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*** 3BLH_A_VS_3MY1_A ***elNémo ID: 22051216131673072Job options:ID = 22051216131673072 JOBID = 3BLH_A_VS_3MY1_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_3MY1_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 173.789 173.789 99.221 90.00 90.00 120.00 H 3 9 ATOM 1 N ASP A 6 37.101 -7.026 -44.024 1.00160.02 A N ANISOU 1 N ASP A 6 20300 24161 16340 -292 -219 -1279 A N ATOM 2 CA ASP A 6 37.871 -5.861 -43.587 1.00162.47 A C ANISOU 2 CA ASP A 6 20616 24452 16663 -277 -103 -1089 A C ATOM 3 C ASP A 6 38.163 -5.852 -42.080 1.00157.43 A C ANISOU 3 C ASP A 6 19893 23595 16328 -214 -61 -1036 A C ATOM 4 O ASP A 6 38.091 -6.892 -41.418 1.00156.50 A O ANISOU 4 O ASP A 6 19715 23344 16403 -175 -82 -1178 A O ATOM 5 CB ASP A 6 37.223 -4.538 -44.046 1.00167.11 A C ANISOU 5 CB ASP A 6 21266 25139 17089 -304 -173 -832 A C ATOM 6 CG ASP A 6 35.724 -4.467 -43.759 1.00170.32 A C ANISOU 6 CG ASP A 6 21649 25485 17579 -291 -372 -724 A C ATOM 7 OD1 ASP A 6 35.174 -5.401 -43.136 1.00173.13 A O ANISOU 7 OD1 ASP A 6 21943 25713 18126 -266 -450 -843 A O ATOM 8 OD2 ASP A 6 35.093 -3.464 -44.165 1.00168.42 A O1- ANISOU 8 OD2 ASP A 6 21452 25322 17219 -305 -446 -515 A O1- ATOM 9 N SER A 7 38.484 -4.672 -41.551 1.00150.45 A N ANISOU 9 N SER A 7 19007 22678 15480 -207 3 -830 A N ATOM 10 CA SER A 7 39.068 -4.550 -40.213 1.00143.16 A C ANISOU 10 CA SER A 7 18010 21585 14799 -162 79 -789 A C ATOM 11 C SER A 7 38.234 -3.663 -39.277 1.00138.59 A C ANISOU 11 C SER A 7 17412 20882 14363 -152 7 -563 A C ATOM 12 O SER A 7 37.574 -2.722 -39.725 1.00142.94 A O ANISOU 12 O SER A 7 18010 21499 14803 -180 -45 -388 A O ATOM 13 CB SER A 7 40.497 -3.996 -40.335 1.00137.60 A C ANISOU 13 CB SER A 7 17305 20946 14030 -173 266 -790 A C ATOM 14 OG SER A 7 41.337 -4.451 -39.288 1.00131.91 A O ANISOU 14 OG SER A 7 16499 20099 13520 -126 344 -870 A O ATOM 15 N VAL A 8 38.271 -3.964 -37.980 1.00126.82 A N ANISOU 15 N VAL A 8 15855 19212 13120 -112 8 -565 A N ATOM 16 CA VAL A 8 37.551 -3.163 -36.985 1.00117.60 A C ANISOU 16 CA VAL A 8 14666 17912 12106 -110 -38 -369 A C ATOM 17 C VAL A 8 38.509 -2.332 -36.126 1.00109.44 A C ANISOU 17 C VAL A 8 13600 16823 11160 -111 99 -271 A C ATOM 18 O VAL A 8 39.556 -2.827 -35.694 1.00101.05 A O ANISOU 18 O VAL A 8 12493 15737 10165 -86 188 -388 A O ATOM 19 CB VAL A 8 36.701 -4.044 -36.038 1.00107.56 A C ANISOU 19 CB VAL A 8 13350 16463 11056 -77 -146 -426 A C ATOM 20 CG1 VAL A 8 35.866 -3.170 -35.122 1.00 99.18 A C ANISOU 20 CG1 VAL A 8 12274 15273 10138 -87 -189 -226 A C ATOM 21 CG2 VAL A 8 35.820 -4.988 -36.829 1.00104.02 A C ANISOU 21 CG2 VAL A 8 12920 16061 10542 -80 -271 -557 A C ATOM 22 N GLU A 9 38.143 -1.075 -35.875 1.00106.21 A N ANISOU 22 N GLU A 9 13205 16393 10757 -141 116 -62 A N ATOM 23 CA GLU A 9 38.954 -0.188 -35.039 1.00104.90 A C ANISOU 23 CA GLU A 9 13006 16173 10677 -156 249 35 A C ATOM 24 C GLU A 9 39.141 -0.804 -33.657 1.00 92.66 A C ANISOU 24 C GLU A 9 11388 14463 9357 -125 243 -28 A C ATOM 25 O GLU A 9 38.208 -1.410 -33.108 1.00 82.93 A O ANISOU 25 O GLU A 9 10144 13110 8254 -104 130 -42 A O ATOM 26 CB GLU A 9 38.297 1.196 -34.890 1.00114.47 A C ANISOU 26 CB GLU A 9 14242 17353 11898 -194 259 272 A C ATOM 27 CG GLU A 9 38.128 1.995 -36.183 1.00127.03 A C ANISOU 27 CG GLU A 9 15906 19096 13263 -222 273 380 A C ATOM 28 CD GLU A 9 39.399 2.708 -36.612 1.00137.19 A C ANISOU 28 CD GLU A 9 17213 20488 14424 -253 453 393 A C ATOM 29 OE1 GLU A 9 40.154 3.156 -35.723 1.00139.01 A O ANISOU 29 OE1 GLU A 9 17395 20647 14775 -268 572 410 A O ATOM 30 OE2 GLU A 9 39.639 2.826 -37.838 1.00139.77 A O1- ANISOU 30 OE2 GLU A 9 17606 20971 14528 -269 479 381 A O1- ATOM 31 N CYS A 10 40.333 -0.650 -33.084 1.00 86.91 A N ANISOU 31 N CYS A 10 10613 13731 8677 -124 364 -64 A N ATOM 32 CA CYS A 10 40.561 -1.205 -31.758 1.00 83.38 A C ANISOU 32 CA CYS A 10 10105 13144 8432 -93 353 -112 A C ATOM 33 C CYS A 10 41.618 -0.478 -30.948 1.00 91.36 A C ANISOU 33 C CYS A 10 11064 14146 9504 -116 479 -67 A C ATOM 34 O CYS A 10 42.689 -1.009 -30.676 1.00113.15 A O ANISOU 34 O CYS A 10 13767 16928 12296 -85 534 -185 A O ATOM 35 CB CYS A 10 40.852 -2.707 -31.830 1.00 73.95 A C ANISOU 35 CB CYS A 10 8886 11934 7278 -30 304 -312 A C ATOM 36 SG CYS A 10 40.482 -3.521 -30.288 1.00107.34 A S ANISOU 36 SG CYS A 10 13073 15959 11753 14 229 -332 A S ATOM 37 N PRO A 11 41.290 0.733 -30.524 1.00 83.67 A N ANISOU 37 N PRO A 11 10099 13133 8558 -172 525 102 A N ATOM 38 CA PRO A 11 42.146 1.678 -29.820 1.00 82.52 A C ANISOU 38 CA PRO A 11 9910 12986 8458 -218 655 165 A C ATOM 39 C PRO A 11 42.680 1.125 -28.511 1.00 82.51 A C ANISOU 39 C PRO A 11 9839 12895 8617 -195 648 97 A C ATOM 40 O PRO A 11 43.789 1.475 -28.122 1.00 78.04 A O ANISOU 40 O PRO A 11 9215 12375 8062 -213 751 67 A O ATOM 41 CB PRO A 11 41.190 2.831 -29.502 1.00 89.12 A C ANISOU 41 CB PRO A 11 10779 13743 9340 -276 662 359 A C ATOM 42 CG PRO A 11 40.076 2.679 -30.442 1.00 93.05 A C ANISOU 42 CG PRO A 11 11340 14261 9754 -259 556 404 A C ATOM 43 CD PRO A 11 39.908 1.216 -30.606 1.00 88.15 A C ANISOU 43 CD PRO A 11 10715 13635 9145 -195 441 242 A C ATOM 44 N PHE A 12 41.906 0.295 -27.821 1.00 78.91 A N ANISOU 44 N PHE A 12 9387 12313 8281 -159 530 76 A N ATOM 45 CA PHE A 12 42.274 -0.056 -26.453 1.00 65.67 A C ANISOU 45 CA PHE A 12 7659 10538 6754 -147 522 53 A C ATOM 46 C PHE A 12 42.595 -1.515 -26.230 1.00 63.75 A C ANISOU 46 C PHE A 12 7389 10262 6572 -61 446 -94 A C ATOM 47 O PHE A 12 42.594 -1.993 -25.102 1.00 65.57 A O ANISOU 47 O PHE A 12 7596 10387 6930 -40 404 -99 A O ATOM 48 CB PHE A 12 41.201 0.386 -25.481 1.00 70.25 A C ANISOU 48 CB PHE A 12 8265 10969 7455 -193 479 178 A C ATOM 49 CG PHE A 12 40.746 1.786 -25.699 1.00 82.32 A C ANISOU 49 CG PHE A 12 9821 12506 8950 -272 552 330 A C ATOM 50 CD1 PHE A 12 41.658 2.786 -25.938 1.00 81.30 A C ANISOU 50 CD1 PHE A 12 9667 12477 8747 -321 688 365 A C ATOM 51 CD2 PHE A 12 39.401 2.109 -25.654 1.00 86.99 A C ANISOU 51 CD2 PHE A 12 10458 12998 9598 -296 492 438 A C ATOM 52 CE1 PHE A 12 41.237 4.084 -26.136 1.00 80.71 A C ANISOU 52 CE1 PHE A 12 9619 12395 8653 -391 768 512 A C ATOM 53 CE2 PHE A 12 38.978 3.407 -25.848 1.00 85.06 A C ANISOU 53 CE2 PHE A 12 10232 12748 9339 -361 564 588 A C ATOM 54 CZ PHE A 12 39.896 4.392 -26.091 1.00 82.83 A C ANISOU 54 CZ PHE A 12 9932 12559 8981 -407 705 628 A C ATOM 55 N CYS A 13 42.887 -2.234 -27.299 1.00 70.62 A N ANISOU 55 N CYS A 13 8263 11219 7350 -13 437 -213 A N ATOM 56 CA CYS A 13 43.354 -3.604 -27.137 1.00 66.38 A C ANISOU 56 CA CYS A 13 7690 10650 6879 73 391 -363 A C ATOM 57 C CYS A 13 44.431 -3.847 -28.164 1.00 67.50 A C ANISOU 57 C CYS A 13 7798 10939 6911 99 470 -489 A C ATOM 58 O CYS A 13 44.134 -4.015 -29.349 1.00 72.02 A O ANISOU 58 O CYS A 13 8416 11587 7360 94 467 -542 A O ATOM 59 CB CYS A 13 42.205 -4.569 -27.337 1.00 64.40 A C ANISOU 59 CB CYS A 13 7492 10304 6673 108 276 -406 A C ATOM 60 SG CYS A 13 42.557 -6.237 -26.917 1.00 73.13 A S ANISOU 60 SG CYS A 13 8564 11320 7903 211 223 -562 A S ATOM 61 N ASP A 14 45.685 -3.824 -27.716 1.00 62.48 A N ANISOU 61 N ASP A 14 7079 10346 6313 120 542 -538 A N ATOM 62 CA ASP A 14 46.818 -3.989 -28.626 1.00 59.50 A C ANISOU 62 CA ASP A 14 6656 10104 5849 139 638 -664 A C ATOM 63 C ASP A 14 47.017 -5.465 -28.972 1.00 65.46 A C ANISOU 63 C ASP A 14 7390 10831 6652 229 595 -831 A C ATOM 64 O ASP A 14 46.669 -6.347 -28.162 1.00 65.72 A O ANISOU 64 O ASP A 14 7412 10735 6823 291 506 -847 A O ATOM 65 CB ASP A 14 48.075 -3.396 -28.012 1.00 66.60 A C ANISOU 65 CB ASP A 14 7459 11061 6786 125 733 -662 A C ATOM 66 CG ASP A 14 48.043 -1.881 -27.970 1.00 86.64 A C ANISOU 66 CG ASP A 14 10016 13650 9252 24 819 -526 A C ATOM 67 OD1 ASP A 14 47.148 -1.287 -28.626 1.00 92.91 A O ANISOU 67 OD1 ASP A 14 10900 14454 9949 -27 816 -437 A O ATOM 68 OD2 ASP A 14 48.917 -1.289 -27.283 1.00 87.51 A O1- ANISOU 68 OD2 ASP A 14 10049 13792 9409 -5 891 -510 A O1- ATOM 69 N GLU A 15 47.534 -5.733 -30.177 1.00 67.79 A N ANISOU 69 N GLU A 15 7684 11238 6834 233 665 -955 A N ATOM 70 CA GLU A 15 47.854 -7.110 -30.580 1.00 79.58 A C ANISOU 70 CA GLU A 15 9148 12709 8378 313 653 -1133 A C ATOM 71 C GLU A 15 49.091 -7.596 -29.813 1.00 75.13 A C ANISOU 71 C GLU A 15 8464 12124 7958 388 691 -1203 A C ATOM 72 O GLU A 15 50.077 -6.864 -29.699 1.00 71.42 A O ANISOU 72 O GLU A 15 7925 11742 7468 363 782 -1190 A O ATOM 73 CB GLU A 15 48.087 -7.229 -32.096 1.00 84.64 A C ANISOU 73 CB GLU A 15 9825 13482 8850 284 731 -1256 A C ATOM 74 CG GLU A 15 47.372 -6.179 -32.951 1.00 95.31 A C ANISOU 74 CG GLU A 15 11276 14930 10007 190 742 -1151 A C ATOM 75 CD GLU A 15 47.439 -6.479 -34.454 1.00108.97 A C ANISOU 75 CD GLU A 15 13061 16787 11557 162 797 -1278 A C ATOM 76 OE1 GLU A 15 48.516 -6.309 -35.062 1.00110.03 A O ANISOU 76 OE1 GLU A 15 13161 17029 11617 147 928 -1366 A O ATOM 77 OE2 GLU A 15 46.404 -6.874 -35.037 1.00118.12 A O1- ANISOU 77 OE2 GLU A 15 14296 17941 12643 147 710 -1294 A O1- ATOM 78 N VAL A 16 49.016 -8.815 -29.277 1.00 66.69 A N ANISOU 78 N VAL A 16 7366 10935 7039 480 621 -1273 A N ATOM 79 CA VAL A 16 50.072 -9.374 -28.438 1.00 67.54 A C ANISOU 79 CA VAL A 16 7357 11003 7301 568 629 -1319 A C ATOM 80 C VAL A 16 51.401 -9.527 -29.197 1.00 72.18 A C ANISOU 80 C VAL A 16 7851 11708 7865 593 753 -1467 A C ATOM 81 O VAL A 16 52.468 -9.678 -28.597 1.00 68.84 A O ANISOU 81 O VAL A 16 7310 11294 7551 651 779 -1496 A O ATOM 82 CB VAL A 16 49.687 -10.754 -27.888 1.00 62.26 A C ANISOU 82 CB VAL A 16 6688 10174 6792 670 540 -1370 A C ATOM 83 CG1 VAL A 16 49.829 -11.799 -28.980 1.00 58.96 A C ANISOU 83 CG1 VAL A 16 6270 9764 6369 713 589 -1557 A C ATOM 84 CG2 VAL A 16 50.580 -11.131 -26.725 1.00 60.65 A C ANISOU 84 CG2 VAL A 16 6377 9916 6751 758 515 -1349 A C ATOM 85 N SER A 17 51.340 -9.494 -30.518 1.00 70.82 A N ANISOU 85 N SER A 17 7729 11629 7552 546 830 -1563 A N ATOM 86 CA SER A 17 52.559 -9.528 -31.308 1.00 73.27 A C ANISOU 86 CA SER A 17 7961 12054 7826 551 968 -1705 A C ATOM 87 C SER A 17 53.528 -8.381 -30.947 1.00 70.86 A C ANISOU 87 C SER A 17 7576 11848 7500 505 1051 -1640 A C ATOM 88 O SER A 17 54.667 -8.372 -31.392 1.00 74.35 A O ANISOU 88 O SER A 17 7928 12377 7945 513 1169 -1754 A O ATOM 89 CB SER A 17 52.208 -9.466 -32.792 1.00 86.24 A C ANISOU 89 CB SER A 17 9696 13793 9277 481 1038 -1794 A C ATOM 90 OG SER A 17 51.589 -8.226 -33.123 1.00 94.38 A O ANISOU 90 OG SER A 17 10822 14903 10136 376 1042 -1654 A O ATOM 91 N LYS A 18 53.098 -7.411 -30.148 1.00 62.94 A N ANISOU 91 N LYS A 18 6600 10833 6483 451 1002 -1469 A N ATOM 92 CA LYS A 18 54.010 -6.334 -29.778 1.00 70.51 A C ANISOU 92 CA LYS A 18 7479 11882 7430 400 1089 -1420 A C ATOM 93 C LYS A 18 55.055 -6.843 -28.800 1.00 72.65 A C ANISOU 93 C LYS A 18 7596 12127 7880 488 1069 -1469 A C ATOM 94 O LYS A 18 56.079 -6.191 -28.579 1.00 64.95 A O ANISOU 94 O LYS A 18 6517 11240 6920 461 1152 -1483 A O ATOM 95 CB LYS A 18 53.269 -5.143 -29.176 1.00 65.16 A C ANISOU 95 CB LYS A 18 6869 11191 6698 311 1055 -1231 A C ATOM 96 CG LYS A 18 52.740 -5.389 -27.793 1.00 70.45 A C ANISOU 96 CG LYS A 18 7531 11735 7501 349 921 -1127 A C ATOM 97 CD LYS A 18 51.731 -4.324 -27.440 1.00 69.87 A C ANISOU 97 CD LYS A 18 7553 11632 7364 255 893 -955 A C ATOM 98 CE LYS A 18 52.171 -3.477 -26.284 1.00 63.86 A C ANISOU 98 CE LYS A 18 6726 10875 6663 210 906 -862 A C ATOM 99 NZ LYS A 18 51.012 -2.677 -25.862 1.00 74.28 A N1+ ANISOU 99 NZ LYS A 18 8144 12125 7953 132 866 -703 A N1+ ATOM 100 N TYR A 19 54.758 -8.000 -28.209 1.00 72.58 A N ANISOU 100 N TYR A 19 7575 11995 8009 591 956 -1488 A N ATOM 101 CA TYR A 19 55.668 -8.720 -27.335 1.00 71.62 A C ANISOU 101 CA TYR A 19 7313 11834 8065 699 915 -1533 A C ATOM 102 C TYR A 19 56.235 -9.909 -28.097 1.00 85.17 A C ANISOU 102 C TYR A 19 8972 13535 9856 792 966 -1714 A C ATOM 103 O TYR A 19 55.559 -10.472 -28.951 1.00 92.62 A O ANISOU 103 O TYR A 19 10007 14441 10742 789 976 -1782 A O ATOM 104 CB TYR A 19 54.927 -9.212 -26.099 1.00 71.23 A C ANISOU 104 CB TYR A 19 7298 11642 8125 755 760 -1415 A C ATOM 105 CG TYR A 19 54.354 -8.092 -25.261 1.00 76.54 A C ANISOU 105 CG TYR A 19 8025 12316 8741 661 715 -1244 A C ATOM 106 CD1 TYR A 19 55.170 -7.372 -24.394 1.00 72.13 A C ANISOU 106 CD1 TYR A 19 7365 11826 8216 636 725 -1193 A C ATOM 107 CD2 TYR A 19 53.001 -7.744 -25.335 1.00 74.10 A C ANISOU 107 CD2 TYR A 19 7861 11941 8352 592 668 -1143 A C ATOM 108 CE1 TYR A 19 54.667 -6.345 -23.625 1.00 69.60 A C ANISOU 108 CE1 TYR A 19 7092 11504 7849 540 699 -1050 A C ATOM 109 CE2 TYR A 19 52.488 -6.704 -24.564 1.00 71.52 A C ANISOU 109 CE2 TYR A 19 7579 11606 7990 503 642 -992 A C ATOM 110 CZ TYR A 19 53.334 -6.014 -23.714 1.00 75.18 A C ANISOU 110 CZ TYR A 19 7945 12134 8486 475 664 -950 A C ATOM 111 OH TYR A 19 52.877 -4.982 -22.944 1.00 78.33 A O ANISOU 111 OH TYR A 19 8382 12524 8855 378 654 -815 A O ATOM 112 N GLU A 20 57.476 -10.278 -27.791 1.00 88.67 A N ANISOU 112 N GLU A 20 9254 14007 10429 872 1001 -1797 A N ATOM 113 CA GLU A 20 58.157 -11.400 -28.433 1.00 87.27 A C ANISOU 113 CA GLU A 20 8996 13807 10355 967 1065 -1975 A C ATOM 114 C GLU A 20 58.233 -12.543 -27.433 1.00 78.98 A C ANISOU 114 C GLU A 20 7879 12616 9513 1113 945 -1954 A C ATOM 115 O GLU A 20 58.889 -12.416 -26.399 1.00 80.47 A O ANISOU 115 O GLU A 20 7955 12813 9806 1167 884 -1887 A O ATOM 116 CB GLU A 20 59.568 -10.961 -28.831 1.00100.32 A C ANISOU 116 CB GLU A 20 10500 15593 12024 955 1202 -2086 A C ATOM 117 CG GLU A 20 60.331 -11.891 -29.766 1.00112.73 A C ANISOU 117 CG GLU A 20 11991 17166 13673 1021 1317 -2293 A C ATOM 118 CD GLU A 20 61.647 -11.278 -30.258 1.00128.46 A C ANISOU 118 CD GLU A 20 13849 19300 15658 981 1475 -2404 A C ATOM 119 OE1 GLU A 20 61.929 -10.087 -29.952 1.00129.80 A O ANISOU 119 OE1 GLU A 20 13998 19571 15748 893 1501 -2321 A O ATOM 120 OE2 GLU A 20 62.398 -11.992 -30.960 1.00133.25 A O1- ANISOU 120 OE2 GLU A 20 14370 19911 16348 1033 1583 -2581 A O1- ATOM 121 N LYS A 21 57.548 -13.649 -27.708 1.00 75.37 A N ANISOU 121 N LYS A 21 7493 12030 9113 1176 910 -2007 A N ATOM 122 CA LYS A 21 57.566 -14.768 -26.757 1.00 82.40 A C ANISOU 122 CA LYS A 21 8334 12768 10205 1319 805 -1975 A C ATOM 123 C LYS A 21 59.002 -15.268 -26.510 1.00 92.01 A C ANISOU 123 C LYS A 21 9353 14008 11597 1437 842 -2060 A C ATOM 124 O LYS A 21 59.877 -15.150 -27.376 1.00 87.25 A O ANISOU 124 O LYS A 21 8663 13505 10985 1422 976 -2205 A O ATOM 125 CB LYS A 21 56.651 -15.913 -27.219 1.00 84.65 A C ANISOU 125 CB LYS A 21 8723 12907 10535 1362 791 -2045 A C ATOM 126 CG LYS A 21 55.150 -15.571 -27.273 1.00 87.53 A C ANISOU 126 CG LYS A 21 9269 13225 10765 1266 723 -1950 A C ATOM 127 CD LYS A 21 54.289 -16.815 -27.558 1.00 94.11 A C ANISOU 127 CD LYS A 21 10183 13898 11675 1319 700 -2025 A C ATOM 128 CE LYS A 21 52.772 -16.516 -27.529 1.00 93.80 A C ANISOU 128 CE LYS A 21 10309 13806 11524 1229 621 -1931 A C ATOM 129 NZ LYS A 21 52.233 -15.808 -28.745 1.00 88.31 A N1+ ANISOU 129 NZ LYS A 21 9703 13235 10617 1097 682 -1985 A N1+ ATOM 130 N LEU A 22 59.258 -15.814 -25.326 1.00101.56 A N ANISOU 130 N LEU A 22 10490 15130 12968 1555 726 -1968 A N ATOM 131 CA LEU A 22 60.602 -16.315 -25.020 1.00104.50 A C ANISOU 131 CA LEU A 22 10662 15522 13522 1681 741 -2034 A C ATOM 132 C LEU A 22 60.639 -17.757 -24.538 1.00117.58 A C ANISOU 132 C LEU A 22 12278 17000 15396 1854 676 -2039 A C ATOM 133 O LEU A 22 61.379 -18.574 -25.090 1.00126.39 A O ANISOU 133 O LEU A 22 13284 18082 16655 1948 763 -2184 A O ATOM 134 CB LEU A 22 61.306 -15.420 -24.013 1.00 92.34 A C ANISOU 134 CB LEU A 22 9014 14096 11977 1665 670 -1921 A C ATOM 135 CG LEU A 22 61.640 -14.077 -24.637 1.00 86.22 A C ANISOU 135 CG LEU A 22 8228 13500 11031 1512 781 -1960 A C ATOM 136 CD1 LEU A 22 62.572 -13.271 -23.746 1.00 82.65 A C ANISOU 136 CD1 LEU A 22 7629 13172 10602 1499 739 -1896 A C ATOM 137 CD2 LEU A 22 62.249 -14.319 -26.006 1.00 75.71 A C ANISOU 137 CD2 LEU A 22 6844 12221 9701 1502 956 -2165 A C ATOM 138 N ALA A 23 59.851 -18.070 -23.514 1.00112.93 A N ANISOU 138 N ALA A 23 11779 16291 14838 1894 536 -1881 A N ATOM 139 CA ALA A 23 59.884 -19.403 -22.928 1.00110.76 A C ANISOU 139 CA ALA A 23 11474 15838 14774 2063 470 -1857 A C ATOM 140 C ALA A 23 58.672 -19.675 -22.057 1.00109.90 A C ANISOU 140 C ALA A 23 11526 15584 14649 2064 346 -1698 A C ATOM 141 O ALA A 23 58.294 -18.837 -21.250 1.00107.88 A O ANISOU 141 O ALA A 23 11327 15380 14284 1988 255 -1548 A O ATOM 142 CB ALA A 23 61.147 -19.573 -22.113 1.00104.16 A C ANISOU 142 CB ALA A 23 10441 15044 14093 2192 409 -1815 A C ATOM 143 N LYS A 24 58.073 -20.851 -22.214 1.00110.50 A N ANISOU 143 N LYS A 24 11673 15473 14840 2143 356 -1737 A N ATOM 144 CA LYS A 24 57.031 -21.287 -21.300 1.00109.93 A C ANISOU 144 CA LYS A 24 11737 15238 14793 2167 246 -1590 A C ATOM 145 C LYS A 24 57.569 -21.262 -19.868 1.00106.16 A C ANISOU 145 C LYS A 24 11189 14754 14391 2261 109 -1412 A C ATOM 146 O LYS A 24 58.647 -21.781 -19.603 1.00108.02 A O ANISOU 146 O LYS A 24 11268 14993 14780 2398 97 -1426 A O ATOM 147 CB LYS A 24 56.548 -22.696 -21.655 1.00120.42 A C ANISOU 147 CB LYS A 24 13118 16357 16280 2263 294 -1677 A C ATOM 148 CG LYS A 24 55.827 -22.810 -22.999 1.00134.31 A C ANISOU 148 CG LYS A 24 14969 18110 17952 2161 413 -1851 A C ATOM 149 CD LYS A 24 54.667 -23.821 -22.923 1.00145.17 A C ANISOU 149 CD LYS A 24 16482 19269 19408 2186 404 -1856 A C ATOM 150 CE LYS A 24 53.908 -23.950 -24.250 1.00146.33 A C ANISOU 150 CE LYS A 24 16717 19423 19460 2077 510 -2036 A C ATOM 151 NZ LYS A 24 52.598 -24.654 -24.082 1.00142.33 A N1+ ANISOU 151 NZ LYS A 24 16357 18730 18992 2061 484 -2023 A N1+ ATOM 152 N ILE A 25 56.821 -20.648 -18.954 1.00104.26 A N ANISOU 152 N ILE A 25 11061 14511 14042 2183 6 -1246 A N ATOM 153 CA ILE A 25 57.199 -20.582 -17.542 1.00105.15 A C ANISOU 153 CA ILE A 25 11134 14624 14194 2251 -132 -1068 A C ATOM 154 C ILE A 25 56.029 -20.964 -16.640 1.00113.45 A C ANISOU 154 C ILE A 25 12359 15503 15243 2246 -218 -920 A C ATOM 155 O ILE A 25 56.170 -21.009 -15.415 1.00112.70 A O ANISOU 155 O ILE A 25 12266 15385 15169 2298 -336 -760 A O ATOM 156 CB ILE A 25 57.628 -19.164 -17.137 1.00 97.70 A C ANISOU 156 CB ILE A 25 10138 13891 13093 2131 -170 -1004 A C ATOM 157 CG1 ILE A 25 56.444 -18.205 -17.270 1.00 99.09 A C ANISOU 157 CG1 ILE A 25 10481 14088 13082 1947 -154 -961 A C ATOM 158 CG2 ILE A 25 58.781 -18.693 -17.986 1.00 95.83 A C ANISOU 158 CG2 ILE A 25 9730 13827 12852 2120 -76 -1149 A C ATOM 159 CD1 ILE A 25 56.622 -16.892 -16.545 1.00101.03 A C ANISOU 159 CD1 ILE A 25 10711 14489 13188 1828 -205 -858 A C ATOM 160 N GLY A 26 54.878 -21.232 -17.257 1.00127.11 A N ANISOU 160 N GLY A 26 14235 17118 16943 2180 -158 -979 A N ATOM 161 CA GLY A 26 53.623 -21.418 -16.540 1.00143.23 A C ANISOU 161 CA GLY A 26 16454 19006 18962 2138 -217 -859 A C ATOM 162 C GLY A 26 53.405 -22.827 -16.031 1.00160.46 A C ANISOU 162 C GLY A 26 18677 20959 21330 2289 -242 -818 A C ATOM 163 O GLY A 26 52.307 -23.387 -16.147 1.00154.10 A O ANISOU 163 O GLY A 26 18009 19985 20555 2265 -214 -831 A O ATOM 164 N GLN A 27 54.462 -23.373 -15.431 1.00180.79 A N ANISOU 164 N GLN A 27 21130 23529 24034 2444 -296 -761 A N ATOM 165 CA GLN A 27 54.557 -24.795 -15.106 1.00189.52 A C ANISOU 165 CA GLN A 27 22235 24424 25350 2620 -300 -737 A C ATOM 166 C GLN A 27 53.424 -25.351 -14.228 1.00195.43 A C ANISOU 166 C GLN A 27 23166 24962 26125 2624 -349 -602 A C ATOM 167 O GLN A 27 52.512 -24.624 -13.811 1.00190.13 A O ANISOU 167 O GLN A 27 22625 24306 25310 2485 -385 -524 A O ATOM 168 CB GLN A 27 55.954 -25.128 -14.558 1.00185.53 A C ANISOU 168 CB GLN A 27 21549 23976 24967 2786 -367 -678 A C ATOM 169 CG GLN A 27 57.055 -24.911 -15.601 1.00184.09 A C ANISOU 169 CG GLN A 27 21179 23947 24819 2807 -280 -853 A C ATOM 170 CD GLN A 27 58.447 -25.239 -15.092 1.00186.78 A C ANISOU 170 CD GLN A 27 21322 24347 25300 2973 -347 -804 A C ATOM 171 NE2 GLN A 27 59.318 -25.673 -15.995 1.00186.38 A N ANISOU 171 NE2 GLN A 27 21116 24318 25383 3055 -246 -968 A N ATOM 172 OE1 GLN A 27 58.738 -25.096 -13.905 1.00187.80 A O ANISOU 172 OE1 GLN A 27 21434 24506 25414 3025 -487 -625 A O ATOM 173 N GLY A 28 53.493 -26.653 -13.969 1.00202.76 A N ANISOU 173 N GLY A 28 24102 25687 27252 2784 -337 -580 A N ATOM 174 CA GLY A 28 52.333 -27.407 -13.535 1.00208.56 A C ANISOU 174 CA GLY A 28 25013 26183 28047 2787 -325 -519 A C ATOM 175 C GLY A 28 51.574 -27.786 -14.796 1.00214.36 A C ANISOU 175 C GLY A 28 25799 26837 28812 2718 -187 -725 A C ATOM 176 O GLY A 28 50.567 -28.499 -14.754 1.00212.71 A O ANISOU 176 O GLY A 28 25722 26424 28674 2709 -142 -737 A O ATOM 177 N THR A 29 52.092 -27.296 -15.923 1.00218.34 A N ANISOU 177 N THR A 29 26194 27508 29258 2665 -119 -892 A N ATOM 178 CA THR A 29 51.492 -27.472 -17.247 1.00216.91 A C ANISOU 178 CA THR A 29 26045 27308 29061 2579 6 -1103 A C ATOM 179 C THR A 29 50.157 -26.732 -17.368 1.00210.60 A C ANISOU 179 C THR A 29 25399 26527 28092 2395 -5 -1095 A C ATOM 180 O THR A 29 49.347 -27.041 -18.240 1.00211.44 A O ANISOU 180 O THR A 29 25571 26571 28195 2325 77 -1239 A O ATOM 181 CB THR A 29 51.346 -28.974 -17.628 1.00193.52 A C ANISOU 181 CB THR A 29 23093 24111 26324 2699 107 -1213 A C ATOM 182 CG2 THR A 29 50.856 -29.139 -19.065 1.00192.05 A C ANISOU 182 CG2 THR A 29 22922 23938 26110 2603 238 -1454 A C ATOM 183 OG1 THR A 29 52.616 -29.622 -17.499 1.00194.87 A O ANISOU 183 OG1 THR A 29 23110 24264 26667 2877 118 -1212 A O ATOM 184 N PHE A 30 49.932 -25.742 -16.505 1.00202.21 A N ANISOU 184 N PHE A 30 24386 25554 26890 2314 -104 -932 A N ATOM 185 CA PHE A 30 48.660 -25.018 -16.529 1.00192.89 A C ANISOU 185 CA PHE A 30 23343 24378 25568 2145 -116 -910 A C ATOM 186 C PHE A 30 48.747 -23.503 -16.681 1.00184.07 A C ANISOU 186 C PHE A 30 22202 23491 24243 2003 -149 -878 A C ATOM 187 O PHE A 30 49.669 -22.859 -16.182 1.00183.40 A O ANISOU 187 O PHE A 30 22028 23548 24107 2021 -203 -794 A O ATOM 188 CB PHE A 30 47.764 -25.410 -15.350 1.00191.46 A C ANISOU 188 CB PHE A 30 23305 24004 25438 2151 -172 -756 A C ATOM 189 CG PHE A 30 46.831 -26.544 -15.668 1.00192.46 A C ANISOU 189 CG PHE A 30 23526 23900 25701 2175 -98 -845 A C ATOM 190 CD1 PHE A 30 45.557 -26.294 -16.155 1.00188.97 A C ANISOU 190 CD1 PHE A 30 23189 23419 25192 2035 -64 -918 A C ATOM 191 CD2 PHE A 30 47.242 -27.863 -15.515 1.00195.08 A C ANISOU 191 CD2 PHE A 30 23833 24053 26235 2337 -57 -865 A C ATOM 192 CE1 PHE A 30 44.701 -27.336 -16.465 1.00189.02 A C ANISOU 192 CE1 PHE A 30 23273 23218 25327 2048 8 -1017 A C ATOM 193 CE2 PHE A 30 46.392 -28.911 -15.821 1.00193.79 A C ANISOU 193 CE2 PHE A 30 23755 23670 26206 2352 27 -960 A C ATOM 194 CZ PHE A 30 45.118 -28.647 -16.297 1.00191.51 A C ANISOU 194 CZ PHE A 30 23569 23352 25844 2203 59 -1043 A C ATOM 195 N GLY A 31 47.753 -22.960 -17.381 1.00175.25 A N ANISOU 195 N GLY A 31 21166 22405 23017 1861 -114 -946 A N ATOM 196 CA GLY A 31 47.709 -21.559 -17.747 1.00163.58 A C ANISOU 196 CA GLY A 31 19675 21127 21349 1721 -121 -934 A C ATOM 197 C GLY A 31 48.171 -21.326 -19.177 1.00154.79 A C ANISOU 197 C GLY A 31 18481 20162 20169 1690 -37 -1109 A C ATOM 198 O GLY A 31 47.500 -20.633 -19.950 1.00148.33 A O ANISOU 198 O GLY A 31 17711 19427 19221 1565 -10 -1161 A O ATOM 199 N GLU A 32 49.303 -21.938 -19.532 1.00148.39 A N ANISOU 199 N GLU A 32 17549 19380 19453 1807 7 -1197 A N ATOM 200 CA GLU A 32 50.068 -21.576 -20.729 1.00131.88 A C ANISOU 200 CA GLU A 32 15358 17459 17291 1782 90 -1347 A C ATOM 201 C GLU A 32 50.613 -20.152 -20.609 1.00114.54 A C ANISOU 201 C GLU A 32 13109 15475 14937 1693 68 -1272 A C ATOM 202 O GLU A 32 50.111 -19.223 -21.243 1.00105.91 A O ANISOU 202 O GLU A 32 12064 14491 13685 1560 94 -1291 A O ATOM 203 CB GLU A 32 49.253 -21.742 -22.011 1.00130.82 A C ANISOU 203 CB GLU A 32 15290 17324 17090 1696 167 -1507 A C ATOM 204 CG GLU A 32 49.650 -22.963 -22.812 1.00137.69 A C ANISOU 204 CG GLU A 32 16108 18114 18096 1789 261 -1691 A C ATOM 205 CD GLU A 32 49.655 -22.706 -24.309 1.00143.53 A C ANISOU 205 CD GLU A 32 16836 18988 18710 1700 358 -1876 A C ATOM 206 OE1 GLU A 32 49.188 -21.622 -24.737 1.00143.10 A O ANISOU 206 OE1 GLU A 32 16832 19075 18465 1567 342 -1849 A O ATOM 207 OE2 GLU A 32 50.131 -23.592 -25.054 1.00145.11 A O1- ANISOU 207 OE2 GLU A 32 16978 19151 19006 1762 453 -2046 A O1- ATOM 208 N VAL A 33 51.646 -20.008 -19.782 1.00107.35 A N ANISOU 208 N VAL A 33 12095 14617 14078 1769 21 -1186 A N ATOM 209 CA VAL A 33 52.257 -18.720 -19.465 1.00 99.47 A C ANISOU 209 CA VAL A 33 11032 13806 12955 1692 -2 -1111 A C ATOM 210 C VAL A 33 53.634 -18.575 -20.123 1.00100.76 A C ANISOU 210 C VAL A 33 11029 14121 13132 1737 69 -1225 A C ATOM 211 O VAL A 33 54.481 -19.450 -19.992 1.00106.60 A O ANISOU 211 O VAL A 33 11663 14815 14026 1878 72 -1268 A O ATOM 212 CB VAL A 33 52.429 -18.581 -17.948 1.00 91.38 A C ANISOU 212 CB VAL A 33 10006 12748 11965 1730 -116 -929 A C ATOM 213 CG1 VAL A 33 53.017 -17.247 -17.599 1.00 87.12 A C ANISOU 213 CG1 VAL A 33 9401 12401 11299 1637 -133 -864 A C ATOM 214 CG2 VAL A 33 51.096 -18.788 -17.247 1.00 94.53 A C ANISOU 214 CG2 VAL A 33 10570 12982 12363 1687 -173 -821 A C ATOM 215 N PHE A 34 53.854 -17.475 -20.836 1.00 97.55 A N ANISOU 215 N PHE A 34 10599 13889 12575 1620 133 -1272 A N ATOM 216 CA PHE A 34 55.134 -17.228 -21.498 1.00 90.60 A C ANISOU 216 CA PHE A 34 9566 13158 11698 1643 217 -1387 A C ATOM 217 C PHE A 34 55.863 -16.058 -20.842 1.00 84.11 A C ANISOU 217 C PHE A 34 8661 12497 10802 1585 187 -1297 A C ATOM 218 O PHE A 34 55.234 -15.113 -20.368 1.00 90.30 A O ANISOU 218 O PHE A 34 9527 13315 11466 1471 148 -1183 A O ATOM 219 CB PHE A 34 54.926 -16.897 -22.982 1.00 96.75 A C ANISOU 219 CB PHE A 34 10381 14023 12356 1548 341 -1535 A C ATOM 220 CG PHE A 34 54.281 -17.997 -23.791 1.00107.05 A C ANISOU 220 CG PHE A 34 11757 15200 13718 1585 387 -1660 A C ATOM 221 CD1 PHE A 34 55.055 -18.956 -24.426 1.00112.58 A C ANISOU 221 CD1 PHE A 34 12361 15870 14545 1686 471 -1819 A C ATOM 222 CD2 PHE A 34 52.903 -18.045 -23.957 1.00110.67 A C ANISOU 222 CD2 PHE A 34 12371 15572 14105 1512 356 -1630 A C ATOM 223 CE1 PHE A 34 54.464 -19.962 -25.190 1.00114.67 A C ANISOU 223 CE1 PHE A 34 12690 16019 14861 1708 526 -1950 A C ATOM 224 CE2 PHE A 34 52.308 -19.048 -24.723 1.00114.40 A C ANISOU 224 CE2 PHE A 34 12904 15937 14628 1535 401 -1761 A C ATOM 225 CZ PHE A 34 53.092 -20.009 -25.337 1.00111.43 A C ANISOU 225 CZ PHE A 34 12435 15530 14372 1630 489 -1923 A C ATOM 226 N LYS A 35 57.187 -16.115 -20.800 1.00 81.48 A N ANISOU 226 N LYS A 35 8156 12257 10547 1659 211 -1353 A N ATOM 227 CA LYS A 35 57.963 -14.909 -20.537 1.00 80.62 A C ANISOU 227 CA LYS A 35 7951 12330 10351 1578 224 -1323 A C ATOM 228 C LYS A 35 58.062 -14.234 -21.888 1.00 80.49 A C ANISOU 228 C LYS A 35 7942 12430 10212 1471 371 -1452 A C ATOM 229 O LYS A 35 58.092 -14.897 -22.920 1.00 80.58 A O ANISOU 229 O LYS A 35 7956 12408 10254 1506 457 -1591 A O ATOM 230 CB LYS A 35 59.352 -15.232 -19.973 1.00 78.49 A C ANISOU 230 CB LYS A 35 7481 12122 10220 1698 188 -1341 A C ATOM 231 CG LYS A 35 60.337 -14.045 -19.902 1.00 80.36 A C ANISOU 231 CG LYS A 35 7586 12564 10385 1615 230 -1359 A C ATOM 232 CD LYS A 35 61.709 -14.453 -19.311 1.00 84.61 A C ANISOU 232 CD LYS A 35 7908 13163 11077 1745 178 -1380 A C ATOM 233 CE LYS A 35 62.652 -13.258 -19.090 1.00 86.68 A C ANISOU 233 CE LYS A 35 8033 13628 11273 1653 208 -1396 A C ATOM 234 NZ LYS A 35 63.990 -13.626 -18.484 1.00 82.39 A N1+ ANISOU 234 NZ LYS A 35 7263 13158 10883 1778 144 -1418 A N1+ ATOM 235 N ALA A 36 58.064 -12.916 -21.907 1.00 80.72 A N ANISOU 235 N ALA A 36 7986 12590 10096 1334 408 -1406 A N ATOM 236 CA ALA A 36 58.186 -12.245 -23.182 1.00 81.54 A C ANISOU 236 CA ALA A 36 8103 12804 10074 1233 552 -1515 A C ATOM 237 C ALA A 36 58.789 -10.872 -23.027 1.00 79.78 A C ANISOU 237 C ALA A 36 7816 12743 9753 1121 607 -1482 A C ATOM 238 O ALA A 36 58.917 -10.347 -21.917 1.00 76.51 A O ANISOU 238 O ALA A 36 7369 12355 9348 1098 527 -1369 A O ATOM 239 CB ALA A 36 56.850 -12.173 -23.892 1.00 76.47 A C ANISOU 239 CB ALA A 36 7645 12098 9312 1153 568 -1501 A C ATOM 240 N ARG A 37 59.152 -10.310 -24.170 1.00 77.95 A N ANISOU 240 N ARG A 37 7574 12619 9426 1045 752 -1588 A N ATOM 241 CA ARG A 37 59.919 -9.091 -24.245 1.00 76.54 A C ANISOU 241 CA ARG A 37 7316 12596 9172 944 845 -1597 A C ATOM 242 C ARG A 37 59.230 -8.130 -25.198 1.00 78.93 A C ANISOU 242 C ARG A 37 7755 12950 9285 802 950 -1583 A C ATOM 243 O ARG A 37 58.900 -8.486 -26.327 1.00 81.95 A O ANISOU 243 O ARG A 37 8212 13322 9603 796 1020 -1669 A O ATOM 244 CB ARG A 37 61.305 -9.434 -24.779 1.00 77.30 A C ANISOU 244 CB ARG A 37 7235 12776 9361 1008 945 -1762 A C ATOM 245 CG ARG A 37 62.060 -8.260 -25.352 1.00 76.05 A C ANISOU 245 CG ARG A 37 7014 12776 9107 890 1099 -1824 A C ATOM 246 CD ARG A 37 63.453 -8.649 -25.784 1.00 63.19 A C ANISOU 246 CD ARG A 37 5195 11221 7595 957 1197 -1993 A C ATOM 247 NE ARG A 37 64.347 -7.500 -25.751 1.00 76.35 A N ANISOU 247 NE ARG A 37 6752 13035 9221 858 1301 -2022 A N ATOM 248 CZ ARG A 37 64.428 -6.581 -26.707 1.00 73.17 A C ANISOU 248 CZ ARG A 37 6403 12720 8676 731 1469 -2072 A C ATOM 249 NH1 ARG A 37 63.669 -6.660 -27.794 1.00 73.45 A N1+ ANISOU 249 NH1 ARG A 37 6601 12724 8582 686 1542 -2094 A N1+ ATOM 250 NH2 ARG A 37 65.270 -5.578 -26.570 1.00 76.24 A N ANISOU 250 NH2 ARG A 37 6685 13231 9052 645 1566 -2100 A N ATOM 251 N HIS A 38 59.003 -6.912 -24.740 1.00 73.06 A N ANISOU 251 N HIS A 38 7046 12263 8452 686 960 -1472 A N ATOM 252 CA HIS A 38 58.430 -5.888 -25.595 1.00 73.59 A C ANISOU 252 CA HIS A 38 7231 12383 8347 554 1065 -1439 A C ATOM 253 C HIS A 38 59.396 -5.585 -26.741 1.00 76.49 A C ANISOU 253 C HIS A 38 7531 12873 8659 520 1239 -1583 A C ATOM 254 O HIS A 38 60.563 -5.278 -26.514 1.00 84.11 A O ANISOU 254 O HIS A 38 8344 13927 9686 520 1305 -1650 A O ATOM 255 CB HIS A 38 58.174 -4.623 -24.776 1.00 76.57 A C ANISOU 255 CB HIS A 38 7631 12792 8672 442 1059 -1300 A C ATOM 256 CG HIS A 38 57.506 -3.534 -25.551 1.00 78.13 A C ANISOU 256 CG HIS A 38 7954 13024 8707 313 1160 -1238 A C ATOM 257 CD2 HIS A 38 56.255 -3.021 -25.467 1.00 68.81 A C ANISOU 257 CD2 HIS A 38 6919 11775 7448 246 1119 -1102 A C ATOM 258 ND1 HIS A 38 58.141 -2.848 -26.567 1.00 78.33 A N ANISOU 258 ND1 HIS A 38 7959 13163 8638 244 1327 -1313 A N ATOM 259 CE1 HIS A 38 57.307 -1.955 -27.073 1.00 81.55 A C ANISOU 259 CE1 HIS A 38 8503 13573 8911 144 1380 -1215 A C ATOM 260 NE2 HIS A 38 56.156 -2.041 -26.426 1.00 75.52 A N ANISOU 260 NE2 HIS A 38 7835 12700 8160 145 1253 -1088 A N ATOM 261 N ARG A 39 58.914 -5.650 -27.973 1.00 70.16 A N ANISOU 261 N ARG A 39 6840 12080 7737 485 1316 -1634 A N ATOM 262 CA ARG A 39 59.806 -5.547 -29.130 1.00 65.24 A C ANISOU 262 CA ARG A 39 6167 11562 7060 459 1486 -1786 A C ATOM 263 C ARG A 39 60.465 -4.184 -29.317 1.00 68.41 A C ANISOU 263 C ARG A 39 6530 12087 7377 340 1633 -1771 A C ATOM 264 O ARG A 39 61.194 -3.973 -30.278 1.00 77.18 A O ANISOU 264 O ARG A 39 7609 13286 8430 302 1792 -1890 A O ATOM 265 CB ARG A 39 59.080 -5.952 -30.420 1.00 67.66 A C ANISOU 265 CB ARG A 39 6616 11857 7234 441 1529 -1842 A C ATOM 266 CG ARG A 39 58.608 -7.401 -30.447 1.00 80.48 A C ANISOU 266 CG ARG A 39 8261 13366 8952 554 1426 -1909 A C ATOM 267 CD ARG A 39 58.063 -7.795 -31.817 1.00 96.72 A C ANISOU 267 CD ARG A 39 10439 15439 10871 523 1489 -2001 A C ATOM 268 NE ARG A 39 57.268 -9.022 -31.741 1.00109.45 A N ANISOU 268 NE ARG A 39 12104 16925 12557 607 1374 -2031 A N ATOM 269 CZ ARG A 39 57.720 -10.240 -32.039 1.00115.47 A C ANISOU 269 CZ ARG A 39 12799 17636 13437 700 1396 -2190 A C ATOM 270 NH1 ARG A 39 58.973 -10.415 -32.453 1.00116.29 A N1+ ANISOU 270 NH1 ARG A 39 12776 17807 13603 726 1527 -2338 A N1+ ATOM 271 NH2 ARG A 39 56.911 -11.289 -31.925 1.00112.28 A N ANISOU 271 NH2 ARG A 39 12454 17107 13102 766 1297 -2207 A N ATOM 272 N LYS A 40 60.221 -3.248 -28.416 1.00 73.60 A N ANISOU 272 N LYS A 40 7192 12746 8027 274 1595 -1634 A N ATOM 273 CA LYS A 40 60.749 -1.908 -28.628 1.00 79.99 A C ANISOU 273 CA LYS A 40 7979 13658 8754 150 1749 -1617 A C ATOM 274 C LYS A 40 61.608 -1.419 -27.469 1.00 84.65 A C ANISOU 274 C LYS A 40 8409 14294 9461 135 1738 -1609 A C ATOM 275 O LYS A 40 62.547 -0.647 -27.669 1.00 87.26 A O ANISOU 275 O LYS A 40 8646 14726 9783 63 1885 -1675 A O ATOM 276 CB LYS A 40 59.606 -0.928 -28.909 1.00 79.09 A C ANISOU 276 CB LYS A 40 8043 13523 8487 43 1767 -1460 A C ATOM 277 CG LYS A 40 59.222 -0.808 -30.374 1.00 78.83 A C ANISOU 277 CG LYS A 40 8142 13526 8284 0 1871 -1487 A C ATOM 278 CD LYS A 40 57.872 -0.155 -30.552 1.00 84.93 A C ANISOU 278 CD LYS A 40 9090 14249 8930 -65 1827 -1315 A C ATOM 279 CE LYS A 40 57.666 0.284 -31.987 1.00 96.03 A C ANISOU 279 CE LYS A 40 10618 15725 10145 -130 1954 -1324 A C ATOM 280 NZ LYS A 40 58.610 1.381 -32.339 1.00105.70 A N1+ ANISOU 280 NZ LYS A 40 11797 17049 11317 -225 2156 -1346 A N1+ ATOM 281 N THR A 41 61.292 -1.889 -26.267 1.00 84.22 A N ANISOU 281 N THR A 41 8323 14168 9510 199 1566 -1534 A N ATOM 282 CA THR A 41 61.904 -1.375 -25.054 1.00 81.74 A C ANISOU 282 CA THR A 41 7878 13897 9281 172 1528 -1502 A C ATOM 283 C THR A 41 62.619 -2.461 -24.272 1.00 85.57 A C ANISOU 283 C THR A 41 8209 14373 9932 309 1400 -1567 A C ATOM 284 O THR A 41 63.357 -2.177 -23.317 1.00 92.97 A O ANISOU 284 O THR A 41 9004 15372 10948 302 1362 -1570 A O ATOM 285 CB THR A 41 60.840 -0.790 -24.143 1.00 81.21 A C ANISOU 285 CB THR A 41 7921 13758 9176 106 1435 -1328 A C ATOM 286 CG2 THR A 41 59.992 0.191 -24.924 1.00 77.14 A C ANISOU 286 CG2 THR A 41 7568 13232 8512 -10 1544 -1243 A C ATOM 287 OG1 THR A 41 60.029 -1.852 -23.625 1.00 83.68 A O ANISOU 287 OG1 THR A 41 8300 13949 9545 210 1257 -1267 A O ATOM 288 N GLY A 42 62.388 -3.705 -24.673 1.00 81.78 A N ANISOU 288 N GLY A 42 7754 13813 9504 432 1332 -1618 A N ATOM 289 CA GLY A 42 63.057 -4.839 -24.066 1.00 80.97 A C ANISOU 289 CA GLY A 42 7509 13684 9570 580 1220 -1678 A C ATOM 290 C GLY A 42 62.426 -5.197 -22.736 1.00 76.97 A C ANISOU 290 C GLY A 42 7037 13090 9120 629 1027 -1537 A C ATOM 291 O GLY A 42 62.826 -6.170 -22.090 1.00 79.21 A O ANISOU 291 O GLY A 42 7223 13333 9539 761 909 -1549 A O ATOM 292 N GLN A 43 61.435 -4.410 -22.328 1.00 66.15 A N ANISOU 292 N GLN A 43 5804 11684 7647 525 1001 -1399 A N ATOM 293 CA GLN A 43 60.728 -4.668 -21.077 1.00 74.09 A C ANISOU 293 CA GLN A 43 6864 12598 8688 550 834 -1262 A C ATOM 294 C GLN A 43 60.155 -6.077 -21.026 1.00 81.54 A C ANISOU 294 C GLN A 43 7868 13401 9712 692 713 -1251 A C ATOM 295 O GLN A 43 59.478 -6.520 -21.952 1.00 80.20 A O ANISOU 295 O GLN A 43 7808 13161 9502 709 748 -1282 A O ATOM 296 CB GLN A 43 59.612 -3.661 -20.903 1.00 65.74 A C ANISOU 296 CB GLN A 43 5965 11503 7511 414 854 -1132 A C ATOM 297 CG GLN A 43 58.683 -3.956 -19.766 1.00 74.85 A C ANISOU 297 CG GLN A 43 7209 12542 8690 428 702 -995 A C ATOM 298 CD GLN A 43 57.398 -3.147 -19.898 1.00 81.36 A C ANISOU 298 CD GLN A 43 8207 13298 9409 310 735 -882 A C ATOM 299 NE2 GLN A 43 56.541 -3.203 -18.873 1.00 58.83 A N ANISOU 299 NE2 GLN A 43 5437 10345 6571 293 626 -761 A N ATOM 300 OE1 GLN A 43 57.184 -2.474 -20.921 1.00 89.20 A O ANISOU 300 OE1 GLN A 43 9257 14326 10309 235 860 -901 A O ATOM 301 N LYS A 44 60.442 -6.793 -19.950 1.00 83.65 A N ANISOU 301 N LYS A 44 8061 13629 10093 794 573 -1209 A N ATOM 302 CA LYS A 44 60.019 -8.180 -19.881 1.00 81.08 A C ANISOU 302 CA LYS A 44 7779 13162 9865 938 472 -1204 A C ATOM 303 C LYS A 44 58.649 -8.237 -19.221 1.00 75.08 A C ANISOU 303 C LYS A 44 7196 12269 9063 905 373 -1057 A C ATOM 304 O LYS A 44 58.322 -7.391 -18.381 1.00 71.18 A O ANISOU 304 O LYS A 44 6740 11797 8507 806 340 -951 A O ATOM 305 CB LYS A 44 61.038 -9.036 -19.123 1.00 75.79 A C ANISOU 305 CB LYS A 44 6941 12503 9351 1083 373 -1228 A C ATOM 306 CG LYS A 44 62.491 -8.676 -19.390 1.00 81.46 A C ANISOU 306 CG LYS A 44 7452 13380 10119 1089 454 -1350 A C ATOM 307 CD LYS A 44 62.980 -9.051 -20.799 1.00 84.82 A C ANISOU 307 CD LYS A 44 7831 13825 10573 1124 600 -1519 A C ATOM 308 CE LYS A 44 64.469 -8.699 -21.002 1.00 91.22 A C ANISOU 308 CE LYS A 44 8421 14788 11450 1129 687 -1647 A C ATOM 309 NZ LYS A 44 65.015 -7.637 -20.055 1.00 98.34 A N1+ ANISOU 309 NZ LYS A 44 9225 15823 12318 1037 656 -1592 A N1+ ATOM 310 N VAL A 45 57.855 -9.227 -19.624 1.00 67.76 A N ANISOU 310 N VAL A 45 6373 11202 8172 981 339 -1065 A N ATOM 311 CA VAL A 45 56.502 -9.406 -19.123 1.00 69.64 A C ANISOU 311 CA VAL A 45 6779 11297 8385 956 257 -945 A C ATOM 312 C VAL A 45 56.141 -10.882 -19.062 1.00 75.13 A C ANISOU 312 C VAL A 45 7511 11835 9200 1100 180 -961 A C ATOM 313 O VAL A 45 56.870 -11.742 -19.561 1.00 80.51 A O ANISOU 313 O VAL A 45 8098 12514 9978 1214 204 -1071 A O ATOM 314 CB VAL A 45 55.446 -8.727 -20.032 1.00 70.01 A C ANISOU 314 CB VAL A 45 6969 11330 8302 837 338 -936 A C ATOM 315 CG1 VAL A 45 55.622 -7.219 -20.055 1.00 53.23 A C ANISOU 315 CG1 VAL A 45 4833 9331 6062 688 423 -897 A C ATOM 316 CG2 VAL A 45 55.489 -9.313 -21.436 1.00 75.19 A C ANISOU 316 CG2 VAL A 45 7635 11988 8947 879 421 -1074 A C ATOM 317 N ALA A 46 55.001 -11.167 -18.448 1.00 71.34 A N ANISOU 317 N ALA A 46 7168 11215 8722 1090 99 -854 A N ATOM 318 CA ALA A 46 54.435 -12.509 -18.483 1.00 72.81 A C ANISOU 318 CA ALA A 46 7420 11231 9015 1205 46 -870 A C ATOM 319 C ALA A 46 53.128 -12.468 -19.271 1.00 69.98 A C ANISOU 319 C ALA A 46 7215 10792 8584 1130 84 -884 A C ATOM 320 O ALA A 46 52.316 -11.575 -19.082 1.00 67.53 A O ANISOU 320 O ALA A 46 6997 10485 8176 1010 83 -798 A O ATOM 321 CB ALA A 46 54.193 -13.016 -17.084 1.00 66.77 A C ANISOU 321 CB ALA A 46 6686 10356 8326 1265 -81 -739 A C ATOM 322 N LEU A 47 52.953 -13.411 -20.184 1.00 63.73 A N ANISOU 322 N LEU A 47 6440 9932 7843 1199 121 -1000 A N ATOM 323 CA LEU A 47 51.735 -13.492 -20.953 1.00 64.29 A C ANISOU 323 CA LEU A 47 6645 9933 7851 1137 145 -1027 A C ATOM 324 C LEU A 47 50.995 -14.729 -20.491 1.00 75.09 A C ANISOU 324 C LEU A 47 8086 11102 9344 1225 76 -1011 A C ATOM 325 O LEU A 47 51.487 -15.847 -20.635 1.00 80.97 A O ANISOU 325 O LEU A 47 8775 11778 10213 1348 82 -1096 A O ATOM 326 CB LEU A 47 52.032 -13.633 -22.442 1.00 58.88 A C ANISOU 326 CB LEU A 47 5933 9329 7111 1130 251 -1190 A C ATOM 327 CG LEU A 47 52.878 -12.575 -23.114 1.00 60.38 A C ANISOU 327 CG LEU A 47 6047 9710 7186 1055 348 -1235 A C ATOM 328 CD1 LEU A 47 52.998 -12.933 -24.569 1.00 63.49 A C ANISOU 328 CD1 LEU A 47 6444 10153 7527 1052 449 -1399 A C ATOM 329 CD2 LEU A 47 52.257 -11.224 -22.957 1.00 61.54 A C ANISOU 329 CD2 LEU A 47 6268 9920 7195 914 351 -1117 A C ATOM 330 N LYS A 48 49.815 -14.528 -19.931 1.00 65.79 A N ANISOU 330 N LYS A 48 7031 9822 8143 1161 20 -906 A N ATOM 331 CA LYS A 48 48.969 -15.636 -19.563 1.00 67.71 A C ANISOU 331 CA LYS A 48 7360 9868 8497 1224 -30 -897 A C ATOM 332 C LYS A 48 47.797 -15.697 -20.562 1.00 72.55 A C ANISOU 332 C LYS A 48 8075 10440 9053 1151 3 -970 A C ATOM 333 O LYS A 48 46.889 -14.872 -20.536 1.00 69.47 A O ANISOU 333 O LYS A 48 7765 10059 8573 1038 -11 -897 A O ATOM 334 CB LYS A 48 48.529 -15.468 -18.105 1.00 74.33 A C ANISOU 334 CB LYS A 48 8260 10613 9369 1210 -116 -730 A C ATOM 335 CG LYS A 48 47.571 -16.534 -17.572 1.00 98.25 A C ANISOU 335 CG LYS A 48 11395 13423 12512 1262 -162 -699 A C ATOM 336 CD LYS A 48 47.376 -16.376 -16.061 1.00109.92 A C ANISOU 336 CD LYS A 48 12924 14825 14016 1254 -240 -533 A C ATOM 337 CE LYS A 48 46.123 -17.077 -15.568 1.00116.59 A C ANISOU 337 CE LYS A 48 13905 15455 14937 1251 -266 -488 A C ATOM 338 NZ LYS A 48 46.108 -17.121 -14.078 1.00120.84 A N1+ ANISOU 338 NZ LYS A 48 14492 15915 15507 1265 -336 -333 A N1+ ATOM 339 N LYS A 49 47.845 -16.653 -21.482 1.00 82.09 A N ANISOU 339 N LYS A 49 9270 11610 10312 1212 49 -1120 A N ATOM 340 CA LYS A 49 46.781 -16.812 -22.477 1.00 83.03 A C ANISOU 340 CA LYS A 49 9474 11702 10373 1146 74 -1208 A C ATOM 341 C LYS A 49 45.518 -17.323 -21.788 1.00 82.09 A C ANISOU 341 C LYS A 49 9464 11391 10334 1137 11 -1142 A C ATOM 342 O LYS A 49 45.596 -18.140 -20.871 1.00 86.61 A O ANISOU 342 O LYS A 49 10044 11818 11047 1226 -23 -1098 A O ATOM 343 CB LYS A 49 47.252 -17.774 -23.572 1.00 87.96 A C ANISOU 343 CB LYS A 49 10049 12333 11038 1212 148 -1400 A C ATOM 344 CG LYS A 49 46.228 -18.249 -24.606 1.00 91.36 A C ANISOU 344 CG LYS A 49 10559 12726 11430 1160 171 -1525 A C ATOM 345 CD LYS A 49 46.957 -19.103 -25.668 1.00104.89 A C ANISOU 345 CD LYS A 49 12206 14472 13175 1219 265 -1726 A C ATOM 346 CE LYS A 49 46.015 -19.846 -26.614 1.00111.06 A C ANISOU 346 CE LYS A 49 13057 15197 13946 1180 290 -1877 A C ATOM 347 NZ LYS A 49 46.746 -20.791 -27.520 1.00110.17 A N1+ ANISOU 347 NZ LYS A 49 12879 15091 13888 1240 393 -2081 A N1+ ATOM 348 N VAL A 50 44.361 -16.813 -22.196 1.00 78.04 A N ANISOU 348 N VAL A 50 9036 10879 9737 1030 -4 -1129 A N ATOM 349 CA VAL A 50 43.098 -17.256 -21.613 1.00 80.88 A C ANISOU 349 CA VAL A 50 9494 11059 10177 1009 -54 -1081 A C ATOM 350 C VAL A 50 42.671 -18.592 -22.208 1.00 91.08 A C ANISOU 350 C VAL A 50 10809 12228 11570 1065 -29 -1235 A C ATOM 351 O VAL A 50 42.361 -18.687 -23.404 1.00 79.56 A O ANISOU 351 O VAL A 50 9352 10839 10037 1023 3 -1367 A O ATOM 352 CB VAL A 50 41.952 -16.256 -21.825 1.00 71.02 A C ANISOU 352 CB VAL A 50 8316 9845 8824 877 -81 -1015 A C ATOM 353 CG1 VAL A 50 40.633 -16.932 -21.513 1.00 59.49 A C ANISOU 353 CG1 VAL A 50 6944 8196 7463 860 -117 -1021 A C ATOM 354 CG2 VAL A 50 42.141 -15.027 -20.955 1.00 66.44 A C ANISOU 354 CG2 VAL A 50 7733 9326 8186 815 -101 -848 A C ATOM 355 N LEU A 51 42.624 -19.602 -21.342 1.00102.45 A N ANISOU 355 N LEU A 51 12270 13482 13173 1154 -42 -1213 A N ATOM 356 CA LEU A 51 42.523 -20.988 -21.754 1.00116.09 A C ANISOU 356 CA LEU A 51 14001 15076 15031 1234 1 -1359 A C ATOM 357 C LEU A 51 41.578 -21.221 -22.938 1.00124.39 A C ANISOU 357 C LEU A 51 15091 16140 16031 1156 27 -1513 A C ATOM 358 O LEU A 51 42.052 -21.436 -24.063 1.00133.80 A O ANISOU 358 O LEU A 51 16233 17439 17168 1160 83 -1664 A O ATOM 359 CB LEU A 51 42.203 -21.874 -20.549 1.00124.06 A C ANISOU 359 CB LEU A 51 15066 15856 16214 1310 -22 -1278 A C ATOM 360 CG LEU A 51 43.348 -21.842 -19.527 1.00124.69 A C ANISOU 360 CG LEU A 51 15089 15944 16343 1410 -49 -1151 A C ATOM 361 CD1 LEU A 51 43.106 -22.755 -18.318 1.00123.52 A C ANISOU 361 CD1 LEU A 51 15004 15571 16356 1496 -74 -1055 A C ATOM 362 CD2 LEU A 51 44.657 -22.190 -20.224 1.00122.81 A C ANISOU 362 CD2 LEU A 51 14729 15810 16123 1502 4 -1261 A C ATOM 363 N MET A 52 40.266 -21.177 -22.702 1.00113.85 A N ANISOU 363 N MET A 52 13842 14704 14713 1082 -13 -1481 A N ATOM 364 CA MET A 52 39.298 -21.389 -23.787 1.00111.67 A C ANISOU 364 CA MET A 52 13596 14447 14387 1003 -6 -1626 A C ATOM 365 C MET A 52 39.073 -22.856 -24.212 1.00121.76 A C ANISOU 365 C MET A 52 14879 15579 15804 1058 53 -1809 A C ATOM 366 O MET A 52 38.544 -23.099 -25.297 1.00114.65 A O ANISOU 366 O MET A 52 13983 14733 14847 997 71 -1967 A O ATOM 367 CB MET A 52 39.710 -20.589 -25.033 1.00 97.20 A C ANISOU 367 CB MET A 52 11716 12855 12359 942 9 -1694 A C ATOM 368 CG MET A 52 39.512 -19.095 -24.930 1.00 95.56 A C ANISOU 368 CG MET A 52 11520 12787 12000 852 -42 -1543 A C ATOM 369 SD MET A 52 37.780 -18.597 -24.975 1.00132.51 A S ANISOU 369 SD MET A 52 16278 17420 16649 734 -116 -1493 A S ATOM 370 CE MET A 52 37.269 -19.298 -26.542 1.00189.75 A C ANISOU 370 CE MET A 52 23525 24740 23831 696 -100 -1724 A C ATOM 371 N GLU A 53 39.460 -23.822 -23.378 1.00141.20 A N ANISOU 371 N GLU A 53 17344 17859 18446 1168 85 -1790 A N ATOM 372 CA GLU A 53 39.491 -25.228 -23.816 1.00158.84 A C ANISOU 372 CA GLU A 53 19569 19955 20826 1234 166 -1969 A C ATOM 373 C GLU A 53 38.261 -25.587 -24.652 1.00162.13 A C ANISOU 373 C GLU A 53 20030 20344 21229 1135 174 -2128 A C ATOM 374 O GLU A 53 38.349 -25.715 -25.874 1.00165.80 A O ANISOU 374 O GLU A 53 20460 20931 21606 1093 213 -2301 A O ATOM 375 CB GLU A 53 39.711 -26.212 -22.645 1.00167.27 A C ANISOU 375 CB GLU A 53 20662 20786 22109 1355 189 -1894 A C ATOM 376 CG GLU A 53 38.497 -26.499 -21.758 1.00172.89 A C ANISOU 376 CG GLU A 53 21476 21293 22921 1320 162 -1817 A C ATOM 377 CD GLU A 53 38.171 -25.367 -20.793 1.00174.90 A C ANISOU 377 CD GLU A 53 21776 21586 23091 1261 75 -1603 A C ATOM 378 OE1 GLU A 53 39.112 -24.768 -20.228 1.00175.63 A O ANISOU 378 OE1 GLU A 53 21831 21770 23130 1308 42 -1468 A O ATOM 379 OE2 GLU A 53 36.970 -25.087 -20.585 1.00173.52 A O1- ANISOU 379 OE2 GLU A 53 21671 21347 22912 1165 44 -1577 A O1- ATOM 380 N ASN A 54 37.117 -25.734 -23.998 1.00159.78 A N ANISOU 380 N ASN A 54 19807 19891 21012 1092 140 -2073 A N ATOM 381 CA ASN A 54 35.859 -25.858 -24.713 1.00159.98 A C ANISOU 381 CA ASN A 54 19864 19910 21009 982 126 -2202 A C ATOM 382 C ASN A 54 35.140 -24.512 -24.710 1.00149.66 A C ANISOU 382 C ASN A 54 18579 18738 19549 872 28 -2078 A C ATOM 383 O ASN A 54 35.044 -23.849 -25.749 1.00148.95 A O ANISOU 383 O ASN A 54 18460 18848 19286 798 -4 -2136 A O ATOM 384 CB ASN A 54 34.990 -26.971 -24.116 1.00165.41 A C ANISOU 384 CB ASN A 54 20612 20330 21906 998 167 -2255 A C ATOM 385 CG ASN A 54 35.122 -27.075 -22.608 1.00165.69 A C ANISOU 385 CG ASN A 54 20700 20183 22070 1072 161 -2059 A C ATOM 386 ND2 ASN A 54 35.781 -28.135 -22.147 1.00165.98 A N ANISOU 386 ND2 ASN A 54 20736 20058 22269 1194 235 -2075 A N ATOM 387 OD1 ASN A 54 34.632 -26.219 -21.865 1.00162.55 A O ANISOU 387 OD1 ASN A 54 20345 19789 21628 1019 93 -1895 A O ATOM 388 N GLU A 55 34.658 -24.109 -23.535 1.00134.97 A N ANISOU 388 N GLU A 55 16770 16763 17751 862 -14 -1903 A N ATOM 389 CA GLU A 55 34.041 -22.802 -23.356 1.00118.11 A C ANISOU 389 CA GLU A 55 14651 14727 15497 767 -93 -1763 A C ATOM 390 C GLU A 55 32.933 -22.567 -24.387 1.00113.71 A C ANISOU 390 C GLU A 55 14090 14255 14861 658 -137 -1876 A C ATOM 391 O GLU A 55 33.128 -21.922 -25.420 1.00114.74 A O ANISOU 391 O GLU A 55 14180 14597 14817 614 -165 -1918 A O ATOM 392 CB GLU A 55 35.105 -21.696 -23.413 1.00109.80 A C ANISOU 392 CB GLU A 55 13554 13876 14290 779 -114 -1644 A C ATOM 393 CG GLU A 55 36.198 -21.813 -22.352 1.00102.40 A C ANISOU 393 CG GLU A 55 12608 12879 13420 879 -90 -1523 A C ATOM 394 CD GLU A 55 35.661 -21.789 -20.918 1.00105.93 A C ANISOU 394 CD GLU A 55 13126 13143 13981 878 -111 -1367 A C ATOM 395 OE1 GLU A 55 34.511 -21.333 -20.698 1.00101.19 A O ANISOU 395 OE1 GLU A 55 12574 12492 13383 785 -146 -1322 A O ATOM 396 OE2 GLU A 55 36.402 -22.221 -20.004 1.00109.69 A O1- ANISOU 396 OE2 GLU A 55 13608 13528 14540 970 -94 -1287 A O1- ATOM 397 N LYS A 56 31.757 -23.096 -24.092 1.00108.47 A N ANISOU 397 N LYS A 56 13466 13425 14323 615 -142 -1925 A N ATOM 398 CA LYS A 56 30.659 -23.054 -25.038 1.00107.23 A C ANISOU 398 CA LYS A 56 13294 13331 14116 518 -188 -2052 A C ATOM 399 C LYS A 56 29.678 -21.954 -24.653 1.00 95.36 A C ANISOU 399 C LYS A 56 11807 11846 12581 431 -269 -1907 A C ATOM 400 O LYS A 56 28.572 -21.876 -25.171 1.00 97.03 A O ANISOU 400 O LYS A 56 12006 12073 12788 350 -320 -1980 A O ATOM 401 CB LYS A 56 29.994 -24.431 -25.099 1.00117.71 A C ANISOU 401 CB LYS A 56 14640 14468 15617 520 -131 -2236 A C ATOM 402 CG LYS A 56 30.963 -25.533 -25.568 1.00124.76 A C ANISOU 402 CG LYS A 56 15511 15339 16553 605 -38 -2393 A C ATOM 403 CD LYS A 56 30.689 -26.890 -24.921 1.00128.47 A C ANISOU 403 CD LYS A 56 16020 15532 17260 657 53 -2477 A C ATOM 404 CE LYS A 56 31.769 -27.905 -25.293 1.00132.83 A C ANISOU 404 CE LYS A 56 16545 16052 17872 756 154 -2605 A C ATOM 405 NZ LYS A 56 31.536 -29.252 -24.690 1.00134.59 A N1+ ANISOU 405 NZ LYS A 56 16808 15994 18336 814 255 -2683 A N1+ ATOM 406 N GLU A 57 30.120 -21.086 -23.753 1.00 81.02 A N ANISOU 406 N GLU A 57 10009 10032 10743 447 -278 -1705 A N ATOM 407 CA GLU A 57 29.301 -20.000 -23.257 1.00 61.81 A C ANISOU 407 CA GLU A 57 7589 7598 8296 370 -334 -1554 A C ATOM 408 C GLU A 57 29.971 -18.650 -23.474 1.00 62.20 A C ANISOU 408 C GLU A 57 7610 7852 8170 355 -367 -1413 A C ATOM 409 O GLU A 57 29.805 -17.727 -22.661 1.00 58.71 A O ANISOU 409 O GLU A 57 7188 7386 7735 321 -379 -1243 A O ATOM 410 CB GLU A 57 29.024 -20.192 -21.765 1.00 59.19 A C ANISOU 410 CB GLU A 57 7322 7039 8130 382 -297 -1437 A C ATOM 411 CG GLU A 57 27.879 -21.108 -21.457 1.00 76.69 A C ANISOU 411 CG GLU A 57 9574 9042 10524 351 -275 -1535 A C ATOM 412 CD GLU A 57 26.594 -20.658 -22.137 1.00 88.93 A C ANISOU 412 CD GLU A 57 11088 10642 12059 250 -342 -1592 A C ATOM 413 OE1 GLU A 57 26.340 -19.433 -22.180 1.00 91.97 A O ANISOU 413 OE1 GLU A 57 11451 11139 12353 196 -398 -1466 A O ATOM 414 OE2 GLU A 57 25.843 -21.525 -22.628 1.00 87.07 A O1- ANISOU 414 OE2 GLU A 57 10841 10333 11908 225 -337 -1763 A O1- ATOM 415 N GLY A 58 30.734 -18.525 -24.558 1.00 65.86 A N ANISOU 415 N GLY A 58 8032 8513 8480 373 -369 -1486 A N ATOM 416 CA GLY A 58 31.378 -17.253 -24.865 1.00 63.26 A C ANISOU 416 CA GLY A 58 7676 8379 7979 355 -386 -1363 A C ATOM 417 C GLY A 58 32.660 -17.024 -24.072 1.00 72.58 A C ANISOU 417 C GLY A 58 8855 9564 9157 421 -333 -1259 A C ATOM 418 O GLY A 58 33.325 -17.990 -23.658 1.00 70.85 A O ANISOU 418 O GLY A 58 8639 9248 9031 502 -285 -1318 A O ATOM 419 N PHE A 59 33.023 -15.757 -23.871 1.00 69.95 A N ANISOU 419 N PHE A 59 8510 9343 8724 388 -341 -1107 A N ATOM 420 CA PHE A 59 34.226 -15.450 -23.107 1.00 67.34 A C ANISOU 420 CA PHE A 59 8168 9034 8386 438 -297 -1011 A C ATOM 421 C PHE A 59 34.051 -15.966 -21.691 1.00 66.59 A C ANISOU 421 C PHE A 59 8117 8729 8456 468 -285 -942 A C ATOM 422 O PHE A 59 33.028 -15.723 -21.064 1.00 76.18 A O ANISOU 422 O PHE A 59 9374 9822 9748 409 -305 -873 A O ATOM 423 CB PHE A 59 34.518 -13.948 -23.084 1.00 66.80 A C ANISOU 423 CB PHE A 59 8081 9108 8193 380 -298 -863 A C ATOM 424 CG PHE A 59 35.886 -13.615 -22.562 1.00 70.48 A C ANISOU 424 CG PHE A 59 8514 9642 8623 426 -251 -798 A C ATOM 425 CD1 PHE A 59 37.003 -13.745 -23.373 1.00 63.86 A C ANISOU 425 CD1 PHE A 59 7623 8953 7687 475 -214 -883 A C ATOM 426 CD2 PHE A 59 36.062 -13.203 -21.254 1.00 78.19 A C ANISOU 426 CD2 PHE A 59 9508 10535 9666 418 -241 -664 A C ATOM 427 CE1 PHE A 59 38.257 -13.455 -22.896 1.00 64.81 A C ANISOU 427 CE1 PHE A 59 7700 9139 7788 517 -173 -833 A C ATOM 428 CE2 PHE A 59 37.325 -12.914 -20.773 1.00 77.10 A C ANISOU 428 CE2 PHE A 59 9329 10472 9493 457 -207 -614 A C ATOM 429 CZ PHE A 59 38.425 -13.047 -21.601 1.00 68.42 A C ANISOU 429 CZ PHE A 59 8167 9521 8308 510 -175 -700 A C ATOM 430 N PRO A 60 35.046 -16.700 -21.188 1.00 59.79 A N ANISOU 430 N PRO A 60 7246 7820 7651 561 -249 -960 A N ATOM 431 CA PRO A 60 34.878 -17.446 -19.939 1.00 58.56 A C ANISOU 431 CA PRO A 60 7143 7453 7652 603 -239 -912 A C ATOM 432 C PRO A 60 34.595 -16.553 -18.760 1.00 65.12 A C ANISOU 432 C PRO A 60 8015 8232 8494 543 -250 -736 A C ATOM 433 O PRO A 60 35.338 -15.615 -18.489 1.00 66.27 A O ANISOU 433 O PRO A 60 8131 8501 8549 527 -247 -636 A O ATOM 434 CB PRO A 60 36.211 -18.160 -19.766 1.00 56.54 A C ANISOU 434 CB PRO A 60 6850 7212 7422 721 -207 -943 A C ATOM 435 CG PRO A 60 36.749 -18.260 -21.152 1.00 66.80 A C ANISOU 435 CG PRO A 60 8084 8674 8622 739 -188 -1084 A C ATOM 436 CD PRO A 60 36.312 -17.022 -21.860 1.00 67.41 A C ANISOU 436 CD PRO A 60 8150 8914 8550 636 -215 -1046 A C ATOM 437 N ILE A 61 33.512 -16.855 -18.057 1.00 68.22 A N ANISOU 437 N ILE A 61 8476 8440 9005 502 -252 -708 A N ATOM 438 CA ILE A 61 33.099 -16.032 -16.933 1.00 69.45 A C ANISOU 438 CA ILE A 61 8679 8529 9180 428 -251 -555 A C ATOM 439 C ILE A 61 34.194 -15.951 -15.846 1.00 73.57 A C ANISOU 439 C ILE A 61 9209 9055 9688 477 -239 -445 A C ATOM 440 O ILE A 61 34.455 -14.883 -15.308 1.00 82.72 A O ANISOU 440 O ILE A 61 10363 10290 10779 417 -236 -329 A O ATOM 441 CB ILE A 61 31.735 -16.506 -16.392 1.00 61.22 A C ANISOU 441 CB ILE A 61 7709 7270 8280 376 -242 -565 A C ATOM 442 CG1 ILE A 61 31.056 -15.437 -15.550 1.00 66.61 A C ANISOU 442 CG1 ILE A 61 8429 7907 8972 268 -234 -429 A C ATOM 443 CG2 ILE A 61 31.866 -17.796 -15.636 1.00 60.03 A C ANISOU 443 CG2 ILE A 61 7619 6932 8257 455 -214 -590 A C ATOM 444 CD1 ILE A 61 29.698 -15.874 -15.086 1.00 69.87 A C ANISOU 444 CD1 ILE A 61 8906 8109 9533 211 -216 -451 A C ATOM 445 N THR A 62 34.864 -17.059 -15.559 1.00 67.13 A N ANISOU 445 N THR A 62 8400 8168 8938 587 -232 -484 A N ATOM 446 CA THR A 62 35.895 -17.038 -14.537 1.00 72.33 A C ANISOU 446 CA THR A 62 9059 8838 9583 642 -236 -378 A C ATOM 447 C THR A 62 37.093 -16.184 -14.947 1.00 74.91 A C ANISOU 447 C THR A 62 9292 9394 9775 653 -245 -356 A C ATOM 448 O THR A 62 37.823 -15.710 -14.091 1.00 74.83 A O ANISOU 448 O THR A 62 9270 9436 9724 654 -255 -252 A O ATOM 449 CB THR A 62 36.372 -18.446 -14.168 1.00 77.32 A C ANISOU 449 CB THR A 62 9712 9338 10326 771 -230 -414 A C ATOM 450 CG2 THR A 62 35.181 -19.313 -13.805 1.00 79.29 A C ANISOU 450 CG2 THR A 62 10059 9352 10716 756 -205 -445 A C ATOM 451 OG1 THR A 62 37.084 -19.025 -15.271 1.00 71.55 A O ANISOU 451 OG1 THR A 62 8901 8699 9587 859 -221 -547 A O ATOM 452 N ALA A 63 37.295 -15.991 -16.249 1.00 69.72 A N ANISOU 452 N ALA A 63 8567 8877 9046 655 -238 -460 A N ATOM 453 CA ALA A 63 38.343 -15.079 -16.724 1.00 62.74 A C ANISOU 453 CA ALA A 63 7598 8210 8031 648 -230 -445 A C ATOM 454 C ALA A 63 37.950 -13.633 -16.528 1.00 70.95 A C ANISOU 454 C ALA A 63 8645 9329 8984 524 -224 -341 A C ATOM 455 O ALA A 63 38.798 -12.811 -16.214 1.00 72.11 A O ANISOU 455 O ALA A 63 8745 9600 9053 504 -212 -273 A O ATOM 456 CB ALA A 63 38.663 -15.316 -18.190 1.00 56.29 A C ANISOU 456 CB ALA A 63 6718 7515 7153 681 -213 -588 A C ATOM 457 N LEU A 64 36.672 -13.321 -16.755 1.00 69.82 A N ANISOU 457 N LEU A 64 8552 9115 8862 441 -227 -335 A N ATOM 458 CA LEU A 64 36.153 -11.987 -16.490 1.00 71.56 A C ANISOU 458 CA LEU A 64 8784 9374 9032 323 -213 -228 A C ATOM 459 C LEU A 64 36.322 -11.633 -15.021 1.00 69.67 A C ANISOU 459 C LEU A 64 8583 9061 8825 285 -201 -106 A C ATOM 460 O LEU A 64 36.622 -10.495 -14.662 1.00 66.69 A O ANISOU 460 O LEU A 64 8186 8772 8381 211 -173 -19 A O ATOM 461 CB LEU A 64 34.672 -11.917 -16.828 1.00 64.28 A C ANISOU 461 CB LEU A 64 7907 8350 8167 255 -225 -244 A C ATOM 462 CG LEU A 64 34.336 -11.972 -18.305 1.00 63.34 A C ANISOU 462 CG LEU A 64 7750 8330 7986 260 -246 -347 A C ATOM 463 CD1 LEU A 64 32.860 -11.919 -18.398 1.00 54.70 A C ANISOU 463 CD1 LEU A 64 6693 7122 6968 193 -269 -348 A C ATOM 464 CD2 LEU A 64 34.978 -10.830 -19.096 1.00 59.37 A C ANISOU 464 CD2 LEU A 64 7189 8038 7332 228 -227 -313 A C ATOM 465 N ARG A 65 36.093 -12.628 -14.181 1.00 59.73 A N ANISOU 465 N ARG A 65 7387 7638 7670 332 -215 -102 A N ATOM 466 CA ARG A 65 36.222 -12.493 -12.748 1.00 63.22 A C ANISOU 466 CA ARG A 65 7883 7998 8138 302 -210 8 A C ATOM 467 C ARG A 65 37.672 -12.127 -12.424 1.00 67.96 A C ANISOU 467 C ARG A 65 8415 8759 8649 341 -218 49 A C ATOM 468 O ARG A 65 37.933 -11.141 -11.740 1.00 74.77 A O ANISOU 468 O ARG A 65 9272 9685 9452 259 -199 137 A O ATOM 469 CB ARG A 65 35.830 -13.840 -12.110 1.00 67.48 A C ANISOU 469 CB ARG A 65 8501 8336 8800 371 -224 -9 A C ATOM 470 CG ARG A 65 35.673 -13.871 -10.598 1.00 67.33 A C ANISOU 470 CG ARG A 65 8571 8194 8817 332 -217 106 A C ATOM 471 CD ARG A 65 35.289 -15.275 -10.121 1.00 81.35 A C ANISOU 471 CD ARG A 65 10430 9765 10716 412 -221 84 A C ATOM 472 NE ARG A 65 36.310 -16.250 -10.486 1.00107.86 A N ANISOU 472 NE ARG A 65 13736 13162 14086 561 -252 30 A N ATOM 473 CZ ARG A 65 36.295 -17.529 -10.123 1.00117.85 A C ANISOU 473 CZ ARG A 65 15054 14268 15455 659 -254 15 A C ATOM 474 NH1 ARG A 65 35.298 -17.995 -9.374 1.00117.94 A N1+ ANISOU 474 NH1 ARG A 65 15182 14071 15559 619 -224 50 A N1+ ATOM 475 NH2 ARG A 65 37.282 -18.336 -10.510 1.00117.15 A N ANISOU 475 NH2 ARG A 65 14904 14223 15387 797 -275 -34 A N ATOM 476 N GLU A 66 38.612 -12.923 -12.939 1.00 66.26 A N ANISOU 476 N GLU A 66 8139 8607 8431 463 -242 -26 A N ATOM 477 CA GLU A 66 40.032 -12.716 -12.696 1.00 65.27 A C ANISOU 477 CA GLU A 66 7930 8630 8239 517 -255 -5 A C ATOM 478 C GLU A 66 40.471 -11.339 -13.187 1.00 68.81 A C ANISOU 478 C GLU A 66 8306 9268 8569 430 -218 9 A C ATOM 479 O GLU A 66 41.091 -10.579 -12.457 1.00 73.71 A O ANISOU 479 O GLU A 66 8898 9973 9133 381 -211 82 A O ATOM 480 CB GLU A 66 40.847 -13.807 -13.373 1.00 71.63 A C ANISOU 480 CB GLU A 66 8672 9462 9082 662 -273 -107 A C ATOM 481 CG GLU A 66 42.320 -13.829 -13.009 1.00 79.67 A C ANISOU 481 CG GLU A 66 9597 10607 10068 740 -296 -88 A C ATOM 482 CD GLU A 66 43.140 -14.718 -13.938 1.00 89.31 A C ANISOU 482 CD GLU A 66 10733 11875 11326 871 -292 -209 A C ATOM 483 OE1 GLU A 66 42.557 -15.488 -14.737 1.00 94.37 A O ANISOU 483 OE1 GLU A 66 11402 12429 12026 908 -273 -307 A O ATOM 484 OE2 GLU A 66 44.382 -14.646 -13.874 1.00 95.32 A O1- ANISOU 484 OE2 GLU A 66 11393 12762 12062 933 -302 -214 A O1- ATOM 485 N ILE A 67 40.126 -11.008 -14.422 1.00 63.94 A N ANISOU 485 N ILE A 67 7664 8717 7913 407 -190 -61 A N ATOM 486 CA ILE A 67 40.414 -9.686 -14.950 1.00 57.07 A C ANISOU 486 CA ILE A 67 6741 8007 6935 321 -143 -39 A C ATOM 487 C ILE A 67 39.791 -8.561 -14.133 1.00 62.42 A C ANISOU 487 C ILE A 67 7464 8650 7602 188 -111 75 A C ATOM 488 O ILE A 67 40.350 -7.484 -14.044 1.00 65.78 A O ANISOU 488 O ILE A 67 7841 9198 7953 120 -66 117 A O ATOM 489 CB ILE A 67 39.936 -9.547 -16.380 1.00 58.62 A C ANISOU 489 CB ILE A 67 6926 8260 7087 312 -125 -116 A C ATOM 490 CG1 ILE A 67 40.774 -10.437 -17.291 1.00 60.09 A C ANISOU 490 CG1 ILE A 67 7051 8522 7258 425 -131 -241 A C ATOM 491 CG2 ILE A 67 40.024 -8.085 -16.833 1.00 53.77 A C ANISOU 491 CG2 ILE A 67 6279 7782 6369 212 -69 -63 A C ATOM 492 CD1 ILE A 67 40.250 -10.456 -18.697 1.00 62.60 A C ANISOU 492 CD1 ILE A 67 7371 8891 7522 415 -121 -329 A C ATOM 493 N LYS A 68 38.627 -8.788 -13.547 1.00 68.72 A N ANISOU 493 N LYS A 68 8351 9276 8482 144 -122 117 A N ATOM 494 CA LYS A 68 38.029 -7.744 -12.725 1.00 69.26 A C ANISOU 494 CA LYS A 68 8462 9299 8555 13 -78 217 A C ATOM 495 C LYS A 68 38.905 -7.541 -11.502 1.00 76.03 A C ANISOU 495 C LYS A 68 9311 10194 9383 -5 -77 279 A C ATOM 496 O LYS A 68 39.279 -6.418 -11.157 1.00 77.50 A O ANISOU 496 O LYS A 68 9465 10472 9508 -98 -27 330 A O ATOM 497 CB LYS A 68 36.627 -8.132 -12.287 1.00 67.55 A C ANISOU 497 CB LYS A 68 8340 8878 8447 -28 -84 239 A C ATOM 498 CG LYS A 68 35.916 -7.086 -11.472 1.00 67.58 A C ANISOU 498 CG LYS A 68 8388 8816 8474 -168 -26 332 A C ATOM 499 CD LYS A 68 34.640 -7.636 -10.892 1.00 72.51 A C ANISOU 499 CD LYS A 68 9105 9225 9219 -200 -28 344 A C ATOM 500 CE LYS A 68 34.926 -8.846 -10.013 1.00 73.09 A C ANISOU 500 CE LYS A 68 9240 9196 9335 -126 -68 339 A C ATOM 501 NZ LYS A 68 33.651 -9.501 -9.617 1.00 77.41 A N1+ ANISOU 501 NZ LYS A 68 9880 9526 10008 -150 -60 332 A N1+ ATOM 502 N ILE A 69 39.251 -8.646 -10.860 1.00 68.58 A N ANISOU 502 N ILE A 69 8395 9181 8482 85 -133 273 A N ATOM 503 CA ILE A 69 40.023 -8.587 -9.633 1.00 65.08 A C ANISOU 503 CA ILE A 69 7952 8769 8007 76 -153 338 A C ATOM 504 C ILE A 69 41.436 -7.999 -9.811 1.00 64.51 A C ANISOU 504 C ILE A 69 7760 8911 7840 91 -150 322 A C ATOM 505 O ILE A 69 41.871 -7.154 -9.021 1.00 63.69 A O ANISOU 505 O ILE A 69 7638 8884 7678 2 -127 377 A O ATOM 506 CB ILE A 69 40.037 -9.956 -8.966 1.00 63.21 A C ANISOU 506 CB ILE A 69 7776 8402 7841 182 -218 347 A C ATOM 507 CG1 ILE A 69 38.593 -10.296 -8.527 1.00 65.29 A C ANISOU 507 CG1 ILE A 69 8166 8447 8196 126 -198 376 A C ATOM 508 CG2 ILE A 69 41.015 -9.963 -7.810 1.00 60.86 A C ANISOU 508 CG2 ILE A 69 7461 8170 7491 195 -260 416 A C ATOM 509 CD1 ILE A 69 38.330 -11.775 -8.186 1.00 61.09 A C ANISOU 509 CD1 ILE A 69 7706 7747 7759 236 -242 365 A C ATOM 510 N LEU A 70 42.142 -8.420 -10.856 1.00 58.47 A N ANISOU 510 N LEU A 70 6912 8242 7062 194 -165 236 A N ATOM 511 CA LEU A 70 43.449 -7.853 -11.143 1.00 55.73 A C ANISOU 511 CA LEU A 70 6444 8095 6636 206 -149 206 A C ATOM 512 C LEU A 70 43.369 -6.338 -11.366 1.00 58.93 A C ANISOU 512 C LEU A 70 6823 8599 6967 63 -61 232 A C ATOM 513 O LEU A 70 44.258 -5.613 -10.976 1.00 62.74 A O ANISOU 513 O LEU A 70 7234 9214 7391 15 -36 244 A O ATOM 514 CB LEU A 70 44.091 -8.534 -12.341 1.00 53.99 A C ANISOU 514 CB LEU A 70 6146 7947 6421 328 -158 98 A C ATOM 515 CG LEU A 70 44.346 -10.024 -12.147 1.00 59.66 A C ANISOU 515 CG LEU A 70 6871 8572 7226 478 -230 65 A C ATOM 516 CD1 LEU A 70 44.539 -10.717 -13.504 1.00 56.13 A C ANISOU 516 CD1 LEU A 70 6377 8148 6800 574 -215 -58 A C ATOM 517 CD2 LEU A 70 45.523 -10.269 -11.181 1.00 51.79 A C ANISOU 517 CD2 LEU A 70 5806 7647 6225 540 -286 104 A C ATOM 518 N GLN A 71 42.299 -5.868 -11.987 1.00 54.90 A N ANISOU 518 N GLN A 71 6367 8023 6469 -3 -14 241 A N ATOM 519 CA GLN A 71 42.142 -4.447 -12.262 1.00 54.15 A C ANISOU 519 CA GLN A 71 6252 8002 6320 -129 77 276 A C ATOM 520 C GLN A 71 41.873 -3.632 -11.006 1.00 59.64 A C ANISOU 520 C GLN A 71 6987 8654 7019 -259 117 361 A C ATOM 521 O GLN A 71 42.153 -2.433 -10.949 1.00 65.34 A O ANISOU 521 O GLN A 71 7670 9463 7694 -364 200 386 A O ATOM 522 CB GLN A 71 41.026 -4.225 -13.283 1.00 47.75 A C ANISOU 522 CB GLN A 71 5486 7128 5527 -151 103 272 A C ATOM 523 CG GLN A 71 41.438 -4.686 -14.655 1.00 54.61 A C ANISOU 523 CG GLN A 71 6306 8090 6354 -57 89 182 A C ATOM 524 CD GLN A 71 40.338 -4.586 -15.665 1.00 63.87 A C ANISOU 524 CD GLN A 71 7523 9213 7532 -71 93 176 A C ATOM 525 NE2 GLN A 71 40.719 -4.367 -16.915 1.00 69.30 A N ANISOU 525 NE2 GLN A 71 8166 10026 8139 -45 119 123 A N ATOM 526 OE1 GLN A 71 39.155 -4.706 -15.337 1.00 67.26 A O ANISOU 526 OE1 GLN A 71 8024 9496 8036 -108 73 216 A O ATOM 527 N LEU A 72 41.332 -4.296 -10.002 1.00 61.43 A N ANISOU 527 N LEU A 72 7296 8742 7304 -256 67 400 A N ATOM 528 CA LEU A 72 40.940 -3.627 -8.786 1.00 65.51 A C ANISOU 528 CA LEU A 72 7867 9198 7825 -387 109 474 A C ATOM 529 C LEU A 72 42.099 -3.620 -7.816 1.00 69.14 A C ANISOU 529 C LEU A 72 8280 9770 8221 -391 77 484 A C ATOM 530 O LEU A 72 42.234 -2.689 -7.028 1.00 78.76 A O ANISOU 530 O LEU A 72 9497 11029 9400 -520 135 520 A O ATOM 531 CB LEU A 72 39.743 -4.329 -8.148 1.00 66.95 A C ANISOU 531 CB LEU A 72 8171 9170 8096 -395 82 512 A C ATOM 532 CG LEU A 72 39.524 -3.986 -6.676 1.00 56.91 A C ANISOU 532 CG LEU A 72 6970 7833 6821 -509 108 581 A C ATOM 533 CD1 LEU A 72 38.807 -2.670 -6.594 1.00 44.86 A C ANISOU 533 CD1 LEU A 72 5458 6274 5312 -669 223 616 A C ATOM 534 CD2 LEU A 72 38.749 -5.091 -5.964 1.00 45.05 A C ANISOU 534 CD2 LEU A 72 5584 6143 5392 -470 56 607 A C ATOM 535 N LEU A 73 42.921 -4.662 -7.870 1.00 67.06 A N ANISOU 535 N LEU A 73 7974 9555 7951 -250 -15 448 A N ATOM 536 CA LEU A 73 44.065 -4.797 -6.965 1.00 66.14 A C ANISOU 536 CA LEU A 73 7800 9552 7779 -230 -71 460 A C ATOM 537 C LEU A 73 45.328 -4.111 -7.491 1.00 69.38 A C ANISOU 537 C LEU A 73 8064 10175 8121 -231 -40 401 A C ATOM 538 O LEU A 73 46.024 -4.621 -8.370 1.00 73.99 A O ANISOU 538 O LEU A 73 8565 10835 8711 -112 -68 334 A O ATOM 539 CB LEU A 73 44.335 -6.269 -6.675 1.00 55.23 A C ANISOU 539 CB LEU A 73 6439 8105 6440 -71 -185 464 A C ATOM 540 CG LEU A 73 43.103 -6.885 -6.019 1.00 57.08 A C ANISOU 540 CG LEU A 73 6824 8123 6739 -89 -199 525 A C ATOM 541 CD1 LEU A 73 43.379 -8.245 -5.354 1.00 56.25 A C ANISOU 541 CD1 LEU A 73 6762 7940 6670 45 -303 559 A C ATOM 542 CD2 LEU A 73 42.592 -5.902 -5.009 1.00 52.97 A C ANISOU 542 CD2 LEU A 73 6371 7577 6180 -265 -138 589 A C ATOM 543 N LYS A 74 45.626 -2.944 -6.947 1.00 63.88 A N ANISOU 543 N LYS A 74 7335 9571 7366 -373 29 418 A N ATOM 544 CA LYS A 74 46.829 -2.221 -7.346 1.00 55.74 A C ANISOU 544 CA LYS A 74 6163 8739 6275 -392 72 357 A C ATOM 545 C LYS A 74 47.647 -1.926 -6.115 1.00 58.97 A C ANISOU 545 C LYS A 74 6524 9258 6624 -456 37 373 A C ATOM 546 O LYS A 74 47.278 -1.100 -5.290 1.00 65.21 A O ANISOU 546 O LYS A 74 7360 10032 7383 -609 96 411 A O ATOM 547 CB LYS A 74 46.458 -0.953 -8.103 1.00 48.36 A C ANISOU 547 CB LYS A 74 5219 7828 5328 -510 213 345 A C ATOM 548 CG LYS A 74 45.768 -1.248 -9.459 1.00 54.10 A C ANISOU 548 CG LYS A 74 5979 8481 6095 -437 234 325 A C ATOM 549 CD LYS A 74 46.679 -2.109 -10.320 1.00 64.80 A C ANISOU 549 CD LYS A 74 7248 9929 7445 -282 175 245 A C ATOM 550 CE LYS A 74 46.020 -2.559 -11.601 1.00 67.63 A C ANISOU 550 CE LYS A 74 7645 10221 7829 -207 181 214 A C ATOM 551 NZ LYS A 74 46.994 -3.339 -12.406 1.00 68.88 A N1+ ANISOU 551 NZ LYS A 74 7713 10476 7981 -71 144 122 A N1+ ATOM 552 N HIS A 75 48.757 -2.634 -5.974 1.00 63.58 A N ANISOU 552 N HIS A 75 7010 9952 7194 -339 -63 341 A N ATOM 553 CA HIS A 75 49.476 -2.605 -4.713 1.00 62.87 A C ANISOU 553 CA HIS A 75 6882 9960 7045 -375 -136 367 A C ATOM 554 C HIS A 75 50.847 -3.253 -4.859 1.00 64.60 A C ANISOU 554 C HIS A 75 6951 10330 7264 -233 -235 316 A C ATOM 555 O HIS A 75 51.019 -4.166 -5.663 1.00 68.49 A O ANISOU 555 O HIS A 75 7416 10787 7821 -75 -277 285 A O ATOM 556 CB HIS A 75 48.652 -3.320 -3.652 1.00 56.17 A C ANISOU 556 CB HIS A 75 6180 8957 6204 -372 -213 463 A C ATOM 557 CG HIS A 75 49.303 -3.344 -2.311 1.00 58.05 A C ANISOU 557 CG HIS A 75 6400 9293 6362 -412 -299 504 A C ATOM 558 CD2 HIS A 75 49.002 -2.690 -1.165 1.00 52.38 A C ANISOU 558 CD2 HIS A 75 5750 8581 5572 -574 -274 548 A C ATOM 559 ND1 HIS A 75 50.412 -4.111 -2.043 1.00 62.25 A N ANISOU 559 ND1 HIS A 75 6831 9941 6882 -276 -432 501 A N ATOM 560 CE1 HIS A 75 50.771 -3.927 -0.781 1.00 67.82 A C ANISOU 560 CE1 HIS A 75 7543 10729 7499 -351 -497 549 A C ATOM 561 NE2 HIS A 75 49.929 -3.072 -0.225 1.00 57.86 A N ANISOU 561 NE2 HIS A 75 6388 9404 6194 -538 -399 573 A N ATOM 562 N GLU A 76 51.823 -2.775 -4.088 1.00 65.53 A N ANISOU 562 N GLU A 76 6967 10618 7315 -292 -267 300 A N ATOM 563 CA GLU A 76 53.211 -3.202 -4.265 1.00 63.45 A C ANISOU 563 CA GLU A 76 6529 10519 7059 -172 -348 239 A C ATOM 564 C GLU A 76 53.419 -4.710 -4.067 1.00 69.00 A C ANISOU 564 C GLU A 76 7240 11156 7822 32 -502 286 A C ATOM 565 O GLU A 76 54.346 -5.303 -4.599 1.00 70.99 A O ANISOU 565 O GLU A 76 7361 11485 8127 175 -553 230 A O ATOM 566 CB GLU A 76 54.137 -2.430 -3.341 1.00 62.27 A C ANISOU 566 CB GLU A 76 6270 10563 6826 -283 -368 216 A C ATOM 567 CG GLU A 76 55.543 -2.369 -3.891 1.00 89.92 A C ANISOU 567 CG GLU A 76 9562 14257 10347 -211 -381 113 A C ATOM 568 CD GLU A 76 56.493 -1.600 -3.002 1.00115.24 A C ANISOU 568 CD GLU A 76 12643 17669 13474 -326 -404 75 A C ATOM 569 OE1 GLU A 76 56.018 -0.976 -2.023 1.00126.52 A O ANISOU 569 OE1 GLU A 76 14156 19093 14822 -483 -387 121 A O ATOM 570 OE2 GLU A 76 57.714 -1.622 -3.283 1.00118.36 A O1- ANISOU 570 OE2 GLU A 76 12851 18230 13891 -263 -434 -10 A O1- ATOM 571 N ASN A 77 52.546 -5.344 -3.310 1.00 68.08 A N ANISOU 571 N ASN A 77 7277 10883 7708 47 -565 388 A N ATOM 572 CA ASN A 77 52.696 -6.764 -3.097 1.00 67.14 A C ANISOU 572 CA ASN A 77 7176 10681 7652 238 -698 442 A C ATOM 573 C ASN A 77 51.701 -7.633 -3.870 1.00 67.84 A C ANISOU 573 C ASN A 77 7381 10556 7839 334 -669 450 A C ATOM 574 O ASN A 77 51.513 -8.800 -3.581 1.00 76.93 A O ANISOU 574 O ASN A 77 8594 11587 9050 468 -756 510 A O ATOM 575 CB ASN A 77 52.664 -7.014 -1.615 1.00 66.93 A C ANISOU 575 CB ASN A 77 7221 10653 7554 209 -808 554 A C ATOM 576 CG ASN A 77 53.707 -6.202 -0.907 1.00 73.55 A C ANISOU 576 CG ASN A 77 7928 11722 8293 117 -846 530 A C ATOM 577 ND2 ASN A 77 54.905 -6.215 -1.457 1.00 67.58 A N ANISOU 577 ND2 ASN A 77 6980 11128 7571 204 -874 447 A N ATOM 578 OD1 ASN A 77 53.445 -5.546 0.102 1.00 81.83 A O ANISOU 578 OD1 ASN A 77 9044 12808 9240 -39 -842 574 A O ATOM 579 N VAL A 78 51.083 -7.061 -4.883 1.00 59.73 A N ANISOU 579 N VAL A 78 6381 9486 6830 266 -545 387 A N ATOM 580 CA VAL A 78 50.215 -7.841 -5.719 1.00 61.15 A C ANISOU 580 CA VAL A 78 6649 9490 7096 351 -519 374 A C ATOM 581 C VAL A 78 50.709 -7.744 -7.140 1.00 66.84 A C ANISOU 581 C VAL A 78 7259 10286 7849 408 -452 258 A C ATOM 582 O VAL A 78 51.167 -6.696 -7.577 1.00 76.89 A O ANISOU 582 O VAL A 78 8447 11698 9068 314 -371 200 A O ATOM 583 CB VAL A 78 48.751 -7.381 -5.603 1.00 59.41 A C ANISOU 583 CB VAL A 78 6592 9112 6868 220 -442 419 A C ATOM 584 CG1 VAL A 78 47.866 -8.140 -6.592 1.00 57.46 A C ANISOU 584 CG1 VAL A 78 6419 8703 6711 302 -415 385 A C ATOM 585 CG2 VAL A 78 48.256 -7.594 -4.180 1.00 49.18 A C ANISOU 585 CG2 VAL A 78 5417 7727 5543 167 -501 529 A C ATOM 586 N VAL A 79 50.638 -8.853 -7.856 1.00 67.68 A N ANISOU 586 N VAL A 79 7370 10301 8046 559 -478 219 A N ATOM 587 CA VAL A 79 51.112 -8.888 -9.217 1.00 69.84 A C ANISOU 587 CA VAL A 79 7548 10642 8348 617 -414 101 A C ATOM 588 C VAL A 79 50.384 -7.777 -9.979 1.00 68.17 A C ANISOU 588 C VAL A 79 7385 10441 8075 471 -292 73 A C ATOM 589 O VAL A 79 49.367 -7.273 -9.524 1.00 65.16 A O ANISOU 589 O VAL A 79 7121 9971 7667 358 -266 142 A O ATOM 590 CB VAL A 79 50.872 -10.274 -9.819 1.00 74.64 A C ANISOU 590 CB VAL A 79 8185 11112 9062 779 -446 64 A C ATOM 591 CG1 VAL A 79 49.402 -10.462 -10.134 1.00 71.42 A C ANISOU 591 CG1 VAL A 79 7937 10524 8674 732 -408 84 A C ATOM 592 CG2 VAL A 79 51.719 -10.471 -11.045 1.00 77.72 A C ANISOU 592 CG2 VAL A 79 8446 11599 9484 862 -396 -65 A C ATOM 593 N ASN A 80 50.921 -7.367 -11.117 1.00 68.35 A N ANISOU 593 N ASN A 80 7318 10574 8078 472 -212 -25 A N ATOM 594 CA ASN A 80 50.416 -6.186 -11.804 1.00 58.88 A C ANISOU 594 CA ASN A 80 6149 9412 6810 334 -96 -38 A C ATOM 595 C ASN A 80 50.038 -6.428 -13.245 1.00 65.59 A C ANISOU 595 C ASN A 80 7019 10235 7666 375 -36 -115 A C ATOM 596 O ASN A 80 50.901 -6.588 -14.104 1.00 73.88 A O ANISOU 596 O ASN A 80 7970 11387 8715 438 0 -212 A O ATOM 597 CB ASN A 80 51.443 -5.062 -11.781 1.00 58.57 A C ANISOU 597 CB ASN A 80 5987 9562 6705 246 -27 -74 A C ATOM 598 CG ASN A 80 50.942 -3.805 -12.476 1.00 72.52 A C ANISOU 598 CG ASN A 80 7789 11358 8407 106 105 -75 A C ATOM 599 ND2 ASN A 80 51.513 -3.510 -13.646 1.00 72.71 A N ANISOU 599 ND2 ASN A 80 7740 11483 8403 120 189 -163 A N ATOM 600 OD1 ASN A 80 50.047 -3.106 -11.968 1.00 75.02 A O ANISOU 600 OD1 ASN A 80 8200 11603 8702 -13 137 4 A O ATOM 601 N LEU A 81 48.740 -6.416 -13.502 1.00 67.99 A N ANISOU 601 N LEU A 81 7451 10407 7974 330 -22 -76 A N ATOM 602 CA LEU A 81 48.211 -6.536 -14.844 1.00 65.71 A C ANISOU 602 CA LEU A 81 7196 10098 7672 346 29 -139 A C ATOM 603 C LEU A 81 48.462 -5.218 -15.536 1.00 65.74 A C ANISOU 603 C LEU A 81 7161 10232 7584 237 139 -151 A C ATOM 604 O LEU A 81 48.053 -4.177 -15.042 1.00 75.27 A O ANISOU 604 O LEU A 81 8404 11440 8757 113 183 -74 A O ATOM 605 CB LEU A 81 46.714 -6.821 -14.790 1.00 55.91 A C ANISOU 605 CB LEU A 81 6095 8683 6466 318 3 -85 A C ATOM 606 CG LEU A 81 46.030 -7.126 -16.112 1.00 63.78 A C ANISOU 606 CG LEU A 81 7134 9648 7452 342 28 -151 A C ATOM 607 CD1 LEU A 81 46.474 -8.473 -16.666 1.00 67.76 A C ANISOU 607 CD1 LEU A 81 7603 10129 8013 486 -11 -256 A C ATOM 608 CD2 LEU A 81 44.547 -7.126 -15.870 1.00 71.00 A C ANISOU 608 CD2 LEU A 81 8171 10405 8402 285 6 -85 A C ATOM 609 N ILE A 82 49.170 -5.272 -16.659 1.00 65.18 A N ANISOU 609 N ILE A 82 7019 10269 7477 281 194 -249 A N ATOM 610 CA ILE A 82 49.542 -4.091 -17.424 1.00 65.36 A C ANISOU 610 CA ILE A 82 7003 10421 7410 190 311 -267 A C ATOM 611 C ILE A 82 48.470 -3.792 -18.444 1.00 65.16 A C ANISOU 611 C ILE A 82 7077 10350 7332 147 351 -250 A C ATOM 612 O ILE A 82 48.092 -2.641 -18.648 1.00 61.75 A O ANISOU 612 O ILE A 82 6676 9946 6841 38 429 -187 A O ATOM 613 CB ILE A 82 50.832 -4.340 -18.221 1.00 62.17 A C ANISOU 613 CB ILE A 82 6478 10155 6989 258 361 -390 A C ATOM 614 CG1 ILE A 82 51.995 -4.572 -17.290 1.00 63.04 A C ANISOU 614 CG1 ILE A 82 6465 10334 7154 304 319 -413 A C ATOM 615 CG2 ILE A 82 51.155 -3.171 -19.142 1.00 55.35 A C ANISOU 615 CG2 ILE A 82 5591 9414 6026 164 497 -412 A C ATOM 616 CD1 ILE A 82 53.192 -5.015 -18.045 1.00 70.28 A C ANISOU 616 CD1 ILE A 82 7257 11359 8085 390 358 -541 A C ATOM 617 N GLU A 83 48.023 -4.846 -19.116 1.00 65.12 A N ANISOU 617 N GLU A 83 7113 10279 7351 237 301 -310 A N ATOM 618 CA GLU A 83 47.059 -4.726 -20.189 1.00 70.73 A C ANISOU 618 CA GLU A 83 7907 10962 8005 210 320 -311 A C ATOM 619 C GLU A 83 46.560 -6.103 -20.573 1.00 74.05 A C ANISOU 619 C GLU A 83 8368 11286 8481 312 244 -386 A C ATOM 620 O GLU A 83 47.057 -7.108 -20.069 1.00 71.94 A O ANISOU 620 O GLU A 83 8061 10974 8300 407 191 -435 A O ATOM 621 CB GLU A 83 47.676 -4.034 -21.404 1.00 67.14 A C ANISOU 621 CB GLU A 83 7413 10659 7437 177 427 -366 A C ATOM 622 CG GLU A 83 48.768 -4.807 -22.086 1.00 72.18 A C ANISOU 622 CG GLU A 83 7968 11385 8071 268 450 -507 A C ATOM 623 CD GLU A 83 49.297 -4.065 -23.289 1.00 81.13 A C ANISOU 623 CD GLU A 83 9080 12662 9082 220 569 -556 A C ATOM 624 OE1 GLU A 83 48.561 -3.213 -23.830 1.00 88.09 A O ANISOU 624 OE1 GLU A 83 10038 13556 9877 138 609 -482 A O ATOM 625 OE2 GLU A 83 50.445 -4.323 -23.695 1.00 80.57 A O1- ANISOU 625 OE2 GLU A 83 8918 12689 9006 264 625 -664 A O1- ATOM 626 N ILE A 84 45.555 -6.135 -21.442 1.00 72.18 A N ANISOU 626 N ILE A 84 8209 11015 8201 289 237 -391 A N ATOM 627 CA ILE A 84 45.066 -7.376 -22.014 1.00 62.04 A C ANISOU 627 CA ILE A 84 6961 9657 6956 370 182 -485 A C ATOM 628 C ILE A 84 45.205 -7.249 -23.518 1.00 62.19 A C ANISOU 628 C ILE A 84 6979 9796 6855 361 238 -573 A C ATOM 629 O ILE A 84 44.981 -6.179 -24.069 1.00 69.35 A O ANISOU 629 O ILE A 84 7909 10785 7656 278 289 -514 A O ATOM 630 CB ILE A 84 43.619 -7.631 -21.600 1.00 63.33 A C ANISOU 630 CB ILE A 84 7220 9661 7181 344 110 -421 A C ATOM 631 CG1 ILE A 84 43.595 -8.350 -20.251 1.00 65.17 A C ANISOU 631 CG1 ILE A 84 7460 9755 7545 393 49 -385 A C ATOM 632 CG2 ILE A 84 42.897 -8.458 -22.636 1.00 64.68 A C ANISOU 632 CG2 ILE A 84 7435 9799 7340 379 78 -518 A C ATOM 633 CD1 ILE A 84 42.549 -7.814 -19.325 1.00 64.34 A C ANISOU 633 CD1 ILE A 84 7428 9533 7485 312 23 -260 A C ATOM 634 N CYS A 85 45.621 -8.321 -24.182 1.00 59.96 A N ANISOU 634 N CYS A 85 6669 9524 6587 444 238 -713 A N ATOM 635 CA CYS A 85 45.976 -8.224 -25.589 1.00 59.61 A C ANISOU 635 CA CYS A 85 6617 9613 6418 433 306 -814 A C ATOM 636 C CYS A 85 45.250 -9.270 -26.389 1.00 70.77 A C ANISOU 636 C CYS A 85 8083 10974 7832 470 264 -923 A C ATOM 637 O CYS A 85 44.877 -10.323 -25.858 1.00 76.82 A O ANISOU 637 O CYS A 85 8860 11602 8726 535 202 -960 A O ATOM 638 CB CYS A 85 47.477 -8.432 -25.763 1.00 74.13 A C ANISOU 638 CB CYS A 85 8350 11552 8265 487 383 -913 A C ATOM 639 SG CYS A 85 48.464 -7.042 -25.268 1.00 71.36 A S ANISOU 639 SG CYS A 85 7925 11321 7867 419 465 -826 A S ATOM 640 N ARG A 86 45.070 -8.985 -27.674 1.00 70.77 A N ANISOU 640 N ARG A 86 8116 11086 7686 424 303 -978 A N ATOM 641 CA ARG A 86 44.414 -9.916 -28.576 1.00 72.19 A C ANISOU 641 CA ARG A 86 8344 11246 7841 443 270 -1100 A C ATOM 642 C ARG A 86 45.369 -10.446 -29.664 1.00 79.50 A C ANISOU 642 C ARG A 86 9228 12285 8694 473 357 -1274 A C ATOM 643 O ARG A 86 46.576 -10.203 -29.618 1.00 76.63 A O ANISOU 643 O ARG A 86 8788 11997 8329 494 440 -1302 A O ATOM 644 CB ARG A 86 43.202 -9.242 -29.207 1.00 68.96 A C ANISOU 644 CB ARG A 86 8019 10871 7313 359 223 -1025 A C ATOM 645 CG ARG A 86 43.518 -7.903 -29.815 1.00 71.70 A C ANISOU 645 CG ARG A 86 8375 11370 7496 284 291 -938 A C ATOM 646 CD ARG A 86 42.413 -7.429 -30.744 1.00 83.64 A C ANISOU 646 CD ARG A 86 9968 12940 8872 219 243 -890 A C ATOM 647 NE ARG A 86 42.817 -6.160 -31.323 1.00100.11 A N ANISOU 647 NE ARG A 86 12067 15166 10804 155 322 -798 A N ATOM 648 CZ ARG A 86 43.297 -6.021 -32.550 1.00109.62 A C ANISOU 648 CZ ARG A 86 13290 16523 11836 131 390 -872 A C ATOM 649 NH1 ARG A 86 43.385 -7.080 -33.342 1.00120.80 A N1+ ANISOU 649 NH1 ARG A 86 14713 17975 13211 161 383 -1047 A N1+ ATOM 650 NH2 ARG A 86 43.672 -4.822 -32.988 1.00104.47 A N ANISOU 650 NH2 ARG A 86 12656 15984 11054 73 473 -773 A N ATOM 651 N THR A 87 44.817 -11.151 -30.648 1.00 81.59 A N ANISOU 651 N THR A 87 9538 12563 8899 467 343 -1397 A N ATOM 652 CA THR A 87 45.628 -11.802 -31.660 1.00 89.76 A C ANISOU 652 CA THR A 87 10540 13685 9879 492 430 -1582 A C ATOM 653 C THR A 87 45.356 -11.358 -33.092 1.00106.94 A C ANISOU 653 C THR A 87 12779 16021 11831 409 466 -1634 A C ATOM 654 O THR A 87 46.294 -11.060 -33.831 1.00113.09 A O ANISOU 654 O THR A 87 13533 16932 12503 389 574 -1703 A O ATOM 655 CB THR A 87 45.425 -13.305 -31.616 1.00 95.02 A C ANISOU 655 CB THR A 87 11194 14223 10684 566 407 -1733 A C ATOM 656 CG2 THR A 87 46.416 -13.976 -32.519 1.00 97.41 A C ANISOU 656 CG2 THR A 87 11447 14601 10962 596 517 -1928 A C ATOM 657 OG1 THR A 87 45.616 -13.773 -30.279 1.00101.59 A O ANISOU 657 OG1 THR A 87 11980 14899 11720 648 366 -1672 A O ATOM 658 N LYS A 88 44.079 -11.351 -33.474 1.00120.36 A N ANISOU 658 N LYS A 88 14559 17710 13463 360 375 -1605 A N ATOM 659 CA LYS A 88 43.633 -11.115 -34.858 1.00131.87 A C ANISOU 659 CA LYS A 88 16085 19316 14702 286 379 -1661 A C ATOM 660 C LYS A 88 43.534 -12.429 -35.650 1.00129.45 A C ANISOU 660 C LYS A 88 15785 19005 14394 301 391 -1888 A C ATOM 661 O LYS A 88 42.590 -12.647 -36.420 1.00123.91 A O ANISOU 661 O LYS A 88 15145 18349 13584 250 326 -1940 A O ATOM 662 CB LYS A 88 44.544 -10.121 -35.593 1.00139.88 A C ANISOU 662 CB LYS A 88 17103 20507 15539 236 491 -1632 A C ATOM 663 CG LYS A 88 45.618 -10.790 -36.448 1.00147.22 A C ANISOU 663 CG LYS A 88 17998 21521 16416 249 616 -1837 A C ATOM 664 CD LYS A 88 46.884 -9.949 -36.522 1.00150.32 A C ANISOU 664 CD LYS A 88 18346 22016 16755 236 749 -1805 A C ATOM 665 CE LYS A 88 47.982 -10.678 -37.281 1.00154.02 A C ANISOU 665 CE LYS A 88 18766 22548 17205 254 883 -2020 A C ATOM 666 NZ LYS A 88 49.248 -9.892 -37.345 1.00156.61 A N1+ ANISOU 666 NZ LYS A 88 19038 22970 17496 239 1022 -2004 A N1+ ATOM 667 N LYS A 96 40.752 -18.336 -34.981 1.00146.54 A N ANISOU 667 N LYS A 96 17946 20512 17219 456 234 -2520 A N ATOM 668 CA LYS A 96 39.873 -18.405 -33.814 1.00148.07 A C ANISOU 668 CA LYS A 96 18155 20527 17579 484 141 -2391 A C ATOM 669 C LYS A 96 39.926 -17.135 -32.964 1.00144.67 A C ANISOU 669 C LYS A 96 17727 20113 17130 481 91 -2143 A C ATOM 670 O LYS A 96 38.889 -16.633 -32.515 1.00144.67 A O ANISOU 670 O LYS A 96 17763 20064 17140 442 -4 -2016 A O ATOM 671 CB LYS A 96 40.211 -19.620 -32.942 1.00148.49 A C ANISOU 671 CB LYS A 96 18169 20363 17887 587 187 -2462 A C ATOM 672 CG LYS A 96 39.907 -20.952 -33.601 1.00150.74 A C ANISOU 672 CG LYS A 96 18456 20580 18238 586 235 -2703 A C ATOM 673 CD LYS A 96 39.909 -22.099 -32.599 1.00147.64 A C ANISOU 673 CD LYS A 96 18044 19936 18118 684 262 -2734 A C ATOM 674 CE LYS A 96 39.490 -23.400 -33.280 1.00145.84 A C ANISOU 674 CE LYS A 96 17820 19630 17961 669 319 -2980 A C ATOM 675 NZ LYS A 96 39.243 -24.514 -32.322 1.00143.80 A N1+ ANISOU 675 NZ LYS A 96 17559 19107 17971 753 342 -3002 A N1+ ATOM 676 N GLY A 97 41.137 -16.628 -32.746 1.00135.66 A N ANISOU 676 N GLY A 97 16540 19036 15969 519 164 -2085 A N ATOM 677 CA GLY A 97 41.341 -15.469 -31.897 1.00129.16 A C ANISOU 677 CA GLY A 97 15710 18225 15141 515 138 -1869 A C ATOM 678 C GLY A 97 41.715 -15.894 -30.490 1.00128.38 A C ANISOU 678 C GLY A 97 15572 17950 15257 604 135 -1798 A C ATOM 679 O GLY A 97 41.195 -16.888 -29.987 1.00137.52 A O ANISOU 679 O GLY A 97 16740 18939 16571 648 105 -1850 A O ATOM 680 N SER A 98 42.623 -15.151 -29.858 1.00115.81 A N ANISOU 680 N SER A 98 13935 16399 13669 627 166 -1681 A N ATOM 681 CA SER A 98 43.100 -15.478 -28.512 1.00 98.68 A C ANISOU 681 CA SER A 98 11723 14090 11680 710 156 -1603 A C ATOM 682 C SER A 98 43.183 -14.223 -27.651 1.00 88.93 A C ANISOU 682 C SER A 98 10487 12887 10414 670 129 -1403 A C ATOM 683 O SER A 98 43.320 -13.114 -28.166 1.00 86.63 A O ANISOU 683 O SER A 98 10201 12744 9972 598 154 -1343 A O ATOM 684 CB SER A 98 44.487 -16.125 -28.563 1.00 94.97 A C ANISOU 684 CB SER A 98 11165 13637 11283 802 241 -1709 A C ATOM 685 OG SER A 98 44.478 -17.375 -29.220 1.00 98.88 A O ANISOU 685 OG SER A 98 11654 14074 11843 846 282 -1899 A O ATOM 686 N ILE A 99 43.120 -14.407 -26.338 1.00 77.94 A N ANISOU 686 N ILE A 99 9092 11356 9166 714 87 -1302 A N ATOM 687 CA ILE A 99 43.255 -13.300 -25.412 1.00 73.50 A C ANISOU 687 CA ILE A 99 8525 10814 8588 674 69 -1127 A C ATOM 688 C ILE A 99 44.377 -13.554 -24.419 1.00 83.34 A C ANISOU 688 C ILE A 99 9697 12029 9939 756 83 -1094 A C ATOM 689 O ILE A 99 44.424 -14.605 -23.781 1.00 89.62 A O ANISOU 689 O ILE A 99 10487 12684 10879 843 56 -1121 A O ATOM 690 CB ILE A 99 41.965 -13.075 -24.632 1.00 71.93 A C ANISOU 690 CB ILE A 99 8402 10482 8445 624 -5 -1009 A C ATOM 691 CG1 ILE A 99 40.929 -12.412 -25.529 1.00 67.48 A C ANISOU 691 CG1 ILE A 99 7894 9985 7761 530 -27 -996 A C ATOM 692 CG2 ILE A 99 42.227 -12.235 -23.382 1.00 79.51 A C ANISOU 692 CG2 ILE A 99 9352 11420 9437 600 -16 -845 A C ATOM 693 CD1 ILE A 99 41.480 -11.304 -26.359 1.00 72.27 A C ANISOU 693 CD1 ILE A 99 8477 10785 8195 473 26 -969 A C ATOM 694 N TYR A 100 45.276 -12.585 -24.282 1.00 76.84 A N ANISOU 694 N TYR A 100 8815 11336 9045 729 124 -1034 A N ATOM 695 CA TYR A 100 46.384 -12.705 -23.350 1.00 67.46 A C ANISOU 695 CA TYR A 100 7542 10146 7942 798 128 -1000 A C ATOM 696 C TYR A 100 46.290 -11.631 -22.239 1.00 71.27 A C ANISOU 696 C TYR A 100 8035 10636 8410 731 98 -831 A C ATOM 697 O TYR A 100 46.037 -10.449 -22.513 1.00 65.42 A O ANISOU 697 O TYR A 100 7315 9985 7556 629 129 -765 A O ATOM 698 CB TYR A 100 47.706 -12.577 -24.102 1.00 62.82 A C ANISOU 698 CB TYR A 100 6853 9713 7303 827 214 -1103 A C ATOM 699 CG TYR A 100 48.012 -13.679 -25.110 1.00 78.73 A C ANISOU 699 CG TYR A 100 8842 11724 9349 897 261 -1284 A C ATOM 700 CD1 TYR A 100 48.700 -14.834 -24.735 1.00 82.09 A C ANISOU 700 CD1 TYR A 100 9197 12061 9931 1023 260 -1357 A C ATOM 701 CD2 TYR A 100 47.660 -13.545 -26.444 1.00 82.03 A C ANISOU 701 CD2 TYR A 100 9302 12228 9638 836 313 -1383 A C ATOM 702 CE1 TYR A 100 48.996 -15.830 -25.654 1.00 80.33 A C ANISOU 702 CE1 TYR A 100 8947 11824 9749 1082 321 -1532 A C ATOM 703 CE2 TYR A 100 47.957 -14.537 -27.372 1.00 87.49 A C ANISOU 703 CE2 TYR A 100 9972 12921 10351 887 368 -1562 A C ATOM 704 CZ TYR A 100 48.624 -15.675 -26.972 1.00 91.64 A C ANISOU 704 CZ TYR A 100 10426 13347 11047 1008 379 -1642 A C ATOM 705 OH TYR A 100 48.913 -16.657 -27.900 1.00101.78 A O ANISOU 705 OH TYR A 100 11685 14621 12365 1052 450 -1829 A O ATOM 706 N LEU A 101 46.456 -12.070 -20.991 1.00 66.09 A N ANISOU 706 N LEU A 101 7369 9876 7867 786 42 -762 A N ATOM 707 CA LEU A 101 46.660 -11.197 -19.837 1.00 64.97 A C ANISOU 707 CA LEU A 101 7216 9753 7718 733 20 -625 A C ATOM 708 C LEU A 101 48.149 -10.905 -19.694 1.00 66.34 A C ANISOU 708 C LEU A 101 7260 10065 7879 770 55 -651 A C ATOM 709 O LEU A 101 48.929 -11.836 -19.529 1.00 66.03 A O ANISOU 709 O LEU A 101 7151 10006 7931 885 37 -711 A O ATOM 710 CB LEU A 101 46.209 -11.897 -18.552 1.00 64.93 A C ANISOU 710 CB LEU A 101 7261 9579 7829 779 -59 -544 A C ATOM 711 CG LEU A 101 44.733 -11.825 -18.175 1.00 63.64 A C ANISOU 711 CG LEU A 101 7223 9273 7686 709 -94 -470 A C ATOM 712 CD1 LEU A 101 43.941 -12.417 -19.272 1.00 67.52 A C ANISOU 712 CD1 LEU A 101 7760 9715 8179 719 -84 -571 A C ATOM 713 CD2 LEU A 101 44.482 -12.574 -16.895 1.00 57.64 A C ANISOU 713 CD2 LEU A 101 6510 8352 7038 761 -157 -396 A C ATOM 714 N VAL A 102 48.536 -9.628 -19.723 1.00 61.51 A N ANISOU 714 N VAL A 102 6614 9587 7170 674 109 -605 A N ATOM 715 CA VAL A 102 49.942 -9.230 -19.699 1.00 56.21 A C ANISOU 715 CA VAL A 102 5812 9064 6482 690 156 -644 A C ATOM 716 C VAL A 102 50.377 -8.693 -18.329 1.00 66.12 A C ANISOU 716 C VAL A 102 7024 10339 7760 660 114 -540 A C ATOM 717 O VAL A 102 49.856 -7.689 -17.870 1.00 75.79 A O ANISOU 717 O VAL A 102 8301 11570 8928 545 128 -445 A O ATOM 718 CB VAL A 102 50.206 -8.178 -20.778 1.00 58.59 A C ANISOU 718 CB VAL A 102 6094 9513 6655 600 266 -685 A C ATOM 719 CG1 VAL A 102 51.686 -8.001 -21.009 1.00 67.57 A C ANISOU 719 CG1 VAL A 102 7089 10794 7789 631 332 -769 A C ATOM 720 CG2 VAL A 102 49.550 -8.596 -22.062 1.00 58.52 A C ANISOU 720 CG2 VAL A 102 6155 9487 6595 606 294 -767 A C ATOM 721 N PHE A 103 51.334 -9.358 -17.680 1.00 72.47 A N ANISOU 721 N PHE A 103 7732 11155 8648 761 63 -559 A N ATOM 722 CA PHE A 103 51.845 -8.921 -16.365 1.00 77.77 A C ANISOU 722 CA PHE A 103 8353 11866 9331 737 9 -468 A C ATOM 723 C PHE A 103 53.266 -8.333 -16.400 1.00 76.28 A C ANISOU 723 C PHE A 103 8003 11860 9120 731 55 -524 A C ATOM 724 O PHE A 103 54.042 -8.672 -17.288 1.00 78.75 A O ANISOU 724 O PHE A 103 8225 12242 9454 796 109 -641 A O ATOM 725 CB PHE A 103 51.864 -10.098 -15.396 1.00 76.72 A C ANISOU 725 CB PHE A 103 8229 11614 9309 858 -105 -422 A C ATOM 726 CG PHE A 103 50.522 -10.683 -15.120 1.00 79.98 A C ANISOU 726 CG PHE A 103 8794 11837 9758 859 -150 -360 A C ATOM 727 CD1 PHE A 103 49.755 -10.221 -14.070 1.00 86.83 A C ANISOU 727 CD1 PHE A 103 9756 12634 10601 771 -190 -237 A C ATOM 728 CD2 PHE A 103 50.031 -11.701 -15.895 1.00 74.20 A C ANISOU 728 CD2 PHE A 103 8109 10995 9088 940 -145 -435 A C ATOM 729 CE1 PHE A 103 48.516 -10.764 -13.807 1.00 84.50 A C ANISOU 729 CE1 PHE A 103 9598 12158 10349 768 -223 -187 A C ATOM 730 CE2 PHE A 103 48.790 -12.241 -15.635 1.00 78.59 A C ANISOU 730 CE2 PHE A 103 8799 11376 9687 935 -181 -388 A C ATOM 731 CZ PHE A 103 48.037 -11.775 -14.584 1.00 76.68 A C ANISOU 731 CZ PHE A 103 8648 11061 9427 851 -219 -263 A C ATOM 732 N ASP A 104 53.611 -7.476 -15.430 1.00 73.46 A N ANISOU 732 N ASP A 104 7607 11579 8727 648 41 -453 A N ATOM 733 CA ASP A 104 55.016 -7.079 -15.220 1.00 69.39 A C ANISOU 733 CA ASP A 104 6922 11231 8215 655 59 -507 A C ATOM 734 C ASP A 104 55.761 -8.338 -14.816 1.00 78.35 A C ANISOU 734 C ASP A 104 7963 12340 9466 825 -43 -533 A C ATOM 735 O ASP A 104 55.370 -9.007 -13.867 1.00 85.27 A O ANISOU 735 O ASP A 104 8897 13111 10391 883 -155 -444 A O ATOM 736 CB ASP A 104 55.165 -6.044 -14.099 1.00 73.43 A C ANISOU 736 CB ASP A 104 7414 11817 8670 532 45 -425 A C ATOM 737 CG ASP A 104 54.999 -4.592 -14.582 1.00 90.77 A C ANISOU 737 CG ASP A 104 9627 14095 10767 366 183 -431 A C ATOM 738 OD1 ASP A 104 55.378 -4.294 -15.739 1.00 88.49 A O ANISOU 738 OD1 ASP A 104 9295 13877 10449 358 291 -521 A O ATOM 739 OD2 ASP A 104 54.509 -3.740 -13.786 1.00 95.10 A O1- ANISOU 739 OD2 ASP A 104 10233 14634 11267 240 191 -346 A O1- ATOM 740 N PHE A 105 56.833 -8.668 -15.526 1.00 82.16 A N ANISOU 740 N PHE A 105 8305 12911 9999 907 1 -653 A N ATOM 741 CA PHE A 105 57.588 -9.875 -15.222 1.00 85.39 A C ANISOU 741 CA PHE A 105 8611 13291 10541 1081 -87 -681 A C ATOM 742 C PHE A 105 58.310 -9.818 -13.868 1.00 85.44 A C ANISOU 742 C PHE A 105 8519 13368 10575 1108 -205 -602 A C ATOM 743 O PHE A 105 58.667 -8.739 -13.367 1.00 77.16 A O ANISOU 743 O PHE A 105 7420 12450 9447 989 -190 -580 A O ATOM 744 CB PHE A 105 58.583 -10.160 -16.334 1.00 90.93 A C ANISOU 744 CB PHE A 105 9176 14075 11299 1150 5 -839 A C ATOM 745 CG PHE A 105 59.228 -11.503 -16.232 1.00 92.35 A C ANISOU 745 CG PHE A 105 9258 14193 11638 1340 -63 -879 A C ATOM 746 CD1 PHE A 105 58.499 -12.655 -16.458 1.00 93.16 A C ANISOU 746 CD1 PHE A 105 9461 14117 11817 1439 -93 -874 A C ATOM 747 CD2 PHE A 105 60.573 -11.620 -15.930 1.00 88.59 A C ANISOU 747 CD2 PHE A 105 8582 13832 11247 1419 -92 -927 A C ATOM 748 CE1 PHE A 105 59.112 -13.910 -16.375 1.00 93.12 A C ANISOU 748 CE1 PHE A 105 9365 14040 11978 1620 -142 -910 A C ATOM 749 CE2 PHE A 105 61.177 -12.870 -15.844 1.00 83.03 A C ANISOU 749 CE2 PHE A 105 7779 13061 10709 1605 -152 -958 A C ATOM 750 CZ PHE A 105 60.452 -14.009 -16.061 1.00 77.89 A C ANISOU 750 CZ PHE A 105 7234 12222 10137 1706 -174 -946 A C ATOM 751 N CYS A 106 58.512 -11.003 -13.296 1.00 84.78 A N ANISOU 751 N CYS A 106 8411 13198 10605 1266 -320 -560 A N ATOM 752 CA CYS A 106 59.123 -11.175 -11.986 1.00 91.94 A C ANISOU 752 CA CYS A 106 9238 14155 11540 1319 -459 -467 A C ATOM 753 C CYS A 106 60.027 -12.391 -12.103 1.00107.80 A C ANISOU 753 C CYS A 106 11110 16139 13709 1523 -518 -512 A C ATOM 754 O CYS A 106 59.564 -13.469 -12.481 1.00109.05 A O ANISOU 754 O CYS A 106 11339 16135 13962 1637 -520 -518 A O ATOM 755 CB CYS A 106 58.050 -11.433 -10.920 1.00 93.05 A C ANISOU 755 CB CYS A 106 9553 14157 11644 1297 -557 -310 A C ATOM 756 SG CYS A 106 56.800 -10.093 -10.676 1.00 99.82 A S ANISOU 756 SG CYS A 106 10587 15001 12339 1060 -487 -244 A S ATOM 757 N GLU A 107 61.313 -12.230 -11.795 1.00112.43 A N ANISOU 757 N GLU A 107 11495 16884 14340 1571 -560 -550 A N ATOM 758 CA GLU A 107 62.284 -13.290 -12.070 1.00112.56 A C ANISOU 758 CA GLU A 107 11351 16889 14528 1764 -593 -614 A C ATOM 759 C GLU A 107 62.090 -14.584 -11.261 1.00108.56 A C ANISOU 759 C GLU A 107 10886 16228 14133 1939 -736 -490 A C ATOM 760 O GLU A 107 62.292 -15.682 -11.786 1.00107.22 A O ANISOU 760 O GLU A 107 10678 15945 14117 2095 -720 -540 A O ATOM 761 CB GLU A 107 63.716 -12.765 -11.930 1.00124.15 A C ANISOU 761 CB GLU A 107 12576 18569 16025 1770 -606 -688 A C ATOM 762 CG GLU A 107 64.813 -13.843 -11.973 1.00137.95 A C ANISOU 762 CG GLU A 107 14131 20315 17969 1981 -667 -733 A C ATOM 763 CD GLU A 107 64.976 -14.505 -13.340 1.00144.28 A C ANISOU 763 CD GLU A 107 14897 21033 18890 2063 -526 -886 A C ATOM 764 OE1 GLU A 107 64.297 -14.081 -14.301 1.00147.47 A O ANISOU 764 OE1 GLU A 107 15421 21403 19208 1950 -383 -964 A O ATOM 765 OE2 GLU A 107 65.790 -15.452 -13.451 1.00141.96 A O1- ANISOU 765 OE2 GLU A 107 14453 20708 18777 2240 -556 -930 A O1- ATOM 766 N HIS A 108 61.688 -14.467 -9.999 1.00102.92 A N ANISOU 766 N HIS A 108 10258 15502 13346 1909 -865 -331 A N ATOM 767 CA HIS A 108 61.679 -15.632 -9.124 1.00108.07 A C ANISOU 767 CA HIS A 108 10933 16031 14098 2078 -1009 -199 A C ATOM 768 C HIS A 108 60.321 -15.915 -8.537 1.00108.30 A C ANISOU 768 C HIS A 108 11206 15880 14064 2035 -1041 -67 A C ATOM 769 O HIS A 108 59.513 -15.010 -8.368 1.00113.52 A O ANISOU 769 O HIS A 108 11996 16557 14580 1857 -1000 -41 A O ATOM 770 CB HIS A 108 62.646 -15.442 -7.948 1.00116.96 A C ANISOU 770 CB HIS A 108 11916 17316 15207 2118 -1169 -109 A C ATOM 771 CG HIS A 108 64.008 -14.958 -8.344 1.00122.61 A C ANISOU 771 CG HIS A 108 12377 18240 15969 2130 -1147 -236 A C ATOM 772 CD2 HIS A 108 65.004 -15.565 -9.030 1.00121.39 A C ANISOU 772 CD2 HIS A 108 12031 18108 15985 2278 -1117 -345 A C ATOM 773 ND1 HIS A 108 64.470 -13.702 -8.021 1.00127.73 A N ANISOU 773 ND1 HIS A 108 12941 19100 16490 1971 -1143 -270 A N ATOM 774 CE1 HIS A 108 65.697 -13.551 -8.494 1.00127.99 A C ANISOU 774 CE1 HIS A 108 12739 19280 16610 2019 -1114 -397 A C ATOM 775 NE2 HIS A 108 66.040 -14.663 -9.112 1.00127.43 A N ANISOU 775 NE2 HIS A 108 12599 19099 16721 2205 -1098 -444 A N ATOM 776 N ASP A 109 60.082 -17.175 -8.196 1.00 96.87 A N ANISOU 776 N ASP A 109 11916 11406 13485 1971 -3317 530 A N ATOM 777 CA ASP A 109 58.998 -17.495 -7.282 1.00104.28 A C ANISOU 777 CA ASP A 109 13081 12142 14399 1685 -3277 569 A C ATOM 778 C ASP A 109 59.508 -18.280 -6.075 1.00108.87 A C ANISOU 778 C ASP A 109 13903 12489 14974 1618 -3436 721 A C ATOM 779 O ASP A 109 60.619 -18.807 -6.081 1.00116.72 A O ANISOU 779 O ASP A 109 14900 13450 15999 1820 -3595 767 A O ATOM 780 CB ASP A 109 57.845 -18.215 -7.978 1.00109.98 A C ANISOU 780 CB ASP A 109 13838 12757 15192 1654 -3226 396 A C ATOM 781 CG ASP A 109 58.222 -19.573 -8.456 1.00117.75 A C ANISOU 781 CG ASP A 109 14899 13550 16288 1844 -3386 307 A C ATOM 782 OD1 ASP A 109 58.938 -19.651 -9.476 1.00120.44 A O ANISOU 782 OD1 ASP A 109 15071 14022 16668 2125 -3437 213 A O ATOM 783 OD2 ASP A 109 57.801 -20.557 -7.813 1.00121.45 A O1- ANISOU 783 OD2 ASP A 109 15603 13736 16808 1716 -3452 334 A O1- ATOM 784 N LEU A 110 58.683 -18.339 -5.039 1.00108.50 A N ANISOU 784 N LEU A 110 14056 12294 14877 1344 -3386 807 A N ATOM 785 CA LEU A 110 59.103 -18.809 -3.731 1.00108.48 A C ANISOU 785 CA LEU A 110 14279 12113 14824 1251 -3504 986 A C ATOM 786 C LEU A 110 59.238 -20.325 -3.709 1.00111.85 A C ANISOU 786 C LEU A 110 14897 12252 15351 1353 -3650 982 A C ATOM 787 O LEU A 110 59.877 -20.887 -2.823 1.00109.10 A O ANISOU 787 O LEU A 110 14718 11759 14974 1377 -3783 1130 A O ATOM 788 CB LEU A 110 58.101 -18.349 -2.669 1.00104.66 A C ANISOU 788 CB LEU A 110 13945 11577 14246 928 -3382 1077 A C ATOM 789 CG LEU A 110 58.568 -18.327 -1.217 1.00103.10 A C ANISOU 789 CG LEU A 110 13933 11303 13938 813 -3464 1280 A C ATOM 790 CD1 LEU A 110 59.656 -17.279 -1.039 1.00105.09 A C ANISOU 790 CD1 LEU A 110 14020 11801 14110 894 -3500 1338 A C ATOM 791 CD2 LEU A 110 57.394 -18.059 -0.291 1.00 94.36 A C ANISOU 791 CD2 LEU A 110 12988 10119 12747 503 -3330 1348 A C ATOM 792 N ALA A 111 58.626 -20.990 -4.680 1.00114.70 A N ANISOU 792 N ALA A 111 15232 12524 15825 1417 -3624 809 A N ATOM 793 CA ALA A 111 58.769 -22.436 -4.781 1.00114.44 A C ANISOU 793 CA ALA A 111 15373 12202 15907 1529 -3755 780 A C ATOM 794 C ALA A 111 60.139 -22.756 -5.358 1.00113.57 A C ANISOU 794 C ALA A 111 15158 12160 15835 1869 -3912 766 A C ATOM 795 O ALA A 111 60.837 -23.648 -4.863 1.00110.79 A O ANISOU 795 O ALA A 111 14970 11616 15509 1984 -4063 866 A O ATOM 796 CB ALA A 111 57.674 -23.020 -5.646 1.00112.73 A C ANISOU 796 CB ALA A 111 15151 11877 15803 1479 -3679 575 A C ATOM 797 N GLY A 112 60.510 -22.016 -6.404 1.00113.56 A N ANISOU 797 N GLY A 112 14882 12438 15830 2038 -3868 651 A N ATOM 798 CA GLY A 112 61.812 -22.149 -7.033 1.00118.45 A C ANISOU 798 CA GLY A 112 15355 13177 16474 2364 -3993 635 A C ATOM 799 C GLY A 112 62.956 -21.914 -6.058 1.00122.70 A C ANISOU 799 C GLY A 112 15928 13761 16932 2408 -4109 836 A C ATOM 800 O GLY A 112 63.952 -22.645 -6.052 1.00126.43 A O ANISOU 800 O GLY A 112 16437 14164 17437 2639 -4271 880 A O ATOM 801 N LEU A 113 62.807 -20.897 -5.217 1.00116.95 A N ANISOU 801 N LEU A 113 15188 13155 16093 2191 -4030 954 A N ATOM 802 CA LEU A 113 63.850 -20.553 -4.260 1.00116.82 A C ANISOU 802 CA LEU A 113 15183 13217 15986 2209 -4137 1128 A C ATOM 803 C LEU A 113 63.912 -21.495 -3.051 1.00116.40 A C ANISOU 803 C LEU A 113 15430 12897 15901 2141 -4262 1285 A C ATOM 804 O LEU A 113 64.988 -21.776 -2.528 1.00115.68 A O ANISOU 804 O LEU A 113 15366 12816 15770 2288 -4418 1401 A O ATOM 805 CB LEU A 113 63.704 -19.094 -3.820 1.00113.80 A C ANISOU 805 CB LEU A 113 14676 13066 15498 2007 -4007 1180 A C ATOM 806 CG LEU A 113 63.878 -18.123 -4.987 1.00112.61 A C ANISOU 806 CG LEU A 113 14220 13191 15374 2115 -3889 1059 A C ATOM 807 CD1 LEU A 113 64.069 -16.709 -4.491 1.00109.97 A C ANISOU 807 CD1 LEU A 113 13761 13075 14947 1958 -3790 1129 A C ATOM 808 CD2 LEU A 113 65.055 -18.551 -5.863 1.00113.10 A C ANISOU 808 CD2 LEU A 113 14120 13347 15508 2456 -4012 1010 A C ATOM 809 N LEU A 114 62.759 -21.987 -2.616 1.00117.02 A N ANISOU 809 N LEU A 114 15726 12743 15995 1925 -4188 1292 A N ATOM 810 CA LEU A 114 62.702 -22.875 -1.465 1.00121.62 A C ANISOU 810 CA LEU A 114 16607 13056 16546 1847 -4278 1455 A C ATOM 811 C LEU A 114 63.223 -24.274 -1.780 1.00125.30 A C ANISOU 811 C LEU A 114 17204 13282 17122 2093 -4428 1446 A C ATOM 812 O LEU A 114 63.631 -25.007 -0.873 1.00124.83 A O ANISOU 812 O LEU A 114 17362 13042 17028 2131 -4543 1609 A O ATOM 813 CB LEU A 114 61.276 -22.968 -0.915 1.00123.53 A C ANISOU 813 CB LEU A 114 17036 13121 16778 1530 -4135 1471 A C ATOM 814 CG LEU A 114 60.762 -21.780 -0.100 1.00119.73 A C ANISOU 814 CG LEU A 114 16534 12804 16155 1261 -4008 1550 A C ATOM 815 CD1 LEU A 114 59.394 -22.101 0.485 1.00116.73 A C ANISOU 815 CD1 LEU A 114 16363 12217 15772 975 -3882 1581 A C ATOM 816 CD2 LEU A 114 61.748 -21.407 0.997 1.00118.12 A C ANISOU 816 CD2 LEU A 114 16372 12701 15809 1285 -4124 1732 A C ATOM 817 N SER A 115 63.198 -24.650 -3.056 1.00124.81 A N ANISOU 817 N SER A 115 17018 13219 17187 2270 -4423 1257 A N ATOM 818 CA SER A 115 63.650 -25.979 -3.458 1.00129.26 A C ANISOU 818 CA SER A 115 17702 13544 17865 2514 -4556 1220 A C ATOM 819 C SER A 115 65.140 -25.963 -3.793 1.00134.75 A C ANISOU 819 C SER A 115 18240 14417 18542 2850 -4709 1247 A C ATOM 820 O SER A 115 65.882 -26.885 -3.427 1.00137.38 A O ANISOU 820 O SER A 115 18721 14586 18892 3041 -4860 1345 A O ATOM 821 CB SER A 115 62.840 -26.489 -4.648 1.00127.29 A C ANISOU 821 CB SER A 115 17414 13189 17761 2539 -4482 984 A C ATOM 822 OG SER A 115 62.972 -25.610 -5.750 1.00125.00 A O ANISOU 822 OG SER A 115 16816 13213 17467 2642 -4414 827 A O ATOM 823 N ASN A 116 65.567 -24.904 -4.480 1.00134.57 A N ANISOU 823 N ASN A 116 17914 14731 18484 2923 -4661 1168 A N ATOM 824 CA ASN A 116 66.977 -24.701 -4.822 1.00137.05 A C ANISOU 824 CA ASN A 116 18030 15268 18776 3217 -4783 1193 A C ATOM 825 C ASN A 116 67.882 -24.539 -3.588 1.00138.54 A C ANISOU 825 C ASN A 116 18282 15511 18844 3219 -4908 1409 A C ATOM 826 O ASN A 116 67.782 -23.540 -2.866 1.00137.20 A O ANISOU 826 O ASN A 116 18063 15502 18566 3006 -4849 1494 A O ATOM 827 CB ASN A 116 67.120 -23.491 -5.755 1.00127.44 A C ANISOU 827 CB ASN A 116 16478 14397 17545 3246 -4669 1078 A C ATOM 828 CG ASN A 116 68.562 -23.228 -6.166 1.00121.82 A C ANISOU 828 CG ASN A 116 15533 13932 16820 3538 -4776 1099 A C ATOM 829 ND2 ASN A 116 68.768 -22.169 -6.948 1.00105.39 A N ANISOU 829 ND2 ASN A 116 13162 12150 14731 3570 -4670 1021 A N ATOM 830 OD1 ASN A 116 69.480 -23.970 -5.789 1.00123.04 A O ANISOU 830 OD1 ASN A 116 15766 14014 16972 3737 -4946 1190 A O ATOM 831 N VAL A 117 68.768 -25.514 -3.365 1.00136.69 A N ANISOU 831 N VAL A 117 18155 15155 18625 3470 -5083 1490 A N ATOM 832 CA VAL A 117 69.615 -25.542 -2.165 1.00137.97 A C ANISOU 832 CA VAL A 117 18402 15354 18667 3502 -5223 1697 A C ATOM 833 C VAL A 117 70.790 -24.545 -2.208 1.00141.87 A C ANISOU 833 C VAL A 117 18593 16229 19081 3613 -5282 1722 A C ATOM 834 O VAL A 117 71.454 -24.314 -1.197 1.00131.86 A O ANISOU 834 O VAL A 117 17348 15059 17695 3598 -5386 1874 A O ATOM 835 CB VAL A 117 70.134 -26.963 -1.847 1.00136.94 A C ANISOU 835 CB VAL A 117 18508 14952 18572 3744 -5387 1791 A C ATOM 836 CG1 VAL A 117 70.713 -27.002 -0.444 1.00139.82 A C ANISOU 836 CG1 VAL A 117 19011 15328 18787 3722 -5508 2021 A C ATOM 837 CG2 VAL A 117 69.015 -27.990 -1.973 1.00136.75 A C ANISOU 837 CG2 VAL A 117 18763 14535 18662 3646 -5318 1740 A C ATOM 838 N LEU A 118 71.026 -23.949 -3.376 1.00152.90 A N ANISOU 838 N LEU A 118 19705 17845 20543 3719 -5211 1572 A N ATOM 839 CA LEU A 118 71.996 -22.858 -3.526 1.00154.93 A C ANISOU 839 CA LEU A 118 19650 18469 20748 3776 -5222 1580 A C ATOM 840 C LEU A 118 71.492 -21.545 -2.918 1.00152.59 A C ANISOU 840 C LEU A 118 19287 18326 20364 3442 -5090 1611 A C ATOM 841 O LEU A 118 72.162 -20.512 -2.995 1.00148.79 A O ANISOU 841 O LEU A 118 18552 18133 19848 3430 -5068 1610 A O ATOM 842 CB LEU A 118 72.292 -22.611 -5.011 1.00154.41 A C ANISOU 842 CB LEU A 118 19309 18578 20781 3983 -5155 1416 A C ATOM 843 CG LEU A 118 73.178 -23.573 -5.804 1.00150.15 A C ANISOU 843 CG LEU A 118 18711 18021 20316 4374 -5286 1365 A C ATOM 844 CD1 LEU A 118 73.249 -23.119 -7.268 1.00144.72 A C ANISOU 844 CD1 LEU A 118 17747 17535 19706 4524 -5174 1197 A C ATOM 845 CD2 LEU A 118 74.570 -23.663 -5.177 1.00143.90 A C ANISOU 845 CD2 LEU A 118 17839 17381 19456 4562 -5469 1501 A C ATOM 846 N VAL A 119 70.301 -21.583 -2.332 1.00151.43 A N ANISOU 846 N VAL A 119 19366 17984 20189 3169 -4993 1634 A N ATOM 847 CA VAL A 119 69.642 -20.370 -1.873 1.00142.21 A C ANISOU 847 CA VAL A 119 18150 16936 18946 2855 -4842 1641 A C ATOM 848 C VAL A 119 69.377 -20.453 -0.387 1.00128.15 A C ANISOU 848 C VAL A 119 16613 15041 17038 2649 -4893 1798 A C ATOM 849 O VAL A 119 68.877 -21.464 0.103 1.00123.85 A O ANISOU 849 O VAL A 119 16344 14221 16493 2630 -4938 1866 A O ATOM 850 CB VAL A 119 68.302 -20.187 -2.586 1.00148.32 A C ANISOU 850 CB VAL A 119 18948 17620 19789 2698 -4645 1511 A C ATOM 851 CG1 VAL A 119 67.658 -18.878 -2.169 1.00149.21 A C ANISOU 851 CG1 VAL A 119 18997 17872 19824 2399 -4480 1516 A C ATOM 852 CG2 VAL A 119 68.496 -20.248 -4.096 1.00149.68 A C ANISOU 852 CG2 VAL A 119 18903 17892 20077 2929 -4599 1350 A C ATOM 853 N LYS A 120 69.703 -19.391 0.336 1.00118.56 A N ANISOU 853 N LYS A 120 15300 14034 15713 2493 -4881 1854 A N ATOM 854 CA LYS A 120 69.549 -19.422 1.785 1.00121.23 A C ANISOU 854 CA LYS A 120 15856 14301 15905 2317 -4942 2003 A C ATOM 855 C LYS A 120 69.038 -18.104 2.323 1.00117.25 A C ANISOU 855 C LYS A 120 15293 13945 15311 2017 -4803 1992 A C ATOM 856 O LYS A 120 69.433 -17.027 1.862 1.00108.35 A O ANISOU 856 O LYS A 120 13908 13058 14204 1992 -4734 1913 A O ATOM 857 CB LYS A 120 70.875 -19.767 2.468 1.00128.26 A C ANISOU 857 CB LYS A 120 16727 15295 16712 2511 -5167 2119 A C ATOM 858 CG LYS A 120 71.086 -21.238 2.791 1.00130.72 A C ANISOU 858 CG LYS A 120 17283 15358 17028 2715 -5320 2227 A C ATOM 859 CD LYS A 120 72.411 -21.405 3.523 1.00133.76 A C ANISOU 859 CD LYS A 120 17620 15900 17303 2903 -5538 2344 A C ATOM 860 CE LYS A 120 72.572 -22.787 4.143 1.00136.36 A C ANISOU 860 CE LYS A 120 18238 15979 17594 3079 -5685 2495 A C ATOM 861 NZ LYS A 120 73.807 -22.866 4.985 1.00135.60 A N1+ ANISOU 861 NZ LYS A 120 18097 16067 17358 3250 -5897 2620 A N1+ ATOM 862 N PHE A 121 68.170 -18.193 3.321 1.00122.74 A N ANISOU 862 N PHE A 121 16237 14492 15906 1792 -4757 2078 A N ATOM 863 CA PHE A 121 67.569 -17.000 3.894 1.00127.33 A C ANISOU 863 CA PHE A 121 16798 15187 16393 1502 -4616 2067 A C ATOM 864 C PHE A 121 68.063 -16.754 5.307 1.00124.49 A C ANISOU 864 C PHE A 121 16539 14909 15853 1413 -4736 2195 A C ATOM 865 O PHE A 121 67.965 -17.634 6.168 1.00126.36 A O ANISOU 865 O PHE A 121 17026 14981 16006 1431 -4836 2329 A O ATOM 866 CB PHE A 121 66.042 -17.121 3.908 1.00133.64 A C ANISOU 866 CB PHE A 121 17782 15789 17206 1285 -4435 2047 A C ATOM 867 CG PHE A 121 65.410 -17.109 2.539 1.00137.98 A C ANISOU 867 CG PHE A 121 18207 16309 17911 1328 -4291 1896 A C ATOM 868 CD1 PHE A 121 65.277 -15.920 1.830 1.00133.46 A C ANISOU 868 CD1 PHE A 121 17397 15941 17373 1265 -4140 1782 A C ATOM 869 CD2 PHE A 121 64.931 -18.284 1.971 1.00139.28 A C ANISOU 869 CD2 PHE A 121 18496 16240 18184 1432 -4304 1865 A C ATOM 870 CE1 PHE A 121 64.693 -15.903 0.580 1.00128.03 A C ANISOU 870 CE1 PHE A 121 16591 15247 16805 1322 -4010 1647 A C ATOM 871 CE2 PHE A 121 64.347 -18.273 0.722 1.00137.78 A C ANISOU 871 CE2 PHE A 121 18184 16044 18121 1477 -4182 1711 A C ATOM 872 CZ PHE A 121 64.228 -17.077 0.025 1.00133.32 A C ANISOU 872 CZ PHE A 121 17377 15708 17572 1429 -4037 1605 A C ATOM 873 N THR A 122 68.596 -15.559 5.544 1.00115.91 A N ANISOU 873 N THR A 122 15259 14075 14708 1321 -4722 2152 A N ATOM 874 CA THR A 122 68.854 -15.114 6.906 1.00115.48 A C ANISOU 874 CA THR A 122 15294 14117 14468 1180 -4802 2240 A C ATOM 875 C THR A 122 67.506 -14.956 7.608 1.00112.57 A C ANISOU 875 C THR A 122 15164 13599 14007 912 -4650 2281 A C ATOM 876 O THR A 122 66.491 -14.717 6.954 1.00118.80 A O ANISOU 876 O THR A 122 15954 14301 14884 799 -4458 2204 A O ATOM 877 CB THR A 122 69.613 -13.773 6.926 1.00119.55 A C ANISOU 877 CB THR A 122 15538 14924 14962 1105 -4793 2152 A C ATOM 878 CG2 THR A 122 70.562 -13.676 5.734 1.00118.57 A C ANISOU 878 CG2 THR A 122 15117 14941 14993 1324 -4828 2064 A C ATOM 879 OG1 THR A 122 68.681 -12.685 6.883 1.00122.41 A O ANISOU 879 OG1 THR A 122 15881 15309 15319 846 -4573 2074 A O ATOM 880 N LEU A 123 67.478 -15.103 8.927 1.00107.61 A N ANISOU 880 N LEU A 123 14736 12954 13198 822 -4733 2403 A N ATOM 881 CA LEU A 123 66.238 -14.905 9.669 1.00108.96 A C ANISOU 881 CA LEU A 123 15127 13006 13265 567 -4586 2450 A C ATOM 882 C LEU A 123 65.520 -13.610 9.262 1.00113.73 A C ANISOU 882 C LEU A 123 15595 13712 13904 350 -4366 2316 A C ATOM 883 O LEU A 123 64.307 -13.605 9.075 1.00120.60 A O ANISOU 883 O LEU A 123 16572 14447 14803 203 -4187 2299 A O ATOM 884 CB LEU A 123 66.498 -14.880 11.173 1.00109.58 A C ANISOU 884 CB LEU A 123 15376 13145 13114 496 -4704 2578 A C ATOM 885 CG LEU A 123 65.235 -14.710 12.023 1.00112.25 A C ANISOU 885 CG LEU A 123 15954 13371 13326 243 -4552 2642 A C ATOM 886 CD1 LEU A 123 64.324 -15.929 11.891 1.00112.58 A C ANISOU 886 CD1 LEU A 123 16234 13108 13433 259 -4491 2742 A C ATOM 887 CD2 LEU A 123 65.569 -14.451 13.480 1.00112.97 A C ANISOU 887 CD2 LEU A 123 16171 13581 13170 172 -4661 2743 A C ATOM 888 N SER A 124 66.272 -12.521 9.127 1.00108.09 A N ANISOU 888 N SER A 124 14645 13235 13191 331 -4375 2222 A N ATOM 889 CA SER A 124 65.696 -11.210 8.839 1.00109.50 A C ANISOU 889 CA SER A 124 14700 13513 13391 132 -4167 2105 A C ATOM 890 C SER A 124 65.076 -11.121 7.439 1.00115.52 A C ANISOU 890 C SER A 124 15337 14217 14339 172 -3991 2005 A C ATOM 891 O SER A 124 64.091 -10.402 7.225 1.00113.78 A O ANISOU 891 O SER A 124 15118 13986 14127 3 -3782 1944 A O ATOM 892 CB SER A 124 66.748 -10.102 9.020 1.00105.78 A C ANISOU 892 CB SER A 124 14003 13295 12895 108 -4225 2029 A C ATOM 893 OG SER A 124 67.627 -10.013 7.906 1.00 97.73 A O ANISOU 893 OG SER A 124 12716 12380 12039 292 -4259 1954 A O ATOM 894 N GLU A 125 65.668 -11.833 6.485 1.00116.01 A N ANISOU 894 N GLU A 125 15284 14257 14538 409 -4076 1984 A N ATOM 895 CA GLU A 125 65.145 -11.846 5.130 1.00113.85 A C ANISOU 895 CA GLU A 125 14889 13943 14428 480 -3930 1884 A C ATOM 896 C GLU A 125 63.785 -12.538 5.163 1.00108.55 A C ANISOU 896 C GLU A 125 14441 13046 13756 380 -3823 1910 A C ATOM 897 O GLU A 125 62.768 -11.973 4.731 1.00 97.92 A O ANISOU 897 O GLU A 125 13072 11693 12439 247 -3621 1838 A O ATOM 898 CB GLU A 125 66.128 -12.531 4.168 1.00120.76 A C ANISOU 898 CB GLU A 125 15604 14847 15433 772 -4061 1857 A C ATOM 899 CG GLU A 125 67.408 -11.712 3.907 1.00133.03 A C ANISOU 899 CG GLU A 125 16880 16649 17016 862 -4124 1811 A C ATOM 900 CD GLU A 125 68.429 -12.431 3.026 1.00140.70 A C ANISOU 900 CD GLU A 125 17693 17664 18101 1165 -4261 1795 A C ATOM 901 OE1 GLU A 125 68.655 -13.643 3.233 1.00147.21 A O ANISOU 901 OE1 GLU A 125 18664 18353 18917 1319 -4418 1868 A O ATOM 902 OE2 GLU A 125 69.017 -11.777 2.135 1.00138.48 A O1- ANISOU 902 OE2 GLU A 125 17145 17553 17918 1256 -4204 1716 A O1- ATOM 903 N ILE A 126 63.769 -13.751 5.706 1.00104.60 A N ANISOU 903 N ILE A 126 14156 12364 13221 443 -3956 2016 A N ATOM 904 CA ILE A 126 62.521 -14.452 5.950 1.00100.74 A C ANISOU 904 CA ILE A 126 13902 11650 12725 319 -3864 2060 A C ATOM 905 C ILE A 126 61.478 -13.490 6.522 1.00101.89 A C ANISOU 905 C ILE A 126 14107 11838 12768 41 -3674 2050 A C ATOM 906 O ILE A 126 60.390 -13.342 5.962 1.00106.56 A O ANISOU 906 O ILE A 126 14693 12374 13420 -59 -3496 1978 A O ATOM 907 CB ILE A 126 62.726 -15.642 6.899 1.00106.50 A C ANISOU 907 CB ILE A 126 14889 12196 13378 371 -4026 2219 A C ATOM 908 CG1 ILE A 126 63.465 -16.775 6.174 1.00108.81 A C ANISOU 908 CG1 ILE A 126 15158 12384 13800 651 -4178 2219 A C ATOM 909 CG2 ILE A 126 61.389 -16.140 7.429 1.00107.85 A C ANISOU 909 CG2 ILE A 126 15313 12154 13512 176 -3904 2286 A C ATOM 910 CD1 ILE A 126 63.882 -17.928 7.063 1.00105.33 A C ANISOU 910 CD1 ILE A 126 14955 11775 13288 752 -4352 2386 A C ATOM 911 N LYS A 127 61.816 -12.835 7.629 1.00 99.30 A N ANISOU 911 N LYS A 127 13829 11619 12280 -74 -3714 2114 A N ATOM 912 CA LYS A 127 60.957 -11.812 8.222 1.00 98.17 A C ANISOU 912 CA LYS A 127 13733 11541 12027 -322 -3541 2096 A C ATOM 913 C LYS A 127 60.387 -10.844 7.181 1.00 91.84 A C ANISOU 913 C LYS A 127 12735 10833 11326 -374 -3332 1953 A C ATOM 914 O LYS A 127 59.203 -10.514 7.210 1.00 88.39 A O ANISOU 914 O LYS A 127 12365 10353 10864 -537 -3147 1930 A O ATOM 915 CB LYS A 127 61.718 -11.017 9.288 1.00102.49 A C ANISOU 915 CB LYS A 127 14274 12255 12414 -394 -3629 2130 A C ATOM 916 CG LYS A 127 61.912 -11.756 10.598 1.00109.29 A C ANISOU 916 CG LYS A 127 15377 13041 13107 -407 -3782 2286 A C ATOM 917 CD LYS A 127 62.348 -10.811 11.714 1.00111.64 A C ANISOU 917 CD LYS A 127 15682 13517 13218 -529 -3827 2293 A C ATOM 918 CE LYS A 127 62.517 -11.557 13.034 1.00113.99 A C ANISOU 918 CE LYS A 127 16226 13761 13325 -524 -3978 2457 A C ATOM 919 NZ LYS A 127 62.926 -10.658 14.150 1.00114.04 A N1+ ANISOU 919 NZ LYS A 127 16242 13956 13131 -639 -4032 2449 A N1+ ATOM 920 N ARG A 128 61.227 -10.382 6.265 1.00 87.03 A N ANISOU 920 N ARG A 128 11879 10361 10827 -227 -3354 1864 A N ATOM 921 CA ARG A 128 60.758 -9.446 5.262 1.00 85.15 A C ANISOU 921 CA ARG A 128 11453 10222 10678 -250 -3153 1744 A C ATOM 922 C ARG A 128 59.771 -10.145 4.338 1.00 87.93 A C ANISOU 922 C ARG A 128 11827 10449 11135 -204 -3054 1696 A C ATOM 923 O ARG A 128 58.701 -9.630 4.042 1.00 93.94 A O ANISOU 923 O ARG A 128 12579 11217 11895 -321 -2857 1641 A O ATOM 924 CB ARG A 128 61.928 -8.876 4.466 1.00 84.78 A C ANISOU 924 CB ARG A 128 11137 10345 10730 -89 -3198 1676 A C ATOM 925 CG ARG A 128 61.543 -7.781 3.471 1.00 82.91 A C ANISOU 925 CG ARG A 128 10701 10225 10575 -103 -2978 1569 A C ATOM 926 CD ARG A 128 61.276 -6.436 4.138 1.00 88.60 A C ANISOU 926 CD ARG A 128 11422 11039 11203 -315 -2837 1553 A C ATOM 927 NE ARG A 128 61.046 -5.412 3.122 1.00 98.05 A N ANISOU 927 NE ARG A 128 12421 12343 12490 -293 -2630 1465 A N ATOM 928 CZ ARG A 128 59.859 -4.874 2.864 1.00 96.86 A C ANISOU 928 CZ ARG A 128 12302 12179 12322 -394 -2411 1429 A C ATOM 929 NH1 ARG A 128 58.803 -5.247 3.575 1.00 97.70 A N1+ ANISOU 929 NH1 ARG A 128 12621 12173 12328 -541 -2372 1467 A N1+ ATOM 930 NH2 ARG A 128 59.732 -3.959 1.908 1.00 90.44 A N ANISOU 930 NH2 ARG A 128 11305 11469 11588 -343 -2227 1362 A N ATOM 931 N VAL A 129 60.141 -11.324 3.876 1.00 91.40 A N ANISOU 931 N VAL A 129 12288 10777 11664 -25 -3192 1708 A N ATOM 932 CA VAL A 129 59.258 -12.093 3.025 1.00 89.17 A C ANISOU 932 CA VAL A 129 12031 10365 11486 20 -3122 1646 A C ATOM 933 C VAL A 129 57.872 -12.193 3.657 1.00 85.21 A C ANISOU 933 C VAL A 129 11723 9743 10911 -213 -2987 1680 A C ATOM 934 O VAL A 129 56.882 -11.827 3.027 1.00 77.89 A O ANISOU 934 O VAL A 129 10730 8844 10020 -281 -2810 1591 A O ATOM 935 CB VAL A 129 59.855 -13.481 2.730 1.00 91.00 A C ANISOU 935 CB VAL A 129 12324 10447 11805 222 -3311 1672 A C ATOM 936 CG1 VAL A 129 58.769 -14.512 2.452 1.00 88.23 A C ANISOU 936 CG1 VAL A 129 12121 9881 11522 179 -3263 1648 A C ATOM 937 CG2 VAL A 129 60.831 -13.378 1.569 1.00 93.21 A C ANISOU 937 CG2 VAL A 129 12356 10860 12200 474 -3370 1584 A C ATOM 938 N MET A 130 57.801 -12.658 4.902 1.00 82.95 A N ANISOU 938 N MET A 130 11666 9339 10511 -328 -3065 1811 A N ATOM 939 CA MET A 130 56.513 -12.766 5.585 1.00 82.18 A C ANISOU 939 CA MET A 130 11756 9133 10336 -554 -2933 1859 A C ATOM 940 C MET A 130 55.796 -11.425 5.680 1.00 87.89 A C ANISOU 940 C MET A 130 12401 10012 10981 -721 -2728 1804 A C ATOM 941 O MET A 130 54.586 -11.328 5.451 1.00 93.99 A O ANISOU 941 O MET A 130 13194 10756 11762 -844 -2558 1760 A O ATOM 942 CB MET A 130 56.670 -13.365 6.979 1.00 75.20 A C ANISOU 942 CB MET A 130 11127 8127 9320 -637 -3046 2028 A C ATOM 943 CG MET A 130 56.994 -14.844 6.958 1.00 85.18 A C ANISOU 943 CG MET A 130 12529 9173 10661 -504 -3203 2102 A C ATOM 944 SD MET A 130 56.140 -15.729 5.640 1.00108.38 A S ANISOU 944 SD MET A 130 15422 11951 13807 -450 -3124 1975 A S ATOM 945 CE MET A 130 54.435 -15.457 6.104 1.00 68.21 A C ANISOU 945 CE MET A 130 10450 6809 8656 -751 -2891 1982 A C ATOM 946 N GLN A 131 56.548 -10.393 6.029 1.00 78.62 A N ANISOU 946 N GLN A 131 11137 9003 9733 -726 -2743 1803 A N ATOM 947 CA GLN A 131 55.983 -9.065 6.116 1.00 78.84 A C ANISOU 947 CA GLN A 131 11092 9170 9693 -868 -2549 1748 A C ATOM 948 C GLN A 131 55.310 -8.660 4.801 1.00 76.06 A C ANISOU 948 C GLN A 131 10557 8884 9457 -813 -2375 1622 A C ATOM 949 O GLN A 131 54.201 -8.146 4.803 1.00 78.43 A O ANISOU 949 O GLN A 131 10876 9209 9715 -946 -2186 1591 A O ATOM 950 CB GLN A 131 57.072 -8.070 6.464 1.00 81.92 A C ANISOU 950 CB GLN A 131 11376 9719 10031 -850 -2607 1740 A C ATOM 951 CG GLN A 131 56.598 -6.931 7.308 1.00 88.36 A C ANISOU 951 CG GLN A 131 12250 10616 10706 -1050 -2470 1740 A C ATOM 952 CD GLN A 131 57.677 -5.910 7.482 1.00 87.84 A C ANISOU 952 CD GLN A 131 12049 10702 10623 -1034 -2515 1700 A C ATOM 953 NE2 GLN A 131 57.681 -5.248 8.625 1.00 87.61 A N ANISOU 953 NE2 GLN A 131 12128 10720 10440 -1193 -2507 1726 A N ATOM 954 OE1 GLN A 131 58.509 -5.718 6.591 1.00 87.81 A O ANISOU 954 OE1 GLN A 131 11842 10778 10744 -882 -2555 1642 A O ATOM 955 N MET A 132 55.984 -8.881 3.681 1.00 70.18 A N ANISOU 955 N MET A 132 9633 8184 8849 -605 -2436 1551 A N ATOM 956 CA MET A 132 55.428 -8.476 2.402 1.00 75.72 A C ANISOU 956 CA MET A 132 10150 8974 9645 -524 -2278 1433 A C ATOM 957 C MET A 132 54.198 -9.318 2.107 1.00 81.67 A C ANISOU 957 C MET A 132 10991 9607 10432 -579 -2212 1400 A C ATOM 958 O MET A 132 53.137 -8.783 1.809 1.00 86.51 A O ANISOU 958 O MET A 132 11564 10282 11025 -666 -2024 1343 A O ATOM 959 CB MET A 132 56.469 -8.559 1.280 1.00 79.03 A C ANISOU 959 CB MET A 132 10358 9480 10192 -274 -2362 1370 A C ATOM 960 CG MET A 132 57.650 -7.594 1.473 1.00 82.31 A C ANISOU 960 CG MET A 132 10648 10037 10590 -235 -2398 1389 A C ATOM 961 SD MET A 132 58.756 -7.474 0.048 1.00 82.18 A S ANISOU 961 SD MET A 132 10345 10158 10722 50 -2438 1316 A S ATOM 962 CE MET A 132 59.725 -8.966 0.267 1.00 66.51 A C ANISOU 962 CE MET A 132 8444 8047 8779 206 -2727 1369 A C ATOM 963 N LEU A 133 54.334 -10.633 2.224 1.00 76.92 A N ANISOU 963 N LEU A 133 10512 8831 9884 -531 -2366 1435 A N ATOM 964 CA LEU A 133 53.212 -11.540 2.054 1.00 74.09 A C ANISOU 964 CA LEU A 133 10254 8327 9570 -609 -2318 1404 A C ATOM 965 C LEU A 133 51.997 -11.148 2.911 1.00 80.39 A C ANISOU 965 C LEU A 133 11184 9107 10252 -864 -2156 1453 A C ATOM 966 O LEU A 133 50.882 -11.015 2.403 1.00 82.49 A O ANISOU 966 O LEU A 133 11394 9409 10541 -932 -2000 1370 A O ATOM 967 CB LEU A 133 53.649 -12.966 2.365 1.00 76.21 A C ANISOU 967 CB LEU A 133 10685 8376 9897 -549 -2510 1471 A C ATOM 968 CG LEU A 133 52.706 -14.105 1.994 1.00 81.85 A C ANISOU 968 CG LEU A 133 11486 8905 10709 -593 -2492 1418 A C ATOM 969 CD1 LEU A 133 53.508 -15.341 1.627 1.00 87.16 A C ANISOU 969 CD1 LEU A 133 12205 9413 11500 -406 -2688 1417 A C ATOM 970 CD2 LEU A 133 51.786 -14.405 3.148 1.00 82.96 A C ANISOU 970 CD2 LEU A 133 11854 8907 10762 -842 -2425 1530 A C ATOM 971 N LEU A 134 52.192 -10.956 4.207 1.00 77.11 A N ANISOU 971 N LEU A 134 10938 8654 9706 -998 -2192 1582 A N ATOM 972 CA LEU A 134 51.060 -10.579 5.042 1.00 71.38 A C ANISOU 972 CA LEU A 134 10339 7922 8860 -1229 -2035 1632 A C ATOM 973 C LEU A 134 50.507 -9.208 4.639 1.00 72.25 A C ANISOU 973 C LEU A 134 10294 8232 8925 -1270 -1829 1546 A C ATOM 974 O LEU A 134 49.303 -8.973 4.655 1.00 74.02 A O ANISOU 974 O LEU A 134 10532 8481 9112 -1400 -1657 1518 A O ATOM 975 CB LEU A 134 51.431 -10.650 6.525 1.00 68.76 A C ANISOU 975 CB LEU A 134 10223 7524 8379 -1344 -2120 1788 A C ATOM 976 CG LEU A 134 51.582 -12.112 6.987 1.00 71.78 A C ANISOU 976 CG LEU A 134 10800 7678 8796 -1334 -2272 1893 A C ATOM 977 CD1 LEU A 134 52.324 -12.273 8.305 1.00 68.45 A C ANISOU 977 CD1 LEU A 134 10564 7211 8231 -1362 -2410 2052 A C ATOM 978 CD2 LEU A 134 50.224 -12.774 7.073 1.00 67.59 A C ANISOU 978 CD2 LEU A 134 10379 7011 8290 -1495 -2147 1904 A C ATOM 979 N ASN A 135 51.382 -8.303 4.238 1.00 72.76 A N ANISOU 979 N ASN A 135 10205 8441 9000 -1153 -1837 1505 A N ATOM 980 CA ASN A 135 50.924 -6.972 3.875 1.00 67.77 A C ANISOU 980 CA ASN A 135 9440 7981 8330 -1180 -1634 1437 A C ATOM 981 C ASN A 135 49.983 -7.029 2.689 1.00 72.50 A C ANISOU 981 C ASN A 135 9895 8639 9013 -1115 -1495 1325 A C ATOM 982 O ASN A 135 48.952 -6.356 2.660 1.00 80.97 A O ANISOU 982 O ASN A 135 10944 9796 10025 -1208 -1301 1293 A O ATOM 983 CB ASN A 135 52.101 -6.066 3.553 1.00 60.30 A C ANISOU 983 CB ASN A 135 8343 7159 7409 -1056 -1667 1413 A C ATOM 984 CG ASN A 135 51.724 -4.612 3.584 1.00 67.48 A C ANISOU 984 CG ASN A 135 9181 8208 8251 -1126 -1461 1380 A C ATOM 985 ND2 ASN A 135 52.339 -3.812 2.714 1.00 69.83 A N ANISOU 985 ND2 ASN A 135 9281 8627 8623 -987 -1405 1320 A N ATOM 986 OD1 ASN A 135 50.877 -4.207 4.378 1.00 73.54 A O ANISOU 986 OD1 ASN A 135 10072 8969 8900 -1299 -1342 1411 A O ATOM 987 N GLY A 136 50.357 -7.827 1.700 1.00 71.01 A N ANISOU 987 N GLY A 136 9605 8419 8957 -942 -1599 1258 A N ATOM 988 CA GLY A 136 49.516 -8.056 0.539 1.00 70.46 A C ANISOU 988 CA GLY A 136 9397 8407 8967 -864 -1501 1136 A C ATOM 989 C GLY A 136 48.196 -8.744 0.857 1.00 72.95 A C ANISOU 989 C GLY A 136 9826 8627 9266 -1035 -1433 1126 A C ATOM 990 O GLY A 136 47.169 -8.438 0.243 1.00 71.00 A O ANISOU 990 O GLY A 136 9473 8487 9018 -1050 -1276 1036 A O ATOM 991 N LEU A 137 48.203 -9.678 1.805 1.00 68.20 A N ANISOU 991 N LEU A 137 9434 7830 8649 -1161 -1546 1222 A N ATOM 992 CA LEU A 137 46.935 -10.252 2.234 1.00 69.14 A C ANISOU 992 CA LEU A 137 9668 7854 8748 -1355 -1460 1232 A C ATOM 993 C LEU A 137 46.058 -9.178 2.878 1.00 74.92 A C ANISOU 993 C LEU A 137 10423 8710 9335 -1519 -1258 1267 A C ATOM 994 O LEU A 137 44.849 -9.166 2.662 1.00 75.66 A O ANISOU 994 O LEU A 137 10476 8851 9420 -1616 -1112 1210 A O ATOM 995 CB LEU A 137 47.122 -11.462 3.154 1.00 68.33 A C ANISOU 995 CB LEU A 137 9799 7505 8658 -1455 -1603 1349 A C ATOM 996 CG LEU A 137 47.712 -12.695 2.454 1.00 71.70 A C ANISOU 996 CG LEU A 137 10219 7779 9246 -1303 -1780 1296 A C ATOM 997 CD1 LEU A 137 47.991 -13.818 3.425 1.00 68.55 A C ANISOU 997 CD1 LEU A 137 10068 7128 8852 -1384 -1914 1436 A C ATOM 998 CD2 LEU A 137 46.825 -13.184 1.326 1.00 73.07 A C ANISOU 998 CD2 LEU A 137 10258 7964 9540 -1277 -1714 1129 A C ATOM 999 N TYR A 138 46.664 -8.263 3.641 1.00 74.76 A N ANISOU 999 N TYR A 138 10455 8748 9201 -1545 -1249 1351 A N ATOM 1000 CA TYR A 138 45.904 -7.175 4.266 1.00 68.92 A C ANISOU 1000 CA TYR A 138 9746 8124 8319 -1686 -1056 1378 A C ATOM 1001 C TYR A 138 45.201 -6.393 3.185 1.00 66.49 A C ANISOU 1001 C TYR A 138 9228 8000 8037 -1602 -875 1255 A C ATOM 1002 O TYR A 138 44.028 -6.035 3.303 1.00 70.32 A O ANISOU 1002 O TYR A 138 9705 8558 8453 -1711 -700 1235 A O ATOM 1003 CB TYR A 138 46.808 -6.224 5.049 1.00 67.60 A C ANISOU 1003 CB TYR A 138 9633 8006 8046 -1694 -1083 1448 A C ATOM 1004 CG TYR A 138 46.084 -5.029 5.664 1.00 68.69 A C ANISOU 1004 CG TYR A 138 9803 8257 8038 -1822 -881 1461 A C ATOM 1005 CD1 TYR A 138 45.427 -5.138 6.894 1.00 71.53 A C ANISOU 1005 CD1 TYR A 138 10360 8560 8259 -2019 -833 1555 A C ATOM 1006 CD2 TYR A 138 46.079 -3.788 5.028 1.00 70.84 A C ANISOU 1006 CD2 TYR A 138 9917 8690 8308 -1735 -732 1386 A C ATOM 1007 CE1 TYR A 138 44.776 -4.052 7.467 1.00 73.99 A C ANISOU 1007 CE1 TYR A 138 10707 8976 8430 -2124 -648 1561 A C ATOM 1008 CE2 TYR A 138 45.420 -2.694 5.586 1.00 72.39 A C ANISOU 1008 CE2 TYR A 138 10154 8978 8375 -1840 -543 1395 A C ATOM 1009 CZ TYR A 138 44.774 -2.834 6.803 1.00 83.18 A C ANISOU 1009 CZ TYR A 138 11715 10289 9602 -2033 -505 1476 A C ATOM 1010 OH TYR A 138 44.121 -1.755 7.354 1.00 93.10 A O ANISOU 1010 OH TYR A 138 13014 11638 10724 -2125 -316 1478 A O ATOM 1011 N TYR A 139 45.930 -6.142 2.112 1.00 62.12 A N ANISOU 1011 N TYR A 139 8496 7529 7577 -1394 -916 1176 A N ATOM 1012 CA TYR A 139 45.420 -5.280 1.065 1.00 63.62 A C ANISOU 1012 CA TYR A 139 8482 7912 7778 -1277 -743 1075 A C ATOM 1013 C TYR A 139 44.255 -5.928 0.348 1.00 69.39 A C ANISOU 1013 C TYR A 139 9131 8676 8557 -1283 -678 975 A C ATOM 1014 O TYR A 139 43.216 -5.292 0.166 1.00 69.35 A O ANISOU 1014 O TYR A 139 9055 8808 8486 -1322 -489 934 A O ATOM 1015 CB TYR A 139 46.531 -4.874 0.088 1.00 59.48 A C ANISOU 1015 CB TYR A 139 7788 7472 7341 -1043 -799 1029 A C ATOM 1016 CG TYR A 139 46.011 -4.182 -1.140 1.00 54.93 A C ANISOU 1016 CG TYR A 139 6997 7091 6784 -886 -632 928 A C ATOM 1017 CD1 TYR A 139 45.614 -2.856 -1.097 1.00 49.40 A C ANISOU 1017 CD1 TYR A 139 6247 6526 5997 -894 -424 941 A C ATOM 1018 CD2 TYR A 139 45.922 -4.851 -2.347 1.00 63.14 A C ANISOU 1018 CD2 TYR A 139 7886 8180 7924 -717 -681 819 A C ATOM 1019 CE1 TYR A 139 45.106 -2.229 -2.215 1.00 48.67 A C ANISOU 1019 CE1 TYR A 139 5964 6617 5911 -732 -263 863 A C ATOM 1020 CE2 TYR A 139 45.440 -4.219 -3.478 1.00 69.41 A C ANISOU 1020 CE2 TYR A 139 8480 9174 8717 -554 -530 730 A C ATOM 1021 CZ TYR A 139 45.033 -2.912 -3.399 1.00 62.85 A C ANISOU 1021 CZ TYR A 139 7608 8478 7795 -559 -319 761 A C ATOM 1022 OH TYR A 139 44.550 -2.285 -4.509 1.00 68.52 A O ANISOU 1022 OH TYR A 139 8134 9398 8501 -380 -163 689 A O ATOM 1023 N ILE A 140 44.411 -7.194 -0.044 1.00 73.55 A N ANISOU 1023 N ILE A 140 9666 9079 9199 -1246 -833 930 A N ATOM 1024 CA ILE A 140 43.367 -7.826 -0.847 1.00 71.71 A C ANISOU 1024 CA ILE A 140 9329 8887 9029 -1243 -784 803 A C ATOM 1025 C ILE A 140 42.116 -8.043 -0.022 1.00 71.31 A C ANISOU 1025 C ILE A 140 9392 8792 8909 -1489 -675 839 A C ATOM 1026 O ILE A 140 41.025 -7.718 -0.464 1.00 76.22 A O ANISOU 1026 O ILE A 140 9897 9564 9500 -1513 -521 756 A O ATOM 1027 CB ILE A 140 43.802 -9.130 -1.538 1.00 66.70 A C ANISOU 1027 CB ILE A 140 8673 8124 8546 -1141 -970 721 A C ATOM 1028 CG1 ILE A 140 43.967 -10.247 -0.536 1.00 77.80 A C ANISOU 1028 CG1 ILE A 140 10310 9264 9985 -1304 -1107 819 A C ATOM 1029 CG2 ILE A 140 45.084 -8.937 -2.326 1.00 61.95 A C ANISOU 1029 CG2 ILE A 140 7957 7573 8007 -888 -1078 694 A C ATOM 1030 CD1 ILE A 140 44.451 -11.491 -1.183 1.00 86.38 A C ANISOU 1030 CD1 ILE A 140 11392 10205 11225 -1193 -1285 741 A C ATOM 1031 N HIS A 141 42.276 -8.558 1.189 1.00 69.77 A N ANISOU 1031 N HIS A 141 9421 8409 8679 -1664 -748 969 A N ATOM 1032 CA HIS A 141 41.136 -8.743 2.077 1.00 70.83 A C ANISOU 1032 CA HIS A 141 9676 8500 8737 -1905 -634 1028 A C ATOM 1033 C HIS A 141 40.385 -7.442 2.370 1.00 74.98 A C ANISOU 1033 C HIS A 141 10153 9223 9114 -1959 -415 1042 A C ATOM 1034 O HIS A 141 39.153 -7.438 2.465 1.00 77.26 A O ANISOU 1034 O HIS A 141 10413 9582 9361 -2086 -271 1012 A O ATOM 1035 CB HIS A 141 41.575 -9.404 3.377 1.00 72.71 A C ANISOU 1035 CB HIS A 141 10172 8515 8939 -2054 -746 1190 A C ATOM 1036 CG HIS A 141 42.123 -10.780 3.186 1.00 69.95 A C ANISOU 1036 CG HIS A 141 9897 7947 8733 -2019 -939 1188 A C ATOM 1037 CD2 HIS A 141 42.010 -11.642 2.148 1.00 67.56 A C ANISOU 1037 CD2 HIS A 141 9487 7595 8589 -1932 -1010 1054 A C ATOM 1038 ND1 HIS A 141 42.918 -11.405 4.125 1.00 67.14 A N ANISOU 1038 ND1 HIS A 141 9753 7392 8363 -2061 -1087 1334 A N ATOM 1039 CE1 HIS A 141 43.265 -12.596 3.672 1.00 75.07 A C ANISOU 1039 CE1 HIS A 141 10785 8222 9518 -1998 -1233 1297 A C ATOM 1040 NE2 HIS A 141 42.724 -12.767 2.476 1.00 75.01 A N ANISOU 1040 NE2 HIS A 141 10587 8295 9620 -1926 -1191 1122 A N ATOM 1041 N ARG A 142 41.128 -6.346 2.506 1.00 72.80 A N ANISOU 1041 N ARG A 142 9864 9033 8763 -1863 -387 1083 A N ATOM 1042 CA ARG A 142 40.525 -5.039 2.731 1.00 66.68 A C ANISOU 1042 CA ARG A 142 9049 8431 7855 -1888 -177 1092 A C ATOM 1043 C ARG A 142 39.642 -4.741 1.537 1.00 66.16 A C ANISOU 1043 C ARG A 142 8757 8560 7821 -1775 -39 956 A C ATOM 1044 O ARG A 142 38.581 -4.145 1.675 1.00 73.81 A O ANISOU 1044 O ARG A 142 9688 9661 8694 -1842 148 944 A O ATOM 1045 CB ARG A 142 41.599 -3.952 2.903 1.00 72.72 A C ANISOU 1045 CB ARG A 142 9820 9238 8572 -1786 -182 1136 A C ATOM 1046 CG ARG A 142 41.110 -2.671 3.574 1.00 82.59 A C ANISOU 1046 CG ARG A 142 11117 10595 9668 -1862 14 1178 A C ATOM 1047 CD ARG A 142 42.246 -1.679 3.935 1.00122.91 A C ANISOU 1047 CD ARG A 142 16263 15701 14737 -1804 -8 1221 A C ATOM 1048 NE ARG A 142 43.082 -1.332 2.783 1.00127.56 A N ANISOU 1048 NE ARG A 142 16671 16356 15438 -1586 -42 1156 A N ATOM 1049 CZ ARG A 142 42.782 -0.398 1.880 1.00130.75 A C ANISOU 1049 CZ ARG A 142 16910 16920 15849 -1443 128 1093 A C ATOM 1050 NH1 ARG A 142 41.656 0.298 1.990 1.00138.87 A N1+ ANISOU 1050 NH1 ARG A 142 17927 18060 16777 -1489 341 1082 A N1+ ATOM 1051 NH2 ARG A 142 43.602 -0.160 0.860 1.00120.39 A N ANISOU 1051 NH2 ARG A 142 15442 15662 14639 -1242 93 1050 A N ATOM 1052 N ASN A 143 40.069 -5.183 0.359 1.00 61.60 A N ANISOU 1052 N ASN A 143 8026 8012 7369 -1593 -134 852 A N ATOM 1053 CA ASN A 143 39.309 -4.938 -0.860 1.00 60.32 A C ANISOU 1053 CA ASN A 143 7635 8054 7228 -1454 -22 714 A C ATOM 1054 C ASN A 143 38.323 -6.043 -1.169 1.00 71.38 A C ANISOU 1054 C ASN A 143 8990 9434 8698 -1551 -47 615 A C ATOM 1055 O ASN A 143 37.859 -6.173 -2.310 1.00 67.87 A O ANISOU 1055 O ASN A 143 8346 9141 8302 -1418 -20 471 A O ATOM 1056 CB ASN A 143 40.239 -4.713 -2.042 1.00 66.20 A C ANISOU 1056 CB ASN A 143 8219 8880 8054 -1185 -89 644 A C ATOM 1057 CG ASN A 143 40.851 -3.330 -2.030 1.00 74.69 A C ANISOU 1057 CG ASN A 143 9265 10054 9058 -1072 21 709 A C ATOM 1058 ND2 ASN A 143 41.958 -3.179 -1.316 1.00 72.08 A N ANISOU 1058 ND2 ASN A 143 9067 9589 8733 -1106 -81 808 A N ATOM 1059 OD1 ASN A 143 40.325 -2.405 -2.645 1.00 77.97 A O ANISOU 1059 OD1 ASN A 143 9543 10666 9416 -956 199 669 A O ATOM 1060 N LYS A 144 38.025 -6.845 -0.143 1.00 75.93 A N ANISOU 1060 N LYS A 144 9750 9823 9278 -1784 -98 693 A N ATOM 1061 CA LYS A 144 36.911 -7.772 -0.192 1.00 73.02 A C ANISOU 1061 CA LYS A 144 9357 9425 8961 -1940 -77 619 A C ATOM 1062 C LYS A 144 37.192 -8.911 -1.170 1.00 75.26 A C ANISOU 1062 C LYS A 144 9553 9627 9415 -1847 -241 481 A C ATOM 1063 O LYS A 144 36.277 -9.458 -1.790 1.00 75.97 A O ANISOU 1063 O LYS A 144 9513 9784 9566 -1885 -211 341 A O ATOM 1064 CB LYS A 144 35.621 -7.017 -0.567 1.00 70.27 A C ANISOU 1064 CB LYS A 144 8839 9339 8521 -1945 138 540 A C ATOM 1065 CG LYS A 144 35.182 -5.972 0.463 1.00 72.64 A C ANISOU 1065 CG LYS A 144 9241 9710 8651 -2055 315 668 A C ATOM 1066 CD LYS A 144 35.209 -6.600 1.849 1.00 95.06 A C ANISOU 1066 CD LYS A 144 12332 12321 11466 -2302 264 814 A C ATOM 1067 CE LYS A 144 34.990 -5.603 2.978 1.00103.14 A C ANISOU 1067 CE LYS A 144 13489 13389 12311 -2401 409 947 A C ATOM 1068 NZ LYS A 144 35.004 -6.306 4.308 1.00105.19 A N1+ ANISOU 1068 NZ LYS A 144 13993 13438 12538 -2630 355 1092 A N1+ ATOM 1069 N ILE A 145 38.463 -9.275 -1.298 1.00 67.20 A N ANISOU 1069 N ILE A 145 8599 8465 8471 -1724 -416 513 A N ATOM 1070 CA ILE A 145 38.849 -10.356 -2.195 1.00 64.42 A C ANISOU 1070 CA ILE A 145 8181 8018 8278 -1616 -581 386 A C ATOM 1071 C ILE A 145 39.456 -11.511 -1.412 1.00 65.70 A C ANISOU 1071 C ILE A 145 8571 7864 8529 -1734 -750 482 A C ATOM 1072 O ILE A 145 40.198 -11.281 -0.463 1.00 71.54 A O ANISOU 1072 O ILE A 145 9482 8494 9206 -1774 -796 647 A O ATOM 1073 CB ILE A 145 39.874 -9.861 -3.218 1.00 63.19 A C ANISOU 1073 CB ILE A 145 7881 7983 8145 -1318 -646 326 A C ATOM 1074 CG1 ILE A 145 39.296 -8.705 -4.033 1.00 63.35 A C ANISOU 1074 CG1 ILE A 145 7681 8314 8073 -1175 -468 246 A C ATOM 1075 CG2 ILE A 145 40.314 -10.985 -4.138 1.00 59.82 A C ANISOU 1075 CG2 ILE A 145 7393 7462 7873 -1189 -820 189 A C ATOM 1076 CD1 ILE A 145 38.227 -9.120 -4.974 1.00 70.46 A C ANISOU 1076 CD1 ILE A 145 8397 9362 9013 -1151 -421 57 A C ATOM 1077 N LEU A 146 39.130 -12.747 -1.797 1.00 66.25 A N ANISOU 1077 N LEU A 146 8644 7788 8741 -1789 -840 376 A N ATOM 1078 CA LEU A 146 39.842 -13.926 -1.297 1.00 69.60 A C ANISOU 1078 CA LEU A 146 9271 7900 9274 -1839 -1016 451 A C ATOM 1079 C LEU A 146 40.734 -14.498 -2.392 1.00 77.81 A C ANISOU 1079 C LEU A 146 10218 8903 10442 -1596 -1185 322 A C ATOM 1080 O LEU A 146 40.305 -14.631 -3.542 1.00 80.50 A O ANISOU 1080 O LEU A 146 10362 9379 10846 -1489 -1174 123 A O ATOM 1081 CB LEU A 146 38.877 -15.004 -0.837 1.00 72.02 A C ANISOU 1081 CB LEU A 146 9684 8014 9667 -2094 -994 441 A C ATOM 1082 CG LEU A 146 37.851 -14.524 0.181 1.00 80.12 A C ANISOU 1082 CG LEU A 146 10781 9090 10569 -2341 -812 555 A C ATOM 1083 CD1 LEU A 146 36.932 -15.660 0.542 1.00 80.90 A C ANISOU 1083 CD1 LEU A 146 10969 8991 10777 -2590 -788 540 A C ATOM 1084 CD2 LEU A 146 38.546 -13.985 1.408 1.00 78.07 A C ANISOU 1084 CD2 LEU A 146 10724 8765 10174 -2378 -817 785 A C ATOM 1085 N HIS A 147 41.970 -14.843 -2.035 1.00 73.89 A N ANISOU 1085 N HIS A 147 9861 8239 9975 -1499 -1342 431 A N ATOM 1086 CA HIS A 147 42.913 -15.359 -3.016 1.00 73.65 A C ANISOU 1086 CA HIS A 147 9751 8176 10056 -1251 -1503 324 A C ATOM 1087 C HIS A 147 42.574 -16.788 -3.388 1.00 74.85 A C ANISOU 1087 C HIS A 147 9954 8107 10377 -1303 -1600 201 A C ATOM 1088 O HIS A 147 42.509 -17.140 -4.574 1.00 71.00 A O ANISOU 1088 O HIS A 147 9304 7693 9981 -1152 -1647 -2 A O ATOM 1089 CB HIS A 147 44.344 -15.293 -2.494 1.00 79.82 A C ANISOU 1089 CB HIS A 147 10655 8857 10815 -1129 -1642 479 A C ATOM 1090 CG HIS A 147 45.359 -15.666 -3.521 1.00 83.21 A C ANISOU 1090 CG HIS A 147 10980 9296 11341 -851 -1791 377 A C ATOM 1091 CD2 HIS A 147 46.079 -14.909 -4.383 1.00 80.64 A C ANISOU 1091 CD2 HIS A 147 10466 9184 10989 -606 -1798 321 A C ATOM 1092 ND1 HIS A 147 45.697 -16.975 -3.789 1.00 85.17 A N ANISOU 1092 ND1 HIS A 147 11314 9313 11733 -797 -1947 316 A N ATOM 1093 CE1 HIS A 147 46.593 -17.006 -4.756 1.00 84.48 A C ANISOU 1093 CE1 HIS A 147 11096 9307 11697 -524 -2050 224 A C ATOM 1094 NE2 HIS A 147 46.845 -15.765 -5.134 1.00 78.84 A N ANISOU 1094 NE2 HIS A 147 10210 8866 10880 -405 -1960 230 A N ATOM 1095 N ARG A 148 42.372 -17.599 -2.353 1.00 75.89 A N ANISOU 1095 N ARG A 148 10320 7965 10548 -1515 -1627 327 A N ATOM 1096 CA ARG A 148 41.886 -18.970 -2.490 1.00 81.28 A C ANISOU 1096 CA ARG A 148 11091 8393 11401 -1630 -1686 235 A C ATOM 1097 C ARG A 148 42.833 -19.912 -3.214 1.00 85.13 A C ANISOU 1097 C ARG A 148 11597 8716 12032 -1418 -1878 141 A C ATOM 1098 O ARG A 148 42.388 -20.893 -3.790 1.00 88.95 A O ANISOU 1098 O ARG A 148 12067 9060 12668 -1452 -1921 -23 A O ATOM 1099 CB ARG A 148 40.549 -18.983 -3.208 1.00 81.67 A C ANISOU 1099 CB ARG A 148 10954 8586 11492 -1742 -1564 28 A C ATOM 1100 CG ARG A 148 39.489 -18.180 -2.519 1.00 91.25 A C ANISOU 1100 CG ARG A 148 12145 9952 12575 -1959 -1367 107 A C ATOM 1101 CD ARG A 148 38.122 -18.768 -2.822 1.00 96.66 A C ANISOU 1101 CD ARG A 148 12745 10628 13353 -2166 -1276 -54 A C ATOM 1102 NE ARG A 148 37.791 -18.681 -4.239 1.00 92.24 A N ANISOU 1102 NE ARG A 148 11915 10290 12842 -2005 -1286 -324 A N ATOM 1103 CZ ARG A 148 36.623 -19.052 -4.745 1.00 94.79 A C ANISOU 1103 CZ ARG A 148 12096 10686 13235 -2140 -1216 -516 A C ATOM 1104 NH1 ARG A 148 35.686 -19.541 -3.946 1.00102.52 A N1+ ANISOU 1104 NH1 ARG A 148 13177 11519 14258 -2449 -1123 -460 A N1+ ATOM 1105 NH2 ARG A 148 36.392 -18.937 -6.045 1.00 93.84 A N ANISOU 1105 NH2 ARG A 148 11725 10792 13137 -1965 -1238 -765 A N ATOM 1106 N ASP A 149 44.128 -19.623 -3.193 1.00 84.59 A N ANISOU 1106 N ASP A 149 11553 8666 11920 -1199 -1994 235 A N ATOM 1107 CA ASP A 149 45.084 -20.482 -3.874 1.00 93.36 A C ANISOU 1107 CA ASP A 149 12678 9637 13158 -973 -2175 153 A C ATOM 1108 C ASP A 149 46.486 -20.126 -3.423 1.00 90.47 A C ANISOU 1108 C ASP A 149 12384 9272 12717 -795 -2287 327 A C ATOM 1109 O ASP A 149 47.429 -20.047 -4.221 1.00 86.90 A O ANISOU 1109 O ASP A 149 11817 8913 12290 -527 -2391 256 A O ATOM 1110 CB ASP A 149 44.945 -20.368 -5.396 1.00101.62 A C ANISOU 1110 CB ASP A 149 13461 10893 14258 -772 -2183 -111 A C ATOM 1111 CG ASP A 149 45.723 -21.447 -6.141 1.00101.70 A C ANISOU 1111 CG ASP A 149 13495 10730 14417 -563 -2362 -232 A C ATOM 1112 OD1 ASP A 149 46.122 -22.438 -5.489 1.00 98.94 A O ANISOU 1112 OD1 ASP A 149 13377 10060 14156 -615 -2465 -131 A O ATOM 1113 OD2 ASP A 149 45.937 -21.295 -7.368 1.00 98.67 A O1- ANISOU 1113 OD2 ASP A 149 12903 10534 14054 -334 -2396 -422 A O1- ATOM 1114 N MET A 150 46.608 -19.906 -2.123 1.00 86.16 A N ANISOU 1114 N MET A 150 12025 8638 12074 -948 -2264 553 A N ATOM 1115 CA MET A 150 47.894 -19.618 -1.526 1.00 84.01 A C ANISOU 1115 CA MET A 150 11837 8360 11724 -813 -2377 725 A C ATOM 1116 C MET A 150 48.793 -20.831 -1.631 1.00 95.42 A C ANISOU 1116 C MET A 150 13413 9550 13292 -656 -2568 740 A C ATOM 1117 O MET A 150 48.412 -21.928 -1.246 1.00106.08 A O ANISOU 1117 O MET A 150 14952 10615 14740 -774 -2597 768 A O ATOM 1118 CB MET A 150 47.709 -19.244 -0.062 1.00 83.05 A C ANISOU 1118 CB MET A 150 11903 8186 11465 -1025 -2313 951 A C ATOM 1119 CG MET A 150 47.111 -17.878 0.126 1.00 78.67 A C ANISOU 1119 CG MET A 150 11225 7902 10764 -1131 -2140 959 A C ATOM 1120 SD MET A 150 48.206 -16.643 -0.566 1.00 89.36 A S ANISOU 1120 SD MET A 150 12353 9551 12047 -871 -2170 920 A S ATOM 1121 CE MET A 150 49.588 -16.827 0.540 1.00 98.72 A C ANISOU 1121 CE MET A 150 13730 10613 13168 -808 -2342 1135 A C ATOM 1122 N LYS A 151 49.986 -20.630 -2.168 1.00 98.77 A N ANISOU 1122 N LYS A 151 13736 10076 13716 -386 -2690 722 A N ATOM 1123 CA LYS A 151 50.996 -21.680 -2.220 1.00100.88 A C ANISOU 1123 CA LYS A 151 14122 10128 14079 -199 -2878 755 A C ATOM 1124 C LYS A 151 52.276 -21.044 -2.736 1.00 97.15 A C ANISOU 1124 C LYS A 151 13484 9869 13561 80 -2973 753 A C ATOM 1125 O LYS A 151 52.235 -20.196 -3.621 1.00 98.50 A O ANISOU 1125 O LYS A 151 13417 10304 13706 179 -2902 629 A O ATOM 1126 CB LYS A 151 50.541 -22.867 -3.089 1.00 98.96 A C ANISOU 1126 CB LYS A 151 13893 9689 14020 -159 -2920 564 A C ATOM 1127 CG LYS A 151 50.467 -22.606 -4.592 1.00103.69 A C ANISOU 1127 CG LYS A 151 14222 10502 14676 29 -2909 310 A C ATOM 1128 CD LYS A 151 49.756 -23.747 -5.341 1.00110.94 A C ANISOU 1128 CD LYS A 151 15160 11226 15767 3 -2929 98 A C ATOM 1129 CE LYS A 151 49.858 -23.585 -6.867 1.00118.03 A C ANISOU 1129 CE LYS A 151 15797 12342 16708 243 -2949 -158 A C ATOM 1130 NZ LYS A 151 48.618 -24.027 -7.609 1.00124.08 A N1+ ANISOU 1130 NZ LYS A 151 16480 13096 17571 121 -2875 -402 A N1+ ATOM 1131 N ALA A 152 53.406 -21.421 -2.160 1.00 96.16 A N ANISOU 1131 N ALA A 152 13479 9640 13418 207 -3125 899 A N ATOM 1132 CA ALA A 152 54.669 -20.778 -2.489 1.00 99.80 A C ANISOU 1132 CA ALA A 152 13782 10309 13827 448 -3214 921 A C ATOM 1133 C ALA A 152 54.829 -20.516 -3.985 1.00103.73 A C ANISOU 1133 C ALA A 152 14017 11001 14395 666 -3199 712 A C ATOM 1134 O ALA A 152 55.474 -19.547 -4.385 1.00109.22 A O ANISOU 1134 O ALA A 152 14516 11954 15029 797 -3180 707 A O ATOM 1135 CB ALA A 152 55.821 -21.605 -1.980 1.00107.21 A C ANISOU 1135 CB ALA A 152 14872 11076 14786 610 -3406 1050 A C ATOM 1136 N ALA A 153 54.244 -21.378 -4.812 1.00 98.51 A N ANISOU 1136 N ALA A 153 13351 10218 13861 704 -3204 537 A N ATOM 1137 CA ALA A 153 54.387 -21.248 -6.261 1.00 97.56 A C ANISOU 1137 CA ALA A 153 12992 10279 13798 933 -3202 328 A C ATOM 1138 C ALA A 153 53.788 -19.938 -6.773 1.00101.80 A C ANISOU 1138 C ALA A 153 13301 11132 14245 883 -3026 258 A C ATOM 1139 O ALA A 153 54.287 -19.322 -7.722 1.00103.93 A O ANISOU 1139 O ALA A 153 13347 11643 14498 1098 -3009 176 A O ATOM 1140 CB ALA A 153 53.759 -22.441 -6.953 1.00 98.98 A C ANISOU 1140 CB ALA A 153 13226 10257 14125 950 -3239 140 A C ATOM 1141 N ASN A 154 52.716 -19.517 -6.118 1.00102.32 A N ANISOU 1141 N ASN A 154 13432 11193 14251 605 -2887 303 A N ATOM 1142 CA ASN A 154 52.018 -18.297 -6.469 1.00 98.94 A C ANISOU 1142 CA ASN A 154 12821 11040 13732 537 -2706 253 A C ATOM 1143 C ASN A 154 52.585 -17.041 -5.791 1.00 98.94 A C ANISOU 1143 C ASN A 154 12782 11210 13600 504 -2646 421 A C ATOM 1144 O ASN A 154 52.036 -15.945 -5.933 1.00 95.77 A O ANISOU 1144 O ASN A 154 12255 11018 13116 436 -2483 408 A O ATOM 1145 CB ASN A 154 50.541 -18.465 -6.152 1.00 94.39 A C ANISOU 1145 CB ASN A 154 12319 10389 13157 263 -2579 204 A C ATOM 1146 CG ASN A 154 49.850 -19.373 -7.129 1.00100.71 A C ANISOU 1146 CG ASN A 154 13064 11121 14081 304 -2598 -22 A C ATOM 1147 ND2 ASN A 154 48.919 -20.177 -6.630 1.00 98.78 A N ANISOU 1147 ND2 ASN A 154 12978 10653 13903 71 -2577 -40 A N ATOM 1148 OD1 ASN A 154 50.140 -19.347 -8.328 1.00105.48 A O ANISOU 1148 OD1 ASN A 154 13481 11879 14719 541 -2627 -184 A O ATOM 1149 N VAL A 155 53.686 -17.199 -5.063 1.00 92.82 A N ANISOU 1149 N VAL A 155 12113 10346 12807 558 -2778 572 A N ATOM 1150 CA VAL A 155 54.341 -16.057 -4.442 1.00 86.86 A C ANISOU 1150 CA VAL A 155 11314 9750 11940 534 -2743 710 A C ATOM 1151 C VAL A 155 55.596 -15.728 -5.236 1.00 81.38 A C ANISOU 1151 C VAL A 155 10427 9221 11273 817 -2820 684 A C ATOM 1152 O VAL A 155 56.552 -16.469 -5.202 1.00 92.40 A O ANISOU 1152 O VAL A 155 11872 10515 12721 971 -2989 718 A O ATOM 1153 CB VAL A 155 54.718 -16.355 -2.973 1.00 87.14 A C ANISOU 1153 CB VAL A 155 11587 9609 11912 387 -2835 904 A C ATOM 1154 CG1 VAL A 155 55.214 -15.105 -2.279 1.00 81.30 A C ANISOU 1154 CG1 VAL A 155 10800 9041 11047 320 -2783 1020 A C ATOM 1155 CG2 VAL A 155 53.527 -16.902 -2.230 1.00 90.98 A C ANISOU 1155 CG2 VAL A 155 12277 9902 12389 128 -2769 938 A C ATOM 1156 N LEU A 156 55.593 -14.621 -5.958 1.00 73.29 A N ANISOU 1156 N LEU A 156 9183 8451 10213 893 -2688 629 A N ATOM 1157 CA LEU A 156 56.742 -14.268 -6.768 1.00 76.29 A C ANISOU 1157 CA LEU A 156 9365 9000 10623 1158 -2737 607 A C ATOM 1158 C LEU A 156 57.611 -13.272 -6.035 1.00 89.94 A C ANISOU 1158 C LEU A 156 11060 10834 12279 1112 -2731 750 A C ATOM 1159 O LEU A 156 57.207 -12.707 -5.022 1.00 97.42 A O ANISOU 1159 O LEU A 156 12118 11756 13142 882 -2663 844 A O ATOM 1160 CB LEU A 156 56.292 -13.637 -8.077 1.00 75.23 A C ANISOU 1160 CB LEU A 156 8997 9090 10496 1294 -2588 468 A C ATOM 1161 CG LEU A 156 55.119 -14.311 -8.786 1.00 76.12 A C ANISOU 1161 CG LEU A 156 9114 9158 10652 1284 -2543 301 A C ATOM 1162 CD1 LEU A 156 54.917 -13.650 -10.130 1.00 77.36 A C ANISOU 1162 CD1 LEU A 156 9017 9578 10797 1478 -2416 175 A C ATOM 1163 CD2 LEU A 156 55.348 -15.802 -8.947 1.00 73.55 A C ANISOU 1163 CD2 LEU A 156 8906 8610 10431 1376 -2727 229 A C ATOM 1164 N ILE A 157 58.812 -13.064 -6.562 1.00 88.89 A N ANISOU 1164 N ILE A 157 10768 10827 12181 1333 -2802 758 A N ATOM 1165 CA ILE A 157 59.685 -11.996 -6.111 1.00 82.85 A C ANISOU 1165 CA ILE A 157 9908 10204 11366 1310 -2777 861 A C ATOM 1166 C ILE A 157 60.420 -11.413 -7.309 1.00 91.23 A C ANISOU 1166 C ILE A 157 10699 11488 12477 1555 -2723 805 A C ATOM 1167 O ILE A 157 60.855 -12.151 -8.191 1.00101.76 A O ANISOU 1167 O ILE A 157 11951 12831 13881 1793 -2812 730 A O ATOM 1168 CB ILE A 157 60.737 -12.502 -5.134 1.00 77.39 A C ANISOU 1168 CB ILE A 157 9332 9410 10663 1311 -2979 978 A C ATOM 1169 CG1 ILE A 157 60.102 -13.346 -4.033 1.00 62.54 A C ANISOU 1169 CG1 ILE A 157 7735 7286 8741 1120 -3057 1044 A C ATOM 1170 CG2 ILE A 157 61.511 -11.324 -4.546 1.00 79.33 A C ANISOU 1170 CG2 ILE A 157 9485 9805 10850 1234 -2946 1069 A C ATOM 1171 CD1 ILE A 157 61.085 -13.650 -2.914 1.00 56.11 A C ANISOU 1171 CD1 ILE A 157 7040 6400 7878 1104 -3236 1181 A C ATOM 1172 N THR A 158 60.571 -10.093 -7.332 1.00 93.12 A N ANISOU 1172 N THR A 158 10804 11899 12679 1500 -2570 846 A N ATOM 1173 CA THR A 158 61.251 -9.414 -8.431 1.00104.03 A C ANISOU 1173 CA THR A 158 11926 13496 14106 1716 -2485 815 A C ATOM 1174 C THR A 158 62.756 -9.366 -8.210 1.00110.17 A C ANISOU 1174 C THR A 158 12609 14330 14921 1823 -2621 891 A C ATOM 1175 O THR A 158 63.237 -9.693 -7.128 1.00104.04 A O ANISOU 1175 O THR A 158 11966 13445 14119 1712 -2769 970 A O ATOM 1176 CB THR A 158 60.758 -7.967 -8.589 1.00107.15 A C ANISOU 1176 CB THR A 158 12215 14040 14457 1613 -2239 833 A C ATOM 1177 CG2 THR A 158 59.273 -7.944 -8.874 1.00105.53 A C ANISOU 1177 CG2 THR A 158 12073 13816 14206 1528 -2095 756 A C ATOM 1178 OG1 THR A 158 61.021 -7.234 -7.384 1.00108.30 A O ANISOU 1178 OG1 THR A 158 12446 14150 14552 1384 -2229 936 A O ATOM 1179 N ARG A 159 63.490 -8.951 -9.240 1.00116.24 A N ANISOU 1179 N ARG A 159 13140 15284 15743 2045 -2567 868 A N ATOM 1180 CA ARG A 159 64.926 -8.770 -9.116 1.00113.84 A C ANISOU 1180 CA ARG A 159 12703 15071 15480 2146 -2670 937 A C ATOM 1181 C ARG A 159 65.200 -7.932 -7.880 1.00105.08 A C ANISOU 1181 C ARG A 159 11655 13946 14324 1889 -2660 1034 A C ATOM 1182 O ARG A 159 66.010 -8.310 -7.042 1.00107.62 A O ANISOU 1182 O ARG A 159 12036 14219 14637 1855 -2841 1094 A O ATOM 1183 CB ARG A 159 65.515 -8.075 -10.348 1.00123.82 A C ANISOU 1183 CB ARG A 159 13687 16562 16800 2365 -2538 917 A C ATOM 1184 CG ARG A 159 65.471 -8.899 -11.632 1.00133.45 A C ANISOU 1184 CG ARG A 159 14814 17833 18057 2665 -2566 815 A C ATOM 1185 CD ARG A 159 66.427 -8.365 -12.716 1.00137.25 A C ANISOU 1185 CD ARG A 159 15011 18546 18591 2917 -2485 825 A C ATOM 1186 NE ARG A 159 67.842 -8.625 -12.419 1.00139.73 A N ANISOU 1186 NE ARG A 159 15236 18900 18954 3012 -2650 889 A N ATOM 1187 CZ ARG A 159 68.468 -9.787 -12.633 1.00141.34 A C ANISOU 1187 CZ ARG A 159 15452 19062 19188 3221 -2851 854 A C ATOM 1188 NH1 ARG A 159 67.811 -10.826 -13.141 1.00143.11 A N1+ ANISOU 1188 NH1 ARG A 159 15786 19183 19408 3347 -2917 747 A N1+ ATOM 1189 NH2 ARG A 159 69.756 -9.918 -12.329 1.00137.21 A N ANISOU 1189 NH2 ARG A 159 14832 18600 18702 3305 -2989 920 A N ATOM 1190 N ASP A 160 64.506 -6.805 -7.752 1.00 88.95 A N ANISOU 1190 N ASP A 160 9603 11950 12244 1714 -2451 1043 A N ATOM 1191 CA ASP A 160 64.803 -5.872 -6.672 1.00 90.38 A C ANISOU 1191 CA ASP A 160 9820 12134 12385 1478 -2421 1115 A C ATOM 1192 C ASP A 160 64.243 -6.296 -5.317 1.00 92.65 A C ANISOU 1192 C ASP A 160 10377 12246 12581 1244 -2525 1151 A C ATOM 1193 O ASP A 160 64.134 -5.465 -4.405 1.00 97.73 A O ANISOU 1193 O ASP A 160 11084 12883 13165 1020 -2464 1192 A O ATOM 1194 CB ASP A 160 64.320 -4.465 -7.017 1.00104.03 A C ANISOU 1194 CB ASP A 160 11447 13966 14113 1385 -2150 1115 A C ATOM 1195 CG ASP A 160 64.934 -3.938 -8.303 1.00122.02 A C ANISOU 1195 CG ASP A 160 13458 16426 16478 1612 -2027 1105 A C ATOM 1196 OD1 ASP A 160 65.602 -4.734 -9.003 1.00127.57 A O ANISOU 1196 OD1 ASP A 160 14058 17181 17233 1850 -2149 1082 A O ATOM 1197 OD2 ASP A 160 64.748 -2.735 -8.615 1.00123.91 A O1- ANISOU 1197 OD2 ASP A 160 13595 16753 16730 1560 -1801 1124 A O1- ATOM 1198 N GLY A 161 63.881 -7.572 -5.187 1.00 85.43 A N ANISOU 1198 N GLY A 161 9620 11185 11653 1296 -2671 1136 A N ATOM 1199 CA GLY A 161 63.436 -8.119 -3.913 1.00 89.45 A C ANISOU 1199 CA GLY A 161 10390 11521 12077 1100 -2780 1189 A C ATOM 1200 C GLY A 161 62.037 -7.763 -3.418 1.00 90.03 A C ANISOU 1200 C GLY A 161 10627 11510 12072 868 -2626 1182 A C ATOM 1201 O GLY A 161 61.781 -7.762 -2.211 1.00 92.96 A O ANISOU 1201 O GLY A 161 11183 11786 12353 666 -2671 1245 A O ATOM 1202 N VAL A 162 61.126 -7.471 -4.340 1.00 78.36 A N ANISOU 1202 N VAL A 162 9077 10079 10616 908 -2445 1107 A N ATOM 1203 CA VAL A 162 59.763 -7.164 -3.969 1.00 78.39 A C ANISOU 1203 CA VAL A 162 9214 10023 10548 710 -2294 1094 A C ATOM 1204 C VAL A 162 58.892 -8.393 -4.166 1.00 86.09 A C ANISOU 1204 C VAL A 162 10322 10853 11536 729 -2354 1043 A C ATOM 1205 O VAL A 162 58.816 -8.924 -5.269 1.00 84.21 A O ANISOU 1205 O VAL A 162 9980 10646 11370 923 -2360 956 A O ATOM 1206 CB VAL A 162 59.203 -6.070 -4.852 1.00 86.61 A C ANISOU 1206 CB VAL A 162 10093 11217 11597 742 -2048 1042 A C ATOM 1207 CG1 VAL A 162 58.080 -5.338 -4.122 1.00 90.58 A C ANISOU 1207 CG1 VAL A 162 10724 11689 12003 498 -1882 1060 A C ATOM 1208 CG2 VAL A 162 60.311 -5.105 -5.288 1.00 78.06 A C ANISOU 1208 CG2 VAL A 162 8798 10292 10567 846 -1995 1066 A C ATOM 1209 N LEU A 163 58.240 -8.845 -3.097 1.00 88.41 A N ANISOU 1209 N LEU A 163 10845 10988 11759 526 -2395 1094 A N ATOM 1210 CA LEU A 163 57.349 -10.002 -3.169 1.00 79.44 A C ANISOU 1210 CA LEU A 163 9850 9688 10644 502 -2438 1052 A C ATOM 1211 C LEU A 163 55.951 -9.637 -3.672 1.00 77.42 A C ANISOU 1211 C LEU A 163 9567 9480 10370 417 -2234 968 A C ATOM 1212 O LEU A 163 55.377 -8.621 -3.288 1.00 80.98 A O ANISOU 1212 O LEU A 163 10019 10007 10742 266 -2071 992 A O ATOM 1213 CB LEU A 163 57.235 -10.657 -1.799 1.00 76.61 A C ANISOU 1213 CB LEU A 163 9750 9140 10219 321 -2554 1158 A C ATOM 1214 CG LEU A 163 56.138 -11.712 -1.634 1.00 73.46 A C ANISOU 1214 CG LEU A 163 9529 8549 9834 220 -2557 1137 A C ATOM 1215 CD1 LEU A 163 56.545 -12.669 -0.542 1.00 75.37 A C ANISOU 1215 CD1 LEU A 163 9998 8591 10048 162 -2735 1256 A C ATOM 1216 CD2 LEU A 163 54.784 -11.083 -1.327 1.00 63.05 A C ANISOU 1216 CD2 LEU A 163 8260 7256 8440 0 -2355 1122 A C ATOM 1217 N LYS A 164 55.388 -10.480 -4.519 1.00 78.96 A N ANISOU 1217 N LYS A 164 9736 9630 10634 517 -2247 861 A N ATOM 1218 CA LYS A 164 54.075 -10.188 -5.076 1.00 76.06 A C ANISOU 1218 CA LYS A 164 9317 9335 10249 457 -2068 765 A C ATOM 1219 C LYS A 164 53.237 -11.440 -5.114 1.00 74.80 A C ANISOU 1219 C LYS A 164 9281 9001 10137 397 -2131 694 A C ATOM 1220 O LYS A 164 53.702 -12.471 -5.575 1.00 83.03 A O ANISOU 1220 O LYS A 164 10331 9945 11270 543 -2281 640 A O ATOM 1221 CB LYS A 164 54.221 -9.603 -6.473 1.00 65.68 A C ANISOU 1221 CB LYS A 164 7748 8237 8970 687 -1966 665 A C ATOM 1222 CG LYS A 164 55.084 -8.339 -6.516 1.00 69.30 A C ANISOU 1222 CG LYS A 164 8072 8858 9402 748 -1885 738 A C ATOM 1223 CD LYS A 164 55.162 -7.794 -7.937 1.00 78.31 A C ANISOU 1223 CD LYS A 164 8969 10212 10575 987 -1765 654 A C ATOM 1224 CE LYS A 164 55.918 -6.477 -8.020 1.00 77.10 A C ANISOU 1224 CE LYS A 164 8678 10208 10408 1032 -1648 731 A C ATOM 1225 NZ LYS A 164 55.451 -5.457 -7.057 1.00 69.50 A N1+ ANISOU 1225 NZ LYS A 164 7808 9236 9362 795 -1509 809 A N1+ ATOM 1226 N LEU A 165 52.016 -11.365 -4.598 1.00 71.37 A N ANISOU 1226 N LEU A 165 8948 8522 9648 178 -2015 694 A N ATOM 1227 CA LEU A 165 51.107 -12.496 -4.684 1.00 71.39 A C ANISOU 1227 CA LEU A 165 9048 8367 9709 96 -2049 614 A C ATOM 1228 C LEU A 165 50.547 -12.526 -6.095 1.00 69.44 A C ANISOU 1228 C LEU A 165 8600 8270 9515 253 -1976 429 A C ATOM 1229 O LEU A 165 50.259 -11.479 -6.678 1.00 71.32 A O ANISOU 1229 O LEU A 165 8668 8734 9696 317 -1822 391 A O ATOM 1230 CB LEU A 165 49.971 -12.378 -3.676 1.00 75.01 A C ANISOU 1230 CB LEU A 165 9663 8749 10090 -194 -1938 677 A C ATOM 1231 CG LEU A 165 50.305 -12.049 -2.227 1.00 84.52 A C ANISOU 1231 CG LEU A 165 11055 9864 11196 -369 -1959 858 A C ATOM 1232 CD1 LEU A 165 49.014 -11.739 -1.483 1.00 90.97 A C ANISOU 1232 CD1 LEU A 165 11972 10670 11924 -627 -1800 892 A C ATOM 1233 CD2 LEU A 165 51.046 -13.192 -1.565 1.00 96.71 A C ANISOU 1233 CD2 LEU A 165 12786 11173 12787 -364 -2163 948 A C ATOM 1234 N ALA A 166 50.400 -13.722 -6.653 1.00 70.20 A N ANISOU 1234 N ALA A 166 8715 8242 9716 326 -2087 311 A N ATOM 1235 CA ALA A 166 49.954 -13.835 -8.036 1.00 76.28 A C ANISOU 1235 CA ALA A 166 9288 9165 10531 499 -2044 115 A C ATOM 1236 C ALA A 166 48.941 -14.947 -8.278 1.00 78.98 A C ANISOU 1236 C ALA A 166 9689 9367 10953 400 -2074 -31 A C ATOM 1237 O ALA A 166 48.528 -15.662 -7.357 1.00 73.71 A O ANISOU 1237 O ALA A 166 9225 8464 10317 181 -2114 30 A O ATOM 1238 CB ALA A 166 51.152 -13.984 -8.975 1.00 77.98 A C ANISOU 1238 CB ALA A 166 9368 9459 10802 810 -2156 66 A C ATOM 1239 N ASP A 167 48.551 -15.071 -9.541 1.00 82.25 A N ANISOU 1239 N ASP A 167 9917 9936 11400 564 -2048 -227 A N ATOM 1240 CA ASP A 167 47.586 -16.066 -9.962 1.00 89.57 A C ANISOU 1240 CA ASP A 167 10854 10768 12409 489 -2074 -410 A C ATOM 1241 C ASP A 167 46.304 -15.912 -9.159 1.00 84.77 A C ANISOU 1241 C ASP A 167 10332 10118 11758 176 -1944 -376 A C ATOM 1242 O ASP A 167 46.079 -16.596 -8.165 1.00 83.40 A O ANISOU 1242 O ASP A 167 10371 9688 11630 -45 -1988 -288 A O ATOM 1243 CB ASP A 167 48.155 -17.480 -9.844 1.00102.69 A C ANISOU 1243 CB ASP A 167 12677 12131 14211 518 -2272 -442 A C ATOM 1244 CG ASP A 167 47.359 -18.494 -10.651 1.00121.52 A C ANISOU 1244 CG ASP A 167 15018 14450 16702 517 -2313 -686 A C ATOM 1245 OD1 ASP A 167 46.505 -18.078 -11.473 1.00116.78 A O ANISOU 1245 OD1 ASP A 167 14226 14084 16060 548 -2207 -848 A O ATOM 1246 OD2 ASP A 167 47.588 -19.709 -10.459 1.00132.92 A O1- ANISOU 1246 OD2 ASP A 167 16623 15608 18273 489 -2450 -720 A O1- ATOM 1247 N PHE A 168 45.477 -14.977 -9.601 1.00 76.97 A N ANISOU 1247 N PHE A 168 9174 9397 10676 174 -1775 -435 A N ATOM 1248 CA PHE A 168 44.161 -14.782 -9.038 1.00 75.73 A C ANISOU 1248 CA PHE A 168 9049 9256 10470 -91 -1635 -434 A C ATOM 1249 C PHE A 168 43.075 -15.503 -9.861 1.00 79.03 A C ANISOU 1249 C PHE A 168 9352 9720 10957 -121 -1629 -677 A C ATOM 1250 O PHE A 168 41.901 -15.120 -9.854 1.00 78.30 A O ANISOU 1250 O PHE A 168 9177 9770 10805 -258 -1488 -734 A O ATOM 1251 CB PHE A 168 43.885 -13.289 -8.931 1.00 65.41 A C ANISOU 1251 CB PHE A 168 7634 8208 9010 -80 -1446 -343 A C ATOM 1252 CG PHE A 168 44.641 -12.617 -7.825 1.00 67.00 A C ANISOU 1252 CG PHE A 168 7983 8329 9144 -157 -1432 -112 A C ATOM 1253 CD1 PHE A 168 43.984 -12.172 -6.691 1.00 68.61 A C ANISOU 1253 CD1 PHE A 168 8315 8489 9265 -410 -1320 16 A C ATOM 1254 CD2 PHE A 168 46.006 -12.421 -7.917 1.00 70.88 A C ANISOU 1254 CD2 PHE A 168 8476 8804 9650 26 -1532 -30 A C ATOM 1255 CE1 PHE A 168 44.674 -11.542 -5.668 1.00 68.61 A C ANISOU 1255 CE1 PHE A 168 8448 8427 9193 -479 -1313 210 A C ATOM 1256 CE2 PHE A 168 46.709 -11.788 -6.893 1.00 67.78 A C ANISOU 1256 CE2 PHE A 168 8206 8353 9194 -51 -1528 165 A C ATOM 1257 CZ PHE A 168 46.041 -11.357 -5.768 1.00 70.46 A C ANISOU 1257 CZ PHE A 168 8679 8645 9447 -304 -1422 279 A C ATOM 1258 N GLY A 169 43.473 -16.564 -10.556 1.00 79.12 A N ANISOU 1258 N GLY A 169 9357 9612 11093 6 -1785 -828 A N ATOM 1259 CA GLY A 169 42.551 -17.300 -11.407 1.00 78.30 A C ANISOU 1259 CA GLY A 169 9135 9549 11064 -8 -1802 -1088 A C ATOM 1260 C GLY A 169 41.432 -17.989 -10.645 1.00 72.19 A C ANISOU 1260 C GLY A 169 8486 8583 10360 -350 -1762 -1108 A C ATOM 1261 O GLY A 169 40.374 -18.285 -11.198 1.00 82.81 A O ANISOU 1261 O GLY A 169 9702 10027 11735 -427 -1718 -1310 A O ATOM 1262 N LEU A 170 41.680 -18.243 -9.365 1.00 65.90 A N ANISOU 1262 N LEU A 170 7935 7518 9585 -554 -1777 -895 A N ATOM 1263 CA LEU A 170 40.696 -18.818 -8.459 1.00 73.65 A C ANISOU 1263 CA LEU A 170 9062 8301 10620 -893 -1718 -857 A C ATOM 1264 C LEU A 170 40.100 -17.782 -7.499 1.00 82.52 A C ANISOU 1264 C LEU A 170 10215 9544 11594 -1079 -1541 -673 A C ATOM 1265 O LEU A 170 39.179 -18.089 -6.737 1.00 90.03 A O ANISOU 1265 O LEU A 170 11261 10383 12563 -1362 -1459 -630 A O ATOM 1266 CB LEU A 170 41.337 -19.934 -7.634 1.00 77.65 A C ANISOU 1266 CB LEU A 170 9848 8403 11253 -994 -1852 -735 A C ATOM 1267 CG LEU A 170 41.258 -21.347 -8.190 1.00 81.93 A C ANISOU 1267 CG LEU A 170 10435 8704 11991 -998 -1982 -929 A C ATOM 1268 CD1 LEU A 170 41.469 -22.359 -7.061 1.00 83.79 A C ANISOU 1268 CD1 LEU A 170 10978 8523 12334 -1198 -2044 -762 A C ATOM 1269 CD2 LEU A 170 39.900 -21.511 -8.817 1.00 89.35 A C ANISOU 1269 CD2 LEU A 170 11198 9780 12972 -1136 -1893 -1168 A C ATOM 1270 N ALA A 171 40.631 -16.565 -7.518 1.00 72.93 A N ANISOU 1270 N ALA A 171 8925 8548 10237 -923 -1476 -563 A N ATOM 1271 CA ALA A 171 40.198 -15.564 -6.563 1.00 70.54 A C ANISOU 1271 CA ALA A 171 8674 8337 9792 -1081 -1316 -385 A C ATOM 1272 C ALA A 171 38.728 -15.221 -6.765 1.00 77.05 A C ANISOU 1272 C ALA A 171 9350 9361 10563 -1223 -1149 -497 A C ATOM 1273 O ALA A 171 38.198 -15.349 -7.869 1.00 79.60 A O ANISOU 1273 O ALA A 171 9466 9863 10917 -1116 -1142 -715 A O ATOM 1274 CB ALA A 171 41.044 -14.324 -6.698 1.00 65.17 A C ANISOU 1274 CB ALA A 171 7920 7852 8988 -873 -1275 -280 A C ATOM 1275 N ARG A 172 38.073 -14.784 -5.693 1.00 77.10 A N ANISOU 1275 N ARG A 172 9458 9352 10482 -1456 -1016 -349 A N ATOM 1276 CA ARG A 172 36.712 -14.263 -5.787 1.00 74.63 A C ANISOU 1276 CA ARG A 172 8999 9266 10091 -1578 -836 -425 A C ATOM 1277 C ARG A 172 36.455 -13.202 -4.722 1.00 77.55 A C ANISOU 1277 C ARG A 172 9457 9709 10300 -1698 -677 -221 A C ATOM 1278 O ARG A 172 37.176 -13.133 -3.723 1.00 78.32 A O ANISOU 1278 O ARG A 172 9766 9626 10366 -1763 -716 -25 A O ATOM 1279 CB ARG A 172 35.686 -15.380 -5.634 1.00 70.79 A C ANISOU 1279 CB ARG A 172 8537 8633 9727 -1832 -839 -535 A C ATOM 1280 CG ARG A 172 35.447 -15.792 -4.199 1.00 76.01 A C ANISOU 1280 CG ARG A 172 9450 9033 10396 -2128 -801 -336 A C ATOM 1281 CD ARG A 172 34.184 -16.612 -4.074 1.00 84.02 A C ANISOU 1281 CD ARG A 172 10439 9978 11507 -2399 -739 -442 A C ATOM 1282 NE ARG A 172 33.033 -15.845 -4.525 1.00 98.82 A N ANISOU 1282 NE ARG A 172 12073 12191 13282 -2417 -575 -559 A N ATOM 1283 CZ ARG A 172 31.815 -16.346 -4.702 1.00109.39 A C ANISOU 1283 CZ ARG A 172 13294 13582 14687 -2612 -504 -706 A C ATOM 1284 NH1 ARG A 172 31.573 -17.634 -4.465 1.00116.69 A N1+ ANISOU 1284 NH1 ARG A 172 14327 14217 15793 -2824 -575 -756 A N1+ ATOM 1285 NH2 ARG A 172 30.841 -15.550 -5.121 1.00106.62 A N ANISOU 1285 NH2 ARG A 172 12713 13574 14223 -2592 -358 -803 A N ATOM 1286 N ALA A 173 35.428 -12.378 -4.938 1.00 72.87 A N ANISOU 1286 N ALA A 173 8700 9389 9597 -1718 -499 -274 A N ATOM 1287 CA ALA A 173 35.027 -11.370 -3.946 1.00 67.42 A C ANISOU 1287 CA ALA A 173 8088 8779 8750 -1838 -329 -101 A C ATOM 1288 C ALA A 173 34.150 -11.985 -2.872 1.00 72.93 A C ANISOU 1288 C ALA A 173 8931 9317 9463 -2164 -270 -26 A C ATOM 1289 O ALA A 173 33.507 -13.014 -3.095 1.00 79.05 A O ANISOU 1289 O ALA A 173 9674 10000 10362 -2302 -309 -146 A O ATOM 1290 CB ALA A 173 34.310 -10.210 -4.597 1.00 48.18 A C ANISOU 1290 CB ALA A 173 5426 6697 6182 -1704 -154 -175 A C ATOM 1291 N PHE A 174 34.126 -11.360 -1.703 1.00 72.91 A N ANISOU 1291 N PHE A 174 9087 9279 9336 -2289 -172 171 A N ATOM 1292 CA PHE A 174 33.344 -11.900 -0.604 1.00 78.96 A C ANISOU 1292 CA PHE A 174 10005 9896 10099 -2591 -103 271 A C ATOM 1293 C PHE A 174 32.573 -10.802 0.080 1.00 93.47 A C ANISOU 1293 C PHE A 174 11833 11926 11754 -2675 106 367 A C ATOM 1294 O PHE A 174 32.926 -9.628 -0.020 1.00 90.14 A O ANISOU 1294 O PHE A 174 11367 11674 11208 -2512 176 407 A O ATOM 1295 CB PHE A 174 34.207 -12.684 0.387 1.00 71.87 A C ANISOU 1295 CB PHE A 174 9390 8660 9256 -2698 -237 443 A C ATOM 1296 CG PHE A 174 35.077 -11.832 1.254 1.00 79.46 A C ANISOU 1296 CG PHE A 174 10511 9604 10077 -2642 -235 635 A C ATOM 1297 CD1 PHE A 174 36.344 -11.459 0.837 1.00 80.25 A C ANISOU 1297 CD1 PHE A 174 10604 9705 10180 -2409 -358 642 A C ATOM 1298 CD2 PHE A 174 34.646 -11.426 2.503 1.00 81.99 A C ANISOU 1298 CD2 PHE A 174 10985 9907 10260 -2826 -114 803 A C ATOM 1299 CE1 PHE A 174 37.164 -10.684 1.651 1.00 80.29 A C ANISOU 1299 CE1 PHE A 174 10747 9696 10065 -2373 -364 804 A C ATOM 1300 CE2 PHE A 174 35.460 -10.649 3.321 1.00 83.78 A C ANISOU 1300 CE2 PHE A 174 11358 10120 10353 -2779 -123 961 A C ATOM 1301 CZ PHE A 174 36.723 -10.283 2.895 1.00 79.85 A C ANISOU 1301 CZ PHE A 174 10847 9622 9871 -2559 -251 956 A C ATOM 1302 N SER A 175 31.501 -11.194 0.758 1.00111.90 A N ANISOU 1302 N SER A 175 14208 14229 14079 -2931 215 401 A N ATOM 1303 CA SER A 175 30.536 -10.239 1.275 1.00119.16 A C ANISOU 1303 CA SER A 175 15078 15365 14831 -3012 430 457 A C ATOM 1304 C SER A 175 30.321 -10.402 2.771 1.00124.71 A C ANISOU 1304 C SER A 175 16026 15902 15458 -3257 497 665 A C ATOM 1305 O SER A 175 30.512 -11.483 3.338 1.00120.33 A O ANISOU 1305 O SER A 175 15640 15075 15003 -3421 405 740 A O ATOM 1306 CB SER A 175 29.204 -10.384 0.532 1.00123.65 A C ANISOU 1306 CB SER A 175 15393 16156 15431 -3068 539 274 A C ATOM 1307 OG SER A 175 28.283 -9.383 0.928 1.00123.43 A O ANISOU 1307 OG SER A 175 15295 16370 15233 -3106 752 319 A O ATOM 1308 N LEU A 176 29.937 -9.299 3.398 1.00137.11 A N ANISOU 1308 N LEU A 176 17617 17638 16841 -3265 663 759 A N ATOM 1309 CA LEU A 176 29.547 -9.291 4.794 1.00148.36 A C ANISOU 1309 CA LEU A 176 19243 18972 18155 -3484 764 944 A C ATOM 1310 C LEU A 176 28.221 -10.046 4.879 1.00158.82 A C ANISOU 1310 C LEU A 176 20483 20317 19543 -3720 869 894 A C ATOM 1311 O LEU A 176 27.187 -9.580 4.394 1.00155.06 A O ANISOU 1311 O LEU A 176 19792 20102 19024 -3716 1015 782 A O ATOM 1312 CB LEU A 176 29.429 -7.845 5.294 1.00147.73 A C ANISOU 1312 CB LEU A 176 19180 19092 17860 -3406 922 1021 A C ATOM 1313 CG LEU A 176 30.658 -6.934 5.071 1.00142.39 A C ANISOU 1313 CG LEU A 176 18541 18432 17129 -3169 844 1040 A C ATOM 1314 CD1 LEU A 176 30.961 -6.675 3.585 1.00132.15 A C ANISOU 1314 CD1 LEU A 176 17011 17278 15923 -2922 790 865 A C ATOM 1315 CD2 LEU A 176 30.516 -5.606 5.817 1.00141.70 A C ANISOU 1315 CD2 LEU A 176 18523 18483 16834 -3145 1007 1134 A C ATOM 1316 N ALA A 177 28.270 -11.234 5.471 1.00172.31 A N ANISOU 1316 N ALA A 177 22356 21751 21364 -3920 796 978 A N ATOM 1317 CA ALA A 177 27.148 -12.163 5.419 1.00187.06 A C ANISOU 1317 CA ALA A 177 24139 23585 23350 -4155 867 912 A C ATOM 1318 C ALA A 177 26.125 -11.953 6.533 1.00200.69 A C ANISOU 1318 C ALA A 177 25933 25374 24945 -4383 1073 1054 A C ATOM 1319 O ALA A 177 26.071 -12.731 7.488 1.00206.88 A O ANISOU 1319 O ALA A 177 26920 25926 25759 -4591 1080 1213 A O ATOM 1320 CB ALA A 177 27.657 -13.603 5.435 1.00188.55 A C ANISOU 1320 CB ALA A 177 24468 23427 23747 -4261 701 925 A C ATOM 1321 N LYS A 178 25.314 -10.906 6.410 1.00204.03 A N ANISOU 1321 N LYS A 178 26187 26113 25220 -4334 1247 1004 A N ATOM 1322 CA LYS A 178 24.186 -10.720 7.320 1.00207.95 A C ANISOU 1322 CA LYS A 178 26698 26714 25599 -4544 1459 1108 A C ATOM 1323 C LYS A 178 22.855 -10.841 6.571 1.00214.90 A C ANISOU 1323 C LYS A 178 27275 27836 26541 -4627 1580 924 A C ATOM 1324 O LYS A 178 22.830 -11.280 5.419 1.00216.89 A O ANISOU 1324 O LYS A 178 27333 28127 26947 -4555 1481 720 A O ATOM 1325 CB LYS A 178 24.293 -9.400 8.095 1.00199.85 A C ANISOU 1325 CB LYS A 178 25771 25843 24319 -4444 1583 1239 A C ATOM 1326 CG LYS A 178 24.549 -8.172 7.243 1.00191.90 A C ANISOU 1326 CG LYS A 178 24602 25088 23224 -4159 1600 1119 A C ATOM 1327 CD LYS A 178 24.654 -6.932 8.115 1.00185.66 A C ANISOU 1327 CD LYS A 178 23940 24406 22198 -4089 1729 1251 A C ATOM 1328 CE LYS A 178 24.864 -5.677 7.283 1.00178.19 A C ANISOU 1328 CE LYS A 178 22840 23693 21171 -3810 1771 1143 A C ATOM 1329 NZ LYS A 178 24.964 -4.457 8.136 1.00173.94 A N1+ ANISOU 1329 NZ LYS A 178 22436 23239 20413 -3748 1902 1259 A N1+ ATOM 1330 N ASN A 179 21.763 -10.457 7.229 1.00216.25 A N ANISOU 1330 N ASN A 179 27399 28180 26585 -4772 1792 990 A N ATOM 1331 CA ASN A 179 20.414 -10.664 6.699 1.00215.84 A C ANISOU 1331 CA ASN A 179 27063 28357 26588 -4895 1919 836 A C ATOM 1332 C ASN A 179 19.971 -12.110 6.890 1.00218.72 A C ANISOU 1332 C ASN A 179 27451 28488 27165 -5197 1891 830 A C ATOM 1333 O ASN A 179 19.086 -12.594 6.185 1.00221.04 A O ANISOU 1333 O ASN A 179 27495 28905 27584 -5303 1923 646 A O ATOM 1334 CB ASN A 179 20.323 -10.280 5.218 1.00213.53 A C ANISOU 1334 CB ASN A 179 26474 28315 26344 -4663 1860 581 A C ATOM 1335 CG ASN A 179 20.654 -8.821 4.969 1.00210.65 A C ANISOU 1335 CG ASN A 179 26069 28189 25779 -4365 1917 588 A C ATOM 1336 ND2 ASN A 179 21.870 -8.559 4.496 1.00206.97 A N ANISOU 1336 ND2 ASN A 179 25684 27620 25334 -4140 1760 576 A N ATOM 1337 OD1 ASN A 179 19.825 -7.939 5.193 1.00210.38 A O ANISOU 1337 OD1 ASN A 179 25930 28426 25579 -4335 2108 605 A O ATOM 1338 N SER A 180 20.605 -12.789 7.844 1.00218.41 A N ANISOU 1338 N SER A 180 27713 28110 27163 -5331 1833 1030 A N ATOM 1339 CA SER A 180 20.302 -14.185 8.174 1.00218.09 A C ANISOU 1339 CA SER A 180 27754 27785 27324 -5621 1816 1071 A C ATOM 1340 C SER A 180 20.323 -15.125 6.966 1.00217.59 A C ANISOU 1340 C SER A 180 27519 27630 27524 -5635 1667 825 A C ATOM 1341 O SER A 180 19.398 -15.917 6.773 1.00219.58 A O ANISOU 1341 O SER A 180 27631 27868 27934 -5872 1732 725 A O ATOM 1342 CB SER A 180 18.961 -14.297 8.909 1.00216.10 A C ANISOU 1342 CB SER A 180 27433 27649 27025 -5897 2052 1149 A C ATOM 1343 OG SER A 180 18.699 -15.638 9.289 1.00214.69 A O ANISOU 1343 OG SER A 180 27353 27170 27050 -6189 2052 1210 A O ATOM 1344 N GLN A 181 21.382 -15.036 6.165 1.00211.67 A N ANISOU 1344 N GLN A 181 26778 26822 26823 -5384 1471 724 A N ATOM 1345 CA GLN A 181 21.560 -15.925 5.018 1.00206.10 A C ANISOU 1345 CA GLN A 181 25939 26015 26356 -5362 1308 490 A C ATOM 1346 C GLN A 181 23.036 -16.181 4.723 1.00198.55 A C ANISOU 1346 C GLN A 181 25163 24814 25462 -5151 1082 511 A C ATOM 1347 O GLN A 181 23.644 -15.462 3.926 1.00198.81 A O ANISOU 1347 O GLN A 181 25095 25014 25431 -4866 993 406 A O ATOM 1348 CB GLN A 181 20.876 -15.356 3.771 1.00203.94 A C ANISOU 1348 CB GLN A 181 25297 26124 26067 -5220 1333 213 A C ATOM 1349 CG GLN A 181 19.359 -15.430 3.794 1.00205.18 A C ANISOU 1349 CG GLN A 181 25216 26510 26232 -5448 1519 121 A C ATOM 1350 CD GLN A 181 18.746 -15.167 2.435 1.00203.60 A C ANISOU 1350 CD GLN A 181 24646 26652 26061 -5314 1498 -186 A C ATOM 1351 NE2 GLN A 181 17.424 -15.266 2.351 1.00203.80 A N ANISOU 1351 NE2 GLN A 181 24428 26903 26103 -5503 1644 -296 A N ATOM 1352 OE1 GLN A 181 19.453 -14.881 1.469 1.00201.42 A O ANISOU 1352 OE1 GLN A 181 24295 26448 25788 -5037 1354 -323 A O ATOM 1353 N PRO A 182 23.619 -17.206 5.367 1.00187.95 A N ANISOU 1353 N PRO A 182 24089 23081 24245 -5284 996 657 A N ATOM 1354 CA PRO A 182 25.023 -17.562 5.135 1.00177.10 A C ANISOU 1354 CA PRO A 182 22891 21461 22940 -5092 778 685 A C ATOM 1355 C PRO A 182 25.334 -17.743 3.653 1.00165.10 A C ANISOU 1355 C PRO A 182 21156 20020 21555 -4897 624 400 A C ATOM 1356 O PRO A 182 24.471 -18.157 2.877 1.00163.74 A O ANISOU 1356 O PRO A 182 20751 19952 21509 -4994 651 176 A O ATOM 1357 CB PRO A 182 25.170 -18.887 5.884 1.00179.55 A C ANISOU 1357 CB PRO A 182 23454 21352 23413 -5324 745 831 A C ATOM 1358 CG PRO A 182 24.192 -18.782 6.991 1.00182.57 A C ANISOU 1358 CG PRO A 182 23898 21774 23697 -5583 964 1010 A C ATOM 1359 CD PRO A 182 23.011 -18.042 6.416 1.00186.32 A C ANISOU 1359 CD PRO A 182 24044 22645 24104 -5610 1113 828 A C ATOM 1360 N ASN A 183 26.566 -17.425 3.274 1.00156.02 A N ANISOU 1360 N ASN A 183 20078 18832 20373 -4622 463 405 A N ATOM 1361 CA ASN A 183 26.990 -17.479 1.879 1.00149.50 A C ANISOU 1361 CA ASN A 183 19057 18102 19642 -4392 316 154 A C ATOM 1362 C ASN A 183 27.097 -18.898 1.342 1.00144.74 A C ANISOU 1362 C ASN A 183 18477 17215 19304 -4485 179 9 A C ATOM 1363 O ASN A 183 27.216 -19.856 2.104 1.00151.45 A O ANISOU 1363 O ASN A 183 19555 17721 20269 -4680 162 146 A O ATOM 1364 CB ASN A 183 28.346 -16.788 1.712 1.00145.15 A C ANISOU 1364 CB ASN A 183 18595 17566 18989 -4083 189 226 A C ATOM 1365 CG ASN A 183 28.287 -15.307 1.995 1.00141.93 A C ANISOU 1365 CG ASN A 183 18131 17457 18338 -3954 315 317 A C ATOM 1366 ND2 ASN A 183 29.230 -14.821 2.802 1.00143.75 A N ANISOU 1366 ND2 ASN A 183 18578 17590 18449 -3871 280 526 A N ATOM 1367 OD1 ASN A 183 27.416 -14.600 1.485 1.00137.86 A O ANISOU 1367 OD1 ASN A 183 17379 17259 17743 -3921 441 194 A O ATOM 1368 N ARG A 184 27.065 -19.029 0.022 1.00132.30 A N ANISOU 1368 N ARG A 184 16668 15778 17821 -4335 85 -269 A N ATOM 1369 CA ARG A 184 27.351 -20.307 -0.605 1.00132.07 A C ANISOU 1369 CA ARG A 184 16663 15479 18037 -4368 -71 -433 A C ATOM 1370 C ARG A 184 28.514 -20.141 -1.560 1.00122.21 A C ANISOU 1370 C ARG A 184 15379 14261 16793 -4023 -258 -541 A C ATOM 1371 O ARG A 184 28.316 -19.885 -2.743 1.00122.15 A O ANISOU 1371 O ARG A 184 15113 14507 16790 -3856 -299 -789 A O ATOM 1372 CB ARG A 184 26.124 -20.844 -1.346 1.00142.29 A C ANISOU 1372 CB ARG A 184 17698 16893 19471 -4544 -19 -711 A C ATOM 1373 CG ARG A 184 25.213 -21.707 -0.488 1.00148.20 A C ANISOU 1373 CG ARG A 184 18545 17415 20349 -4936 102 -632 A C ATOM 1374 CD ARG A 184 24.908 -23.025 -1.180 1.00154.05 A C ANISOU 1374 CD ARG A 184 19225 17935 21372 -5085 9 -879 A C ATOM 1375 NE ARG A 184 24.639 -24.096 -0.225 1.00161.28 A N ANISOU 1375 NE ARG A 184 20374 18449 22455 -5413 70 -726 A N ATOM 1376 CZ ARG A 184 24.387 -25.355 -0.569 1.00170.15 A C ANISOU 1376 CZ ARG A 184 21513 19287 23849 -5599 13 -890 A C ATOM 1377 NH1 ARG A 184 24.365 -25.703 -1.850 1.00171.74 A N1+ ANISOU 1377 NH1 ARG A 184 21504 19574 24175 -5488 -118 -1230 A N1+ ATOM 1378 NH2 ARG A 184 24.153 -26.265 0.367 1.00174.82 A N ANISOU 1378 NH2 ARG A 184 22333 19504 24585 -5894 92 -716 A N ATOM 1379 N TYR A 185 29.731 -20.258 -1.041 1.00116.16 A N ANISOU 1379 N TYR A 185 14866 13259 16013 -3906 -368 -350 A N ATOM 1380 CA TYR A 185 30.906 -20.166 -1.897 1.00115.32 A C ANISOU 1380 CA TYR A 185 14735 13162 15921 -3583 -546 -436 A C ATOM 1381 C TYR A 185 31.370 -21.571 -2.238 1.00115.48 A C ANISOU 1381 C TYR A 185 14871 12827 16178 -3608 -709 -535 A C ATOM 1382 O TYR A 185 31.079 -22.516 -1.512 1.00122.03 A O ANISOU 1382 O TYR A 185 15885 13344 17136 -3859 -687 -445 A O ATOM 1383 CB TYR A 185 32.055 -19.382 -1.234 1.00116.49 A C ANISOU 1383 CB TYR A 185 15058 13297 15907 -3404 -583 -189 A C ATOM 1384 CG TYR A 185 31.753 -17.938 -0.879 1.00105.86 A C ANISOU 1384 CG TYR A 185 13625 12272 14326 -3354 -430 -86 A C ATOM 1385 CD1 TYR A 185 30.934 -17.164 -1.684 1.00106.32 A C ANISOU 1385 CD1 TYR A 185 13397 12694 14307 -3283 -325 -259 A C ATOM 1386 CD2 TYR A 185 32.301 -17.349 0.253 1.00 97.72 A C ANISOU 1386 CD2 TYR A 185 12799 11182 13147 -3365 -393 180 A C ATOM 1387 CE1 TYR A 185 30.649 -15.844 -1.372 1.00100.58 A C ANISOU 1387 CE1 TYR A 185 12600 12244 13370 -3225 -175 -164 A C ATOM 1388 CE2 TYR A 185 32.020 -16.024 0.579 1.00 98.75 A C ANISOU 1388 CE2 TYR A 185 12860 11591 13070 -3320 -248 261 A C ATOM 1389 CZ TYR A 185 31.190 -15.275 -0.245 1.00 98.34 A C ANISOU 1389 CZ TYR A 185 12531 11880 12955 -3248 -135 91 A C ATOM 1390 OH TYR A 185 30.892 -13.953 0.039 1.00 94.45 A O ANISOU 1390 OH TYR A 185 11973 11655 12261 -3189 18 167 A O HETATM 1391 N TPO A 186 32.088 -21.693 -3.348 1.00111.46 A N ANISOU 1391 N TPO A 186 14256 12368 15724 -3340 -863 -719 A N HETATM 1392 CA TPO A 186 32.678 -22.985 -3.812 1.00106.12 A C ANISOU 1392 CA TPO A 186 13686 11366 15270 -3302 -1037 -838 A C HETATM 1393 C TPO A 186 33.597 -23.566 -2.781 1.00107.39 A C ANISOU 1393 C TPO A 186 14185 11147 15470 -3334 -1108 -572 A C HETATM 1394 O TPO A 186 34.441 -22.867 -2.220 1.00107.09 A O ANISOU 1394 O TPO A 186 14259 11152 15280 -3191 -1127 -358 A O HETATM 1395 CB TPO A 186 33.417 -22.562 -5.066 1.00101.57 A C ANISOU 1395 CB TPO A 186 12926 11011 14654 -2943 -1163 -1021 A C HETATM 1396 CG2 TPO A 186 33.479 -23.653 -6.118 1.00 92.67 A C ANISOU 1396 CG2 TPO A 186 11729 9749 13733 -2882 -1305 -1307 A C HETATM 1397 OG1 TPO A 186 32.593 -21.511 -5.548 1.00106.41 A O ANISOU 1397 OG1 TPO A 186 13268 12045 15120 -2907 -1034 -1125 A O HETATM 1398 P TPO A 186 32.998 -20.463 -6.689 1.00105.90 A P ANISOU 1398 P TPO A 186 12953 12373 14911 -2550 -1061 -1254 A P HETATM 1399 O1P TPO A 186 32.904 -19.182 -5.913 1.00 98.98 A O ANISOU 1399 O1P TPO A 186 12093 11692 13822 -2556 -909 -1024 A O HETATM 1400 O2P TPO A 186 34.375 -20.879 -7.194 1.00 85.80 A O1- ANISOU 1400 O2P TPO A 186 10498 9670 12433 -2282 -1253 -1269 A O1- HETATM 1401 O3P TPO A 186 31.865 -20.620 -7.681 1.00113.52 A O ANISOU 1401 O3P TPO A 186 13632 13580 15920 -2592 -1022 -1561 A O ATOM 1402 N ASN A 187 33.448 -24.853 -2.499 1.00114.92 A N ANISOU 1402 N ASN A 187 15310 11726 16629 -3522 -1146 -579 A N ATOM 1403 CA ASN A 187 34.217 -25.450 -1.415 1.00119.69 A C ANISOU 1403 CA ASN A 187 16251 11961 17262 -3567 -1194 -300 A C ATOM 1404 C ASN A 187 35.579 -25.990 -1.829 1.00123.04 A C ANISOU 1404 C ASN A 187 16798 12188 17762 -3290 -1401 -308 A C ATOM 1405 O ASN A 187 36.578 -25.774 -1.144 1.00118.10 A O ANISOU 1405 O ASN A 187 16358 11476 17037 -3159 -1464 -72 A O ATOM 1406 CB ASN A 187 33.433 -26.559 -0.736 1.00123.92 A C ANISOU 1406 CB ASN A 187 16954 12155 17975 -3908 -1110 -244 A C ATOM 1407 CG ASN A 187 34.274 -27.304 0.268 1.00129.12 A C ANISOU 1407 CG ASN A 187 17969 12414 18678 -3919 -1172 33 A C ATOM 1408 ND2 ASN A 187 34.161 -26.917 1.535 1.00132.61 A N ANISOU 1408 ND2 ASN A 187 18578 12834 18973 -4052 -1057 331 A N ATOM 1409 OD1 ASN A 187 35.047 -28.199 -0.092 1.00125.73 A O ANISOU 1409 OD1 ASN A 187 17663 11708 18400 -3789 -1323 -18 A O ATOM 1410 N ARG A 188 35.607 -26.707 -2.943 1.00127.41 A N ANISOU 1410 N ARG A 188 17243 12678 18489 -3199 -1509 -587 A N ATOM 1411 CA ARG A 188 36.834 -27.318 -3.429 1.00130.65 A C ANISOU 1411 CA ARG A 188 17757 12896 18988 -2932 -1704 -624 A C ATOM 1412 C ARG A 188 37.826 -26.281 -3.994 1.00124.36 A C ANISOU 1412 C ARG A 188 16823 12411 18017 -2578 -1791 -624 A C ATOM 1413 O ARG A 188 38.232 -26.347 -5.156 1.00126.04 A O ANISOU 1413 O ARG A 188 16876 12739 18274 -2340 -1901 -850 A O ATOM 1414 CB ARG A 188 36.480 -28.411 -4.447 1.00138.60 A C ANISOU 1414 CB ARG A 188 18688 13740 20234 -2956 -1783 -942 A C ATOM 1415 CG ARG A 188 35.421 -29.389 -3.897 1.00153.81 A C ANISOU 1415 CG ARG A 188 20732 15362 22348 -3339 -1676 -951 A C ATOM 1416 CD ARG A 188 34.578 -30.063 -4.991 1.00158.68 A C ANISOU 1416 CD ARG A 188 21150 15983 23159 -3438 -1692 -1334 A C ATOM 1417 NE ARG A 188 33.293 -30.562 -4.489 1.00154.39 A N ANISOU 1417 NE ARG A 188 20614 15305 22741 -3842 -1537 -1355 A N ATOM 1418 CZ ARG A 188 32.320 -31.047 -5.261 1.00149.80 A C ANISOU 1418 CZ ARG A 188 19836 14763 22317 -4008 -1514 -1676 A C ATOM 1419 NH1 ARG A 188 32.476 -31.106 -6.578 1.00142.57 A N1+ ANISOU 1419 NH1 ARG A 188 18708 14020 21441 -3794 -1642 -2009 A N1+ ATOM 1420 NH2 ARG A 188 31.186 -31.473 -4.718 1.00152.18 A N ANISOU 1420 NH2 ARG A 188 20148 14942 22734 -4388 -1363 -1670 A N ATOM 1421 N VAL A 189 38.214 -25.320 -3.159 1.00117.16 A N ANISOU 1421 N VAL A 189 15973 11635 16906 -2546 -1735 -370 A N ATOM 1422 CA VAL A 189 39.230 -24.336 -3.538 1.00112.09 A C ANISOU 1422 CA VAL A 189 15229 11250 16109 -2236 -1807 -333 A C ATOM 1423 C VAL A 189 40.552 -24.562 -2.806 1.00109.70 A C ANISOU 1423 C VAL A 189 15168 10737 15777 -2095 -1931 -93 A C ATOM 1424 O VAL A 189 40.609 -25.270 -1.796 1.00106.76 A O ANISOU 1424 O VAL A 189 15056 10057 15453 -2251 -1933 97 A O ATOM 1425 CB VAL A 189 38.765 -22.884 -3.292 1.00106.30 A C ANISOU 1425 CB VAL A 189 14341 10887 15159 -2263 -1654 -259 A C ATOM 1426 CG1 VAL A 189 38.025 -22.349 -4.497 1.00103.58 A C ANISOU 1426 CG1 VAL A 189 13679 10878 14798 -2190 -1594 -530 A C ATOM 1427 CG2 VAL A 189 37.908 -22.787 -2.033 1.00106.48 A C ANISOU 1427 CG2 VAL A 189 14506 10831 15122 -2582 -1497 -65 A C ATOM 1428 N VAL A 190 41.611 -23.956 -3.328 1.00107.66 A N ANISOU 1428 N VAL A 190 14815 10656 15435 -1795 -2031 -101 A N ATOM 1429 CA VAL A 190 42.938 -24.051 -2.718 1.00108.87 A C ANISOU 1429 CA VAL A 190 15152 10670 15543 -1631 -2159 110 A C ATOM 1430 C VAL A 190 43.546 -25.439 -2.863 1.00115.47 A C ANISOU 1430 C VAL A 190 16166 11144 16564 -1547 -2314 82 A C ATOM 1431 O VAL A 190 42.893 -26.435 -2.554 1.00114.15 A O ANISOU 1431 O VAL A 190 16145 10689 16539 -1754 -2285 70 A O ATOM 1432 CB VAL A 190 42.915 -23.720 -1.209 1.00 99.48 A C ANISOU 1432 CB VAL A 190 14174 9402 14223 -1814 -2084 411 A C ATOM 1433 CG1 VAL A 190 44.337 -23.556 -0.695 1.00 94.72 A C ANISOU 1433 CG1 VAL A 190 13697 8758 13535 -1607 -2222 603 A C ATOM 1434 CG2 VAL A 190 42.088 -22.474 -0.941 1.00 97.70 A C ANISOU 1434 CG2 VAL A 190 13807 9483 13831 -1951 -1906 436 A C ATOM 1435 N THR A 191 44.802 -25.488 -3.315 1.00120.56 A N ANISOU 1435 N THR A 191 16798 11802 17207 -1244 -2471 80 A N ATOM 1436 CA THR A 191 45.581 -26.725 -3.362 1.00122.06 A C ANISOU 1436 CA THR A 191 17175 11656 17547 -1115 -2628 89 A C ATOM 1437 C THR A 191 45.356 -27.529 -2.096 1.00125.15 A C ANISOU 1437 C THR A 191 17877 11690 17984 -1338 -2601 315 A C ATOM 1438 O THR A 191 45.072 -26.967 -1.034 1.00129.05 A O ANISOU 1438 O THR A 191 18458 12233 18341 -1509 -2502 528 A O ATOM 1439 CB THR A 191 47.092 -26.443 -3.467 1.00125.68 A C ANISOU 1439 CB THR A 191 17630 12194 17930 -789 -2781 184 A C ATOM 1440 CG2 THR A 191 47.889 -27.744 -3.410 1.00131.18 A C ANISOU 1440 CG2 THR A 191 18541 12532 18772 -650 -2938 218 A C ATOM 1441 OG1 THR A 191 47.377 -25.768 -4.697 1.00124.11 A O ANISOU 1441 OG1 THR A 191 17147 12309 17698 -560 -2805 -17 A O ATOM 1442 N LEU A 192 45.494 -28.843 -2.197 1.00123.43 A N ANISOU 1442 N LEU A 192 17835 11109 17955 -1327 -2683 274 A N ATOM 1443 CA LEU A 192 45.244 -29.690 -1.047 1.00121.15 A C ANISOU 1443 CA LEU A 192 17851 10453 17726 -1534 -2643 492 A C ATOM 1444 C LEU A 192 46.182 -29.374 0.125 1.00123.35 A C ANISOU 1444 C LEU A 192 18316 10715 17836 -1449 -2695 819 A C ATOM 1445 O LEU A 192 45.726 -29.158 1.250 1.00125.35 A O ANISOU 1445 O LEU A 192 18708 10928 17990 -1663 -2587 1035 A O ATOM 1446 CB LEU A 192 45.338 -31.161 -1.430 1.00119.33 A C ANISOU 1446 CB LEU A 192 17783 9819 17739 -1504 -2727 386 A C ATOM 1447 CG LEU A 192 44.869 -32.087 -0.310 1.00124.43 A C ANISOU 1447 CG LEU A 192 18741 10063 18474 -1756 -2649 598 A C ATOM 1448 CD1 LEU A 192 43.367 -31.925 -0.083 1.00123.91 A C ANISOU 1448 CD1 LEU A 192 18609 10031 18441 -2130 -2450 542 A C ATOM 1449 CD2 LEU A 192 45.231 -33.531 -0.612 1.00130.43 A C ANISOU 1449 CD2 LEU A 192 19699 10390 19468 -1670 -2748 533 A C ATOM 1450 N TRP A 193 47.485 -29.333 -0.133 1.00122.96 A N ANISOU 1450 N TRP A 193 18260 10713 17747 -1133 -2860 851 A N ATOM 1451 CA TRP A 193 48.456 -29.187 0.955 1.00127.49 A C ANISOU 1451 CA TRP A 193 19015 11251 18174 -1032 -2936 1147 A C ATOM 1452 C TRP A 193 48.303 -27.864 1.720 1.00118.16 A C ANISOU 1452 C TRP A 193 17756 10380 16758 -1141 -2841 1294 A C ATOM 1453 O TRP A 193 48.479 -27.806 2.946 1.00105.50 A O ANISOU 1453 O TRP A 193 16348 8706 15031 -1223 -2826 1554 A O ATOM 1454 CB TRP A 193 49.890 -29.352 0.435 1.00136.05 A C ANISOU 1454 CB TRP A 193 20065 12366 19263 -661 -3133 1128 A C ATOM 1455 CG TRP A 193 50.176 -30.702 -0.190 1.00144.71 A C ANISOU 1455 CG TRP A 193 21277 13129 20576 -522 -3238 1011 A C ATOM 1456 CD1 TRP A 193 49.506 -31.870 0.033 1.00147.62 A C ANISOU 1456 CD1 TRP A 193 21861 13107 21122 -694 -3190 1011 A C ATOM 1457 CD2 TRP A 193 51.219 -31.012 -1.131 1.00147.91 A C ANISOU 1457 CD2 TRP A 193 21594 13559 21047 -181 -3402 877 A C ATOM 1458 CE2 TRP A 193 51.114 -32.382 -1.435 1.00147.47 A C ANISOU 1458 CE2 TRP A 193 21714 13113 21205 -157 -3450 792 A C ATOM 1459 CE3 TRP A 193 52.229 -30.263 -1.747 1.00146.19 A C ANISOU 1459 CE3 TRP A 193 21162 13653 20731 105 -3506 822 A C ATOM 1460 NE1 TRP A 193 50.061 -32.883 -0.715 1.00150.05 A N ANISOU 1460 NE1 TRP A 193 22226 13183 21603 -480 -3316 876 A N ATOM 1461 CZ2 TRP A 193 51.978 -33.016 -2.326 1.00143.72 A C ANISOU 1461 CZ2 TRP A 193 21212 12557 20837 155 -3601 649 A C ATOM 1462 CZ3 TRP A 193 53.085 -30.899 -2.633 1.00140.33 A C ANISOU 1462 CZ3 TRP A 193 20385 12842 20094 411 -3652 688 A C ATOM 1463 CH2 TRP A 193 52.952 -32.257 -2.914 1.00137.89 A C ANISOU 1463 CH2 TRP A 193 20256 12148 19986 440 -3701 600 A C ATOM 1464 N TYR A 194 47.972 -26.804 0.990 1.00119.80 A N ANISOU 1464 N TYR A 194 17685 10931 16902 -1134 -2775 1125 A N ATOM 1465 CA TYR A 194 47.818 -25.493 1.598 1.00112.82 A C ANISOU 1465 CA TYR A 194 16715 10345 15809 -1225 -2678 1233 A C ATOM 1466 C TYR A 194 46.358 -25.179 1.886 1.00113.44 A C ANISOU 1466 C TYR A 194 16764 10470 15867 -1542 -2475 1206 A C ATOM 1467 O TYR A 194 46.020 -24.037 2.199 1.00114.14 A O ANISOU 1467 O TYR A 194 16745 10826 15795 -1626 -2368 1244 A O ATOM 1468 CB TYR A 194 48.388 -24.421 0.691 1.00105.20 A C ANISOU 1468 CB TYR A 194 15467 9733 14771 -1013 -2713 1094 A C ATOM 1469 CG TYR A 194 49.820 -24.631 0.284 1.00107.86 A C ANISOU 1469 CG TYR A 194 15783 10074 15127 -692 -2903 1099 A C ATOM 1470 CD1 TYR A 194 50.842 -23.905 0.878 1.00114.89 A C ANISOU 1470 CD1 TYR A 194 16671 11120 15861 -569 -2976 1260 A C ATOM 1471 CD2 TYR A 194 50.151 -25.531 -0.711 1.00112.31 A C ANISOU 1471 CD2 TYR A 194 16314 10500 15861 -509 -3009 931 A C ATOM 1472 CE1 TYR A 194 52.164 -24.073 0.497 1.00121.05 A C ANISOU 1472 CE1 TYR A 194 17408 11927 16657 -274 -3148 1263 A C ATOM 1473 CE2 TYR A 194 51.469 -25.712 -1.099 1.00123.56 A C ANISOU 1473 CE2 TYR A 194 17708 11944 17297 -201 -3179 936 A C ATOM 1474 CZ TYR A 194 52.475 -24.978 -0.494 1.00125.87 A C ANISOU 1474 CZ TYR A 194 17988 12403 17435 -85 -3246 1106 A C ATOM 1475 OH TYR A 194 53.790 -25.154 -0.880 1.00126.00 A O ANISOU 1475 OH TYR A 194 17955 12456 17462 220 -3413 1111 A O ATOM 1476 N ARG A 195 45.496 -26.187 1.771 1.00110.13 A N ANISOU 1476 N ARG A 195 16436 9791 15616 -1716 -2419 1135 A N ATOM 1477 CA ARG A 195 44.089 -26.018 2.107 1.00107.53 A C ANISOU 1477 CA ARG A 195 16088 9485 15282 -2033 -2225 1119 A C ATOM 1478 C ARG A 195 43.889 -26.141 3.617 1.00111.18 A C ANISOU 1478 C ARG A 195 16811 9795 15636 -2227 -2148 1417 A C ATOM 1479 O ARG A 195 44.566 -26.934 4.272 1.00114.97 A O ANISOU 1479 O ARG A 195 17536 10008 16141 -2164 -2242 1599 A O ATOM 1480 CB ARG A 195 43.223 -27.041 1.365 1.00108.10 A C ANISOU 1480 CB ARG A 195 16136 9350 15588 -2161 -2190 908 A C ATOM 1481 CG ARG A 195 41.727 -26.854 1.584 1.00111.85 A C ANISOU 1481 CG ARG A 195 16544 9884 16071 -2487 -1988 860 A C ATOM 1482 CD ARG A 195 40.909 -27.860 0.821 1.00121.92 A C ANISOU 1482 CD ARG A 195 17775 10965 17585 -2620 -1964 628 A C ATOM 1483 NE ARG A 195 41.266 -27.919 -0.593 1.00128.91 A N ANISOU 1483 NE ARG A 195 18449 11968 18564 -2389 -2080 338 A N ATOM 1484 CZ ARG A 195 40.772 -28.816 -1.444 1.00128.29 A C ANISOU 1484 CZ ARG A 195 18313 11734 18697 -2439 -2104 90 A C ATOM 1485 NH1 ARG A 195 39.903 -29.725 -1.016 1.00127.15 A N1+ ANISOU 1485 NH1 ARG A 195 18307 11296 18710 -2727 -2014 99 A N1+ ATOM 1486 NH2 ARG A 195 41.145 -28.803 -2.719 1.00123.04 A N ANISOU 1486 NH2 ARG A 195 17453 11208 18089 -2204 -2213 -171 A N ATOM 1487 N PRO A 196 42.967 -25.336 4.174 1.00109.90 A N ANISOU 1487 N PRO A 196 16597 9817 15343 -2445 -1975 1473 A N ATOM 1488 CA PRO A 196 42.640 -25.291 5.605 1.00110.03 A C ANISOU 1488 CA PRO A 196 16833 9748 15225 -2640 -1875 1746 A C ATOM 1489 C PRO A 196 41.499 -26.224 5.982 1.00113.65 A C ANISOU 1489 C PRO A 196 17423 9940 15818 -2932 -1737 1781 A C ATOM 1490 O PRO A 196 40.717 -26.603 5.111 1.00119.15 A O ANISOU 1490 O PRO A 196 17979 10606 16687 -3031 -1684 1557 A O ATOM 1491 CB PRO A 196 42.172 -23.844 5.810 1.00100.51 A C ANISOU 1491 CB PRO A 196 15457 8916 13816 -2709 -1748 1739 A C ATOM 1492 CG PRO A 196 41.966 -23.267 4.439 1.00 98.08 A C ANISOU 1492 CG PRO A 196 14840 8856 13571 -2601 -1745 1453 A C ATOM 1493 CD PRO A 196 42.216 -24.322 3.418 1.00101.50 A C ANISOU 1493 CD PRO A 196 15243 9091 14232 -2487 -1864 1273 A C ATOM 1494 N PRO A 197 41.374 -26.552 7.277 1.00115.05 A N ANISOU 1494 N PRO A 197 17858 9944 15911 -3074 -1671 2057 A N ATOM 1495 CA PRO A 197 40.352 -27.500 7.744 1.00118.75 A C ANISOU 1495 CA PRO A 197 18479 10127 16512 -3359 -1529 2130 A C ATOM 1496 C PRO A 197 38.935 -27.096 7.343 1.00120.98 A C ANISOU 1496 C PRO A 197 18549 10581 16837 -3612 -1340 1957 A C ATOM 1497 O PRO A 197 38.180 -27.968 6.930 1.00131.15 A O ANISOU 1497 O PRO A 197 19829 11662 18339 -3783 -1278 1838 A O ATOM 1498 CB PRO A 197 40.489 -27.452 9.271 1.00115.69 A C ANISOU 1498 CB PRO A 197 18356 9667 15935 -3437 -1470 2473 A C ATOM 1499 CG PRO A 197 41.864 -26.908 9.520 1.00114.32 A C ANISOU 1499 CG PRO A 197 18221 9626 15589 -3145 -1648 2572 A C ATOM 1500 CD PRO A 197 42.136 -25.964 8.391 1.00109.07 A C ANISOU 1500 CD PRO A 197 17248 9281 14913 -2985 -1713 2312 A C ATOM 1501 N GLU A 198 38.584 -25.816 7.455 1.00113.73 A N ANISOU 1501 N GLU A 198 17460 10029 15722 -3633 -1251 1936 A N ATOM 1502 CA GLU A 198 37.211 -25.378 7.211 1.00116.54 A C ANISOU 1502 CA GLU A 198 17623 10572 16087 -3868 -1059 1803 A C ATOM 1503 C GLU A 198 36.678 -25.972 5.932 1.00117.18 A C ANISOU 1503 C GLU A 198 17511 10601 16409 -3902 -1076 1500 A C ATOM 1504 O GLU A 198 35.512 -26.375 5.846 1.00119.23 A O ANISOU 1504 O GLU A 198 17709 10808 16785 -4159 -935 1416 A O ATOM 1505 CB GLU A 198 37.121 -23.860 7.070 1.00122.90 A C ANISOU 1505 CB GLU A 198 18214 11805 16677 -3788 -1004 1743 A C ATOM 1506 CG GLU A 198 37.817 -23.061 8.132 1.00126.09 A C ANISOU 1506 CG GLU A 198 18757 12321 16829 -3702 -1020 1979 A C ATOM 1507 CD GLU A 198 39.136 -22.534 7.655 1.00129.31 A C ANISOU 1507 CD GLU A 198 19105 12850 17178 -3391 -1207 1932 A C ATOM 1508 OE1 GLU A 198 39.865 -23.308 7.008 1.00130.14 A O ANISOU 1508 OE1 GLU A 198 19231 12776 17439 -3233 -1365 1854 A O ATOM 1509 OE2 GLU A 198 39.444 -21.354 7.919 1.00133.28 A O1- ANISOU 1509 OE2 GLU A 198 19536 13620 17482 -3307 -1190 1968 A O1- ATOM 1510 N LEU A 199 37.539 -25.999 4.924 1.00112.98 A N ANISOU 1510 N LEU A 199 16875 10107 15946 -3637 -1250 1328 A N ATOM 1511 CA LEU A 199 37.111 -26.385 3.589 1.00115.21 A C ANISOU 1511 CA LEU A 199 16939 10414 16422 -3619 -1282 1006 A C ATOM 1512 C LEU A 199 36.969 -27.908 3.457 1.00112.88 A C ANISOU 1512 C LEU A 199 16802 9693 16393 -3733 -1322 961 A C ATOM 1513 O LEU A 199 36.048 -28.406 2.806 1.00111.65 A O ANISOU 1513 O LEU A 199 16517 9494 16412 -3901 -1260 742 A O ATOM 1514 CB LEU A 199 38.067 -25.799 2.541 1.00105.73 A C ANISOU 1514 CB LEU A 199 15557 9433 15181 -3283 -1440 839 A C ATOM 1515 CG LEU A 199 38.234 -24.279 2.616 1.00 97.65 A C ANISOU 1515 CG LEU A 199 14376 8810 13915 -3169 -1392 877 A C ATOM 1516 CD1 LEU A 199 39.127 -23.782 1.488 1.00103.05 A C ANISOU 1516 CD1 LEU A 199 14871 9694 14588 -2847 -1533 705 A C ATOM 1517 CD2 LEU A 199 36.888 -23.554 2.599 1.00 84.90 A C ANISOU 1517 CD2 LEU A 199 12575 7456 12227 -3378 -1191 797 A C ATOM 1518 N LEU A 200 37.881 -28.639 4.086 1.00110.28 A N ANISOU 1518 N LEU A 200 16755 9051 16094 -3640 -1424 1166 A N ATOM 1519 CA LEU A 200 37.801 -30.086 4.115 1.00121.20 A C ANISOU 1519 CA LEU A 200 18337 9990 17723 -3744 -1448 1168 A C ATOM 1520 C LEU A 200 36.510 -30.546 4.797 1.00127.24 A C ANISOU 1520 C LEU A 200 19177 10598 18569 -4128 -1239 1249 A C ATOM 1521 O LEU A 200 35.837 -31.459 4.315 1.00126.18 A O ANISOU 1521 O LEU A 200 19025 10239 18678 -4304 -1199 1081 A O ATOM 1522 CB LEU A 200 39.036 -30.654 4.801 1.00122.58 A C ANISOU 1522 CB LEU A 200 18811 9892 17872 -3552 -1581 1419 A C ATOM 1523 CG LEU A 200 40.281 -30.085 4.116 1.00119.24 A C ANISOU 1523 CG LEU A 200 18274 9675 17357 -3181 -1777 1333 A C ATOM 1524 CD1 LEU A 200 41.586 -30.512 4.797 1.00119.60 A C ANISOU 1524 CD1 LEU A 200 18584 9516 17344 -2958 -1922 1581 A C ATOM 1525 CD2 LEU A 200 40.276 -30.463 2.639 1.00117.64 A C ANISOU 1525 CD2 LEU A 200 17869 9482 17345 -3063 -1871 982 A C ATOM 1526 N LEU A 201 36.155 -29.894 5.901 1.00129.75 A N ANISOU 1526 N LEU A 201 19569 11044 18686 -4260 -1102 1495 A N ATOM 1527 CA LEU A 201 34.895 -30.182 6.575 1.00139.34 A C ANISOU 1527 CA LEU A 201 20827 12167 19947 -4621 -884 1583 A C ATOM 1528 C LEU A 201 33.705 -29.652 5.789 1.00144.71 A C ANISOU 1528 C LEU A 201 21175 13142 20665 -4788 -769 1305 A C ATOM 1529 O LEU A 201 32.587 -29.626 6.300 1.00152.84 A O ANISOU 1529 O LEU A 201 22175 14202 21695 -5080 -575 1358 A O ATOM 1530 CB LEU A 201 34.868 -29.578 7.976 1.00140.40 A C ANISOU 1530 CB LEU A 201 21128 12389 19830 -4692 -770 1921 A C ATOM 1531 CG LEU A 201 35.927 -30.066 8.955 1.00144.30 A C ANISOU 1531 CG LEU A 201 21961 12619 20246 -4552 -860 2236 A C ATOM 1532 CD1 LEU A 201 35.405 -29.947 10.385 1.00147.09 A C ANISOU 1532 CD1 LEU A 201 22508 12942 20438 -4756 -680 2557 A C ATOM 1533 CD2 LEU A 201 36.314 -31.494 8.634 1.00145.85 A C ANISOU 1533 CD2 LEU A 201 22340 12362 20713 -4526 -950 2213 A C ATOM 1534 N GLY A 202 33.949 -29.219 4.556 1.00139.65 A N ANISOU 1534 N GLY A 202 20279 12735 20046 -4590 -885 1015 A N ATOM 1535 CA GLY A 202 32.890 -28.725 3.693 1.00134.41 A C ANISOU 1535 CA GLY A 202 19284 12375 19410 -4701 -798 730 A C ATOM 1536 C GLY A 202 32.240 -27.419 4.130 1.00129.61 A C ANISOU 1536 C GLY A 202 18522 12169 18556 -4766 -645 803 A C ATOM 1537 O GLY A 202 31.017 -27.306 4.145 1.00125.82 A O ANISOU 1537 O GLY A 202 17892 11813 18100 -5015 -480 724 A O ATOM 1538 N GLU A 203 33.042 -26.418 4.477 1.00128.99 A N ANISOU 1538 N GLU A 203 18471 12298 18241 -4545 -696 946 A N ATOM 1539 CA GLU A 203 32.472 -25.112 4.792 1.00125.22 A C ANISOU 1539 CA GLU A 203 17840 12207 17531 -4576 -556 988 A C ATOM 1540 C GLU A 203 32.201 -24.317 3.518 1.00121.75 A C ANISOU 1540 C GLU A 203 17057 12136 17068 -4429 -577 691 A C ATOM 1541 O GLU A 203 32.937 -24.423 2.541 1.00117.32 A O ANISOU 1541 O GLU A 203 16409 11589 16578 -4191 -739 520 A O ATOM 1542 CB GLU A 203 33.378 -24.317 5.727 1.00120.42 A C ANISOU 1542 CB GLU A 203 17400 11674 16679 -4421 -588 1254 A C ATOM 1543 CG GLU A 203 32.914 -22.888 5.930 1.00120.68 A C ANISOU 1543 CG GLU A 203 17269 12110 16473 -4410 -459 1267 A C ATOM 1544 CD GLU A 203 31.871 -22.758 7.018 1.00124.83 A C ANISOU 1544 CD GLU A 203 17872 12656 16904 -4693 -245 1442 A C ATOM 1545 OE1 GLU A 203 32.011 -23.429 8.060 1.00122.27 A O ANISOU 1545 OE1 GLU A 203 17819 12058 16582 -4817 -220 1683 A O ATOM 1546 OE2 GLU A 203 30.922 -21.969 6.842 1.00126.99 A O1- ANISOU 1546 OE2 GLU A 203 17935 13227 17087 -4779 -97 1348 A O1- ATOM 1547 N ARG A 204 31.130 -23.535 3.531 1.00126.70 A N ANISOU 1547 N ARG A 204 17486 13064 17589 -4560 -407 634 A N ATOM 1548 CA ARG A 204 30.775 -22.701 2.387 1.00126.60 A C ANISOU 1548 CA ARG A 204 17145 13431 17526 -4415 -402 373 A C ATOM 1549 C ARG A 204 30.569 -21.242 2.799 1.00115.09 A C ANISOU 1549 C ARG A 204 15599 12329 15802 -4349 -278 477 A C ATOM 1550 O ARG A 204 30.298 -20.387 1.957 1.00105.19 A O ANISOU 1550 O ARG A 204 14087 11410 14469 -4208 -252 303 A O ATOM 1551 CB ARG A 204 29.520 -23.238 1.690 1.00131.56 A C ANISOU 1551 CB ARG A 204 17553 14114 18320 -4623 -321 121 A C ATOM 1552 CG ARG A 204 29.733 -24.533 0.946 1.00134.11 A C ANISOU 1552 CG ARG A 204 17897 14144 18912 -4639 -460 -70 A C ATOM 1553 CD ARG A 204 28.429 -25.027 0.359 1.00145.24 A C ANISOU 1553 CD ARG A 204 19085 15621 20480 -4878 -371 -323 A C ATOM 1554 NE ARG A 204 27.962 -24.181 -0.732 1.00146.28 A N ANISOU 1554 NE ARG A 204 18869 16188 20524 -4729 -363 -583 A N ATOM 1555 CZ ARG A 204 28.337 -24.329 -1.998 1.00146.25 A C ANISOU 1555 CZ ARG A 204 18698 16274 20595 -4510 -512 -854 A C ATOM 1556 NH1 ARG A 204 29.200 -25.287 -2.331 1.00144.36 A N1+ ANISOU 1556 NH1 ARG A 204 18610 15714 20527 -4416 -683 -908 A N1+ ATOM 1557 NH2 ARG A 204 27.855 -23.515 -2.929 1.00144.48 A N ANISOU 1557 NH2 ARG A 204 18161 16468 20268 -4370 -487 -1066 A N ATOM 1558 N ASP A 205 30.671 -20.980 4.101 1.00116.68 A N ANISOU 1558 N ASP A 205 16019 12453 15862 -4450 -195 759 A N ATOM 1559 CA ASP A 205 30.663 -19.622 4.627 1.00123.29 A C ANISOU 1559 CA ASP A 205 16827 13577 16441 -4373 -93 880 A C ATOM 1560 C ASP A 205 32.037 -19.350 5.241 1.00121.31 A C ANISOU 1560 C ASP A 205 16800 13213 16079 -4186 -222 1078 A C ATOM 1561 O ASP A 205 32.195 -19.244 6.461 1.00124.15 A O ANISOU 1561 O ASP A 205 17379 13480 16312 -4275 -171 1324 A O ATOM 1562 CB ASP A 205 29.539 -19.420 5.653 1.00126.95 A C ANISOU 1562 CB ASP A 205 17333 14098 16802 -4647 126 1025 A C ATOM 1563 CG ASP A 205 29.419 -17.971 6.118 1.00135.11 A C ANISOU 1563 CG ASP A 205 18317 15448 17571 -4564 245 1115 A C ATOM 1564 OD1 ASP A 205 29.815 -17.050 5.360 1.00134.40 A O ANISOU 1564 OD1 ASP A 205 18064 15600 17402 -4327 201 994 A O ATOM 1565 OD2 ASP A 205 28.922 -17.755 7.246 1.00137.73 A O1- ANISOU 1565 OD2 ASP A 205 18778 15781 17772 -4734 390 1309 A O1- ATOM 1566 N TYR A 206 33.035 -19.264 4.373 1.00108.52 A N ANISOU 1566 N TYR A 206 15115 11612 14507 -3922 -393 963 A N ATOM 1567 CA TYR A 206 34.394 -19.037 4.811 1.00106.51 A C ANISOU 1567 CA TYR A 206 15035 11269 14166 -3729 -533 1118 A C ATOM 1568 C TYR A 206 34.815 -17.640 4.413 1.00 97.67 A C ANISOU 1568 C TYR A 206 13757 10473 12881 -3513 -524 1069 A C ATOM 1569 O TYR A 206 34.106 -16.967 3.672 1.00 90.84 A O ANISOU 1569 O TYR A 206 12652 9877 11988 -3484 -424 905 A O ATOM 1570 CB TYR A 206 35.334 -20.067 4.192 1.00111.34 A C ANISOU 1570 CB TYR A 206 15713 11628 14964 -3585 -740 1048 A C ATOM 1571 CG TYR A 206 35.241 -20.160 2.689 1.00105.36 A C ANISOU 1571 CG TYR A 206 14698 10995 14340 -3441 -805 753 A C ATOM 1572 CD1 TYR A 206 34.459 -21.130 2.080 1.00104.47 A C ANISOU 1572 CD1 TYR A 206 14505 10761 14426 -3580 -794 574 A C ATOM 1573 CD2 TYR A 206 35.941 -19.288 1.880 1.00 96.17 A C ANISOU 1573 CD2 TYR A 206 13368 10069 13102 -3166 -875 652 A C ATOM 1574 CE1 TYR A 206 34.376 -21.223 0.708 1.00 98.93 A C ANISOU 1574 CE1 TYR A 206 13567 10191 13831 -3438 -861 292 A C ATOM 1575 CE2 TYR A 206 35.859 -19.371 0.506 1.00 93.92 A C ANISOU 1575 CE2 TYR A 206 12849 9914 12921 -3016 -931 390 A C ATOM 1576 CZ TYR A 206 35.076 -20.340 -0.073 1.00 95.08 A C ANISOU 1576 CZ TYR A 206 12922 9955 13251 -3148 -930 206 A C ATOM 1577 OH TYR A 206 35.000 -20.421 -1.442 1.00 94.48 A O ANISOU 1577 OH TYR A 206 12609 10026 13261 -2988 -993 -67 A O ATOM 1578 N GLY A 207 35.968 -17.207 4.909 1.00 99.21 A N ANISOU 1578 N GLY A 207 14086 10642 12968 -3360 -625 1212 A N ATOM 1579 CA GLY A 207 36.442 -15.866 4.622 1.00 99.29 A C ANISOU 1579 CA GLY A 207 13967 10928 12829 -3170 -609 1182 A C ATOM 1580 C GLY A 207 37.950 -15.718 4.580 1.00 96.12 A C ANISOU 1580 C GLY A 207 13640 10470 12411 -2940 -792 1241 A C ATOM 1581 O GLY A 207 38.681 -16.694 4.407 1.00 91.75 A O ANISOU 1581 O GLY A 207 13182 9691 11987 -2868 -955 1248 A O ATOM 1582 N PRO A 208 38.426 -14.478 4.743 1.00 98.06 A N ANISOU 1582 N PRO A 208 13839 10921 12500 -2824 -760 1281 A N ATOM 1583 CA PRO A 208 39.858 -14.178 4.777 1.00 91.01 A C ANISOU 1583 CA PRO A 208 12996 10010 11575 -2621 -919 1339 A C ATOM 1584 C PRO A 208 40.698 -15.234 5.481 1.00 89.89 A C ANISOU 1584 C PRO A 208 13091 9581 11482 -2626 -1088 1487 A C ATOM 1585 O PRO A 208 41.815 -15.476 5.033 1.00 95.26 A O ANISOU 1585 O PRO A 208 13761 10206 12229 -2430 -1257 1464 A O ATOM 1586 CB PRO A 208 39.895 -12.856 5.524 1.00 86.00 A C ANISOU 1586 CB PRO A 208 12382 9562 10734 -2640 -810 1434 A C ATOM 1587 CG PRO A 208 38.661 -12.156 4.999 1.00 85.83 A C ANISOU 1587 CG PRO A 208 12170 9764 10678 -2701 -608 1312 A C ATOM 1588 CD PRO A 208 37.617 -13.248 4.828 1.00 95.15 A C ANISOU 1588 CD PRO A 208 13347 10823 11982 -2872 -565 1256 A C ATOM 1589 N PRO A 209 40.176 -15.865 6.546 1.00 83.78 A N ANISOU 1589 N PRO A 209 12526 8633 10675 -2836 -1039 1641 A N ATOM 1590 CA PRO A 209 41.039 -16.829 7.238 1.00 79.62 A C ANISOU 1590 CA PRO A 209 12236 7838 10179 -2812 -1198 1801 A C ATOM 1591 C PRO A 209 41.595 -17.980 6.386 1.00 85.62 A C ANISOU 1591 C PRO A 209 12989 8391 11153 -2682 -1361 1708 A C ATOM 1592 O PRO A 209 42.659 -18.495 6.721 1.00 93.73 A O ANISOU 1592 O PRO A 209 14159 9263 12191 -2560 -1525 1815 A O ATOM 1593 CB PRO A 209 40.141 -17.342 8.363 1.00 73.67 A C ANISOU 1593 CB PRO A 209 11681 6941 9371 -3070 -1077 1966 A C ATOM 1594 CG PRO A 209 39.274 -16.161 8.698 1.00 68.17 A C ANISOU 1594 CG PRO A 209 10890 6502 8507 -3184 -881 1957 A C ATOM 1595 CD PRO A 209 38.984 -15.524 7.350 1.00 79.17 A C ANISOU 1595 CD PRO A 209 11991 8114 9975 -3072 -838 1718 A C ATOM 1596 N ILE A 210 40.930 -18.367 5.305 1.00 79.40 A N ANISOU 1596 N ILE A 210 12034 7610 10524 -2693 -1324 1508 A N ATOM 1597 CA ILE A 210 41.436 -19.494 4.528 1.00 84.25 A C ANISOU 1597 CA ILE A 210 12656 8015 11340 -2573 -1478 1409 A C ATOM 1598 C ILE A 210 42.784 -19.194 3.861 1.00 92.96 A C ANISOU 1598 C ILE A 210 13671 9200 12450 -2272 -1649 1354 A C ATOM 1599 O ILE A 210 43.541 -20.125 3.512 1.00 88.69 A O ANISOU 1599 O ILE A 210 13199 8462 12039 -2135 -1809 1336 A O ATOM 1600 CB ILE A 210 40.457 -19.960 3.432 1.00 83.98 A C ANISOU 1600 CB ILE A 210 12442 7992 11473 -2638 -1414 1172 A C ATOM 1601 CG1 ILE A 210 40.520 -19.026 2.229 1.00 78.11 A C ANISOU 1601 CG1 ILE A 210 11407 7561 10710 -2451 -1401 966 A C ATOM 1602 CG2 ILE A 210 39.029 -20.106 3.969 1.00 90.80 A C ANISOU 1602 CG2 ILE A 210 13334 8836 12332 -2942 -1223 1198 A C ATOM 1603 CD1 ILE A 210 39.912 -19.634 0.988 1.00 78.08 A C ANISOU 1603 CD1 ILE A 210 11225 7561 10880 -2432 -1407 709 A C ATOM 1604 N ASP A 211 43.072 -17.905 3.662 1.00 90.15 A N ANISOU 1604 N ASP A 211 13160 9130 11962 -2168 -1607 1325 A N ATOM 1605 CA ASP A 211 44.341 -17.494 3.056 1.00 85.58 A C ANISOU 1605 CA ASP A 211 12478 8655 11383 -1896 -1748 1282 A C ATOM 1606 C ASP A 211 45.412 -17.427 4.128 1.00 88.82 A C ANISOU 1606 C ASP A 211 13075 8988 11683 -1849 -1862 1490 A C ATOM 1607 O ASP A 211 46.569 -17.748 3.885 1.00 89.82 A O ANISOU 1607 O ASP A 211 13213 9059 11857 -1649 -2033 1502 A O ATOM 1608 CB ASP A 211 44.226 -16.148 2.334 1.00 82.14 A C ANISOU 1608 CB ASP A 211 11794 8546 10869 -1800 -1646 1163 A C ATOM 1609 CG ASP A 211 43.351 -16.218 1.095 1.00 86.81 A C ANISOU 1609 CG ASP A 211 12169 9251 11564 -1777 -1564 939 A C ATOM 1610 OD1 ASP A 211 43.224 -17.339 0.545 1.00 89.44 A O ANISOU 1610 OD1 ASP A 211 12515 9413 12056 -1762 -1645 839 A O ATOM 1611 OD2 ASP A 211 42.798 -15.157 0.673 1.00 77.85 A O1- ANISOU 1611 OD2 ASP A 211 10855 8377 10349 -1767 -1421 861 A O1- ATOM 1612 N LEU A 212 45.017 -17.018 5.324 1.00 97.36 A N ANISOU 1612 N LEU A 212 14301 10081 12612 -2029 -1770 1649 A N ATOM 1613 CA LEU A 212 45.958 -16.908 6.425 1.00103.14 A C ANISOU 1613 CA LEU A 212 15210 10767 13213 -1995 -1875 1843 A C ATOM 1614 C LEU A 212 46.580 -18.250 6.727 1.00 99.61 A C ANISOU 1614 C LEU A 212 14958 10031 12858 -1933 -2037 1947 A C ATOM 1615 O LEU A 212 47.768 -18.333 7.022 1.00 98.65 A O ANISOU 1615 O LEU A 212 14898 9888 12696 -1771 -2200 2033 A O ATOM 1616 CB LEU A 212 45.255 -16.378 7.659 1.00108.21 A C ANISOU 1616 CB LEU A 212 15986 11454 13673 -2212 -1735 1987 A C ATOM 1617 CG LEU A 212 44.966 -14.898 7.509 1.00107.02 A C ANISOU 1617 CG LEU A 212 15666 11595 13401 -2226 -1601 1910 A C ATOM 1618 CD1 LEU A 212 43.947 -14.495 8.558 1.00120.46 A C ANISOU 1618 CD1 LEU A 212 17483 13335 14949 -2459 -1426 2015 A C ATOM 1619 CD2 LEU A 212 46.267 -14.140 7.644 1.00 94.20 A C ANISOU 1619 CD2 LEU A 212 14002 10096 11693 -2055 -1723 1937 A C ATOM 1620 N TRP A 213 45.763 -19.297 6.653 1.00 99.75 A N ANISOU 1620 N TRP A 213 15069 9827 13003 -2063 -1989 1938 A N ATOM 1621 CA TRP A 213 46.237 -20.664 6.825 1.00100.22 A C ANISOU 1621 CA TRP A 213 15321 9576 13182 -2006 -2123 2023 A C ATOM 1622 C TRP A 213 47.295 -20.978 5.777 1.00 93.22 A C ANISOU 1622 C TRP A 213 14316 8682 12421 -1728 -2299 1896 A C ATOM 1623 O TRP A 213 48.375 -21.459 6.106 1.00 91.82 A O ANISOU 1623 O TRP A 213 14258 8393 12236 -1566 -2463 2006 A O ATOM 1624 CB TRP A 213 45.076 -21.645 6.708 1.00108.14 A C ANISOU 1624 CB TRP A 213 16400 10352 14334 -2207 -2016 1986 A C ATOM 1625 CG TRP A 213 45.448 -23.084 6.874 1.00115.05 A C ANISOU 1625 CG TRP A 213 17489 10871 15352 -2167 -2127 2072 A C ATOM 1626 CD1 TRP A 213 45.897 -23.937 5.904 1.00118.27 A C ANISOU 1626 CD1 TRP A 213 17858 11122 15956 -2005 -2250 1934 A C ATOM 1627 CD2 TRP A 213 45.384 -23.848 8.084 1.00123.89 A C ANISOU 1627 CD2 TRP A 213 18904 11738 16429 -2282 -2117 2320 A C ATOM 1628 CE2 TRP A 213 45.815 -25.159 7.776 1.00126.24 A C ANISOU 1628 CE2 TRP A 213 19336 11716 16912 -2182 -2232 2324 A C ATOM 1629 CE3 TRP A 213 45.008 -23.553 9.401 1.00125.70 A C ANISOU 1629 CE3 TRP A 213 19302 11982 16475 -2450 -2016 2542 A C ATOM 1630 NE1 TRP A 213 46.121 -25.188 6.439 1.00125.67 A N ANISOU 1630 NE1 TRP A 213 19055 11710 16985 -2015 -2315 2078 A N ATOM 1631 CZ2 TRP A 213 45.879 -26.170 8.736 1.00126.43 A C ANISOU 1631 CZ2 TRP A 213 19660 11428 16949 -2243 -2243 2555 A C ATOM 1632 CZ3 TRP A 213 45.074 -24.559 10.354 1.00128.44 A C ANISOU 1632 CZ3 TRP A 213 19941 12036 16823 -2509 -2029 2771 A C ATOM 1633 CH2 TRP A 213 45.505 -25.851 10.015 1.00128.51 A C ANISOU 1633 CH2 TRP A 213 20082 11721 17025 -2405 -2139 2782 A C ATOM 1634 N GLY A 214 46.990 -20.698 4.514 1.00 86.77 A N ANISOU 1634 N GLY A 214 13260 7999 11709 -1660 -2263 1666 A N ATOM 1635 CA GLY A 214 48.000 -20.815 3.481 1.00 92.74 A C ANISOU 1635 CA GLY A 214 13875 8803 12557 -1382 -2413 1540 A C ATOM 1636 C GLY A 214 49.297 -20.148 3.925 1.00 99.81 A C ANISOU 1636 C GLY A 214 14766 9836 13321 -1210 -2532 1655 A C ATOM 1637 O GLY A 214 50.380 -20.736 3.854 1.00105.10 A O ANISOU 1637 O GLY A 214 15492 10404 14037 -1011 -2706 1699 A O ATOM 1638 N ALA A 215 49.179 -18.913 4.408 1.00 91.88 A N ANISOU 1638 N ALA A 215 13694 9065 12152 -1290 -2437 1701 A N ATOM 1639 CA ALA A 215 50.339 -18.131 4.804 1.00 87.78 A C ANISOU 1639 CA ALA A 215 13138 8705 11508 -1155 -2534 1783 A C ATOM 1640 C ALA A 215 51.130 -18.819 5.906 1.00 93.25 A C ANISOU 1640 C ALA A 215 14070 9227 12134 -1122 -2682 1988 A C ATOM 1641 O ALA A 215 52.344 -18.617 6.032 1.00 91.63 A O ANISOU 1641 O ALA A 215 13836 9098 11881 -944 -2830 2037 A O ATOM 1642 CB ALA A 215 49.913 -16.742 5.243 1.00 85.70 A C ANISOU 1642 CB ALA A 215 12795 8683 11084 -1287 -2385 1795 A C ATOM 1643 N GLY A 216 50.439 -19.614 6.717 1.00 96.49 A N ANISOU 1643 N GLY A 216 14711 9415 12536 -1291 -2636 2115 A N ATOM 1644 CA GLY A 216 51.108 -20.403 7.731 1.00100.25 A C ANISOU 1644 CA GLY A 216 15433 9704 12952 -1246 -2768 2323 A C ATOM 1645 C GLY A 216 51.964 -21.460 7.061 1.00100.64 A C ANISOU 1645 C GLY A 216 15499 9578 13160 -1011 -2942 2288 A C ATOM 1646 O GLY A 216 53.193 -21.457 7.156 1.00106.95 A O ANISOU 1646 O GLY A 216 16286 10432 13919 -800 -3110 2341 A O ATOM 1647 N CYS A 217 51.306 -22.361 6.354 1.00 93.82 A N ANISOU 1647 N CYS A 217 14654 8510 12482 -1045 -2901 2185 A N ATOM 1648 CA CYS A 217 52.005 -23.405 5.639 1.00100.01 A C ANISOU 1648 CA CYS A 217 15459 9108 13432 -826 -3050 2127 A C ATOM 1649 C CYS A 217 53.223 -22.847 4.915 1.00106.01 A C ANISOU 1649 C CYS A 217 16008 10088 14183 -553 -3188 2035 A C ATOM 1650 O CYS A 217 54.234 -23.525 4.779 1.00120.21 A O ANISOU 1650 O CYS A 217 17857 11785 16033 -326 -3356 2073 A O ATOM 1651 CB CYS A 217 51.050 -24.083 4.665 1.00101.18 A C ANISOU 1651 CB CYS A 217 15558 9103 13784 -905 -2966 1939 A C ATOM 1652 SG CYS A 217 49.552 -24.684 5.486 1.00116.90 A S ANISOU 1652 SG CYS A 217 17764 10851 15801 -1258 -2782 2037 A S ATOM 1653 N ILE A 218 53.135 -21.604 4.463 1.00102.80 A N ANISOU 1653 N ILE A 218 15367 9983 13711 -568 -3109 1923 A N ATOM 1654 CA ILE A 218 54.270 -20.985 3.788 1.00103.17 A C ANISOU 1654 CA ILE A 218 15200 10250 13749 -326 -3216 1845 A C ATOM 1655 C ILE A 218 55.337 -20.491 4.767 1.00106.25 A C ANISOU 1655 C ILE A 218 15639 10756 13975 -258 -3330 2012 A C ATOM 1656 O ILE A 218 56.522 -20.561 4.465 1.00109.62 A O ANISOU 1656 O ILE A 218 15982 11251 14418 -23 -3484 2009 A O ATOM 1657 CB ILE A 218 53.843 -19.829 2.855 1.00 93.77 A C ANISOU 1657 CB ILE A 218 13733 9336 12561 -346 -3083 1664 A C ATOM 1658 CG1 ILE A 218 52.636 -20.239 2.015 1.00 92.04 A C ANISOU 1658 CG1 ILE A 218 13463 9035 12472 -446 -2959 1499 A C ATOM 1659 CG2 ILE A 218 55.002 -19.406 1.951 1.00 84.58 A C ANISOU 1659 CG2 ILE A 218 12344 8361 11432 -74 -3188 1571 A C ATOM 1660 CD1 ILE A 218 52.399 -19.351 0.810 1.00 90.51 A C ANISOU 1660 CD1 ILE A 218 12981 9100 12307 -370 -2865 1302 A C ATOM 1661 N MET A 219 54.931 -19.983 5.927 1.00106.98 A N ANISOU 1661 N MET A 219 15855 10886 13905 -456 -3257 2149 A N ATOM 1662 CA MET A 219 55.915 -19.549 6.912 1.00108.21 A C ANISOU 1662 CA MET A 219 16063 11157 13894 -399 -3374 2296 A C ATOM 1663 C MET A 219 56.867 -20.696 7.180 1.00115.04 A C ANISOU 1663 C MET A 219 17077 11841 14792 -194 -3572 2413 A C ATOM 1664 O MET A 219 58.090 -20.529 7.116 1.00118.04 A O ANISOU 1664 O MET A 219 17360 12348 15140 12 -3729 2426 A O ATOM 1665 CB MET A 219 55.265 -19.107 8.227 1.00107.61 A C ANISOU 1665 CB MET A 219 16155 11097 13633 -637 -3275 2440 A C ATOM 1666 CG MET A 219 55.297 -17.608 8.457 1.00110.49 A C ANISOU 1666 CG MET A 219 16367 11753 13861 -728 -3194 2392 A C ATOM 1667 SD MET A 219 55.424 -17.078 10.178 1.00105.79 A S ANISOU 1667 SD MET A 219 15958 11239 13000 -869 -3209 2582 A S ATOM 1668 CE MET A 219 57.193 -16.871 10.321 1.00127.06 A C ANISOU 1668 CE MET A 219 18551 14089 15636 -622 -3454 2608 A C ATOM 1669 N ALA A 220 56.300 -21.866 7.471 1.00109.48 A N ANISOU 1669 N ALA A 220 16603 10837 14156 -250 -3560 2499 A N ATOM 1670 CA ALA A 220 57.106 -23.029 7.827 1.00107.31 A C ANISOU 1670 CA ALA A 220 16513 10353 13909 -60 -3731 2636 A C ATOM 1671 C ALA A 220 57.936 -23.518 6.637 1.00111.89 A C ANISOU 1671 C ALA A 220 16945 10914 14653 218 -3858 2499 A C ATOM 1672 O ALA A 220 59.091 -23.914 6.788 1.00111.00 A O ANISOU 1672 O ALA A 220 16855 10803 14517 454 -4037 2577 A O ATOM 1673 CB ALA A 220 56.227 -24.132 8.369 1.00 99.06 A C ANISOU 1673 CB ALA A 220 15751 8971 12916 -201 -3658 2757 A C ATOM 1674 N GLU A 221 57.346 -23.468 5.450 1.00114.95 A N ANISOU 1674 N GLU A 221 17175 11305 15196 200 -3766 2292 A N ATOM 1675 CA GLU A 221 58.040 -23.862 4.230 1.00120.87 A C ANISOU 1675 CA GLU A 221 17768 12062 16096 462 -3868 2139 A C ATOM 1676 C GLU A 221 59.282 -22.991 4.005 1.00121.61 A C ANISOU 1676 C GLU A 221 17635 12460 16110 659 -3978 2118 A C ATOM 1677 O GLU A 221 60.090 -23.257 3.117 1.00123.46 A O ANISOU 1677 O GLU A 221 17732 12739 16438 910 -4083 2023 A O ATOM 1678 CB GLU A 221 57.075 -23.765 3.041 1.00122.83 A C ANISOU 1678 CB GLU A 221 17865 12317 16490 383 -3730 1910 A C ATOM 1679 CG GLU A 221 57.511 -24.474 1.769 1.00126.98 A C ANISOU 1679 CG GLU A 221 18285 12772 17190 630 -3817 1739 A C ATOM 1680 CD GLU A 221 56.323 -24.873 0.910 1.00128.58 A C ANISOU 1680 CD GLU A 221 18459 12854 17543 508 -3691 1549 A C ATOM 1681 OE1 GLU A 221 55.289 -25.268 1.496 1.00125.54 A O ANISOU 1681 OE1 GLU A 221 18252 12275 17173 262 -3587 1604 A O ATOM 1682 OE2 GLU A 221 56.423 -24.797 -0.338 1.00127.90 A O1- ANISOU 1682 OE2 GLU A 221 18168 12875 17553 659 -3697 1344 A O1- ATOM 1683 N MET A 222 59.430 -21.946 4.812 1.00118.50 A N ANISOU 1683 N MET A 222 17201 12279 15545 540 -3950 2202 A N ATOM 1684 CA MET A 222 60.560 -21.038 4.679 1.00115.02 A C ANISOU 1684 CA MET A 222 16541 12131 15032 685 -4040 2180 A C ATOM 1685 C MET A 222 61.765 -21.599 5.414 1.00126.13 A C ANISOU 1685 C MET A 222 18050 13511 16362 878 -4249 2338 A C ATOM 1686 O MET A 222 62.908 -21.242 5.130 1.00130.03 A O ANISOU 1686 O MET A 222 18363 14200 16841 1073 -4371 2313 A O ATOM 1687 CB MET A 222 60.204 -19.661 5.229 1.00102.60 A C ANISOU 1687 CB MET A 222 14880 10788 13315 469 -3919 2185 A C ATOM 1688 CG MET A 222 59.180 -18.907 4.401 1.00 91.78 A C ANISOU 1688 CG MET A 222 13356 9510 12009 325 -3716 2021 A C ATOM 1689 SD MET A 222 59.858 -18.285 2.851 1.00107.72 A S ANISOU 1689 SD MET A 222 15026 11757 14147 545 -3716 1827 A S ATOM 1690 CE MET A 222 61.352 -17.499 3.444 1.00118.75 A C ANISOU 1690 CE MET A 222 16302 13391 15425 656 -3859 1911 A C ATOM 1691 N TRP A 223 61.498 -22.485 6.364 1.00129.88 A N ANISOU 1691 N TRP A 223 18814 13750 16784 827 -4286 2507 A N ATOM 1692 CA TRP A 223 62.561 -23.157 7.097 1.00131.10 A C ANISOU 1692 CA TRP A 223 19098 13855 16858 1027 -4483 2675 A C ATOM 1693 C TRP A 223 62.694 -24.620 6.662 1.00128.06 A C ANISOU 1693 C TRP A 223 18872 13161 16626 1221 -4562 2698 A C ATOM 1694 O TRP A 223 63.798 -25.108 6.438 1.00126.00 A O ANISOU 1694 O TRP A 223 18571 12916 16388 1503 -4732 2722 A O ATOM 1695 CB TRP A 223 62.328 -23.044 8.607 1.00133.96 A C ANISOU 1695 CB TRP A 223 19680 14201 17017 866 -4480 2879 A C ATOM 1696 CG TRP A 223 62.697 -21.700 9.166 1.00139.46 A C ANISOU 1696 CG TRP A 223 20223 15226 17541 768 -4481 2871 A C ATOM 1697 CD1 TRP A 223 63.945 -21.278 9.513 1.00141.93 A C ANISOU 1697 CD1 TRP A 223 20412 15770 17745 926 -4649 2905 A C ATOM 1698 CD2 TRP A 223 61.813 -20.601 9.441 1.00140.46 A C ANISOU 1698 CD2 TRP A 223 20298 15484 17588 489 -4306 2816 A C ATOM 1699 CE2 TRP A 223 62.600 -19.551 9.954 1.00136.64 A C ANISOU 1699 CE2 TRP A 223 19671 15292 16954 489 -4377 2815 A C ATOM 1700 CE3 TRP A 223 60.436 -20.405 9.301 1.00137.20 A C ANISOU 1700 CE3 TRP A 223 19940 14972 17216 243 -4095 2763 A C ATOM 1701 NE1 TRP A 223 63.896 -19.989 9.987 1.00140.82 A N ANISOU 1701 NE1 TRP A 223 20152 15883 17471 751 -4590 2867 A N ATOM 1702 CZ2 TRP A 223 62.057 -18.325 10.330 1.00129.46 A C ANISOU 1702 CZ2 TRP A 223 18691 14558 15939 257 -4242 2763 A C ATOM 1703 CZ3 TRP A 223 59.900 -19.187 9.678 1.00131.03 A C ANISOU 1703 CZ3 TRP A 223 19083 14381 16320 25 -3961 2721 A C ATOM 1704 CH2 TRP A 223 60.709 -18.163 10.186 1.00127.65 A C ANISOU 1704 CH2 TRP A 223 18529 14223 15747 36 -4033 2721 A C ATOM 1705 N THR A 224 61.567 -25.309 6.519 1.00124.04 A N ANISOU 1705 N THR A 224 18533 12371 16226 1070 -4436 2682 A N ATOM 1706 CA THR A 224 61.584 -26.716 6.142 1.00119.67 A C ANISOU 1706 CA THR A 224 18154 11484 15830 1222 -4493 2695 A C ATOM 1707 C THR A 224 61.835 -26.912 4.649 1.00119.53 A C ANISOU 1707 C THR A 224 17932 11484 16000 1406 -4517 2465 A C ATOM 1708 O THR A 224 61.948 -28.041 4.171 1.00125.18 A O ANISOU 1708 O THR A 224 18761 11941 16862 1564 -4575 2436 A O ATOM 1709 CB THR A 224 60.276 -27.428 6.541 1.00112.42 A C ANISOU 1709 CB THR A 224 17494 10241 14978 976 -4344 2754 A C ATOM 1710 CG2 THR A 224 59.901 -27.080 7.973 1.00102.19 A C ANISOU 1710 CG2 THR A 224 16376 8969 13481 772 -4288 2969 A C ATOM 1711 OG1 THR A 224 59.218 -27.043 5.652 1.00111.39 A O ANISOU 1711 OG1 THR A 224 17223 10133 14968 790 -4180 2544 A O ATOM 1712 N ARG A 225 61.918 -25.809 3.918 1.00114.30 A N ANISOU 1712 N ARG A 225 16974 11125 15329 1391 -4467 2304 A N ATOM 1713 CA ARG A 225 62.170 -25.861 2.482 1.00116.45 A C ANISOU 1713 CA ARG A 225 17027 11466 15754 1575 -4480 2087 A C ATOM 1714 C ARG A 225 61.217 -26.811 1.746 1.00120.11 A C ANISOU 1714 C ARG A 225 17595 11637 16403 1525 -4400 1953 A C ATOM 1715 O ARG A 225 61.403 -27.089 0.558 1.00117.01 A O ANISOU 1715 O ARG A 225 17062 11254 16143 1701 -4425 1769 A O ATOM 1716 CB ARG A 225 63.618 -26.266 2.221 1.00116.08 A C ANISOU 1716 CB ARG A 225 16907 11483 15714 1928 -4679 2116 A C ATOM 1717 CG ARG A 225 64.623 -25.475 3.029 1.00113.40 A C ANISOU 1717 CG ARG A 225 16477 11414 15196 1982 -4781 2251 A C ATOM 1718 CD ARG A 225 64.577 -24.016 2.656 1.00108.73 A C ANISOU 1718 CD ARG A 225 15599 11163 14551 1864 -4683 2140 A C ATOM 1719 NE ARG A 225 65.145 -23.771 1.334 1.00114.16 A N ANISOU 1719 NE ARG A 225 16012 12019 15345 2076 -4701 1965 A N ATOM 1720 CZ ARG A 225 66.182 -22.963 1.100 1.00120.39 A C ANISOU 1720 CZ ARG A 225 16548 13109 16084 2210 -4766 1946 A C ATOM 1721 NH1 ARG A 225 66.777 -22.316 2.104 1.00116.75 A N1+ ANISOU 1721 NH1 ARG A 225 16071 12817 15472 2149 -4831 2075 A N1+ ATOM 1722 NH2 ARG A 225 66.624 -22.798 -0.144 1.00120.79 A N ANISOU 1722 NH2 ARG A 225 16357 13299 16237 2405 -4763 1793 A N ATOM 1723 N SER A 226 60.186 -27.282 2.445 1.00123.99 A N ANISOU 1723 N SER A 226 18326 11881 16904 1280 -4300 2038 A N ATOM 1724 CA SER A 226 59.289 -28.304 1.908 1.00126.65 A C ANISOU 1724 CA SER A 226 18794 11900 17426 1208 -4231 1928 A C ATOM 1725 C SER A 226 57.876 -28.205 2.489 1.00121.84 A C ANISOU 1725 C SER A 226 18315 11172 16808 844 -4048 1963 A C ATOM 1726 O SER A 226 57.703 -28.163 3.712 1.00117.32 A O ANISOU 1726 O SER A 226 17929 10536 16111 697 -4021 2178 A O ATOM 1727 CB SER A 226 59.867 -29.702 2.183 1.00129.20 A C ANISOU 1727 CB SER A 226 19372 11885 17834 1404 -4363 2041 A C ATOM 1728 OG SER A 226 58.998 -30.724 1.727 1.00129.42 A O ANISOU 1728 OG SER A 226 19546 11574 18054 1315 -4293 1934 A O ATOM 1729 N PRO A 227 56.860 -28.180 1.611 1.00120.49 A N ANISOU 1729 N PRO A 227 18038 10980 16762 706 -3923 1750 A N ATOM 1730 CA PRO A 227 55.458 -28.171 2.038 1.00120.54 A C ANISOU 1730 CA PRO A 227 18146 10870 16784 364 -3744 1757 A C ATOM 1731 C PRO A 227 55.248 -29.135 3.197 1.00124.52 A C ANISOU 1731 C PRO A 227 18993 11031 17289 255 -3743 1989 A C ATOM 1732 O PRO A 227 55.440 -30.342 3.061 1.00132.16 A O ANISOU 1732 O PRO A 227 20137 11679 18399 362 -3811 2001 A O ATOM 1733 CB PRO A 227 54.718 -28.642 0.790 1.00118.11 A C ANISOU 1733 CB PRO A 227 17734 10471 16673 344 -3686 1485 A C ATOM 1734 CG PRO A 227 55.558 -28.127 -0.333 1.00116.34 A C ANISOU 1734 CG PRO A 227 17236 10513 16453 621 -3775 1315 A C ATOM 1735 CD PRO A 227 56.987 -28.203 0.143 1.00119.18 A C ANISOU 1735 CD PRO A 227 17646 10910 16727 881 -3947 1485 A C ATOM 1736 N ILE A 228 54.849 -28.588 4.335 1.00121.14 A N ANISOU 1736 N ILE A 228 18661 10669 16696 47 -3657 2175 A N ATOM 1737 CA ILE A 228 54.918 -29.305 5.600 1.00120.65 A C ANISOU 1737 CA ILE A 228 18915 10356 16570 -7 -3673 2448 A C ATOM 1738 C ILE A 228 53.867 -30.387 5.807 1.00123.50 A C ANISOU 1738 C ILE A 228 19508 10329 17086 -214 -3556 2481 A C ATOM 1739 O ILE A 228 54.012 -31.225 6.688 1.00134.46 A O ANISOU 1739 O ILE A 228 21180 11446 18464 -209 -3578 2703 A O ATOM 1740 CB ILE A 228 54.850 -28.322 6.773 1.00121.03 A C ANISOU 1740 CB ILE A 228 18986 10627 16373 -153 -3620 2633 A C ATOM 1741 CG1 ILE A 228 53.594 -27.452 6.651 1.00125.86 A C ANISOU 1741 CG1 ILE A 228 19465 11395 16959 -452 -3419 2521 A C ATOM 1742 CG2 ILE A 228 56.115 -27.465 6.808 1.00111.70 A C ANISOU 1742 CG2 ILE A 228 17635 9766 15039 74 -3768 2651 A C ATOM 1743 CD1 ILE A 228 52.858 -27.245 7.969 1.00127.25 A C ANISOU 1743 CD1 ILE A 228 19828 11537 16982 -711 -3291 2732 A C ATOM 1744 N MET A 229 52.809 -30.371 5.009 1.00124.97 A N ANISOU 1744 N MET A 229 19575 10492 17415 -398 -3427 2263 A N ATOM 1745 CA MET A 229 51.744 -31.359 5.149 1.00132.38 A C ANISOU 1745 CA MET A 229 20706 11073 18521 -627 -3304 2267 A C ATOM 1746 C MET A 229 51.282 -31.875 3.789 1.00141.10 A C ANISOU 1746 C MET A 229 21674 12073 19863 -617 -3293 1958 A C ATOM 1747 O MET A 229 50.321 -31.354 3.203 1.00138.85 A O ANISOU 1747 O MET A 229 21199 11942 19618 -804 -3171 1763 A O ATOM 1748 CB MET A 229 50.553 -30.770 5.910 1.00126.91 A C ANISOU 1748 CB MET A 229 20033 10458 17728 -976 -3105 2351 A C ATOM 1749 CG MET A 229 50.848 -30.369 7.341 1.00122.74 A C ANISOU 1749 CG MET A 229 19673 9998 16964 -1017 -3097 2657 A C ATOM 1750 SD MET A 229 49.347 -29.856 8.201 1.00137.04 A S ANISOU 1750 SD MET A 229 21531 11856 18681 -1429 -2847 2749 A S ATOM 1751 CE MET A 229 48.817 -28.489 7.173 1.00176.39 A C ANISOU 1751 CE MET A 229 26126 17259 23637 -1496 -2771 2455 A C ATOM 1752 N GLN A 230 51.968 -32.899 3.290 1.00144.52 A N ANISOU 1752 N GLN A 230 22207 12256 20448 -388 -3423 1908 A N ATOM 1753 CA GLN A 230 51.627 -33.482 1.997 1.00143.67 A C ANISOU 1753 CA GLN A 230 21989 12034 20566 -349 -3433 1603 A C ATOM 1754 C GLN A 230 50.651 -34.646 2.164 1.00145.11 A C ANISOU 1754 C GLN A 230 22394 11785 20959 -587 -3326 1591 A C ATOM 1755 O GLN A 230 50.927 -35.606 2.882 1.00150.09 A O ANISOU 1755 O GLN A 230 23321 12060 21645 -560 -3349 1794 A O ATOM 1756 CB GLN A 230 52.891 -33.919 1.254 1.00143.93 A C ANISOU 1756 CB GLN A 230 21986 12047 20654 40 -3628 1521 A C ATOM 1757 CG GLN A 230 53.975 -32.845 1.209 1.00143.59 A C ANISOU 1757 CG GLN A 230 21742 12405 20409 278 -3737 1570 A C ATOM 1758 CD GLN A 230 55.194 -33.269 0.410 1.00147.66 A C ANISOU 1758 CD GLN A 230 22196 12923 20984 664 -3921 1477 A C ATOM 1759 NE2 GLN A 230 56.268 -32.490 0.506 1.00144.94 A N ANISOU 1759 NE2 GLN A 230 21712 12882 20475 882 -4027 1558 A N ATOM 1760 OE1 GLN A 230 55.171 -34.285 -0.288 1.00151.45 A O ANISOU 1760 OE1 GLN A 230 22750 13136 21658 763 -3964 1327 A O ATOM 1761 N GLY A 231 49.501 -34.544 1.510 1.00142.72 A N ANISOU 1761 N GLY A 231 21941 11517 20770 -821 -3202 1355 A N ATOM 1762 CA GLY A 231 48.468 -35.553 1.625 1.00145.74 A C ANISOU 1762 CA GLY A 231 22494 11519 21362 -1091 -3083 1315 A C ATOM 1763 C GLY A 231 48.036 -36.084 0.274 1.00152.92 A C ANISOU 1763 C GLY A 231 23255 12349 22497 -1082 -3103 945 A C ATOM 1764 O GLY A 231 48.057 -35.355 -0.717 1.00150.91 A O ANISOU 1764 O GLY A 231 22705 12433 22201 -977 -3140 705 A O ATOM 1765 N ASN A 232 47.650 -37.359 0.238 1.00162.87 A N ANISOU 1765 N ASN A 232 24728 13160 23997 -1187 -3076 900 A N ATOM 1766 CA ASN A 232 47.150 -37.994 -0.980 1.00163.10 A C ANISOU 1766 CA ASN A 232 24645 13067 24261 -1212 -3090 534 A C ATOM 1767 C ASN A 232 45.754 -37.486 -1.341 1.00160.73 A C ANISOU 1767 C ASN A 232 24119 12958 23991 -1545 -2934 328 A C ATOM 1768 O ASN A 232 45.503 -37.091 -2.484 1.00155.24 A O ANISOU 1768 O ASN A 232 23143 12522 23318 -1485 -2966 12 A O ATOM 1769 CB ASN A 232 47.143 -39.523 -0.838 1.00166.79 A C ANISOU 1769 CB ASN A 232 25423 12963 24985 -1245 -3097 552 A C ATOM 1770 CG ASN A 232 48.548 -40.117 -0.707 1.00168.32 A C ANISOU 1770 CG ASN A 232 25818 12968 25170 -865 -3267 702 A C ATOM 1771 ND2 ASN A 232 48.621 -41.443 -0.585 1.00170.57 A N ANISOU 1771 ND2 ASN A 232 26390 12744 25675 -858 -3274 730 A N ATOM 1772 OD1 ASN A 232 49.550 -39.396 -0.713 1.00163.41 A O ANISOU 1772 OD1 ASN A 232 25090 12650 24349 -582 -3386 791 A O ATOM 1773 N THR A 233 44.852 -37.488 -0.360 1.00162.47 A N ANISOU 1773 N THR A 233 24460 13068 24202 -1884 -2764 513 A N ATOM 1774 CA THR A 233 43.486 -37.006 -0.569 1.00160.23 A C ANISOU 1774 CA THR A 233 23971 12970 23938 -2215 -2603 350 A C ATOM 1775 C THR A 233 42.980 -36.156 0.600 1.00158.89 A C ANISOU 1775 C THR A 233 23825 12983 23562 -2433 -2453 631 A C ATOM 1776 O THR A 233 43.684 -35.969 1.594 1.00161.11 A O ANISOU 1776 O THR A 233 24291 13237 23687 -2335 -2477 950 A O ATOM 1777 CB THR A 233 42.519 -38.173 -0.754 1.00157.03 A C ANISOU 1777 CB THR A 233 23673 12165 23826 -2498 -2511 195 A C ATOM 1778 CG2 THR A 233 42.913 -39.002 -1.972 1.00155.94 A C ANISOU 1778 CG2 THR A 233 23498 11855 23897 -2299 -2654 -128 A C ATOM 1779 OG1 THR A 233 42.553 -38.992 0.421 1.00156.14 A O ANISOU 1779 OG1 THR A 233 23919 11627 23780 -2630 -2437 513 A O ATOM 1780 N GLU A 234 41.752 -35.656 0.477 1.00150.89 A N ANISOU 1780 N GLU A 234 22621 12163 22546 -2722 -2300 505 A N ATOM 1781 CA GLU A 234 41.140 -34.823 1.512 1.00142.04 A C ANISOU 1781 CA GLU A 234 21500 11236 21234 -2942 -2141 737 A C ATOM 1782 C GLU A 234 41.082 -35.510 2.879 1.00147.93 A C ANISOU 1782 C GLU A 234 22596 11617 21993 -3107 -2050 1089 A C ATOM 1783 O GLU A 234 41.084 -34.843 3.912 1.00145.58 A O ANISOU 1783 O GLU A 234 22370 11462 21483 -3166 -1974 1360 A O ATOM 1784 CB GLU A 234 39.739 -34.385 1.084 1.00137.76 A C ANISOU 1784 CB GLU A 234 20704 10911 20729 -3234 -1986 519 A C ATOM 1785 CG GLU A 234 39.724 -33.509 -0.155 1.00138.14 A C ANISOU 1785 CG GLU A 234 20393 11386 20707 -3067 -2052 211 A C ATOM 1786 CD GLU A 234 38.392 -33.536 -0.888 1.00144.97 A C ANISOU 1786 CD GLU A 234 21020 12367 21697 -3317 -1942 -91 A C ATOM 1787 OE1 GLU A 234 37.653 -34.539 -0.760 1.00150.96 A O ANISOU 1787 OE1 GLU A 234 21887 12795 22675 -3579 -1865 -148 A O ATOM 1788 OE2 GLU A 234 38.092 -32.556 -1.607 1.00142.59 A O1- ANISOU 1788 OE2 GLU A 234 20416 12489 21274 -3247 -1932 -274 A O1- ATOM 1789 N GLN A 235 41.031 -36.839 2.884 1.00157.44 A N ANISOU 1789 N GLN A 235 24025 12351 23446 -3175 -2052 1086 A N ATOM 1790 CA GLN A 235 40.986 -37.594 4.137 1.00160.30 A C ANISOU 1790 CA GLN A 235 24738 12330 23838 -3318 -1956 1429 A C ATOM 1791 C GLN A 235 42.371 -37.817 4.741 1.00152.59 A C ANISOU 1791 C GLN A 235 24006 11226 22743 -2993 -2102 1702 A C ATOM 1792 O GLN A 235 42.541 -37.721 5.959 1.00144.06 A O ANISOU 1792 O GLN A 235 23136 10094 21507 -3028 -2041 2048 A O ATOM 1793 CB GLN A 235 40.273 -38.932 3.943 1.00169.87 A C ANISOU 1793 CB GLN A 235 26099 13065 25379 -3555 -1869 1325 A C ATOM 1794 CG GLN A 235 38.773 -38.812 3.779 1.00175.95 A C ANISOU 1794 CG GLN A 235 26687 13910 26254 -3955 -1679 1156 A C ATOM 1795 CD GLN A 235 38.127 -40.134 3.417 1.00186.77 A C ANISOU 1795 CD GLN A 235 28170 14816 27977 -4182 -1613 993 A C ATOM 1796 NE2 GLN A 235 36.798 -40.163 3.401 1.00188.99 A N ANISOU 1796 NE2 GLN A 235 28319 15116 28371 -4563 -1434 874 A N ATOM 1797 OE1 GLN A 235 38.816 -41.120 3.150 1.00191.31 A O ANISOU 1797 OE1 GLN A 235 28944 15019 28726 -4018 -1720 970 A O ATOM 1798 N HIS A 236 43.353 -38.125 3.894 1.00154.04 A N ANISOU 1798 N HIS A 236 24161 11372 22994 -2671 -2295 1546 A N ATOM 1799 CA HIS A 236 44.731 -38.240 4.357 1.00159.30 A C ANISOU 1799 CA HIS A 236 25010 11983 23533 -2328 -2453 1777 A C ATOM 1800 C HIS A 236 45.186 -36.882 4.876 1.00168.63 A C ANISOU 1800 C HIS A 236 26056 13626 24390 -2221 -2483 1928 A C ATOM 1801 O HIS A 236 45.872 -36.792 5.898 1.00176.94 A O ANISOU 1801 O HIS A 236 27301 14661 25269 -2107 -2519 2240 A O ATOM 1802 CB HIS A 236 45.664 -38.726 3.239 1.00156.37 A C ANISOU 1802 CB HIS A 236 24585 11541 23289 -1995 -2651 1547 A C ATOM 1803 CG HIS A 236 47.088 -38.914 3.676 1.00162.42 A C ANISOU 1803 CG HIS A 236 25528 12246 23937 -1632 -2816 1775 A C ATOM 1804 CD2 HIS A 236 47.628 -39.650 4.678 1.00169.90 A C ANISOU 1804 CD2 HIS A 236 26813 12873 24868 -1552 -2828 2099 A C ATOM 1805 ND1 HIS A 236 48.153 -38.295 3.050 1.00161.03 A N ANISOU 1805 ND1 HIS A 236 25168 12379 23637 -1290 -2995 1678 A N ATOM 1806 CE1 HIS A 236 49.279 -38.643 3.644 1.00162.48 A C ANISOU 1806 CE1 HIS A 236 25556 12443 23735 -1021 -3115 1921 A C ATOM 1807 NE2 HIS A 236 48.989 -39.464 4.638 1.00167.68 A N ANISOU 1807 NE2 HIS A 236 26537 12724 24450 -1164 -3021 2181 A N ATOM 1808 N GLN A 237 44.796 -35.824 4.171 1.00162.24 A N ANISOU 1808 N GLN A 237 24917 13230 23498 -2256 -2467 1701 A N ATOM 1809 CA GLN A 237 45.174 -34.479 4.569 1.00155.11 A C ANISOU 1809 CA GLN A 237 23866 12762 22305 -2169 -2484 1809 A C ATOM 1810 C GLN A 237 44.632 -34.191 5.955 1.00153.37 A C ANISOU 1810 C GLN A 237 23810 12536 21927 -2404 -2331 2114 A C ATOM 1811 O GLN A 237 45.395 -33.986 6.894 1.00157.74 A O ANISOU 1811 O GLN A 237 24523 13118 22295 -2274 -2387 2389 A O ATOM 1812 CB GLN A 237 44.635 -33.441 3.585 1.00152.87 A C ANISOU 1812 CB GLN A 237 23215 12889 21982 -2208 -2451 1517 A C ATOM 1813 CG GLN A 237 45.173 -32.031 3.811 1.00147.07 A C ANISOU 1813 CG GLN A 237 22313 12596 20971 -2072 -2485 1593 A C ATOM 1814 CD GLN A 237 46.613 -31.891 3.364 1.00147.56 A C ANISOU 1814 CD GLN A 237 22331 12758 20976 -1690 -2693 1579 A C ATOM 1815 NE2 GLN A 237 47.233 -30.770 3.704 1.00143.39 A N ANISOU 1815 NE2 GLN A 237 21699 12563 20219 -1568 -2733 1681 A N ATOM 1816 OE1 GLN A 237 47.161 -32.781 2.717 1.00153.80 A O ANISOU 1816 OE1 GLN A 237 23177 13326 21932 -1508 -2812 1472 A O ATOM 1817 N LEU A 238 43.311 -34.195 6.082 1.00147.58 A N ANISOU 1817 N LEU A 238 23032 11776 21264 -2747 -2138 2062 A N ATOM 1818 CA LEU A 238 42.671 -33.760 7.317 1.00147.53 A C ANISOU 1818 CA LEU A 238 23133 11833 21090 -2982 -1972 2323 A C ATOM 1819 C LEU A 238 43.219 -34.479 8.556 1.00153.90 A C ANISOU 1819 C LEU A 238 24305 12334 21836 -2936 -1979 2692 A C ATOM 1820 O LEU A 238 43.246 -33.917 9.649 1.00157.23 A O ANISOU 1820 O LEU A 238 24822 12892 22024 -2980 -1919 2948 A O ATOM 1821 CB LEU A 238 41.151 -33.900 7.213 1.00145.22 A C ANISOU 1821 CB LEU A 238 22754 11496 20929 -3360 -1761 2206 A C ATOM 1822 CG LEU A 238 40.294 -33.433 8.393 1.00144.53 A C ANISOU 1822 CG LEU A 238 22741 11496 20680 -3635 -1558 2443 A C ATOM 1823 CD1 LEU A 238 40.460 -31.960 8.696 1.00131.24 A C ANISOU 1823 CD1 LEU A 238 20887 10281 18697 -3561 -1557 2485 A C ATOM 1824 CD2 LEU A 238 38.841 -33.737 8.114 1.00153.65 A C ANISOU 1824 CD2 LEU A 238 23789 12578 22013 -3992 -1365 2290 A C ATOM 1825 N ALA A 239 43.664 -35.717 8.387 1.00155.05 A N ANISOU 1825 N ALA A 239 24660 12070 22182 -2833 -2053 2718 A N ATOM 1826 CA ALA A 239 44.307 -36.423 9.486 1.00153.10 A C ANISOU 1826 CA ALA A 239 24763 11536 21873 -2731 -2078 3070 A C ATOM 1827 C ALA A 239 45.671 -35.796 9.756 1.00150.20 A C ANISOU 1827 C ALA A 239 24388 11418 21264 -2378 -2273 3191 A C ATOM 1828 O ALA A 239 45.992 -35.436 10.886 1.00146.90 A O ANISOU 1828 O ALA A 239 24111 11094 20611 -2346 -2262 3478 A O ATOM 1829 CB ALA A 239 44.451 -37.902 9.160 1.00149.79 A C ANISOU 1829 CB ALA A 239 24566 10605 21743 -2691 -2105 3053 A C ATOM 1830 N LEU A 240 46.458 -35.660 8.693 1.00150.97 A N ANISOU 1830 N LEU A 240 24308 11635 21419 -2116 -2450 2958 A N ATOM 1831 CA LEU A 240 47.812 -35.122 8.760 1.00150.43 A C ANISOU 1831 CA LEU A 240 24195 11801 21160 -1769 -2648 3028 A C ATOM 1832 C LEU A 240 47.842 -33.750 9.440 1.00146.50 A C ANISOU 1832 C LEU A 240 23568 11734 20362 -1810 -2620 3132 A C ATOM 1833 O LEU A 240 48.801 -33.406 10.135 1.00145.47 A O ANISOU 1833 O LEU A 240 23512 11736 20023 -1610 -2734 3327 A O ATOM 1834 CB LEU A 240 48.396 -35.045 7.346 1.00150.22 A C ANISOU 1834 CB LEU A 240 23931 11888 21257 -1537 -2801 2710 A C ATOM 1835 CG LEU A 240 49.890 -34.792 7.161 1.00152.00 A C ANISOU 1835 CG LEU A 240 24109 12278 21365 -1145 -3023 2740 A C ATOM 1836 CD1 LEU A 240 50.704 -35.657 8.099 1.00155.21 A C ANISOU 1836 CD1 LEU A 240 24842 12402 21728 -970 -3105 3047 A C ATOM 1837 CD2 LEU A 240 50.263 -35.071 5.723 1.00152.44 A C ANISOU 1837 CD2 LEU A 240 23982 12331 21606 -952 -3137 2425 A C ATOM 1838 N ILE A 241 46.785 -32.972 9.230 1.00144.30 A N ANISOU 1838 N ILE A 241 23091 11674 20061 -2067 -2469 2993 A N ATOM 1839 CA ILE A 241 46.622 -31.690 9.903 1.00139.45 A C ANISOU 1839 CA ILE A 241 22370 11437 19177 -2149 -2407 3083 A C ATOM 1840 C ILE A 241 46.430 -31.919 11.397 1.00138.97 A C ANISOU 1840 C ILE A 241 22594 11249 18958 -2270 -2313 3431 A C ATOM 1841 O ILE A 241 47.115 -31.316 12.219 1.00141.10 A O ANISOU 1841 O ILE A 241 22918 11714 18980 -2147 -2383 3614 A O ATOM 1842 CB ILE A 241 45.414 -30.896 9.337 1.00118.88 A C ANISOU 1842 CB ILE A 241 19505 9066 16599 -2402 -2244 2859 A C ATOM 1843 CG1 ILE A 241 45.755 -30.285 7.977 1.00110.88 A C ANISOU 1843 CG1 ILE A 241 18176 8308 15644 -2234 -2345 2544 A C ATOM 1844 CG2 ILE A 241 44.984 -29.791 10.293 1.00119.31 A C ANISOU 1844 CG2 ILE A 241 19532 9410 16390 -2551 -2125 3005 A C ATOM 1845 CD1 ILE A 241 44.602 -29.530 7.350 1.00103.32 A C ANISOU 1845 CD1 ILE A 241 16956 7591 14709 -2447 -2194 2320 A C ATOM 1846 N SER A 242 45.499 -32.803 11.740 1.00140.56 A N ANISOU 1846 N SER A 242 22975 11127 19305 -2511 -2153 3520 A N ATOM 1847 CA SER A 242 45.216 -33.121 13.135 1.00144.60 A C ANISOU 1847 CA SER A 242 23770 11490 19681 -2638 -2038 3862 A C ATOM 1848 C SER A 242 46.434 -33.755 13.809 1.00149.64 A C ANISOU 1848 C SER A 242 24669 11955 20230 -2352 -2196 4120 A C ATOM 1849 O SER A 242 46.566 -33.715 15.035 1.00150.03 A O ANISOU 1849 O SER A 242 24923 12010 20070 -2356 -2158 4419 A O ATOM 1850 CB SER A 242 44.001 -34.050 13.239 1.00143.40 A C ANISOU 1850 CB SER A 242 23750 10989 19747 -2952 -1830 3893 A C ATOM 1851 OG SER A 242 43.368 -33.921 14.500 1.00141.20 A O ANISOU 1851 OG SER A 242 23640 10710 19300 -3154 -1656 4172 A O ATOM 1852 N GLN A 243 47.323 -34.333 13.003 1.00151.91 A N ANISOU 1852 N GLN A 243 24946 12106 20667 -2092 -2373 4001 A N ATOM 1853 CA GLN A 243 48.566 -34.900 13.517 1.00157.60 A C ANISOU 1853 CA GLN A 243 25882 12696 21305 -1778 -2544 4218 A C ATOM 1854 C GLN A 243 49.622 -33.807 13.657 1.00157.26 A C ANISOU 1854 C GLN A 243 25675 13077 21001 -1538 -2719 4215 A C ATOM 1855 O GLN A 243 50.825 -34.074 13.667 1.00160.61 A O ANISOU 1855 O GLN A 243 26155 13493 21375 -1223 -2912 4283 A O ATOM 1856 CB GLN A 243 49.079 -36.024 12.612 1.00162.39 A C ANISOU 1856 CB GLN A 243 26554 12964 22184 -1590 -2656 4096 A C ATOM 1857 CG GLN A 243 49.953 -37.041 13.342 1.00165.89 A C ANISOU 1857 CG GLN A 243 27328 13101 22602 -1350 -2748 4390 A C ATOM 1858 CD GLN A 243 50.748 -37.923 12.402 1.00165.50 A C ANISOU 1858 CD GLN A 243 27303 12809 22770 -1078 -2905 4250 A C ATOM 1859 NE2 GLN A 243 51.594 -38.777 12.968 1.00165.34 A N ANISOU 1859 NE2 GLN A 243 27557 12541 22722 -827 -2999 4496 A N ATOM 1860 OE1 GLN A 243 50.608 -37.836 11.181 1.00164.53 A O ANISOU 1860 OE1 GLN A 243 26956 12729 22827 -1078 -2941 3926 A O ATOM 1861 N LEU A 244 49.155 -32.567 13.759 1.00151.10 A N ANISOU 1861 N LEU A 244 24686 12666 20061 -1690 -2647 4129 A N ATOM 1862 CA LEU A 244 50.034 -31.434 13.985 1.00134.15 A C ANISOU 1862 CA LEU A 244 22382 10923 17664 -1515 -2783 4125 A C ATOM 1863 C LEU A 244 49.373 -30.378 14.879 1.00132.68 A C ANISOU 1863 C LEU A 244 22162 11015 17236 -1731 -2646 4216 A C ATOM 1864 O LEU A 244 50.044 -29.745 15.695 1.00138.50 A O ANISOU 1864 O LEU A 244 22926 11982 17714 -1619 -2730 4356 A O ATOM 1865 CB LEU A 244 50.455 -30.816 12.661 1.00127.59 A C ANISOU 1865 CB LEU A 244 21229 10318 16931 -1384 -2890 3805 A C ATOM 1866 CG LEU A 244 51.304 -29.556 12.863 1.00133.36 A C ANISOU 1866 CG LEU A 244 21776 11472 17421 -1237 -3009 3786 A C ATOM 1867 CD1 LEU A 244 52.731 -29.942 13.230 1.00138.56 A C ANISOU 1867 CD1 LEU A 244 22544 12116 17989 -909 -3229 3935 A C ATOM 1868 CD2 LEU A 244 51.276 -28.633 11.642 1.00123.87 A C ANISOU 1868 CD2 LEU A 244 20226 10547 16291 -1221 -3021 3473 A C ATOM 1869 N CYS A 245 48.059 -30.207 14.746 1.00130.58 A N ANISOU 1869 N CYS A 245 21837 10730 17048 -2038 -2435 4132 A N ATOM 1870 CA CYS A 245 47.348 -29.130 15.450 1.00134.35 A C ANISOU 1870 CA CYS A 245 22248 11491 17309 -2244 -2291 4178 A C ATOM 1871 C CYS A 245 46.499 -29.564 16.653 1.00137.82 A C ANISOU 1871 C CYS A 245 22945 11764 17656 -2466 -2106 4450 A C ATOM 1872 O CYS A 245 46.066 -28.725 17.453 1.00135.55 A O ANISOU 1872 O CYS A 245 22651 11711 17143 -2596 -2004 4538 A O ATOM 1873 CB CYS A 245 46.466 -28.355 14.467 1.00132.22 A C ANISOU 1873 CB CYS A 245 21679 11416 17141 -2419 -2178 3882 A C ATOM 1874 SG CYS A 245 47.361 -27.677 13.063 1.00138.10 A S ANISOU 1874 SG CYS A 245 22101 12406 17966 -2171 -2361 3570 A S ATOM 1875 N GLY A 246 46.261 -30.865 16.776 1.00139.94 A N ANISOU 1875 N GLY A 246 23443 11626 18101 -2508 -2055 4583 A N ATOM 1876 CA GLY A 246 45.393 -31.383 17.816 1.00139.34 A C ANISOU 1876 CA GLY A 246 23610 11354 17978 -2731 -1856 4842 A C ATOM 1877 C GLY A 246 44.135 -31.934 17.187 1.00140.46 A C ANISOU 1877 C GLY A 246 23701 11270 18397 -3023 -1663 4704 A C ATOM 1878 O GLY A 246 43.920 -31.795 15.985 1.00133.42 A O ANISOU 1878 O GLY A 246 22573 10420 17700 -3047 -1690 4400 A O ATOM 1879 N SER A 247 43.298 -32.573 17.990 1.00149.45 A N ANISOU 1879 N SER A 247 25056 12174 19556 -3244 -1467 4926 A N ATOM 1880 CA SER A 247 42.071 -33.136 17.452 1.00156.01 A C ANISOU 1880 CA SER A 247 25835 12782 20658 -3546 -1276 4800 A C ATOM 1881 C SER A 247 41.000 -32.064 17.362 1.00149.12 A C ANISOU 1881 C SER A 247 24716 12243 19701 -3796 -1114 4651 A C ATOM 1882 O SER A 247 40.893 -31.195 18.231 1.00147.30 A O ANISOU 1882 O SER A 247 24492 12289 19187 -3823 -1057 4787 A O ATOM 1883 CB SER A 247 41.589 -34.334 18.281 1.00166.18 A C ANISOU 1883 CB SER A 247 27451 13650 22040 -3696 -1115 5095 A C ATOM 1884 OG SER A 247 41.348 -33.973 19.627 1.00170.37 A O ANISOU 1884 OG SER A 247 28144 14303 22288 -3766 -995 5399 A O ATOM 1885 N ILE A 248 40.224 -32.123 16.289 1.00144.23 A N ANISOU 1885 N ILE A 248 23876 11604 19321 -3962 -1047 4362 A N ATOM 1886 CA ILE A 248 39.137 -31.186 16.095 1.00143.51 A C ANISOU 1886 CA ILE A 248 23536 11815 19175 -4195 -887 4203 A C ATOM 1887 C ILE A 248 37.993 -31.530 17.046 1.00153.97 A C ANISOU 1887 C ILE A 248 25007 13013 20480 -4507 -627 4420 A C ATOM 1888 O ILE A 248 37.422 -32.619 16.971 1.00159.83 A O ANISOU 1888 O ILE A 248 25867 13396 21464 -4687 -518 4459 A O ATOM 1889 CB ILE A 248 38.662 -31.210 14.638 1.00139.54 A C ANISOU 1889 CB ILE A 248 22748 11337 18932 -4261 -902 3827 A C ATOM 1890 CG1 ILE A 248 39.860 -31.017 13.697 1.00130.59 A C ANISOU 1890 CG1 ILE A 248 21496 10289 17831 -3933 -1156 3637 A C ATOM 1891 CG2 ILE A 248 37.600 -30.150 14.415 1.00138.62 A C ANISOU 1891 CG2 ILE A 248 22360 11577 18734 -4462 -748 3663 A C ATOM 1892 CD1 ILE A 248 39.524 -31.085 12.212 1.00121.48 A C ANISOU 1892 CD1 ILE A 248 20072 9165 16920 -3949 -1194 3263 A C ATOM 1893 N THR A 249 37.681 -30.606 17.954 1.00153.11 A N ANISOU 1893 N THR A 249 24897 13195 20084 -4570 -525 4563 A N ATOM 1894 CA THR A 249 36.646 -30.821 18.967 1.00153.00 A C ANISOU 1894 CA THR A 249 25022 13109 20001 -4844 -273 4796 A C ATOM 1895 C THR A 249 35.936 -29.514 19.304 1.00154.71 A C ANISOU 1895 C THR A 249 25052 13751 19980 -4962 -145 4747 A C ATOM 1896 O THR A 249 36.536 -28.445 19.214 1.00146.03 A O ANISOU 1896 O THR A 249 23825 12978 18680 -4778 -268 4654 A O ATOM 1897 CB THR A 249 37.239 -31.383 20.274 1.00143.56 A C ANISOU 1897 CB THR A 249 24190 11725 18632 -4740 -276 5192 A C ATOM 1898 CG2 THR A 249 37.885 -32.741 20.030 1.00136.95 A C ANISOU 1898 CG2 THR A 249 23570 10435 18030 -4623 -378 5274 A C ATOM 1899 OG1 THR A 249 38.217 -30.466 20.790 1.00139.01 A O ANISOU 1899 OG1 THR A 249 23626 11451 17738 -4480 -437 5262 A O ATOM 1900 N PRO A 250 34.654 -29.594 19.702 1.00163.35 A N ANISOU 1900 N PRO A 250 26128 14839 21099 -5270 111 4810 A N ATOM 1901 CA PRO A 250 33.957 -28.376 20.128 1.00161.36 A C ANISOU 1901 CA PRO A 250 25722 14984 20602 -5372 248 4790 A C ATOM 1902 C PRO A 250 34.732 -27.667 21.244 1.00161.37 A C ANISOU 1902 C PRO A 250 25888 15186 20238 -5179 178 5015 A C ATOM 1903 O PRO A 250 34.635 -26.446 21.390 1.00155.09 A O ANISOU 1903 O PRO A 250 24946 14760 19219 -5143 192 4933 A O ATOM 1904 CB PRO A 250 32.612 -28.904 20.643 1.00162.76 A C ANISOU 1904 CB PRO A 250 25948 15031 20864 -5715 535 4921 A C ATOM 1905 CG PRO A 250 32.402 -30.186 19.905 1.00162.78 A C ANISOU 1905 CG PRO A 250 25977 14631 21242 -5834 537 4835 A C ATOM 1906 CD PRO A 250 33.777 -30.780 19.744 1.00164.87 A C ANISOU 1906 CD PRO A 250 26426 14665 21553 -5540 291 4891 A C ATOM 1907 N GLU A 251 35.501 -28.431 22.015 1.00168.61 A N ANISOU 1907 N GLU A 251 27109 15862 21095 -5048 101 5290 A N ATOM 1908 CA GLU A 251 36.313 -27.864 23.088 1.00169.07 A C ANISOU 1908 CA GLU A 251 27333 16102 20804 -4848 12 5503 A C ATOM 1909 C GLU A 251 37.332 -26.879 22.529 1.00160.66 A C ANISOU 1909 C GLU A 251 26095 15319 19630 -4588 -225 5290 A C ATOM 1910 O GLU A 251 37.406 -25.735 22.968 1.00153.08 A O ANISOU 1910 O GLU A 251 25059 14700 18406 -4541 -226 5268 A O ATOM 1911 CB GLU A 251 37.024 -28.967 23.880 1.00175.61 A C ANISOU 1911 CB GLU A 251 28509 16605 21611 -4722 -49 5823 A C ATOM 1912 CG GLU A 251 37.899 -28.440 25.011 1.00177.60 A C ANISOU 1912 CG GLU A 251 28935 17056 21490 -4500 -157 6043 A C ATOM 1913 CD GLU A 251 38.565 -29.545 25.812 1.00185.13 A C ANISOU 1913 CD GLU A 251 30232 17702 22406 -4359 -209 6376 A C ATOM 1914 OE1 GLU A 251 38.331 -30.736 25.508 1.00186.76 A O ANISOU 1914 OE1 GLU A 251 30560 17513 22889 -4442 -147 6447 A O ATOM 1915 OE2 GLU A 251 39.323 -29.217 26.749 1.00187.90 A O1- ANISOU 1915 OE2 GLU A 251 30735 18208 22449 -4160 -311 6563 A O1- ATOM 1916 N VAL A 252 38.114 -27.334 21.557 1.00161.03 A N ANISOU 1916 N VAL A 252 26080 15216 19888 -4423 -419 5132 A N ATOM 1917 CA VAL A 252 39.124 -26.496 20.920 1.00156.04 A C ANISOU 1917 CA VAL A 252 25273 14825 19191 -4176 -643 4927 A C ATOM 1918 C VAL A 252 38.486 -25.583 19.870 1.00150.17 A C ANISOU 1918 C VAL A 252 24188 14333 18535 -4270 -587 4599 A C ATOM 1919 O VAL A 252 38.936 -24.456 19.663 1.00149.93 A O ANISOU 1919 O VAL A 252 23997 14614 18356 -4143 -675 4462 A O ATOM 1920 CB VAL A 252 40.247 -27.359 20.276 1.00111.19 A C ANISOU 1920 CB VAL A 252 19658 8896 13695 -3940 -871 4892 A C ATOM 1921 CG1 VAL A 252 41.384 -26.491 19.771 1.00 98.31 A C ANISOU 1921 CG1 VAL A 252 17862 7525 11966 -3674 -1100 4723 A C ATOM 1922 CG2 VAL A 252 40.778 -28.367 21.283 1.00118.24 A C ANISOU 1922 CG2 VAL A 252 20897 9510 14520 -3848 -905 5229 A C ATOM 1923 N TRP A 253 37.420 -26.064 19.233 1.00146.09 A N ANISOU 1923 N TRP A 253 23565 13686 18257 -4495 -435 4479 A N ATOM 1924 CA TRP A 253 36.796 -25.369 18.104 1.00138.11 A C ANISOU 1924 CA TRP A 253 22226 12888 17362 -4568 -390 4158 A C ATOM 1925 C TRP A 253 35.264 -25.358 18.218 1.00140.44 A C ANISOU 1925 C TRP A 253 22434 13219 17710 -4887 -121 4140 A C ATOM 1926 O TRP A 253 34.591 -26.194 17.618 1.00142.95 A O ANISOU 1926 O TRP A 253 22700 13321 18291 -5053 -46 4047 A O ATOM 1927 CB TRP A 253 37.243 -26.033 16.790 1.00129.54 A C ANISOU 1927 CB TRP A 253 21026 11621 16571 -4460 -542 3932 A C ATOM 1928 CG TRP A 253 36.629 -25.478 15.524 1.00127.15 A C ANISOU 1928 CG TRP A 253 20389 11515 16408 -4514 -508 3596 A C ATOM 1929 CD1 TRP A 253 35.641 -24.534 15.421 1.00127.45 A C ANISOU 1929 CD1 TRP A 253 20221 11848 16358 -4663 -343 3482 A C ATOM 1930 CD2 TRP A 253 36.971 -25.843 14.180 1.00121.25 A C ANISOU 1930 CD2 TRP A 253 19476 10693 15900 -4399 -644 3335 A C ATOM 1931 CE2 TRP A 253 36.148 -25.084 13.315 1.00118.12 A C ANISOU 1931 CE2 TRP A 253 18774 10564 15543 -4485 -552 3073 A C ATOM 1932 CE3 TRP A 253 37.895 -26.731 13.623 1.00116.63 A C ANISOU 1932 CE3 TRP A 253 18974 9851 15491 -4217 -832 3295 A C ATOM 1933 NE1 TRP A 253 35.347 -24.292 14.094 1.00119.48 A N ANISOU 1933 NE1 TRP A 253 18927 10956 15515 -4644 -369 3171 A N ATOM 1934 CZ2 TRP A 253 36.221 -25.197 11.929 1.00113.59 A C ANISOU 1934 CZ2 TRP A 253 17977 10014 15170 -4397 -645 2779 A C ATOM 1935 CZ3 TRP A 253 37.968 -26.838 12.243 1.00112.26 A C ANISOU 1935 CZ3 TRP A 253 18198 9314 15141 -4134 -922 2996 A C ATOM 1936 CH2 TRP A 253 37.136 -26.081 11.414 1.00112.33 A C ANISOU 1936 CH2 TRP A 253 17906 9598 15177 -4224 -830 2742 A C ATOM 1937 N PRO A 254 34.709 -24.395 18.976 1.00139.20 A N ANISOU 1937 N PRO A 254 22250 13341 17300 -4974 22 4217 A N ATOM 1938 CA PRO A 254 33.266 -24.309 19.253 1.00140.10 A C ANISOU 1938 CA PRO A 254 22288 13525 17418 -5266 289 4234 A C ATOM 1939 C PRO A 254 32.381 -24.551 18.026 1.00147.80 A C ANISOU 1939 C PRO A 254 22998 14486 18674 -5422 360 3954 A C ATOM 1940 O PRO A 254 32.696 -24.085 16.940 1.00151.05 A O ANISOU 1940 O PRO A 254 23187 15038 19167 -5287 239 3690 A O ATOM 1941 CB PRO A 254 33.098 -22.868 19.746 1.00130.98 A C ANISOU 1941 CB PRO A 254 21038 12769 15959 -5227 355 4221 A C ATOM 1942 CG PRO A 254 34.395 -22.551 20.389 1.00127.69 A C ANISOU 1942 CG PRO A 254 20797 12389 15330 -4978 167 4356 A C ATOM 1943 CD PRO A 254 35.448 -23.267 19.574 1.00131.58 A C ANISOU 1943 CD PRO A 254 21305 12662 16028 -4789 -66 4269 A C ATOM 1944 N ASN A 255 31.283 -25.277 18.210 1.00158.99 A N ANISOU 1944 N ASN A 255 24432 15743 20233 -5702 558 4013 A N ATOM 1945 CA ASN A 255 30.327 -25.533 17.130 1.00164.98 A C ANISOU 1945 CA ASN A 255 24930 16505 21251 -5882 640 3746 A C ATOM 1946 C ASN A 255 30.902 -26.216 15.887 1.00159.04 A C ANISOU 1946 C ASN A 255 24092 15556 20778 -5766 450 3514 A C ATOM 1947 O ASN A 255 30.305 -26.146 14.811 1.00155.65 A O ANISOU 1947 O ASN A 255 23396 15225 20519 -5837 466 3230 A O ATOM 1948 CB ASN A 255 29.606 -24.241 16.720 1.00167.49 A C ANISOU 1948 CB ASN A 255 24947 17254 21437 -5904 736 3547 A C ATOM 1949 CG ASN A 255 28.216 -24.121 17.331 1.00174.20 A C ANISOU 1949 CG ASN A 255 25743 18214 22232 -6195 1015 3631 A C ATOM 1950 ND2 ASN A 255 27.551 -22.999 17.063 1.00167.12 A N ANISOU 1950 ND2 ASN A 255 24600 17694 21204 -6206 1113 3481 A N ATOM 1951 OD1 ASN A 255 27.742 -25.026 18.031 1.00182.26 A O ANISOU 1951 OD1 ASN A 255 26938 18984 23328 -6402 1148 3835 A O ATOM 1952 N VAL A 256 32.050 -26.874 16.029 1.00156.12 A N ANISOU 1952 N VAL A 256 23946 14925 20448 -5579 270 3631 A N ATOM 1953 CA VAL A 256 32.632 -27.613 14.915 1.00155.38 A C ANISOU 1953 CA VAL A 256 23801 14618 20618 -5459 91 3429 A C ATOM 1954 C VAL A 256 31.812 -28.862 14.643 1.00167.72 A C ANISOU 1954 C VAL A 256 25398 15842 22488 -5721 204 3391 A C ATOM 1955 O VAL A 256 31.908 -29.466 13.577 1.00166.06 A O ANISOU 1955 O VAL A 256 25083 15480 22532 -5696 105 3156 A O ATOM 1956 CB VAL A 256 34.086 -28.032 15.185 1.00149.80 A C ANISOU 1956 CB VAL A 256 23333 13715 19870 -5179 -127 3578 A C ATOM 1957 CG1 VAL A 256 34.162 -28.926 16.409 1.00152.55 A C ANISOU 1957 CG1 VAL A 256 24030 13747 20185 -5263 -49 3933 A C ATOM 1958 CG2 VAL A 256 34.660 -28.744 13.970 1.00146.38 A C ANISOU 1958 CG2 VAL A 256 22828 13085 19705 -5042 -306 3348 A C ATOM 1959 N ASP A 257 31.001 -29.245 15.621 1.00182.51 A N ANISOU 1959 N ASP A 257 27415 17594 24335 -5974 417 3622 A N ATOM 1960 CA ASP A 257 30.165 -30.426 15.492 1.00192.46 A C ANISOU 1960 CA ASP A 257 28720 18518 25889 -6260 555 3613 A C ATOM 1961 C ASP A 257 29.226 -30.319 14.289 1.00190.46 A C ANISOU 1961 C ASP A 257 28117 18408 25840 -6421 601 3243 A C ATOM 1962 O ASP A 257 29.082 -31.273 13.523 1.00192.31 A O ANISOU 1962 O ASP A 257 28321 18370 26378 -6509 562 3071 A O ATOM 1963 CB ASP A 257 29.360 -30.644 16.771 1.00203.60 A C ANISOU 1963 CB ASP A 257 30304 19852 27201 -6513 806 3926 A C ATOM 1964 CG ASP A 257 28.428 -31.834 16.671 1.00220.78 A C ANISOU 1964 CG ASP A 257 32515 21680 29692 -6840 974 3923 A C ATOM 1965 OD1 ASP A 257 28.621 -32.658 15.752 1.00226.65 A O ANISOU 1965 OD1 ASP A 257 33227 22161 30728 -6840 868 3722 A O ATOM 1966 OD2 ASP A 257 27.504 -31.951 17.506 1.00227.25 A O1- ANISOU 1966 OD2 ASP A 257 33390 22486 30469 -7101 1216 4115 A O1- ATOM 1967 N ASN A 258 28.609 -29.149 14.122 1.00185.53 A N ANISOU 1967 N ASN A 258 27231 18216 25044 -6445 679 3117 A N ATOM 1968 CA ASN A 258 27.544 -28.940 13.129 1.00180.44 A C ANISOU 1968 CA ASN A 258 26240 17772 24547 -6615 759 2794 A C ATOM 1969 C ASN A 258 27.887 -29.282 11.670 1.00171.65 A C ANISOU 1969 C ASN A 258 24941 16612 23666 -6491 572 2443 A C ATOM 1970 O ASN A 258 26.994 -29.369 10.824 1.00166.89 A O ANISOU 1970 O ASN A 258 24071 16113 23226 -6650 630 2169 A O ATOM 1971 CB ASN A 258 27.000 -27.505 13.210 1.00179.13 A C ANISOU 1971 CB ASN A 258 25843 18103 24116 -6588 854 2736 A C ATOM 1972 CG ASN A 258 26.407 -27.171 14.573 1.00181.00 A C ANISOU 1972 CG ASN A 258 26217 18417 24137 -6752 1072 3040 A C ATOM 1973 ND2 ASN A 258 25.518 -26.184 14.600 1.00178.36 A N ANISOU 1973 ND2 ASN A 258 25654 18464 23648 -6833 1220 2964 A N ATOM 1974 OD1 ASN A 258 26.751 -27.783 15.587 1.00183.35 A O ANISOU 1974 OD1 ASN A 258 26823 18444 24397 -6789 1108 3342 A O ATOM 1975 N TYR A 259 29.171 -29.460 11.374 1.00168.36 A N ANISOU 1975 N TYR A 259 24655 16061 23253 -6200 348 2444 A N ATOM 1976 CA TYR A 259 29.588 -29.847 10.030 1.00165.96 A C ANISOU 1976 CA TYR A 259 24203 15694 23160 -6058 165 2128 A C ATOM 1977 C TYR A 259 29.195 -31.296 9.794 1.00166.29 A C ANISOU 1977 C TYR A 259 24345 15300 23538 -6277 199 2069 A C ATOM 1978 O TYR A 259 29.562 -32.179 10.567 1.00166.62 A O ANISOU 1978 O TYR A 259 24700 14958 23649 -6323 218 2322 A O ATOM 1979 CB TYR A 259 31.105 -29.695 9.854 1.00167.69 A C ANISOU 1979 CB TYR A 259 24550 15875 23291 -5686 -75 2171 A C ATOM 1980 CG TYR A 259 31.634 -28.268 9.831 1.00163.32 A C ANISOU 1980 CG TYR A 259 23866 15743 22447 -5443 -143 2163 A C ATOM 1981 CD1 TYR A 259 32.250 -27.753 8.698 1.00158.04 A C ANISOU 1981 CD1 TYR A 259 22992 15275 21782 -5185 -313 1911 A C ATOM 1982 CD2 TYR A 259 31.531 -27.447 10.947 1.00162.65 A C ANISOU 1982 CD2 TYR A 259 23869 15844 22086 -5470 -32 2410 A C ATOM 1983 CE1 TYR A 259 32.738 -26.464 8.674 1.00156.38 A C ANISOU 1983 CE1 TYR A 259 22668 15423 21325 -4974 -361 1910 A C ATOM 1984 CE2 TYR A 259 32.014 -26.156 10.933 1.00157.69 A C ANISOU 1984 CE2 TYR A 259 23131 15575 21210 -5260 -89 2393 A C ATOM 1985 CZ TYR A 259 32.618 -25.667 9.795 1.00157.78 A C ANISOU 1985 CZ TYR A 259 22940 15764 21246 -5018 -249 2147 A C ATOM 1986 OH TYR A 259 33.108 -24.377 9.783 1.00154.33 A O ANISOU 1986 OH TYR A 259 22397 15665 20575 -4819 -293 2137 A O ATOM 1987 N GLU A 260 28.448 -31.544 8.726 1.00170.13 A N ANISOU 1987 N GLU A 260 24567 15840 24233 -6408 210 1733 A N ATOM 1988 CA GLU A 260 28.021 -32.903 8.425 1.00180.34 A C ANISOU 1988 CA GLU A 260 25932 16722 25868 -6636 243 1633 A C ATOM 1989 C GLU A 260 29.181 -33.894 8.500 1.00181.55 A C ANISOU 1989 C GLU A 260 26399 16431 26152 -6456 84 1748 A C ATOM 1990 O GLU A 260 29.022 -35.006 8.999 1.00190.02 A O ANISOU 1990 O GLU A 260 27709 17070 27421 -6642 166 1894 A O ATOM 1991 CB GLU A 260 27.363 -32.986 7.042 1.00186.21 A C ANISOU 1991 CB GLU A 260 26331 17615 26806 -6706 199 1193 A C ATOM 1992 CG GLU A 260 25.929 -32.471 6.974 1.00189.89 A C ANISOU 1992 CG GLU A 260 26502 18398 27250 -6990 397 1065 A C ATOM 1993 CD GLU A 260 25.172 -33.009 5.766 1.00192.36 A C ANISOU 1993 CD GLU A 260 26537 18718 27833 -7145 374 655 A C ATOM 1994 OE1 GLU A 260 25.204 -34.241 5.540 1.00193.23 A O ANISOU 1994 OE1 GLU A 260 26777 18404 28238 -7279 344 577 A O ATOM 1995 OE2 GLU A 260 24.542 -32.201 5.049 1.00191.17 A O1- ANISOU 1995 OE2 GLU A 260 26041 18997 27596 -7130 387 407 A O1- ATOM 1996 N LEU A 261 30.347 -33.484 8.012 1.00172.37 A N ANISOU 1996 N LEU A 261 25236 15376 24881 -6091 -135 1689 A N ATOM 1997 CA LEU A 261 31.455 -34.413 7.809 1.00169.23 A C ANISOU 1997 CA LEU A 261 25076 14597 24626 -5884 -313 1721 A C ATOM 1998 C LEU A 261 32.340 -34.615 9.036 1.00170.86 A C ANISOU 1998 C LEU A 261 25647 14589 24683 -5754 -328 2133 A C ATOM 1999 O LEU A 261 33.333 -35.338 8.974 1.00166.18 A O ANISOU 1999 O LEU A 261 25268 13695 24177 -5552 -476 2198 A O ATOM 2000 CB LEU A 261 32.307 -33.967 6.616 1.00163.90 A C ANISOU 2000 CB LEU A 261 24215 14134 23927 -5544 -545 1445 A C ATOM 2001 CG LEU A 261 31.620 -33.982 5.251 1.00160.81 A C ANISOU 2001 CG LEU A 261 23489 13902 23709 -5612 -573 1012 A C ATOM 2002 CD1 LEU A 261 32.574 -33.521 4.162 1.00153.95 A C ANISOU 2002 CD1 LEU A 261 22466 13244 22785 -5241 -798 787 A C ATOM 2003 CD2 LEU A 261 31.084 -35.375 4.944 1.00163.63 A C ANISOU 2003 CD2 LEU A 261 23930 13822 24419 -5855 -531 876 A C ATOM 2004 N TYR A 262 31.982 -33.984 10.149 1.00179.21 A N ANISOU 2004 N TYR A 262 26774 15811 25508 -5860 -178 2406 A N ATOM 2005 CA TYR A 262 32.816 -34.032 11.350 1.00189.30 A C ANISOU 2005 CA TYR A 262 28375 16957 26592 -5717 -198 2795 A C ATOM 2006 C TYR A 262 33.023 -35.465 11.853 1.00193.22 A C ANISOU 2006 C TYR A 262 29212 16901 27300 -5794 -165 2999 A C ATOM 2007 O TYR A 262 34.052 -36.087 11.579 1.00195.05 A O ANISOU 2007 O TYR A 262 29606 16886 27618 -5554 -342 3009 A O ATOM 2008 CB TYR A 262 32.238 -33.117 12.442 1.00196.08 A C ANISOU 2008 CB TYR A 262 29233 18101 27167 -5846 -21 3028 A C ATOM 2009 CG TYR A 262 32.800 -33.341 13.830 1.00204.58 A C ANISOU 2009 CG TYR A 262 30661 19009 28062 -5782 14 3448 A C ATOM 2010 CD1 TYR A 262 34.170 -33.321 14.067 1.00206.39 A C ANISOU 2010 CD1 TYR A 262 31069 19189 28160 -5446 -189 3585 A C ATOM 2011 CD2 TYR A 262 31.954 -33.553 14.910 1.00209.42 A C ANISOU 2011 CD2 TYR A 262 31415 19534 28621 -6051 251 3710 A C ATOM 2012 CE1 TYR A 262 34.679 -33.525 15.340 1.00209.93 A C ANISOU 2012 CE1 TYR A 262 31832 19508 28425 -5374 -165 3965 A C ATOM 2013 CE2 TYR A 262 32.453 -33.756 16.182 1.00213.04 A C ANISOU 2013 CE2 TYR A 262 32195 19856 28895 -5979 286 4099 A C ATOM 2014 CZ TYR A 262 33.813 -33.742 16.394 1.00213.15 A C ANISOU 2014 CZ TYR A 262 32385 19829 28776 -5637 73 4223 A C ATOM 2015 OH TYR A 262 34.304 -33.946 17.665 1.00215.46 A O ANISOU 2015 OH TYR A 262 32989 20007 28868 -5552 101 4606 A O ATOM 2016 N GLU A 263 32.039 -35.979 12.583 1.00193.80 A N ANISOU 2016 N GLU A 263 29393 16784 27457 -6126 69 3167 A N ATOM 2017 CA GLU A 263 32.060 -37.354 13.068 1.00197.07 A C ANISOU 2017 CA GLU A 263 30128 16654 28096 -6246 145 3367 A C ATOM 2018 C GLU A 263 31.772 -38.294 11.909 1.00196.02 A C ANISOU 2018 C GLU A 263 29900 16234 28343 -6354 99 3035 A C ATOM 2019 O GLU A 263 32.002 -39.499 11.987 1.00194.26 A O ANISOU 2019 O GLU A 263 29928 15524 28357 -6389 105 3118 A O ATOM 2020 CB GLU A 263 30.995 -37.533 14.150 1.00199.87 A C ANISOU 2020 CB GLU A 263 30588 16928 28425 -6591 433 3632 A C ATOM 2021 CG GLU A 263 30.866 -38.943 14.688 1.00205.61 A C ANISOU 2021 CG GLU A 263 31642 17084 29398 -6759 557 3856 A C ATOM 2022 CD GLU A 263 31.865 -39.245 15.785 1.00206.76 A C ANISOU 2022 CD GLU A 263 32171 17030 29360 -6523 515 4274 A C ATOM 2023 OE1 GLU A 263 32.750 -38.394 16.036 1.00199.95 A O ANISOU 2023 OE1 GLU A 263 31308 16470 28195 -6216 357 4352 A O ATOM 2024 OE2 GLU A 263 31.756 -40.336 16.397 1.00210.27 A O1- ANISOU 2024 OE2 GLU A 263 32913 17016 29962 -6647 643 4522 A O1- ATOM 2025 N LYS A 264 31.267 -37.715 10.827 1.00195.96 A N ANISOU 2025 N LYS A 264 29528 16540 28386 -6398 54 2655 A N ATOM 2026 CA LYS A 264 30.849 -38.462 9.653 1.00199.09 A C ANISOU 2026 CA LYS A 264 29774 16751 29121 -6520 14 2285 A C ATOM 2027 C LYS A 264 32.008 -38.645 8.671 1.00196.62 A C ANISOU 2027 C LYS A 264 29454 16386 28868 -6158 -260 2075 A C ATOM 2028 O LYS A 264 31.796 -38.750 7.462 1.00192.19 A O ANISOU 2028 O LYS A 264 28656 15892 28477 -6155 -350 1690 A O ATOM 2029 CB LYS A 264 29.698 -37.716 8.977 1.00199.98 A C ANISOU 2029 CB LYS A 264 29481 17268 29233 -6732 102 1977 A C ATOM 2030 CG LYS A 264 28.782 -38.568 8.126 1.00208.48 A C ANISOU 2030 CG LYS A 264 30405 18141 30666 -7021 162 1652 A C ATOM 2031 CD LYS A 264 27.596 -37.752 7.627 1.00209.43 A C ANISOU 2031 CD LYS A 264 30124 18710 30741 -7229 266 1395 A C ATOM 2032 CE LYS A 264 26.559 -38.641 6.952 1.00213.98 A C ANISOU 2032 CE LYS A 264 30550 19081 31671 -7574 355 1096 A C ATOM 2033 NZ LYS A 264 25.401 -37.852 6.449 1.00212.81 A N1+ ANISOU 2033 NZ LYS A 264 29994 19396 31469 -7762 450 839 A N1+ ATOM 2034 N LEU A 265 33.232 -38.677 9.196 1.00198.59 A N ANISOU 2034 N LEU A 265 29955 16534 28966 -5847 -391 2327 A N ATOM 2035 CA LEU A 265 34.429 -38.797 8.363 1.00199.30 A C ANISOU 2035 CA LEU A 265 30047 16597 29081 -5474 -650 2168 A C ATOM 2036 C LEU A 265 35.556 -39.487 9.124 1.00199.91 A C ANISOU 2036 C LEU A 265 30509 16323 29125 -5243 -733 2496 A C ATOM 2037 O LEU A 265 36.726 -39.398 8.746 1.00196.05 A O ANISOU 2037 O LEU A 265 30052 15872 28564 -4885 -947 2466 A O ATOM 2038 CB LEU A 265 34.887 -37.416 7.866 1.00196.85 A C ANISOU 2038 CB LEU A 265 29457 16837 28500 -5222 -785 2030 A C ATOM 2039 CG LEU A 265 36.134 -37.293 6.980 1.00191.74 A C ANISOU 2039 CG LEU A 265 28755 16267 27830 -4819 -1047 1863 A C ATOM 2040 CD1 LEU A 265 36.169 -38.394 5.929 1.00197.81 A C ANISOU 2040 CD1 LEU A 265 29523 16705 28930 -4810 -1134 1573 A C ATOM 2041 CD2 LEU A 265 36.209 -35.917 6.329 1.00178.04 A C ANISOU 2041 CD2 LEU A 265 26679 15086 25881 -4667 -1122 1667 A C ATOM 2042 N GLU A 266 35.194 -40.180 10.198 1.00204.54 A N ANISOU 2042 N GLU A 266 31382 16574 29760 -5443 -558 2816 A N ATOM 2043 CA GLU A 266 36.170 -40.923 10.986 1.00207.65 A C ANISOU 2043 CA GLU A 266 32161 16609 30128 -5235 -614 3152 A C ATOM 2044 C GLU A 266 37.413 -40.063 11.200 1.00204.50 A C ANISOU 2044 C GLU A 266 31762 16530 29409 -4835 -816 3270 A C ATOM 2045 O GLU A 266 38.492 -40.362 10.689 1.00204.60 A O ANISOU 2045 O GLU A 266 31834 16450 29456 -4516 -1022 3201 A O ATOM 2046 CB GLU A 266 36.530 -42.247 10.294 1.00207.35 A C ANISOU 2046 CB GLU A 266 32283 16069 30432 -5174 -695 3010 A C ATOM 2047 CG GLU A 266 36.442 -43.485 11.188 1.00208.93 A C ANISOU 2047 CG GLU A 266 32883 15704 30798 -5303 -547 3332 A C ATOM 2048 CD GLU A 266 36.628 -44.784 10.413 1.00213.14 A C ANISOU 2048 CD GLU A 266 33551 15727 31706 -5288 -603 3142 A C ATOM 2049 OE1 GLU A 266 36.897 -44.712 9.196 1.00213.73 A O ANISOU 2049 OE1 GLU A 266 33411 15907 31889 -5152 -774 2761 A O ATOM 2050 OE2 GLU A 266 36.505 -45.875 11.015 1.00214.16 A O1- ANISOU 2050 OE2 GLU A 266 34005 15346 32020 -5407 -472 3371 A O1- ATOM 2051 N LEU A 267 37.243 -38.975 11.938 1.00200.67 A N ANISOU 2051 N LEU A 267 31197 16434 28616 -4860 -752 3432 A N ATOM 2052 CA LEU A 267 38.357 -38.116 12.302 1.00198.93 A C ANISOU 2052 CA LEU A 267 30985 16521 28080 -4521 -921 3567 A C ATOM 2053 C LEU A 267 39.050 -38.700 13.532 1.00203.63 A C ANISOU 2053 C LEU A 267 31965 16849 28556 -4390 -917 3993 A C ATOM 2054 O LEU A 267 38.385 -39.101 14.487 1.00210.04 A O ANISOU 2054 O LEU A 267 32971 17471 29362 -4619 -715 4256 A O ATOM 2055 CB LEU A 267 37.847 -36.702 12.581 1.00196.30 A C ANISOU 2055 CB LEU A 267 30409 16702 27474 -4611 -847 3548 A C ATOM 2056 CG LEU A 267 38.853 -35.587 12.857 1.00195.20 A C ANISOU 2056 CG LEU A 267 30207 16954 27007 -4307 -1007 3624 A C ATOM 2057 CD1 LEU A 267 38.177 -34.251 12.679 1.00192.26 A C ANISOU 2057 CD1 LEU A 267 29527 17061 26463 -4423 -931 3472 A C ATOM 2058 CD2 LEU A 267 39.450 -35.692 14.252 1.00199.28 A C ANISOU 2058 CD2 LEU A 267 31034 17388 27293 -4201 -999 4039 A C ATOM 2059 N VAL A 268 40.379 -38.755 13.509 1.00199.93 A N ANISOU 2059 N VAL A 268 31601 16376 27987 -4015 -1135 4065 A N ATOM 2060 CA VAL A 268 41.135 -39.370 14.602 1.00198.20 A C ANISOU 2060 CA VAL A 268 31747 15907 27654 -3842 -1157 4458 A C ATOM 2061 C VAL A 268 40.882 -38.674 15.944 1.00189.33 A C ANISOU 2061 C VAL A 268 30715 15015 26207 -3926 -1033 4780 A C ATOM 2062 O VAL A 268 41.180 -37.488 16.107 1.00182.35 A O ANISOU 2062 O VAL A 268 29657 14579 25049 -3822 -1109 4753 A O ATOM 2063 CB VAL A 268 42.647 -39.404 14.304 1.00197.27 A C ANISOU 2063 CB VAL A 268 31675 15825 27453 -3402 -1431 4456 A C ATOM 2064 CG1 VAL A 268 43.384 -40.156 15.403 1.00200.14 A C ANISOU 2064 CG1 VAL A 268 32423 15907 27716 -3217 -1449 4861 A C ATOM 2065 CG2 VAL A 268 42.904 -40.053 12.953 1.00195.78 A C ANISOU 2065 CG2 VAL A 268 31387 15431 27569 -3302 -1553 4126 A C ATOM 2066 N LYS A 269 40.349 -39.433 16.900 1.00183.55 A N ANISOU 2066 N LYS A 269 30263 13966 25510 -4108 -839 5085 A N ATOM 2067 CA LYS A 269 39.882 -38.890 18.178 1.00175.44 A C ANISOU 2067 CA LYS A 269 29332 13124 24202 -4241 -676 5387 A C ATOM 2068 C LYS A 269 40.988 -38.402 19.121 1.00173.80 A C ANISOU 2068 C LYS A 269 29273 13130 23634 -3920 -819 5662 A C ATOM 2069 O LYS A 269 40.836 -37.363 19.770 1.00169.49 A O ANISOU 2069 O LYS A 269 28638 12969 22791 -3948 -784 5740 A O ATOM 2070 CB LYS A 269 39.043 -39.935 18.922 1.00175.47 A C ANISOU 2070 CB LYS A 269 29611 12701 24359 -4512 -420 5655 A C ATOM 2071 CG LYS A 269 37.920 -40.572 18.123 1.00166.50 A C ANISOU 2071 CG LYS A 269 28363 11299 23599 -4859 -259 5415 A C ATOM 2072 CD LYS A 269 37.246 -41.643 18.953 1.00159.83 A C ANISOU 2072 CD LYS A 269 27824 10005 22900 -5101 -9 5723 A C ATOM 2073 CE LYS A 269 36.145 -42.354 18.187 1.00157.75 A C ANISOU 2073 CE LYS A 269 27457 9446 23034 -5465 153 5482 A C ATOM 2074 NZ LYS A 269 35.672 -43.571 18.930 1.00162.83 A N1+ ANISOU 2074 NZ LYS A 269 28438 9565 23867 -5667 382 5791 A N1+ ATOM 2075 N GLY A 270 42.082 -39.161 19.212 1.00175.47 A N ANISOU 2075 N GLY A 270 29709 13091 23868 -3616 -979 5803 A N ATOM 2076 CA GLY A 270 43.120 -38.904 20.202 1.00178.05 A C ANISOU 2076 CA GLY A 270 30215 13569 23866 -3313 -1106 6098 A C ATOM 2077 C GLY A 270 44.379 -38.232 19.681 1.00180.22 A C ANISOU 2077 C GLY A 270 30322 14152 24003 -2958 -1399 5933 A C ATOM 2078 O GLY A 270 45.272 -38.899 19.154 1.00177.63 A O ANISOU 2078 O GLY A 270 30067 13618 23808 -2699 -1569 5888 A O ATOM 2079 N GLN A 271 44.453 -36.910 19.853 1.00181.58 A N ANISOU 2079 N GLN A 271 30271 14812 23907 -2946 -1451 5849 A N ATOM 2080 CA GLN A 271 45.544 -36.090 19.317 1.00180.41 A C ANISOU 2080 CA GLN A 271 29912 15007 23630 -2656 -1706 5663 A C ATOM 2081 C GLN A 271 45.682 -34.749 20.058 1.00176.61 A C ANISOU 2081 C GLN A 271 29313 15011 22782 -2639 -1729 5718 A C ATOM 2082 O GLN A 271 44.728 -33.971 20.126 1.00173.38 A O ANISOU 2082 O GLN A 271 28747 14817 22311 -2896 -1574 5628 A O ATOM 2083 CB GLN A 271 45.317 -35.822 17.825 1.00178.51 A C ANISOU 2083 CB GLN A 271 29356 14835 23634 -2711 -1759 5245 A C ATOM 2084 CG GLN A 271 45.611 -36.999 16.907 1.00180.81 A C ANISOU 2084 CG GLN A 271 29720 14723 24258 -2610 -1832 5122 A C ATOM 2085 CD GLN A 271 47.098 -37.229 16.713 1.00181.60 A C ANISOU 2085 CD GLN A 271 29874 14822 24302 -2196 -2093 5151 A C ATOM 2086 NE2 GLN A 271 47.440 -38.238 15.920 1.00183.73 A N ANISOU 2086 NE2 GLN A 271 30215 14751 24846 -2072 -2169 5042 A N ATOM 2087 OE1 GLN A 271 47.930 -36.507 17.266 1.00178.84 A O ANISOU 2087 OE1 GLN A 271 29498 14784 23669 -1989 -2227 5259 A O ATOM 2088 N LYS A 272 46.870 -34.477 20.598 1.00173.07 A N ANISOU 2088 N LYS A 272 28932 14736 22090 -2332 -1925 5855 A N ATOM 2089 CA LYS A 272 47.121 -33.226 21.322 1.00165.44 A C ANISOU 2089 CA LYS A 272 27865 14222 20775 -2295 -1970 5897 A C ATOM 2090 C LYS A 272 48.119 -32.329 20.579 1.00164.75 A C ANISOU 2090 C LYS A 272 27501 14469 20628 -2070 -2204 5643 A C ATOM 2091 O LYS A 272 49.058 -32.825 19.956 1.00166.94 A O ANISOU 2091 O LYS A 272 27768 14635 21026 -1818 -2388 5574 A O ATOM 2092 CB LYS A 272 47.579 -33.514 22.759 1.00161.23 A C ANISOU 2092 CB LYS A 272 27631 13672 19956 -2160 -1982 6282 A C ATOM 2093 CG LYS A 272 46.435 -33.914 23.695 1.00157.17 A C ANISOU 2093 CG LYS A 272 27335 12984 19398 -2431 -1709 6537 A C ATOM 2094 CD LYS A 272 46.852 -34.939 24.745 1.00148.31 A C ANISOU 2094 CD LYS A 272 26589 11590 18172 -2273 -1699 6935 A C ATOM 2095 CE LYS A 272 45.669 -35.308 25.629 1.00151.01 A C ANISOU 2095 CE LYS A 272 27133 11765 18481 -2558 -1406 7187 A C ATOM 2096 NZ LYS A 272 45.888 -36.578 26.405 1.00161.68 A N1+ ANISOU 2096 NZ LYS A 272 28866 12723 19840 -2443 -1347 7565 A N1+ ATOM 2097 N ARG A 273 47.906 -31.014 20.658 1.00162.24 A N ANISOU 2097 N ARG A 273 26965 14552 20127 -2161 -2186 5511 A N ATOM 2098 CA ARG A 273 48.601 -30.029 19.812 1.00164.23 A C ANISOU 2098 CA ARG A 273 26911 15126 20362 -2020 -2353 5230 A C ATOM 2099 C ARG A 273 50.132 -30.084 19.812 1.00167.05 A C ANISOU 2099 C ARG A 273 27272 15572 20625 -1659 -2625 5263 A C ATOM 2100 O ARG A 273 50.777 -29.636 20.762 1.00167.45 A O ANISOU 2100 O ARG A 273 27395 15835 20393 -1532 -2719 5422 A O ATOM 2101 CB ARG A 273 48.152 -28.605 20.158 1.00161.15 A C ANISOU 2101 CB ARG A 273 26341 15138 19750 -2170 -2274 5141 A C ATOM 2102 CG ARG A 273 48.840 -27.541 19.323 1.00156.08 A C ANISOU 2102 CG ARG A 273 25391 14821 19093 -2039 -2424 4867 A C ATOM 2103 CD ARG A 273 48.249 -26.173 19.569 1.00155.46 A C ANISOU 2103 CD ARG A 273 25140 15091 18836 -2212 -2313 4763 A C ATOM 2104 NE ARG A 273 48.601 -25.246 18.499 1.00154.38 A N ANISOU 2104 NE ARG A 273 24689 15198 18770 -2145 -2393 4467 A N ATOM 2105 CZ ARG A 273 47.867 -25.044 17.408 1.00155.29 A C ANISOU 2105 CZ ARG A 273 24600 15313 19092 -2273 -2291 4230 A C ATOM 2106 NH1 ARG A 273 46.727 -25.696 17.233 1.00155.48 A N1+ ANISOU 2106 NH1 ARG A 273 24685 15112 19277 -2490 -2111 4235 A N1+ ATOM 2107 NH2 ARG A 273 48.271 -24.182 16.487 1.00156.86 A N ANISOU 2107 NH2 ARG A 273 24523 15744 19331 -2183 -2367 3987 A N ATOM 2108 N LYS A 274 50.702 -30.586 18.718 1.00166.02 A N ANISOU 2108 N LYS A 274 27046 15306 20729 -1493 -2753 5094 A N ATOM 2109 CA LYS A 274 52.146 -30.795 18.609 1.00162.70 A C ANISOU 2109 CA LYS A 274 26626 14935 20259 -1138 -3007 5121 A C ATOM 2110 C LYS A 274 52.783 -29.956 17.499 1.00156.15 A C ANISOU 2110 C LYS A 274 25457 14381 19490 -1015 -3147 4815 A C ATOM 2111 O LYS A 274 53.499 -30.485 16.648 1.00156.46 A O ANISOU 2111 O LYS A 274 25438 14310 19701 -803 -3285 4707 A O ATOM 2112 CB LYS A 274 52.445 -32.285 18.389 1.00163.21 A C ANISOU 2112 CB LYS A 274 26918 14564 20531 -987 -3050 5238 A C ATOM 2113 CG LYS A 274 51.999 -33.179 19.548 1.00164.34 A C ANISOU 2113 CG LYS A 274 27423 14418 20602 -1060 -2923 5584 A C ATOM 2114 CD LYS A 274 52.510 -34.608 19.425 1.00163.63 A C ANISOU 2114 CD LYS A 274 27578 13908 20688 -854 -2989 5727 A C ATOM 2115 CE LYS A 274 52.425 -35.338 20.763 1.00161.54 A C ANISOU 2115 CE LYS A 274 27677 13437 20265 -832 -2909 6123 A C ATOM 2116 NZ LYS A 274 52.803 -36.773 20.649 1.00161.22 A N1+ ANISOU 2116 NZ LYS A 274 27900 12941 20417 -649 -2939 6275 A N1+ ATOM 2117 N VAL A 275 52.538 -28.649 17.527 1.00149.55 A N ANISOU 2117 N VAL A 275 24408 13902 18513 -1139 -3105 4684 A N ATOM 2118 CA VAL A 275 52.945 -27.761 16.437 1.00147.08 A C ANISOU 2118 CA VAL A 275 23764 13848 18271 -1069 -3188 4391 A C ATOM 2119 C VAL A 275 54.275 -27.044 16.673 1.00141.78 A C ANISOU 2119 C VAL A 275 22975 13486 17410 -826 -3401 4388 A C ATOM 2120 O VAL A 275 55.189 -27.136 15.850 1.00134.62 A O ANISOU 2120 O VAL A 275 21922 12619 16609 -601 -3561 4260 A O ATOM 2121 CB VAL A 275 51.858 -26.719 16.154 1.00147.71 A C ANISOU 2121 CB VAL A 275 23654 14126 18342 -1347 -3002 4218 A C ATOM 2122 CG1 VAL A 275 51.263 -26.235 17.463 1.00153.54 A C ANISOU 2122 CG1 VAL A 275 24537 14973 18829 -1530 -2876 4409 A C ATOM 2123 CG2 VAL A 275 52.424 -25.564 15.338 1.00137.41 A C ANISOU 2123 CG2 VAL A 275 22028 13157 17025 -1254 -3090 3973 A C ATOM 2124 N LYS A 276 54.376 -26.311 17.780 1.00144.12 A N ANISOU 2124 N LYS A 276 23322 14011 17427 -875 -3401 4517 A N ATOM 2125 CA LYS A 276 55.646 -25.701 18.153 1.00147.01 A C ANISOU 2125 CA LYS A 276 23596 14663 17600 -656 -3609 4530 A C ATOM 2126 C LYS A 276 56.732 -26.779 18.179 1.00154.88 A C ANISOU 2126 C LYS A 276 24722 15489 18635 -348 -3805 4663 A C ATOM 2127 O LYS A 276 57.792 -26.618 17.570 1.00155.48 A O ANISOU 2127 O LYS A 276 24622 15699 18754 -122 -3985 4548 A O ATOM 2128 CB LYS A 276 55.556 -24.999 19.516 1.00143.66 A C ANISOU 2128 CB LYS A 276 23273 14456 16855 -748 -3583 4685 A C ATOM 2129 CG LYS A 276 54.788 -23.683 19.506 1.00138.60 A C ANISOU 2129 CG LYS A 276 22460 14067 16134 -994 -3433 4527 A C ATOM 2130 CD LYS A 276 55.285 -22.723 20.591 1.00140.87 A C ANISOU 2130 CD LYS A 276 22745 14674 16104 -981 -3507 4588 A C ATOM 2131 CE LYS A 276 54.765 -21.288 20.354 1.00140.29 A C ANISOU 2131 CE LYS A 276 22451 14871 15983 -1176 -3389 4377 A C ATOM 2132 NZ LYS A 276 55.622 -20.180 20.928 1.00131.70 A N1+ ANISOU 2132 NZ LYS A 276 21247 14129 14665 -1110 -3521 4321 A N1+ ATOM 2133 N ASP A 277 56.443 -27.884 18.865 1.00155.67 A N ANISOU 2133 N ASP A 277 25130 15290 18727 -337 -3759 4911 A N ATOM 2134 CA ASP A 277 57.395 -28.982 19.044 1.00157.91 A C ANISOU 2134 CA ASP A 277 25588 15384 19028 -38 -3926 5081 A C ATOM 2135 C ASP A 277 57.933 -29.606 17.753 1.00153.50 A C ANISOU 2135 C ASP A 277 24914 14665 18746 152 -4026 4914 A C ATOM 2136 O ASP A 277 59.144 -29.694 17.561 1.00152.81 A O ANISOU 2136 O ASP A 277 24746 14687 18626 443 -4235 4903 A O ATOM 2137 CB ASP A 277 56.788 -30.072 19.925 1.00166.84 A C ANISOU 2137 CB ASP A 277 27082 16174 20135 -96 -3808 5375 A C ATOM 2138 CG ASP A 277 57.168 -29.919 21.384 1.00174.31 A C ANISOU 2138 CG ASP A 277 28209 17279 20741 -19 -3864 5644 A C ATOM 2139 OD1 ASP A 277 58.228 -29.316 21.665 1.00175.05 A O ANISOU 2139 OD1 ASP A 277 28179 17688 20645 176 -4061 5623 A O ATOM 2140 OD2 ASP A 277 56.409 -30.410 22.248 1.00176.99 A O1- ANISOU 2140 OD2 ASP A 277 28811 17434 21002 -153 -3710 5875 A O1- ATOM 2141 N ARG A 278 57.040 -30.048 16.877 1.00151.29 A N ANISOU 2141 N ARG A 278 24621 14133 18730 -5 -3881 4778 A N ATOM 2142 CA ARG A 278 57.459 -30.689 15.632 1.00153.12 A C ANISOU 2142 CA ARG A 278 24757 14197 19227 168 -3964 4606 A C ATOM 2143 C ARG A 278 58.199 -29.718 14.698 1.00145.30 A C ANISOU 2143 C ARG A 278 23410 13546 18252 289 -4088 4347 A C ATOM 2144 O ARG A 278 58.719 -30.122 13.654 1.00144.36 A O ANISOU 2144 O ARG A 278 23177 13355 18319 474 -4180 4195 A O ATOM 2145 CB ARG A 278 56.248 -31.305 14.922 1.00159.53 A C ANISOU 2145 CB ARG A 278 25618 14688 20307 -58 -3774 4495 A C ATOM 2146 CG ARG A 278 56.581 -32.314 13.821 1.00164.82 A C ANISOU 2146 CG ARG A 278 26290 15078 21256 122 -3846 4366 A C ATOM 2147 CD ARG A 278 55.311 -32.805 13.125 1.00166.97 A C ANISOU 2147 CD ARG A 278 26583 15072 21787 -137 -3655 4220 A C ATOM 2148 NE ARG A 278 55.580 -33.722 12.017 1.00168.43 A N ANISOU 2148 NE ARG A 278 26757 14999 22241 23 -3722 4059 A N ATOM 2149 CZ ARG A 278 55.737 -33.350 10.746 1.00167.08 A C ANISOU 2149 CZ ARG A 278 26308 14969 22204 91 -3773 3761 A C ATOM 2150 NH1 ARG A 278 55.668 -32.065 10.397 1.00156.56 A N1+ ANISOU 2150 NH1 ARG A 278 24684 14029 20772 16 -3760 3598 A N1+ ATOM 2151 NH2 ARG A 278 55.974 -34.270 9.820 1.00169.25 A N ANISOU 2151 NH2 ARG A 278 26604 14990 22713 247 -3833 3627 A N ATOM 2152 N LEU A 279 58.254 -28.445 15.082 1.00136.19 A N ANISOU 2152 N LEU A 279 22086 12756 16903 188 -4083 4298 A N ATOM 2153 CA LEU A 279 58.870 -27.427 14.240 1.00132.13 A C ANISOU 2153 CA LEU A 279 21233 12564 16404 267 -4168 4061 A C ATOM 2154 C LEU A 279 60.115 -26.764 14.839 1.00140.36 A C ANISOU 2154 C LEU A 279 22177 13930 17223 457 -4360 4121 A C ATOM 2155 O LEU A 279 60.935 -26.198 14.111 1.00133.12 A O ANISOU 2155 O LEU A 279 20998 13236 16344 602 -4473 3956 A O ATOM 2156 CB LEU A 279 57.842 -26.366 13.858 1.00129.33 A C ANISOU 2156 CB LEU A 279 20698 12371 16069 -23 -3983 3880 A C ATOM 2157 CG LEU A 279 56.910 -26.742 12.702 1.00126.39 A C ANISOU 2157 CG LEU A 279 20256 11802 15963 -144 -3844 3691 A C ATOM 2158 CD1 LEU A 279 56.103 -25.535 12.266 1.00119.66 A C ANISOU 2158 CD1 LEU A 279 19178 11186 15103 -371 -3690 3502 A C ATOM 2159 CD2 LEU A 279 57.703 -27.298 11.523 1.00122.97 A C ANISOU 2159 CD2 LEU A 279 19698 11298 15728 118 -3980 3544 A C ATOM 2160 N LYS A 280 60.257 -26.835 16.159 1.00156.34 A N ANISOU 2160 N LYS A 280 24402 15989 19012 456 -4395 4353 A N ATOM 2161 CA LYS A 280 61.422 -26.264 16.841 1.00164.38 A C ANISOU 2161 CA LYS A 280 25339 17319 19798 631 -4587 4414 A C ATOM 2162 C LYS A 280 62.738 -26.620 16.143 1.00161.89 A C ANISOU 2162 C LYS A 280 24878 17062 19571 964 -4802 4350 A C ATOM 2163 O LYS A 280 63.599 -25.759 15.946 1.00159.13 A O ANISOU 2163 O LYS A 280 24275 17034 19152 1054 -4924 4229 A O ATOM 2164 CB LYS A 280 61.473 -26.724 18.302 1.00172.66 A C ANISOU 2164 CB LYS A 280 26682 18320 20602 662 -4619 4709 A C ATOM 2165 CG LYS A 280 60.344 -26.198 19.187 1.00175.83 A C ANISOU 2165 CG LYS A 280 27209 18750 20849 357 -4428 4788 A C ATOM 2166 CD LYS A 280 60.441 -26.781 20.599 1.00180.58 A C ANISOU 2166 CD LYS A 280 28117 19290 21206 425 -4462 5098 A C ATOM 2167 CE LYS A 280 59.240 -26.405 21.455 1.00178.96 A C ANISOU 2167 CE LYS A 280 28061 19077 20860 127 -4251 5195 A C ATOM 2168 NZ LYS A 280 59.295 -27.038 22.802 1.00179.93 A N1+ ANISOU 2168 NZ LYS A 280 28494 19127 20744 205 -4269 5513 A N1+ ATOM 2169 N ALA A 281 62.883 -27.891 15.775 1.00158.32 A N ANISOU 2169 N ALA A 281 24585 16292 19275 1143 -4840 4429 A N ATOM 2170 CA ALA A 281 64.086 -28.385 15.103 1.00152.88 A C ANISOU 2170 CA ALA A 281 23787 15622 18680 1481 -5036 4381 A C ATOM 2171 C ALA A 281 64.471 -27.609 13.829 1.00146.66 A C ANISOU 2171 C ALA A 281 22637 15051 18037 1515 -5063 4094 A C ATOM 2172 O ALA A 281 65.651 -27.538 13.472 1.00144.12 A O ANISOU 2172 O ALA A 281 22142 14908 17710 1774 -5242 4045 A O ATOM 2173 CB ALA A 281 63.944 -29.878 14.794 1.00149.52 A C ANISOU 2173 CB ALA A 281 23607 14767 18437 1628 -5027 4483 A C ATOM 2174 N TYR A 282 63.486 -27.039 13.139 1.00136.49 A N ANISOU 2174 N TYR A 282 21231 13754 16874 1263 -4883 3913 A N ATOM 2175 CA TYR A 282 63.763 -26.336 11.895 1.00133.19 A C ANISOU 2175 CA TYR A 282 20485 13525 16596 1298 -4885 3654 A C ATOM 2176 C TYR A 282 63.897 -24.834 12.134 1.00137.94 A C ANISOU 2176 C TYR A 282 20854 14507 17050 1151 -4864 3560 A C ATOM 2177 O TYR A 282 64.905 -24.220 11.763 1.00131.70 A O ANISOU 2177 O TYR A 282 19815 13984 16240 1300 -4987 3464 A O ATOM 2178 CB TYR A 282 62.674 -26.614 10.862 1.00132.48 A C ANISOU 2178 CB TYR A 282 20379 13218 16739 1148 -4710 3491 A C ATOM 2179 CG TYR A 282 62.584 -28.053 10.387 1.00140.31 A C ANISOU 2179 CG TYR A 282 21559 13831 17922 1295 -4731 3523 A C ATOM 2180 CD1 TYR A 282 61.718 -28.956 11.000 1.00145.07 A C ANISOU 2180 CD1 TYR A 282 22475 14092 18553 1161 -4627 3679 A C ATOM 2181 CD2 TYR A 282 63.343 -28.502 9.308 1.00142.73 A C ANISOU 2181 CD2 TYR A 282 21729 14115 18387 1563 -4842 3391 A C ATOM 2182 CE1 TYR A 282 61.621 -30.270 10.562 1.00151.94 A C ANISOU 2182 CE1 TYR A 282 23525 14590 19614 1282 -4636 3699 A C ATOM 2183 CE2 TYR A 282 63.252 -29.816 8.859 1.00149.28 A C ANISOU 2183 CE2 TYR A 282 22738 14584 19397 1699 -4858 3403 A C ATOM 2184 CZ TYR A 282 62.390 -30.697 9.491 1.00154.96 A C ANISOU 2184 CZ TYR A 282 23776 14950 20152 1553 -4755 3554 A C ATOM 2185 OH TYR A 282 62.295 -32.006 9.057 1.00157.34 A O ANISOU 2185 OH TYR A 282 24266 14869 20647 1677 -4763 3561 A O ATOM 2186 N VAL A 283 62.874 -24.246 12.751 1.00145.80 A N ANISOU 2186 N VAL A 283 21930 15520 17949 857 -4701 3586 A N ATOM 2187 CA VAL A 283 62.890 -22.827 13.106 1.00144.82 A C ANISOU 2187 CA VAL A 283 21626 15723 17674 696 -4662 3507 A C ATOM 2188 C VAL A 283 63.287 -22.628 14.568 1.00147.19 A C ANISOU 2188 C VAL A 283 22071 16153 17700 688 -4756 3693 A C ATOM 2189 O VAL A 283 62.621 -23.117 15.484 1.00144.99 A O ANISOU 2189 O VAL A 283 22062 15711 17316 582 -4688 3870 A O ATOM 2190 CB VAL A 283 61.527 -22.139 12.837 1.00146.83 A C ANISOU 2190 CB VAL A 283 21848 15961 17978 385 -4419 3394 A C ATOM 2191 CG1 VAL A 283 60.375 -23.058 13.194 1.00148.30 A C ANISOU 2191 CG1 VAL A 283 22316 15824 18209 238 -4282 3515 A C ATOM 2192 CG2 VAL A 283 61.426 -20.833 13.610 1.00146.75 A C ANISOU 2192 CG2 VAL A 283 21762 16232 17766 204 -4370 3379 A C ATOM 2193 N ARG A 284 64.379 -21.906 14.781 1.00151.98 A N ANISOU 2193 N ARG A 284 22490 17064 18190 802 -4910 3651 A N ATOM 2194 CA ARG A 284 64.893 -21.698 16.126 1.00159.60 A C ANISOU 2194 CA ARG A 284 23562 18195 18885 825 -5029 3803 A C ATOM 2195 C ARG A 284 64.186 -20.544 16.834 1.00156.76 A C ANISOU 2195 C ARG A 284 23195 18006 18362 537 -4897 3763 A C ATOM 2196 O ARG A 284 63.703 -20.706 17.958 1.00159.11 A O ANISOU 2196 O ARG A 284 23726 18260 18470 439 -4860 3926 A O ATOM 2197 CB ARG A 284 66.401 -21.459 16.085 1.00166.45 A C ANISOU 2197 CB ARG A 284 24223 19327 19695 1072 -5265 3765 A C ATOM 2198 CG ARG A 284 67.171 -22.574 15.401 1.00173.32 A C ANISOU 2198 CG ARG A 284 25092 20051 20713 1384 -5403 3804 A C ATOM 2199 CD ARG A 284 68.647 -22.238 15.283 1.00180.70 A C ANISOU 2199 CD ARG A 284 25777 21281 21597 1618 -5624 3747 A C ATOM 2200 NE ARG A 284 69.414 -23.355 14.737 1.00188.89 A N ANISOU 2200 NE ARG A 284 26833 22185 22750 1943 -5763 3804 A N ATOM 2201 CZ ARG A 284 70.742 -23.398 14.691 1.00195.50 A C ANISOU 2201 CZ ARG A 284 27500 23237 23544 2207 -5975 3801 A C ATOM 2202 NH1 ARG A 284 71.456 -22.383 15.161 1.00197.91 A N1+ ANISOU 2202 NH1 ARG A 284 27596 23901 23700 2169 -6075 3737 A N1+ ATOM 2203 NH2 ARG A 284 71.358 -24.456 14.179 1.00196.63 A N ANISOU 2203 NH2 ARG A 284 27678 23237 23795 2508 -6086 3856 A N ATOM 2204 N ASP A 285 64.121 -19.389 16.173 1.00146.48 A N ANISOU 2204 N ASP A 285 21631 16893 17131 411 -4818 3551 A N ATOM 2205 CA ASP A 285 63.515 -18.191 16.763 1.00141.05 A C ANISOU 2205 CA ASP A 285 20915 16378 16301 151 -4691 3487 A C ATOM 2206 C ASP A 285 62.120 -18.442 17.364 1.00135.92 A C ANISOU 2206 C ASP A 285 20522 15535 15586 -71 -4494 3596 A C ATOM 2207 O ASP A 285 61.183 -18.818 16.651 1.00128.51 A O ANISOU 2207 O ASP A 285 19619 14385 14822 -163 -4333 3560 A O ATOM 2208 CB ASP A 285 63.460 -17.058 15.734 1.00138.81 A C ANISOU 2208 CB ASP A 285 20333 16248 16162 53 -4589 3248 A C ATOM 2209 CG ASP A 285 62.847 -15.788 16.295 1.00134.74 A C ANISOU 2209 CG ASP A 285 19787 15897 15510 -205 -4449 3172 A C ATOM 2210 OD1 ASP A 285 63.563 -15.028 16.984 1.00135.47 A O ANISOU 2210 OD1 ASP A 285 19801 16229 15441 -212 -4555 3144 A O ATOM 2211 OD2 ASP A 285 61.646 -15.551 16.043 1.00128.11 A O1- ANISOU 2211 OD2 ASP A 285 18999 14950 14728 -397 -4234 3133 A O1- ATOM 2212 N PRO A 286 61.981 -18.216 18.683 1.00135.17 A N ANISOU 2212 N PRO A 286 20596 15529 15232 -157 -4507 3725 A N ATOM 2213 CA PRO A 286 60.753 -18.520 19.424 1.00130.96 A C ANISOU 2213 CA PRO A 286 20324 14830 14603 -346 -4333 3865 A C ATOM 2214 C PRO A 286 59.615 -17.616 19.011 1.00126.88 A C ANISOU 2214 C PRO A 286 19719 14336 14152 -612 -4094 3717 A C ATOM 2215 O PRO A 286 58.465 -17.959 19.260 1.00129.03 A O ANISOU 2215 O PRO A 286 20166 14435 14425 -773 -3918 3800 A O ATOM 2216 CB PRO A 286 61.139 -18.216 20.868 1.00132.77 A C ANISOU 2216 CB PRO A 286 20685 15248 14515 -342 -4433 3993 A C ATOM 2217 CG PRO A 286 62.156 -17.150 20.740 1.00135.74 A C ANISOU 2217 CG PRO A 286 20794 15938 14843 -292 -4570 3817 A C ATOM 2218 CD PRO A 286 62.973 -17.548 19.542 1.00137.06 A C ANISOU 2218 CD PRO A 286 20765 16064 15248 -91 -4680 3724 A C ATOM 2219 N TYR A 287 59.935 -16.473 18.410 1.00125.88 A N ANISOU 2219 N TYR A 287 19327 14423 14079 -653 -4083 3507 A N ATOM 2220 CA TYR A 287 58.918 -15.546 17.922 1.00122.06 A C ANISOU 2220 CA TYR A 287 18738 13975 13664 -876 -3857 3357 A C ATOM 2221 C TYR A 287 58.292 -16.079 16.628 1.00119.76 A C ANISOU 2221 C TYR A 287 18376 13484 13645 -873 -3741 3278 A C ATOM 2222 O TYR A 287 57.066 -16.085 16.475 1.00122.78 A O ANISOU 2222 O TYR A 287 18823 13752 14076 -1051 -3540 3268 A O ATOM 2223 CB TYR A 287 59.504 -14.143 17.694 1.00123.66 A C ANISOU 2223 CB TYR A 287 18687 14457 13841 -910 -3876 3167 A C ATOM 2224 CG TYR A 287 59.802 -13.331 18.952 1.00130.66 A C ANISOU 2224 CG TYR A 287 19629 15558 14456 -991 -3930 3188 A C ATOM 2225 CD1 TYR A 287 58.778 -12.901 19.794 1.00128.58 A C ANISOU 2225 CD1 TYR A 287 19525 15302 14026 -1197 -3768 3234 A C ATOM 2226 CD2 TYR A 287 61.108 -12.962 19.273 1.00137.05 A C ANISOU 2226 CD2 TYR A 287 20317 16579 15178 -863 -4142 3147 A C ATOM 2227 CE1 TYR A 287 59.052 -12.149 20.937 1.00131.12 A C ANISOU 2227 CE1 TYR A 287 19900 15828 14092 -1265 -3821 3237 A C ATOM 2228 CE2 TYR A 287 61.392 -12.208 20.411 1.00138.11 A C ANISOU 2228 CE2 TYR A 287 20492 16921 15063 -941 -4202 3141 A C ATOM 2229 CZ TYR A 287 60.362 -11.803 21.240 1.00134.74 A C ANISOU 2229 CZ TYR A 287 20238 16490 14466 -1138 -4042 3183 A C ATOM 2230 OH TYR A 287 60.648 -11.056 22.370 1.00131.79 A O ANISOU 2230 OH TYR A 287 19909 16329 13837 -1207 -4105 3163 A O ATOM 2231 N ALA A 288 59.138 -16.526 15.702 1.00111.80 A N ANISOU 2231 N ALA A 288 17225 12447 12807 -666 -3872 3215 A N ATOM 2232 CA ALA A 288 58.665 -17.164 14.473 1.00101.87 A C ANISOU 2232 CA ALA A 288 15907 10999 11800 -627 -3795 3136 A C ATOM 2233 C ALA A 288 57.760 -18.357 14.784 1.00114.09 A C ANISOU 2233 C ALA A 288 17719 12246 13383 -692 -3717 3285 A C ATOM 2234 O ALA A 288 56.689 -18.511 14.196 1.00116.63 A O ANISOU 2234 O ALA A 288 18040 12437 13836 -827 -3545 3219 A O ATOM 2235 CB ALA A 288 59.838 -17.599 13.615 1.00 87.10 A C ANISOU 2235 CB ALA A 288 13881 9143 10072 -361 -3974 3076 A C ATOM 2236 N LEU A 289 58.200 -19.202 15.709 1.00118.01 A N ANISOU 2236 N LEU A 289 18437 12639 13762 -592 -3842 3487 A N ATOM 2237 CA LEU A 289 57.389 -20.322 16.158 1.00120.18 A C ANISOU 2237 CA LEU A 289 18986 12619 14055 -661 -3761 3659 A C ATOM 2238 C LEU A 289 56.002 -19.853 16.595 1.00120.40 A C ANISOU 2238 C LEU A 289 19095 12635 14016 -953 -3525 3669 A C ATOM 2239 O LEU A 289 54.996 -20.383 16.131 1.00124.04 A O ANISOU 2239 O LEU A 289 19612 12891 14628 -1076 -3374 3652 A O ATOM 2240 CB LEU A 289 58.089 -21.063 17.303 1.00125.03 A C ANISOU 2240 CB LEU A 289 19834 13180 14493 -516 -3918 3899 A C ATOM 2241 CG LEU A 289 59.259 -21.973 16.909 1.00127.27 A C ANISOU 2241 CG LEU A 289 20114 13374 14869 -211 -4133 3943 A C ATOM 2242 CD1 LEU A 289 60.288 -22.137 18.045 1.00124.47 A C ANISOU 2242 CD1 LEU A 289 19876 13143 14274 -35 -4329 4124 A C ATOM 2243 CD2 LEU A 289 58.738 -23.324 16.434 1.00129.25 A C ANISOU 2243 CD2 LEU A 289 20537 13249 15323 -177 -4076 4015 A C ATOM 2244 N ASP A 290 55.953 -18.853 17.475 1.00117.74 A N ANISOU 2244 N ASP A 290 18757 12524 13453 -1064 -3494 3686 A N ATOM 2245 CA ASP A 290 54.684 -18.366 18.021 1.00119.78 A C ANISOU 2245 CA ASP A 290 19103 12795 13613 -1326 -3273 3710 A C ATOM 2246 C ASP A 290 53.739 -17.867 16.938 1.00124.80 A C ANISOU 2246 C ASP A 290 19557 13430 14431 -1471 -3086 3514 A C ATOM 2247 O ASP A 290 52.528 -18.083 17.012 1.00126.34 A O ANISOU 2247 O ASP A 290 19840 13504 14657 -1659 -2897 3544 A O ATOM 2248 CB ASP A 290 54.908 -17.248 19.038 1.00119.77 A C ANISOU 2248 CB ASP A 290 19099 13066 13342 -1395 -3284 3719 A C ATOM 2249 CG ASP A 290 53.619 -16.822 19.732 1.00122.06 A C ANISOU 2249 CG ASP A 290 19508 13367 13503 -1646 -3060 3769 A C ATOM 2250 OD1 ASP A 290 52.889 -17.702 20.240 1.00128.61 A O ANISOU 2250 OD1 ASP A 290 20558 13994 14314 -1724 -2970 3944 A O ATOM 2251 OD2 ASP A 290 53.337 -15.609 19.776 1.00117.08 A O1- ANISOU 2251 OD2 ASP A 290 18752 12944 12790 -1763 -2966 3637 A O1- ATOM 2252 N LEU A 291 54.286 -17.181 15.939 1.00122.91 A N ANISOU 2252 N LEU A 291 19056 13340 14305 -1381 -3133 3316 A N ATOM 2253 CA LEU A 291 53.462 -16.689 14.841 1.00114.02 A C ANISOU 2253 CA LEU A 291 17743 12236 13343 -1483 -2965 3127 A C ATOM 2254 C LEU A 291 52.922 -17.855 14.010 1.00110.28 A C ANISOU 2254 C LEU A 291 17306 11499 13097 -1465 -2927 3113 A C ATOM 2255 O LEU A 291 51.714 -17.955 13.790 1.00114.79 A O ANISOU 2255 O LEU A 291 17896 11985 13735 -1643 -2743 3079 A O ATOM 2256 CB LEU A 291 54.237 -15.701 13.966 1.00102.00 A C ANISOU 2256 CB LEU A 291 15937 10933 11884 -1371 -3021 2937 A C ATOM 2257 CG LEU A 291 53.492 -15.149 12.751 1.00 90.29 A C ANISOU 2257 CG LEU A 291 14244 9499 10563 -1434 -2856 2743 A C ATOM 2258 CD1 LEU A 291 52.197 -14.483 13.172 1.00 87.26 A C ANISOU 2258 CD1 LEU A 291 13903 9166 10084 -1674 -2629 2735 A C ATOM 2259 CD2 LEU A 291 54.381 -14.179 11.991 1.00 87.66 A C ANISOU 2259 CD2 LEU A 291 13650 9381 10277 -1307 -2915 2589 A C ATOM 2260 N ILE A 292 53.817 -18.730 13.557 1.00 97.69 A N ANISOU 2260 N ILE A 292 15716 9781 11620 -1252 -3101 3130 A N ATOM 2261 CA ILE A 292 53.412 -19.921 12.826 1.00103.50 A C ANISOU 2261 CA ILE A 292 16511 10244 12573 -1220 -3085 3113 A C ATOM 2262 C ILE A 292 52.272 -20.612 13.556 1.00108.86 A C ANISOU 2262 C ILE A 292 17429 10705 13228 -1426 -2939 3260 A C ATOM 2263 O ILE A 292 51.343 -21.134 12.936 1.00112.48 A O ANISOU 2263 O ILE A 292 17883 10998 13855 -1537 -2817 3188 A O ATOM 2264 CB ILE A 292 54.568 -20.928 12.683 1.00109.91 A C ANISOU 2264 CB ILE A 292 17390 10913 13456 -958 -3303 3186 A C ATOM 2265 CG1 ILE A 292 55.675 -20.353 11.805 1.00115.46 A C ANISOU 2265 CG1 ILE A 292 17834 11819 14216 -747 -3439 3030 A C ATOM 2266 CG2 ILE A 292 54.077 -22.226 12.079 1.00104.37 A C ANISOU 2266 CG2 ILE A 292 16796 9889 12971 -945 -3276 3182 A C ATOM 2267 CD1 ILE A 292 56.457 -21.417 11.060 1.00117.18 A C ANISOU 2267 CD1 ILE A 292 18049 11869 14604 -498 -3594 3011 A C ATOM 2268 N ASP A 293 52.347 -20.605 14.881 1.00107.72 A N ANISOU 2268 N ASP A 293 17486 10573 12870 -1478 -2951 3464 A N ATOM 2269 CA ASP A 293 51.341 -21.255 15.706 1.00114.85 A C ANISOU 2269 CA ASP A 293 18632 11279 13726 -1666 -2809 3638 A C ATOM 2270 C ASP A 293 49.981 -20.559 15.641 1.00117.45 A C ANISOU 2270 C ASP A 293 18888 11694 14045 -1932 -2569 3551 A C ATOM 2271 O ASP A 293 48.948 -21.214 15.529 1.00125.17 A O ANISOU 2271 O ASP A 293 19947 12475 15136 -2092 -2423 3575 A O ATOM 2272 CB ASP A 293 51.817 -21.322 17.155 1.00122.30 A C ANISOU 2272 CB ASP A 293 19798 12258 14411 -1631 -2884 3879 A C ATOM 2273 CG ASP A 293 50.978 -22.253 17.998 1.00125.73 A C ANISOU 2273 CG ASP A 293 20516 12443 14814 -1772 -2761 4102 A C ATOM 2274 OD1 ASP A 293 50.819 -23.418 17.584 1.00125.77 A O ANISOU 2274 OD1 ASP A 293 20624 12150 15014 -1742 -2761 4147 A O ATOM 2275 OD2 ASP A 293 50.485 -21.823 19.066 1.00126.81 A O1- ANISOU 2275 OD2 ASP A 293 20772 12678 14733 -1910 -2660 4231 A O1- ATOM 2276 N LYS A 294 49.980 -19.235 15.719 1.00115.88 A N ANISOU 2276 N LYS A 294 18532 11784 13711 -1979 -2523 3449 A N ATOM 2277 CA LYS A 294 48.730 -18.487 15.752 1.00115.89 A C ANISOU 2277 CA LYS A 294 18469 11892 13671 -2211 -2295 3378 A C ATOM 2278 C LYS A 294 48.085 -18.428 14.374 1.00112.50 A C ANISOU 2278 C LYS A 294 17822 11451 13470 -2249 -2199 3159 A C ATOM 2279 O LYS A 294 46.917 -18.042 14.243 1.00110.37 A O ANISOU 2279 O LYS A 294 17493 11232 13209 -2437 -2001 3094 A O ATOM 2280 CB LYS A 294 48.957 -17.090 16.337 1.00116.64 A C ANISOU 2280 CB LYS A 294 18488 12286 13543 -2239 -2275 3344 A C ATOM 2281 CG LYS A 294 49.382 -17.150 17.798 1.00118.13 A C ANISOU 2281 CG LYS A 294 18903 12502 13478 -2232 -2346 3557 A C ATOM 2282 CD LYS A 294 49.593 -15.792 18.435 1.00115.87 A C ANISOU 2282 CD LYS A 294 18557 12502 12967 -2270 -2330 3509 A C ATOM 2283 CE LYS A 294 49.815 -15.964 19.936 1.00122.73 A C ANISOU 2283 CE LYS A 294 19670 13391 13569 -2282 -2380 3726 A C ATOM 2284 NZ LYS A 294 50.326 -14.737 20.611 1.00125.86 A N1+ ANISOU 2284 NZ LYS A 294 20017 14064 13738 -2276 -2426 3671 A N1+ ATOM 2285 N LEU A 295 48.849 -18.834 13.359 1.00107.09 A N ANISOU 2285 N LEU A 295 17018 10710 12961 -2058 -2340 3046 A N ATOM 2286 CA LEU A 295 48.350 -18.892 11.988 1.00 99.82 A C ANISOU 2286 CA LEU A 295 15893 9779 12257 -2055 -2276 2832 A C ATOM 2287 C LEU A 295 47.767 -20.266 11.676 1.00106.30 A C ANISOU 2287 C LEU A 295 16830 10289 13268 -2112 -2251 2854 A C ATOM 2288 O LEU A 295 46.787 -20.378 10.936 1.00109.69 A O ANISOU 2288 O LEU A 295 17153 10690 13836 -2232 -2120 2715 A O ATOM 2289 CB LEU A 295 49.444 -18.521 10.975 1.00 89.43 A C ANISOU 2289 CB LEU A 295 14363 8590 11025 -1815 -2425 2678 A C ATOM 2290 CG LEU A 295 49.760 -17.019 10.842 1.00 90.66 A C ANISOU 2290 CG LEU A 295 14322 9061 11065 -1789 -2393 2577 A C ATOM 2291 CD1 LEU A 295 51.154 -16.763 10.286 1.00 91.44 A C ANISOU 2291 CD1 LEU A 295 14276 9265 11199 -1542 -2578 2510 A C ATOM 2292 CD2 LEU A 295 48.727 -16.299 9.998 1.00 88.11 A C ANISOU 2292 CD2 LEU A 295 13804 8869 10806 -1896 -2203 2401 A C ATOM 2293 N LEU A 296 48.362 -21.309 12.250 1.00104.62 A N ANISOU 2293 N LEU A 296 16839 9846 13065 -2027 -2374 3027 A N ATOM 2294 CA LEU A 296 47.901 -22.677 12.009 1.00100.18 A C ANISOU 2294 CA LEU A 296 16417 8950 12697 -2075 -2355 3061 A C ATOM 2295 C LEU A 296 46.850 -23.087 13.017 1.00102.24 A C ANISOU 2295 C LEU A 296 16890 9064 12894 -2326 -2187 3240 A C ATOM 2296 O LEU A 296 46.725 -24.251 13.356 1.00110.26 A O ANISOU 2296 O LEU A 296 18117 9777 13999 -2356 -2190 3377 A O ATOM 2297 CB LEU A 296 49.066 -23.662 12.053 1.00102.07 A C ANISOU 2297 CB LEU A 296 16796 8989 12998 -1839 -2562 3162 A C ATOM 2298 CG LEU A 296 50.103 -23.502 10.944 1.00103.59 A C ANISOU 2298 CG LEU A 296 16784 9283 13293 -1577 -2730 2984 A C ATOM 2299 CD1 LEU A 296 51.247 -24.477 11.152 1.00102.49 A C ANISOU 2299 CD1 LEU A 296 16803 8953 13186 -1339 -2930 3112 A C ATOM 2300 CD2 LEU A 296 49.454 -23.709 9.583 1.00101.53 A C ANISOU 2300 CD2 LEU A 296 16338 8979 13260 -1609 -2661 2735 A C ATOM 2301 N VAL A 297 46.092 -22.118 13.499 1.00104.14 A N ANISOU 2301 N VAL A 297 17075 9514 12979 -2501 -2031 3243 A N ATOM 2302 CA VAL A 297 44.986 -22.400 14.400 1.00111.16 A C ANISOU 2302 CA VAL A 297 18133 10301 13801 -2752 -1844 3399 A C ATOM 2303 C VAL A 297 43.826 -23.116 13.675 1.00115.81 A C ANISOU 2303 C VAL A 297 18671 10705 14627 -2937 -1700 3285 A C ATOM 2304 O VAL A 297 43.493 -22.784 12.531 1.00110.13 A O ANISOU 2304 O VAL A 297 17711 10091 14044 -2934 -1674 3040 A O ATOM 2305 CB VAL A 297 44.519 -21.090 15.088 1.00101.23 A C ANISOU 2305 CB VAL A 297 16815 9344 12301 -2871 -1717 3417 A C ATOM 2306 CG1 VAL A 297 43.096 -21.200 15.606 1.00103.44 A C ANISOU 2306 CG1 VAL A 297 17166 9578 12558 -3153 -1478 3489 A C ATOM 2307 CG2 VAL A 297 45.483 -20.709 16.208 1.00101.90 A C ANISOU 2307 CG2 VAL A 297 17048 9533 12135 -2751 -1837 3597 A C ATOM 2308 N LEU A 298 43.222 -24.100 14.342 1.00121.64 A N ANISOU 2308 N LEU A 298 19632 11173 15413 -3095 -1605 3461 A N ATOM 2309 CA LEU A 298 42.127 -24.874 13.749 1.00124.13 A C ANISOU 2309 CA LEU A 298 19915 11286 15964 -3294 -1468 3362 A C ATOM 2310 C LEU A 298 40.846 -24.069 13.497 1.00124.08 A C ANISOU 2310 C LEU A 298 19708 11501 15935 -3519 -1261 3222 A C ATOM 2311 O LEU A 298 40.301 -24.085 12.393 1.00125.04 A O ANISOU 2311 O LEU A 298 19618 11655 16234 -3565 -1223 2982 A O ATOM 2312 CB LEU A 298 41.803 -26.088 14.618 1.00127.22 A C ANISOU 2312 CB LEU A 298 20605 11325 16407 -3422 -1399 3609 A C ATOM 2313 CG LEU A 298 42.777 -27.266 14.546 1.00130.24 A C ANISOU 2313 CG LEU A 298 21180 11385 16921 -3229 -1571 3705 A C ATOM 2314 CD1 LEU A 298 42.462 -28.288 15.631 1.00137.06 A C ANISOU 2314 CD1 LEU A 298 22366 11931 17779 -3351 -1476 4003 A C ATOM 2315 CD2 LEU A 298 42.764 -27.917 13.168 1.00124.93 A C ANISOU 2315 CD2 LEU A 298 20368 10553 16548 -3179 -1636 3448 A C ATOM 2316 N ASP A 299 40.362 -23.385 14.527 1.00120.23 A N ANISOU 2316 N ASP A 299 19288 11173 15223 -3649 -1128 3370 A N ATOM 2317 CA ASP A 299 39.134 -22.602 14.423 1.00117.21 A C ANISOU 2317 CA ASP A 299 18733 11010 14793 -3854 -920 3265 A C ATOM 2318 C ASP A 299 39.357 -21.249 13.702 1.00118.07 A C ANISOU 2318 C ASP A 299 18572 11472 14817 -3729 -950 3052 A C ATOM 2319 O ASP A 299 40.025 -20.352 14.218 1.00114.35 A O ANISOU 2319 O ASP A 299 18116 11194 14137 -3612 -1009 3112 A O ATOM 2320 CB ASP A 299 38.545 -22.395 15.823 1.00117.51 A C ANISOU 2320 CB ASP A 299 18954 11081 14612 -4025 -761 3512 A C ATOM 2321 CG ASP A 299 37.234 -21.639 15.801 1.00127.38 A C ANISOU 2321 CG ASP A 299 20040 12552 15806 -4239 -534 3423 A C ATOM 2322 OD1 ASP A 299 36.526 -21.707 14.771 1.00134.59 A O ANISOU 2322 OD1 ASP A 299 20741 13493 16906 -4320 -470 3205 A O ATOM 2323 OD2 ASP A 299 36.910 -20.978 16.816 1.00125.01 A O1- ANISOU 2323 OD2 ASP A 299 19822 12409 15268 -4315 -421 3567 A O1- ATOM 2324 N PRO A 300 38.786 -21.100 12.502 1.00117.72 A N ANISOU 2324 N PRO A 300 18278 11513 14935 -3754 -905 2801 A N ATOM 2325 CA PRO A 300 38.951 -19.883 11.695 1.00114.68 A C ANISOU 2325 CA PRO A 300 17633 11446 14494 -3624 -918 2598 A C ATOM 2326 C PRO A 300 38.858 -18.623 12.525 1.00115.74 A C ANISOU 2326 C PRO A 300 17771 11844 14362 -3648 -825 2683 A C ATOM 2327 O PRO A 300 39.795 -17.838 12.557 1.00121.30 A O ANISOU 2327 O PRO A 300 18443 12697 14949 -3471 -933 2673 A O ATOM 2328 CB PRO A 300 37.753 -19.925 10.750 1.00115.35 A C ANISOU 2328 CB PRO A 300 17498 11601 14731 -3763 -778 2387 A C ATOM 2329 CG PRO A 300 37.423 -21.363 10.627 1.00114.40 A C ANISOU 2329 CG PRO A 300 17489 11149 14829 -3881 -789 2406 A C ATOM 2330 CD PRO A 300 37.854 -22.060 11.888 1.00116.44 A C ANISOU 2330 CD PRO A 300 18068 11161 15013 -3923 -819 2697 A C ATOM 2331 N ALA A 301 37.730 -18.430 13.191 1.00121.08 A N ANISOU 2331 N ALA A 301 18483 12576 14945 -3868 -623 2760 A N ATOM 2332 CA ALA A 301 37.505 -17.206 13.948 1.00127.78 A C ANISOU 2332 CA ALA A 301 19328 13681 15540 -3900 -513 2819 A C ATOM 2333 C ALA A 301 38.422 -17.060 15.170 1.00129.99 A C ANISOU 2333 C ALA A 301 19845 13935 15611 -3824 -611 3036 A C ATOM 2334 O ALA A 301 38.327 -16.073 15.896 1.00130.45 A O ANISOU 2334 O ALA A 301 19927 14192 15446 -3844 -535 3088 A O ATOM 2335 CB ALA A 301 36.041 -17.091 14.353 1.00130.55 A C ANISOU 2335 CB ALA A 301 19656 14103 15844 -4148 -267 2849 A C ATOM 2336 N GLN A 302 39.301 -18.037 15.395 1.00129.11 A N ANISOU 2336 N GLN A 302 19906 13585 15565 -3730 -779 3154 A N ATOM 2337 CA GLN A 302 40.329 -17.931 16.440 1.00126.72 A C ANISOU 2337 CA GLN A 302 19805 13277 15067 -3615 -910 3341 A C ATOM 2338 C GLN A 302 41.722 -17.751 15.830 1.00122.13 A C ANISOU 2338 C GLN A 302 19145 12726 14531 -3357 -1143 3247 A C ATOM 2339 O GLN A 302 42.690 -17.444 16.525 1.00123.47 A O ANISOU 2339 O GLN A 302 19418 12956 14537 -3233 -1273 3349 A O ATOM 2340 CB GLN A 302 40.317 -19.153 17.367 1.00130.44 A C ANISOU 2340 CB GLN A 302 20560 13468 15532 -3686 -918 3594 A C ATOM 2341 CG GLN A 302 39.352 -19.064 18.560 1.00137.62 A C ANISOU 2341 CG GLN A 302 21624 14405 16259 -3895 -716 3782 A C ATOM 2342 CD GLN A 302 39.256 -20.374 19.358 1.00144.24 A C ANISOU 2342 CD GLN A 302 22739 14939 17126 -3971 -699 4039 A C ATOM 2343 NE2 GLN A 302 39.545 -20.301 20.656 1.00146.33 A N ANISOU 2343 NE2 GLN A 302 23226 15231 17140 -3954 -701 4273 A N ATOM 2344 OE1 GLN A 302 38.918 -21.431 18.812 1.00142.67 A O ANISOU 2344 OE1 GLN A 302 22556 14483 17170 -4042 -680 4025 A O ATOM 2345 N ARG A 303 41.810 -17.942 14.521 1.00115.03 A N ANISOU 2345 N ARG A 303 18053 11802 13851 -3275 -1195 3048 A N ATOM 2346 CA ARG A 303 43.068 -17.804 13.804 1.00108.45 A C ANISOU 2346 CA ARG A 303 17118 11004 13083 -3029 -1401 2947 A C ATOM 2347 C ARG A 303 43.437 -16.328 13.612 1.00104.01 A C ANISOU 2347 C ARG A 303 16379 10750 12390 -2945 -1395 2829 A C ATOM 2348 O ARG A 303 42.558 -15.482 13.404 1.00102.55 A O ANISOU 2348 O ARG A 303 16062 10742 12161 -3051 -1223 2730 A O ATOM 2349 CB ARG A 303 42.946 -18.492 12.451 1.00102.52 A C ANISOU 2349 CB ARG A 303 16217 10134 12602 -2972 -1439 2766 A C ATOM 2350 CG ARG A 303 44.241 -18.662 11.691 1.00107.62 A C ANISOU 2350 CG ARG A 303 16785 10762 13345 -2711 -1656 2682 A C ATOM 2351 CD ARG A 303 43.937 -19.382 10.406 1.00110.79 A C ANISOU 2351 CD ARG A 303 17051 11044 14000 -2677 -1669 2499 A C ATOM 2352 NE ARG A 303 42.782 -20.240 10.620 1.00124.36 A N ANISOU 2352 NE ARG A 303 18872 12565 15814 -2901 -1533 2541 A N ATOM 2353 CZ ARG A 303 42.276 -21.066 9.716 1.00130.67 A C ANISOU 2353 CZ ARG A 303 19600 13210 16839 -2940 -1518 2400 A C ATOM 2354 NH1 ARG A 303 42.827 -21.150 8.515 1.00131.95 A N1+ ANISOU 2354 NH1 ARG A 303 19591 13402 17141 -2751 -1635 2206 A N1+ ATOM 2355 NH2 ARG A 303 41.218 -21.807 10.021 1.00132.51 A N ANISOU 2355 NH2 ARG A 303 19929 13264 17155 -3170 -1384 2448 A N ATOM 2356 N ILE A 304 44.738 -16.039 13.659 1.00 93.53 A N ANISOU 2356 N ILE A 304 15046 9481 11011 -2751 -1580 2836 A N ATOM 2357 CA ILE A 304 45.243 -14.668 13.608 1.00 94.76 A C ANISOU 2357 CA ILE A 304 15060 9902 11042 -2674 -1587 2745 A C ATOM 2358 C ILE A 304 44.997 -14.028 12.256 1.00 95.07 A C ANISOU 2358 C ILE A 304 14824 10080 11219 -2615 -1521 2518 A C ATOM 2359 O ILE A 304 45.002 -14.713 11.226 1.00 98.51 A O ANISOU 2359 O ILE A 304 15161 10414 11854 -2539 -1568 2417 A O ATOM 2360 CB ILE A 304 46.759 -14.625 13.909 1.00 99.56 A C ANISOU 2360 CB ILE A 304 15708 10530 11588 -2481 -1815 2798 A C ATOM 2361 CG1 ILE A 304 47.218 -13.205 14.251 1.00 92.60 A C ANISOU 2361 CG1 ILE A 304 14739 9906 10539 -2457 -1807 2743 A C ATOM 2362 CG2 ILE A 304 47.554 -15.181 12.748 1.00102.03 A C ANISOU 2362 CG2 ILE A 304 15890 10766 12111 -2285 -1967 2690 A C ATOM 2363 CD1 ILE A 304 48.604 -13.160 14.871 1.00 81.75 A C ANISOU 2363 CD1 ILE A 304 13434 8568 9059 -2312 -2021 2821 A C ATOM 2364 N ASP A 305 44.767 -12.717 12.255 1.00 85.00 A N ANISOU 2364 N ASP A 305 13429 9035 9832 -2641 -1407 2438 A N ATOM 2365 CA ASP A 305 44.542 -12.019 10.990 1.00 85.53 A C ANISOU 2365 CA ASP A 305 13237 9251 10010 -2566 -1331 2239 A C ATOM 2366 C ASP A 305 45.763 -11.223 10.533 1.00 89.57 A C ANISOU 2366 C ASP A 305 13613 9895 10523 -2376 -1448 2161 A C ATOM 2367 O ASP A 305 46.726 -11.043 11.286 1.00 91.39 A O ANISOU 2367 O ASP A 305 13940 10135 10648 -2325 -1577 2248 A O ATOM 2368 CB ASP A 305 43.254 -11.170 11.006 1.00 86.14 A C ANISOU 2368 CB ASP A 305 13237 9482 10009 -2715 -1088 2180 A C ATOM 2369 CG ASP A 305 43.344 -9.957 11.924 1.00100.24 A C ANISOU 2369 CG ASP A 305 15078 11431 11579 -2764 -1013 2227 A C ATOM 2370 OD1 ASP A 305 44.441 -9.688 12.460 1.00110.60 A O ANISOU 2370 OD1 ASP A 305 16459 12757 12808 -2683 -1154 2282 A O ATOM 2371 OD2 ASP A 305 42.314 -9.262 12.104 1.00 95.35 A O1- ANISOU 2371 OD2 ASP A 305 14426 10932 10871 -2882 -812 2200 A O1- ATOM 2372 N SER A 306 45.718 -10.769 9.288 1.00 82.36 A N ANISOU 2372 N SER A 306 12470 9091 9730 -2269 -1402 1996 A N ATOM 2373 CA SER A 306 46.844 -10.090 8.666 1.00 79.33 A C ANISOU 2373 CA SER A 306 11932 8825 9384 -2083 -1498 1916 A C ATOM 2374 C SER A 306 47.331 -8.886 9.477 1.00 84.38 A C ANISOU 2374 C SER A 306 12599 9607 9854 -2113 -1474 1952 A C ATOM 2375 O SER A 306 48.535 -8.735 9.717 1.00 86.64 A O ANISOU 2375 O SER A 306 12889 9911 10119 -2011 -1631 1979 A O ATOM 2376 CB SER A 306 46.415 -9.658 7.282 1.00 85.50 A C ANISOU 2376 CB SER A 306 12472 9727 10288 -1992 -1390 1746 A C ATOM 2377 OG SER A 306 45.360 -10.506 6.866 1.00101.52 A O ANISOU 2377 OG SER A 306 14501 11663 12409 -2069 -1321 1706 A O ATOM 2378 N ASP A 307 46.391 -8.030 9.880 1.00 80.09 A N ANISOU 2378 N ASP A 307 12068 9169 9193 -2251 -1278 1942 A N ATOM 2379 CA ASP A 307 46.669 -6.891 10.761 1.00 78.91 A C ANISOU 2379 CA ASP A 307 11972 9140 8870 -2310 -1232 1968 A C ATOM 2380 C ASP A 307 47.434 -7.327 12.021 1.00 81.54 A C ANISOU 2380 C ASP A 307 12511 9395 9074 -2343 -1401 2108 A C ATOM 2381 O ASP A 307 48.591 -6.985 12.198 1.00 87.88 A O ANISOU 2381 O ASP A 307 13290 10245 9854 -2253 -1543 2103 A O ATOM 2382 CB ASP A 307 45.347 -6.206 11.142 1.00 89.24 A C ANISOU 2382 CB ASP A 307 13311 10533 10063 -2467 -993 1961 A C ATOM 2383 CG ASP A 307 45.533 -4.785 11.655 1.00100.85 A C ANISOU 2383 CG ASP A 307 14775 12151 11392 -2496 -901 1927 A C ATOM 2384 OD1 ASP A 307 45.634 -3.850 10.822 1.00108.51 A O ANISOU 2384 OD1 ASP A 307 15567 13235 12426 -2409 -811 1812 A O ATOM 2385 OD2 ASP A 307 45.548 -4.603 12.893 1.00102.06 A O1- ANISOU 2385 OD2 ASP A 307 15105 12304 11370 -2604 -911 2014 A O1- ATOM 2386 N ASP A 308 46.791 -8.103 12.886 1.00 88.10 A N ANISOU 2386 N ASP A 308 13541 10114 9820 -2470 -1384 2237 A N ATOM 2387 CA ASP A 308 47.438 -8.585 14.107 1.00 92.00 A C ANISOU 2387 CA ASP A 308 14244 10539 10172 -2489 -1535 2388 A C ATOM 2388 C ASP A 308 48.730 -9.356 13.821 1.00 88.37 A C ANISOU 2388 C ASP A 308 13771 9993 9812 -2315 -1781 2415 A C ATOM 2389 O ASP A 308 49.699 -9.259 14.565 1.00 92.71 A O ANISOU 2389 O ASP A 308 14396 10578 10251 -2263 -1934 2477 A O ATOM 2390 CB ASP A 308 46.466 -9.435 14.946 1.00 94.80 A C ANISOU 2390 CB ASP A 308 14809 10766 10444 -2641 -1458 2537 A C ATOM 2391 CG ASP A 308 45.345 -8.601 15.575 1.00100.07 A C ANISOU 2391 CG ASP A 308 15524 11547 10952 -2811 -1234 2540 A C ATOM 2392 OD1 ASP A 308 45.475 -7.359 15.619 1.00105.15 A O ANISOU 2392 OD1 ASP A 308 16084 12357 11511 -2808 -1167 2447 A O ATOM 2393 OD2 ASP A 308 44.335 -9.179 16.035 1.00 96.45 A O1- ANISOU 2393 OD2 ASP A 308 15186 11008 10452 -2948 -1119 2637 A O1- ATOM 2394 N ALA A 309 48.748 -10.124 12.744 1.00 85.82 A N ANISOU 2394 N ALA A 309 13349 9568 9693 -2217 -1822 2361 A N ATOM 2395 CA ALA A 309 49.947 -10.880 12.412 1.00 91.57 A C ANISOU 2395 CA ALA A 309 14058 10213 10520 -2036 -2047 2382 A C ATOM 2396 C ALA A 309 51.118 -9.945 12.192 1.00 87.84 A C ANISOU 2396 C ALA A 309 13432 9908 10034 -1912 -2145 2299 A C ATOM 2397 O ALA A 309 52.241 -10.264 12.540 1.00 94.67 A O ANISOU 2397 O ALA A 309 14332 10766 10874 -1799 -2342 2356 A O ATOM 2398 CB ALA A 309 49.719 -11.740 11.186 1.00100.16 A C ANISOU 2398 CB ALA A 309 15045 11180 11833 -1946 -2056 2305 A C ATOM 2399 N LEU A 310 50.844 -8.785 11.610 1.00 86.45 A N ANISOU 2399 N LEU A 310 13083 9884 9878 -1933 -2001 2168 A N ATOM 2400 CA LEU A 310 51.883 -7.817 11.281 1.00 83.90 A C ANISOU 2400 CA LEU A 310 12593 9714 9571 -1833 -2061 2077 A C ATOM 2401 C LEU A 310 52.403 -7.065 12.505 1.00 88.88 A C ANISOU 2401 C LEU A 310 13320 10444 10006 -1912 -2110 2121 A C ATOM 2402 O LEU A 310 53.531 -6.561 12.495 1.00 93.73 A O ANISOU 2402 O LEU A 310 13833 11155 10623 -1828 -2230 2076 A O ATOM 2403 CB LEU A 310 51.361 -6.815 10.251 1.00 74.72 A C ANISOU 2403 CB LEU A 310 11227 8668 8495 -1826 -1868 1934 A C ATOM 2404 CG LEU A 310 51.599 -7.205 8.799 1.00 76.58 A C ANISOU 2404 CG LEU A 310 11269 8893 8937 -1654 -1891 1842 A C ATOM 2405 CD1 LEU A 310 50.871 -6.259 7.890 1.00 72.37 A C ANISOU 2405 CD1 LEU A 310 10564 8477 8456 -1656 -1676 1724 A C ATOM 2406 CD2 LEU A 310 53.084 -7.198 8.494 1.00 83.38 A C ANISOU 2406 CD2 LEU A 310 12017 9798 9865 -1484 -2080 1825 A C ATOM 2407 N ASN A 311 51.565 -6.975 13.538 1.00 83.36 A N ANISOU 2407 N ASN A 311 12805 9731 9138 -2076 -2013 2199 A N ATOM 2408 CA ASN A 311 51.915 -6.274 14.764 1.00 90.52 A C ANISOU 2408 CA ASN A 311 13821 10736 9835 -2161 -2047 2231 A C ATOM 2409 C ASN A 311 52.529 -7.248 15.744 1.00 98.01 A C ANISOU 2409 C ASN A 311 14955 11612 10671 -2123 -2252 2383 A C ATOM 2410 O ASN A 311 52.824 -6.895 16.886 1.00 99.06 A O ANISOU 2410 O ASN A 311 15210 11824 10605 -2182 -2310 2431 A O ATOM 2411 CB ASN A 311 50.683 -5.603 15.389 1.00101.66 A C ANISOU 2411 CB ASN A 311 15335 12190 11101 -2342 -1826 2235 A C ATOM 2412 CG ASN A 311 51.024 -4.772 16.639 1.00115.40 A C ANISOU 2412 CG ASN A 311 17184 14047 12615 -2427 -1852 2242 A C ATOM 2413 ND2 ASN A 311 50.123 -4.789 17.621 1.00120.04 A N ANISOU 2413 ND2 ASN A 311 17960 14629 13020 -2563 -1745 2326 A N ATOM 2414 OD1 ASN A 311 52.073 -4.121 16.713 1.00113.42 A O ANISOU 2414 OD1 ASN A 311 16844 13896 12355 -2374 -1965 2165 A O ATOM 2415 N HIS A 312 52.716 -8.484 15.289 1.00104.58 A N ANISOU 2415 N HIS A 312 15813 12296 11628 -2016 -2359 2455 A N ATOM 2416 CA HIS A 312 53.314 -9.526 16.118 1.00107.42 A C ANISOU 2416 CA HIS A 312 16353 12563 11898 -1949 -2551 2615 A C ATOM 2417 C HIS A 312 54.804 -9.256 16.395 1.00105.10 A C ANISOU 2417 C HIS A 312 15984 12394 11554 -1814 -2776 2595 A C ATOM 2418 O HIS A 312 55.534 -8.752 15.525 1.00 88.66 A O ANISOU 2418 O HIS A 312 13683 10398 9606 -1716 -2822 2466 A O ATOM 2419 CB HIS A 312 53.119 -10.905 15.485 1.00101.10 A C ANISOU 2419 CB HIS A 312 15598 11550 11265 -1863 -2595 2686 A C ATOM 2420 CG HIS A 312 53.550 -12.037 16.363 1.00103.61 A C ANISOU 2420 CG HIS A 312 16134 11740 11492 -1798 -2756 2875 A C ATOM 2421 CD2 HIS A 312 52.851 -12.811 17.228 1.00107.28 A C ANISOU 2421 CD2 HIS A 312 16842 12065 11853 -1890 -2708 3047 A C ATOM 2422 ND1 HIS A 312 54.854 -12.485 16.416 1.00102.82 A N ANISOU 2422 ND1 HIS A 312 16015 11653 11400 -1607 -2991 2914 A N ATOM 2423 CE1 HIS A 312 54.937 -13.488 17.269 1.00108.28 A C ANISOU 2423 CE1 HIS A 312 16934 12215 11991 -1573 -3083 3103 A C ATOM 2424 NE2 HIS A 312 53.735 -13.706 17.778 1.00111.53 A N ANISOU 2424 NE2 HIS A 312 17513 12526 12336 -1746 -2911 3192 A N ATOM 2425 N ASP A 313 55.241 -9.597 17.608 1.00108.12 A N ANISOU 2425 N ASP A 313 16545 12796 11739 -1807 -2911 2724 A N ATOM 2426 CA ASP A 313 56.590 -9.272 18.057 1.00111.08 A C ANISOU 2426 CA ASP A 313 16856 13324 12026 -1701 -3125 2701 A C ATOM 2427 C ASP A 313 57.644 -9.772 17.073 1.00103.14 A C ANISOU 2427 C ASP A 313 15676 12298 11215 -1495 -3288 2659 A C ATOM 2428 O ASP A 313 58.707 -9.177 16.938 1.00 98.75 A O ANISOU 2428 O ASP A 313 14951 11898 10671 -1419 -3410 2565 A O ATOM 2429 CB ASP A 313 56.842 -9.831 19.460 1.00120.15 A C ANISOU 2429 CB ASP A 313 18240 14481 12931 -1689 -3257 2872 A C ATOM 2430 CG ASP A 313 55.912 -9.232 20.509 1.00128.31 A C ANISOU 2430 CG ASP A 313 19437 15572 13743 -1880 -3105 2905 A C ATOM 2431 OD1 ASP A 313 55.585 -8.025 20.414 1.00128.18 A O ANISOU 2431 OD1 ASP A 313 19318 15676 13708 -2003 -2971 2758 A O ATOM 2432 OD2 ASP A 313 55.516 -9.972 21.439 1.00132.03 A O1- ANISOU 2432 OD2 ASP A 313 20144 15967 14056 -1900 -3115 3085 A O1- ATOM 2433 N PHE A 314 57.335 -10.862 16.381 1.00 99.71 A N ANISOU 2433 N PHE A 314 15277 11671 10936 -1410 -3283 2721 A N ATOM 2434 CA PHE A 314 58.214 -11.400 15.350 1.00102.62 A C ANISOU 2434 CA PHE A 314 15486 12005 11500 -1205 -3417 2675 A C ATOM 2435 C PHE A 314 58.819 -10.308 14.457 1.00102.07 A C ANISOU 2435 C PHE A 314 15127 12109 11546 -1170 -3397 2489 A C ATOM 2436 O PHE A 314 60.026 -10.307 14.202 1.00100.62 A O ANISOU 2436 O PHE A 314 14801 12022 11408 -1015 -3568 2456 A O ATOM 2437 CB PHE A 314 57.444 -12.430 14.511 1.00107.58 A C ANISOU 2437 CB PHE A 314 16163 12405 12308 -1174 -3334 2703 A C ATOM 2438 CG PHE A 314 58.221 -12.993 13.341 1.00110.46 A C ANISOU 2438 CG PHE A 314 16364 12726 12881 -959 -3448 2639 A C ATOM 2439 CD1 PHE A 314 59.477 -13.547 13.517 1.00107.62 A C ANISOU 2439 CD1 PHE A 314 15993 12390 12509 -758 -3681 2700 A C ATOM 2440 CD2 PHE A 314 57.671 -12.998 12.063 1.00110.06 A C ANISOU 2440 CD2 PHE A 314 16170 12617 13029 -946 -3322 2517 A C ATOM 2441 CE1 PHE A 314 60.177 -14.074 12.439 1.00105.35 A C ANISOU 2441 CE1 PHE A 314 15555 12065 12406 -550 -3779 2640 A C ATOM 2442 CE2 PHE A 314 58.370 -13.525 10.986 1.00105.46 A C ANISOU 2442 CE2 PHE A 314 15441 12002 12626 -738 -3424 2453 A C ATOM 2443 CZ PHE A 314 59.622 -14.066 11.176 1.00102.22 A C ANISOU 2443 CZ PHE A 314 15024 11609 12205 -541 -3649 2515 A C ATOM 2444 N PHE A 315 57.982 -9.379 13.996 1.00101.60 A N ANISOU 2444 N PHE A 315 14980 12093 11531 -1309 -3180 2377 A N ATOM 2445 CA PHE A 315 58.408 -8.336 13.052 1.00 99.13 A C ANISOU 2445 CA PHE A 315 14401 11919 11344 -1280 -3118 2213 A C ATOM 2446 C PHE A 315 59.035 -7.125 13.731 1.00100.40 A C ANISOU 2446 C PHE A 315 14492 12271 11383 -1363 -3143 2143 A C ATOM 2447 O PHE A 315 59.408 -6.153 13.064 1.00103.28 A O ANISOU 2447 O PHE A 315 14647 12749 11846 -1361 -3077 2013 A O ATOM 2448 CB PHE A 315 57.224 -7.862 12.196 1.00 94.09 A C ANISOU 2448 CB PHE A 315 13696 11245 10811 -1372 -2865 2126 A C ATOM 2449 CG PHE A 315 56.655 -8.923 11.308 1.00 93.29 A C ANISOU 2449 CG PHE A 315 13605 10980 10862 -1289 -2835 2145 A C ATOM 2450 CD1 PHE A 315 55.510 -9.618 11.680 1.00 93.07 A C ANISOU 2450 CD1 PHE A 315 13770 10801 10792 -1399 -2742 2229 A C ATOM 2451 CD2 PHE A 315 57.266 -9.236 10.107 1.00 89.21 A C ANISOU 2451 CD2 PHE A 315 12902 10463 10530 -1104 -2898 2074 A C ATOM 2452 CE1 PHE A 315 54.984 -10.598 10.871 1.00 89.66 A C ANISOU 2452 CE1 PHE A 315 13344 10212 10510 -1339 -2717 2227 A C ATOM 2453 CE2 PHE A 315 56.744 -10.217 9.294 1.00 93.82 A C ANISOU 2453 CE2 PHE A 315 13499 10898 11252 -1027 -2877 2071 A C ATOM 2454 CZ PHE A 315 55.600 -10.901 9.679 1.00 93.15 A C ANISOU 2454 CZ PHE A 315 13606 10653 11132 -1151 -2789 2142 A C ATOM 2455 N TRP A 316 59.132 -7.178 15.055 1.00101.16 A N ANISOU 2455 N TRP A 316 14768 12403 11266 -1438 -3231 2226 A N ATOM 2456 CA TRP A 316 59.638 -6.053 15.834 1.00106.41 A C ANISOU 2456 CA TRP A 316 15393 13247 11792 -1538 -3258 2147 A C ATOM 2457 C TRP A 316 60.670 -6.504 16.884 1.00113.19 A C ANISOU 2457 C TRP A 316 16330 14191 12484 -1461 -3517 2226 A C ATOM 2458 O TRP A 316 60.690 -6.016 18.017 1.00107.15 A O ANISOU 2458 O TRP A 316 15675 13528 11511 -1567 -3548 2228 A O ATOM 2459 CB TRP A 316 58.472 -5.306 16.485 1.00105.44 A C ANISOU 2459 CB TRP A 316 15407 13125 11529 -1746 -3051 2130 A C ATOM 2460 CG TRP A 316 57.378 -4.947 15.521 1.00105.81 A C ANISOU 2460 CG TRP A 316 15390 13096 11716 -1808 -2799 2069 A C ATOM 2461 CD1 TRP A 316 56.159 -5.535 15.420 1.00108.66 A C ANISOU 2461 CD1 TRP A 316 15883 13323 12081 -1864 -2659 2144 A C ATOM 2462 CD2 TRP A 316 57.409 -3.918 14.519 1.00107.56 A C ANISOU 2462 CD2 TRP A 316 15392 13383 12091 -1814 -2657 1921 A C ATOM 2463 CE2 TRP A 316 56.171 -3.945 13.857 1.00102.86 A C ANISOU 2463 CE2 TRP A 316 14810 12701 11571 -1859 -2440 1915 A C ATOM 2464 CE3 TRP A 316 58.365 -2.978 14.124 1.00103.99 A C ANISOU 2464 CE3 TRP A 316 14733 13058 11721 -1785 -2687 1798 A C ATOM 2465 NE1 TRP A 316 55.425 -4.941 14.423 1.00104.32 A N ANISOU 2465 NE1 TRP A 316 15204 12768 11667 -1897 -2448 2045 A N ATOM 2466 CZ2 TRP A 316 55.865 -3.073 12.822 1.00100.40 A C ANISOU 2466 CZ2 TRP A 316 14318 12430 11397 -1856 -2257 1799 A C ATOM 2467 CZ3 TRP A 316 58.056 -2.117 13.098 1.00 97.75 A C ANISOU 2467 CZ3 TRP A 316 13772 12287 11080 -1793 -2493 1691 A C ATOM 2468 CH2 TRP A 316 56.822 -2.171 12.454 1.00 99.56 A C ANISOU 2468 CH2 TRP A 316 14025 12435 11367 -1818 -2283 1696 A C ATOM 2469 N SER A 317 61.521 -7.445 16.481 1.00118.01 A N ANISOU 2469 N SER A 317 16884 14770 13184 -1262 -3702 2287 A N ATOM 2470 CA SER A 317 62.575 -7.983 17.325 1.00120.24 A C ANISOU 2470 CA SER A 317 17218 15141 13327 -1142 -3960 2370 A C ATOM 2471 C SER A 317 63.868 -8.005 16.528 1.00125.40 A C ANISOU 2471 C SER A 317 17615 15896 14136 -965 -4117 2296 A C ATOM 2472 O SER A 317 63.847 -7.999 15.299 1.00122.88 A O ANISOU 2472 O SER A 317 17133 15520 14034 -899 -4035 2230 A O ATOM 2473 CB SER A 317 62.239 -9.411 17.747 1.00122.64 A C ANISOU 2473 CB SER A 317 17763 15270 13565 -1042 -4034 2572 A C ATOM 2474 OG SER A 317 61.019 -9.458 18.458 1.00125.24 A O ANISOU 2474 OG SER A 317 18325 15502 13759 -1206 -3877 2655 A O ATOM 2475 N ASP A 318 64.998 -8.027 17.221 1.00131.60 A N ANISOU 2475 N ASP A 318 18355 16845 14803 -881 -4343 2305 A N ATOM 2476 CA ASP A 318 66.264 -8.227 16.543 1.00133.67 A C ANISOU 2476 CA ASP A 318 18383 17206 15198 -690 -4513 2260 A C ATOM 2477 C ASP A 318 66.339 -9.704 16.177 1.00126.52 A C ANISOU 2477 C ASP A 318 17582 16132 14358 -471 -4612 2411 A C ATOM 2478 O ASP A 318 66.026 -10.565 17.002 1.00130.21 A O ANISOU 2478 O ASP A 318 18297 16501 14675 -435 -4678 2570 A O ATOM 2479 CB ASP A 318 67.426 -7.799 17.442 1.00144.42 A C ANISOU 2479 CB ASP A 318 19657 18814 16404 -671 -4729 2216 A C ATOM 2480 CG ASP A 318 67.364 -6.318 17.805 1.00149.52 A C ANISOU 2480 CG ASP A 318 20204 19610 16999 -900 -4628 2045 A C ATOM 2481 OD1 ASP A 318 66.695 -5.548 17.075 1.00143.12 A O ANISOU 2481 OD1 ASP A 318 19319 18733 16329 -1029 -4400 1947 A O ATOM 2482 OD2 ASP A 318 67.988 -5.925 18.816 1.00155.47 A O1- ANISOU 2482 OD2 ASP A 318 20955 20548 17569 -944 -4777 2005 A O1- ATOM 2483 N PRO A 319 66.717 -10.006 14.926 1.00114.55 A N ANISOU 2483 N PRO A 319 15885 14572 13068 -322 -4610 2365 A N ATOM 2484 CA PRO A 319 67.120 -9.067 13.871 1.00111.12 A C ANISOU 2484 CA PRO A 319 15154 14249 12818 -338 -4523 2198 A C ATOM 2485 C PRO A 319 65.921 -8.466 13.147 1.00109.54 A C ANISOU 2485 C PRO A 319 14951 13940 12730 -494 -4243 2123 A C ATOM 2486 O PRO A 319 64.934 -9.164 12.919 1.00106.36 A O ANISOU 2486 O PRO A 319 14714 13342 12356 -500 -4141 2195 A O ATOM 2487 CB PRO A 319 67.892 -9.952 12.881 1.00111.06 A C ANISOU 2487 CB PRO A 319 15011 14209 12979 -72 -4641 2222 A C ATOM 2488 CG PRO A 319 67.724 -11.402 13.382 1.00113.03 A C ANISOU 2488 CG PRO A 319 15518 14283 13146 71 -4765 2401 A C ATOM 2489 CD PRO A 319 66.664 -11.391 14.433 1.00110.53 A C ANISOU 2489 CD PRO A 319 15478 13868 12649 -121 -4673 2485 A C ATOM 2490 N MET A 320 66.019 -7.193 12.774 1.00110.89 A N ANISOU 2490 N MET A 320 14931 14236 12967 -614 -4119 1980 A N ATOM 2491 CA MET A 320 64.943 -6.510 12.061 1.00106.80 A C ANISOU 2491 CA MET A 320 14390 13642 12549 -744 -3849 1905 A C ATOM 2492 C MET A 320 64.834 -6.970 10.617 1.00114.32 A C ANISOU 2492 C MET A 320 15209 14511 13716 -587 -3776 1883 A C ATOM 2493 O MET A 320 65.818 -7.400 10.021 1.00123.79 A O ANISOU 2493 O MET A 320 16250 15764 15019 -395 -3913 1878 A O ATOM 2494 CB MET A 320 65.139 -4.995 12.103 1.00105.95 A C ANISOU 2494 CB MET A 320 14124 13682 12449 -906 -3734 1766 A C ATOM 2495 CG MET A 320 64.749 -4.384 13.425 1.00111.29 A C ANISOU 2495 CG MET A 320 14969 14403 12914 -1109 -3717 1759 A C ATOM 2496 SD MET A 320 63.144 -4.988 13.982 1.00110.56 A S ANISOU 2496 SD MET A 320 15199 14119 12689 -1214 -3578 1876 A S ATOM 2497 CE MET A 320 62.121 -3.557 13.641 1.00 70.73 A C ANISOU 2497 CE MET A 320 10109 9079 7685 -1420 -3266 1749 A C ATOM 2498 N PRO A 321 63.628 -6.877 10.045 1.00111.92 A N ANISOU 2498 N PRO A 321 14962 14089 13474 -662 -3561 1864 A N ATOM 2499 CA PRO A 321 63.496 -7.288 8.648 1.00112.14 A C ANISOU 2499 CA PRO A 321 14857 14057 13696 -507 -3492 1826 A C ATOM 2500 C PRO A 321 64.471 -6.517 7.758 1.00106.32 A C ANISOU 2500 C PRO A 321 13820 13480 13095 -412 -3483 1726 A C ATOM 2501 O PRO A 321 64.567 -5.291 7.834 1.00 94.79 A O ANISOU 2501 O PRO A 321 12250 12132 11632 -541 -3371 1648 A O ATOM 2502 CB PRO A 321 62.042 -6.933 8.314 1.00113.60 A C ANISOU 2502 CB PRO A 321 15119 14150 13894 -647 -3241 1794 A C ATOM 2503 CG PRO A 321 61.338 -6.921 9.639 1.00113.43 A C ANISOU 2503 CG PRO A 321 15346 14072 13678 -836 -3225 1867 A C ATOM 2504 CD PRO A 321 62.351 -6.424 10.623 1.00112.14 A C ANISOU 2504 CD PRO A 321 15167 14048 13392 -875 -3377 1871 A C ATOM 2505 N SER A 322 65.196 -7.255 6.927 1.00110.71 A N ANISOU 2505 N SER A 322 14250 14041 13774 -184 -3597 1732 A N ATOM 2506 CA SER A 322 66.174 -6.672 6.028 1.00111.84 A C ANISOU 2506 CA SER A 322 14103 14339 14054 -67 -3596 1654 A C ATOM 2507 C SER A 322 65.679 -6.815 4.604 1.00105.44 A C ANISOU 2507 C SER A 322 13180 13483 13399 59 -3446 1603 A C ATOM 2508 O SER A 322 64.907 -7.724 4.313 1.00 93.23 A O ANISOU 2508 O SER A 322 11770 11786 11867 115 -3431 1632 A O ATOM 2509 CB SER A 322 67.507 -7.413 6.158 1.00113.09 A C ANISOU 2509 CB SER A 322 14178 14571 14220 129 -3854 1698 A C ATOM 2510 OG SER A 322 67.427 -8.723 5.605 1.00109.99 A O ANISOU 2510 OG SER A 322 13857 14047 13888 335 -3941 1751 A O ATOM 2511 N ASP A 323 66.150 -5.943 3.716 1.00106.15 A N ANISOU 2511 N ASP A 323 13019 13707 13606 108 -3337 1527 A N ATOM 2512 CA ASP A 323 65.839 -6.071 2.302 1.00108.61 A C ANISOU 2512 CA ASP A 323 13196 14013 14057 266 -3210 1480 A C ATOM 2513 C ASP A 323 66.444 -7.341 1.711 1.00109.12 A C ANISOU 2513 C ASP A 323 13226 14041 14191 527 -3387 1504 A C ATOM 2514 O ASP A 323 67.156 -8.074 2.393 1.00116.57 A O ANISOU 2514 O ASP A 323 14243 14968 15082 591 -3603 1566 A O ATOM 2515 CB ASP A 323 66.254 -4.817 1.531 1.00119.84 A C ANISOU 2515 CB ASP A 323 14362 15591 15580 266 -3044 1412 A C ATOM 2516 CG ASP A 323 65.115 -3.796 1.422 1.00131.01 A C ANISOU 2516 CG ASP A 323 15819 16984 16976 92 -2778 1372 A C ATOM 2517 OD1 ASP A 323 63.928 -4.199 1.537 1.00134.12 A O ANISOU 2517 OD1 ASP A 323 16394 17255 17310 30 -2705 1383 A O ATOM 2518 OD2 ASP A 323 65.403 -2.594 1.213 1.00131.32 A O1- ANISOU 2518 OD2 ASP A 323 15708 17125 17063 20 -2635 1333 A O1- ATOM 2519 N LEU A 324 66.129 -7.622 0.452 1.00112.77 A N ANISOU 2519 N LEU A 324 13588 14493 14765 688 -3293 1453 A N ATOM 2520 CA LEU A 324 66.547 -8.877 -0.169 1.00118.49 A C ANISOU 2520 CA LEU A 324 14304 15159 15557 940 -3444 1459 A C ATOM 2521 C LEU A 324 67.517 -8.657 -1.329 1.00127.51 A C ANISOU 2521 C LEU A 324 15159 16466 16823 1168 -3440 1411 A C ATOM 2522 O LEU A 324 67.234 -7.923 -2.281 1.00117.17 A O ANISOU 2522 O LEU A 324 13690 15247 15584 1196 -3250 1350 A O ATOM 2523 CB LEU A 324 65.339 -9.716 -0.605 1.00114.94 A C ANISOU 2523 CB LEU A 324 14015 14533 15125 958 -3380 1433 A C ATOM 2524 CG LEU A 324 64.595 -10.494 0.495 1.00109.86 A C ANISOU 2524 CG LEU A 324 13675 13688 14380 810 -3453 1506 A C ATOM 2525 CD1 LEU A 324 64.020 -9.551 1.530 1.00113.37 A C ANISOU 2525 CD1 LEU A 324 14222 14150 14703 531 -3347 1538 A C ATOM 2526 CD2 LEU A 324 63.489 -11.389 -0.067 1.00 96.96 A C ANISOU 2526 CD2 LEU A 324 12166 11880 12793 838 -3393 1465 A C ATOM 2527 N LYS A 325 68.677 -9.293 -1.209 1.00145.98 A N ANISOU 2527 N LYS A 325 17434 18852 19178 1339 -3649 1448 A N ATOM 2528 CA LYS A 325 69.772 -9.156 -2.159 1.00155.09 A C ANISOU 2528 CA LYS A 325 18311 20178 20438 1563 -3675 1417 A C ATOM 2529 C LYS A 325 70.489 -10.498 -2.234 1.00156.39 A C ANISOU 2529 C LYS A 325 18514 20289 20618 1813 -3906 1450 A C ATOM 2530 O LYS A 325 71.315 -10.733 -3.117 1.00157.23 A O ANISOU 2530 O LYS A 325 18422 20508 20811 2055 -3951 1424 A O ATOM 2531 CB LYS A 325 70.757 -8.073 -1.702 1.00157.73 A C ANISOU 2531 CB LYS A 325 18458 20702 20770 1463 -3681 1429 A C ATOM 2532 CG LYS A 325 70.190 -6.655 -1.633 1.00158.86 A C ANISOU 2532 CG LYS A 325 18550 20897 20912 1224 -3447 1395 A C ATOM 2533 CD LYS A 325 71.241 -5.678 -1.102 1.00161.77 A C ANISOU 2533 CD LYS A 325 18743 21433 21290 1114 -3476 1395 A C ATOM 2534 CE LYS A 325 70.731 -4.242 -1.064 1.00161.40 A C ANISOU 2534 CE LYS A 325 18648 21420 21257 884 -3233 1356 A C ATOM 2535 NZ LYS A 325 71.746 -3.327 -0.470 1.00163.36 A N1+ ANISOU 2535 NZ LYS A 325 18738 21811 21522 751 -3271 1340 A N1+ ATOM 2536 N GLY A 326 70.173 -11.372 -1.285 1.00152.18 A N ANISOU 2536 N GLY A 326 18242 19582 19998 1759 -4045 1514 A N ATOM 2537 CA GLY A 326 70.666 -12.731 -1.319 1.00149.02 A C ANISOU 2537 CA GLY A 326 17931 19079 19610 1992 -4247 1553 A C ATOM 2538 C GLY A 326 69.934 -13.527 -2.380 1.00151.18 A C ANISOU 2538 C GLY A 326 18258 19212 19971 2138 -4181 1482 A C ATOM 2539 O GLY A 326 69.491 -14.645 -2.129 1.00147.97 A O ANISOU 2539 O GLY A 326 18077 18591 19554 2182 -4270 1509 A O ATOM 2540 N MET A 327 69.804 -12.945 -3.569 1.00157.78 A N ANISOU 2540 N MET A 327 18886 20169 20893 2215 -4022 1390 A N ATOM 2541 CA MET A 327 69.094 -13.587 -4.671 1.00166.37 A C ANISOU 2541 CA MET A 327 19993 21164 22057 2357 -3949 1296 A C ATOM 2542 C MET A 327 68.985 -12.667 -5.886 1.00163.85 A C ANISOU 2542 C MET A 327 19421 21032 21802 2422 -3750 1209 A C ATOM 2543 O MET A 327 69.663 -12.872 -6.893 1.00162.05 A O ANISOU 2543 O MET A 327 19005 20920 21646 2680 -3770 1162 A O ATOM 2544 CB MET A 327 67.703 -14.051 -4.218 1.00173.74 A C ANISOU 2544 CB MET A 327 21200 21863 22951 2166 -3890 1288 A C ATOM 2545 CG MET A 327 66.951 -13.050 -3.342 1.00172.78 A C ANISOU 2545 CG MET A 327 21160 21749 22739 1845 -3756 1329 A C ATOM 2546 SD MET A 327 65.902 -13.842 -2.098 1.00299.29 A S ANISOU 2546 SD MET A 327 37551 37493 38673 1622 -3804 1403 A S ATOM 2547 CE MET A 327 67.093 -14.483 -0.907 1.00 87.31 A C ANISOU 2547 CE MET A 327 10813 10610 11750 1689 -4067 1543 A C TER CONECT 1381 1391 CONECT 1391 1381 1392 CONECT 1392 1391 1393 1395 CONECT 1393 1392 1394 1402 CONECT 1394 1393 CONECT 1395 1392 1396 1397 CONECT 1396 1395 CONECT 1397 1395 1398 CONECT 1398 1397 1399 1400 1401 CONECT 1399 1398 CONECT 1400 1398 CONECT 1401 1398 CONECT 1402 1393 END 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