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*** 3BLH_A_VS_4bcg_A ***elNémo ID: 22051216393486404Job options:ID = 22051216393486404 JOBID = 3BLH_A_VS_4bcg_A USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = on DORMSD = on NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 3BLH_A_VS_4bcg_A CRYST1 172.920 172.920 95.760 90.00 90.00 120.00 H 3 9 ATOM 1 N VAL A 8 38.365 -4.357 -38.054 1.00115.79 A N ANISOU 1 N VAL A 8 14119 17287 12589 1000 -36 -1013 A N ATOM 2 CA VAL A 8 37.673 -3.858 -36.866 1.00115.57 A C ANISOU 2 CA VAL A 8 14029 17153 12730 1001 -102 -876 A C ATOM 3 C VAL A 8 38.654 -3.207 -35.889 1.00108.34 A C ANISOU 3 C VAL A 8 13115 16091 11958 978 36 -748 A C ATOM 4 O VAL A 8 39.592 -3.854 -35.418 1.00107.78 A O ANISOU 4 O VAL A 8 12994 15926 12033 932 120 -832 A O ATOM 5 CB VAL A 8 36.842 -4.981 -36.179 1.00 71.68 A C ANISOU 5 CB VAL A 8 8350 11529 7357 954 -233 -1002 A C ATOM 6 CG1 VAL A 8 36.690 -4.735 -34.688 1.00 60.19 A C ANISOU 6 CG1 VAL A 8 6819 9916 6135 929 -230 -895 A C ATOM 7 CG2 VAL A 8 35.481 -5.104 -36.843 1.00 75.83 A C ANISOU 7 CG2 VAL A 8 8857 12207 7749 976 -403 -1038 A C ATOM 8 N GLU A 9 38.433 -1.925 -35.599 1.00101.15 A N ANISOU 8 N GLU A 9 12269 15162 11001 1014 52 -549 A N ATOM 9 CA GLU A 9 39.327 -1.154 -34.734 1.00 98.88 A C ANISOU 9 CA GLU A 9 12007 14743 10821 980 175 -416 A C ATOM 10 C GLU A 9 39.383 -1.675 -33.298 1.00 89.71 A C ANISOU 10 C GLU A 9 10734 13417 9934 934 161 -439 A C ATOM 11 O GLU A 9 38.397 -2.191 -32.773 1.00 91.86 A O ANISOU 11 O GLU A 9 10928 13666 10307 941 43 -481 A O ATOM 12 CB GLU A 9 38.931 0.320 -34.732 1.00109.84 A C ANISOU 12 CB GLU A 9 13515 16126 12095 1033 175 -204 A C ATOM 13 CG GLU A 9 39.405 1.094 -35.944 1.00124.01 A C ANISOU 13 CG GLU A 9 15458 18029 13631 1047 251 -128 A C ATOM 14 CD GLU A 9 39.238 2.586 -35.757 1.00138.02 A C ANISOU 14 CD GLU A 9 17377 19739 15324 1087 271 95 A C ATOM 15 OE1 GLU A 9 39.154 3.022 -34.588 1.00140.54 A O ANISOU 15 OE1 GLU A 9 17679 19910 15811 1081 272 179 A O ATOM 16 OE2 GLU A 9 39.189 3.319 -36.771 1.00144.03 A O1- ANISOU 16 OE2 GLU A 9 18284 20591 15849 1124 283 186 A O1- ATOM 17 N CYS A 10 40.539 -1.529 -32.659 1.00 80.19 A N ANISOU 17 N CYS A 10 9519 12109 8841 878 281 -407 A N ATOM 18 CA CYS A 10 40.726 -2.086 -31.325 1.00 75.50 A C ANISOU 18 CA CYS A 10 8829 11364 8495 832 269 -433 A C ATOM 19 C CYS A 10 41.778 -1.370 -30.469 1.00 74.72 A C ANISOU 19 C CYS A 10 8745 11154 8492 779 381 -319 A C ATOM 20 O CYS A 10 42.726 -1.987 -29.995 1.00 78.98 A O ANISOU 20 O CYS A 10 9212 11632 9164 734 437 -388 A O ATOM 21 CB CYS A 10 41.058 -3.569 -31.423 1.00 66.58 A C ANISOU 21 CB CYS A 10 7611 10223 7465 811 249 -632 A C ATOM 22 SG CYS A 10 40.824 -4.391 -29.866 1.00 83.94 A S ANISOU 22 SG CYS A 10 9710 12241 9942 764 180 -662 A S ATOM 23 N PRO A 11 41.571 -0.070 -30.235 1.00 71.68 A N ANISOU 23 N PRO A 11 8457 10737 8040 788 401 -146 A N ATOM 24 CA PRO A 11 42.486 0.855 -29.557 1.00 62.50 A C ANISOU 24 CA PRO A 11 7347 9477 6924 724 503 -19 A C ATOM 25 C PRO A 11 42.965 0.388 -28.191 1.00 62.86 A C ANISOU 25 C PRO A 11 7299 9385 7201 666 504 -40 A C ATOM 26 O PRO A 11 44.059 0.757 -27.775 1.00 70.13 A O ANISOU 26 O PRO A 11 8218 10256 8172 592 596 6 A O ATOM 27 CB PRO A 11 41.622 2.107 -29.356 1.00 67.75 A C ANISOU 27 CB PRO A 11 8136 10098 7507 775 463 145 A C ATOM 28 CG PRO A 11 40.563 2.021 -30.389 1.00 69.50 A C ANISOU 28 CG PRO A 11 8388 10451 7569 871 374 118 A C ATOM 29 CD PRO A 11 40.293 0.574 -30.595 1.00 70.23 A C ANISOU 29 CD PRO A 11 8344 10607 7733 871 308 -66 A C ATOM 30 N PHE A 12 42.145 -0.384 -27.490 1.00 61.40 A N ANISOU 30 N PHE A 12 7037 9145 7147 690 402 -103 A N ATOM 31 CA PHE A 12 42.365 -0.607 -26.065 1.00 55.29 A C ANISOU 31 CA PHE A 12 6208 8229 6571 640 388 -83 A C ATOM 32 C PHE A 12 42.671 -2.060 -25.769 1.00 53.85 A C ANISOU 32 C PHE A 12 5910 8015 6536 621 352 -233 A C ATOM 33 O PHE A 12 42.691 -2.485 -24.613 1.00 51.23 A O ANISOU 33 O PHE A 12 5530 7568 6368 586 316 -232 A O ATOM 34 CB PHE A 12 41.151 -0.140 -25.250 1.00 58.58 A C ANISOU 34 CB PHE A 12 6651 8583 7023 675 309 0 A C ATOM 35 CG PHE A 12 40.795 1.295 -25.474 1.00 62.39 A C ANISOU 35 CG PHE A 12 7265 9071 7368 720 335 147 A C ATOM 36 CD1 PHE A 12 41.770 2.280 -25.410 1.00 69.97 A C ANISOU 36 CD1 PHE A 12 8324 9978 8284 667 433 249 A C ATOM 37 CD2 PHE A 12 39.498 1.665 -25.753 1.00 64.29 A C ANISOU 37 CD2 PHE A 12 7536 9370 7523 815 257 184 A C ATOM 38 CE1 PHE A 12 41.452 3.612 -25.613 1.00 71.51 A C ANISOU 38 CE1 PHE A 12 8672 10149 8351 706 453 388 A C ATOM 39 CE2 PHE A 12 39.173 2.996 -25.958 1.00 71.60 A C ANISOU 39 CE2 PHE A 12 8600 10284 8322 880 274 322 A C ATOM 40 CZ PHE A 12 40.150 3.970 -25.887 1.00 70.18 A C ANISOU 40 CZ PHE A 12 8545 10022 8098 825 372 425 A C ATOM 41 N CYS A 13 42.903 -2.826 -26.824 1.00 53.55 A N ANISOU 41 N CYS A 13 5843 8073 6431 647 360 -362 A N ATOM 42 CA CYS A 13 43.351 -4.189 -26.651 1.00 59.28 A C ANISOU 42 CA CYS A 13 6483 8755 7287 642 336 -512 A C ATOM 43 C CYS A 13 44.513 -4.422 -27.599 1.00 61.56 A C ANISOU 43 C CYS A 13 6752 9136 7501 660 437 -597 A C ATOM 44 O CYS A 13 44.310 -4.560 -28.805 1.00 63.29 A O ANISOU 44 O CYS A 13 7003 9478 7566 698 448 -671 A O ATOM 45 CB CYS A 13 42.210 -5.149 -26.950 1.00 62.45 A C ANISOU 45 CB CYS A 13 6867 9170 7691 664 220 -622 A C ATOM 46 SG CYS A 13 42.517 -6.822 -26.424 1.00 60.87 A S ANISOU 46 SG CYS A 13 6599 8848 7681 647 162 -784 A S ATOM 47 N ASP A 14 45.731 -4.441 -27.059 1.00 57.62 A N ANISOU 47 N ASP A 14 6196 8594 7103 632 511 -588 A N ATOM 48 CA ASP A 14 46.935 -4.608 -27.884 1.00 56.52 A C ANISOU 48 CA ASP A 14 6011 8564 6900 649 625 -665 A C ATOM 49 C ASP A 14 47.162 -6.069 -28.253 1.00 53.38 A C ANISOU 49 C ASP A 14 5552 8163 6567 719 596 -864 A C ATOM 50 O ASP A 14 46.776 -6.978 -27.505 1.00 54.86 A O ANISOU 50 O ASP A 14 5717 8219 6908 732 496 -923 A O ATOM 51 CB ASP A 14 48.173 -4.061 -27.162 1.00 60.34 A C ANISOU 51 CB ASP A 14 6433 9025 7469 591 712 -582 A C ATOM 52 CG ASP A 14 48.230 -2.542 -27.149 1.00 74.14 A C ANISOU 52 CG ASP A 14 8265 10800 9106 513 778 -404 A C ATOM 53 OD1 ASP A 14 47.494 -1.888 -27.931 1.00 78.47 A O ANISOU 53 OD1 ASP A 14 8920 11411 9484 523 779 -349 A O ATOM 54 OD2 ASP A 14 49.027 -2.004 -26.348 1.00 79.61 A O1- ANISOU 54 OD2 ASP A 14 8924 11446 9879 440 821 -318 A O1- ATOM 55 N GLU A 15 47.785 -6.293 -29.405 1.00 62.03 A N ANISOU 55 N GLU A 15 6634 9397 7538 763 685 -968 A N ATOM 56 CA GLU A 15 48.183 -7.644 -29.800 1.00 66.86 A C ANISOU 56 CA GLU A 15 7196 10003 8204 846 677 -1171 A C ATOM 57 C GLU A 15 49.356 -8.140 -28.958 1.00 60.94 A C ANISOU 57 C GLU A 15 6332 9181 7640 874 710 -1201 A C ATOM 58 O GLU A 15 50.310 -7.396 -28.710 1.00 57.50 A O ANISOU 58 O GLU A 15 5829 8809 7210 835 809 -1110 A O ATOM 59 CB GLU A 15 48.545 -7.684 -31.279 1.00 69.37 A C ANISOU 59 CB GLU A 15 7535 10506 8318 893 777 -1277 A C ATOM 60 CG GLU A 15 47.522 -7.020 -32.174 1.00 82.84 A C ANISOU 60 CG GLU A 15 9354 12310 9811 868 750 -1224 A C ATOM 61 CD GLU A 15 47.873 -7.148 -33.644 1.00103.19 A C ANISOU 61 CD GLU A 15 11964 15071 12171 913 844 -1338 A C ATOM 62 OE1 GLU A 15 48.456 -8.188 -34.037 1.00107.36 A O ANISOU 62 OE1 GLU A 15 12447 15618 12727 988 877 -1525 A O ATOM 63 OE2 GLU A 15 47.560 -6.209 -34.408 1.00112.30 A O1- ANISOU 63 OE2 GLU A 15 13201 16348 13120 880 883 -1242 A O1- ATOM 64 N VAL A 16 49.277 -9.399 -28.532 1.00 56.98 A N ANISOU 64 N VAL A 16 5815 8548 7288 937 622 -1327 A N ATOM 65 CA VAL A 16 50.275 -10.001 -27.644 1.00 57.10 A C ANISOU 65 CA VAL A 16 5731 8470 7494 986 620 -1357 A C ATOM 66 C VAL A 16 51.672 -10.074 -28.303 1.00 54.43 A C ANISOU 66 C VAL A 16 5279 8286 7115 1064 762 -1444 A C ATOM 67 O VAL A 16 52.691 -10.265 -27.633 1.00 56.59 A O ANISOU 67 O VAL A 16 5438 8541 7523 1101 786 -1440 A O ATOM 68 CB VAL A 16 49.810 -11.405 -27.154 1.00 54.27 A C ANISOU 68 CB VAL A 16 5413 7920 7286 1044 487 -1477 A C ATOM 69 CG1 VAL A 16 50.026 -12.443 -28.227 1.00 51.28 A C ANISOU 69 CG1 VAL A 16 5056 7579 6850 1158 508 -1695 A C ATOM 70 CG2 VAL A 16 50.531 -11.819 -25.887 1.00 52.71 A C ANISOU 70 CG2 VAL A 16 5145 7585 7297 1069 442 -1439 A C ATOM 71 N SER A 17 51.714 -9.897 -29.618 1.00 52.35 A N ANISOU 71 N SER A 17 5042 8191 6658 1088 858 -1521 A N ATOM 72 CA SER A 17 52.978 -9.841 -30.360 1.00 59.79 A C ANISOU 72 CA SER A 17 5873 9320 7526 1148 1017 -1598 A C ATOM 73 C SER A 17 53.934 -8.765 -29.838 1.00 62.89 A C ANISOU 73 C SER A 17 6151 9804 7940 1058 1116 -1440 A C ATOM 74 O SER A 17 55.116 -8.808 -30.132 1.00 74.13 A O ANISOU 74 O SER A 17 7437 11371 9359 1102 1237 -1496 A O ATOM 75 CB SER A 17 52.713 -9.594 -31.849 1.00 64.98 A C ANISOU 75 CB SER A 17 6603 10154 7931 1153 1108 -1668 A C ATOM 76 OG SER A 17 52.241 -8.267 -32.087 1.00 71.17 A O ANISOU 76 OG SER A 17 7460 11017 8564 1025 1142 -1489 A O ATOM 77 N LYS A 18 53.425 -7.797 -29.083 1.00 55.14 A N ANISOU 77 N LYS A 18 5225 8748 6977 931 1066 -1250 A N ATOM 78 CA LYS A 18 54.281 -6.781 -28.474 1.00 58.00 A C ANISOU 78 CA LYS A 18 5500 9167 7371 824 1140 -1100 A C ATOM 79 C LYS A 18 55.273 -7.431 -27.503 1.00 67.73 A C ANISOU 79 C LYS A 18 6573 10347 8813 883 1111 -1141 A C ATOM 80 O LYS A 18 56.356 -6.891 -27.216 1.00 61.61 A O ANISOU 80 O LYS A 18 5664 9678 8066 827 1195 -1081 A O ATOM 81 CB LYS A 18 53.438 -5.732 -27.728 1.00 46.88 A C ANISOU 81 CB LYS A 18 4207 7646 5958 695 1070 -906 A C ATOM 82 CG LYS A 18 52.725 -6.271 -26.501 1.00 54.66 A C ANISOU 82 CG LYS A 18 5229 8416 7124 711 909 -884 A C ATOM 83 CD LYS A 18 51.678 -5.289 -25.962 1.00 60.00 A C ANISOU 83 CD LYS A 18 6036 8998 7762 611 847 -719 A C ATOM 84 CE LYS A 18 52.321 -4.061 -25.340 1.00 54.76 A C ANISOU 84 CE LYS A 18 5358 8350 7098 487 906 -556 A C ATOM 85 NZ LYS A 18 51.301 -3.213 -24.662 1.00 58.05 A N1+ ANISOU 85 NZ LYS A 18 5909 8645 7501 417 835 -412 A N1+ ATOM 86 N TYR A 19 54.864 -8.585 -26.981 1.00 66.69 A N ANISOU 86 N TYR A 19 6465 10048 8826 988 983 -1238 A N ATOM 87 CA TYR A 19 55.681 -9.383 -26.087 1.00 58.72 A C ANISOU 87 CA TYR A 19 5332 8962 8016 1077 928 -1288 A C ATOM 88 C TYR A 19 56.268 -10.525 -26.892 1.00 62.90 A C ANISOU 88 C TYR A 19 5793 9556 8551 1257 975 -1501 A C ATOM 89 O TYR A 19 55.650 -11.024 -27.828 1.00 69.74 A O ANISOU 89 O TYR A 19 6760 10427 9313 1315 981 -1621 A O ATOM 90 CB TYR A 19 54.849 -9.909 -24.913 1.00 61.73 A C ANISOU 90 CB TYR A 19 5808 9095 8552 1071 753 -1241 A C ATOM 91 CG TYR A 19 54.247 -8.805 -24.076 1.00 62.50 A C ANISOU 91 CG TYR A 19 5977 9128 8643 910 711 -1044 A C ATOM 92 CD1 TYR A 19 55.021 -8.107 -23.156 1.00 64.91 A C ANISOU 92 CD1 TYR A 19 6194 9449 9021 829 721 -921 A C ATOM 93 CD2 TYR A 19 52.912 -8.440 -24.222 1.00 60.76 A C ANISOU 93 CD2 TYR A 19 5910 8840 8337 843 662 -986 A C ATOM 94 CE1 TYR A 19 54.483 -7.081 -22.397 1.00 59.18 A C ANISOU 94 CE1 TYR A 19 5551 8654 8279 688 687 -752 A C ATOM 95 CE2 TYR A 19 52.358 -7.408 -23.470 1.00 54.59 A C ANISOU 95 CE2 TYR A 19 5196 8001 7544 718 631 -815 A C ATOM 96 CZ TYR A 19 53.149 -6.734 -22.557 1.00 63.27 A C ANISOU 96 CZ TYR A 19 6228 9099 8714 642 647 -701 A C ATOM 97 OH TYR A 19 52.612 -5.709 -21.796 1.00 61.84 A O ANISOU 97 OH TYR A 19 6132 8848 8516 524 618 -543 A O ATOM 98 N GLU A 20 57.482 -10.920 -26.547 1.00 70.95 A N ANISOU 98 N GLU A 20 6638 10636 9683 1351 1008 -1553 A N ATOM 99 CA GLU A 20 58.135 -11.993 -27.257 1.00 69.65 A C ANISOU 99 CA GLU A 20 6397 10535 9532 1549 1059 -1762 A C ATOM 100 C GLU A 20 58.182 -13.219 -26.359 1.00 65.13 A C ANISOU 100 C GLU A 20 5836 9741 9170 1694 907 -1835 A C ATOM 101 O GLU A 20 58.767 -13.189 -25.278 1.00 62.60 A O ANISOU 101 O GLU A 20 5415 9370 9000 1696 843 -1751 A O ATOM 102 CB GLU A 20 59.527 -11.547 -27.657 1.00 79.76 A C ANISOU 102 CB GLU A 20 7453 12081 10771 1570 1225 -1780 A C ATOM 103 CG GLU A 20 60.271 -12.510 -28.543 1.00 96.78 A C ANISOU 103 CG GLU A 20 9511 14356 12906 1783 1317 -2004 A C ATOM 104 CD GLU A 20 61.737 -12.141 -28.641 1.00113.93 A C ANISOU 104 CD GLU A 20 11413 16790 15085 1811 1462 -2010 A C ATOM 105 OE1 GLU A 20 62.107 -11.046 -28.148 1.00113.97 A O ANISOU 105 OE1 GLU A 20 11328 16891 15083 1630 1499 -1835 A O ATOM 106 OE2 GLU A 20 62.512 -12.944 -29.202 1.00119.96 A O1- ANISOU 106 OE2 GLU A 20 12054 17666 15859 2011 1540 -2193 A O1- ATOM 107 N LYS A 21 57.532 -14.292 -26.792 1.00 62.35 A N ANISOU 107 N LYS A 21 5623 9247 8822 1805 840 -1987 A N ATOM 108 CA LYS A 21 57.463 -15.502 -25.977 1.00 70.81 A C ANISOU 108 CA LYS A 21 6751 10071 10083 1933 687 -2052 A C ATOM 109 C LYS A 21 58.836 -16.148 -25.805 1.00 78.68 A C ANISOU 109 C LYS A 21 7568 11129 11199 2139 718 -2153 A C ATOM 110 O LYS A 21 59.482 -16.522 -26.783 1.00 84.88 A O ANISOU 110 O LYS A 21 8275 12063 11914 2285 835 -2320 A O ATOM 111 CB LYS A 21 56.485 -16.506 -26.591 1.00 67.62 A C ANISOU 111 CB LYS A 21 6547 9503 9641 1991 616 -2206 A C ATOM 112 CG LYS A 21 55.047 -16.291 -26.202 1.00 57.97 A C ANISOU 112 CG LYS A 21 5502 8123 8400 1817 502 -2099 A C ATOM 113 CD LYS A 21 54.132 -17.025 -27.154 1.00 63.07 A C ANISOU 113 CD LYS A 21 6315 8700 8948 1838 470 -2258 A C ATOM 114 CE LYS A 21 52.668 -16.705 -26.861 1.00 70.46 A C ANISOU 114 CE LYS A 21 7394 9531 9847 1654 368 -2150 A C ATOM 115 NZ LYS A 21 51.782 -16.928 -28.050 1.00 73.41 A N1+ ANISOU 115 NZ LYS A 21 7889 9950 10054 1627 374 -2274 A N1+ ATOM 116 N LEU A 22 59.276 -16.284 -24.560 1.00 77.96 A N ANISOU 116 N LEU A 22 7409 10931 11282 2159 612 -2055 A N ATOM 117 CA LEU A 22 60.575 -16.887 -24.278 1.00 83.37 A C ANISOU 117 CA LEU A 22 7910 11674 12094 2367 617 -2135 A C ATOM 118 C LEU A 22 60.494 -18.370 -23.916 1.00 91.57 A C ANISOU 118 C LEU A 22 9065 12447 13281 2578 475 -2262 A C ATOM 119 O LEU A 22 61.284 -19.174 -24.405 1.00100.69 A O ANISOU 119 O LEU A 22 10140 13646 14472 2814 517 -2436 A O ATOM 120 CB LEU A 22 61.278 -16.133 -23.153 1.00 82.46 A C ANISOU 120 CB LEU A 22 7627 11630 12073 2277 582 -1955 A C ATOM 121 CG LEU A 22 61.674 -14.699 -23.464 1.00 81.60 A C ANISOU 121 CG LEU A 22 7375 11794 11837 2087 730 -1840 A C ATOM 122 CD1 LEU A 22 62.369 -14.080 -22.267 1.00 82.18 A C ANISOU 122 CD1 LEU A 22 7300 11909 12017 1998 669 -1677 A C ATOM 123 CD2 LEU A 22 62.567 -14.686 -24.679 1.00 83.29 A C ANISOU 123 CD2 LEU A 22 7417 12285 11945 2194 918 -1986 A C ATOM 124 N ALA A 23 59.541 -18.730 -23.059 1.00 93.20 A N ANISOU 124 N ALA A 23 9467 12377 13569 2493 311 -2174 A N ATOM 125 CA ALA A 23 59.498 -20.074 -22.493 1.00 89.95 A C ANISOU 125 CA ALA A 23 9182 11684 13312 2663 157 -2252 A C ATOM 126 C ALA A 23 58.184 -20.371 -21.770 1.00 96.69 A C ANISOU 126 C ALA A 23 10281 12251 14205 2507 4 -2155 A C ATOM 127 O ALA A 23 57.735 -19.574 -20.946 1.00 99.47 A O ANISOU 127 O ALA A 23 10638 12595 14560 2312 -38 -1964 A O ATOM 128 CB ALA A 23 60.670 -20.255 -21.533 1.00 80.63 A C ANISOU 128 CB ALA A 23 7828 10520 12289 2806 94 -2196 A C ATOM 129 N LYS A 24 57.576 -21.519 -22.070 1.00 98.45 A N ANISOU 129 N LYS A 24 10709 12242 14455 2587 -75 -2290 A N ATOM 130 CA LYS A 24 56.436 -22.001 -21.293 1.00 95.64 A C ANISOU 130 CA LYS A 24 10580 11600 14160 2452 -230 -2207 A C ATOM 131 C LYS A 24 56.870 -22.193 -19.852 1.00 94.42 A C ANISOU 131 C LYS A 24 10407 11303 14166 2479 -360 -2059 A C ATOM 132 O LYS A 24 57.993 -22.609 -19.592 1.00 97.58 A O ANISOU 132 O LYS A 24 10694 11716 14665 2688 -378 -2100 A O ATOM 133 CB LYS A 24 55.917 -23.338 -21.825 1.00 99.58 A C ANISOU 133 CB LYS A 24 11299 11857 14679 2551 -301 -2393 A C ATOM 134 CG LYS A 24 55.051 -23.249 -23.070 1.00109.15 A C ANISOU 134 CG LYS A 24 12604 13143 15725 2458 -225 -2518 A C ATOM 135 CD LYS A 24 54.505 -24.626 -23.453 1.00116.78 A C ANISOU 135 CD LYS A 24 13813 13836 16723 2530 -320 -2697 A C ATOM 136 CE LYS A 24 54.158 -24.711 -24.941 1.00117.14 A C ANISOU 136 CE LYS A 24 13907 14001 16599 2542 -223 -2896 A C ATOM 137 NZ LYS A 24 53.607 -26.044 -25.335 1.00113.63 A N1+ ANISOU 137 NZ LYS A 24 13715 13283 16177 2595 -321 -3082 A N1+ ATOM 138 N ILE A 25 55.981 -21.883 -18.918 1.00 95.62 A N ANISOU 138 N ILE A 25 10665 11330 14335 2272 -450 -1887 A N ATOM 139 CA ILE A 25 56.249 -22.126 -17.508 1.00 99.21 A C ANISOU 139 CA ILE A 25 11144 11626 14924 2277 -586 -1740 A C ATOM 140 C ILE A 25 55.007 -22.699 -16.841 1.00109.45 A C ANISOU 140 C ILE A 25 12688 12646 16252 2121 -713 -1668 A C ATOM 141 O ILE A 25 54.803 -22.539 -15.635 1.00104.23 A O ANISOU 141 O ILE A 25 12069 11886 15649 2017 -806 -1497 A O ATOM 142 CB ILE A 25 56.725 -20.854 -16.778 1.00 87.85 A C ANISOU 142 CB ILE A 25 9521 10387 13470 2164 -549 -1559 A C ATOM 143 CG1 ILE A 25 55.640 -19.778 -16.799 1.00 82.93 A C ANISOU 143 CG1 ILE A 25 8938 9847 12726 1899 -492 -1443 A C ATOM 144 CG2 ILE A 25 58.002 -20.331 -17.412 1.00 85.66 A C ANISOU 144 CG2 ILE A 25 8989 10391 13167 2299 -423 -1628 A C ATOM 145 CD1 ILE A 25 56.097 -18.435 -16.252 1.00 77.11 A C ANISOU 145 CD1 ILE A 25 8038 9310 11952 1783 -436 -1286 A C ATOM 146 N GLY A 26 54.183 -23.368 -17.646 1.00118.30 A N ANISOU 146 N GLY A 26 13970 13653 17327 2096 -714 -1803 A N ATOM 147 CA GLY A 26 52.993 -24.040 -17.157 1.00120.13 A C ANISOU 147 CA GLY A 26 14435 13624 17584 1942 -829 -1761 A C ATOM 148 C GLY A 26 51.834 -24.070 -18.142 1.00121.06 A C ANISOU 148 C GLY A 26 14652 13761 17584 1800 -785 -1861 A C ATOM 149 O GLY A 26 51.979 -23.717 -19.317 1.00111.77 A O ANISOU 149 O GLY A 26 13392 12775 16302 1851 -672 -1987 A O ATOM 150 N GLN A 27 50.681 -24.520 -17.652 1.00129.16 A N ANISOU 150 N GLN A 27 15857 14594 18624 1616 -880 -1802 A N ATOM 151 CA GLN A 27 49.425 -24.470 -18.399 1.00128.92 A C ANISOU 151 CA GLN A 27 15905 14594 18483 1437 -860 -1864 A C ATOM 152 C GLN A 27 48.252 -24.223 -17.457 1.00125.74 A C ANISOU 152 C GLN A 27 15574 14120 18082 1182 -923 -1692 A C ATOM 153 O GLN A 27 47.798 -25.140 -16.765 1.00127.76 A O ANISOU 153 O GLN A 27 16003 14119 18419 1109 -1037 -1661 A O ATOM 154 CB GLN A 27 49.180 -25.757 -19.188 1.00126.18 A C ANISOU 154 CB GLN A 27 15745 14050 18148 1503 -916 -2073 A C ATOM 155 CG GLN A 27 47.735 -25.889 -19.646 1.00125.53 A C ANISOU 155 CG GLN A 27 15773 13945 17976 1272 -944 -2109 A C ATOM 156 CD GLN A 27 47.615 -26.422 -21.054 1.00133.20 A C ANISOU 156 CD GLN A 27 16813 14937 18859 1340 -914 -2347 A C ATOM 157 NE2 GLN A 27 46.556 -26.019 -21.748 1.00127.11 A N ANISOU 157 NE2 GLN A 27 16035 14303 17958 1166 -891 -2377 A N ATOM 158 OE1 GLN A 27 48.465 -27.187 -21.518 1.00143.06 A O ANISOU 158 OE1 GLN A 27 18120 16086 20150 1557 -914 -2507 A O ATOM 159 N GLY A 28 47.765 -22.985 -17.447 1.00116.33 A N ANISOU 159 N GLY A 28 14252 13155 16793 1051 -844 -1582 A N ATOM 160 CA GLY A 28 46.701 -22.570 -16.549 1.00116.04 A C ANISOU 160 CA GLY A 28 14246 13101 16745 828 -880 -1416 A C ATOM 161 C GLY A 28 45.326 -23.166 -16.815 1.00117.75 A C ANISOU 161 C GLY A 28 14592 13224 16924 643 -937 -1464 A C ATOM 162 O GLY A 28 45.189 -24.173 -17.518 1.00122.46 A O ANISOU 162 O GLY A 28 15310 13689 17532 674 -984 -1626 A O ATOM 163 N THR A 29 44.304 -22.528 -16.248 1.00112.67 A N ANISOU 163 N THR A 29 13917 12658 16235 446 -931 -1328 A N ATOM 164 CA THR A 29 42.931 -23.032 -16.300 1.00111.22 A C ANISOU 164 CA THR A 29 13827 12409 16022 239 -988 -1345 A C ATOM 165 C THR A 29 42.299 -22.936 -17.689 1.00108.03 A C ANISOU 165 C THR A 29 13390 12155 15500 212 -956 -1496 A C ATOM 166 O THR A 29 41.432 -23.737 -18.040 1.00105.12 A O ANISOU 166 O THR A 29 13126 11692 15121 84 -1024 -1584 A O ATOM 167 CB THR A 29 42.019 -22.298 -15.287 1.00103.98 A C ANISOU 167 CB THR A 29 12858 11569 15082 51 -978 -1156 A C ATOM 168 CG2 THR A 29 40.619 -22.914 -15.268 1.00 98.19 A C ANISOU 168 CG2 THR A 29 12205 10775 14328 -176 -1038 -1171 A C ATOM 169 OG1 THR A 29 42.590 -22.384 -13.977 1.00107.58 A O ANISOU 169 OG1 THR A 29 13357 11890 15630 67 -1012 -1014 A O ATOM 170 N PHE A 30 42.740 -21.962 -18.479 1.00104.42 A N ANISOU 170 N PHE A 30 12795 11930 14948 323 -857 -1524 A N ATOM 171 CA PHE A 30 42.092 -21.666 -19.750 1.00 98.79 A C ANISOU 171 CA PHE A 30 12039 11397 14098 293 -824 -1637 A C ATOM 172 C PHE A 30 43.038 -21.767 -20.932 1.00 97.86 A C ANISOU 172 C PHE A 30 11908 11350 13926 485 -765 -1803 A C ATOM 173 O PHE A 30 42.661 -21.404 -22.047 1.00101.93 A O ANISOU 173 O PHE A 30 12384 12040 14307 483 -725 -1892 A O ATOM 174 CB PHE A 30 41.490 -20.260 -19.705 1.00 99.05 A C ANISOU 174 CB PHE A 30 11928 11680 14027 223 -753 -1504 A C ATOM 175 CG PHE A 30 40.480 -20.072 -18.609 1.00100.12 A C ANISOU 175 CG PHE A 30 12059 11787 14196 42 -793 -1352 A C ATOM 176 CD1 PHE A 30 39.208 -20.632 -18.719 1.00 92.42 A C ANISOU 176 CD1 PHE A 30 11127 10789 13199 -137 -864 -1389 A C ATOM 177 CD2 PHE A 30 40.801 -19.350 -17.464 1.00 96.37 A C ANISOU 177 CD2 PHE A 30 11533 11317 13768 42 -758 -1178 A C ATOM 178 CE1 PHE A 30 38.282 -20.471 -17.715 1.00 93.16 A C ANISOU 178 CE1 PHE A 30 11200 10879 13318 -305 -887 -1252 A C ATOM 179 CE2 PHE A 30 39.875 -19.185 -16.452 1.00 92.72 A C ANISOU 179 CE2 PHE A 30 11068 10839 13324 -119 -783 -1045 A C ATOM 180 CZ PHE A 30 38.612 -19.745 -16.579 1.00 93.25 A C ANISOU 180 CZ PHE A 30 11165 10896 13369 -290 -842 -1081 A C ATOM 181 N GLY A 31 44.256 -22.255 -20.680 1.00 92.43 A N ANISOU 181 N GLY A 31 11247 10537 13336 654 -759 -1841 A N ATOM 182 CA GLY A 31 45.327 -22.262 -21.667 1.00 98.32 A C ANISOU 182 CA GLY A 31 11947 11373 14037 858 -680 -1983 A C ATOM 183 C GLY A 31 46.726 -22.256 -21.049 1.00110.46 A C ANISOU 183 C GLY A 31 13423 12863 15684 1036 -650 -1939 A C ATOM 184 O GLY A 31 46.879 -22.459 -19.844 1.00122.00 A O ANISOU 184 O GLY A 31 14914 14176 17266 1010 -714 -1814 A O ATOM 185 N GLU A 32 47.749 -22.010 -21.868 1.00 99.83 A N ANISOU 185 N GLU A 32 11982 11660 14287 1214 -551 -2040 A N ATOM 186 CA GLU A 32 49.137 -22.111 -21.423 1.00 91.49 A C ANISOU 186 CA GLU A 32 10846 10583 13333 1402 -524 -2029 A C ATOM 187 C GLU A 32 49.708 -20.844 -20.769 1.00 82.56 A C ANISOU 187 C GLU A 32 9540 9629 12200 1381 -453 -1846 A C ATOM 188 O GLU A 32 49.203 -19.742 -20.971 1.00 83.07 A O ANISOU 188 O GLU A 32 9534 9875 12155 1260 -387 -1755 A O ATOM 189 CB GLU A 32 50.027 -22.550 -22.584 1.00101.75 A C ANISOU 189 CB GLU A 32 12117 11956 14587 1610 -447 -2238 A C ATOM 190 CG GLU A 32 49.753 -23.971 -23.049 1.00110.67 A C ANISOU 190 CG GLU A 32 13443 12854 15753 1676 -532 -2433 A C ATOM 191 CD GLU A 32 50.916 -24.575 -23.818 1.00114.80 A C ANISOU 191 CD GLU A 32 13942 13394 16284 1941 -469 -2630 A C ATOM 192 OE1 GLU A 32 51.218 -24.083 -24.927 1.00114.27 A O ANISOU 192 OE1 GLU A 32 13780 13560 16076 2001 -343 -2732 A O ATOM 193 OE2 GLU A 32 51.518 -25.551 -23.316 1.00114.49 A O1- ANISOU 193 OE2 GLU A 32 13983 13134 16384 2095 -545 -2683 A O1- ATOM 194 N VAL A 33 50.764 -21.019 -19.979 1.00 74.59 A N ANISOU 194 N VAL A 33 8471 8559 11312 1502 -475 -1795 A N ATOM 195 CA VAL A 33 51.442 -19.904 -19.327 1.00 77.98 A C ANISOU 195 CA VAL A 33 8737 9144 11748 1484 -418 -1637 A C ATOM 196 C VAL A 33 52.863 -19.718 -19.871 1.00 82.68 A C ANISOU 196 C VAL A 33 9165 9908 12343 1673 -320 -1718 A C ATOM 197 O VAL A 33 53.664 -20.653 -19.848 1.00 87.21 A O ANISOU 197 O VAL A 33 9741 10382 13014 1861 -359 -1822 A O ATOM 198 CB VAL A 33 51.521 -20.114 -17.808 1.00 74.74 A C ANISOU 198 CB VAL A 33 8369 8560 11470 1442 -532 -1483 A C ATOM 199 CG1 VAL A 33 51.943 -18.822 -17.115 1.00 69.05 A C ANISOU 199 CG1 VAL A 33 7504 8003 10728 1367 -480 -1310 A C ATOM 200 CG2 VAL A 33 50.188 -20.579 -17.283 1.00 75.87 A C ANISOU 200 CG2 VAL A 33 8686 8515 11626 1273 -630 -1428 A C ATOM 201 N PHE A 34 53.170 -18.507 -20.343 1.00 75.25 A N ANISOU 201 N PHE A 34 8079 9222 11290 1624 -193 -1666 A N ATOM 202 CA PHE A 34 54.476 -18.194 -20.935 1.00 67.52 A C ANISOU 202 CA PHE A 34 6919 8449 10288 1766 -76 -1735 A C ATOM 203 C PHE A 34 55.237 -17.108 -20.189 1.00 67.86 A C ANISOU 203 C PHE A 34 6798 8636 10351 1706 -35 -1572 A C ATOM 204 O PHE A 34 54.647 -16.117 -19.745 1.00 66.15 A O ANISOU 204 O PHE A 34 6597 8458 10080 1526 -28 -1418 A O ATOM 205 CB PHE A 34 54.300 -17.693 -22.364 1.00 66.88 A C ANISOU 205 CB PHE A 34 6809 8575 10028 1752 63 -1834 A C ATOM 206 CG PHE A 34 53.734 -18.704 -23.296 1.00 78.75 A C ANISOU 206 CG PHE A 34 8453 9983 11486 1824 42 -2025 A C ATOM 207 CD1 PHE A 34 54.559 -19.641 -23.903 1.00 86.35 A C ANISOU 207 CD1 PHE A 34 9395 10933 12481 2040 70 -2217 A C ATOM 208 CD2 PHE A 34 52.380 -18.718 -23.579 1.00 78.31 A C ANISOU 208 CD2 PHE A 34 8546 9859 11350 1679 -8 -2021 A C ATOM 209 CE1 PHE A 34 54.042 -20.578 -24.771 1.00 87.51 A C ANISOU 209 CE1 PHE A 34 9692 10981 12578 2102 48 -2406 A C ATOM 210 CE2 PHE A 34 51.854 -19.652 -24.447 1.00 88.89 A C ANISOU 210 CE2 PHE A 34 10019 11114 12641 1727 -37 -2205 A C ATOM 211 CZ PHE A 34 52.689 -20.587 -25.044 1.00 90.51 A C ANISOU 211 CZ PHE A 34 10226 11288 12875 1936 -9 -2400 A C ATOM 212 N LYS A 35 56.552 -17.276 -20.077 1.00 68.92 A N ANISOU 212 N LYS A 35 6771 8859 10559 1857 -7 -1611 A N ATOM 213 CA LYS A 35 57.411 -16.158 -19.715 1.00 65.96 A C ANISOU 213 CA LYS A 35 6208 8687 10169 1792 65 -1491 A C ATOM 214 C LYS A 35 57.714 -15.400 -21.001 1.00 67.86 A C ANISOU 214 C LYS A 35 6344 9189 10249 1771 245 -1555 A C ATOM 215 O LYS A 35 57.975 -16.012 -22.036 1.00 72.85 A O ANISOU 215 O LYS A 35 6961 9882 10836 1912 314 -1728 A O ATOM 216 CB LYS A 35 58.708 -16.628 -19.069 1.00 67.73 A C ANISOU 216 CB LYS A 35 6275 8927 10533 1956 16 -1504 A C ATOM 217 CG LYS A 35 59.594 -15.471 -18.613 1.00 69.20 A C ANISOU 217 CG LYS A 35 6260 9325 10707 1859 75 -1376 A C ATOM 218 CD LYS A 35 60.952 -15.943 -18.138 1.00 72.59 A C ANISOU 218 CD LYS A 35 6494 9822 11264 2037 33 -1409 A C ATOM 219 CE LYS A 35 61.773 -14.777 -17.594 1.00 82.49 A C ANISOU 219 CE LYS A 35 7553 11283 12507 1904 74 -1274 A C ATOM 220 NZ LYS A 35 63.114 -15.192 -17.073 1.00 84.89 A N1+ ANISOU 220 NZ LYS A 35 7637 11681 12936 2069 19 -1298 A N1+ ATOM 221 N ALA A 36 57.658 -14.074 -20.956 1.00 57.10 A N ANISOU 221 N ALA A 36 4931 7974 8792 1594 322 -1418 A N ATOM 222 CA ALA A 36 57.924 -13.302 -22.162 1.00 59.33 A C ANISOU 222 CA ALA A 36 5136 8498 8908 1554 493 -1457 A C ATOM 223 C ALA A 36 58.585 -11.959 -21.908 1.00 62.36 A C ANISOU 223 C ALA A 36 5386 9068 9241 1406 581 -1313 A C ATOM 224 O ALA A 36 58.715 -11.497 -20.769 1.00 59.24 A O ANISOU 224 O ALA A 36 4970 8611 8926 1312 504 -1173 A O ATOM 225 CB ALA A 36 56.657 -13.126 -22.992 1.00 56.87 A C ANISOU 225 CB ALA A 36 5000 8157 8452 1473 516 -1480 A C ATOM 226 N ARG A 37 58.973 -11.330 -23.007 1.00 66.49 A N ANISOU 226 N ARG A 37 5832 9815 9615 1375 743 -1349 A N ATOM 227 CA ARG A 37 59.831 -10.163 -22.982 1.00 65.31 A C ANISOU 227 CA ARG A 37 5534 9873 9409 1244 853 -1243 A C ATOM 228 C ARG A 37 59.205 -9.082 -23.834 1.00 63.33 A C ANISOU 228 C ARG A 37 5388 9716 8958 1088 963 -1173 A C ATOM 229 O ARG A 37 58.906 -9.307 -25.007 1.00 60.50 A O ANISOU 229 O ARG A 37 5081 9435 8472 1144 1046 -1279 A O ATOM 230 CB ARG A 37 61.195 -10.548 -23.563 1.00 63.26 A C ANISOU 230 CB ARG A 37 5039 9833 9162 1380 965 -1370 A C ATOM 231 CG ARG A 37 62.213 -9.447 -23.575 1.00 60.01 A C ANISOU 231 CG ARG A 37 4440 9662 8698 1238 1086 -1276 A C ATOM 232 CD ARG A 37 63.483 -9.891 -24.297 1.00 56.73 A C ANISOU 232 CD ARG A 37 3778 9497 8280 1383 1216 -1420 A C ATOM 233 NE ARG A 37 64.456 -8.811 -24.288 1.00 67.41 A N ANISOU 233 NE ARG A 37 4938 11093 9580 1214 1334 -1322 A N ATOM 234 CZ ARG A 37 64.464 -7.808 -25.157 1.00 68.35 A C ANISOU 234 CZ ARG A 37 5076 11382 9514 1045 1495 -1267 A C ATOM 235 NH1 ARG A 37 63.559 -7.763 -26.129 1.00 59.96 A N1+ ANISOU 235 NH1 ARG A 37 4205 10282 8294 1042 1554 -1305 A N1+ ATOM 236 NH2 ARG A 37 65.389 -6.862 -25.060 1.00 74.43 A N ANISOU 236 NH2 ARG A 37 5672 12359 10248 873 1594 -1174 A N ATOM 237 N HIS A 38 58.993 -7.913 -23.247 1.00 58.50 A N ANISOU 237 N HIS A 38 4824 9090 8313 897 957 -997 A N ATOM 238 CA HIS A 38 58.520 -6.786 -24.021 1.00 57.48 A C ANISOU 238 CA HIS A 38 4796 9049 7993 753 1062 -913 A C ATOM 239 C HIS A 38 59.540 -6.475 -25.110 1.00 64.55 A C ANISOU 239 C HIS A 38 5545 10211 8768 747 1245 -972 A C ATOM 240 O HIS A 38 60.733 -6.377 -24.826 1.00 66.91 A O ANISOU 240 O HIS A 38 5643 10647 9132 735 1297 -972 A O ATOM 241 CB HIS A 38 58.313 -5.573 -23.127 1.00 61.91 A C ANISOU 241 CB HIS A 38 5427 9544 8552 560 1028 -719 A C ATOM 242 CG HIS A 38 57.665 -4.432 -23.835 1.00 68.71 A C ANISOU 242 CG HIS A 38 6436 10445 9224 429 1110 -620 A C ATOM 243 CD2 HIS A 38 56.409 -3.930 -23.759 1.00 55.77 A C ANISOU 243 CD2 HIS A 38 5000 8675 7517 378 1053 -535 A C ATOM 244 ND1 HIS A 38 58.321 -3.688 -24.794 1.00 77.72 A N ANISOU 244 ND1 HIS A 38 7525 11790 10214 346 1272 -602 A N ATOM 245 CE1 HIS A 38 57.499 -2.767 -25.266 1.00 77.58 A C ANISOU 245 CE1 HIS A 38 7690 11746 10041 250 1302 -502 A C ATOM 246 NE2 HIS A 38 56.333 -2.893 -24.654 1.00 61.03 A N ANISOU 246 NE2 HIS A 38 5742 9451 7995 278 1169 -464 A N ATOM 247 N ARG A 39 59.086 -6.319 -26.352 1.00 62.30 A N ANISOU 247 N ARG A 39 5352 10017 8303 753 1342 -1021 A N ATOM 248 CA ARG A 39 60.023 -6.226 -27.469 1.00 56.86 A C ANISOU 248 CA ARG A 39 4526 9589 7488 771 1524 -1104 A C ATOM 249 C ARG A 39 60.839 -4.936 -27.502 1.00 64.42 A C ANISOU 249 C ARG A 39 5397 10719 8361 568 1652 -963 A C ATOM 250 O ARG A 39 61.858 -4.864 -28.197 1.00 63.22 A O ANISOU 250 O ARG A 39 5075 10807 8137 565 1807 -1022 A O ATOM 251 CB ARG A 39 59.332 -6.463 -28.811 1.00 63.98 A C ANISOU 251 CB ARG A 39 5559 10546 8203 834 1590 -1202 A C ATOM 252 CG ARG A 39 58.978 -7.930 -29.060 1.00 82.79 A C ANISOU 252 CG ARG A 39 7965 12834 10657 1051 1513 -1403 A C ATOM 253 CD ARG A 39 58.545 -8.208 -30.513 1.00 87.87 A C ANISOU 253 CD ARG A 39 8706 13584 11096 1116 1600 -1531 A C ATOM 254 NE ARG A 39 57.662 -9.375 -30.604 1.00 86.40 A N ANISOU 254 NE ARG A 39 8643 13222 10962 1258 1471 -1674 A N ATOM 255 CZ ARG A 39 58.058 -10.612 -30.906 1.00 92.85 A C ANISOU 255 CZ ARG A 39 9404 14031 11843 1449 1469 -1880 A C ATOM 256 NH1 ARG A 39 59.338 -10.867 -31.171 1.00 88.28 A N1+ ANISOU 256 NH1 ARG A 39 8627 13630 11284 1548 1596 -1975 A N1+ ATOM 257 NH2 ARG A 39 57.167 -11.600 -30.946 1.00 90.56 A N ANISOU 257 NH2 ARG A 39 9257 13555 11597 1543 1341 -1995 A N ATOM 258 N LYS A 40 60.412 -3.927 -26.744 1.00 66.18 A N ANISOU 258 N LYS A 40 5735 10822 8590 395 1590 -783 A N ATOM 259 CA LYS A 40 61.090 -2.627 -26.774 1.00 57.70 A C ANISOU 259 CA LYS A 40 4622 9877 7424 174 1703 -639 A C ATOM 260 C LYS A 40 61.938 -2.345 -25.540 1.00 57.24 A C ANISOU 260 C LYS A 40 4415 9809 7526 78 1646 -564 A C ATOM 261 O LYS A 40 62.994 -1.728 -25.637 1.00 62.91 A O ANISOU 261 O LYS A 40 4979 10713 8211 -59 1757 -520 A O ATOM 262 CB LYS A 40 60.084 -1.500 -26.967 1.00 60.25 A C ANISOU 262 CB LYS A 40 5204 10090 7599 30 1697 -484 A C ATOM 263 CG LYS A 40 59.543 -1.369 -28.383 1.00 60.52 A C ANISOU 263 CG LYS A 40 5366 10217 7414 58 1797 -518 A C ATOM 264 CD LYS A 40 58.246 -0.557 -28.374 1.00 62.25 A C ANISOU 264 CD LYS A 40 5856 10264 7531 -6 1724 -384 A C ATOM 265 CE LYS A 40 57.819 -0.187 -29.779 1.00 70.53 A C ANISOU 265 CE LYS A 40 7037 11424 8335 -11 1826 -381 A C ATOM 266 NZ LYS A 40 58.930 0.462 -30.535 1.00 77.24 A N1+ ANISOU 266 NZ LYS A 40 7799 12503 9044 -147 2019 -344 A N1+ ATOM 267 N THR A 41 61.473 -2.806 -24.387 1.00 56.83 A N ANISOU 267 N THR A 41 4407 9548 7640 141 1472 -551 A N ATOM 268 CA THR A 41 62.071 -2.457 -23.103 1.00 59.34 A C ANISOU 268 CA THR A 41 4634 9819 8094 38 1388 -461 A C ATOM 269 C THR A 41 62.729 -3.653 -22.429 1.00 64.95 A C ANISOU 269 C THR A 41 5147 10533 8998 213 1292 -573 A C ATOM 270 O THR A 41 63.546 -3.485 -21.525 1.00 67.06 A O ANISOU 270 O THR A 41 5268 10838 9372 148 1240 -526 A O ATOM 271 CB THR A 41 60.988 -1.978 -22.134 1.00 58.16 A C ANISOU 271 CB THR A 41 4711 9410 7977 -34 1249 -339 A C ATOM 272 CG2 THR A 41 60.062 -0.959 -22.822 1.00 42.40 A C ANISOU 272 CG2 THR A 41 2950 7365 5795 -144 1314 -241 A C ATOM 273 OG1 THR A 41 60.232 -3.116 -21.691 1.00 54.30 A O ANISOU 273 OG1 THR A 41 4278 8750 7604 150 1112 -420 A O ATOM 274 N GLY A 42 62.345 -4.857 -22.847 1.00 63.28 A N ANISOU 274 N GLY A 42 4946 10270 8828 436 1258 -719 A N ATOM 275 CA GLY A 42 62.902 -6.077 -22.296 1.00 55.56 A C ANISOU 275 CA GLY A 42 3814 9268 8027 633 1163 -832 A C ATOM 276 C GLY A 42 62.192 -6.507 -21.028 1.00 58.04 A C ANISOU 276 C GLY A 42 4256 9314 8482 667 964 -777 A C ATOM 277 O GLY A 42 62.521 -7.542 -20.445 1.00 58.07 A O ANISOU 277 O GLY A 42 4178 9250 8637 830 858 -851 A O ATOM 278 N GLN A 43 61.209 -5.721 -20.597 1.00 59.41 A N ANISOU 278 N GLN A 43 4638 9335 8602 518 916 -646 A N ATOM 279 CA GLN A 43 60.478 -6.032 -19.366 1.00 63.14 A C ANISOU 279 CA GLN A 43 5238 9565 9187 527 742 -583 A C ATOM 280 C GLN A 43 59.894 -7.432 -19.426 1.00 64.88 A C ANISOU 280 C GLN A 43 5519 9641 9492 731 651 -706 A C ATOM 281 O GLN A 43 59.164 -7.754 -20.363 1.00 62.02 A O ANISOU 281 O GLN A 43 5258 9262 9045 792 696 -784 A O ATOM 282 CB GLN A 43 59.368 -5.013 -19.120 1.00 58.21 A C ANISOU 282 CB GLN A 43 4838 8814 8467 366 729 -448 A C ATOM 283 CG GLN A 43 58.425 -5.379 -17.985 1.00 67.60 A C ANISOU 283 CG GLN A 43 6173 9763 9747 381 570 -395 A C ATOM 284 CD GLN A 43 57.065 -4.707 -18.125 1.00 79.33 A C ANISOU 284 CD GLN A 43 7881 11137 11125 301 573 -319 A C ATOM 285 NE2 GLN A 43 56.366 -4.546 -17.008 1.00 80.63 A N ANISOU 285 NE2 GLN A 43 8165 11132 11340 249 466 -231 A N ATOM 286 OE1 GLN A 43 56.647 -4.344 -19.230 1.00 82.30 A O ANISOU 286 OE1 GLN A 43 8317 11587 11367 295 670 -339 A O ATOM 287 N LYS A 44 60.230 -8.266 -18.442 1.00 67.15 A N ANISOU 287 N LYS A 44 5751 9822 9940 831 517 -722 A N ATOM 288 CA LYS A 44 59.729 -9.639 -18.402 1.00 62.06 A C ANISOU 288 CA LYS A 44 5182 9011 9387 1016 418 -832 A C ATOM 289 C LYS A 44 58.324 -9.682 -17.814 1.00 67.84 A C ANISOU 289 C LYS A 44 6146 9513 10118 946 316 -758 A C ATOM 290 O LYS A 44 58.030 -9.004 -16.828 1.00 71.23 A O ANISOU 290 O LYS A 44 6640 9865 10558 812 255 -620 A O ATOM 291 CB LYS A 44 60.642 -10.538 -17.578 1.00 58.94 A C ANISOU 291 CB LYS A 44 4655 8581 9160 1160 308 -869 A C ATOM 292 CG LYS A 44 62.105 -10.572 -18.022 1.00 60.60 A C ANISOU 292 CG LYS A 44 4595 9038 9393 1250 397 -946 A C ATOM 293 CD LYS A 44 62.259 -11.006 -19.462 1.00 63.52 A C ANISOU 293 CD LYS A 44 4914 9539 9681 1378 537 -1109 A C ATOM 294 CE LYS A 44 63.729 -10.981 -19.873 1.00 67.03 A C ANISOU 294 CE LYS A 44 5068 10259 10142 1461 641 -1183 A C ATOM 295 NZ LYS A 44 64.408 -9.713 -19.484 1.00 63.66 A N1+ ANISOU 295 NZ LYS A 44 4502 10009 9675 1245 696 -1046 A N1+ ATOM 296 N VAL A 45 57.462 -10.486 -18.427 1.00 65.74 A N ANISOU 296 N VAL A 45 6001 9146 9833 1035 299 -857 A N ATOM 297 CA VAL A 45 56.073 -10.607 -18.003 1.00 62.79 A C ANISOU 297 CA VAL A 45 5827 8581 9451 969 212 -803 A C ATOM 298 C VAL A 45 55.630 -12.071 -18.088 1.00 66.60 A C ANISOU 298 C VAL A 45 6390 8898 10018 1111 120 -927 A C ATOM 299 O VAL A 45 56.318 -12.899 -18.682 1.00 62.33 A O ANISOU 299 O VAL A 45 5771 8396 9517 1271 141 -1067 A O ATOM 300 CB VAL A 45 55.143 -9.764 -18.903 1.00 63.21 A C ANISOU 300 CB VAL A 45 5978 8702 9337 869 304 -779 A C ATOM 301 CG1 VAL A 45 55.593 -8.298 -18.931 1.00 60.37 A C ANISOU 301 CG1 VAL A 45 5567 8489 8881 727 402 -659 A C ATOM 302 CG2 VAL A 45 55.098 -10.344 -20.317 1.00 60.38 A C ANISOU 302 CG2 VAL A 45 5612 8432 8897 978 381 -940 A C ATOM 303 N ALA A 46 54.483 -12.391 -17.494 1.00 66.68 A N ANISOU 303 N ALA A 46 6560 8722 10054 1051 21 -879 A N ATOM 304 CA ALA A 46 53.877 -13.709 -17.670 1.00 61.16 A C ANISOU 304 CA ALA A 46 5971 7854 9413 1143 -62 -991 A C ATOM 305 C ALA A 46 52.604 -13.567 -18.484 1.00 61.21 A C ANISOU 305 C ALA A 46 6093 7863 9300 1069 -32 -1025 A C ATOM 306 O ALA A 46 51.763 -12.714 -18.192 1.00 61.10 A O ANISOU 306 O ALA A 46 6137 7859 9218 931 -26 -910 A O ATOM 307 CB ALA A 46 53.576 -14.364 -16.328 1.00 56.04 A C ANISOU 307 CB ALA A 46 5413 6986 8892 1125 -210 -914 A C ATOM 308 N LEU A 47 52.475 -14.400 -19.511 1.00 63.90 A N ANISOU 308 N LEU A 47 6466 8200 9612 1169 -15 -1189 A N ATOM 309 CA LEU A 47 51.280 -14.421 -20.336 1.00 56.27 A C ANISOU 309 CA LEU A 47 5607 7240 8534 1107 -7 -1242 A C ATOM 310 C LEU A 47 50.469 -15.669 -20.012 1.00 61.29 A C ANISOU 310 C LEU A 47 6381 7654 9254 1112 -133 -1308 A C ATOM 311 O LEU A 47 50.947 -16.791 -20.174 1.00 71.65 A O ANISOU 311 O LEU A 47 7718 8859 10646 1240 -176 -1436 A O ATOM 312 CB LEU A 47 51.656 -14.407 -21.819 1.00 56.35 A C ANISOU 312 CB LEU A 47 5572 7420 8420 1193 106 -1385 A C ATOM 313 CG LEU A 47 52.596 -13.301 -22.294 1.00 58.76 A C ANISOU 313 CG LEU A 47 5739 7955 8633 1190 247 -1338 A C ATOM 314 CD1 LEU A 47 52.877 -13.424 -23.788 1.00 52.71 A C ANISOU 314 CD1 LEU A 47 4947 7351 7730 1273 359 -1490 A C ATOM 315 CD2 LEU A 47 52.028 -11.926 -21.961 1.00 52.49 A C ANISOU 315 CD2 LEU A 47 4965 7225 7753 1028 276 -1160 A C ATOM 316 N LYS A 48 49.248 -15.474 -19.536 1.00 58.96 A N ANISOU 316 N LYS A 48 6175 7286 8940 971 -193 -1220 A N ATOM 317 CA LYS A 48 48.357 -16.589 -19.252 1.00 59.05 A C ANISOU 317 CA LYS A 48 6320 7101 9017 931 -307 -1271 A C ATOM 318 C LYS A 48 47.215 -16.581 -20.247 1.00 56.51 A C ANISOU 318 C LYS A 48 6055 6845 8571 860 -299 -1347 A C ATOM 319 O LYS A 48 46.416 -15.648 -20.271 1.00 66.32 A O ANISOU 319 O LYS A 48 7281 8197 9722 754 -271 -1252 A O ATOM 320 CB LYS A 48 47.827 -16.502 -17.824 1.00 58.57 A C ANISOU 320 CB LYS A 48 6307 6908 9038 813 -388 -1112 A C ATOM 321 CG LYS A 48 48.928 -16.510 -16.785 1.00 76.38 A C ANISOU 321 CG LYS A 48 8514 9101 11407 876 -415 -1031 A C ATOM 322 CD LYS A 48 48.394 -16.891 -15.418 1.00 95.97 A C ANISOU 322 CD LYS A 48 11089 11398 13976 778 -521 -912 A C ATOM 323 CE LYS A 48 49.493 -16.852 -14.352 1.00101.67 A C ANISOU 323 CE LYS A 48 11764 12068 14797 840 -562 -822 A C ATOM 324 NZ LYS A 48 48.906 -16.967 -12.979 1.00103.23 A N1+ ANISOU 324 NZ LYS A 48 12057 12122 15045 719 -649 -680 A N1+ ATOM 325 N LYS A 49 47.147 -17.615 -21.079 1.00 55.76 A N ANISOU 325 N LYS A 49 6029 6687 8470 927 -327 -1524 A N ATOM 326 CA LYS A 49 46.148 -17.673 -22.136 1.00 65.46 A C ANISOU 326 CA LYS A 49 7309 7995 9569 866 -328 -1618 A C ATOM 327 C LYS A 49 44.783 -18.046 -21.560 1.00 67.66 A C ANISOU 327 C LYS A 49 7673 8157 9876 701 -434 -1567 A C ATOM 328 O LYS A 49 44.719 -18.785 -20.583 1.00 63.13 A O ANISOU 328 O LYS A 49 7170 7385 9434 663 -518 -1530 A O ATOM 329 CB LYS A 49 46.567 -18.690 -23.188 1.00 73.25 A C ANISOU 329 CB LYS A 49 8353 8944 10534 988 -327 -1837 A C ATOM 330 CG LYS A 49 45.911 -18.508 -24.547 1.00 83.16 A C ANISOU 330 CG LYS A 49 9629 10355 11613 963 -293 -1949 A C ATOM 331 CD LYS A 49 46.205 -19.704 -25.442 1.00 95.55 A C ANISOU 331 CD LYS A 49 11294 11841 13172 1070 -313 -2181 A C ATOM 332 CE LYS A 49 45.632 -19.518 -26.838 1.00107.41 A C ANISOU 332 CE LYS A 49 12819 13513 14478 1049 -280 -2301 A C ATOM 333 NZ LYS A 49 46.366 -18.482 -27.621 1.00111.80 A N1+ ANISOU 333 NZ LYS A 49 13264 14320 14894 1132 -134 -2282 A N1+ ATOM 334 N VAL A 50 43.712 -17.499 -22.142 1.00 68.78 A N ANISOU 334 N VAL A 50 7804 8437 9891 603 -430 -1556 A N ATOM 335 CA VAL A 50 42.330 -17.933 -21.864 1.00 72.15 A C ANISOU 335 CA VAL A 50 8291 8798 10324 443 -526 -1544 A C ATOM 336 C VAL A 50 41.815 -18.732 -23.071 1.00 65.18 A C ANISOU 336 C VAL A 50 7479 7926 9359 432 -571 -1736 A C ATOM 337 O VAL A 50 42.543 -18.900 -24.036 1.00 77.24 A O ANISOU 337 O VAL A 50 9016 9508 10826 558 -521 -1868 A O ATOM 338 CB VAL A 50 41.413 -16.741 -21.580 1.00 66.23 A C ANISOU 338 CB VAL A 50 7463 8208 9493 345 -502 -1392 A C ATOM 339 CG1 VAL A 50 40.035 -17.220 -21.132 1.00 58.84 A C ANISOU 339 CG1 VAL A 50 6560 7218 8580 176 -596 -1371 A C ATOM 340 CG2 VAL A 50 42.042 -15.854 -20.533 1.00 58.13 A C ANISOU 340 CG2 VAL A 50 6379 7183 8524 368 -445 -1223 A C ATOM 341 N GLU A 55 34.243 -21.482 -23.167 1.00114.74 A N ANISOU 341 N GLU A 55 13847 14217 15532 -647 -1114 -1890 A N ATOM 342 CA GLU A 55 33.913 -22.704 -23.898 1.00107.99 A C ANISOU 342 CA GLU A 55 13120 13247 14665 -751 -1215 -2084 A C ATOM 343 C GLU A 55 32.520 -22.752 -24.538 1.00 94.71 A C ANISOU 343 C GLU A 55 11357 11753 12874 -934 -1302 -2144 A C ATOM 344 O GLU A 55 32.324 -22.308 -25.673 1.00 91.60 A O ANISOU 344 O GLU A 55 10910 11564 12332 -869 -1309 -2229 A O ATOM 345 CB GLU A 55 34.071 -23.878 -22.930 1.00112.24 A C ANISOU 345 CB GLU A 55 13814 13467 15365 -864 -1270 -2079 A C ATOM 346 CG GLU A 55 35.163 -23.640 -21.861 1.00111.05 A C ANISOU 346 CG GLU A 55 13690 13169 15336 -725 -1197 -1943 A C ATOM 347 CD GLU A 55 34.820 -22.550 -20.827 1.00 97.45 A C ANISOU 347 CD GLU A 55 11815 11586 13627 -756 -1132 -1722 A C ATOM 348 OE1 GLU A 55 33.649 -22.123 -20.728 1.00 96.90 A O ANISOU 348 OE1 GLU A 55 11626 11691 13499 -903 -1148 -1661 A O ATOM 349 OE2 GLU A 55 35.734 -22.124 -20.095 1.00 88.45 A O1- ANISOU 349 OE2 GLU A 55 10673 10381 12554 -629 -1067 -1614 A O1- ATOM 350 N LYS A 56 31.558 -23.304 -23.805 1.00 86.51 A N ANISOU 350 N LYS A 56 10311 10654 11906 -1169 -1373 -2097 A N ATOM 351 CA LYS A 56 30.210 -23.509 -24.332 1.00 88.06 A C ANISOU 351 CA LYS A 56 10422 11021 12017 -1374 -1470 -2163 A C ATOM 352 C LYS A 56 29.295 -22.296 -24.128 1.00 71.63 A C ANISOU 352 C LYS A 56 8099 9256 9861 -1388 -1438 -2016 A C ATOM 353 O LYS A 56 28.183 -22.241 -24.641 1.00 73.81 A O ANISOU 353 O LYS A 56 8257 9740 10048 -1518 -1514 -2058 A O ATOM 354 CB LYS A 56 29.578 -24.753 -23.695 1.00 96.37 A C ANISOU 354 CB LYS A 56 11580 11862 13175 -1649 -1562 -2193 A C ATOM 355 CG LYS A 56 30.190 -26.085 -24.138 1.00100.23 A C ANISOU 355 CG LYS A 56 12326 12044 13712 -1667 -1630 -2379 A C ATOM 356 CD LYS A 56 29.293 -27.248 -23.731 1.00104.59 A C ANISOU 356 CD LYS A 56 12976 12432 14332 -1986 -1740 -2421 A C ATOM 357 CE LYS A 56 29.517 -28.461 -24.614 1.00108.68 A C ANISOU 357 CE LYS A 56 13728 12731 14834 -2035 -1838 -2657 A C ATOM 358 NZ LYS A 56 28.268 -29.262 -24.764 1.00108.31 A N1+ ANISOU 358 NZ LYS A 56 13699 12686 14768 -2378 -1964 -2735 A N1+ ATOM 359 N GLU A 57 29.767 -21.325 -23.371 1.00 59.49 A N ANISOU 359 N GLU A 57 6489 7756 8359 -1247 -1331 -1848 A N ATOM 360 CA GLU A 57 28.948 -20.180 -23.045 1.00 56.26 A C ANISOU 360 CA GLU A 57 5872 7611 7891 -1239 -1293 -1704 A C ATOM 361 C GLU A 57 29.724 -18.899 -23.313 1.00 53.32 A C ANISOU 361 C GLU A 57 5458 7353 7449 -981 -1191 -1624 A C ATOM 362 O GLU A 57 29.783 -18.016 -22.463 1.00 51.92 A O ANISOU 362 O GLU A 57 5204 7220 7301 -915 -1111 -1463 A O ATOM 363 CB GLU A 57 28.517 -20.264 -21.581 1.00 47.59 A C ANISOU 363 CB GLU A 57 4731 6439 6912 -1379 -1263 -1554 A C ATOM 364 CG GLU A 57 27.575 -21.421 -21.295 1.00 61.14 A C ANISOU 364 CG GLU A 57 6467 8083 8682 -1671 -1359 -1610 A C ATOM 365 CD GLU A 57 26.213 -21.249 -21.972 1.00 73.72 A C ANISOU 365 CD GLU A 57 7873 9969 10166 -1801 -1437 -1661 A C ATOM 366 OE1 GLU A 57 25.706 -20.103 -22.027 1.00 68.01 A O ANISOU 366 OE1 GLU A 57 6961 9517 9364 -1698 -1396 -1571 A O ATOM 367 OE2 GLU A 57 25.651 -22.261 -22.450 1.00 81.92 A O1- ANISOU 367 OE2 GLU A 57 8959 10967 11198 -2006 -1545 -1794 A O1- ATOM 368 N GLY A 58 30.331 -18.807 -24.492 1.00 52.24 A N ANISOU 368 N GLY A 58 5383 7255 7211 -843 -1191 -1738 A N ATOM 369 CA GLY A 58 31.170 -17.666 -24.814 1.00 50.78 A C ANISOU 369 CA GLY A 58 5181 7159 6954 -617 -1090 -1668 A C ATOM 370 C GLY A 58 32.355 -17.506 -23.871 1.00 52.06 A C ANISOU 370 C GLY A 58 5415 7128 7238 -520 -991 -1573 A C ATOM 371 O GLY A 58 32.876 -18.489 -23.328 1.00 54.13 A O ANISOU 371 O GLY A 58 5789 7152 7625 -574 -1008 -1616 A O ATOM 372 N PHE A 59 32.773 -16.259 -23.670 1.00 49.72 A N ANISOU 372 N PHE A 59 5058 6931 6901 -377 -897 -1442 A N ATOM 373 CA PHE A 59 33.896 -15.957 -22.797 1.00 45.22 A C ANISOU 373 CA PHE A 59 4537 6213 6431 -287 -807 -1345 A C ATOM 374 C PHE A 59 33.649 -16.439 -21.368 1.00 51.33 A C ANISOU 374 C PHE A 59 5323 6829 7353 -414 -822 -1254 A C ATOM 375 O PHE A 59 32.670 -16.062 -20.752 1.00 58.91 A O ANISOU 375 O PHE A 59 6190 7883 8312 -504 -830 -1159 A O ATOM 376 CB PHE A 59 34.213 -14.459 -22.806 1.00 45.03 A C ANISOU 376 CB PHE A 59 4449 6333 6326 -146 -712 -1213 A C ATOM 377 CG PHE A 59 35.557 -14.140 -22.226 1.00 54.50 A C ANISOU 377 CG PHE A 59 5702 7404 7600 -44 -622 -1147 A C ATOM 378 CD1 PHE A 59 36.689 -14.113 -23.035 1.00 55.58 A C ANISOU 378 CD1 PHE A 59 5890 7533 7694 78 -570 -1223 A C ATOM 379 CD2 PHE A 59 35.705 -13.910 -20.871 1.00 52.36 A C ANISOU 379 CD2 PHE A 59 5425 7030 7439 -79 -592 -1015 A C ATOM 380 CE1 PHE A 59 37.947 -13.848 -22.507 1.00 49.41 A C ANISOU 380 CE1 PHE A 59 5136 6654 6985 163 -492 -1167 A C ATOM 381 CE2 PHE A 59 36.960 -13.642 -20.334 1.00 54.07 A C ANISOU 381 CE2 PHE A 59 5684 7139 7723 6 -524 -959 A C ATOM 382 CZ PHE A 59 38.085 -13.615 -21.158 1.00 45.80 A C ANISOU 382 CZ PHE A 59 4669 6093 6639 125 -476 -1036 A C ATOM 383 N PRO A 60 34.549 -17.274 -20.837 1.00 60.98 A N ANISOU 383 N PRO A 60 6658 7814 8696 -412 -823 -1282 A N ATOM 384 CA PRO A 60 34.385 -17.913 -19.523 1.00 56.85 A C ANISOU 384 CA PRO A 60 6182 7110 8308 -540 -850 -1205 A C ATOM 385 C PRO A 60 34.084 -16.921 -18.396 1.00 55.85 A C ANISOU 385 C PRO A 60 5969 7057 8194 -552 -787 -1019 A C ATOM 386 O PRO A 60 34.867 -16.001 -18.091 1.00 51.46 A O ANISOU 386 O PRO A 60 5398 6522 7632 -420 -708 -930 A O ATOM 387 CB PRO A 60 35.747 -18.587 -19.285 1.00 52.29 A C ANISOU 387 CB PRO A 60 5735 6300 7833 -444 -842 -1247 A C ATOM 388 CG PRO A 60 36.301 -18.775 -20.646 1.00 54.87 A C ANISOU 388 CG PRO A 60 6093 6670 8084 -325 -840 -1407 A C ATOM 389 CD PRO A 60 35.856 -17.585 -21.437 1.00 56.89 A C ANISOU 389 CD PRO A 60 6230 7197 8190 -266 -792 -1380 A C ATOM 390 N ILE A 61 32.942 -17.144 -17.759 1.00 52.19 A N ANISOU 390 N ILE A 61 5452 6629 7747 -721 -820 -966 A N ATOM 391 CA ILE A 61 32.475 -16.301 -16.671 1.00 41.47 A C ANISOU 391 CA ILE A 61 4013 5352 6393 -746 -761 -806 A C ATOM 392 C ILE A 61 33.480 -16.300 -15.526 1.00 50.16 A C ANISOU 392 C ILE A 61 5206 6263 7590 -707 -719 -707 A C ATOM 393 O ILE A 61 33.616 -15.322 -14.788 1.00 59.40 A O ANISOU 393 O ILE A 61 6336 7488 8746 -649 -649 -583 A O ATOM 394 CB ILE A 61 31.048 -16.716 -16.223 1.00 57.85 A C ANISOU 394 CB ILE A 61 6004 7508 8468 -953 -802 -785 A C ATOM 395 CG1 ILE A 61 30.510 -15.786 -15.138 1.00 52.46 A C ANISOU 395 CG1 ILE A 61 5225 6935 7772 -962 -726 -629 A C ATOM 396 CG2 ILE A 61 30.975 -18.225 -15.822 1.00 37.73 A C ANISOU 396 CG2 ILE A 61 3579 4737 6022 -1144 -879 -838 A C ATOM 397 CD1 ILE A 61 29.031 -15.976 -14.919 1.00 46.73 A C ANISOU 397 CD1 ILE A 61 4365 6371 7019 -1136 -750 -618 A C ATOM 398 N THR A 62 34.216 -17.391 -15.409 1.00 56.85 A N ANISOU 398 N THR A 62 6185 6885 8529 -728 -770 -767 A N ATOM 399 CA THR A 62 35.244 -17.516 -14.385 1.00 54.91 A C ANISOU 399 CA THR A 62 6031 6455 8376 -680 -753 -682 A C ATOM 400 C THR A 62 36.419 -16.592 -14.667 1.00 55.21 A C ANISOU 400 C THR A 62 6049 6538 8391 -480 -686 -664 A C ATOM 401 O THR A 62 36.977 -15.979 -13.747 1.00 54.86 A O ANISOU 401 O THR A 62 6008 6465 8372 -437 -641 -547 A O ATOM 402 CB THR A 62 35.701 -18.984 -14.255 1.00 62.32 A C ANISOU 402 CB THR A 62 7125 7133 9420 -735 -838 -757 A C ATOM 403 CG2 THR A 62 37.143 -19.076 -13.884 1.00 75.29 A C ANISOU 403 CG2 THR A 62 8848 8621 11139 -584 -830 -737 A C ATOM 404 OG1 THR A 62 34.939 -19.604 -13.217 1.00 66.43 A O ANISOU 404 OG1 THR A 62 7695 7556 9990 -932 -874 -677 A O ATOM 405 N ALA A 63 36.788 -16.479 -15.940 1.00 48.05 A N ANISOU 405 N ALA A 63 5122 5711 7425 -372 -677 -780 A N ATOM 406 CA ALA A 63 37.846 -15.550 -16.328 1.00 50.48 A C ANISOU 406 CA ALA A 63 5398 6091 7692 -203 -603 -763 A C ATOM 407 C ALA A 63 37.399 -14.086 -16.174 1.00 56.20 A C ANISOU 407 C ALA A 63 6031 7001 8322 -177 -529 -649 A C ATOM 408 O ALA A 63 38.180 -13.240 -15.742 1.00 52.10 A O ANISOU 408 O ALA A 63 5506 6488 7802 -98 -467 -563 A O ATOM 409 CB ALA A 63 38.329 -15.835 -17.750 1.00 48.29 A C ANISOU 409 CB ALA A 63 5130 5860 7360 -103 -603 -918 A C ATOM 410 N LEU A 64 36.142 -13.790 -16.509 1.00 57.96 A N ANISOU 410 N LEU A 64 6184 7373 8466 -241 -540 -648 A N ATOM 411 CA LEU A 64 35.619 -12.440 -16.302 1.00 51.64 A C ANISOU 411 CA LEU A 64 5307 6734 7580 -201 -477 -539 A C ATOM 412 C LEU A 64 35.730 -12.063 -14.848 1.00 49.79 A C ANISOU 412 C LEU A 64 5091 6421 7404 -239 -441 -405 A C ATOM 413 O LEU A 64 36.119 -10.952 -14.520 1.00 55.28 A O ANISOU 413 O LEU A 64 5783 7159 8062 -160 -375 -317 A O ATOM 414 CB LEU A 64 34.156 -12.320 -16.724 1.00 47.26 A C ANISOU 414 CB LEU A 64 4659 6351 6947 -265 -508 -557 A C ATOM 415 CG LEU A 64 33.916 -12.415 -18.226 1.00 51.66 A C ANISOU 415 CG LEU A 64 5189 7034 7407 -216 -545 -677 A C ATOM 416 CD1 LEU A 64 32.439 -12.539 -18.502 1.00 56.11 A C ANISOU 416 CD1 LEU A 64 5649 7757 7914 -308 -602 -701 A C ATOM 417 CD2 LEU A 64 34.531 -11.235 -18.976 1.00 39.16 A C ANISOU 417 CD2 LEU A 64 3606 5556 5719 -55 -478 -648 A C ATOM 418 N ARG A 65 35.386 -12.992 -13.969 1.00 46.53 A N ANISOU 418 N ARG A 65 4713 5888 7077 -369 -487 -390 A N ATOM 419 CA ARG A 65 35.422 -12.707 -12.540 1.00 48.63 A C ANISOU 419 CA ARG A 65 5008 6086 7386 -419 -457 -262 A C ATOM 420 C ARG A 65 36.842 -12.373 -12.086 1.00 51.38 A C ANISOU 420 C ARG A 65 5424 6320 7778 -326 -431 -215 A C ATOM 421 O ARG A 65 37.057 -11.386 -11.376 1.00 53.32 A O ANISOU 421 O ARG A 65 5670 6594 7994 -291 -374 -115 A O ATOM 422 CB ARG A 65 34.855 -13.880 -11.755 1.00 46.57 A C ANISOU 422 CB ARG A 65 4789 5705 7199 -588 -514 -254 A C ATOM 423 CG ARG A 65 34.662 -13.639 -10.289 1.00 58.98 A C ANISOU 423 CG ARG A 65 6387 7232 8790 -663 -481 -123 A C ATOM 424 CD ARG A 65 34.256 -14.946 -9.655 1.00 66.42 A C ANISOU 424 CD ARG A 65 7400 8033 9806 -838 -544 -120 A C ATOM 425 NE ARG A 65 35.167 -15.999 -10.094 1.00 85.64 A N ANISOU 425 NE ARG A 65 9941 10277 12324 -811 -621 -204 A N ATOM 426 CZ ARG A 65 35.173 -17.242 -9.625 1.00 93.20 A C ANISOU 426 CZ ARG A 65 11010 11042 13359 -930 -693 -209 A C ATOM 427 NH1 ARG A 65 34.299 -17.608 -8.692 1.00 92.09 A N1+ ANISOU 427 NH1 ARG A 65 10887 10883 13220 -1110 -693 -128 A N1+ ATOM 428 NH2 ARG A 65 36.059 -18.116 -10.092 1.00 93.92 A N ANISOU 428 NH2 ARG A 65 11202 10958 13523 -866 -760 -294 A N ATOM 429 N GLU A 66 37.807 -13.181 -12.523 1.00 47.74 A N ANISOU 429 N GLU A 66 5018 5739 7383 -281 -474 -296 A N ATOM 430 CA GLU A 66 39.202 -12.981 -12.146 1.00 49.78 A C ANISOU 430 CA GLU A 66 5316 5906 7691 -192 -460 -263 A C ATOM 431 C GLU A 66 39.717 -11.631 -12.639 1.00 52.31 A C ANISOU 431 C GLU A 66 5586 6362 7929 -86 -379 -234 A C ATOM 432 O GLU A 66 40.315 -10.864 -11.880 1.00 50.64 A O ANISOU 432 O GLU A 66 5387 6136 7718 -66 -342 -141 A O ATOM 433 CB GLU A 66 40.072 -14.101 -12.704 1.00 53.94 A C ANISOU 433 CB GLU A 66 5891 6308 8297 -136 -517 -375 A C ATOM 434 CG GLU A 66 41.550 -13.960 -12.373 1.00 62.82 A C ANISOU 434 CG GLU A 66 7027 7362 9479 -32 -508 -352 A C ATOM 435 CD GLU A 66 42.386 -15.092 -12.951 1.00 74.95 A C ANISOU 435 CD GLU A 66 8601 8783 11093 51 -561 -474 A C ATOM 436 OE1 GLU A 66 41.809 -15.970 -13.628 1.00 79.36 A O ANISOU 436 OE1 GLU A 66 9197 9301 11656 21 -604 -581 A O ATOM 437 OE2 GLU A 66 43.621 -15.106 -12.737 1.00 73.52 A O1- ANISOU 437 OE2 GLU A 66 8409 8556 10967 150 -562 -469 A O1- ATOM 438 N ILE A 67 39.474 -11.349 -13.916 1.00 45.00 A N ANISOU 438 N ILE A 67 4613 5561 6922 -29 -354 -313 A N ATOM 439 CA ILE A 67 39.837 -10.073 -14.500 1.00 49.40 A C ANISOU 439 CA ILE A 67 5139 6246 7383 59 -277 -281 A C ATOM 440 C ILE A 67 39.231 -8.914 -13.703 1.00 51.53 A C ANISOU 440 C ILE A 67 5408 6572 7598 38 -231 -155 A C ATOM 441 O ILE A 67 39.920 -7.943 -13.375 1.00 44.36 A O ANISOU 441 O ILE A 67 4522 5667 6666 76 -177 -82 A O ATOM 442 CB ILE A 67 39.386 -9.994 -15.975 1.00 48.60 A C ANISOU 442 CB ILE A 67 5002 6282 7183 109 -269 -375 A C ATOM 443 CG1 ILE A 67 40.171 -11.001 -16.811 1.00 48.48 A C ANISOU 443 CG1 ILE A 67 5000 6215 7206 153 -297 -509 A C ATOM 444 CG2 ILE A 67 39.561 -8.582 -16.526 1.00 38.49 A C ANISOU 444 CG2 ILE A 67 3709 5132 5785 186 -191 -316 A C ATOM 445 CD1 ILE A 67 39.667 -11.134 -18.238 1.00 51.87 A C ANISOU 445 CD1 ILE A 67 5408 6769 7531 186 -303 -620 A C ATOM 446 N LYS A 68 37.946 -9.020 -13.374 1.00 45.10 A N ANISOU 446 N LYS A 68 4568 5804 6765 -27 -250 -135 A N ATOM 447 CA LYS A 68 37.278 -7.947 -12.636 1.00 47.95 A C ANISOU 447 CA LYS A 68 4924 6227 7068 -28 -201 -30 A C ATOM 448 C LYS A 68 38.002 -7.722 -11.309 1.00 47.11 A C ANISOU 448 C LYS A 68 4883 6000 7018 -61 -184 59 A C ATOM 449 O LYS A 68 38.285 -6.591 -10.934 1.00 46.91 A O ANISOU 449 O LYS A 68 4891 5991 6941 -19 -129 133 A O ATOM 450 CB LYS A 68 35.795 -8.264 -12.406 1.00 41.00 A C ANISOU 450 CB LYS A 68 3981 5427 6169 -99 -223 -30 A C ATOM 451 CG LYS A 68 35.105 -7.366 -11.388 1.00 49.59 A C ANISOU 451 CG LYS A 68 5064 6563 7216 -103 -169 72 A C ATOM 452 CD LYS A 68 33.791 -7.970 -10.875 1.00 58.74 A C ANISOU 452 CD LYS A 68 6149 7784 8385 -209 -189 73 A C ATOM 453 CE LYS A 68 34.050 -9.212 -10.016 1.00 62.07 A C ANISOU 453 CE LYS A 68 6621 8052 8909 -351 -235 75 A C ATOM 454 NZ LYS A 68 32.822 -9.761 -9.374 1.00 60.85 A N1+ ANISOU 454 NZ LYS A 68 6405 7955 8760 -484 -240 93 A N1+ ATOM 455 N ILE A 69 38.328 -8.815 -10.626 1.00 43.83 A N ANISOU 455 N ILE A 69 4499 5454 6701 -137 -240 51 A N ATOM 456 CA ILE A 69 39.046 -8.754 -9.354 1.00 41.50 A C ANISOU 456 CA ILE A 69 4269 5042 6456 -172 -245 133 A C ATOM 457 C ILE A 69 40.494 -8.231 -9.464 1.00 46.43 A C ANISOU 457 C ILE A 69 4916 5632 7095 -102 -230 143 A C ATOM 458 O ILE A 69 40.913 -7.381 -8.672 1.00 45.94 A O ANISOU 458 O ILE A 69 4893 5552 7009 -106 -199 225 A O ATOM 459 CB ILE A 69 38.964 -10.092 -8.615 1.00 46.05 A C ANISOU 459 CB ILE A 69 4887 5484 7126 -270 -319 131 A C ATOM 460 CG1 ILE A 69 37.501 -10.327 -8.173 1.00 37.54 A C ANISOU 460 CG1 ILE A 69 3785 4460 6017 -375 -312 156 A C ATOM 461 CG2 ILE A 69 39.885 -10.079 -7.410 1.00 39.58 A C ANISOU 461 CG2 ILE A 69 4141 4545 6354 -289 -342 212 A C ATOM 462 CD1 ILE A 69 37.135 -11.760 -7.910 1.00 35.40 A C ANISOU 462 CD1 ILE A 69 3549 4081 5822 -491 -385 127 A C ATOM 463 N LEU A 70 41.247 -8.719 -10.448 1.00 50.83 A N ANISOU 463 N LEU A 70 5442 6187 7684 -42 -247 57 A N ATOM 464 CA LEU A 70 42.592 -8.197 -10.720 1.00 43.34 A C ANISOU 464 CA LEU A 70 4482 5246 6740 22 -219 57 A C ATOM 465 C LEU A 70 42.561 -6.689 -11.032 1.00 48.27 A C ANISOU 465 C LEU A 70 5111 5975 7255 50 -136 112 A C ATOM 466 O LEU A 70 43.439 -5.945 -10.620 1.00 46.36 A O ANISOU 466 O LEU A 70 4888 5720 7005 47 -108 167 A O ATOM 467 CB LEU A 70 43.229 -8.951 -11.888 1.00 48.09 A C ANISOU 467 CB LEU A 70 5037 5862 7372 92 -233 -61 A C ATOM 468 CG LEU A 70 44.168 -10.150 -11.644 1.00 58.22 A C ANISOU 468 CG LEU A 70 6321 7024 8775 120 -303 -114 A C ATOM 469 CD1 LEU A 70 44.191 -10.612 -10.206 1.00 52.26 A C ANISOU 469 CD1 LEU A 70 5626 6134 8096 55 -371 -33 A C ATOM 470 CD2 LEU A 70 43.814 -11.310 -12.580 1.00 41.61 A C ANISOU 470 CD2 LEU A 70 4216 4896 6698 151 -342 -244 A C ATOM 471 N GLN A 71 41.545 -6.228 -11.753 1.00 48.62 A N ANISOU 471 N GLN A 71 5143 6119 7211 75 -101 99 A N ATOM 472 CA GLN A 71 41.459 -4.805 -12.056 1.00 48.55 A C ANISOU 472 CA GLN A 71 5165 6188 7095 114 -29 157 A C ATOM 473 C GLN A 71 41.147 -3.944 -10.832 1.00 49.83 A C ANISOU 473 C GLN A 71 5394 6306 7232 79 -6 259 A C ATOM 474 O GLN A 71 41.518 -2.776 -10.784 1.00 45.04 A O ANISOU 474 O GLN A 71 4844 5707 6561 96 46 316 A O ATOM 475 CB GLN A 71 40.419 -4.557 -13.132 1.00 37.08 A C ANISOU 475 CB GLN A 71 3684 4855 5549 169 -13 121 A C ATOM 476 CG GLN A 71 40.889 -4.938 -14.521 1.00 44.83 A C ANISOU 476 CG GLN A 71 4627 5903 6504 218 -10 29 A C ATOM 477 CD GLN A 71 39.723 -5.059 -15.475 1.00 55.74 A C ANISOU 477 CD GLN A 71 5974 7398 7807 255 -29 -22 A C ATOM 478 NE2 GLN A 71 38.508 -5.139 -14.928 1.00 61.29 A N ANISOU 478 NE2 GLN A 71 6655 8121 8510 229 -58 3 A N ATOM 479 OE1 GLN A 71 39.906 -5.091 -16.684 1.00 59.41 A O ANISOU 479 OE1 GLN A 71 6423 7944 8206 304 -18 -84 A O ATOM 480 N LEU A 72 40.454 -4.529 -9.858 1.00 43.14 A N ANISOU 480 N LEU A 72 4551 5411 6430 23 -42 278 A N ATOM 481 CA LEU A 72 40.106 -3.839 -8.629 1.00 39.36 A C ANISOU 481 CA LEU A 72 4138 4894 5923 -11 -17 363 A C ATOM 482 C LEU A 72 41.301 -3.734 -7.687 1.00 45.91 A C ANISOU 482 C LEU A 72 5025 5621 6799 -63 -37 410 A C ATOM 483 O LEU A 72 41.533 -2.674 -7.103 1.00 46.17 A O ANISOU 483 O LEU A 72 5133 5633 6776 -70 2 471 A O ATOM 484 CB LEU A 72 38.964 -4.573 -7.912 1.00 44.70 A C ANISOU 484 CB LEU A 72 4791 5571 6621 -68 -41 368 A C ATOM 485 CG LEU A 72 38.608 -4.006 -6.528 1.00 48.83 A C ANISOU 485 CG LEU A 72 5385 6059 7111 -110 -10 449 A C ATOM 486 CD1 LEU A 72 37.984 -2.592 -6.637 1.00 35.55 A C ANISOU 486 CD1 LEU A 72 3738 4452 5319 -26 67 483 A C ATOM 487 CD2 LEU A 72 37.678 -4.944 -5.779 1.00 42.13 A C ANISOU 487 CD2 LEU A 72 4508 5208 6293 -195 -34 456 A C ATOM 488 N LEU A 73 42.052 -4.833 -7.549 1.00 39.18 A N ANISOU 488 N LEU A 73 4142 4702 6045 -93 -103 377 A N ATOM 489 CA LEU A 73 43.111 -4.942 -6.550 1.00 45.22 A C ANISOU 489 CA LEU A 73 4944 5375 6862 -141 -147 422 A C ATOM 490 C LEU A 73 44.458 -4.347 -6.998 1.00 50.58 A C ANISOU 490 C LEU A 73 5601 6074 7543 -118 -132 417 A C ATOM 491 O LEU A 73 45.153 -4.930 -7.826 1.00 52.54 A O ANISOU 491 O LEU A 73 5774 6345 7843 -75 -148 352 A O ATOM 492 CB LEU A 73 43.288 -6.406 -6.149 1.00 46.94 A C ANISOU 492 CB LEU A 73 5146 5505 7184 -169 -234 398 A C ATOM 493 CG LEU A 73 42.020 -7.060 -5.601 1.00 47.59 A C ANISOU 493 CG LEU A 73 5254 5563 7265 -229 -249 414 A C ATOM 494 CD1 LEU A 73 42.263 -8.525 -5.160 1.00 37.98 A C ANISOU 494 CD1 LEU A 73 4055 4227 6150 -270 -343 402 A C ATOM 495 CD2 LEU A 73 41.469 -6.214 -4.454 1.00 36.28 A C ANISOU 495 CD2 LEU A 73 3893 4134 5757 -280 -208 500 A C ATOM 496 N LYS A 74 44.822 -3.192 -6.450 1.00 44.35 A N ANISOU 496 N LYS A 74 4878 5280 6695 -153 -98 480 A N ATOM 497 CA LYS A 74 46.129 -2.588 -6.746 1.00 47.45 A C ANISOU 497 CA LYS A 74 5247 5695 7086 -167 -84 485 A C ATOM 498 C LYS A 74 46.926 -2.325 -5.475 1.00 47.99 A C ANISOU 498 C LYS A 74 5362 5699 7173 -246 -135 545 A C ATOM 499 O LYS A 74 46.651 -1.379 -4.747 1.00 55.50 A O ANISOU 499 O LYS A 74 6418 6618 8051 -295 -109 601 A O ATOM 500 CB LYS A 74 45.974 -1.302 -7.549 1.00 39.49 A C ANISOU 500 CB LYS A 74 4282 4748 5974 -151 6 499 A C ATOM 501 CG LYS A 74 45.209 -1.509 -8.841 1.00 52.29 A C ANISOU 501 CG LYS A 74 5859 6447 7560 -70 46 444 A C ATOM 502 CD LYS A 74 45.806 -2.675 -9.616 1.00 59.82 A C ANISOU 502 CD LYS A 74 6698 7437 8595 -33 12 360 A C ATOM 503 CE LYS A 74 45.041 -2.955 -10.896 1.00 60.82 A C ANISOU 503 CE LYS A 74 6789 7644 8678 39 41 294 A C ATOM 504 NZ LYS A 74 45.897 -3.716 -11.839 1.00 54.71 A N1+ ANISOU 504 NZ LYS A 74 5921 6918 7948 80 38 208 A N1+ ATOM 505 N HIS A 75 47.927 -3.160 -5.220 1.00 43.97 A N ANISOU 505 N HIS A 75 4778 5172 6757 -250 -211 528 A N ATOM 506 CA HIS A 75 48.615 -3.121 -3.944 1.00 44.06 A C ANISOU 506 CA HIS A 75 4826 5126 6789 -320 -286 585 A C ATOM 507 C HIS A 75 49.993 -3.794 -4.043 1.00 55.62 A C ANISOU 507 C HIS A 75 6168 6614 8350 -298 -359 556 A C ATOM 508 O HIS A 75 50.161 -4.752 -4.806 1.00 58.25 A O ANISOU 508 O HIS A 75 6409 6965 8756 -213 -374 490 A O ATOM 509 CB HIS A 75 47.729 -3.792 -2.897 1.00 37.47 A C ANISOU 509 CB HIS A 75 4072 4204 5960 -339 -336 622 A C ATOM 510 CG HIS A 75 48.294 -3.758 -1.517 1.00 52.09 A C ANISOU 510 CG HIS A 75 5986 5995 7809 -412 -417 687 A C ATOM 511 CD2 HIS A 75 48.119 -2.878 -0.503 1.00 50.92 A C ANISOU 511 CD2 HIS A 75 5955 5818 7573 -490 -408 746 A C ATOM 512 ND1 HIS A 75 49.162 -4.722 -1.048 1.00 54.19 A N ANISOU 512 ND1 HIS A 75 6202 6224 8165 -400 -530 694 A N ATOM 513 CE1 HIS A 75 49.498 -4.434 0.198 1.00 58.09 A C ANISOU 513 CE1 HIS A 75 6774 6676 8621 -476 -592 760 A C ATOM 514 NE2 HIS A 75 48.879 -3.321 0.553 1.00 60.83 A N ANISOU 514 NE2 HIS A 75 7226 7027 8858 -537 -517 788 A N ATOM 515 N GLU A 76 50.978 -3.288 -3.293 1.00 46.98 A N ANISOU 515 N GLU A 76 5070 5527 7252 -369 -406 600 A N ATOM 516 CA GLU A 76 52.342 -3.808 -3.388 1.00 52.69 A C ANISOU 516 CA GLU A 76 5651 6305 8064 -342 -475 574 A C ATOM 517 C GLU A 76 52.433 -5.324 -3.172 1.00 49.95 A C ANISOU 517 C GLU A 76 5258 5896 7826 -245 -575 547 A C ATOM 518 O GLU A 76 53.301 -5.978 -3.736 1.00 52.62 A O ANISOU 518 O GLU A 76 5461 6285 8246 -160 -605 490 A O ATOM 519 CB GLU A 76 53.284 -3.082 -2.419 1.00 65.71 A C ANISOU 519 CB GLU A 76 7307 7971 9688 -450 -534 632 A C ATOM 520 CG GLU A 76 54.182 -2.051 -3.080 1.00 91.01 A C ANISOU 520 CG GLU A 76 10432 11290 12858 -519 -467 620 A C ATOM 521 CD GLU A 76 55.550 -2.606 -3.457 1.00108.04 A C ANISOU 521 CD GLU A 76 12382 13560 15108 -476 -515 577 A C ATOM 522 OE1 GLU A 76 56.285 -3.048 -2.546 1.00114.20 A O ANISOU 522 OE1 GLU A 76 13110 14337 15943 -483 -637 602 A O ATOM 523 OE2 GLU A 76 55.901 -2.584 -4.660 1.00111.39 A O1- ANISOU 523 OE2 GLU A 76 12692 14087 15545 -432 -430 518 A O1- ATOM 524 N ASN A 77 51.537 -5.871 -2.357 1.00 41.34 A N ANISOU 524 N ASN A 77 4285 4693 6730 -257 -623 588 A N ATOM 525 CA ASN A 77 51.554 -7.300 -2.045 1.00 46.58 A C ANISOU 525 CA ASN A 77 4945 5264 7488 -182 -726 578 A C ATOM 526 C ASN A 77 50.465 -8.107 -2.749 1.00 51.56 A C ANISOU 526 C ASN A 77 5610 5841 8139 -130 -687 525 A C ATOM 527 O ASN A 77 50.102 -9.196 -2.317 1.00 54.71 A O ANISOU 527 O ASN A 77 6067 6128 8591 -109 -762 535 A O ATOM 528 CB ASN A 77 51.519 -7.517 -0.528 1.00 47.47 A C ANISOU 528 CB ASN A 77 5169 5284 7585 -248 -830 672 A C ATOM 529 CG ASN A 77 52.622 -6.742 0.183 1.00 55.30 A C ANISOU 529 CG ASN A 77 6126 6334 8550 -309 -885 719 A C ATOM 530 ND2 ASN A 77 53.867 -7.028 -0.175 1.00 53.37 A N ANISOU 530 ND2 ASN A 77 5730 6161 8387 -241 -941 682 A N ATOM 531 OD1 ASN A 77 52.355 -5.870 1.005 1.00 56.39 A O ANISOU 531 OD1 ASN A 77 6367 6465 8594 -417 -873 778 A O ATOM 532 N VAL A 78 49.952 -7.564 -3.845 1.00 47.60 A N ANISOU 532 N VAL A 78 5077 5418 7591 -118 -576 470 A N ATOM 533 CA VAL A 78 49.025 -8.295 -4.684 1.00 40.84 A C ANISOU 533 CA VAL A 78 4228 4539 6751 -70 -545 403 A C ATOM 534 C VAL A 78 49.537 -8.267 -6.105 1.00 44.15 A C ANISOU 534 C VAL A 78 4533 5058 7184 15 -484 305 A C ATOM 535 O VAL A 78 50.018 -7.238 -6.583 1.00 47.28 A O ANISOU 535 O VAL A 78 4878 5563 7524 0 -411 306 A O ATOM 536 CB VAL A 78 47.615 -7.698 -4.618 1.00 43.01 A C ANISOU 536 CB VAL A 78 4587 4824 6931 -137 -471 434 A C ATOM 537 CG1 VAL A 78 46.698 -8.408 -5.597 1.00 40.06 A C ANISOU 537 CG1 VAL A 78 4197 4454 6570 -97 -445 356 A C ATOM 538 CG2 VAL A 78 47.076 -7.817 -3.195 1.00 44.69 A C ANISOU 538 CG2 VAL A 78 4910 4947 7122 -222 -520 525 A C ATOM 539 N VAL A 79 49.471 -9.413 -6.767 1.00 47.67 A N ANISOU 539 N VAL A 79 4951 5462 7698 100 -514 219 A N ATOM 540 CA VAL A 79 49.986 -9.535 -8.122 1.00 48.67 A C ANISOU 540 CA VAL A 79 4975 5685 7834 193 -457 111 A C ATOM 541 C VAL A 79 49.308 -8.491 -8.987 1.00 51.65 A C ANISOU 541 C VAL A 79 5354 6173 8096 155 -342 104 A C ATOM 542 O VAL A 79 48.145 -8.130 -8.764 1.00 52.53 A O ANISOU 542 O VAL A 79 5548 6264 8145 93 -320 147 A O ATOM 543 CB VAL A 79 49.775 -10.961 -8.687 1.00 55.66 A C ANISOU 543 CB VAL A 79 5868 6484 8796 285 -508 9 A C ATOM 544 CG1 VAL A 79 48.340 -11.162 -9.132 1.00 48.79 A C ANISOU 544 CG1 VAL A 79 5075 5588 7874 236 -480 -17 A C ATOM 545 CG2 VAL A 79 50.730 -11.233 -9.817 1.00 62.55 A C ANISOU 545 CG2 VAL A 79 6623 7447 9696 406 -470 -104 A C ATOM 546 N ASN A 80 50.059 -7.981 -9.949 1.00 47.38 A N ANISOU 546 N ASN A 80 4722 5757 7522 195 -269 57 A N ATOM 547 CA ASN A 80 49.593 -6.907 -10.798 1.00 43.64 A C ANISOU 547 CA ASN A 80 4261 5389 6930 164 -163 63 A C ATOM 548 C ASN A 80 49.331 -7.316 -12.239 1.00 48.73 A C ANISOU 548 C ASN A 80 4867 6109 7540 242 -111 -47 A C ATOM 549 O ASN A 80 50.247 -7.658 -12.986 1.00 55.83 A O ANISOU 549 O ASN A 80 5672 7079 8461 312 -83 -126 A O ATOM 550 CB ASN A 80 50.589 -5.757 -10.790 1.00 44.08 A C ANISOU 550 CB ASN A 80 4270 5538 6941 113 -104 115 A C ATOM 551 CG ASN A 80 50.152 -4.614 -11.686 1.00 49.67 A C ANISOU 551 CG ASN A 80 5016 6337 7519 81 4 133 A C ATOM 552 ND2 ASN A 80 50.977 -4.285 -12.672 1.00 44.81 A N ANISOU 552 ND2 ASN A 80 4318 5843 6865 97 80 93 A N ATOM 553 OD1 ASN A 80 49.077 -4.042 -11.499 1.00 55.62 A O ANISOU 553 OD1 ASN A 80 5874 7057 8204 49 19 184 A O ATOM 554 N LEU A 81 48.067 -7.257 -12.622 1.00 50.47 A N ANISOU 554 N LEU A 81 5154 6326 7696 229 -96 -54 A N ATOM 555 CA LEU A 81 47.667 -7.466 -13.998 1.00 52.67 A C ANISOU 555 CA LEU A 81 5413 6689 7909 287 -50 -148 A C ATOM 556 C LEU A 81 48.017 -6.203 -14.768 1.00 56.04 A C ANISOU 556 C LEU A 81 5826 7248 8218 275 54 -115 A C ATOM 557 O LEU A 81 47.529 -5.121 -14.451 1.00 55.45 A O ANISOU 557 O LEU A 81 5817 7181 8069 218 86 -20 A O ATOM 558 CB LEU A 81 46.164 -7.747 -14.069 1.00 42.11 A C ANISOU 558 CB LEU A 81 4142 5320 6538 264 -81 -156 A C ATOM 559 CG LEU A 81 45.555 -7.934 -15.455 1.00 46.28 A C ANISOU 559 CG LEU A 81 4660 5942 6982 311 -51 -250 A C ATOM 560 CD1 LEU A 81 46.022 -9.260 -16.100 1.00 40.03 A C ANISOU 560 CD1 LEU A 81 3833 5118 6257 381 -87 -391 A C ATOM 561 CD2 LEU A 81 44.019 -7.876 -15.363 1.00 39.20 A C ANISOU 561 CD2 LEU A 81 3810 5046 6037 268 -80 -227 A C ATOM 562 N ILE A 82 48.883 -6.328 -15.765 1.00 55.75 A N ANISOU 562 N ILE A 82 5712 7311 8159 328 111 -191 A N ATOM 563 CA ILE A 82 49.303 -5.162 -16.523 1.00 51.19 A C ANISOU 563 CA ILE A 82 5128 6860 7463 300 216 -152 A C ATOM 564 C ILE A 82 48.251 -4.776 -17.546 1.00 52.54 A C ANISOU 564 C ILE A 82 5366 7095 7501 320 254 -165 A C ATOM 565 O ILE A 82 47.875 -3.618 -17.651 1.00 54.10 A O ANISOU 565 O ILE A 82 5635 7323 7596 277 300 -75 A O ATOM 566 CB ILE A 82 50.641 -5.395 -17.231 1.00 50.86 A C ANISOU 566 CB ILE A 82 4967 6928 7431 342 278 -226 A C ATOM 567 CG1 ILE A 82 51.758 -5.530 -16.197 1.00 49.09 A C ANISOU 567 CG1 ILE A 82 4660 6669 7324 317 240 -193 A C ATOM 568 CG2 ILE A 82 50.933 -4.250 -18.183 1.00 36.69 A C ANISOU 568 CG2 ILE A 82 3181 5270 5490 298 396 -187 A C ATOM 569 CD1 ILE A 82 52.940 -6.311 -16.701 1.00 53.32 A C ANISOU 569 CD1 ILE A 82 5049 7288 7922 406 262 -300 A C ATOM 570 N GLU A 83 47.776 -5.758 -18.298 1.00 57.52 A N ANISOU 570 N GLU A 83 5981 7742 8131 389 225 -280 A N ATOM 571 CA GLU A 83 46.811 -5.510 -19.357 1.00 45.51 A C ANISOU 571 CA GLU A 83 4510 6302 6480 415 246 -307 A C ATOM 572 C GLU A 83 46.323 -6.841 -19.887 1.00 52.97 A C ANISOU 572 C GLU A 83 5438 7228 7459 471 184 -446 A C ATOM 573 O GLU A 83 46.829 -7.905 -19.503 1.00 55.53 A O ANISOU 573 O GLU A 83 5723 7469 7906 500 137 -521 A O ATOM 574 CB GLU A 83 47.459 -4.735 -20.507 1.00 44.59 A C ANISOU 574 CB GLU A 83 4385 6330 6228 426 355 -307 A C ATOM 575 CG GLU A 83 48.489 -5.564 -21.298 1.00 52.77 A C ANISOU 575 CG GLU A 83 5327 7441 7281 487 398 -438 A C ATOM 576 CD GLU A 83 49.126 -4.782 -22.448 1.00 62.71 A C ANISOU 576 CD GLU A 83 6577 8862 8389 483 521 -433 A C ATOM 577 OE1 GLU A 83 48.451 -3.909 -23.029 1.00 71.99 A O ANISOU 577 OE1 GLU A 83 7841 10092 9421 461 551 -366 A O ATOM 578 OE2 GLU A 83 50.302 -5.045 -22.780 1.00 60.71 A O1- ANISOU 578 OE2 GLU A 83 6225 8687 8154 504 589 -495 A O1- ATOM 579 N ILE A 84 45.344 -6.771 -20.782 1.00 57.51 A N ANISOU 579 N ILE A 84 6051 7876 7922 489 178 -482 A N ATOM 580 CA ILE A 84 44.856 -7.945 -21.495 1.00 53.09 A C ANISOU 580 CA ILE A 84 5489 7319 7365 529 122 -627 A C ATOM 581 C ILE A 84 45.155 -7.828 -22.987 1.00 52.46 A C ANISOU 581 C ILE A 84 5405 7387 7141 586 190 -713 A C ATOM 582 O ILE A 84 44.924 -6.785 -23.594 1.00 58.16 A O ANISOU 582 O ILE A 84 6159 8219 7720 581 245 -643 A O ATOM 583 CB ILE A 84 43.355 -8.156 -21.229 1.00 49.67 A C ANISOU 583 CB ILE A 84 5091 6854 6926 486 35 -612 A C ATOM 584 CG1 ILE A 84 43.185 -8.659 -19.799 1.00 45.42 A C ANISOU 584 CG1 ILE A 84 4555 6161 6541 428 -31 -562 A C ATOM 585 CG2 ILE A 84 42.752 -9.130 -22.238 1.00 48.63 A C ANISOU 585 CG2 ILE A 84 4967 6762 6749 508 -17 -761 A C ATOM 586 CD1 ILE A 84 42.112 -7.961 -19.050 1.00 51.80 A C ANISOU 586 CD1 ILE A 84 5386 6967 7331 372 -53 -447 A C ATOM 587 N CYS A 85 45.694 -8.893 -23.570 1.00 52.43 A N ANISOU 587 N CYS A 85 5375 7380 7167 645 188 -865 A N ATOM 588 CA CYS A 85 46.124 -8.837 -24.956 1.00 50.48 A C ANISOU 588 CA CYS A 85 5123 7280 6777 703 267 -959 A C ATOM 589 C CYS A 85 45.392 -9.852 -25.812 1.00 57.17 A C ANISOU 589 C CYS A 85 6010 8135 7575 736 201 -1118 A C ATOM 590 O CYS A 85 44.993 -10.919 -25.339 1.00 62.14 A O ANISOU 590 O CYS A 85 6657 8631 8323 728 106 -1193 A O ATOM 591 CB CYS A 85 47.645 -9.019 -25.056 1.00 64.22 A C ANISOU 591 CB CYS A 85 6783 9054 8563 759 357 -1010 A C ATOM 592 SG CYS A 85 48.612 -7.528 -24.578 1.00 61.02 A S ANISOU 592 SG CYS A 85 6330 8722 8133 695 468 -833 A S ATOM 593 N ARG A 86 45.204 -9.498 -27.076 1.00 58.33 A N ANISOU 593 N ARG A 86 6187 8438 7540 762 248 -1164 A N ATOM 594 CA ARG A 86 44.520 -10.355 -28.032 1.00 56.67 A C ANISOU 594 CA ARG A 86 6023 8261 7248 785 187 -1321 A C ATOM 595 C ARG A 86 45.518 -10.971 -29.003 1.00 66.52 A C ANISOU 595 C ARG A 86 7261 9576 8438 874 267 -1485 A C ATOM 596 O ARG A 86 46.730 -10.795 -28.880 1.00 57.89 A O ANISOU 596 O ARG A 86 6105 8508 7384 919 368 -1476 A O ATOM 597 CB ARG A 86 43.511 -9.538 -28.843 1.00 49.23 A C ANISOU 597 CB ARG A 86 5127 7464 6114 761 169 -1265 A C ATOM 598 CG ARG A 86 44.173 -8.436 -29.654 1.00 55.98 A C ANISOU 598 CG ARG A 86 5994 8478 6798 789 296 -1194 A C ATOM 599 CD ARG A 86 43.190 -7.581 -30.426 1.00 68.52 A C ANISOU 599 CD ARG A 86 7645 10199 8192 781 268 -1121 A C ATOM 600 NE ARG A 86 43.765 -6.266 -30.715 1.00 81.50 A N ANISOU 600 NE ARG A 86 9319 11935 9714 779 382 -978 A N ATOM 601 CZ ARG A 86 44.132 -5.839 -31.922 1.00 87.75 A C ANISOU 601 CZ ARG A 86 10158 12880 10303 805 464 -994 A C ATOM 602 NH1 ARG A 86 43.979 -6.621 -32.981 1.00 89.14 A N1+ ANISOU 602 NH1 ARG A 86 10355 13147 10367 845 446 -1157 A N1+ ATOM 603 NH2 ARG A 86 44.643 -4.620 -32.071 1.00 87.75 A N ANISOU 603 NH2 ARG A 86 10198 12940 10202 780 566 -845 A N ATOM 604 N THR A 87 44.966 -11.665 -29.990 1.00 79.84 A N ANISOU 604 N THR A 87 9006 11308 10022 896 221 -1637 A N ATOM 605 CA THR A 87 45.709 -12.315 -31.043 1.00 84.69 A C ANISOU 605 CA THR A 87 9633 11994 10551 987 290 -1819 A C ATOM 606 C THR A 87 44.640 -13.017 -31.838 1.00 96.49 A C ANISOU 606 C THR A 87 11215 13501 11946 966 185 -1956 A C ATOM 607 O THR A 87 44.471 -12.792 -33.035 1.00109.37 A O ANISOU 607 O THR A 87 12889 15293 13372 986 218 -2022 A O ATOM 608 CB THR A 87 46.581 -13.407 -30.482 1.00 89.76 A C ANISOU 608 CB THR A 87 10244 12483 11376 1062 288 -1933 A C ATOM 609 CG2 THR A 87 45.743 -14.648 -30.222 1.00 73.33 A C ANISOU 609 CG2 THR A 87 8244 10223 9393 1037 141 -2052 A C ATOM 610 OG1 THR A 87 47.614 -13.716 -31.424 1.00109.33 A O ANISOU 610 OG1 THR A 87 12701 15071 13769 1174 405 -2078 A O ATOM 611 N SER A 98 42.372 -15.667 -29.626 1.00 92.62 A N ANISOU 611 N SER A 98 10827 12477 11888 756 -211 -2058 A N ATOM 612 CA SER A 98 42.627 -15.890 -28.202 1.00 90.12 A C ANISOU 612 CA SER A 98 10485 11975 11783 728 -237 -1956 A C ATOM 613 C SER A 98 42.800 -14.615 -27.369 1.00 81.23 A C ANISOU 613 C SER A 98 9274 10907 10682 708 -176 -1735 A C ATOM 614 O SER A 98 42.746 -13.498 -27.884 1.00 88.42 A O ANISOU 614 O SER A 98 10151 11992 11452 719 -108 -1650 A O ATOM 615 CB SER A 98 43.851 -16.782 -28.015 1.00 93.03 A C ANISOU 615 CB SER A 98 10874 12201 12271 842 -202 -2067 A C ATOM 616 OG SER A 98 43.586 -18.089 -28.481 1.00106.12 A O ANISOU 616 OG SER A 98 12640 13734 13947 848 -282 -2264 A O ATOM 617 N ILE A 99 43.015 -14.813 -26.073 1.00 63.07 A N ANISOU 617 N ILE A 99 6959 8448 8558 678 -204 -1645 A N ATOM 618 CA ILE A 99 43.178 -13.729 -25.117 1.00 57.43 A C ANISOU 618 CA ILE A 99 6182 7754 7886 650 -160 -1447 A C ATOM 619 C ILE A 99 44.224 -14.109 -24.067 1.00 57.43 A C ANISOU 619 C ILE A 99 6162 7602 8059 690 -149 -1413 A C ATOM 620 O ILE A 99 44.338 -15.274 -23.680 1.00 62.21 A O ANISOU 620 O ILE A 99 6816 8036 8785 701 -220 -1498 A O ATOM 621 CB ILE A 99 41.830 -13.394 -24.438 1.00 59.27 A C ANISOU 621 CB ILE A 99 6415 7976 8130 529 -238 -1334 A C ATOM 622 CG1 ILE A 99 40.953 -12.596 -25.398 1.00 63.90 A C ANISOU 622 CG1 ILE A 99 6990 8757 8532 516 -233 -1317 A C ATOM 623 CG2 ILE A 99 42.029 -12.629 -23.137 1.00 48.82 A C ANISOU 623 CG2 ILE A 99 5055 6598 6897 497 -213 -1153 A C ATOM 624 CD1 ILE A 99 41.624 -11.359 -25.945 1.00 59.60 A C ANISOU 624 CD1 ILE A 99 6423 8360 7863 587 -119 -1237 A C ATOM 625 N TYR A 100 44.993 -13.126 -23.614 1.00 52.35 A N ANISOU 625 N TYR A 100 5453 7018 7421 711 -67 -1287 A N ATOM 626 CA TYR A 100 46.037 -13.375 -22.635 1.00 54.85 A C ANISOU 626 CA TYR A 100 5732 7222 7887 751 -62 -1246 A C ATOM 627 C TYR A 100 45.936 -12.369 -21.511 1.00 56.19 A C ANISOU 627 C TYR A 100 5874 7382 8093 673 -55 -1054 A C ATOM 628 O TYR A 100 45.764 -11.166 -21.752 1.00 55.90 A O ANISOU 628 O TYR A 100 5818 7474 7946 641 11 -958 A O ATOM 629 CB TYR A 100 47.433 -13.215 -23.259 1.00 59.98 A C ANISOU 629 CB TYR A 100 6306 7975 8509 866 45 -1308 A C ATOM 630 CG TYR A 100 47.822 -14.218 -24.316 1.00 60.35 A C ANISOU 630 CG TYR A 100 6372 8032 8525 976 59 -1512 A C ATOM 631 CD1 TYR A 100 48.644 -15.293 -24.007 1.00 65.33 A C ANISOU 631 CD1 TYR A 100 6997 8534 9291 1084 28 -1614 A C ATOM 632 CD2 TYR A 100 47.395 -14.075 -25.627 1.00 64.40 A C ANISOU 632 CD2 TYR A 100 6916 8686 8868 985 102 -1605 A C ATOM 633 CE1 TYR A 100 49.019 -16.205 -24.967 1.00 64.26 A C ANISOU 633 CE1 TYR A 100 6890 8399 9125 1203 47 -1813 A C ATOM 634 CE2 TYR A 100 47.768 -14.988 -26.601 1.00 70.73 A C ANISOU 634 CE2 TYR A 100 7747 9500 9628 1089 121 -1805 A C ATOM 635 CZ TYR A 100 48.582 -16.051 -26.266 1.00 69.65 A C ANISOU 635 CZ TYR A 100 7608 9225 9632 1201 97 -1913 A C ATOM 636 OH TYR A 100 48.955 -16.968 -27.231 1.00 78.56 A O ANISOU 636 OH TYR A 100 8777 10354 10717 1322 119 -2124 A O ATOM 637 N LEU A 101 46.070 -12.852 -20.282 1.00 50.06 A N ANISOU 637 N LEU A 101 5112 6446 7463 647 -123 -999 A N ATOM 638 CA LEU A 101 46.256 -11.954 -19.162 1.00 48.30 A C ANISOU 638 CA LEU A 101 4864 6210 7278 588 -110 -833 A C ATOM 639 C LEU A 101 47.750 -11.705 -19.041 1.00 56.25 A C ANISOU 639 C LEU A 101 5789 7256 8328 661 -50 -825 A C ATOM 640 O LEU A 101 48.534 -12.652 -19.013 1.00 47.71 A O ANISOU 640 O LEU A 101 4684 6102 7340 749 -78 -916 A O ATOM 641 CB LEU A 101 45.690 -12.561 -17.875 1.00 55.71 A C ANISOU 641 CB LEU A 101 5859 6973 8335 515 -211 -770 A C ATOM 642 CG LEU A 101 44.181 -12.363 -17.661 1.00 51.17 A C ANISOU 642 CG LEU A 101 5331 6402 7711 407 -249 -717 A C ATOM 643 CD1 LEU A 101 43.410 -13.036 -18.756 1.00 42.49 A C ANISOU 643 CD1 LEU A 101 4258 5337 6550 407 -278 -849 A C ATOM 644 CD2 LEU A 101 43.757 -12.902 -16.315 1.00 49.45 A C ANISOU 644 CD2 LEU A 101 5163 6024 7601 324 -329 -641 A C ATOM 645 N VAL A 102 48.149 -10.436 -19.000 1.00 54.64 A N ANISOU 645 N VAL A 102 5541 7167 8053 625 32 -720 A N ATOM 646 CA VAL A 102 49.560 -10.106 -18.849 1.00 52.92 A C ANISOU 646 CA VAL A 102 5227 7010 7872 665 90 -703 A C ATOM 647 C VAL A 102 49.911 -9.659 -17.427 1.00 54.16 A C ANISOU 647 C VAL A 102 5374 7088 8116 598 48 -567 A C ATOM 648 O VAL A 102 49.392 -8.652 -16.958 1.00 59.43 A O ANISOU 648 O VAL A 102 6087 7764 8727 505 63 -448 A O ATOM 649 CB VAL A 102 49.995 -9.016 -19.847 1.00 49.09 A C ANISOU 649 CB VAL A 102 4697 6715 7241 654 219 -687 A C ATOM 650 CG1 VAL A 102 51.511 -8.879 -19.834 1.00 44.64 A C ANISOU 650 CG1 VAL A 102 4006 6238 6719 693 284 -699 A C ATOM 651 CG2 VAL A 102 49.505 -9.360 -21.237 1.00 45.02 A C ANISOU 651 CG2 VAL A 102 4211 6286 6610 708 255 -808 A C ATOM 652 N PHE A 103 50.798 -10.398 -16.755 1.00 50.73 A N ANISOU 652 N PHE A 103 4887 6577 7811 656 -8 -590 A N ATOM 653 CA PHE A 103 51.282 -10.010 -15.423 1.00 53.71 A C ANISOU 653 CA PHE A 103 5248 6895 8264 598 -56 -468 A C ATOM 654 C PHE A 103 52.777 -9.672 -15.377 1.00 59.19 A C ANISOU 654 C PHE A 103 5801 7698 8990 633 -13 -465 A C ATOM 655 O PHE A 103 53.587 -10.283 -16.083 1.00 58.16 A O ANISOU 655 O PHE A 103 5573 7637 8888 748 18 -578 A O ATOM 656 CB PHE A 103 51.063 -11.134 -14.413 1.00 56.13 A C ANISOU 656 CB PHE A 103 5615 7012 8699 622 -186 -467 A C ATOM 657 CG PHE A 103 49.657 -11.662 -14.358 1.00 53.03 A C ANISOU 657 CG PHE A 103 5346 6508 8295 574 -238 -476 A C ATOM 658 CD1 PHE A 103 48.778 -11.219 -13.384 1.00 48.09 A C ANISOU 658 CD1 PHE A 103 4800 5817 7656 459 -273 -358 A C ATOM 659 CD2 PHE A 103 49.231 -12.634 -15.249 1.00 54.23 A C ANISOU 659 CD2 PHE A 103 5533 6625 8448 637 -254 -610 A C ATOM 660 CE1 PHE A 103 47.488 -11.725 -13.308 1.00 54.71 A C ANISOU 660 CE1 PHE A 103 5728 6574 8485 403 -317 -366 A C ATOM 661 CE2 PHE A 103 47.936 -13.140 -15.181 1.00 63.76 A C ANISOU 661 CE2 PHE A 103 6842 7739 9646 569 -308 -620 A C ATOM 662 CZ PHE A 103 47.067 -12.690 -14.207 1.00 58.20 A C ANISOU 662 CZ PHE A 103 6194 6987 8932 449 -337 -495 A C ATOM 663 N ASP A 104 53.144 -8.723 -14.517 1.00 63.65 A N ANISOU 663 N ASP A 104 6351 8283 9551 533 -13 -341 A N ATOM 664 CA ASP A 104 54.543 -8.540 -14.121 1.00 63.46 A C ANISOU 664 CA ASP A 104 6185 8340 9586 544 -12 -323 A C ATOM 665 C ASP A 104 55.111 -9.910 -13.732 1.00 63.50 A C ANISOU 665 C ASP A 104 6136 8258 9732 686 -114 -399 A C ATOM 666 O ASP A 104 54.496 -10.639 -12.957 1.00 70.33 A O ANISOU 666 O ASP A 104 7106 8949 10665 698 -223 -377 A O ATOM 667 CB ASP A 104 54.640 -7.573 -12.932 1.00 73.14 A C ANISOU 667 CB ASP A 104 7446 9537 10806 406 -47 -178 A C ATOM 668 CG ASP A 104 54.602 -6.088 -13.349 1.00 85.78 A C ANISOU 668 CG ASP A 104 9069 11248 12276 278 65 -106 A C ATOM 669 OD1 ASP A 104 55.263 -5.719 -14.345 1.00 90.93 A O ANISOU 669 OD1 ASP A 104 9625 12055 12870 283 169 -151 A O ATOM 670 OD2 ASP A 104 53.931 -5.282 -12.659 1.00 81.50 A O1- ANISOU 670 OD2 ASP A 104 8648 10634 11686 171 51 -4 A O1- ATOM 671 N PHE A 105 56.270 -10.274 -14.273 1.00 64.40 A N ANISOU 671 N PHE A 105 6091 8492 9887 799 -78 -488 A N ATOM 672 CA PHE A 105 56.856 -11.597 -14.013 1.00 64.85 A C ANISOU 672 CA PHE A 105 6098 8465 10077 970 -173 -574 A C ATOM 673 C PHE A 105 57.451 -11.739 -12.606 1.00 72.43 A C ANISOU 673 C PHE A 105 7027 9350 11142 964 -302 -478 A C ATOM 674 O PHE A 105 58.045 -10.797 -12.082 1.00 74.07 A O ANISOU 674 O PHE A 105 7151 9662 11328 859 -290 -386 A O ATOM 675 CB PHE A 105 57.919 -11.919 -15.065 1.00 57.19 A C ANISOU 675 CB PHE A 105 4951 7666 9111 1114 -83 -709 A C ATOM 676 CG PHE A 105 58.592 -13.249 -14.872 1.00 54.80 A C ANISOU 676 CG PHE A 105 4593 7284 8944 1324 -175 -808 A C ATOM 677 CD1 PHE A 105 57.966 -14.418 -15.253 1.00 55.60 A C ANISOU 677 CD1 PHE A 105 4824 7220 9083 1444 -224 -917 A C ATOM 678 CD2 PHE A 105 59.878 -13.323 -14.336 1.00 60.60 A C ANISOU 678 CD2 PHE A 105 5143 8114 9767 1406 -216 -796 A C ATOM 679 CE1 PHE A 105 58.605 -15.652 -15.091 1.00 63.98 A C ANISOU 679 CE1 PHE A 105 5856 8183 10268 1654 -311 -1012 A C ATOM 680 CE2 PHE A 105 60.530 -14.553 -14.171 1.00 55.59 A C ANISOU 680 CE2 PHE A 105 4456 7406 9260 1630 -307 -888 A C ATOM 681 CZ PHE A 105 59.894 -15.715 -14.546 1.00 57.43 A C ANISOU 681 CZ PHE A 105 4844 7448 9530 1760 -354 -995 A C ATOM 682 N CYS A 106 57.273 -12.914 -11.999 1.00 72.07 A N ANISOU 682 N CYS A 106 7064 9117 11202 1069 -432 -497 A N ATOM 683 CA CYS A 106 57.809 -13.196 -10.666 1.00 70.32 A C ANISOU 683 CA CYS A 106 6833 8810 11074 1083 -574 -406 A C ATOM 684 C CYS A 106 58.537 -14.531 -10.700 1.00 79.32 A C ANISOU 684 C CYS A 106 7922 9877 12340 1311 -663 -503 A C ATOM 685 O CYS A 106 57.962 -15.562 -11.070 1.00 72.26 A O ANISOU 685 O CYS A 106 7151 8823 11480 1408 -695 -588 A O ATOM 686 CB CYS A 106 56.711 -13.213 -9.587 1.00 70.90 A C ANISOU 686 CB CYS A 106 7111 8690 11138 956 -664 -287 A C ATOM 687 SG CYS A 106 55.596 -11.713 -9.486 1.00 97.97 A S ANISOU 687 SG CYS A 106 10640 12166 14418 714 -565 -179 A S ATOM 688 N GLU A 107 59.809 -14.499 -10.312 1.00 85.91 A N ANISOU 688 N GLU A 107 8574 10827 13239 1397 -708 -494 A N ATOM 689 CA GLU A 107 60.692 -15.648 -10.436 1.00 80.86 A C ANISOU 689 CA GLU A 107 7843 10162 12717 1647 -780 -595 A C ATOM 690 C GLU A 107 60.333 -16.773 -9.462 1.00 78.33 A C ANISOU 690 C GLU A 107 7705 9565 12493 1732 -961 -550 A C ATOM 691 O GLU A 107 60.244 -17.941 -9.849 1.00 74.27 A O ANISOU 691 O GLU A 107 7272 8902 12046 1909 -1004 -654 A O ATOM 692 CB GLU A 107 62.143 -15.198 -10.230 1.00 97.95 A C ANISOU 692 CB GLU A 107 9736 12560 14920 1703 -782 -585 A C ATOM 693 CG GLU A 107 63.173 -16.325 -10.281 1.00108.45 A C ANISOU 693 CG GLU A 107 10937 13893 16378 1990 -864 -685 A C ATOM 694 CD GLU A 107 63.325 -16.924 -11.667 1.00113.93 A C ANISOU 694 CD GLU A 107 11573 14646 17068 2169 -743 -875 A C ATOM 695 OE1 GLU A 107 63.496 -16.150 -12.637 1.00118.86 A O ANISOU 695 OE1 GLU A 107 12071 15491 17599 2094 -571 -930 A O ATOM 696 OE2 GLU A 107 63.277 -18.169 -11.783 1.00109.64 A O1- ANISOU 696 OE2 GLU A 107 11126 13923 16609 2383 -820 -968 A O1- ATOM 697 N HIS A 108 60.113 -16.420 -8.200 1.00 81.56 A N ANISOU 697 N HIS A 108 8195 9896 12898 1599 -1065 -393 A N ATOM 698 CA HIS A 108 59.935 -17.428 -7.156 1.00 80.59 A C ANISOU 698 CA HIS A 108 8234 9528 12857 1671 -1245 -326 A C ATOM 699 C HIS A 108 58.515 -17.555 -6.609 1.00 72.53 A C ANISOU 699 C HIS A 108 7478 8292 11786 1501 -1275 -239 A C ATOM 700 O HIS A 108 57.669 -16.688 -6.807 1.00 67.01 A O ANISOU 700 O HIS A 108 6826 7647 10986 1312 -1172 -204 A O ATOM 701 CB HIS A 108 60.895 -17.153 -5.997 1.00 83.11 A C ANISOU 701 CB HIS A 108 8446 9916 13216 1680 -1372 -213 A C ATOM 702 CG HIS A 108 62.277 -16.807 -6.442 1.00 93.15 A C ANISOU 702 CG HIS A 108 9420 11450 14524 1798 -1334 -280 A C ATOM 703 CD2 HIS A 108 63.314 -17.591 -6.818 1.00 92.82 A C ANISOU 703 CD2 HIS A 108 9217 11469 14582 2059 -1374 -384 A C ATOM 704 ND1 HIS A 108 62.711 -15.503 -6.570 1.00 91.06 A N ANISOU 704 ND1 HIS A 108 8982 11433 14184 1637 -1234 -246 A N ATOM 705 CE1 HIS A 108 63.962 -15.502 -6.995 1.00 91.45 A C ANISOU 705 CE1 HIS A 108 8765 11698 14285 1775 -1213 -321 A C ATOM 706 NE2 HIS A 108 64.350 -16.755 -7.157 1.00 93.72 A N ANISOU 706 NE2 HIS A 108 9043 11885 14679 2043 -1294 -409 A N ATOM 707 N ASP A 109 58.285 -18.654 -5.902 1.00 71.10 A N ANISOU 707 N ASP A 109 7469 7869 11676 1575 -1420 -201 A N ATOM 708 CA ASP A 109 57.056 -18.882 -5.174 1.00 74.56 A C ANISOU 708 CA ASP A 109 8151 8104 12075 1412 -1469 -100 A C ATOM 709 C ASP A 109 57.359 -19.621 -3.860 1.00 74.11 A C ANISOU 709 C ASP A 109 8213 7865 12079 1464 -1658 19 A C ATOM 710 O ASP A 109 58.192 -20.524 -3.817 1.00 79.47 A O ANISOU 710 O ASP A 109 8870 8467 12859 1681 -1765 -23 A O ATOM 711 CB ASP A 109 56.083 -19.680 -6.030 1.00 84.70 A C ANISOU 711 CB ASP A 109 9584 9236 13363 1420 -1422 -206 A C ATOM 712 CG ASP A 109 56.497 -21.113 -6.182 1.00 99.71 A C ANISOU 712 CG ASP A 109 11571 10937 15377 1638 -1531 -289 A C ATOM 713 OD1 ASP A 109 57.436 -21.380 -6.964 1.00114.12 A O ANISOU 713 OD1 ASP A 109 13248 12856 17257 1847 -1504 -418 A O ATOM 714 OD2 ASP A 109 55.882 -21.970 -5.512 1.00103.73 A O1- ANISOU 714 OD2 ASP A 109 12303 11194 15915 1601 -1639 -224 A O1- ATOM 715 N LEU A 110 56.679 -19.221 -2.793 1.00 67.96 A N ANISOU 715 N LEU A 110 7566 7023 11232 1271 -1697 167 A N ATOM 716 CA LEU A 110 56.919 -19.762 -1.464 1.00 65.65 A C ANISOU 716 CA LEU A 110 7398 6578 10966 1286 -1872 302 A C ATOM 717 C LEU A 110 56.999 -21.295 -1.417 1.00 70.41 A C ANISOU 717 C LEU A 110 8161 6920 11672 1462 -2002 275 A C ATOM 718 O LEU A 110 57.826 -21.847 -0.691 1.00 72.45 A O ANISOU 718 O LEU A 110 8429 7106 11991 1606 -2159 335 A O ATOM 719 CB LEU A 110 55.859 -19.238 -0.498 1.00 65.97 A C ANISOU 719 CB LEU A 110 7603 6564 10899 1035 -1862 444 A C ATOM 720 CG LEU A 110 56.274 -19.006 0.949 1.00 68.44 A C ANISOU 720 CG LEU A 110 7965 6865 11175 980 -1994 603 A C ATOM 721 CD1 LEU A 110 57.655 -18.362 1.019 1.00 73.69 A C ANISOU 721 CD1 LEU A 110 8392 7742 11865 1080 -2034 592 A C ATOM 722 CD2 LEU A 110 55.229 -18.147 1.655 1.00 64.26 A C ANISOU 722 CD2 LEU A 110 7546 6358 10514 724 -1923 707 A C ATOM 723 N ALA A 111 56.157 -21.987 -2.181 1.00 68.41 A N ANISOU 723 N ALA A 111 8039 6519 11434 1454 -1947 184 A N ATOM 724 CA ALA A 111 56.210 -23.452 -2.197 1.00 67.45 A C ANISOU 724 CA ALA A 111 8097 6122 11408 1615 -2067 146 A C ATOM 725 C ALA A 111 57.560 -23.966 -2.717 1.00 78.15 A C ANISOU 725 C ALA A 111 9298 7521 12873 1929 -2125 33 A C ATOM 726 O ALA A 111 58.140 -24.912 -2.158 1.00 80.00 A O ANISOU 726 O ALA A 111 9629 7578 13191 2109 -2287 70 A O ATOM 727 CB ALA A 111 55.068 -24.039 -3.008 1.00 58.25 A C ANISOU 727 CB ALA A 111 7092 4808 10234 1529 -1992 52 A C ATOM 728 N GLY A 112 58.048 -23.341 -3.788 1.00 73.86 A N ANISOU 728 N GLY A 112 8519 7220 12326 2000 -1990 -103 A N ATOM 729 CA GLY A 112 59.350 -23.665 -4.346 1.00 73.60 A C ANISOU 729 CA GLY A 112 8290 7293 12383 2288 -2011 -221 A C ATOM 730 C GLY A 112 60.516 -23.379 -3.411 1.00 79.50 A C ANISOU 730 C GLY A 112 8879 8161 13167 2389 -2134 -119 A C ATOM 731 O GLY A 112 61.373 -24.247 -3.190 1.00 84.24 A O ANISOU 731 O GLY A 112 9467 8673 13867 2648 -2270 -140 A O ATOM 732 N LEU A 113 60.554 -22.166 -2.862 1.00 72.97 A N ANISOU 732 N LEU A 113 7934 7534 12256 2192 -2095 -13 A N ATOM 733 CA LEU A 113 61.636 -21.772 -1.970 1.00 74.11 A C ANISOU 733 CA LEU A 113 7917 7823 12419 2250 -2213 83 A C ATOM 734 C LEU A 113 61.677 -22.667 -0.724 1.00 85.35 A C ANISOU 734 C LEU A 113 9548 9000 13881 2319 -2433 220 A C ATOM 735 O LEU A 113 62.749 -23.021 -0.228 1.00 92.65 A O ANISOU 735 O LEU A 113 10366 9961 14875 2518 -2581 249 A O ATOM 736 CB LEU A 113 61.505 -20.300 -1.581 1.00 70.41 A C ANISOU 736 CB LEU A 113 7339 7575 11837 1988 -2130 171 A C ATOM 737 CG LEU A 113 61.415 -19.287 -2.734 1.00 71.80 A C ANISOU 737 CG LEU A 113 7338 7988 11956 1888 -1915 64 A C ATOM 738 CD1 LEU A 113 60.827 -17.940 -2.286 1.00 58.16 A C ANISOU 738 CD1 LEU A 113 5626 6372 10102 1594 -1833 166 A C ATOM 739 CD2 LEU A 113 62.771 -19.081 -3.391 1.00 71.54 A C ANISOU 739 CD2 LEU A 113 6990 8211 11982 2065 -1880 -40 A C ATOM 740 N LEU A 114 60.505 -23.046 -0.234 1.00 79.57 A N ANISOU 740 N LEU A 114 9109 8025 13101 2156 -2455 307 A N ATOM 741 CA LEU A 114 60.416 -23.862 0.965 1.00 82.04 A C ANISOU 741 CA LEU A 114 9654 8091 13427 2183 -2651 455 A C ATOM 742 C LEU A 114 60.781 -25.333 0.709 1.00 91.54 A C ANISOU 742 C LEU A 114 10985 9042 14752 2469 -2774 390 A C ATOM 743 O LEU A 114 61.232 -26.038 1.620 1.00 81.21 A O ANISOU 743 O LEU A 114 9796 7578 13484 2597 -2969 497 A O ATOM 744 CB LEU A 114 59.016 -23.758 1.577 1.00 81.41 A C ANISOU 744 CB LEU A 114 9839 7851 13243 1892 -2617 572 A C ATOM 745 CG LEU A 114 58.681 -22.455 2.302 1.00 78.83 A C ANISOU 745 CG LEU A 114 9459 7707 12787 1631 -2558 686 A C ATOM 746 CD1 LEU A 114 57.314 -22.545 2.959 1.00 72.85 A C ANISOU 746 CD1 LEU A 114 8970 6775 11934 1382 -2535 799 A C ATOM 747 CD2 LEU A 114 59.751 -22.118 3.327 1.00 81.05 A C ANISOU 747 CD2 LEU A 114 9633 8103 13059 1693 -2711 794 A C ATOM 748 N SER A 115 60.579 -25.795 -0.523 1.00 94.63 A N ANISOU 748 N SER A 115 11370 9387 15197 2572 -2665 214 A N ATOM 749 CA SER A 115 60.927 -27.164 -0.879 1.00 92.96 A C ANISOU 749 CA SER A 115 11289 8931 15101 2856 -2767 125 A C ATOM 750 C SER A 115 62.373 -27.225 -1.363 1.00100.65 A C ANISOU 750 C SER A 115 11973 10100 16170 3182 -2795 9 A C ATOM 751 O SER A 115 62.788 -28.196 -2.000 1.00105.25 A O ANISOU 751 O SER A 115 12589 10552 16850 3459 -2828 -125 A O ATOM 752 CB SER A 115 59.989 -27.704 -1.957 1.00 88.94 A C ANISOU 752 CB SER A 115 10936 8262 14596 2809 -2646 -21 A C ATOM 753 OG SER A 115 60.375 -27.238 -3.241 1.00 91.66 A O ANISOU 753 OG SER A 115 11032 8846 14950 2899 -2481 -210 A O ATOM 754 N ASN A 116 63.135 -26.181 -1.059 1.00100.19 A N ANISOU 754 N ASN A 116 11629 10360 16080 3146 -2779 55 A N ATOM 755 CA ASN A 116 64.532 -26.107 -1.465 1.00106.34 A C ANISOU 755 CA ASN A 116 12085 11380 16939 3422 -2795 -45 A C ATOM 756 C ASN A 116 65.472 -26.000 -0.259 1.00114.28 A C ANISOU 756 C ASN A 116 12987 12470 17965 3510 -2996 103 A C ATOM 757 O ASN A 116 65.547 -24.953 0.394 1.00114.76 A O ANISOU 757 O ASN A 116 12935 12727 17943 3293 -2994 215 A O ATOM 758 CB ASN A 116 64.740 -24.931 -2.420 1.00102.18 A C ANISOU 758 CB ASN A 116 11256 11208 16358 3308 -2577 -155 A C ATOM 759 CG ASN A 116 66.093 -24.962 -3.101 1.00106.41 A C ANISOU 759 CG ASN A 116 11454 11999 16976 3594 -2551 -295 A C ATOM 760 ND2 ASN A 116 66.117 -24.584 -4.371 1.00103.83 A N ANISOU 760 ND2 ASN A 116 10968 11853 16630 3596 -2346 -460 A N ATOM 761 OD1 ASN A 116 67.107 -25.314 -2.493 1.00110.78 A O ANISOU 761 OD1 ASN A 116 11884 12601 17605 3812 -2713 -254 A O ATOM 762 N VAL A 117 66.188 -27.086 0.028 1.00110.73 A N ANISOU 762 N VAL A 117 12584 11867 17622 3834 -3177 98 A N ATOM 763 CA VAL A 117 67.047 -27.148 1.206 1.00111.92 A C ANISOU 763 CA VAL A 117 12668 12064 17792 3946 -3401 246 A C ATOM 764 C VAL A 117 68.141 -26.077 1.217 1.00111.61 A C ANISOU 764 C VAL A 117 12206 12457 17744 3944 -3374 230 A C ATOM 765 O VAL A 117 68.570 -25.637 2.284 1.00115.51 A O ANISOU 765 O VAL A 117 12637 13055 18196 3870 -3519 378 A O ATOM 766 CB VAL A 117 67.689 -28.546 1.375 1.00115.89 A C ANISOU 766 CB VAL A 117 13283 12330 18421 4345 -3600 226 A C ATOM 767 CG1 VAL A 117 66.612 -29.601 1.588 1.00117.56 A C ANISOU 767 CG1 VAL A 117 13953 12084 18631 4306 -3661 280 A C ATOM 768 CG2 VAL A 117 68.557 -28.889 0.171 1.00111.16 A C ANISOU 768 CG2 VAL A 117 12423 11882 17932 4674 -3511 0 A C ATOM 769 N LEU A 118 68.586 -25.658 0.036 1.00106.01 A N ANISOU 769 N LEU A 118 11213 12001 17064 4010 -3189 51 A N ATOM 770 CA LEU A 118 69.630 -24.640 -0.063 1.00106.01 A C ANISOU 770 CA LEU A 118 10801 12423 17056 3987 -3142 25 A C ATOM 771 C LEU A 118 69.113 -23.266 0.348 1.00105.62 A C ANISOU 771 C LEU A 118 10729 12532 16871 3577 -3050 131 A C ATOM 772 O LEU A 118 69.870 -22.439 0.852 1.00108.98 A O ANISOU 772 O LEU A 118 10912 13230 17267 3491 -3099 191 A O ATOM 773 CB LEU A 118 70.209 -24.583 -1.481 1.00112.09 A C ANISOU 773 CB LEU A 118 11288 13420 17881 4156 -2951 -194 A C ATOM 774 CG LEU A 118 70.922 -25.839 -2.004 1.00116.13 A C ANISOU 774 CG LEU A 118 11753 13841 18529 4602 -3020 -334 A C ATOM 775 CD1 LEU A 118 71.402 -25.632 -3.438 1.00116.82 A C ANISOU 775 CD1 LEU A 118 11561 14186 18640 4721 -2794 -554 A C ATOM 776 CD2 LEU A 118 72.081 -26.252 -1.091 1.00108.83 A C ANISOU 776 CD2 LEU A 118 10667 12996 17689 4868 -3266 -255 A C ATOM 777 N VAL A 119 67.821 -23.034 0.121 1.00103.14 A N ANISOU 777 N VAL A 119 10670 12046 16474 3329 -2920 146 A N ATOM 778 CA VAL A 119 67.162 -21.785 0.489 1.00 91.89 A C ANISOU 778 CA VAL A 119 9276 10723 14916 2954 -2825 241 A C ATOM 779 C VAL A 119 66.974 -21.724 1.997 1.00 95.61 A C ANISOU 779 C VAL A 119 9925 11076 15326 2827 -3018 442 A C ATOM 780 O VAL A 119 66.470 -22.676 2.592 1.00 98.73 A O ANISOU 780 O VAL A 119 10607 11169 15736 2896 -3149 522 A O ATOM 781 CB VAL A 119 65.764 -21.694 -0.157 1.00 84.12 A C ANISOU 781 CB VAL A 119 8528 9569 13865 2760 -2648 201 A C ATOM 782 CG1 VAL A 119 65.082 -20.401 0.240 1.00 69.37 A C ANISOU 782 CG1 VAL A 119 6694 7802 11861 2402 -2552 296 A C ATOM 783 CG2 VAL A 119 65.854 -21.831 -1.672 1.00 83.03 A C ANISOU 783 CG2 VAL A 119 8254 9523 13770 2884 -2462 1 A C ATOM 784 N LYS A 120 67.358 -20.611 2.617 1.00 97.12 A N ANISOU 784 N LYS A 120 9966 11497 15438 2629 -3034 523 A N ATOM 785 CA LYS A 120 67.288 -20.511 4.076 1.00102.53 A C ANISOU 785 CA LYS A 120 10806 12102 16051 2515 -3225 707 A C ATOM 786 C LYS A 120 66.784 -19.147 4.563 1.00104.84 A C ANISOU 786 C LYS A 120 11121 12517 16197 2153 -3137 785 A C ATOM 787 O LYS A 120 67.338 -18.103 4.208 1.00100.92 A O ANISOU 787 O LYS A 120 10369 12301 15673 2041 -3043 734 A O ATOM 788 CB LYS A 120 68.656 -20.836 4.693 1.00104.34 A C ANISOU 788 CB LYS A 120 10821 12474 16349 2742 -3446 744 A C ATOM 789 CG LYS A 120 68.598 -21.475 6.077 1.00108.58 A C ANISOU 789 CG LYS A 120 11596 12805 16853 2782 -3700 920 A C ATOM 790 CD LYS A 120 69.917 -22.167 6.415 1.00114.66 A C ANISOU 790 CD LYS A 120 12172 13666 17729 3113 -3927 927 A C ATOM 791 CE LYS A 120 69.802 -23.058 7.652 1.00116.55 A C ANISOU 791 CE LYS A 120 12698 13641 17945 3211 -4187 1100 A C ATOM 792 NZ LYS A 120 71.049 -23.843 7.914 1.00117.30 A N1+ ANISOU 792 NZ LYS A 120 12618 13799 18151 3580 -4417 1103 A N1+ ATOM 793 N PHE A 121 65.729 -19.165 5.375 1.00106.39 A N ANISOU 793 N PHE A 121 11631 12498 16294 1970 -3164 907 A N ATOM 794 CA PHE A 121 65.184 -17.939 5.955 1.00101.86 A C ANISOU 794 CA PHE A 121 11120 12009 15574 1647 -3093 985 A C ATOM 795 C PHE A 121 65.668 -17.766 7.395 1.00 99.74 A C ANISOU 795 C PHE A 121 10897 11769 15231 1588 -3308 1135 A C ATOM 796 O PHE A 121 65.728 -18.735 8.159 1.00 99.59 A O ANISOU 796 O PHE A 121 11041 11569 15230 1722 -3495 1230 A O ATOM 797 CB PHE A 121 63.648 -17.965 5.967 1.00100.44 A C ANISOU 797 CB PHE A 121 11245 11605 15311 1464 -2969 1021 A C ATOM 798 CG PHE A 121 63.010 -18.055 4.601 1.00105.13 A C ANISOU 798 CG PHE A 121 11823 12170 15953 1482 -2761 882 A C ATOM 799 CD1 PHE A 121 62.736 -16.908 3.867 1.00 97.60 A C ANISOU 799 CD1 PHE A 121 10750 11392 14941 1313 -2561 810 A C ATOM 800 CD2 PHE A 121 62.645 -19.285 4.069 1.00105.63 A C ANISOU 800 CD2 PHE A 121 12013 12016 16106 1661 -2771 827 A C ATOM 801 CE1 PHE A 121 62.137 -16.990 2.624 1.00 84.33 A C ANISOU 801 CE1 PHE A 121 9062 9690 13289 1331 -2382 689 A C ATOM 802 CE2 PHE A 121 62.043 -19.368 2.825 1.00 96.83 A C ANISOU 802 CE2 PHE A 121 10891 10879 15020 1668 -2589 695 A C ATOM 803 CZ PHE A 121 61.794 -18.219 2.103 1.00 83.85 A C ANISOU 803 CZ PHE A 121 9114 9430 13314 1506 -2397 628 A C ATOM 804 N THR A 122 66.007 -16.533 7.760 1.00 91.73 A N ANISOU 804 N THR A 122 9754 10974 14125 1382 -3285 1156 A N ATOM 805 CA THR A 122 66.232 -16.189 9.159 1.00 88.96 A C ANISOU 805 CA THR A 122 9495 10644 13663 1259 -3463 1296 A C ATOM 806 C THR A 122 64.889 -15.873 9.809 1.00 88.65 A C ANISOU 806 C THR A 122 9786 10419 13478 1020 -3389 1386 A C ATOM 807 O THR A 122 63.900 -15.630 9.112 1.00 92.98 A O ANISOU 807 O THR A 122 10426 10892 14010 920 -3185 1329 A O ATOM 808 CB THR A 122 67.156 -14.959 9.313 1.00 92.06 A C ANISOU 808 CB THR A 122 9625 11346 14009 1113 -3473 1273 A C ATOM 809 CG2 THR A 122 68.502 -15.200 8.629 1.00 90.13 A C ANISOU 809 CG2 THR A 122 9012 11329 13905 1333 -3526 1177 A C ATOM 810 OG1 THR A 122 66.524 -13.796 8.754 1.00 85.28 A O ANISOU 810 OG1 THR A 122 8771 10557 13073 869 -3244 1214 A O ATOM 811 N LEU A 123 64.845 -15.868 11.137 1.00 80.69 A N ANISOU 811 N LEU A 123 8949 9352 12356 932 -3552 1525 A N ATOM 812 CA LEU A 123 63.623 -15.496 11.839 1.00 84.20 A C ANISOU 812 CA LEU A 123 9691 9656 12646 699 -3477 1610 A C ATOM 813 C LEU A 123 63.129 -14.122 11.377 1.00 86.06 A C ANISOU 813 C LEU A 123 9874 10023 12803 465 -3258 1535 A C ATOM 814 O LEU A 123 61.928 -13.867 11.295 1.00 86.77 A O ANISOU 814 O LEU A 123 10151 9999 12818 325 -3101 1539 A O ATOM 815 CB LEU A 123 63.854 -15.476 13.349 1.00 85.31 A C ANISOU 815 CB LEU A 123 9983 9778 12654 622 -3684 1759 A C ATOM 816 CG LEU A 123 62.670 -14.996 14.194 1.00 87.58 A C ANISOU 816 CG LEU A 123 10566 9954 12757 373 -3606 1846 A C ATOM 817 CD1 LEU A 123 61.487 -15.941 14.053 1.00 87.14 A C ANISOU 817 CD1 LEU A 123 10760 9636 12712 396 -3525 1886 A C ATOM 818 CD2 LEU A 123 63.063 -14.851 15.654 1.00 85.84 A C ANISOU 818 CD2 LEU A 123 10467 9760 12389 293 -3813 1980 A C ATOM 819 N SER A 124 64.076 -13.244 11.071 1.00 84.90 A N ANISOU 819 N SER A 124 9468 10118 12673 427 -3253 1468 A N ATOM 820 CA SER A 124 63.782 -11.865 10.727 1.00 78.86 A C ANISOU 820 CA SER A 124 8659 9479 11826 202 -3074 1409 A C ATOM 821 C SER A 124 63.053 -11.754 9.383 1.00 83.68 A C ANISOU 821 C SER A 124 9240 10057 12499 214 -2835 1301 A C ATOM 822 O SER A 124 62.179 -10.901 9.191 1.00 71.99 A O ANISOU 822 O SER A 124 7866 8558 10928 39 -2666 1282 A O ATOM 823 CB SER A 124 65.089 -11.074 10.678 1.00 76.03 A C ANISOU 823 CB SER A 124 8017 9387 11484 160 -3142 1366 A C ATOM 824 OG SER A 124 64.840 -9.698 10.461 1.00 81.77 A O ANISOU 824 OG SER A 124 8737 10213 12117 -77 -2988 1322 A O ATOM 825 N GLU A 125 63.431 -12.616 8.449 1.00 88.58 A N ANISOU 825 N GLU A 125 9715 10672 13267 432 -2826 1226 A N ATOM 826 CA GLU A 125 62.860 -12.583 7.114 1.00 87.01 A C ANISOU 826 CA GLU A 125 9472 10461 13128 462 -2616 1115 A C ATOM 827 C GLU A 125 61.495 -13.273 7.106 1.00 80.98 A C ANISOU 827 C GLU A 125 8976 9451 12343 459 -2549 1143 A C ATOM 828 O GLU A 125 60.546 -12.794 6.477 1.00 73.32 A O ANISOU 828 O GLU A 125 8073 8454 11331 355 -2365 1097 A O ATOM 829 CB GLU A 125 63.831 -13.222 6.119 1.00 92.42 A C ANISOU 829 CB GLU A 125 9897 11250 13967 697 -2628 1011 A C ATOM 830 CG GLU A 125 65.136 -12.445 5.971 1.00 95.11 A C ANISOU 830 CG GLU A 125 9935 11875 14328 673 -2658 970 A C ATOM 831 CD GLU A 125 66.312 -13.322 5.569 1.00102.74 A C ANISOU 831 CD GLU A 125 10652 12946 15440 945 -2767 911 A C ATOM 832 OE1 GLU A 125 66.433 -14.451 6.095 1.00102.03 A O ANISOU 832 OE1 GLU A 125 10649 12711 15409 1137 -2934 961 A O ATOM 833 OE2 GLU A 125 67.124 -12.872 4.731 1.00107.92 A O1- ANISOU 833 OE2 GLU A 125 11027 13832 16148 970 -2683 815 A O1- ATOM 834 N ILE A 126 61.401 -14.388 7.821 1.00 81.36 A N ANISOU 834 N ILE A 126 9177 9323 12415 567 -2704 1226 A N ATOM 835 CA ILE A 126 60.125 -15.058 8.006 1.00 72.36 A C ANISOU 835 CA ILE A 126 8305 7949 11241 528 -2660 1274 A C ATOM 836 C ILE A 126 59.115 -14.048 8.547 1.00 75.64 A C ANISOU 836 C ILE A 126 8874 8368 11497 273 -2544 1325 A C ATOM 837 O ILE A 126 57.972 -14.001 8.090 1.00 75.66 A O ANISOU 837 O ILE A 126 8985 8289 11471 195 -2391 1297 A O ATOM 838 CB ILE A 126 60.244 -16.259 8.956 1.00 70.93 A C ANISOU 838 CB ILE A 126 8296 7579 11076 638 -2865 1388 A C ATOM 839 CG1 ILE A 126 61.085 -17.366 8.322 1.00 78.18 A C ANISOU 839 CG1 ILE A 126 9092 8452 12159 922 -2966 1325 A C ATOM 840 CG2 ILE A 126 58.871 -16.806 9.315 1.00 64.28 A C ANISOU 840 CG2 ILE A 126 7746 6509 10168 532 -2812 1458 A C ATOM 841 CD1 ILE A 126 61.144 -18.648 9.158 1.00 74.91 A C ANISOU 841 CD1 ILE A 126 8882 7811 11770 1054 -3169 1439 A C ATOM 842 N LYS A 127 59.541 -13.225 9.504 1.00 78.86 A N ANISOU 842 N LYS A 127 9286 8880 11799 149 -2618 1392 A N ATOM 843 CA LYS A 127 58.691 -12.148 10.012 1.00 77.23 A C ANISOU 843 CA LYS A 127 9216 8693 11436 -78 -2504 1423 A C ATOM 844 C LYS A 127 58.230 -11.232 8.887 1.00 77.27 A C ANISOU 844 C LYS A 127 9125 8789 11445 -146 -2286 1314 A C ATOM 845 O LYS A 127 57.060 -10.840 8.818 1.00 76.55 A O ANISOU 845 O LYS A 127 9171 8640 11275 -258 -2142 1313 A O ATOM 846 CB LYS A 127 59.428 -11.309 11.054 1.00 72.09 A C ANISOU 846 CB LYS A 127 8552 8163 10678 -193 -2619 1482 A C ATOM 847 CG LYS A 127 59.302 -11.830 12.457 1.00 72.26 A C ANISOU 847 CG LYS A 127 8781 8075 10598 -226 -2784 1617 A C ATOM 848 CD LYS A 127 60.091 -10.981 13.426 1.00 71.20 A C ANISOU 848 CD LYS A 127 8623 8076 10353 -340 -2907 1660 A C ATOM 849 CE LYS A 127 60.204 -11.688 14.765 1.00 77.82 A C ANISOU 849 CE LYS A 127 9644 8820 11105 -329 -3111 1799 A C ATOM 850 NZ LYS A 127 60.615 -10.751 15.842 1.00 85.90 A N1+ ANISOU 850 NZ LYS A 127 10718 9953 11967 -493 -3203 1844 A N1+ ATOM 851 N ARG A 128 59.162 -10.882 8.009 1.00 68.55 A N ANISOU 851 N ARG A 128 7781 7838 10426 -77 -2262 1224 A N ATOM 852 CA ARG A 128 58.864 -9.948 6.944 1.00 70.59 A C ANISOU 852 CA ARG A 128 7948 8195 10678 -145 -2067 1130 A C ATOM 853 C ARG A 128 57.868 -10.556 5.968 1.00 68.32 A C ANISOU 853 C ARG A 128 7713 7803 10445 -72 -1935 1072 A C ATOM 854 O ARG A 128 56.888 -9.908 5.584 1.00 60.39 A O ANISOU 854 O ARG A 128 6786 6788 9372 -173 -1779 1048 A O ATOM 855 CB ARG A 128 60.146 -9.537 6.227 1.00 73.67 A C ANISOU 855 CB ARG A 128 8065 8781 11144 -92 -2073 1055 A C ATOM 856 CG ARG A 128 59.949 -8.439 5.213 1.00 67.70 A C ANISOU 856 CG ARG A 128 7228 8135 10359 -189 -1880 976 A C ATOM 857 CD ARG A 128 59.510 -7.140 5.861 1.00 68.42 A C ANISOU 857 CD ARG A 128 7455 8240 10302 -406 -1824 1019 A C ATOM 858 NE ARG A 128 59.180 -6.157 4.831 1.00 67.48 A N ANISOU 858 NE ARG A 128 7298 8189 10154 -482 -1636 951 A N ATOM 859 CZ ARG A 128 57.959 -5.689 4.598 1.00 62.99 A C ANISOU 859 CZ ARG A 128 6888 7536 9508 -545 -1496 948 A C ATOM 860 NH1 ARG A 128 56.931 -6.081 5.348 1.00 62.69 A N1+ ANISOU 860 NH1 ARG A 128 7049 7356 9413 -558 -1511 1004 A N1+ ATOM 861 NH2 ARG A 128 57.772 -4.812 3.622 1.00 56.31 A N ANISOU 861 NH2 ARG A 128 6001 6757 8638 -595 -1342 892 A N ATOM 862 N VAL A 129 58.124 -11.804 5.577 1.00 67.03 A N ANISOU 862 N VAL A 129 7509 7559 10401 108 -2007 1045 A N ATOM 863 CA VAL A 129 57.230 -12.535 4.688 1.00 65.18 A C ANISOU 863 CA VAL A 129 7334 7209 10221 178 -1909 984 A C ATOM 864 C VAL A 129 55.791 -12.545 5.222 1.00 68.84 A C ANISOU 864 C VAL A 129 8031 7537 10588 42 -1846 1049 A C ATOM 865 O VAL A 129 54.851 -12.164 4.522 1.00 66.87 A O ANISOU 865 O VAL A 129 7806 7294 10307 -19 -1691 998 A O ATOM 866 CB VAL A 129 57.730 -13.982 4.451 1.00 67.45 A C ANISOU 866 CB VAL A 129 7598 7386 10643 391 -2029 960 A C ATOM 867 CG1 VAL A 129 56.602 -14.870 3.901 1.00 70.79 A C ANISOU 867 CG1 VAL A 129 8167 7631 11097 418 -1962 926 A C ATOM 868 CG2 VAL A 129 58.922 -13.978 3.507 1.00 57.86 A C ANISOU 868 CG2 VAL A 129 6123 6329 9532 548 -2025 853 A C ATOM 869 N MET A 130 55.625 -12.970 6.469 1.00 68.44 A N ANISOU 869 N MET A 130 8145 7377 10483 -6 -1966 1164 A N ATOM 870 CA MET A 130 54.305 -12.996 7.085 1.00 66.71 A C ANISOU 870 CA MET A 130 8137 7048 10160 -145 -1905 1233 A C ATOM 871 C MET A 130 53.665 -11.607 7.147 1.00 72.59 A C ANISOU 871 C MET A 130 8897 7902 10780 -303 -1756 1223 A C ATOM 872 O MET A 130 52.440 -11.464 7.060 1.00 72.41 A O ANISOU 872 O MET A 130 8975 7840 10696 -388 -1635 1223 A O ATOM 873 CB MET A 130 54.380 -13.616 8.478 1.00 64.76 A C ANISOU 873 CB MET A 130 8062 6685 9857 -176 -2064 1367 A C ATOM 874 CG MET A 130 54.656 -15.113 8.454 1.00 76.09 A C ANISOU 874 CG MET A 130 9554 7953 11404 -27 -2200 1393 A C ATOM 875 SD MET A 130 53.676 -15.957 7.191 1.00 77.23 A S ANISOU 875 SD MET A 130 9722 7978 11643 22 -2077 1296 A S ATOM 876 CE MET A 130 52.011 -15.556 7.718 1.00 52.82 A C ANISOU 876 CE MET A 130 6812 4850 8406 -211 -1936 1358 A C ATOM 877 N GLN A 131 54.499 -10.586 7.293 1.00 68.89 A N ANISOU 877 N GLN A 131 8328 7571 10274 -340 -1768 1211 A N ATOM 878 CA GLN A 131 54.020 -9.218 7.372 1.00 56.59 A C ANISOU 878 CA GLN A 131 6804 6100 8599 -479 -1640 1199 A C ATOM 879 C GLN A 131 53.445 -8.791 6.028 1.00 56.16 A C ANISOU 879 C GLN A 131 6665 6096 8576 -457 -1467 1101 A C ATOM 880 O GLN A 131 52.354 -8.220 5.956 1.00 51.90 A O ANISOU 880 O GLN A 131 6216 5550 7955 -535 -1339 1096 A O ATOM 881 CB GLN A 131 55.153 -8.282 7.784 1.00 64.36 A C ANISOU 881 CB GLN A 131 7704 7207 9545 -534 -1708 1204 A C ATOM 882 CG GLN A 131 54.700 -6.877 8.122 1.00 68.08 A C ANISOU 882 CG GLN A 131 8262 7730 9876 -688 -1602 1204 A C ATOM 883 CD GLN A 131 55.810 -6.046 8.725 1.00 67.29 A C ANISOU 883 CD GLN A 131 8112 7729 9725 -771 -1696 1218 A C ATOM 884 NE2 GLN A 131 55.581 -5.544 9.929 1.00 59.10 A N ANISOU 884 NE2 GLN A 131 7243 6664 8550 -891 -1739 1280 A N ATOM 885 OE1 GLN A 131 56.864 -5.859 8.116 1.00 64.40 A O ANISOU 885 OE1 GLN A 131 7558 7472 9438 -736 -1728 1171 A O ATOM 886 N MET A 132 54.175 -9.070 4.957 1.00 55.31 A N ANISOU 886 N MET A 132 6383 6049 8582 -343 -1464 1021 A N ATOM 887 CA MET A 132 53.696 -8.712 3.634 1.00 55.65 A C ANISOU 887 CA MET A 132 6349 6148 8647 -316 -1310 929 A C ATOM 888 C MET A 132 52.416 -9.499 3.308 1.00 60.15 A C ANISOU 888 C MET A 132 7018 6608 9228 -296 -1251 918 A C ATOM 889 O MET A 132 51.446 -8.936 2.813 1.00 55.32 A O ANISOU 889 O MET A 132 6439 6021 8559 -346 -1119 889 A O ATOM 890 CB MET A 132 54.781 -8.966 2.587 1.00 54.91 A C ANISOU 890 CB MET A 132 6051 6149 8664 -193 -1320 845 A C ATOM 891 CG MET A 132 55.999 -8.053 2.718 1.00 62.69 A C ANISOU 891 CG MET A 132 6904 7280 9635 -239 -1350 845 A C ATOM 892 SD MET A 132 57.362 -8.526 1.614 1.00 66.04 A S ANISOU 892 SD MET A 132 7060 7838 10193 -83 -1370 749 A S ATOM 893 CE MET A 132 57.133 -7.331 0.305 1.00 92.26 A C ANISOU 893 CE MET A 132 10309 11288 13459 -155 -1167 675 A C ATOM 894 N LEU A 133 52.423 -10.797 3.601 1.00 54.19 A N ANISOU 894 N LEU A 133 6314 5730 8545 -226 -1356 942 A N ATOM 895 CA LEU A 133 51.287 -11.656 3.312 1.00 55.40 A C ANISOU 895 CA LEU A 133 6562 5770 8717 -227 -1317 931 A C ATOM 896 C LEU A 133 50.039 -11.139 4.018 1.00 58.22 A C ANISOU 896 C LEU A 133 7058 6111 8949 -374 -1237 995 A C ATOM 897 O LEU A 133 49.008 -10.920 3.387 1.00 59.30 A O ANISOU 897 O LEU A 133 7199 6275 9059 -407 -1116 951 A O ATOM 898 CB LEU A 133 51.590 -13.101 3.715 1.00 57.89 A C ANISOU 898 CB LEU A 133 6947 5930 9120 -145 -1462 966 A C ATOM 899 CG LEU A 133 50.640 -14.207 3.247 1.00 68.96 A C ANISOU 899 CG LEU A 133 8437 7194 10570 -134 -1444 937 A C ATOM 900 CD1 LEU A 133 51.376 -15.525 3.133 1.00 71.41 A C ANISOU 900 CD1 LEU A 133 8761 7367 11003 13 -1581 921 A C ATOM 901 CD2 LEU A 133 49.466 -14.346 4.193 1.00 73.75 A C ANISOU 901 CD2 LEU A 133 9220 7719 11083 -290 -1424 1034 A C ATOM 902 N LEU A 134 50.146 -10.921 5.323 1.00 56.98 A N ANISOU 902 N LEU A 134 7011 5927 8712 -455 -1304 1094 A N ATOM 903 CA LEU A 134 49.032 -10.416 6.114 1.00 50.50 A C ANISOU 903 CA LEU A 134 6323 5104 7760 -588 -1225 1154 A C ATOM 904 C LEU A 134 48.584 -9.035 5.641 1.00 48.50 A C ANISOU 904 C LEU A 134 6024 4973 7429 -628 -1077 1102 A C ATOM 905 O LEU A 134 47.393 -8.703 5.684 1.00 51.05 A O ANISOU 905 O LEU A 134 6405 5314 7677 -689 -965 1104 A O ATOM 906 CB LEU A 134 49.396 -10.395 7.602 1.00 52.15 A C ANISOU 906 CB LEU A 134 6660 5271 7883 -661 -1332 1264 A C ATOM 907 CG LEU A 134 49.458 -11.783 8.257 1.00 57.75 A C ANISOU 907 CG LEU A 134 7477 5832 8634 -646 -1466 1345 A C ATOM 908 CD1 LEU A 134 50.024 -11.702 9.655 1.00 57.26 A C ANISOU 908 CD1 LEU A 134 7528 5746 8481 -701 -1591 1453 A C ATOM 909 CD2 LEU A 134 48.072 -12.449 8.268 1.00 50.72 A C ANISOU 909 CD2 LEU A 134 6690 4861 7718 -725 -1386 1368 A C ATOM 910 N ASN A 135 49.534 -8.242 5.166 1.00 45.12 A N ANISOU 910 N ASN A 135 5490 4632 7019 -590 -1075 1057 A N ATOM 911 CA ASN A 135 49.216 -6.920 4.640 1.00 43.90 A C ANISOU 911 CA ASN A 135 5310 4575 6796 -621 -943 1011 A C ATOM 912 C ASN A 135 48.458 -7.002 3.310 1.00 47.34 A C ANISOU 912 C ASN A 135 5669 5045 7272 -561 -831 932 A C ATOM 913 O ASN A 135 47.566 -6.204 3.043 1.00 50.23 A O ANISOU 913 O ASN A 135 6065 5458 7562 -587 -713 916 A O ATOM 914 CB ASN A 135 50.482 -6.080 4.476 1.00 43.74 A C ANISOU 914 CB ASN A 135 5202 4634 6781 -622 -975 990 A C ATOM 915 CG ASN A 135 50.177 -4.593 4.332 1.00 54.88 A C ANISOU 915 CG ASN A 135 6656 6108 8088 -688 -859 973 A C ATOM 916 ND2 ASN A 135 50.944 -3.908 3.498 1.00 48.55 A N ANISOU 916 ND2 ASN A 135 5750 5385 7312 -676 -826 925 A N ATOM 917 OD1 ASN A 135 49.248 -4.076 4.954 1.00 55.87 A O ANISOU 917 OD1 ASN A 135 6911 6208 8108 -746 -795 1001 A O ATOM 918 N GLY A 136 48.822 -7.968 2.476 1.00 47.79 A N ANISOU 918 N GLY A 136 5631 5081 7444 -470 -872 881 A N ATOM 919 CA GLY A 136 48.073 -8.244 1.268 1.00 47.77 A C ANISOU 919 CA GLY A 136 5571 5102 7476 -419 -786 804 A C ATOM 920 C GLY A 136 46.641 -8.661 1.593 1.00 54.16 A C ANISOU 920 C GLY A 136 6472 5865 8241 -480 -742 830 A C ATOM 921 O GLY A 136 45.679 -8.135 1.023 1.00 54.48 A O ANISOU 921 O GLY A 136 6498 5972 8231 -489 -633 797 A O ATOM 922 N LEU A 137 46.494 -9.602 2.519 1.00 43.00 A N ANISOU 922 N LEU A 137 5150 4345 6843 -524 -827 895 A N ATOM 923 CA LEU A 137 45.174 -10.049 2.939 1.00 48.35 A C ANISOU 923 CA LEU A 137 5912 4985 7474 -609 -784 930 A C ATOM 924 C LEU A 137 44.321 -8.898 3.470 1.00 53.18 A C ANISOU 924 C LEU A 137 6569 5685 7953 -680 -673 961 A C ATOM 925 O LEU A 137 43.147 -8.779 3.133 1.00 56.01 A O ANISOU 925 O LEU A 137 6910 6097 8272 -707 -578 939 A O ATOM 926 CB LEU A 137 45.288 -11.156 3.987 1.00 50.77 A C ANISOU 926 CB LEU A 137 6335 5155 7800 -662 -897 1015 A C ATOM 927 CG LEU A 137 45.739 -12.490 3.387 1.00 54.59 A C ANISOU 927 CG LEU A 137 6802 5525 8416 -587 -994 976 A C ATOM 928 CD1 LEU A 137 45.910 -13.539 4.480 1.00 54.72 A C ANISOU 928 CD1 LEU A 137 6961 5385 8445 -633 -1118 1076 A C ATOM 929 CD2 LEU A 137 44.763 -12.966 2.291 1.00 47.96 A C ANISOU 929 CD2 LEU A 137 5914 4693 7614 -590 -922 892 A C ATOM 930 N TYR A 138 44.913 -8.043 4.293 1.00 51.15 A N ANISOU 930 N TYR A 138 6366 5444 7624 -706 -687 1007 A N ATOM 931 CA TYR A 138 44.175 -6.924 4.849 1.00 41.91 A C ANISOU 931 CA TYR A 138 5260 4340 6322 -757 -584 1028 A C ATOM 932 C TYR A 138 43.604 -6.095 3.710 1.00 49.55 A C ANISOU 932 C TYR A 138 6144 5405 7278 -695 -466 953 A C ATOM 933 O TYR A 138 42.450 -5.661 3.750 1.00 47.14 A O ANISOU 933 O TYR A 138 5854 5159 6898 -708 -364 948 A O ATOM 934 CB TYR A 138 45.097 -6.055 5.704 1.00 47.18 A C ANISOU 934 CB TYR A 138 5997 5006 6922 -787 -627 1065 A C ATOM 935 CG TYR A 138 44.486 -4.726 6.070 1.00 53.29 A C ANISOU 935 CG TYR A 138 6843 5840 7565 -813 -515 1061 A C ATOM 936 CD1 TYR A 138 43.750 -4.572 7.251 1.00 55.20 A C ANISOU 936 CD1 TYR A 138 7209 6077 7688 -887 -478 1114 A C ATOM 937 CD2 TYR A 138 44.639 -3.618 5.236 1.00 49.40 A C ANISOU 937 CD2 TYR A 138 6306 5404 7059 -760 -442 1004 A C ATOM 938 CE1 TYR A 138 43.183 -3.343 7.588 1.00 54.56 A C ANISOU 938 CE1 TYR A 138 7202 6045 7482 -890 -370 1098 A C ATOM 939 CE2 TYR A 138 44.071 -2.388 5.563 1.00 57.97 A C ANISOU 939 CE2 TYR A 138 7480 6522 8024 -768 -343 997 A C ATOM 940 CZ TYR A 138 43.343 -2.259 6.741 1.00 64.80 A C ANISOU 940 CZ TYR A 138 8464 7380 8777 -824 -307 1038 A C ATOM 941 OH TYR A 138 42.779 -1.043 7.071 1.00 80.67 A O ANISOU 941 OH TYR A 138 10569 9417 10666 -810 -205 1019 A O ATOM 942 N TYR A 139 44.429 -5.872 2.692 1.00 42.21 A N ANISOU 942 N TYR A 139 5122 4499 6416 -622 -481 896 A N ATOM 943 CA TYR A 139 44.016 -5.091 1.537 1.00 39.91 A C ANISOU 943 CA TYR A 139 4763 4294 6107 -558 -382 832 A C ATOM 944 C TYR A 139 42.897 -5.755 0.730 1.00 49.35 A C ANISOU 944 C TYR A 139 5893 5526 7332 -531 -336 788 A C ATOM 945 O TYR A 139 41.905 -5.106 0.405 1.00 50.37 A O ANISOU 945 O TYR A 139 6013 5732 7394 -510 -243 771 A O ATOM 946 CB TYR A 139 45.205 -4.807 0.617 1.00 39.42 A C ANISOU 946 CB TYR A 139 4616 4257 6104 -501 -406 787 A C ATOM 947 CG TYR A 139 44.789 -4.119 -0.644 1.00 37.53 A C ANISOU 947 CG TYR A 139 4318 4101 5841 -437 -310 729 A C ATOM 948 CD1 TYR A 139 44.553 -2.748 -0.654 1.00 36.20 A C ANISOU 948 CD1 TYR A 139 4209 3970 5574 -437 -229 741 A C ATOM 949 CD2 TYR A 139 44.596 -4.834 -1.826 1.00 27.90 A C ANISOU 949 CD2 TYR A 139 3000 2914 4688 -373 -306 662 A C ATOM 950 CE1 TYR A 139 44.153 -2.091 -1.817 1.00 33.49 A C ANISOU 950 CE1 TYR A 139 3829 3696 5198 -370 -148 700 A C ATOM 951 CE2 TYR A 139 44.189 -4.187 -2.999 1.00 35.76 A C ANISOU 951 CE2 TYR A 139 3950 3993 5644 -314 -224 615 A C ATOM 952 CZ TYR A 139 43.964 -2.816 -2.982 1.00 44.88 A C ANISOU 952 CZ TYR A 139 5166 5186 6700 -310 -147 641 A C ATOM 953 OH TYR A 139 43.572 -2.154 -4.127 1.00 48.28 A O ANISOU 953 OH TYR A 139 5570 5691 7084 -244 -76 607 A O ATOM 954 N ILE A 140 43.052 -7.033 0.388 1.00 50.63 A N ANISOU 954 N ILE A 140 6012 5633 7591 -527 -408 765 A N ATOM 955 CA ILE A 140 42.044 -7.676 -0.453 1.00 57.05 A C ANISOU 955 CA ILE A 140 6763 6480 8431 -517 -375 711 A C ATOM 956 C ILE A 140 40.706 -7.782 0.288 1.00 55.60 A C ANISOU 956 C ILE A 140 6622 6323 8181 -602 -324 754 A C ATOM 957 O ILE A 140 39.649 -7.581 -0.298 1.00 50.03 A O ANISOU 957 O ILE A 140 5855 5713 7442 -591 -253 718 A O ATOM 958 CB ILE A 140 42.487 -9.051 -1.052 1.00 48.95 A C ANISOU 958 CB ILE A 140 5702 5373 7524 -494 -464 661 A C ATOM 959 CG1 ILE A 140 42.450 -10.155 -0.018 1.00 46.36 A C ANISOU 959 CG1 ILE A 140 5465 4918 7233 -575 -548 725 A C ATOM 960 CG2 ILE A 140 43.883 -8.988 -1.678 1.00 52.19 A C ANISOU 960 CG2 ILE A 140 6056 5773 7999 -402 -509 617 A C ATOM 961 CD1 ILE A 140 42.404 -11.521 -0.652 1.00 56.40 A C ANISOU 961 CD1 ILE A 140 6727 6100 8605 -565 -616 669 A C ATOM 962 N HIS A 141 40.756 -8.058 1.585 1.00 50.00 A N ANISOU 962 N HIS A 141 6011 5545 7442 -685 -358 834 A N ATOM 963 CA HIS A 141 39.536 -8.154 2.374 1.00 48.72 A C ANISOU 963 CA HIS A 141 5886 5421 7203 -777 -297 880 A C ATOM 964 C HIS A 141 38.832 -6.798 2.513 1.00 49.56 A C ANISOU 964 C HIS A 141 5985 5651 7196 -740 -177 876 A C ATOM 965 O HIS A 141 37.621 -6.695 2.392 1.00 54.15 A O ANISOU 965 O HIS A 141 6512 6332 7731 -754 -96 862 A O ATOM 966 CB HIS A 141 39.854 -8.728 3.745 1.00 42.59 A C ANISOU 966 CB HIS A 141 5234 4543 6405 -875 -361 973 A C ATOM 967 CG HIS A 141 40.301 -10.152 3.705 1.00 52.93 A C ANISOU 967 CG HIS A 141 6574 5719 7819 -910 -477 987 A C ATOM 968 CD2 HIS A 141 40.130 -11.113 2.765 1.00 44.34 A C ANISOU 968 CD2 HIS A 141 5430 4590 6828 -900 -514 928 A C ATOM 969 ND1 HIS A 141 41.046 -10.725 4.714 1.00 52.63 A N ANISOU 969 ND1 HIS A 141 6651 5559 7788 -954 -579 1068 A N ATOM 970 CE1 HIS A 141 41.292 -11.989 4.407 1.00 51.61 A C ANISOU 970 CE1 HIS A 141 6539 5308 7760 -960 -672 1063 A C ATOM 971 NE2 HIS A 141 40.752 -12.247 3.229 1.00 46.55 A N ANISOU 971 NE2 HIS A 141 5801 4711 7177 -931 -632 973 A N ATOM 972 N ARG A 142 39.617 -5.766 2.777 1.00 49.45 A N ANISOU 972 N ARG A 142 6027 5624 7137 -692 -172 886 A N ATOM 973 CA ARG A 142 39.133 -4.402 2.858 1.00 45.54 A C ANISOU 973 CA ARG A 142 5555 5211 6537 -637 -69 876 A C ATOM 974 C ARG A 142 38.382 -4.057 1.579 1.00 48.94 A C ANISOU 974 C ARG A 142 5874 5746 6977 -545 -4 811 A C ATOM 975 O ARG A 142 37.486 -3.216 1.585 1.00 50.97 A O ANISOU 975 O ARG A 142 6125 6092 7151 -491 89 801 A O ATOM 976 CB ARG A 142 40.334 -3.476 3.052 1.00 51.12 A C ANISOU 976 CB ARG A 142 6339 5864 7222 -610 -98 884 A C ATOM 977 CG ARG A 142 40.010 -2.053 3.350 1.00 60.84 A C ANISOU 977 CG ARG A 142 7648 7131 8338 -566 -8 881 A C ATOM 978 CD ARG A 142 41.291 -1.251 3.502 1.00 85.56 A C ANISOU 978 CD ARG A 142 10857 10196 11457 -574 -53 888 A C ATOM 979 NE ARG A 142 41.026 0.172 3.679 1.00109.75 A N ANISOU 979 NE ARG A 142 14022 13268 14412 -530 31 877 A N ATOM 980 CZ ARG A 142 41.859 1.020 4.274 1.00122.41 A C ANISOU 980 CZ ARG A 142 15746 14807 15959 -572 8 890 A C ATOM 981 NH1 ARG A 142 43.017 0.583 4.753 1.00123.08 A N1+ ANISOU 981 NH1 ARG A 142 15841 14837 16086 -657 -100 918 A N1+ ATOM 982 NH2 ARG A 142 41.531 2.303 4.393 1.00124.56 A N ANISOU 982 NH2 ARG A 142 16130 15067 16129 -526 87 874 A N ATOM 983 N ASN A 143 38.745 -4.730 0.489 1.00 47.27 A N ANISOU 983 N ASN A 143 5576 5524 6860 -518 -58 763 A N ATOM 984 CA ASN A 143 38.122 -4.515 -0.810 1.00 45.68 A C ANISOU 984 CA ASN A 143 5270 5421 6663 -435 -16 700 A C ATOM 985 C ASN A 143 37.084 -5.563 -1.135 1.00 48.19 A C ANISOU 985 C ASN A 143 5497 5794 7017 -486 -22 672 A C ATOM 986 O ASN A 143 36.719 -5.732 -2.298 1.00 45.22 A O ANISOU 986 O ASN A 143 5028 5488 6666 -436 -23 610 A O ATOM 987 CB ASN A 143 39.177 -4.509 -1.913 1.00 45.67 A C ANISOU 987 CB ASN A 143 5234 5394 6726 -374 -61 653 A C ATOM 988 CG ASN A 143 39.894 -3.192 -2.012 1.00 51.79 A C ANISOU 988 CG ASN A 143 6068 6165 7445 -316 -25 666 A C ATOM 989 ND2 ASN A 143 41.066 -3.094 -1.373 1.00 45.59 A N ANISOU 989 ND2 ASN A 143 5347 5294 6680 -360 -75 698 A N ATOM 990 OD1 ASN A 143 39.405 -2.263 -2.655 1.00 58.58 A O ANISOU 990 OD1 ASN A 143 6921 7096 8241 -237 41 649 A O ATOM 991 N LYS A 144 36.636 -6.284 -0.108 1.00 49.92 A N ANISOU 991 N LYS A 144 5752 5983 7234 -599 -31 720 A N ATOM 992 CA LYS A 144 35.505 -7.194 -0.231 1.00 49.94 A C ANISOU 992 CA LYS A 144 5675 6047 7254 -682 -23 706 A C ATOM 993 C LYS A 144 35.825 -8.359 -1.137 1.00 52.73 A C ANISOU 993 C LYS A 144 5988 6335 7714 -709 -112 651 A C ATOM 994 O LYS A 144 34.966 -8.861 -1.846 1.00 57.43 A O ANISOU 994 O LYS A 144 6489 7007 8324 -738 -109 600 A O ATOM 995 CB LYS A 144 34.272 -6.452 -0.751 1.00 52.24 A C ANISOU 995 CB LYS A 144 5856 6519 7474 -616 68 671 A C ATOM 996 CG LYS A 144 33.895 -5.275 0.109 1.00 55.71 A C ANISOU 996 CG LYS A 144 6343 7020 7804 -565 162 711 A C ATOM 997 CD LYS A 144 33.802 -5.723 1.546 1.00 73.95 A C ANISOU 997 CD LYS A 144 8738 9279 10081 -693 175 782 A C ATOM 998 CE LYS A 144 33.723 -4.548 2.501 1.00 88.42 A C ANISOU 998 CE LYS A 144 10659 11136 11799 -639 259 816 A C ATOM 999 NZ LYS A 144 33.730 -5.008 3.926 1.00 95.12 A N1+ ANISOU 999 NZ LYS A 144 11608 11933 12599 -770 266 887 A N1+ ATOM 1000 N ILE A 145 37.072 -8.798 -1.107 1.00 52.49 A N ANISOU 1000 N ILE A 145 6027 6164 7753 -696 -194 655 A N ATOM 1001 CA ILE A 145 37.452 -9.980 -1.855 1.00 43.61 A C ANISOU 1001 CA ILE A 145 4887 4953 6731 -709 -280 598 A C ATOM 1002 C ILE A 145 37.954 -11.068 -0.924 1.00 47.99 A C ANISOU 1002 C ILE A 145 5550 5341 7344 -801 -365 656 A C ATOM 1003 O ILE A 145 38.683 -10.790 0.024 1.00 52.10 A O ANISOU 1003 O ILE A 145 6154 5795 7847 -801 -388 727 A O ATOM 1004 CB ILE A 145 38.536 -9.674 -2.889 1.00 38.42 A C ANISOU 1004 CB ILE A 145 4199 4283 6117 -581 -307 533 A C ATOM 1005 CG1 ILE A 145 38.095 -8.533 -3.820 1.00 40.04 A C ANISOU 1005 CG1 ILE A 145 4321 4641 6251 -488 -226 490 A C ATOM 1006 CG2 ILE A 145 38.877 -10.929 -3.657 1.00 44.13 A C ANISOU 1006 CG2 ILE A 145 4912 4918 6939 -581 -389 459 A C ATOM 1007 CD1 ILE A 145 36.886 -8.852 -4.645 1.00 44.58 A C ANISOU 1007 CD1 ILE A 145 4804 5326 6810 -504 -206 430 A C ATOM 1008 N LEU A 146 37.524 -12.299 -1.187 1.00 51.59 A N ANISOU 1008 N LEU A 146 6014 5727 7861 -885 -418 629 A N ATOM 1009 CA LEU A 146 38.085 -13.488 -0.568 1.00 47.98 A C ANISOU 1009 CA LEU A 146 5677 5079 7476 -950 -519 672 A C ATOM 1010 C LEU A 146 38.967 -14.144 -1.610 1.00 55.17 A C ANISOU 1010 C LEU A 146 6577 5897 8489 -847 -599 579 A C ATOM 1011 O LEU A 146 38.574 -14.276 -2.774 1.00 57.84 A O ANISOU 1011 O LEU A 146 6834 6299 8845 -817 -583 478 A O ATOM 1012 CB LEU A 146 36.974 -14.457 -0.186 1.00 56.80 A C ANISOU 1012 CB LEU A 146 6830 6162 8590 -1126 -522 701 A C ATOM 1013 CG LEU A 146 35.867 -13.912 0.709 1.00 52.15 A C ANISOU 1013 CG LEU A 146 6220 5704 7892 -1240 -422 776 A C ATOM 1014 CD1 LEU A 146 34.867 -15.012 1.003 1.00 49.41 A C ANISOU 1014 CD1 LEU A 146 5903 5320 7552 -1436 -430 803 A C ATOM 1015 CD2 LEU A 146 36.443 -13.347 2.001 1.00 50.89 A C ANISOU 1015 CD2 LEU A 146 6160 5508 7669 -1234 -413 880 A C ATOM 1016 N HIS A 147 40.167 -14.537 -1.205 1.00 52.90 A N ANISOU 1016 N HIS A 147 6366 5470 8262 -784 -685 607 A N ATOM 1017 CA HIS A 147 41.102 -15.155 -2.129 1.00 53.73 A C ANISOU 1017 CA HIS A 147 6457 5493 8465 -663 -756 514 A C ATOM 1018 C HIS A 147 40.734 -16.614 -2.402 1.00 53.18 A C ANISOU 1018 C HIS A 147 6470 5267 8470 -727 -831 472 A C ATOM 1019 O HIS A 147 40.771 -17.067 -3.544 1.00 49.01 A O ANISOU 1019 O HIS A 147 5902 4730 7988 -667 -845 354 A O ATOM 1020 CB HIS A 147 42.530 -15.074 -1.598 1.00 56.04 A C ANISOU 1020 CB HIS A 147 6783 5708 8800 -560 -827 556 A C ATOM 1021 CG HIS A 147 43.532 -15.736 -2.490 1.00 47.81 A C ANISOU 1021 CG HIS A 147 5714 4594 7859 -418 -893 458 A C ATOM 1022 CD2 HIS A 147 44.470 -15.218 -3.318 1.00 45.66 A C ANISOU 1022 CD2 HIS A 147 5334 4407 7608 -278 -872 382 A C ATOM 1023 ND1 HIS A 147 43.625 -17.106 -2.613 1.00 48.84 A N ANISOU 1023 ND1 HIS A 147 5937 4545 8077 -410 -987 423 A N ATOM 1024 CE1 HIS A 147 44.581 -17.404 -3.475 1.00 56.09 A C ANISOU 1024 CE1 HIS A 147 6802 5443 9067 -252 -1019 322 A C ATOM 1025 NE2 HIS A 147 45.115 -16.275 -3.910 1.00 55.98 A N ANISOU 1025 NE2 HIS A 147 6657 5600 9014 -175 -947 298 A N ATOM 1026 N ARG A 148 40.407 -17.346 -1.342 1.00 57.46 A N ANISOU 1026 N ARG A 148 7141 5677 9014 -853 -882 569 A N ATOM 1027 CA ARG A 148 39.835 -18.690 -1.459 1.00 59.66 A C ANISOU 1027 CA ARG A 148 7525 5797 9346 -964 -945 548 A C ATOM 1028 C ARG A 148 40.783 -19.757 -2.005 1.00 64.31 A C ANISOU 1028 C ARG A 148 8196 6189 10050 -844 -1058 472 A C ATOM 1029 O ARG A 148 40.379 -20.889 -2.222 1.00 78.09 A O ANISOU 1029 O ARG A 148 10047 7778 11844 -924 -1117 437 A O ATOM 1030 CB ARG A 148 38.563 -18.666 -2.312 1.00 58.50 A C ANISOU 1030 CB ARG A 148 7286 5778 9164 -1067 -874 467 A C ATOM 1031 CG ARG A 148 37.462 -17.816 -1.741 1.00 56.56 A C ANISOU 1031 CG ARG A 148 6962 5717 8811 -1189 -767 538 A C ATOM 1032 CD ARG A 148 36.109 -18.326 -2.174 1.00 60.90 A C ANISOU 1032 CD ARG A 148 7468 6329 9342 -1356 -739 495 A C ATOM 1033 NE ARG A 148 35.891 -18.188 -3.605 1.00 62.74 A N ANISOU 1033 NE ARG A 148 7584 6666 9587 -1281 -728 353 A N ATOM 1034 CZ ARG A 148 34.766 -18.548 -4.209 1.00 63.33 A C ANISOU 1034 CZ ARG A 148 7592 6827 9644 -1407 -713 291 A C ATOM 1035 NH1 ARG A 148 33.781 -19.062 -3.489 1.00 64.90 A N1+ ANISOU 1035 NH1 ARG A 148 7820 7021 9818 -1621 -701 359 A N1+ ATOM 1036 NH2 ARG A 148 34.626 -18.396 -5.520 1.00 60.77 A N ANISOU 1036 NH2 ARG A 148 7169 6603 9319 -1329 -713 162 A N ATOM 1037 N ASP A 149 42.037 -19.408 -2.236 1.00 59.38 A N ANISOU 1037 N ASP A 149 7523 5572 9467 -655 -1087 441 A N ATOM 1038 CA ASP A 149 42.987 -20.403 -2.683 1.00 59.28 A C ANISOU 1038 CA ASP A 149 7579 5383 9563 -514 -1190 368 A C ATOM 1039 C ASP A 149 44.366 -20.175 -2.050 1.00 60.86 A C ANISOU 1039 C ASP A 149 7776 5549 9799 -362 -1256 428 A C ATOM 1040 O ASP A 149 45.401 -20.342 -2.695 1.00 59.41 A O ANISOU 1040 O ASP A 149 7536 5353 9686 -178 -1292 341 A O ATOM 1041 CB ASP A 149 43.058 -20.440 -4.211 1.00 63.71 A C ANISOU 1041 CB ASP A 149 8040 6016 10151 -410 -1152 195 A C ATOM 1042 CG ASP A 149 43.621 -21.757 -4.739 1.00 72.97 A C ANISOU 1042 CG ASP A 149 9323 6973 11429 -306 -1254 97 A C ATOM 1043 OD1 ASP A 149 43.618 -22.762 -3.988 1.00 68.19 A O ANISOU 1043 OD1 ASP A 149 8894 6142 10873 -358 -1353 163 A O ATOM 1044 OD2 ASP A 149 44.071 -21.780 -5.905 1.00 76.11 A O1- ANISOU 1044 OD2 ASP A 149 9643 7424 11853 -168 -1232 -48 A O1- ATOM 1045 N MET A 150 44.358 -19.809 -0.772 1.00 59.55 A N ANISOU 1045 N MET A 150 7667 5381 9580 -443 -1273 575 A N ATOM 1046 CA MET A 150 45.589 -19.617 -0.015 1.00 61.66 A C ANISOU 1046 CA MET A 150 7939 5619 9868 -327 -1354 647 A C ATOM 1047 C MET A 150 46.427 -20.885 0.019 1.00 75.15 A C ANISOU 1047 C MET A 150 9760 7105 11690 -196 -1498 632 A C ATOM 1048 O MET A 150 45.993 -21.919 0.538 1.00 82.24 A O ANISOU 1048 O MET A 150 10841 7798 12608 -279 -1575 691 A O ATOM 1049 CB MET A 150 45.273 -19.178 1.422 1.00 58.25 A C ANISOU 1049 CB MET A 150 7590 5198 9344 -464 -1358 809 A C ATOM 1050 CG MET A 150 44.853 -17.712 1.568 1.00 53.91 A C ANISOU 1050 CG MET A 150 6925 4874 8684 -530 -1230 829 A C ATOM 1051 SD MET A 150 46.206 -16.551 1.244 1.00 74.96 A S ANISOU 1051 SD MET A 150 9426 7698 11356 -367 -1219 787 A S ATOM 1052 CE MET A 150 45.978 -16.247 -0.494 1.00 66.75 A C ANISOU 1052 CE MET A 150 8233 6782 10347 -289 -1114 622 A C ATOM 1053 N LYS A 151 47.627 -20.803 -0.547 1.00 76.33 A N ANISOU 1053 N LYS A 151 9799 7294 11909 11 -1532 551 A N ATOM 1054 CA LYS A 151 48.620 -21.864 -0.408 1.00 76.17 A C ANISOU 1054 CA LYS A 151 9861 7086 11996 183 -1676 542 A C ATOM 1055 C LYS A 151 50.000 -21.347 -0.786 1.00 71.44 A C ANISOU 1055 C LYS A 151 9076 6624 11443 393 -1689 482 A C ATOM 1056 O LYS A 151 50.118 -20.361 -1.508 1.00 73.58 A O ANISOU 1056 O LYS A 151 9170 7110 11679 406 -1575 410 A O ATOM 1057 CB LYS A 151 48.246 -23.096 -1.238 1.00 80.21 A C ANISOU 1057 CB LYS A 151 10486 7406 12584 220 -1708 431 A C ATOM 1058 CG LYS A 151 48.120 -22.858 -2.734 1.00 75.54 A C ANISOU 1058 CG LYS A 151 9756 6941 12003 285 -1604 250 A C ATOM 1059 CD LYS A 151 47.406 -24.032 -3.409 1.00 75.28 A C ANISOU 1059 CD LYS A 151 9873 6714 12015 245 -1630 152 A C ATOM 1060 CE LYS A 151 47.721 -24.094 -4.902 1.00 77.19 A C ANISOU 1060 CE LYS A 151 10004 7035 12290 393 -1572 -48 A C ATOM 1061 NZ LYS A 151 46.682 -24.844 -5.669 1.00 73.01 A N1+ ANISOU 1061 NZ LYS A 151 9586 6397 11757 280 -1558 -152 A N1+ ATOM 1062 N ALA A 152 51.039 -22.009 -0.290 1.00 72.48 A N ANISOU 1062 N ALA A 152 9248 6639 11652 554 -1830 516 A N ATOM 1063 CA ALA A 152 52.413 -21.561 -0.507 1.00 74.92 A C ANISOU 1063 CA ALA A 152 9364 7094 12008 749 -1856 472 A C ATOM 1064 C ALA A 152 52.713 -21.285 -1.978 1.00 69.67 A C ANISOU 1064 C ALA A 152 8520 6577 11375 863 -1743 294 A C ATOM 1065 O ALA A 152 53.395 -20.317 -2.309 1.00 69.70 A O ANISOU 1065 O ALA A 152 8322 6804 11357 906 -1675 262 A O ATOM 1066 CB ALA A 152 53.400 -22.571 0.055 1.00 81.85 A C ANISOU 1066 CB ALA A 152 10317 7802 12982 941 -2034 510 A C ATOM 1067 N ALA A 153 52.193 -22.125 -2.860 1.00 66.61 A N ANISOU 1067 N ALA A 153 8215 6064 11028 897 -1721 178 A N ATOM 1068 CA ALA A 153 52.468 -21.967 -4.284 1.00 72.58 A C ANISOU 1068 CA ALA A 153 8823 6951 11802 1012 -1618 1 A C ATOM 1069 C ALA A 153 51.770 -20.748 -4.910 1.00 72.41 A C ANISOU 1069 C ALA A 153 8683 7154 11674 861 -1455 -24 A C ATOM 1070 O ALA A 153 52.149 -20.301 -5.993 1.00 76.78 A O ANISOU 1070 O ALA A 153 9084 7873 12216 944 -1358 -143 A O ATOM 1071 CB ALA A 153 52.121 -23.243 -5.037 1.00 65.33 A C ANISOU 1071 CB ALA A 153 8048 5825 10949 1092 -1652 -125 A C ATOM 1072 N ASN A 154 50.762 -20.211 -4.226 1.00 67.06 A N ANISOU 1072 N ASN A 154 8080 6486 10912 648 -1423 90 A N ATOM 1073 CA ASN A 154 50.078 -18.998 -4.691 1.00 63.07 A C ANISOU 1073 CA ASN A 154 7475 6186 10303 518 -1280 83 A C ATOM 1074 C ASN A 154 50.642 -17.718 -4.088 1.00 64.60 A C ANISOU 1074 C ASN A 154 7551 6555 10439 483 -1244 175 A C ATOM 1075 O ASN A 154 50.133 -16.630 -4.349 1.00 66.55 A O ANISOU 1075 O ASN A 154 7735 6957 10596 383 -1133 185 A O ATOM 1076 CB ASN A 154 48.585 -19.071 -4.399 1.00 57.66 A C ANISOU 1076 CB ASN A 154 6918 5439 9554 316 -1249 136 A C ATOM 1077 CG ASN A 154 47.873 -20.003 -5.328 1.00 68.55 A C ANISOU 1077 CG ASN A 154 8372 6714 10961 310 -1244 17 A C ATOM 1078 ND2 ASN A 154 46.668 -20.432 -4.946 1.00 62.92 A N ANISOU 1078 ND2 ASN A 154 7789 5901 10218 135 -1254 66 A N ATOM 1079 OD1 ASN A 154 48.401 -20.346 -6.387 1.00 75.70 A O ANISOU 1079 OD1 ASN A 154 9218 7636 11909 455 -1231 -123 A O ATOM 1080 N VAL A 155 51.671 -17.860 -3.255 1.00 53.57 A N ANISOU 1080 N VAL A 155 6138 5126 9091 564 -1348 243 A N ATOM 1081 CA VAL A 155 52.394 -16.716 -2.721 1.00 53.53 A C ANISOU 1081 CA VAL A 155 6014 5286 9038 538 -1332 314 A C ATOM 1082 C VAL A 155 53.672 -16.528 -3.532 1.00 64.99 A C ANISOU 1082 C VAL A 155 7267 6881 10545 704 -1312 215 A C ATOM 1083 O VAL A 155 54.549 -17.394 -3.539 1.00 72.29 A O ANISOU 1083 O VAL A 155 8161 7739 11567 874 -1408 176 A O ATOM 1084 CB VAL A 155 52.731 -16.926 -1.235 1.00 58.35 A C ANISOU 1084 CB VAL A 155 6720 5798 9652 505 -1467 457 A C ATOM 1085 CG1 VAL A 155 53.499 -15.746 -0.680 1.00 52.30 A C ANISOU 1085 CG1 VAL A 155 5835 5202 8832 464 -1461 520 A C ATOM 1086 CG2 VAL A 155 51.463 -17.169 -0.437 1.00 57.36 A C ANISOU 1086 CG2 VAL A 155 6791 5540 9464 334 -1474 554 A C ATOM 1087 N LEU A 156 53.771 -15.407 -4.235 1.00 59.81 A N ANISOU 1087 N LEU A 156 6478 6424 9824 659 -1183 176 A N ATOM 1088 CA LEU A 156 54.945 -15.138 -5.058 1.00 60.37 A C ANISOU 1088 CA LEU A 156 6347 6660 9930 788 -1140 84 A C ATOM 1089 C LEU A 156 55.931 -14.221 -4.354 1.00 73.94 A C ANISOU 1089 C LEU A 156 7943 8520 11630 748 -1166 164 A C ATOM 1090 O LEU A 156 55.552 -13.424 -3.493 1.00 77.17 A O ANISOU 1090 O LEU A 156 8419 8936 11964 593 -1170 273 A O ATOM 1091 CB LEU A 156 54.535 -14.511 -6.386 1.00 61.40 A C ANISOU 1091 CB LEU A 156 6408 6929 9993 761 -979 -12 A C ATOM 1092 CG LEU A 156 53.552 -15.356 -7.196 1.00 68.06 A C ANISOU 1092 CG LEU A 156 7359 7658 10842 788 -952 -106 A C ATOM 1093 CD1 LEU A 156 53.362 -14.779 -8.584 1.00 64.04 A C ANISOU 1093 CD1 LEU A 156 6763 7307 10262 792 -807 -210 A C ATOM 1094 CD2 LEU A 156 54.040 -16.785 -7.270 1.00 68.34 A C ANISOU 1094 CD2 LEU A 156 7433 7541 10994 963 -1056 -182 A C ATOM 1095 N ILE A 157 57.202 -14.343 -4.724 1.00 82.33 A N ANISOU 1095 N ILE A 157 8821 9702 12759 889 -1185 102 A N ATOM 1096 CA ILE A 157 58.232 -13.433 -4.243 1.00 76.48 A C ANISOU 1096 CA ILE A 157 7925 9134 12000 841 -1201 158 A C ATOM 1097 C ILE A 157 59.066 -12.956 -5.423 1.00 74.90 A C ANISOU 1097 C ILE A 157 7503 9154 11800 901 -1081 51 A C ATOM 1098 O ILE A 157 59.544 -13.767 -6.211 1.00 88.11 A O ANISOU 1098 O ILE A 157 9087 10846 13547 1084 -1071 -63 A O ATOM 1099 CB ILE A 157 59.110 -14.094 -3.181 1.00 68.32 A C ANISOU 1099 CB ILE A 157 6865 8044 11048 941 -1383 219 A C ATOM 1100 CG1 ILE A 157 58.229 -14.612 -2.045 1.00 65.77 A C ANISOU 1100 CG1 ILE A 157 6784 7496 10709 871 -1493 330 A C ATOM 1101 CG2 ILE A 157 60.120 -13.102 -2.641 1.00 65.43 A C ANISOU 1101 CG2 ILE A 157 6336 7869 10655 862 -1409 277 A C ATOM 1102 CD1 ILE A 157 58.978 -14.962 -0.794 1.00 71.72 A C ANISOU 1102 CD1 ILE A 157 7545 8205 11500 915 -1676 430 A C ATOM 1103 N THR A 158 59.203 -11.640 -5.566 1.00 65.78 A N ANISOU 1103 N THR A 158 6277 8160 10557 745 -982 87 A N ATOM 1104 CA THR A 158 59.940 -11.066 -6.695 1.00 73.76 A C ANISOU 1104 CA THR A 158 7090 9389 11545 763 -850 2 A C ATOM 1105 C THR A 158 61.441 -11.084 -6.451 1.00 82.39 A C ANISOU 1105 C THR A 158 7947 10649 12708 838 -911 -9 A C ATOM 1106 O THR A 158 61.893 -11.239 -5.310 1.00 73.57 A O ANISOU 1106 O THR A 158 6825 9494 11634 836 -1058 71 A O ATOM 1107 CB THR A 158 59.531 -9.606 -6.989 1.00 67.36 A C ANISOU 1107 CB THR A 158 6308 8679 10606 555 -718 51 A C ATOM 1108 CG2 THR A 158 58.085 -9.530 -7.345 1.00 59.46 A C ANISOU 1108 CG2 THR A 158 5505 7553 9535 499 -651 53 A C ATOM 1109 OG1 THR A 158 59.788 -8.786 -5.838 1.00 65.98 A O ANISOU 1109 OG1 THR A 158 6158 8514 10397 402 -786 167 A O ATOM 1110 N ARG A 159 62.206 -10.909 -7.527 1.00 92.02 A N ANISOU 1110 N ARG A 159 8965 12069 13929 901 -796 -107 A N ATOM 1111 CA ARG A 159 63.661 -10.866 -7.436 1.00 94.44 A C ANISOU 1111 CA ARG A 159 9003 12582 14297 969 -831 -130 A C ATOM 1112 C ARG A 159 64.088 -9.858 -6.383 1.00 83.13 A C ANISOU 1112 C ARG A 159 7538 11223 12827 770 -899 -6 A C ATOM 1113 O ARG A 159 65.182 -9.961 -5.836 1.00 90.46 A O ANISOU 1113 O ARG A 159 8280 12273 13818 815 -1000 8 A O ATOM 1114 CB ARG A 159 64.299 -10.510 -8.785 1.00113.97 A C ANISOU 1114 CB ARG A 159 11271 15294 16739 997 -655 -239 A C ATOM 1115 CG ARG A 159 64.410 -11.673 -9.775 1.00135.90 A C ANISOU 1115 CG ARG A 159 13994 18062 19578 1253 -613 -392 A C ATOM 1116 CD ARG A 159 65.107 -11.242 -11.068 1.00154.31 A C ANISOU 1116 CD ARG A 159 16112 20660 21858 1267 -427 -495 A C ATOM 1117 NE ARG A 159 64.595 -11.956 -12.239 1.00168.87 A N ANISOU 1117 NE ARG A 159 18025 22455 23683 1415 -329 -631 A N ATOM 1118 CZ ARG A 159 64.850 -11.613 -13.500 1.00177.96 A C ANISOU 1118 CZ ARG A 159 19066 23798 24754 1416 -149 -724 A C ATOM 1119 NH1 ARG A 159 65.620 -10.563 -13.764 1.00181.48 A N1+ ANISOU 1119 NH1 ARG A 159 19325 24496 25135 1267 -40 -688 A N1+ ATOM 1120 NH2 ARG A 159 64.335 -12.320 -14.501 1.00177.42 A N ANISOU 1120 NH2 ARG A 159 19083 23669 24661 1552 -77 -852 A N ATOM 1121 N ASP A 160 63.221 -8.893 -6.092 1.00 65.97 A N ANISOU 1121 N ASP A 160 5546 8974 10546 556 -851 78 A N ATOM 1122 CA ASP A 160 63.553 -7.842 -5.138 1.00 71.77 A C ANISOU 1122 CA ASP A 160 6282 9762 11225 348 -903 185 A C ATOM 1123 C ASP A 160 62.964 -8.066 -3.747 1.00 77.43 A C ANISOU 1123 C ASP A 160 7200 10280 11938 307 -1060 288 A C ATOM 1124 O ASP A 160 62.987 -7.169 -2.902 1.00 78.43 A O ANISOU 1124 O ASP A 160 7391 10412 11996 123 -1100 376 A O ATOM 1125 CB ASP A 160 63.136 -6.484 -5.686 1.00 84.63 A C ANISOU 1125 CB ASP A 160 7977 11451 12727 134 -745 211 A C ATOM 1126 CG ASP A 160 63.753 -6.200 -7.036 1.00107.16 A C ANISOU 1126 CG ASP A 160 10640 14512 15563 151 -585 124 A C ATOM 1127 OD1 ASP A 160 64.430 -7.104 -7.580 1.00107.06 A O ANISOU 1127 OD1 ASP A 160 10444 14596 15637 343 -587 29 A O ATOM 1128 OD2 ASP A 160 63.566 -5.078 -7.555 1.00118.76 A O1- ANISOU 1128 OD2 ASP A 160 12151 16046 16927 -23 -455 149 A O1- ATOM 1129 N GLY A 161 62.434 -9.264 -3.517 1.00 74.69 A N ANISOU 1129 N GLY A 161 6965 9756 11658 470 -1145 275 A N ATOM 1130 CA GLY A 161 61.986 -9.658 -2.196 1.00 67.78 A C ANISOU 1130 CA GLY A 161 6268 8701 10784 450 -1300 374 A C ATOM 1131 C GLY A 161 60.630 -9.106 -1.816 1.00 68.11 A C ANISOU 1131 C GLY A 161 6565 8593 10721 291 -1246 441 A C ATOM 1132 O GLY A 161 60.321 -8.978 -0.632 1.00 75.79 A O ANISOU 1132 O GLY A 161 7678 9466 11651 203 -1346 538 A O ATOM 1133 N VAL A 162 59.823 -8.764 -2.814 1.00 60.83 A N ANISOU 1133 N VAL A 162 5699 7664 9749 260 -1089 390 A N ATOM 1134 CA VAL A 162 58.449 -8.340 -2.559 1.00 59.73 A C ANISOU 1134 CA VAL A 162 5785 7391 9518 144 -1032 441 A C ATOM 1135 C VAL A 162 57.478 -9.515 -2.732 1.00 61.51 A C ANISOU 1135 C VAL A 162 6139 7445 9788 254 -1052 412 A C ATOM 1136 O VAL A 162 57.417 -10.128 -3.800 1.00 61.38 A O ANISOU 1136 O VAL A 162 6064 7439 9818 374 -993 314 A O ATOM 1137 CB VAL A 162 58.032 -7.180 -3.477 1.00 59.63 A C ANISOU 1137 CB VAL A 162 5777 7469 9410 34 -860 416 A C ATOM 1138 CG1 VAL A 162 56.654 -6.687 -3.102 1.00 47.83 A C ANISOU 1138 CG1 VAL A 162 4501 5851 7821 -69 -813 473 A C ATOM 1139 CG2 VAL A 162 59.048 -6.040 -3.394 1.00 58.01 A C ANISOU 1139 CG2 VAL A 162 5451 7428 9163 -93 -835 441 A C ATOM 1140 N LEU A 163 56.743 -9.831 -1.666 1.00 65.88 A N ANISOU 1140 N LEU A 163 6870 7842 10318 203 -1135 496 A N ATOM 1141 CA LEU A 163 55.729 -10.894 -1.672 1.00 59.42 A C ANISOU 1141 CA LEU A 163 6197 6850 9531 260 -1158 487 A C ATOM 1142 C LEU A 163 54.418 -10.426 -2.315 1.00 58.72 A C ANISOU 1142 C LEU A 163 6204 6746 9363 178 -1020 464 A C ATOM 1143 O LEU A 163 53.930 -9.333 -2.020 1.00 52.74 A O ANISOU 1143 O LEU A 163 5505 6030 8505 46 -952 516 A O ATOM 1144 CB LEU A 163 55.469 -11.377 -0.247 1.00 50.95 A C ANISOU 1144 CB LEU A 163 5276 5632 8450 217 -1294 597 A C ATOM 1145 CG LEU A 163 54.445 -12.500 -0.063 1.00 55.51 A C ANISOU 1145 CG LEU A 163 6021 6016 9052 241 -1331 610 A C ATOM 1146 CD1 LEU A 163 54.782 -13.337 1.175 1.00 57.18 A C ANISOU 1146 CD1 LEU A 163 6333 6095 9298 271 -1504 705 A C ATOM 1147 CD2 LEU A 163 53.031 -11.949 0.016 1.00 46.64 A C ANISOU 1147 CD2 LEU A 163 5030 4863 7827 95 -1224 641 A C ATOM 1148 N LYS A 164 53.867 -11.250 -3.203 1.00 60.13 A N ANISOU 1148 N LYS A 164 6397 6867 9583 264 -984 381 A N ATOM 1149 CA LYS A 164 52.616 -10.924 -3.893 1.00 55.60 A C ANISOU 1149 CA LYS A 164 5894 6293 8939 202 -869 351 A C ATOM 1150 C LYS A 164 51.663 -12.078 -3.749 1.00 56.19 A C ANISOU 1150 C LYS A 164 6096 6204 9051 216 -918 343 A C ATOM 1151 O LYS A 164 52.037 -13.231 -4.008 1.00 56.50 A O ANISOU 1151 O LYS A 164 6129 6155 9183 333 -990 285 A O ATOM 1152 CB LYS A 164 52.832 -10.706 -5.392 1.00 51.11 A C ANISOU 1152 CB LYS A 164 5207 5848 8366 273 -759 237 A C ATOM 1153 CG LYS A 164 54.036 -9.875 -5.765 1.00 54.71 A C ANISOU 1153 CG LYS A 164 5505 6471 8812 283 -713 221 A C ATOM 1154 CD LYS A 164 53.735 -8.410 -5.671 1.00 54.60 A C ANISOU 1154 CD LYS A 164 5521 6540 8683 141 -623 284 A C ATOM 1155 CE LYS A 164 54.755 -7.594 -6.440 1.00 54.63 A C ANISOU 1155 CE LYS A 164 5375 6719 8663 134 -543 250 A C ATOM 1156 NZ LYS A 164 54.482 -6.124 -6.258 1.00 59.38 A N1+ ANISOU 1156 NZ LYS A 164 6041 7369 9151 -15 -466 321 A N1+ ATOM 1157 N LEU A 165 50.430 -11.781 -3.351 1.00 51.06 A N ANISOU 1157 N LEU A 165 5562 5512 8325 97 -878 397 A N ATOM 1158 CA LEU A 165 49.369 -12.777 -3.429 1.00 51.85 A C ANISOU 1158 CA LEU A 165 5767 5487 8447 78 -897 379 A C ATOM 1159 C LEU A 165 49.031 -12.958 -4.906 1.00 52.21 A C ANISOU 1159 C LEU A 165 5748 5592 8499 141 -819 252 A C ATOM 1160 O LEU A 165 48.893 -11.985 -5.638 1.00 58.64 A O ANISOU 1160 O LEU A 165 6492 6546 9244 128 -715 222 A O ATOM 1161 CB LEU A 165 48.141 -12.328 -2.651 1.00 59.62 A C ANISOU 1161 CB LEU A 165 6860 6452 9341 -68 -859 465 A C ATOM 1162 CG LEU A 165 48.324 -12.025 -1.167 1.00 64.95 A C ANISOU 1162 CG LEU A 165 7619 7083 9977 -149 -920 590 A C ATOM 1163 CD1 LEU A 165 47.025 -11.503 -0.553 1.00 66.07 A C ANISOU 1163 CD1 LEU A 165 7852 7235 10015 -282 -851 655 A C ATOM 1164 CD2 LEU A 165 48.801 -13.271 -0.461 1.00 70.53 A C ANISOU 1164 CD2 LEU A 165 8401 7630 10765 -110 -1061 630 A C ATOM 1165 N ALA A 166 48.925 -14.202 -5.348 1.00 49.96 A N ANISOU 1165 N ALA A 166 5500 5193 8289 209 -873 177 A N ATOM 1166 CA ALA A 166 48.742 -14.488 -6.764 1.00 49.38 A C ANISOU 1166 CA ALA A 166 5372 5171 8220 280 -813 42 A C ATOM 1167 C ALA A 166 47.578 -15.440 -6.973 1.00 55.60 A C ANISOU 1167 C ALA A 166 6270 5837 9019 221 -838 2 A C ATOM 1168 O ALA A 166 47.045 -15.997 -6.004 1.00 53.51 A O ANISOU 1168 O ALA A 166 6122 5436 8772 133 -907 82 A O ATOM 1169 CB ALA A 166 50.018 -15.087 -7.341 1.00 49.19 A C ANISOU 1169 CB ALA A 166 5263 5146 8282 451 -849 -52 A C ATOM 1170 N ASP A 167 47.188 -15.636 -8.233 1.00 53.97 A N ANISOU 1170 N ASP A 167 6030 5684 8793 257 -786 -120 A N ATOM 1171 CA ASP A 167 46.167 -16.634 -8.559 1.00 65.04 A C ANISOU 1171 CA ASP A 167 7529 6972 10209 197 -821 -179 A C ATOM 1172 C ASP A 167 44.807 -16.342 -7.943 1.00 57.99 A C ANISOU 1172 C ASP A 167 6694 6088 9252 20 -801 -91 A C ATOM 1173 O ASP A 167 44.412 -16.980 -6.971 1.00 56.88 A O ANISOU 1173 O ASP A 167 6661 5806 9144 -71 -868 -14 A O ATOM 1174 CB ASP A 167 46.617 -18.025 -8.120 1.00 74.45 A C ANISOU 1174 CB ASP A 167 8834 7940 11513 253 -941 -198 A C ATOM 1175 CG ASP A 167 47.692 -18.588 -9.015 1.00102.76 A C ANISOU 1175 CG ASP A 167 12370 11510 15164 445 -956 -333 A C ATOM 1176 OD1 ASP A 167 47.424 -18.729 -10.229 1.00108.32 A O ANISOU 1176 OD1 ASP A 167 13044 12275 15837 482 -904 -465 A O ATOM 1177 OD2 ASP A 167 48.802 -18.881 -8.509 1.00114.13 A O1- ANISOU 1177 OD2 ASP A 167 13796 12889 16680 565 -1020 -309 A O1- ATOM 1178 N PHE A 168 44.089 -15.400 -8.540 1.00 48.64 A N ANISOU 1178 N PHE A 168 5435 5073 7972 -23 -708 -102 A N ATOM 1179 CA PHE A 168 42.768 -15.018 -8.064 1.00 58.69 A C ANISOU 1179 CA PHE A 168 6729 6394 9177 -168 -675 -31 A C ATOM 1180 C PHE A 168 41.645 -15.701 -8.840 1.00 54.73 A C ANISOU 1180 C PHE A 168 6239 5895 8660 -240 -683 -119 A C ATOM 1181 O PHE A 168 40.499 -15.266 -8.796 1.00 58.26 A O ANISOU 1181 O PHE A 168 6655 6443 9038 -339 -640 -88 A O ATOM 1182 CB PHE A 168 42.627 -13.485 -8.092 1.00 56.33 A C ANISOU 1182 CB PHE A 168 6349 6276 8778 -162 -577 25 A C ATOM 1183 CG PHE A 168 43.371 -12.807 -6.986 1.00 55.96 A C ANISOU 1183 CG PHE A 168 6319 6213 8730 -161 -578 136 A C ATOM 1184 CD1 PHE A 168 42.711 -12.407 -5.832 1.00 39.50 A C ANISOU 1184 CD1 PHE A 168 4287 4120 6600 -265 -566 246 A C ATOM 1185 CD2 PHE A 168 44.756 -12.635 -7.065 1.00 54.08 A C ANISOU 1185 CD2 PHE A 168 6042 5972 8534 -59 -594 124 A C ATOM 1186 CE1 PHE A 168 43.415 -11.794 -4.786 1.00 45.33 A C ANISOU 1186 CE1 PHE A 168 5056 4841 7327 -270 -575 341 A C ATOM 1187 CE2 PHE A 168 45.463 -12.030 -6.027 1.00 45.26 A C ANISOU 1187 CE2 PHE A 168 4938 4845 7413 -72 -610 222 A C ATOM 1188 CZ PHE A 168 44.792 -11.605 -4.887 1.00 45.42 A C ANISOU 1188 CZ PHE A 168 5029 4847 7381 -179 -604 329 A C ATOM 1189 N GLY A 169 41.979 -16.783 -9.533 1.00 50.22 A N ANISOU 1189 N GLY A 169 5712 5215 8154 -188 -742 -232 A N ATOM 1190 CA GLY A 169 41.027 -17.463 -10.394 1.00 42.70 A C ANISOU 1190 CA GLY A 169 4777 4263 7185 -257 -760 -338 A C ATOM 1191 C GLY A 169 39.893 -18.141 -9.655 1.00 48.28 A C ANISOU 1191 C GLY A 169 5561 4879 7903 -445 -804 -282 A C ATOM 1192 O GLY A 169 38.877 -18.486 -10.251 1.00 70.87 A O ANISOU 1192 O GLY A 169 8409 7787 10731 -545 -810 -348 A O ATOM 1193 N LEU A 170 40.071 -18.345 -8.357 1.00 53.38 A N ANISOU 1193 N LEU A 170 6287 5405 8590 -505 -837 -159 A N ATOM 1194 CA LEU A 170 39.016 -18.895 -7.519 1.00 56.16 A C ANISOU 1194 CA LEU A 170 6714 5687 8939 -703 -863 -82 A C ATOM 1195 C LEU A 170 38.524 -17.847 -6.531 1.00 57.72 A C ANISOU 1195 C LEU A 170 6854 6016 9062 -772 -789 55 A C ATOM 1196 O LEU A 170 37.652 -18.124 -5.706 1.00 54.38 A O ANISOU 1196 O LEU A 170 6473 5571 8618 -938 -787 136 A O ATOM 1197 CB LEU A 170 39.508 -20.112 -6.744 1.00 61.05 A C ANISOU 1197 CB LEU A 170 7507 6039 9651 -735 -966 -41 A C ATOM 1198 CG LEU A 170 39.940 -21.373 -7.497 1.00 73.41 A C ANISOU 1198 CG LEU A 170 9180 7411 11301 -676 -1054 -170 A C ATOM 1199 CD1 LEU A 170 39.992 -22.561 -6.533 1.00 72.68 A C ANISOU 1199 CD1 LEU A 170 9288 7047 11281 -768 -1156 -95 A C ATOM 1200 CD2 LEU A 170 39.018 -21.671 -8.659 1.00 69.84 A C ANISOU 1200 CD2 LEU A 170 8690 7033 10816 -753 -1042 -305 A C ATOM 1201 N ALA A 171 39.090 -16.643 -6.598 1.00 47.41 A N ANISOU 1201 N ALA A 171 5460 4843 7710 -651 -725 79 A N ATOM 1202 CA ALA A 171 38.652 -15.590 -5.695 1.00 45.67 A C ANISOU 1202 CA ALA A 171 5203 4739 7413 -700 -652 194 A C ATOM 1203 C ALA A 171 37.214 -15.141 -6.011 1.00 57.90 A C ANISOU 1203 C ALA A 171 6656 6464 8880 -793 -583 183 A C ATOM 1204 O ALA A 171 36.649 -15.464 -7.053 1.00 57.53 A O ANISOU 1204 O ALA A 171 6553 6479 8828 -805 -592 84 A O ATOM 1205 CB ALA A 171 39.595 -14.425 -5.741 1.00 41.86 A C ANISOU 1205 CB ALA A 171 4667 4338 6899 -562 -606 216 A C ATOM 1206 N ARG A 172 36.639 -14.374 -5.101 1.00 54.75 A N ANISOU 1206 N ARG A 172 6234 6155 8411 -849 -518 282 A N ATOM 1207 CA ARG A 172 35.248 -14.011 -5.191 1.00 51.46 A C ANISOU 1207 CA ARG A 172 5720 5910 7922 -935 -454 284 A C ATOM 1208 C ARG A 172 34.981 -12.781 -4.322 1.00 51.69 A C ANISOU 1208 C ARG A 172 5722 6055 7865 -910 -363 378 A C ATOM 1209 O ARG A 172 35.505 -12.672 -3.216 1.00 53.99 A O ANISOU 1209 O ARG A 172 6103 6256 8153 -930 -363 466 A O ATOM 1210 CB ARG A 172 34.398 -15.197 -4.712 1.00 57.68 A C ANISOU 1210 CB ARG A 172 6552 6623 8739 -1135 -493 302 A C ATOM 1211 CG ARG A 172 33.154 -14.799 -3.977 1.00 66.75 A C ANISOU 1211 CG ARG A 172 7629 7924 9810 -1257 -413 372 A C ATOM 1212 CD ARG A 172 32.305 -15.978 -3.596 1.00 77.45 A C ANISOU 1212 CD ARG A 172 9019 9221 11190 -1480 -446 389 A C ATOM 1213 NE ARG A 172 30.908 -15.569 -3.460 1.00 86.48 A N ANISOU 1213 NE ARG A 172 10013 10590 12255 -1581 -363 403 A N ATOM 1214 CZ ARG A 172 30.037 -15.532 -4.466 1.00 87.36 A C ANISOU 1214 CZ ARG A 172 9976 10869 12347 -1597 -361 313 A C ATOM 1215 NH1 ARG A 172 30.406 -15.887 -5.688 1.00 88.79 A N1+ ANISOU 1215 NH1 ARG A 172 10155 11008 12572 -1528 -434 201 A N1+ ATOM 1216 NH2 ARG A 172 28.793 -15.142 -4.251 1.00 92.94 A N ANISOU 1216 NH2 ARG A 172 10531 11797 12984 -1678 -286 333 A N ATOM 1217 N ALA A 173 34.169 -11.855 -4.822 1.00 54.16 A N ANISOU 1217 N ALA A 173 5916 6562 8100 -858 -290 355 A N ATOM 1218 CA ALA A 173 33.667 -10.751 -3.996 1.00 54.94 A C ANISOU 1218 CA ALA A 173 5990 6774 8109 -837 -197 432 A C ATOM 1219 C ALA A 173 32.702 -11.258 -2.921 1.00 51.33 A C ANISOU 1219 C ALA A 173 5535 6341 7629 -1005 -167 497 A C ATOM 1220 O ALA A 173 31.991 -12.239 -3.128 1.00 52.67 A O ANISOU 1220 O ALA A 173 5666 6516 7830 -1140 -199 469 A O ATOM 1221 CB ALA A 173 32.974 -9.717 -4.867 1.00 44.92 A C ANISOU 1221 CB ALA A 173 4599 5701 6767 -723 -137 388 A C ATOM 1222 N PHE A 174 32.672 -10.595 -1.772 1.00 53.04 A N ANISOU 1222 N PHE A 174 5800 6573 7782 -1009 -101 582 A N ATOM 1223 CA PHE A 174 31.728 -10.973 -0.724 1.00 54.58 A C ANISOU 1223 CA PHE A 174 5990 6816 7931 -1167 -51 648 A C ATOM 1224 C PHE A 174 30.991 -9.755 -0.186 1.00 66.06 A C ANISOU 1224 C PHE A 174 7378 8448 9274 -1100 70 678 A C ATOM 1225 O PHE A 174 31.292 -8.620 -0.568 1.00 67.68 A O ANISOU 1225 O PHE A 174 7571 8704 9442 -931 104 655 A O ATOM 1226 CB PHE A 174 32.426 -11.746 0.410 1.00 59.74 A C ANISOU 1226 CB PHE A 174 6811 7276 8612 -1280 -102 734 A C ATOM 1227 CG PHE A 174 33.305 -10.893 1.302 1.00 69.93 A C ANISOU 1227 CG PHE A 174 8210 8506 9853 -1196 -83 799 A C ATOM 1228 CD1 PHE A 174 34.629 -10.627 0.959 1.00 67.25 A C ANISOU 1228 CD1 PHE A 174 7935 8052 9564 -1074 -150 780 A C ATOM 1229 CD2 PHE A 174 32.819 -10.384 2.497 1.00 68.35 A C ANISOU 1229 CD2 PHE A 174 8046 8373 9551 -1248 3 873 A C ATOM 1230 CE1 PHE A 174 35.447 -9.862 1.789 1.00 59.79 A C ANISOU 1230 CE1 PHE A 174 7087 7058 8573 -1019 -144 837 A C ATOM 1231 CE2 PHE A 174 33.635 -9.613 3.327 1.00 65.69 A C ANISOU 1231 CE2 PHE A 174 7824 7977 9160 -1183 11 924 A C ATOM 1232 CZ PHE A 174 34.951 -9.357 2.969 1.00 63.52 A C ANISOU 1232 CZ PHE A 174 7611 7584 8941 -1075 -68 907 A C ATOM 1233 N SER A 175 30.027 -9.996 0.699 1.00 86.88 A N ANISOU 1233 N SER A 175 9980 11175 11854 -1232 139 728 A N ATOM 1234 CA SER A 175 29.191 -8.928 1.243 1.00 98.05 A C ANISOU 1234 CA SER A 175 11320 12777 13160 -1165 265 745 A C ATOM 1235 C SER A 175 28.544 -9.321 2.564 1.00107.29 A C ANISOU 1235 C SER A 175 12515 13988 14263 -1333 338 823 A C ATOM 1236 O SER A 175 29.045 -10.186 3.287 1.00102.97 A O ANISOU 1236 O SER A 175 12104 13281 13740 -1477 288 888 A O ATOM 1237 CB SER A 175 28.096 -8.570 0.245 1.00 95.46 A C ANISOU 1237 CB SER A 175 10784 12670 12815 -1094 301 672 A C ATOM 1238 OG SER A 175 27.347 -9.725 -0.085 1.00 93.82 A O ANISOU 1238 OG SER A 175 10477 12516 12655 -1274 264 649 A O ATOM 1239 N LEU A 176 27.426 -8.665 2.868 1.00124.29 A N ANISOU 1239 N LEU A 176 14538 16362 16325 -1303 460 817 A N ATOM 1240 CA LEU A 176 26.609 -8.986 4.036 1.00136.59 A C ANISOU 1240 CA LEU A 176 16078 18017 17801 -1465 557 881 A C ATOM 1241 C LEU A 176 25.129 -8.840 3.704 1.00139.06 A C ANISOU 1241 C LEU A 176 16145 18617 18074 -1480 650 837 A C ATOM 1242 O LEU A 176 24.677 -7.747 3.376 1.00141.58 A O ANISOU 1242 O LEU A 176 16356 19096 18343 -1284 717 788 A O ATOM 1243 CB LEU A 176 26.955 -8.068 5.211 1.00139.42 A C ANISOU 1243 CB LEU A 176 16569 18353 18049 -1386 641 931 A C ATOM 1244 CG LEU A 176 28.175 -8.416 6.064 1.00142.00 A C ANISOU 1244 CG LEU A 176 17135 18438 18380 -1452 569 1007 A C ATOM 1245 CD1 LEU A 176 28.137 -7.637 7.367 1.00140.22 A C ANISOU 1245 CD1 LEU A 176 17013 18249 18013 -1429 674 1055 A C ATOM 1246 CD2 LEU A 176 28.218 -9.908 6.346 1.00146.55 A C ANISOU 1246 CD2 LEU A 176 17770 18898 19013 -1689 495 1068 A C ATOM 1247 N PRO A 182 21.666 -13.852 4.052 1.00133.24 A N ANISOU 1247 N PRO A 182 15047 18151 17426 -2660 640 926 A N ATOM 1248 CA PRO A 182 22.243 -15.170 4.337 1.00132.58 A C ANISOU 1248 CA PRO A 182 15180 17788 17405 -2892 540 990 A C ATOM 1249 C PRO A 182 22.983 -15.703 3.110 1.00129.22 A C ANISOU 1249 C PRO A 182 14826 17161 17111 -2832 371 910 A C ATOM 1250 O PRO A 182 22.366 -16.354 2.265 1.00135.17 A O ANISOU 1250 O PRO A 182 15460 17980 17919 -2960 316 843 A O ATOM 1251 CB PRO A 182 21.011 -16.038 4.634 1.00134.85 A C ANISOU 1251 CB PRO A 182 15334 18239 17663 -3214 601 1021 A C ATOM 1252 CG PRO A 182 19.858 -15.069 4.804 1.00134.55 A C ANISOU 1252 CG PRO A 182 15011 18586 17526 -3135 761 990 A C ATOM 1253 CD PRO A 182 20.199 -13.904 3.943 1.00133.50 A C ANISOU 1253 CD PRO A 182 14795 18514 17413 -2787 735 896 A C ATOM 1254 N ASN A 183 24.282 -15.426 3.013 1.00115.42 A N ANISOU 1254 N ASN A 183 13264 15184 15407 -2645 292 911 A N ATOM 1255 CA ASN A 183 25.063 -15.781 1.827 1.00103.61 A C ANISOU 1255 CA ASN A 183 11826 13519 14024 -2544 150 825 A C ATOM 1256 C ASN A 183 25.213 -17.287 1.611 1.00 99.96 A C ANISOU 1256 C ASN A 183 11495 12835 13648 -2770 35 828 A C ATOM 1257 O ASN A 183 25.423 -18.042 2.560 1.00100.27 A O ANISOU 1257 O ASN A 183 11711 12707 13681 -2941 24 929 A O ATOM 1258 CB ASN A 183 26.452 -15.138 1.888 1.00100.72 A C ANISOU 1258 CB ASN A 183 11618 12973 13678 -2306 105 834 A C ATOM 1259 CG ASN A 183 26.404 -13.620 1.832 1.00 92.86 A C ANISOU 1259 CG ASN A 183 10514 12158 12610 -2065 196 809 A C ATOM 1260 ND2 ASN A 183 27.355 -12.975 2.502 1.00 88.09 A N ANISOU 1260 ND2 ASN A 183 10055 11439 11975 -1935 206 861 A N ATOM 1261 OD1 ASN A 183 25.534 -13.037 1.187 1.00 87.06 A O ANISOU 1261 OD1 ASN A 183 9575 11658 11845 -1995 248 744 A O ATOM 1262 N ARG A 184 25.111 -17.715 0.356 1.00 94.11 A N ANISOU 1262 N ARG A 184 10688 12088 12983 -2764 -55 715 A N ATOM 1263 CA ARG A 184 25.320 -19.116 0.009 1.00100.51 A C ANISOU 1263 CA ARG A 184 11645 12664 13882 -2950 -176 694 A C ATOM 1264 C ARG A 184 26.472 -19.240 -0.967 1.00102.74 A C ANISOU 1264 C ARG A 184 12036 12746 14254 -2752 -296 604 A C ATOM 1265 O ARG A 184 26.267 -19.569 -2.135 1.00107.62 A O ANISOU 1265 O ARG A 184 12584 13389 14917 -2749 -364 485 A O ATOM 1266 CB ARG A 184 24.072 -19.729 -0.630 1.00102.97 A C ANISOU 1266 CB ARG A 184 11787 13139 14196 -3175 -183 625 A C ATOM 1267 CG ARG A 184 23.017 -20.210 0.340 1.00109.27 A C ANISOU 1267 CG ARG A 184 12536 14048 14932 -3477 -96 720 A C ATOM 1268 CD ARG A 184 21.796 -20.692 -0.420 1.00120.43 A C ANISOU 1268 CD ARG A 184 13743 15665 16351 -3687 -109 636 A C ATOM 1269 NE ARG A 184 20.694 -21.046 0.468 1.00136.65 A N ANISOU 1269 NE ARG A 184 15700 17883 18336 -3984 -6 723 A N ATOM 1270 CZ ARG A 184 19.531 -21.539 0.050 1.00151.37 A C ANISOU 1270 CZ ARG A 184 17374 19946 20195 -4230 -3 673 A C ATOM 1271 NH1 ARG A 184 19.319 -21.734 -1.246 1.00155.93 A N1+ ANISOU 1271 NH1 ARG A 184 17847 20573 20826 -4207 -107 535 A N1+ ATOM 1272 NH2 ARG A 184 18.577 -21.839 0.924 1.00154.32 A N ANISOU 1272 NH2 ARG A 184 17656 20480 20500 -4508 105 761 A N ATOM 1273 N TYR A 185 27.684 -18.976 -0.493 1.00 97.39 A N ANISOU 1273 N TYR A 185 11523 11885 13595 -2589 -322 656 A N ATOM 1274 CA TYR A 185 28.860 -19.106 -1.341 1.00 89.38 A C ANISOU 1274 CA TYR A 185 10606 10690 12665 -2398 -425 575 A C ATOM 1275 C TYR A 185 29.190 -20.579 -1.508 1.00 88.05 A C ANISOU 1275 C TYR A 185 10627 10241 12586 -2540 -547 556 A C ATOM 1276 O TYR A 185 28.790 -21.405 -0.694 1.00 93.70 A O ANISOU 1276 O TYR A 185 11453 10851 13296 -2767 -553 644 A O ATOM 1277 CB TYR A 185 30.051 -18.347 -0.751 1.00 83.65 A C ANISOU 1277 CB TYR A 185 9976 9877 11930 -2190 -416 637 A C ATOM 1278 CG TYR A 185 29.782 -16.880 -0.493 1.00 82.44 A C ANISOU 1278 CG TYR A 185 9678 9961 11684 -2052 -298 660 A C ATOM 1279 CD1 TYR A 185 28.965 -16.143 -1.347 1.00 79.42 A C ANISOU 1279 CD1 TYR A 185 9087 9828 11262 -1984 -241 579 A C ATOM 1280 CD2 TYR A 185 30.355 -16.225 0.597 1.00 80.52 A C ANISOU 1280 CD2 TYR A 185 9520 9684 11388 -1982 -252 759 A C ATOM 1281 CE1 TYR A 185 28.720 -14.796 -1.122 1.00 77.69 A C ANISOU 1281 CE1 TYR A 185 8758 9803 10958 -1840 -138 598 A C ATOM 1282 CE2 TYR A 185 30.117 -14.876 0.834 1.00 74.99 A C ANISOU 1282 CE2 TYR A 185 8714 9179 10600 -1853 -146 770 A C ATOM 1283 CZ TYR A 185 29.300 -14.168 -0.032 1.00 76.66 A C ANISOU 1283 CZ TYR A 185 8728 9619 10779 -1776 -88 690 A C ATOM 1284 OH TYR A 185 29.050 -12.834 0.189 1.00 72.72 A O ANISOU 1284 OH TYR A 185 8144 9293 10194 -1632 13 699 A O HETATM 1285 N TPO A 186 29.918 -20.902 -2.568 1.00 84.95 A N ANISOU 1285 N TPO A 186 10281 9725 12270 -2405 -639 442 A N HETATM 1286 CA TPO A 186 30.295 -22.314 -2.873 1.00 86.63 A C ANISOU 1286 CA TPO A 186 10691 9651 12575 -2503 -763 397 A C HETATM 1287 C TPO A 186 31.300 -22.892 -1.898 1.00 91.82 A C ANISOU 1287 C TPO A 186 11587 10022 13277 -2479 -824 504 A C HETATM 1288 O TPO A 186 32.189 -22.191 -1.403 1.00 83.48 A O ANISOU 1288 O TPO A 186 10551 8958 12211 -2296 -808 563 A O HETATM 1289 CB TPO A 186 30.765 -22.285 -4.321 1.00 82.32 A C ANISOU 1289 CB TPO A 186 10097 9105 12076 -2327 -821 231 A C HETATM 1290 CG2 TPO A 186 31.801 -23.357 -4.638 1.00 71.45 A C ANISOU 1290 CG2 TPO A 186 8941 7406 10800 -2261 -943 174 A C HETATM 1291 OG1 TPO A 186 31.309 -20.982 -4.506 1.00 91.79 A O ANISOU 1291 OG1 TPO A 186 11174 10466 13237 -2084 -756 229 A O HETATM 1292 P TPO A 186 31.017 -20.067 -5.798 1.00 84.75 A P ANISOU 1292 P TPO A 186 10078 9823 12300 -1937 -719 107 A P HETATM 1293 O1P TPO A 186 32.198 -20.328 -6.716 1.00 71.11 A O ANISOU 1293 O1P TPO A 186 8436 7946 10636 -1746 -791 1 A O HETATM 1294 O2P TPO A 186 29.701 -20.589 -6.322 1.00106.18 A O1- ANISOU 1294 O2P TPO A 186 12692 12660 14991 -2146 -731 42 A O1- HETATM 1295 O3P TPO A 186 30.929 -18.691 -5.183 1.00 77.23 A O ANISOU 1295 O3P TPO A 186 9008 9066 11270 -1830 -609 197 A O ATOM 1296 N ASN A 187 31.087 -24.151 -1.533 1.00 95.68 A N ANISOU 1296 N ASN A 187 12268 10271 13813 -2671 -905 532 A N ATOM 1297 CA ASN A 187 31.914 -24.807 -0.530 1.00100.57 A C ANISOU 1297 CA ASN A 187 13135 10615 14462 -2691 -972 659 A C ATOM 1298 C ASN A 187 33.043 -25.534 -1.228 1.00105.79 A C ANISOU 1298 C ASN A 187 13976 10985 15233 -2503 -1105 590 A C ATOM 1299 O ASN A 187 33.932 -26.101 -0.591 1.00104.40 A O ANISOU 1299 O ASN A 187 13958 10626 15083 -2400 -1164 683 A O ATOM 1300 CB ASN A 187 31.081 -25.793 0.290 1.00110.35 A C ANISOU 1300 CB ASN A 187 14502 11748 15676 -3026 -977 754 A C ATOM 1301 CG ASN A 187 31.806 -26.277 1.531 1.00111.02 A C ANISOU 1301 CG ASN A 187 14808 11635 15738 -3079 -1006 933 A C ATOM 1302 ND2 ASN A 187 31.082 -26.367 2.641 1.00108.62 A N ANISOU 1302 ND2 ASN A 187 14766 11014 15490 -3210 -1115 975 A N ATOM 1303 OD1 ASN A 187 33.002 -26.566 1.493 1.00114.50 A O ANISOU 1303 OD1 ASN A 187 15198 12202 16105 -3006 -935 1034 A O ATOM 1304 N ARG A 188 33.015 -25.522 -2.555 1.00115.50 A N ANISOU 1304 N ARG A 188 15179 12185 16521 -2450 -1154 423 A N ATOM 1305 CA ARG A 188 34.092 -26.118 -3.336 1.00122.39 A C ANISOU 1305 CA ARG A 188 16206 12804 17495 -2255 -1268 329 A C ATOM 1306 C ARG A 188 35.252 -25.132 -3.393 1.00112.62 A C ANISOU 1306 C ARG A 188 14889 11628 16273 -1941 -1257 318 A C ATOM 1307 O ARG A 188 35.715 -24.764 -4.473 1.00115.58 A O ANISOU 1307 O ARG A 188 15264 11943 16709 -1738 -1304 188 A O ATOM 1308 CB ARG A 188 33.610 -26.445 -4.750 1.00133.83 A C ANISOU 1308 CB ARG A 188 17614 14259 18976 -2265 -1302 135 A C ATOM 1309 CG ARG A 188 34.731 -26.669 -5.752 1.00137.97 A C ANISOU 1309 CG ARG A 188 17865 15115 19443 -2149 -1213 31 A C ATOM 1310 CD ARG A 188 34.531 -25.828 -7.002 1.00143.43 A C ANISOU 1310 CD ARG A 188 18548 15771 20180 -1952 -1261 -158 A C ATOM 1311 NE ARG A 188 35.379 -26.274 -8.103 1.00146.52 A N ANISOU 1311 NE ARG A 188 18981 16068 20622 -1665 -1284 -162 A N ATOM 1312 CZ ARG A 188 36.484 -25.648 -8.495 1.00143.90 A C ANISOU 1312 CZ ARG A 188 18606 15756 20315 -1445 -1295 -308 A C ATOM 1313 NH1 ARG A 188 36.879 -24.544 -7.876 1.00146.28 A N1+ ANISOU 1313 NH1 ARG A 188 18835 16158 20586 -1473 -1291 -463 A N1+ ATOM 1314 NH2 ARG A 188 37.195 -26.126 -9.508 1.00137.23 A N ANISOU 1314 NH2 ARG A 188 17781 14842 19517 -1201 -1310 -300 A N ATOM 1315 N VAL A 189 35.711 -24.700 -2.222 1.00101.54 A N ANISOU 1315 N VAL A 189 13420 10351 14810 -1906 -1193 449 A N ATOM 1316 CA VAL A 189 36.738 -23.670 -2.144 1.00 88.42 A C ANISOU 1316 CA VAL A 189 11645 8804 13147 -1645 -1166 433 A C ATOM 1317 C VAL A 189 37.956 -24.039 -1.300 1.00 82.24 A C ANISOU 1317 C VAL A 189 11009 7830 12409 -1512 -1249 531 A C ATOM 1318 O VAL A 189 37.836 -24.592 -0.207 1.00 77.34 A O ANISOU 1318 O VAL A 189 10552 7058 11775 -1640 -1293 667 A O ATOM 1319 CB VAL A 189 36.161 -22.335 -1.637 1.00 88.06 A C ANISOU 1319 CB VAL A 189 11399 9062 12997 -1663 -1034 482 A C ATOM 1320 CG1 VAL A 189 35.322 -21.675 -2.720 1.00 83.16 A C ANISOU 1320 CG1 VAL A 189 10598 8655 12342 -1695 -968 357 A C ATOM 1321 CG2 VAL A 189 35.339 -22.557 -0.377 1.00 90.40 A C ANISOU 1321 CG2 VAL A 189 11751 9379 13219 -1875 -989 640 A C ATOM 1322 N VAL A 190 39.128 -23.712 -1.833 1.00 83.43 A N ANISOU 1322 N VAL A 190 11095 7999 12606 -1258 -1272 462 A N ATOM 1323 CA VAL A 190 40.412 -23.867 -1.139 1.00 82.29 A C ANISOU 1323 CA VAL A 190 11047 7711 12511 -1094 -1360 535 A C ATOM 1324 C VAL A 190 40.947 -25.290 -1.233 1.00 82.67 A C ANISOU 1324 C VAL A 190 11305 7444 12662 -1040 -1498 505 A C ATOM 1325 O VAL A 190 40.223 -26.246 -0.975 1.00 82.09 A O ANISOU 1325 O VAL A 190 11398 7197 12596 -1225 -1541 540 A O ATOM 1326 CB VAL A 190 40.322 -23.485 0.362 1.00 71.29 A C ANISOU 1326 CB VAL A 190 9716 6331 11042 -1197 -1352 724 A C ATOM 1327 CG1 VAL A 190 41.714 -23.530 1.020 1.00 61.37 A C ANISOU 1327 CG1 VAL A 190 8529 4960 9827 -1010 -1454 793 A C ATOM 1328 CG2 VAL A 190 39.639 -22.117 0.551 1.00 55.17 A C ANISOU 1328 CG2 VAL A 190 7493 4581 8888 -1266 -1209 755 A C ATOM 1329 N THR A 191 42.219 -25.427 -1.592 1.00 86.78 A N ANISOU 1329 N THR A 191 11820 7891 13261 -786 -1567 442 A N ATOM 1330 CA THR A 191 42.867 -26.732 -1.592 1.00 84.38 A C ANISOU 1330 CA THR A 191 11723 7278 13059 -685 -1706 418 A C ATOM 1331 C THR A 191 42.668 -27.413 -0.247 1.00 89.88 A C ANISOU 1331 C THR A 191 12646 7764 13740 -827 -1792 601 A C ATOM 1332 O THR A 191 42.708 -26.764 0.801 1.00 88.77 A O ANISOU 1332 O THR A 191 12481 7720 13528 -882 -1772 749 A O ATOM 1333 CB THR A 191 44.365 -26.615 -1.880 1.00 89.52 A C ANISOU 1333 CB THR A 191 12306 7923 13786 -373 -1764 358 A C ATOM 1334 CG2 THR A 191 45.101 -27.877 -1.443 1.00 98.87 A C ANISOU 1334 CG2 THR A 191 13721 8782 15064 -252 -1925 391 A C ATOM 1335 OG1 THR A 191 44.555 -26.422 -3.284 1.00 90.14 A O ANISOU 1335 OG1 THR A 191 12243 8116 13892 -244 -1704 165 A O ATOM 1336 N LEU A 192 42.455 -28.725 -0.286 1.00 90.83 A N ANISOU 1336 N LEU A 192 13003 7590 13919 -890 -1889 591 A N ATOM 1337 CA LEU A 192 42.132 -29.497 0.909 1.00 90.28 A C ANISOU 1337 CA LEU A 192 13184 7293 13827 -1061 -1970 768 A C ATOM 1338 C LEU A 192 43.053 -29.251 2.120 1.00 84.98 A C ANISOU 1338 C LEU A 192 12565 6587 13135 -942 -2047 933 A C ATOM 1339 O LEU A 192 42.573 -29.086 3.243 1.00 92.64 A O ANISOU 1339 O LEU A 192 13613 7572 14013 -1127 -2033 1104 A O ATOM 1340 CB LEU A 192 42.087 -30.994 0.579 1.00 87.60 A C ANISOU 1340 CB LEU A 192 13117 6593 13574 -1079 -2089 716 A C ATOM 1341 CG LEU A 192 41.634 -31.873 1.746 1.00 92.88 A C ANISOU 1341 CG LEU A 192 14078 7003 14210 -1294 -2170 904 A C ATOM 1342 CD1 LEU A 192 40.134 -31.714 2.011 1.00 87.48 A C ANISOU 1342 CD1 LEU A 192 13375 6440 13426 -1670 -2056 967 A C ATOM 1343 CD2 LEU A 192 42.006 -33.335 1.508 1.00105.76 A C ANISOU 1343 CD2 LEU A 192 16012 8227 15944 -1220 -2322 863 A C ATOM 1344 N TRP A 193 44.365 -29.235 1.902 1.00 65.37 A N ANISOU 1344 N TRP A 193 10035 4072 10731 -640 -2130 882 A N ATOM 1345 CA TRP A 193 45.302 -29.128 3.022 1.00 75.63 A C ANISOU 1345 CA TRP A 193 11393 5324 12019 -517 -2233 1033 A C ATOM 1346 C TRP A 193 45.240 -27.766 3.710 1.00 83.41 A C ANISOU 1346 C TRP A 193 12194 6608 12892 -586 -2138 1125 A C ATOM 1347 O TRP A 193 45.634 -27.609 4.875 1.00 76.99 A O ANISOU 1347 O TRP A 193 11456 5776 12022 -591 -2206 1284 A O ATOM 1348 CB TRP A 193 46.732 -29.401 2.562 1.00 83.16 A C ANISOU 1348 CB TRP A 193 12300 6208 13087 -168 -2341 942 A C ATOM 1349 CG TRP A 193 46.947 -30.782 2.032 1.00 87.64 A C ANISOU 1349 CG TRP A 193 13084 6450 13765 -55 -2454 859 A C ATOM 1350 CD1 TRP A 193 46.093 -31.852 2.134 1.00 89.39 A C ANISOU 1350 CD1 TRP A 193 13577 6396 13991 -247 -2496 891 A C ATOM 1351 CD2 TRP A 193 48.104 -31.257 1.342 1.00 87.23 A C ANISOU 1351 CD2 TRP A 193 13006 6306 13834 277 -2540 727 A C ATOM 1352 CE2 TRP A 193 47.883 -32.620 1.041 1.00 92.48 A C ANISOU 1352 CE2 TRP A 193 13948 6619 14571 285 -2634 678 A C ATOM 1353 CE3 TRP A 193 49.304 -30.664 0.943 1.00 83.99 A C ANISOU 1353 CE3 TRP A 193 12360 6078 13473 564 -2542 643 A C ATOM 1354 NE1 TRP A 193 46.647 -32.956 1.532 1.00 90.26 A N ANISOU 1354 NE1 TRP A 193 13850 6227 14217 -50 -2608 783 A N ATOM 1355 CZ2 TRP A 193 48.821 -33.396 0.365 1.00 88.10 A C ANISOU 1355 CZ2 TRP A 193 13448 5889 14136 595 -2729 541 A C ATOM 1356 CZ3 TRP A 193 50.235 -31.438 0.269 1.00 90.54 A C ANISOU 1356 CZ3 TRP A 193 13220 6758 14422 864 -2629 510 A C ATOM 1357 CH2 TRP A 193 49.990 -32.789 -0.009 1.00 87.05 A C ANISOU 1357 CH2 TRP A 193 13064 5963 14050 889 -2721 458 A C ATOM 1358 N TYR A 194 44.743 -26.777 2.979 1.00 79.45 A N ANISOU 1358 N TYR A 194 11463 6374 12351 -635 -1986 1023 A N ATOM 1359 CA TYR A 194 44.679 -25.435 3.509 1.00 76.54 A C ANISOU 1359 CA TYR A 194 10925 6278 11879 -685 -1889 1087 A C ATOM 1360 C TYR A 194 43.256 -25.063 3.905 1.00 75.88 A C ANISOU 1360 C TYR A 194 10847 6305 11681 -972 -1764 1152 A C ATOM 1361 O TYR A 194 43.022 -23.994 4.473 1.00 67.66 A O ANISOU 1361 O TYR A 194 9701 5471 10538 -1039 -1676 1216 A O ATOM 1362 CB TYR A 194 45.253 -24.451 2.494 1.00 76.62 A C ANISOU 1362 CB TYR A 194 10673 6521 11918 -511 -1810 941 A C ATOM 1363 CG TYR A 194 46.744 -24.606 2.289 1.00 82.35 A C ANISOU 1363 CG TYR A 194 11349 7203 12738 -231 -1917 895 A C ATOM 1364 CD1 TYR A 194 47.642 -23.797 2.979 1.00 89.71 A C ANISOU 1364 CD1 TYR A 194 12183 8265 13637 -139 -1948 970 A C ATOM 1365 CD2 TYR A 194 47.256 -25.556 1.414 1.00 77.46 A C ANISOU 1365 CD2 TYR A 194 10773 6422 12237 -59 -1988 771 A C ATOM 1366 CE1 TYR A 194 49.009 -23.928 2.803 1.00 89.95 A C ANISOU 1366 CE1 TYR A 194 12138 8285 13754 112 -2047 928 A C ATOM 1367 CE2 TYR A 194 48.624 -25.696 1.230 1.00 80.79 A C ANISOU 1367 CE2 TYR A 194 11126 6827 12745 213 -2079 723 A C ATOM 1368 CZ TYR A 194 49.497 -24.876 1.926 1.00 87.03 A C ANISOU 1368 CZ TYR A 194 11795 7768 13504 295 -2108 805 A C ATOM 1369 OH TYR A 194 50.864 -24.986 1.753 1.00 86.04 A O ANISOU 1369 OH TYR A 194 11569 7658 13464 559 -2198 758 A O ATOM 1370 N ARG A 195 42.309 -25.959 3.630 1.00 76.93 A N ANISOU 1370 N ARG A 195 11104 6298 11828 -1145 -1758 1135 A N ATOM 1371 CA ARG A 195 40.899 -25.650 3.857 1.00 81.02 A C ANISOU 1371 CA ARG A 195 11589 6949 12245 -1419 -1631 1176 A C ATOM 1372 C ARG A 195 40.537 -25.612 5.339 1.00 78.57 A C ANISOU 1372 C ARG A 195 11413 6619 11820 -1595 -1628 1374 A C ATOM 1373 O ARG A 195 40.850 -26.534 6.076 1.00 87.67 A O ANISOU 1373 O ARG A 195 12798 7528 12985 -1625 -1747 1488 A O ATOM 1374 CB ARG A 195 39.988 -26.621 3.107 1.00 82.01 A C ANISOU 1374 CB ARG A 195 11795 6949 12416 -1576 -1628 1094 A C ATOM 1375 CG ARG A 195 38.514 -26.259 3.228 1.00 84.54 A C ANISOU 1375 CG ARG A 195 12032 7453 12638 -1854 -1491 1119 A C ATOM 1376 CD ARG A 195 37.654 -27.269 2.516 1.00 81.26 A C ANISOU 1376 CD ARG A 195 11697 6910 12267 -2030 -1505 1039 A C ATOM 1377 NE ARG A 195 38.143 -27.463 1.162 1.00 82.70 A N ANISOU 1377 NE ARG A 195 11813 7060 12551 -1843 -1544 850 A N ATOM 1378 CZ ARG A 195 38.061 -28.604 0.493 1.00 84.72 A C ANISOU 1378 CZ ARG A 195 12218 7084 12887 -1876 -1627 758 A C ATOM 1379 NH1 ARG A 195 37.506 -29.673 1.055 1.00 89.07 A N1+ ANISOU 1379 NH1 ARG A 195 13003 7401 13437 -2101 -1686 846 A N1+ ATOM 1380 NH2 ARG A 195 38.545 -28.675 -0.739 1.00 79.72 A N ANISOU 1380 NH2 ARG A 195 11513 6450 12329 -1688 -1649 576 A N ATOM 1381 N PRO A 196 39.879 -24.527 5.775 1.00 80.37 A N ANISOU 1381 N PRO A 196 11502 7103 11930 -1704 -1491 1415 A N ATOM 1382 CA PRO A 196 39.482 -24.310 7.172 1.00 79.99 A C ANISOU 1382 CA PRO A 196 11556 7089 11748 -1869 -1459 1590 A C ATOM 1383 C PRO A 196 38.328 -25.228 7.594 1.00 81.72 A C ANISOU 1383 C PRO A 196 11930 7199 11919 -2160 -1432 1675 A C ATOM 1384 O PRO A 196 37.581 -25.690 6.735 1.00 74.75 A O ANISOU 1384 O PRO A 196 11006 6307 11089 -2263 -1396 1579 A O ATOM 1385 CB PRO A 196 38.999 -22.856 7.155 1.00 72.87 A C ANISOU 1385 CB PRO A 196 10428 6509 10750 -1876 -1299 1553 A C ATOM 1386 CG PRO A 196 38.498 -22.675 5.753 1.00 71.66 A C ANISOU 1386 CG PRO A 196 10093 6469 10667 -1844 -1227 1383 A C ATOM 1387 CD PRO A 196 39.558 -23.354 4.944 1.00 73.46 A C ANISOU 1387 CD PRO A 196 10365 6510 11035 -1645 -1359 1292 A C ATOM 1388 N PRO A 197 38.181 -25.468 8.910 1.00 88.43 A N ANISOU 1388 N PRO A 197 12957 7980 12662 -2305 -1449 1854 A N ATOM 1389 CA PRO A 197 37.126 -26.293 9.511 1.00 90.56 A C ANISOU 1389 CA PRO A 197 13391 8157 12861 -2610 -1415 1966 A C ATOM 1390 C PRO A 197 35.745 -25.945 8.969 1.00 94.38 A C ANISOU 1390 C PRO A 197 13685 8870 13307 -2808 -1245 1887 A C ATOM 1391 O PRO A 197 35.027 -26.853 8.544 1.00 89.71 A O ANISOU 1391 O PRO A 197 13161 8168 12758 -2992 -1251 1864 A O ATOM 1392 CB PRO A 197 37.185 -25.906 10.987 1.00 94.24 A C ANISOU 1392 CB PRO A 197 13964 8675 13169 -2690 -1395 2146 A C ATOM 1393 CG PRO A 197 38.574 -25.444 11.212 1.00 90.11 A C ANISOU 1393 CG PRO A 197 13444 8119 12674 -2412 -1510 2151 A C ATOM 1394 CD PRO A 197 39.067 -24.867 9.924 1.00 85.43 A C ANISOU 1394 CD PRO A 197 12622 7630 12206 -2185 -1500 1960 A C ATOM 1395 N GLU A 198 35.391 -24.656 8.992 1.00 92.79 A N ANISOU 1395 N GLU A 198 13254 8978 13025 -2767 -1104 1845 A N ATOM 1396 CA GLU A 198 34.087 -24.174 8.521 1.00 89.05 A C ANISOU 1396 CA GLU A 198 12568 8762 12505 -2919 -941 1770 A C ATOM 1397 C GLU A 198 33.677 -24.848 7.221 1.00 86.69 A C ANISOU 1397 C GLU A 198 12208 8403 12327 -2957 -971 1631 A C ATOM 1398 O GLU A 198 32.598 -25.429 7.119 1.00 92.25 A O ANISOU 1398 O GLU A 198 12910 9128 13012 -3208 -920 1636 A O ATOM 1399 CB GLU A 198 34.090 -22.653 8.283 1.00 95.04 A C ANISOU 1399 CB GLU A 198 13078 9819 13213 -2753 -825 1690 A C ATOM 1400 CG GLU A 198 34.757 -21.796 9.352 1.00 98.05 A C ANISOU 1400 CG GLU A 198 13504 10260 13491 -2648 -813 1783 A C ATOM 1401 CD GLU A 198 36.179 -21.399 8.991 1.00 96.41 A C ANISOU 1401 CD GLU A 198 13291 9973 13366 -2367 -926 1729 A C ATOM 1402 OE1 GLU A 198 37.080 -22.240 9.159 1.00102.11 A O ANISOU 1402 OE1 GLU A 198 14188 10450 14159 -2302 -1080 1777 A O ATOM 1403 OE2 GLU A 198 36.400 -20.246 8.551 1.00 91.29 A O1- ANISOU 1403 OE2 GLU A 198 12467 9510 12711 -2211 -861 1640 A O1- ATOM 1404 N LEU A 199 34.539 -24.752 6.218 1.00 85.89 A N ANISOU 1404 N LEU A 199 12052 8242 12342 -2713 -1051 1500 A N ATOM 1405 CA LEU A 199 34.224 -25.312 4.915 1.00 89.55 A C ANISOU 1405 CA LEU A 199 12457 8660 12909 -2722 -1081 1349 A C ATOM 1406 C LEU A 199 34.046 -26.830 4.991 1.00 91.33 A C ANISOU 1406 C LEU A 199 12932 8577 13191 -2905 -1188 1390 A C ATOM 1407 O LEU A 199 33.105 -27.374 4.420 1.00 91.57 A O ANISOU 1407 O LEU A 199 12936 8619 13238 -3103 -1163 1328 A O ATOM 1408 CB LEU A 199 35.282 -24.919 3.883 1.00 84.19 A C ANISOU 1408 CB LEU A 199 11686 7973 12330 -2415 -1142 1207 A C ATOM 1409 CG LEU A 199 35.448 -23.405 3.723 1.00 81.72 A C ANISOU 1409 CG LEU A 199 11141 7949 11961 -2250 -1037 1164 A C ATOM 1410 CD1 LEU A 199 36.412 -23.084 2.598 1.00 86.17 A C ANISOU 1410 CD1 LEU A 199 11610 8512 12617 -1982 -1086 1021 A C ATOM 1411 CD2 LEU A 199 34.110 -22.737 3.483 1.00 72.05 A C ANISOU 1411 CD2 LEU A 199 9714 7006 10654 -2394 -889 1129 A C ATOM 1412 N LEU A 200 34.940 -27.502 5.709 1.00 89.75 A N ANISOU 1412 N LEU A 200 12981 8102 13016 -2842 -1313 1498 A N ATOM 1413 CA LEU A 200 34.866 -28.950 5.865 1.00 92.94 A C ANISOU 1413 CA LEU A 200 13670 8173 13472 -2997 -1428 1554 A C ATOM 1414 C LEU A 200 33.573 -29.393 6.565 1.00 95.69 A C ANISOU 1414 C LEU A 200 14088 8551 13719 -3379 -1345 1672 A C ATOM 1415 O LEU A 200 33.103 -30.509 6.370 1.00 96.47 A O ANISOU 1415 O LEU A 200 14359 8438 13858 -3583 -1401 1676 A O ATOM 1416 CB LEU A 200 36.091 -29.456 6.623 1.00 90.13 A C ANISOU 1416 CB LEU A 200 13561 7540 13145 -2831 -1578 1668 A C ATOM 1417 CG LEU A 200 37.407 -29.259 5.877 1.00 84.15 A C ANISOU 1417 CG LEU A 200 12747 6721 12504 -2466 -1676 1546 A C ATOM 1418 CD1 LEU A 200 38.580 -29.290 6.846 1.00 87.41 A C ANISOU 1418 CD1 LEU A 200 13308 6997 12908 -2286 -1793 1678 A C ATOM 1419 CD2 LEU A 200 37.565 -30.303 4.775 1.00 79.69 A C ANISOU 1419 CD2 LEU A 200 12288 5918 12074 -2412 -1773 1403 A C ATOM 1420 N LEU A 201 33.000 -28.510 7.374 1.00 94.64 A N ANISOU 1420 N LEU A 201 13822 8685 13452 -3479 -1207 1763 A N ATOM 1421 CA LEU A 201 31.735 -28.794 8.034 1.00 92.54 A C ANISOU 1421 CA LEU A 201 13573 8512 13077 -3837 -1098 1868 A C ATOM 1422 C LEU A 201 30.543 -28.317 7.209 1.00102.52 A C ANISOU 1422 C LEU A 201 14542 10080 14329 -3967 -964 1739 A C ATOM 1423 O LEU A 201 29.407 -28.369 7.675 1.00107.62 A O ANISOU 1423 O LEU A 201 15126 10885 14881 -4254 -848 1806 A O ATOM 1424 CB LEU A 201 31.699 -28.149 9.417 1.00 85.73 A C ANISOU 1424 CB LEU A 201 12732 7783 12058 -3884 -1013 2037 A C ATOM 1425 CG LEU A 201 32.457 -28.911 10.500 1.00 85.99 A C ANISOU 1425 CG LEU A 201 13104 7512 12057 -3900 -1138 2220 A C ATOM 1426 CD1 LEU A 201 32.370 -28.192 11.847 1.00 85.63 A C ANISOU 1426 CD1 LEU A 201 13070 7633 11834 -3952 -1044 2375 A C ATOM 1427 CD2 LEU A 201 31.929 -30.343 10.599 1.00 83.05 A C ANISOU 1427 CD2 LEU A 201 12988 6860 11706 -4192 -1203 2298 A C ATOM 1428 N GLY A 202 30.810 -27.834 5.998 1.00106.18 A N ANISOU 1428 N GLY A 202 14819 10641 14882 -3752 -978 1559 A N ATOM 1429 CA GLY A 202 29.761 -27.452 5.064 1.00103.64 A C ANISOU 1429 CA GLY A 202 14229 10588 14561 -3844 -883 1424 A C ATOM 1430 C GLY A 202 29.240 -26.019 5.116 1.00 98.61 A C ANISOU 1430 C GLY A 202 13287 10347 13833 -3758 -724 1396 A C ATOM 1431 O GLY A 202 28.134 -25.754 4.645 1.00102.13 A O ANISOU 1431 O GLY A 202 13515 11043 14248 -3894 -630 1328 A O ATOM 1432 N GLU A 203 30.020 -25.093 5.671 1.00 88.02 A N ANISOU 1432 N GLU A 203 11931 9065 12448 -3532 -700 1443 A N ATOM 1433 CA GLU A 203 29.605 -23.686 5.735 1.00 87.78 A C ANISOU 1433 CA GLU A 203 11643 9379 12331 -3424 -555 1414 A C ATOM 1434 C GLU A 203 29.597 -23.002 4.360 1.00 85.60 A C ANISOU 1434 C GLU A 203 11139 9266 12120 -3228 -547 1235 A C ATOM 1435 O GLU A 203 30.503 -23.198 3.551 1.00 83.72 A O ANISOU 1435 O GLU A 203 10953 8873 11983 -3042 -655 1145 A O ATOM 1436 CB GLU A 203 30.497 -22.901 6.698 1.00 86.75 A C ANISOU 1436 CB GLU A 203 11587 9242 12134 -3247 -544 1507 A C ATOM 1437 CG GLU A 203 30.262 -21.400 6.663 1.00 85.43 A C ANISOU 1437 CG GLU A 203 11188 9383 11889 -3089 -412 1458 A C ATOM 1438 CD GLU A 203 28.992 -20.983 7.380 1.00 92.05 A C ANISOU 1438 CD GLU A 203 11902 10482 12593 -3279 -245 1517 A C ATOM 1439 OE1 GLU A 203 28.944 -21.097 8.624 1.00 89.52 A O ANISOU 1439 OE1 GLU A 203 11716 10132 12167 -3400 -204 1656 A O ATOM 1440 OE2 GLU A 203 28.046 -20.526 6.704 1.00 95.29 A O1- ANISOU 1440 OE2 GLU A 203 12074 11137 12993 -3299 -153 1424 A O1- ATOM 1441 N ARG A 204 28.569 -22.200 4.104 1.00 83.16 A N ANISOU 1441 N ARG A 204 10578 9275 11744 -3264 -418 1186 A N ATOM 1442 CA ARG A 204 28.434 -21.511 2.822 1.00 83.77 A C ANISOU 1442 CA ARG A 204 10439 9528 11863 -3090 -407 1030 A C ATOM 1443 C ARG A 204 28.290 -20.016 3.038 1.00 85.80 A C ANISOU 1443 C ARG A 204 10514 10054 12031 -2913 -284 1028 A C ATOM 1444 O ARG A 204 28.243 -19.237 2.092 1.00 92.92 A O ANISOU 1444 O ARG A 204 11247 11111 12948 -2739 -265 920 A O ATOM 1445 CB ARG A 204 27.231 -22.047 2.042 1.00 84.35 A C ANISOU 1445 CB ARG A 204 10367 9731 11951 -3296 -394 947 A C ATOM 1446 CG ARG A 204 27.373 -23.499 1.638 1.00 90.73 A C ANISOU 1446 CG ARG A 204 11364 10258 12852 -3463 -525 920 A C ATOM 1447 CD ARG A 204 26.135 -23.999 0.935 1.00101.25 A C ANISOU 1447 CD ARG A 204 12549 11734 14186 -3699 -514 839 A C ATOM 1448 NE ARG A 204 25.964 -23.396 -0.382 1.00105.13 A N ANISOU 1448 NE ARG A 204 12830 12412 14702 -3532 -524 679 A N ATOM 1449 CZ ARG A 204 26.527 -23.863 -1.491 1.00110.29 A C ANISOU 1449 CZ ARG A 204 13551 12911 15442 -3430 -640 551 A C ATOM 1450 NH1 ARG A 204 27.310 -24.936 -1.438 1.00109.15 A N1+ ANISOU 1450 NH1 ARG A 204 13676 12417 15378 -3461 -756 557 A N1+ ATOM 1451 NH2 ARG A 204 26.316 -23.254 -2.652 1.00111.15 A N ANISOU 1451 NH2 ARG A 204 13466 13214 15551 -3286 -641 416 A N ATOM 1452 N ASP A 205 28.205 -19.625 4.300 1.00 83.08 A N ANISOU 1452 N ASP A 205 10223 9758 11588 -2962 -200 1150 A N ATOM 1453 CA ASP A 205 28.143 -18.227 4.664 1.00 88.72 A C ANISOU 1453 CA ASP A 205 10813 10688 12210 -2793 -85 1155 A C ATOM 1454 C ASP A 205 29.437 -17.901 5.400 1.00 88.39 A C ANISOU 1454 C ASP A 205 10959 10468 12158 -2644 -138 1226 A C ATOM 1455 O ASP A 205 29.436 -17.618 6.597 1.00 92.21 A O ANISOU 1455 O ASP A 205 11525 10970 12539 -2694 -76 1333 A O ATOM 1456 CB ASP A 205 26.934 -17.975 5.560 1.00 96.56 A C ANISOU 1456 CB ASP A 205 11702 11910 13077 -2969 67 1225 A C ATOM 1457 CG ASP A 205 26.499 -16.528 5.556 1.00110.14 A C ANISOU 1457 CG ASP A 205 13228 13907 14711 -2789 197 1181 A C ATOM 1458 OD1 ASP A 205 27.108 -15.722 4.824 1.00115.21 A O ANISOU 1458 OD1 ASP A 205 13825 14558 15393 -2543 165 1101 A O ATOM 1459 OD2 ASP A 205 25.543 -16.197 6.287 1.00119.12 A O1- ANISOU 1459 OD2 ASP A 205 14264 15255 15739 -2891 334 1225 A O1- ATOM 1460 N TYR A 206 30.546 -17.978 4.673 1.00 82.43 A N ANISOU 1460 N TYR A 206 10267 9549 11504 -2466 -254 1164 A N ATOM 1461 CA TYR A 206 31.870 -17.768 5.249 1.00 78.23 A C ANISOU 1461 CA TYR A 206 9896 8848 10981 -2324 -328 1221 A C ATOM 1462 C TYR A 206 32.454 -16.455 4.747 1.00 77.09 A C ANISOU 1462 C TYR A 206 9642 8819 10830 -2075 -297 1148 A C ATOM 1463 O TYR A 206 31.948 -15.870 3.783 1.00 78.78 A O ANISOU 1463 O TYR A 206 9681 9200 11054 -1996 -243 1047 A O ATOM 1464 CB TYR A 206 32.795 -18.924 4.872 1.00 68.48 A C ANISOU 1464 CB TYR A 206 8824 7327 9869 -2308 -490 1213 A C ATOM 1465 CG TYR A 206 32.829 -19.172 3.389 1.00 70.89 A C ANISOU 1465 CG TYR A 206 9026 7628 10280 -2223 -538 1065 A C ATOM 1466 CD1 TYR A 206 32.067 -20.188 2.809 1.00 70.30 A C ANISOU 1466 CD1 TYR A 206 8950 7506 10254 -2394 -568 1018 A C ATOM 1467 CD2 TYR A 206 33.602 -18.374 2.558 1.00 67.60 A C ANISOU 1467 CD2 TYR A 206 8520 7263 9904 -1985 -552 972 A C ATOM 1468 CE1 TYR A 206 32.093 -20.411 1.435 1.00 69.00 A C ANISOU 1468 CE1 TYR A 206 8702 7343 10173 -2316 -615 874 A C ATOM 1469 CE2 TYR A 206 33.633 -18.581 1.193 1.00 68.19 A C ANISOU 1469 CE2 TYR A 206 8507 7346 10057 -1907 -589 837 A C ATOM 1470 CZ TYR A 206 32.884 -19.598 0.634 1.00 70.30 A C ANISOU 1470 CZ TYR A 206 8779 7565 10368 -2066 -624 784 A C ATOM 1471 OH TYR A 206 32.938 -19.780 -0.730 1.00 68.47 A O ANISOU 1471 OH TYR A 206 8469 7346 10199 -1983 -664 642 A O ATOM 1472 N GLY A 207 33.520 -15.999 5.401 1.00 71.12 A N ANISOU 1472 N GLY A 207 8997 7974 10054 -1961 -337 1202 A N ATOM 1473 CA GLY A 207 34.137 -14.725 5.075 1.00 65.16 A C ANISOU 1473 CA GLY A 207 8165 7311 9280 -1754 -307 1148 A C ATOM 1474 C GLY A 207 35.650 -14.777 5.097 1.00 66.80 A C ANISOU 1474 C GLY A 207 8479 7347 9554 -1619 -428 1157 A C ATOM 1475 O GLY A 207 36.240 -15.838 4.874 1.00 63.24 A O ANISOU 1475 O GLY A 207 8117 6711 9200 -1629 -546 1159 A O ATOM 1476 N PRO A 208 36.290 -13.622 5.354 1.00 65.47 A N ANISOU 1476 N PRO A 208 8299 7242 9335 -1490 -401 1157 A N ATOM 1477 CA PRO A 208 37.755 -13.468 5.355 1.00 59.50 A C ANISOU 1477 CA PRO A 208 7605 6370 8634 -1358 -506 1159 A C ATOM 1478 C PRO A 208 38.517 -14.440 6.255 1.00 61.57 A C ANISOU 1478 C PRO A 208 8037 6436 8921 -1411 -635 1256 A C ATOM 1479 O PRO A 208 39.658 -14.766 5.949 1.00 60.73 A O ANISOU 1479 O PRO A 208 7956 6215 8904 -1302 -748 1238 A O ATOM 1480 CB PRO A 208 37.952 -12.026 5.828 1.00 52.59 A C ANISOU 1480 CB PRO A 208 6711 5615 7655 -1285 -430 1167 A C ATOM 1481 CG PRO A 208 36.742 -11.321 5.313 1.00 59.46 A C ANISOU 1481 CG PRO A 208 7453 6671 8470 -1285 -292 1109 A C ATOM 1482 CD PRO A 208 35.603 -12.316 5.404 1.00 58.41 A C ANISOU 1482 CD PRO A 208 7304 6552 8338 -1444 -264 1131 A C ATOM 1483 N PRO A 209 37.907 -14.892 7.357 1.00 66.64 A N ANISOU 1483 N PRO A 209 8794 7048 9479 -1571 -617 1362 A N ATOM 1484 CA PRO A 209 38.608 -15.865 8.199 1.00 63.98 A C ANISOU 1484 CA PRO A 209 8639 6511 9159 -1619 -751 1468 A C ATOM 1485 C PRO A 209 39.107 -17.115 7.468 1.00 62.61 A C ANISOU 1485 C PRO A 209 8510 6145 9133 -1581 -879 1435 A C ATOM 1486 O PRO A 209 40.051 -17.735 7.954 1.00 63.83 A O ANISOU 1486 O PRO A 209 8795 6131 9328 -1535 -1015 1499 A O ATOM 1487 CB PRO A 209 37.555 -16.233 9.243 1.00 65.58 A C ANISOU 1487 CB PRO A 209 8939 6734 9243 -1829 -680 1574 A C ATOM 1488 CG PRO A 209 36.775 -14.974 9.403 1.00 63.67 A C ANISOU 1488 CG PRO A 209 8582 6725 8886 -1832 -516 1541 A C ATOM 1489 CD PRO A 209 36.696 -14.371 8.017 1.00 61.73 A C ANISOU 1489 CD PRO A 209 8147 6584 8723 -1695 -473 1401 A C ATOM 1490 N ILE A 210 38.521 -17.489 6.335 1.00 59.42 A N ANISOU 1490 N ILE A 210 8009 5762 8808 -1589 -846 1333 A N ATOM 1491 CA ILE A 210 39.026 -18.682 5.641 1.00 70.23 A C ANISOU 1491 CA ILE A 210 9441 6933 10312 -1543 -969 1288 A C ATOM 1492 C ILE A 210 40.422 -18.454 5.069 1.00 67.25 A C ANISOU 1492 C ILE A 210 9016 6510 10024 -1316 -1058 1221 A C ATOM 1493 O ILE A 210 41.246 -19.375 5.033 1.00 67.48 A O ANISOU 1493 O ILE A 210 9146 6347 10144 -1240 -1190 1229 A O ATOM 1494 CB ILE A 210 38.097 -19.192 4.511 1.00 68.12 A C ANISOU 1494 CB ILE A 210 9090 6692 10102 -1612 -924 1181 A C ATOM 1495 CG1 ILE A 210 38.166 -18.256 3.298 1.00 59.34 A C ANISOU 1495 CG1 ILE A 210 7777 5756 9014 -1464 -856 1043 A C ATOM 1496 CG2 ILE A 210 36.665 -19.411 5.031 1.00 56.32 A C ANISOU 1496 CG2 ILE A 210 7606 5274 8519 -1854 -829 1242 A C ATOM 1497 CD1 ILE A 210 37.367 -18.749 2.092 1.00 57.53 A C ANISOU 1497 CD1 ILE A 210 7462 5559 8836 -1512 -832 926 A C ATOM 1498 N ASP A 211 40.687 -17.229 4.626 1.00 56.85 A N ANISOU 1498 N ASP A 211 7548 5371 8681 -1207 -984 1156 A N ATOM 1499 CA ASP A 211 41.997 -16.901 4.081 1.00 61.03 A C ANISOU 1499 CA ASP A 211 8009 5894 9283 -1012 -1049 1094 A C ATOM 1500 C ASP A 211 43.048 -16.875 5.189 1.00 65.56 A C ANISOU 1500 C ASP A 211 8682 6389 9838 -969 -1154 1198 A C ATOM 1501 O ASP A 211 44.221 -17.208 4.970 1.00 59.29 A O ANISOU 1501 O ASP A 211 7881 5515 9131 -825 -1264 1175 A O ATOM 1502 CB ASP A 211 41.966 -15.568 3.323 1.00 57.45 A C ANISOU 1502 CB ASP A 211 7386 5647 8795 -933 -937 1008 A C ATOM 1503 CG ASP A 211 41.266 -15.677 1.979 1.00 58.67 A C ANISOU 1503 CG ASP A 211 7430 5871 8991 -918 -871 887 A C ATOM 1504 OD1 ASP A 211 41.111 -16.810 1.474 1.00 58.77 A O ANISOU 1504 OD1 ASP A 211 7486 5761 9082 -936 -930 843 A O ATOM 1505 OD2 ASP A 211 40.872 -14.631 1.426 1.00 61.13 A O1- ANISOU 1505 OD2 ASP A 211 7623 6355 9250 -888 -767 836 A O1- ATOM 1506 N LEU A 212 42.618 -16.495 6.386 1.00 61.00 A N ANISOU 1506 N LEU A 212 8192 5845 9140 -1090 -1123 1309 A N ATOM 1507 CA LEU A 212 43.550 -16.374 7.500 1.00 64.17 A C ANISOU 1507 CA LEU A 212 8691 6194 9498 -1064 -1225 1411 A C ATOM 1508 C LEU A 212 43.966 -17.728 8.064 1.00 68.15 A C ANISOU 1508 C LEU A 212 9366 6475 10054 -1071 -1379 1499 A C ATOM 1509 O LEU A 212 45.109 -17.912 8.479 1.00 69.20 A O ANISOU 1509 O LEU A 212 9539 6535 10220 -963 -1514 1541 A O ATOM 1510 CB LEU A 212 42.988 -15.443 8.573 1.00 60.70 A C ANISOU 1510 CB LEU A 212 8297 5872 8894 -1181 -1136 1489 A C ATOM 1511 CG LEU A 212 43.294 -13.997 8.166 1.00 64.22 A C ANISOU 1511 CG LEU A 212 8603 6493 9305 -1099 -1052 1411 A C ATOM 1512 CD1 LEU A 212 42.279 -13.044 8.718 1.00 76.10 A C ANISOU 1512 CD1 LEU A 212 10115 8136 10664 -1201 -906 1431 A C ATOM 1513 CD2 LEU A 212 44.704 -13.604 8.601 1.00 62.22 A C ANISOU 1513 CD2 LEU A 212 8354 6227 9060 -1003 -1168 1436 A C ATOM 1514 N TRP A 213 43.035 -18.675 8.058 1.00 72.45 A N ANISOU 1514 N TRP A 213 10011 6912 10606 -1200 -1364 1527 A N ATOM 1515 CA TRP A 213 43.346 -20.046 8.408 1.00 68.13 A C ANISOU 1515 CA TRP A 213 9646 6120 10119 -1207 -1508 1601 A C ATOM 1516 C TRP A 213 44.475 -20.507 7.509 1.00 67.59 A C ANISOU 1516 C TRP A 213 9518 5958 10204 -987 -1620 1505 A C ATOM 1517 O TRP A 213 45.428 -21.149 7.958 1.00 67.65 A O ANISOU 1517 O TRP A 213 9627 5814 10260 -880 -1776 1565 A O ATOM 1518 CB TRP A 213 42.131 -20.945 8.193 1.00 70.72 A C ANISOU 1518 CB TRP A 213 10061 6356 10453 -1387 -1457 1609 A C ATOM 1519 CG TRP A 213 42.473 -22.393 8.344 1.00 74.84 A C ANISOU 1519 CG TRP A 213 10785 6594 11056 -1381 -1608 1665 A C ATOM 1520 CD1 TRP A 213 42.911 -23.239 7.367 1.00 76.60 A C ANISOU 1520 CD1 TRP A 213 11019 6663 11425 -1255 -1691 1565 A C ATOM 1521 CD2 TRP A 213 42.432 -23.158 9.551 1.00 74.04 A C ANISOU 1521 CD2 TRP A 213 10925 6319 10888 -1497 -1699 1835 A C ATOM 1522 CE2 TRP A 213 42.851 -24.463 9.231 1.00 81.22 A C ANISOU 1522 CE2 TRP A 213 11989 6955 11915 -1429 -1840 1834 A C ATOM 1523 CE3 TRP A 213 42.078 -22.868 10.871 1.00 78.60 A C ANISOU 1523 CE3 TRP A 213 11614 6942 11308 -1649 -1672 1988 A C ATOM 1524 NE1 TRP A 213 43.140 -24.485 7.891 1.00 83.34 A N ANISOU 1524 NE1 TRP A 213 12110 7241 12313 -1277 -1830 1660 A N ATOM 1525 CZ2 TRP A 213 42.925 -25.478 10.183 1.00 81.56 A C ANISOU 1525 CZ2 TRP A 213 12303 6758 11927 -1510 -1962 1992 A C ATOM 1526 CZ3 TRP A 213 42.152 -23.880 11.819 1.00 79.86 A C ANISOU 1526 CZ3 TRP A 213 12035 6880 11428 -1739 -1788 2146 A C ATOM 1527 CH2 TRP A 213 42.572 -25.165 11.469 1.00 79.29 A C ANISOU 1527 CH2 TRP A 213 12120 6527 11479 -1670 -1935 2152 A C ATOM 1528 N GLY A 214 44.357 -20.171 6.229 1.00 65.43 A N ANISOU 1528 N GLY A 214 9075 5785 10000 -911 -1539 1355 A N ATOM 1529 CA GLY A 214 45.396 -20.476 5.267 1.00 71.50 A C ANISOU 1529 CA GLY A 214 9758 6508 10901 -697 -1614 1243 A C ATOM 1530 C GLY A 214 46.703 -19.757 5.564 1.00 66.66 A C ANISOU 1530 C GLY A 214 9048 5985 10293 -541 -1677 1255 A C ATOM 1531 O GLY A 214 47.779 -20.278 5.279 1.00 66.35 A O ANISOU 1531 O GLY A 214 8991 5864 10356 -362 -1792 1219 A O ATOM 1532 N ALA A 215 46.611 -18.553 6.119 1.00 58.26 A N ANISOU 1532 N ALA A 215 7920 5096 9119 -609 -1602 1297 A N ATOM 1533 CA ALA A 215 47.797 -17.797 6.485 1.00 58.44 A C ANISOU 1533 CA ALA A 215 7857 5215 9131 -502 -1663 1313 A C ATOM 1534 C ALA A 215 48.496 -18.571 7.590 1.00 63.90 A C ANISOU 1534 C ALA A 215 8701 5753 9824 -469 -1839 1439 A C ATOM 1535 O ALA A 215 49.713 -18.737 7.579 1.00 62.14 A O ANISOU 1535 O ALA A 215 8421 5517 9674 -307 -1962 1430 A O ATOM 1536 CB ALA A 215 47.420 -16.387 6.964 1.00 49.91 A C ANISOU 1536 CB ALA A 215 6724 4323 7917 -608 -1548 1339 A C ATOM 1537 N GLY A 216 47.704 -19.049 8.542 1.00 65.03 A N ANISOU 1537 N GLY A 216 9036 5790 9880 -625 -1851 1560 A N ATOM 1538 CA GLY A 216 48.206 -19.923 9.581 1.00 75.55 A C ANISOU 1538 CA GLY A 216 10555 6948 11202 -610 -2022 1695 A C ATOM 1539 C GLY A 216 48.996 -21.111 9.051 1.00 78.66 A C ANISOU 1539 C GLY A 216 10983 7153 11750 -423 -2168 1659 A C ATOM 1540 O GLY A 216 50.142 -21.321 9.454 1.00 81.96 A O ANISOU 1540 O GLY A 216 11400 7534 12207 -270 -2323 1700 A O ATOM 1541 N CYS A 217 48.390 -21.892 8.155 1.00 73.65 A N ANISOU 1541 N CYS A 217 10380 6402 11200 -428 -2124 1579 A N ATOM 1542 CA CYS A 217 49.038 -23.098 7.639 1.00 76.26 A C ANISOU 1542 CA CYS A 217 10778 6524 11673 -248 -2257 1534 A C ATOM 1543 C CYS A 217 50.343 -22.759 6.927 1.00 79.94 A C ANISOU 1543 C CYS A 217 11033 7099 12242 4 -2305 1421 A C ATOM 1544 O CYS A 217 51.315 -23.523 6.976 1.00 82.08 A O ANISOU 1544 O CYS A 217 11341 7242 12606 202 -2460 1427 A O ATOM 1545 CB CYS A 217 48.112 -23.865 6.690 1.00 77.03 A C ANISOU 1545 CB CYS A 217 10935 6499 11835 -315 -2185 1440 A C ATOM 1546 SG CYS A 217 46.545 -24.427 7.411 1.00 83.65 A S ANISOU 1546 SG CYS A 217 12007 7209 12567 -632 -2126 1563 A S ATOM 1547 N ILE A 218 50.359 -21.608 6.266 1.00 71.19 A N ANISOU 1547 N ILE A 218 9704 6231 11114 -1 -2170 1322 A N ATOM 1548 CA ILE A 218 51.546 -21.155 5.556 1.00 69.07 A C ANISOU 1548 CA ILE A 218 9213 6103 10926 203 -2187 1215 A C ATOM 1549 C ILE A 218 52.616 -20.682 6.534 1.00 74.32 A C ANISOU 1549 C ILE A 218 9831 6852 11556 266 -2308 1310 A C ATOM 1550 O ILE A 218 53.808 -20.960 6.357 1.00 71.93 A O ANISOU 1550 O ILE A 218 9425 6560 11344 472 -2420 1275 A O ATOM 1551 CB ILE A 218 51.209 -20.028 4.561 1.00 53.72 A C ANISOU 1551 CB ILE A 218 7068 4387 8957 157 -2003 1093 A C ATOM 1552 CG1 ILE A 218 50.473 -20.602 3.363 1.00 50.32 A C ANISOU 1552 CG1 ILE A 218 6643 3890 8588 162 -1916 968 A C ATOM 1553 CG2 ILE A 218 52.479 -19.326 4.070 1.00 54.95 A C ANISOU 1553 CG2 ILE A 218 6993 4726 9162 319 -2011 1016 A C ATOM 1554 CD1 ILE A 218 49.644 -19.571 2.612 1.00 53.76 A C ANISOU 1554 CD1 ILE A 218 6955 4514 8956 47 -1732 891 A C ATOM 1555 N MET A 219 52.194 -19.961 7.566 1.00 71.81 A N ANISOU 1555 N MET A 219 9581 6603 11099 90 -2285 1423 A N ATOM 1556 CA MET A 219 53.149 -19.482 8.549 1.00 72.07 A C ANISOU 1556 CA MET A 219 9585 6720 11080 123 -2407 1513 A C ATOM 1557 C MET A 219 53.900 -20.670 9.139 1.00 69.23 A C ANISOU 1557 C MET A 219 9350 6170 10784 275 -2622 1599 A C ATOM 1558 O MET A 219 55.124 -20.691 9.146 1.00 73.55 A O ANISOU 1558 O MET A 219 9768 6780 11399 456 -2746 1582 A O ATOM 1559 CB MET A 219 52.473 -18.660 9.650 1.00 65.97 A C ANISOU 1559 CB MET A 219 8917 6017 10133 -96 -2354 1624 A C ATOM 1560 CG MET A 219 53.475 -17.954 10.547 1.00 67.82 A C ANISOU 1560 CG MET A 219 9095 6375 10299 -78 -2466 1690 A C ATOM 1561 SD MET A 219 52.748 -16.803 11.715 1.00 80.61 A S ANISOU 1561 SD MET A 219 10823 8103 11702 -323 -2382 1783 A S ATOM 1562 CE MET A 219 54.138 -16.464 12.791 1.00 97.49 A C ANISOU 1562 CE MET A 219 12933 10322 13787 -264 -2591 1867 A C ATOM 1563 N ALA A 220 53.154 -21.661 9.617 1.00 72.82 A N ANISOU 1563 N ALA A 220 10055 6396 11218 201 -2667 1691 A N ATOM 1564 CA ALA A 220 53.741 -22.862 10.204 1.00 81.97 A C ANISOU 1564 CA ALA A 220 11383 7333 12429 339 -2876 1788 A C ATOM 1565 C ALA A 220 54.678 -23.538 9.212 1.00 83.64 A C ANISOU 1565 C ALA A 220 11471 7492 12817 620 -2950 1663 A C ATOM 1566 O ALA A 220 55.673 -24.144 9.595 1.00 83.69 A O ANISOU 1566 O ALA A 220 11496 7418 12883 819 -3138 1711 A O ATOM 1567 CB ALA A 220 52.644 -23.831 10.643 1.00 83.79 A C ANISOU 1567 CB ALA A 220 11911 7312 12615 187 -2877 1889 A C ATOM 1568 N GLU A 221 54.348 -23.414 7.932 1.00 86.20 A N ANISOU 1568 N GLU A 221 11665 7869 13216 644 -2802 1500 A N ATOM 1569 CA GLU A 221 55.107 -24.038 6.860 1.00 84.11 A C ANISOU 1569 CA GLU A 221 11284 7564 13108 901 -2837 1356 A C ATOM 1570 C GLU A 221 56.465 -23.367 6.667 1.00 81.43 A C ANISOU 1570 C GLU A 221 10664 7459 12817 1085 -2882 1297 A C ATOM 1571 O GLU A 221 57.373 -23.954 6.078 1.00 90.12 A O ANISOU 1571 O GLU A 221 11663 8536 14042 1341 -2958 1207 A O ATOM 1572 CB GLU A 221 54.292 -23.995 5.564 1.00 92.97 A C ANISOU 1572 CB GLU A 221 12352 8704 14268 844 -2654 1200 A C ATOM 1573 CG GLU A 221 54.781 -24.917 4.460 1.00101.27 A C ANISOU 1573 CG GLU A 221 13370 9642 15467 1083 -2682 1049 A C ATOM 1574 CD GLU A 221 53.678 -25.283 3.472 1.00102.77 A C ANISOU 1574 CD GLU A 221 13637 9741 15671 978 -2548 937 A C ATOM 1575 OE1 GLU A 221 52.486 -25.116 3.816 1.00 96.30 A O ANISOU 1575 OE1 GLU A 221 12944 8886 14758 723 -2470 1006 A O ATOM 1576 OE2 GLU A 221 54.007 -25.748 2.358 1.00104.77 A O1- ANISOU 1576 OE2 GLU A 221 13820 9967 16022 1150 -2523 777 A O1- ATOM 1577 N MET A 222 56.608 -22.145 7.175 1.00 73.98 A N ANISOU 1577 N MET A 222 9596 6742 11772 952 -2836 1343 A N ATOM 1578 CA MET A 222 57.871 -21.408 7.062 1.00 81.93 A C ANISOU 1578 CA MET A 222 10330 7991 12810 1077 -2877 1296 A C ATOM 1579 C MET A 222 58.996 -22.056 7.878 1.00 86.33 A C ANISOU 1579 C MET A 222 10898 8492 13413 1273 -3117 1385 A C ATOM 1580 O MET A 222 60.178 -21.837 7.606 1.00 79.98 A O ANISOU 1580 O MET A 222 9852 7856 12679 1449 -3179 1323 A O ATOM 1581 CB MET A 222 57.690 -19.939 7.469 1.00 77.10 A C ANISOU 1581 CB MET A 222 9620 7606 12067 861 -2776 1328 A C ATOM 1582 CG MET A 222 56.746 -19.144 6.562 1.00 76.81 A C ANISOU 1582 CG MET A 222 9526 7665 11991 708 -2543 1229 A C ATOM 1583 SD MET A 222 57.397 -18.856 4.895 1.00 73.68 A S ANISOU 1583 SD MET A 222 8841 7442 11711 868 -2420 1028 A S ATOM 1584 CE MET A 222 58.850 -17.862 5.243 1.00 70.63 A C ANISOU 1584 CE MET A 222 8194 7326 11317 913 -2489 1036 A C ATOM 1585 N TRP A 223 58.616 -22.849 8.878 1.00 87.74 A N ANISOU 1585 N TRP A 223 11352 8442 13544 1238 -3251 1534 A N ATOM 1586 CA TRP A 223 59.577 -23.572 9.704 1.00 85.80 A C ANISOU 1586 CA TRP A 223 11162 8108 13331 1431 -3497 1637 A C ATOM 1587 C TRP A 223 59.558 -25.064 9.387 1.00 94.14 A C ANISOU 1587 C TRP A 223 12402 8862 14503 1636 -3597 1627 A C ATOM 1588 O TRP A 223 60.610 -25.677 9.237 1.00 96.65 A O ANISOU 1588 O TRP A 223 12631 9159 14934 1923 -3744 1595 A O ATOM 1589 CB TRP A 223 59.299 -23.359 11.194 1.00 80.14 A C ANISOU 1589 CB TRP A 223 10643 7352 12454 1253 -3605 1834 A C ATOM 1590 CG TRP A 223 59.683 -22.001 11.705 1.00 80.48 A C ANISOU 1590 CG TRP A 223 10511 7680 12388 1114 -3580 1853 A C ATOM 1591 CD1 TRP A 223 60.907 -21.617 12.167 1.00 79.25 A C ANISOU 1591 CD1 TRP A 223 10172 7704 12235 1224 -3733 1876 A C ATOM 1592 CD2 TRP A 223 58.831 -20.848 11.818 1.00 78.51 A C ANISOU 1592 CD2 TRP A 223 10261 7561 12007 835 -3396 1847 A C ATOM 1593 CE2 TRP A 223 59.609 -19.805 12.355 1.00 78.23 A C ANISOU 1593 CE2 TRP A 223 10060 7764 11899 785 -3448 1865 A C ATOM 1594 CE3 TRP A 223 57.486 -20.600 11.518 1.00 73.19 A C ANISOU 1594 CE3 TRP A 223 9708 6831 11271 630 -3197 1826 A C ATOM 1595 NE1 TRP A 223 60.872 -20.298 12.558 1.00 81.67 A N ANISOU 1595 NE1 TRP A 223 10378 8233 12418 1015 -3657 1883 A N ATOM 1596 CZ2 TRP A 223 59.091 -18.533 12.592 1.00 77.11 A C ANISOU 1596 CZ2 TRP A 223 9895 7778 11624 545 -3306 1858 A C ATOM 1597 CZ3 TRP A 223 56.971 -19.339 11.762 1.00 68.05 A C ANISOU 1597 CZ3 TRP A 223 9016 6351 10490 410 -3056 1823 A C ATOM 1598 CH2 TRP A 223 57.771 -18.322 12.290 1.00 72.95 A C ANISOU 1598 CH2 TRP A 223 9496 7182 11041 373 -3109 1837 A C ATOM 1599 N THR A 224 58.368 -25.652 9.283 1.00 95.44 A N ANISOU 1599 N THR A 224 12825 8796 14644 1491 -3519 1650 A N ATOM 1600 CA THR A 224 58.278 -27.088 9.018 1.00 98.14 A C ANISOU 1600 CA THR A 224 13385 8815 15087 1656 -3616 1644 A C ATOM 1601 C THR A 224 58.660 -27.432 7.583 1.00100.41 A C ANISOU 1601 C THR A 224 13507 9117 15528 1875 -3539 1431 A C ATOM 1602 O THR A 224 58.872 -28.600 7.262 1.00104.45 A O ANISOU 1602 O THR A 224 14159 9381 16145 2082 -3636 1393 A O ATOM 1603 CB THR A 224 56.880 -27.676 9.312 1.00 90.11 A C ANISOU 1603 CB THR A 224 12700 7540 13999 1411 -3558 1730 A C ATOM 1604 CG2 THR A 224 56.438 -27.341 10.725 1.00 88.66 A C ANISOU 1604 CG2 THR A 224 12689 7353 13646 1183 -3613 1938 A C ATOM 1605 OG1 THR A 224 55.930 -27.168 8.367 1.00 82.15 A O ANISOU 1605 OG1 THR A 224 11610 6624 12981 1235 -3328 1601 A O ATOM 1606 N ARG A 225 58.734 -26.424 6.720 1.00 97.73 A N ANISOU 1606 N ARG A 225 12886 9055 15193 1831 -3364 1291 A N ATOM 1607 CA ARG A 225 59.152 -26.655 5.343 1.00 95.56 A C ANISOU 1607 CA ARG A 225 12433 8832 15042 2035 -3278 1084 A C ATOM 1608 C ARG A 225 58.231 -27.651 4.634 1.00 97.73 A C ANISOU 1608 C ARG A 225 12940 8828 15366 2017 -3220 1007 A C ATOM 1609 O ARG A 225 58.621 -28.289 3.657 1.00 97.64 A O ANISOU 1609 O ARG A 225 12882 8749 15467 2240 -3210 851 A O ATOM 1610 CB ARG A 225 60.585 -27.179 5.325 1.00 91.53 A C ANISOU 1610 CB ARG A 225 11781 8347 14648 2390 -3444 1048 A C ATOM 1611 CG ARG A 225 61.618 -26.131 5.637 1.00 88.57 A C ANISOU 1611 CG ARG A 225 11091 8312 14250 2425 -3470 1062 A C ATOM 1612 CD ARG A 225 61.912 -25.300 4.407 1.00 90.28 A C ANISOU 1612 CD ARG A 225 10992 8810 14499 2439 -3275 879 A C ATOM 1613 NE ARG A 225 62.783 -24.176 4.723 1.00 93.13 A N ANISOU 1613 NE ARG A 225 11063 9501 14821 2404 -3280 900 A N ATOM 1614 CZ ARG A 225 63.663 -23.650 3.879 1.00 93.29 A C ANISOU 1614 CZ ARG A 225 10754 9792 14899 2525 -3199 764 A C ATOM 1615 NH1 ARG A 225 63.800 -24.158 2.658 1.00 86.85 A N1+ ANISOU 1615 NH1 ARG A 225 9859 8962 14179 2708 -3101 591 A N1+ ATOM 1616 NH2 ARG A 225 64.416 -22.621 4.264 1.00 94.15 A N ANISOU 1616 NH2 ARG A 225 10619 10189 14963 2453 -3214 799 A N ATOM 1617 N SER A 226 57.004 -27.773 5.125 1.00 98.72 A N ANISOU 1617 N SER A 226 13311 8798 15400 1744 -3179 1109 A N ATOM 1618 CA SER A 226 56.077 -28.764 4.603 1.00102.85 A C ANISOU 1618 CA SER A 226 14078 9041 15958 1685 -3145 1058 A C ATOM 1619 C SER A 226 54.691 -28.550 5.201 1.00100.98 A C ANISOU 1619 C SER A 226 14033 8741 15595 1326 -3064 1178 A C ATOM 1620 O SER A 226 54.567 -28.226 6.384 1.00104.85 A O ANISOU 1620 O SER A 226 14606 9249 15982 1189 -3124 1354 A O ATOM 1621 CB SER A 226 56.588 -30.170 4.933 1.00105.52 A C ANISOU 1621 CB SER A 226 14657 9047 16389 1915 -3351 1103 A C ATOM 1622 OG SER A 226 55.779 -31.157 4.327 1.00112.23 A O ANISOU 1622 OG SER A 226 15746 9613 17284 1868 -3322 1030 A O ATOM 1623 N PRO A 227 53.642 -28.731 4.385 1.00 93.56 A N ANISOU 1623 N PRO A 227 13155 7740 14654 1174 -2927 1079 A N ATOM 1624 CA PRO A 227 52.261 -28.503 4.833 1.00 93.64 A C ANISOU 1624 CA PRO A 227 13306 7726 14546 830 -2828 1174 A C ATOM 1625 C PRO A 227 51.894 -29.333 6.064 1.00 89.90 A C ANISOU 1625 C PRO A 227 13154 6984 14020 714 -2964 1375 A C ATOM 1626 O PRO A 227 51.839 -30.555 5.997 1.00 88.57 A O ANISOU 1626 O PRO A 227 13226 6506 13920 779 -3068 1381 A O ATOM 1627 CB PRO A 227 51.422 -28.915 3.619 1.00 92.43 A C ANISOU 1627 CB PRO A 227 13180 7502 14439 762 -2711 1011 A C ATOM 1628 CG PRO A 227 52.338 -28.734 2.453 1.00 91.40 A C ANISOU 1628 CG PRO A 227 12818 7503 14407 1029 -2677 817 A C ATOM 1629 CD PRO A 227 53.712 -29.084 2.957 1.00 91.16 A C ANISOU 1629 CD PRO A 227 12764 7423 14449 1316 -2849 863 A C ATOM 1630 N ILE A 228 51.633 -28.649 7.173 1.00 90.41 A N ANISOU 1630 N ILE A 228 13235 7164 13954 535 -2957 1536 A N ATOM 1631 CA ILE A 228 51.387 -29.278 8.469 1.00 88.31 A C ANISOU 1631 CA ILE A 228 13258 6688 13607 420 -3084 1748 A C ATOM 1632 C ILE A 228 50.283 -30.344 8.496 1.00 90.43 A C ANISOU 1632 C ILE A 228 13829 6664 13867 221 -3076 1797 A C ATOM 1633 O ILE A 228 50.365 -31.294 9.276 1.00105.06 A O ANISOU 1633 O ILE A 228 15966 8242 15708 222 -3227 1942 A O ATOM 1634 CB ILE A 228 51.074 -28.212 9.536 1.00 87.01 A C ANISOU 1634 CB ILE A 228 13044 6740 13277 216 -3027 1886 A C ATOM 1635 CG1 ILE A 228 49.880 -27.361 9.091 1.00 84.49 A C ANISOU 1635 CG1 ILE A 228 12606 6615 12881 -39 -2798 1818 A C ATOM 1636 CG2 ILE A 228 52.287 -27.329 9.760 1.00 89.65 A C ANISOU 1636 CG2 ILE A 228 13143 7308 13613 403 -3088 1875 A C ATOM 1637 CD1 ILE A 228 49.368 -26.402 10.141 1.00 79.58 A C ANISOU 1637 CD1 ILE A 228 11977 6175 12086 -257 -2723 1947 A C ATOM 1638 N MET A 229 49.263 -30.192 7.655 1.00 84.55 A N ANISOU 1638 N MET A 229 13026 5976 13122 45 -2908 1682 A N ATOM 1639 CA MET A 229 48.113 -31.101 7.662 1.00 94.76 A C ANISOU 1639 CA MET A 229 14577 7031 14396 -195 -2883 1722 A C ATOM 1640 C MET A 229 47.722 -31.584 6.261 1.00100.20 A C ANISOU 1640 C MET A 229 15234 7646 15193 -169 -2814 1516 A C ATOM 1641 O MET A 229 46.960 -30.914 5.558 1.00 96.68 A O ANISOU 1641 O MET A 229 14608 7409 14717 -310 -2647 1409 A O ATOM 1642 CB MET A 229 46.912 -30.424 8.323 1.00 96.39 A C ANISOU 1642 CB MET A 229 14778 7401 14445 -542 -2738 1829 A C ATOM 1643 CG MET A 229 47.085 -30.178 9.808 1.00 97.09 A C ANISOU 1643 CG MET A 229 14984 7504 14402 -622 -2808 2047 A C ATOM 1644 SD MET A 229 45.715 -29.235 10.499 1.00125.97 A S ANISOU 1644 SD MET A 229 18589 11406 17868 -995 -2607 2139 A S ATOM 1645 CE MET A 229 45.980 -27.656 9.713 1.00101.82 A C ANISOU 1645 CE MET A 229 15128 8741 14816 -884 -2456 1969 A C ATOM 1646 N GLN A 230 48.219 -32.759 5.876 1.00109.24 A N ANISOU 1646 N GLN A 230 16568 8485 16454 13 -2949 1463 A N ATOM 1647 CA GLN A 230 48.071 -33.250 4.504 1.00112.31 A C ANISOU 1647 CA GLN A 230 16930 8794 16948 94 -2904 1245 A C ATOM 1648 C GLN A 230 47.052 -34.375 4.353 1.00113.40 A C ANISOU 1648 C GLN A 230 17370 8624 17094 -132 -2920 1251 A C ATOM 1649 O GLN A 230 47.415 -35.500 4.024 1.00112.68 A O ANISOU 1649 O GLN A 230 17500 8213 17101 14 -3042 1196 A O ATOM 1650 CB GLN A 230 49.424 -33.713 3.960 1.00112.34 A C ANISOU 1650 CB GLN A 230 16899 8699 17088 498 -3026 1130 A C ATOM 1651 CG GLN A 230 50.582 -32.829 4.380 1.00110.43 A C ANISOU 1651 CG GLN A 230 16414 8704 16842 721 -3063 1169 A C ATOM 1652 CD GLN A 230 51.847 -33.113 3.603 1.00108.27 A C ANISOU 1652 CD GLN A 230 16016 8422 16701 1113 -3136 1013 A C ATOM 1653 NE2 GLN A 230 52.990 -32.759 4.181 1.00101.63 A N ANISOU 1653 NE2 GLN A 230 15046 7694 15876 1334 -3238 1081 A N ATOM 1654 OE1 GLN A 230 51.799 -33.638 2.493 1.00114.48 A O ANISOU 1654 OE1 GLN A 230 16814 9114 17570 1214 -3101 828 A O ATOM 1655 N GLY A 231 45.778 -34.060 4.566 1.00117.64 A N ANISOU 1655 N GLY A 231 17908 9262 17528 -488 -2795 1308 A N ATOM 1656 CA GLY A 231 44.718 -35.049 4.470 1.00122.41 A C ANISOU 1656 CA GLY A 231 18775 9611 18126 -759 -2797 1323 A C ATOM 1657 C GLY A 231 44.547 -35.645 3.084 1.00126.24 A C ANISOU 1657 C GLY A 231 19271 9982 18712 -698 -2783 1092 A C ATOM 1658 O GLY A 231 45.105 -35.148 2.106 1.00126.06 A O ANISOU 1658 O GLY A 231 19014 10135 18748 -472 -2734 910 A O ATOM 1659 N ASN A 232 43.769 -36.721 3.001 1.00128.03 A N ANISOU 1659 N ASN A 232 19783 9912 18950 -915 -2824 1098 A N ATOM 1660 CA ASN A 232 43.505 -37.378 1.726 1.00125.08 A C ANISOU 1660 CA ASN A 232 19464 9403 18660 -897 -2820 878 A C ATOM 1661 C ASN A 232 42.047 -37.261 1.318 1.00121.82 A C ANISOU 1661 C ASN A 232 18999 9110 18176 -1284 -2691 833 A C ATOM 1662 O ASN A 232 41.720 -37.285 0.132 1.00120.82 A O ANISOU 1662 O ASN A 232 18773 9049 18085 -1287 -2635 627 A O ATOM 1663 CB ASN A 232 43.941 -38.839 1.776 1.00130.00 A C ANISOU 1663 CB ASN A 232 20480 9541 19375 -784 -2998 880 A C ATOM 1664 CG ASN A 232 45.447 -38.988 1.771 1.00134.43 A C ANISOU 1664 CG ASN A 232 21037 10009 20031 -327 -3122 845 A C ATOM 1665 ND2 ASN A 232 46.097 -38.345 0.806 1.00135.10 A N ANISOU 1665 ND2 ASN A 232 20826 10338 20167 -64 -3056 651 A N ATOM 1666 OD1 ASN A 232 46.024 -39.656 2.631 1.00136.22 A O ANISOU 1666 OD1 ASN A 232 21516 9962 20281 -212 -3276 995 A O ATOM 1667 N THR A 233 41.176 -37.140 2.315 1.00121.27 A N ANISOU 1667 N THR A 233 18993 9082 18002 -1610 -2645 1027 A N ATOM 1668 CA THR A 233 39.772 -36.820 2.084 1.00119.55 A C ANISOU 1668 CA THR A 233 18658 9065 17703 -1981 -2505 1009 A C ATOM 1669 C THR A 233 39.331 -35.789 3.118 1.00111.75 A C ANISOU 1669 C THR A 233 17495 8379 16585 -2141 -2394 1189 A C ATOM 1670 O THR A 233 40.041 -35.540 4.093 1.00111.72 A O ANISOU 1670 O THR A 233 17537 8361 16552 -2012 -2446 1343 A O ATOM 1671 CB THR A 233 38.860 -38.070 2.179 1.00115.44 A C ANISOU 1671 CB THR A 233 18463 8217 17181 -2312 -2561 1048 A C ATOM 1672 CG2 THR A 233 39.403 -39.203 1.320 1.00116.23 A C ANISOU 1672 CG2 THR A 233 18809 7947 17406 -2134 -2696 886 A C ATOM 1673 OG1 THR A 233 38.768 -38.505 3.542 1.00118.01 A O ANISOU 1673 OG1 THR A 233 19039 8357 17442 -2473 -2620 1301 A O ATOM 1674 N GLU A 234 38.163 -35.192 2.903 1.00104.37 A N ANISOU 1674 N GLU A 234 16361 7723 15571 -2412 -2244 1163 A N ATOM 1675 CA GLU A 234 37.609 -34.236 3.858 1.00106.20 A C ANISOU 1675 CA GLU A 234 16433 8245 15672 -2578 -2123 1319 A C ATOM 1676 C GLU A 234 37.566 -34.787 5.290 1.00111.91 A C ANISOU 1676 C GLU A 234 17434 8766 16323 -2741 -2184 1567 A C ATOM 1677 O GLU A 234 37.884 -34.080 6.252 1.00106.38 A O ANISOU 1677 O GLU A 234 16673 8209 15537 -2691 -2156 1708 A O ATOM 1678 CB GLU A 234 36.215 -33.783 3.420 1.00107.52 A C ANISOU 1678 CB GLU A 234 16393 8691 15771 -2875 -1968 1258 A C ATOM 1679 CG GLU A 234 36.182 -33.126 2.050 1.00114.65 A C ANISOU 1679 CG GLU A 234 17013 9828 16720 -2726 -1902 1030 A C ATOM 1680 CD GLU A 234 34.927 -32.305 1.835 1.00121.42 A C ANISOU 1680 CD GLU A 234 17599 11050 17486 -2956 -1740 1003 A C ATOM 1681 OE1 GLU A 234 34.090 -32.258 2.761 1.00124.91 A O ANISOU 1681 OE1 GLU A 234 18061 11568 17832 -3230 -1671 1155 A O ATOM 1682 OE2 GLU A 234 34.779 -31.703 0.749 1.00119.43 A O1- ANISOU 1682 OE2 GLU A 234 17112 11014 17252 -2856 -1682 833 A O1- ATOM 1683 N GLN A 235 37.173 -36.049 5.433 1.00118.83 A N ANISOU 1683 N GLN A 235 18627 9301 17221 -2944 -2271 1621 A N ATOM 1684 CA GLN A 235 37.136 -36.670 6.753 1.00121.97 A C ANISOU 1684 CA GLN A 235 19326 9474 17543 -3107 -2339 1864 A C ATOM 1685 C GLN A 235 38.532 -36.827 7.346 1.00114.64 A C ANISOU 1685 C GLN A 235 18553 8352 16655 -2768 -2495 1954 A C ATOM 1686 O GLN A 235 38.730 -36.626 8.545 1.00111.17 A O ANISOU 1686 O GLN A 235 18202 7924 16115 -2802 -2513 2156 A O ATOM 1687 CB GLN A 235 36.411 -38.014 6.714 1.00130.87 A C ANISOU 1687 CB GLN A 235 20781 10256 18688 -3412 -2401 1901 A C ATOM 1688 CG GLN A 235 34.904 -37.879 6.784 1.00142.04 A C ANISOU 1688 CG GLN A 235 22086 11879 20004 -3854 -2245 1928 A C ATOM 1689 CD GLN A 235 34.236 -39.108 7.367 1.00159.23 A C ANISOU 1689 CD GLN A 235 24630 13726 22143 -4219 -2300 2076 A C ATOM 1690 NE2 GLN A 235 33.080 -38.909 7.994 1.00163.07 A N ANISOU 1690 NE2 GLN A 235 25048 14412 22499 -4608 -2161 2196 A N ATOM 1691 OE1 GLN A 235 34.750 -40.224 7.256 1.00166.85 A O ANISOU 1691 OE1 GLN A 235 25942 14262 23192 -4152 -2463 2082 A O ATOM 1692 N HIS A 236 39.497 -37.186 6.506 1.00108.62 A N ANISOU 1692 N HIS A 236 17815 7424 16031 -2438 -2608 1801 A N ATOM 1693 CA HIS A 236 40.880 -37.286 6.952 1.00106.12 A C ANISOU 1693 CA HIS A 236 17593 6962 15765 -2079 -2759 1862 A C ATOM 1694 C HIS A 236 41.391 -35.904 7.352 1.00108.96 A C ANISOU 1694 C HIS A 236 17638 7702 16061 -1919 -2682 1891 A C ATOM 1695 O HIS A 236 42.101 -35.752 8.352 1.00109.71 A O ANISOU 1695 O HIS A 236 17808 7769 16106 -1800 -2767 2050 A O ATOM 1696 CB HIS A 236 41.759 -37.900 5.859 1.00106.89 A C ANISOU 1696 CB HIS A 236 17738 6848 16025 -1750 -2871 1664 A C ATOM 1697 CG HIS A 236 43.156 -38.204 6.306 1.00114.93 A C ANISOU 1697 CG HIS A 236 18879 7682 17109 -1379 -3045 1726 A C ATOM 1698 CD2 HIS A 236 43.669 -38.430 7.540 1.00118.92 A C ANISOU 1698 CD2 HIS A 236 19578 8048 17558 -1331 -3165 1949 A C ATOM 1699 ND1 HIS A 236 44.219 -38.284 5.431 1.00114.88 A N ANISOU 1699 ND1 HIS A 236 18779 7638 17233 -990 -3116 1546 A N ATOM 1700 CE1 HIS A 236 45.322 -38.557 6.104 1.00115.12 A C ANISOU 1700 CE1 HIS A 236 18927 7518 17294 -715 -3274 1653 A C ATOM 1701 NE2 HIS A 236 45.017 -38.648 7.386 1.00119.24 A N ANISOU 1701 NE2 HIS A 236 19629 7972 17703 -913 -3314 1899 A N ATOM 1702 N GLN A 237 41.011 -34.896 6.571 1.00103.66 A N ANISOU 1702 N GLN A 237 16624 7378 15383 -1925 -2527 1739 A N ATOM 1703 CA GLN A 237 41.386 -33.518 6.854 1.00100.82 A C ANISOU 1703 CA GLN A 237 15966 7381 14959 -1802 -2439 1750 A C ATOM 1704 C GLN A 237 40.798 -33.078 8.191 1.00101.19 A C ANISOU 1704 C GLN A 237 16056 7549 14843 -2047 -2374 1964 A C ATOM 1705 O GLN A 237 41.496 -32.500 9.026 1.00 91.05 A O ANISOU 1705 O GLN A 237 14740 6356 13498 -1919 -2411 2072 A O ATOM 1706 CB GLN A 237 40.911 -32.587 5.732 1.00 97.37 A C ANISOU 1706 CB GLN A 237 15193 7269 14536 -1802 -2280 1555 A C ATOM 1707 CG GLN A 237 41.600 -31.231 5.714 1.00 99.80 A C ANISOU 1707 CG GLN A 237 15204 7897 14818 -1589 -2215 1518 A C ATOM 1708 CD GLN A 237 43.093 -31.328 5.422 1.00102.19 A C ANISOU 1708 CD GLN A 237 15489 8109 15228 -1213 -2345 1454 A C ATOM 1709 NE2 GLN A 237 43.450 -32.110 4.407 1.00103.21 A N ANISOU 1709 NE2 GLN A 237 15679 8054 15482 -1060 -2412 1300 A N ATOM 1710 OE1 GLN A 237 43.915 -30.710 6.107 1.00100.08 A O ANISOU 1710 OE1 GLN A 237 15152 7946 14928 -1065 -2385 1538 A O ATOM 1711 N LEU A 238 39.512 -33.361 8.391 1.00106.82 A N ANISOU 1711 N LEU A 238 16839 8271 15478 -2404 -2276 2020 A N ATOM 1712 CA LEU A 238 38.839 -32.987 9.632 1.00109.91 A C ANISOU 1712 CA LEU A 238 17270 8790 15701 -2660 -2191 2215 A C ATOM 1713 C LEU A 238 39.440 -33.716 10.826 1.00113.80 A C ANISOU 1713 C LEU A 238 18092 9002 16143 -2646 -2346 2430 A C ATOM 1714 O LEU A 238 39.502 -33.178 11.934 1.00113.61 A O ANISOU 1714 O LEU A 238 18081 9103 15984 -2697 -2321 2587 A O ATOM 1715 CB LEU A 238 37.336 -33.249 9.545 1.00110.87 A C ANISOU 1715 CB LEU A 238 17391 8978 15757 -3053 -2056 2224 A C ATOM 1716 CG LEU A 238 36.481 -32.034 9.179 1.00112.42 A C ANISOU 1716 CG LEU A 238 17228 9600 15887 -3149 -1851 2129 A C ATOM 1717 CD1 LEU A 238 35.043 -32.454 8.907 1.00117.27 A C ANISOU 1717 CD1 LEU A 238 17827 10266 16464 -3516 -1741 2112 A C ATOM 1718 CD2 LEU A 238 36.541 -30.978 10.279 1.00104.06 A C ANISOU 1718 CD2 LEU A 238 16069 8791 14679 -3146 -1765 2258 A C ATOM 1719 N ALA A 239 39.884 -34.946 10.594 1.00112.88 A N ANISOU 1719 N ALA A 239 18257 8501 16131 -2569 -2510 2435 A N ATOM 1720 CA ALA A 239 40.543 -35.709 11.636 1.00110.80 A C ANISOU 1720 CA ALA A 239 18328 7939 15833 -2512 -2683 2636 A C ATOM 1721 C ALA A 239 41.891 -35.072 11.926 1.00108.41 A C ANISOU 1721 C ALA A 239 17909 7729 15552 -2142 -2786 2642 A C ATOM 1722 O ALA A 239 42.228 -34.822 13.084 1.00114.11 A O ANISOU 1722 O ALA A 239 18719 8482 16156 -2143 -2836 2823 A O ATOM 1723 CB ALA A 239 40.713 -37.159 11.214 1.00107.68 A C ANISOU 1723 CB ALA A 239 18262 7095 15555 -2487 -2838 2621 A C ATOM 1724 N LEU A 240 42.659 -34.808 10.872 1.00 98.96 A N ANISOU 1724 N LEU A 240 16511 6591 14500 -1835 -2815 2442 A N ATOM 1725 CA LEU A 240 43.982 -34.214 11.034 1.00103.15 A C ANISOU 1725 CA LEU A 240 16900 7226 15065 -1484 -2911 2428 A C ATOM 1726 C LEU A 240 43.910 -32.905 11.812 1.00101.82 A C ANISOU 1726 C LEU A 240 16523 7414 14752 -1551 -2805 2506 A C ATOM 1727 O LEU A 240 44.693 -32.691 12.742 1.00 99.48 A O ANISOU 1727 O LEU A 240 16281 7125 14392 -1428 -2914 2638 A O ATOM 1728 CB LEU A 240 44.665 -34.008 9.681 1.00104.63 A C ANISOU 1728 CB LEU A 240 16857 7484 15415 -1189 -2912 2184 A C ATOM 1729 CG LEU A 240 45.271 -35.277 9.079 1.00113.57 A C ANISOU 1729 CG LEU A 240 18210 8242 16698 -979 -3075 2111 A C ATOM 1730 CD1 LEU A 240 46.017 -34.976 7.791 1.00115.42 A C ANISOU 1730 CD1 LEU A 240 18192 8588 17073 -672 -3060 1868 A C ATOM 1731 CD2 LEU A 240 46.195 -35.934 10.083 1.00117.03 A C ANISOU 1731 CD2 LEU A 240 18906 8429 17133 -804 -3287 2290 A C ATOM 1732 N ILE A 241 42.963 -32.047 11.432 1.00 98.50 A N ANISOU 1732 N ILE A 241 15870 7282 14274 -1742 -2600 2422 A N ATOM 1733 CA ILE A 241 42.721 -30.777 12.122 1.00101.72 A C ANISOU 1733 CA ILE A 241 16090 8023 14534 -1829 -2475 2479 A C ATOM 1734 C ILE A 241 42.458 -30.968 13.618 1.00103.92 A C ANISOU 1734 C ILE A 241 16604 8239 14641 -2022 -2507 2721 A C ATOM 1735 O ILE A 241 42.939 -30.194 14.449 1.00 99.49 A O ANISOU 1735 O ILE A 241 15989 7839 13975 -1959 -2521 2804 A O ATOM 1736 CB ILE A 241 41.535 -29.988 11.488 1.00 87.84 A C ANISOU 1736 CB ILE A 241 14088 6549 12737 -2029 -2247 2361 A C ATOM 1737 CG1 ILE A 241 41.970 -29.310 10.182 1.00 83.95 A C ANISOU 1737 CG1 ILE A 241 13302 6229 12368 -1803 -2198 2137 A C ATOM 1738 CG2 ILE A 241 40.989 -28.943 12.463 1.00 80.98 A C ANISOU 1738 CG2 ILE A 241 13127 5957 11686 -2194 -2112 2464 A C ATOM 1739 CD1 ILE A 241 40.861 -28.534 9.491 1.00 77.09 A C ANISOU 1739 CD1 ILE A 241 12193 5632 11464 -1963 -1995 2019 A C ATOM 1740 N SER A 242 41.691 -31.999 13.957 1.00107.88 A N ANISOU 1740 N SER A 242 17377 8508 15106 -2269 -2520 2833 A N ATOM 1741 CA SER A 242 41.391 -32.297 15.353 1.00111.37 A C ANISOU 1741 CA SER A 242 18073 8869 15373 -2476 -2547 3073 A C ATOM 1742 C SER A 242 42.633 -32.763 16.107 1.00109.91 A C ANISOU 1742 C SER A 242 18105 8469 15188 -2243 -2781 3209 A C ATOM 1743 O SER A 242 42.811 -32.447 17.285 1.00105.13 A O ANISOU 1743 O SER A 242 17595 7929 14422 -2294 -2813 3378 A O ATOM 1744 CB SER A 242 40.280 -33.345 15.458 1.00118.76 A C ANISOU 1744 CB SER A 242 19254 9594 16275 -2813 -2504 3160 A C ATOM 1745 OG SER A 242 39.005 -32.759 15.255 1.00120.47 A O ANISOU 1745 OG SER A 242 19276 10082 16415 -3092 -2275 3103 A O ATOM 1746 N GLN A 243 43.490 -33.510 15.418 1.00113.49 A N ANISOU 1746 N GLN A 243 18631 8675 15816 -1979 -2946 3131 A N ATOM 1747 CA GLN A 243 44.713 -34.024 16.022 1.00117.52 A C ANISOU 1747 CA GLN A 243 19329 8974 16348 -1717 -3186 3246 A C ATOM 1748 C GLN A 243 45.744 -32.916 16.222 1.00116.60 A C ANISOU 1748 C GLN A 243 18951 9132 16218 -1460 -3224 3202 A C ATOM 1749 O GLN A 243 46.811 -33.145 16.801 1.00117.96 A O ANISOU 1749 O GLN A 243 19223 9204 16393 -1235 -3423 3297 A O ATOM 1750 CB GLN A 243 45.295 -35.157 15.175 1.00121.21 A C ANISOU 1750 CB GLN A 243 19943 9100 17012 -1492 -3342 3157 A C ATOM 1751 CG GLN A 243 44.436 -36.415 15.151 1.00127.92 A C ANISOU 1751 CG GLN A 243 21135 9601 17867 -1741 -3356 3233 A C ATOM 1752 CD GLN A 243 44.869 -37.384 14.072 1.00131.15 A C ANISOU 1752 CD GLN A 243 21643 9709 18479 -1528 -3467 3083 A C ATOM 1753 NE2 GLN A 243 44.169 -38.510 13.962 1.00122.98 A N ANISOU 1753 NE2 GLN A 243 20920 8343 17462 -1738 -3491 3130 A N ATOM 1754 OE1 GLN A 243 45.822 -37.120 13.338 1.00138.23 A O ANISOU 1754 OE1 GLN A 243 22340 10672 19509 -1183 -3526 2923 A O ATOM 1755 N LEU A 244 45.419 -31.715 15.749 1.00108.24 A N ANISOU 1755 N LEU A 244 17561 8421 15143 -1499 -3040 3062 A N ATOM 1756 CA LEU A 244 46.301 -30.567 15.922 1.00 99.10 A C ANISOU 1756 CA LEU A 244 16152 7539 13963 -1302 -3055 3014 A C ATOM 1757 C LEU A 244 45.681 -29.464 16.769 1.00 99.42 A C ANISOU 1757 C LEU A 244 16105 7867 13802 -1520 -2904 3086 A C ATOM 1758 O LEU A 244 46.335 -28.910 17.655 1.00100.72 A O ANISOU 1758 O LEU A 244 16267 8141 13861 -1450 -2983 3177 A O ATOM 1759 CB LEU A 244 46.726 -29.987 14.575 1.00 94.37 A C ANISOU 1759 CB LEU A 244 15229 7102 13526 -1094 -2989 2772 A C ATOM 1760 CG LEU A 244 47.802 -28.903 14.710 1.00 93.45 A C ANISOU 1760 CG LEU A 244 14867 7237 13404 -878 -3031 2725 A C ATOM 1761 CD1 LEU A 244 49.091 -29.524 15.205 1.00 93.80 A C ANISOU 1761 CD1 LEU A 244 15033 7109 13498 -616 -3285 2814 A C ATOM 1762 CD2 LEU A 244 48.030 -28.177 13.396 1.00 92.97 A C ANISOU 1762 CD2 LEU A 244 14478 7376 13469 -736 -2920 2495 A C ATOM 1763 N CYS A 245 44.423 -29.139 16.497 1.00 99.54 A N ANISOU 1763 N CYS A 245 16046 8013 13762 -1777 -2690 3038 A N ATOM 1764 CA CYS A 245 43.810 -27.964 17.110 1.00108.47 A C ANISOU 1764 CA CYS A 245 17045 9450 14720 -1946 -2518 3060 A C ATOM 1765 C CYS A 245 42.840 -28.312 18.235 1.00107.71 A C ANISOU 1765 C CYS A 245 17185 9313 14428 -2260 -2451 3250 A C ATOM 1766 O CYS A 245 42.064 -27.465 18.679 1.00100.87 A O ANISOU 1766 O CYS A 245 16222 8692 13413 -2438 -2273 3259 A O ATOM 1767 CB CYS A 245 43.096 -27.122 16.043 1.00115.57 A C ANISOU 1767 CB CYS A 245 17643 10592 15675 -1987 -2309 2864 A C ATOM 1768 SG CYS A 245 44.075 -26.793 14.543 1.00104.70 A S ANISOU 1768 SG CYS A 245 15994 9264 14525 -1657 -2355 2630 A S ATOM 1769 N GLY A 246 42.898 -29.553 18.704 1.00113.29 A N ANISOU 1769 N GLY A 246 18207 9708 15128 -2321 -2591 3404 A N ATOM 1770 CA GLY A 246 41.903 -30.051 19.635 1.00115.75 A C ANISOU 1770 CA GLY A 246 18761 9952 15266 -2649 -2518 3585 A C ATOM 1771 C GLY A 246 40.709 -30.508 18.827 1.00120.43 A C ANISOU 1771 C GLY A 246 19316 10514 15926 -2875 -2364 3503 A C ATOM 1772 O GLY A 246 40.772 -30.539 17.601 1.00116.27 A O ANISOU 1772 O GLY A 246 18617 9981 15579 -2752 -2348 3319 A O ATOM 1773 N SER A 247 39.617 -30.859 19.493 1.00130.20 A N ANISOU 1773 N SER A 247 20706 11748 17014 -3214 -2248 3635 A N ATOM 1774 CA SER A 247 38.454 -31.364 18.772 1.00130.95 A C ANISOU 1774 CA SER A 247 20770 11817 17168 -3460 -2112 3567 A C ATOM 1775 C SER A 247 37.310 -30.360 18.716 1.00128.71 A C ANISOU 1775 C SER A 247 20211 11910 16781 -3658 -1848 3489 A C ATOM 1776 O SER A 247 37.160 -29.509 19.595 1.00125.93 A O ANISOU 1776 O SER A 247 19804 11790 16253 -3707 -1751 3556 A O ATOM 1777 CB SER A 247 37.984 -32.698 19.356 1.00135.97 A C ANISOU 1777 CB SER A 247 21780 12138 17745 -3722 -2178 3759 A C ATOM 1778 OG SER A 247 37.876 -32.631 20.764 1.00139.74 A O ANISOU 1778 OG SER A 247 22453 12647 17996 -3877 -2169 3978 A O ATOM 1779 N ILE A 248 36.512 -30.472 17.660 1.00127.94 A N ANISOU 1779 N ILE A 248 19945 11872 16794 -3758 -1738 3342 A N ATOM 1780 CA ILE A 248 35.397 -29.568 17.420 1.00121.02 A C ANISOU 1780 CA ILE A 248 18781 11354 15849 -3916 -1497 3246 A C ATOM 1781 C ILE A 248 34.359 -29.705 18.531 1.00120.76 A C ANISOU 1781 C ILE A 248 18864 11417 15601 -4268 -1355 3417 A C ATOM 1782 O ILE A 248 33.639 -30.701 18.604 1.00113.99 A O ANISOU 1782 O ILE A 248 18176 10404 14733 -4547 -1342 3503 A O ATOM 1783 CB ILE A 248 34.733 -29.866 16.059 1.00115.32 A C ANISOU 1783 CB ILE A 248 17888 10642 15286 -3974 -1438 3068 A C ATOM 1784 CG1 ILE A 248 35.721 -30.557 15.109 1.00110.58 A C ANISOU 1784 CG1 ILE A 248 17368 9753 14895 -3723 -1635 2968 A C ATOM 1785 CG2 ILE A 248 34.169 -28.599 15.441 1.00100.53 A C ANISOU 1785 CG2 ILE A 248 15635 9154 13409 -3920 -1254 2899 A C ATOM 1786 CD1 ILE A 248 36.718 -29.633 14.464 1.00 87.77 A C ANISOU 1786 CD1 ILE A 248 14254 6992 12104 -3359 -1678 2815 A C ATOM 1787 N THR A 249 34.290 -28.699 19.396 1.00126.88 A N ANISOU 1787 N THR A 249 19554 12451 16202 -4260 -1247 3465 A N ATOM 1788 CA THR A 249 33.409 -28.744 20.554 1.00134.00 A C ANISOU 1788 CA THR A 249 20570 13469 16875 -4567 -1105 3630 A C ATOM 1789 C THR A 249 32.563 -27.489 20.633 1.00128.62 A C ANISOU 1789 C THR A 249 19582 13207 16082 -4613 -861 3534 A C ATOM 1790 O THR A 249 33.086 -26.386 20.545 1.00124.23 A O ANISOU 1790 O THR A 249 18854 12824 15525 -4369 -845 3432 A O ATOM 1791 CB THR A 249 34.218 -28.850 21.855 1.00139.96 A C ANISOU 1791 CB THR A 249 21609 14099 17471 -4521 -1229 3826 A C ATOM 1792 CG2 THR A 249 33.293 -28.860 23.059 1.00143.91 A C ANISOU 1792 CG2 THR A 249 22226 14738 17712 -4843 -1066 3995 A C ATOM 1793 OG1 THR A 249 34.991 -30.055 21.839 1.00143.30 A O ANISOU 1793 OG1 THR A 249 22336 14120 17991 -4465 -1466 3930 A O ATOM 1794 N PRO A 250 31.245 -27.652 20.805 1.00127.77 A N ANISOU 1794 N PRO A 250 19404 13264 15878 -4928 -668 3565 A N ATOM 1795 CA PRO A 250 30.368 -26.489 20.967 1.00124.22 A C ANISOU 1795 CA PRO A 250 18668 13222 15307 -4969 -425 3481 A C ATOM 1796 C PRO A 250 30.851 -25.595 22.105 1.00120.90 A C ANISOU 1796 C PRO A 250 18312 12933 14690 -4858 -394 3552 A C ATOM 1797 O PRO A 250 30.461 -24.430 22.185 1.00119.02 A O ANISOU 1797 O PRO A 250 17847 13005 14371 -4781 -230 3452 A O ATOM 1798 CB PRO A 250 29.017 -27.119 21.313 1.00123.66 A C ANISOU 1798 CB PRO A 250 18609 13247 15129 -5369 -258 3572 A C ATOM 1799 CG PRO A 250 29.071 -28.473 20.686 1.00119.95 A C ANISOU 1799 CG PRO A 250 18316 12444 14816 -5501 -406 3607 A C ATOM 1800 CD PRO A 250 30.497 -28.921 20.823 1.00121.97 A C ANISOU 1800 CD PRO A 250 18846 12350 15149 -5262 -664 3673 A C ATOM 1801 N GLU A 251 31.694 -26.141 22.975 1.00120.08 A N ANISOU 1801 N GLU A 251 18527 12589 14508 -4845 -559 3720 A N ATOM 1802 CA GLU A 251 32.288 -25.357 24.045 1.00121.70 A C ANISOU 1802 CA GLU A 251 18822 12891 14529 -4731 -568 3787 A C ATOM 1803 C GLU A 251 33.401 -24.498 23.480 1.00115.72 A C ANISOU 1803 C GLU A 251 17928 12141 13898 -4366 -689 3640 A C ATOM 1804 O GLU A 251 33.524 -23.318 23.806 1.00113.56 A O ANISOU 1804 O GLU A 251 17529 12094 13525 -4241 -604 3568 A O ATOM 1805 CB GLU A 251 32.859 -26.262 25.128 1.00132.56 A C ANISOU 1805 CB GLU A 251 20586 14003 15776 -4832 -727 4021 A C ATOM 1806 CG GLU A 251 33.895 -25.563 25.982 1.00141.64 A C ANISOU 1806 CG GLU A 251 21842 15175 16799 -4627 -836 4067 A C ATOM 1807 CD GLU A 251 34.614 -26.506 26.914 1.00154.41 A C ANISOU 1807 CD GLU A 251 23843 16505 18319 -4675 -1042 4293 A C ATOM 1808 OE1 GLU A 251 34.019 -27.538 27.290 1.00158.67 A O ANISOU 1808 OE1 GLU A 251 24597 16898 18791 -4947 -1024 4452 A O ATOM 1809 OE2 GLU A 251 35.775 -26.213 27.271 1.00158.02 A O1- ANISOU 1809 OE2 GLU A 251 24391 16885 18765 -4444 -1227 4315 A O1- ATOM 1810 N VAL A 252 34.217 -25.112 22.634 1.00112.24 A N ANISOU 1810 N VAL A 252 17523 11448 13675 -4201 -887 3596 A N ATOM 1811 CA VAL A 252 35.326 -24.434 21.981 1.00105.47 A C ANISOU 1811 CA VAL A 252 16531 10582 12960 -3864 -1012 3459 A C ATOM 1812 C VAL A 252 34.812 -23.524 20.860 1.00110.29 A C ANISOU 1812 C VAL A 252 16792 11430 13683 -3768 -861 3241 A C ATOM 1813 O VAL A 252 35.262 -22.386 20.694 1.00108.74 A O ANISOU 1813 O VAL A 252 16432 11396 13488 -3566 -836 3129 A O ATOM 1814 CB VAL A 252 36.332 -25.478 21.432 1.00 97.75 A C ANISOU 1814 CB VAL A 252 15707 9259 12175 -3719 -1264 3482 A C ATOM 1815 CG1 VAL A 252 37.199 -24.896 20.353 1.00 95.82 A C ANISOU 1815 CG1 VAL A 252 15247 9036 12124 -3409 -1345 3298 A C ATOM 1816 CG2 VAL A 252 37.198 -26.016 22.557 1.00 99.69 A C ANISOU 1816 CG2 VAL A 252 16267 9300 12308 -3696 -1452 3678 A C ATOM 1817 N TRP A 253 33.833 -24.033 20.125 1.00112.44 A N ANISOU 1817 N TRP A 253 16961 11722 14039 -3929 -762 3188 A N ATOM 1818 CA TRP A 253 33.312 -23.393 18.927 1.00103.56 A C ANISOU 1818 CA TRP A 253 15521 10787 13039 -3845 -648 2990 A C ATOM 1819 C TRP A 253 31.792 -23.307 19.043 1.00104.05 A C ANISOU 1819 C TRP A 253 15449 11086 12999 -4109 -418 2987 A C ATOM 1820 O TRP A 253 31.072 -24.171 18.531 1.00 98.54 A O ANISOU 1820 O TRP A 253 14741 10324 12375 -4301 -397 2988 A O ATOM 1821 CB TRP A 253 33.695 -24.248 17.720 1.00102.05 A C ANISOU 1821 CB TRP A 253 15325 10369 13080 -3764 -790 2908 A C ATOM 1822 CG TRP A 253 33.267 -23.732 16.392 1.00 97.74 A C ANISOU 1822 CG TRP A 253 14483 9983 12671 -3669 -708 2708 A C ATOM 1823 CD1 TRP A 253 32.397 -22.713 16.141 1.00 93.31 A C ANISOU 1823 CD1 TRP A 253 13660 9740 12053 -3681 -514 2606 A C ATOM 1824 CD2 TRP A 253 33.663 -24.248 15.116 1.00 90.32 A C ANISOU 1824 CD2 TRP A 253 13487 8888 11940 -3544 -820 2587 A C ATOM 1825 CE2 TRP A 253 33.006 -23.484 14.134 1.00 84.56 A C ANISOU 1825 CE2 TRP A 253 12461 8403 11264 -3495 -689 2420 A C ATOM 1826 CE3 TRP A 253 34.517 -25.276 14.710 1.00 89.55 A C ANISOU 1826 CE3 TRP A 253 13569 8472 11985 -3456 -1018 2599 A C ATOM 1827 NE1 TRP A 253 32.241 -22.551 14.783 1.00 89.67 A N ANISOU 1827 NE1 TRP A 253 12987 9334 11751 -3573 -508 2438 A N ATOM 1828 CZ2 TRP A 253 33.177 -23.715 12.774 1.00 81.65 A C ANISOU 1828 CZ2 TRP A 253 11975 7975 11073 -3377 -750 2269 A C ATOM 1829 CZ3 TRP A 253 34.684 -25.505 13.364 1.00 89.92 A C ANISOU 1829 CZ3 TRP A 253 13494 8458 12212 -3332 -1069 2440 A C ATOM 1830 CH2 TRP A 253 34.018 -24.727 12.410 1.00 86.22 A C ANISOU 1830 CH2 TRP A 253 12734 8244 11782 -3301 -935 2278 A C ATOM 1831 N PRO A 254 31.301 -22.267 19.733 1.00106.57 A N ANISOU 1831 N PRO A 254 15663 11685 13143 -4122 -245 2981 A N ATOM 1832 CA PRO A 254 29.882 -22.006 20.006 1.00107.97 A C ANISOU 1832 CA PRO A 254 15689 12143 13193 -4344 -5 2978 A C ATOM 1833 C PRO A 254 28.974 -22.232 18.800 1.00109.95 A C ANISOU 1833 C PRO A 254 15693 12494 13589 -4417 70 2851 A C ATOM 1834 O PRO A 254 29.089 -21.518 17.808 1.00108.90 A O ANISOU 1834 O PRO A 254 15338 12463 13576 -4205 75 2686 A O ATOM 1835 CB PRO A 254 29.875 -20.524 20.386 1.00107.13 A C ANISOU 1835 CB PRO A 254 15436 12305 12964 -4169 125 2895 A C ATOM 1836 CG PRO A 254 31.197 -20.310 21.023 1.00108.34 A C ANISOU 1836 CG PRO A 254 15799 12288 13076 -4000 -40 2958 A C ATOM 1837 CD PRO A 254 32.170 -21.229 20.314 1.00107.99 A C ANISOU 1837 CD PRO A 254 15869 11928 13235 -3905 -278 2968 A C ATOM 1838 N ASN A 255 28.080 -23.212 18.897 1.00118.66 A N ANISOU 1838 N ASN A 255 16841 13573 14671 -4726 124 2932 A N ATOM 1839 CA ASN A 255 27.104 -23.493 17.841 1.00122.55 A C ANISOU 1839 CA ASN A 255 17101 14182 15280 -4845 197 2820 A C ATOM 1840 C ASN A 255 27.604 -24.421 16.736 1.00118.08 A C ANISOU 1840 C ASN A 255 16602 13331 14934 -4807 7 2762 A C ATOM 1841 O ASN A 255 26.857 -24.734 15.805 1.00115.46 A O ANISOU 1841 O ASN A 255 16097 13071 14701 -4912 42 2664 A O ATOM 1842 CB ASN A 255 26.559 -22.200 17.219 1.00123.47 A C ANISOU 1842 CB ASN A 255 16865 14643 15406 -4666 346 2646 A C ATOM 1843 CG ASN A 255 25.249 -21.761 17.836 1.00127.96 A C ANISOU 1843 CG ASN A 255 17257 15558 15802 -4856 592 2665 A C ATOM 1844 ND2 ASN A 255 24.494 -20.952 17.100 1.00126.08 A N ANISOU 1844 ND2 ASN A 255 16693 15613 15600 -4760 717 2513 A N ATOM 1845 OD1 ASN A 255 24.914 -22.146 18.957 1.00132.74 A O ANISOU 1845 OD1 ASN A 255 18017 16178 16240 -5082 669 2815 A O ATOM 1846 N VAL A 256 28.855 -24.863 16.834 1.00113.58 A N ANISOU 1846 N VAL A 256 16277 12446 14433 -4653 -195 2816 A N ATOM 1847 CA VAL A 256 29.417 -25.732 15.803 1.00110.74 A C ANISOU 1847 CA VAL A 256 15995 11804 14277 -4581 -376 2750 A C ATOM 1848 C VAL A 256 28.490 -26.905 15.493 1.00118.09 A C ANISOU 1848 C VAL A 256 16984 12638 15248 -4909 -363 2783 A C ATOM 1849 O VAL A 256 28.376 -27.334 14.345 1.00115.51 A O ANISOU 1849 O VAL A 256 16574 12235 15078 -4895 -426 2658 A O ATOM 1850 CB VAL A 256 30.809 -26.275 16.173 1.00101.42 A C ANISOU 1850 CB VAL A 256 15112 10279 13144 -4415 -596 2841 A C ATOM 1851 CG1 VAL A 256 30.751 -27.085 17.462 1.00103.02 A C ANISOU 1851 CG1 VAL A 256 15630 10313 13199 -4649 -625 3067 A C ATOM 1852 CG2 VAL A 256 31.345 -27.122 15.035 1.00 92.22 A C ANISOU 1852 CG2 VAL A 256 14005 8844 12192 -4315 -765 2748 A C ATOM 1853 N ASP A 257 27.824 -27.422 16.516 1.00129.69 A N ANISOU 1853 N ASP A 257 18598 14113 16563 -5218 -281 2950 A N ATOM 1854 CA ASP A 257 26.905 -28.530 16.306 1.00142.55 A C ANISOU 1854 CA ASP A 257 20291 15656 18214 -5574 -259 2995 A C ATOM 1855 C ASP A 257 25.634 -28.068 15.605 1.00146.29 A C ANISOU 1855 C ASP A 257 20400 16486 18698 -5705 -82 2859 A C ATOM 1856 O ASP A 257 24.597 -27.871 16.240 1.00151.52 A O ANISOU 1856 O ASP A 257 20947 17412 19212 -5949 105 2922 A O ATOM 1857 CB ASP A 257 26.595 -29.241 17.621 1.00146.24 A C ANISOU 1857 CB ASP A 257 21037 16021 18506 -5883 -222 3227 A C ATOM 1858 CG ASP A 257 27.666 -30.242 17.997 1.00152.76 A C ANISOU 1858 CG ASP A 257 22273 16396 19373 -5837 -448 3363 A C ATOM 1859 OD1 ASP A 257 28.479 -30.609 17.118 1.00148.79 A O ANISOU 1859 OD1 ASP A 257 21830 15645 19056 -5621 -628 3267 A O ATOM 1860 OD2 ASP A 257 27.694 -30.666 19.169 1.00162.67 A O1- ANISOU 1860 OD2 ASP A 257 23790 17548 20469 -6010 -446 3568 A O1- ATOM 1861 N ASN A 258 25.742 -27.895 14.289 1.00139.60 A N ANISOU 1861 N ASN A 258 19367 15654 18021 -5532 -144 2671 A N ATOM 1862 CA ASN A 258 24.621 -27.509 13.443 1.00130.81 A C ANISOU 1862 CA ASN A 258 17904 14857 16939 -5622 -17 2526 A C ATOM 1863 C ASN A 258 24.827 -27.928 11.986 1.00127.61 A C ANISOU 1863 C ASN A 258 17438 14316 16731 -5525 -152 2358 A C ATOM 1864 O ASN A 258 24.646 -27.116 11.084 1.00123.60 A O ANISOU 1864 O ASN A 258 16646 14034 16283 -5337 -112 2194 A O ATOM 1865 CB ASN A 258 24.383 -25.995 13.512 1.00121.43 A C ANISOU 1865 CB ASN A 258 16412 14053 15674 -5398 139 2441 A C ATOM 1866 CG ASN A 258 23.565 -25.578 14.726 1.00124.39 A C ANISOU 1866 CG ASN A 258 16729 14696 15840 -5585 343 2558 A C ATOM 1867 ND2 ASN A 258 23.645 -24.302 15.081 1.00118.90 A N ANISOU 1867 ND2 ASN A 258 15877 14245 15053 -5356 455 2516 A N ATOM 1868 OD1 ASN A 258 22.863 -26.387 15.328 1.00136.87 A O ANISOU 1868 OD1 ASN A 258 18408 16262 17336 -5936 404 2682 A O ATOM 1869 N TYR A 259 25.209 -29.184 11.747 1.00128.88 A N ANISOU 1869 N TYR A 259 17878 14105 16987 -5645 -312 2395 A N ATOM 1870 CA TYR A 259 25.343 -29.657 10.368 1.00131.69 A C ANISOU 1870 CA TYR A 259 18193 14328 17517 -5577 -435 2227 A C ATOM 1871 C TYR A 259 25.232 -31.158 10.148 1.00125.05 A C ANISOU 1871 C TYR A 259 17630 13134 16749 -5845 -561 2266 A C ATOM 1872 O TYR A 259 24.273 -31.612 9.539 1.00128.61 A O ANISOU 1872 O TYR A 259 17967 13670 17228 -6103 -529 2194 A O ATOM 1873 CB TYR A 259 26.629 -29.161 9.720 1.00145.99 A C ANISOU 1873 CB TYR A 259 20015 16015 19441 -5149 -560 2117 A C ATOM 1874 CG TYR A 259 26.687 -29.498 8.248 1.00151.91 A C ANISOU 1874 CG TYR A 259 20682 16691 20347 -5064 -657 1924 A C ATOM 1875 CD1 TYR A 259 26.329 -28.555 7.291 1.00148.37 A C ANISOU 1875 CD1 TYR A 259 19897 16549 19928 -4908 -587 1756 A C ATOM 1876 CD2 TYR A 259 27.074 -30.766 7.815 1.00153.57 A C ANISOU 1876 CD2 TYR A 259 21163 16522 20666 -5141 -820 1910 A C ATOM 1877 CE1 TYR A 259 26.371 -28.851 5.947 1.00148.48 A C ANISOU 1877 CE1 TYR A 259 19842 16509 20066 -4835 -675 1580 A C ATOM 1878 CE2 TYR A 259 27.119 -31.072 6.469 1.00153.87 A C ANISOU 1878 CE2 TYR A 259 21135 16496 20833 -5064 -904 1723 A C ATOM 1879 CZ TYR A 259 26.766 -30.108 5.539 1.00152.25 A C ANISOU 1879 CZ TYR A 259 20587 16616 20645 -4915 -830 1559 A C ATOM 1880 OH TYR A 259 26.804 -30.393 4.194 1.00151.87 A O ANISOU 1880 OH TYR A 259 20477 16521 20708 -4840 -913 1372 A O ATOM 1881 N LEU A 267 33.175 -37.282 13.695 1.00130.94 A N ANISOU 1881 N LEU A 267 21227 10754 17771 -4925 -1958 3140 A N ATOM 1882 CA LEU A 267 34.387 -36.660 14.230 1.00132.12 A C ANISOU 1882 CA LEU A 267 21367 10929 17903 -4558 -2048 3190 A C ATOM 1883 C LEU A 267 34.929 -37.304 15.498 1.00144.48 A C ANISOU 1883 C LEU A 267 23316 12216 19365 -4580 -2180 3447 A C ATOM 1884 O LEU A 267 34.287 -38.172 16.096 1.00144.50 A O ANISOU 1884 O LEU A 267 23601 12021 19281 -4913 -2179 3612 A O ATOM 1885 CB LEU A 267 34.141 -35.177 14.504 1.00120.95 A C ANISOU 1885 CB LEU A 267 19583 9991 16381 -4505 -1869 3152 A C ATOM 1886 CG LEU A 267 33.795 -34.303 13.300 1.00116.05 A C ANISOU 1886 CG LEU A 267 18559 9681 15852 -4400 -1749 2906 A C ATOM 1887 CD1 LEU A 267 33.357 -32.921 13.760 1.00110.90 A C ANISOU 1887 CD1 LEU A 267 17600 9472 15065 -4411 -1560 2906 A C ATOM 1888 CD2 LEU A 267 34.982 -34.213 12.358 1.00117.10 A C ANISOU 1888 CD2 LEU A 267 18631 9702 16160 -3990 -1889 2740 A C ATOM 1889 N VAL A 268 36.119 -36.856 15.897 1.00151.42 A N ANISOU 1889 N VAL A 268 24198 13089 20247 -4229 -2297 3480 A N ATOM 1890 CA VAL A 268 36.764 -37.310 17.126 1.00157.94 A C ANISOU 1890 CA VAL A 268 25356 13692 20963 -4194 -2440 3721 A C ATOM 1891 C VAL A 268 36.074 -36.671 18.323 1.00159.65 A C ANISOU 1891 C VAL A 268 25538 14182 20940 -4456 -2282 3891 A C ATOM 1892 O VAL A 268 35.191 -35.828 18.158 1.00159.59 A O ANISOU 1892 O VAL A 268 25229 14540 20869 -4618 -2066 3806 A O ATOM 1893 CB VAL A 268 38.253 -36.919 17.165 1.00151.83 A C ANISOU 1893 CB VAL A 268 24543 12885 20261 -3732 -2613 3689 A C ATOM 1894 CG1 VAL A 268 38.978 -37.433 15.931 1.00149.20 A C ANISOU 1894 CG1 VAL A 268 24196 12333 20162 -3436 -2748 3497 A C ATOM 1895 CG2 VAL A 268 38.389 -35.416 17.275 1.00143.81 A C ANISOU 1895 CG2 VAL A 268 23150 12315 19178 -3604 -2481 3607 A C ATOM 1896 N LYS A 269 36.483 -37.060 19.527 1.00156.09 A N ANISOU 1896 N LYS A 269 25397 13562 20349 -4486 -2389 4128 A N ATOM 1897 CA LYS A 269 35.830 -36.554 20.728 1.00151.03 A C ANISOU 1897 CA LYS A 269 24767 13158 19458 -4750 -2240 4301 A C ATOM 1898 C LYS A 269 36.793 -36.261 21.879 1.00145.89 A C ANISOU 1898 C LYS A 269 24273 12489 18669 -4559 -2371 4471 A C ATOM 1899 O LYS A 269 36.492 -35.444 22.748 1.00141.71 A O ANISOU 1899 O LYS A 269 23652 12249 17942 -4662 -2242 4549 A O ATOM 1900 CB LYS A 269 34.727 -37.518 21.177 1.00155.56 A C ANISOU 1900 CB LYS A 269 25608 13573 19925 -5210 -2163 4466 A C ATOM 1901 CG LYS A 269 33.686 -37.802 20.095 1.00151.75 A C ANISOU 1901 CG LYS A 269 24961 13136 19561 -5444 -2032 4302 A C ATOM 1902 CD LYS A 269 32.697 -38.880 20.510 1.00146.87 A C ANISOU 1902 CD LYS A 269 24637 12315 18852 -5909 -1985 4469 A C ATOM 1903 CE LYS A 269 31.710 -39.157 19.389 1.00142.51 A C ANISOU 1903 CE LYS A 269 23906 11817 18425 -6137 -1874 4292 A C ATOM 1904 NZ LYS A 269 30.646 -40.103 19.813 1.00149.80 A N1+ ANISOU 1904 NZ LYS A 269 25073 12599 19246 -6640 -1801 4450 A N1+ ATOM 1905 N GLY A 270 37.953 -36.913 21.879 1.00146.83 A N ANISOU 1905 N GLY A 270 24622 12280 18888 -4273 -2628 4521 A N ATOM 1906 CA GLY A 270 38.892 -36.771 22.980 1.00151.48 A C ANISOU 1906 CA GLY A 270 25386 12823 19346 -4096 -2786 4696 A C ATOM 1907 C GLY A 270 40.095 -35.872 22.735 1.00151.24 A C ANISOU 1907 C GLY A 270 25105 12958 19400 -3671 -2890 4566 A C ATOM 1908 O GLY A 270 40.797 -35.492 23.674 1.00148.43 A O ANISOU 1908 O GLY A 270 24819 12664 18913 -3544 -2991 4689 A O ATOM 1909 N GLN A 271 40.333 -35.526 21.474 1.00152.21 A N ANISOU 1909 N GLN A 271 24937 13162 19735 -3463 -2865 4318 A N ATOM 1910 CA GLN A 271 41.531 -34.783 21.092 1.00152.74 A C ANISOU 1910 CA GLN A 271 24768 13358 19910 -3060 -2971 4183 A C ATOM 1911 C GLN A 271 41.722 -33.490 21.889 1.00150.80 A C ANISOU 1911 C GLN A 271 24331 13474 19492 -3032 -2892 4209 A C ATOM 1912 O GLN A 271 40.756 -32.832 22.267 1.00152.30 A O ANISOU 1912 O GLN A 271 24413 13924 19530 -3291 -2677 4222 A O ATOM 1913 CB GLN A 271 41.508 -34.486 19.591 1.00153.41 A C ANISOU 1913 CB GLN A 271 24542 13534 20214 -2913 -2895 3908 A C ATOM 1914 CG GLN A 271 41.378 -35.725 18.713 1.00156.04 A C ANISOU 1914 CG GLN A 271 25056 13511 20722 -2917 -2978 3849 A C ATOM 1915 CD GLN A 271 42.658 -36.540 18.642 1.00159.64 A C ANISOU 1915 CD GLN A 271 25720 13631 21304 -2573 -3251 3880 A C ATOM 1916 NE2 GLN A 271 42.515 -37.854 18.515 1.00165.42 A N ANISOU 1916 NE2 GLN A 271 26793 13959 22102 -2642 -3364 3950 A N ATOM 1917 OE1 GLN A 271 43.760 -35.995 18.695 1.00157.90 A O ANISOU 1917 OE1 GLN A 271 25355 13517 21124 -2249 -3360 3839 A O ATOM 1918 N LYS A 272 42.978 -33.133 22.137 1.00147.18 A N ANISOU 1918 N LYS A 272 23829 13034 19057 -2714 -3068 4211 A N ATOM 1919 CA LYS A 272 43.304 -31.930 22.895 1.00143.21 A C ANISOU 1919 CA LYS A 272 23169 12848 18397 -2669 -3027 4229 A C ATOM 1920 C LYS A 272 44.351 -31.103 22.153 1.00140.87 A C ANISOU 1920 C LYS A 272 22554 12717 18253 -2324 -3089 4036 A C ATOM 1921 O LYS A 272 45.209 -31.659 21.469 1.00144.52 A O ANISOU 1921 O LYS A 272 23013 12993 18906 -2058 -3255 3966 A O ATOM 1922 CB LYS A 272 43.808 -32.306 24.287 1.00145.33 A C ANISOU 1922 CB LYS A 272 23753 12991 18474 -2682 -3201 4481 A C ATOM 1923 CG LYS A 272 42.904 -33.290 25.017 1.00149.00 A C ANISOU 1923 CG LYS A 272 24581 13239 18792 -3012 -3169 4696 A C ATOM 1924 CD LYS A 272 43.529 -33.751 26.317 1.00149.90 A C ANISOU 1924 CD LYS A 272 25034 13194 18728 -2986 -3375 4951 A C ATOM 1925 CE LYS A 272 42.602 -34.684 27.068 1.00155.54 A C ANISOU 1925 CE LYS A 272 26120 13704 19276 -3342 -3328 5177 A C ATOM 1926 NZ LYS A 272 43.246 -35.219 28.302 1.00159.07 A N1+ ANISOU 1926 NZ LYS A 272 26930 13964 19545 -3303 -3550 5440 A N1+ ATOM 1927 N ARG A 273 44.278 -29.781 22.299 1.00133.63 A N ANISOU 1927 N ARG A 273 21379 12148 17247 -2332 -2953 3949 A N ATOM 1928 CA ARG A 273 45.105 -28.853 21.519 1.00131.34 A C ANISOU 1928 CA ARG A 273 20759 12052 17091 -2061 -2965 3753 A C ATOM 1929 C ARG A 273 46.606 -29.111 21.620 1.00118.26 A C ANISOU 1929 C ARG A 273 19128 10280 15524 -1735 -3234 3777 A C ATOM 1930 O ARG A 273 47.192 -29.033 22.699 1.00112.78 A O ANISOU 1930 O ARG A 273 18572 9589 14688 -1700 -3375 3926 A O ATOM 1931 CB ARG A 273 44.813 -27.400 21.908 1.00143.31 A C ANISOU 1931 CB ARG A 273 22063 13931 18458 -2143 -2796 3695 A C ATOM 1932 CG ARG A 273 43.390 -26.951 21.639 1.00156.05 A C ANISOU 1932 CG ARG A 273 23567 15717 20006 -2408 -2516 3627 A C ATOM 1933 CD ARG A 273 43.177 -25.503 22.064 1.00166.29 A C ANISOU 1933 CD ARG A 273 24677 17352 21154 -2451 -2363 3567 A C ATOM 1934 NE ARG A 273 41.760 -25.188 22.233 1.00174.93 A N ANISOU 1934 NE ARG A 273 25740 18603 22122 -2728 -2111 3566 A N ATOM 1935 CZ ARG A 273 41.295 -24.013 22.647 1.00178.09 A C ANISOU 1935 CZ ARG A 273 26009 19285 22372 -2803 -1941 3519 A C ATOM 1936 NH1 ARG A 273 42.135 -23.028 22.937 1.00176.98 A N1+ ANISOU 1936 NH1 ARG A 273 25772 19286 22185 -2641 -1997 3470 A N1+ ATOM 1937 NH2 ARG A 273 39.988 -23.822 22.772 1.00179.73 A N ANISOU 1937 NH2 ARG A 273 26180 19636 22474 -3041 -1714 3517 A N ATOM 1938 N LYS A 274 47.224 -29.388 20.478 1.00112.11 A N ANISOU 1938 N LYS A 274 18200 9421 14974 -1492 -3301 3622 A N ATOM 1939 CA LYS A 274 48.653 -29.662 20.426 1.00109.48 A C ANISOU 1939 CA LYS A 274 17848 8997 14753 -1156 -3545 3620 A C ATOM 1940 C LYS A 274 49.376 -28.737 19.443 1.00102.88 A C ANISOU 1940 C LYS A 274 16632 8396 14062 -932 -3506 3399 A C ATOM 1941 O LYS A 274 50.493 -29.034 19.012 1.00 99.73 A O ANISOU 1941 O LYS A 274 16152 7931 13809 -636 -3673 3342 A O ATOM 1942 CB LYS A 274 48.899 -31.133 20.056 1.00112.85 A C ANISOU 1942 CB LYS A 274 18515 9042 15323 -1031 -3708 3665 A C ATOM 1943 CG LYS A 274 48.084 -32.123 20.885 1.00117.95 A C ANISOU 1943 CG LYS A 274 19555 9422 15838 -1286 -3729 3879 A C ATOM 1944 CD LYS A 274 48.659 -33.524 20.844 1.00125.08 A C ANISOU 1944 CD LYS A 274 20749 9924 16852 -1107 -3962 3969 A C ATOM 1945 CE LYS A 274 48.016 -34.393 21.923 1.00137.27 A C ANISOU 1945 CE LYS A 274 22715 11219 18223 -1362 -4013 4226 A C ATOM 1946 NZ LYS A 274 48.798 -35.627 22.252 1.00139.90 A N1+ ANISOU 1946 NZ LYS A 274 23375 11169 18612 -1152 -4292 4370 A N1+ ATOM 1947 N VAL A 275 48.742 -27.616 19.093 1.00 96.82 A N ANISOU 1947 N VAL A 275 15634 7905 13249 -1069 -3283 3279 A N ATOM 1948 CA VAL A 275 49.308 -26.706 18.097 1.00 90.27 A C ANISOU 1948 CA VAL A 275 14457 7296 12546 -892 -3221 3073 A C ATOM 1949 C VAL A 275 50.686 -26.231 18.509 1.00 88.56 A C ANISOU 1949 C VAL A 275 14129 7189 12332 -666 -3400 3086 A C ATOM 1950 O VAL A 275 51.619 -26.234 17.703 1.00 86.63 A O ANISOU 1950 O VAL A 275 13693 6968 12252 -414 -3478 2963 A O ATOM 1951 CB VAL A 275 48.426 -25.461 17.848 1.00 85.49 A C ANISOU 1951 CB VAL A 275 13650 6975 11857 -1077 -2967 2970 A C ATOM 1952 CG1 VAL A 275 49.181 -24.442 16.982 1.00 65.35 A C ANISOU 1952 CG1 VAL A 275 10768 4649 9411 -891 -2929 2786 A C ATOM 1953 CG2 VAL A 275 47.101 -25.852 17.201 1.00 85.18 A C ANISOU 1953 CG2 VAL A 275 13643 6874 11846 -1274 -2783 2918 A C ATOM 1954 N LYS A 276 50.810 -25.818 19.764 1.00 92.79 A N ANISOU 1954 N LYS A 276 14775 7805 12674 -763 -3463 3231 A N ATOM 1955 CA LYS A 276 52.082 -25.310 20.261 1.00104.43 A C ANISOU 1955 CA LYS A 276 16144 9409 14128 -582 -3642 3251 A C ATOM 1956 C LYS A 276 53.075 -26.427 20.586 1.00110.46 A C ANISOU 1956 C LYS A 276 17062 9945 14964 -351 -3923 3362 A C ATOM 1957 O LYS A 276 54.283 -26.228 20.488 1.00113.05 A O ANISOU 1957 O LYS A 276 17222 10361 15371 -113 -4082 3319 A O ATOM 1958 CB LYS A 276 51.881 -24.383 21.466 1.00106.19 A C ANISOU 1958 CB LYS A 276 16425 9817 14106 -767 -3610 3348 A C ATOM 1959 CG LYS A 276 51.551 -22.943 21.093 1.00 98.29 A C ANISOU 1959 CG LYS A 276 15173 9107 13064 -864 -3400 3197 A C ATOM 1960 CD LYS A 276 51.525 -22.026 22.307 1.00 99.76 A C ANISOU 1960 CD LYS A 276 15427 9466 13011 -1012 -3396 3279 A C ATOM 1961 CE LYS A 276 51.319 -20.569 21.881 1.00109.50 A C ANISOU 1961 CE LYS A 276 16418 10967 14220 -1075 -3205 3117 A C ATOM 1962 NZ LYS A 276 51.799 -19.552 22.875 1.00111.75 A N1+ ANISOU 1962 NZ LYS A 276 16706 11435 14320 -1133 -3260 3149 A N1+ ATOM 1963 N ASP A 277 52.566 -27.597 20.959 1.00113.38 A N ANISOU 1963 N ASP A 277 17747 10024 15307 -419 -3986 3505 A N ATOM 1964 CA ASP A 277 53.424 -28.747 21.247 1.00118.88 A C ANISOU 1964 CA ASP A 277 18631 10463 16075 -189 -4256 3619 A C ATOM 1965 C ASP A 277 54.029 -29.371 19.987 1.00111.36 A C ANISOU 1965 C ASP A 277 17541 9388 15383 96 -4310 3463 A C ATOM 1966 O ASP A 277 55.218 -29.692 19.947 1.00106.12 A O ANISOU 1966 O ASP A 277 16809 8694 14820 394 -4520 3459 A O ATOM 1967 CB ASP A 277 52.654 -29.818 22.027 1.00130.77 A C ANISOU 1967 CB ASP A 277 20550 11671 17465 -367 -4302 3828 A C ATOM 1968 CG ASP A 277 52.643 -29.560 23.519 1.00141.44 A C ANISOU 1968 CG ASP A 277 22100 13081 18560 -516 -4388 4037 A C ATOM 1969 OD1 ASP A 277 52.873 -28.399 23.925 1.00144.36 A O ANISOU 1969 OD1 ASP A 277 22287 13746 18817 -565 -4341 3999 A O ATOM 1970 OD2 ASP A 277 52.408 -30.521 24.284 1.00146.14 A O1- ANISOU 1970 OD2 ASP A 277 23047 13420 19058 -588 -4505 4239 A O1- ATOM 1971 N ARG A 278 53.205 -29.544 18.960 1.00107.83 A N ANISOU 1971 N ARG A 278 17048 8882 15040 6 -4121 3329 A N ATOM 1972 CA ARG A 278 53.640 -30.235 17.757 1.00108.95 A C ANISOU 1972 CA ARG A 278 17105 8880 15411 253 -4156 3178 A C ATOM 1973 C ARG A 278 54.552 -29.356 16.910 1.00103.03 A C ANISOU 1973 C ARG A 278 15957 8408 14783 469 -4126 2982 A C ATOM 1974 O ARG A 278 55.377 -29.860 16.151 1.00104.83 A O ANISOU 1974 O ARG A 278 16082 8563 15186 759 -4222 2876 A O ATOM 1975 CB ARG A 278 52.432 -30.712 16.944 1.00119.21 A C ANISOU 1975 CB ARG A 278 18497 10032 16766 66 -3969 3097 A C ATOM 1976 CG ARG A 278 52.717 -31.907 16.036 1.00129.32 A C ANISOU 1976 CG ARG A 278 19877 11017 18242 282 -4059 3011 A C ATOM 1977 CD ARG A 278 51.453 -32.385 15.334 1.00135.10 A C ANISOU 1977 CD ARG A 278 20724 11602 19005 52 -3885 2943 A C ATOM 1978 NE ARG A 278 51.747 -33.192 14.153 1.00141.32 A N ANISOU 1978 NE ARG A 278 21506 12197 19992 267 -3919 2781 A N ATOM 1979 CZ ARG A 278 52.000 -32.694 12.944 1.00144.47 A C ANISOU 1979 CZ ARG A 278 21603 12773 20516 403 -3809 2553 A C ATOM 1980 NH1 ARG A 278 52.003 -31.381 12.744 1.00137.25 A N1+ ANISOU 1980 NH1 ARG A 278 20371 12223 19555 346 -3664 2469 A N1+ ATOM 1981 NH2 ARG A 278 52.256 -33.511 11.932 1.00150.66 A N ANISOU 1981 NH2 ARG A 278 22417 13363 21465 599 -3846 2410 A N ATOM 1982 N LEU A 279 54.407 -28.041 17.053 1.00 97.48 A N ANISOU 1982 N LEU A 279 15036 8020 13981 326 -3989 2934 A N ATOM 1983 CA LEU A 279 55.216 -27.086 16.301 1.00 90.64 A C ANISOU 1983 CA LEU A 279 13797 7434 13207 482 -3943 2760 A C ATOM 1984 C LEU A 279 56.345 -26.516 17.155 1.00 84.24 A C ANISOU 1984 C LEU A 279 12879 6801 12326 594 -4119 2834 A C ATOM 1985 O LEU A 279 57.282 -25.891 16.642 1.00 80.18 A O ANISOU 1985 O LEU A 279 12065 6499 11899 760 -4139 2713 A O ATOM 1986 CB LEU A 279 54.340 -25.952 15.767 1.00 87.81 A C ANISOU 1986 CB LEU A 279 13262 7303 12797 259 -3674 2641 A C ATOM 1987 CG LEU A 279 53.438 -26.337 14.601 1.00 91.74 A C ANISOU 1987 CG LEU A 279 13754 7704 13400 200 -3499 2509 A C ATOM 1988 CD1 LEU A 279 52.697 -25.115 14.071 1.00 93.52 A C ANISOU 1988 CD1 LEU A 279 13775 8185 13573 19 -3253 2392 A C ATOM 1989 CD2 LEU A 279 54.266 -26.982 13.504 1.00 90.56 A C ANISOU 1989 CD2 LEU A 279 13482 7468 13458 498 -3573 2368 A C ATOM 1990 N LYS A 280 56.218 -26.716 18.463 1.00 84.75 A N ANISOU 1990 N LYS A 280 13190 6787 12222 481 -4240 3035 A N ATOM 1991 CA LYS A 280 57.244 -26.368 19.446 1.00103.46 A C ANISOU 1991 CA LYS A 280 15524 9285 14501 576 -4449 3138 A C ATOM 1992 C LYS A 280 58.654 -26.690 18.940 1.00112.93 A C ANISOU 1992 C LYS A 280 16509 10521 15879 935 -4638 3061 A C ATOM 1993 O LYS A 280 59.594 -25.916 19.148 1.00106.46 A O ANISOU 1993 O LYS A 280 15452 9953 15046 1018 -4723 3028 A O ATOM 1994 CB LYS A 280 56.973 -27.151 20.738 1.00109.59 A C ANISOU 1994 CB LYS A 280 16678 9843 15117 491 -4609 3379 A C ATOM 1995 CG LYS A 280 57.729 -26.693 21.973 1.00107.97 A C ANISOU 1995 CG LYS A 280 16496 9782 14748 499 -4802 3514 A C ATOM 1996 CD LYS A 280 57.389 -27.604 23.153 1.00107.18 A C ANISOU 1996 CD LYS A 280 16802 9432 14488 419 -4953 3760 A C ATOM 1997 CE LYS A 280 58.214 -27.257 24.378 1.00108.22 A C ANISOU 1997 CE LYS A 280 16972 9694 14453 454 -5179 3900 A C ATOM 1998 NZ LYS A 280 57.939 -28.172 25.517 1.00109.32 A N1+ ANISOU 1998 NZ LYS A 280 17520 9588 14427 389 -5339 4150 A N1+ ATOM 1999 N ALA A 281 58.787 -27.845 18.286 1.00119.45 A N ANISOU 1999 N ALA A 281 17422 11097 16868 1144 -4704 3030 A N ATOM 2000 CA ALA A 281 60.059 -28.291 17.723 1.00112.02 A C ANISOU 2000 CA ALA A 281 16286 10169 16108 1515 -4869 2945 A C ATOM 2001 C ALA A 281 60.614 -27.281 16.719 1.00104.25 A C ANISOU 2001 C ALA A 281 14878 9504 15228 1583 -4735 2731 A C ATOM 2002 O ALA A 281 61.633 -26.628 16.963 1.00 99.34 A O ANISOU 2002 O ALA A 281 14010 9132 14601 1686 -4838 2713 A O ATOM 2003 CB ALA A 281 59.892 -29.665 17.061 1.00103.46 A C ANISOU 2003 CB ALA A 281 15394 8739 15177 1699 -4911 2918 A C ATOM 2004 N TYR A 282 59.912 -27.148 15.599 1.00100.24 A N ANISOU 2004 N TYR A 282 14293 8990 14803 1508 -4504 2574 A N ATOM 2005 CA TYR A 282 60.361 -26.340 14.472 1.00 91.14 A C ANISOU 2005 CA TYR A 282 12770 8099 13760 1583 -4360 2366 A C ATOM 2006 C TYR A 282 60.527 -24.853 14.770 1.00 92.98 A C ANISOU 2006 C TYR A 282 12777 8669 13880 1400 -4272 2344 A C ATOM 2007 O TYR A 282 61.512 -24.240 14.353 1.00 94.17 A O ANISOU 2007 O TYR A 282 12615 9066 14100 1529 -4291 2242 A O ATOM 2008 CB TYR A 282 59.398 -26.525 13.301 1.00 86.27 A C ANISOU 2008 CB TYR A 282 12173 7386 13221 1502 -4132 2225 A C ATOM 2009 CG TYR A 282 59.188 -27.969 12.934 1.00 93.53 A C ANISOU 2009 CG TYR A 282 13328 7959 14251 1660 -4207 2227 A C ATOM 2010 CD1 TYR A 282 58.173 -28.713 13.521 1.00 98.07 A C ANISOU 2010 CD1 TYR A 282 14269 8249 14745 1482 -4218 2365 A C ATOM 2011 CD2 TYR A 282 60.018 -28.598 12.012 1.00100.52 A C ANISOU 2011 CD2 TYR A 282 14077 8799 15317 1984 -4266 2090 A C ATOM 2012 CE1 TYR A 282 57.984 -30.046 13.195 1.00104.30 A C ANISOU 2012 CE1 TYR A 282 15301 8697 15633 1610 -4293 2369 A C ATOM 2013 CE2 TYR A 282 59.838 -29.929 11.676 1.00105.89 A C ANISOU 2013 CE2 TYR A 282 14998 9138 16096 2138 -4339 2082 A C ATOM 2014 CZ TYR A 282 58.818 -30.649 12.270 1.00109.11 A C ANISOU 2014 CZ TYR A 282 15787 9246 16423 1943 -4357 2224 A C ATOM 2015 OH TYR A 282 58.631 -31.975 11.941 1.00115.12 A O ANISOU 2015 OH TYR A 282 16813 9647 17282 2077 -4434 2217 A O ATOM 2016 N VAL A 283 59.566 -24.274 15.486 1.00 97.75 A N ANISOU 2016 N VAL A 283 13544 9286 14309 1099 -4172 2435 A N ATOM 2017 CA VAL A 283 59.474 -22.817 15.588 1.00102.70 A C ANISOU 2017 CA VAL A 283 13990 10201 14831 900 -4037 2384 A C ATOM 2018 C VAL A 283 60.377 -22.217 16.665 1.00105.98 A C ANISOU 2018 C VAL A 283 14341 10791 15135 895 -4216 2479 A C ATOM 2019 O VAL A 283 61.171 -21.312 16.387 1.00108.27 A O ANISOU 2019 O VAL A 283 14347 11339 15450 924 -4209 2386 A O ATOM 2020 CB VAL A 283 58.011 -22.356 15.803 1.00100.71 A C ANISOU 2020 CB VAL A 283 13916 9911 14439 589 -3827 2414 A C ATOM 2021 CG1 VAL A 283 57.906 -20.834 15.742 1.00 92.71 A C ANISOU 2021 CG1 VAL A 283 12715 9177 13335 414 -3672 2336 A C ATOM 2022 CG2 VAL A 283 57.104 -22.993 14.766 1.00 96.73 A C ANISOU 2022 CG2 VAL A 283 13474 9240 14039 581 -3669 2325 A C ATOM 2023 N ARG A 284 60.234 -22.709 17.892 1.00101.02 A N ANISOU 2023 N ARG A 284 13984 10026 14374 841 -4375 2664 A N ATOM 2024 CA ARG A 284 61.082 -22.277 19.004 1.00104.65 A C ANISOU 2024 CA ARG A 284 14420 10631 14713 842 -4578 2768 A C ATOM 2025 C ARG A 284 60.739 -20.884 19.550 1.00 98.50 A C ANISOU 2025 C ARG A 284 13601 10071 13752 565 -4461 2760 A C ATOM 2026 O ARG A 284 60.518 -20.732 20.752 1.00 94.93 A O ANISOU 2026 O ARG A 284 13354 9607 13107 421 -4545 2900 A O ATOM 2027 CB ARG A 284 62.563 -22.368 18.622 1.00109.74 A C ANISOU 2027 CB ARG A 284 14766 11424 15505 1128 -4756 2699 A C ATOM 2028 CG ARG A 284 63.011 -23.779 18.272 1.00115.77 A C ANISOU 2028 CG ARG A 284 15595 11963 16430 1438 -4911 2722 A C ATOM 2029 CD ARG A 284 64.448 -23.801 17.787 1.00123.47 A C ANISOU 2029 CD ARG A 284 16231 13123 17560 1733 -5055 2628 A C ATOM 2030 NE ARG A 284 64.952 -25.165 17.644 1.00134.50 A N ANISOU 2030 NE ARG A 284 17714 14297 19091 2060 -5239 2666 A N ATOM 2031 CZ ARG A 284 66.241 -25.475 17.536 1.00140.22 A C ANISOU 2031 CZ ARG A 284 18209 15137 19932 2367 -5435 2636 A C ATOM 2032 NH1 ARG A 284 67.159 -24.515 17.556 1.00138.59 A N1+ ANISOU 2032 NH1 ARG A 284 17659 15277 19721 2364 -5471 2571 A N1+ ATOM 2033 NH2 ARG A 284 66.614 -26.744 17.412 1.00141.84 A N ANISOU 2033 NH2 ARG A 284 18527 15111 20257 2678 -5596 2671 A N ATOM 2034 N ASP A 285 60.691 -19.877 18.678 1.00 94.78 A N ANISOU 2034 N ASP A 285 12886 9791 13335 494 -4268 2596 A N ATOM 2035 CA ASP A 285 60.314 -18.528 19.105 1.00 87.24 A C ANISOU 2035 CA ASP A 285 11911 9020 12216 240 -4140 2572 A C ATOM 2036 C ASP A 285 58.898 -18.471 19.672 1.00 85.07 A C ANISOU 2036 C ASP A 285 11926 8619 11776 4 -3989 2650 A C ATOM 2037 O ASP A 285 57.936 -18.838 18.999 1.00 81.97 A O ANISOU 2037 O ASP A 285 11601 8101 11442 -33 -3815 2609 A O ATOM 2038 CB ASP A 285 60.443 -17.529 17.960 1.00 89.17 A C ANISOU 2038 CB ASP A 285 11868 9457 12557 214 -3950 2387 A C ATOM 2039 CG ASP A 285 60.090 -16.109 18.385 1.00 95.92 A C ANISOU 2039 CG ASP A 285 12719 10480 13246 -35 -3826 2358 A C ATOM 2040 OD1 ASP A 285 58.889 -15.762 18.421 1.00 83.88 A O ANISOU 2040 OD1 ASP A 285 11349 8895 11626 -209 -3633 2355 A O ATOM 2041 OD2 ASP A 285 61.023 -15.334 18.684 1.00108.39 A O1- ANISOU 2041 OD2 ASP A 285 14140 12254 14790 -55 -3923 2333 A O1- ATOM 2042 N PRO A 286 58.768 -17.998 20.917 1.00 89.67 A N ANISOU 2042 N PRO A 286 12675 9252 12145 -159 -4053 2759 A N ATOM 2043 CA PRO A 286 57.474 -17.901 21.599 1.00 90.73 A C ANISOU 2043 CA PRO A 286 13081 9297 12095 -387 -3911 2840 A C ATOM 2044 C PRO A 286 56.438 -17.132 20.775 1.00 90.04 A C ANISOU 2044 C PRO A 286 12920 9269 12024 -524 -3612 2708 A C ATOM 2045 O PRO A 286 55.319 -17.625 20.609 1.00 96.15 A O ANISOU 2045 O PRO A 286 13840 9906 12786 -607 -3471 2733 A O ATOM 2046 CB PRO A 286 57.806 -17.118 22.874 1.00 84.55 A C ANISOU 2046 CB PRO A 286 12387 8649 11088 -522 -4016 2917 A C ATOM 2047 CG PRO A 286 59.249 -17.325 23.086 1.00 90.02 A C ANISOU 2047 CG PRO A 286 12936 9420 11846 -340 -4287 2942 A C ATOM 2048 CD PRO A 286 59.865 -17.452 21.731 1.00 91.00 A C ANISOU 2048 CD PRO A 286 12762 9590 12224 -146 -4257 2798 A C ATOM 2049 N TYR A 287 56.803 -15.950 20.276 1.00 81.69 A N ANISOU 2049 N TYR A 287 11641 8411 10988 -553 -3523 2574 A N ATOM 2050 CA TYR A 287 55.850 -15.071 19.583 1.00 90.57 A C ANISOU 2050 CA TYR A 287 12706 9604 12102 -681 -3251 2455 A C ATOM 2051 C TYR A 287 55.291 -15.688 18.307 1.00 86.61 A C ANISOU 2051 C TYR A 287 12124 9005 11781 -594 -3115 2373 A C ATOM 2052 O TYR A 287 54.084 -15.639 18.060 1.00 79.10 A O ANISOU 2052 O TYR A 287 11258 8004 10792 -708 -2925 2354 A O ATOM 2053 CB TYR A 287 56.469 -13.703 19.278 1.00 91.59 A C ANISOU 2053 CB TYR A 287 12629 9948 12223 -720 -3204 2336 A C ATOM 2054 CG TYR A 287 56.828 -12.924 20.516 1.00 98.49 A C ANISOU 2054 CG TYR A 287 13603 10925 12896 -851 -3303 2395 A C ATOM 2055 CD1 TYR A 287 55.901 -12.745 21.536 1.00100.17 A C ANISOU 2055 CD1 TYR A 287 14072 11093 12897 -1019 -3237 2477 A C ATOM 2056 CD2 TYR A 287 58.092 -12.368 20.671 1.00 99.40 A C ANISOU 2056 CD2 TYR A 287 13554 11191 13023 -815 -3461 2363 A C ATOM 2057 CE1 TYR A 287 56.222 -12.039 22.675 1.00100.03 A C ANISOU 2057 CE1 TYR A 287 14162 11166 12678 -1138 -3328 2522 A C ATOM 2058 CE2 TYR A 287 58.422 -11.656 21.807 1.00 98.69 A C ANISOU 2058 CE2 TYR A 287 13565 11193 12739 -947 -3562 2409 A C ATOM 2059 CZ TYR A 287 57.483 -11.494 22.806 1.00 98.61 A C ANISOU 2059 CZ TYR A 287 13828 11124 12514 -1105 -3496 2486 A C ATOM 2060 OH TYR A 287 57.803 -10.786 23.940 1.00 97.91 A O ANISOU 2060 OH TYR A 287 13857 11127 12219 -1236 -3595 2522 A O ATOM 2061 N ALA A 288 56.180 -16.260 17.503 1.00 86.36 A N ANISOU 2061 N ALA A 288 11919 8956 11937 -389 -3216 2317 A N ATOM 2062 CA ALA A 288 55.777 -16.996 16.318 1.00 86.17 A C ANISOU 2062 CA ALA A 288 11836 8821 12082 -284 -3121 2238 A C ATOM 2063 C ALA A 288 54.751 -18.077 16.665 1.00 88.23 A C ANISOU 2063 C ALA A 288 12359 8856 12310 -345 -3104 2341 A C ATOM 2064 O ALA A 288 53.722 -18.215 15.998 1.00 87.77 A O ANISOU 2064 O ALA A 288 12324 8740 12283 -417 -2929 2286 A O ATOM 2065 CB ALA A 288 56.983 -17.609 15.651 1.00 81.67 A C ANISOU 2065 CB ALA A 288 11083 8252 11698 -34 -3268 2185 A C ATOM 2066 N LEU A 289 55.031 -18.845 17.708 1.00 90.35 A N ANISOU 2066 N LEU A 289 12824 8998 12507 -326 -3292 2496 A N ATOM 2067 CA LEU A 289 54.119 -19.907 18.109 1.00 91.54 A C ANISOU 2067 CA LEU A 289 13244 8922 12615 -403 -3289 2612 A C ATOM 2068 C LEU A 289 52.784 -19.335 18.578 1.00 88.00 A C ANISOU 2068 C LEU A 289 12926 8515 11994 -665 -3088 2643 A C ATOM 2069 O LEU A 289 51.728 -19.907 18.306 1.00 85.67 A O ANISOU 2069 O LEU A 289 12744 8099 11709 -761 -2968 2655 A O ATOM 2070 CB LEU A 289 54.742 -20.795 19.190 1.00 88.47 A C ANISOU 2070 CB LEU A 289 13057 8389 12167 -329 -3543 2787 A C ATOM 2071 CG LEU A 289 55.809 -21.789 18.723 1.00 89.81 A C ANISOU 2071 CG LEU A 289 13165 8436 12522 -45 -3745 2780 A C ATOM 2072 CD1 LEU A 289 56.609 -22.301 19.911 1.00 85.84 A C ANISOU 2072 CD1 LEU A 289 12818 7867 11932 37 -4015 2950 A C ATOM 2073 CD2 LEU A 289 55.191 -22.951 17.952 1.00 88.63 A C ANISOU 2073 CD2 LEU A 289 13128 8040 12506 9 -3696 2760 A C ATOM 2074 N ASP A 290 52.824 -18.200 19.270 1.00 82.37 A N ANISOU 2074 N ASP A 290 12194 7981 11123 -780 -3048 2646 A N ATOM 2075 CA ASP A 290 51.588 -17.607 19.759 1.00 83.08 A C ANISOU 2075 CA ASP A 290 12400 8127 11040 -1006 -2853 2667 A C ATOM 2076 C ASP A 290 50.713 -17.121 18.607 1.00 81.40 A C ANISOU 2076 C ASP A 290 12035 7982 10911 -1046 -2613 2520 A C ATOM 2077 O ASP A 290 49.501 -17.344 18.607 1.00 84.57 A O ANISOU 2077 O ASP A 290 12534 8340 11258 -1184 -2460 2539 A O ATOM 2078 CB ASP A 290 51.857 -16.462 20.726 1.00 88.91 A C ANISOU 2078 CB ASP A 290 13160 9034 11587 -1105 -2863 2685 A C ATOM 2079 CG ASP A 290 50.579 -15.919 21.342 1.00 93.86 A C ANISOU 2079 CG ASP A 290 13928 9715 12019 -1321 -2664 2711 A C ATOM 2080 OD1 ASP A 290 49.809 -16.717 21.921 1.00 91.94 A O ANISOU 2080 OD1 ASP A 290 13891 9352 11688 -1426 -2644 2831 A O ATOM 2081 OD2 ASP A 290 50.344 -14.696 21.245 1.00 94.29 A O1- ANISOU 2081 OD2 ASP A 290 13891 9931 12005 -1383 -2524 2611 A O1- ATOM 2082 N LEU A 291 51.326 -16.464 17.625 1.00 70.45 A N ANISOU 2082 N LEU A 291 10406 6712 9651 -929 -2583 2377 A N ATOM 2083 CA LEU A 291 50.578 -15.993 16.465 1.00 73.11 A C ANISOU 2083 CA LEU A 291 10596 7116 10068 -947 -2373 2238 A C ATOM 2084 C LEU A 291 49.983 -17.142 15.646 1.00 77.68 A C ANISOU 2084 C LEU A 291 11199 7534 10780 -908 -2338 2221 A C ATOM 2085 O LEU A 291 48.818 -17.069 15.228 1.00 74.56 A O ANISOU 2085 O LEU A 291 10810 7151 10369 -1017 -2161 2181 A O ATOM 2086 CB LEU A 291 51.433 -15.084 15.577 1.00 64.64 A C ANISOU 2086 CB LEU A 291 9272 6194 9093 -834 -2356 2100 A C ATOM 2087 CG LEU A 291 50.754 -14.548 14.305 1.00 60.90 A C ANISOU 2087 CG LEU A 291 8645 5797 8699 -835 -2151 1958 A C ATOM 2088 CD1 LEU A 291 49.369 -13.987 14.595 1.00 58.24 A C ANISOU 2088 CD1 LEU A 291 8399 5506 8225 -1005 -1959 1964 A C ATOM 2089 CD2 LEU A 291 51.624 -13.494 13.627 1.00 61.21 A C ANISOU 2089 CD2 LEU A 291 8469 5996 8793 -760 -2132 1845 A C ATOM 2090 N ILE A 292 50.772 -18.194 15.415 1.00 72.74 A N ANISOU 2090 N ILE A 292 10588 6764 10285 -752 -2509 2246 A N ATOM 2091 CA ILE A 292 50.276 -19.337 14.653 1.00 75.03 A C ANISOU 2091 CA ILE A 292 10930 6876 10704 -712 -2493 2223 A C ATOM 2092 C ILE A 292 49.103 -19.971 15.374 1.00 82.12 A C ANISOU 2092 C ILE A 292 12068 7646 11488 -909 -2441 2344 A C ATOM 2093 O ILE A 292 48.129 -20.398 14.753 1.00 87.11 A O ANISOU 2093 O ILE A 292 12718 8217 12164 -991 -2320 2302 A O ATOM 2094 CB ILE A 292 51.325 -20.422 14.468 1.00 73.88 A C ANISOU 2094 CB ILE A 292 10806 6567 10698 -501 -2701 2245 A C ATOM 2095 CG1 ILE A 292 52.498 -19.910 13.639 1.00 69.57 A C ANISOU 2095 CG1 ILE A 292 9995 6160 10280 -299 -2743 2115 A C ATOM 2096 CG2 ILE A 292 50.686 -21.645 13.809 1.00 75.46 A C ANISOU 2096 CG2 ILE A 292 11117 6548 11006 -491 -2684 2229 A C ATOM 2097 CD1 ILE A 292 53.734 -20.810 13.717 1.00 72.55 A C ANISOU 2097 CD1 ILE A 292 10371 6425 10770 -65 -2973 2148 A C ATOM 2098 N ASP A 293 49.210 -20.037 16.694 1.00 82.03 A N ANISOU 2098 N ASP A 293 12238 7604 11323 -993 -2534 2497 A N ATOM 2099 CA ASP A 293 48.131 -20.552 17.522 1.00 92.45 A C ANISOU 2099 CA ASP A 293 13793 8829 12504 -1203 -2476 2629 A C ATOM 2100 C ASP A 293 46.841 -19.736 17.340 1.00 90.91 A C ANISOU 2100 C ASP A 293 13530 8794 12217 -1388 -2223 2564 A C ATOM 2101 O ASP A 293 45.734 -20.283 17.351 1.00 89.79 A O ANISOU 2101 O ASP A 293 13488 8585 12042 -1546 -2118 2603 A O ATOM 2102 CB ASP A 293 48.570 -20.549 18.989 1.00102.42 A C ANISOU 2102 CB ASP A 293 15247 10077 13592 -1254 -2615 2795 A C ATOM 2103 CG ASP A 293 47.602 -21.275 19.892 1.00107.33 A C ANISOU 2103 CG ASP A 293 16141 10573 14068 -1463 -2583 2955 A C ATOM 2104 OD1 ASP A 293 46.924 -22.214 19.418 1.00115.95 A O ANISOU 2104 OD1 ASP A 293 17313 11504 15238 -1522 -2541 2967 A O ATOM 2105 OD2 ASP A 293 47.525 -20.903 21.081 1.00103.83 A O1- ANISOU 2105 OD2 ASP A 293 15834 10195 13422 -1577 -2598 3067 A O1- ATOM 2106 N LYS A 294 46.993 -18.426 17.164 1.00 87.10 A N ANISOU 2106 N LYS A 294 12874 8524 11695 -1365 -2128 2465 A N ATOM 2107 CA LYS A 294 45.847 -17.536 17.005 1.00 84.33 A C ANISOU 2107 CA LYS A 294 12451 8337 11255 -1502 -1896 2397 A C ATOM 2108 C LYS A 294 45.293 -17.529 15.580 1.00 80.15 A C ANISOU 2108 C LYS A 294 11741 7838 10875 -1460 -1768 2253 A C ATOM 2109 O LYS A 294 44.149 -17.134 15.361 1.00 77.48 A O ANISOU 2109 O LYS A 294 11357 7600 10482 -1577 -1585 2210 A O ATOM 2110 CB LYS A 294 46.206 -16.127 17.468 1.00 85.14 A C ANISOU 2110 CB LYS A 294 12482 8629 11238 -1498 -1853 2356 A C ATOM 2111 CG LYS A 294 46.547 -16.094 18.940 1.00 91.24 A C ANISOU 2111 CG LYS A 294 13449 9390 11827 -1574 -1959 2496 A C ATOM 2112 CD LYS A 294 46.831 -14.696 19.442 1.00 91.54 A C ANISOU 2112 CD LYS A 294 13443 9605 11732 -1591 -1912 2447 A C ATOM 2113 CE LYS A 294 47.149 -14.738 20.928 1.00 92.57 A C ANISOU 2113 CE LYS A 294 13786 9722 11664 -1675 -2028 2586 A C ATOM 2114 NZ LYS A 294 47.393 -13.385 21.491 1.00 96.25 A N1+ ANISOU 2114 NZ LYS A 294 14239 10349 11981 -1710 -1986 2533 A N1+ ATOM 2115 N LEU A 295 46.109 -17.968 14.622 1.00 77.06 A N ANISOU 2115 N LEU A 295 11245 7371 10664 -1287 -1867 2175 A N ATOM 2116 CA LEU A 295 45.659 -18.181 13.249 1.00 69.16 A C ANISOU 2116 CA LEU A 295 10102 6370 9805 -1240 -1775 2044 A C ATOM 2117 C LEU A 295 44.911 -19.515 13.096 1.00 79.17 A C ANISOU 2117 C LEU A 295 11509 7449 11124 -1330 -1787 2091 A C ATOM 2118 O LEU A 295 43.835 -19.565 12.503 1.00 80.64 A O ANISOU 2118 O LEU A 295 11645 7676 11320 -1435 -1647 2033 A O ATOM 2119 CB LEU A 295 46.841 -18.146 12.282 1.00 59.91 A C ANISOU 2119 CB LEU A 295 8770 5199 8795 -1020 -1867 1936 A C ATOM 2120 CG LEU A 295 47.531 -16.804 12.054 1.00 62.63 A C ANISOU 2120 CG LEU A 295 8935 5739 9122 -940 -1829 1855 A C ATOM 2121 CD1 LEU A 295 48.794 -17.007 11.250 1.00 65.61 A C ANISOU 2121 CD1 LEU A 295 9171 6103 9654 -734 -1942 1774 A C ATOM 2122 CD2 LEU A 295 46.603 -15.851 11.341 1.00 60.33 A C ANISOU 2122 CD2 LEU A 295 8519 5605 8800 -1005 -1624 1752 A C ATOM 2123 N LEU A 296 45.475 -20.596 13.630 1.00 78.41 A N ANISOU 2123 N LEU A 296 11592 7143 11057 -1294 -1961 2199 A N ATOM 2124 CA LEU A 296 44.836 -21.904 13.497 1.00 83.90 A C ANISOU 2124 CA LEU A 296 12451 7625 11803 -1386 -1987 2248 A C ATOM 2125 C LEU A 296 43.792 -22.135 14.586 1.00 88.93 A C ANISOU 2125 C LEU A 296 13276 8242 12270 -1642 -1917 2395 A C ATOM 2126 O LEU A 296 43.783 -23.169 15.239 1.00 94.98 A O ANISOU 2126 O LEU A 296 14275 8803 13011 -1713 -2025 2530 A O ATOM 2127 CB LEU A 296 45.871 -23.032 13.476 1.00 81.97 A C ANISOU 2127 CB LEU A 296 12333 7135 11676 -1217 -2205 2292 A C ATOM 2128 CG LEU A 296 46.892 -22.971 12.335 1.00 77.53 A C ANISOU 2128 CG LEU A 296 11582 6588 11290 -958 -2268 2140 A C ATOM 2129 CD1 LEU A 296 47.841 -24.158 12.387 1.00 79.52 A C ANISOU 2129 CD1 LEU A 296 11972 6591 11652 -778 -2482 2186 A C ATOM 2130 CD2 LEU A 296 46.194 -22.904 10.990 1.00 74.24 A C ANISOU 2130 CD2 LEU A 296 11015 6226 10965 -973 -2124 1976 A C ATOM 2131 N VAL A 297 42.916 -21.152 14.766 1.00 88.64 A N ANISOU 2131 N VAL A 297 13140 8425 12114 -1774 -1732 2367 A N ATOM 2132 CA VAL A 297 41.810 -21.244 15.713 1.00 79.44 A C ANISOU 2132 CA VAL A 297 12109 7296 10779 -2022 -1623 2484 A C ATOM 2133 C VAL A 297 40.581 -21.827 15.018 1.00 81.24 A C ANISOU 2133 C VAL A 297 12306 7505 11055 -2182 -1500 2438 A C ATOM 2134 O VAL A 297 40.272 -21.463 13.882 1.00 81.29 A O ANISOU 2134 O VAL A 297 12113 7613 11163 -2122 -1413 2287 A O ATOM 2135 CB VAL A 297 41.495 -19.855 16.322 1.00 78.91 A C ANISOU 2135 CB VAL A 297 11950 7484 10547 -2068 -1483 2470 A C ATOM 2136 CG1 VAL A 297 40.066 -19.777 16.819 1.00 79.56 A C ANISOU 2136 CG1 VAL A 297 12066 7679 10486 -2307 -1296 2518 A C ATOM 2137 CG2 VAL A 297 42.469 -19.538 17.437 1.00 78.52 A C ANISOU 2137 CG2 VAL A 297 12024 7423 10388 -2009 -1614 2571 A C ATOM 2138 N LEU A 298 39.888 -22.737 15.700 1.00 84.28 A N ANISOU 2138 N LEU A 298 12893 7766 11365 -2394 -1497 2572 A N ATOM 2139 CA LEU A 298 38.770 -23.473 15.110 1.00 79.41 A C ANISOU 2139 CA LEU A 298 12273 7103 10796 -2577 -1407 2545 A C ATOM 2140 C LEU A 298 37.562 -22.605 14.750 1.00 78.46 A C ANISOU 2140 C LEU A 298 11933 7265 10615 -2695 -1180 2452 A C ATOM 2141 O LEU A 298 37.087 -22.628 13.619 1.00 76.21 A O ANISOU 2141 O LEU A 298 11484 7031 10439 -2682 -1120 2319 A O ATOM 2142 CB LEU A 298 38.332 -24.591 16.048 1.00 78.51 A C ANISOU 2142 CB LEU A 298 12441 6796 10592 -2803 -1454 2729 A C ATOM 2143 CG LEU A 298 39.260 -25.797 16.120 1.00 86.33 A C ANISOU 2143 CG LEU A 298 13672 7447 11681 -2708 -1682 2812 A C ATOM 2144 CD1 LEU A 298 38.908 -26.651 17.334 1.00 90.14 A C ANISOU 2144 CD1 LEU A 298 14462 7766 12022 -2932 -1724 3029 A C ATOM 2145 CD2 LEU A 298 39.188 -26.607 14.829 1.00 82.97 A C ANISOU 2145 CD2 LEU A 298 13212 6860 11452 -2659 -1726 2687 A C ATOM 2146 N ASP A 299 37.046 -21.859 15.717 1.00 81.04 A N ANISOU 2146 N ASP A 299 12258 7777 10758 -2804 -1057 2520 A N ATOM 2147 CA ASP A 299 35.914 -20.987 15.451 1.00 86.95 A C ANISOU 2147 CA ASP A 299 12794 8804 11440 -2887 -842 2433 A C ATOM 2148 C ASP A 299 36.377 -19.793 14.612 1.00 94.07 A C ANISOU 2148 C ASP A 299 13468 9862 12411 -2652 -809 2273 A C ATOM 2149 O ASP A 299 37.167 -18.963 15.074 1.00 93.30 A O ANISOU 2149 O ASP A 299 13377 9815 12257 -2516 -843 2276 A O ATOM 2150 CB ASP A 299 35.282 -20.519 16.762 1.00 94.03 A C ANISOU 2150 CB ASP A 299 13765 9851 12112 -3049 -714 2545 A C ATOM 2151 CG ASP A 299 34.036 -19.686 16.545 1.00103.34 A C ANISOU 2151 CG ASP A 299 14724 11323 13217 -3130 -486 2460 A C ATOM 2152 OD1 ASP A 299 33.489 -19.718 15.421 1.00106.65 A O ANISOU 2152 OD1 ASP A 299 14957 11809 13756 -3117 -434 2340 A O ATOM 2153 OD2 ASP A 299 33.602 -18.999 17.497 1.00105.71 A O1- ANISOU 2153 OD2 ASP A 299 15038 11793 13335 -3198 -361 2508 A O1- ATOM 2154 N PRO A 300 35.888 -19.710 13.366 1.00 94.16 A N ANISOU 2154 N PRO A 300 13287 9949 12541 -2613 -748 2134 A N ATOM 2155 CA PRO A 300 36.239 -18.634 12.431 1.00 81.40 A C ANISOU 2155 CA PRO A 300 11460 8475 10993 -2404 -712 1983 A C ATOM 2156 C PRO A 300 36.083 -17.266 13.069 1.00 81.54 A C ANISOU 2156 C PRO A 300 11409 8708 10866 -2361 -590 1977 A C ATOM 2157 O PRO A 300 36.777 -16.326 12.691 1.00 85.27 A O ANISOU 2157 O PRO A 300 11791 9242 11365 -2178 -603 1897 A O ATOM 2158 CB PRO A 300 35.196 -18.795 11.315 1.00 77.38 A C ANISOU 2158 CB PRO A 300 10776 8068 10559 -2467 -615 1873 A C ATOM 2159 CG PRO A 300 34.107 -19.648 11.928 1.00 85.15 A C ANISOU 2159 CG PRO A 300 11848 9038 11468 -2742 -552 1972 A C ATOM 2160 CD PRO A 300 34.873 -20.602 12.785 1.00 91.15 A C ANISOU 2160 CD PRO A 300 12877 9538 12217 -2792 -702 2114 A C ATOM 2161 N ALA A 301 35.175 -17.160 14.031 1.00 83.74 A N ANISOU 2161 N ALA A 301 11737 9095 10985 -2534 -469 2059 A N ATOM 2162 CA ALA A 301 34.857 -15.873 14.635 1.00 83.47 A C ANISOU 2162 CA ALA A 301 11642 9271 10800 -2498 -331 2039 A C ATOM 2163 C ALA A 301 35.823 -15.524 15.750 1.00 81.43 A C ANISOU 2163 C ALA A 301 11561 8946 10434 -2452 -416 2125 A C ATOM 2164 O ALA A 301 35.905 -14.365 16.159 1.00 81.84 A O ANISOU 2164 O ALA A 301 11584 9132 10379 -2376 -342 2089 A O ATOM 2165 CB ALA A 301 33.430 -15.863 15.149 1.00 84.55 A C ANISOU 2165 CB ALA A 301 11733 9587 10805 -2690 -147 2073 A C ATOM 2166 N GLN A 302 36.545 -16.526 16.243 1.00 81.38 A N ANISOU 2166 N GLN A 302 11746 8727 10450 -2497 -579 2239 A N ATOM 2167 CA GLN A 302 37.545 -16.304 17.282 1.00 84.99 A C ANISOU 2167 CA GLN A 302 12372 9112 10808 -2451 -694 2328 A C ATOM 2168 C GLN A 302 38.951 -16.304 16.686 1.00 84.55 A C ANISOU 2168 C GLN A 302 12295 8928 10902 -2246 -879 2279 A C ATOM 2169 O GLN A 302 39.934 -16.021 17.376 1.00 80.92 A O ANISOU 2169 O GLN A 302 11934 8426 10386 -2176 -995 2330 A O ATOM 2170 CB GLN A 302 37.438 -17.360 18.378 1.00 86.23 A C ANISOU 2170 CB GLN A 302 12771 9132 10861 -2629 -760 2505 A C ATOM 2171 CG GLN A 302 36.174 -17.293 19.220 1.00 93.33 A C ANISOU 2171 CG GLN A 302 13713 10178 11572 -2847 -574 2574 A C ATOM 2172 CD GLN A 302 36.167 -18.347 20.325 1.00102.85 A C ANISOU 2172 CD GLN A 302 15184 11234 12662 -3032 -649 2765 A C ATOM 2173 NE2 GLN A 302 35.159 -19.215 20.313 1.00 95.84 A N ANISOU 2173 NE2 GLN A 302 14325 10327 11763 -3246 -566 2827 A N ATOM 2174 OE1 GLN A 302 37.066 -18.383 21.171 1.00108.16 A O ANISOU 2174 OE1 GLN A 302 16036 11809 13252 -2989 -786 2860 A O ATOM 2175 N ARG A 303 39.033 -16.626 15.399 1.00 80.38 A N ANISOU 2175 N ARG A 303 11628 8353 10557 -2155 -903 2178 A N ATOM 2176 CA ARG A 303 40.291 -16.600 14.663 1.00 73.81 A C ANISOU 2176 CA ARG A 303 10736 7433 9876 -1954 -1049 2110 A C ATOM 2177 C ARG A 303 40.744 -15.164 14.425 1.00 73.55 A C ANISOU 2177 C ARG A 303 10566 7562 9818 -1823 -995 2011 A C ATOM 2178 O ARG A 303 39.969 -14.326 13.954 1.00 83.38 A O ANISOU 2178 O ARG A 303 11677 8969 11034 -1823 -836 1922 A O ATOM 2179 CB ARG A 303 40.119 -17.318 13.326 1.00 71.02 A C ANISOU 2179 CB ARG A 303 10276 7004 9705 -1905 -1064 2017 A C ATOM 2180 CG ARG A 303 41.397 -17.523 12.531 1.00 67.52 A C ANISOU 2180 CG ARG A 303 9777 6455 9422 -1701 -1213 1949 A C ATOM 2181 CD ARG A 303 41.094 -18.423 11.353 1.00 68.90 A C ANISOU 2181 CD ARG A 303 9896 6531 9750 -1683 -1225 1868 A C ATOM 2182 NE ARG A 303 40.268 -19.548 11.782 1.00 73.92 A N ANISOU 2182 NE ARG A 303 10689 7037 10360 -1872 -1228 1962 A N ATOM 2183 CZ ARG A 303 39.318 -20.124 11.052 1.00 69.51 A C ANISOU 2183 CZ ARG A 303 10088 6465 9857 -1977 -1159 1908 A C ATOM 2184 NH1 ARG A 303 39.039 -19.691 9.828 1.00 62.57 A N1+ ANISOU 2184 NH1 ARG A 303 9012 5701 9059 -1900 -1084 1758 A N1+ ATOM 2185 NH2 ARG A 303 38.635 -21.135 11.563 1.00 71.73 A N ANISOU 2185 NH2 ARG A 303 10531 6619 10103 -2174 -1169 2008 A N ATOM 2186 N ILE A 304 42.002 -14.888 14.747 1.00 64.10 A N ANISOU 2186 N ILE A 304 9406 6319 8630 -1711 -1134 2028 A N ATOM 2187 CA ILE A 304 42.562 -13.547 14.588 1.00 64.83 A C ANISOU 2187 CA ILE A 304 9394 6543 8695 -1608 -1102 1943 A C ATOM 2188 C ILE A 304 42.443 -13.041 13.138 1.00 63.43 A C ANISOU 2188 C ILE A 304 9009 6445 8646 -1499 -1019 1796 A C ATOM 2189 O ILE A 304 42.475 -13.826 12.186 1.00 62.12 A O ANISOU 2189 O ILE A 304 8774 6202 8626 -1448 -1057 1752 A O ATOM 2190 CB ILE A 304 44.037 -13.511 15.062 1.00 65.91 A C ANISOU 2190 CB ILE A 304 9583 6613 8847 -1515 -1292 1985 A C ATOM 2191 CG1 ILE A 304 44.474 -12.082 15.372 1.00 61.14 A C ANISOU 2191 CG1 ILE A 304 8939 6144 8147 -1484 -1253 1933 A C ATOM 2192 CG2 ILE A 304 44.958 -14.174 14.039 1.00 66.18 A C ANISOU 2192 CG2 ILE A 304 9514 6549 9081 -1365 -1418 1931 A C ATOM 2193 CD1 ILE A 304 45.859 -12.001 15.961 1.00 60.83 A C ANISOU 2193 CD1 ILE A 304 8945 6066 8099 -1425 -1441 1979 A C ATOM 2194 N ASP A 305 42.272 -11.733 12.971 1.00 63.49 A N ANISOU 2194 N ASP A 305 8934 6599 8591 -1463 -906 1721 A N ATOM 2195 CA ASP A 305 42.171 -11.159 11.628 1.00 62.34 A C ANISOU 2195 CA ASP A 305 8608 6532 8545 -1359 -829 1593 A C ATOM 2196 C ASP A 305 43.492 -10.518 11.213 1.00 61.91 A C ANISOU 2196 C ASP A 305 8485 6482 8554 -1235 -916 1540 A C ATOM 2197 O ASP A 305 44.406 -10.373 12.027 1.00 59.46 A O ANISOU 2197 O ASP A 305 8255 6139 8199 -1235 -1026 1596 A O ATOM 2198 CB ASP A 305 41.015 -10.161 11.526 1.00 65.06 A C ANISOU 2198 CB ASP A 305 8897 7032 8791 -1388 -639 1539 A C ATOM 2199 CG ASP A 305 41.187 -8.957 12.448 1.00 82.31 A C ANISOU 2199 CG ASP A 305 11163 9290 10822 -1397 -594 1550 A C ATOM 2200 OD1 ASP A 305 42.328 -8.655 12.874 1.00 85.97 A O ANISOU 2200 OD1 ASP A 305 11683 9707 11274 -1366 -708 1571 A O ATOM 2201 OD2 ASP A 305 40.170 -8.295 12.739 1.00 87.22 A O1- ANISOU 2201 OD2 ASP A 305 11789 10020 11330 -1433 -444 1531 A O1- ATOM 2202 N SER A 306 43.601 -10.143 9.947 1.00 59.02 A N ANISOU 2202 N SER A 306 7968 6168 8288 -1137 -870 1435 A N ATOM 2203 CA SER A 306 44.869 -9.647 9.449 1.00 62.61 A C ANISOU 2203 CA SER A 306 8340 6635 8813 -1033 -946 1386 A C ATOM 2204 C SER A 306 45.313 -8.404 10.219 1.00 68.23 A C ANISOU 2204 C SER A 306 9109 7414 9404 -1061 -935 1398 A C ATOM 2205 O SER A 306 46.499 -8.220 10.500 1.00 73.08 A O ANISOU 2205 O SER A 306 9720 8014 10034 -1034 -1051 1412 A O ATOM 2206 CB SER A 306 44.789 -9.381 7.948 1.00 65.02 A C ANISOU 2206 CB SER A 306 8486 7000 9219 -939 -874 1274 A C ATOM 2207 OG SER A 306 43.663 -8.590 7.641 1.00 77.89 A O ANISOU 2207 OG SER A 306 10090 8729 10776 -962 -717 1232 A O ATOM 2208 N ASP A 307 44.358 -7.565 10.595 1.00 67.05 A N ANISOU 2208 N ASP A 307 9011 7337 9126 -1116 -799 1390 A N ATOM 2209 CA ASP A 307 44.707 -6.322 11.266 1.00 62.11 A C ANISOU 2209 CA ASP A 307 8459 6761 8379 -1141 -777 1385 A C ATOM 2210 C ASP A 307 45.349 -6.582 12.619 1.00 66.71 A C ANISOU 2210 C ASP A 307 9182 7291 8873 -1216 -903 1476 A C ATOM 2211 O ASP A 307 46.390 -6.009 12.941 1.00 71.15 A O ANISOU 2211 O ASP A 307 9761 7859 9414 -1216 -993 1473 A O ATOM 2212 CB ASP A 307 43.491 -5.407 11.416 1.00 66.98 A C ANISOU 2212 CB ASP A 307 9116 7459 8873 -1163 -601 1351 A C ATOM 2213 CG ASP A 307 43.883 -3.973 11.729 1.00 79.69 A C ANISOU 2213 CG ASP A 307 10791 9106 10382 -1158 -566 1311 A C ATOM 2214 OD1 ASP A 307 44.606 -3.344 10.912 1.00 84.96 A O ANISOU 2214 OD1 ASP A 307 11380 9782 11117 -1101 -582 1254 A O ATOM 2215 OD2 ASP A 307 43.471 -3.478 12.799 1.00 82.90 A O1- ANISOU 2215 OD2 ASP A 307 11335 9527 10634 -1219 -519 1336 A O1- ATOM 2216 N ASP A 308 44.730 -7.448 13.412 1.00 65.29 A N ANISOU 2216 N ASP A 308 9106 7066 8635 -1291 -914 1560 A N ATOM 2217 CA ASP A 308 45.258 -7.759 14.734 1.00 72.17 A C ANISOU 2217 CA ASP A 308 10131 7887 9404 -1365 -1037 1659 A C ATOM 2218 C ASP A 308 46.534 -8.579 14.630 1.00 68.62 A C ANISOU 2218 C ASP A 308 9644 7354 9074 -1305 -1239 1699 A C ATOM 2219 O ASP A 308 47.441 -8.465 15.462 1.00 65.61 A O ANISOU 2219 O ASP A 308 9335 6961 8633 -1325 -1375 1751 A O ATOM 2220 CB ASP A 308 44.217 -8.500 15.572 1.00 80.26 A C ANISOU 2220 CB ASP A 308 11283 8886 10326 -1470 -984 1748 A C ATOM 2221 CG ASP A 308 43.003 -7.649 15.866 1.00 86.22 A C ANISOU 2221 CG ASP A 308 12072 9747 10939 -1523 -786 1711 A C ATOM 2222 OD1 ASP A 308 43.165 -6.421 16.031 1.00 91.34 A O ANISOU 2222 OD1 ASP A 308 12740 10460 11503 -1501 -732 1650 A O ATOM 2223 OD2 ASP A 308 41.888 -8.206 15.927 1.00 83.68 A O1- ANISOU 2223 OD2 ASP A 308 11757 9447 10591 -1586 -684 1740 A O1- ATOM 2224 N ALA A 309 46.596 -9.406 13.597 1.00 65.51 A N ANISOU 2224 N ALA A 309 9134 6910 8847 -1225 -1260 1669 A N ATOM 2225 CA ALA A 309 47.750 -10.251 13.391 1.00 62.00 A C ANISOU 2225 CA ALA A 309 8640 6386 8529 -1137 -1441 1694 A C ATOM 2226 C ALA A 309 48.935 -9.355 13.115 1.00 61.48 A C ANISOU 2226 C ALA A 309 8464 6401 8495 -1077 -1501 1634 A C ATOM 2227 O ALA A 309 50.023 -9.582 13.642 1.00 63.59 A O ANISOU 2227 O ALA A 309 8737 6652 8773 -1050 -1668 1681 A O ATOM 2228 CB ALA A 309 47.514 -11.218 12.235 1.00 60.44 A C ANISOU 2228 CB ALA A 309 8345 6123 8498 -1055 -1429 1647 A C ATOM 2229 N LEU A 310 48.721 -8.330 12.292 1.00 57.91 A N ANISOU 2229 N LEU A 310 7910 6040 8052 -1062 -1368 1535 A N ATOM 2230 CA LEU A 310 49.789 -7.386 11.975 1.00 62.53 A C ANISOU 2230 CA LEU A 310 8394 6706 8659 -1034 -1405 1478 A C ATOM 2231 C LEU A 310 50.282 -6.679 13.236 1.00 65.94 A C ANISOU 2231 C LEU A 310 8947 7164 8942 -1129 -1482 1528 A C ATOM 2232 O LEU A 310 51.450 -6.298 13.335 1.00 57.44 A O ANISOU 2232 O LEU A 310 7805 6135 7886 -1125 -1594 1517 A O ATOM 2233 CB LEU A 310 49.327 -6.374 10.933 1.00 57.66 A C ANISOU 2233 CB LEU A 310 7690 6165 8053 -1017 -1239 1378 A C ATOM 2234 CG LEU A 310 49.293 -6.955 9.524 1.00 56.77 A C ANISOU 2234 CG LEU A 310 7420 6052 8097 -909 -1200 1311 A C ATOM 2235 CD1 LEU A 310 48.814 -5.912 8.522 1.00 49.90 A C ANISOU 2235 CD1 LEU A 310 6481 5260 7219 -894 -1041 1224 A C ATOM 2236 CD2 LEU A 310 50.665 -7.472 9.153 1.00 50.94 A C ANISOU 2236 CD2 LEU A 310 6552 5318 7483 -825 -1342 1300 A C ATOM 2237 N ASN A 311 49.386 -6.535 14.207 1.00 63.32 A N ANISOU 2237 N ASN A 311 8789 6812 8457 -1221 -1422 1579 A N ATOM 2238 CA ASN A 311 49.695 -5.826 15.438 1.00 69.30 A C ANISOU 2238 CA ASN A 311 9691 7595 9047 -1319 -1477 1616 A C ATOM 2239 C ASN A 311 50.409 -6.711 16.465 1.00 74.30 A C ANISOU 2239 C ASN A 311 10407 8178 9648 -1338 -1679 1726 A C ATOM 2240 O ASN A 311 51.032 -6.214 17.404 1.00 77.48 A O ANISOU 2240 O ASN A 311 10896 8610 9932 -1407 -1780 1755 A O ATOM 2241 CB ASN A 311 48.409 -5.242 16.022 1.00 73.53 A C ANISOU 2241 CB ASN A 311 10376 8145 9417 -1397 -1311 1614 A C ATOM 2242 CG ASN A 311 48.660 -4.381 17.242 1.00 83.40 A C ANISOU 2242 CG ASN A 311 11791 9421 10475 -1496 -1345 1629 A C ATOM 2243 ND2 ASN A 311 47.879 -4.609 18.295 1.00 86.79 A N ANISOU 2243 ND2 ASN A 311 12391 9838 10746 -1570 -1304 1693 A N ATOM 2244 OD1 ASN A 311 49.541 -3.517 17.240 1.00 78.47 A O ANISOU 2244 OD1 ASN A 311 11146 8833 9837 -1517 -1405 1582 A O ATOM 2245 N HIS A 312 50.319 -8.022 16.263 1.00 74.43 A N ANISOU 2245 N HIS A 312 10405 8110 9766 -1275 -1744 1785 A N ATOM 2246 CA HIS A 312 50.918 -9.015 17.153 1.00 71.11 A C ANISOU 2246 CA HIS A 312 10077 7617 9327 -1269 -1940 1902 A C ATOM 2247 C HIS A 312 52.411 -8.782 17.407 1.00 71.99 A C ANISOU 2247 C HIS A 312 10105 7781 9466 -1228 -2136 1905 A C ATOM 2248 O HIS A 312 53.152 -8.361 16.513 1.00 65.39 A O ANISOU 2248 O HIS A 312 9079 7014 8750 -1160 -2143 1819 A O ATOM 2249 CB HIS A 312 50.696 -10.421 16.591 1.00 67.83 A C ANISOU 2249 CB HIS A 312 9632 7083 9056 -1181 -1977 1940 A C ATOM 2250 CG HIS A 312 51.067 -11.516 17.540 1.00 77.81 A C ANISOU 2250 CG HIS A 312 11039 8240 10287 -1176 -2162 2077 A C ATOM 2251 CD2 HIS A 312 50.302 -12.307 18.332 1.00 79.19 A C ANISOU 2251 CD2 HIS A 312 11410 8312 10365 -1256 -2164 2191 A C ATOM 2252 ND1 HIS A 312 52.371 -11.909 17.751 1.00 79.10 A N ANISOU 2252 ND1 HIS A 312 11147 8392 10513 -1077 -2380 2114 A N ATOM 2253 CE1 HIS A 312 52.395 -12.892 18.632 1.00 86.52 A C ANISOU 2253 CE1 HIS A 312 12258 9218 11399 -1084 -2517 2248 A C ATOM 2254 NE2 HIS A 312 51.152 -13.154 18.998 1.00 86.82 A N ANISOU 2254 NE2 HIS A 312 12458 9193 11336 -1201 -2386 2300 A N ATOM 2255 N ASP A 313 52.845 -9.076 18.631 1.00 78.63 A N ANISOU 2255 N ASP A 313 11087 8602 10189 -1275 -2298 2009 A N ATOM 2256 CA ASP A 313 54.212 -8.784 19.064 1.00 85.29 A C ANISOU 2256 CA ASP A 313 11862 9519 11025 -1259 -2497 2020 A C ATOM 2257 C ASP A 313 55.282 -9.440 18.188 1.00 86.28 A C ANISOU 2257 C ASP A 313 11764 9655 11364 -1095 -2625 1993 A C ATOM 2258 O ASP A 313 56.433 -9.005 18.168 1.00 87.40 A O ANISOU 2258 O ASP A 313 11765 9902 11539 -1074 -2747 1962 A O ATOM 2259 CB ASP A 313 54.409 -9.182 20.529 1.00 96.89 A C ANISOU 2259 CB ASP A 313 13533 10954 12325 -1325 -2664 2151 A C ATOM 2260 CG ASP A 313 53.780 -8.191 21.494 1.00102.18 A C ANISOU 2260 CG ASP A 313 14394 11670 12759 -1492 -2570 2149 A C ATOM 2261 OD1 ASP A 313 53.650 -6.997 21.133 1.00 97.84 A O ANISOU 2261 OD1 ASP A 313 13794 11198 12180 -1549 -2440 2039 A O ATOM 2262 OD2 ASP A 313 53.424 -8.611 22.618 1.00106.72 A O1- ANISOU 2262 OD2 ASP A 313 15179 12198 13170 -1562 -2626 2258 A O1- ATOM 2263 N PHE A 314 54.897 -10.489 17.473 1.00 84.22 A N ANISOU 2263 N PHE A 314 11469 9289 11240 -984 -2593 2001 A N ATOM 2264 CA PHE A 314 55.788 -11.157 16.532 1.00 78.85 A C ANISOU 2264 CA PHE A 314 10583 8610 10765 -807 -2683 1958 A C ATOM 2265 C PHE A 314 56.405 -10.169 15.517 1.00 73.52 A C ANISOU 2265 C PHE A 314 9670 8087 10179 -789 -2603 1824 A C ATOM 2266 O PHE A 314 57.534 -10.353 15.078 1.00 75.26 A O ANISOU 2266 O PHE A 314 9696 8381 10518 -676 -2717 1791 A O ATOM 2267 CB PHE A 314 55.011 -12.281 15.833 1.00 73.85 A C ANISOU 2267 CB PHE A 314 9984 7828 10246 -720 -2611 1961 A C ATOM 2268 CG PHE A 314 55.767 -12.977 14.728 1.00 73.95 A C ANISOU 2268 CG PHE A 314 9798 7830 10468 -526 -2668 1893 A C ATOM 2269 CD1 PHE A 314 56.790 -13.867 15.017 1.00 78.51 A C ANISOU 2269 CD1 PHE A 314 10341 8365 11125 -375 -2886 1950 A C ATOM 2270 CD2 PHE A 314 55.414 -12.774 13.398 1.00 73.09 A C ANISOU 2270 CD2 PHE A 314 9548 7753 10471 -482 -2501 1770 A C ATOM 2271 CE1 PHE A 314 57.463 -14.521 14.004 1.00 81.31 A C ANISOU 2271 CE1 PHE A 314 10515 8712 11668 -179 -2927 1876 A C ATOM 2272 CE2 PHE A 314 56.081 -13.423 12.380 1.00 75.64 A C ANISOU 2272 CE2 PHE A 314 9698 8070 10972 -301 -2540 1698 A C ATOM 2273 CZ PHE A 314 57.109 -14.299 12.683 1.00 82.51 A C ANISOU 2273 CZ PHE A 314 10529 8899 11922 -146 -2749 1746 A C ATOM 2274 N PHE A 315 55.670 -9.123 15.150 1.00 61.58 A N ANISOU 2274 N PHE A 315 8173 6623 8602 -898 -2408 1752 A N ATOM 2275 CA PHE A 315 56.182 -8.144 14.191 1.00 71.62 A C ANISOU 2275 CA PHE A 315 9251 8022 9939 -901 -2321 1637 A C ATOM 2276 C PHE A 315 56.807 -6.935 14.888 1.00 78.79 A C ANISOU 2276 C PHE A 315 10173 9041 10723 -1038 -2371 1629 A C ATOM 2277 O PHE A 315 57.312 -6.018 14.233 1.00 78.93 A O ANISOU 2277 O PHE A 315 10053 9164 10774 -1076 -2312 1545 A O ATOM 2278 CB PHE A 315 55.070 -7.682 13.231 1.00 68.67 A C ANISOU 2278 CB PHE A 315 8879 7632 9580 -921 -2085 1558 A C ATOM 2279 CG PHE A 315 54.392 -8.807 12.520 1.00 65.38 A C ANISOU 2279 CG PHE A 315 8454 7112 9275 -812 -2032 1555 A C ATOM 2280 CD1 PHE A 315 53.149 -9.256 12.935 1.00 65.59 A C ANISOU 2280 CD1 PHE A 315 8657 7035 9230 -864 -1956 1608 A C ATOM 2281 CD2 PHE A 315 55.011 -9.445 11.458 1.00 66.77 A C ANISOU 2281 CD2 PHE A 315 8446 7299 9623 -664 -2061 1497 A C ATOM 2282 CE1 PHE A 315 52.522 -10.314 12.288 1.00 63.64 A C ANISOU 2282 CE1 PHE A 315 8409 6688 9084 -787 -1916 1603 A C ATOM 2283 CE2 PHE A 315 54.401 -10.512 10.819 1.00 65.72 A C ANISOU 2283 CE2 PHE A 315 8326 7058 9589 -570 -2023 1486 A C ATOM 2284 CZ PHE A 315 53.148 -10.942 11.229 1.00 56.26 A C ANISOU 2284 CZ PHE A 315 7310 5747 8320 -640 -1954 1539 A C ATOM 2285 N TRP A 316 56.782 -6.938 16.216 1.00 79.17 A N ANISOU 2285 N TRP A 316 10399 9062 10619 -1124 -2481 1715 A N ATOM 2286 CA TRP A 316 57.205 -5.762 16.965 1.00 79.52 A C ANISOU 2286 CA TRP A 316 10505 9194 10517 -1277 -2519 1700 A C ATOM 2287 C TRP A 316 58.208 -6.069 18.083 1.00 79.84 A C ANISOU 2287 C TRP A 316 10567 9278 10489 -1297 -2771 1781 A C ATOM 2288 O TRP A 316 58.393 -5.284 19.014 1.00 76.36 A O ANISOU 2288 O TRP A 316 10246 8883 9884 -1439 -2828 1791 A O ATOM 2289 CB TRP A 316 55.974 -5.011 17.472 1.00 71.79 A C ANISOU 2289 CB TRP A 316 9754 8160 9365 -1400 -2351 1691 A C ATOM 2290 CG TRP A 316 55.072 -4.586 16.333 1.00 74.45 A C ANISOU 2290 CG TRP A 316 10044 8477 9768 -1373 -2119 1606 A C ATOM 2291 CD1 TRP A 316 53.875 -5.146 15.980 1.00 69.34 A C ANISOU 2291 CD1 TRP A 316 9457 7747 9141 -1321 -1980 1616 A C ATOM 2292 CD2 TRP A 316 55.314 -3.530 15.387 1.00 73.36 A C ANISOU 2292 CD2 TRP A 316 9787 8408 9679 -1399 -2008 1504 A C ATOM 2293 CE2 TRP A 316 54.217 -3.507 14.500 1.00 70.85 A C ANISOU 2293 CE2 TRP A 316 9470 8045 9406 -1344 -1811 1459 A C ATOM 2294 CE3 TRP A 316 56.346 -2.600 15.209 1.00 71.70 A C ANISOU 2294 CE3 TRP A 316 9476 8295 9473 -1475 -2059 1451 A C ATOM 2295 NE1 TRP A 316 53.355 -4.499 14.888 1.00 63.67 A N ANISOU 2295 NE1 TRP A 316 8660 7051 8480 -1301 -1799 1525 A N ATOM 2296 CZ2 TRP A 316 54.122 -2.584 13.448 1.00 68.60 A C ANISOU 2296 CZ2 TRP A 316 9100 7800 9163 -1348 -1668 1369 A C ATOM 2297 CZ3 TRP A 316 56.248 -1.681 14.163 1.00 66.89 A C ANISOU 2297 CZ3 TRP A 316 8789 7718 8908 -1496 -1907 1363 A C ATOM 2298 CH2 TRP A 316 55.146 -1.682 13.299 1.00 68.33 A C ANISOU 2298 CH2 TRP A 316 8988 7846 9129 -1425 -1716 1326 A C ATOM 2299 N SER A 317 58.863 -7.216 17.965 1.00 82.45 A N ANISOU 2299 N SER A 317 10785 9596 10945 -1145 -2929 1835 A N ATOM 2300 CA SER A 317 59.944 -7.577 18.866 1.00 86.12 A C ANISOU 2300 CA SER A 317 11225 10121 11374 -1125 -3189 1911 A C ATOM 2301 C SER A 317 61.165 -7.991 18.050 1.00 89.66 A C ANISOU 2301 C SER A 317 11370 10677 12020 -972 -3302 1869 A C ATOM 2302 O SER A 317 61.059 -8.245 16.844 1.00 82.98 A O ANISOU 2302 O SER A 317 10372 9824 11334 -864 -3179 1797 A O ATOM 2303 CB SER A 317 59.511 -8.695 19.816 1.00 88.36 A C ANISOU 2303 CB SER A 317 11720 10269 11583 -1073 -3305 2048 A C ATOM 2304 OG SER A 317 59.121 -9.854 19.105 1.00 95.48 A O ANISOU 2304 OG SER A 317 12594 11048 12637 -910 -3266 2068 A O ATOM 2305 N ASP A 318 62.324 -8.032 18.704 1.00 98.73 A N ANISOU 2305 N ASP A 318 12423 11941 13150 -963 -3533 1909 A N ATOM 2306 CA ASP A 318 63.575 -8.394 18.039 1.00 99.74 A C ANISOU 2306 CA ASP A 318 12237 12205 13453 -814 -3655 1870 A C ATOM 2307 C ASP A 318 63.652 -9.898 17.825 1.00 93.36 A C ANISOU 2307 C ASP A 318 11406 11285 12780 -564 -3753 1931 A C ATOM 2308 O ASP A 318 63.145 -10.667 18.640 1.00 91.48 A O ANISOU 2308 O ASP A 318 11398 10895 12464 -531 -3839 2043 A O ATOM 2309 CB ASP A 318 64.774 -7.928 18.864 1.00103.63 A C ANISOU 2309 CB ASP A 318 12625 12876 13874 -893 -3883 1893 A C ATOM 2310 CG ASP A 318 64.727 -6.444 19.167 1.00115.08 A C ANISOU 2310 CG ASP A 318 14133 14416 15178 -1157 -3804 1832 A C ATOM 2311 OD1 ASP A 318 64.244 -5.666 18.311 1.00117.77 A O ANISOU 2311 OD1 ASP A 318 14449 14752 15547 -1239 -3578 1738 A O ATOM 2312 OD2 ASP A 318 65.176 -6.053 20.264 1.00121.85 A O1- ANISOU 2312 OD2 ASP A 318 15072 15340 15884 -1280 -3973 1877 A O1- ATOM 2313 N PRO A 319 64.279 -10.321 16.716 1.00 87.67 A N ANISOU 2313 N PRO A 319 10422 10633 12258 -389 -3736 1855 A N ATOM 2314 CA PRO A 319 64.821 -9.421 15.694 1.00 83.99 A C ANISOU 2314 CA PRO A 319 9691 10346 11874 -442 -3611 1726 A C ATOM 2315 C PRO A 319 63.681 -8.851 14.870 1.00 86.75 A C ANISOU 2315 C PRO A 319 10136 10612 12214 -537 -3330 1653 A C ATOM 2316 O PRO A 319 62.846 -9.620 14.394 1.00 84.94 A O ANISOU 2316 O PRO A 319 10005 10225 12045 -430 -3232 1656 A O ATOM 2317 CB PRO A 319 65.642 -10.368 14.815 1.00 85.74 A C ANISOU 2317 CB PRO A 319 9650 10626 12303 -180 -3673 1683 A C ATOM 2318 CG PRO A 319 64.945 -11.691 14.962 1.00 86.00 A C ANISOU 2318 CG PRO A 319 9880 10423 12375 -8 -3710 1757 A C ATOM 2319 CD PRO A 319 64.591 -11.731 16.417 1.00 87.40 A C ANISOU 2319 CD PRO A 319 10329 10506 12372 -120 -3849 1891 A C ATOM 2320 N MET A 320 63.641 -7.535 14.706 1.00 83.51 A N ANISOU 2320 N MET A 320 9705 10299 11725 -735 -3210 1590 A N ATOM 2321 CA MET A 320 62.591 -6.913 13.913 1.00 79.57 A C ANISOU 2321 CA MET A 320 9292 9730 11210 -815 -2952 1522 A C ATOM 2322 C MET A 320 62.640 -7.415 12.474 1.00 84.71 A C ANISOU 2322 C MET A 320 9749 10396 12039 -652 -2831 1440 A C ATOM 2323 O MET A 320 63.695 -7.858 12.013 1.00 82.49 A O ANISOU 2323 O MET A 320 9221 10236 11885 -521 -2923 1409 A O ATOM 2324 CB MET A 320 62.723 -5.393 13.958 1.00 72.31 A C ANISOU 2324 CB MET A 320 8377 8913 10185 -1041 -2867 1468 A C ATOM 2325 CG MET A 320 62.379 -4.814 15.304 1.00 76.69 A C ANISOU 2325 CG MET A 320 9179 9419 10540 -1211 -2936 1528 A C ATOM 2326 SD MET A 320 60.613 -4.815 15.623 1.00 88.69 A S ANISOU 2326 SD MET A 320 11029 10732 11937 -1249 -2756 1559 A S ATOM 2327 CE MET A 320 60.061 -3.611 14.413 1.00 54.04 A C ANISOU 2327 CE MET A 320 6603 6362 7568 -1333 -2489 1443 A C ATOM 2328 N PRO A 321 61.493 -7.354 11.762 1.00 86.85 A N ANISOU 2328 N PRO A 321 10128 10556 12314 -655 -2626 1401 A N ATOM 2329 CA PRO A 321 61.384 -7.838 10.375 1.00 82.71 A C ANISOU 2329 CA PRO A 321 9456 10033 11938 -510 -2500 1319 A C ATOM 2330 C PRO A 321 62.444 -7.215 9.465 1.00 79.71 A C ANISOU 2330 C PRO A 321 8793 9856 11637 -514 -2461 1230 A C ATOM 2331 O PRO A 321 62.695 -6.013 9.556 1.00 76.43 A O ANISOU 2331 O PRO A 321 8359 9541 11140 -694 -2413 1210 A O ATOM 2332 CB PRO A 321 59.991 -7.370 9.944 1.00 67.57 A C ANISOU 2332 CB PRO A 321 7710 8008 9954 -593 -2286 1293 A C ATOM 2333 CG PRO A 321 59.237 -7.168 11.212 1.00 68.49 A C ANISOU 2333 CG PRO A 321 8087 8021 9914 -715 -2322 1380 A C ATOM 2334 CD PRO A 321 60.227 -6.774 12.253 1.00 76.30 A C ANISOU 2334 CD PRO A 321 9056 9103 10830 -799 -2502 1428 A C ATOM 2335 N SER A 322 63.047 -8.016 8.594 1.00 78.51 A N ANISOU 2335 N SER A 322 8434 9760 11636 -322 -2473 1175 A N ATOM 2336 CA SER A 322 64.084 -7.507 7.705 1.00 84.36 A C ANISOU 2336 CA SER A 322 8886 10715 12450 -321 -2427 1091 A C ATOM 2337 C SER A 322 63.822 -7.880 6.250 1.00 86.93 A C ANISOU 2337 C SER A 322 9106 11044 12880 -189 -2258 995 A C ATOM 2338 O SER A 322 63.109 -8.841 5.971 1.00 89.53 A O ANISOU 2338 O SER A 322 9540 11218 13261 -46 -2235 990 A O ATOM 2339 CB SER A 322 65.475 -7.996 8.147 1.00 83.40 A C ANISOU 2339 CB SER A 322 8539 10745 12403 -215 -2637 1108 A C ATOM 2340 OG SER A 322 65.627 -9.399 7.979 1.00 78.69 A O ANISOU 2340 OG SER A 322 7900 10070 11929 51 -2729 1109 A O ATOM 2341 N ASP A 323 64.419 -7.121 5.335 1.00 87.02 A N ANISOU 2341 N ASP A 323 8915 11235 12914 -249 -2144 919 A N ATOM 2342 CA ASP A 323 64.235 -7.325 3.903 1.00 93.05 A C ANISOU 2342 CA ASP A 323 9572 12031 13751 -146 -1972 822 A C ATOM 2343 C ASP A 323 64.788 -8.644 3.366 1.00 96.75 A C ANISOU 2343 C ASP A 323 9877 12518 14367 127 -2034 767 A C ATOM 2344 O ASP A 323 65.625 -9.287 3.996 1.00101.45 A O ANISOU 2344 O ASP A 323 10366 13157 15023 244 -2215 796 A O ATOM 2345 CB ASP A 323 64.818 -6.150 3.121 1.00 99.27 A C ANISOU 2345 CB ASP A 323 10190 13017 14510 -296 -1840 767 A C ATOM 2346 CG ASP A 323 63.936 -4.923 3.188 1.00118.78 A C ANISOU 2346 CG ASP A 323 12870 15415 16846 -520 -1711 794 A C ATOM 2347 OD1 ASP A 323 62.690 -5.087 3.209 1.00123.52 A O ANISOU 2347 OD1 ASP A 323 13697 15833 17402 -504 -1643 811 A O ATOM 2348 OD2 ASP A 323 64.485 -3.800 3.220 1.00125.60 A O1- ANISOU 2348 OD2 ASP A 323 13673 16403 17648 -711 -1681 796 A O1- ATOM 2349 N LEU A 324 64.308 -9.029 2.186 1.00 97.12 A N ANISOU 2349 N LEU A 324 9910 12528 14463 234 -1886 682 A N ATOM 2350 CA LEU A 324 64.664 -10.298 1.568 1.00 97.32 A C ANISOU 2350 CA LEU A 324 9822 12534 14619 502 -1920 611 A C ATOM 2351 C LEU A 324 65.728 -10.124 0.480 1.00108.78 A C ANISOU 2351 C LEU A 324 10961 14234 16138 580 -1832 504 A C ATOM 2352 O LEU A 324 65.711 -9.144 -0.272 1.00101.38 A O ANISOU 2352 O LEU A 324 9954 13422 15142 434 -1668 464 A O ATOM 2353 CB LEU A 324 63.415 -10.962 0.985 1.00 87.74 A C ANISOU 2353 CB LEU A 324 8812 11112 13412 574 -1823 577 A C ATOM 2354 CG LEU A 324 62.541 -11.815 1.912 1.00 82.83 A C ANISOU 2354 CG LEU A 324 8456 10234 12782 608 -1938 661 A C ATOM 2355 CD1 LEU A 324 62.327 -11.153 3.253 1.00 79.66 A C ANISOU 2355 CD1 LEU A 324 8197 9797 12272 421 -2030 785 A C ATOM 2356 CD2 LEU A 324 61.203 -12.133 1.249 1.00 79.22 A C ANISOU 2356 CD2 LEU A 324 8183 9612 12306 601 -1807 624 A C ATOM 2357 N LYS A 325 66.650 -11.086 0.411 1.00121.66 A N ANISOU 2357 N LYS A 325 12406 15932 17886 815 -1942 459 A N ATOM 2358 CA LYS A 325 67.731 -11.078 -0.578 1.00128.29 A C ANISOU 2358 CA LYS A 325 12922 17024 18797 926 -1865 350 A C ATOM 2359 C LYS A 325 68.316 -12.473 -0.840 1.00126.93 A C ANISOU 2359 C LYS A 325 12630 16833 18763 1263 -1958 277 A C ATOM 2360 O LYS A 325 68.359 -13.331 0.045 1.00120.23 A O ANISOU 2360 O LYS A 325 11879 15837 17965 1402 -2149 338 A O ATOM 2361 CB LYS A 325 68.841 -10.108 -0.161 1.00132.55 A C ANISOU 2361 CB LYS A 325 13224 17831 19309 765 -1911 383 A C ATOM 2362 CG LYS A 325 68.525 -8.654 -0.472 1.00135.97 A C ANISOU 2362 CG LYS A 325 13697 18345 19620 458 -1749 400 A C ATOM 2363 CD LYS A 325 69.614 -7.712 0.011 1.00138.05 A C ANISOU 2363 CD LYS A 325 13746 18853 19852 271 -1809 435 A C ATOM 2364 CE LYS A 325 69.196 -6.257 -0.176 1.00135.54 A C ANISOU 2364 CE LYS A 325 13538 18558 19405 -47 -1664 465 A C ATOM 2365 NZ LYS A 325 70.263 -5.302 0.243 1.00136.46 A N1+ ANISOU 2365 NZ LYS A 325 13455 18907 19485 -262 -1717 493 A N1+ TER CONECT 1275 1285 CONECT 1285 1275 1286 CONECT 1286 1285 1287 1289 CONECT 1287 1286 1288 1296 CONECT 1288 1287 CONECT 1289 1286 1290 1291 CONECT 1290 1289 CONECT 1291 1289 1292 CONECT 1292 1291 1293 1294 1295 CONECT 1293 1292 CONECT 1294 1292 CONECT 1295 1292 CONECT 1296 1287 END A second structure was input as follows:CRYST1 172.800 172.800 98.880 90.00 90.00 120.00 H 3 9 ATOM 1 N SER A 7 38.394 -6.576 -41.180 1.00125.82 A N ANISOU 1 N SER A 7 17143 19120 11540 1440 -2133 -1310 A N ATOM 2 CA SER A 7 39.010 -6.387 -39.812 1.00135.15 A C ANISOU 2 CA SER A 7 18172 20127 13051 1425 -1913 -1243 A C ATOM 3 C SER A 7 38.676 -4.996 -39.225 1.00128.71 A C ANISOU 3 C SER A 7 17172 19324 12407 1468 -1873 -978 A C ATOM 4 O SER A 7 38.372 -4.056 -39.983 1.00117.81 A O ANISOU 4 O SER A 7 15822 18079 10860 1553 -1935 -817 A O ATOM 5 CB SER A 7 40.528 -6.593 -39.841 1.00138.24 A C ANISOU 5 CB SER A 7 18692 20458 13373 1506 -1628 -1277 A C ATOM 6 OG SER A 7 41.147 -5.449 -40.416 1.00142.21 A O ANISOU 6 OG SER A 7 19245 21070 13716 1621 -1484 -1073 A O ATOM 7 N VAL A 8 38.750 -4.871 -37.891 1.00115.00 A N ANISOU 7 N VAL A 8 15266 17439 10989 1415 -1768 -935 A N ATOM 8 CA VAL A 8 38.016 -3.804 -37.186 1.00109.96 A C ANISOU 8 CA VAL A 8 14436 16789 10553 1427 -1797 -743 A C ATOM 9 C VAL A 8 38.792 -2.965 -36.141 1.00108.07 A C ANISOU 9 C VAL A 8 14126 16418 10518 1452 -1556 -596 A C ATOM 10 O VAL A 8 39.659 -3.462 -35.432 1.00 95.73 A O ANISOU 10 O VAL A 8 12568 14734 9069 1405 -1396 -670 A O ATOM 11 CB VAL A 8 36.696 -4.358 -36.569 1.00106.89 A C ANISOU 11 CB VAL A 8 13862 16388 10361 1314 -2005 -822 A C ATOM 12 CG1 VAL A 8 36.989 -5.416 -35.497 1.00 96.17 A C ANISOU 12 CG1 VAL A 8 12457 14862 9220 1189 -1930 -981 A C ATOM 13 CG2 VAL A 8 35.819 -3.220 -36.041 1.00101.76 A C ANISOU 13 CG2 VAL A 8 13020 15764 9879 1366 -2047 -622 A C ATOM 14 N GLU A 9 38.441 -1.679 -36.077 1.00113.76 A N ANISOU 14 N GLU A 9 14787 17159 11275 1529 -1545 -385 A N ATOM 15 CA GLU A 9 38.931 -0.708 -35.085 1.00107.24 A C ANISOU 15 CA GLU A 9 13899 16201 10644 1544 -1357 -232 A C ATOM 16 C GLU A 9 39.120 -1.313 -33.721 1.00 94.03 A C ANISOU 16 C GLU A 9 12114 14377 9236 1437 -1272 -332 A C ATOM 17 O GLU A 9 38.218 -1.939 -33.201 1.00 99.20 A O ANISOU 17 O GLU A 9 12645 15015 10029 1369 -1398 -427 A O ATOM 18 CB GLU A 9 37.906 0.434 -34.943 1.00128.06 A C ANISOU 18 CB GLU A 9 16437 18854 13363 1623 -1445 -52 A C ATOM 19 CG GLU A 9 37.750 1.349 -36.152 1.00138.17 A C ANISOU 19 CG GLU A 9 17831 20259 14406 1750 -1509 112 A C ATOM 20 CD GLU A 9 39.037 2.089 -36.453 1.00140.76 A C ANISOU 20 CD GLU A 9 18320 20543 14619 1783 -1293 239 A C ATOM 21 OE1 GLU A 9 39.997 2.000 -35.633 1.00130.14 A O ANISOU 21 OE1 GLU A 9 16970 19072 13405 1710 -1100 211 A O ATOM 22 OE2 GLU A 9 39.078 2.760 -37.512 1.00145.69 A O1- ANISOU 22 OE2 GLU A 9 19070 21268 15017 1875 -1322 376 A O1- ATOM 23 N CYS A 10 40.271 -1.113 -33.118 1.00 91.01 A N ANISOU 23 N CYS A 10 11765 13889 8924 1414 -1064 -299 A N ATOM 24 CA CYS A 10 40.490 -1.732 -31.819 1.00 86.76 A C ANISOU 24 CA CYS A 10 11132 13213 8619 1314 -994 -390 A C ATOM 25 C CYS A 10 41.536 -1.039 -30.944 1.00 83.67 A C ANISOU 25 C CYS A 10 10739 12704 8345 1291 -785 -285 A C ATOM 26 O CYS A 10 42.496 -1.666 -30.505 1.00 91.69 A O ANISOU 26 O CYS A 10 11767 13664 9404 1239 -676 -358 A O ATOM 27 CB CYS A 10 40.839 -3.205 -31.981 1.00 92.50 A C ANISOU 27 CB CYS A 10 11905 13936 9302 1257 -1024 -597 A C ATOM 28 SG CYS A 10 40.605 -4.068 -30.429 1.00107.68 A S ANISOU 28 SG CYS A 10 13699 15699 11514 1128 -1015 -703 A S ATOM 29 N PRO A 11 41.318 0.249 -30.661 1.00 75.82 A N ANISOU 29 N PRO A 11 9732 11668 7408 1329 -741 -114 A N ATOM 30 CA PRO A 11 42.223 1.167 -29.979 1.00 64.02 A C ANISOU 30 CA PRO A 11 8264 10064 5995 1299 -564 11 A C ATOM 31 C PRO A 11 42.768 0.657 -28.661 1.00 77.75 A C ANISOU 31 C PRO A 11 9933 11682 7926 1190 -474 -64 A C ATOM 32 O PRO A 11 43.877 1.035 -28.294 1.00 88.42 A O ANISOU 32 O PRO A 11 11316 12979 9297 1142 -331 0 A O ATOM 33 CB PRO A 11 41.319 2.380 -29.675 1.00 65.56 A C ANISOU 33 CB PRO A 11 8436 10200 6272 1359 -598 152 A C ATOM 34 CG PRO A 11 40.256 2.326 -30.701 1.00 79.26 A C ANISOU 34 CG PRO A 11 10164 12070 7880 1458 -774 157 A C ATOM 35 CD PRO A 11 40.016 0.872 -30.964 1.00 88.83 A C ANISOU 35 CD PRO A 11 11330 13367 9055 1405 -885 -37 A C ATOM 36 N PHE A 12 41.980 -0.150 -27.941 1.00 83.31 A N ANISOU 36 N PHE A 12 10538 12348 8768 1143 -562 -183 A N ATOM 37 CA PHE A 12 42.318 -0.422 -26.542 1.00 72.29 A C ANISOU 37 CA PHE A 12 9080 10824 7563 1044 -483 -221 A C ATOM 38 C PHE A 12 42.659 -1.874 -26.304 1.00 73.19 A C ANISOU 38 C PHE A 12 9170 10930 7707 981 -505 -381 A C ATOM 39 O PHE A 12 42.648 -2.344 -25.158 1.00 77.53 A O ANISOU 39 O PHE A 12 9659 11384 8414 898 -483 -431 A O ATOM 40 CB PHE A 12 41.188 0.013 -25.612 1.00 65.36 A C ANISOU 40 CB PHE A 12 8111 9875 6846 1033 -523 -196 A C ATOM 41 CG PHE A 12 40.797 1.448 -25.778 1.00 66.86 A C ANISOU 41 CG PHE A 12 8338 10044 7022 1119 -498 -41 A C ATOM 42 CD1 PHE A 12 41.748 2.438 -25.744 1.00 57.80 A C ANISOU 42 CD1 PHE A 12 7293 8827 5839 1114 -372 77 A C ATOM 43 CD2 PHE A 12 39.471 1.801 -25.996 1.00 76.76 A C ANISOU 43 CD2 PHE A 12 9520 11344 8299 1206 -606 -9 A C ATOM 44 CE1 PHE A 12 41.394 3.768 -25.909 1.00 63.51 A C ANISOU 44 CE1 PHE A 12 8080 9500 6549 1194 -348 223 A C ATOM 45 CE2 PHE A 12 39.113 3.125 -26.142 1.00 63.24 A C ANISOU 45 CE2 PHE A 12 7854 9595 6579 1312 -579 139 A C ATOM 46 CZ PHE A 12 40.072 4.107 -26.111 1.00 61.83 A C ANISOU 46 CZ PHE A 12 7810 9319 6361 1307 -450 254 A C ATOM 47 N CYS A 13 42.879 -2.611 -27.377 1.00 66.59 A N ANISOU 47 N CYS A 13 8396 10188 6715 1026 -555 -465 A N ATOM 48 CA CYS A 13 43.242 -4.010 -27.222 1.00 64.82 A C ANISOU 48 CA CYS A 13 8182 9934 6513 985 -572 -622 A C ATOM 49 C CYS A 13 44.344 -4.315 -28.212 1.00 70.36 A C ANISOU 49 C CYS A 13 8984 10714 7035 1058 -495 -649 A C ATOM 50 O CYS A 13 44.089 -4.533 -29.417 1.00 80.10 A O ANISOU 50 O CYS A 13 10300 12052 8083 1126 -566 -699 A O ATOM 51 CB CYS A 13 42.047 -4.925 -27.446 1.00 74.71 A C ANISOU 51 CB CYS A 13 9408 11201 7776 952 -747 -753 A C ATOM 52 SG CYS A 13 42.330 -6.609 -26.876 1.00 70.35 A S ANISOU 52 SG CYS A 13 8874 10539 7313 872 -770 -935 A S ATOM 53 N ASP A 14 45.575 -4.349 -27.708 1.00 66.67 A N ANISOU 53 N ASP A 14 8507 10209 6616 1046 -350 -615 A N ATOM 54 CA ASP A 14 46.758 -4.549 -28.544 1.00 62.83 A C ANISOU 54 CA ASP A 14 8086 9811 5975 1125 -237 -616 A C ATOM 55 C ASP A 14 46.949 -6.023 -28.874 1.00 65.57 A C ANISOU 55 C ASP A 14 8490 10145 6275 1170 -270 -802 A C ATOM 56 O ASP A 14 46.563 -6.913 -28.099 1.00 74.97 A O ANISOU 56 O ASP A 14 9656 11223 7607 1113 -341 -905 A O ATOM 57 CB ASP A 14 48.021 -4.033 -27.851 1.00 72.51 A C ANISOU 57 CB ASP A 14 9248 11018 7282 1091 -74 -500 A C ATOM 58 CG ASP A 14 48.103 -2.521 -27.774 1.00 85.61 A C ANISOU 58 CG ASP A 14 10896 12690 8941 1051 -15 -313 A C ATOM 59 OD1 ASP A 14 47.096 -1.820 -28.042 1.00 82.73 A O ANISOU 59 OD1 ASP A 14 10563 12322 8549 1059 -99 -264 A O ATOM 60 OD2 ASP A 14 49.196 -2.051 -27.390 1.00 89.93 A O1- ANISOU 60 OD2 ASP A 14 11401 13241 9525 1007 111 -213 A O1- ATOM 61 N GLU A 15 47.550 -6.285 -30.032 1.00 75.68 A N ANISOU 61 N GLU A 15 9867 11534 7351 1276 -211 -844 A N ATOM 62 CA GLU A 15 47.935 -7.653 -30.391 1.00 74.40 A C ANISOU 62 CA GLU A 15 9789 11348 7130 1346 -208 -1023 A C ATOM 63 C GLU A 15 49.129 -8.101 -29.548 1.00 68.84 A C ANISOU 63 C GLU A 15 9010 10583 6560 1364 -70 -1009 A C ATOM 64 O GLU A 15 50.077 -7.342 -29.361 1.00 63.97 A O ANISOU 64 O GLU A 15 8311 10033 5959 1371 70 -865 A O ATOM 65 CB GLU A 15 48.262 -7.719 -31.882 1.00 69.86 A C ANISOU 65 CB GLU A 15 9349 10917 6275 1469 -164 -1069 A C ATOM 66 CG GLU A 15 47.384 -6.794 -32.715 1.00 81.56 A C ANISOU 66 CG GLU A 15 10877 12505 7607 1459 -262 -990 A C ATOM 67 CD GLU A 15 47.478 -7.047 -34.203 1.00114.05 A C ANISOU 67 CD GLU A 15 15157 16756 11420 1568 -262 -1067 A C ATOM 68 OE1 GLU A 15 47.995 -8.099 -34.636 1.00123.49 A O ANISOU 68 OE1 GLU A 15 16455 17945 12518 1649 -215 -1227 A O ATOM 69 OE2 GLU A 15 46.982 -6.184 -34.968 1.00134.24 A O1- ANISOU 69 OE2 GLU A 15 17758 19424 13824 1579 -316 -968 A O1- ATOM 70 N VAL A 16 49.059 -9.328 -29.038 1.00 65.40 A N ANISOU 70 N VAL A 16 8603 10020 6225 1364 -122 -1151 A N ATOM 71 CA VAL A 16 50.074 -9.841 -28.102 1.00 63.80 A C ANISOU 71 CA VAL A 16 8322 9744 6174 1384 -22 -1133 A C ATOM 72 C VAL A 16 51.457 -9.969 -28.778 1.00 63.96 A C ANISOU 72 C VAL A 16 8344 9883 6074 1539 157 -1115 A C ATOM 73 O VAL A 16 52.493 -10.080 -28.123 1.00 67.20 A O ANISOU 73 O VAL A 16 8646 10293 6591 1569 264 -1046 A O ATOM 74 CB VAL A 16 49.624 -11.189 -27.481 1.00 63.66 A C ANISOU 74 CB VAL A 16 8364 9546 6278 1358 -127 -1286 A C ATOM 75 CG1 VAL A 16 49.792 -12.318 -28.470 1.00 60.80 A C ANISOU 75 CG1 VAL A 16 8169 9163 5766 1489 -129 -1470 A C ATOM 76 CG2 VAL A 16 50.354 -11.471 -26.190 1.00 59.33 A C ANISOU 76 CG2 VAL A 16 7710 8905 5927 1332 -70 -1220 A C ATOM 77 N SER A 17 51.466 -9.911 -30.107 1.00 62.51 A N ANISOU 77 N SER A 17 8272 9819 5659 1638 192 -1166 A N ATOM 78 CA SER A 17 52.719 -9.929 -30.870 1.00 63.46 A C ANISOU 78 CA SER A 17 8390 10084 5637 1791 386 -1139 A C ATOM 79 C SER A 17 53.632 -8.751 -30.527 1.00 63.45 A C ANISOU 79 C SER A 17 8215 10205 5688 1743 528 -914 A C ATOM 80 O SER A 17 54.795 -8.741 -30.899 1.00 61.09 A O ANISOU 80 O SER A 17 7853 10034 5323 1847 704 -859 A O ATOM 81 CB SER A 17 52.411 -9.927 -32.360 1.00 68.67 A C ANISOU 81 CB SER A 17 9218 10859 6012 1882 388 -1222 A C ATOM 82 OG SER A 17 51.749 -8.722 -32.707 1.00 72.87 A O ANISOU 82 OG SER A 17 9742 11474 6469 1786 329 -1094 A O ATOM 83 N LYS A 18 53.125 -7.743 -29.824 1.00 64.90 A N ANISOU 83 N LYS A 18 8321 10352 5986 1583 459 -782 A N ATOM 84 CA LYS A 18 53.972 -6.651 -29.346 1.00 63.84 A C ANISOU 84 CA LYS A 18 8036 10294 5922 1503 573 -576 A C ATOM 85 C LYS A 18 55.014 -7.188 -28.369 1.00 67.79 A C ANISOU 85 C LYS A 18 8393 10768 6593 1513 644 -553 A C ATOM 86 O LYS A 18 56.070 -6.560 -28.152 1.00 73.09 A O ANISOU 86 O LYS A 18 8924 11547 7299 1480 769 -401 A O ATOM 87 CB LYS A 18 53.138 -5.559 -28.649 1.00 59.58 A C ANISOU 87 CB LYS A 18 7474 9675 5488 1335 472 -467 A C ATOM 88 CG LYS A 18 52.543 -6.025 -27.325 1.00 67.36 A C ANISOU 88 CG LYS A 18 8420 10486 6687 1244 350 -525 A C ATOM 89 CD LYS A 18 51.527 -5.026 -26.791 1.00 72.37 A C ANISOU 89 CD LYS A 18 9059 11043 7395 1114 254 -449 A C ATOM 90 CE LYS A 18 52.185 -3.767 -26.246 1.00 70.40 A C ANISOU 90 CE LYS A 18 8728 10813 7205 1007 340 -263 A C ATOM 91 NZ LYS A 18 51.165 -3.005 -25.444 1.00 71.81 A N1+ ANISOU 91 NZ LYS A 18 8922 10869 7491 897 245 -221 A N1+ ATOM 92 N TYR A 19 54.685 -8.330 -27.762 1.00 63.43 A N ANISOU 92 N TYR A 19 7875 10072 6151 1546 553 -693 A N ATOM 93 CA TYR A 19 55.574 -9.022 -26.857 1.00 64.58 A C ANISOU 93 CA TYR A 19 7908 10177 6451 1583 595 -683 A C ATOM 94 C TYR A 19 56.236 -10.155 -27.605 1.00 69.91 A C ANISOU 94 C TYR A 19 8637 10892 7033 1801 690 -807 A C ATOM 95 O TYR A 19 55.648 -10.753 -28.487 1.00 81.52 A O ANISOU 95 O TYR A 19 10279 12330 8362 1890 655 -962 A O ATOM 96 CB TYR A 19 54.824 -9.531 -25.617 1.00 62.04 A C ANISOU 96 CB TYR A 19 7598 9656 6316 1479 442 -736 A C ATOM 97 CG TYR A 19 54.187 -8.416 -24.826 1.00 60.42 A C ANISOU 97 CG TYR A 19 7346 9409 6199 1283 369 -623 A C ATOM 98 CD1 TYR A 19 54.952 -7.627 -23.983 1.00 61.86 A C ANISOU 98 CD1 TYR A 19 7389 9634 6482 1181 419 -464 A C ATOM 99 CD2 TYR A 19 52.833 -8.113 -24.957 1.00 65.47 A C ANISOU 99 CD2 TYR A 19 8084 9976 6816 1206 250 -674 A C ATOM 100 CE1 TYR A 19 54.390 -6.575 -23.277 1.00 62.34 A C ANISOU 100 CE1 TYR A 19 7436 9639 6609 1011 363 -373 A C ATOM 101 CE2 TYR A 19 52.255 -7.062 -24.245 1.00 66.41 A C ANISOU 101 CE2 TYR A 19 8165 10054 7013 1056 202 -572 A C ATOM 102 CZ TYR A 19 53.037 -6.328 -23.375 1.00 60.80 A C ANISOU 102 CZ TYR A 19 7344 9359 6397 962 261 -431 A C ATOM 103 OH TYR A 19 52.481 -5.287 -22.677 1.00 66.18 A O ANISOU 103 OH TYR A 19 8019 9980 7143 823 222 -345 A O ATOM 104 N GLU A 20 57.481 -10.428 -27.257 1.00 77.71 A N ANISOU 104 N GLU A 20 9476 11955 8092 1889 810 -737 A N ATOM 105 CA GLU A 20 58.200 -11.512 -27.869 1.00 85.30 A C ANISOU 105 CA GLU A 20 10475 12949 8983 2126 920 -847 A C ATOM 106 C GLU A 20 58.358 -12.639 -26.874 1.00 79.74 A C ANISOU 106 C GLU A 20 9761 12074 8460 2186 850 -912 A C ATOM 107 O GLU A 20 58.961 -12.459 -25.816 1.00 76.52 A O ANISOU 107 O GLU A 20 9179 11674 8220 2122 844 -782 A O ATOM 108 CB GLU A 20 59.552 -10.990 -28.339 1.00 98.00 A C ANISOU 108 CB GLU A 20 11903 14802 10528 2215 1130 -704 A C ATOM 109 CG GLU A 20 60.321 -11.969 -29.195 1.00123.16 A C ANISOU 109 CG GLU A 20 15130 18064 13600 2493 1288 -813 A C ATOM 110 CD GLU A 20 61.519 -11.296 -29.836 1.00145.84 A C ANISOU 110 CD GLU A 20 17819 21216 16376 2563 1513 -661 A C ATOM 111 OE1 GLU A 20 61.883 -10.180 -29.377 1.00142.67 A O ANISOU 111 OE1 GLU A 20 17234 20923 16048 2379 1528 -459 A O ATOM 112 OE2 GLU A 20 62.068 -11.866 -30.807 1.00153.21 A O1- ANISOU 112 OE2 GLU A 20 18803 22255 17153 2792 1678 -744 A O1- ATOM 113 N LYS A 21 57.795 -13.798 -27.179 1.00 77.37 A N ANISOU 113 N LYS A 21 9661 11609 8124 2294 785 -1109 A N ATOM 114 CA LYS A 21 57.936 -14.945 -26.270 1.00 74.13 A C ANISOU 114 CA LYS A 21 9273 11010 7882 2360 720 -1169 A C ATOM 115 C LYS A 21 59.372 -15.412 -26.063 1.00 75.39 A C ANISOU 115 C LYS A 21 9276 11260 8108 2566 867 -1097 A C ATOM 116 O LYS A 21 60.175 -15.538 -26.983 1.00 74.11 A O ANISOU 116 O LYS A 21 9089 11247 7820 2765 1038 -1117 A O ATOM 117 CB LYS A 21 57.007 -16.084 -26.644 1.00 72.29 A C ANISOU 117 CB LYS A 21 9307 10558 7600 2410 613 -1394 A C ATOM 118 CG LYS A 21 55.562 -15.847 -26.250 1.00 73.85 A C ANISOU 118 CG LYS A 21 9598 10622 7840 2172 419 -1433 A C ATOM 119 CD LYS A 21 54.649 -16.821 -26.939 1.00 82.01 A C ANISOU 119 CD LYS A 21 10891 11491 8776 2201 320 -1656 A C ATOM 120 CE LYS A 21 53.186 -16.462 -26.688 1.00 84.24 A C ANISOU 120 CE LYS A 21 11225 11694 9085 1960 135 -1679 A C ATOM 121 NZ LYS A 21 52.258 -17.375 -27.410 1.00 92.99 A N1+ ANISOU 121 NZ LYS A 21 12577 12661 10093 1954 18 -1895 A N1+ ATOM 122 N LEU A 22 59.756 -15.554 -24.804 1.00 80.29 A N ANISOU 122 N LEU A 22 9758 11820 8926 2512 807 -987 A N ATOM 123 CA LEU A 22 61.087 -16.058 -24.452 1.00 83.43 A C ANISOU 123 CA LEU A 22 9982 12299 9416 2708 914 -902 A C ATOM 124 C LEU A 22 61.052 -17.519 -24.014 1.00 94.89 A C ANISOU 124 C LEU A 22 11575 13512 10965 2874 853 -1020 A C ATOM 125 O LEU A 22 61.830 -18.323 -24.513 1.00 98.36 A O ANISOU 125 O LEU A 22 12028 13968 11375 3151 977 -1080 A O ATOM 126 CB LEU A 22 61.724 -15.222 -23.348 1.00 76.77 A C ANISOU 126 CB LEU A 22 8872 11577 8719 2550 886 -678 A C ATOM 127 CG LEU A 22 61.955 -13.756 -23.669 1.00 70.51 A C ANISOU 127 CG LEU A 22 7925 11010 7853 2381 955 -534 A C ATOM 128 CD1 LEU A 22 62.295 -12.981 -22.417 1.00 74.18 A C ANISOU 128 CD1 LEU A 22 8196 11522 8467 2168 871 -347 A C ATOM 129 CD2 LEU A 22 63.017 -13.631 -24.721 1.00 65.27 A C ANISOU 129 CD2 LEU A 22 7138 10588 7073 2570 1170 -496 A C ATOM 130 N ALA A 23 60.142 -17.864 -23.096 1.00 94.03 A N ANISOU 130 N ALA A 23 11581 13177 10969 2711 673 -1050 A N ATOM 131 CA ALA A 23 60.132 -19.206 -22.525 1.00 82.68 A C ANISOU 131 CA ALA A 23 10275 11494 9643 2839 604 -1127 A C ATOM 132 C ALA A 23 58.846 -19.524 -21.765 1.00 84.32 A C ANISOU 132 C ALA A 23 10655 11453 9930 2617 411 -1185 A C ATOM 133 O ALA A 23 58.353 -18.679 -21.031 1.00105.75 A O ANISOU 133 O ALA A 23 13277 14205 12699 2374 325 -1079 A O ATOM 134 CB ALA A 23 61.325 -19.375 -21.610 1.00 79.90 A C ANISOU 134 CB ALA A 23 9698 11218 9441 2950 636 -954 A C ATOM 135 N LYS A 24 58.330 -20.741 -21.939 1.00 79.13 A N ANISOU 135 N LYS A 24 10248 10540 9277 2702 353 -1352 A N ATOM 136 CA LYS A 24 57.263 -21.242 -21.069 1.00 78.08 A C ANISOU 136 CA LYS A 24 10259 10158 9249 2506 179 -1384 A C ATOM 137 C LYS A 24 57.764 -21.310 -19.646 1.00 85.83 A C ANISOU 137 C LYS A 24 11099 11107 10404 2464 125 -1203 A C ATOM 138 O LYS A 24 58.921 -21.656 -19.423 1.00103.34 A O ANISOU 138 O LYS A 24 13204 13380 12679 2674 200 -1119 A O ATOM 139 CB LYS A 24 56.793 -22.634 -21.493 1.00 77.35 A C ANISOU 139 CB LYS A 24 10467 9780 9140 2614 132 -1585 A C ATOM 140 CG LYS A 24 55.587 -22.648 -22.397 1.00102.03 A C ANISOU 140 CG LYS A 24 13793 12839 12135 2480 61 -1769 A C ATOM 141 CD LYS A 24 54.997 -24.053 -22.547 1.00127.16 A C ANISOU 141 CD LYS A 24 17285 15695 15334 2511 -27 -1955 A C ATOM 142 CE LYS A 24 53.600 -23.998 -23.151 1.00134.74 A C ANISOU 142 CE LYS A 24 18406 16589 16197 2288 -153 -2106 A C ATOM 143 NZ LYS A 24 53.113 -25.316 -23.647 1.00149.03 A N1+ ANISOU 143 NZ LYS A 24 20543 18108 17972 2328 -226 -2323 A N1+ ATOM 144 N ILE A 25 56.922 -20.974 -18.680 1.00 90.97 A N ANISOU 144 N ILE A 25 11745 11685 11132 2203 0 -1137 A N ATOM 145 CA ILE A 25 57.286 -21.099 -17.282 1.00 99.13 A C ANISOU 145 CA ILE A 25 12685 12671 12309 2144 -67 -974 A C ATOM 146 C ILE A 25 56.131 -21.678 -16.458 1.00117.39 A C ANISOU 146 C ILE A 25 15169 14735 14697 1946 -208 -1005 A C ATOM 147 O ILE A 25 56.195 -21.616 -15.238 1.00123.87 A O ANISOU 147 O ILE A 25 15926 15526 15613 1838 -274 -866 A O ATOM 148 CB ILE A 25 57.742 -19.756 -16.671 1.00 92.71 A C ANISOU 148 CB ILE A 25 11614 12102 11507 2005 -52 -792 A C ATOM 149 CG1 ILE A 25 56.591 -18.760 -16.620 1.00 88.50 A C ANISOU 149 CG1 ILE A 25 11093 11604 10926 1734 -104 -807 A C ATOM 150 CG2 ILE A 25 58.895 -19.175 -17.478 1.00103.89 A C ANISOU 150 CG2 ILE A 25 12844 13773 12854 2173 91 -744 A C ATOM 151 CD1 ILE A 25 56.988 -17.350 -16.231 1.00 81.72 A C ANISOU 151 CD1 ILE A 25 10024 10968 10055 1600 -75 -657 A C ATOM 152 N GLY A 26 55.036 -22.117 -17.091 1.00125.10 A N ANISOU 152 N GLY A 26 16346 15561 15622 1867 -256 -1174 A N ATOM 153 CA GLY A 26 53.916 -22.722 -16.358 1.00134.95 A C ANISOU 153 CA GLY A 26 17746 16579 16946 1665 -382 -1201 A C ATOM 154 C GLY A 26 53.329 -23.923 -17.060 1.00151.08 A C ANISOU 154 C GLY A 26 20059 18375 18969 1713 -426 -1392 A C ATOM 155 O GLY A 26 52.218 -23.865 -17.529 1.00155.71 A O ANISOU 155 O GLY A 26 20738 18919 19506 1547 -489 -1505 A O ATOM 156 N GLN A 27 54.065 -25.021 -17.156 1.00165.23 A N ANISOU 156 N GLN A 27 21983 19997 20797 1943 -399 -1432 A N ATOM 157 CA GLN A 27 53.571 -26.180 -17.949 1.00160.27 A C ANISOU 157 CA GLN A 27 21650 19111 20131 2003 -435 -1641 A C ATOM 158 C GLN A 27 52.355 -26.837 -17.300 1.00148.11 A C ANISOU 158 C GLN A 27 20281 17318 18675 1740 -577 -1668 A C ATOM 159 O GLN A 27 51.359 -27.119 -17.963 1.00136.07 A O ANISOU 159 O GLN A 27 18912 15695 17093 1601 -647 -1827 A O ATOM 160 CB GLN A 27 54.661 -27.232 -18.209 1.00162.79 A C ANISOU 160 CB GLN A 27 22096 19281 20472 2338 -360 -1684 A C ATOM 161 CG GLN A 27 55.721 -26.835 -19.226 1.00164.75 A C ANISOU 161 CG GLN A 27 22237 19752 20608 2621 -201 -1724 A C ATOM 162 CD GLN A 27 56.828 -25.970 -18.625 1.00171.38 A C ANISOU 162 CD GLN A 27 22751 20867 21498 2710 -119 -1505 A C ATOM 163 NE2 GLN A 27 57.039 -24.796 -19.219 1.00165.05 A N ANISOU 163 NE2 GLN A 27 21752 20366 20592 2682 -36 -1477 A N ATOM 164 OE1 GLN A 27 57.486 -26.347 -17.640 1.00167.13 A O ANISOU 164 OE1 GLN A 27 22143 20272 21086 2794 -138 -1356 A O ATOM 165 N GLY A 28 52.436 -27.047 -15.992 1.00149.70 A N ANISOU 165 N GLY A 28 20442 17432 19005 1660 -623 -1501 A N ATOM 166 CA GLY A 28 51.406 -27.776 -15.269 1.00161.47 A C ANISOU 166 CA GLY A 28 22096 18672 20584 1423 -739 -1499 A C ATOM 167 C GLY A 28 50.621 -26.971 -14.261 1.00174.15 A C ANISOU 167 C GLY A 28 23540 20395 22234 1134 -786 -1357 A C ATOM 168 O GLY A 28 49.679 -27.503 -13.675 1.00157.54 A O ANISOU 168 O GLY A 28 21548 18113 20196 913 -870 -1348 A O ATOM 169 N THR A 29 50.975 -25.694 -14.074 1.00195.92 A N ANISOU 169 N THR A 29 26044 23444 24951 1127 -727 -1252 A N ATOM 170 CA THR A 29 50.219 -24.818 -13.159 1.00188.85 A C ANISOU 170 CA THR A 29 25002 22670 24080 869 -755 -1134 A C ATOM 171 C THR A 29 49.159 -24.009 -13.900 1.00187.16 A C ANISOU 171 C THR A 29 24721 22597 23792 708 -766 -1233 A C ATOM 172 O THR A 29 49.446 -22.992 -14.560 1.00165.39 A O ANISOU 172 O THR A 29 21823 20067 20949 775 -705 -1245 A O ATOM 173 CB THR A 29 51.128 -23.874 -12.361 1.00162.34 A C ANISOU 173 CB THR A 29 21430 19521 20727 920 -700 -954 A C ATOM 174 CG2 THR A 29 52.199 -24.686 -11.567 1.00130.27 A C ANISOU 174 CG2 THR A 29 17414 15339 16742 1086 -709 -833 A C ATOM 175 OG1 THR A 29 51.713 -22.914 -13.262 1.00138.82 A O ANISOU 175 OG1 THR A 29 18303 16782 17659 1043 -620 -986 A O ATOM 176 N PHE A 30 47.928 -24.509 -13.810 1.00198.71 A N ANISOU 176 N PHE A 30 26289 23920 25291 493 -848 -1296 A N ATOM 177 CA PHE A 30 46.790 -23.926 -14.490 1.00205.91 A C ANISOU 177 CA PHE A 30 27145 24944 26147 332 -884 -1388 A C ATOM 178 C PHE A 30 47.104 -23.801 -15.977 1.00199.19 A C ANISOU 178 C PHE A 30 26334 24173 25173 498 -866 -1544 A C ATOM 179 O PHE A 30 47.629 -24.745 -16.589 1.00205.23 A O ANISOU 179 O PHE A 30 27281 24781 25914 656 -869 -1656 A O ATOM 180 CB PHE A 30 46.443 -22.581 -13.848 1.00212.08 A C ANISOU 180 CB PHE A 30 27701 25954 26926 213 -842 -1261 A C ATOM 181 CG PHE A 30 46.038 -22.686 -12.400 1.00210.06 A C ANISOU 181 CG PHE A 30 27419 25630 26763 40 -851 -1119 A C ATOM 182 CD1 PHE A 30 46.833 -23.400 -11.483 1.00192.20 A C ANISOU 182 CD1 PHE A 30 25240 23223 24563 106 -847 -1017 A C ATOM 183 CD2 PHE A 30 44.868 -22.067 -11.944 1.00195.16 A C ANISOU 183 CD2 PHE A 30 25423 23832 24894 -176 -859 -1080 A C ATOM 184 CE1 PHE A 30 46.457 -23.510 -10.167 1.00155.65 A C ANISOU 184 CE1 PHE A 30 20606 18536 19997 -55 -855 -882 A C ATOM 185 CE2 PHE A 30 44.491 -22.167 -10.615 1.00179.59 A C ANISOU 185 CE2 PHE A 30 23436 21808 22989 -332 -849 -951 A C ATOM 186 CZ PHE A 30 45.292 -22.890 -9.729 1.00171.34 A C ANISOU 186 CZ PHE A 30 22494 20617 21990 -278 -848 -852 A C ATOM 187 N GLY A 31 46.803 -22.640 -16.552 1.00183.80 A N ANISOU 187 N GLY A 31 24233 22463 23140 475 -841 -1550 A N ATOM 188 CA GLY A 31 47.038 -22.403 -17.973 1.00165.10 A C ANISOU 188 CA GLY A 31 21898 20200 20630 617 -820 -1682 A C ATOM 189 C GLY A 31 48.513 -22.234 -18.289 1.00139.73 A C ANISOU 189 C GLY A 31 18656 17069 17365 886 -701 -1650 A C ATOM 190 O GLY A 31 49.319 -22.001 -17.395 1.00141.69 A O ANISOU 190 O GLY A 31 18801 17350 17685 944 -641 -1505 A O ATOM 191 N GLU A 32 48.867 -22.337 -19.562 1.00128.32 A N ANISOU 191 N GLU A 32 17293 15673 15787 1047 -665 -1782 A N ATOM 192 CA GLU A 32 50.228 -22.060 -19.990 1.00123.48 A C ANISOU 192 CA GLU A 32 16618 15186 15110 1303 -531 -1748 A C ATOM 193 C GLU A 32 50.606 -20.617 -19.688 1.00102.13 A C ANISOU 193 C GLU A 32 13667 12742 12394 1275 -457 -1585 A C ATOM 194 O GLU A 32 49.868 -19.680 -19.995 1.00 88.12 A O ANISOU 194 O GLU A 32 11812 11105 10561 1147 -482 -1574 A O ATOM 195 CB GLU A 32 50.381 -22.266 -21.491 1.00140.34 A C ANISOU 195 CB GLU A 32 18884 17365 17074 1456 -495 -1922 A C ATOM 196 CG GLU A 32 49.350 -23.134 -22.185 1.00133.73 A C ANISOU 196 CG GLU A 32 18281 16352 16177 1360 -619 -2122 A C ATOM 197 CD GLU A 32 48.985 -22.537 -23.525 1.00146.81 A C ANISOU 197 CD GLU A 32 19959 18184 17638 1375 -623 -2230 A C ATOM 198 OE1 GLU A 32 48.421 -21.420 -23.526 1.00172.54 A O ANISOU 198 OE1 GLU A 32 23050 21634 20872 1243 -647 -2142 A O ATOM 199 OE2 GLU A 32 49.293 -23.145 -24.576 1.00149.93 A O1- ANISOU 199 OE2 GLU A 32 20543 18530 17893 1531 -596 -2397 A O1- ATOM 200 N VAL A 33 51.785 -20.462 -19.107 1.00 93.20 A N ANISOU 200 N VAL A 33 12420 11672 11317 1402 -370 -1457 A N ATOM 201 CA VAL A 33 52.328 -19.147 -18.759 1.00 75.52 A C ANISOU 201 CA VAL A 33 9958 9663 9073 1373 -299 -1296 A C ATOM 202 C VAL A 33 53.664 -18.942 -19.477 1.00 77.51 A C ANISOU 202 C VAL A 33 10127 10072 9249 1606 -164 -1272 A C ATOM 203 O VAL A 33 54.522 -19.818 -19.420 1.00 89.96 A O ANISOU 203 O VAL A 33 11743 11573 10864 1794 -121 -1283 A O ATOM 204 CB VAL A 33 52.557 -19.072 -17.244 1.00 66.83 A C ANISOU 204 CB VAL A 33 8763 8516 8110 1273 -331 -1137 A C ATOM 205 CG1 VAL A 33 52.952 -17.688 -16.808 1.00 68.01 A C ANISOU 205 CG1 VAL A 33 8712 8874 8252 1195 -282 -987 A C ATOM 206 CG2 VAL A 33 51.283 -19.497 -16.531 1.00 64.71 A C ANISOU 206 CG2 VAL A 33 8593 8076 7917 1063 -444 -1165 A C ATOM 207 N PHE A 34 53.827 -17.804 -20.147 1.00 71.01 A N ANISOU 207 N PHE A 34 9192 9467 8322 1598 -93 -1232 A N ATOM 208 CA PHE A 34 55.078 -17.483 -20.860 1.00 65.66 A C ANISOU 208 CA PHE A 34 8409 8974 7563 1795 52 -1190 A C ATOM 209 C PHE A 34 55.808 -16.282 -20.285 1.00 66.87 A C ANISOU 209 C PHE A 34 8330 9322 7753 1722 110 -995 A C ATOM 210 O PHE A 34 55.176 -15.304 -19.877 1.00 77.25 A O ANISOU 210 O PHE A 34 9592 10680 9078 1525 61 -926 A O ATOM 211 CB PHE A 34 54.770 -17.164 -22.305 1.00 73.11 A C ANISOU 211 CB PHE A 34 9433 10021 8323 1853 103 -1303 A C ATOM 212 CG PHE A 34 54.276 -18.333 -23.089 1.00 95.77 A C ANISOU 212 CG PHE A 34 12541 12726 11119 1952 63 -1511 A C ATOM 213 CD1 PHE A 34 55.178 -19.165 -23.728 1.00 94.96 A C ANISOU 213 CD1 PHE A 34 12516 12605 10957 2208 169 -1596 A C ATOM 214 CD2 PHE A 34 52.917 -18.554 -23.263 1.00104.31 A C ANISOU 214 CD2 PHE A 34 13770 13685 12177 1790 -76 -1626 A C ATOM 215 CE1 PHE A 34 54.744 -20.228 -24.492 1.00 99.50 A C ANISOU 215 CE1 PHE A 34 13345 13012 11447 2300 134 -1805 A C ATOM 216 CE2 PHE A 34 52.472 -19.622 -24.014 1.00104.59 A C ANISOU 216 CE2 PHE A 34 14039 13565 12135 1857 -128 -1827 A C ATOM 217 CZ PHE A 34 53.386 -20.471 -24.621 1.00107.23 A C ANISOU 217 CZ PHE A 34 14484 13852 12405 2110 -24 -1924 A C ATOM 218 N LYS A 35 57.134 -16.353 -20.251 1.00 69.25 A N ANISOU 218 N LYS A 35 8494 9741 8077 1880 212 -906 A N ATOM 219 CA LYS A 35 57.923 -15.143 -20.021 1.00 71.63 A C ANISOU 219 CA LYS A 35 8574 10263 8379 1810 281 -733 A C ATOM 220 C LYS A 35 58.092 -14.482 -21.379 1.00 74.30 A C ANISOU 220 C LYS A 35 8899 10776 8552 1876 401 -762 A C ATOM 221 O LYS A 35 58.352 -15.170 -22.372 1.00 79.45 A O ANISOU 221 O LYS A 35 9639 11438 9109 2077 483 -876 A O ATOM 222 CB LYS A 35 59.287 -15.450 -19.416 1.00 72.00 A C ANISOU 222 CB LYS A 35 8441 10393 8520 1935 332 -607 A C ATOM 223 CG LYS A 35 60.134 -14.209 -19.158 1.00 66.31 A C ANISOU 223 CG LYS A 35 7483 9905 7806 1830 389 -424 A C ATOM 224 CD LYS A 35 61.551 -14.555 -18.782 1.00 67.39 A C ANISOU 224 CD LYS A 35 7413 10169 8023 1978 446 -302 A C ATOM 225 CE LYS A 35 62.358 -13.328 -18.392 1.00 68.82 A C ANISOU 225 CE LYS A 35 7352 10571 8223 1823 473 -112 A C ATOM 226 NZ LYS A 35 63.828 -13.642 -18.188 1.00 70.71 A N1+ ANISOU 226 NZ LYS A 35 7343 10987 8533 1979 538 16 A N1+ ATOM 227 N ALA A 36 57.937 -13.166 -21.442 1.00 73.28 A N ANISOU 227 N ALA A 36 8686 10776 8380 1714 416 -662 A N ATOM 228 CA ALA A 36 58.127 -12.477 -22.707 1.00 75.73 A C ANISOU 228 CA ALA A 36 8989 11258 8528 1766 533 -662 A C ATOM 229 C ALA A 36 58.727 -11.082 -22.573 1.00 80.46 A C ANISOU 229 C ALA A 36 9410 12038 9120 1632 598 -477 A C ATOM 230 O ALA A 36 58.889 -10.544 -21.476 1.00 79.22 A O ANISOU 230 O ALA A 36 9149 11868 9079 1473 538 -359 A O ATOM 231 CB ALA A 36 56.847 -12.439 -23.515 1.00 71.67 A C ANISOU 231 CB ALA A 36 8670 10667 7894 1726 469 -799 A C ATOM 232 N ARG A 37 59.045 -10.511 -23.725 1.00 73.94 A N ANISOU 232 N ARG A 37 8571 11377 8144 1689 722 -455 A N ATOM 233 CA ARG A 37 59.830 -9.303 -23.804 1.00 64.62 A C ANISOU 233 CA ARG A 37 7223 10384 6943 1588 817 -275 A C ATOM 234 C ARG A 37 59.129 -8.310 -24.700 1.00 68.14 A C ANISOU 234 C ARG A 37 7773 10874 7240 1505 836 -265 A C ATOM 235 O ARG A 37 58.794 -8.622 -25.836 1.00 85.39 A O ANISOU 235 O ARG A 37 10085 13090 9268 1632 884 -369 A O ATOM 236 CB ARG A 37 61.196 -9.651 -24.406 1.00 67.61 A C ANISOU 236 CB ARG A 37 7446 10962 7279 1774 992 -223 A C ATOM 237 CG ARG A 37 62.080 -8.444 -24.613 1.00 65.25 A C ANISOU 237 CG ARG A 37 6959 10880 6950 1661 1107 -28 A C ATOM 238 CD ARG A 37 63.408 -8.842 -25.203 1.00 60.51 A C ANISOU 238 CD ARG A 37 6179 10498 6313 1853 1293 26 A C ATOM 239 NE ARG A 37 64.257 -7.658 -25.289 1.00 63.90 A N ANISOU 239 NE ARG A 37 6407 11137 6733 1700 1393 233 A N ATOM 240 CZ ARG A 37 64.188 -6.790 -26.284 1.00 70.77 A C ANISOU 240 CZ ARG A 37 7323 12120 7446 1646 1500 289 A C ATOM 241 NH1 ARG A 37 63.340 -7.003 -27.291 1.00 74.20 A N1+ ANISOU 241 NH1 ARG A 37 7987 12497 7709 1750 1517 152 A N1+ ATOM 242 NH2 ARG A 37 65.000 -5.750 -26.304 1.00 81.29 A N ANISOU 242 NH2 ARG A 37 8473 13629 8784 1488 1588 487 A N ATOM 243 N HIS A 38 58.884 -7.116 -24.184 1.00 65.04 A N ANISOU 243 N HIS A 38 7347 10475 6890 1296 792 -142 A N ATOM 244 CA HIS A 38 58.295 -6.078 -25.017 1.00 70.10 A C ANISOU 244 CA HIS A 38 8083 11157 7396 1226 814 -102 A C ATOM 245 C HIS A 38 59.269 -5.769 -26.153 1.00 70.25 A C ANISOU 245 C HIS A 38 8030 11393 7268 1318 996 -22 A C ATOM 246 O HIS A 38 60.460 -5.550 -25.906 1.00 68.94 A O ANISOU 246 O HIS A 38 7675 11364 7155 1297 1097 104 A O ATOM 247 CB HIS A 38 58.024 -4.833 -24.196 1.00 71.73 A C ANISOU 247 CB HIS A 38 8266 11303 7685 998 752 25 A C ATOM 248 CG HIS A 38 57.297 -3.777 -24.955 1.00 69.35 A C ANISOU 248 CG HIS A 38 8083 11004 7262 939 756 70 A C ATOM 249 CD2 HIS A 38 56.024 -3.333 -24.852 1.00 65.15 A C ANISOU 249 CD2 HIS A 38 7685 10341 6726 878 646 30 A C ATOM 250 ND1 HIS A 38 57.886 -3.056 -25.983 1.00 78.94 A N ANISOU 250 ND1 HIS A 38 9280 12378 8336 951 888 180 A N ATOM 251 CE1 HIS A 38 56.993 -2.223 -26.486 1.00 84.96 A C ANISOU 251 CE1 HIS A 38 10179 13092 9010 904 848 206 A C ATOM 252 NE2 HIS A 38 55.862 -2.354 -25.800 1.00 77.28 A N ANISOU 252 NE2 HIS A 38 9290 11948 8125 864 701 117 A N ATOM 253 N ARG A 39 58.768 -5.743 -27.389 1.00 69.96 A N ANISOU 253 N ARG A 39 8136 11403 7040 1414 1036 -88 A N ATOM 254 CA ARG A 39 59.667 -5.692 -28.542 1.00 69.78 A C ANISOU 254 CA ARG A 39 8068 11592 6851 1539 1226 -40 A C ATOM 255 C ARG A 39 60.393 -4.361 -28.704 1.00 63.82 A C ANISOU 255 C ARG A 39 7194 10985 6068 1391 1338 182 A C ATOM 256 O ARG A 39 61.381 -4.295 -29.432 1.00 65.16 A O ANISOU 256 O ARG A 39 7261 11356 6137 1469 1519 261 A O ATOM 257 CB ARG A 39 58.933 -6.048 -29.839 1.00 84.64 A C ANISOU 257 CB ARG A 39 10160 13489 8508 1678 1232 -176 A C ATOM 258 CG ARG A 39 58.689 -7.540 -30.002 1.00100.28 A C ANISOU 258 CG ARG A 39 12244 15382 10472 1868 1193 -398 A C ATOM 259 CD ARG A 39 58.164 -7.923 -31.407 1.00 97.51 A C ANISOU 259 CD ARG A 39 12105 15079 9864 2011 1217 -538 A C ATOM 260 NE ARG A 39 57.369 -9.154 -31.343 1.00 96.50 A N ANISOU 260 NE ARG A 39 12140 14775 9750 2096 1082 -765 A N ATOM 261 CZ ARG A 39 57.839 -10.385 -31.546 1.00111.39 A C ANISOU 261 CZ ARG A 39 14075 16630 11615 2289 1144 -914 A C ATOM 262 NH1 ARG A 39 59.112 -10.581 -31.880 1.00129.75 A N1+ ANISOU 262 NH1 ARG A 39 16285 19115 13898 2447 1352 -864 A N1+ ATOM 263 NH2 ARG A 39 57.021 -11.424 -31.383 1.00 98.60 A N ANISOU 263 NH2 ARG A 39 12619 14815 10028 2321 997 -1110 A N ATOM 264 N LYS A 40 59.918 -3.320 -28.019 1.00 68.01 A N ANISOU 264 N LYS A 40 7741 11411 6686 1178 1240 283 A N ATOM 265 CA LYS A 40 60.511 -2.000 -28.166 1.00 77.28 A C ANISOU 265 CA LYS A 40 8842 12685 7835 1011 1330 493 A C ATOM 266 C LYS A 40 61.390 -1.563 -26.999 1.00 78.78 A C ANISOU 266 C LYS A 40 8836 12885 8212 831 1323 625 A C ATOM 267 O LYS A 40 62.417 -0.922 -27.199 1.00 70.96 A O ANISOU 267 O LYS A 40 7698 12055 7209 737 1448 792 A O ATOM 268 CB LYS A 40 59.419 -0.964 -28.423 1.00 69.83 A C ANISOU 268 CB LYS A 40 8085 11622 6824 904 1246 533 A C ATOM 269 CG LYS A 40 58.963 -0.927 -29.892 1.00 68.80 A C ANISOU 269 CG LYS A 40 8110 11578 6450 1037 1305 503 A C ATOM 270 CD LYS A 40 57.655 -0.167 -29.991 1.00 79.92 A C ANISOU 270 CD LYS A 40 9704 12838 7822 974 1170 506 A C ATOM 271 CE LYS A 40 57.037 -0.284 -31.366 1.00 87.62 A C ANISOU 271 CE LYS A 40 10845 13889 8557 1116 1179 453 A C ATOM 272 NZ LYS A 40 57.722 0.595 -32.334 1.00 97.55 A N1+ ANISOU 272 NZ LYS A 40 12113 15306 9642 1088 1340 633 A N1+ ATOM 273 N THR A 41 60.983 -1.939 -25.794 1.00 74.75 A N ANISOU 273 N THR A 41 8322 12212 7865 775 1174 552 A N ATOM 274 CA THR A 41 61.561 -1.425 -24.564 1.00 72.00 A C ANISOU 274 CA THR A 41 7840 11834 7681 574 1118 663 A C ATOM 275 C THR A 41 62.312 -2.498 -23.784 1.00 73.90 A C ANISOU 275 C THR A 41 7906 12121 8050 654 1096 624 A C ATOM 276 O THR A 41 63.085 -2.183 -22.860 1.00 71.65 A O ANISOU 276 O THR A 41 7461 11875 7885 503 1064 733 A O ATOM 277 CB THR A 41 60.441 -0.947 -23.633 1.00 70.99 A C ANISOU 277 CB THR A 41 7866 11469 7635 437 955 616 A C ATOM 278 CG2 THR A 41 59.511 -0.023 -24.361 1.00 70.53 A C ANISOU 278 CG2 THR A 41 7997 11337 7463 405 953 636 A C ATOM 279 OG1 THR A 41 59.756 -2.093 -23.088 1.00 76.87 A O ANISOU 279 OG1 THR A 41 8664 12094 8449 555 846 448 A O ATOM 280 N GLY A 42 62.028 -3.758 -24.108 1.00 68.74 A N ANISOU 280 N GLY A 42 7301 11445 7371 883 1094 466 A N ATOM 281 CA GLY A 42 62.698 -4.878 -23.481 1.00 66.64 A C ANISOU 281 CA GLY A 42 6895 11206 7218 1004 1079 425 A C ATOM 282 C GLY A 42 62.036 -5.271 -22.175 1.00 63.18 A C ANISOU 282 C GLY A 42 6522 10561 6920 927 897 356 A C ATOM 283 O GLY A 42 62.428 -6.235 -21.531 1.00 67.03 A O ANISOU 283 O GLY A 42 6930 11029 7507 1022 854 320 A O ATOM 284 N GLN A 43 61.001 -4.525 -21.789 1.00 54.96 A N ANISOU 284 N GLN A 43 5634 9363 5882 766 797 341 A N ATOM 285 CA GLN A 43 60.290 -4.799 -20.559 1.00 59.84 A C ANISOU 285 CA GLN A 43 6326 9794 6617 680 642 280 A C ATOM 286 C GLN A 43 59.863 -6.250 -20.449 1.00 68.20 A C ANISOU 286 C GLN A 43 7448 10753 7709 861 588 126 A C ATOM 287 O GLN A 43 59.219 -6.761 -21.354 1.00 80.60 A O ANISOU 287 O GLN A 43 9144 12290 9188 998 610 4 A O ATOM 288 CB GLN A 43 59.074 -3.889 -20.430 1.00 63.15 A C ANISOU 288 CB GLN A 43 6920 10065 7008 543 573 259 A C ATOM 289 CG GLN A 43 58.278 -4.146 -19.147 1.00 77.45 A C ANISOU 289 CG GLN A 43 8808 11692 8927 455 433 196 A C ATOM 290 CD GLN A 43 56.966 -3.396 -19.192 1.00 88.45 A C ANISOU 290 CD GLN A 43 10368 12951 10285 380 385 155 A C ATOM 291 NE2 GLN A 43 56.225 -3.435 -18.084 1.00 72.21 A N ANISOU 291 NE2 GLN A 43 8379 10746 8311 291 288 113 A N ATOM 292 OE1 GLN A 43 56.621 -2.787 -20.242 1.00 87.25 A O ANISOU 292 OE1 GLN A 43 10283 12839 10026 414 441 168 A O ATOM 293 N LYS A 44 60.265 -6.932 -19.381 1.00 64.13 A N ANISOU 293 N LYS A 44 6856 10193 7317 860 515 136 A N ATOM 294 CA LYS A 44 59.902 -8.349 -19.215 1.00 64.42 A C ANISOU 294 CA LYS A 44 6970 10110 7397 1025 462 2 A C ATOM 295 C LYS A 44 58.509 -8.493 -18.630 1.00 64.08 A C ANISOU 295 C LYS A 44 7106 9855 7384 934 337 -97 A C ATOM 296 O LYS A 44 58.166 -7.766 -17.684 1.00 71.59 A O ANISOU 296 O LYS A 44 8067 10745 8388 746 265 -37 A O ATOM 297 CB LYS A 44 60.922 -9.070 -18.340 1.00 61.90 A C ANISOU 297 CB LYS A 44 6497 9827 7192 1083 434 70 A C ATOM 298 CG LYS A 44 62.367 -8.989 -18.820 1.00 70.34 A C ANISOU 298 CG LYS A 44 7340 11131 8254 1182 559 184 A C ATOM 299 CD LYS A 44 62.566 -9.434 -20.254 1.00 66.87 A C ANISOU 299 CD LYS A 44 6924 10785 7697 1407 709 105 A C ATOM 300 CE LYS A 44 64.041 -9.419 -20.625 1.00 71.39 A C ANISOU 300 CE LYS A 44 7242 11608 8275 1519 849 230 A C ATOM 301 NZ LYS A 44 64.657 -8.077 -20.621 1.00 67.37 A N1+ ANISOU 301 NZ LYS A 44 6569 11274 7751 1309 898 404 A N1+ ATOM 302 N VAL A 45 57.699 -9.403 -19.164 1.00 61.89 A N ANISOU 302 N VAL A 45 6972 9470 7071 1055 312 -248 A N ATOM 303 CA VAL A 45 56.325 -9.581 -18.690 1.00 65.15 A C ANISOU 303 CA VAL A 45 7533 9703 7515 963 200 -340 A C ATOM 304 C VAL A 45 55.955 -11.067 -18.638 1.00 62.51 A C ANISOU 304 C VAL A 45 7300 9228 7221 1085 144 -472 A C ATOM 305 O VAL A 45 56.681 -11.897 -19.170 1.00 67.83 A O ANISOU 305 O VAL A 45 7959 9934 7875 1266 202 -513 A O ATOM 306 CB VAL A 45 55.313 -8.866 -19.630 1.00 61.25 A C ANISOU 306 CB VAL A 45 7142 9217 6911 931 206 -393 A C ATOM 307 CG1 VAL A 45 55.673 -7.401 -19.806 1.00 61.98 A C ANISOU 307 CG1 VAL A 45 7167 9426 6956 824 269 -259 A C ATOM 308 CG2 VAL A 45 55.246 -9.571 -20.966 1.00 59.75 A C ANISOU 308 CG2 VAL A 45 7030 9065 6604 1108 253 -511 A C ATOM 309 N ALA A 46 54.829 -11.396 -18.013 1.00 56.57 A N ANISOU 309 N ALA A 46 6655 8315 6523 987 40 -537 A N ATOM 310 CA ALA A 46 54.302 -12.752 -18.040 1.00 55.50 A C ANISOU 310 CA ALA A 46 6645 8022 6421 1066 -21 -666 A C ATOM 311 C ALA A 46 53.005 -12.779 -18.825 1.00 62.53 A C ANISOU 311 C ALA A 46 7662 8858 7239 1032 -69 -792 A C ATOM 312 O ALA A 46 52.101 -11.979 -18.581 1.00 69.92 A O ANISOU 312 O ALA A 46 8598 9791 8175 891 -110 -769 A O ATOM 313 CB ALA A 46 54.068 -13.290 -16.625 1.00 48.19 A C ANISOU 313 CB ALA A 46 5735 6952 5623 967 -109 -629 A C ATOM 314 N LEU A 47 52.891 -13.722 -19.751 1.00 54.67 A N ANISOU 314 N LEU A 47 6777 7813 6178 1165 -70 -929 A N ATOM 315 CA LEU A 47 51.678 -13.908 -20.510 1.00 55.68 A C ANISOU 315 CA LEU A 47 7030 7890 6234 1127 -142 -1058 A C ATOM 316 C LEU A 47 50.916 -15.146 -20.043 1.00 66.01 A C ANISOU 316 C LEU A 47 8462 8991 7625 1080 -249 -1166 A C ATOM 317 O LEU A 47 51.465 -16.243 -19.948 1.00 76.13 A O ANISOU 317 O LEU A 47 9818 10162 8945 1190 -243 -1219 A O ATOM 318 CB LEU A 47 51.974 -14.020 -22.009 1.00 59.24 A C ANISOU 318 CB LEU A 47 7551 8438 6518 1283 -80 -1152 A C ATOM 319 CG LEU A 47 52.823 -12.917 -22.637 1.00 59.14 A C ANISOU 319 CG LEU A 47 7430 8636 6404 1343 45 -1044 A C ATOM 320 CD1 LEU A 47 53.079 -13.183 -24.116 1.00 61.71 A C ANISOU 320 CD1 LEU A 47 7850 9052 6545 1506 114 -1147 A C ATOM 321 CD2 LEU A 47 52.208 -11.553 -22.424 1.00 54.65 A C ANISOU 321 CD2 LEU A 47 6792 8139 5831 1187 22 -937 A C ATOM 322 N LYS A 48 49.610 -14.978 -19.846 1.00 66.41 A N ANISOU 322 N LYS A 48 8542 8990 7701 922 -345 -1198 A N ATOM 323 CA LYS A 48 48.733 -16.106 -19.582 1.00 65.79 A C ANISOU 323 CA LYS A 48 8582 8726 7686 845 -452 -1304 A C ATOM 324 C LYS A 48 47.626 -16.148 -20.607 1.00 69.75 A C ANISOU 324 C LYS A 48 9160 9247 8094 796 -537 -1428 A C ATOM 325 O LYS A 48 46.790 -15.253 -20.631 1.00 82.19 A O ANISOU 325 O LYS A 48 10654 10915 9656 692 -571 -1384 A O ATOM 326 CB LYS A 48 48.116 -15.939 -18.187 1.00 69.12 A C ANISOU 326 CB LYS A 48 8940 9077 8245 666 -496 -1210 A C ATOM 327 CG LYS A 48 48.250 -17.163 -17.327 1.00 81.56 A C ANISOU 327 CG LYS A 48 10602 10457 9930 645 -536 -1221 A C ATOM 328 CD LYS A 48 47.130 -17.191 -16.268 1.00 97.50 A C ANISOU 328 CD LYS A 48 12601 12395 12049 434 -601 -1178 A C ATOM 329 CE LYS A 48 46.908 -18.592 -15.703 1.00108.19 A C ANISOU 329 CE LYS A 48 14087 13525 13493 383 -666 -1220 A C ATOM 330 NZ LYS A 48 46.415 -18.526 -14.277 1.00132.95 A N1+ ANISOU 330 NZ LYS A 48 17178 16606 16731 213 -678 -1106 A N1+ ATOM 331 N LYS A 49 47.550 -17.211 -21.396 1.00 73.52 A N ANISOU 331 N LYS A 49 9798 9625 8509 864 -584 -1584 A N ATOM 332 CA LYS A 49 46.433 -17.379 -22.338 1.00 79.20 A C ANISOU 332 CA LYS A 49 10603 10354 9135 791 -699 -1714 A C ATOM 333 C LYS A 49 45.163 -17.777 -21.589 1.00 69.49 A C ANISOU 333 C LYS A 49 9363 9010 8030 573 -824 -1724 A C ATOM 334 O LYS A 49 45.258 -18.497 -20.593 1.00 82.11 A O ANISOU 334 O LYS A 49 10989 10448 9760 514 -829 -1697 A O ATOM 335 CB LYS A 49 46.808 -18.444 -23.357 1.00 87.54 A C ANISOU 335 CB LYS A 49 11863 11320 10078 924 -710 -1890 A C ATOM 336 CG LYS A 49 45.846 -18.655 -24.510 1.00 84.59 A C ANISOU 336 CG LYS A 49 11606 10970 9563 867 -834 -2043 A C ATOM 337 CD LYS A 49 46.124 -19.998 -25.193 1.00 96.86 A C ANISOU 337 CD LYS A 49 13410 12350 11040 961 -862 -2240 A C ATOM 338 CE LYS A 49 45.696 -20.026 -26.655 1.00108.03 A C ANISOU 338 CE LYS A 49 14963 13849 12233 992 -934 -2396 A C ATOM 339 NZ LYS A 49 46.459 -19.031 -27.470 1.00140.07 A N1+ ANISOU 339 NZ LYS A 49 18955 18140 16123 1164 -803 -2334 A N1+ ATOM 340 N VAL A 50 44.011 -17.286 -22.034 1.00 66.13 A N ANISOU 340 N VAL A 50 8883 8679 7563 457 -919 -1745 A N ATOM 341 CA VAL A 50 42.707 -17.655 -21.452 1.00 68.49 A C ANISOU 341 CA VAL A 50 9144 8904 7974 242 -1038 -1756 A C ATOM 342 C VAL A 50 42.191 -18.901 -22.162 1.00 81.36 A C ANISOU 342 C VAL A 50 10955 10397 9561 179 -1171 -1937 A C ATOM 343 O VAL A 50 41.913 -18.839 -23.372 1.00 77.18 A O ANISOU 343 O VAL A 50 10491 9952 8879 216 -1242 -2043 A O ATOM 344 CB VAL A 50 41.726 -16.476 -21.544 1.00 60.94 A C ANISOU 344 CB VAL A 50 8014 8132 7007 163 -1074 -1675 A C ATOM 345 CG1 VAL A 50 40.296 -16.873 -21.189 1.00 63.88 A C ANISOU 345 CG1 VAL A 50 8324 8472 7476 -48 -1203 -1698 A C ATOM 346 CG2 VAL A 50 42.202 -15.375 -20.631 1.00 52.48 A C ANISOU 346 CG2 VAL A 50 6801 7136 6000 198 -945 -1507 A C ATOM 347 N LEU A 51 42.099 -20.016 -21.420 1.00 84.39 A N ANISOU 347 N LEU A 51 11435 10561 10065 82 -1205 -1969 A N ATOM 348 CA LEU A 51 41.743 -21.319 -21.980 1.00 92.27 A C ANISOU 348 CA LEU A 51 12648 11373 11037 14 -1325 -2145 A C ATOM 349 C LEU A 51 40.294 -21.404 -22.415 1.00 96.28 A C ANISOU 349 C LEU A 51 13116 11929 11535 -205 -1497 -2213 A C ATOM 350 O LEU A 51 39.356 -20.923 -21.704 1.00107.72 A O ANISOU 350 O LEU A 51 14370 13461 13095 -375 -1529 -2103 A O ATOM 351 CB LEU A 51 42.009 -22.417 -20.955 1.00 98.69 A C ANISOU 351 CB LEU A 51 13572 11926 11999 -43 -1312 -2129 A C ATOM 352 CG LEU A 51 43.431 -22.692 -20.477 1.00102.78 A C ANISOU 352 CG LEU A 51 14159 12347 12545 167 -1176 -2075 A C ATOM 353 CD1 LEU A 51 44.291 -23.303 -21.590 1.00 86.92 A C ANISOU 353 CD1 LEU A 51 12357 10269 10399 387 -1147 -2233 A C ATOM 354 CD2 LEU A 51 44.034 -21.417 -19.862 1.00122.97 A C ANISOU 354 CD2 LEU A 51 16494 15105 15121 252 -1047 -1894 A C ATOM 355 N MET A 52 40.090 -22.048 -23.562 1.00 93.52 A N ANISOU 355 N MET A 52 12949 11532 11053 -205 -1610 -2395 A N ATOM 356 CA MET A 52 38.755 -22.086 -24.137 1.00 94.15 A C ANISOU 356 CA MET A 52 12983 11691 11097 -411 -1797 -2465 A C ATOM 357 C MET A 52 38.299 -23.502 -24.467 1.00101.85 A C ANISOU 357 C MET A 52 14195 12429 12072 -572 -1949 -2646 A C ATOM 358 O MET A 52 37.912 -23.787 -25.606 1.00105.37 A O ANISOU 358 O MET A 52 14770 12902 12364 -605 -2086 -2805 A O ATOM 359 CB MET A 52 38.707 -21.172 -25.355 1.00 91.81 A C ANISOU 359 CB MET A 52 12644 11638 10601 -292 -1827 -2495 A C ATOM 360 CG MET A 52 39.139 -19.745 -25.098 1.00 91.38 A C ANISOU 360 CG MET A 52 12380 11797 10541 -145 -1684 -2317 A C ATOM 361 SD MET A 52 37.885 -18.782 -24.239 1.00108.09 A S ANISOU 361 SD MET A 52 14179 14076 12812 -319 -1723 -2140 A S ATOM 362 CE MET A 52 36.419 -18.920 -25.279 1.00 95.02 A C ANISOU 362 CE MET A 52 12481 12550 11069 -493 -1974 -2240 A C ATOM 363 N GLU A 53 38.317 -24.362 -23.444 1.00111.59 A N ANISOU 363 N GLU A 53 15493 13429 13475 -684 -1930 -2614 A N ATOM 364 CA GLU A 53 37.911 -25.750 -23.584 1.00124.03 A C ANISOU 364 CA GLU A 53 17313 14732 15081 -858 -2064 -2767 A C ATOM 365 C GLU A 53 36.449 -25.991 -23.338 1.00127.33 A C ANISOU 365 C GLU A 53 17609 15171 15599 -1201 -2235 -2754 A C ATOM 366 O GLU A 53 36.106 -26.843 -22.529 1.00123.73 A O ANISOU 366 O GLU A 53 17214 14503 15294 -1392 -2264 -2728 A O ATOM 367 CB GLU A 53 38.771 -26.663 -22.695 1.00136.70 A C ANISOU 367 CB GLU A 53 19093 16041 16804 -786 -1958 -2741 A C ATOM 368 CG GLU A 53 39.866 -27.428 -23.450 1.00138.89 A C ANISOU 368 CG GLU A 53 19686 16127 16958 -544 -1911 -2910 A C ATOM 369 CD GLU A 53 40.532 -26.575 -24.524 1.00140.48 A C ANISOU 369 CD GLU A 53 19859 16561 16953 -288 -1836 -2961 A C ATOM 370 OE1 GLU A 53 40.615 -25.309 -24.357 1.00138.59 A O ANISOU 370 OE1 GLU A 53 19352 16598 16706 -220 -1753 -2809 A O ATOM 371 OE2 GLU A 53 40.944 -27.183 -25.543 1.00142.14 A O1- ANISOU 371 OE2 GLU A 53 20330 16668 17005 -163 -1859 -3155 A O1- ATOM 372 N ASN A 54 35.599 -25.257 -24.069 1.00135.49 A N ANISOU 372 N ASN A 54 18471 16463 16544 -1276 -2351 -2764 A N ATOM 373 CA ASN A 54 34.134 -25.285 -23.932 1.00140.22 A C ANISOU 373 CA ASN A 54 18879 17163 17233 -1589 -2520 -2732 A C ATOM 374 C ASN A 54 33.587 -24.877 -22.539 1.00129.99 A C ANISOU 374 C ASN A 54 17303 15932 16152 -1722 -2428 -2516 A C ATOM 375 O ASN A 54 33.157 -25.755 -21.771 1.00134.16 A O ANISOU 375 O ASN A 54 17874 16273 16827 -1947 -2458 -2495 A O ATOM 376 CB ASN A 54 33.557 -26.644 -24.421 1.00172.40 A C ANISOU 376 CB ASN A 54 23199 21007 21295 -1841 -2723 -2920 A C ATOM 377 CG ASN A 54 34.372 -27.865 -23.948 1.00169.96 A C ANISOU 377 CG ASN A 54 23215 20313 21049 -1813 -2654 -2995 A C ATOM 378 ND2 ASN A 54 33.973 -28.445 -22.819 1.00162.84 A N ANISOU 378 ND2 ASN A 54 22275 19248 20347 -2023 -2638 -2891 A N ATOM 379 OD1 ASN A 54 35.340 -28.279 -24.600 1.00172.56 A O ANISOU 379 OD1 ASN A 54 23825 20497 21244 -1597 -2610 -3138 A O ATOM 380 N GLU A 55 33.530 -23.583 -22.196 1.00123.48 A N ANISOU 380 N GLU A 55 16207 15365 15345 -1601 -2318 -2357 A N ATOM 381 CA GLU A 55 33.488 -22.435 -23.096 1.00118.72 A C ANISOU 381 CA GLU A 55 15474 15036 14597 -1435 -2335 -2348 A C ATOM 382 C GLU A 55 32.585 -22.653 -24.304 1.00113.77 A C ANISOU 382 C GLU A 55 14858 14516 13850 -1570 -2573 -2481 A C ATOM 383 O GLU A 55 32.924 -22.394 -25.441 1.00119.58 A O ANISOU 383 O GLU A 55 15707 15336 14390 -1426 -2629 -2582 A O ATOM 384 CB GLU A 55 34.852 -21.912 -23.429 1.00119.95 A C ANISOU 384 CB GLU A 55 15753 15195 14628 -1122 -2181 -2353 A C ATOM 385 CG GLU A 55 35.467 -21.218 -22.194 1.00126.12 A C ANISOU 385 CG GLU A 55 16401 15989 15530 -1009 -1969 -2168 A C ATOM 386 CD GLU A 55 35.887 -22.205 -21.102 1.00115.36 A C ANISOU 386 CD GLU A 55 15162 14361 14308 -1087 -1898 -2147 A C ATOM 387 OE1 GLU A 55 35.948 -23.422 -21.394 1.00127.30 A O ANISOU 387 OE1 GLU A 55 16905 15649 15812 -1173 -1988 -2283 A O ATOM 388 OE2 GLU A 55 36.131 -21.767 -19.957 1.00100.89 A O1- ANISOU 388 OE2 GLU A 55 13211 12537 12586 -1065 -1759 -1993 A O1- ATOM 389 N LYS A 56 31.402 -23.166 -23.982 1.00112.15 A N ANISOU 389 N LYS A 56 14529 14312 13769 -1870 -2713 -2470 A N ATOM 390 CA LYS A 56 30.270 -23.191 -24.905 1.00114.92 A C ANISOU 390 CA LYS A 56 14779 14834 14050 -2049 -2957 -2542 A C ATOM 391 C LYS A 56 29.372 -21.998 -24.554 1.00 94.14 A C ANISOU 391 C LYS A 56 11745 12519 11503 -2049 -2940 -2353 A C ATOM 392 O LYS A 56 28.258 -21.832 -25.031 1.00 97.79 A O ANISOU 392 O LYS A 56 12010 13181 11963 -2203 -3124 -2345 A O ATOM 393 CB LYS A 56 29.526 -24.528 -24.733 1.00126.74 A C ANISOU 393 CB LYS A 56 16374 16134 15645 -2400 -3124 -2638 A C ATOM 394 CG LYS A 56 30.452 -25.740 -24.925 1.00124.75 A C ANISOU 394 CG LYS A 56 16545 15519 15332 -2379 -3114 -2817 A C ATOM 395 CD LYS A 56 29.676 -27.038 -24.960 1.00142.17 A C ANISOU 395 CD LYS A 56 18890 17520 17609 -2739 -3311 -2933 A C ATOM 396 CE LYS A 56 30.336 -28.087 -25.843 1.00145.68 A C ANISOU 396 CE LYS A 56 19779 17678 17893 -2706 -3400 -3183 A C ATOM 397 NZ LYS A 56 31.235 -28.978 -25.055 1.00133.18 A N1+ ANISOU 397 NZ LYS A 56 18464 15729 16407 -2646 -3249 -3196 A N1+ ATOM 398 N GLU A 57 29.911 -21.114 -23.743 1.00 87.60 A N ANISOU 398 N GLU A 57 10800 11742 10742 -1854 -2715 -2199 A N ATOM 399 CA GLU A 57 29.180 -19.990 -23.234 1.00 78.68 A C ANISOU 399 CA GLU A 57 9323 10864 9707 -1822 -2653 -2018 A C ATOM 400 C GLU A 57 29.987 -18.718 -23.464 1.00 80.81 A C ANISOU 400 C GLU A 57 9579 11254 9871 -1498 -2505 -1941 A C ATOM 401 O GLU A 57 30.065 -17.872 -22.600 1.00 81.32 A O ANISOU 401 O GLU A 57 9483 11385 10028 -1397 -2334 -1791 A O ATOM 402 CB GLU A 57 28.926 -20.213 -21.743 1.00 67.03 A C ANISOU 402 CB GLU A 57 7721 9302 8445 -1953 -2506 -1891 A C ATOM 403 CG GLU A 57 27.828 -21.292 -21.573 1.00 73.71 A C ANISOU 403 CG GLU A 57 8500 10097 9408 -2312 -2670 -1929 A C ATOM 404 CD GLU A 57 26.458 -20.723 -21.905 1.00 84.10 A C ANISOU 404 CD GLU A 57 9467 11721 10767 -2424 -2808 -1856 A C ATOM 405 OE1 GLU A 57 26.164 -19.593 -21.411 1.00 96.28 A O ANISOU 405 OE1 GLU A 57 10747 13467 12368 -2280 -2677 -1698 A O ATOM 406 OE2 GLU A 57 25.665 -21.373 -22.624 1.00 81.05 A O1- ANISOU 406 OE2 GLU A 57 9059 11376 10358 -2651 -3045 -1949 A O1- ATOM 407 N GLY A 58 30.584 -18.633 -24.653 1.00 80.38 A N ANISOU 407 N GLY A 58 9712 11216 9610 -1352 -2575 -2052 A N ATOM 408 CA GLY A 58 31.422 -17.507 -24.991 1.00 75.78 A C ANISOU 408 CA GLY A 58 9149 10733 8911 -1065 -2442 -1986 A C ATOM 409 C GLY A 58 32.598 -17.318 -24.056 1.00 70.83 A C ANISOU 409 C GLY A 58 8609 9956 8346 -922 -2198 -1919 A C ATOM 410 O GLY A 58 33.130 -18.290 -23.468 1.00 74.72 A O ANISOU 410 O GLY A 58 9260 10221 8907 -993 -2145 -1977 A O ATOM 411 N PHE A 59 32.996 -16.061 -23.901 1.00 64.10 A N ANISOU 411 N PHE A 59 7656 9226 7471 -727 -2060 -1789 A N ATOM 412 CA PHE A 59 34.127 -15.712 -23.046 1.00 59.10 A C ANISOU 412 CA PHE A 59 7084 8484 6884 -593 -1841 -1713 A C ATOM 413 C PHE A 59 33.892 -16.141 -21.605 1.00 60.95 A C ANISOU 413 C PHE A 59 7242 8599 7317 -735 -1754 -1645 A C ATOM 414 O PHE A 59 32.912 -15.757 -20.997 1.00 61.03 A O ANISOU 414 O PHE A 59 7038 8709 7442 -832 -1754 -1551 A O ATOM 415 CB PHE A 59 34.440 -14.228 -23.142 1.00 53.62 A C ANISOU 415 CB PHE A 59 6289 7945 6136 -395 -1728 -1582 A C ATOM 416 CG PHE A 59 35.737 -13.841 -22.502 1.00 59.32 A C ANISOU 416 CG PHE A 59 7099 8571 6867 -259 -1528 -1520 A C ATOM 417 CD1 PHE A 59 36.945 -13.929 -23.184 1.00 58.59 A C ANISOU 417 CD1 PHE A 59 7190 8435 6636 -114 -1475 -1579 A C ATOM 418 CD2 PHE A 59 35.754 -13.451 -21.166 1.00 64.42 A C ANISOU 418 CD2 PHE A 59 7640 9174 7660 -289 -1394 -1405 A C ATOM 419 CE1 PHE A 59 38.134 -13.563 -22.590 1.00 56.00 A C ANISOU 419 CE1 PHE A 59 6910 8042 6325 -3 -1302 -1509 A C ATOM 420 CE2 PHE A 59 36.936 -13.041 -20.572 1.00 60.30 A C ANISOU 420 CE2 PHE A 59 7189 8580 7140 -179 -1231 -1342 A C ATOM 421 CZ PHE A 59 38.133 -13.099 -21.283 1.00 59.68 A C ANISOU 421 CZ PHE A 59 7267 8473 6935 -42 -1191 -1390 A C ATOM 422 N PRO A 60 34.811 -16.945 -21.049 1.00 64.43 A N ANISOU 422 N PRO A 60 7859 8828 7791 -738 -1673 -1684 A N ATOM 423 CA PRO A 60 34.634 -17.590 -19.741 1.00 60.80 A C ANISOU 423 CA PRO A 60 7377 8224 7497 -891 -1611 -1631 A C ATOM 424 C PRO A 60 34.285 -16.605 -18.643 1.00 63.88 A C ANISOU 424 C PRO A 60 7561 8718 7991 -884 -1476 -1466 A C ATOM 425 O PRO A 60 35.026 -15.627 -18.385 1.00 67.89 A O ANISOU 425 O PRO A 60 8057 9275 8463 -713 -1342 -1386 A O ATOM 426 CB PRO A 60 35.991 -18.233 -19.478 1.00 60.85 A C ANISOU 426 CB PRO A 60 7610 8025 7482 -791 -1522 -1672 A C ATOM 427 CG PRO A 60 36.549 -18.463 -20.848 1.00 68.58 A C ANISOU 427 CG PRO A 60 8758 9006 8293 -664 -1596 -1811 A C ATOM 428 CD PRO A 60 36.110 -17.274 -21.652 1.00 67.54 A C ANISOU 428 CD PRO A 60 8483 9117 8060 -576 -1628 -1773 A C ATOM 429 N ILE A 61 33.153 -16.852 -17.997 1.00 67.26 A N ANISOU 429 N ILE A 61 7829 9180 8543 -1075 -1506 -1417 A N ATOM 430 CA ILE A 61 32.716 -16.046 -16.865 1.00 63.04 A C ANISOU 430 CA ILE A 61 7109 8734 8108 -1081 -1365 -1272 A C ATOM 431 C ILE A 61 33.769 -16.035 -15.759 1.00 60.69 A C ANISOU 431 C ILE A 61 6930 8293 7836 -1022 -1199 -1208 A C ATOM 432 O ILE A 61 33.911 -15.080 -15.000 1.00 59.89 A O ANISOU 432 O ILE A 61 6748 8254 7752 -939 -1059 -1104 A O ATOM 433 CB ILE A 61 31.342 -16.553 -16.333 1.00 60.74 A C ANISOU 433 CB ILE A 61 6633 8494 7949 -1321 -1417 -1235 A C ATOM 434 CG1 ILE A 61 30.778 -15.602 -15.291 1.00 59.58 A C ANISOU 434 CG1 ILE A 61 6275 8476 7885 -1296 -1259 -1091 A C ATOM 435 CG2 ILE A 61 31.498 -17.865 -15.634 1.00 66.89 A C ANISOU 435 CG2 ILE A 61 7551 9056 8805 -1511 -1421 -1259 A C ATOM 436 CD1 ILE A 61 29.258 -15.634 -15.299 1.00 63.32 A C ANISOU 436 CD1 ILE A 61 6479 9123 8456 -1452 -1330 -1050 A C ATOM 437 N THR A 62 34.553 -17.099 -15.719 1.00 68.24 A N ANISOU 437 N THR A 62 8093 9050 8785 -1053 -1225 -1276 A N ATOM 438 CA THR A 62 35.637 -17.239 -14.774 1.00 68.55 A C ANISOU 438 CA THR A 62 8255 8950 8839 -993 -1101 -1219 A C ATOM 439 C THR A 62 36.747 -16.238 -15.042 1.00 66.61 A C ANISOU 439 C THR A 62 8045 8765 8496 -766 -1013 -1193 A C ATOM 440 O THR A 62 37.317 -15.647 -14.119 1.00 59.43 A O ANISOU 440 O THR A 62 7125 7853 7601 -712 -888 -1096 A O ATOM 441 CB THR A 62 36.225 -18.668 -14.908 1.00 71.98 A C ANISOU 441 CB THR A 62 8913 9154 9281 -1046 -1172 -1309 A C ATOM 442 CG2 THR A 62 37.610 -18.715 -14.364 1.00 82.10 A C ANISOU 442 CG2 THR A 62 10329 10323 10540 -903 -1072 -1267 A C ATOM 443 OG1 THR A 62 35.404 -19.518 -14.147 1.00 83.45 A O ANISOU 443 OG1 THR A 62 10348 10511 10846 -1274 -1200 -1278 A O ATOM 444 N ALA A 63 37.060 -16.066 -16.326 1.00 65.26 A N ANISOU 444 N ALA A 63 7925 8653 8218 -647 -1084 -1279 A N ATOM 445 CA ALA A 63 38.050 -15.086 -16.736 1.00 61.51 A C ANISOU 445 CA ALA A 63 7471 8254 7643 -448 -1004 -1249 A C ATOM 446 C ALA A 63 37.565 -13.651 -16.491 1.00 63.76 A C ANISOU 446 C ALA A 63 7592 8702 7929 -399 -931 -1144 A C ATOM 447 O ALA A 63 38.345 -12.798 -16.059 1.00 61.13 A O ANISOU 447 O ALA A 63 7266 8386 7573 -299 -818 -1067 A O ATOM 448 CB ALA A 63 38.460 -15.294 -18.193 1.00 59.52 A C ANISOU 448 CB ALA A 63 7324 8031 7260 -337 -1086 -1363 A C ATOM 449 N LEU A 64 36.283 -13.385 -16.736 1.00 61.70 A N ANISOU 449 N LEU A 64 7184 8556 7700 -470 -997 -1139 A N ATOM 450 CA LEU A 64 35.727 -12.069 -16.435 1.00 57.30 A C ANISOU 450 CA LEU A 64 6473 8137 7159 -407 -921 -1038 A C ATOM 451 C LEU A 64 35.918 -11.744 -14.978 1.00 61.68 A C ANISOU 451 C LEU A 64 7010 8633 7792 -442 -774 -946 A C ATOM 452 O LEU A 64 36.301 -10.630 -14.629 1.00 64.55 A O ANISOU 452 O LEU A 64 7364 9033 8128 -339 -667 -873 A O ATOM 453 CB LEU A 64 34.243 -12.000 -16.770 1.00 51.02 A C ANISOU 453 CB LEU A 64 5494 7477 6413 -485 -1016 -1037 A C ATOM 454 CG LEU A 64 33.953 -12.083 -18.270 1.00 62.79 A C ANISOU 454 CG LEU A 64 6990 9065 7802 -441 -1178 -1116 A C ATOM 455 CD1 LEU A 64 32.450 -12.110 -18.486 1.00 73.65 A C ANISOU 455 CD1 LEU A 64 8155 10584 9242 -543 -1290 -1104 A C ATOM 456 CD2 LEU A 64 34.636 -10.967 -19.043 1.00 57.46 A C ANISOU 456 CD2 LEU A 64 6366 8465 7000 -236 -1139 -1083 A C ATOM 457 N ARG A 65 35.649 -12.715 -14.126 1.00 59.03 A N ANISOU 457 N ARG A 65 6686 8199 7541 -597 -771 -948 A N ATOM 458 CA ARG A 65 35.760 -12.511 -12.686 1.00 59.93 A C ANISOU 458 CA ARG A 65 6796 8262 7713 -648 -636 -860 A C ATOM 459 C ARG A 65 37.197 -12.121 -12.299 1.00 61.77 A C ANISOU 459 C ARG A 65 7168 8417 7884 -545 -555 -828 A C ATOM 460 O ARG A 65 37.430 -11.154 -11.566 1.00 55.15 A O ANISOU 460 O ARG A 65 6318 7605 7032 -497 -443 -756 A O ATOM 461 CB ARG A 65 35.372 -13.810 -11.972 1.00 61.61 A C ANISOU 461 CB ARG A 65 7035 8362 8011 -840 -663 -867 A C ATOM 462 CG ARG A 65 35.132 -13.673 -10.495 1.00 69.21 A C ANISOU 462 CG ARG A 65 7967 9302 9026 -925 -531 -770 A C ATOM 463 CD ARG A 65 34.781 -15.049 -9.961 1.00 80.02 A C ANISOU 463 CD ARG A 65 9383 10549 10471 -1121 -574 -771 A C ATOM 464 NE ARG A 65 35.772 -16.008 -10.443 1.00108.91 A N ANISOU 464 NE ARG A 65 13230 14047 14103 -1100 -666 -840 A N ATOM 465 CZ ARG A 65 35.898 -17.256 -10.008 1.00103.31 A C ANISOU 465 CZ ARG A 65 12640 13168 13442 -1228 -706 -842 A C ATOM 466 NH1 ARG A 65 35.086 -17.712 -9.056 1.00 88.17 A N1+ ANISOU 466 NH1 ARG A 65 10671 11228 11601 -1413 -662 -771 A N1+ ATOM 467 NH2 ARG A 65 36.820 -18.055 -10.545 1.00 95.21 A N ANISOU 467 NH2 ARG A 65 11790 11995 12389 -1167 -784 -912 A N ATOM 468 N GLU A 66 38.157 -12.893 -12.815 1.00 58.55 A N ANISOU 468 N GLU A 66 6892 7915 7437 -510 -616 -887 A N ATOM 469 CA GLU A 66 39.560 -12.673 -12.493 1.00 54.09 A C ANISOU 469 CA GLU A 66 6433 7292 6825 -419 -555 -852 A C ATOM 470 C GLU A 66 40.025 -11.297 -12.971 1.00 61.53 A C ANISOU 470 C GLU A 66 7346 8342 7690 -284 -499 -816 A C ATOM 471 O GLU A 66 40.651 -10.535 -12.233 1.00 59.14 A O ANISOU 471 O GLU A 66 7062 8037 7371 -260 -410 -743 A O ATOM 472 CB GLU A 66 40.429 -13.756 -13.120 1.00 55.17 A C ANISOU 472 CB GLU A 66 6696 7327 6936 -375 -626 -927 A C ATOM 473 CG GLU A 66 41.914 -13.587 -12.836 1.00 61.00 A C ANISOU 473 CG GLU A 66 7510 8031 7635 -271 -568 -881 A C ATOM 474 CD GLU A 66 42.753 -14.750 -13.328 1.00 81.82 A C ANISOU 474 CD GLU A 66 10266 10558 10261 -206 -621 -948 A C ATOM 475 OE1 GLU A 66 42.178 -15.704 -13.900 1.00 92.27 A O ANISOU 475 OE1 GLU A 66 11645 11810 11602 -250 -706 -1044 A O ATOM 476 OE2 GLU A 66 43.991 -14.737 -13.109 1.00 91.73 A O1- ANISOU 476 OE2 GLU A 66 11561 11794 11495 -111 -578 -906 A O1- ATOM 477 N ILE A 67 39.710 -10.992 -14.225 1.00 62.78 A N ANISOU 477 N ILE A 67 7470 8589 7791 -207 -559 -866 A N ATOM 478 CA ILE A 67 40.011 -9.697 -14.800 1.00 55.27 A C ANISOU 478 CA ILE A 67 6499 7736 6765 -86 -514 -823 A C ATOM 479 C ILE A 67 39.430 -8.569 -13.946 1.00 52.11 A C ANISOU 479 C ILE A 67 6027 7371 6401 -96 -422 -739 A C ATOM 480 O ILE A 67 40.126 -7.587 -13.641 1.00 60.30 A O ANISOU 480 O ILE A 67 7103 8406 7399 -41 -339 -677 A O ATOM 481 CB ILE A 67 39.477 -9.612 -16.248 1.00 53.88 A C ANISOU 481 CB ILE A 67 6293 7659 6519 -17 -609 -881 A C ATOM 482 CG1 ILE A 67 40.273 -10.574 -17.135 1.00 58.51 A C ANISOU 482 CG1 ILE A 67 6989 8203 7035 24 -674 -973 A C ATOM 483 CG2 ILE A 67 39.593 -8.193 -16.785 1.00 45.69 A C ANISOU 483 CG2 ILE A 67 5232 6718 5408 101 -561 -813 A C ATOM 484 CD1 ILE A 67 39.772 -10.679 -18.554 1.00 65.29 A C ANISOU 484 CD1 ILE A 67 7853 9153 7801 75 -782 -1049 A C ATOM 485 N LYS A 68 38.169 -8.708 -13.542 1.00 49.00 A N ANISOU 485 N LYS A 68 5529 7008 6079 -168 -430 -738 A N ATOM 486 CA LYS A 68 37.536 -7.680 -12.727 1.00 56.99 A C ANISOU 486 CA LYS A 68 6473 8055 7124 -156 -325 -668 A C ATOM 487 C LYS A 68 38.344 -7.479 -11.446 1.00 67.20 A C ANISOU 487 C LYS A 68 7862 9254 8416 -202 -220 -620 A C ATOM 488 O LYS A 68 38.629 -6.348 -11.046 1.00 69.93 A O ANISOU 488 O LYS A 68 8246 9596 8728 -146 -131 -571 A O ATOM 489 CB LYS A 68 36.075 -8.038 -12.386 1.00 56.37 A C ANISOU 489 CB LYS A 68 6245 8037 7133 -237 -337 -669 A C ATOM 490 CG LYS A 68 35.448 -7.071 -11.385 1.00 68.39 A C ANISOU 490 CG LYS A 68 7706 9588 8690 -213 -198 -601 A C ATOM 491 CD LYS A 68 34.128 -7.576 -10.795 1.00 78.76 A C ANISOU 491 CD LYS A 68 8861 10963 10098 -315 -176 -589 A C ATOM 492 CE LYS A 68 34.372 -8.772 -9.873 1.00 85.89 A C ANISOU 492 CE LYS A 68 9827 11768 11038 -488 -167 -597 A C ATOM 493 NZ LYS A 68 33.129 -9.417 -9.361 1.00 80.09 A N1+ ANISOU 493 NZ LYS A 68 8940 11093 10397 -622 -150 -578 A N1+ ATOM 494 N ILE A 69 38.736 -8.589 -10.826 1.00 65.96 A N ANISOU 494 N ILE A 69 7759 9013 8289 -306 -241 -635 A N ATOM 495 CA ILE A 69 39.479 -8.547 -9.560 1.00 63.80 A C ANISOU 495 CA ILE A 69 7576 8659 8005 -364 -164 -585 A C ATOM 496 C ILE A 69 40.906 -7.986 -9.717 1.00 64.02 A C ANISOU 496 C ILE A 69 7697 8664 7962 -296 -154 -560 A C ATOM 497 O ILE A 69 41.340 -7.161 -8.905 1.00 60.93 A O ANISOU 497 O ILE A 69 7359 8253 7537 -308 -79 -509 A O ATOM 498 CB ILE A 69 39.473 -9.933 -8.879 1.00 57.03 A C ANISOU 498 CB ILE A 69 6754 7714 7199 -489 -200 -591 A C ATOM 499 CG1 ILE A 69 38.067 -10.213 -8.332 1.00 56.64 A C ANISOU 499 CG1 ILE A 69 6605 7696 7218 -591 -165 -582 A C ATOM 500 CG2 ILE A 69 40.505 -10.005 -7.777 1.00 51.79 A C ANISOU 500 CG2 ILE A 69 6201 6973 6504 -529 -158 -534 A C ATOM 501 CD1 ILE A 69 37.697 -11.643 -8.122 1.00 51.58 A C ANISOU 501 CD1 ILE A 69 5972 6983 6642 -726 -228 -598 A C ATOM 502 N LEU A 70 41.605 -8.403 -10.779 1.00 57.01 A N ANISOU 502 N LEU A 70 6827 7787 7046 -229 -227 -597 A N ATOM 503 CA LEU A 70 42.951 -7.890 -11.052 1.00 42.46 A C ANISOU 503 CA LEU A 70 5039 5951 5141 -165 -212 -564 A C ATOM 504 C LEU A 70 42.908 -6.372 -11.292 1.00 52.72 A C ANISOU 504 C LEU A 70 6335 7303 6392 -109 -149 -521 A C ATOM 505 O LEU A 70 43.807 -5.637 -10.888 1.00 57.10 A O ANISOU 505 O LEU A 70 6942 7843 6908 -119 -104 -467 A O ATOM 506 CB LEU A 70 43.548 -8.589 -12.263 1.00 41.25 A C ANISOU 506 CB LEU A 70 4895 5819 4958 -84 -281 -617 A C ATOM 507 CG LEU A 70 44.511 -9.745 -12.062 1.00 50.91 A C ANISOU 507 CG LEU A 70 6169 6974 6198 -84 -317 -630 A C ATOM 508 CD1 LEU A 70 44.657 -10.124 -10.597 1.00 45.83 A C ANISOU 508 CD1 LEU A 70 5559 6250 5604 -187 -299 -576 A C ATOM 509 CD2 LEU A 70 44.171 -10.939 -12.949 1.00 57.76 A C ANISOU 509 CD2 LEU A 70 7059 7810 7078 -52 -397 -727 A C ATOM 510 N GLN A 71 41.855 -5.904 -11.959 1.00 55.45 A N ANISOU 510 N GLN A 71 6622 7705 6741 -54 -154 -539 A N ATOM 511 CA GLN A 71 41.727 -4.481 -12.206 1.00 51.93 A C ANISOU 511 CA GLN A 71 6189 7287 6254 15 -96 -491 A C ATOM 512 C GLN A 71 41.485 -3.680 -10.937 1.00 53.09 A C ANISOU 512 C GLN A 71 6379 7374 6416 -33 0 -452 A C ATOM 513 O GLN A 71 41.991 -2.575 -10.817 1.00 59.06 A O ANISOU 513 O GLN A 71 7211 8100 7128 -12 55 -407 A O ATOM 514 CB GLN A 71 40.611 -4.220 -13.212 1.00 41.46 A C ANISOU 514 CB GLN A 71 4782 6042 4929 103 -137 -510 A C ATOM 515 CG GLN A 71 41.064 -4.498 -14.622 1.00 48.52 A C ANISOU 515 CG GLN A 71 5680 6999 5756 175 -215 -536 A C ATOM 516 CD GLN A 71 39.965 -4.826 -15.549 1.00 53.45 A C ANISOU 516 CD GLN A 71 6220 7707 6380 220 -304 -580 A C ATOM 517 NE2 GLN A 71 40.340 -5.117 -16.776 1.00 50.32 A N ANISOU 517 NE2 GLN A 71 5850 7367 5902 280 -374 -614 A N ATOM 518 OE1 GLN A 71 38.792 -4.893 -15.170 1.00 67.42 A O ANISOU 518 OE1 GLN A 71 7897 9500 8217 195 -314 -586 A O ATOM 519 N LEU A 72 40.814 -4.298 -9.966 1.00 53.28 A N ANISOU 519 N LEU A 72 6375 7373 6492 -110 22 -469 A N ATOM 520 CA LEU A 72 40.504 -3.649 -8.710 1.00 53.44 A C ANISOU 520 CA LEU A 72 6448 7344 6510 -154 125 -444 A C ATOM 521 C LEU A 72 41.729 -3.556 -7.802 1.00 53.47 A C ANISOU 521 C LEU A 72 6574 7277 6464 -243 142 -415 A C ATOM 522 O LEU A 72 41.999 -2.491 -7.251 1.00 52.69 A O ANISOU 522 O LEU A 72 6570 7132 6317 -250 209 -391 A O ATOM 523 CB LEU A 72 39.399 -4.404 -7.957 1.00 48.66 A C ANISOU 523 CB LEU A 72 5767 6752 5966 -219 155 -461 A C ATOM 524 CG LEU A 72 39.069 -3.771 -6.584 1.00 45.43 A C ANISOU 524 CG LEU A 72 5428 6299 5534 -259 284 -440 A C ATOM 525 CD1 LEU A 72 38.319 -2.460 -6.767 1.00 50.95 A C ANISOU 525 CD1 LEU A 72 6114 7015 6227 -135 373 -434 A C ATOM 526 CD2 LEU A 72 38.286 -4.738 -5.706 1.00 53.09 A C ANISOU 526 CD2 LEU A 72 6340 7282 6549 -360 317 -442 A C ATOM 527 N LEU A 73 42.474 -4.652 -7.703 1.00 54.72 A N ANISOU 527 N LEU A 73 6733 7426 6632 -304 71 -417 A N ATOM 528 CA LEU A 73 43.601 -4.757 -6.780 1.00 53.65 A C ANISOU 528 CA LEU A 73 6685 7243 6455 -391 63 -378 A C ATOM 529 C LEU A 73 44.867 -4.054 -7.274 1.00 52.51 A C ANISOU 529 C LEU A 73 6575 7112 6262 -372 39 -342 A C ATOM 530 O LEU A 73 45.451 -4.477 -8.263 1.00 62.35 A O ANISOU 530 O LEU A 73 7769 8404 7517 -314 -14 -345 A O ATOM 531 CB LEU A 73 43.878 -6.247 -6.520 1.00 52.67 A C ANISOU 531 CB LEU A 73 6540 7099 6370 -441 -7 -381 A C ATOM 532 CG LEU A 73 42.658 -6.967 -5.914 1.00 56.64 A C ANISOU 532 CG LEU A 73 7014 7582 6921 -499 19 -399 A C ATOM 533 CD1 LEU A 73 42.936 -8.425 -5.572 1.00 67.82 A C ANISOU 533 CD1 LEU A 73 8445 8947 8376 -562 -48 -390 A C ATOM 534 CD2 LEU A 73 42.201 -6.232 -4.654 1.00 54.20 A C ANISOU 534 CD2 LEU A 73 6771 7252 6568 -563 123 -375 A C ATOM 535 N LYS A 74 45.264 -2.976 -6.613 1.00 51.98 A N ANISOU 535 N LYS A 74 6601 7007 6139 -426 86 -311 A N ATOM 536 CA LYS A 74 46.529 -2.293 -6.954 1.00 56.82 A C ANISOU 536 CA LYS A 74 7244 7635 6710 -450 62 -263 A C ATOM 537 C LYS A 74 47.377 -2.073 -5.706 1.00 61.48 A C ANISOU 537 C LYS A 74 7922 8187 7248 -586 46 -226 A C ATOM 538 O LYS A 74 47.096 -1.168 -4.911 1.00 58.13 A O ANISOU 538 O LYS A 74 7616 7697 6774 -647 101 -234 A O ATOM 539 CB LYS A 74 46.265 -0.959 -7.653 1.00 56.84 A C ANISOU 539 CB LYS A 74 7289 7621 6687 -392 117 -255 A C ATOM 540 CG LYS A 74 45.577 -1.135 -9.001 1.00 72.92 A C ANISOU 540 CG LYS A 74 9236 9716 8754 -256 110 -277 A C ATOM 541 CD LYS A 74 46.298 -2.176 -9.834 1.00 71.68 A C ANISOU 541 CD LYS A 74 8988 9637 8609 -223 38 -279 A C ATOM 542 CE LYS A 74 45.523 -2.548 -11.084 1.00 59.41 A C ANISOU 542 CE LYS A 74 7361 8141 7068 -103 14 -320 A C ATOM 543 NZ LYS A 74 46.308 -3.521 -11.887 1.00 62.95 A N1+ ANISOU 543 NZ LYS A 74 7755 8652 7510 -63 -42 -335 A N1+ ATOM 544 N HIS A 75 48.419 -2.878 -5.527 1.00 56.39 A N ANISOU 544 N HIS A 75 7229 7586 6610 -628 -32 -186 A N ATOM 545 CA HIS A 75 49.157 -2.853 -4.279 1.00 53.36 A C ANISOU 545 CA HIS A 75 6915 7183 6173 -760 -74 -144 A C ATOM 546 C HIS A 75 50.565 -3.452 -4.456 1.00 61.14 A C ANISOU 546 C HIS A 75 7807 8248 7174 -775 -169 -76 A C ATOM 547 O HIS A 75 50.746 -4.371 -5.259 1.00 66.85 A O ANISOU 547 O HIS A 75 8425 9018 7955 -669 -195 -78 A O ATOM 548 CB HIS A 75 48.350 -3.607 -3.224 1.00 55.41 A C ANISOU 548 CB HIS A 75 7227 7396 6428 -794 -60 -167 A C ATOM 549 CG HIS A 75 48.968 -3.597 -1.866 1.00 56.17 A C ANISOU 549 CG HIS A 75 7419 7474 6447 -930 -105 -124 A C ATOM 550 CD2 HIS A 75 48.778 -2.782 -0.805 1.00 56.77 A C ANISOU 550 CD2 HIS A 75 7644 7497 6427 -1034 -65 -138 A C ATOM 551 ND1 HIS A 75 49.912 -4.523 -1.476 1.00 57.71 A N ANISOU 551 ND1 HIS A 75 7569 7710 6647 -963 -209 -59 A N ATOM 552 CE1 HIS A 75 50.286 -4.270 -0.237 1.00 70.64 A C ANISOU 552 CE1 HIS A 75 9314 9333 8192 -1093 -245 -26 A C ATOM 553 NE2 HIS A 75 49.596 -3.231 0.207 1.00 66.02 A N ANISOU 553 NE2 HIS A 75 8858 8688 7537 -1144 -156 -81 A N ATOM 554 N GLU A 76 51.551 -2.921 -3.723 1.00 57.76 A N ANISOU 554 N GLU A 76 7416 7838 6690 -902 -220 -18 A N ATOM 555 CA GLU A 76 52.931 -3.370 -3.852 1.00 53.55 A C ANISOU 555 CA GLU A 76 6766 7406 6175 -917 -310 62 A C ATOM 556 C GLU A 76 53.109 -4.882 -3.727 1.00 60.37 A C ANISOU 556 C GLU A 76 7551 8292 7093 -830 -369 81 A C ATOM 557 O GLU A 76 54.016 -5.450 -4.313 1.00 61.49 A O ANISOU 557 O GLU A 76 7564 8519 7281 -752 -411 128 A O ATOM 558 CB GLU A 76 53.860 -2.658 -2.860 1.00 63.25 A C ANISOU 558 CB GLU A 76 8046 8654 7331 -1097 -382 124 A C ATOM 559 CG GLU A 76 54.687 -1.535 -3.494 1.00 93.22 A C ANISOU 559 CG GLU A 76 11802 12502 11114 -1170 -377 167 A C ATOM 560 CD GLU A 76 56.071 -1.999 -3.919 1.00124.46 A C ANISOU 560 CD GLU A 76 15563 16610 15114 -1160 -452 264 A C ATOM 561 OE1 GLU A 76 56.853 -2.395 -3.028 1.00119.65 A O ANISOU 561 OE1 GLU A 76 14914 16059 14487 -1244 -560 329 A O ATOM 562 OE2 GLU A 76 56.390 -1.956 -5.135 1.00130.83 A O1- ANISOU 562 OE2 GLU A 76 16252 17490 15966 -1063 -402 282 A O1- ATOM 563 N ASN A 77 52.255 -5.528 -2.929 1.00 56.41 A N ANISOU 563 N ASN A 77 7135 7712 6585 -842 -365 51 A N ATOM 564 CA ASN A 77 52.363 -6.959 -2.706 1.00 54.51 A C ANISOU 564 CA ASN A 77 6857 7458 6393 -775 -423 77 A C ATOM 565 C ASN A 77 51.347 -7.815 -3.458 1.00 62.00 A C ANISOU 565 C ASN A 77 7794 8349 7414 -659 -376 3 A C ATOM 566 O ASN A 77 51.092 -8.960 -3.099 1.00 65.99 A O ANISOU 566 O ASN A 77 8321 8796 7955 -634 -409 11 A O ATOM 567 CB ASN A 77 52.366 -7.259 -1.201 1.00 56.76 A C ANISOU 567 CB ASN A 77 7245 7703 6614 -892 -478 127 A C ATOM 568 CG ASN A 77 53.457 -6.498 -0.480 1.00 69.57 A C ANISOU 568 CG ASN A 77 8878 9395 8159 -1019 -556 199 A C ATOM 569 ND2 ASN A 77 54.706 -6.703 -0.898 1.00 80.92 A N ANISOU 569 ND2 ASN A 77 10174 10936 9636 -979 -635 273 A N ATOM 570 OD1 ASN A 77 53.183 -5.684 0.398 1.00 85.72 A O ANISOU 570 OD1 ASN A 77 11053 11408 10108 -1154 -541 184 A O ATOM 571 N VAL A 78 50.765 -7.233 -4.496 1.00 66.31 A N ANISOU 571 N VAL A 78 8314 8906 7975 -600 -307 -62 A N ATOM 572 CA VAL A 78 49.857 -7.983 -5.350 1.00 60.29 A C ANISOU 572 CA VAL A 78 7528 8106 7272 -500 -282 -136 A C ATOM 573 C VAL A 78 50.327 -7.843 -6.783 1.00 65.05 A C ANISOU 573 C VAL A 78 8044 8780 7890 -380 -272 -161 A C ATOM 574 O VAL A 78 50.699 -6.767 -7.237 1.00 70.32 A O ANISOU 574 O VAL A 78 8689 9509 8521 -388 -238 -143 A O ATOM 575 CB VAL A 78 48.419 -7.507 -5.218 1.00 54.01 A C ANISOU 575 CB VAL A 78 6783 7266 6470 -536 -209 -196 A C ATOM 576 CG1 VAL A 78 47.534 -8.251 -6.190 1.00 53.19 A C ANISOU 576 CG1 VAL A 78 6635 7146 6428 -450 -207 -269 A C ATOM 577 CG2 VAL A 78 47.930 -7.689 -3.789 1.00 51.92 A C ANISOU 577 CG2 VAL A 78 6608 6942 6177 -650 -196 -171 A C ATOM 578 N VAL A 79 50.362 -8.974 -7.464 1.00 66.60 A N ANISOU 578 N VAL A 79 8209 8961 8135 -273 -301 -198 A N ATOM 579 CA VAL A 79 50.827 -9.022 -8.839 1.00 58.05 A C ANISOU 579 CA VAL A 79 7058 7947 7048 -144 -285 -230 A C ATOM 580 C VAL A 79 50.026 -8.012 -9.652 1.00 50.04 A C ANISOU 580 C VAL A 79 6048 6965 5997 -138 -229 -276 A C ATOM 581 O VAL A 79 48.887 -7.729 -9.334 1.00 51.67 A O ANISOU 581 O VAL A 79 6299 7123 6209 -193 -211 -310 A O ATOM 582 CB VAL A 79 50.684 -10.455 -9.405 1.00 58.84 A C ANISOU 582 CB VAL A 79 7172 7988 7196 -33 -321 -296 A C ATOM 583 CG1 VAL A 79 49.228 -10.736 -9.777 1.00 47.84 A C ANISOU 583 CG1 VAL A 79 5829 6527 5818 -52 -320 -390 A C ATOM 584 CG2 VAL A 79 51.620 -10.638 -10.569 1.00 72.83 A C ANISOU 584 CG2 VAL A 79 8879 9843 8950 114 -302 -308 A C ATOM 585 N ASN A 80 50.649 -7.435 -10.658 1.00 59.04 A N ANISOU 585 N ASN A 80 7138 8197 7098 -70 -197 -262 A N ATOM 586 CA ASN A 80 50.049 -6.329 -11.418 1.00 53.24 A C ANISOU 586 CA ASN A 80 6415 7495 6317 -62 -148 -276 A C ATOM 587 C ASN A 80 49.669 -6.670 -12.852 1.00 56.08 A C ANISOU 587 C ASN A 80 6759 7900 6647 63 -144 -345 A C ATOM 588 O ASN A 80 50.539 -6.934 -13.686 1.00 59.87 A O ANISOU 588 O ASN A 80 7198 8455 7095 153 -128 -339 A O ATOM 589 CB ASN A 80 51.028 -5.154 -11.452 1.00 53.19 A C ANISOU 589 CB ASN A 80 6386 7557 6267 -113 -109 -187 A C ATOM 590 CG ASN A 80 50.530 -4.016 -12.308 1.00 55.71 A C ANISOU 590 CG ASN A 80 6734 7898 6534 -92 -57 -183 A C ATOM 591 ND2 ASN A 80 51.205 -3.765 -13.429 1.00 54.80 A N ANISOU 591 ND2 ASN A 80 6572 7877 6370 -22 -24 -153 A N ATOM 592 OD1 ASN A 80 49.494 -3.427 -12.012 1.00 68.96 A O ANISOU 592 OD1 ASN A 80 8475 9511 8215 -121 -42 -206 A O ATOM 593 N LEU A 81 48.376 -6.616 -13.138 1.00 56.71 A N ANISOU 593 N LEU A 81 6868 7946 6730 70 -155 -407 A N ATOM 594 CA LEU A 81 47.913 -6.877 -14.494 1.00 56.53 A C ANISOU 594 CA LEU A 81 6842 7973 6662 174 -172 -475 A C ATOM 595 C LEU A 81 48.124 -5.604 -15.295 1.00 59.52 A C ANISOU 595 C LEU A 81 7218 8432 6964 209 -120 -419 A C ATOM 596 O LEU A 81 47.559 -4.573 -14.959 1.00 60.16 A O ANISOU 596 O LEU A 81 7320 8492 7047 162 -95 -378 A O ATOM 597 CB LEU A 81 46.439 -7.291 -14.497 1.00 54.13 A C ANISOU 597 CB LEU A 81 6548 7623 6395 153 -222 -550 A C ATOM 598 CG LEU A 81 45.799 -7.552 -15.863 1.00 47.06 A C ANISOU 598 CG LEU A 81 5653 6783 5443 239 -268 -626 A C ATOM 599 CD1 LEU A 81 46.327 -8.823 -16.520 1.00 61.77 A C ANISOU 599 CD1 LEU A 81 7550 8634 7285 307 -309 -708 A C ATOM 600 CD2 LEU A 81 44.286 -7.600 -15.740 1.00 42.23 A C ANISOU 600 CD2 LEU A 81 5015 6154 4874 192 -318 -668 A C ATOM 601 N ILE A 82 48.951 -5.681 -16.333 1.00 66.27 A N ANISOU 601 N ILE A 82 8056 9374 7749 296 -95 -411 A N ATOM 602 CA ILE A 82 49.265 -4.527 -17.136 1.00 54.22 A C ANISOU 602 CA ILE A 82 6533 7926 6139 322 -39 -340 A C ATOM 603 C ILE A 82 48.128 -4.230 -18.116 1.00 56.00 A C ANISOU 603 C ILE A 82 6794 8176 6304 390 -70 -382 A C ATOM 604 O ILE A 82 47.675 -3.109 -18.225 1.00 56.79 A O ANISOU 604 O ILE A 82 6921 8273 6382 378 -49 -322 A O ATOM 605 CB ILE A 82 50.559 -4.706 -17.942 1.00 48.05 A C ANISOU 605 CB ILE A 82 5711 7252 5292 393 15 -306 A C ATOM 606 CG1 ILE A 82 51.746 -4.844 -17.026 1.00 57.70 A C ANISOU 606 CG1 ILE A 82 6868 8480 6574 329 38 -239 A C ATOM 607 CG2 ILE A 82 50.744 -3.528 -18.874 1.00 44.47 A C ANISOU 607 CG2 ILE A 82 5275 6879 4741 411 75 -226 A C ATOM 608 CD1 ILE A 82 52.928 -5.540 -17.656 1.00 55.68 A C ANISOU 608 CD1 ILE A 82 6540 8328 6286 431 83 -233 A C ATOM 609 N GLU A 83 47.687 -5.250 -18.830 1.00 59.79 A N ANISOU 609 N GLU A 83 7283 8677 6756 463 -128 -484 A N ATOM 610 CA GLU A 83 46.746 -5.077 -19.923 1.00 65.30 A C ANISOU 610 CA GLU A 83 8008 9429 7373 531 -178 -525 A C ATOM 611 C GLU A 83 46.314 -6.452 -20.402 1.00 74.54 A C ANISOU 611 C GLU A 83 9199 10589 8532 570 -261 -661 A C ATOM 612 O GLU A 83 46.874 -7.479 -19.985 1.00 75.13 A O ANISOU 612 O GLU A 83 9280 10608 8655 565 -262 -714 A O ATOM 613 CB GLU A 83 47.378 -4.330 -21.101 1.00 53.93 A C ANISOU 613 CB GLU A 83 6595 8098 5796 610 -121 -461 A C ATOM 614 CG GLU A 83 48.430 -5.157 -21.847 1.00 61.90 A C ANISOU 614 CG GLU A 83 7613 9178 6725 692 -81 -506 A C ATOM 615 CD GLU A 83 48.937 -4.507 -23.134 1.00 74.13 A C ANISOU 615 CD GLU A 83 9196 10855 8115 774 -17 -448 A C ATOM 616 OE1 GLU A 83 48.172 -3.758 -23.784 1.00 77.78 A O ANISOU 616 OE1 GLU A 83 9699 11351 8501 796 -50 -413 A O ATOM 617 OE2 GLU A 83 50.110 -4.758 -23.504 1.00 66.21 A O1- ANISOU 617 OE2 GLU A 83 8172 9925 7058 825 70 -428 A O1- ATOM 618 N ILE A 84 45.303 -6.456 -21.258 1.00 66.57 A N ANISOU 618 N ILE A 84 8207 9627 7459 605 -340 -713 A N ATOM 619 CA ILE A 84 44.820 -7.679 -21.897 1.00 53.74 A C ANISOU 619 CA ILE A 84 6624 7994 5798 626 -438 -852 A C ATOM 620 C ILE A 84 45.016 -7.586 -23.401 1.00 58.52 A C ANISOU 620 C ILE A 84 7297 8713 6223 735 -450 -885 A C ATOM 621 O ILE A 84 44.689 -6.570 -24.018 1.00 81.50 A O ANISOU 621 O ILE A 84 10202 11711 9050 772 -450 -810 A O ATOM 622 CB ILE A 84 43.344 -7.941 -21.532 1.00 54.24 A C ANISOU 622 CB ILE A 84 6641 8023 5944 542 -548 -898 A C ATOM 623 CG1 ILE A 84 43.296 -8.433 -20.082 1.00 52.41 A C ANISOU 623 CG1 ILE A 84 6371 7670 5869 435 -527 -891 A C ATOM 624 CG2 ILE A 84 42.723 -8.962 -22.468 1.00 54.31 A C ANISOU 624 CG2 ILE A 84 6703 8049 5884 549 -673 -1034 A C ATOM 625 CD1 ILE A 84 42.224 -7.762 -19.291 1.00 54.08 A C ANISOU 625 CD1 ILE A 84 6497 7877 6173 362 -533 -832 A C ATOM 626 N CYS A 85 45.536 -8.640 -24.003 1.00 61.68 A N ANISOU 626 N CYS A 85 7775 9107 6553 796 -458 -996 A N ATOM 627 CA CYS A 85 45.896 -8.590 -25.416 1.00 61.86 A C ANISOU 627 CA CYS A 85 7881 9244 6379 910 -443 -1032 A C ATOM 628 C CYS A 85 45.140 -9.641 -26.206 1.00 64.91 A C ANISOU 628 C CYS A 85 8364 9615 6681 917 -577 -1200 A C ATOM 629 O CYS A 85 44.813 -10.719 -25.694 1.00 71.37 A O ANISOU 629 O CYS A 85 9209 10311 7597 855 -645 -1305 A O ATOM 630 CB CYS A 85 47.406 -8.780 -25.587 1.00 70.16 A C ANISOU 630 CB CYS A 85 8951 10325 7380 1005 -299 -1011 A C ATOM 631 SG CYS A 85 48.435 -7.368 -25.130 1.00 76.11 A S ANISOU 631 SG CYS A 85 9605 11151 8162 990 -147 -805 A S ATOM 632 N ARG A 86 44.834 -9.288 -27.446 1.00 70.32 A N ANISOU 632 N ARG A 86 9113 10422 7182 981 -622 -1217 A N ATOM 633 CA ARG A 86 44.213 -10.239 -28.370 1.00 72.99 A C ANISOU 633 CA ARG A 86 9570 10764 7397 988 -757 -1386 A C ATOM 634 C ARG A 86 45.263 -10.803 -29.297 1.00 75.25 A C ANISOU 634 C ARG A 86 9997 11085 7507 1124 -666 -1476 A C ATOM 635 O ARG A 86 46.460 -10.642 -29.074 1.00 73.70 A O ANISOU 635 O ARG A 86 9779 10899 7324 1205 -500 -1411 A O ATOM 636 CB ARG A 86 43.139 -9.551 -29.181 1.00 79.43 A C ANISOU 636 CB ARG A 86 10375 11705 8099 974 -887 -1356 A C ATOM 637 CG ARG A 86 43.667 -8.443 -30.066 1.00 79.89 A C ANISOU 637 CG ARG A 86 10461 11913 7980 1085 -798 -1235 A C ATOM 638 CD ARG A 86 42.525 -7.683 -30.762 1.00 84.01 A C ANISOU 638 CD ARG A 86 10960 12552 8405 1080 -942 -1176 A C ATOM 639 NE ARG A 86 43.054 -6.389 -31.225 1.00111.86 A N ANISOU 639 NE ARG A 86 14491 16183 11827 1167 -831 -1003 A N ATOM 640 CZ ARG A 86 43.606 -6.196 -32.421 1.00117.13 A C ANISOU 640 CZ ARG A 86 15281 16969 12252 1267 -784 -994 A C ATOM 641 NH1 ARG A 86 43.622 -7.188 -33.316 1.00107.08 A N1+ ANISOU 641 NH1 ARG A 86 14144 15734 10805 1303 -850 -1163 A N1+ ATOM 642 NH2 ARG A 86 44.099 -4.999 -32.726 1.00115.14 A N ANISOU 642 NH2 ARG A 86 15028 16792 11926 1323 -674 -816 A N ATOM 643 N THR A 87 44.830 -11.462 -30.358 1.00 83.60 A N ANISOU 643 N THR A 87 11200 12170 8392 1152 -771 -1625 A N ATOM 644 CA THR A 87 45.789 -12.230 -31.088 1.00 86.39 A C ANISOU 644 CA THR A 87 11707 12520 8596 1287 -677 -1745 A C ATOM 645 C THR A 87 45.655 -11.930 -32.557 1.00 98.75 A C ANISOU 645 C THR A 87 13400 14244 9875 1368 -707 -1786 A C ATOM 646 O THR A 87 46.650 -11.621 -33.215 1.00107.28 A O ANISOU 646 O THR A 87 14530 15431 10801 1505 -546 -1748 A O ATOM 647 CB THR A 87 45.607 -13.703 -30.770 1.00 86.29 A C ANISOU 647 CB THR A 87 11806 12317 8661 1249 -755 -1933 A C ATOM 648 CG2 THR A 87 44.624 -14.316 -31.690 1.00 85.94 A C ANISOU 648 CG2 THR A 87 11914 12272 8467 1192 -944 -2101 A C ATOM 649 OG1 THR A 87 46.872 -14.360 -30.822 1.00103.22 A O ANISOU 649 OG1 THR A 87 14031 14407 10779 1400 -594 -1989 A O ATOM 650 N LYS A 88 44.429 -11.949 -33.069 1.00106.42 A N ANISOU 650 N LYS A 88 14411 15253 10771 1280 -911 -1846 A N ATOM 651 CA LYS A 88 44.193 -11.770 -34.509 1.00117.72 A C ANISOU 651 CA LYS A 88 15988 16837 11903 1347 -977 -1900 A C ATOM 652 C LYS A 88 44.334 -13.089 -35.252 1.00114.65 A C ANISOU 652 C LYS A 88 15833 16375 11352 1391 -1024 -2147 A C ATOM 653 O LYS A 88 43.783 -13.244 -36.329 1.00133.21 A O ANISOU 653 O LYS A 88 18329 18813 13471 1389 -1157 -2248 A O ATOM 654 CB LYS A 88 45.167 -10.744 -35.114 1.00117.39 A C ANISOU 654 CB LYS A 88 15943 16956 11703 1485 -785 -1747 A C ATOM 655 CG LYS A 88 44.579 -9.886 -36.223 1.00121.27 A C ANISOU 655 CG LYS A 88 16487 17632 11958 1507 -877 -1672 A C ATOM 656 CD LYS A 88 43.887 -8.632 -35.672 1.00124.66 A C ANISOU 656 CD LYS A 88 16733 18104 12529 1435 -934 -1459 A C ATOM 657 CE LYS A 88 44.061 -7.401 -36.573 1.00117.12 A C ANISOU 657 CE LYS A 88 15808 17324 11367 1518 -880 -1283 A C ATOM 658 NZ LYS A 88 42.990 -7.207 -37.601 1.00110.25 A N1+ ANISOU 658 NZ LYS A 88 15018 16581 10290 1515 -1094 -1300 A N1+ ATOM 659 N GLY A 97 41.079 -17.276 -32.740 1.00 89.60 A N ANISOU 659 N GLY A 97 12743 12458 8842 705 -1678 -2659 A N ATOM 660 CA GLY A 97 41.606 -16.074 -32.074 1.00 94.97 A C ANISOU 660 CA GLY A 97 13206 13245 9631 791 -1506 -2428 A C ATOM 661 C GLY A 97 41.635 -16.196 -30.548 1.00 98.68 A C ANISOU 661 C GLY A 97 13520 13573 10401 702 -1444 -2330 A C ATOM 662 O GLY A 97 40.717 -16.750 -29.981 1.00104.53 A O ANISOU 662 O GLY A 97 14217 14213 11283 522 -1581 -2370 A O ATOM 663 N SER A 98 42.684 -15.694 -29.879 1.00 96.68 A N ANISOU 663 N SER A 98 13180 13316 10235 816 -1241 -2200 A N ATOM 664 CA SER A 98 42.891 -15.884 -28.439 1.00 85.11 A C ANISOU 664 CA SER A 98 11602 11712 9024 751 -1172 -2115 A C ATOM 665 C SER A 98 43.004 -14.599 -27.621 1.00 80.87 A C ANISOU 665 C SER A 98 10847 11275 8603 746 -1073 -1899 A C ATOM 666 O SER A 98 42.976 -13.492 -28.158 1.00 87.08 A O ANISOU 666 O SER A 98 11567 12231 9287 803 -1045 -1800 A O ATOM 667 CB SER A 98 44.124 -16.752 -28.180 1.00 85.49 A C ANISOU 667 CB SER A 98 11771 11611 9098 879 -1036 -2179 A C ATOM 668 OG SER A 98 43.812 -18.120 -28.366 1.00112.39 A O ANISOU 668 OG SER A 98 15371 14829 12501 825 -1142 -2369 A O ATOM 669 N ILE A 99 43.141 -14.768 -26.306 1.00 74.29 A N ANISOU 669 N ILE A 99 9923 10324 7978 676 -1021 -1827 A N ATOM 670 CA ILE A 99 43.193 -13.636 -25.383 1.00 64.92 A C ANISOU 670 CA ILE A 99 8555 9201 6910 650 -936 -1641 A C ATOM 671 C ILE A 99 44.214 -13.906 -24.276 1.00 62.57 A C ANISOU 671 C ILE A 99 8234 8791 6747 677 -808 -1578 A C ATOM 672 O ILE A 99 44.321 -15.034 -23.759 1.00 68.91 A O ANISOU 672 O ILE A 99 9113 9429 7638 639 -833 -1655 A O ATOM 673 CB ILE A 99 41.829 -13.356 -24.758 1.00 70.30 A C ANISOU 673 CB ILE A 99 9106 9888 7715 485 -1047 -1595 A C ATOM 674 CG1 ILE A 99 40.858 -12.771 -25.776 1.00 63.05 A C ANISOU 674 CG1 ILE A 99 8156 9126 6673 478 -1169 -1603 A C ATOM 675 CG2 ILE A 99 41.975 -12.398 -23.562 1.00 76.40 A C ANISOU 675 CG2 ILE A 99 9728 10670 8627 459 -939 -1426 A C ATOM 676 CD1 ILE A 99 41.364 -11.499 -26.407 1.00 63.24 A C ANISOU 676 CD1 ILE A 99 8155 9303 6569 613 -1081 -1490 A C ATOM 677 N TYR A 100 44.977 -12.879 -23.915 1.00 58.55 A N ANISOU 677 N TYR A 100 7628 8366 6250 736 -681 -1433 A N ATOM 678 CA TYR A 100 46.101 -13.069 -23.009 1.00 59.40 A C ANISOU 678 CA TYR A 100 7708 8405 6456 775 -567 -1367 A C ATOM 679 C TYR A 100 46.066 -12.033 -21.903 1.00 63.77 A C ANISOU 679 C TYR A 100 8123 8983 7122 691 -516 -1209 A C ATOM 680 O TYR A 100 45.817 -10.865 -22.153 1.00 70.67 A O ANISOU 680 O TYR A 100 8934 9968 7949 687 -493 -1123 A O ATOM 681 CB TYR A 100 47.413 -12.912 -23.756 1.00 57.31 A C ANISOU 681 CB TYR A 100 7474 8231 6070 945 -442 -1354 A C ATOM 682 CG TYR A 100 47.792 -14.060 -24.658 1.00 69.06 A C ANISOU 682 CG TYR A 100 9118 9668 7451 1068 -447 -1514 A C ATOM 683 CD1 TYR A 100 47.368 -14.103 -25.971 1.00 79.10 A C ANISOU 683 CD1 TYR A 100 10497 11017 8540 1118 -497 -1620 A C ATOM 684 CD2 TYR A 100 48.657 -15.050 -24.212 1.00 85.30 A C ANISOU 684 CD2 TYR A 100 11224 11606 9580 1152 -392 -1554 A C ATOM 685 CE1 TYR A 100 47.773 -15.131 -26.819 1.00 79.86 A C ANISOU 685 CE1 TYR A 100 10765 11062 8517 1242 -487 -1780 A C ATOM 686 CE2 TYR A 100 49.054 -16.079 -25.041 1.00 86.80 A C ANISOU 686 CE2 TYR A 100 11576 11735 9669 1291 -378 -1706 A C ATOM 687 CZ TYR A 100 48.611 -16.119 -26.339 1.00 81.53 A C ANISOU 687 CZ TYR A 100 11030 11135 8810 1333 -421 -1827 A C ATOM 688 OH TYR A 100 49.033 -17.138 -27.167 1.00 96.13 A O ANISOU 688 OH TYR A 100 13067 12916 10542 1480 -397 -1994 A O ATOM 689 N LEU A 101 46.294 -12.483 -20.675 1.00 55.89 A N ANISOU 689 N LEU A 101 7098 7870 6265 625 -501 -1172 A N ATOM 690 CA LEU A 101 46.490 -11.557 -19.584 1.00 54.33 A C ANISOU 690 CA LEU A 101 6798 7690 6153 556 -440 -1032 A C ATOM 691 C LEU A 101 47.969 -11.236 -19.543 1.00 61.73 A C ANISOU 691 C LEU A 101 7705 8684 7063 649 -330 -953 A C ATOM 692 O LEU A 101 48.805 -12.140 -19.535 1.00 72.95 A O ANISOU 692 O LEU A 101 9162 10056 8496 731 -308 -990 A O ATOM 693 CB LEU A 101 46.023 -12.171 -18.265 1.00 56.08 A C ANISOU 693 CB LEU A 101 7011 7778 6519 432 -479 -1021 A C ATOM 694 CG LEU A 101 44.556 -12.102 -17.914 1.00 60.40 A C ANISOU 694 CG LEU A 101 7522 8301 7124 301 -554 -1038 A C ATOM 695 CD1 LEU A 101 43.666 -12.378 -19.091 1.00 57.81 A C ANISOU 695 CD1 LEU A 101 7225 8017 6721 311 -649 -1144 A C ATOM 696 CD2 LEU A 101 44.253 -13.114 -16.810 1.00 63.32 A C ANISOU 696 CD2 LEU A 101 7919 8523 7615 190 -588 -1050 A C ATOM 697 N VAL A 102 48.312 -9.953 -19.540 1.00 61.75 A N ANISOU 697 N VAL A 102 7639 8789 7032 640 -262 -840 A N ATOM 698 CA VAL A 102 49.723 -9.563 -19.466 1.00 56.52 A C ANISOU 698 CA VAL A 102 6920 8200 6352 696 -162 -747 A C ATOM 699 C VAL A 102 50.097 -9.033 -18.089 1.00 56.58 A C ANISOU 699 C VAL A 102 6861 8172 6464 585 -142 -634 A C ATOM 700 O VAL A 102 49.564 -8.026 -17.648 1.00 63.09 A O ANISOU 700 O VAL A 102 7669 8997 7303 490 -140 -573 A O ATOM 701 CB VAL A 102 50.069 -8.511 -20.532 1.00 64.12 A C ANISOU 701 CB VAL A 102 7868 9307 7186 753 -91 -690 A C ATOM 702 CG1 VAL A 102 51.574 -8.330 -20.602 1.00 71.21 A C ANISOU 702 CG1 VAL A 102 8693 10297 8063 813 16 -604 A C ATOM 703 CG2 VAL A 102 49.534 -8.944 -21.888 1.00 64.15 A C ANISOU 703 CG2 VAL A 102 7958 9355 7061 849 -127 -802 A C ATOM 704 N PHE A 103 51.044 -9.705 -17.418 1.00 60.06 A N ANISOU 704 N PHE A 103 7270 8582 6967 606 -128 -607 A N ATOM 705 CA PHE A 103 51.508 -9.261 -16.087 1.00 66.17 A C ANISOU 705 CA PHE A 103 7985 9332 7821 494 -125 -499 A C ATOM 706 C PHE A 103 52.957 -8.776 -16.055 1.00 65.50 A C ANISOU 706 C PHE A 103 7800 9363 7722 519 -57 -390 A C ATOM 707 O PHE A 103 53.761 -9.170 -16.911 1.00 73.63 A O ANISOU 707 O PHE A 103 8792 10478 8705 652 -4 -401 A O ATOM 708 CB PHE A 103 51.388 -10.393 -15.078 1.00 64.98 A C ANISOU 708 CB PHE A 103 7868 9054 7765 467 -188 -525 A C ATOM 709 CG PHE A 103 50.008 -10.977 -14.959 1.00 59.24 A C ANISOU 709 CG PHE A 103 7223 8212 7071 412 -255 -619 A C ATOM 710 CD1 PHE A 103 49.103 -10.490 -14.023 1.00 51.07 A C ANISOU 710 CD1 PHE A 103 6194 7127 6081 272 -276 -589 A C ATOM 711 CD2 PHE A 103 49.660 -12.092 -15.700 1.00 54.28 A C ANISOU 711 CD2 PHE A 103 6670 7521 6433 493 -296 -736 A C ATOM 712 CE1 PHE A 103 47.851 -11.061 -13.881 1.00 53.21 A C ANISOU 712 CE1 PHE A 103 6512 7313 6392 211 -330 -661 A C ATOM 713 CE2 PHE A 103 48.414 -12.700 -15.549 1.00 54.42 A C ANISOU 713 CE2 PHE A 103 6751 7433 6491 413 -369 -815 A C ATOM 714 CZ PHE A 103 47.503 -12.167 -14.642 1.00 59.47 A C ANISOU 714 CZ PHE A 103 7364 8049 7182 269 -384 -770 A C ATOM 715 N ASP A 104 53.264 -7.862 -15.137 1.00 61.57 A N ANISOU 715 N ASP A 104 7260 8879 7255 386 -55 -286 A N ATOM 716 CA ASP A 104 54.664 -7.538 -14.827 1.00 63.97 A C ANISOU 716 CA ASP A 104 7448 9286 7569 368 -20 -172 A C ATOM 717 C ASP A 104 55.377 -8.845 -14.470 1.00 71.17 A C ANISOU 717 C ASP A 104 8314 10183 8542 472 -50 -181 A C ATOM 718 O ASP A 104 54.843 -9.662 -13.713 1.00 67.88 A O ANISOU 718 O ASP A 104 7966 9640 8185 457 -120 -225 A O ATOM 719 CB ASP A 104 54.741 -6.578 -13.646 1.00 71.32 A C ANISOU 719 CB ASP A 104 8377 10192 8529 183 -49 -83 A C ATOM 720 CG ASP A 104 54.519 -5.106 -14.036 1.00 83.92 A C ANISOU 720 CG ASP A 104 10001 11819 10065 92 0 -35 A C ATOM 721 OD1 ASP A 104 54.861 -4.698 -15.165 1.00 98.84 A O ANISOU 721 OD1 ASP A 104 11858 13806 11891 157 68 -13 A O ATOM 722 OD2 ASP A 104 54.048 -4.356 -13.175 1.00 87.81 A O1- ANISOU 722 OD2 ASP A 104 10560 12234 10570 -41 -22 -14 A O1- ATOM 723 N PHE A 105 56.584 -9.051 -14.994 1.00 77.40 A N ANISOU 723 N PHE A 105 8987 11102 9319 584 7 -130 A N ATOM 724 CA PHE A 105 57.312 -10.303 -14.685 1.00 69.74 A C ANISOU 724 CA PHE A 105 7969 10116 8413 720 -15 -130 A C ATOM 725 C PHE A 105 57.956 -10.296 -13.294 1.00 70.62 A C ANISOU 725 C PHE A 105 8001 10228 8602 618 -91 -15 A C ATOM 726 O PHE A 105 58.513 -9.279 -12.866 1.00 72.04 A O ANISOU 726 O PHE A 105 8088 10508 8775 479 -92 92 A O ATOM 727 CB PHE A 105 58.357 -10.579 -15.747 1.00 66.51 A C ANISOU 727 CB PHE A 105 7451 9855 7964 905 87 -119 A C ATOM 728 CG PHE A 105 59.133 -11.842 -15.523 1.00 77.26 A C ANISOU 728 CG PHE A 105 8763 11200 9392 1085 78 -119 A C ATOM 729 CD1 PHE A 105 58.572 -13.087 -15.790 1.00 80.81 A C ANISOU 729 CD1 PHE A 105 9359 11489 9854 1226 54 -251 A C ATOM 730 CD2 PHE A 105 60.442 -11.790 -15.069 1.00 85.22 A C ANISOU 730 CD2 PHE A 105 9575 12351 10453 1118 91 17 A C ATOM 731 CE1 PHE A 105 59.310 -14.249 -15.597 1.00 76.18 A C ANISOU 731 CE1 PHE A 105 8746 10863 9332 1414 51 -248 A C ATOM 732 CE2 PHE A 105 61.216 -12.954 -14.938 1.00 81.02 A C ANISOU 732 CE2 PHE A 105 8982 11813 9985 1325 91 28 A C ATOM 733 CZ PHE A 105 60.628 -14.182 -15.161 1.00 78.20 A C ANISOU 733 CZ PHE A 105 8798 11270 9643 1477 72 -104 A C ATOM 734 N CYS A 106 57.919 -11.432 -12.612 1.00 70.49 A N ANISOU 734 N CYS A 106 8030 10100 8653 682 -160 -33 A N ATOM 735 CA CYS A 106 58.591 -11.586 -11.308 1.00 71.18 A C ANISOU 735 CA CYS A 106 8048 10195 8802 611 -247 84 A C ATOM 736 C CYS A 106 59.627 -12.682 -11.430 1.00 73.38 A C ANISOU 736 C CYS A 106 8229 10513 9136 824 -245 122 A C ATOM 737 O CYS A 106 59.313 -13.799 -11.899 1.00 82.03 A O ANISOU 737 O CYS A 106 9425 11489 10252 993 -232 25 A O ATOM 738 CB CYS A 106 57.577 -11.953 -10.221 1.00 76.13 A C ANISOU 738 CB CYS A 106 8829 10641 9455 492 -336 54 A C ATOM 739 SG CYS A 106 56.367 -10.690 -9.949 1.00 74.44 A S ANISOU 739 SG CYS A 106 8715 10382 9183 271 -326 16 A S ATOM 740 N GLU A 107 60.852 -12.390 -11.007 1.00 62.32 A N ANISOU 740 N GLU A 107 6639 9275 7764 819 -263 262 A N ATOM 741 CA GLU A 107 61.977 -13.286 -11.187 1.00 68.41 A C ANISOU 741 CA GLU A 107 7269 10130 8593 1045 -247 321 A C ATOM 742 C GLU A 107 61.822 -14.642 -10.489 1.00 72.99 A C ANISOU 742 C GLU A 107 7956 10532 9244 1167 -333 310 A C ATOM 743 O GLU A 107 62.066 -15.694 -11.094 1.00 75.20 A O ANISOU 743 O GLU A 107 8263 10753 9555 1413 -285 253 A O ATOM 744 CB GLU A 107 63.270 -12.597 -10.759 1.00 74.66 A C ANISOU 744 CB GLU A 107 7807 11151 9406 976 -270 493 A C ATOM 745 CG GLU A 107 64.528 -13.430 -10.941 1.00 95.29 A C ANISOU 745 CG GLU A 107 10221 13895 12089 1223 -246 578 A C ATOM 746 CD GLU A 107 64.732 -13.884 -12.380 1.00110.62 A C ANISOU 746 CD GLU A 107 12143 15883 14004 1477 -80 485 A C ATOM 747 OE1 GLU A 107 64.035 -13.355 -13.280 1.00102.27 A O ANISOU 747 OE1 GLU A 107 11191 14803 12862 1427 8 378 A O ATOM 748 OE2 GLU A 107 65.554 -14.796 -12.592 1.00119.31 A O1- ANISOU 748 OE2 GLU A 107 13135 17034 15160 1735 -42 517 A O1- ATOM 749 N HIS A 108 61.425 -14.612 -9.224 1.00 74.04 A N ANISOU 749 N HIS A 108 8167 10570 9393 999 -455 365 A N ATOM 750 CA HIS A 108 61.355 -15.836 -8.422 1.00 77.42 A C ANISOU 750 CA HIS A 108 8696 10835 9884 1090 -547 392 A C ATOM 751 C HIS A 108 59.954 -16.290 -8.064 1.00 77.28 A C ANISOU 751 C HIS A 108 8930 10576 9857 989 -582 289 A C ATOM 752 O HIS A 108 59.016 -15.502 -8.107 1.00 82.34 A O ANISOU 752 O HIS A 108 9648 11193 10443 807 -560 222 A O ATOM 753 CB HIS A 108 62.184 -15.690 -7.129 1.00 76.01 A C ANISOU 753 CB HIS A 108 8398 10752 9730 1004 -675 570 A C ATOM 754 CG HIS A 108 63.519 -15.062 -7.368 1.00 75.17 A C ANISOU 754 CG HIS A 108 8011 10913 9634 1039 -658 689 A C ATOM 755 CD2 HIS A 108 64.030 -13.875 -6.966 1.00 79.78 A C ANISOU 755 CD2 HIS A 108 8450 11681 10181 831 -697 785 A C ATOM 756 ND1 HIS A 108 64.480 -15.648 -8.165 1.00 71.55 A N ANISOU 756 ND1 HIS A 108 7390 10565 9230 1308 -582 714 A N ATOM 757 CE1 HIS A 108 65.525 -14.847 -8.242 1.00 85.39 A C ANISOU 757 CE1 HIS A 108 8884 12576 10983 1258 -572 832 A C ATOM 758 NE2 HIS A 108 65.282 -13.768 -7.518 1.00 90.52 A N ANISOU 758 NE2 HIS A 108 9545 13269 11580 959 -650 877 A N ATOM 759 N ASP A 109 59.846 -17.554 -7.646 1.00 78.86 A N ANISOU 759 N ASP A 109 9249 10598 10115 1105 -639 293 A N ATOM 760 CA ASP A 109 58.623 -18.062 -7.049 1.00 81.58 A C ANISOU 760 CA ASP A 109 9814 10719 10461 980 -688 237 A C ATOM 761 C ASP A 109 58.915 -18.807 -5.739 1.00 87.28 A C ANISOU 761 C ASP A 109 10589 11348 11222 971 -807 373 A C ATOM 762 O ASP A 109 59.730 -19.720 -5.720 1.00 82.09 A O ANISOU 762 O ASP A 109 9903 10657 10627 1182 -837 436 A O ATOM 763 CB ASP A 109 57.911 -18.985 -8.032 1.00 77.72 A C ANISOU 763 CB ASP A 109 9484 10049 9994 1106 -634 77 A C ATOM 764 CG ASP A 109 56.960 -19.890 -7.323 1.00 91.61 A C ANISOU 764 CG ASP A 109 11454 11564 11788 1020 -701 59 A C ATOM 765 OD1 ASP A 109 56.376 -19.391 -6.345 1.00107.74 A O ANISOU 765 OD1 ASP A 109 13527 13604 13802 803 -746 117 A O ATOM 766 OD2 ASP A 109 56.865 -21.085 -7.633 1.00108.53 A O1- ANISOU 766 OD2 ASP A 109 13733 13518 13982 1164 -710 3 A O1- ATOM 767 N LEU A 110 58.285 -18.385 -4.645 1.00 93.61 A N ANISOU 767 N LEU A 110 11469 12118 11981 741 -868 424 A N ATOM 768 CA LEU A 110 58.566 -18.935 -3.325 1.00 81.67 A C ANISOU 768 CA LEU A 110 10011 10545 10475 703 -984 570 A C ATOM 769 C LEU A 110 58.581 -20.470 -3.284 1.00 87.53 A C ANISOU 769 C LEU A 110 10891 11069 11296 887 -1021 585 A C ATOM 770 O LEU A 110 59.411 -21.059 -2.589 1.00100.11 A O ANISOU 770 O LEU A 110 12455 12661 12920 993 -1113 730 A O ATOM 771 CB LEU A 110 57.557 -18.385 -2.318 1.00 66.58 A C ANISOU 771 CB LEU A 110 8223 8586 8487 431 -1008 578 A C ATOM 772 CG LEU A 110 57.847 -18.669 -0.850 1.00 68.01 A C ANISOU 772 CG LEU A 110 8462 8749 8630 344 -1129 739 A C ATOM 773 CD1 LEU A 110 59.177 -18.044 -0.444 1.00 63.03 A C ANISOU 773 CD1 LEU A 110 7635 8341 7970 359 -1213 870 A C ATOM 774 CD2 LEU A 110 56.702 -18.179 0.008 1.00 76.56 A C ANISOU 774 CD2 LEU A 110 9690 9773 9625 91 -1114 718 A C ATOM 775 N ALA A 111 57.679 -21.127 -4.004 1.00 77.29 A N ANISOU 775 N ALA A 111 9752 9582 10032 921 -960 443 A N ATOM 776 CA ALA A 111 57.741 -22.601 -4.081 1.00 82.07 A C ANISOU 776 CA ALA A 111 10513 9952 10718 1103 -990 444 A C ATOM 777 C ALA A 111 59.132 -23.030 -4.617 1.00 93.61 A C ANISOU 777 C ALA A 111 11834 11496 12236 1415 -984 494 A C ATOM 778 O ALA A 111 59.757 -23.962 -4.095 1.00 81.75 A O ANISOU 778 O ALA A 111 10374 9894 10793 1578 -1055 608 A O ATOM 779 CB ALA A 111 56.623 -23.138 -4.964 1.00 73.11 A C ANISOU 779 CB ALA A 111 9555 8620 9602 1083 -927 260 A C ATOM 780 N GLY A 112 59.590 -22.325 -5.657 1.00101.66 A N ANISOU 780 N GLY A 112 12685 12704 13235 1499 -891 416 A N ATOM 781 CA GLY A 112 60.888 -22.583 -6.242 1.00 89.63 A C ANISOU 781 CA GLY A 112 10991 11306 11757 1786 -853 460 A C ATOM 782 C GLY A 112 62.060 -22.329 -5.312 1.00 87.17 A C ANISOU 782 C GLY A 112 10472 11183 11464 1822 -947 672 A C ATOM 783 O GLY A 112 62.934 -23.190 -5.167 1.00 92.10 A O ANISOU 783 O GLY A 112 11053 11779 12162 2073 -984 768 A O ATOM 784 N LEU A 113 62.094 -21.148 -4.695 1.00 84.02 A N ANISOU 784 N LEU A 113 9947 10976 10999 1578 -992 746 A N ATOM 785 CA LEU A 113 63.187 -20.788 -3.798 1.00 90.33 A C ANISOU 785 CA LEU A 113 10543 11978 11800 1565 -1103 944 A C ATOM 786 C LEU A 113 63.266 -21.775 -2.612 1.00 96.66 A C ANISOU 786 C LEU A 113 11471 12623 12630 1607 -1245 1085 A C ATOM 787 O LEU A 113 64.341 -22.161 -2.164 1.00 94.51 A O ANISOU 787 O LEU A 113 11054 12449 12405 1769 -1334 1246 A O ATOM 788 CB LEU A 113 62.952 -19.383 -3.238 1.00 82.80 A C ANISOU 788 CB LEU A 113 9518 11189 10750 1246 -1137 969 A C ATOM 789 CG LEU A 113 62.933 -18.198 -4.176 1.00 76.19 A C ANISOU 789 CG LEU A 113 8553 10522 9871 1154 -1023 875 A C ATOM 790 CD1 LEU A 113 62.132 -17.030 -3.577 1.00 78.90 A C ANISOU 790 CD1 LEU A 113 8973 10885 10116 826 -1044 847 A C ATOM 791 CD2 LEU A 113 64.357 -17.745 -4.496 1.00 67.76 A C ANISOU 791 CD2 LEU A 113 7177 9735 8834 1258 -1020 987 A C ATOM 792 N LEU A 114 62.099 -22.160 -2.111 1.00 92.68 A N ANISOU 792 N LEU A 114 11232 11886 12097 1455 -1265 1033 A N ATOM 793 CA LEU A 114 62.036 -23.045 -0.959 1.00 85.32 A C ANISOU 793 CA LEU A 114 10453 10791 11174 1456 -1391 1171 A C ATOM 794 C LEU A 114 62.478 -24.477 -1.306 1.00 93.27 A C ANISOU 794 C LEU A 114 11544 11601 12291 1784 -1395 1197 A C ATOM 795 O LEU A 114 62.997 -25.184 -0.450 1.00 97.06 A O ANISOU 795 O LEU A 114 12057 12022 12799 1885 -1514 1368 A O ATOM 796 CB LEU A 114 60.617 -23.055 -0.384 1.00 81.18 A C ANISOU 796 CB LEU A 114 10182 10075 10585 1192 -1386 1109 A C ATOM 797 CG LEU A 114 60.209 -21.891 0.511 1.00 81.87 A C ANISOU 797 CG LEU A 114 10249 10305 10550 880 -1423 1146 A C ATOM 798 CD1 LEU A 114 58.879 -22.189 1.198 1.00 70.95 A C ANISOU 798 CD1 LEU A 114 9121 8718 9117 672 -1414 1117 A C ATOM 799 CD2 LEU A 114 61.279 -21.614 1.560 1.00 93.84 A C ANISOU 799 CD2 LEU A 114 11632 12003 12019 864 -1573 1347 A C ATOM 800 N SER A 115 62.252 -24.884 -2.555 1.00 96.43 A N ANISOU 800 N SER A 115 11998 11895 12745 1948 -1267 1026 A N ATOM 801 CA SER A 115 62.586 -26.234 -2.973 1.00 97.15 A C ANISOU 801 CA SER A 115 12213 11765 12934 2263 -1252 1016 A C ATOM 802 C SER A 115 64.028 -26.286 -3.476 1.00103.20 A C ANISOU 802 C SER A 115 12712 12735 13761 2585 -1224 1090 A C ATOM 803 O SER A 115 64.469 -27.303 -3.988 1.00123.40 A O ANISOU 803 O SER A 115 15335 15147 16403 2901 -1183 1069 A O ATOM 804 CB SER A 115 61.647 -26.736 -4.061 1.00103.80 A C ANISOU 804 CB SER A 115 13271 12375 13791 2289 -1135 786 A C ATOM 805 OG SER A 115 62.012 -26.195 -5.325 1.00116.42 A O ANISOU 805 OG SER A 115 14711 14145 15376 2410 -1004 651 A O ATOM 806 N ASN A 116 64.755 -25.203 -3.265 1.00 97.46 A N ANISOU 806 N ASN A 116 11692 12341 12996 2497 -1250 1185 A N ATOM 807 CA ASN A 116 66.124 -25.103 -3.734 1.00107.78 A C ANISOU 807 CA ASN A 116 12693 13898 14361 2762 -1217 1269 A C ATOM 808 C ASN A 116 67.109 -25.161 -2.561 1.00113.63 A C ANISOU 808 C ASN A 116 13254 14793 15125 2801 -1392 1528 A C ATOM 809 O ASN A 116 67.232 -24.207 -1.788 1.00112.75 A O ANISOU 809 O ASN A 116 13012 14884 14941 2537 -1494 1628 A O ATOM 810 CB ASN A 116 66.335 -23.844 -4.561 1.00107.37 A C ANISOU 810 CB ASN A 116 12410 14130 14255 2649 -1104 1187 A C ATOM 811 CG ASN A 116 67.673 -23.841 -5.292 1.00108.22 A C ANISOU 811 CG ASN A 116 12207 14484 14427 2947 -1021 1248 A C ATOM 812 ND2 ASN A 116 67.701 -23.188 -6.428 1.00115.10 A N ANISOU 812 ND2 ASN A 116 12973 15496 15262 2950 -862 1120 A N ATOM 813 OD1 ASN A 116 68.663 -24.451 -4.855 1.00107.86 A O ANISOU 813 OD1 ASN A 116 12016 14504 14461 3184 -1095 1414 A O ATOM 814 N VAL A 117 67.805 -26.289 -2.447 1.00117.21 A N ANISOU 814 N VAL A 117 13711 15145 15676 3138 -1431 1634 A N ATOM 815 CA VAL A 117 68.735 -26.520 -1.353 1.00118.37 A C ANISOU 815 CA VAL A 117 13702 15419 15854 3220 -1614 1893 A C ATOM 816 C VAL A 117 69.845 -25.467 -1.258 1.00119.80 A C ANISOU 816 C VAL A 117 13461 16031 16023 3166 -1661 2021 A C ATOM 817 O VAL A 117 70.328 -25.178 -0.168 1.00108.17 A O ANISOU 817 O VAL A 117 11867 14715 14517 3043 -1848 2217 A O ATOM 818 CB VAL A 117 69.352 -27.934 -1.438 1.00114.19 A C ANISOU 818 CB VAL A 117 13234 14704 15448 3654 -1624 1977 A C ATOM 819 CG1 VAL A 117 68.248 -28.995 -1.357 1.00106.31 A C ANISOU 819 CG1 VAL A 117 12680 13253 14459 3659 -1610 1875 A C ATOM 820 CG2 VAL A 117 70.141 -28.094 -2.733 1.00114.10 A C ANISOU 820 CG2 VAL A 117 13019 14813 15519 4003 -1444 1889 A C ATOM 821 N LEU A 118 70.233 -24.888 -2.393 1.00135.64 A N ANISOU 821 N LEU A 118 15256 18232 18048 3238 -1496 1915 A N ATOM 822 CA LEU A 118 71.229 -23.827 -2.416 1.00139.79 A C ANISOU 822 CA LEU A 118 15382 19165 18565 3149 -1520 2026 A C ATOM 823 C LEU A 118 70.764 -22.542 -1.716 1.00131.02 A C ANISOU 823 C LEU A 118 14269 18181 17331 2686 -1619 2034 A C ATOM 824 O LEU A 118 71.535 -21.868 -1.051 1.00124.03 A O ANISOU 824 O LEU A 118 13133 17568 16424 2546 -1757 2197 A O ATOM 825 CB LEU A 118 71.614 -23.501 -3.874 1.00140.03 A C ANISOU 825 CB LEU A 118 15229 19348 18628 3313 -1291 1896 A C ATOM 826 CG LEU A 118 72.463 -24.556 -4.603 1.00125.30 A C ANISOU 826 CG LEU A 118 13249 17476 16881 3802 -1178 1918 A C ATOM 827 CD1 LEU A 118 72.536 -24.269 -6.098 1.00123.52 A C ANISOU 827 CD1 LEU A 118 12944 17340 16647 3932 -924 1742 A C ATOM 828 CD2 LEU A 118 73.841 -24.561 -3.962 1.00118.35 A C ANISOU 828 CD2 LEU A 118 11982 16903 16081 3947 -1311 2184 A C ATOM 829 N VAL A 119 69.477 -22.245 -1.872 1.00134.39 A N ANISOU 829 N VAL A 119 14987 18396 17676 2458 -1549 1853 A N ATOM 830 CA VAL A 119 68.888 -20.996 -1.390 1.00114.71 A C ANISOU 830 CA VAL A 119 12532 15987 15064 2046 -1596 1817 A C ATOM 831 C VAL A 119 68.809 -21.006 0.129 1.00107.94 A C ANISOU 831 C VAL A 119 11767 15107 14136 1853 -1813 1970 A C ATOM 832 O VAL A 119 68.400 -22.004 0.708 1.00104.89 A O ANISOU 832 O VAL A 119 11605 14485 13761 1945 -1879 2010 A O ATOM 833 CB VAL A 119 67.453 -20.832 -1.930 1.00106.68 A C ANISOU 833 CB VAL A 119 11814 14730 13990 1897 -1463 1590 A C ATOM 834 CG1 VAL A 119 66.837 -19.543 -1.404 1.00 97.96 A C ANISOU 834 CG1 VAL A 119 10754 13699 12764 1502 -1500 1555 A C ATOM 835 CG2 VAL A 119 67.455 -20.850 -3.458 1.00109.08 A C ANISOU 835 CG2 VAL A 119 12062 15044 14336 2082 -1255 1429 A C ATOM 836 N LYS A 120 69.185 -19.901 0.765 1.00103.83 A N ANISOU 836 N LYS A 120 11095 14821 13534 1576 -1924 2052 A N ATOM 837 CA LYS A 120 69.105 -19.823 2.227 1.00104.60 A C ANISOU 837 CA LYS A 120 11299 14914 13531 1369 -2134 2188 A C ATOM 838 C LYS A 120 68.484 -18.562 2.806 1.00110.24 A C ANISOU 838 C LYS A 120 12115 15675 14095 961 -2169 2123 A C ATOM 839 O LYS A 120 68.702 -17.447 2.293 1.00118.68 A O ANISOU 839 O LYS A 120 13029 16920 15143 804 -2107 2062 A O ATOM 840 CB LYS A 120 70.480 -20.095 2.840 1.00108.59 A C ANISOU 840 CB LYS A 120 11519 15658 14080 1503 -2323 2429 A C ATOM 841 CG LYS A 120 70.578 -21.434 3.564 1.00118.93 A C ANISOU 841 CG LYS A 120 12964 16795 15428 1734 -2445 2572 A C ATOM 842 CD LYS A 120 71.980 -22.040 3.358 1.00129.80 A C ANISOU 842 CD LYS A 120 14004 18373 16939 2079 -2513 2755 A C ATOM 843 CE LYS A 120 72.083 -23.464 3.888 1.00136.53 A C ANISOU 843 CE LYS A 120 15004 19016 17853 2376 -2607 2890 A C ATOM 844 NZ LYS A 120 73.504 -23.899 4.119 1.00127.07 A N1+ ANISOU 844 NZ LYS A 120 13463 18064 16754 2656 -2749 3129 A N1+ ATOM 845 N PHE A 121 67.660 -18.715 3.849 1.00102.31 A N ANISOU 845 N PHE A 121 11393 14501 12980 788 -2252 2131 A N ATOM 846 CA PHE A 121 67.006 -17.560 4.482 1.00 96.80 A C ANISOU 846 CA PHE A 121 10829 13825 12126 419 -2274 2061 A C ATOM 847 C PHE A 121 67.518 -17.340 5.904 1.00100.18 A C ANISOU 847 C PHE A 121 11258 14378 12426 242 -2511 2234 A C ATOM 848 O PHE A 121 67.657 -18.302 6.670 1.00122.12 A O ANISOU 848 O PHE A 121 14124 17079 15195 357 -2635 2373 A O ATOM 849 CB PHE A 121 65.486 -17.773 4.573 1.00 96.83 A C ANISOU 849 CB PHE A 121 11175 13542 12072 324 -2155 1911 A C ATOM 850 CG PHE A 121 64.780 -17.842 3.243 1.00112.80 A C ANISOU 850 CG PHE A 121 13235 15437 14185 432 -1938 1720 A C ATOM 851 CD1 PHE A 121 64.308 -16.674 2.635 1.00120.79 A C ANISOU 851 CD1 PHE A 121 14232 16504 15157 257 -1818 1573 A C ATOM 852 CD2 PHE A 121 64.542 -19.059 2.621 1.00100.48 A C ANISOU 852 CD2 PHE A 121 11752 13686 12738 699 -1862 1685 A C ATOM 853 CE1 PHE A 121 63.622 -16.725 1.441 1.00103.44 A C ANISOU 853 CE1 PHE A 121 12079 14198 13024 349 -1636 1406 A C ATOM 854 CE2 PHE A 121 63.865 -19.115 1.417 1.00107.39 A C ANISOU 854 CE2 PHE A 121 12679 14448 13674 778 -1680 1503 A C ATOM 855 CZ PHE A 121 63.408 -17.945 0.825 1.00117.78 A C ANISOU 855 CZ PHE A 121 13963 15844 14942 604 -1571 1368 A C ATOM 856 N THR A 122 67.768 -16.088 6.271 1.00 93.08 A N ANISOU 856 N THR A 122 10289 13656 11419 -42 -2578 2225 A N ATOM 857 CA THR A 122 67.971 -15.745 7.674 1.00 95.66 A C ANISOU 857 CA THR A 122 10705 14065 11576 -274 -2791 2340 A C ATOM 858 C THR A 122 66.608 -15.514 8.314 1.00 99.57 A C ANISOU 858 C THR A 122 11570 14341 11920 -477 -2719 2217 A C ATOM 859 O THR A 122 65.606 -15.284 7.624 1.00 96.48 A O ANISOU 859 O THR A 122 11309 13790 11556 -493 -2514 2038 A O ATOM 860 CB THR A 122 68.837 -14.483 7.870 1.00 95.72 A C ANISOU 860 CB THR A 122 10505 14347 11518 -522 -2912 2377 A C ATOM 861 CG2 THR A 122 70.199 -14.632 7.215 1.00 92.09 A C ANISOU 861 CG2 THR A 122 9636 14140 11211 -341 -2970 2508 A C ATOM 862 OG1 THR A 122 68.153 -13.342 7.332 1.00104.34 A O ANISOU 862 OG1 THR A 122 11688 15388 12567 -727 -2751 2186 A O ATOM 863 N LEU A 123 66.567 -15.583 9.640 1.00113.11 A N ANISOU 863 N LEU A 123 13449 16059 13468 -628 -2885 2320 A N ATOM 864 CA LEU A 123 65.339 -15.284 10.358 1.00110.56 A C ANISOU 864 CA LEU A 123 13466 15565 12978 -835 -2813 2216 A C ATOM 865 C LEU A 123 64.810 -13.901 9.964 1.00111.39 A C ANISOU 865 C LEU A 123 13614 15684 13025 -1061 -2681 2024 A C ATOM 866 O LEU A 123 63.607 -13.681 9.915 1.00103.48 A O ANISOU 866 O LEU A 123 12834 14508 11973 -1137 -2513 1878 A O ATOM 867 CB LEU A 123 65.584 -15.316 11.877 1.00100.14 A C ANISOU 867 CB LEU A 123 12290 14308 11447 -1001 -3031 2361 A C ATOM 868 CG LEU A 123 64.371 -14.883 12.716 1.00 92.69 A C ANISOU 868 CG LEU A 123 11697 13220 10298 -1233 -2948 2255 A C ATOM 869 CD1 LEU A 123 63.239 -15.889 12.571 1.00 87.20 A C ANISOU 869 CD1 LEU A 123 11204 12267 9659 -1098 -2780 2217 A C ATOM 870 CD2 LEU A 123 64.732 -14.576 14.138 1.00 90.00 A C ANISOU 870 CD2 LEU A 123 11489 12992 9713 -1444 -3163 2368 A C ATOM 871 N SER A 124 65.725 -12.978 9.692 1.00109.17 A N ANISOU 871 N SER A 124 13115 15611 12754 -1168 -2758 2036 A N ATOM 872 CA SER A 124 65.375 -11.596 9.415 1.00100.64 A C ANISOU 872 CA SER A 124 12084 14545 11607 -1400 -2664 1880 A C ATOM 873 C SER A 124 64.612 -11.442 8.097 1.00 97.73 A C ANISOU 873 C SER A 124 11706 14050 11375 -1284 -2410 1713 A C ATOM 874 O SER A 124 63.669 -10.639 7.982 1.00 89.45 A O ANISOU 874 O SER A 124 10836 12889 10259 -1422 -2271 1556 A O ATOM 875 CB SER A 124 66.637 -10.742 9.383 1.00 99.20 A C ANISOU 875 CB SER A 124 11651 14617 11423 -1543 -2820 1956 A C ATOM 876 OG SER A 124 66.281 -9.370 9.307 1.00115.32 A O ANISOU 876 OG SER A 124 13800 16642 13374 -1801 -2751 1813 A O ATOM 877 N GLU A 125 65.005 -12.241 7.113 1.00 95.82 A N ANISOU 877 N GLU A 125 11265 13824 11317 -1016 -2352 1749 A N ATOM 878 CA GLU A 125 64.388 -12.203 5.801 1.00 80.87 A C ANISOU 878 CA GLU A 125 9348 11830 9547 -886 -2132 1603 A C ATOM 879 C GLU A 125 63.020 -12.916 5.837 1.00 84.58 A C ANISOU 879 C GLU A 125 10076 12048 10012 -814 -2000 1504 A C ATOM 880 O GLU A 125 62.026 -12.440 5.261 1.00 97.01 A O ANISOU 880 O GLU A 125 11760 13508 11589 -857 -1832 1346 A O ATOM 881 CB GLU A 125 65.321 -12.901 4.803 1.00 87.58 A C ANISOU 881 CB GLU A 125 9914 12787 10574 -613 -2119 1676 A C ATOM 882 CG GLU A 125 66.625 -12.156 4.560 1.00113.37 A C ANISOU 882 CG GLU A 125 12879 16324 13870 -682 -2210 1769 A C ATOM 883 CD GLU A 125 67.713 -13.030 3.958 1.00120.96 A C ANISOU 883 CD GLU A 125 13546 17427 14986 -395 -2240 1897 A C ATOM 884 OE1 GLU A 125 68.181 -13.971 4.643 1.00107.15 A O ANISOU 884 OE1 GLU A 125 11766 15695 13250 -261 -2382 2041 A O ATOM 885 OE2 GLU A 125 68.110 -12.798 2.793 1.00144.77 A O1- ANISOU 885 OE2 GLU A 125 16361 20537 18105 -285 -2113 1859 A O1- ATOM 886 N ILE A 126 62.999 -14.063 6.506 1.00 81.07 A N ANISOU 886 N ILE A 126 9716 11520 9564 -705 -2084 1610 A N ATOM 887 CA ILE A 126 61.763 -14.794 6.681 1.00 85.80 A C ANISOU 887 CA ILE A 126 10557 11887 10153 -670 -1981 1545 A C ATOM 888 C ILE A 126 60.712 -13.872 7.294 1.00 83.78 A C ANISOU 888 C ILE A 126 10520 11569 9744 -921 -1904 1435 A C ATOM 889 O ILE A 126 59.558 -13.856 6.872 1.00 75.47 A O ANISOU 889 O ILE A 126 9590 10372 8713 -926 -1739 1303 A O ATOM 890 CB ILE A 126 61.958 -16.049 7.546 1.00 83.71 A C ANISOU 890 CB ILE A 126 10382 11546 9875 -566 -2107 1706 A C ATOM 891 CG1 ILE A 126 62.901 -17.035 6.846 1.00 89.40 A C ANISOU 891 CG1 ILE A 126 10904 12295 10767 -269 -2154 1801 A C ATOM 892 CG2 ILE A 126 60.622 -16.730 7.799 1.00 71.78 A C ANISOU 892 CG2 ILE A 126 9134 9795 8344 -581 -1994 1646 A C ATOM 893 CD1 ILE A 126 63.151 -18.312 7.594 1.00100.61 A C ANISOU 893 CD1 ILE A 126 12411 13619 12194 -128 -2279 1970 A C ATOM 894 N LYS A 127 61.127 -13.079 8.280 1.00 84.05 A N ANISOU 894 N LYS A 127 10597 11718 9618 -1128 -2026 1486 A N ATOM 895 CA LYS A 127 60.241 -12.071 8.872 1.00 85.15 A C ANISOU 895 CA LYS A 127 10947 11808 9597 -1359 -1949 1372 A C ATOM 896 C LYS A 127 59.701 -11.128 7.807 1.00 86.47 A C ANISOU 896 C LYS A 127 11075 11949 9832 -1378 -1774 1201 A C ATOM 897 O LYS A 127 58.508 -10.796 7.801 1.00 84.64 A O ANISOU 897 O LYS A 127 11007 11592 9557 -1435 -1620 1077 A O ATOM 898 CB LYS A 127 60.989 -11.237 9.919 1.00 90.79 A C ANISOU 898 CB LYS A 127 11693 12668 10133 -1578 -2122 1438 A C ATOM 899 CG LYS A 127 60.952 -11.847 11.301 1.00 96.62 A C ANISOU 899 CG LYS A 127 12612 13391 10707 -1647 -2253 1559 A C ATOM 900 CD LYS A 127 61.682 -10.984 12.297 1.00 87.95 A C ANISOU 900 CD LYS A 127 11559 12442 9415 -1878 -2437 1609 A C ATOM 901 CE LYS A 127 61.851 -11.719 13.605 1.00 81.51 A C ANISOU 901 CE LYS A 127 10890 11643 8437 -1916 -2601 1764 A C ATOM 902 NZ LYS A 127 62.221 -10.775 14.703 1.00 80.80 A N1+ ANISOU 902 NZ LYS A 127 10938 11663 8099 -2186 -2752 1767 A N1+ ATOM 903 N ARG A 128 60.586 -10.684 6.920 1.00 88.37 A N ANISOU 903 N ARG A 128 11089 12315 10172 -1329 -1796 1206 A N ATOM 904 CA ARG A 128 60.203 -9.713 5.915 1.00 82.23 A C ANISOU 904 CA ARG A 128 10273 11525 9444 -1357 -1648 1068 A C ATOM 905 C ARG A 128 59.199 -10.314 4.940 1.00 78.11 A C ANISOU 905 C ARG A 128 9774 10861 9040 -1182 -1473 966 A C ATOM 906 O ARG A 128 58.165 -9.695 4.625 1.00 76.60 A O ANISOU 906 O ARG A 128 9696 10577 8829 -1234 -1330 835 A O ATOM 907 CB ARG A 128 61.429 -9.196 5.187 1.00 74.82 A C ANISOU 907 CB ARG A 128 9079 10764 8583 -1346 -1709 1120 A C ATOM 908 CG ARG A 128 61.136 -8.052 4.241 1.00 77.42 A C ANISOU 908 CG ARG A 128 9388 11088 8940 -1409 -1573 999 A C ATOM 909 CD ARG A 128 60.658 -6.817 4.990 1.00 85.53 A C ANISOU 909 CD ARG A 128 10622 12062 9810 -1659 -1567 922 A C ATOM 910 NE ARG A 128 60.172 -5.822 4.044 1.00 93.08 A N ANISOU 910 NE ARG A 128 11595 12968 10802 -1683 -1416 804 A N ATOM 911 CZ ARG A 128 58.905 -5.440 3.927 1.00 93.46 A C ANISOU 911 CZ ARG A 128 11827 12863 10819 -1682 -1265 675 A C ATOM 912 NH1 ARG A 128 57.968 -5.961 4.715 1.00 94.96 A N1+ ANISOU 912 NH1 ARG A 128 12195 12942 10940 -1674 -1230 641 A N1+ ATOM 913 NH2 ARG A 128 58.575 -4.536 3.011 1.00 92.80 A N ANISOU 913 NH2 ARG A 128 11739 12745 10773 -1685 -1145 590 A N ATOM 914 N VAL A 129 59.500 -11.522 4.476 1.00 73.19 A N ANISOU 914 N VAL A 129 9051 10219 8538 -973 -1493 1026 A N ATOM 915 CA VAL A 129 58.603 -12.249 3.578 1.00 61.62 A C ANISOU 915 CA VAL A 129 7620 8610 7180 -813 -1354 932 A C ATOM 916 C VAL A 129 57.193 -12.353 4.161 1.00 61.70 A C ANISOU 916 C VAL A 129 7858 8463 7121 -908 -1266 858 A C ATOM 917 O VAL A 129 56.204 -11.984 3.510 1.00 70.30 A O ANISOU 917 O VAL A 129 8992 9480 8237 -912 -1125 730 A O ATOM 918 CB VAL A 129 59.146 -13.676 3.289 1.00 67.86 A C ANISOU 918 CB VAL A 129 8330 9367 8086 -585 -1411 1020 A C ATOM 919 CG1 VAL A 129 58.047 -14.611 2.816 1.00 59.68 A C ANISOU 919 CG1 VAL A 129 7419 8134 7123 -480 -1305 934 A C ATOM 920 CG2 VAL A 129 60.320 -13.615 2.330 1.00 84.23 A C ANISOU 920 CG2 VAL A 129 10153 11590 10259 -435 -1429 1055 A C ATOM 921 N MET A 130 57.099 -12.862 5.384 1.00 70.41 A N ANISOU 921 N MET A 130 9096 9524 8132 -982 -1347 950 A N ATOM 922 CA MET A 130 55.812 -12.997 6.051 1.00 71.17 A C ANISOU 922 CA MET A 130 9398 9491 8149 -1083 -1255 901 A C ATOM 923 C MET A 130 55.097 -11.658 6.208 1.00 68.72 A C ANISOU 923 C MET A 130 9172 9198 7738 -1241 -1148 784 A C ATOM 924 O MET A 130 53.853 -11.593 6.161 1.00 62.32 A O ANISOU 924 O MET A 130 8463 8293 6923 -1270 -1007 694 A O ATOM 925 CB MET A 130 55.998 -13.657 7.417 1.00 66.47 A C ANISOU 925 CB MET A 130 8937 8876 7441 -1151 -1370 1041 A C ATOM 926 CG MET A 130 56.302 -15.155 7.272 1.00 73.37 A C ANISOU 926 CG MET A 130 9787 9661 8427 -976 -1437 1147 A C ATOM 927 SD MET A 130 55.140 -15.938 6.140 1.00 78.17 A S ANISOU 927 SD MET A 130 10416 10087 9195 -857 -1274 1025 A S ATOM 928 CE MET A 130 53.568 -15.567 6.926 1.00 68.62 A C ANISOU 928 CE MET A 130 9407 8797 7868 -1059 -1134 957 A C ATOM 929 N GLN A 131 55.884 -10.604 6.397 1.00 64.15 A N ANISOU 929 N GLN A 131 8551 8737 7084 -1342 -1216 790 A N ATOM 930 CA GLN A 131 55.333 -9.283 6.560 1.00 66.08 A C ANISOU 930 CA GLN A 131 8898 8979 7231 -1484 -1124 681 A C ATOM 931 C GLN A 131 54.673 -8.804 5.274 1.00 71.57 A C ANISOU 931 C GLN A 131 9519 9633 8038 -1397 -974 556 A C ATOM 932 O GLN A 131 53.548 -8.292 5.292 1.00 72.59 A O ANISOU 932 O GLN A 131 9757 9689 8134 -1434 -836 455 A O ATOM 933 CB GLN A 131 56.425 -8.300 6.987 1.00 65.33 A C ANISOU 933 CB GLN A 131 8778 9005 7039 -1626 -1251 719 A C ATOM 934 CG GLN A 131 55.846 -6.924 7.291 1.00 74.50 A C ANISOU 934 CG GLN A 131 10098 10127 8079 -1780 -1159 602 A C ATOM 935 CD GLN A 131 56.776 -6.074 8.098 1.00 73.55 A C ANISOU 935 CD GLN A 131 10036 10094 7816 -1973 -1303 640 A C ATOM 936 NE2 GLN A 131 56.304 -5.675 9.296 1.00 75.86 A N ANISOU 936 NE2 GLN A 131 10569 10339 7915 -2119 -1297 605 A N ATOM 937 OE1 GLN A 131 57.900 -5.787 7.674 1.00 69.75 A O ANISOU 937 OE1 GLN A 131 9387 9726 7387 -1999 -1418 699 A O ATOM 938 N MET A 132 55.365 -8.973 4.157 1.00 70.54 A N ANISOU 938 N MET A 132 9202 9562 8037 -1273 -998 568 A N ATOM 939 CA MET A 132 54.805 -8.562 2.885 1.00 65.19 A C ANISOU 939 CA MET A 132 8457 8858 7452 -1185 -870 461 A C ATOM 940 C MET A 132 53.553 -9.391 2.565 1.00 70.06 A C ANISOU 940 C MET A 132 9127 9358 8135 -1094 -766 397 A C ATOM 941 O MET A 132 52.528 -8.850 2.143 1.00 67.04 A O ANISOU 941 O MET A 132 8785 8926 7758 -1098 -644 297 A O ATOM 942 CB MET A 132 55.840 -8.692 1.762 1.00 59.51 A C ANISOU 942 CB MET A 132 7532 8238 6841 -1063 -909 495 A C ATOM 943 CG MET A 132 57.090 -7.870 2.002 1.00 68.16 A C ANISOU 943 CG MET A 132 8538 9468 7888 -1171 -1011 569 A C ATOM 944 SD MET A 132 58.393 -8.159 0.805 1.00 70.48 A S ANISOU 944 SD MET A 132 8559 9912 8307 -1020 -1047 638 A S ATOM 945 CE MET A 132 58.149 -6.726 -0.252 1.00 92.99 A C ANISOU 945 CE MET A 132 11393 12781 11158 -1079 -924 546 A C ATOM 946 N LEU A 133 53.650 -10.703 2.765 1.00 70.46 A N ANISOU 946 N LEU A 133 9174 9361 8237 -1015 -823 463 A N ATOM 947 CA LEU A 133 52.544 -11.603 2.458 1.00 66.02 A C ANISOU 947 CA LEU A 133 8659 8680 7745 -952 -745 413 A C ATOM 948 C LEU A 133 51.301 -11.208 3.260 1.00 66.99 A C ANISOU 948 C LEU A 133 8926 8746 7781 -1081 -645 368 A C ATOM 949 O LEU A 133 50.229 -11.015 2.693 1.00 60.33 A O ANISOU 949 O LEU A 133 8077 7862 6981 -1065 -531 274 A O ATOM 950 CB LEU A 133 52.960 -13.038 2.739 1.00 57.22 A C ANISOU 950 CB LEU A 133 7555 7501 6683 -869 -836 508 A C ATOM 951 CG LEU A 133 52.019 -14.174 2.380 1.00 57.24 A C ANISOU 951 CG LEU A 133 7611 7361 6775 -809 -786 472 A C ATOM 952 CD1 LEU A 133 52.764 -15.479 2.313 1.00 67.92 A C ANISOU 952 CD1 LEU A 133 8955 8647 8204 -677 -886 559 A C ATOM 953 CD2 LEU A 133 50.917 -14.243 3.429 1.00 62.49 A C ANISOU 953 CD2 LEU A 133 8423 7958 7360 -959 -724 484 A C ATOM 954 N LEU A 134 51.461 -11.067 4.576 1.00 65.01 A N ANISOU 954 N LEU A 134 8795 8506 7399 -1205 -686 437 A N ATOM 955 CA LEU A 134 50.366 -10.663 5.440 1.00 64.32 A C ANISOU 955 CA LEU A 134 8852 8380 7206 -1322 -576 400 A C ATOM 956 C LEU A 134 49.814 -9.286 5.074 1.00 63.06 A C ANISOU 956 C LEU A 134 8698 8246 7014 -1350 -460 284 A C ATOM 957 O LEU A 134 48.613 -9.020 5.179 1.00 67.35 A O ANISOU 957 O LEU A 134 9292 8751 7544 -1369 -321 216 A O ATOM 958 CB LEU A 134 50.811 -10.696 6.916 1.00 62.18 A C ANISOU 958 CB LEU A 134 8726 8131 6768 -1448 -654 497 A C ATOM 959 CG LEU A 134 50.927 -12.144 7.465 1.00 59.08 A C ANISOU 959 CG LEU A 134 8376 7678 6392 -1428 -733 622 A C ATOM 960 CD1 LEU A 134 51.554 -12.170 8.830 1.00 53.24 A C ANISOU 960 CD1 LEU A 134 7768 6981 5480 -1538 -842 736 A C ATOM 961 CD2 LEU A 134 49.520 -12.783 7.526 1.00 61.55 A C ANISOU 961 CD2 LEU A 134 8750 7892 6744 -1446 -593 593 A C ATOM 962 N ASN A 135 50.697 -8.414 4.617 1.00 60.16 A N ANISOU 962 N ASN A 135 8272 7943 6643 -1346 -514 268 A N ATOM 963 CA ASN A 135 50.287 -7.083 4.187 1.00 55.51 A C ANISOU 963 CA ASN A 135 7701 7356 6032 -1362 -414 169 A C ATOM 964 C ASN A 135 49.441 -7.155 2.904 1.00 59.00 A C ANISOU 964 C ASN A 135 8034 7774 6608 -1234 -316 92 A C ATOM 965 O ASN A 135 48.448 -6.462 2.791 1.00 64.05 A O ANISOU 965 O ASN A 135 8714 8384 7235 -1228 -193 15 A O ATOM 966 CB ASN A 135 51.515 -6.200 3.955 1.00 55.97 A C ANISOU 966 CB ASN A 135 7719 7483 6061 -1409 -507 189 A C ATOM 967 CG ASN A 135 51.169 -4.728 3.848 1.00 62.27 A C ANISOU 967 CG ASN A 135 8605 8253 6799 -1465 -417 101 A C ATOM 968 ND2 ASN A 135 51.866 -4.016 2.976 1.00 70.30 A N ANISOU 968 ND2 ASN A 135 9535 9309 7864 -1453 -445 97 A N ATOM 969 OD1 ASN A 135 50.283 -4.239 4.539 1.00 68.93 A O ANISOU 969 OD1 ASN A 135 9598 9037 7553 -1514 -315 42 A O ATOM 970 N GLY A 136 49.836 -8.023 1.977 1.00 59.03 A N ANISOU 970 N GLY A 136 7907 7791 6730 -1125 -375 114 A N ATOM 971 CA GLY A 136 49.060 -8.261 0.784 1.00 57.74 A C ANISOU 971 CA GLY A 136 7652 7607 6677 -1013 -307 42 A C ATOM 972 C GLY A 136 47.672 -8.800 1.109 1.00 63.56 A C ANISOU 972 C GLY A 136 8431 8283 7433 -1032 -218 9 A C ATOM 973 O GLY A 136 46.649 -8.299 0.607 1.00 64.57 A O ANISOU 973 O GLY A 136 8531 8411 7591 -1000 -119 -64 A O ATOM 974 N LEU A 137 47.615 -9.784 1.997 1.00 65.26 A N ANISOU 974 N LEU A 137 8711 8454 7628 -1089 -253 75 A N ATOM 975 CA LEU A 137 46.333 -10.325 2.430 1.00 66.39 A C ANISOU 975 CA LEU A 137 8892 8548 7784 -1138 -163 64 A C ATOM 976 C LEU A 137 45.439 -9.256 3.058 1.00 64.95 A C ANISOU 976 C LEU A 137 8775 8391 7512 -1199 -26 17 A C ATOM 977 O LEU A 137 44.246 -9.169 2.769 1.00 65.88 A O ANISOU 977 O LEU A 137 8843 8511 7678 -1183 81 -34 A O ATOM 978 CB LEU A 137 46.536 -11.498 3.371 1.00 64.87 A C ANISOU 978 CB LEU A 137 8782 8297 7565 -1203 -224 164 A C ATOM 979 CG LEU A 137 47.034 -12.759 2.654 1.00 60.43 A C ANISOU 979 CG LEU A 137 8165 7672 7121 -1116 -328 194 A C ATOM 980 CD1 LEU A 137 47.244 -13.894 3.656 1.00 58.84 A C ANISOU 980 CD1 LEU A 137 8071 7393 6892 -1175 -390 311 A C ATOM 981 CD2 LEU A 137 46.097 -13.182 1.519 1.00 56.76 A C ANISOU 981 CD2 LEU A 137 7613 7171 6781 -1060 -282 107 A C ATOM 982 N TYR A 138 46.020 -8.435 3.915 1.00 68.00 A N ANISOU 982 N TYR A 138 9273 8798 7766 -1267 -31 34 A N ATOM 983 CA TYR A 138 45.263 -7.383 4.569 1.00 70.96 A C ANISOU 983 CA TYR A 138 9744 9178 8038 -1311 105 -19 A C ATOM 984 C TYR A 138 44.617 -6.508 3.505 1.00 66.81 A C ANISOU 984 C TYR A 138 9127 8664 7590 -1208 191 -109 A C ATOM 985 O TYR A 138 43.460 -6.119 3.627 1.00 71.69 A O ANISOU 985 O TYR A 138 9742 9286 8208 -1185 331 -157 A O ATOM 986 CB TYR A 138 46.179 -6.537 5.452 1.00 68.54 A C ANISOU 986 CB TYR A 138 9586 8880 7575 -1399 56 -5 A C ATOM 987 CG TYR A 138 45.544 -5.247 5.908 1.00 63.42 A C ANISOU 987 CG TYR A 138 9058 8216 6823 -1417 196 -88 A C ATOM 988 CD1 TYR A 138 45.627 -4.093 5.127 1.00 65.46 A C ANISOU 988 CD1 TYR A 138 9298 8460 7112 -1355 225 -160 A C ATOM 989 CD2 TYR A 138 44.863 -5.173 7.119 1.00 64.44 A C ANISOU 989 CD2 TYR A 138 9333 8335 6815 -1488 308 -93 A C ATOM 990 CE1 TYR A 138 45.015 -2.914 5.527 1.00 63.23 A C ANISOU 990 CE1 TYR A 138 9146 8136 6741 -1349 360 -239 A C ATOM 991 CE2 TYR A 138 44.274 -3.977 7.548 1.00 59.10 A C ANISOU 991 CE2 TYR A 138 8785 7633 6037 -1480 453 -181 A C ATOM 992 CZ TYR A 138 44.330 -2.868 6.734 1.00 60.07 A C ANISOU 992 CZ TYR A 138 8891 7724 6208 -1403 478 -256 A C ATOM 993 OH TYR A 138 43.704 -1.699 7.119 1.00 79.38 A O ANISOU 993 OH TYR A 138 11476 10119 8563 -1371 628 -344 A O ATOM 994 N TYR A 139 45.380 -6.189 2.469 1.00 62.44 A N ANISOU 994 N TYR A 139 8496 8127 7101 -1140 109 -123 A N ATOM 995 CA TYR A 139 44.893 -5.350 1.385 1.00 58.80 A C ANISOU 995 CA TYR A 139 7958 7677 6704 -1038 170 -192 A C ATOM 996 C TYR A 139 43.753 -5.997 0.597 1.00 58.46 A C ANISOU 996 C TYR A 139 7781 7651 6779 -960 217 -222 A C ATOM 997 O TYR A 139 42.722 -5.365 0.369 1.00 52.14 A O ANISOU 997 O TYR A 139 6949 6864 5997 -904 325 -270 A O ATOM 998 CB TYR A 139 46.030 -4.978 0.426 1.00 57.70 A C ANISOU 998 CB TYR A 139 7762 7561 6598 -994 72 -182 A C ATOM 999 CG TYR A 139 45.535 -4.256 -0.798 1.00 52.13 A C ANISOU 999 CG TYR A 139 6980 6870 5957 -883 124 -236 A C ATOM 1000 CD1 TYR A 139 45.238 -2.898 -0.746 1.00 47.81 A C ANISOU 1000 CD1 TYR A 139 6515 6291 5358 -869 208 -273 A C ATOM 1001 CD2 TYR A 139 45.344 -4.927 -1.995 1.00 59.45 A C ANISOU 1001 CD2 TYR A 139 7771 7830 6986 -786 86 -249 A C ATOM 1002 CE1 TYR A 139 44.773 -2.219 -1.858 1.00 46.22 A C ANISOU 1002 CE1 TYR A 139 6253 6097 5211 -757 250 -305 A C ATOM 1003 CE2 TYR A 139 44.899 -4.248 -3.149 1.00 56.38 A C ANISOU 1003 CE2 TYR A 139 7318 7465 6639 -682 121 -288 A C ATOM 1004 CZ TYR A 139 44.616 -2.895 -3.065 1.00 52.83 A C ANISOU 1004 CZ TYR A 139 6943 6988 6142 -665 201 -307 A C ATOM 1005 OH TYR A 139 44.137 -2.200 -4.135 1.00 65.64 A O ANISOU 1005 OH TYR A 139 8514 8625 7798 -555 234 -330 A O ATOM 1006 N ILE A 140 43.928 -7.248 0.171 1.00 64.20 A N ANISOU 1006 N ILE A 140 8432 8375 7586 -953 131 -194 A N ATOM 1007 CA ILE A 140 42.895 -7.873 -0.659 1.00 54.49 A C ANISOU 1007 CA ILE A 140 7081 7158 6466 -901 150 -231 A C ATOM 1008 C ILE A 140 41.605 -8.056 0.142 1.00 54.05 A C ANISOU 1008 C ILE A 140 7023 7107 6404 -965 267 -228 A C ATOM 1009 O ILE A 140 40.517 -7.859 -0.379 1.00 49.44 A O ANISOU 1009 O ILE A 140 6334 6567 5883 -920 333 -268 A O ATOM 1010 CB ILE A 140 43.353 -9.193 -1.349 1.00 46.70 A C ANISOU 1010 CB ILE A 140 6040 6141 5563 -881 32 -219 A C ATOM 1011 CG1 ILE A 140 43.415 -10.341 -0.379 1.00 48.78 A C ANISOU 1011 CG1 ILE A 140 6372 6342 5820 -978 2 -153 A C ATOM 1012 CG2 ILE A 140 44.715 -9.055 -2.028 1.00 55.65 A C ANISOU 1012 CG2 ILE A 140 7166 7286 6691 -809 -62 -210 A C ATOM 1013 CD1 ILE A 140 43.678 -11.650 -1.087 1.00 57.33 A C ANISOU 1013 CD1 ILE A 140 7423 7365 6995 -945 -99 -153 A C ATOM 1014 N HIS A 141 41.732 -8.419 1.417 1.00 59.49 A N ANISOU 1014 N HIS A 141 7821 7767 7013 -1070 293 -172 A N ATOM 1015 CA HIS A 141 40.573 -8.610 2.266 1.00 51.73 A C ANISOU 1015 CA HIS A 141 6842 6802 6009 -1141 422 -156 A C ATOM 1016 C HIS A 141 39.825 -7.299 2.522 1.00 57.93 A C ANISOU 1016 C HIS A 141 7636 7634 6739 -1085 576 -208 A C ATOM 1017 O HIS A 141 38.598 -7.235 2.475 1.00 68.15 A O ANISOU 1017 O HIS A 141 8827 8983 8083 -1064 691 -224 A O ATOM 1018 CB HIS A 141 40.993 -9.223 3.584 1.00 50.67 A C ANISOU 1018 CB HIS A 141 6849 6628 5772 -1262 414 -76 A C ATOM 1019 CG HIS A 141 41.473 -10.627 3.467 1.00 61.08 A C ANISOU 1019 CG HIS A 141 8167 7884 7155 -1309 287 -11 A C ATOM 1020 CD2 HIS A 141 41.322 -11.545 2.481 1.00 63.59 A C ANISOU 1020 CD2 HIS A 141 8385 8167 7609 -1279 208 -24 A C ATOM 1021 ND1 HIS A 141 42.217 -11.235 4.455 1.00 73.46 A N ANISOU 1021 ND1 HIS A 141 9868 9405 8638 -1389 225 78 A N ATOM 1022 CE1 HIS A 141 42.519 -12.464 4.070 1.00 83.81 A C ANISOU 1022 CE1 HIS A 141 11158 10644 10040 -1392 117 123 A C ATOM 1023 NE2 HIS A 141 41.977 -12.682 2.881 1.00 68.03 A N ANISOU 1023 NE2 HIS A 141 9027 8645 8173 -1331 108 54 A N ATOM 1024 N ARG A 142 40.590 -6.260 2.812 1.00 59.84 A N ANISOU 1024 N ARG A 142 8002 7853 6880 -1063 577 -230 A N ATOM 1025 CA ARG A 142 40.059 -4.923 3.011 1.00 64.15 A C ANISOU 1025 CA ARG A 142 8599 8406 7367 -993 713 -288 A C ATOM 1026 C ARG A 142 39.236 -4.523 1.795 1.00 58.36 A C ANISOU 1026 C ARG A 142 7699 7717 6757 -857 745 -331 A C ATOM 1027 O ARG A 142 38.322 -3.722 1.893 1.00 68.83 A O ANISOU 1027 O ARG A 142 9004 9067 8078 -774 884 -366 A O ATOM 1028 CB ARG A 142 41.226 -3.971 3.224 1.00 64.38 A C ANISOU 1028 CB ARG A 142 8789 8380 7292 -1008 656 -306 A C ATOM 1029 CG ARG A 142 40.868 -2.547 3.513 1.00 63.23 A C ANISOU 1029 CG ARG A 142 8757 8198 7067 -946 785 -371 A C ATOM 1030 CD ARG A 142 42.129 -1.690 3.351 1.00 93.15 A C ANISOU 1030 CD ARG A 142 12673 11926 10793 -977 685 -384 A C ATOM 1031 NE ARG A 142 41.882 -0.297 3.701 1.00128.82 A N ANISOU 1031 NE ARG A 142 17351 16372 15223 -935 799 -451 A N ATOM 1032 CZ ARG A 142 42.814 0.520 4.184 1.00156.52 A C ANISOU 1032 CZ ARG A 142 21051 19804 18613 -1022 751 -472 A C ATOM 1033 NH1 ARG A 142 44.052 0.073 4.366 1.00166.72 A N1+ ANISOU 1033 NH1 ARG A 142 22364 21113 19869 -1153 588 -419 A N1+ ATOM 1034 NH2 ARG A 142 42.505 1.777 4.482 1.00165.72 A N ANISOU 1034 NH2 ARG A 142 22387 20877 19701 -978 863 -544 A N ATOM 1035 N ASN A 143 39.563 -5.108 0.648 1.00 56.67 A N ANISOU 1035 N ASN A 143 7368 7516 6647 -826 615 -327 A N ATOM 1036 CA ASN A 143 38.866 -4.834 -0.600 1.00 59.15 A C ANISOU 1036 CA ASN A 143 7526 7881 7065 -706 610 -361 A C ATOM 1037 C ASN A 143 37.856 -5.907 -0.943 1.00 63.74 A C ANISOU 1037 C ASN A 143 7940 8524 7754 -735 600 -351 A C ATOM 1038 O ASN A 143 37.433 -6.016 -2.091 1.00 71.25 A O ANISOU 1038 O ASN A 143 8755 9523 8793 -664 541 -374 A O ATOM 1039 CB ASN A 143 39.851 -4.704 -1.750 1.00 64.53 A C ANISOU 1039 CB ASN A 143 8197 8548 7774 -650 478 -370 A C ATOM 1040 CG ASN A 143 40.514 -3.356 -1.787 1.00 67.87 A C ANISOU 1040 CG ASN A 143 8735 8928 8122 -599 502 -383 A C ATOM 1041 ND2 ASN A 143 41.722 -3.251 -1.203 1.00 65.03 A N ANISOU 1041 ND2 ASN A 143 8507 8520 7682 -686 447 -360 A N ATOM 1042 OD1 ASN A 143 39.960 -2.425 -2.347 1.00 80.85 A O ANISOU 1042 OD1 ASN A 143 10352 10582 9784 -488 560 -407 A O ATOM 1043 N LYS A 144 37.477 -6.696 0.057 1.00 65.24 A N ANISOU 1043 N LYS A 144 8148 8711 7926 -853 653 -312 A N ATOM 1044 CA LYS A 144 36.395 -7.657 -0.083 1.00 72.95 A C ANISOU 1044 CA LYS A 144 8970 9744 9001 -916 666 -293 A C ATOM 1045 C LYS A 144 36.741 -8.760 -1.052 1.00 68.69 A C ANISOU 1045 C LYS A 144 8373 9173 8552 -952 498 -299 A C ATOM 1046 O LYS A 144 35.860 -9.263 -1.739 1.00 80.39 A O ANISOU 1046 O LYS A 144 9702 10709 10132 -966 468 -314 A O ATOM 1047 CB LYS A 144 35.107 -6.950 -0.525 1.00 79.59 A C ANISOU 1047 CB LYS A 144 9640 10693 9906 -815 768 -318 A C ATOM 1048 CG LYS A 144 34.625 -5.913 0.474 1.00 84.80 A C ANISOU 1048 CG LYS A 144 10361 11379 10481 -759 963 -318 A C ATOM 1049 CD LYS A 144 34.567 -6.557 1.846 1.00112.91 A C ANISOU 1049 CD LYS A 144 14015 14921 13962 -906 1052 -268 A C ATOM 1050 CE LYS A 144 34.649 -5.525 2.965 1.00113.15 A C ANISOU 1050 CE LYS A 144 14215 14929 13845 -865 1215 -285 A C ATOM 1051 NZ LYS A 144 34.998 -6.195 4.264 1.00111.83 A N1+ ANISOU 1051 NZ LYS A 144 14201 14726 13562 -1022 1253 -231 A N1+ ATOM 1052 N ILE A 145 38.007 -9.138 -1.138 1.00 57.08 A N ANISOU 1052 N ILE A 145 7021 7620 7047 -963 387 -292 A N ATOM 1053 CA ILE A 145 38.375 -10.243 -2.012 1.00 66.12 A C ANISOU 1053 CA ILE A 145 8136 8717 8267 -979 241 -306 A C ATOM 1054 C ILE A 145 38.984 -11.387 -1.224 1.00 69.55 A C ANISOU 1054 C ILE A 145 8686 9053 8687 -1089 190 -246 A C ATOM 1055 O ILE A 145 39.796 -11.147 -0.318 1.00 59.47 A O ANISOU 1055 O ILE A 145 7534 7742 7318 -1109 205 -198 A O ATOM 1056 CB ILE A 145 39.377 -9.794 -3.087 1.00 61.04 A C ANISOU 1056 CB ILE A 145 7509 8069 7613 -856 147 -349 A C ATOM 1057 CG1 ILE A 145 38.820 -8.623 -3.893 1.00 53.58 A C ANISOU 1057 CG1 ILE A 145 6472 7210 6673 -740 191 -393 A C ATOM 1058 CG2 ILE A 145 39.719 -10.953 -3.996 1.00 56.60 A C ANISOU 1058 CG2 ILE A 145 6932 7457 7117 -855 15 -378 A C ATOM 1059 CD1 ILE A 145 37.574 -8.949 -4.657 1.00 54.89 A C ANISOU 1059 CD1 ILE A 145 6479 7448 6928 -734 176 -426 A C ATOM 1060 N LEU A 146 38.572 -12.610 -1.559 1.00 60.68 A N ANISOU 1060 N LEU A 146 7528 7877 7650 -1165 122 -245 A N ATOM 1061 CA LEU A 146 39.162 -13.812 -0.991 1.00 55.05 A C ANISOU 1061 CA LEU A 146 6935 7041 6939 -1250 54 -184 A C ATOM 1062 C LEU A 146 40.021 -14.407 -2.084 1.00 63.81 A C ANISOU 1062 C LEU A 146 8068 8080 8096 -1160 -85 -235 A C ATOM 1063 O LEU A 146 39.572 -14.529 -3.235 1.00 69.20 A O ANISOU 1063 O LEU A 146 8663 8785 8842 -1119 -135 -314 A O ATOM 1064 CB LEU A 146 38.086 -14.822 -0.610 1.00 54.85 A C ANISOU 1064 CB LEU A 146 6879 6979 6982 -1409 81 -146 A C ATOM 1065 CG LEU A 146 37.078 -14.376 0.444 1.00 58.17 A C ANISOU 1065 CG LEU A 146 7252 7487 7363 -1504 243 -91 A C ATOM 1066 CD1 LEU A 146 36.117 -15.526 0.730 1.00 60.11 A C ANISOU 1066 CD1 LEU A 146 7459 7691 7687 -1684 256 -38 A C ATOM 1067 CD2 LEU A 146 37.746 -13.979 1.743 1.00 56.99 A C ANISOU 1067 CD2 LEU A 146 7251 7323 7078 -1519 313 -18 A C ATOM 1068 N HIS A 147 41.253 -14.764 -1.736 1.00 61.69 A N ANISOU 1068 N HIS A 147 7915 7736 7788 -1120 -148 -189 A N ATOM 1069 CA HIS A 147 42.165 -15.294 -2.735 1.00 57.98 A C ANISOU 1069 CA HIS A 147 7465 7208 7354 -1006 -259 -234 A C ATOM 1070 C HIS A 147 41.864 -16.756 -3.054 1.00 57.69 A C ANISOU 1070 C HIS A 147 7485 7030 7404 -1059 -335 -249 A C ATOM 1071 O HIS A 147 41.873 -17.163 -4.214 1.00 71.78 A O ANISOU 1071 O HIS A 147 9251 8784 9236 -992 -403 -339 A O ATOM 1072 CB HIS A 147 43.612 -15.139 -2.274 1.00 60.55 A C ANISOU 1072 CB HIS A 147 7866 7522 7618 -930 -299 -171 A C ATOM 1073 CG HIS A 147 44.606 -15.710 -3.237 1.00 56.89 A C ANISOU 1073 CG HIS A 147 7412 7012 7192 -792 -392 -207 A C ATOM 1074 CD2 HIS A 147 45.472 -15.115 -4.094 1.00 55.04 A C ANISOU 1074 CD2 HIS A 147 7123 6853 6937 -657 -412 -246 A C ATOM 1075 ND1 HIS A 147 44.771 -17.065 -3.405 1.00 62.53 A N ANISOU 1075 ND1 HIS A 147 8206 7581 7969 -779 -465 -205 A N ATOM 1076 CE1 HIS A 147 45.698 -17.286 -4.314 1.00 72.06 A C ANISOU 1076 CE1 HIS A 147 9407 8780 9190 -624 -520 -250 A C ATOM 1077 NE2 HIS A 147 46.149 -16.117 -4.745 1.00 67.47 A N ANISOU 1077 NE2 HIS A 147 8735 8343 8557 -552 -485 -270 A N ATOM 1078 N ARG A 148 41.627 -17.543 -2.013 1.00 57.76 A N ANISOU 1078 N ARG A 148 7582 6944 7420 -1185 -325 -161 A N ATOM 1079 CA ARG A 148 41.135 -18.921 -2.156 1.00 67.84 A C ANISOU 1079 CA ARG A 148 8929 8063 8782 -1281 -385 -162 A C ATOM 1080 C ARG A 148 42.133 -19.894 -2.767 1.00 73.35 A C ANISOU 1080 C ARG A 148 9741 8608 9517 -1164 -498 -189 A C ATOM 1081 O ARG A 148 41.793 -21.029 -3.098 1.00 79.68 A O ANISOU 1081 O ARG A 148 10626 9253 10393 -1223 -559 -216 A O ATOM 1082 CB ARG A 148 39.827 -18.943 -2.940 1.00 73.03 A C ANISOU 1082 CB ARG A 148 9470 8769 9508 -1369 -376 -249 A C ATOM 1083 CG ARG A 148 38.722 -18.136 -2.269 1.00 80.83 A C ANISOU 1083 CG ARG A 148 10333 9902 10475 -1479 -250 -209 A C ATOM 1084 CD ARG A 148 37.361 -18.616 -2.621 1.00 80.89 A C ANISOU 1084 CD ARG A 148 10238 9925 10571 -1631 -250 -240 A C ATOM 1085 NE ARG A 148 37.029 -18.533 -4.033 1.00 84.02 A N ANISOU 1085 NE ARG A 148 10540 10367 11014 -1572 -335 -363 A N ATOM 1086 CZ ARG A 148 35.831 -18.856 -4.511 1.00 86.17 A C ANISOU 1086 CZ ARG A 148 10695 10683 11363 -1702 -362 -401 A C ATOM 1087 NH1 ARG A 148 34.867 -19.206 -3.669 1.00 93.89 A N1+ ANISOU 1087 NH1 ARG A 148 11613 11676 12383 -1893 -288 -319 A N1+ ATOM 1088 NH2 ARG A 148 35.568 -18.775 -5.807 1.00 81.05 A N ANISOU 1088 NH2 ARG A 148 9973 10083 10737 -1648 -458 -514 A N ATOM 1089 N ASP A 149 43.380 -19.473 -2.911 1.00 81.28 A N ANISOU 1089 N ASP A 149 10753 9653 10474 -998 -522 -179 A N ATOM 1090 CA ASP A 149 44.385 -20.397 -3.409 1.00 77.56 A C ANISOU 1090 CA ASP A 149 10381 9049 10039 -858 -611 -193 A C ATOM 1091 C ASP A 149 45.769 -20.075 -2.849 1.00 73.78 A C ANISOU 1091 C ASP A 149 9912 8615 9504 -731 -628 -100 A C ATOM 1092 O ASP A 149 46.782 -20.123 -3.558 1.00 73.37 A O ANISOU 1092 O ASP A 149 9843 8576 9457 -553 -667 -133 A O ATOM 1093 CB ASP A 149 44.373 -20.427 -4.936 1.00 82.60 A C ANISOU 1093 CB ASP A 149 10979 9700 10706 -745 -646 -343 A C ATOM 1094 CG ASP A 149 45.004 -21.685 -5.503 1.00 85.21 A C ANISOU 1094 CG ASP A 149 11447 9840 11087 -631 -725 -386 A C ATOM 1095 OD1 ASP A 149 45.140 -22.685 -4.745 1.00 80.46 A O ANISOU 1095 OD1 ASP A 149 10981 9064 10525 -676 -761 -303 A O ATOM 1096 OD2 ASP A 149 45.364 -21.642 -6.699 1.00 78.81 A O1- ANISOU 1096 OD2 ASP A 149 10619 9055 10268 -490 -745 -500 A O1- ATOM 1097 N MET A 150 45.803 -19.806 -1.549 1.00 77.83 A N ANISOU 1097 N MET A 150 10454 9158 9960 -829 -601 22 A N ATOM 1098 CA MET A 150 47.081 -19.537 -0.869 1.00 71.37 A C ANISOU 1098 CA MET A 150 9645 8390 9079 -742 -641 127 A C ATOM 1099 C MET A 150 47.994 -20.745 -0.928 1.00 77.05 A C ANISOU 1099 C MET A 150 10461 8959 9855 -611 -734 181 A C ATOM 1100 O MET A 150 47.656 -21.818 -0.415 1.00 93.94 A O ANISOU 1100 O MET A 150 12736 10925 12032 -676 -765 243 A O ATOM 1101 CB MET A 150 46.825 -19.138 0.579 1.00 74.96 A C ANISOU 1101 CB MET A 150 10147 8889 9443 -892 -603 242 A C ATOM 1102 CG MET A 150 46.358 -17.693 0.762 1.00 80.23 A C ANISOU 1102 CG MET A 150 10725 9728 10031 -963 -510 200 A C ATOM 1103 SD MET A 150 47.768 -16.688 0.217 1.00 83.49 A S ANISOU 1103 SD MET A 150 11035 10282 10404 -810 -554 183 A S ATOM 1104 CE MET A 150 47.177 -16.150 -1.377 1.00102.43 A C ANISOU 1104 CE MET A 150 13316 12736 12864 -735 -502 23 A C ATOM 1105 N LYS A 151 49.153 -20.583 -1.554 1.00 78.11 A N ANISOU 1105 N LYS A 151 10526 9155 9995 -422 -772 166 A N ATOM 1106 CA LYS A 151 50.194 -21.615 -1.515 1.00 81.55 A C ANISOU 1106 CA LYS A 151 11031 9474 10479 -255 -854 237 A C ATOM 1107 C LYS A 151 51.524 -21.040 -1.963 1.00 82.14 A C ANISOU 1107 C LYS A 151 10966 9705 10536 -72 -873 250 A C ATOM 1108 O LYS A 151 51.567 -20.022 -2.681 1.00 85.71 A O ANISOU 1108 O LYS A 151 11291 10316 10959 -58 -820 168 A O ATOM 1109 CB LYS A 151 49.811 -22.839 -2.367 1.00 82.45 A C ANISOU 1109 CB LYS A 151 11265 9374 10688 -186 -873 143 A C ATOM 1110 CG LYS A 151 49.590 -22.535 -3.848 1.00 83.90 A C ANISOU 1110 CG LYS A 151 11376 9609 10890 -102 -833 -33 A C ATOM 1111 CD LYS A 151 49.007 -23.716 -4.577 1.00 74.40 A C ANISOU 1111 CD LYS A 151 10324 8184 9760 -89 -860 -140 A C ATOM 1112 CE LYS A 151 49.206 -23.631 -6.070 1.00 81.66 A C ANISOU 1112 CE LYS A 151 11205 9141 10680 64 -842 -304 A C ATOM 1113 NZ LYS A 151 48.244 -24.459 -6.848 1.00 96.09 A N1+ ANISOU 1113 NZ LYS A 151 13166 10793 12550 -5 -867 -445 A N1+ ATOM 1114 N ALA A 152 52.613 -21.702 -1.583 1.00 75.95 A N ANISOU 1114 N ALA A 152 10200 8880 9777 73 -948 362 A N ATOM 1115 CA ALA A 152 53.952 -21.244 -1.926 1.00 81.06 A C ANISOU 1115 CA ALA A 152 10687 9692 10417 247 -970 400 A C ATOM 1116 C ALA A 152 54.082 -20.885 -3.401 1.00 74.83 A C ANISOU 1116 C ALA A 152 9800 8980 9653 374 -898 252 A C ATOM 1117 O ALA A 152 54.729 -19.884 -3.738 1.00 77.97 A O ANISOU 1117 O ALA A 152 10032 9580 10010 404 -871 255 A O ATOM 1118 CB ALA A 152 54.989 -22.324 -1.580 1.00109.89 A C ANISOU 1118 CB ALA A 152 14378 13250 14125 441 -1057 522 A C ATOM 1119 N ALA A 153 53.505 -21.727 -4.262 1.00 72.46 A N ANISOU 1119 N ALA A 153 9609 8512 9407 441 -874 129 A N ATOM 1120 CA ALA A 153 53.681 -21.560 -5.701 1.00 66.08 A C ANISOU 1120 CA ALA A 153 8739 7762 8604 585 -812 -12 A C ATOM 1121 C ALA A 153 52.995 -20.302 -6.268 1.00 69.24 A C ANISOU 1121 C ALA A 153 9043 8321 8941 455 -744 -103 A C ATOM 1122 O ALA A 153 53.431 -19.760 -7.295 1.00 70.32 A O ANISOU 1122 O ALA A 153 9077 8588 9051 565 -691 -172 A O ATOM 1123 CB ALA A 153 53.267 -22.811 -6.444 1.00 56.51 A C ANISOU 1123 CB ALA A 153 7699 6320 7452 684 -817 -128 A C ATOM 1124 N ASN A 154 52.012 -19.797 -5.534 1.00 65.62 A N ANISOU 1124 N ASN A 154 8612 7864 8454 235 -741 -84 A N ATOM 1125 CA ASN A 154 51.287 -18.594 -5.888 1.00 62.42 A C ANISOU 1125 CA ASN A 154 8128 7593 7995 115 -680 -150 A C ATOM 1126 C ASN A 154 51.865 -17.319 -5.268 1.00 74.40 A C ANISOU 1126 C ASN A 154 9526 9292 9447 51 -664 -59 A C ATOM 1127 O ASN A 154 51.287 -16.230 -5.399 1.00 79.71 A O ANISOU 1127 O ASN A 154 10151 10061 10072 -50 -612 -97 A O ATOM 1128 CB ASN A 154 49.825 -18.732 -5.460 1.00 65.49 A C ANISOU 1128 CB ASN A 154 8603 7886 8393 -77 -671 -185 A C ATOM 1129 CG ASN A 154 49.051 -19.650 -6.366 1.00 74.58 A C ANISOU 1129 CG ASN A 154 9845 8896 9596 -59 -684 -310 A C ATOM 1130 ND2 ASN A 154 47.908 -20.118 -5.895 1.00 74.66 A N ANISOU 1130 ND2 ASN A 154 9935 8794 9637 -227 -693 -317 A N ATOM 1131 OD1 ASN A 154 49.480 -19.943 -7.487 1.00 85.34 A O ANISOU 1131 OD1 ASN A 154 11208 10253 10964 96 -684 -402 A O ATOM 1132 N VAL A 155 52.969 -17.447 -4.545 1.00 73.04 A N ANISOU 1132 N VAL A 155 9317 9161 9272 102 -718 64 A N ATOM 1133 CA VAL A 155 53.690 -16.299 -4.012 1.00 63.55 A C ANISOU 1133 CA VAL A 155 8004 8133 8007 37 -724 149 A C ATOM 1134 C VAL A 155 54.934 -16.047 -4.852 1.00 67.01 A C ANISOU 1134 C VAL A 155 8290 8710 8457 201 -715 164 A C ATOM 1135 O VAL A 155 55.807 -16.918 -4.967 1.00 72.62 A O ANISOU 1135 O VAL A 155 8971 9400 9219 368 -754 213 A O ATOM 1136 CB VAL A 155 54.077 -16.539 -2.537 1.00 59.24 A C ANISOU 1136 CB VAL A 155 7507 7569 7432 -48 -807 293 A C ATOM 1137 CG1 VAL A 155 54.887 -15.377 -1.979 1.00 57.32 A C ANISOU 1137 CG1 VAL A 155 7160 7503 7115 -132 -835 374 A C ATOM 1138 CG2 VAL A 155 52.828 -16.772 -1.710 1.00 58.05 A C ANISOU 1138 CG2 VAL A 155 7504 7294 7256 -214 -792 285 A C ATOM 1139 N LEU A 156 55.051 -14.849 -5.418 1.00 61.37 A N ANISOU 1139 N LEU A 156 7478 8141 7698 159 -657 133 A N ATOM 1140 CA LEU A 156 56.234 -14.515 -6.214 1.00 65.30 A C ANISOU 1140 CA LEU A 156 7815 8794 8200 290 -632 161 A C ATOM 1141 C LEU A 156 57.107 -13.495 -5.499 1.00 78.94 A C ANISOU 1141 C LEU A 156 9427 10681 9885 175 -671 279 A C ATOM 1142 O LEU A 156 56.629 -12.787 -4.599 1.00 80.36 A O ANISOU 1142 O LEU A 156 9673 10850 10010 -14 -696 302 A O ATOM 1143 CB LEU A 156 55.823 -13.957 -7.577 1.00 62.17 A C ANISOU 1143 CB LEU A 156 7393 8447 7778 336 -535 45 A C ATOM 1144 CG LEU A 156 54.861 -14.849 -8.355 1.00 60.54 A C ANISOU 1144 CG LEU A 156 7310 8096 7597 418 -510 -88 A C ATOM 1145 CD1 LEU A 156 54.423 -14.212 -9.638 1.00 62.35 A C ANISOU 1145 CD1 LEU A 156 7519 8391 7778 448 -432 -191 A C ATOM 1146 CD2 LEU A 156 55.456 -16.209 -8.576 1.00 61.06 A C ANISOU 1146 CD2 LEU A 156 7405 8071 7722 611 -535 -92 A C ATOM 1147 N ILE A 157 58.382 -13.402 -5.886 1.00 73.53 A N ANISOU 1147 N ILE A 157 8569 10147 9219 281 -675 353 A N ATOM 1148 CA ILE A 157 59.258 -12.366 -5.394 1.00 69.11 A C ANISOU 1148 CA ILE A 157 7877 9757 8622 153 -716 461 A C ATOM 1149 C ILE A 157 60.068 -11.762 -6.537 1.00 75.50 A C ANISOU 1149 C ILE A 157 8511 10739 9436 231 -634 467 A C ATOM 1150 O ILE A 157 60.687 -12.494 -7.288 1.00 78.97 A O ANISOU 1150 O ILE A 157 8854 11225 9924 441 -593 468 A O ATOM 1151 CB ILE A 157 60.207 -12.854 -4.291 1.00 70.51 A C ANISOU 1151 CB ILE A 157 7983 9987 8818 154 -845 607 A C ATOM 1152 CG1 ILE A 157 59.442 -13.613 -3.221 1.00 68.84 A C ANISOU 1152 CG1 ILE A 157 7959 9599 8596 101 -917 614 A C ATOM 1153 CG2 ILE A 157 60.894 -11.649 -3.662 1.00 64.59 A C ANISOU 1153 CG2 ILE A 157 7132 9397 8009 -47 -907 701 A C ATOM 1154 CD1 ILE A 157 60.327 -14.007 -2.065 1.00 59.79 A C ANISOU 1154 CD1 ILE A 157 6762 8509 7446 86 -1060 771 A C ATOM 1155 N THR A 158 60.106 -10.428 -6.613 1.00 77.71 A N ANISOU 1155 N THR A 158 8756 11110 9660 59 -606 481 A N ATOM 1156 CA THR A 158 60.799 -9.705 -7.671 1.00 74.37 A C ANISOU 1156 CA THR A 158 8180 10849 9228 90 -519 501 A C ATOM 1157 C THR A 158 62.295 -9.670 -7.464 1.00 77.58 A C ANISOU 1157 C THR A 158 8352 11455 9669 108 -567 647 A C ATOM 1158 O THR A 158 62.773 -9.922 -6.352 1.00 96.51 A O ANISOU 1158 O THR A 158 10714 13873 12082 43 -692 741 A O ATOM 1159 CB THR A 158 60.325 -8.236 -7.802 1.00 77.07 A C ANISOU 1159 CB THR A 158 8583 11197 9500 -112 -476 478 A C ATOM 1160 CG2 THR A 158 58.857 -8.192 -8.116 1.00 74.59 A C ANISOU 1160 CG2 THR A 158 8463 10718 9157 -110 -421 344 A C ATOM 1161 OG1 THR A 158 60.581 -7.515 -6.584 1.00 74.58 A O ANISOU 1161 OG1 THR A 158 8288 10895 9152 -334 -575 554 A O ATOM 1162 N ARG A 159 63.029 -9.350 -8.534 1.00 84.37 A N ANISOU 1162 N ARG A 159 9044 12475 10535 192 -468 674 A N ATOM 1163 CA ARG A 159 64.492 -9.322 -8.438 1.00 95.19 A C ANISOU 1163 CA ARG A 159 10146 14070 11950 218 -498 824 A C ATOM 1164 C ARG A 159 64.903 -8.372 -7.320 1.00 80.59 A C ANISOU 1164 C ARG A 159 8256 12289 10075 -65 -627 931 A C ATOM 1165 O ARG A 159 66.004 -8.497 -6.794 1.00 80.30 A O ANISOU 1165 O ARG A 159 8017 12413 10077 -82 -719 1066 A O ATOM 1166 CB ARG A 159 65.154 -8.953 -9.758 1.00109.53 A C ANISOU 1166 CB ARG A 159 11789 16063 13761 316 -350 844 A C ATOM 1167 CG ARG A 159 66.548 -9.578 -9.978 1.00126.04 A C ANISOU 1167 CG ARG A 159 13592 18372 15925 501 -333 965 A C ATOM 1168 CD ARG A 159 67.149 -9.203 -11.338 1.00117.96 A C ANISOU 1168 CD ARG A 159 12404 17534 14880 600 -155 982 A C ATOM 1169 NE ARG A 159 67.432 -7.773 -11.455 1.00125.58 A N ANISOU 1169 NE ARG A 159 13293 18619 15800 329 -135 1061 A N ATOM 1170 CZ ARG A 159 66.555 -6.862 -11.887 1.00141.16 A C ANISOU 1170 CZ ARG A 159 15454 20484 17694 181 -81 983 A C ATOM 1171 NH1 ARG A 159 65.338 -7.233 -12.271 1.00141.32 A N1+ ANISOU 1171 NH1 ARG A 159 15721 20301 17672 279 -43 826 A N1+ ATOM 1172 NH2 ARG A 159 66.886 -5.576 -11.931 1.00136.26 A N ANISOU 1172 NH2 ARG A 159 14777 19954 17040 -66 -70 1068 A N ATOM 1173 N ASP A 160 64.012 -7.468 -6.923 1.00 72.08 A N ANISOU 1173 N ASP A 160 7376 11084 8928 -280 -641 867 A N ATOM 1174 CA ASP A 160 64.344 -6.503 -5.885 1.00 76.53 A C ANISOU 1174 CA ASP A 160 7945 11685 9445 -561 -758 943 A C ATOM 1175 C ASP A 160 63.785 -6.866 -4.505 1.00 83.92 A C ANISOU 1175 C ASP A 160 9058 12482 10345 -649 -890 927 A C ATOM 1176 O ASP A 160 63.812 -6.039 -3.584 1.00 77.02 A O ANISOU 1176 O ASP A 160 8263 11597 9404 -892 -982 955 A O ATOM 1177 CB ASP A 160 63.891 -5.103 -6.281 1.00 89.34 A C ANISOU 1177 CB ASP A 160 9675 13266 11005 -756 -686 899 A C ATOM 1178 CG ASP A 160 64.459 -4.663 -7.595 1.00113.46 A C ANISOU 1178 CG ASP A 160 12569 16463 14077 -698 -556 934 A C ATOM 1179 OD1 ASP A 160 64.993 -5.517 -8.332 1.00136.14 A O ANISOU 1179 OD1 ASP A 160 15276 19447 17003 -470 -492 957 A O ATOM 1180 OD2 ASP A 160 64.381 -3.446 -7.897 1.00129.66 A O1- ANISOU 1180 OD2 ASP A 160 14671 18509 16082 -878 -511 941 A O1- ATOM 1181 N GLY A 161 63.287 -8.090 -4.374 1.00 82.84 A N ANISOU 1181 N GLY A 161 8996 12234 10243 -460 -894 883 A N ATOM 1182 CA GLY A 161 62.872 -8.593 -3.074 1.00 76.40 A C ANISOU 1182 CA GLY A 161 8329 11306 9394 -523 -1014 895 A C ATOM 1183 C GLY A 161 61.509 -8.124 -2.635 1.00 70.85 A C ANISOU 1183 C GLY A 161 7891 10413 8614 -655 -977 779 A C ATOM 1184 O GLY A 161 61.212 -8.067 -1.447 1.00 82.85 A O ANISOU 1184 O GLY A 161 9544 11867 10066 -792 -1066 796 A O ATOM 1185 N VAL A 162 60.664 -7.764 -3.590 1.00 62.31 A N ANISOU 1185 N VAL A 162 6885 9254 7536 -611 -840 665 A N ATOM 1186 CA VAL A 162 59.263 -7.465 -3.268 1.00 56.21 A C ANISOU 1186 CA VAL A 162 6341 8306 6710 -688 -789 553 A C ATOM 1187 C VAL A 162 58.381 -8.684 -3.539 1.00 60.69 A C ANISOU 1187 C VAL A 162 6988 8743 7326 -516 -748 479 A C ATOM 1188 O VAL A 162 58.335 -9.181 -4.649 1.00 69.66 A O ANISOU 1188 O VAL A 162 8063 9885 8519 -346 -677 431 A O ATOM 1189 CB VAL A 162 58.751 -6.252 -4.058 1.00 52.62 A C ANISOU 1189 CB VAL A 162 5933 7834 6223 -757 -680 481 A C ATOM 1190 CG1 VAL A 162 57.335 -5.915 -3.638 1.00 48.43 A C ANISOU 1190 CG1 VAL A 162 5616 7141 5644 -822 -629 379 A C ATOM 1191 CG2 VAL A 162 59.669 -5.057 -3.859 1.00 54.24 A C ANISOU 1191 CG2 VAL A 162 6071 8150 6387 -943 -721 559 A C ATOM 1192 N LEU A 163 57.684 -9.166 -2.525 1.00 65.40 A N ANISOU 1192 N LEU A 163 7731 9222 7894 -571 -792 469 A N ATOM 1193 CA LEU A 163 56.752 -10.306 -2.629 1.00 68.34 A C ANISOU 1193 CA LEU A 163 8201 9452 8312 -457 -761 405 A C ATOM 1194 C LEU A 163 55.406 -9.895 -3.244 1.00 71.18 A C ANISOU 1194 C LEU A 163 8659 9720 8664 -472 -649 276 A C ATOM 1195 O LEU A 163 54.849 -8.841 -2.909 1.00 69.00 A O ANISOU 1195 O LEU A 163 8460 9432 8324 -607 -609 244 A O ATOM 1196 CB LEU A 163 56.528 -10.902 -1.240 1.00 70.00 A C ANISOU 1196 CB LEU A 163 8530 9584 8483 -539 -846 466 A C ATOM 1197 CG LEU A 163 55.554 -12.068 -1.104 1.00 69.23 A C ANISOU 1197 CG LEU A 163 8553 9325 8425 -473 -825 424 A C ATOM 1198 CD1 LEU A 163 55.943 -12.973 0.059 1.00 84.72 A C ANISOU 1198 CD1 LEU A 163 10573 11244 10370 -485 -936 540 A C ATOM 1199 CD2 LEU A 163 54.135 -11.543 -0.936 1.00 63.39 A C ANISOU 1199 CD2 LEU A 163 7944 8499 7642 -588 -732 327 A C ATOM 1200 N LYS A 164 54.904 -10.717 -4.168 1.00 64.06 A N ANISOU 1200 N LYS A 164 7756 8755 7826 -326 -602 202 A N ATOM 1201 CA LYS A 164 53.636 -10.460 -4.837 1.00 61.63 A C ANISOU 1201 CA LYS A 164 7517 8379 7519 -326 -516 87 A C ATOM 1202 C LYS A 164 52.745 -11.668 -4.751 1.00 69.54 A C ANISOU 1202 C LYS A 164 8605 9245 8569 -282 -524 37 A C ATOM 1203 O LYS A 164 53.160 -12.786 -5.121 1.00 68.65 A O ANISOU 1203 O LYS A 164 8479 9091 8514 -153 -559 39 A O ATOM 1204 CB LYS A 164 53.838 -10.151 -6.323 1.00 58.27 A C ANISOU 1204 CB LYS A 164 7004 8027 7108 -207 -455 31 A C ATOM 1205 CG LYS A 164 54.941 -9.184 -6.648 1.00 56.38 A C ANISOU 1205 CG LYS A 164 6651 7931 6839 -225 -444 98 A C ATOM 1206 CD LYS A 164 54.500 -7.751 -6.439 1.00 62.94 A C ANISOU 1206 CD LYS A 164 7535 8771 7608 -373 -403 91 A C ATOM 1207 CE LYS A 164 55.520 -6.802 -7.038 1.00 75.16 A C ANISOU 1207 CE LYS A 164 8975 10449 9132 -395 -380 151 A C ATOM 1208 NZ LYS A 164 55.146 -5.390 -6.710 1.00 87.30 A N1+ ANISOU 1208 NZ LYS A 164 10598 11960 10610 -552 -350 150 A N1+ ATOM 1209 N LEU A 165 51.500 -11.450 -4.312 1.00 64.78 A N ANISOU 1209 N LEU A 165 8094 8571 7948 -386 -484 -9 A N ATOM 1210 CA LEU A 165 50.484 -12.479 -4.380 1.00 69.09 A C ANISOU 1210 CA LEU A 165 8709 8997 8545 -376 -480 -65 A C ATOM 1211 C LEU A 165 50.003 -12.614 -5.824 1.00 69.70 A C ANISOU 1211 C LEU A 165 8747 9077 8659 -272 -446 -173 A C ATOM 1212 O LEU A 165 49.740 -11.627 -6.502 1.00 68.65 A O ANISOU 1212 O LEU A 165 8568 9020 8495 -267 -394 -216 A O ATOM 1213 CB LEU A 165 49.297 -12.134 -3.469 1.00 67.39 A C ANISOU 1213 CB LEU A 165 8571 8735 8296 -523 -433 -72 A C ATOM 1214 CG LEU A 165 49.607 -12.031 -1.983 1.00 71.28 A C ANISOU 1214 CG LEU A 165 9139 9220 8724 -639 -460 23 A C ATOM 1215 CD1 LEU A 165 48.402 -11.531 -1.180 1.00 71.84 A C ANISOU 1215 CD1 LEU A 165 9284 9265 8744 -768 -379 3 A C ATOM 1216 CD2 LEU A 165 50.005 -13.428 -1.524 1.00 74.04 A C ANISOU 1216 CD2 LEU A 165 9536 9479 9115 -606 -539 91 A C ATOM 1217 N ALA A 166 49.897 -13.851 -6.288 1.00 59.71 A N ANISOU 1217 N ALA A 166 7517 7717 7451 -190 -481 -216 A N ATOM 1218 CA ALA A 166 49.646 -14.114 -7.694 1.00 56.91 A C ANISOU 1218 CA ALA A 166 7144 7366 7113 -80 -468 -323 A C ATOM 1219 C ALA A 166 48.529 -15.137 -7.853 1.00 66.05 A C ANISOU 1219 C ALA A 166 8385 8387 8320 -121 -495 -400 A C ATOM 1220 O ALA A 166 48.038 -15.704 -6.866 1.00 72.79 A O ANISOU 1220 O ALA A 166 9308 9143 9206 -228 -515 -356 A O ATOM 1221 CB ALA A 166 50.926 -14.630 -8.347 1.00 59.38 A C ANISOU 1221 CB ALA A 166 7420 7707 7435 91 -484 -314 A C ATOM 1222 N ASP A 167 48.116 -15.374 -9.098 1.00 65.21 A N ANISOU 1222 N ASP A 167 8281 8279 8214 -50 -498 -511 A N ATOM 1223 CA ASP A 167 47.072 -16.325 -9.405 1.00 67.42 A C ANISOU 1223 CA ASP A 167 8637 8438 8540 -104 -540 -597 A C ATOM 1224 C ASP A 167 45.740 -16.054 -8.735 1.00 73.74 A C ANISOU 1224 C ASP A 167 9423 9231 9363 -282 -526 -585 A C ATOM 1225 O ASP A 167 45.376 -16.717 -7.760 1.00 79.99 A O ANISOU 1225 O ASP A 167 10275 9918 10198 -391 -540 -533 A O ATOM 1226 CB ASP A 167 47.542 -17.697 -9.040 1.00 78.84 A C ANISOU 1226 CB ASP A 167 10196 9717 10041 -64 -592 -582 A C ATOM 1227 CG ASP A 167 46.952 -18.769 -9.931 1.00 96.32 A C ANISOU 1227 CG ASP A 167 12512 11799 12287 -47 -644 -709 A C ATOM 1228 OD1 ASP A 167 45.791 -18.612 -10.382 1.00 78.45 A O ANISOU 1228 OD1 ASP A 167 10230 9553 10021 -152 -659 -783 A O ATOM 1229 OD2 ASP A 167 47.667 -19.765 -10.159 1.00110.30 A O1- ANISOU 1229 OD2 ASP A 167 14381 13446 14081 74 -674 -731 A O1- ATOM 1230 N PHE A 168 44.989 -15.096 -9.282 1.00 68.76 A N ANISOU 1230 N PHE A 168 8709 8714 8701 -305 -493 -626 A N ATOM 1231 CA PHE A 168 43.661 -14.795 -8.736 1.00 70.36 A C ANISOU 1231 CA PHE A 168 8868 8933 8930 -449 -467 -617 A C ATOM 1232 C PHE A 168 42.541 -15.560 -9.439 1.00 68.95 A C ANISOU 1232 C PHE A 168 8688 8709 8798 -514 -527 -708 A C ATOM 1233 O PHE A 168 41.387 -15.196 -9.371 1.00 78.87 A O ANISOU 1233 O PHE A 168 9862 10026 10076 -606 -511 -714 A O ATOM 1234 CB PHE A 168 43.449 -13.299 -8.686 1.00 61.31 A C ANISOU 1234 CB PHE A 168 7635 7925 7735 -438 -394 -588 A C ATOM 1235 CG PHE A 168 44.199 -12.637 -7.552 1.00 71.45 A C ANISOU 1235 CG PHE A 168 8941 9224 8982 -461 -339 -490 A C ATOM 1236 CD1 PHE A 168 45.571 -12.431 -7.619 1.00 68.85 A C ANISOU 1236 CD1 PHE A 168 8627 8916 8614 -376 -350 -451 A C ATOM 1237 CD2 PHE A 168 43.520 -12.243 -6.399 1.00 65.62 A C ANISOU 1237 CD2 PHE A 168 8206 8487 8240 -574 -276 -438 A C ATOM 1238 CE1 PHE A 168 46.261 -11.846 -6.559 1.00 67.58 A C ANISOU 1238 CE1 PHE A 168 8488 8775 8414 -422 -323 -363 A C ATOM 1239 CE2 PHE A 168 44.200 -11.656 -5.339 1.00 51.69 A C ANISOU 1239 CE2 PHE A 168 6488 6731 6421 -608 -238 -361 A C ATOM 1240 CZ PHE A 168 45.568 -11.413 -5.428 1.00 51.75 A C ANISOU 1240 CZ PHE A 168 6511 6759 6389 -541 -271 -324 A C ATOM 1241 N GLY A 169 42.914 -16.683 -10.033 1.00 64.43 A N ANISOU 1241 N GLY A 169 8212 8022 8245 -469 -600 -774 A N ATOM 1242 CA GLY A 169 42.004 -17.451 -10.869 1.00 63.22 A C ANISOU 1242 CA GLY A 169 8084 7816 8121 -531 -681 -881 A C ATOM 1243 C GLY A 169 40.883 -18.115 -10.114 1.00 72.70 A C ANISOU 1243 C GLY A 169 9283 8936 9402 -733 -700 -855 A C ATOM 1244 O GLY A 169 39.807 -18.377 -10.664 1.00 99.74 A O ANISOU 1244 O GLY A 169 12662 12377 12855 -835 -759 -922 A O ATOM 1245 N LEU A 170 41.092 -18.343 -8.827 1.00 74.67 A N ANISOU 1245 N LEU A 170 9573 9115 9683 -805 -651 -747 A N ATOM 1246 CA LEU A 170 40.018 -18.900 -8.001 1.00 86.27 A C ANISOU 1246 CA LEU A 170 11032 10524 11221 -1011 -644 -698 A C ATOM 1247 C LEU A 170 39.472 -17.830 -7.071 1.00 82.39 A C ANISOU 1247 C LEU A 170 10416 10175 10711 -1072 -533 -608 A C ATOM 1248 O LEU A 170 38.597 -18.113 -6.246 1.00 82.91 A O ANISOU 1248 O LEU A 170 10452 10229 10821 -1235 -491 -548 A O ATOM 1249 CB LEU A 170 40.505 -20.086 -7.191 1.00 99.02 A C ANISOU 1249 CB LEU A 170 12810 11936 12876 -1066 -669 -636 A C ATOM 1250 CG LEU A 170 40.703 -21.460 -7.823 1.00 93.78 A C ANISOU 1250 CG LEU A 170 12309 11063 12259 -1064 -773 -715 A C ATOM 1251 CD1 LEU A 170 40.587 -22.549 -6.752 1.00 87.79 A C ANISOU 1251 CD1 LEU A 170 11685 10108 11561 -1205 -782 -618 A C ATOM 1252 CD2 LEU A 170 39.680 -21.694 -8.932 1.00109.66 A C ANISOU 1252 CD2 LEU A 170 14277 13095 14293 -1150 -850 -845 A C ATOM 1253 N ALA A 171 40.037 -16.624 -7.151 1.00 73.28 A N ANISOU 1253 N ALA A 171 9206 9147 9489 -942 -475 -594 A N ATOM 1254 CA ALA A 171 39.592 -15.576 -6.255 1.00 65.84 A C ANISOU 1254 CA ALA A 171 8181 8316 8519 -981 -363 -522 A C ATOM 1255 C ALA A 171 38.145 -15.147 -6.534 1.00 64.90 A C ANISOU 1255 C ALA A 171 7906 8312 8438 -1053 -331 -548 A C ATOM 1256 O ALA A 171 37.574 -15.439 -7.580 1.00 71.64 A O ANISOU 1256 O ALA A 171 8699 9193 9328 -1057 -412 -626 A O ATOM 1257 CB ALA A 171 40.513 -14.394 -6.306 1.00 68.98 A C ANISOU 1257 CB ALA A 171 8575 8796 8838 -842 -318 -506 A C ATOM 1258 N ARG A 172 37.559 -14.474 -5.569 1.00 73.95 A N ANISOU 1258 N ARG A 172 8990 9533 9573 -1106 -214 -480 A N ATOM 1259 CA ARG A 172 36.147 -14.147 -5.616 1.00 68.00 A C ANISOU 1259 CA ARG A 172 8069 8898 8869 -1175 -163 -481 A C ATOM 1260 C ARG A 172 35.896 -13.004 -4.615 1.00 80.39 A C ANISOU 1260 C ARG A 172 9601 10557 10387 -1144 -4 -418 A C ATOM 1261 O ARG A 172 36.501 -12.949 -3.528 1.00 63.91 A O ANISOU 1261 O ARG A 172 7630 8411 8239 -1171 63 -358 A O ATOM 1262 CB ARG A 172 35.351 -15.389 -5.205 1.00 66.25 A C ANISOU 1262 CB ARG A 172 7835 8608 8728 -1375 -187 -454 A C ATOM 1263 CG ARG A 172 34.169 -15.084 -4.314 1.00 74.69 A C ANISOU 1263 CG ARG A 172 8767 9783 9825 -1484 -55 -383 A C ATOM 1264 CD ARG A 172 33.378 -16.310 -3.964 1.00 87.27 A C ANISOU 1264 CD ARG A 172 10338 11316 11502 -1706 -78 -344 A C ATOM 1265 NE ARG A 172 31.980 -15.987 -3.720 1.00102.56 A N ANISOU 1265 NE ARG A 172 12053 13418 13495 -1796 15 -305 A N ATOM 1266 CZ ARG A 172 31.067 -15.792 -4.673 1.00 98.74 A C ANISOU 1266 CZ ARG A 172 11371 13066 13080 -1796 -48 -356 A C ATOM 1267 NH1 ARG A 172 31.414 -15.844 -5.948 1.00106.77 A N1+ ANISOU 1267 NH1 ARG A 172 12407 14063 14096 -1711 -204 -454 A N1+ ATOM 1268 NH2 ARG A 172 29.817 -15.520 -4.362 1.00107.13 A N ANISOU 1268 NH2 ARG A 172 12209 14293 14202 -1873 45 -304 A N ATOM 1269 N ALA A 173 35.013 -12.083 -4.987 1.00 80.22 A N ANISOU 1269 N ALA A 173 9425 10673 10380 -1078 51 -434 A N ATOM 1270 CA ALA A 173 34.558 -11.049 -4.042 1.00 62.10 A C ANISOU 1270 CA ALA A 173 7094 8455 8044 -1044 219 -385 A C ATOM 1271 C ALA A 173 33.671 -11.659 -2.957 1.00 66.85 A C ANISOU 1271 C ALA A 173 7645 9075 8679 -1205 321 -320 A C ATOM 1272 O ALA A 173 32.981 -12.645 -3.196 1.00 71.62 A O ANISOU 1272 O ALA A 173 8160 9681 9368 -1339 262 -314 A O ATOM 1273 CB ALA A 173 33.826 -9.955 -4.772 1.00 55.09 A C ANISOU 1273 CB ALA A 173 6055 7700 7174 -907 251 -413 A C ATOM 1274 N PHE A 174 33.702 -11.102 -1.756 1.00 73.54 A N ANISOU 1274 N PHE A 174 8560 9930 9450 -1207 473 -269 A N ATOM 1275 CA PHE A 174 32.838 -11.571 -0.687 1.00 74.04 A C ANISOU 1275 CA PHE A 174 8575 10031 9523 -1350 600 -198 A C ATOM 1276 C PHE A 174 32.124 -10.399 -0.019 1.00 82.62 A C ANISOU 1276 C PHE A 174 9593 11238 10562 -1260 799 -184 A C ATOM 1277 O PHE A 174 32.471 -9.239 -0.252 1.00 84.96 A O ANISOU 1277 O PHE A 174 9930 11547 10804 -1093 831 -228 A O ATOM 1278 CB PHE A 174 33.613 -12.407 0.341 1.00 67.81 A C ANISOU 1278 CB PHE A 174 7987 9111 8667 -1477 595 -134 A C ATOM 1279 CG PHE A 174 34.485 -11.585 1.264 1.00 71.89 A C ANISOU 1279 CG PHE A 174 8682 9592 9037 -1408 674 -119 A C ATOM 1280 CD1 PHE A 174 33.954 -11.034 2.432 1.00 70.85 A C ANISOU 1280 CD1 PHE A 174 8575 9525 8818 -1430 863 -78 A C ATOM 1281 CD2 PHE A 174 35.797 -11.288 0.929 1.00 69.84 A C ANISOU 1281 CD2 PHE A 174 8558 9252 8724 -1318 565 -152 A C ATOM 1282 CE1 PHE A 174 34.739 -10.242 3.263 1.00 70.58 A C ANISOU 1282 CE1 PHE A 174 8725 9455 8634 -1378 923 -79 A C ATOM 1283 CE2 PHE A 174 36.604 -10.529 1.777 1.00 71.51 A C ANISOU 1283 CE2 PHE A 174 8930 9438 8801 -1282 617 -138 A C ATOM 1284 CZ PHE A 174 36.084 -10.056 2.975 1.00 72.16 A C ANISOU 1284 CZ PHE A 174 9064 9565 8786 -1323 787 -104 A C ATOM 1285 N SER A 175 31.170 -10.714 0.850 1.00 95.38 A N ANISOU 1285 N SER A 175 11121 12928 12189 -1370 943 -120 A N ATOM 1286 CA SER A 175 30.361 -9.684 1.498 1.00103.67 A C ANISOU 1286 CA SER A 175 12089 14103 13197 -1272 1158 -108 A C ATOM 1287 C SER A 175 29.846 -10.107 2.862 1.00108.24 A C ANISOU 1287 C SER A 175 12693 14716 13715 -1411 1337 -26 A C ATOM 1288 O SER A 175 30.048 -11.245 3.317 1.00100.98 A O ANISOU 1288 O SER A 175 11848 13723 12794 -1600 1289 36 A O ATOM 1289 CB SER A 175 29.219 -9.269 0.601 1.00 96.57 A C ANISOU 1289 CB SER A 175 10907 13362 12420 -1178 1167 -126 A C ATOM 1290 OG SER A 175 28.476 -10.411 0.231 1.00112.12 A O ANISOU 1290 OG SER A 175 12698 15388 14512 -1355 1087 -87 A O ATOM 1291 N LEU A 176 29.283 -9.156 3.584 1.00125.90 A N ANISOU 1291 N LEU A 176 14907 17047 15881 -1306 1552 -25 A N ATOM 1292 CA LEU A 176 29.200 -9.353 5.042 1.00148.74 A C ANISOU 1292 CA LEU A 176 17931 19941 18643 -1410 1732 39 A C ATOM 1293 C LEU A 176 27.808 -9.662 5.482 1.00157.36 A C ANISOU 1293 C LEU A 176 18789 21204 19797 -1488 1917 112 A C ATOM 1294 O LEU A 176 26.858 -8.921 5.199 1.00144.27 A O ANISOU 1294 O LEU A 176 16916 19697 18203 -1348 2040 93 A O ATOM 1295 CB LEU A 176 29.828 -8.190 5.788 1.00157.24 A C ANISOU 1295 CB LEU A 176 19238 20963 19541 -1271 1846 -14 A C ATOM 1296 CG LEU A 176 31.372 -8.154 5.873 1.00160.51 A C ANISOU 1296 CG LEU A 176 19934 21205 19847 -1285 1683 -46 A C ATOM 1297 CD1 LEU A 176 32.094 -8.253 4.523 1.00160.53 A C ANISOU 1297 CD1 LEU A 176 19901 21135 19957 -1230 1446 -95 A C ATOM 1298 CD2 LEU A 176 31.811 -6.889 6.591 1.00137.01 A C ANISOU 1298 CD2 LEU A 176 17166 18192 16700 -1162 1803 -107 A C ATOM 1299 N ALA A 177 27.682 -10.811 6.151 1.00170.42 A N ANISOU 1299 N ALA A 177 20474 22836 21440 -1718 1932 208 A N ATOM 1300 CA ALA A 177 26.391 -11.454 6.418 1.00173.32 A C ANISOU 1300 CA ALA A 177 20590 23359 21901 -1867 2062 302 A C ATOM 1301 C ALA A 177 25.616 -11.656 5.084 1.00169.81 A C ANISOU 1301 C ALA A 177 19831 23018 21670 -1863 1928 280 A C ATOM 1302 O ALA A 177 26.190 -12.237 4.142 1.00163.15 A O ANISOU 1302 O ALA A 177 19027 22056 20904 -1914 1682 240 A O ATOM 1303 CB ALA A 177 25.609 -10.682 7.476 1.00155.84 A C ANISOU 1303 CB ALA A 177 18328 21301 19582 -1783 2376 332 A C ATOM 1304 N LYS A 178 24.375 -11.168 4.967 1.00174.14 A N ANISOU 1304 N LYS A 178 20076 23784 22304 -1790 2079 301 A N ATOM 1305 CA LYS A 178 23.691 -10.390 6.018 1.00186.27 A C ANISOU 1305 CA LYS A 178 21561 25466 23746 -1684 2391 335 A C ATOM 1306 C LYS A 178 22.231 -10.809 6.193 1.00192.33 A C ANISOU 1306 C LYS A 178 21967 26474 24636 -1800 2546 439 A C ATOM 1307 O LYS A 178 21.667 -11.473 5.340 1.00195.54 A O ANISOU 1307 O LYS A 178 22127 26952 25215 -1929 2396 468 A O ATOM 1308 CB LYS A 178 23.779 -8.868 5.765 1.00174.63 A C ANISOU 1308 CB LYS A 178 20110 24019 22223 -1356 2471 235 A C ATOM 1309 CG LYS A 178 23.309 -8.062 6.977 1.00169.56 A C ANISOU 1309 CG LYS A 178 19515 23470 21439 -1231 2800 246 A C ATOM 1310 CD LYS A 178 23.248 -6.551 6.866 1.00155.10 A C ANISOU 1310 CD LYS A 178 17719 21654 19557 -904 2921 152 A C ATOM 1311 CE LYS A 178 22.752 -6.042 8.219 1.00157.05 A C ANISOU 1311 CE LYS A 178 18039 21985 19646 -833 3262 169 A C ATOM 1312 NZ LYS A 178 22.619 -4.571 8.358 1.00155.96 A N1+ ANISOU 1312 NZ LYS A 178 17980 21845 19433 -511 3436 75 A N1+ ATOM 1313 N ASN A 179 21.627 -10.402 7.308 1.00194.70 A N ANISOU 1313 N ASN A 179 22236 26904 24837 -1757 2852 492 A N ATOM 1314 CA ASN A 179 20.222 -10.671 7.604 1.00208.55 A C ANISOU 1314 CA ASN A 179 23627 28918 26692 -1845 3051 602 A C ATOM 1315 C ASN A 179 20.040 -12.067 8.184 1.00214.35 A C ANISOU 1315 C ASN A 179 24367 29636 27439 -2208 3052 733 A C ATOM 1316 O ASN A 179 18.904 -12.527 8.321 1.00219.28 A O ANISOU 1316 O ASN A 179 24672 30469 28174 -2355 3174 843 A O ATOM 1317 CB ASN A 179 19.320 -10.481 6.366 1.00205.87 A C ANISOU 1317 CB ASN A 179 22884 28759 26577 -1767 2936 594 A C ATOM 1318 CG ASN A 179 19.253 -9.036 5.887 1.00212.26 A C ANISOU 1318 CG ASN A 179 23645 29620 27381 -1390 2988 496 A C ATOM 1319 ND2 ASN A 179 18.949 -8.872 4.612 1.00208.21 A N ANISOU 1319 ND2 ASN A 179 22907 29174 27029 -1308 2785 465 A N ATOM 1320 OD1 ASN A 179 19.467 -8.083 6.644 1.00224.36 A O ANISOU 1320 OD1 ASN A 179 25357 31126 28762 -1177 3202 449 A O ATOM 1321 N SER A 180 21.155 -12.726 8.529 1.00204.85 A N ANISOU 1321 N SER A 180 23521 28187 26124 -2348 2916 733 A N ATOM 1322 CA SER A 180 21.159 -14.106 9.032 1.00193.46 A C ANISOU 1322 CA SER A 180 22151 26668 24687 -2689 2879 860 A C ATOM 1323 C SER A 180 20.857 -15.126 7.910 1.00195.11 A C ANISOU 1323 C SER A 180 22169 26843 25118 -2901 2615 880 A C ATOM 1324 O SER A 180 20.553 -16.302 8.154 1.00202.55 A O ANISOU 1324 O SER A 180 23090 27750 26120 -3206 2584 994 A O ATOM 1325 CB SER A 180 20.202 -14.247 10.205 1.00172.35 A C ANISOU 1325 CB SER A 180 19350 24188 21945 -2804 3207 997 A C ATOM 1326 OG SER A 180 18.888 -13.993 9.780 1.00188.37 A O ANISOU 1326 OG SER A 180 20937 26493 24141 -2777 3322 1032 A O ATOM 1327 N GLN A 181 20.991 -14.656 6.671 1.00185.35 A N ANISOU 1327 N GLN A 181 20828 25604 23993 -2738 2416 763 A N ATOM 1328 CA GLN A 181 21.064 -15.533 5.504 1.00171.19 A C ANISOU 1328 CA GLN A 181 18967 23716 22362 -2898 2114 734 A C ATOM 1329 C GLN A 181 22.528 -15.701 5.128 1.00168.50 A C ANISOU 1329 C GLN A 181 18992 23088 21941 -2831 1890 638 A C ATOM 1330 O GLN A 181 23.219 -14.713 4.763 1.00174.22 A O ANISOU 1330 O GLN A 181 19828 23771 22597 -2562 1850 527 A O ATOM 1331 CB GLN A 181 20.311 -14.983 4.312 1.00166.66 A C ANISOU 1331 CB GLN A 181 18053 23326 21945 -2770 2015 671 A C ATOM 1332 CG GLN A 181 18.905 -14.472 4.567 1.00177.48 A C ANISOU 1332 CG GLN A 181 19017 25020 23396 -2730 2243 749 A C ATOM 1333 CD GLN A 181 18.396 -13.663 3.380 1.00175.91 A C ANISOU 1333 CD GLN A 181 18535 24983 23318 -2511 2130 674 A C ATOM 1334 NE2 GLN A 181 17.076 -13.589 3.254 1.00163.99 A N ANISOU 1334 NE2 GLN A 181 16598 23763 21944 -2550 2226 756 A N ATOM 1335 OE1 GLN A 181 19.181 -13.118 2.576 1.00161.96 A O ANISOU 1335 OE1 GLN A 181 16926 23090 21521 -2312 1956 555 A O ATOM 1336 N PRO A 182 23.013 -16.941 5.279 1.00169.07 A N ANISOU 1336 N PRO A 182 19258 22960 22021 -3074 1759 690 A N ATOM 1337 CA PRO A 182 24.408 -17.258 5.044 1.00157.04 A C ANISOU 1337 CA PRO A 182 18076 21166 20425 -3024 1563 623 A C ATOM 1338 C PRO A 182 24.760 -17.137 3.568 1.00132.04 A C ANISOU 1338 C PRO A 182 14865 17945 17359 -2910 1309 489 A C ATOM 1339 O PRO A 182 23.962 -17.477 2.693 1.00132.53 A O ANISOU 1339 O PRO A 182 14686 18097 17569 -3009 1203 472 A O ATOM 1340 CB PRO A 182 24.533 -18.715 5.515 1.00155.95 A C ANISOU 1340 CB PRO A 182 18094 20852 20306 -3327 1500 734 A C ATOM 1341 CG PRO A 182 23.389 -18.903 6.443 1.00166.91 A C ANISOU 1341 CG PRO A 182 19295 22421 21699 -3508 1743 877 A C ATOM 1342 CD PRO A 182 22.279 -18.056 5.902 1.00167.62 A C ANISOU 1342 CD PRO A 182 18998 22796 21892 -3400 1835 838 A C ATOM 1343 N ASN A 183 25.933 -16.577 3.291 1.00119.26 A N ANISOU 1343 N ASN A 183 13465 16198 15647 -2700 1218 394 A N ATOM 1344 CA ASN A 183 26.555 -16.713 1.965 1.00125.57 A C ANISOU 1344 CA ASN A 183 14309 16889 16510 -2619 965 277 A C ATOM 1345 C ASN A 183 26.695 -18.181 1.562 1.00122.91 A C ANISOU 1345 C ASN A 183 14067 16372 16262 -2855 777 292 A C ATOM 1346 O ASN A 183 26.996 -19.041 2.404 1.00127.09 A O ANISOU 1346 O ASN A 183 14778 16756 16753 -3018 806 384 A O ATOM 1347 CB ASN A 183 27.950 -16.061 1.978 1.00124.10 A C ANISOU 1347 CB ASN A 183 14384 16572 16195 -2400 918 206 A C ATOM 1348 CG ASN A 183 27.891 -14.554 2.167 1.00113.66 A C ANISOU 1348 CG ASN A 183 13001 15391 14792 -2158 1067 165 A C ATOM 1349 ND2 ASN A 183 28.873 -13.995 2.877 1.00105.98 A N ANISOU 1349 ND2 ASN A 183 12263 14333 13671 -2047 1127 158 A N ATOM 1350 OD1 ASN A 183 26.947 -13.901 1.713 1.00121.39 A O ANISOU 1350 OD1 ASN A 183 13727 16553 15842 -2076 1128 146 A O ATOM 1351 N ARG A 184 26.467 -18.461 0.280 1.00108.13 A N ANISOU 1351 N ARG A 184 12086 14499 14498 -2871 583 203 A N ATOM 1352 CA ARG A 184 26.640 -19.816 -0.235 1.00 99.45 A C ANISOU 1352 CA ARG A 184 11107 13201 13477 -3076 389 187 A C ATOM 1353 C ARG A 184 27.749 -19.862 -1.262 1.00 95.45 A C ANISOU 1353 C ARG A 184 10788 12535 12944 -2913 189 54 A C ATOM 1354 O ARG A 184 27.510 -20.065 -2.437 1.00 93.62 A O ANISOU 1354 O ARG A 184 10476 12312 12780 -2923 22 -41 A O ATOM 1355 CB ARG A 184 25.351 -20.315 -0.882 1.00104.07 A C ANISOU 1355 CB ARG A 184 11418 13913 14210 -3290 314 191 A C ATOM 1356 CG ARG A 184 24.198 -20.481 0.062 1.00111.49 A C ANISOU 1356 CG ARG A 184 12147 15014 15199 -3497 504 335 A C ATOM 1357 CD ARG A 184 22.860 -20.569 -0.668 1.00104.64 A C ANISOU 1357 CD ARG A 184 10918 14362 14478 -3646 441 334 A C ATOM 1358 NE ARG A 184 21.764 -20.781 0.269 1.00114.65 A N ANISOU 1358 NE ARG A 184 11964 15797 15799 -3858 639 487 A N ATOM 1359 CZ ARG A 184 20.543 -21.185 -0.077 1.00139.36 A C ANISOU 1359 CZ ARG A 184 14779 19098 19070 -4090 601 536 A C ATOM 1360 NH1 ARG A 184 20.269 -21.423 -1.351 1.00160.52 A N1+ ANISOU 1360 NH1 ARG A 184 17349 21796 21842 -4140 355 434 A N1+ ATOM 1361 NH2 ARG A 184 19.603 -21.360 0.846 1.00130.04 A N ANISOU 1361 NH2 ARG A 184 13394 18082 17932 -4279 808 689 A N ATOM 1362 N TYR A 185 28.979 -19.629 -0.808 1.00 99.37 A N ANISOU 1362 N TYR A 185 11528 12899 13328 -2758 211 52 A N ATOM 1363 CA TYR A 185 30.127 -19.695 -1.694 1.00104.04 A C ANISOU 1363 CA TYR A 185 12296 13346 13888 -2596 46 -57 A C ATOM 1364 C TYR A 185 30.476 -21.158 -1.930 1.00107.76 A C ANISOU 1364 C TYR A 185 12961 13566 14414 -2755 -103 -64 A C ATOM 1365 O TYR A 185 30.060 -22.026 -1.162 1.00113.32 A O ANISOU 1365 O TYR A 185 13715 14183 15155 -2976 -62 38 A O ATOM 1366 CB TYR A 185 31.327 -18.945 -1.109 1.00107.99 A C ANISOU 1366 CB TYR A 185 12964 13807 14257 -2388 116 -46 A C ATOM 1367 CG TYR A 185 31.046 -17.498 -0.766 1.00 94.64 A C ANISOU 1367 CG TYR A 185 11137 12321 12501 -2233 274 -41 A C ATOM 1368 CD1 TYR A 185 30.187 -16.731 -1.554 1.00 85.07 A C ANISOU 1368 CD1 TYR A 185 9683 11295 11343 -2159 281 -98 A C ATOM 1369 CD2 TYR A 185 31.628 -16.893 0.355 1.00 82.05 A C ANISOU 1369 CD2 TYR A 185 9665 10725 10784 -2159 411 19 A C ATOM 1370 CE1 TYR A 185 29.900 -15.415 -1.226 1.00 78.55 A C ANISOU 1370 CE1 TYR A 185 8749 10633 10462 -2002 433 -92 A C ATOM 1371 CE2 TYR A 185 31.357 -15.571 0.675 1.00 84.00 A C ANISOU 1371 CE2 TYR A 185 9818 11132 10966 -2018 559 10 A C ATOM 1372 CZ TYR A 185 30.507 -14.830 -0.138 1.00 87.97 A C ANISOU 1372 CZ TYR A 185 10089 11800 11535 -1929 573 -46 A C ATOM 1373 OH TYR A 185 30.222 -13.514 0.155 1.00 89.58 A O ANISOU 1373 OH TYR A 185 10215 12140 11681 -1769 723 -55 A O HETATM 1374 N TPO A 186 31.278 -21.409 -2.960 1.00101.09 A N ANISOU 1374 N TPO A 186 12244 12600 13566 -2634 -266 -182 A N HETATM 1375 CA TPO A 186 31.731 -22.745 -3.388 1.00 94.49 A C ANISOU 1375 CA TPO A 186 11623 11502 12776 -2729 -421 -223 A C HETATM 1376 C TPO A 186 32.638 -23.415 -2.398 1.00101.15 A C ANISOU 1376 C TPO A 186 12719 12135 13578 -2734 -389 -124 A C HETATM 1377 O TPO A 186 33.596 -22.795 -1.909 1.00101.25 A O ANISOU 1377 O TPO A 186 12810 12162 13496 -2547 -329 -93 A O HETATM 1378 CB TPO A 186 32.692 -22.480 -4.530 1.00 87.76 A C ANISOU 1378 CB TPO A 186 10861 10605 11879 -2496 -542 -364 A C HETATM 1379 CG2 TPO A 186 32.780 -23.635 -5.526 1.00 78.95 A C ANISOU 1379 CG2 TPO A 186 9890 9288 10817 -2572 -724 -475 A C HETATM 1380 OG1 TPO A 186 32.438 -21.095 -4.935 1.00 91.67 A O ANISOU 1380 OG1 TPO A 186 11147 11352 12331 -2337 -482 -402 A O HETATM 1381 P TPO A 186 32.215 -20.330 -6.308 1.00 82.42 A P ANISOU 1381 P TPO A 186 9832 10337 11147 -2198 -570 -529 A P HETATM 1382 O1P TPO A 186 33.540 -20.515 -7.090 1.00 77.25 A O ANISOU 1382 O1P TPO A 186 9382 9541 10427 -2007 -668 -626 A O HETATM 1383 O2P TPO A 186 30.963 -20.963 -6.860 1.00 93.70 A O1- ANISOU 1383 O2P TPO A 186 11119 11809 12671 -2419 -668 -561 A O1- HETATM 1384 O3P TPO A 186 31.955 -18.966 -5.746 1.00 75.75 A O ANISOU 1384 O3P TPO A 186 8819 9702 10258 -2082 -411 -464 A O ATOM 1385 N ASN A 187 32.394 -24.700 -2.120 1.00118.08 A N ANISOU 1385 N ASN A 187 15003 14072 15790 -2948 -445 -71 A N ATOM 1386 CA ASN A 187 33.223 -25.391 -1.162 1.00112.43 A C ANISOU 1386 CA ASN A 187 14536 13147 15035 -2949 -424 42 A C ATOM 1387 C ASN A 187 34.502 -25.931 -1.780 1.00116.11 A C ANISOU 1387 C ASN A 187 15236 13393 15487 -2758 -558 -38 A C ATOM 1388 O ASN A 187 35.491 -26.146 -1.080 1.00101.68 A O ANISOU 1388 O ASN A 187 13584 11447 13603 -2651 -544 45 A O ATOM 1389 CB ASN A 187 32.472 -26.485 -0.426 1.00102.73 A C ANISOU 1389 CB ASN A 187 13379 11779 13875 -3252 -401 169 A C ATOM 1390 CG ASN A 187 33.252 -26.988 0.786 1.00110.32 A C ANISOU 1390 CG ASN A 187 14574 12573 14768 -3244 -348 326 A C ATOM 1391 ND2 ASN A 187 32.566 -27.571 1.730 1.00120.67 A N ANISOU 1391 ND2 ASN A 187 15912 13840 16096 -3491 -263 479 A N ATOM 1392 OD1 ASN A 187 34.456 -26.823 0.856 1.00114.11 A O ANISOU 1392 OD1 ASN A 187 15198 12980 15177 -3016 -384 317 A O ATOM 1393 N ARG A 188 34.472 -26.178 -3.080 1.00132.76 A N ANISOU 1393 N ARG A 188 17346 15454 17642 -2715 -689 -198 A N ATOM 1394 CA ARG A 188 35.611 -26.761 -3.769 1.00136.52 A C ANISOU 1394 CA ARG A 188 18043 15722 18107 -2528 -805 -290 A C ATOM 1395 C ARG A 188 36.664 -25.696 -4.051 1.00129.54 A C ANISOU 1395 C ARG A 188 17107 14981 17128 -2225 -773 -335 A C ATOM 1396 O ARG A 188 36.988 -25.416 -5.209 1.00126.66 A O ANISOU 1396 O ARG A 188 16720 14658 16746 -2074 -843 -478 A O ATOM 1397 CB ARG A 188 35.134 -27.402 -5.079 1.00132.91 A C ANISOU 1397 CB ARG A 188 17620 15168 17712 -2604 -950 -457 A C ATOM 1398 CG ARG A 188 36.126 -28.287 -5.791 1.00139.69 A C ANISOU 1398 CG ARG A 188 18745 15759 18569 -2451 -1065 -562 A C ATOM 1399 CD ARG A 188 36.877 -27.551 -6.903 1.00167.83 A C ANISOU 1399 CD ARG A 188 22265 19445 22057 -2170 -1097 -709 A C ATOM 1400 NE ARG A 188 36.058 -27.271 -8.078 1.00166.31 A N ANISOU 1400 NE ARG A 188 21944 19381 21864 -2237 -1177 -858 A N ATOM 1401 CZ ARG A 188 36.167 -26.170 -8.819 1.00158.34 A C ANISOU 1401 CZ ARG A 188 20768 18610 20784 -2073 -1163 -934 A C ATOM 1402 NH1 ARG A 188 37.068 -25.231 -8.512 1.00152.68 A N1+ ANISOU 1402 NH1 ARG A 188 19992 18021 19996 -1845 -1066 -880 A N1+ ATOM 1403 NH2 ARG A 188 35.375 -26.008 -9.870 1.00146.45 A N ANISOU 1403 NH2 ARG A 188 19159 17211 19272 -2147 -1255 -1058 A N ATOM 1404 N VAL A 189 37.250 -25.143 -2.995 1.00114.63 A N ANISOU 1404 N VAL A 189 15219 13161 15172 -2145 -674 -209 A N ATOM 1405 CA VAL A 189 38.269 -24.095 -3.150 1.00106.45 A C ANISOU 1405 CA VAL A 189 14132 12265 14049 -1890 -643 -235 A C ATOM 1406 C VAL A 189 39.555 -24.402 -2.381 1.00108.32 A C ANISOU 1406 C VAL A 189 14536 12383 14238 -1757 -649 -132 A C ATOM 1407 O VAL A 189 39.492 -25.035 -1.328 1.00107.98 A O ANISOU 1407 O VAL A 189 14606 12224 14197 -1875 -626 2 A O ATOM 1408 CB VAL A 189 37.720 -22.726 -2.696 1.00 92.49 A C ANISOU 1408 CB VAL A 189 12152 10764 12222 -1901 -517 -199 A C ATOM 1409 CG1 VAL A 189 36.779 -22.156 -3.735 1.00 81.41 A C ANISOU 1409 CG1 VAL A 189 10558 9518 10853 -1924 -531 -316 A C ATOM 1410 CG2 VAL A 189 37.039 -22.829 -1.340 1.00103.76 A C ANISOU 1410 CG2 VAL A 189 13572 12212 13639 -2093 -407 -51 A C ATOM 1411 N VAL A 190 40.696 -23.967 -2.922 1.00 98.92 A N ANISOU 1411 N VAL A 190 13351 11230 13003 -1517 -681 -187 A N ATOM 1412 CA VAL A 190 41.997 -24.089 -2.260 1.00 96.18 A C ANISOU 1412 CA VAL A 190 13111 10822 12608 -1366 -695 -88 A C ATOM 1413 C VAL A 190 42.616 -25.477 -2.445 1.00 93.37 A C ANISOU 1413 C VAL A 190 12968 10193 12314 -1297 -791 -80 A C ATOM 1414 O VAL A 190 41.955 -26.487 -2.237 1.00 86.85 A O ANISOU 1414 O VAL A 190 12267 9178 11554 -1460 -821 -54 A O ATOM 1415 CB VAL A 190 41.919 -23.816 -0.728 1.00 93.20 A C ANISOU 1415 CB VAL A 190 12749 10496 12166 -1478 -620 83 A C ATOM 1416 CG1 VAL A 190 43.327 -23.813 -0.114 1.00 94.88 A C ANISOU 1416 CG1 VAL A 190 13046 10686 12318 -1312 -659 184 A C ATOM 1417 CG2 VAL A 190 41.161 -22.519 -0.430 1.00 89.16 A C ANISOU 1417 CG2 VAL A 190 12056 10225 11593 -1557 -506 75 A C ATOM 1418 N THR A 191 43.888 -25.513 -2.822 1.00 87.60 A N ANISOU 1418 N THR A 191 12277 9438 11565 -1054 -834 -97 A N ATOM 1419 CA THR A 191 44.613 -26.766 -2.921 1.00 88.87 A C ANISOU 1419 CA THR A 191 12642 9342 11782 -936 -913 -78 A C ATOM 1420 C THR A 191 44.472 -27.558 -1.630 1.00100.32 A C ANISOU 1420 C THR A 191 14243 10627 13247 -1071 -923 100 A C ATOM 1421 O THR A 191 44.513 -26.978 -0.533 1.00 90.89 A O ANISOU 1421 O THR A 191 12991 9561 11982 -1141 -875 237 A O ATOM 1422 CB THR A 191 46.119 -26.511 -3.139 1.00 96.43 A C ANISOU 1422 CB THR A 191 13573 10359 12705 -645 -933 -62 A C ATOM 1423 CG2 THR A 191 46.880 -27.823 -2.983 1.00105.55 A C ANISOU 1423 CG2 THR A 191 14940 11244 13920 -507 -1004 -3 A C ATOM 1424 OG1 THR A 191 46.314 -25.960 -4.422 1.00 99.14 A O ANISOU 1424 OG1 THR A 191 13812 10822 13034 -511 -921 -224 A O ATOM 1425 N LEU A 192 44.337 -28.873 -1.752 1.00107.47 A N ANISOU 1425 N LEU A 192 15360 11240 14231 -1104 -987 100 A N ATOM 1426 CA LEU A 192 44.103 -29.730 -0.586 1.00 99.45 A C ANISOU 1426 CA LEU A 192 14516 10036 13234 -1254 -999 278 A C ATOM 1427 C LEU A 192 45.091 -29.512 0.579 1.00 99.84 A C ANISOU 1427 C LEU A 192 14580 10145 13207 -1141 -1001 472 A C ATOM 1428 O LEU A 192 44.685 -29.415 1.744 1.00102.49 A O ANISOU 1428 O LEU A 192 14935 10518 13486 -1313 -960 626 A O ATOM 1429 CB LEU A 192 44.099 -31.213 -0.984 1.00 92.69 A C ANISOU 1429 CB LEU A 192 13924 8816 12477 -1248 -1082 249 A C ATOM 1430 CG LEU A 192 43.824 -32.071 0.281 1.00 99.33 A C ANISOU 1430 CG LEU A 192 14952 9457 13332 -1421 -1090 460 A C ATOM 1431 CD1 LEU A 192 42.324 -32.136 0.529 1.00100.97 A C ANISOU 1431 CD1 LEU A 192 15124 9674 13564 -1782 -1038 467 A C ATOM 1432 CD2 LEU A 192 44.478 -33.444 0.322 1.00 96.76 A C ANISOU 1432 CD2 LEU A 192 14920 8765 13077 -1293 -1179 521 A C ATOM 1433 N TRP A 193 46.386 -29.434 0.280 1.00102.45 A N ANISOU 1433 N TRP A 193 14898 10499 13528 -855 -1049 469 A N ATOM 1434 CA TRP A 193 47.389 -29.322 1.333 1.00 99.64 A C ANISOU 1434 CA TRP A 193 14555 10197 13107 -743 -1081 656 A C ATOM 1435 C TRP A 193 47.267 -28.040 2.147 1.00 99.50 A C ANISOU 1435 C TRP A 193 14365 10473 12966 -853 -1018 724 A C ATOM 1436 O TRP A 193 47.690 -27.958 3.301 1.00 98.83 A O ANISOU 1436 O TRP A 193 14319 10432 12800 -874 -1039 897 A O ATOM 1437 CB TRP A 193 48.797 -29.472 0.776 1.00 95.43 A C ANISOU 1437 CB TRP A 193 14001 9659 12599 -411 -1144 638 A C ATOM 1438 CG TRP A 193 49.070 -30.832 0.207 1.00100.33 A C ANISOU 1438 CG TRP A 193 14838 9956 13326 -265 -1204 602 A C ATOM 1439 CD1 TRP A 193 48.288 -31.945 0.324 1.00112.15 A C ANISOU 1439 CD1 TRP A 193 16568 11151 14891 -416 -1226 615 A C ATOM 1440 CD2 TRP A 193 50.247 -31.240 -0.496 1.00107.99 A C ANISOU 1440 CD2 TRP A 193 15824 10861 14344 67 -1244 558 A C ATOM 1441 CE2 TRP A 193 50.090 -32.603 -0.817 1.00110.44 A C ANISOU 1441 CE2 TRP A 193 16403 10810 14749 116 -1287 528 A C ATOM 1442 CE3 TRP A 193 51.413 -30.587 -0.893 1.00113.64 A C ANISOU 1442 CE3 TRP A 193 16353 11790 15033 325 -1241 543 A C ATOM 1443 NE1 TRP A 193 48.878 -33.005 -0.326 1.00118.51 A N ANISOU 1443 NE1 TRP A 193 17556 11687 15783 -197 -1282 561 A N ATOM 1444 CZ2 TRP A 193 51.071 -33.331 -1.486 1.00113.80 A C ANISOU 1444 CZ2 TRP A 193 16924 11076 15237 442 -1319 480 A C ATOM 1445 CZ3 TRP A 193 52.390 -31.313 -1.560 1.00107.56 A C ANISOU 1445 CZ3 TRP A 193 15649 10887 14329 641 -1269 507 A C ATOM 1446 CH2 TRP A 193 52.208 -32.664 -1.857 1.00110.13 A C ANISOU 1446 CH2 TRP A 193 16251 10849 14743 710 -1303 470 A C ATOM 1447 N TYR A 194 46.695 -27.026 1.508 1.00 86.58 A N ANISOU 1447 N TYR A 194 12550 9034 11311 -915 -945 580 A N ATOM 1448 CA TYR A 194 46.614 -25.719 2.112 1.00 81.01 A C ANISOU 1448 CA TYR A 194 11690 8594 10493 -989 -878 611 A C ATOM 1449 C TYR A 194 45.186 -25.415 2.564 1.00 89.67 A C ANISOU 1449 C TYR A 194 12763 9743 11565 -1256 -777 608 A C ATOM 1450 O TYR A 194 44.911 -24.373 3.165 1.00 92.19 A O ANISOU 1450 O TYR A 194 12982 10260 11785 -1339 -699 630 A O ATOM 1451 CB TYR A 194 47.127 -24.677 1.132 1.00 77.69 A C ANISOU 1451 CB TYR A 194 11085 8371 10063 -837 -862 474 A C ATOM 1452 CG TYR A 194 48.600 -24.829 0.804 1.00 89.04 A C ANISOU 1452 CG TYR A 194 12504 9813 11513 -576 -942 500 A C ATOM 1453 CD1 TYR A 194 49.030 -25.738 -0.167 1.00 95.88 A C ANISOU 1453 CD1 TYR A 194 13439 10514 12474 -397 -989 422 A C ATOM 1454 CD2 TYR A 194 49.558 -24.083 1.467 1.00 87.63 A C ANISOU 1454 CD2 TYR A 194 12238 9807 11248 -510 -968 600 A C ATOM 1455 CE1 TYR A 194 50.373 -25.875 -0.468 1.00 92.15 A C ANISOU 1455 CE1 TYR A 194 12929 10066 12017 -139 -1042 451 A C ATOM 1456 CE2 TYR A 194 50.908 -24.228 1.193 1.00 86.19 A C ANISOU 1456 CE2 TYR A 194 12004 9655 11086 -277 -1041 640 A C ATOM 1457 CZ TYR A 194 51.313 -25.115 0.213 1.00 95.77 A C ANISOU 1457 CZ TYR A 194 13265 10719 12401 -81 -1068 567 A C ATOM 1458 OH TYR A 194 52.659 -25.247 -0.071 1.00112.98 A O ANISOU 1458 OH TYR A 194 15370 12950 14605 170 -1122 611 A O ATOM 1459 N ARG A 195 44.270 -26.342 2.290 1.00 95.84 A N ANISOU 1459 N ARG A 195 13636 10342 12434 -1394 -774 580 A N ATOM 1460 CA ARG A 195 42.867 -26.126 2.609 1.00 95.71 A C ANISOU 1460 CA ARG A 195 13563 10388 12415 -1649 -674 577 A C ATOM 1461 C ARG A 195 42.578 -26.179 4.103 1.00 89.42 A C ANISOU 1461 C ARG A 195 12845 9606 11521 -1811 -611 764 A C ATOM 1462 O ARG A 195 42.980 -27.114 4.775 1.00 90.08 A O ANISOU 1462 O ARG A 195 13114 9510 11601 -1822 -668 906 A O ATOM 1463 CB ARG A 195 41.948 -27.088 1.860 1.00105.59 A C ANISOU 1463 CB ARG A 195 14873 11455 13791 -1781 -701 496 A C ATOM 1464 CG ARG A 195 40.468 -26.729 2.064 1.00104.07 A C ANISOU 1464 CG ARG A 195 14553 11381 13605 -2039 -594 486 A C ATOM 1465 CD ARG A 195 39.585 -27.727 1.351 1.00109.61 A C ANISOU 1465 CD ARG A 195 15310 11902 14432 -2201 -643 414 A C ATOM 1466 NE ARG A 195 39.940 -27.794 -0.060 1.00 99.16 A N ANISOU 1466 NE ARG A 195 13971 10536 13168 -2041 -735 229 A N ATOM 1467 CZ ARG A 195 39.914 -28.916 -0.774 1.00101.21 A C ANISOU 1467 CZ ARG A 195 14392 10543 13519 -2059 -836 155 A C ATOM 1468 NH1 ARG A 195 39.582 -30.069 -0.207 1.00108.30 A N1+ ANISOU 1468 NH1 ARG A 195 15483 11193 14473 -2232 -863 260 A N1+ ATOM 1469 NH2 ARG A 195 40.282 -28.881 -2.041 1.00107.23 A N ANISOU 1469 NH2 ARG A 195 15145 11291 14305 -1897 -906 -19 A N ATOM 1470 N PRO A 196 41.880 -25.157 4.622 1.00 85.68 A N ANISOU 1470 N PRO A 196 12241 9349 10961 -1926 -487 765 A N ATOM 1471 CA PRO A 196 41.522 -25.041 6.032 1.00 91.08 A C ANISOU 1471 CA PRO A 196 12992 10089 11523 -2082 -397 924 A C ATOM 1472 C PRO A 196 40.435 -26.043 6.444 1.00109.09 A C ANISOU 1472 C PRO A 196 15361 12227 13859 -2325 -344 1015 A C ATOM 1473 O PRO A 196 39.663 -26.482 5.587 1.00111.83 A O ANISOU 1473 O PRO A 196 15649 12502 14336 -2411 -350 920 A O ATOM 1474 CB PRO A 196 40.964 -23.613 6.112 1.00 83.90 A C ANISOU 1474 CB PRO A 196 11897 9446 10534 -2105 -265 843 A C ATOM 1475 CG PRO A 196 40.408 -23.373 4.765 1.00 83.09 A C ANISOU 1475 CG PRO A 196 11633 9380 10555 -2071 -268 668 A C ATOM 1476 CD PRO A 196 41.391 -24.011 3.834 1.00 84.58 A C ANISOU 1476 CD PRO A 196 11889 9416 10829 -1896 -420 608 A C ATOM 1477 N PRO A 197 40.343 -26.347 7.751 1.00109.67 A N ANISOU 1477 N PRO A 197 15568 12277 13823 -2451 -291 1199 A N ATOM 1478 CA PRO A 197 39.340 -27.243 8.341 1.00108.29 A C ANISOU 1478 CA PRO A 197 15484 11984 13674 -2707 -219 1324 A C ATOM 1479 C PRO A 197 37.929 -26.903 7.880 1.00106.14 A C ANISOU 1479 C PRO A 197 15010 11839 13478 -2884 -92 1228 A C ATOM 1480 O PRO A 197 37.214 -27.792 7.423 1.00116.48 A O ANISOU 1480 O PRO A 197 16336 13001 14920 -3043 -115 1223 A O ATOM 1481 CB PRO A 197 39.451 -26.965 9.835 1.00106.11 A C ANISOU 1481 CB PRO A 197 15310 11803 13203 -2780 -132 1502 A C ATOM 1482 CG PRO A 197 40.833 -26.452 10.028 1.00114.83 A C ANISOU 1482 CG PRO A 197 16464 12958 14207 -2548 -241 1507 A C ATOM 1483 CD PRO A 197 41.246 -25.770 8.760 1.00108.89 A C ANISOU 1483 CD PRO A 197 15540 12284 13549 -2358 -300 1303 A C ATOM 1484 N GLU A 198 37.538 -25.628 7.987 1.00 90.64 A N ANISOU 1484 N GLU A 198 12859 10143 11436 -2856 32 1155 A N ATOM 1485 CA GLU A 198 36.165 -25.194 7.655 1.00 84.64 A C ANISOU 1485 CA GLU A 198 11876 9543 10738 -3002 167 1083 A C ATOM 1486 C GLU A 198 35.695 -25.835 6.363 1.00 89.13 A C ANISOU 1486 C GLU A 198 12367 9999 11499 -3050 65 965 A C ATOM 1487 O GLU A 198 34.633 -26.448 6.300 1.00 90.85 A O ANISOU 1487 O GLU A 198 12529 10182 11808 -3277 108 998 A O ATOM 1488 CB GLU A 198 36.075 -23.667 7.477 1.00 85.07 A C ANISOU 1488 CB GLU A 198 11738 9862 10720 -2863 263 963 A C ATOM 1489 CG GLU A 198 36.794 -22.818 8.504 1.00 97.03 A C ANISOU 1489 CG GLU A 198 13341 11487 12038 -2762 324 1020 A C ATOM 1490 CD GLU A 198 38.143 -22.329 8.055 1.00 97.96 A C ANISOU 1490 CD GLU A 198 13505 11590 12124 -2529 184 944 A C ATOM 1491 OE1 GLU A 198 39.108 -23.142 8.078 1.00107.43 A O ANISOU 1491 OE1 GLU A 198 14865 12615 13338 -2466 37 1010 A O ATOM 1492 OE2 GLU A 198 38.291 -21.151 7.676 1.00 93.80 A O1- ANISOU 1492 OE2 GLU A 198 12858 11219 11562 -2401 218 827 A O1- ATOM 1493 N LEU A 199 36.481 -25.647 5.307 1.00 92.08 A N ANISOU 1493 N LEU A 199 12731 10331 11925 -2841 -67 822 A N ATOM 1494 CA LEU A 199 36.107 -26.145 4.005 1.00 93.94 A C ANISOU 1494 CA LEU A 199 12906 10474 12312 -2862 -171 685 A C ATOM 1495 C LEU A 199 35.981 -27.668 4.005 1.00 89.28 A C ANISOU 1495 C LEU A 199 12516 9586 11817 -3024 -263 756 A C ATOM 1496 O LEU A 199 35.016 -28.213 3.473 1.00 95.39 A O ANISOU 1496 O LEU A 199 13229 10309 12704 -3219 -282 712 A O ATOM 1497 CB LEU A 199 37.125 -25.659 2.963 1.00 99.24 A C ANISOU 1497 CB LEU A 199 13562 11155 12989 -2588 -283 533 A C ATOM 1498 CG LEU A 199 37.157 -24.132 2.832 1.00 92.64 A C ANISOU 1498 CG LEU A 199 12530 10595 12073 -2449 -198 455 A C ATOM 1499 CD1 LEU A 199 38.087 -23.716 1.706 1.00 99.00 A C ANISOU 1499 CD1 LEU A 199 13314 11408 12893 -2207 -304 314 A C ATOM 1500 CD2 LEU A 199 35.756 -23.588 2.597 1.00 80.71 A C ANISOU 1500 CD2 LEU A 199 10789 9269 10606 -2589 -91 408 A C ATOM 1501 N LEU A 200 36.956 -28.340 4.612 1.00 78.91 A N ANISOU 1501 N LEU A 200 11444 8077 10460 -2947 -327 870 A N ATOM 1502 CA LEU A 200 36.952 -29.790 4.686 1.00 81.22 A C ANISOU 1502 CA LEU A 200 11971 8050 10836 -3074 -415 952 A C ATOM 1503 C LEU A 200 35.732 -30.327 5.455 1.00 88.09 A C ANISOU 1503 C LEU A 200 12840 8900 11728 -3414 -310 1094 A C ATOM 1504 O LEU A 200 35.283 -31.441 5.223 1.00 91.06 A O ANISOU 1504 O LEU A 200 13344 9040 12213 -3600 -373 1121 A O ATOM 1505 CB LEU A 200 38.246 -30.285 5.323 1.00 91.02 A C ANISOU 1505 CB LEU A 200 13455 9116 12011 -2898 -492 1076 A C ATOM 1506 CG LEU A 200 39.512 -29.976 4.545 1.00 98.38 A C ANISOU 1506 CG LEU A 200 14395 10039 12943 -2571 -603 956 A C ATOM 1507 CD1 LEU A 200 40.748 -30.202 5.423 1.00115.74 A C ANISOU 1507 CD1 LEU A 200 16766 12158 15051 -2400 -657 1113 A C ATOM 1508 CD2 LEU A 200 39.625 -30.736 3.245 1.00 93.63 A C ANISOU 1508 CD2 LEU A 200 13869 9226 12477 -2501 -724 798 A C ATOM 1509 N LEU A 201 35.191 -29.523 6.361 1.00 93.63 A N ANISOU 1509 N LEU A 201 13401 9850 12322 -3499 -142 1183 A N ATOM 1510 CA LEU A 201 33.993 -29.895 7.098 1.00 97.49 A C ANISOU 1510 CA LEU A 201 13844 10375 12819 -3815 -8 1321 A C ATOM 1511 C LEU A 201 32.724 -29.389 6.416 1.00108.41 A C ANISOU 1511 C LEU A 201 14921 11971 14296 -3957 64 1207 A C ATOM 1512 O LEU A 201 31.650 -29.355 7.051 1.00113.16 A O ANISOU 1512 O LEU A 201 15394 12709 14892 -4193 219 1313 A O ATOM 1513 CB LEU A 201 34.060 -29.349 8.520 1.00 98.75 A C ANISOU 1513 CB LEU A 201 14031 10694 12795 -3829 153 1489 A C ATOM 1514 CG LEU A 201 34.830 -30.218 9.516 1.00 96.29 A C ANISOU 1514 CG LEU A 201 14033 10156 12394 -3840 106 1691 A C ATOM 1515 CD1 LEU A 201 34.789 -29.609 10.922 1.00 96.67 A C ANISOU 1515 CD1 LEU A 201 14103 10395 12232 -3875 272 1848 A C ATOM 1516 CD2 LEU A 201 34.293 -31.629 9.497 1.00 98.26 A C ANISOU 1516 CD2 LEU A 201 14444 10122 12767 -4096 57 1798 A C ATOM 1517 N GLY A 202 32.870 -28.889 5.191 1.00105.42 A N ANISOU 1517 N GLY A 202 14409 11658 13986 -3797 -31 1004 A N ATOM 1518 CA GLY A 202 31.720 -28.549 4.365 1.00 94.45 A C ANISOU 1518 CA GLY A 202 12742 10442 12702 -3921 -12 891 A C ATOM 1519 C GLY A 202 31.201 -27.115 4.445 1.00 94.91 A C ANISOU 1519 C GLY A 202 12507 10857 12697 -3823 138 842 A C ATOM 1520 O GLY A 202 30.038 -26.863 4.144 1.00 95.89 A O ANISOU 1520 O GLY A 202 12377 11160 12896 -3970 203 816 A O ATOM 1521 N GLU A 203 32.039 -26.171 4.866 1.00 97.48 A N ANISOU 1521 N GLU A 203 12863 11286 12886 -3580 194 833 A N ATOM 1522 CA GLU A 203 31.545 -24.791 5.025 1.00 98.56 A C ANISOU 1522 CA GLU A 203 12757 11733 12956 -3483 350 789 A C ATOM 1523 C GLU A 203 31.349 -24.071 3.685 1.00 97.51 A C ANISOU 1523 C GLU A 203 12419 11727 12902 -3340 271 603 A C ATOM 1524 O GLU A 203 32.177 -24.211 2.780 1.00 94.62 A O ANISOU 1524 O GLU A 203 12147 11239 12565 -3188 108 490 A O ATOM 1525 CB GLU A 203 32.448 -23.990 5.948 1.00 91.55 A C ANISOU 1525 CB GLU A 203 11987 10908 11889 -3301 433 838 A C ATOM 1526 CG GLU A 203 32.003 -22.559 6.129 1.00102.90 A C ANISOU 1526 CG GLU A 203 13221 12626 13249 -3186 595 783 A C ATOM 1527 CD GLU A 203 30.701 -22.402 6.897 1.00 98.44 A C ANISOU 1527 CD GLU A 203 12490 12241 12670 -3369 812 879 A C ATOM 1528 OE1 GLU A 203 30.636 -22.793 8.076 1.00100.23 A O ANISOU 1528 OE1 GLU A 203 12846 12440 12796 -3498 924 1032 A O ATOM 1529 OE2 GLU A 203 29.729 -21.901 6.291 1.00 97.86 A O1- ANISOU 1529 OE2 GLU A 203 12147 12346 12688 -3381 869 809 A O1- ATOM 1530 N ARG A 204 30.265 -23.311 3.552 1.00 87.91 A N ANISOU 1530 N ARG A 204 10923 10760 11716 -3379 389 577 A N ATOM 1531 CA ARG A 204 30.023 -22.527 2.344 1.00 98.23 A C ANISOU 1531 CA ARG A 204 12028 12210 13083 -3233 321 420 A C ATOM 1532 C ARG A 204 29.857 -21.056 2.687 1.00 99.78 A C ANISOU 1532 C ARG A 204 12070 12653 13189 -3051 486 402 A C ATOM 1533 O ARG A 204 29.721 -20.205 1.807 1.00106.74 A O ANISOU 1533 O ARG A 204 12795 13665 14096 -2893 452 289 A O ATOM 1534 CB ARG A 204 28.785 -23.036 1.608 1.00104.63 A C ANISOU 1534 CB ARG A 204 12622 13086 14045 -3443 265 393 A C ATOM 1535 CG ARG A 204 28.956 -24.416 1.018 1.00112.58 A C ANISOU 1535 CG ARG A 204 13798 13830 15147 -3609 73 368 A C ATOM 1536 CD ARG A 204 27.654 -24.935 0.443 1.00122.08 A C ANISOU 1536 CD ARG A 204 14786 15108 16491 -3871 20 357 A C ATOM 1537 NE ARG A 204 27.121 -24.053 -0.592 1.00122.02 A N ANISOU 1537 NE ARG A 204 14509 15328 16522 -3753 -27 234 A N ATOM 1538 CZ ARG A 204 27.455 -24.126 -1.872 1.00120.98 A C ANISOU 1538 CZ ARG A 204 14413 15135 16419 -3657 -222 78 A C ATOM 1539 NH1 ARG A 204 28.362 -25.013 -2.273 1.00133.06 A N1+ ANISOU 1539 NH1 ARG A 204 16234 16378 17944 -3643 -373 14 A N1+ ATOM 1540 NH2 ARG A 204 26.917 -23.285 -2.747 1.00110.37 A N ANISOU 1540 NH2 ARG A 204 12821 14016 15098 -3553 -260 -11 A N ATOM 1541 N ASP A 205 29.799 -20.775 3.981 1.00 92.78 A N ANISOU 1541 N ASP A 205 11237 11824 12190 -3082 669 517 A N ATOM 1542 CA ASP A 205 29.734 -19.424 4.469 1.00 99.95 A C ANISOU 1542 CA ASP A 205 12062 12924 12988 -2909 837 500 A C ATOM 1543 C ASP A 205 31.032 -19.132 5.206 1.00 97.53 A C ANISOU 1543 C ASP A 205 12024 12512 12520 -2779 834 521 A C ATOM 1544 O ASP A 205 31.059 -18.967 6.429 1.00 96.33 A O ANISOU 1544 O ASP A 205 11972 12391 12235 -2820 982 619 A O ATOM 1545 CB ASP A 205 28.540 -19.266 5.412 1.00111.03 A C ANISOU 1545 CB ASP A 205 13306 14508 14372 -3049 1073 608 A C ATOM 1546 CG ASP A 205 28.230 -17.822 5.701 1.00115.91 A C ANISOU 1546 CG ASP A 205 13798 15338 14905 -2853 1255 562 A C ATOM 1547 OD1 ASP A 205 28.667 -16.959 4.903 1.00125.96 A O ANISOU 1547 OD1 ASP A 205 15040 16636 16181 -2637 1177 440 A O ATOM 1548 OD2 ASP A 205 27.538 -17.546 6.708 1.00116.40 A O1- ANISOU 1548 OD2 ASP A 205 13798 15534 14892 -2910 1482 649 A O1- ATOM 1549 N TYR A 206 32.116 -19.041 4.449 1.00 90.15 A N ANISOU 1549 N TYR A 206 11198 11466 11589 -2622 663 430 A N ATOM 1550 CA TYR A 206 33.445 -18.783 5.010 1.00 86.21 A C ANISOU 1550 CA TYR A 206 10926 10875 10953 -2497 623 448 A C ATOM 1551 C TYR A 206 33.901 -17.398 4.559 1.00 84.91 A C ANISOU 1551 C TYR A 206 10705 10822 10732 -2272 636 335 A C ATOM 1552 O TYR A 206 33.209 -16.752 3.764 1.00 74.94 A O ANISOU 1552 O TYR A 206 9246 9685 9543 -2205 663 250 A O ATOM 1553 CB TYR A 206 34.428 -19.851 4.528 1.00 75.36 A C ANISOU 1553 CB TYR A 206 9723 9277 9632 -2492 420 449 A C ATOM 1554 CG TYR A 206 34.422 -19.998 3.033 1.00 81.14 A C ANISOU 1554 CG TYR A 206 10355 9978 10496 -2419 275 316 A C ATOM 1555 CD1 TYR A 206 35.138 -19.112 2.236 1.00 73.21 A C ANISOU 1555 CD1 TYR A 206 9319 9027 9469 -2204 214 204 A C ATOM 1556 CD2 TYR A 206 33.665 -20.996 2.405 1.00 89.53 A C ANISOU 1556 CD2 TYR A 206 11359 10963 11695 -2578 202 303 A C ATOM 1557 CE1 TYR A 206 35.097 -19.204 0.857 1.00 72.22 A C ANISOU 1557 CE1 TYR A 206 9108 8890 9440 -2134 92 84 A C ATOM 1558 CE2 TYR A 206 33.625 -21.101 1.026 1.00 90.28 A C ANISOU 1558 CE2 TYR A 206 11376 11039 11885 -2515 66 170 A C ATOM 1559 CZ TYR A 206 34.368 -20.210 0.254 1.00 78.72 A C ANISOU 1559 CZ TYR A 206 9889 9637 10383 -2283 13 62 A C ATOM 1560 OH TYR A 206 34.354 -20.304 -1.118 1.00 74.81 A O ANISOU 1560 OH TYR A 206 9332 9131 9958 -2215 -115 -65 A O ATOM 1561 N GLY A 207 35.022 -16.931 5.101 1.00 87.80 A N ANISOU 1561 N GLY A 207 11242 11148 10967 -2168 615 346 A N ATOM 1562 CA GLY A 207 35.559 -15.624 4.761 1.00 77.18 A C ANISOU 1562 CA GLY A 207 9878 9886 9560 -1980 623 251 A C ATOM 1563 C GLY A 207 37.070 -15.585 4.774 1.00 78.70 A C ANISOU 1563 C GLY A 207 10240 9980 9682 -1883 486 250 A C ATOM 1564 O GLY A 207 37.742 -16.607 4.568 1.00 72.49 A O ANISOU 1564 O GLY A 207 9544 9056 8942 -1905 346 288 A O ATOM 1565 N PRO A 208 37.641 -14.400 5.080 1.00 75.19 A N ANISOU 1565 N PRO A 208 9845 9601 9121 -1776 527 212 A N ATOM 1566 CA PRO A 208 39.097 -14.158 5.053 1.00 67.94 A C ANISOU 1566 CA PRO A 208 9051 8628 8136 -1685 398 209 A C ATOM 1567 C PRO A 208 39.931 -15.174 5.818 1.00 69.17 A C ANISOU 1567 C PRO A 208 9370 8671 8238 -1755 299 324 A C ATOM 1568 O PRO A 208 41.067 -15.427 5.432 1.00 77.42 A O ANISOU 1568 O PRO A 208 10461 9653 9299 -1673 153 328 A O ATOM 1569 CB PRO A 208 39.240 -12.761 5.626 1.00 62.84 A C ANISOU 1569 CB PRO A 208 8451 8071 7351 -1630 499 171 A C ATOM 1570 CG PRO A 208 37.945 -12.090 5.222 1.00 65.97 A C ANISOU 1570 CG PRO A 208 8689 8569 7805 -1598 648 101 A C ATOM 1571 CD PRO A 208 36.886 -13.150 5.214 1.00 70.92 A C ANISOU 1571 CD PRO A 208 9217 9195 8533 -1717 689 153 A C ATOM 1572 N PRO A 209 39.385 -15.745 6.899 1.00 71.00 A N ANISOU 1572 N PRO A 209 9686 8886 8404 -1896 383 428 A N ATOM 1573 CA PRO A 209 40.204 -16.700 7.658 1.00 78.41 A C ANISOU 1573 CA PRO A 209 10797 9711 9282 -1953 279 556 A C ATOM 1574 C PRO A 209 40.743 -17.871 6.836 1.00 77.65 A C ANISOU 1574 C PRO A 209 10707 9465 9330 -1912 114 572 A C ATOM 1575 O PRO A 209 41.745 -18.463 7.233 1.00 82.56 A O ANISOU 1575 O PRO A 209 11457 9998 9914 -1884 -5 661 A O ATOM 1576 CB PRO A 209 39.265 -17.161 8.755 1.00 74.61 A C ANISOU 1576 CB PRO A 209 10381 9239 8727 -2123 419 661 A C ATOM 1577 CG PRO A 209 38.422 -15.963 9.022 1.00 73.26 A C ANISOU 1577 CG PRO A 209 10127 9226 8482 -2116 608 588 A C ATOM 1578 CD PRO A 209 38.197 -15.321 7.659 1.00 70.73 A C ANISOU 1578 CD PRO A 209 9618 8953 8302 -1989 586 444 A C ATOM 1579 N ILE A 210 40.125 -18.211 5.710 1.00 73.13 A N ANISOU 1579 N ILE A 210 10006 8863 8914 -1899 100 487 A N ATOM 1580 CA ILE A 210 40.662 -19.338 4.928 1.00 80.78 A C ANISOU 1580 CA ILE A 210 11016 9670 10005 -1852 -51 485 A C ATOM 1581 C ILE A 210 42.009 -18.994 4.301 1.00 80.24 A C ANISOU 1581 C ILE A 210 10949 9601 9934 -1661 -174 435 A C ATOM 1582 O ILE A 210 42.883 -19.866 4.168 1.00 85.29 A O ANISOU 1582 O ILE A 210 11681 10113 10613 -1592 -297 484 A O ATOM 1583 CB ILE A 210 39.702 -19.846 3.822 1.00 67.56 A C ANISOU 1583 CB ILE A 210 9225 7955 8487 -1897 -57 394 A C ATOM 1584 CG1 ILE A 210 39.653 -18.846 2.661 1.00 71.84 A C ANISOU 1584 CG1 ILE A 210 9606 8622 9068 -1764 -59 245 A C ATOM 1585 CG2 ILE A 210 38.315 -20.155 4.379 1.00 68.31 A C ANISOU 1585 CG2 ILE A 210 9273 8079 8602 -2102 68 448 A C ATOM 1586 CD1 ILE A 210 38.881 -19.354 1.459 1.00 72.62 A C ANISOU 1586 CD1 ILE A 210 9601 8687 9304 -1791 -105 147 A C ATOM 1587 N ASP A 211 42.181 -17.728 3.921 1.00 68.28 A N ANISOU 1587 N ASP A 211 9334 8229 8377 -1573 -135 347 A N ATOM 1588 CA ASP A 211 43.451 -17.294 3.342 1.00 68.25 A C ANISOU 1588 CA ASP A 211 9312 8252 8365 -1412 -236 310 A C ATOM 1589 C ASP A 211 44.557 -17.293 4.392 1.00 71.47 A C ANISOU 1589 C ASP A 211 9837 8658 8659 -1404 -302 427 A C ATOM 1590 O ASP A 211 45.738 -17.558 4.098 1.00 68.71 A O ANISOU 1590 O ASP A 211 9496 8282 8328 -1287 -421 453 A O ATOM 1591 CB ASP A 211 43.319 -15.930 2.668 1.00 60.05 A C ANISOU 1591 CB ASP A 211 8150 7354 7312 -1339 -176 199 A C ATOM 1592 CG ASP A 211 42.582 -16.003 1.337 1.00 71.08 A C ANISOU 1592 CG ASP A 211 9423 8756 8828 -1294 -169 85 A C ATOM 1593 OD1 ASP A 211 42.534 -17.132 0.764 1.00 82.47 A O ANISOU 1593 OD1 ASP A 211 10885 10083 10366 -1290 -245 74 A O ATOM 1594 OD2 ASP A 211 42.068 -14.955 0.864 1.00 63.93 A O1- ANISOU 1594 OD2 ASP A 211 8414 7960 7915 -1260 -97 8 A O1- ATOM 1595 N LEU A 212 44.170 -17.020 5.634 1.00 69.06 A N ANISOU 1595 N LEU A 212 9619 8392 8229 -1529 -224 502 A N ATOM 1596 CA LEU A 212 45.157 -16.922 6.704 1.00 67.68 A C ANISOU 1596 CA LEU A 212 9563 8236 7915 -1541 -296 613 A C ATOM 1597 C LEU A 212 45.656 -18.294 7.149 1.00 71.18 A C ANISOU 1597 C LEU A 212 10122 8540 8383 -1544 -407 750 A C ATOM 1598 O LEU A 212 46.832 -18.451 7.508 1.00 69.40 A O ANISOU 1598 O LEU A 212 9944 8315 8108 -1475 -534 835 A O ATOM 1599 CB LEU A 212 44.599 -16.092 7.852 1.00 69.30 A C ANISOU 1599 CB LEU A 212 9844 8534 7951 -1664 -173 632 A C ATOM 1600 CG LEU A 212 44.814 -14.616 7.540 1.00 79.08 A C ANISOU 1600 CG LEU A 212 11015 9893 9135 -1611 -131 520 A C ATOM 1601 CD1 LEU A 212 43.745 -13.724 8.132 1.00106.99 A C ANISOU 1601 CD1 LEU A 212 14577 13504 12571 -1692 52 468 A C ATOM 1602 CD2 LEU A 212 46.185 -14.208 8.060 1.00 85.04 A C ANISOU 1602 CD2 LEU A 212 11839 10693 9778 -1589 -262 575 A C ATOM 1603 N TRP A 213 44.768 -19.288 7.107 1.00 71.07 A N ANISOU 1603 N TRP A 213 10148 8404 8450 -1625 -364 779 A N ATOM 1604 CA TRP A 213 45.178 -20.658 7.344 1.00 79.20 A C ANISOU 1604 CA TRP A 213 11300 9259 9530 -1615 -469 901 A C ATOM 1605 C TRP A 213 46.292 -20.996 6.384 1.00 73.68 A C ANISOU 1605 C TRP A 213 10552 8507 8936 -1415 -606 864 A C ATOM 1606 O TRP A 213 47.311 -21.592 6.765 1.00 70.77 A O ANISOU 1606 O TRP A 213 10262 8074 8551 -1327 -728 978 A O ATOM 1607 CB TRP A 213 44.020 -21.618 7.137 1.00 80.34 A C ANISOU 1607 CB TRP A 213 11478 9267 9779 -1737 -406 905 A C ATOM 1608 CG TRP A 213 44.457 -23.049 7.196 1.00 79.08 A C ANISOU 1608 CG TRP A 213 11463 8886 9694 -1710 -519 1013 A C ATOM 1609 CD1 TRP A 213 44.897 -23.815 6.160 1.00 79.12 A C ANISOU 1609 CD1 TRP A 213 11470 8745 9844 -1576 -618 954 A C ATOM 1610 CD2 TRP A 213 44.505 -23.876 8.361 1.00 88.46 A C ANISOU 1610 CD2 TRP A 213 12838 9965 10808 -1809 -542 1202 A C ATOM 1611 CE2 TRP A 213 44.971 -25.142 7.954 1.00 90.69 A C ANISOU 1611 CE2 TRP A 213 13230 10017 11210 -1723 -660 1253 A C ATOM 1612 CE3 TRP A 213 44.189 -23.674 9.708 1.00 87.66 A C ANISOU 1612 CE3 TRP A 213 12836 9931 10537 -1957 -469 1333 A C ATOM 1613 NE1 TRP A 213 45.215 -25.077 6.607 1.00 88.06 A N ANISOU 1613 NE1 TRP A 213 12783 9666 11008 -1577 -701 1091 A N ATOM 1614 CZ2 TRP A 213 45.135 -26.203 8.848 1.00 85.21 A C ANISOU 1614 CZ2 TRP A 213 12740 9151 10484 -1780 -714 1444 A C ATOM 1615 CZ3 TRP A 213 44.349 -24.724 10.597 1.00 96.52 A C ANISOU 1615 CZ3 TRP A 213 14155 10901 11614 -2024 -522 1525 A C ATOM 1616 CH2 TRP A 213 44.821 -25.978 10.157 1.00 91.61 A C ANISOU 1616 CH2 TRP A 213 13639 10041 11127 -1934 -648 1584 A C ATOM 1617 N GLY A 214 46.102 -20.604 5.123 1.00 75.94 A N ANISOU 1617 N GLY A 214 10701 8829 9323 -1333 -582 709 A N ATOM 1618 CA GLY A 214 47.122 -20.861 4.103 1.00 73.90 A C ANISOU 1618 CA GLY A 214 10384 8539 9155 -1133 -685 657 A C ATOM 1619 C GLY A 214 48.437 -20.140 4.428 1.00 83.04 A C ANISOU 1619 C GLY A 214 11491 9831 10228 -1029 -760 711 A C ATOM 1620 O GLY A 214 49.526 -20.665 4.175 1.00 82.96 A O ANISOU 1620 O GLY A 214 11475 9782 10263 -873 -867 761 A O ATOM 1621 N ALA A 215 48.322 -18.946 4.992 1.00 83.43 A N ANISOU 1621 N ALA A 215 11505 10037 10158 -1118 -702 700 A N ATOM 1622 CA ALA A 215 49.461 -18.149 5.370 1.00 78.35 A C ANISOU 1622 CA ALA A 215 10817 9530 9422 -1072 -776 745 A C ATOM 1623 C ALA A 215 50.252 -18.909 6.419 1.00 80.77 A C ANISOU 1623 C ALA A 215 11234 9789 9665 -1068 -897 921 A C ATOM 1624 O ALA A 215 51.482 -19.002 6.354 1.00 79.05 A O ANISOU 1624 O ALA A 215 10958 9619 9456 -945 -1019 987 A O ATOM 1625 CB ALA A 215 49.012 -16.791 5.939 1.00 77.57 A C ANISOU 1625 CB ALA A 215 10716 9566 9189 -1202 -684 698 A C ATOM 1626 N GLY A 216 49.526 -19.470 7.384 1.00 83.39 A N ANISOU 1626 N GLY A 216 11718 10035 9931 -1200 -861 1008 A N ATOM 1627 CA GLY A 216 50.127 -20.367 8.353 1.00 88.44 A C ANISOU 1627 CA GLY A 216 12489 10598 10513 -1196 -976 1191 A C ATOM 1628 C GLY A 216 50.943 -21.485 7.713 1.00 89.37 A C ANISOU 1628 C GLY A 216 12593 10586 10775 -1000 -1092 1243 A C ATOM 1629 O GLY A 216 52.124 -21.669 8.043 1.00 82.39 A O ANISOU 1629 O GLY A 216 11691 9745 9867 -887 -1230 1357 A O ATOM 1630 N CYS A 217 50.330 -22.240 6.804 1.00 86.22 A N ANISOU 1630 N CYS A 217 12205 10030 10524 -954 -1042 1161 A N ATOM 1631 CA CYS A 217 50.994 -23.368 6.163 1.00 86.33 A C ANISOU 1631 CA CYS A 217 12244 9884 10674 -759 -1133 1190 A C ATOM 1632 C CYS A 217 52.265 -22.941 5.450 1.00 88.94 A C ANISOU 1632 C CYS A 217 12405 10342 11045 -548 -1206 1157 A C ATOM 1633 O CYS A 217 53.273 -23.666 5.430 1.00105.01 A O ANISOU 1633 O CYS A 217 14444 12320 13133 -363 -1314 1254 A O ATOM 1634 CB CYS A 217 50.065 -24.051 5.149 1.00 83.62 A C ANISOU 1634 CB CYS A 217 11936 9366 10469 -764 -1060 1060 A C ATOM 1635 SG CYS A 217 48.579 -24.743 5.896 1.00 99.66 A S ANISOU 1635 SG CYS A 217 14146 11235 12485 -1022 -977 1116 A S ATOM 1636 N ILE A 218 52.207 -21.758 4.852 1.00 77.16 A N ANISOU 1636 N ILE A 218 10759 9024 9532 -571 -1140 1027 A N ATOM 1637 CA ILE A 218 53.350 -21.224 4.130 1.00 77.42 A C ANISOU 1637 CA ILE A 218 10613 9202 9598 -402 -1188 994 A C ATOM 1638 C ILE A 218 54.432 -20.766 5.100 1.00 84.79 A C ANISOU 1638 C ILE A 218 11498 10291 10427 -407 -1304 1142 A C ATOM 1639 O ILE A 218 55.624 -20.993 4.868 1.00 90.15 A O ANISOU 1639 O ILE A 218 12067 11032 11153 -231 -1399 1212 A O ATOM 1640 CB ILE A 218 52.940 -20.044 3.226 1.00 78.55 A C ANISOU 1640 CB ILE A 218 10624 9480 9741 -444 -1083 826 A C ATOM 1641 CG1 ILE A 218 52.031 -20.524 2.122 1.00 85.99 A C ANISOU 1641 CG1 ILE A 218 11589 10294 10789 -411 -999 681 A C ATOM 1642 CG2 ILE A 218 54.185 -19.368 2.655 1.00 68.02 A C ANISOU 1642 CG2 ILE A 218 9104 8322 8418 -308 -1128 823 A C ATOM 1643 CD1 ILE A 218 51.257 -19.417 1.438 1.00 86.68 A C ANISOU 1643 CD1 ILE A 218 11585 10489 10857 -495 -890 534 A C ATOM 1644 N MET A 219 54.019 -20.110 6.185 1.00 80.88 A N ANISOU 1644 N MET A 219 11078 9867 9782 -609 -1295 1189 A N ATOM 1645 CA MET A 219 54.987 -19.641 7.153 1.00 82.58 A C ANISOU 1645 CA MET A 219 11267 10234 9876 -647 -1421 1321 A C ATOM 1646 C MET A 219 55.817 -20.824 7.645 1.00 86.71 A C ANISOU 1646 C MET A 219 11839 10676 10430 -506 -1567 1503 A C ATOM 1647 O MET A 219 57.044 -20.793 7.604 1.00 89.06 A O ANISOU 1647 O MET A 219 11999 11091 10748 -374 -1690 1589 A O ATOM 1648 CB MET A 219 54.322 -18.916 8.322 1.00 82.77 A C ANISOU 1648 CB MET A 219 11421 10312 9713 -885 -1384 1339 A C ATOM 1649 CG MET A 219 55.339 -18.257 9.255 1.00 89.52 A C ANISOU 1649 CG MET A 219 12252 11342 10419 -949 -1526 1447 A C ATOM 1650 SD MET A 219 54.618 -17.254 10.549 1.00 97.04 A S ANISOU 1650 SD MET A 219 13377 12366 11125 -1220 -1470 1433 A S ATOM 1651 CE MET A 219 56.087 -16.736 11.441 1.00 91.22 A C ANISOU 1651 CE MET A 219 12594 11822 10240 -1263 -1697 1569 A C ATOM 1652 N ALA A 220 55.140 -21.876 8.099 1.00 85.53 A N ANISOU 1652 N ALA A 220 11879 10324 10291 -531 -1553 1571 A N ATOM 1653 CA ALA A 220 55.825 -23.069 8.602 1.00 89.41 A C ANISOU 1653 CA ALA A 220 12455 10700 10814 -391 -1688 1757 A C ATOM 1654 C ALA A 220 56.778 -23.621 7.544 1.00 91.46 A C ANISOU 1654 C ALA A 220 12571 10934 11244 -104 -1737 1742 A C ATOM 1655 O ALA A 220 57.866 -24.114 7.838 1.00 93.19 A O ANISOU 1655 O ALA A 220 12738 11184 11484 65 -1876 1894 A O ATOM 1656 CB ALA A 220 54.806 -24.132 8.993 1.00 87.67 A C ANISOU 1656 CB ALA A 220 12471 10227 10609 -468 -1634 1806 A C ATOM 1657 N GLU A 221 56.353 -23.486 6.289 1.00 86.44 A N ANISOU 1657 N GLU A 221 11863 10257 10720 -45 -1616 1555 A N ATOM 1658 CA GLU A 221 57.088 -24.035 5.154 1.00 82.54 A C ANISOU 1658 CA GLU A 221 11259 9722 10380 229 -1621 1505 A C ATOM 1659 C GLU A 221 58.400 -23.276 4.922 1.00 86.89 A C ANISOU 1659 C GLU A 221 11553 10535 10926 349 -1690 1543 A C ATOM 1660 O GLU A 221 59.303 -23.784 4.269 1.00 88.29 A O ANISOU 1660 O GLU A 221 11616 10718 11209 605 -1721 1566 A O ATOM 1661 CB GLU A 221 56.204 -23.962 3.915 1.00 84.13 A C ANISOU 1661 CB GLU A 221 11464 9836 10664 222 -1474 1288 A C ATOM 1662 CG GLU A 221 56.649 -24.763 2.719 1.00 88.89 A C ANISOU 1662 CG GLU A 221 12039 10324 11411 489 -1452 1208 A C ATOM 1663 CD GLU A 221 55.485 -25.091 1.781 1.00104.28 A C ANISOU 1663 CD GLU A 221 14099 12098 13423 434 -1338 1020 A C ATOM 1664 OE1 GLU A 221 54.322 -25.059 2.244 1.00 99.62 A O ANISOU 1664 OE1 GLU A 221 13636 11425 12790 203 -1295 998 A O ATOM 1665 OE2 GLU A 221 55.731 -25.403 0.593 1.00121.17 A O1- ANISOU 1665 OE2 GLU A 221 16198 14191 15648 619 -1293 897 A O1- ATOM 1666 N MET A 222 58.506 -22.078 5.495 1.00 87.51 A N ANISOU 1666 N MET A 222 11546 10825 10876 159 -1713 1555 A N ATOM 1667 CA MET A 222 59.716 -21.263 5.349 1.00 84.49 A C ANISOU 1667 CA MET A 222 10916 10703 10481 216 -1787 1599 A C ATOM 1668 C MET A 222 60.913 -21.885 6.079 1.00 95.77 A C ANISOU 1668 C MET A 222 12279 12197 11912 362 -1970 1817 A C ATOM 1669 O MET A 222 62.060 -21.573 5.760 1.00116.49 A O ANISOU 1669 O MET A 222 14663 15016 14579 487 -2036 1872 A O ATOM 1670 CB MET A 222 59.474 -19.834 5.877 1.00 79.51 A C ANISOU 1670 CB MET A 222 10256 10249 9703 -52 -1778 1556 A C ATOM 1671 CG MET A 222 58.464 -19.033 5.052 1.00 82.96 A C ANISOU 1671 CG MET A 222 10705 10667 10147 -162 -1605 1350 A C ATOM 1672 SD MET A 222 59.086 -18.539 3.426 1.00 86.73 A S ANISOU 1672 SD MET A 222 10938 11267 10747 7 -1521 1228 A S ATOM 1673 CE MET A 222 60.514 -17.537 3.881 1.00 78.28 A C ANISOU 1673 CE MET A 222 9642 10489 9612 -48 -1654 1349 A C ATOM 1674 N TRP A 223 60.634 -22.759 7.049 1.00 86.34 A N ANISOU 1674 N TRP A 223 11288 10845 10671 344 -2049 1951 A N ATOM 1675 CA TRP A 223 61.691 -23.483 7.745 1.00 88.21 A C ANISOU 1675 CA TRP A 223 11486 11115 10914 507 -2231 2175 A C ATOM 1676 C TRP A 223 61.736 -24.945 7.308 1.00 93.83 A C ANISOU 1676 C TRP A 223 12304 11569 11775 782 -2220 2218 A C ATOM 1677 O TRP A 223 62.799 -25.461 7.006 1.00 96.90 A O ANISOU 1677 O TRP A 223 12546 12005 12265 1054 -2295 2314 A O ATOM 1678 CB TRP A 223 61.503 -23.412 9.265 1.00 97.61 A C ANISOU 1678 CB TRP A 223 12842 12325 11919 300 -2357 2331 A C ATOM 1679 CG TRP A 223 61.863 -22.088 9.863 1.00 98.61 A C ANISOU 1679 CG TRP A 223 12856 12722 11888 78 -2430 2336 A C ATOM 1680 CD1 TRP A 223 63.100 -21.676 10.270 1.00 93.93 A C ANISOU 1680 CD1 TRP A 223 12061 12375 11252 105 -2610 2470 A C ATOM 1681 CD2 TRP A 223 60.971 -20.990 10.119 1.00 94.83 A C ANISOU 1681 CD2 TRP A 223 12468 12290 11272 -209 -2328 2196 A C ATOM 1682 CE2 TRP A 223 61.746 -19.937 10.644 1.00 92.36 A C ANISOU 1682 CE2 TRP A 223 12023 12232 10836 -346 -2452 2240 A C ATOM 1683 CE3 TRP A 223 59.596 -20.793 9.933 1.00 83.29 A C ANISOU 1683 CE3 TRP A 223 11178 10681 9786 -356 -2144 2038 A C ATOM 1684 NE1 TRP A 223 63.040 -20.385 10.728 1.00 94.42 A N ANISOU 1684 NE1 TRP A 223 12097 12618 11158 -163 -2630 2411 A N ATOM 1685 CZ2 TRP A 223 61.194 -18.704 10.983 1.00 85.60 A C ANISOU 1685 CZ2 TRP A 223 11232 11461 9831 -614 -2390 2122 A C ATOM 1686 CZ3 TRP A 223 59.047 -19.573 10.269 1.00 77.08 A C ANISOU 1686 CZ3 TRP A 223 10430 9999 8859 -601 -2077 1931 A C ATOM 1687 CH2 TRP A 223 59.844 -18.545 10.798 1.00 81.88 A C ANISOU 1687 CH2 TRP A 223 10936 10833 9341 -723 -2196 1969 A C ATOM 1688 N THR A 224 60.574 -25.590 7.258 1.00 93.66 A N ANISOU 1688 N THR A 224 12537 11276 11770 707 -2121 2145 A N ATOM 1689 CA THR A 224 60.514 -27.005 6.919 1.00 92.27 A C ANISOU 1689 CA THR A 224 12520 10810 11726 932 -2114 2181 A C ATOM 1690 C THR A 224 60.830 -27.256 5.447 1.00 93.36 A C ANISOU 1690 C THR A 224 12539 10907 12026 1183 -2011 2022 A C ATOM 1691 O THR A 224 61.073 -28.387 5.045 1.00 99.84 A O ANISOU 1691 O THR A 224 13457 11511 12965 1432 -2014 2046 A O ATOM 1692 CB THR A 224 59.137 -27.638 7.233 1.00 96.57 A C ANISOU 1692 CB THR A 224 13373 11069 12250 748 -2036 2143 A C ATOM 1693 CG2 THR A 224 58.744 -27.369 8.686 1.00 93.86 A C ANISOU 1693 CG2 THR A 224 13162 10773 11724 491 -2108 2294 A C ATOM 1694 OG1 THR A 224 58.134 -27.110 6.352 1.00105.37 A O ANISOU 1694 OG1 THR A 224 14484 12161 13390 608 -1869 1908 A O ATOM 1695 N ARG A 225 60.830 -26.194 4.644 1.00 88.34 A N ANISOU 1695 N ARG A 225 11709 10470 11384 1121 -1916 1860 A N ATOM 1696 CA ARG A 225 61.179 -26.324 3.242 1.00 91.90 A C ANISOU 1696 CA ARG A 225 12038 10921 11959 1351 -1811 1712 A C ATOM 1697 C ARG A 225 60.280 -27.328 2.511 1.00 99.08 A C ANISOU 1697 C ARG A 225 13187 11501 12956 1418 -1711 1572 A C ATOM 1698 O ARG A 225 60.641 -27.855 1.470 1.00 92.66 A O ANISOU 1698 O ARG A 225 12350 10608 12247 1669 -1647 1477 A O ATOM 1699 CB ARG A 225 62.631 -26.748 3.123 1.00 82.52 A C ANISOU 1699 CB ARG A 225 10657 9844 10852 1674 -1897 1850 A C ATOM 1700 CG ARG A 225 63.601 -25.652 3.495 1.00 80.06 A C ANISOU 1700 CG ARG A 225 10047 9896 10475 1613 -1981 1949 A C ATOM 1701 CD ARG A 225 63.741 -24.654 2.366 1.00 79.34 A C ANISOU 1701 CD ARG A 225 9740 10003 10399 1596 -1851 1781 A C ATOM 1702 NE ARG A 225 64.755 -23.656 2.700 1.00 79.92 A N ANISOU 1702 NE ARG A 225 9524 10417 10425 1534 -1939 1889 A N ATOM 1703 CZ ARG A 225 65.590 -23.121 1.813 1.00 93.79 A C ANISOU 1703 CZ ARG A 225 11001 12397 12238 1657 -1877 1854 A C ATOM 1704 NH1 ARG A 225 65.555 -23.513 0.542 1.00 91.85 A N1+ ANISOU 1704 NH1 ARG A 225 10739 12072 12085 1874 -1722 1711 A N1+ ATOM 1705 NH2 ARG A 225 66.479 -22.214 2.207 1.00108.44 A N ANISOU 1705 NH2 ARG A 225 12597 14555 14047 1557 -1973 1965 A N ATOM 1706 N SER A 226 59.089 -27.553 3.057 1.00101.09 A N ANISOU 1706 N SER A 226 13674 11574 13161 1176 -1694 1554 A N ATOM 1707 CA SER A 226 58.191 -28.554 2.517 1.00 99.74 A C ANISOU 1707 CA SER A 226 13746 11079 13069 1189 -1625 1443 A C ATOM 1708 C SER A 226 56.821 -28.435 3.179 1.00108.65 A C ANISOU 1708 C SER A 226 15053 12106 14122 850 -1592 1428 A C ATOM 1709 O SER A 226 56.729 -28.209 4.385 1.00124.75 A O ANISOU 1709 O SER A 226 17133 14206 16059 687 -1658 1583 A O ATOM 1710 CB SER A 226 58.775 -29.944 2.723 1.00101.43 A C ANISOU 1710 CB SER A 226 14118 11042 13376 1448 -1705 1573 A C ATOM 1711 OG SER A 226 57.955 -30.934 2.106 1.00115.77 A O ANISOU 1711 OG SER A 226 16188 12521 15275 1460 -1642 1449 A O ATOM 1712 N PRO A 227 55.752 -28.598 2.378 1.00 98.83 A N ANISOU 1712 N PRO A 227 13911 10717 12922 746 -1488 1242 A N ATOM 1713 CA PRO A 227 54.378 -28.481 2.874 1.00105.63 A C ANISOU 1713 CA PRO A 227 14905 11499 13728 427 -1436 1215 A C ATOM 1714 C PRO A 227 54.092 -29.402 4.061 1.00112.76 A C ANISOU 1714 C PRO A 227 16038 12195 14608 330 -1505 1407 A C ATOM 1715 O PRO A 227 54.145 -30.618 3.930 1.00117.00 A O ANISOU 1715 O PRO A 227 16767 12449 15237 449 -1542 1446 A O ATOM 1716 CB PRO A 227 53.533 -28.878 1.659 1.00103.32 A C ANISOU 1716 CB PRO A 227 14690 11040 13524 413 -1350 1000 A C ATOM 1717 CG PRO A 227 54.398 -28.535 0.494 1.00102.26 A C ANISOU 1717 CG PRO A 227 14385 11033 13433 666 -1324 878 A C ATOM 1718 CD PRO A 227 55.801 -28.819 0.925 1.00 89.33 A C ANISOU 1718 CD PRO A 227 12678 9451 11812 921 -1413 1043 A C ATOM 1719 N ILE A 228 53.799 -28.794 5.204 1.00102.43 A N ANISOU 1719 N ILE A 228 14724 11025 13169 116 -1517 1525 A N ATOM 1720 CA ILE A 228 53.649 -29.500 6.475 1.00 91.14 A C ANISOU 1720 CA ILE A 228 13496 9457 11676 17 -1586 1740 A C ATOM 1721 C ILE A 228 52.590 -30.603 6.501 1.00 96.46 A C ANISOU 1721 C ILE A 228 14425 9807 12416 -116 -1543 1743 A C ATOM 1722 O ILE A 228 52.720 -31.563 7.275 1.00106.39 A O ANISOU 1722 O ILE A 228 15887 10864 13672 -102 -1617 1929 A O ATOM 1723 CB ILE A 228 53.360 -28.500 7.605 1.00 99.93 A C ANISOU 1723 CB ILE A 228 14561 10799 12607 -218 -1575 1824 A C ATOM 1724 CG1 ILE A 228 52.090 -27.695 7.302 1.00112.44 A C ANISOU 1724 CG1 ILE A 228 16095 12467 14159 -465 -1423 1654 A C ATOM 1725 CG2 ILE A 228 54.531 -27.551 7.790 1.00102.51 A C ANISOU 1725 CG2 ILE A 228 14674 11414 12859 -105 -1657 1865 A C ATOM 1726 CD1 ILE A 228 51.599 -26.897 8.520 1.00 95.95 A C ANISOU 1726 CD1 ILE A 228 14026 10543 11884 -708 -1385 1738 A C ATOM 1727 N MET A 229 51.524 -30.452 5.713 1.00104.44 A N ANISOU 1727 N MET A 229 15427 10773 13480 -265 -1432 1552 A N ATOM 1728 CA MET A 229 50.430 -31.430 5.699 1.00103.57 A C ANISOU 1728 CA MET A 229 15538 10375 13437 -441 -1393 1545 A C ATOM 1729 C MET A 229 50.031 -31.891 4.294 1.00103.19 A C ANISOU 1729 C MET A 229 15515 10161 13528 -380 -1356 1326 A C ATOM 1730 O MET A 229 49.211 -31.245 3.636 1.00109.12 A O ANISOU 1730 O MET A 229 16148 11029 14284 -521 -1272 1153 A O ATOM 1731 CB MET A 229 49.215 -30.861 6.426 1.00 99.30 A C ANISOU 1731 CB MET A 229 14987 9944 12796 -780 -1293 1566 A C ATOM 1732 CG MET A 229 49.510 -30.634 7.913 1.00 98.73 A C ANISOU 1732 CG MET A 229 14968 9979 12565 -862 -1329 1794 A C ATOM 1733 SD MET A 229 48.225 -29.784 8.811 1.00109.89 A S ANISOU 1733 SD MET A 229 16348 11575 13829 -1216 -1186 1812 A S ATOM 1734 CE MET A 229 48.206 -28.207 7.962 1.00106.25 A C ANISOU 1734 CE MET A 229 15588 11432 13348 -1180 -1109 1580 A C ATOM 1735 N GLN A 230 50.613 -33.000 3.851 1.00110.63 A N ANISOU 1735 N GLN A 230 16623 10833 14576 -163 -1424 1334 A N ATOM 1736 CA GLN A 230 50.413 -33.475 2.477 1.00113.52 A C ANISOU 1736 CA GLN A 230 17040 11034 15057 -64 -1402 1114 A C ATOM 1737 C GLN A 230 49.393 -34.591 2.370 1.00125.35 A C ANISOU 1737 C GLN A 230 18806 12184 16637 -257 -1402 1088 A C ATOM 1738 O GLN A 230 49.742 -35.710 2.005 1.00130.67 A O ANISOU 1738 O GLN A 230 19702 12543 17403 -97 -1456 1081 A O ATOM 1739 CB GLN A 230 51.753 -33.948 1.907 1.00115.52 A C ANISOU 1739 CB GLN A 230 17304 11213 15375 331 -1461 1106 A C ATOM 1740 CG GLN A 230 52.878 -32.969 2.133 1.00119.09 A C ANISOU 1740 CG GLN A 230 17491 11998 15757 515 -1479 1174 A C ATOM 1741 CD GLN A 230 54.107 -33.279 1.300 1.00112.39 A C ANISOU 1741 CD GLN A 230 16585 11136 14981 905 -1502 1122 A C ATOM 1742 NE2 GLN A 230 55.218 -32.641 1.638 1.00112.82 A N ANISOU 1742 NE2 GLN A 230 16422 11452 14991 1077 -1542 1231 A N ATOM 1743 OE1 GLN A 230 54.058 -34.070 0.362 1.00115.99 A O ANISOU 1743 OE1 GLN A 230 17186 11356 15526 1045 -1482 982 A O ATOM 1744 N GLY A 231 48.126 -34.281 2.651 1.00130.67 A N ANISOU 1744 N GLY A 231 19455 12912 17279 -600 -1338 1069 A N ATOM 1745 CA GLY A 231 47.059 -35.277 2.530 1.00131.02 A C ANISOU 1745 CA GLY A 231 19724 12651 17403 -837 -1337 1043 A C ATOM 1746 C GLY A 231 46.890 -35.826 1.119 1.00132.98 A C ANISOU 1746 C GLY A 231 20062 12708 17756 -757 -1358 805 A C ATOM 1747 O GLY A 231 47.387 -35.251 0.154 1.00118.03 A O ANISOU 1747 O GLY A 231 18016 10972 15857 -555 -1345 636 A O ATOM 1748 N ASN A 232 46.219 -36.966 0.995 1.00143.82 A N ANISOU 1748 N ASN A 232 21699 13729 19215 -917 -1392 793 A N ATOM 1749 CA ASN A 232 45.915 -37.550 -0.313 1.00131.73 A C ANISOU 1749 CA ASN A 232 20293 11989 17767 -893 -1422 554 A C ATOM 1750 C ASN A 232 44.441 -37.367 -0.685 1.00138.26 A C ANISOU 1750 C ASN A 232 21055 12865 18612 -1274 -1393 436 A C ATOM 1751 O ASN A 232 44.076 -37.275 -1.843 1.00132.21 A O ANISOU 1751 O ASN A 232 20254 12110 17868 -1285 -1407 208 A O ATOM 1752 CB ASN A 232 46.228 -39.035 -0.324 1.00126.90 A C ANISOU 1752 CB ASN A 232 20059 10906 17249 -798 -1498 597 A C ATOM 1753 CG ASN A 232 47.707 -39.324 -0.295 1.00142.74 A C ANISOU 1753 CG ASN A 232 22131 12840 19263 -361 -1532 663 A C ATOM 1754 ND2 ASN A 232 48.473 -38.571 -1.078 1.00150.81 A N ANISOU 1754 ND2 ASN A 232 22939 14110 20249 -87 -1503 525 A N ATOM 1755 OD1 ASN A 232 48.158 -40.220 0.414 1.00159.25 A O ANISOU 1755 OD1 ASN A 232 24454 14658 21392 -268 -1584 846 A O ATOM 1756 N THR A 233 43.613 -37.362 0.350 1.00149.73 A N ANISOU 1756 N THR A 233 22495 14346 20048 -1583 -1356 608 A N ATOM 1757 CA THR A 233 42.193 -37.080 0.214 1.00128.63 A C ANISOU 1757 CA THR A 233 19700 11783 17390 -1956 -1314 544 A C ATOM 1758 C THR A 233 41.778 -36.184 1.380 1.00125.02 A C ANISOU 1758 C THR A 233 19029 11630 16840 -2122 -1213 723 A C ATOM 1759 O THR A 233 42.529 -35.999 2.340 1.00127.69 A O ANISOU 1759 O THR A 233 19382 12027 17105 -1990 -1196 903 A O ATOM 1760 CB THR A 233 41.340 -38.373 0.239 1.00120.03 A C ANISOU 1760 CB THR A 233 18889 10313 16402 -2246 -1367 567 A C ATOM 1761 CG2 THR A 233 41.867 -39.378 -0.770 1.00118.20 A C ANISOU 1761 CG2 THR A 233 18941 9720 16249 -2058 -1469 404 A C ATOM 1762 OG1 THR A 233 41.365 -38.944 1.564 1.00128.91 A O ANISOU 1762 OG1 THR A 233 20176 11286 17516 -2359 -1349 841 A O ATOM 1763 N GLU A 234 40.572 -35.639 1.285 1.00114.73 A N ANISOU 1763 N GLU A 234 17532 10522 15537 -2406 -1147 669 A N ATOM 1764 CA GLU A 234 40.039 -34.795 2.346 1.00112.87 A C ANISOU 1764 CA GLU A 234 17102 10571 15211 -2572 -1029 819 A C ATOM 1765 C GLU A 234 40.098 -35.451 3.724 1.00126.39 A C ANISOU 1765 C GLU A 234 19005 12129 16885 -2691 -1004 1086 A C ATOM 1766 O GLU A 234 40.448 -34.799 4.717 1.00131.69 A O ANISOU 1766 O GLU A 234 19599 12999 17438 -2642 -938 1233 A O ATOM 1767 CB GLU A 234 38.617 -34.366 1.972 1.00110.96 A C ANISOU 1767 CB GLU A 234 16649 10506 15005 -2871 -967 726 A C ATOM 1768 CG GLU A 234 38.486 -34.194 0.434 1.00118.09 A C ANISOU 1768 CG GLU A 234 17466 11433 15968 -2788 -1042 459 A C ATOM 1769 CD GLU A 234 37.450 -33.164 0.065 1.00131.97 A C ANISOU 1769 CD GLU A 234 18904 13523 17713 -2938 -972 367 A C ATOM 1770 OE1 GLU A 234 36.604 -32.864 0.932 1.00132.78 A O ANISOU 1770 OE1 GLU A 234 18880 13775 17796 -3167 -866 499 A O ATOM 1771 OE2 GLU A 234 37.505 -32.639 -1.071 1.00142.91 A O1- ANISOU 1771 OE2 GLU A 234 20166 15029 19102 -2810 -1015 171 A O1- ATOM 1772 N GLN A 235 39.773 -36.739 3.784 1.00131.02 A N ANISOU 1772 N GLN A 235 19860 12355 17563 -2851 -1063 1151 A N ATOM 1773 CA GLN A 235 39.830 -37.453 5.063 1.00135.37 A C ANISOU 1773 CA GLN A 235 20626 12728 18077 -2968 -1045 1422 A C ATOM 1774 C GLN A 235 41.264 -37.583 5.567 1.00129.15 A C ANISOU 1774 C GLN A 235 19979 11866 17226 -2626 -1111 1543 A C ATOM 1775 O GLN A 235 41.529 -37.456 6.769 1.00132.87 A O ANISOU 1775 O GLN A 235 20488 12410 17585 -2640 -1074 1766 A O ATOM 1776 CB GLN A 235 39.183 -38.832 4.962 1.00133.69 A C ANISOU 1776 CB GLN A 235 20694 12115 17987 -3221 -1101 1467 A C ATOM 1777 CG GLN A 235 37.679 -38.803 4.975 1.00139.62 A C ANISOU 1777 CG GLN A 235 21310 12957 18783 -3643 -1021 1459 A C ATOM 1778 CD GLN A 235 37.069 -40.063 5.552 1.00159.02 A C ANISOU 1778 CD GLN A 235 24044 15067 21308 -3957 -1034 1638 A C ATOM 1779 NE2 GLN A 235 35.852 -39.940 6.062 1.00180.15 A N ANISOU 1779 NE2 GLN A 235 26577 17888 23983 -4335 -922 1733 A N ATOM 1780 OE1 GLN A 235 37.680 -41.135 5.536 1.00162.68 A O ANISOU 1780 OE1 GLN A 235 24847 15135 21829 -3860 -1137 1694 A O ATOM 1781 N HIS A 236 42.190 -37.836 4.642 1.00118.14 A N ANISOU 1781 N HIS A 236 18655 10337 15893 -2315 -1209 1400 A N ATOM 1782 CA HIS A 236 43.589 -37.920 5.002 1.00121.33 A C ANISOU 1782 CA HIS A 236 19144 10703 16252 -1963 -1276 1504 A C ATOM 1783 C HIS A 236 44.087 -36.557 5.477 1.00125.41 A C ANISOU 1783 C HIS A 236 19378 11640 16629 -1843 -1221 1534 A C ATOM 1784 O HIS A 236 44.852 -36.453 6.448 1.00156.17 A O ANISOU 1784 O HIS A 236 23311 15595 20429 -1723 -1246 1727 A O ATOM 1785 CB HIS A 236 44.423 -38.428 3.821 1.00123.73 A C ANISOU 1785 CB HIS A 236 19553 10803 16653 -1647 -1368 1325 A C ATOM 1786 CG HIS A 236 45.846 -38.735 4.188 1.00145.62 A C ANISOU 1786 CG HIS A 236 22430 13490 19408 -1279 -1442 1454 A C ATOM 1787 CD2 HIS A 236 46.403 -39.071 5.379 1.00142.83 A C ANISOU 1787 CD2 HIS A 236 22200 13074 18994 -1220 -1479 1722 A C ATOM 1788 ND1 HIS A 236 46.889 -38.637 3.291 1.00148.91 A N ANISOU 1788 ND1 HIS A 236 22796 13920 19860 -910 -1486 1312 A N ATOM 1789 CE1 HIS A 236 48.019 -38.947 3.898 1.00141.05 A C ANISOU 1789 CE1 HIS A 236 21880 12865 18845 -636 -1550 1489 A C ATOM 1790 NE2 HIS A 236 47.753 -39.214 5.167 1.00132.61 A N ANISOU 1790 NE2 HIS A 236 20922 11746 17715 -817 -1557 1740 A N ATOM 1791 N GLN A 237 43.629 -35.510 4.798 1.00102.09 A N ANISOU 1791 N GLN A 237 16154 8974 13660 -1886 -1155 1345 A N ATOM 1792 CA GLN A 237 43.992 -34.143 5.163 1.00 99.74 A C ANISOU 1792 CA GLN A 237 15596 9063 13236 -1801 -1096 1349 A C ATOM 1793 C GLN A 237 43.460 -33.824 6.551 1.00108.17 A C ANISOU 1793 C GLN A 237 16656 10265 14179 -2029 -1011 1551 A C ATOM 1794 O GLN A 237 44.186 -33.281 7.400 1.00129.46 A O ANISOU 1794 O GLN A 237 19317 13123 16746 -1921 -1017 1679 A O ATOM 1795 CB GLN A 237 43.430 -33.142 4.144 1.00110.51 A C ANISOU 1795 CB GLN A 237 16697 10673 14615 -1832 -1034 1114 A C ATOM 1796 CG GLN A 237 44.165 -31.814 4.109 1.00 99.75 A C ANISOU 1796 CG GLN A 237 15102 9643 13155 -1640 -1008 1066 A C ATOM 1797 CD GLN A 237 45.583 -31.937 3.564 1.00108.69 A C ANISOU 1797 CD GLN A 237 16255 10731 14309 -1288 -1102 1028 A C ATOM 1798 NE2 GLN A 237 46.490 -31.155 4.144 1.00 92.79 A N ANISOU 1798 NE2 GLN A 237 14129 8930 12193 -1142 -1112 1116 A N ATOM 1799 OE1 GLN A 237 45.873 -32.693 2.609 1.00136.05 A O ANISOU 1799 OE1 GLN A 237 19829 13984 17879 -1145 -1163 916 A O ATOM 1800 N LEU A 238 42.190 -34.157 6.791 1.00109.20 A N ANISOU 1800 N LEU A 238 16817 10336 14337 -2353 -931 1583 A N ATOM 1801 CA LEU A 238 41.583 -33.898 8.092 1.00113.28 A C ANISOU 1801 CA LEU A 238 17331 10983 14727 -2583 -823 1774 A C ATOM 1802 C LEU A 238 42.268 -34.684 9.197 1.00113.68 A C ANISOU 1802 C LEU A 238 17642 10846 14705 -2539 -886 2031 A C ATOM 1803 O LEU A 238 42.450 -34.194 10.310 1.00114.93 A O ANISOU 1803 O LEU A 238 17792 11176 14697 -2568 -839 2188 A O ATOM 1804 CB LEU A 238 40.086 -34.176 8.082 1.00116.86 A C ANISOU 1804 CB LEU A 238 17747 11412 15239 -2941 -718 1767 A C ATOM 1805 CG LEU A 238 39.199 -32.923 7.937 1.00111.34 A C ANISOU 1805 CG LEU A 238 16734 11074 14493 -3058 -576 1648 A C ATOM 1806 CD1 LEU A 238 37.738 -33.298 7.771 1.00124.63 A C ANISOU 1806 CD1 LEU A 238 18352 12734 16267 -3397 -491 1635 A C ATOM 1807 CD2 LEU A 238 39.370 -31.993 9.138 1.00100.57 A C ANISOU 1807 CD2 LEU A 238 15300 9977 12932 -3050 -469 1777 A C ATOM 1808 N ALA A 239 42.739 -35.879 8.861 1.00115.11 A N ANISOU 1808 N ALA A 239 18063 10672 14998 -2437 -1004 2069 A N ATOM 1809 CA ALA A 239 43.485 -36.672 9.821 1.00132.63 A C ANISOU 1809 CA ALA A 239 20539 12691 17161 -2348 -1086 2319 A C ATOM 1810 C ALA A 239 44.787 -35.954 10.156 1.00128.40 A C ANISOU 1810 C ALA A 239 19908 12365 16513 -2040 -1158 2362 A C ATOM 1811 O ALA A 239 45.094 -35.725 11.325 1.00123.73 A O ANISOU 1811 O ALA A 239 19361 11889 15761 -2062 -1159 2562 A O ATOM 1812 CB ALA A 239 43.737 -38.065 9.294 1.00141.70 A C ANISOU 1812 CB ALA A 239 21971 13400 18468 -2269 -1196 2332 A C ATOM 1813 N LEU A 240 45.523 -35.579 9.116 1.00127.54 A N ANISOU 1813 N LEU A 240 19660 12318 16479 -1771 -1218 2172 A N ATOM 1814 CA LEU A 240 46.816 -34.925 9.294 1.00120.18 A C ANISOU 1814 CA LEU A 240 18610 11585 15465 -1478 -1297 2202 A C ATOM 1815 C LEU A 240 46.680 -33.673 10.153 1.00115.88 A C ANISOU 1815 C LEU A 240 17886 11408 14732 -1594 -1222 2249 A C ATOM 1816 O LEU A 240 47.451 -33.472 11.106 1.00112.49 A O ANISOU 1816 O LEU A 240 17491 11081 14167 -1509 -1289 2423 A O ATOM 1817 CB LEU A 240 47.448 -34.569 7.942 1.00111.27 A C ANISOU 1817 CB LEU A 240 17317 10514 14444 -1215 -1333 1967 A C ATOM 1818 CG LEU A 240 47.997 -35.762 7.164 1.00107.05 A C ANISOU 1818 CG LEU A 240 16976 9631 14067 -993 -1426 1930 A C ATOM 1819 CD1 LEU A 240 48.544 -35.355 5.811 1.00 98.25 A C ANISOU 1819 CD1 LEU A 240 15694 8601 13033 -748 -1434 1688 A C ATOM 1820 CD2 LEU A 240 49.078 -36.371 8.027 1.00110.87 A C ANISOU 1820 CD2 LEU A 240 17612 10000 14511 -783 -1542 2173 A C ATOM 1821 N ILE A 241 45.696 -32.841 9.814 1.00112.91 A N ANISOU 1821 N ILE A 241 17331 11224 14344 -1784 -1089 2093 A N ATOM 1822 CA ILE A 241 45.421 -31.598 10.550 1.00103.10 A C ANISOU 1822 CA ILE A 241 15931 10315 12927 -1900 -991 2104 A C ATOM 1823 C ILE A 241 45.148 -31.880 12.037 1.00106.53 A C ANISOU 1823 C ILE A 241 16538 10741 13196 -2083 -956 2353 A C ATOM 1824 O ILE A 241 45.589 -31.125 12.915 1.00102.10 A O ANISOU 1824 O ILE A 241 15944 10397 12451 -2066 -958 2437 A O ATOM 1825 CB ILE A 241 44.204 -30.835 9.953 1.00101.59 A C ANISOU 1825 CB ILE A 241 15543 10284 12770 -2086 -838 1914 A C ATOM 1826 CG1 ILE A 241 44.570 -30.115 8.656 1.00102.45 A C ANISOU 1826 CG1 ILE A 241 15443 10514 12969 -1899 -861 1676 A C ATOM 1827 CG2 ILE A 241 43.627 -29.845 10.961 1.00106.90 A C ANISOU 1827 CG2 ILE A 241 16133 11225 13258 -2261 -702 1970 A C ATOM 1828 CD1 ILE A 241 43.380 -29.457 7.960 1.00105.41 A C ANISOU 1828 CD1 ILE A 241 15631 11025 13394 -2058 -735 1495 A C ATOM 1829 N SER A 242 44.412 -32.961 12.312 1.00113.42 A N ANISOU 1829 N SER A 242 17606 11362 14125 -2270 -925 2470 A N ATOM 1830 CA SER A 242 44.110 -33.334 13.688 1.00114.68 A C ANISOU 1830 CA SER A 242 17952 11493 14126 -2454 -883 2722 A C ATOM 1831 C SER A 242 45.361 -33.787 14.435 1.00116.55 A C ANISOU 1831 C SER A 242 18365 11647 14270 -2254 -1048 2932 A C ATOM 1832 O SER A 242 45.512 -33.527 15.626 1.00119.22 A O ANISOU 1832 O SER A 242 18783 12113 14400 -2323 -1041 3110 A O ATOM 1833 CB SER A 242 43.044 -34.434 13.732 1.00121.39 A C ANISOU 1833 CB SER A 242 18971 12075 15076 -2715 -814 2807 A C ATOM 1834 OG SER A 242 41.744 -33.888 13.590 1.00129.04 A O ANISOU 1834 OG SER A 242 19770 13208 16050 -2974 -632 2700 A O ATOM 1835 N GLN A 243 46.259 -34.464 13.724 1.00119.56 A N ANISOU 1835 N GLN A 243 18805 11821 14799 -1995 -1199 2910 A N ATOM 1836 CA GLN A 243 47.498 -34.945 14.333 1.00127.48 A C ANISOU 1836 CA GLN A 243 19949 12744 15742 -1764 -1371 3112 A C ATOM 1837 C GLN A 243 48.416 -33.787 14.722 1.00140.68 A C ANISOU 1837 C GLN A 243 21434 14760 17256 -1619 -1434 3102 A C ATOM 1838 O GLN A 243 49.333 -33.951 15.534 1.00136.94 A O ANISOU 1838 O GLN A 243 21049 14314 16667 -1492 -1570 3301 A O ATOM 1839 CB GLN A 243 48.215 -35.895 13.390 1.00130.55 A C ANISOU 1839 CB GLN A 243 20422 12841 16340 -1494 -1496 3068 A C ATOM 1840 CG GLN A 243 47.516 -37.226 13.175 1.00130.77 A C ANISOU 1840 CG GLN A 243 20713 12462 16509 -1621 -1479 3124 A C ATOM 1841 CD GLN A 243 48.093 -37.979 11.990 1.00136.27 A C ANISOU 1841 CD GLN A 243 21468 12888 17419 -1353 -1569 2993 A C ATOM 1842 NE2 GLN A 243 47.587 -39.182 11.736 1.00144.14 A N ANISOU 1842 NE2 GLN A 243 22726 13492 18547 -1442 -1575 3026 A N ATOM 1843 OE1 GLN A 243 48.989 -37.479 11.315 1.00134.78 A O ANISOU 1843 OE1 GLN A 243 21098 12841 17271 -1072 -1628 2863 A O ATOM 1844 N LEU A 244 48.112 -32.608 14.182 1.00153.32 A N ANISOU 1844 N LEU A 244 22785 16622 18845 -1660 -1337 2881 A N ATOM 1845 CA LEU A 244 48.946 -31.432 14.425 1.00141.19 A C ANISOU 1845 CA LEU A 244 21066 15403 17174 -1545 -1392 2841 A C ATOM 1846 C LEU A 244 48.275 -30.383 15.304 1.00127.43 A C ANISOU 1846 C LEU A 244 19281 13923 15213 -1779 -1263 2838 A C ATOM 1847 O LEU A 244 48.903 -29.818 16.206 1.00121.99 A O ANISOU 1847 O LEU A 244 18604 13419 14326 -1765 -1334 2942 A O ATOM 1848 CB LEU A 244 49.357 -30.797 13.105 1.00127.77 A C ANISOU 1848 CB LEU A 244 19122 13804 15620 -1363 -1398 2595 A C ATOM 1849 CG LEU A 244 50.365 -29.656 13.267 1.00121.92 A C ANISOU 1849 CG LEU A 244 18193 13365 14766 -1235 -1477 2564 A C ATOM 1850 CD1 LEU A 244 51.687 -30.225 13.758 1.00128.87 A C ANISOU 1850 CD1 LEU A 244 19141 14203 15620 -1014 -1679 2765 A C ATOM 1851 CD2 LEU A 244 50.564 -28.902 11.962 1.00115.30 A C ANISOU 1851 CD2 LEU A 244 17109 12645 14054 -1109 -1441 2316 A C ATOM 1852 N CYS A 245 47.001 -30.114 15.039 1.00120.86 A N ANISOU 1852 N CYS A 245 18397 13112 14412 -1991 -1075 2715 A N ATOM 1853 CA CYS A 245 46.328 -29.007 15.719 1.00121.79 A C ANISOU 1853 CA CYS A 245 18445 13491 14339 -2177 -924 2671 A C ATOM 1854 C CYS A 245 45.380 -29.464 16.820 1.00138.03 A C ANISOU 1854 C CYS A 245 20689 15500 16256 -2435 -797 2846 A C ATOM 1855 O CYS A 245 44.585 -28.680 17.329 1.00144.96 A O ANISOU 1855 O CYS A 245 21518 16566 16992 -2605 -627 2802 A O ATOM 1856 CB CYS A 245 45.578 -28.141 14.707 1.00114.47 A C ANISOU 1856 CB CYS A 245 17284 12689 13519 -2214 -784 2410 A C ATOM 1857 SG CYS A 245 46.545 -27.659 13.266 1.00115.44 A S ANISOU 1857 SG CYS A 245 17190 12855 13815 -1933 -902 2200 A S ATOM 1858 N GLY A 246 45.485 -30.729 17.200 1.00150.34 A N ANISOU 1858 N GLY A 246 22469 16804 17849 -2455 -874 3050 A N ATOM 1859 CA GLY A 246 44.522 -31.321 18.119 1.00143.41 A C ANISOU 1859 CA GLY A 246 21775 15844 16869 -2718 -744 3228 A C ATOM 1860 C GLY A 246 43.365 -31.815 17.273 1.00130.19 A C ANISOU 1860 C GLY A 246 20037 14019 15406 -2874 -614 3119 A C ATOM 1861 O GLY A 246 43.403 -31.709 16.032 1.00127.48 A O ANISOU 1861 O GLY A 246 19533 13634 15266 -2761 -646 2913 A O ATOM 1862 N SER A 247 42.367 -32.429 17.902 1.00126.50 A N ANISOU 1862 N SER A 247 19702 13461 14898 -3138 -481 3266 A N ATOM 1863 CA SER A 247 41.211 -32.880 17.138 1.00129.10 A C ANISOU 1863 CA SER A 247 19954 13670 15427 -3326 -364 3170 A C ATOM 1864 C SER A 247 39.994 -31.974 17.305 1.00111.45 A C ANISOU 1864 C SER A 247 17518 11706 13121 -3535 -122 3071 A C ATOM 1865 O SER A 247 39.831 -31.282 18.294 1.00100.72 A O ANISOU 1865 O SER A 247 16167 10568 11532 -3603 -5 3140 A O ATOM 1866 CB SER A 247 40.870 -34.352 17.387 1.00148.19 A C ANISOU 1866 CB SER A 247 22629 15745 17931 -3484 -393 3374 A C ATOM 1867 OG SER A 247 40.929 -34.675 18.752 1.00163.36 A O ANISOU 1867 OG SER A 247 24772 17663 19634 -3595 -363 3648 A O ATOM 1868 N ILE A 248 39.197 -31.933 16.240 1.00113.57 A N ANISOU 1868 N ILE A 248 17595 11961 13593 -3606 -60 2887 A N ATOM 1869 CA ILE A 248 38.089 -31.000 16.112 1.00112.38 A C ANISOU 1869 CA ILE A 248 17195 12077 13427 -3745 149 2754 A C ATOM 1870 C ILE A 248 37.039 -31.283 17.175 1.00120.61 A C ANISOU 1870 C ILE A 248 18303 13175 14346 -4041 353 2942 A C ATOM 1871 O ILE A 248 36.307 -32.273 17.102 1.00121.96 A O ANISOU 1871 O ILE A 248 18538 13162 14636 -4263 388 3043 A O ATOM 1872 CB ILE A 248 37.470 -31.136 14.710 1.00105.73 A C ANISOU 1872 CB ILE A 248 16157 11171 12845 -3771 134 2551 A C ATOM 1873 CG1 ILE A 248 38.582 -31.493 13.699 1.00 94.42 A C ANISOU 1873 CG1 ILE A 248 14776 9544 11554 -3509 -95 2439 A C ATOM 1874 CG2 ILE A 248 36.693 -29.922 14.305 1.00106.61 A C ANISOU 1874 CG2 ILE A 248 15966 11583 12956 -3786 289 2364 A C ATOM 1875 CD1 ILE A 248 38.629 -30.612 12.513 1.00 90.58 A C ANISOU 1875 CD1 ILE A 248 14039 9206 11171 -3353 -115 2176 A C ATOM 1876 N THR A 249 36.959 -30.406 18.168 1.00119.88 A N ANISOU 1876 N THR A 249 18202 13338 14008 -4053 494 2988 A N ATOM 1877 CA THR A 249 36.062 -30.603 19.304 1.00120.27 A C ANISOU 1877 CA THR A 249 18331 13472 13892 -4311 708 3180 A C ATOM 1878 C THR A 249 35.209 -29.371 19.526 1.00127.76 A C ANISOU 1878 C THR A 249 19048 14759 14733 -4353 955 3056 A C ATOM 1879 O THR A 249 35.718 -28.261 19.486 1.00142.01 A O ANISOU 1879 O THR A 249 20775 16745 16436 -4159 944 2908 A O ATOM 1880 CB THR A 249 36.880 -30.847 20.580 1.00115.09 A C ANISOU 1880 CB THR A 249 17974 12783 12971 -4279 648 3405 A C ATOM 1881 CG2 THR A 249 35.982 -30.946 21.805 1.00115.19 A C ANISOU 1881 CG2 THR A 249 18080 12915 12771 -4535 890 3602 A C ATOM 1882 OG1 THR A 249 37.619 -32.063 20.425 1.00111.56 A O ANISOU 1882 OG1 THR A 249 17750 12005 12629 -4232 428 3547 A O ATOM 1883 N PRO A 250 33.898 -29.556 19.727 1.00126.97 A N ANISOU 1883 N PRO A 250 18829 14744 14667 -4604 1180 3114 A N ATOM 1884 CA PRO A 250 33.024 -28.426 20.031 1.00122.75 A C ANISOU 1884 CA PRO A 250 18078 14537 14023 -4632 1443 3018 A C ATOM 1885 C PRO A 250 33.546 -27.619 21.205 1.00124.58 A C ANISOU 1885 C PRO A 250 18470 14942 13920 -4535 1524 3064 A C ATOM 1886 O PRO A 250 33.139 -26.474 21.395 1.00126.84 A O ANISOU 1886 O PRO A 250 18614 15485 14094 -4468 1703 2936 A O ATOM 1887 CB PRO A 250 31.693 -29.090 20.373 1.00132.10 A C ANISOU 1887 CB PRO A 250 19186 15747 15259 -4950 1659 3169 A C ATOM 1888 CG PRO A 250 31.715 -30.367 19.606 1.00144.66 A C ANISOU 1888 CG PRO A 250 20835 17023 17105 -5069 1474 3225 A C ATOM 1889 CD PRO A 250 33.149 -30.812 19.616 1.00139.47 A C ANISOU 1889 CD PRO A 250 20458 16123 16409 -4873 1202 3266 A C ATOM 1890 N GLU A 251 34.443 -28.208 21.989 1.00130.46 A N ANISOU 1890 N GLU A 251 19522 15544 14503 -4522 1385 3247 A N ATOM 1891 CA GLU A 251 35.097 -27.485 23.065 1.00139.36 A C ANISOU 1891 CA GLU A 251 20829 16820 15300 -4425 1405 3286 A C ATOM 1892 C GLU A 251 36.144 -26.543 22.494 1.00142.02 A C ANISOU 1892 C GLU A 251 21107 17210 15644 -4149 1222 3076 A C ATOM 1893 O GLU A 251 36.245 -25.386 22.887 1.00143.43 A O ANISOU 1893 O GLU A 251 21262 17599 15633 -4059 1313 2958 A O ATOM 1894 CB GLU A 251 35.776 -28.444 24.037 1.00146.07 A C ANISOU 1894 CB GLU A 251 22020 17503 15977 -4492 1281 3561 A C ATOM 1895 CG GLU A 251 36.851 -27.759 24.863 1.00160.62 A C ANISOU 1895 CG GLU A 251 24053 19453 17521 -4335 1172 3572 A C ATOM 1896 CD GLU A 251 37.105 -28.433 26.191 1.00193.90 A C ANISOU 1896 CD GLU A 251 28595 23620 21456 -4456 1165 3862 A C ATOM 1897 OE1 GLU A 251 36.802 -29.637 26.312 1.00222.87 A O ANISOU 1897 OE1 GLU A 251 32381 27085 25214 -4613 1155 4073 A O ATOM 1898 OE2 GLU A 251 37.595 -27.744 27.107 1.00194.96 A O1- ANISOU 1898 OE2 GLU A 251 28879 23918 21276 -4401 1168 3877 A O1- ATOM 1899 N VAL A 252 36.929 -27.069 21.560 1.00139.93 A N ANISOU 1899 N VAL A 252 20828 16740 15597 -4021 967 3031 A N ATOM 1900 CA VAL A 252 37.971 -26.301 20.899 1.00119.33 A C ANISOU 1900 CA VAL A 252 18145 14164 13028 -3768 781 2848 A C ATOM 1901 C VAL A 252 37.361 -25.360 19.860 1.00118.79 A C ANISOU 1901 C VAL A 252 17774 14235 13124 -3698 884 2589 A C ATOM 1902 O VAL A 252 37.754 -24.195 19.733 1.00131.29 A O ANISOU 1902 O VAL A 252 19281 15975 14628 -3548 883 2427 A O ATOM 1903 CB VAL A 252 39.014 -27.239 20.255 1.00118.41 A C ANISOU 1903 CB VAL A 252 18114 13788 13086 -3641 492 2900 A C ATOM 1904 CG1 VAL A 252 39.848 -26.489 19.245 1.00114.37 A C ANISOU 1904 CG1 VAL A 252 17442 13319 12693 -3399 339 2683 A C ATOM 1905 CG2 VAL A 252 39.941 -27.807 21.324 1.00131.27 A C ANISOU 1905 CG2 VAL A 252 20035 15332 14509 -3623 347 3133 A C ATOM 1906 N TRP A 253 36.361 -25.868 19.150 1.00119.04 A N ANISOU 1906 N TRP A 253 17640 14209 13378 -3820 974 2562 A N ATOM 1907 CA TRP A 253 35.751 -25.184 18.020 1.00118.76 A C ANISOU 1907 CA TRP A 253 17311 14276 13536 -3756 1036 2338 A C ATOM 1908 C TRP A 253 34.239 -25.161 18.213 1.00116.85 A C ANISOU 1908 C TRP A 253 16904 14169 13323 -3961 1306 2363 A C ATOM 1909 O TRP A 253 33.519 -26.012 17.670 1.00119.51 A O ANISOU 1909 O TRP A 253 17147 14399 13861 -4117 1312 2403 A O ATOM 1910 CB TRP A 253 36.100 -25.956 16.744 1.00115.20 A C ANISOU 1910 CB TRP A 253 16799 13606 13364 -3694 826 2271 A C ATOM 1911 CG TRP A 253 35.598 -25.363 15.472 1.00107.50 A C ANISOU 1911 CG TRP A 253 15543 12714 12589 -3619 843 2049 A C ATOM 1912 CD1 TRP A 253 34.675 -24.362 15.331 1.00111.50 A C ANISOU 1912 CD1 TRP A 253 15823 13454 13088 -3628 1038 1929 A C ATOM 1913 CD2 TRP A 253 35.964 -25.763 14.150 1.00 95.64 A C ANISOU 1913 CD2 TRP A 253 13962 11059 11316 -3517 658 1927 A C ATOM 1914 CE2 TRP A 253 35.235 -24.955 13.250 1.00 94.41 A C ANISOU 1914 CE2 TRP A 253 13532 11064 11276 -3479 739 1740 A C ATOM 1915 CE3 TRP A 253 36.847 -26.715 13.638 1.00 92.92 A C ANISOU 1915 CE3 TRP A 253 13761 10460 11084 -3438 435 1957 A C ATOM 1916 NE1 TRP A 253 34.460 -24.107 13.993 1.00101.43 A N ANISOU 1916 NE1 TRP A 253 14329 12184 12025 -3541 969 1749 A N ATOM 1917 CZ2 TRP A 253 35.351 -25.083 11.872 1.00 92.67 A C ANISOU 1917 CZ2 TRP A 253 13185 10762 11260 -3385 601 1586 A C ATOM 1918 CZ3 TRP A 253 36.968 -26.832 12.258 1.00 97.28 A C ANISOU 1918 CZ3 TRP A 253 14189 10929 11844 -3334 313 1789 A C ATOM 1919 CH2 TRP A 253 36.225 -26.035 11.401 1.00 96.79 A C ANISOU 1919 CH2 TRP A 253 13865 11034 11875 -3318 393 1609 A C ATOM 1920 N PRO A 254 33.749 -24.191 18.996 1.00114.71 A N ANISOU 1920 N PRO A 254 16598 14136 12848 -3964 1532 2340 A N ATOM 1921 CA PRO A 254 32.338 -24.041 19.386 1.00107.19 A C ANISOU 1921 CA PRO A 254 15485 13362 11877 -4135 1830 2379 A C ATOM 1922 C PRO A 254 31.364 -24.206 18.232 1.00105.23 A C ANISOU 1922 C PRO A 254 14923 13134 11923 -4199 1863 2281 A C ATOM 1923 O PRO A 254 31.364 -23.399 17.308 1.00 96.33 A O ANISOU 1923 O PRO A 254 13601 12087 10913 -4032 1824 2081 A O ATOM 1924 CB PRO A 254 32.285 -22.623 19.933 1.00106.77 A C ANISOU 1924 CB PRO A 254 15409 13550 11607 -3993 2004 2258 A C ATOM 1925 CG PRO A 254 33.633 -22.463 20.575 1.00112.22 A C ANISOU 1925 CG PRO A 254 16392 14164 12080 -3881 1829 2292 A C ATOM 1926 CD PRO A 254 34.599 -23.162 19.620 1.00120.72 A C ANISOU 1926 CD PRO A 254 17493 15009 13364 -3797 1513 2275 A C ATOM 1927 N ASN A 255 30.556 -25.266 18.278 1.00117.88 A N ANISOU 1927 N ASN A 255 16487 14659 13641 -4452 1921 2430 A N ATOM 1928 CA ASN A 255 29.518 -25.498 17.273 1.00128.96 A C ANISOU 1928 CA ASN A 255 17586 16099 15311 -4563 1953 2358 A C ATOM 1929 C ASN A 255 29.974 -26.241 16.025 1.00125.26 A C ANISOU 1929 C ASN A 255 17112 15387 15093 -4542 1672 2278 A C ATOM 1930 O ASN A 255 29.154 -26.551 15.162 1.00116.34 A O ANISOU 1930 O ASN A 255 15758 14264 14182 -4659 1662 2222 A O ATOM 1931 CB ASN A 255 28.817 -24.189 16.873 1.00124.07 A C ANISOU 1931 CB ASN A 255 16661 15764 14714 -4423 2122 2178 A C ATOM 1932 CG ASN A 255 27.536 -23.963 17.656 1.00145.15 A C ANISOU 1932 CG ASN A 255 19166 18679 17304 -4581 2452 2277 A C ATOM 1933 ND2 ASN A 255 26.588 -23.260 17.051 1.00151.88 A N ANISOU 1933 ND2 ASN A 255 19677 19746 18285 -4533 2583 2158 A N ATOM 1934 OD1 ASN A 255 27.378 -24.463 18.777 1.00150.45 A O ANISOU 1934 OD1 ASN A 255 20007 19349 17805 -4747 2590 2470 A O ATOM 1935 N VAL A 256 31.275 -26.524 15.921 1.00130.21 A N ANISOU 1935 N VAL A 256 17981 15807 15684 -4390 1443 2270 A N ATOM 1936 CA VAL A 256 31.776 -27.398 14.858 1.00126.04 A C ANISOU 1936 CA VAL A 256 17504 15013 15370 -4369 1188 2217 A C ATOM 1937 C VAL A 256 30.843 -28.599 14.657 1.00139.76 A C ANISOU 1937 C VAL A 256 19215 16608 17278 -4673 1202 2330 A C ATOM 1938 O VAL A 256 30.649 -29.078 13.543 1.00138.95 A O ANISOU 1938 O VAL A 256 19021 16379 17393 -4709 1064 2227 A O ATOM 1939 CB VAL A 256 33.189 -27.944 15.181 1.00118.91 A C ANISOU 1939 CB VAL A 256 16921 13877 14382 -4235 981 2299 A C ATOM 1940 CG1 VAL A 256 33.238 -28.368 16.638 1.00114.93 A C ANISOU 1940 CG1 VAL A 256 16654 13354 13659 -4371 1083 2543 A C ATOM 1941 CG2 VAL A 256 33.537 -29.113 14.277 1.00128.11 A C ANISOU 1941 CG2 VAL A 256 18184 14731 15761 -4258 761 2290 A C ATOM 1942 N ASP A 257 30.211 -29.036 15.740 1.00156.43 A N ANISOU 1942 N ASP A 257 21400 18755 19280 -4906 1380 2539 A N ATOM 1943 CA ASP A 257 29.362 -30.195 15.689 1.00152.70 A C ANISOU 1943 CA ASP A 257 20928 18139 18952 -5227 1401 2677 A C ATOM 1944 C ASP A 257 28.175 -30.095 14.733 1.00134.19 A C ANISOU 1944 C ASP A 257 18232 15925 16827 -5373 1452 2559 A C ATOM 1945 O ASP A 257 27.421 -31.053 14.602 1.00135.31 A O ANISOU 1945 O ASP A 257 18350 15952 17107 -5669 1454 2662 A O ATOM 1946 CB ASP A 257 28.951 -30.671 17.098 1.00145.81 A C ANISOU 1946 CB ASP A 257 20213 17288 17898 -5457 1597 2948 A C ATOM 1947 CG ASP A 257 28.401 -29.558 17.991 1.00137.68 A C ANISOU 1947 CG ASP A 257 19036 16619 16656 -5423 1887 2961 A C ATOM 1948 OD1 ASP A 257 27.235 -29.128 17.819 1.00124.37 A O ANISOU 1948 OD1 ASP A 257 17036 15174 15043 -5536 2084 2921 A O ATOM 1949 OD2 ASP A 257 29.122 -29.125 18.906 1.00140.75 A O1- ANISOU 1949 OD2 ASP A 257 19630 17053 16794 -5284 1923 3019 A O1- ATOM 1950 N ASN A 258 28.039 -29.017 13.958 1.00122.63 A N ANISOU 1950 N ASN A 258 16505 14672 15415 -5174 1458 2344 A N ATOM 1951 CA ASN A 258 26.782 -28.840 13.243 1.00113.41 A C ANISOU 1951 CA ASN A 258 14976 13689 14425 -5322 1537 2268 A C ATOM 1952 C ASN A 258 26.911 -28.906 11.751 1.00110.14 A C ANISOU 1952 C ASN A 258 14449 13180 14218 -5237 1307 2063 A C ATOM 1953 O ASN A 258 25.997 -28.525 11.017 1.00106.54 A O ANISOU 1953 O ASN A 258 13670 12912 13896 -5290 1339 1963 A O ATOM 1954 CB ASN A 258 26.047 -27.595 13.714 1.00109.89 A C ANISOU 1954 CB ASN A 258 14258 13622 13872 -5239 1807 2238 A C ATOM 1955 CG ASN A 258 26.186 -27.407 15.214 1.00126.18 A C ANISOU 1955 CG ASN A 258 16502 15767 15673 -5257 2022 2411 A C ATOM 1956 ND2 ASN A 258 25.095 -27.607 15.930 1.00131.73 A N ANISOU 1956 ND2 ASN A 258 17067 16635 16346 -5500 2269 2568 A N ATOM 1957 OD1 ASN A 258 27.272 -27.116 15.728 1.00144.83 A O ANISOU 1957 OD1 ASN A 258 19126 18048 17855 -5065 1963 2409 A O ATOM 1958 N TYR A 259 28.042 -29.425 11.271 1.00117.97 A N ANISOU 1958 N TYR A 259 15702 13883 15235 -5101 1069 2004 A N ATOM 1959 CA TYR A 259 28.115 -29.777 9.854 1.00142.10 A C ANISOU 1959 CA TYR A 259 18702 16801 18488 -5073 846 1829 A C ATOM 1960 C TYR A 259 27.565 -31.152 9.777 1.00147.24 A C ANISOU 1960 C TYR A 259 19456 17213 19275 -5409 777 1941 A C ATOM 1961 O TYR A 259 27.877 -31.993 10.629 1.00144.90 A O ANISOU 1961 O TYR A 259 19435 16706 18914 -5533 789 2128 A O ATOM 1962 CB TYR A 259 29.534 -29.846 9.354 1.00157.22 A C ANISOU 1962 CB TYR A 259 20859 18498 20379 -4791 636 1722 A C ATOM 1963 CG TYR A 259 30.175 -28.496 9.420 1.00148.01 A C ANISOU 1963 CG TYR A 259 19612 17546 19078 -4473 687 1615 A C ATOM 1964 CD1 TYR A 259 29.709 -27.459 8.619 1.00138.00 A C ANISOU 1964 CD1 TYR A 259 18049 16522 17863 -4354 719 1442 A C ATOM 1965 CD2 TYR A 259 31.237 -28.242 10.282 1.00133.00 A C ANISOU 1965 CD2 TYR A 259 17931 15604 16996 -4301 694 1691 A C ATOM 1966 CE1 TYR A 259 30.273 -26.206 8.677 1.00130.77 A C ANISOU 1966 CE1 TYR A 259 17076 15782 16827 -4078 768 1347 A C ATOM 1967 CE2 TYR A 259 31.812 -26.985 10.352 1.00117.86 A C ANISOU 1967 CE2 TYR A 259 15947 13878 14955 -4040 734 1589 A C ATOM 1968 CZ TYR A 259 31.320 -25.972 9.546 1.00123.49 A C ANISOU 1968 CZ TYR A 259 16381 14809 15728 -3933 777 1417 A C ATOM 1969 OH TYR A 259 31.887 -24.719 9.590 1.00122.52 A O ANISOU 1969 OH TYR A 259 16212 14849 15488 -3684 815 1317 A O ATOM 1970 N GLU A 260 26.789 -31.387 8.726 1.00149.90 A N ANISOU 1970 N GLU A 260 19590 17567 19797 -5555 686 1826 A N ATOM 1971 CA GLU A 260 26.296 -32.717 8.397 1.00151.96 A C ANISOU 1971 CA GLU A 260 19959 17565 20214 -5886 570 1888 A C ATOM 1972 C GLU A 260 27.459 -33.664 8.042 1.00149.96 A C ANISOU 1972 C GLU A 260 20107 16887 19983 -5779 343 1854 A C ATOM 1973 O GLU A 260 27.255 -34.840 7.681 1.00174.54 A O ANISOU 1973 O GLU A 260 23391 19703 23223 -6014 211 1880 A O ATOM 1974 CB GLU A 260 25.298 -32.619 7.249 1.00150.29 A C ANISOU 1974 CB GLU A 260 19430 17493 20178 -6031 492 1739 A C ATOM 1975 CG GLU A 260 24.454 -33.868 7.044 1.00164.63 A C ANISOU 1975 CG GLU A 260 21278 19118 22155 -6459 415 1823 A C ATOM 1976 CD GLU A 260 23.598 -33.792 5.799 1.00172.55 A C ANISOU 1976 CD GLU A 260 21991 20245 23325 -6589 285 1654 A C ATOM 1977 OE1 GLU A 260 23.713 -32.792 5.055 1.00173.37 A O ANISOU 1977 OE1 GLU A 260 21889 20567 23417 -6322 248 1474 A O ATOM 1978 OE2 GLU A 260 22.807 -34.732 5.566 1.00177.70 A O1- ANISOU 1978 OE2 GLU A 260 22627 20776 24115 -6968 213 1708 A O1- ATOM 1979 N LEU A 261 28.678 -33.148 8.171 1.00129.64 A N ANISOU 1979 N LEU A 261 17686 14284 17285 -5426 301 1802 A N ATOM 1980 CA LEU A 261 29.881 -33.908 7.880 1.00122.98 A C ANISOU 1980 CA LEU A 261 17193 13080 16451 -5257 106 1773 A C ATOM 1981 C LEU A 261 30.747 -34.143 9.103 1.00120.84 A C ANISOU 1981 C LEU A 261 17200 12691 16022 -5160 156 1973 A C ATOM 1982 O LEU A 261 31.841 -34.726 8.984 1.00116.49 A O ANISOU 1982 O LEU A 261 16935 11858 15467 -4979 3 1975 A O ATOM 1983 CB LEU A 261 30.693 -33.233 6.763 1.00116.78 A C ANISOU 1983 CB LEU A 261 16353 12337 15681 -4912 -32 1528 A C ATOM 1984 CG LEU A 261 30.266 -33.561 5.335 1.00114.55 A C ANISOU 1984 CG LEU A 261 15984 11975 15563 -4979 -191 1324 A C ATOM 1985 CD1 LEU A 261 31.355 -33.156 4.372 1.00103.29 A C ANISOU 1985 CD1 LEU A 261 14617 10503 14123 -4618 -333 1123 A C ATOM 1986 CD2 LEU A 261 29.951 -35.056 5.219 1.00123.69 A C ANISOU 1986 CD2 LEU A 261 17389 12762 16844 -5270 -302 1392 A C ATOM 1987 N TYR A 262 30.259 -33.687 10.261 1.00119.94 A N ANISOU 1987 N TYR A 262 16998 12800 15772 -5270 369 2141 A N ATOM 1988 CA TYR A 262 30.956 -33.869 11.515 1.00124.82 A C ANISOU 1988 CA TYR A 262 17869 13343 16212 -5212 426 2348 A C ATOM 1989 C TYR A 262 30.914 -35.367 11.800 1.00137.44 A C ANISOU 1989 C TYR A 262 19773 14561 17885 -5450 345 2527 A C ATOM 1990 O TYR A 262 31.940 -35.996 12.112 1.00145.33 A O ANISOU 1990 O TYR A 262 21091 15288 18837 -5309 222 2619 A O ATOM 1991 CB TYR A 262 30.300 -33.061 12.653 1.00123.55 A C ANISOU 1991 CB TYR A 262 17549 13516 15877 -5305 690 2476 A C ATOM 1992 CG TYR A 262 31.049 -33.213 13.959 1.00128.81 A C ANISOU 1992 CG TYR A 262 18493 14120 16327 -5243 737 2686 A C ATOM 1993 CD1 TYR A 262 31.462 -34.475 14.397 1.00135.54 A C ANISOU 1993 CD1 TYR A 262 19683 14626 17187 -5354 635 2877 A C ATOM 1994 CD2 TYR A 262 31.377 -32.112 14.747 1.00129.29 A C ANISOU 1994 CD2 TYR A 262 18502 14451 16168 -5070 867 2694 A C ATOM 1995 CE1 TYR A 262 32.177 -34.640 15.565 1.00134.57 A C ANISOU 1995 CE1 TYR A 262 19821 14446 16860 -5288 653 3080 A C ATOM 1996 CE2 TYR A 262 32.089 -32.270 15.938 1.00130.13 A C ANISOU 1996 CE2 TYR A 262 18878 14505 16059 -5022 885 2886 A C ATOM 1997 CZ TYR A 262 32.495 -33.540 16.331 1.00134.13 A C ANISOU 1997 CZ TYR A 262 19701 14681 16578 -5126 772 3084 A C ATOM 1998 OH TYR A 262 33.198 -33.734 17.481 1.00137.37 A O ANISOU 1998 OH TYR A 262 20380 15040 16773 -5076 770 3287 A O ATOM 1999 N GLU A 263 29.714 -35.929 11.651 1.00144.69 A N ANISOU 1999 N GLU A 263 20583 15460 18929 -5811 407 2577 A N ATOM 2000 CA GLU A 263 29.428 -37.337 11.910 1.00150.47 A C ANISOU 2000 CA GLU A 263 21581 15839 19749 -6113 353 2754 A C ATOM 2001 C GLU A 263 30.090 -38.275 10.903 1.00142.17 A C ANISOU 2001 C GLU A 263 20786 14378 18854 -6027 94 2631 A C ATOM 2002 O GLU A 263 30.733 -39.270 11.273 1.00135.25 A O ANISOU 2002 O GLU A 263 20277 13138 17974 -6020 -2 2770 A O ATOM 2003 CB GLU A 263 27.908 -37.536 11.888 1.00162.25 A C ANISOU 2003 CB GLU A 263 22822 17473 21349 -6533 488 2811 A C ATOM 2004 CG GLU A 263 27.138 -36.595 12.809 1.00171.66 A C ANISOU 2004 CG GLU A 263 23729 19093 22399 -6611 771 2918 A C ATOM 2005 CD GLU A 263 27.590 -36.713 14.266 1.00184.60 A C ANISOU 2005 CD GLU A 263 25612 20711 23814 -6597 906 3176 A C ATOM 2006 OE1 GLU A 263 28.664 -37.297 14.542 1.00182.58 A O ANISOU 2006 OE1 GLU A 263 25716 20156 23497 -6445 765 3253 A O ATOM 2007 OE2 GLU A 263 26.865 -36.228 15.160 1.00196.98 A O1- ANISOU 2007 OE2 GLU A 263 27015 22570 25256 -6734 1158 3309 A O1- ATOM 2008 N LYS A 264 29.904 -37.936 9.629 1.00136.52 A N ANISOU 2008 N LYS A 264 19876 13726 18266 -5954 -9 2369 A N ATOM 2009 CA LYS A 264 30.386 -38.728 8.513 1.00143.33 A C ANISOU 2009 CA LYS A 264 20943 14240 19274 -5880 -240 2205 A C ATOM 2010 C LYS A 264 31.899 -38.805 8.522 1.00151.31 A C ANISOU 2010 C LYS A 264 22223 15057 20211 -5476 -359 2182 A C ATOM 2011 O LYS A 264 32.469 -39.852 8.225 1.00159.01 A O ANISOU 2011 O LYS A 264 23525 15628 21262 -5433 -510 2187 A O ATOM 2012 CB LYS A 264 29.869 -38.154 7.187 1.00141.86 A C ANISOU 2012 CB LYS A 264 20463 14239 19199 -5863 -310 1928 A C ATOM 2013 CG LYS A 264 28.351 -38.201 7.095 1.00149.44 A C ANISOU 2013 CG LYS A 264 21146 15376 20258 -6277 -223 1957 A C ATOM 2014 CD LYS A 264 27.772 -37.601 5.828 1.00149.74 A C ANISOU 2014 CD LYS A 264 20871 15628 20394 -6269 -302 1704 A C ATOM 2015 CE LYS A 264 26.261 -37.760 5.866 1.00148.95 A C ANISOU 2015 CE LYS A 264 20493 15701 20398 -6706 -220 1774 A C ATOM 2016 NZ LYS A 264 25.587 -37.111 4.712 1.00146.26 A N1+ ANISOU 2016 NZ LYS A 264 19806 15620 20145 -6711 -293 1555 A N1+ ATOM 2017 N LEU A 265 32.543 -37.698 8.884 1.00166.04 A N ANISOU 2017 N LEU A 265 23949 17208 21928 -5181 -289 2161 A N ATOM 2018 CA LEU A 265 34.002 -37.644 8.937 1.00173.37 A C ANISOU 2018 CA LEU A 265 25074 18016 22780 -4794 -397 2149 A C ATOM 2019 C LEU A 265 34.561 -38.670 9.916 1.00170.78 A C ANISOU 2019 C LEU A 265 25116 17371 22400 -4819 -432 2406 A C ATOM 2020 O LEU A 265 35.593 -39.291 9.649 1.00163.88 A O ANISOU 2020 O LEU A 265 24498 16207 21559 -4582 -584 2397 A O ATOM 2021 CB LEU A 265 34.504 -36.249 9.314 1.00185.10 A C ANISOU 2021 CB LEU A 265 26344 19882 24104 -4536 -306 2111 A C ATOM 2022 CG LEU A 265 36.036 -36.098 9.445 1.00192.89 A C ANISOU 2022 CG LEU A 265 27491 20795 25002 -4149 -417 2117 A C ATOM 2023 CD1 LEU A 265 36.753 -36.312 8.117 1.00184.90 A C ANISOU 2023 CD1 LEU A 265 26520 19618 24115 -3900 -587 1894 A C ATOM 2024 CD2 LEU A 265 36.427 -34.750 10.036 1.00191.35 A C ANISOU 2024 CD2 LEU A 265 27105 20970 24629 -3972 -317 2117 A C ATOM 2025 N GLU A 266 33.880 -38.838 11.047 1.00168.68 A N ANISOU 2025 N GLU A 266 24873 17167 22049 -5094 -284 2642 A N ATOM 2026 CA GLU A 266 34.366 -39.736 12.076 1.00177.67 A C ANISOU 2026 CA GLU A 266 26359 18034 23110 -5126 -306 2916 A C ATOM 2027 C GLU A 266 35.839 -39.420 12.353 1.00176.61 A C ANISOU 2027 C GLU A 266 26350 17894 22857 -4707 -407 2935 A C ATOM 2028 O GLU A 266 36.712 -40.307 12.339 1.00173.50 A O ANISOU 2028 O GLU A 266 26262 17156 22503 -4544 -556 3012 A O ATOM 2029 CB GLU A 266 34.215 -41.197 11.650 1.00183.22 A C ANISOU 2029 CB GLU A 266 27371 18256 23986 -5301 -434 2959 A C ATOM 2030 CG GLU A 266 34.213 -42.133 12.848 1.00193.56 A C ANISOU 2030 CG GLU A 266 29001 19319 25222 -5483 -398 3291 A C ATOM 2031 CD GLU A 266 35.107 -43.347 12.674 1.00196.18 A C ANISOU 2031 CD GLU A 266 29753 19146 25638 -5328 -588 3361 A C ATOM 2032 OE1 GLU A 266 34.718 -44.254 11.919 1.00200.22 A O ANISOU 2032 OE1 GLU A 266 30419 19324 26331 -5494 -679 3280 A O ATOM 2033 OE2 GLU A 266 36.180 -43.419 13.317 1.00193.13 A O1- ANISOU 2033 OE2 GLU A 266 29554 18689 25135 -5046 -648 3504 A O1- ATOM 2034 N LEU A 267 36.105 -38.142 12.578 1.00171.88 A N ANISOU 2034 N LEU A 267 25507 17680 22120 -4532 -329 2862 A N ATOM 2035 CA LEU A 267 37.476 -37.670 12.849 1.00175.42 A C ANISOU 2035 CA LEU A 267 26016 18190 22446 -4156 -423 2872 A C ATOM 2036 C LEU A 267 38.056 -38.266 14.127 1.00177.04 A C ANISOU 2036 C LEU A 267 26511 18251 22502 -4144 -446 3173 A C ATOM 2037 O LEU A 267 37.326 -38.526 15.082 1.00169.01 A O ANISOU 2037 O LEU A 267 25568 17255 21390 -4423 -316 3378 A O ATOM 2038 CB LEU A 267 37.478 -36.150 12.924 1.00180.11 A C ANISOU 2038 CB LEU A 267 26296 19224 22910 -4040 -317 2745 A C ATOM 2039 CG LEU A 267 38.768 -35.406 13.235 1.00199.26 A C ANISOU 2039 CG LEU A 267 28717 21799 25193 -3701 -394 2739 A C ATOM 2040 CD1 LEU A 267 39.885 -35.855 12.305 1.00208.27 A C ANISOU 2040 CD1 LEU A 267 29953 22718 26462 -3395 -595 2629 A C ATOM 2041 CD2 LEU A 267 38.546 -33.908 13.151 1.00196.19 A C ANISOU 2041 CD2 LEU A 267 28020 21815 24707 -3644 -278 2581 A C ATOM 2042 N VAL A 268 39.369 -38.472 14.126 1.00181.23 A N ANISOU 2042 N VAL A 268 27196 18651 23009 -3816 -610 3206 A N ATOM 2043 CA VAL A 268 40.119 -38.970 15.278 1.00171.23 A C ANISOU 2043 CA VAL A 268 26197 17267 21594 -3735 -672 3489 A C ATOM 2044 C VAL A 268 39.788 -38.158 16.524 1.00167.44 A C ANISOU 2044 C VAL A 268 25638 17121 20861 -3872 -520 3635 A C ATOM 2045 O VAL A 268 39.446 -36.969 16.405 1.00177.70 A O ANISOU 2045 O VAL A 268 26654 18772 22089 -3877 -405 3476 A O ATOM 2046 CB VAL A 268 41.642 -38.825 15.018 1.00162.80 A C ANISOU 2046 CB VAL A 268 25164 16174 20517 -3307 -858 3450 A C ATOM 2047 CG1 VAL A 268 41.954 -39.152 13.551 1.00142.04 A C ANISOU 2047 CG1 VAL A 268 22497 13353 18118 -3120 -965 3203 A C ATOM 2048 CG2 VAL A 268 42.071 -37.388 15.329 1.00165.40 A C ANISOU 2048 CG2 VAL A 268 25235 16937 20670 -3168 -815 3368 A C ATOM 2049 N LYS A 269 39.948 -38.751 17.716 1.00148.98 A N ANISOU 2049 N LYS A 269 23561 14673 18370 -3957 -520 3934 A N ATOM 2050 CA LYS A 269 39.585 -38.033 18.918 1.00154.60 A C ANISOU 2050 CA LYS A 269 24229 15693 18818 -4100 -363 4072 A C ATOM 2051 C LYS A 269 40.493 -38.169 20.113 1.00159.59 A C ANISOU 2051 C LYS A 269 25091 16328 19214 -3977 -453 4330 A C ATOM 2052 O LYS A 269 40.155 -37.659 21.181 1.00167.05 A O ANISOU 2052 O LYS A 269 26046 17511 19914 -4118 -318 4458 A O ATOM 2053 CB LYS A 269 38.104 -38.271 19.301 1.00157.98 A C ANISOU 2053 CB LYS A 269 24628 16154 19240 -4514 -137 4158 A C ATOM 2054 CG LYS A 269 37.149 -37.512 18.373 1.00163.62 A C ANISOU 2054 CG LYS A 269 24991 17086 20090 -4622 -4 3883 A C ATOM 2055 CD LYS A 269 35.768 -37.303 18.976 1.00166.95 A C ANISOU 2055 CD LYS A 269 25291 17704 20436 -4982 257 3967 A C ATOM 2056 CE LYS A 269 34.784 -36.838 17.911 1.00166.50 A C ANISOU 2056 CE LYS A 269 24902 17788 20570 -5097 349 3717 A C ATOM 2057 NZ LYS A 269 33.456 -37.513 18.078 1.00192.38 A N1+ ANISOU 2057 NZ LYS A 269 28156 21004 23933 -5505 505 3838 A N1+ ATOM 2058 N GLY A 270 41.635 -38.833 19.966 1.00158.28 A N ANISOU 2058 N GLY A 270 25111 15918 19109 -3710 -677 4410 A N ATOM 2059 CA GLY A 270 42.668 -38.777 21.026 1.00158.00 A C ANISOU 2059 CA GLY A 270 25241 15949 18843 -3535 -801 4632 A C ATOM 2060 C GLY A 270 43.694 -37.644 20.868 1.00157.48 A C ANISOU 2060 C GLY A 270 24962 16183 18687 -3239 -906 4478 A C ATOM 2061 O GLY A 270 44.364 -37.251 21.816 1.00148.35 A O ANISOU 2061 O GLY A 270 23871 15201 17294 -3155 -975 4622 A O ATOM 2062 N GLN A 271 43.779 -37.107 19.659 1.00161.97 A N ANISOU 2062 N GLN A 271 25279 16821 19440 -3104 -916 4184 A N ATOM 2063 CA GLN A 271 44.828 -36.160 19.302 1.00143.57 A C ANISOU 2063 CA GLN A 271 22749 14722 17078 -2813 -1032 4031 A C ATOM 2064 C GLN A 271 44.843 -34.918 20.185 1.00143.53 A C ANISOU 2064 C GLN A 271 22632 15105 16794 -2874 -954 4029 A C ATOM 2065 O GLN A 271 43.805 -34.395 20.561 1.00152.04 A O ANISOU 2065 O GLN A 271 23648 16351 17769 -3121 -747 3992 A O ATOM 2066 CB GLN A 271 44.692 -35.767 17.829 1.00131.10 A C ANISOU 2066 CB GLN A 271 20921 13158 15733 -2712 -1014 3714 A C ATOM 2067 CG GLN A 271 44.741 -36.964 16.869 1.00131.39 A C ANISOU 2067 CG GLN A 271 21084 12803 16036 -2631 -1101 3680 A C ATOM 2068 CD GLN A 271 46.121 -37.606 16.821 1.00153.98 A C ANISOU 2068 CD GLN A 271 24084 15478 18943 -2291 -1322 3792 A C ATOM 2069 NE2 GLN A 271 46.157 -38.927 16.685 1.00169.05 A N ANISOU 2069 NE2 GLN A 271 26257 16985 20987 -2267 -1396 3916 A N ATOM 2070 OE1 GLN A 271 47.139 -36.925 16.935 1.00167.21 A O ANISOU 2070 OE1 GLN A 271 25630 17367 20532 -2057 -1426 3776 A O ATOM 2071 N LYS A 272 46.044 -34.415 20.467 1.00137.75 A N ANISOU 2071 N LYS A 272 21865 14524 15948 -2641 -1121 4055 A N ATOM 2072 CA LYS A 272 46.209 -33.184 21.248 1.00130.73 A C ANISOU 2072 CA LYS A 272 20886 13994 14790 -2680 -1080 4028 A C ATOM 2073 C LYS A 272 47.202 -32.267 20.536 1.00132.87 A C ANISOU 2073 C LYS A 272 20917 14450 15117 -2428 -1206 3830 A C ATOM 2074 O LYS A 272 48.120 -32.758 19.880 1.00136.88 A O ANISOU 2074 O LYS A 272 21398 14819 15792 -2182 -1381 3828 A O ATOM 2075 CB LYS A 272 46.705 -33.518 22.660 1.00129.15 A C ANISOU 2075 CB LYS A 272 20939 13813 14316 -2709 -1178 4330 A C ATOM 2076 CG LYS A 272 46.058 -34.758 23.268 1.00134.93 A C ANISOU 2076 CG LYS A 272 21957 14273 15035 -2891 -1121 4587 A C ATOM 2077 CD LYS A 272 45.972 -34.679 24.791 1.00134.69 A C ANISOU 2077 CD LYS A 272 22146 14377 14654 -3049 -1089 4836 A C ATOM 2078 CE LYS A 272 45.020 -35.754 25.303 1.00143.31 A C ANISOU 2078 CE LYS A 272 23482 15230 15738 -3301 -955 5058 A C ATOM 2079 NZ LYS A 272 44.758 -35.642 26.751 1.00160.15 A N1+ ANISOU 2079 NZ LYS A 272 25825 17510 17513 -3486 -875 5289 A N1+ ATOM 2080 N ARG A 273 47.045 -30.956 20.692 1.00137.58 A N ANISOU 2080 N ARG A 273 21352 15353 15570 -2487 -1114 3674 A N ATOM 2081 CA ARG A 273 47.788 -29.977 19.874 1.00149.88 A C ANISOU 2081 CA ARG A 273 22658 17087 17203 -2295 -1193 3454 A C ATOM 2082 C ARG A 273 49.303 -30.133 19.925 1.00144.12 A C ANISOU 2082 C ARG A 273 21922 16369 16469 -2037 -1457 3554 A C ATOM 2083 O ARG A 273 49.908 -30.002 20.979 1.00153.70 A O ANISOU 2083 O ARG A 273 23249 17694 17455 -2040 -1573 3726 A O ATOM 2084 CB ARG A 273 47.402 -28.538 20.223 1.00156.04 A C ANISOU 2084 CB ARG A 273 23318 18175 17793 -2413 -1057 3301 A C ATOM 2085 CG ARG A 273 45.911 -28.297 20.284 1.00163.35 A C ANISOU 2085 CG ARG A 273 24228 19134 18702 -2652 -784 3217 A C ATOM 2086 CD ARG A 273 45.517 -26.831 20.350 1.00190.96 A C ANISOU 2086 CD ARG A 273 27577 22908 22069 -2712 -638 3019 A C ATOM 2087 NE ARG A 273 44.293 -26.645 21.147 1.00222.50 A N ANISOU 2087 NE ARG A 273 31655 26984 25901 -2950 -392 3057 A N ATOM 2088 CZ ARG A 273 43.525 -25.561 21.117 1.00219.12 A C ANISOU 2088 CZ ARG A 273 31102 26749 25404 -3027 -191 2882 A C ATOM 2089 NH1 ARG A 273 43.828 -24.554 20.306 1.00226.22 A N1+ ANISOU 2089 NH1 ARG A 273 31801 27765 26387 -2900 -212 2658 A N1+ ATOM 2090 NH2 ARG A 273 42.449 -25.503 21.890 1.00186.52 A N ANISOU 2090 NH2 ARG A 273 27050 22692 21125 -3226 39 2940 A N ATOM 2091 N LYS A 274 49.909 -30.342 18.763 1.00137.76 A N ANISOU 2091 N LYS A 274 20964 15473 15906 -1813 -1548 3436 A N ATOM 2092 CA LYS A 274 51.348 -30.579 18.676 1.00131.26 A C ANISOU 2092 CA LYS A 274 20096 14655 15120 -1539 -1788 3531 A C ATOM 2093 C LYS A 274 52.054 -29.533 17.784 1.00124.94 A C ANISOU 2093 C LYS A 274 19001 14070 14400 -1385 -1830 3314 A C ATOM 2094 O LYS A 274 53.176 -29.757 17.340 1.00124.99 A O ANISOU 2094 O LYS A 274 18904 14072 14512 -1133 -1996 3344 A O ATOM 2095 CB LYS A 274 51.618 -31.983 18.132 1.00140.84 A C ANISOU 2095 CB LYS A 274 21425 15532 16555 -1361 -1872 3631 A C ATOM 2096 CG LYS A 274 50.776 -33.094 18.710 1.00142.01 A C ANISOU 2096 CG LYS A 274 21861 15406 16690 -1529 -1804 3812 A C ATOM 2097 CD LYS A 274 51.250 -34.474 18.269 1.00135.56 A C ANISOU 2097 CD LYS A 274 21194 14236 16074 -1320 -1923 3932 A C ATOM 2098 CE LYS A 274 50.380 -35.538 18.944 1.00148.15 A C ANISOU 2098 CE LYS A 274 23099 15552 17636 -1529 -1853 4132 A C ATOM 2099 NZ LYS A 274 50.858 -36.933 18.785 1.00152.95 A N1+ ANISOU 2099 NZ LYS A 274 23927 15786 18399 -1340 -1982 4301 A N1+ ATOM 2100 N VAL A 275 51.358 -28.430 17.500 1.00115.44 A N ANISOU 2100 N VAL A 275 17663 13043 13155 -1532 -1669 3103 A N ATOM 2101 CA VAL A 275 51.821 -27.490 16.485 1.00110.93 A C ANISOU 2101 CA VAL A 275 16827 12632 12690 -1410 -1673 2882 A C ATOM 2102 C VAL A 275 53.202 -26.956 16.828 1.00116.60 A C ANISOU 2102 C VAL A 275 17440 13550 13311 -1270 -1876 2954 A C ATOM 2103 O VAL A 275 54.099 -26.919 15.979 1.00118.37 A O ANISOU 2103 O VAL A 275 17481 13804 13688 -1053 -1974 2895 A O ATOM 2104 CB VAL A 275 50.877 -26.278 16.309 1.00106.62 A C ANISOU 2104 CB VAL A 275 16176 12257 12075 -1594 -1476 2670 A C ATOM 2105 CG1 VAL A 275 51.519 -25.248 15.388 1.00 99.73 A C ANISOU 2105 CG1 VAL A 275 15050 11558 11281 -1468 -1507 2479 A C ATOM 2106 CG2 VAL A 275 49.506 -26.709 15.804 1.00115.74 A C ANISOU 2106 CG2 VAL A 275 17367 13254 13354 -1727 -1279 2578 A C ATOM 2107 N LYS A 276 53.366 -26.543 18.077 1.00115.00 A N ANISOU 2107 N LYS A 276 17351 13495 12847 -1402 -1937 3083 A N ATOM 2108 CA LYS A 276 54.622 -25.967 18.525 1.00110.31 A C ANISOU 2108 CA LYS A 276 16662 13117 12132 -1319 -2145 3158 A C ATOM 2109 C LYS A 276 55.694 -27.026 18.784 1.00121.81 A C ANISOU 2109 C LYS A 276 18159 14481 13641 -1104 -2374 3399 A C ATOM 2110 O LYS A 276 56.881 -26.754 18.617 1.00139.92 A O ANISOU 2110 O LYS A 276 20276 16923 15962 -942 -2554 3434 A O ATOM 2111 CB LYS A 276 54.413 -25.114 19.785 1.00106.32 A C ANISOU 2111 CB LYS A 276 16285 12805 11303 -1547 -2140 3197 A C ATOM 2112 CG LYS A 276 53.837 -23.745 19.527 1.00 99.71 A C ANISOU 2112 CG LYS A 276 15350 12132 10400 -1695 -1977 2952 A C ATOM 2113 CD LYS A 276 53.672 -22.929 20.812 1.00102.35 A C ANISOU 2113 CD LYS A 276 15849 12641 10398 -1906 -1972 2984 A C ATOM 2114 CE LYS A 276 53.465 -21.450 20.470 1.00115.32 A C ANISOU 2114 CE LYS A 276 17370 14454 11990 -1997 -1865 2736 A C ATOM 2115 NZ LYS A 276 53.840 -20.481 21.535 1.00124.64 A N1+ ANISOU 2115 NZ LYS A 276 18662 15834 12861 -2147 -1947 2741 A N1+ ATOM 2116 N ASP A 277 55.271 -28.228 19.185 1.00124.01 A N ANISOU 2116 N ASP A 277 18665 14514 13937 -1102 -2365 3572 A N ATOM 2117 CA ASP A 277 56.209 -29.327 19.409 1.00132.88 A C ANISOU 2117 CA ASP A 277 19854 15507 15125 -873 -2572 3812 A C ATOM 2118 C ASP A 277 56.781 -29.896 18.106 1.00135.63 A C ANISOU 2118 C ASP A 277 20036 15716 15780 -578 -2601 3731 A C ATOM 2119 O ASP A 277 57.984 -30.152 18.003 1.00141.38 A O ANISOU 2119 O ASP A 277 20642 16501 16572 -330 -2790 3842 A O ATOM 2120 CB ASP A 277 55.550 -30.459 20.207 1.00123.33 A C ANISOU 2120 CB ASP A 277 18967 14046 13846 -965 -2545 4027 A C ATOM 2121 CG ASP A 277 55.728 -30.305 21.701 1.00126.28 A C ANISOU 2121 CG ASP A 277 19521 14559 13899 -1110 -2656 4248 A C ATOM 2122 OD1 ASP A 277 56.042 -29.183 22.151 1.00139.13 A O ANISOU 2122 OD1 ASP A 277 21051 16476 15334 -1212 -2703 4183 A O ATOM 2123 OD2 ASP A 277 55.565 -31.316 22.419 1.00123.69 A O1- ANISOU 2123 OD2 ASP A 277 19448 14042 13506 -1123 -2702 4488 A O1- ATOM 2124 N ARG A 278 55.909 -30.097 17.123 1.00121.80 A N ANISOU 2124 N ARG A 278 18279 13791 14208 -605 -2412 3540 A N ATOM 2125 CA ARG A 278 56.315 -30.760 15.893 1.00115.66 A C ANISOU 2125 CA ARG A 278 17403 12840 13703 -336 -2417 3455 A C ATOM 2126 C ARG A 278 57.178 -29.839 15.033 1.00111.90 A C ANISOU 2126 C ARG A 278 16602 12608 13306 -181 -2453 3294 A C ATOM 2127 O ARG A 278 58.070 -30.313 14.343 1.00117.89 A O ANISOU 2127 O ARG A 278 17242 13320 14230 107 -2537 3309 A O ATOM 2128 CB ARG A 278 55.094 -31.249 15.125 1.00131.32 A C ANISOU 2128 CB ARG A 278 19493 14569 15832 -440 -2220 3297 A C ATOM 2129 CG ARG A 278 55.256 -32.541 14.325 1.00143.74 A C ANISOU 2129 CG ARG A 278 21168 15808 17637 -211 -2241 3311 A C ATOM 2130 CD ARG A 278 53.889 -33.209 14.071 1.00136.82 A C ANISOU 2130 CD ARG A 278 20498 14649 16836 -414 -2080 3241 A C ATOM 2131 NE ARG A 278 53.853 -33.916 12.788 1.00130.18 A N ANISOU 2131 NE ARG A 278 19662 13564 16234 -239 -2042 3089 A N ATOM 2132 CZ ARG A 278 53.592 -33.329 11.620 1.00129.36 A C ANISOU 2132 CZ ARG A 278 19370 13543 16236 -222 -1939 2822 A C ATOM 2133 NH1 ARG A 278 53.318 -32.036 11.556 1.00111.43 A N1+ ANISOU 2133 NH1 ARG A 278 16892 11574 13869 -366 -1861 2684 A N1+ ATOM 2134 NH2 ARG A 278 53.600 -34.036 10.499 1.00148.10 A N ANISOU 2134 NH2 ARG A 278 21782 15687 18803 -56 -1916 2691 A N ATOM 2135 N LEU A 279 56.974 -28.531 15.178 1.00109.39 A N ANISOU 2135 N LEU A 279 16153 12555 12855 -370 -2396 3164 A N ATOM 2136 CA LEU A 279 57.702 -27.534 14.424 1.00109.77 A C ANISOU 2136 CA LEU A 279 15906 12844 12958 -279 -2417 3014 A C ATOM 2137 C LEU A 279 58.855 -26.921 15.214 1.00119.51 A C ANISOU 2137 C LEU A 279 17016 14351 14039 -260 -2621 3156 A C ATOM 2138 O LEU A 279 59.756 -26.274 14.644 1.00116.56 A O ANISOU 2138 O LEU A 279 16378 14178 13728 -145 -2686 3092 A O ATOM 2139 CB LEU A 279 56.745 -26.427 13.979 1.00106.32 A C ANISOU 2139 CB LEU A 279 15403 12507 12485 -496 -2224 2770 A C ATOM 2140 CG LEU A 279 55.824 -26.818 12.823 1.00105.37 A C ANISOU 2140 CG LEU A 279 15295 12186 12555 -474 -2045 2583 A C ATOM 2141 CD1 LEU A 279 55.013 -25.600 12.376 1.00 94.08 A C ANISOU 2141 CD1 LEU A 279 13760 10899 11087 -658 -1878 2357 A C ATOM 2142 CD2 LEU A 279 56.678 -27.337 11.671 1.00111.41 A C ANISOU 2142 CD2 LEU A 279 15910 12885 13535 -168 -2095 2537 A C ATOM 2143 N LYS A 280 58.785 -27.122 16.526 1.00136.04 A N ANISOU 2143 N LYS A 280 19306 16457 15925 -392 -2718 3350 A N ATOM 2144 CA LYS A 280 59.813 -26.708 17.480 1.00135.31 A C ANISOU 2144 CA LYS A 280 19153 16604 15652 -401 -2946 3522 A C ATOM 2145 C LYS A 280 61.227 -26.889 16.930 1.00124.00 A C ANISOU 2145 C LYS A 280 17451 15288 14374 -108 -3123 3598 A C ATOM 2146 O LYS A 280 62.077 -26.001 17.062 1.00119.84 A O ANISOU 2146 O LYS A 280 16712 15044 13776 -134 -3250 3597 A O ATOM 2147 CB LYS A 280 59.625 -27.519 18.758 1.00135.60 A C ANISOU 2147 CB LYS A 280 19478 16529 15512 -469 -3044 3776 A C ATOM 2148 CG LYS A 280 60.598 -27.337 19.893 1.00127.15 A C ANISOU 2148 CG LYS A 280 18408 15671 14229 -481 -3304 3999 A C ATOM 2149 CD LYS A 280 60.188 -28.253 21.058 1.00116.96 A C ANISOU 2149 CD LYS A 280 17450 14220 12768 -553 -3358 4244 A C ATOM 2150 CE LYS A 280 61.306 -29.216 21.420 1.00115.12 A C ANISOU 2150 CE LYS A 280 17207 13955 12578 -286 -3617 4532 A C ATOM 2151 NZ LYS A 280 60.778 -30.566 21.772 1.00119.02 A N1+ ANISOU 2151 NZ LYS A 280 18000 14118 13104 -223 -3586 4720 A N1+ ATOM 2152 N ALA A 281 61.454 -28.036 16.288 1.00118.70 A N ANISOU 2152 N ALA A 281 16788 14393 13917 168 -3121 3657 A N ATOM 2153 CA ALA A 281 62.750 -28.398 15.723 1.00114.57 A C ANISOU 2153 CA ALA A 281 16018 13948 13562 498 -3261 3742 A C ATOM 2154 C ALA A 281 63.252 -27.349 14.734 1.00128.04 A C ANISOU 2154 C ALA A 281 17392 15894 15361 527 -3207 3544 A C ATOM 2155 O ALA A 281 64.237 -26.645 14.992 1.00131.01 A O ANISOU 2155 O ALA A 281 17537 16564 15675 526 -3363 3610 A O ATOM 2156 CB ALA A 281 62.648 -29.765 15.028 1.00106.62 A C ANISOU 2156 CB ALA A 281 15124 12606 12780 780 -3200 3772 A C ATOM 2157 N TYR A 282 62.541 -27.224 13.618 1.00128.13 A N ANISOU 2157 N TYR A 282 17387 15782 15512 528 -2989 3306 A N ATOM 2158 CA TYR A 282 62.941 -26.357 12.517 1.00102.01 A C ANISOU 2158 CA TYR A 282 13788 12657 12311 580 -2909 3117 A C ATOM 2159 C TYR A 282 62.995 -24.868 12.871 1.00103.16 A C ANISOU 2159 C TYR A 282 13809 13094 12292 306 -2928 3034 A C ATOM 2160 O TYR A 282 63.928 -24.169 12.482 1.00108.53 A O ANISOU 2160 O TYR A 282 14208 14019 13008 359 -2995 3018 A O ATOM 2161 CB TYR A 282 62.028 -26.552 11.328 1.00 94.09 A C ANISOU 2161 CB TYR A 282 12841 11449 11458 610 -2679 2885 A C ATOM 2162 CG TYR A 282 61.762 -27.981 10.965 1.00111.37 A C ANISOU 2162 CG TYR A 282 15214 13306 13796 826 -2640 2927 A C ATOM 2163 CD1 TYR A 282 60.698 -28.670 11.544 1.00117.33 A C ANISOU 2163 CD1 TYR A 282 16286 13798 14496 678 -2589 2968 A C ATOM 2164 CD2 TYR A 282 62.550 -28.644 10.032 1.00115.30 A C ANISOU 2164 CD2 TYR A 282 15580 13741 14486 1171 -2643 2921 A C ATOM 2165 CE1 TYR A 282 60.420 -29.977 11.191 1.00116.75 A C ANISOU 2165 CE1 TYR A 282 16406 13390 14562 849 -2554 3000 A C ATOM 2166 CE2 TYR A 282 62.292 -29.962 9.686 1.00120.06 A C ANISOU 2166 CE2 TYR A 282 16387 14005 15222 1370 -2606 2944 A C ATOM 2167 CZ TYR A 282 61.222 -30.621 10.265 1.00121.48 A C ANISOU 2167 CZ TYR A 282 16895 13909 15349 1198 -2568 2982 A C ATOM 2168 OH TYR A 282 60.944 -31.925 9.919 1.00124.48 A O ANISOU 2168 OH TYR A 282 17502 13929 15863 1368 -2535 3002 A O ATOM 2169 N VAL A 283 61.995 -24.389 13.600 1.00109.23 A N ANISOU 2169 N VAL A 283 14791 13828 12880 13 -2860 2981 A N ATOM 2170 CA VAL A 283 61.776 -22.949 13.745 1.00115.81 A C ANISOU 2170 CA VAL A 283 15558 14869 13573 -247 -2816 2840 A C ATOM 2171 C VAL A 283 62.643 -22.296 14.818 1.00131.22 A C ANISOU 2171 C VAL A 283 17452 17076 15327 -377 -3037 2982 A C ATOM 2172 O VAL A 283 63.331 -21.301 14.540 1.00143.73 A O ANISOU 2172 O VAL A 283 18814 18891 16904 -434 -3093 2921 A O ATOM 2173 CB VAL A 283 60.280 -22.650 14.016 1.00110.03 A C ANISOU 2173 CB VAL A 283 15073 13998 12733 -491 -2622 2703 A C ATOM 2174 CG1 VAL A 283 60.014 -21.145 14.067 1.00 99.17 A C ANISOU 2174 CG1 VAL A 283 13642 12807 11228 -728 -2554 2538 A C ATOM 2175 CG2 VAL A 283 59.439 -23.287 12.909 1.00105.74 A C ANISOU 2175 CG2 VAL A 283 14565 13219 12389 -381 -2426 2561 A C ATOM 2176 N ARG A 284 62.627 -22.854 16.026 1.00120.34 A N ANISOU 2176 N ARG A 284 16278 15658 13785 -433 -3170 3176 A N ATOM 2177 CA ARG A 284 63.534 -22.369 17.090 1.00138.25 A C ANISOU 2177 CA ARG A 284 18501 18173 15853 -541 -3420 3336 A C ATOM 2178 C ARG A 284 63.034 -21.067 17.743 1.00144.45 A C ANISOU 2178 C ARG A 284 19400 19090 16393 -882 -3384 3206 A C ATOM 2179 O ARG A 284 62.837 -21.014 18.951 1.00161.93 A O ANISOU 2179 O ARG A 284 21833 21334 18358 -1052 -3475 3307 A O ATOM 2180 CB ARG A 284 64.942 -22.128 16.537 1.00134.59 A C ANISOU 2180 CB ARG A 284 17673 17939 15524 -371 -3583 3396 A C ATOM 2181 CG ARG A 284 65.589 -23.338 15.886 1.00144.50 A C ANISOU 2181 CG ARG A 284 18790 19093 17018 0 -3623 3523 A C ATOM 2182 CD ARG A 284 66.805 -22.914 15.059 1.00145.11 A C ANISOU 2182 CD ARG A 284 18466 19412 17255 160 -3697 3519 A C ATOM 2183 NE ARG A 284 67.812 -23.970 14.999 1.00166.80 A N ANISOU 2183 NE ARG A 284 21061 22171 20144 500 -3849 3738 A N ATOM 2184 CZ ARG A 284 69.110 -23.749 14.786 1.00174.38 A C ANISOU 2184 CZ ARG A 284 21667 23403 21185 639 -4007 3846 A C ATOM 2185 NH1 ARG A 284 69.550 -22.510 14.609 1.00177.18 A N1+ ANISOU 2185 NH1 ARG A 284 21796 24030 21491 438 -4038 3756 A N1+ ATOM 2186 NH2 ARG A 284 69.966 -24.763 14.758 1.00170.84 A N ANISOU 2186 NH2 ARG A 284 21088 22954 20869 977 -4133 4052 A N ATOM 2187 N ASP A 285 62.875 -20.022 16.934 1.00129.14 A N ANISOU 2187 N ASP A 285 17320 17228 14519 -967 -3253 2987 A N ATOM 2188 CA ASP A 285 62.435 -18.723 17.451 1.00113.86 A C ANISOU 2188 CA ASP A 285 15493 15398 12369 -1267 -3207 2845 A C ATOM 2189 C ASP A 285 61.053 -18.789 18.107 1.00110.51 A C ANISOU 2189 C ASP A 285 15400 14805 11781 -1429 -3028 2780 A C ATOM 2190 O ASP A 285 60.080 -19.204 17.491 1.00107.75 A O ANISOU 2190 O ASP A 285 15114 14264 11560 -1369 -2812 2680 A O ATOM 2191 CB ASP A 285 62.397 -17.680 16.338 1.00110.40 A C ANISOU 2191 CB ASP A 285 14863 15023 12058 -1301 -3068 2624 A C ATOM 2192 CG ASP A 285 61.981 -16.305 16.835 1.00115.13 A C ANISOU 2192 CG ASP A 285 15588 15707 12447 -1593 -3020 2472 A C ATOM 2193 OD1 ASP A 285 60.789 -16.046 17.076 1.00112.97 A O ANISOU 2193 OD1 ASP A 285 15541 15305 12075 -1713 -2829 2348 A O ATOM 2194 OD2 ASP A 285 62.866 -15.436 16.900 1.00117.67 A O1- ANISOU 2194 OD2 ASP A 285 15765 16226 12717 -1699 -3166 2468 A O1- ATOM 2195 N PRO A 286 60.977 -18.384 19.378 1.00114.70 A N ANISOU 2195 N PRO A 286 16140 15420 12019 -1639 -3121 2841 A N ATOM 2196 CA PRO A 286 59.729 -18.464 20.157 1.00113.63 A C ANISOU 2196 CA PRO A 286 16323 15155 11694 -1795 -2953 2807 A C ATOM 2197 C PRO A 286 58.583 -17.717 19.477 1.00109.77 A C ANISOU 2197 C PRO A 286 15861 14580 11265 -1878 -2662 2550 A C ATOM 2198 O PRO A 286 57.487 -18.266 19.325 1.00114.00 A O ANISOU 2198 O PRO A 286 16517 14941 11857 -1862 -2459 2514 A O ATOM 2199 CB PRO A 286 60.089 -17.785 21.471 1.00115.71 A C ANISOU 2199 CB PRO A 286 16754 15587 11620 -2015 -3118 2867 A C ATOM 2200 CG PRO A 286 61.568 -17.920 21.571 1.00121.33 A C ANISOU 2200 CG PRO A 286 17259 16481 12360 -1930 -3432 3034 A C ATOM 2201 CD PRO A 286 62.089 -17.828 20.160 1.00116.77 A C ANISOU 2201 CD PRO A 286 16344 15918 12101 -1748 -3396 2948 A C ATOM 2202 N TYR A 287 58.839 -16.478 19.058 1.00106.87 A N ANISOU 2202 N TYR A 287 15376 14335 10893 -1968 -2646 2382 A N ATOM 2203 CA TYR A 287 57.806 -15.615 18.467 1.00101.46 A C ANISOU 2203 CA TYR A 287 14719 13584 10244 -2046 -2387 2143 A C ATOM 2204 C TYR A 287 57.251 -16.195 17.160 1.00 93.42 A C ANISOU 2204 C TYR A 287 13555 12418 9522 -1862 -2214 2064 A C ATOM 2205 O TYR A 287 56.043 -16.201 16.943 1.00 95.05 A O ANISOU 2205 O TYR A 287 13858 12502 9754 -1893 -1989 1954 A O ATOM 2206 CB TYR A 287 58.356 -14.209 18.206 1.00100.15 A C ANISOU 2206 CB TYR A 287 14451 13564 10035 -2161 -2434 2001 A C ATOM 2207 CG TYR A 287 58.779 -13.475 19.440 1.00109.83 A C ANISOU 2207 CG TYR A 287 15851 14923 10954 -2378 -2587 2030 A C ATOM 2208 CD1 TYR A 287 57.905 -13.324 20.504 1.00111.52 A C ANISOU 2208 CD1 TYR A 287 16374 15089 10907 -2526 -2484 2005 A C ATOM 2209 CD2 TYR A 287 60.049 -12.907 19.542 1.00123.18 A C ANISOU 2209 CD2 TYR A 287 17401 16795 12606 -2446 -2833 2078 A C ATOM 2210 CE1 TYR A 287 58.273 -12.622 21.639 1.00119.82 A C ANISOU 2210 CE1 TYR A 287 17617 16257 11649 -2731 -2622 2012 A C ATOM 2211 CE2 TYR A 287 60.438 -12.243 20.689 1.00131.51 A C ANISOU 2211 CE2 TYR A 287 18633 17969 13364 -2666 -2995 2097 A C ATOM 2212 CZ TYR A 287 59.541 -12.084 21.723 1.00129.34 A C ANISOU 2212 CZ TYR A 287 18693 17632 12818 -2805 -2887 2054 A C ATOM 2213 OH TYR A 287 59.919 -11.395 22.851 1.00133.60 A O ANISOU 2213 OH TYR A 287 19436 18286 13040 -3027 -3045 2055 A O ATOM 2214 N ALA A 288 58.153 -16.655 16.291 1.00 82.66 A N ANISOU 2214 N ALA A 288 11952 11079 8373 -1673 -2324 2120 A N ATOM 2215 CA ALA A 288 57.769 -17.335 15.079 1.00 82.11 A C ANISOU 2215 CA ALA A 288 11761 10868 8567 -1484 -2193 2060 A C ATOM 2216 C ALA A 288 56.811 -18.494 15.366 1.00 93.44 A C ANISOU 2216 C ALA A 288 13381 12098 10021 -1453 -2091 2129 A C ATOM 2217 O ALA A 288 55.778 -18.646 14.708 1.00 99.99 A O ANISOU 2217 O ALA A 288 14231 12796 10962 -1442 -1893 2006 A O ATOM 2218 CB ALA A 288 58.997 -17.840 14.350 1.00 79.93 A C ANISOU 2218 CB ALA A 288 11238 10653 8477 -1268 -2346 2151 A C ATOM 2219 N LEU A 289 57.149 -19.309 16.352 1.00 90.24 A N ANISOU 2219 N LEU A 289 13110 11669 9505 -1449 -2232 2334 A N ATOM 2220 CA LEU A 289 56.311 -20.443 16.701 1.00 88.52 A C ANISOU 2220 CA LEU A 289 13084 11250 9296 -1438 -2148 2429 A C ATOM 2221 C LEU A 289 54.953 -19.983 17.222 1.00 87.64 A C ANISOU 2221 C LEU A 289 13163 11098 9036 -1649 -1935 2328 A C ATOM 2222 O LEU A 289 53.926 -20.589 16.930 1.00 90.57 A O ANISOU 2222 O LEU A 289 13606 11305 9500 -1656 -1768 2296 A O ATOM 2223 CB LEU A 289 57.008 -21.361 17.719 1.00 90.83 A C ANISOU 2223 CB LEU A 289 13498 11531 9480 -1392 -2356 2693 A C ATOM 2224 CG LEU A 289 58.134 -22.235 17.153 1.00106.46 A C ANISOU 2224 CG LEU A 289 15311 13481 11657 -1124 -2532 2824 A C ATOM 2225 CD1 LEU A 289 59.063 -22.719 18.243 1.00120.17 A C ANISOU 2225 CD1 LEU A 289 17118 15296 13244 -1091 -2784 3082 A C ATOM 2226 CD2 LEU A 289 57.602 -23.380 16.322 1.00117.08 A C ANISOU 2226 CD2 LEU A 289 16684 14567 13233 -961 -2418 2814 A C ATOM 2227 N ASP A 290 54.944 -18.900 17.987 1.00 89.53 A N ANISOU 2227 N ASP A 290 13481 11490 9044 -1822 -1936 2274 A N ATOM 2228 CA ASP A 290 53.700 -18.388 18.522 1.00 96.95 A C ANISOU 2228 CA ASP A 290 14596 12411 9827 -2001 -1719 2175 A C ATOM 2229 C ASP A 290 52.767 -17.890 17.426 1.00103.61 A C ANISOU 2229 C ASP A 290 15320 13199 10845 -1982 -1493 1958 A C ATOM 2230 O ASP A 290 51.563 -18.184 17.437 1.00103.58 A O ANISOU 2230 O ASP A 290 15398 13097 10861 -2040 -1294 1919 A O ATOM 2231 CB ASP A 290 53.943 -17.282 19.542 1.00 96.75 A C ANISOU 2231 CB ASP A 290 14701 12552 9507 -2174 -1769 2143 A C ATOM 2232 CG ASP A 290 52.657 -16.859 20.235 1.00102.22 A C ANISOU 2232 CG ASP A 290 15602 13224 10013 -2337 -1531 2060 A C ATOM 2233 OD1 ASP A 290 52.016 -17.746 20.835 1.00113.44 A O ANISOU 2233 OD1 ASP A 290 17177 14555 11370 -2375 -1457 2188 A O ATOM 2234 OD2 ASP A 290 52.331 -15.658 20.207 1.00100.83 A O1- ANISOU 2234 OD2 ASP A 290 15440 13121 9749 -2422 -1421 1881 A O1- ATOM 2235 N LEU A 291 53.322 -17.149 16.472 1.00102.52 A N ANISOU 2235 N LEU A 291 14981 13135 10837 -1904 -1527 1829 A N ATOM 2236 CA LEU A 291 52.536 -16.641 15.356 1.00 89.73 A C ANISOU 2236 CA LEU A 291 13236 11473 9381 -1869 -1338 1633 A C ATOM 2237 C LEU A 291 51.975 -17.772 14.484 1.00 85.87 A C ANISOU 2237 C LEU A 291 12682 10818 9125 -1748 -1263 1643 A C ATOM 2238 O LEU A 291 50.790 -17.735 14.104 1.00 85.33 A O ANISOU 2238 O LEU A 291 12621 10680 9119 -1791 -1069 1538 A O ATOM 2239 CB LEU A 291 53.352 -15.668 14.492 1.00 77.94 A C ANISOU 2239 CB LEU A 291 11548 10091 7975 -1808 -1404 1519 A C ATOM 2240 CG LEU A 291 52.637 -15.113 13.247 1.00 75.58 A C ANISOU 2240 CG LEU A 291 11114 9757 7844 -1753 -1229 1327 A C ATOM 2241 CD1 LEU A 291 51.251 -14.588 13.603 1.00 79.54 A C ANISOU 2241 CD1 LEU A 291 11743 10226 8252 -1872 -1006 1220 A C ATOM 2242 CD2 LEU A 291 53.467 -14.033 12.575 1.00 72.40 A C ANISOU 2242 CD2 LEU A 291 10556 9471 7480 -1729 -1292 1234 A C ATOM 2243 N ILE A 292 52.816 -18.759 14.169 1.00 83.10 A N ANISOU 2243 N ILE A 292 12269 10404 8899 -1598 -1418 1765 A N ATOM 2244 CA ILE A 292 52.372 -19.879 13.348 1.00 83.38 A C ANISOU 2244 CA ILE A 292 12275 10257 9148 -1482 -1365 1768 A C ATOM 2245 C ILE A 292 51.239 -20.615 14.047 1.00 95.51 A C ANISOU 2245 C ILE A 292 14006 11659 10622 -1610 -1248 1841 A C ATOM 2246 O ILE A 292 50.271 -21.046 13.415 1.00 97.80 A O ANISOU 2246 O ILE A 292 14284 11826 11047 -1623 -1112 1765 A O ATOM 2247 CB ILE A 292 53.481 -20.910 13.125 1.00 73.78 A C ANISOU 2247 CB ILE A 292 11013 8973 8045 -1289 -1551 1912 A C ATOM 2248 CG1 ILE A 292 54.633 -20.292 12.348 1.00 77.51 A C ANISOU 2248 CG1 ILE A 292 11259 9588 8601 -1149 -1655 1854 A C ATOM 2249 CG2 ILE A 292 52.916 -22.130 12.420 1.00 75.37 A C ANISOU 2249 CG2 ILE A 292 11252 8945 8438 -1193 -1490 1913 A C ATOM 2250 CD1 ILE A 292 55.885 -21.141 12.324 1.00 86.28 A C ANISOU 2250 CD1 ILE A 292 12302 10691 9790 -950 -1850 2017 A C ATOM 2251 N ASP A 293 51.383 -20.762 15.362 1.00 91.13 A N ANISOU 2251 N ASP A 293 13630 11138 9857 -1716 -1310 1997 A N ATOM 2252 CA ASP A 293 50.368 -21.398 16.164 1.00 93.04 A C ANISOU 2252 CA ASP A 293 14066 11278 10006 -1859 -1193 2091 A C ATOM 2253 C ASP A 293 49.027 -20.662 16.067 1.00 93.98 A C ANISOU 2253 C ASP A 293 14176 11438 10093 -2001 -945 1931 A C ATOM 2254 O ASP A 293 47.952 -21.285 16.059 1.00115.56 A O ANISOU 2254 O ASP A 293 16964 14059 12882 -2084 -800 1948 A O ATOM 2255 CB ASP A 293 50.829 -21.478 17.623 1.00 96.44 A C ANISOU 2255 CB ASP A 293 14692 11778 10171 -1952 -1303 2278 A C ATOM 2256 CG ASP A 293 49.922 -22.361 18.466 1.00103.74 A C ANISOU 2256 CG ASP A 293 15833 12579 11003 -2084 -1200 2424 A C ATOM 2257 OD1 ASP A 293 49.413 -23.365 17.918 1.00112.22 A O ANISOU 2257 OD1 ASP A 293 16909 13463 12264 -2051 -1148 2457 A O ATOM 2258 OD2 ASP A 293 49.697 -22.035 19.647 1.00105.21 A O1- ANISOU 2258 OD2 ASP A 293 16190 12857 10925 -2232 -1164 2500 A O1- ATOM 2259 N LYS A 294 49.089 -19.330 15.994 1.00 75.02 A N ANISOU 2259 N LYS A 294 11701 9196 7607 -2029 -896 1783 A N ATOM 2260 CA LYS A 294 47.853 -18.534 15.970 1.00 74.67 A C ANISOU 2260 CA LYS A 294 11649 9203 7520 -2137 -659 1636 A C ATOM 2261 C LYS A 294 47.258 -18.436 14.565 1.00 85.36 A C ANISOU 2261 C LYS A 294 12804 10508 9121 -2054 -560 1475 A C ATOM 2262 O LYS A 294 46.079 -18.121 14.404 1.00 87.69 A O ANISOU 2262 O LYS A 294 13065 10813 9437 -2125 -364 1382 A O ATOM 2263 CB LYS A 294 48.038 -17.180 16.609 1.00 72.26 A C ANISOU 2263 CB LYS A 294 11400 9058 6995 -2209 -629 1550 A C ATOM 2264 CG LYS A 294 48.517 -17.276 18.028 1.00 84.54 A C ANISOU 2264 CG LYS A 294 13173 10669 8278 -2311 -724 1700 A C ATOM 2265 CD LYS A 294 48.695 -15.954 18.734 1.00 92.95 A C ANISOU 2265 CD LYS A 294 14337 11878 9100 -2402 -702 1605 A C ATOM 2266 CE LYS A 294 49.027 -16.233 20.202 1.00105.25 A C ANISOU 2266 CE LYS A 294 16142 13484 10364 -2518 -790 1769 A C ATOM 2267 NZ LYS A 294 49.318 -15.017 20.982 1.00127.00 A N1+ ANISOU 2267 NZ LYS A 294 19035 16369 12850 -2620 -803 1681 A N1+ ATOM 2268 N LEU A 295 48.081 -18.744 13.554 1.00 82.31 A N ANISOU 2268 N LEU A 295 12282 10075 8914 -1898 -698 1451 A N ATOM 2269 CA LEU A 295 47.599 -18.895 12.186 1.00 78.60 A C ANISOU 2269 CA LEU A 295 11650 9540 8674 -1811 -634 1320 A C ATOM 2270 C LEU A 295 46.926 -20.256 11.959 1.00 85.70 A C ANISOU 2270 C LEU A 295 12598 10255 9708 -1831 -606 1390 A C ATOM 2271 O LEU A 295 45.843 -20.330 11.370 1.00 83.51 A O ANISOU 2271 O LEU A 295 12252 9939 9535 -1882 -472 1297 A O ATOM 2272 CB LEU A 295 48.734 -18.701 11.182 1.00 80.94 A C ANISOU 2272 CB LEU A 295 11796 9863 9094 -1635 -775 1264 A C ATOM 2273 CG LEU A 295 49.283 -17.262 11.051 1.00 77.79 A C ANISOU 2273 CG LEU A 295 11309 9633 8615 -1625 -785 1160 A C ATOM 2274 CD1 LEU A 295 50.526 -17.268 10.187 1.00 83.88 A C ANISOU 2274 CD1 LEU A 295 11933 10437 9501 -1462 -934 1153 A C ATOM 2275 CD2 LEU A 295 48.242 -16.375 10.422 1.00 70.37 A C ANISOU 2275 CD2 LEU A 295 10289 8732 7715 -1659 -606 988 A C ATOM 2276 N LEU A 296 47.544 -21.324 12.453 1.00 88.12 A N ANISOU 2276 N LEU A 296 13027 10446 10007 -1800 -737 1560 A N ATOM 2277 CA LEU A 296 46.968 -22.653 12.292 1.00 83.58 A C ANISOU 2277 CA LEU A 296 12536 9665 9556 -1832 -723 1638 A C ATOM 2278 C LEU A 296 45.971 -22.998 13.382 1.00 85.73 A C ANISOU 2278 C LEU A 296 12964 9908 9701 -2040 -597 1752 A C ATOM 2279 O LEU A 296 46.059 -24.055 14.002 1.00 99.15 A O ANISOU 2279 O LEU A 296 14829 11465 11379 -2081 -655 1929 A O ATOM 2280 CB LEU A 296 48.074 -23.722 12.189 1.00 76.77 A C ANISOU 2280 CB LEU A 296 11741 8655 8773 -1673 -915 1768 A C ATOM 2281 CG LEU A 296 48.987 -23.564 10.970 1.00 80.18 A C ANISOU 2281 CG LEU A 296 12005 9101 9357 -1452 -1014 1656 A C ATOM 2282 CD1 LEU A 296 50.033 -24.649 10.922 1.00 83.20 A C ANISOU 2282 CD1 LEU A 296 12453 9339 9818 -1272 -1183 1791 A C ATOM 2283 CD2 LEU A 296 48.164 -23.501 9.680 1.00 70.85 A C ANISOU 2283 CD2 LEU A 296 10704 7871 8345 -1442 -906 1464 A C ATOM 2284 N VAL A 297 45.020 -22.109 13.610 1.00 86.82 A N ANISOU 2284 N VAL A 297 13050 10181 9755 -2163 -416 1659 A N ATOM 2285 CA VAL A 297 43.963 -22.335 14.601 1.00 87.39 A C ANISOU 2285 CA VAL A 297 13241 10260 9703 -2363 -255 1754 A C ATOM 2286 C VAL A 297 42.758 -22.974 13.926 1.00 88.83 A C ANISOU 2286 C VAL A 297 13345 10339 10068 -2457 -134 1711 A C ATOM 2287 O VAL A 297 42.373 -22.570 12.827 1.00 91.76 A O ANISOU 2287 O VAL A 297 13534 10740 10591 -2401 -95 1542 A O ATOM 2288 CB VAL A 297 43.583 -21.015 15.311 1.00 80.33 A C ANISOU 2288 CB VAL A 297 12344 9576 8601 -2433 -109 1681 A C ATOM 2289 CG1 VAL A 297 42.174 -21.061 15.866 1.00 74.23 A C ANISOU 2289 CG1 VAL A 297 11593 8841 7767 -2612 127 1705 A C ATOM 2290 CG2 VAL A 297 44.589 -20.695 16.396 1.00 74.90 A C ANISOU 2290 CG2 VAL A 297 11818 8963 7676 -2426 -226 1786 A C ATOM 2291 N LEU A 298 42.158 -23.966 14.588 1.00 91.29 A N ANISOU 2291 N LEU A 298 13794 10533 10358 -2614 -81 1870 A N ATOM 2292 CA LEU A 298 41.053 -24.738 14.007 1.00 81.26 A C ANISOU 2292 CA LEU A 298 12464 9144 9266 -2740 8 1856 A C ATOM 2293 C LEU A 298 39.784 -23.921 13.768 1.00 87.14 A C ANISOU 2293 C LEU A 298 13020 10059 10028 -2843 221 1727 A C ATOM 2294 O LEU A 298 39.254 -23.888 12.656 1.00 88.55 A O ANISOU 2294 O LEU A 298 13024 10227 10392 -2825 235 1588 A O ATOM 2295 CB LEU A 298 40.734 -25.936 14.881 1.00 79.89 A C ANISOU 2295 CB LEU A 298 12496 8808 9048 -2908 21 2078 A C ATOM 2296 CG LEU A 298 41.742 -27.078 14.832 1.00 93.60 A C ANISOU 2296 CG LEU A 298 14410 10301 10850 -2806 -190 2209 A C ATOM 2297 CD1 LEU A 298 41.531 -28.027 15.998 1.00122.14 A C ANISOU 2297 CD1 LEU A 298 18267 13791 14349 -2970 -169 2462 A C ATOM 2298 CD2 LEU A 298 41.679 -27.816 13.504 1.00 88.27 A C ANISOU 2298 CD2 LEU A 298 13668 9428 10439 -2740 -275 2103 A C ATOM 2299 N ASP A 299 39.282 -23.271 14.807 1.00 89.90 A N ANISOU 2299 N ASP A 299 13406 10572 10180 -2942 390 1773 A N ATOM 2300 CA ASP A 299 38.098 -22.440 14.652 1.00 90.17 A C ANISOU 2300 CA ASP A 299 13255 10783 10222 -3007 607 1659 A C ATOM 2301 C ASP A 299 38.465 -21.163 13.891 1.00 89.38 A C ANISOU 2301 C ASP A 299 13002 10813 10145 -2823 586 1455 A C ATOM 2302 O ASP A 299 39.221 -20.317 14.392 1.00 88.81 A O ANISOU 2302 O ASP A 299 13008 10829 9904 -2732 557 1429 A O ATOM 2303 CB ASP A 299 37.506 -22.114 16.018 1.00 97.99 A C ANISOU 2303 CB ASP A 299 14348 11907 10976 -3143 810 1765 A C ATOM 2304 CG ASP A 299 36.215 -21.332 15.927 1.00109.00 A C ANISOU 2304 CG ASP A 299 15543 13487 12384 -3199 1060 1666 A C ATOM 2305 OD1 ASP A 299 35.626 -21.275 14.820 1.00104.21 A O ANISOU 2305 OD1 ASP A 299 14714 12889 11992 -3175 1067 1548 A O ATOM 2306 OD2 ASP A 299 35.782 -20.812 16.983 1.00118.34 A O1- ANISOU 2306 OD2 ASP A 299 16797 14810 13355 -3263 1249 1713 A O1- ATOM 2307 N PRO A 300 37.926 -21.015 12.675 1.00 89.03 A N ANISOU 2307 N PRO A 300 12746 10777 10301 -2778 594 1315 A N ATOM 2308 CA PRO A 300 38.187 -19.852 11.816 1.00 85.39 A C ANISOU 2308 CA PRO A 300 12135 10426 9883 -2607 576 1130 A C ATOM 2309 C PRO A 300 37.946 -18.546 12.558 1.00 82.33 A C ANISOU 2309 C PRO A 300 11751 10222 9307 -2583 740 1078 A C ATOM 2310 O PRO A 300 38.554 -17.535 12.228 1.00 88.39 A O ANISOU 2310 O PRO A 300 12492 11054 10037 -2444 696 965 A O ATOM 2311 CB PRO A 300 37.133 -20.002 10.709 1.00 77.27 A C ANISOU 2311 CB PRO A 300 10884 9411 9063 -2638 627 1032 A C ATOM 2312 CG PRO A 300 36.126 -20.952 11.264 1.00 80.50 A C ANISOU 2312 CG PRO A 300 11309 9779 9498 -2856 734 1163 A C ATOM 2313 CD PRO A 300 36.938 -21.914 12.064 1.00 81.57 A C ANISOU 2313 CD PRO A 300 11694 9749 9546 -2910 626 1328 A C ATOM 2314 N ALA A 301 37.069 -18.580 13.550 1.00 81.40 A N ANISOU 2314 N ALA A 301 11677 10182 9070 -2721 933 1163 A N ATOM 2315 CA ALA A 301 36.676 -17.386 14.275 1.00 79.31 A C ANISOU 2315 CA ALA A 301 11426 10084 8621 -2697 1124 1105 A C ATOM 2316 C ALA A 301 37.659 -17.056 15.384 1.00 82.61 A C ANISOU 2316 C ALA A 301 12095 10507 8783 -2689 1069 1164 A C ATOM 2317 O ALA A 301 37.655 -15.949 15.918 1.00 87.40 A O ANISOU 2317 O ALA A 301 12764 11226 9219 -2641 1178 1086 A O ATOM 2318 CB ALA A 301 35.276 -17.539 14.849 1.00 75.76 A C ANISOU 2318 CB ALA A 301 10900 9738 8146 -2837 1379 1166 A C ATOM 2319 N GLN A 302 38.485 -18.026 15.761 1.00 79.59 A N ANISOU 2319 N GLN A 302 11872 10000 8367 -2737 898 1305 A N ATOM 2320 CA GLN A 302 39.530 -17.781 16.750 1.00 85.59 A C ANISOU 2320 CA GLN A 302 12859 10770 8890 -2729 797 1374 A C ATOM 2321 C GLN A 302 40.895 -17.617 16.081 1.00 92.26 A C ANISOU 2321 C GLN A 302 13694 11555 9804 -2586 542 1323 A C ATOM 2322 O GLN A 302 41.881 -17.283 16.737 1.00 99.73 A O ANISOU 2322 O GLN A 302 14788 12529 10576 -2565 422 1360 A O ATOM 2323 CB GLN A 302 39.570 -18.885 17.790 1.00101.01 A C ANISOU 2323 CB GLN A 302 15009 12650 10720 -2871 780 1592 A C ATOM 2324 CG GLN A 302 38.320 -18.990 18.673 1.00113.16 A C ANISOU 2324 CG GLN A 302 16585 14274 12134 -3031 1049 1668 A C ATOM 2325 CD GLN A 302 38.453 -20.094 19.711 1.00121.15 A C ANISOU 2325 CD GLN A 302 17817 15204 13008 -3177 1020 1904 A C ATOM 2326 NE2 GLN A 302 37.583 -21.116 19.640 1.00108.09 A N ANISOU 2326 NE2 GLN A 302 16116 13473 11479 -3319 1110 2020 A N ATOM 2327 OE1 GLN A 302 39.347 -20.034 20.562 1.00122.48 A O ANISOU 2327 OE1 GLN A 302 18200 15377 12959 -3169 904 1988 A O ATOM 2328 N ARG A 303 40.935 -17.839 14.779 1.00 97.08 A N ANISOU 2328 N ARG A 303 14124 12100 10661 -2493 462 1239 A N ATOM 2329 CA ARG A 303 42.161 -17.715 13.989 1.00 76.40 A C ANISOU 2329 CA ARG A 303 11459 9436 8133 -2346 246 1186 A C ATOM 2330 C ARG A 303 42.546 -16.259 13.802 1.00 74.20 A C ANISOU 2330 C ARG A 303 11136 9279 7778 -2260 261 1038 A C ATOM 2331 O ARG A 303 41.714 -15.442 13.418 1.00 80.52 A O ANISOU 2331 O ARG A 303 11827 10153 8610 -2242 419 912 A O ATOM 2332 CB ARG A 303 41.973 -18.389 12.628 1.00 74.89 A C ANISOU 2332 CB ARG A 303 11102 9141 8211 -2277 184 1130 A C ATOM 2333 CG ARG A 303 43.249 -18.533 11.817 1.00 76.19 A C ANISOU 2333 CG ARG A 303 11227 9246 8476 -2120 -28 1103 A C ATOM 2334 CD ARG A 303 42.947 -19.293 10.536 1.00 71.19 A C ANISOU 2334 CD ARG A 303 10467 8498 8082 -2063 -68 1043 A C ATOM 2335 NE ARG A 303 42.239 -20.522 10.846 1.00 83.96 A N ANISOU 2335 NE ARG A 303 12163 9982 9755 -2191 -36 1155 A N ATOM 2336 CZ ARG A 303 41.297 -21.085 10.099 1.00 83.50 A C ANISOU 2336 CZ ARG A 303 12011 9854 9860 -2250 17 1106 A C ATOM 2337 NH1 ARG A 303 40.944 -20.550 8.940 1.00 73.42 A N1+ ANISOU 2337 NH1 ARG A 303 10554 8633 8706 -2176 37 945 A N1+ ATOM 2338 NH2 ARG A 303 40.704 -22.195 10.516 1.00 96.56 A N ANISOU 2338 NH2 ARG A 303 13760 11379 11548 -2398 43 1227 A N ATOM 2339 N ILE A 304 43.810 -15.939 14.046 1.00 72.73 A N ANISOU 2339 N ILE A 304 11025 9109 7498 -2208 90 1060 A N ATOM 2340 CA ILE A 304 44.316 -14.573 13.912 1.00 74.02 A C ANISOU 2340 CA ILE A 304 11171 9369 7582 -2152 78 931 A C ATOM 2341 C ILE A 304 44.058 -13.976 12.524 1.00 72.58 A C ANISOU 2341 C ILE A 304 10784 9195 7595 -2038 114 776 A C ATOM 2342 O ILE A 304 44.102 -14.695 11.532 1.00 74.72 A O ANISOU 2342 O ILE A 304 10927 9396 8066 -1967 46 775 A O ATOM 2343 CB ILE A 304 45.840 -14.522 14.226 1.00 78.14 A C ANISOU 2343 CB ILE A 304 11766 9906 8017 -2124 -154 1000 A C ATOM 2344 CG1 ILE A 304 46.272 -13.097 14.572 1.00 77.84 A C ANISOU 2344 CG1 ILE A 304 11790 9969 7817 -2144 -152 896 A C ATOM 2345 CG2 ILE A 304 46.654 -15.105 13.082 1.00 73.32 A C ANISOU 2345 CG2 ILE A 304 10998 9234 7623 -1992 -320 1009 A C ATOM 2346 CD1 ILE A 304 47.703 -12.983 14.992 1.00 74.08 A C ANISOU 2346 CD1 ILE A 304 11375 9534 7236 -2154 -382 969 A C ATOM 2347 N ASP A 305 43.829 -12.664 12.456 1.00 67.58 A N ANISOU 2347 N ASP A 305 10141 8639 6895 -2014 214 646 A N ATOM 2348 CA ASP A 305 43.683 -12.003 11.159 1.00 66.68 A C ANISOU 2348 CA ASP A 305 9851 8536 6947 -1899 233 513 A C ATOM 2349 C ASP A 305 44.966 -11.279 10.747 1.00 76.65 A C ANISOU 2349 C ASP A 305 11102 9820 8198 -1838 76 472 A C ATOM 2350 O ASP A 305 45.900 -11.145 11.546 1.00 72.93 A O ANISOU 2350 O ASP A 305 10758 9372 7580 -1895 -38 533 A O ATOM 2351 CB ASP A 305 42.487 -11.060 11.152 1.00 63.84 A C ANISOU 2351 CB ASP A 305 9460 8232 6563 -1889 455 402 A C ATOM 2352 CG ASP A 305 42.638 -9.888 12.105 1.00 74.02 A C ANISOU 2352 CG ASP A 305 10924 9570 7628 -1927 530 348 A C ATOM 2353 OD1 ASP A 305 43.765 -9.607 12.569 1.00 94.34 A O ANISOU 2353 OD1 ASP A 305 13621 12144 10080 -1964 384 374 A O ATOM 2354 OD2 ASP A 305 41.652 -9.160 12.292 1.00 74.42 A O1- ANISOU 2354 OD2 ASP A 305 10981 9659 7634 -1907 730 268 A O1- ATOM 2355 N SER A 306 45.007 -10.812 9.503 1.00 76.79 A N ANISOU 2355 N SER A 306 10967 9843 8368 -1731 68 375 A N ATOM 2356 CA SER A 306 46.217 -10.194 9.010 1.00 78.65 A C ANISOU 2356 CA SER A 306 11167 10105 8611 -1682 -70 350 A C ATOM 2357 C SER A 306 46.606 -8.963 9.828 1.00 69.63 A C ANISOU 2357 C SER A 306 10172 9006 7276 -1758 -58 308 A C ATOM 2358 O SER A 306 47.788 -8.694 10.066 1.00 67.86 A O ANISOU 2358 O SER A 306 9986 8813 6984 -1795 -212 346 A O ATOM 2359 CB SER A 306 46.102 -9.879 7.523 1.00 69.72 A C ANISOU 2359 CB SER A 306 9858 8974 7658 -1559 -59 259 A C ATOM 2360 OG SER A 306 44.813 -9.474 7.174 1.00 79.99 A O ANISOU 2360 OG SER A 306 11109 10276 9006 -1532 110 174 A O ATOM 2361 N ASP A 307 45.621 -8.227 10.294 1.00 70.33 A N ANISOU 2361 N ASP A 307 10349 9098 7272 -1786 121 231 A N ATOM 2362 CA ASP A 307 45.906 -7.005 11.047 1.00 72.56 A C ANISOU 2362 CA ASP A 307 10808 9397 7365 -1855 147 167 A C ATOM 2363 C ASP A 307 46.623 -7.317 12.355 1.00 69.54 A C ANISOU 2363 C ASP A 307 10607 9037 6775 -1986 37 259 A C ATOM 2364 O ASP A 307 47.641 -6.701 12.675 1.00 78.47 A O ANISOU 2364 O ASP A 307 11823 10190 7799 -2055 -98 256 A O ATOM 2365 CB ASP A 307 44.637 -6.203 11.311 1.00 78.50 A C ANISOU 2365 CB ASP A 307 11629 10140 8056 -1829 386 62 A C ATOM 2366 CG ASP A 307 44.919 -4.747 11.616 1.00 80.74 A C ANISOU 2366 CG ASP A 307 12073 10402 8201 -1851 419 -45 A C ATOM 2367 OD1 ASP A 307 45.466 -4.031 10.740 1.00 86.99 A O ANISOU 2367 OD1 ASP A 307 12799 11172 9082 -1805 349 -98 A O ATOM 2368 OD2 ASP A 307 44.530 -4.289 12.704 1.00 79.50 A O1- ANISOU 2368 OD2 ASP A 307 12120 10242 7844 -1914 530 -82 A O1- ATOM 2369 N ASP A 308 46.109 -8.275 13.103 1.00 69.45 A N ANISOU 2369 N ASP A 308 10656 9024 6704 -2032 84 351 A N ATOM 2370 CA ASP A 308 46.720 -8.657 14.371 1.00 73.98 A C ANISOU 2370 CA ASP A 308 11414 9625 7068 -2153 -22 458 A C ATOM 2371 C ASP A 308 48.051 -9.364 14.143 1.00 66.28 A C ANISOU 2371 C ASP A 308 10358 8664 6159 -2145 -281 577 A C ATOM 2372 O ASP A 308 48.979 -9.244 14.941 1.00 71.94 A O ANISOU 2372 O ASP A 308 11192 9427 6713 -2234 -438 641 A O ATOM 2373 CB ASP A 308 45.778 -9.581 15.164 1.00 83.92 A C ANISOU 2373 CB ASP A 308 12752 10875 8257 -2202 107 546 A C ATOM 2374 CG ASP A 308 44.565 -8.847 15.687 1.00 92.79 A C ANISOU 2374 CG ASP A 308 13979 12017 9260 -2220 368 446 A C ATOM 2375 OD1 ASP A 308 44.736 -7.728 16.201 1.00 91.41 A O ANISOU 2375 OD1 ASP A 308 13963 11859 8910 -2255 405 349 A O ATOM 2376 OD2 ASP A 308 43.443 -9.402 15.640 1.00103.44 A O1- ANISOU 2376 OD2 ASP A 308 15257 13363 10680 -2205 540 469 A O1- ATOM 2377 N ALA A 309 48.117 -10.104 13.047 1.00 67.15 A N ANISOU 2377 N ALA A 309 10268 8740 6506 -2033 -323 604 A N ATOM 2378 CA ALA A 309 49.299 -10.866 12.734 1.00 71.53 A C ANISOU 2378 CA ALA A 309 10725 9303 7148 -1985 -540 716 A C ATOM 2379 C ALA A 309 50.428 -9.888 12.489 1.00 76.97 A C ANISOU 2379 C ALA A 309 11372 10064 7807 -2001 -674 675 A C ATOM 2380 O ALA A 309 51.545 -10.096 12.951 1.00 72.98 A O ANISOU 2380 O ALA A 309 10876 9617 7234 -2040 -868 777 A O ATOM 2381 CB ALA A 309 49.069 -11.738 11.499 1.00 66.78 A C ANISOU 2381 CB ALA A 309 9934 8638 6801 -1847 -530 718 A C ATOM 2382 N LEU A 310 50.124 -8.806 11.766 1.00 77.67 A N ANISOU 2382 N LEU A 310 11410 10152 7948 -1975 -573 533 A N ATOM 2383 CA LEU A 310 51.165 -7.825 11.460 1.00 71.57 A C ANISOU 2383 CA LEU A 310 10596 9437 7159 -2011 -690 496 A C ATOM 2384 C LEU A 310 51.667 -7.166 12.734 1.00 78.79 A C ANISOU 2384 C LEU A 310 11718 10396 7823 -2180 -775 508 A C ATOM 2385 O LEU A 310 52.821 -6.739 12.811 1.00 97.30 A O ANISOU 2385 O LEU A 310 14033 12810 10125 -2252 -951 542 A O ATOM 2386 CB LEU A 310 50.648 -6.795 10.470 1.00 67.55 A C ANISOU 2386 CB LEU A 310 10023 8895 6744 -1954 -554 352 A C ATOM 2387 CG LEU A 310 50.604 -7.348 9.038 1.00 59.97 A C ANISOU 2387 CG LEU A 310 8834 7925 6025 -1796 -543 349 A C ATOM 2388 CD1 LEU A 310 50.044 -6.290 8.105 1.00 59.80 A C ANISOU 2388 CD1 LEU A 310 8767 7876 6077 -1740 -413 219 A C ATOM 2389 CD2 LEU A 310 52.008 -7.767 8.631 1.00 59.09 A C ANISOU 2389 CD2 LEU A 310 8577 7884 5988 -1765 -740 445 A C ATOM 2390 N ASN A 311 50.799 -7.121 13.738 1.00 75.79 A N ANISOU 2390 N ASN A 311 11544 9984 7269 -2249 -651 484 A N ATOM 2391 CA ASN A 311 51.134 -6.487 15.002 1.00 73.73 A C ANISOU 2391 CA ASN A 311 11523 9756 6735 -2412 -711 475 A C ATOM 2392 C ASN A 311 51.913 -7.399 15.942 1.00 74.26 A C ANISOU 2392 C ASN A 311 11647 9890 6678 -2484 -909 645 A C ATOM 2393 O ASN A 311 52.554 -6.942 16.891 1.00 80.13 A O ANISOU 2393 O ASN A 311 12554 10690 7201 -2629 -1041 663 A O ATOM 2394 CB ASN A 311 49.860 -6.004 15.706 1.00 80.10 A C ANISOU 2394 CB ASN A 311 12539 10509 7383 -2442 -471 372 A C ATOM 2395 CG ASN A 311 50.178 -5.085 16.866 1.00 89.49 A C ANISOU 2395 CG ASN A 311 14007 11715 8279 -2603 -510 313 A C ATOM 2396 ND2 ASN A 311 49.587 -5.342 18.034 1.00103.92 A N ANISOU 2396 ND2 ASN A 311 16050 13550 9883 -2669 -417 334 A N ATOM 2397 OD1 ASN A 311 50.916 -4.117 16.697 1.00111.24 A O ANISOU 2397 OD1 ASN A 311 16793 14471 11001 -2677 -614 242 A O ATOM 2398 N HIS A 312 51.861 -8.699 15.660 1.00 74.33 A N ANISOU 2398 N HIS A 312 11529 9884 6827 -2382 -940 771 A N ATOM 2399 CA HIS A 312 52.516 -9.726 16.463 1.00 78.10 A C ANISOU 2399 CA HIS A 312 12051 10405 7218 -2412 -1120 956 A C ATOM 2400 C HIS A 312 53.990 -9.435 16.727 1.00 84.76 A C ANISOU 2400 C HIS A 312 12851 11360 7991 -2482 -1392 1032 A C ATOM 2401 O HIS A 312 54.694 -8.908 15.860 1.00 89.71 A O ANISOU 2401 O HIS A 312 13299 12030 8756 -2449 -1467 987 A O ATOM 2402 CB HIS A 312 52.374 -11.090 15.780 1.00 84.51 A C ANISOU 2402 CB HIS A 312 12700 11154 8254 -2259 -1122 1063 A C ATOM 2403 CG HIS A 312 52.779 -12.240 16.648 1.00100.07 A C ANISOU 2403 CG HIS A 312 14754 13129 10138 -2270 -1264 1261 A C ATOM 2404 CD2 HIS A 312 52.035 -13.151 17.326 1.00 90.28 A C ANISOU 2404 CD2 HIS A 312 13652 11820 8828 -2291 -1183 1359 A C ATOM 2405 ND1 HIS A 312 54.096 -12.571 16.878 1.00 93.30 A N ANISOU 2405 ND1 HIS A 312 13830 12354 9264 -2257 -1522 1399 A N ATOM 2406 CE1 HIS A 312 54.152 -13.610 17.681 1.00 93.78 A C ANISOU 2406 CE1 HIS A 312 14000 12390 9240 -2257 -1602 1572 A C ATOM 2407 NE2 HIS A 312 52.911 -13.994 17.957 1.00 89.56 A N ANISOU 2407 NE2 HIS A 312 13598 11756 8672 -2284 -1396 1552 A N ATOM 2408 N ASP A 313 54.459 -9.795 17.922 1.00 87.43 A N ANISOU 2408 N ASP A 313 13343 11760 8114 -2584 -1545 1158 A N ATOM 2409 CA ASP A 313 55.817 -9.441 18.348 1.00 85.89 A C ANISOU 2409 CA ASP A 313 13121 11696 7815 -2685 -1820 1234 A C ATOM 2410 C ASP A 313 56.900 -9.993 17.418 1.00 83.96 A C ANISOU 2410 C ASP A 313 12568 11517 7815 -2550 -1992 1342 A C ATOM 2411 O ASP A 313 58.027 -9.480 17.379 1.00 88.05 A O ANISOU 2411 O ASP A 313 12975 12159 8321 -2620 -2191 1373 A O ATOM 2412 CB ASP A 313 56.056 -9.851 19.789 1.00 93.79 A C ANISOU 2412 CB ASP A 313 14343 12756 8534 -2804 -1960 1367 A C ATOM 2413 CG ASP A 313 55.390 -8.903 20.787 1.00103.94 A C ANISOU 2413 CG ASP A 313 15947 14028 9517 -2982 -1843 1236 A C ATOM 2414 OD1 ASP A 313 55.156 -7.723 20.450 1.00116.39 A O ANISOU 2414 OD1 ASP A 313 17563 15574 11083 -3042 -1739 1050 A O ATOM 2415 OD2 ASP A 313 55.128 -9.331 21.927 1.00115.15 A O1- ANISOU 2415 OD2 ASP A 313 17591 15463 10697 -3057 -1857 1321 A O1- ATOM 2416 N PHE A 314 56.550 -11.027 16.665 1.00 83.88 A N ANISOU 2416 N PHE A 314 12420 11425 8025 -2361 -1911 1394 A N ATOM 2417 CA PHE A 314 57.426 -11.585 15.648 1.00 87.74 A C ANISOU 2417 CA PHE A 314 12623 11953 8758 -2193 -2020 1470 A C ATOM 2418 C PHE A 314 57.985 -10.520 14.696 1.00 87.78 A C ANISOU 2418 C PHE A 314 12444 12031 8874 -2208 -2025 1356 A C ATOM 2419 O PHE A 314 59.124 -10.623 14.251 1.00 97.63 A O ANISOU 2419 O PHE A 314 13472 13394 10228 -2151 -2187 1441 A O ATOM 2420 CB PHE A 314 56.672 -12.687 14.873 1.00 83.80 A C ANISOU 2420 CB PHE A 314 12059 11311 8469 -2001 -1872 1481 A C ATOM 2421 CG PHE A 314 57.448 -13.274 13.715 1.00 92.19 A C ANISOU 2421 CG PHE A 314 12851 12391 9785 -1801 -1942 1528 A C ATOM 2422 CD1 PHE A 314 58.552 -14.094 13.934 1.00101.83 A C ANISOU 2422 CD1 PHE A 314 13962 13682 11044 -1700 -2153 1713 A C ATOM 2423 CD2 PHE A 314 57.068 -13.011 12.408 1.00 94.84 A C ANISOU 2423 CD2 PHE A 314 13044 12677 10313 -1699 -1792 1392 A C ATOM 2424 CE1 PHE A 314 59.267 -14.621 12.884 1.00 99.50 A C ANISOU 2424 CE1 PHE A 314 13422 13408 10973 -1495 -2196 1751 A C ATOM 2425 CE2 PHE A 314 57.784 -13.531 11.342 1.00 94.12 A C ANISOU 2425 CE2 PHE A 314 12720 12608 10431 -1509 -1840 1426 A C ATOM 2426 CZ PHE A 314 58.877 -14.341 11.580 1.00102.17 A C ANISOU 2426 CZ PHE A 314 13634 13696 11488 -1402 -2032 1601 A C ATOM 2427 N PHE A 315 57.184 -9.501 14.382 1.00 82.57 A N ANISOU 2427 N PHE A 315 11871 11308 8190 -2281 -1841 1175 A N ATOM 2428 CA PHE A 315 57.621 -8.464 13.456 1.00 86.63 A C ANISOU 2428 CA PHE A 315 12239 11868 8805 -2302 -1827 1071 A C ATOM 2429 C PHE A 315 58.227 -7.261 14.175 1.00 92.50 A C ANISOU 2429 C PHE A 315 13098 12695 9353 -2533 -1949 1031 A C ATOM 2430 O PHE A 315 58.688 -6.315 13.531 1.00 95.87 A O ANISOU 2430 O PHE A 315 13426 13158 9840 -2592 -1959 959 A O ATOM 2431 CB PHE A 315 56.467 -8.019 12.557 1.00 81.85 A C ANISOU 2431 CB PHE A 315 11647 11140 8310 -2228 -1572 905 A C ATOM 2432 CG PHE A 315 55.846 -9.133 11.789 1.00 73.58 A C ANISOU 2432 CG PHE A 315 10494 10010 7453 -2030 -1463 927 A C ATOM 2433 CD1 PHE A 315 56.464 -9.635 10.659 1.00 70.90 A C ANISOU 2433 CD1 PHE A 315 9910 9704 7326 -1869 -1505 966 A C ATOM 2434 CD2 PHE A 315 54.625 -9.652 12.178 1.00 79.51 A C ANISOU 2434 CD2 PHE A 315 11393 10651 8165 -2012 -1309 900 A C ATOM 2435 CE1 PHE A 315 55.886 -10.679 9.937 1.00 74.76 A C ANISOU 2435 CE1 PHE A 315 10328 10098 7979 -1694 -1412 970 A C ATOM 2436 CE2 PHE A 315 54.017 -10.678 11.451 1.00 67.30 A C ANISOU 2436 CE2 PHE A 315 9757 9017 6796 -1856 -1218 913 A C ATOM 2437 CZ PHE A 315 54.664 -11.195 10.342 1.00 68.55 A C ANISOU 2437 CZ PHE A 315 9698 9192 7156 -1700 -1278 943 A C ATOM 2438 N TRP A 316 58.254 -7.325 15.504 1.00 98.19 A N ANISOU 2438 N TRP A 316 14035 13441 9830 -2671 -2048 1083 A N ATOM 2439 CA TRP A 316 58.666 -6.163 16.283 1.00 94.41 A C ANISOU 2439 CA TRP A 316 13729 13014 9128 -2911 -2152 1016 A C ATOM 2440 C TRP A 316 59.733 -6.462 17.334 1.00 90.12 A C ANISOU 2440 C TRP A 316 13209 12621 8411 -3041 -2445 1173 A C ATOM 2441 O TRP A 316 59.922 -5.712 18.280 1.00105.85 A O ANISOU 2441 O TRP A 316 15417 14645 10154 -3256 -2542 1127 A O ATOM 2442 CB TRP A 316 57.422 -5.503 16.884 1.00 90.76 A C ANISOU 2442 CB TRP A 316 13584 12418 8482 -2988 -1938 854 A C ATOM 2443 CG TRP A 316 56.464 -5.054 15.797 1.00 87.68 A C ANISOU 2443 CG TRP A 316 13141 11902 8268 -2865 -1676 704 A C ATOM 2444 CD1 TRP A 316 55.287 -5.649 15.438 1.00 83.27 A C ANISOU 2444 CD1 TRP A 316 12583 11244 7809 -2707 -1455 671 A C ATOM 2445 CD2 TRP A 316 56.627 -3.933 14.916 1.00 85.64 A C ANISOU 2445 CD2 TRP A 316 12815 11614 8111 -2895 -1625 585 A C ATOM 2446 CE2 TRP A 316 55.517 -3.913 14.060 1.00 80.99 A C ANISOU 2446 CE2 TRP A 316 12189 10911 7672 -2735 -1376 486 A C ATOM 2447 CE3 TRP A 316 57.600 -2.931 14.782 1.00 95.92 A C ANISOU 2447 CE3 TRP A 316 14087 12972 9386 -3056 -1770 559 A C ATOM 2448 NE1 TRP A 316 54.716 -4.972 14.404 1.00 79.05 A N ANISOU 2448 NE1 TRP A 316 11978 10633 7425 -2629 -1282 538 A N ATOM 2449 CZ2 TRP A 316 55.347 -2.929 13.070 1.00 84.33 A C ANISOU 2449 CZ2 TRP A 316 12556 11271 8212 -2710 -1269 368 A C ATOM 2450 CZ3 TRP A 316 57.422 -1.955 13.794 1.00 86.42 A C ANISOU 2450 CZ3 TRP A 316 12836 11693 8305 -3044 -1650 441 A C ATOM 2451 CH2 TRP A 316 56.304 -1.955 12.971 1.00 75.26 A C ANISOU 2451 CH2 TRP A 316 11401 10163 7029 -2865 -1403 349 A C ATOM 2452 N SER A 317 60.462 -7.544 17.115 1.00 87.85 A N ANISOU 2452 N SER A 317 12694 12426 8259 -2901 -2592 1356 A N ATOM 2453 CA SER A 317 61.570 -7.922 17.969 1.00 95.34 A C ANISOU 2453 CA SER A 317 13600 13540 9083 -2985 -2892 1535 A C ATOM 2454 C SER A 317 62.793 -8.227 17.109 1.00 99.81 A C ANISOU 2454 C SER A 317 13784 14255 9882 -2876 -3051 1659 A C ATOM 2455 O SER A 317 62.677 -8.321 15.877 1.00 90.79 A O ANISOU 2455 O SER A 317 12439 13068 8986 -2713 -2907 1611 A O ATOM 2456 CB SER A 317 61.193 -9.117 18.845 1.00 97.05 A C ANISOU 2456 CB SER A 317 13961 13722 9190 -2901 -2920 1677 A C ATOM 2457 OG SER A 317 60.778 -10.222 18.067 1.00104.02 A O ANISOU 2457 OG SER A 317 14703 14508 10308 -2646 -2791 1735 A O ATOM 2458 N ASP A 318 63.957 -8.384 17.741 1.00106.63 A N ANISOU 2458 N ASP A 318 14543 15308 10663 -2960 -3345 1823 A N ATOM 2459 CA ASP A 318 65.195 -8.652 17.026 1.00105.73 A C ANISOU 2459 CA ASP A 318 14044 15372 10757 -2861 -3506 1959 A C ATOM 2460 C ASP A 318 65.272 -10.103 16.576 1.00102.05 A C ANISOU 2460 C ASP A 318 13404 14882 10487 -2542 -3485 2109 A C ATOM 2461 O ASP A 318 64.760 -10.985 17.253 1.00101.58 A O ANISOU 2461 O ASP A 318 13524 14731 10340 -2462 -3480 2186 A O ATOM 2462 CB ASP A 318 66.400 -8.328 17.906 1.00111.42 A C ANISOU 2462 CB ASP A 318 14695 16320 11317 -3064 -3842 2093 A C ATOM 2463 CG ASP A 318 66.588 -6.837 18.105 1.00126.54 A C ANISOU 2463 CG ASP A 318 16717 18271 13089 -3386 -3890 1946 A C ATOM 2464 OD1 ASP A 318 66.002 -6.038 17.332 1.00125.27 A O ANISOU 2464 OD1 ASP A 318 16603 17982 13011 -3415 -3669 1763 A O ATOM 2465 OD2 ASP A 318 67.321 -6.480 19.035 1.00153.51 A O1- ANISOU 2465 OD2 ASP A 318 20181 21838 16307 -3609 -4157 2018 A O1- ATOM 2466 N PRO A 319 65.910 -10.344 15.420 1.00104.52 A N ANISOU 2466 N PRO A 319 13381 15268 11063 -2361 -3462 2149 A N ATOM 2467 CA PRO A 319 66.374 -9.290 14.515 1.00104.83 A C ANISOU 2467 CA PRO A 319 13223 15394 11211 -2456 -3419 2051 A C ATOM 2468 C PRO A 319 65.193 -8.730 13.758 1.00 96.24 A C ANISOU 2468 C PRO A 319 12286 14104 10176 -2448 -3121 1831 A C ATOM 2469 O PRO A 319 64.371 -9.511 13.274 1.00102.51 A O ANISOU 2469 O PRO A 319 13127 14742 11078 -2238 -2939 1795 A O ATOM 2470 CB PRO A 319 67.268 -10.066 13.526 1.00107.06 A C ANISOU 2470 CB PRO A 319 13118 15799 11758 -2188 -3448 2183 A C ATOM 2471 CG PRO A 319 66.720 -11.439 13.534 1.00111.36 A C ANISOU 2471 CG PRO A 319 13738 16198 12375 -1916 -3372 2249 A C ATOM 2472 CD PRO A 319 66.349 -11.680 14.973 1.00107.95 A C ANISOU 2472 CD PRO A 319 13602 15720 11692 -2050 -3497 2312 A C ATOM 2473 N MET A 320 65.084 -7.412 13.648 1.00 94.28 A N ANISOU 2473 N MET A 320 12120 13848 9855 -2672 -3075 1690 A N ATOM 2474 CA MET A 320 63.981 -6.815 12.901 1.00 90.87 A C ANISOU 2474 CA MET A 320 11820 13229 9476 -2651 -2799 1491 A C ATOM 2475 C MET A 320 64.006 -7.266 11.444 1.00 87.88 A C ANISOU 2475 C MET A 320 11182 12839 9367 -2402 -2649 1486 A C ATOM 2476 O MET A 320 65.061 -7.649 10.933 1.00 94.05 A O ANISOU 2476 O MET A 320 11662 13783 10288 -2302 -2756 1612 A O ATOM 2477 CB MET A 320 64.032 -5.296 12.994 1.00 83.17 A C ANISOU 2477 CB MET A 320 10964 12247 8388 -2924 -2797 1360 A C ATOM 2478 CG MET A 320 63.714 -4.768 14.366 1.00 84.31 A C ANISOU 2478 CG MET A 320 11443 12347 8241 -3159 -2883 1307 A C ATOM 2479 SD MET A 320 61.955 -4.896 14.740 1.00 92.74 A S ANISOU 2479 SD MET A 320 12870 13165 9199 -3082 -2606 1149 A S ATOM 2480 CE MET A 320 61.285 -3.688 13.611 1.00 81.35 A C ANISOU 2480 CE MET A 320 11453 11582 7870 -3091 -2361 946 A C ATOM 2481 N PRO A 321 62.833 -7.231 10.772 1.00 82.67 A N ANISOU 2481 N PRO A 321 10638 11998 8775 -2297 -2400 1340 A N ATOM 2482 CA PRO A 321 62.705 -7.725 9.383 1.00 80.11 A C ANISOU 2482 CA PRO A 321 10111 11643 8681 -2055 -2248 1318 A C ATOM 2483 C PRO A 321 63.657 -6.980 8.453 1.00 80.74 A C ANISOU 2483 C PRO A 321 9935 11868 8872 -2092 -2272 1330 A C ATOM 2484 O PRO A 321 63.813 -5.777 8.604 1.00 90.68 A O ANISOU 2484 O PRO A 321 11260 13150 10045 -2318 -2294 1268 A O ATOM 2485 CB PRO A 321 61.257 -7.410 9.029 1.00 81.18 A C ANISOU 2485 CB PRO A 321 10455 11579 8811 -2032 -2009 1143 A C ATOM 2486 CG PRO A 321 60.544 -7.306 10.359 1.00 85.40 A C ANISOU 2486 CG PRO A 321 11289 12026 9129 -2178 -2023 1113 A C ATOM 2487 CD PRO A 321 61.549 -6.760 11.326 1.00 84.49 A C ANISOU 2487 CD PRO A 321 11193 12051 8854 -2394 -2251 1194 A C ATOM 2488 N SER A 322 64.285 -7.678 7.511 1.00 86.82 A N ANISOU 2488 N SER A 322 10429 12729 9827 -1877 -2259 1409 A N ATOM 2489 CA SER A 322 65.255 -7.034 6.627 1.00 91.42 A C ANISOU 2489 CA SER A 322 10743 13477 10513 -1907 -2271 1443 A C ATOM 2490 C SER A 322 64.965 -7.321 5.153 1.00 99.18 A C ANISOU 2490 C SER A 322 11595 14416 11670 -1676 -2068 1378 A C ATOM 2491 O SER A 322 64.289 -8.287 4.826 1.00 91.58 A O ANISOU 2491 O SER A 322 10689 13332 10775 -1459 -1967 1343 A O ATOM 2492 CB SER A 322 66.686 -7.449 6.980 1.00 89.17 A C ANISOU 2492 CB SER A 322 10182 13433 10263 -1899 -2493 1638 A C ATOM 2493 OG SER A 322 66.932 -8.836 6.687 1.00102.81 A O ANISOU 2493 OG SER A 322 11764 15180 12119 -1591 -2495 1737 A O ATOM 2494 N ASP A 323 65.578 -6.530 4.281 1.00100.96 A N ANISOU 2494 N ASP A 323 11636 14758 11965 -1731 -2024 1378 A N ATOM 2495 CA ASP A 323 65.515 -6.708 2.841 1.00106.41 A C ANISOU 2495 CA ASP A 323 12176 15453 12800 -1528 -1847 1335 A C ATOM 2496 C ASP A 323 66.055 -8.042 2.326 1.00101.02 A C ANISOU 2496 C ASP A 323 11280 14847 12253 -1222 -1845 1425 A C ATOM 2497 O ASP A 323 66.812 -8.737 3.014 1.00 97.16 A O ANISOU 2497 O ASP A 323 10677 14466 11772 -1169 -2006 1564 A O ATOM 2498 CB ASP A 323 66.265 -5.559 2.148 1.00122.34 A C ANISOU 2498 CB ASP A 323 14022 17613 14845 -1682 -1825 1356 A C ATOM 2499 CG ASP A 323 65.474 -4.274 2.145 1.00144.14 A C ANISOU 2499 CG ASP A 323 17024 20229 17513 -1898 -1740 1224 A C ATOM 2500 OD1 ASP A 323 64.228 -4.344 2.010 1.00137.50 A O ANISOU 2500 OD1 ASP A 323 16408 19187 16645 -1822 -1606 1092 A O ATOM 2501 OD2 ASP A 323 66.096 -3.198 2.276 1.00146.90 A O1- ANISOU 2501 OD2 ASP A 323 17334 20662 17818 -2145 -1809 1256 A O1- ATOM 2502 N LEU A 324 65.647 -8.395 1.105 1.00 92.89 A N ANISOU 2502 N LEU A 324 10213 13757 11324 -1012 -1663 1345 A N ATOM 2503 CA LEU A 324 66.014 -9.690 0.528 1.00 84.55 A C ANISOU 2503 CA LEU A 324 9007 12727 10389 -696 -1631 1396 A C ATOM 2504 C LEU A 324 67.275 -9.599 -0.322 1.00108.07 A C ANISOU 2504 C LEU A 324 11645 15946 13467 -595 -1613 1495 A C ATOM 2505 O LEU A 324 67.256 -9.626 -1.549 1.00104.06 A O ANISOU 2505 O LEU A 324 11050 15457 13028 -445 -1449 1436 A O ATOM 2506 CB LEU A 324 64.853 -10.304 -0.195 1.00 80.48 A C ANISOU 2506 CB LEU A 324 8666 12002 9911 -520 -1466 1251 A C ATOM 2507 CG LEU A 324 63.613 -10.411 0.697 1.00 87.46 A C ANISOU 2507 CG LEU A 324 9856 12672 10702 -630 -1478 1171 A C ATOM 2508 CD1 LEU A 324 62.620 -11.423 0.140 1.00 88.33 A C ANISOU 2508 CD1 LEU A 324 10100 12588 10872 -428 -1361 1070 A C ATOM 2509 CD2 LEU A 324 63.959 -10.764 2.129 1.00 83.58 A C ANISOU 2509 CD2 LEU A 324 9421 12200 10135 -724 -1665 1290 A C ATOM 2510 N LYS A 325 68.409 -9.466 0.355 1.00142.63 A N ANISOU 2510 N LYS A 325 15818 20530 17843 -688 -1786 1655 A N ATOM 2511 CA LYS A 325 69.611 -9.112 -0.393 1.00154.13 A C ANISOU 2511 CA LYS A 325 16927 22248 19384 -660 -1764 1758 A C ATOM 2512 C LYS A 325 70.364 -10.353 -0.831 1.00150.36 A C ANISOU 2512 C LYS A 325 16216 21879 19034 -309 -1748 1855 A C ATOM 2513 O LYS A 325 70.531 -11.311 -0.053 1.00139.97 A O ANISOU 2513 O LYS A 325 14915 20533 17732 -178 -1878 1938 A O ATOM 2514 CB LYS A 325 70.494 -8.146 0.404 1.00164.02 A C ANISOU 2514 CB LYS A 325 18042 23699 20578 -975 -1950 1879 A C ATOM 2515 CG LYS A 325 69.880 -6.786 0.627 1.00174.32 A C ANISOU 2515 CG LYS A 325 19567 24900 21766 -1312 -1936 1775 A C ATOM 2516 CD LYS A 325 70.844 -5.634 0.355 1.00179.36 A C ANISOU 2516 CD LYS A 325 19984 25753 22412 -1563 -1975 1858 A C ATOM 2517 CE LYS A 325 70.089 -4.321 0.113 1.00166.98 A C ANISOU 2517 CE LYS A 325 18659 24027 20758 -1817 -1878 1725 A C ATOM 2518 NZ LYS A 325 70.854 -3.362 -0.750 1.00164.94 A N1+ ANISOU 2518 NZ LYS A 325 18184 23935 20548 -1963 -1809 1786 A N1+ ATOM 2519 N GLY A 326 70.756 -10.353 -2.107 1.00156.61 A N ANISOU 2519 N GLY A 326 16817 22777 19910 -141 -1574 1839 A N ATOM 2520 CA GLY A 326 71.384 -11.499 -2.745 1.00155.00 A C ANISOU 2520 CA GLY A 326 16414 22655 19824 232 -1502 1897 A C ATOM 2521 C GLY A 326 70.323 -12.511 -3.084 1.00162.41 A C ANISOU 2521 C GLY A 326 17629 23307 20772 468 -1397 1750 A C ATOM 2522 O GLY A 326 69.108 -12.201 -3.032 1.00166.90 A O ANISOU 2522 O GLY A 326 18498 23651 21263 335 -1349 1602 A O ATOM 2523 N MET A 327 70.774 -13.724 -3.407 1.00163.67 A N ANISOU 2523 N MET A 327 17689 23470 21028 817 -1364 1793 A N ATOM 2524 CA MET A 327 69.867 -14.815 -3.747 1.00158.41 A C ANISOU 2524 CA MET A 327 17283 22523 20381 1052 -1275 1661 A C ATOM 2525 C MET A 327 69.030 -14.379 -4.930 1.00148.92 A C ANISOU 2525 C MET A 327 16218 21220 19142 1039 -1072 1473 A C ATOM 2526 O MET A 327 68.889 -15.124 -5.888 1.00139.45 A O ANISOU 2526 O MET A 327 15054 19942 17985 1307 -931 1381 A O ATOM 2527 CB MET A 327 68.922 -15.130 -2.581 1.00150.72 A C ANISOU 2527 CB MET A 327 16614 21310 19342 913 -1410 1636 A C ATOM 2528 CG MET A 327 69.396 -14.591 -1.238 1.00123.20 A C ANISOU 2528 CG MET A 327 13066 17949 15794 662 -1629 1786 A C ATOM 2529 SD MET A 327 67.997 -14.227 -0.141 1.00134.51 A S ANISOU 2529 SD MET A 327 14891 19131 17085 364 -1705 1692 A S ATOM 2530 CE MET A 327 66.756 -15.449 -0.608 1.00 97.42 A C ANISOU 2530 CE MET A 327 10489 14099 12427 588 -1575 1542 A C TER CONECT 1364 1374 1374 CONECT 1374 1364 1364 1375 CONECT 1375 1374 1376 1378 CONECT 1376 1375 1377 1385 CONECT 1377 1376 CONECT 1378 1375 1379 1380 CONECT 1379 1378 CONECT 1380 1378 1381 CONECT 1381 1380 1382 1383 1384 CONECT 1382 1381 CONECT 1383 1381 CONECT 1384 1381 CONECT 1385 1376 END If you find results from this site helpful for your research, please cite one of our papers:
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