 1206 CB ALA A 153 421 3844 2797 -359 103 -483 A C ATOM 1207 N PHE A 154 8.178 5.104 10.921 1.00 15.01 A N ANISOU 1207 N PHE A 154 289 3177 2236 -315 90 -329 A N ATOM 1208 CA PHE A 154 9.435 5.761 11.289 1.00 13.87 A C ANISOU 1208 CA PHE A 154 267 2863 2140 -186 44 -205 A C ATOM 1209 C PHE A 154 9.854 6.618 10.107 1.00 13.36 A C ANISOU 1209 C PHE A 154 262 2828 1985 -150 8 -283 A C ATOM 1210 O PHE A 154 10.002 6.113 8.997 1.00 14.14 A O ANISOU 1210 O PHE A 154 263 2974 2134 -5 137 -345 A O ATOM 1211 CB PHE A 154 10.494 4.718 11.675 1.00 14.09 A C ANISOU 1211 CB PHE A 154 284 2949 2122 -153 96 -120 A C ATOM 1212 CG PHE A 154 11.793 5.307 12.167 1.00 13.49 A C ANISOU 1212 CG PHE A 154 465 2587 2073 -140 228 -135 A C ATOM 1213 CD1 PHE A 154 11.868 5.965 13.390 1.00 12.71 A C ANISOU 1213 CD1 PHE A 154 263 2453 2113 -136 55 -115 A C ATOM 1214 CD2 PHE A 154 12.943 5.184 11.408 1.00 13.30 A C ANISOU 1214 CD2 PHE A 154 320 2714 2019 -87 296 -71 A C ATOM 1215 CE1 PHE A 154 13.064 6.499 13.844 1.00 13.66 A C ANISOU 1215 CE1 PHE A 154 518 2565 2108 19 329 -160 A C ATOM 1216 CE2 PHE A 154 14.143 5.715 11.859 1.00 13.17 A C ANISOU 1216 CE2 PHE A 154 306 2648 2048 -65 305 -153 A C ATOM 1217 CZ PHE A 154 14.201 6.369 13.076 1.00 13.14 A C ANISOU 1217 CZ PHE A 154 333 2498 2159 -1 390 -57 A C ATOM 1218 N VAL A 155 10.039 7.909 10.358 1.00 13.22 A N ANISOU 1218 N VAL A 155 262 2851 1908 -146 43 -217 A N ATOM 1219 CA VAL A 155 10.333 8.875 9.307 1.00 13.67 A C ANISOU 1219 CA VAL A 155 264 3066 1862 -170 44 -87 A C ATOM 1220 C VAL A 155 9.734 8.571 7.940 1.00 14.04 A C ANISOU 1220 C VAL A 155 359 3131 1844 -181 131 -186 A C ATOM 1221 O VAL A 155 10.446 8.458 6.946 1.00 14.77 A O ANISOU 1221 O VAL A 155 259 3310 2044 -6 103 -190 A O ATOM 1222 CB VAL A 155 11.855 9.070 9.163 1.00 13.68 A C ANISOU 1222 CB VAL A 155 264 3177 1755 -164 59 17 A C ATOM 1223 CG1 VAL A 155 12.149 10.387 8.469 1.00 15.32 A C ANISOU 1223 CG1 VAL A 155 513 3300 2008 -98 142 163 A C ATOM 1224 CG2 VAL A 155 12.524 9.024 10.530 1.00 14.09 A C ANISOU 1224 CG2 VAL A 155 335 3174 1844 -131 120 -12 A C ATOM 1225 N GLU A 156 8.412 8.444 7.902 1.00 14.46 A N ANISOU 1225 N GLU A 156 258 3321 1914 -115 -17 -153 A N ATOM 1226 CA GLU A 156 7.692 8.304 6.643 1.00 15.42 A C ANISOU 1226 CA GLU A 156 265 3690 1903 -202 0 -258 A C ATOM 1227 C GLU A 156 7.804 9.525 5.733 1.00 15.40 A C ANISOU 1227 C GLU A 156 254 3779 1819 -57 -8 -201 A C ATOM 1228 O GLU A 156 7.679 9.413 4.516 1.00 17.35 A O ANISOU 1228 O GLU A 156 754 3901 1938 -93 -74 -195 A O ATOM 1229 CB GLU A 156 6.222 7.961 6.906 1.00 16.18 A C ANISOU 1229 CB GLU A 156 280 3822 2046 -307 35 -297 A C ATOM 1230 CG GLU A 156 6.019 6.853 7.929 1.00 17.90 A C ANISOU 1230 CG GLU A 156 472 3862 2467 -353 17 -346 A C ATOM 1231 CD GLU A 156 6.546 5.512 7.455 1.00 20.00 A C ANISOU 1231 CD GLU A 156 795 4032 2772 -439 -120 -526 A C ATOM 1232 OE1 GLU A 156 6.276 5.140 6.296 1.00 22.40 A O ANISOU 1232 OE1 GLU A 156 872 4598 3041 -388 -241 -763 A O ATOM 1233 OE2 GLU A 156 7.228 4.824 8.244 1.00 19.97 A O ANISOU 1233 OE2 GLU A 156 752 4041 2793 -494 170 -461 A O ATOM 1234 N ASN A 157 8.046 10.686 6.332 1.00 15.50 A N ANISOU 1234 N ASN A 157 254 3781 1853 45 27 -147 A N ATOM 1235 CA ASN A 157 8.144 11.946 5.589 1.00 15.38 A C ANISOU 1235 CA ASN A 157 263 3824 1758 118 88 -126 A C ATOM 1236 C ASN A 157 9.379 11.894 4.674 1.00 15.20 A C ANISOU 1236 C ASN A 157 295 3785 1694 175 38 -208 A C ATOM 1237 O ASN A 157 10.500 11.840 5.169 1.00 15.75 A O ANISOU 1237 O ASN A 157 262 4005 1717 182 -6 -131 A O ATOM 1238 CB ASN A 157 8.210 13.106 6.593 1.00 15.21 A C ANISOU 1238 CB ASN A 157 326 3761 1694 297 252 -63 A C ATOM 1239 CG ASN A 157 8.334 14.472 5.937 1.00 15.78 A C ANISOU 1239 CG ASN A 157 453 3785 1756 544 203 -17 A C ATOM 1240 ND2 ASN A 157 7.773 15.479 6.606 1.00 15.67 A N ANISOU 1240 ND2 ASN A 157 350 3813 1791 575 52 -136 A N ATOM 1241 OD1 ASN A 157 8.961 14.633 4.883 1.00 18.14 A O ANISOU 1241 OD1 ASN A 157 1005 3878 2008 535 537 103 A O ATOM 1242 N PRO A 158 9.185 11.852 3.349 1.00 16.48 A N ANISOU 1242 N PRO A 158 496 4142 1622 131 0 -115 A N ATOM 1243 CA PRO A 158 10.350 11.688 2.468 1.00 17.26 A C ANISOU 1243 CA PRO A 158 819 4088 1650 263 126 -76 A C ATOM 1244 C PRO A 158 11.292 12.887 2.459 1.00 16.34 A C ANISOU 1244 C PRO A 158 652 3855 1703 487 237 115 A C ATOM 1245 O PRO A 158 12.476 12.711 2.157 1.00 16.53 A O ANISOU 1245 O PRO A 158 427 3973 1879 588 151 5 A O ATOM 1246 CB PRO A 158 9.725 11.476 1.085 1.00 18.60 A C ANISOU 1246 CB PRO A 158 1007 4386 1676 226 87 -98 A C ATOM 1247 CG PRO A 158 8.367 12.086 1.179 1.00 19.58 A C ANISOU 1247 CG PRO A 158 1106 4623 1712 104 -153 -197 A C ATOM 1248 CD PRO A 158 7.910 11.913 2.595 1.00 16.77 A C ANISOU 1248 CD PRO A 158 577 4117 1676 115 -120 -20 A C ATOM 1249 N SER A 159 10.799 14.088 2.764 1.00 15.77 A N ANISOU 1249 N SER A 159 597 3709 1684 606 152 230 A N ATOM 1250 CA ASER A 159 11.662 15.274 2.850 0.50 15.49 A C ANISOU 1250 CA ASER A 159 636 3528 1720 634 216 364 A C ATOM 1251 CA BSER A 159 11.675 15.252 2.822 0.50 15.30 A C ANISOU 1251 CA BSER A 159 575 3560 1676 593 197 364 A C ATOM 1252 C SER A 159 12.608 15.170 4.038 1.00 14.66 A C ANISOU 1252 C SER A 159 544 3413 1612 621 219 218 A C ATOM 1253 O SER A 159 13.788 15.554 3.963 1.00 14.86 A O ANISOU 1253 O SER A 159 553 3303 1790 454 261 197 A O ATOM 1254 CB ASER A 159 10.868 16.576 2.968 0.50 16.22 A C ANISOU 1254 CB ASER A 159 708 3567 1886 640 219 452 A C ATOM 1255 CB BSER A 159 10.847 16.538 2.793 0.50 15.89 A C ANISOU 1255 CB BSER A 159 597 3625 1817 586 175 414 A C ATOM 1256 OG ASER A 159 11.745 17.666 3.258 0.50 17.47 A O ANISOU 1256 OG ASER A 159 750 3621 2266 820 342 469 A O ATOM 1257 OG BSER A 159 10.100 16.606 1.579 0.50 15.63 A O ANISOU 1257 OG BSER A 159 353 3655 1932 535 249 593 A O ATOM 1258 N PHE A 160 12.117 14.651 5.150 1.00 14.35 A N ANISOU 1258 N PHE A 160 500 3420 1534 540 205 175 A N ATOM 1259 CA PHE A 160 12.967 14.476 6.326 1.00 13.11 A C ANISOU 1259 CA PHE A 160 388 3127 1465 489 252 30 A C ATOM 1260 C PHE A 160 14.016 13.402 6.032 1.00 12.99 A C ANISOU 1260 C PHE A 160 318 2976 1641 335 171 -60 A C ATOM 1261 O PHE A 160 15.194 13.562 6.378 1.00 13.24 A O ANISOU 1261 O PHE A 160 287 3084 1659 290 79 68 A O ATOM 1262 CB PHE A 160 12.118 14.077 7.537 1.00 13.31 A C ANISOU 1262 CB PHE A 160 379 3185 1492 518 209 46 A C ATOM 1263 CG PHE A 160 11.265 15.195 8.104 1.00 13.56 A C ANISOU 1263 CG PHE A 160 337 3179 1634 469 115 80 A C ATOM 1264 CD1 PHE A 160 11.256 16.472 7.546 1.00 14.65 A C ANISOU 1264 CD1 PHE A 160 434 3183 1948 678 226 113 A C ATOM 1265 CD2 PHE A 160 10.486 14.958 9.210 1.00 14.06 A C ANISOU 1265 CD2 PHE A 160 366 3476 1500 474 6 -52 A C ATOM 1266 CE1 PHE A 160 10.455 17.484 8.094 1.00 14.87 A C ANISOU 1266 CE1 PHE A 160 560 3210 1879 634 137 196 A C ATOM 1267 CE2 PHE A 160 9.680 15.952 9.758 1.00 13.77 A C ANISOU 1267 CE2 PHE A 160 328 3416 1489 461 98 34 A C ATOM 1268 CZ PHE A 160 9.680 17.211 9.215 1.00 14.71 A C ANISOU 1268 CZ PHE A 160 372 3517 1699 617 92 219 A C ATOM 1269 N LYS A 161 13.616 12.306 5.389 1.00 12.88 A N ANISOU 1269 N LYS A 161 403 2752 1738 291 313 -76 A N ATOM 1270 CA LYS A 161 14.591 11.267 5.002 1.00 13.43 A C ANISOU 1270 CA LYS A 161 693 2594 1815 173 403 65 A C ATOM 1271 C LYS A 161 15.644 11.847 4.082 1.00 12.49 A C ANISOU 1271 C LYS A 161 579 2544 1624 241 285 151 A C ATOM 1272 O LYS A 161 16.840 11.547 4.243 1.00 12.93 A O ANISOU 1272 O LYS A 161 326 2689 1897 366 186 115 A O ATOM 1273 CB LYS A 161 13.931 10.072 4.319 1.00 14.32 A C ANISOU 1273 CB LYS A 161 805 2680 1956 24 518 -68 A C ATOM 1274 CG LYS A 161 13.158 9.217 5.300 1.00 18.69 A C ANISOU 1274 CG LYS A 161 1524 3095 2483 -364 656 -68 A C ATOM 1275 CD LYS A 161 12.722 7.915 4.699 1.00 21.76 A C ANISOU 1275 CD LYS A 161 1753 3445 3070 -653 575 -296 A C ATOM 1276 CE LYS A 161 11.544 8.133 3.784 1.00 24.97 A C ANISOU 1276 CE LYS A 161 1949 3822 3716 -759 259 -445 A C ATOM 1277 NZ LYS A 161 10.552 7.040 3.999 1.00 25.44 A N ANISOU 1277 NZ LYS A 161 1500 3921 4246 -820 303 -666 A N ATOM 1278 N ARG A 162 15.228 12.667 3.131 1.00 12.06 A N ANISOU 1278 N ARG A 162 438 2599 1544 153 226 274 A N ATOM 1279 CA ARG A 162 16.176 13.289 2.188 1.00 12.25 A C ANISOU 1279 CA ARG A 162 710 2524 1421 52 207 219 A C ATOM 1280 C ARG A 162 17.216 14.101 2.959 1.00 11.93 A C ANISOU 1280 C ARG A 162 540 2457 1536 194 263 24 A C ATOM 1281 O ARG A 162 18.417 14.040 2.656 1.00 12.93 A O ANISOU 1281 O ARG A 162 340 2829 1744 252 307 35 A O ATOM 1282 CB ARG A 162 15.455 14.215 1.215 1.00 12.87 A C ANISOU 1282 CB ARG A 162 864 2599 1427 86 218 320 A C ATOM 1283 CG ARG A 162 16.381 14.864 0.168 1.00 14.02 A C ANISOU 1283 CG ARG A 162 1086 2689 1553 98 263 438 A C ATOM 1284 CD ARG A 162 15.773 16.115 -0.432 1.00 16.03 A C ANISOU 1284 CD ARG A 162 1351 2621 2117 115 377 480 A C ATOM 1285 NE ARG A 162 15.878 17.258 0.484 1.00 16.82 A N ANISOU 1285 NE ARG A 162 1404 2685 2301 280 205 342 A N ATOM 1286 CZ ARG A 162 14.853 17.965 0.947 1.00 15.46 A C ANISOU 1286 CZ ARG A 162 1023 2781 2071 41 13 291 A C ATOM 1287 NH1 ARG A 162 13.592 17.641 0.624 1.00 18.03 A N ANISOU 1287 NH1 ARG A 162 864 3379 2608 -65 -147 527 A N ATOM 1288 NH2 ARG A 162 15.065 18.987 1.752 1.00 17.65 A N ANISOU 1288 NH2 ARG A 162 1676 3021 2008 15 17 164 A N ATOM 1289 N GLN A 163 16.770 14.861 3.951 1.00 12.32 A N ANISOU 1289 N GLN A 163 603 2417 1659 241 208 -113 A N ATOM 1290 CA GLN A 163 17.668 15.710 4.753 1.00 12.31 A C ANISOU 1290 CA GLN A 163 675 2290 1712 239 164 -38 A C ATOM 1291 C GLN A 163 18.657 14.885 5.565 1.00 12.52 A C ANISOU 1291 C GLN A 163 522 2356 1879 219 148 46 A C ATOM 1292 O GLN A 163 19.836 15.263 5.690 1.00 13.84 A O ANISOU 1292 O GLN A 163 439 2745 2073 -74 205 43 A O ATOM 1293 CB GLN A 163 16.868 16.659 5.638 1.00 12.54 A C ANISOU 1293 CB GLN A 163 665 2442 1657 284 65 -87 A C ATOM 1294 CG GLN A 163 16.171 17.712 4.786 1.00 13.50 A C ANISOU 1294 CG GLN A 163 675 2596 1859 438 126 0 A C ATOM 1295 CD GLN A 163 15.263 18.590 5.618 1.00 14.05 A C ANISOU 1295 CD GLN A 163 849 2714 1773 666 -59 -115 A C ATOM 1296 NE2 GLN A 163 13.970 18.657 5.244 1.00 15.99 A N ANISOU 1296 NE2 GLN A 163 777 3260 2037 715 92 93 A N ATOM 1297 OE1 GLN A 163 15.714 19.227 6.580 1.00 16.73 A O ANISOU 1297 OE1 GLN A 163 1402 2989 1967 522 -109 -296 A O ATOM 1298 N ILE A 164 18.229 13.758 6.111 1.00 12.06 A N ANISOU 1298 N ILE A 164 410 2381 1791 285 173 163 A N ATOM 1299 CA ILE A 164 19.122 12.845 6.808 1.00 12.76 A C ANISOU 1299 CA ILE A 164 439 2504 1905 351 159 135 A C ATOM 1300 C ILE A 164 20.155 12.293 5.828 1.00 13.08 A C ANISOU 1300 C ILE A 164 392 2630 1946 247 186 -3 A C ATOM 1301 O ILE A 164 21.360 12.235 6.152 1.00 13.75 A O ANISOU 1301 O ILE A 164 285 2966 1972 140 211 57 A O ATOM 1302 CB ILE A 164 18.360 11.675 7.463 1.00 13.19 A C ANISOU 1302 CB ILE A 164 497 2617 1897 417 153 208 A C ATOM 1303 CG1 ILE A 164 17.485 12.214 8.607 1.00 14.54 A C ANISOU 1303 CG1 ILE A 164 509 3145 1870 388 208 87 A C ATOM 1304 CG2 ILE A 164 19.328 10.586 7.945 1.00 14.43 A C ANISOU 1304 CG2 ILE A 164 364 2861 2256 500 241 397 A C ATOM 1305 CD1 ILE A 164 18.270 12.566 9.848 1.00 17.86 A C ANISOU 1305 CD1 ILE A 164 1097 3643 2046 423 3 -54 A C ATOM 1306 N ILE A 165 19.716 11.869 4.651 1.00 12.68 A N ANISOU 1306 N ILE A 165 340 2671 1808 93 280 26 A N ATOM 1307 CA ILE A 165 20.642 11.315 3.662 1.00 13.20 A C ANISOU 1307 CA ILE A 165 504 2642 1870 124 248 57 A C ATOM 1308 C ILE A 165 21.676 12.353 3.253 1.00 13.49 A C ANISOU 1308 C ILE A 165 348 2669 2109 142 403 96 A C ATOM 1309 O ILE A 165 22.887 12.043 3.126 1.00 14.94 A O ANISOU 1309 O ILE A 165 372 3152 2152 307 414 115 A O ATOM 1310 CB ILE A 165 19.871 10.786 2.422 1.00 12.96 A C ANISOU 1310 CB ILE A 165 285 2795 1842 92 212 -8 A C ATOM 1311 CG1 ILE A 165 19.092 9.519 2.808 1.00 13.98 A C ANISOU 1311 CG1 ILE A 165 447 2829 2037 15 87 -104 A C ATOM 1312 CG2 ILE A 165 20.813 10.508 1.251 1.00 15.49 A C ANISOU 1312 CG2 ILE A 165 744 3125 2016 208 384 -148 A C ATOM 1313 CD1 ILE A 165 17.922 9.222 1.872 1.00 15.36 A C ANISOU 1313 CD1 ILE A 165 362 2982 2492 140 -194 -295 A C ATOM 1314 N GLU A 166 21.242 13.581 3.006 1.00 14.05 A N ANISOU 1314 N GLU A 166 491 2655 2194 10 491 230 A N ATOM 1315 CA GLU A 166 22.167 14.666 2.625 1.00 15.72 A C ANISOU 1315 CA GLU A 166 810 2894 2266 -87 500 136 A C ATOM 1316 C GLU A 166 23.228 14.922 3.701 1.00 16.32 A C ANISOU 1316 C GLU A 166 662 3142 2395 -137 500 -15 A C ATOM 1317 O GLU A 166 24.429 15.048 3.403 1.00 18.77 A O ANISOU 1317 O GLU A 166 614 3833 2685 -130 621 -142 A O ATOM 1318 CB GLU A 166 21.384 15.947 2.337 1.00 16.51 A C ANISOU 1318 CB GLU A 166 1001 2799 2474 -197 520 315 A C ATOM 1319 CG GLU A 166 20.546 15.850 1.079 1.00 17.77 A C ANISOU 1319 CG GLU A 166 891 3282 2578 93 571 537 A C ATOM 1320 CD GLU A 166 19.459 16.915 0.990 1.00 21.46 A C ANISOU 1320 CD GLU A 166 1676 3364 3115 164 368 754 A C ATOM 1321 OE1 GLU A 166 19.162 17.598 1.999 1.00 23.81 A O ANISOU 1321 OE1 GLU A 166 1727 3797 3524 617 599 653 A O ATOM 1322 OE2 GLU A 166 18.897 17.074 -0.113 1.00 23.76 A O ANISOU 1322 OE2 GLU A 166 1949 3546 3531 -74 -86 1013 A O ATOM 1323 N LYS A 167 22.798 14.994 4.961 1.00 16.60 A N ANISOU 1323 N LYS A 167 814 3194 2301 -41 388 -65 A N ATOM 1324 CA LYS A 167 23.703 15.331 6.059 1.00 16.87 A C ANISOU 1324 CA LYS A 167 867 3109 2433 -102 335 -126 A C ATOM 1325 C LYS A 167 24.689 14.210 6.403 1.00 16.31 A C ANISOU 1325 C LYS A 167 541 3203 2451 -35 333 -104 A C ATOM 1326 O LYS A 167 25.896 14.451 6.572 1.00 17.98 A O ANISOU 1326 O LYS A 167 357 3619 2854 -186 322 -104 A O ATOM 1327 CB LYS A 167 22.878 15.682 7.305 1.00 17.64 A C ANISOU 1327 CB LYS A 167 1130 3212 2360 57 285 -228 A C ATOM 1328 CG LYS A 167 23.685 15.898 8.577 1.00 21.59 A C ANISOU 1328 CG LYS A 167 1747 3781 2675 -219 49 -454 A C ATOM 1329 CD LYS A 167 24.322 17.271 8.631 1.00 26.41 A C ANISOU 1329 CD LYS A 167 2492 4359 3183 -496 5 -715 A C ATOM 1330 CE LYS A 167 24.840 17.568 10.036 1.00 26.97 A C ANISOU 1330 CE LYS A 167 2416 4514 3318 -644 0 -886 A C ATOM 1331 NZ LYS A 167 25.630 18.831 10.084 1.00 29.39 A N ANISOU 1331 NZ LYS A 167 2734 4877 3553 -687 241 -841 A N ATOM 1332 N TYR A 168 24.192 12.983 6.495 1.00 15.80 A N ANISOU 1332 N TYR A 168 410 3134 2460 120 368 -63 A N ATOM 1333 CA TYR A 168 24.966 11.898 7.090 1.00 16.26 A C ANISOU 1333 CA TYR A 168 527 3298 2353 261 274 -147 A C ATOM 1334 C TYR A 168 25.478 10.857 6.103 1.00 16.33 A C ANISOU 1334 C TYR A 168 395 3528 2283 443 285 -185 A C ATOM 1335 O TYR A 168 26.368 10.078 6.467 1.00 18.30 A O ANISOU 1335 O TYR A 168 562 3860 2531 688 65 -307 A O ATOM 1336 CB TYR A 168 24.142 11.210 8.193 1.00 15.89 A C ANISOU 1336 CB TYR A 168 593 3296 2148 274 274 -120 A C ATOM 1337 CG TYR A 168 23.803 12.153 9.321 1.00 15.31 A C ANISOU 1337 CG TYR A 168 289 3228 2299 197 197 -197 A C ATOM 1338 CD1 TYR A 168 24.767 12.525 10.253 1.00 16.07 A C ANISOU 1338 CD1 TYR A 168 362 3384 2361 197 3 -292 A C ATOM 1339 CD2 TYR A 168 22.505 12.676 9.459 1.00 15.27 A C ANISOU 1339 CD2 TYR A 168 311 3330 2161 241 262 -93 A C ATOM 1340 CE1 TYR A 168 24.495 13.396 11.278 1.00 15.94 A C ANISOU 1340 CE1 TYR A 168 285 3362 2409 83 243 -289 A C ATOM 1341 CE2 TYR A 168 22.226 13.542 10.479 1.00 15.06 A C ANISOU 1341 CE2 TYR A 168 478 3093 2152 -102 131 -115 A C ATOM 1342 CZ TYR A 168 23.200 13.902 11.400 1.00 15.10 A C ANISOU 1342 CZ TYR A 168 262 3111 2363 87 98 -296 A C ATOM 1343 OH TYR A 168 22.901 14.782 12.419 1.00 16.98 A O ANISOU 1343 OH TYR A 168 256 3535 2659 -52 77 -610 A O ATOM 1344 N VAL A 169 24.945 10.833 4.884 1.00 16.94 A N ANISOU 1344 N VAL A 169 342 3785 2308 328 324 -214 A N ATOM 1345 CA VAL A 169 25.348 9.824 3.904 1.00 19.42 A C ANISOU 1345 CA VAL A 169 645 4219 2515 537 388 -164 A C ATOM 1346 C VAL A 169 26.101 10.414 2.709 1.00 22.34 A C ANISOU 1346 C VAL A 169 804 4820 2863 494 894 27 A C ATOM 1347 O VAL A 169 27.180 9.937 2.362 1.00 23.60 A O ANISOU 1347 O VAL A 169 646 5317 3003 798 850 -31 A O ATOM 1348 CB VAL A 169 24.158 8.967 3.410 1.00 18.33 A C ANISOU 1348 CB VAL A 169 638 3844 2480 573 194 -263 A C ATOM 1349 CG1 VAL A 169 24.650 7.899 2.431 1.00 20.33 A C ANISOU 1349 CG1 VAL A 169 895 4162 2666 724 31 -410 A C ATOM 1350 CG2 VAL A 169 23.450 8.323 4.584 1.00 19.34 A C ANISOU 1350 CG2 VAL A 169 1053 3671 2623 507 97 -196 A C ATOM 1351 N AILE A 170 25.536 11.445 2.090 0.50 25.94 A N ANISOU 1351 N AILE A 170 1238 5400 3219 381 1167 408 A N ATOM 1352 N BILE A 170 25.537 11.439 2.079 0.50 25.94 A N ANISOU 1352 N BILE A 170 1237 5400 3219 383 1167 408 A N ATOM 1353 CA AILE A 170 26.162 12.092 0.940 0.50 32.66 A C ANISOU 1353 CA AILE A 170 2319 6280 3810 -57 1448 728 A C ATOM 1354 CA BILE A 170 26.180 12.076 0.932 0.50 32.66 A C ANISOU 1354 CA BILE A 170 2319 6280 3810 -57 1448 728 A C ATOM 1355 C AILE A 170 27.315 12.971 1.403 0.50 36.82 A C ANISOU 1355 C AILE A 170 2773 6977 4239 -584 1456 697 A C ATOM 1356 C BILE A 170 27.270 13.027 1.419 0.50 36.81 A C ANISOU 1356 C BILE A 170 2773 6977 4237 -584 1456 697 A C ATOM 1357 O AILE A 170 27.122 13.890 2.196 0.50 40.85 A O ANISOU 1357 O AILE A 170 3231 7713 4578 -1010 1526 513 A O ATOM 1358 O BILE A 170 27.016 13.900 2.250 0.50 40.85 A O ANISOU 1358 O BILE A 170 3231 7713 4578 -1010 1526 515 A O ATOM 1359 CB AILE A 170 25.158 12.967 0.147 0.50 32.66 A C ANISOU 1359 CB AILE A 170 2469 6171 3768 -17 1410 929 A C ATOM 1360 CB BILE A 170 25.170 12.863 0.065 0.50 32.66 A C ANISOU 1360 CB BILE A 170 2469 6171 3767 -17 1411 929 A C ATOM 1361 CG1AILE A 170 23.922 12.148 -0.273 0.50 33.07 A C ANISOU 1361 CG1AILE A 170 2574 6165 3826 197 1360 820 A C ATOM 1362 CG1BILE A 170 24.114 11.919 -0.515 0.50 33.06 A C ANISOU 1362 CG1BILE A 170 2569 6165 3826 197 1360 820 A C ATOM 1363 CG2AILE A 170 25.846 13.613 -1.066 0.50 34.05 A C ANISOU 1363 CG2AILE A 170 2576 6557 3806 120 1571 1014 A C ATOM 1364 CG2BILE A 170 25.898 13.617 -1.052 0.50 34.05 A C ANISOU 1364 CG2BILE A 170 2574 6557 3806 120 1571 1014 A C ATOM 1365 CD1AILE A 170 24.248 10.789 -0.885 0.50 32.94 A C ANISOU 1365 CD1AILE A 170 2585 6082 3849 362 1149 807 A C ATOM 1366 CD1BILE A 170 22.939 12.636 -1.178 0.50 33.14 A C ANISOU 1366 CD1BILE A 170 2594 6093 3903 384 1106 807 A C TER END If you find results from this site helpful for your research, please cite one of our papers:
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