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*** ***elNémo ID: 2605290810191805816Job options:ID = 2605290810191805816 JOBID = 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: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 HETATM 1367 P PO4 A-999 5.072 13.619 13.693 1.00 13.65 B P ANISOU 1367 P PO4 A-999 320 3075 1791 -46 274 -34 B P HETATM 1368 O1 PO4 A-999 6.106 14.649 13.264 1.00 13.51 B O ANISOU 1368 O1 PO4 A-999 291 2935 1905 230 175 60 B O HETATM 1369 O2 PO4 A-999 4.360 13.130 12.425 1.00 14.95 B O ANISOU 1369 O2 PO4 A-999 410 3366 1905 82 489 -328 B O HETATM 1370 O3 PO4 A-999 5.643 12.397 14.359 1.00 13.69 B O ANISOU 1370 O3 PO4 A-999 384 2831 1985 -285 412 3 B O HETATM 1371 O4 PO4 A-999 4.038 14.233 14.641 1.00 14.45 B O ANISOU 1371 O4 PO4 A-999 318 3348 1826 164 285 -164 B O HETATM 1372 C1 BME A 174 4.781 11.652 4.964 0.50 27.69 C C ANISOU 1372 C1 BME A 174 3370 3418 3734 13 48 -35 C C HETATM 1373 O1 BME A 174 4.809 12.940 4.394 0.50 30.81 C O ANISOU 1373 O1 BME A 174 3704 4007 3995 -87 -109 -142 C O HETATM 1374 C2 BME A 174 4.822 11.780 6.481 0.50 29.48 C C ANISOU 1374 C2 BME A 174 3522 3774 3905 -3 -40 242 C C HETATM 1375 S2 BME A 174 3.897 10.470 7.314 0.50 37.46 C S ANISOU 1375 S2 BME A 174 4505 4910 4816 -82 0 -65 C S HETATM 1376 C1 BME A-998 31.941 5.668 9.642 1.00 45.25 D C ANISOU 1376 C1 BME A-998 5758 5799 5636 126 -161 -81 D C HETATM 1377 O1 BME A-998 32.848 4.826 8.968 1.00 44.94 D O ANISOU 1377 O1 BME A-998 5651 5741 5683 153 -160 -51 D O HETATM 1378 C2 BME A-998 32.113 7.084 9.118 1.00 46.23 D C ANISOU 1378 C2 BME A-998 5881 5896 5787 115 -184 -15 D C HETATM 1379 S2 BME A-998 30.905 8.216 9.837 1.00 49.10 D S ANISOU 1379 S2 BME A-998 6111 6334 6211 114 -65 -137 D S CONECT 1367 1368 1369 1370 1371 CONECT 1368 1367 CONECT 1369 1367 CONECT 1370 1367 CONECT 1371 1367 CONECT 1372 1373 1374 CONECT 1373 1372 CONECT 1374 1372 1375 CONECT 1375 1374 CONECT 1376 1377 1378 CONECT 1377 1376 CONECT 1378 1376 1379 CONECT 1379 1378 END If you find results from this site helpful for your research, please cite one of our papers:
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