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*** 3blh_a_vs_3lq5_a ***elNémo ID: 22051215591366107Job options:ID = 22051215591366107 JOBID = 3blh_a_vs_3lq5_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_3lq5_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 HETATM 2366 N TRS B 260 12.851 1.543 -16.890 1.00 72.25 C N HETATM 2367 C TRS B 260 11.898 1.666 -17.985 1.00 74.78 C C HETATM 2368 C1 TRS B 260 11.292 3.076 -17.931 1.00 88.90 C C HETATM 2369 O1 TRS B 260 11.282 3.644 -16.637 1.00 92.56 C O HETATM 2370 C2 TRS B 260 12.627 1.513 -19.312 1.00 71.54 C C HETATM 2371 O2 TRS B 260 12.052 2.330 -20.303 1.00 67.41 C O HETATM 2372 C3 TRS B 260 10.924 0.504 -17.749 1.00 81.60 C C HETATM 2373 O3 TRS B 260 10.829 0.150 -16.374 1.00 69.96 C O HETATM 2374 O HOH A 331 42.052 -19.542 0.836 1.00 61.27 D O HETATM 2375 O HOH A 332 59.676 -6.244 -7.029 1.00 63.68 D O HETATM 2376 O HOH A 333 41.851 -17.269 -5.989 1.00 47.71 D O HETATM 2377 O HOH A 334 53.214 -8.452 -9.576 1.00 61.90 D O HETATM 2378 O HOH A 335 48.924 -1.543 2.892 1.00 61.06 D O HETATM 2379 O HOH A 336 48.219 -5.216 -7.390 1.00 53.37 D O HETATM 2380 O HOH A 337 57.943 -2.371 -20.677 1.00 56.74 D O HETATM 2381 O HOH A 338 43.788 -18.085 -14.312 1.00 66.21 D O HETATM 2382 O HOH A 339 23.567 -22.198 -24.411 1.00 59.32 D O HETATM 2383 O HOH A 340 46.186 -4.388 -23.953 1.00 56.81 D O HETATM 2384 O HOH A 341 48.210 -14.805 -10.804 1.00 44.05 D O HETATM 2385 O HOH A 342 57.150 -4.244 12.272 1.00 56.06 D O HETATM 2386 O HOH A 343 53.311 -5.736 11.352 1.00 53.65 D O HETATM 2387 O HOH A 344 45.262 -14.171 -10.855 1.00 43.77 D O HETATM 2388 O HOH A 345 41.223 -10.105 7.583 1.00 53.20 D O HETATM 2389 O HOH A 346 37.857 -15.374 -9.623 1.00 63.19 D O HETATM 2390 O HOH A 347 52.048 -5.606 -7.606 1.00 57.64 D O HETATM 2391 O HOH A 348 32.609 -12.274 -7.587 1.00 35.64 D O HETATM 2392 O HOH A 349 59.864 -5.370 1.470 1.00 77.98 D O HETATM 2393 O HOH A 350 63.618 -0.464 -27.806 1.00 61.77 D O HETATM 2394 O HOH A 351 50.452 -0.688 -1.675 1.00 53.47 D O HETATM 2395 O HOH A 352 56.360 -14.412 -29.461 1.00 70.36 D O HETATM 2396 O HOH A 353 36.201 -6.091 4.933 1.00 72.23 D O HETATM 2397 O HOH A 354 57.295 -4.744 -6.637 1.00 73.03 D O HETATM 2398 O HOH A 355 31.510 -16.319 -8.541 1.00 70.64 D O HETATM 2399 O HOH A 356 54.556 -3.246 -15.032 1.00 70.01 D O HETATM 2400 O HOH A 357 53.872 -2.066 -17.419 1.00 71.79 D O HETATM 2401 O HOH A 358 62.643 -19.414 15.468 1.00 69.04 D O HETATM 2402 O HOH A 359 41.391 -7.139 9.425 1.00 63.29 D O HETATM 2403 O HOH A 360 48.647 -3.845 -31.313 1.00 60.00 D O HETATM 2404 O HOH A 361 50.688 -4.724 -29.553 1.00 66.16 D O HETATM 2405 O HOH A 362 44.684 -40.111 11.135 1.00 77.16 D O HETATM 2406 O HOH A 363 62.867 -17.728 -15.388 1.00 78.43 D O HETATM 2407 O HOH A 364 25.667 -18.542 -19.911 1.00 42.91 D O HETATM 2408 O HOH A 365 25.237 -20.276 -17.969 1.00 56.61 D O HETATM 2409 O HOH A 366 42.729 -4.812 -23.079 1.00 54.94 D O HETATM 2410 O HOH A 367 46.367 -6.662 -10.379 1.00 56.64 D O HETATM 2411 O HOH A 368 40.978 -10.663 15.414 1.00 64.69 D O HETATM 2412 O HOH A 369 44.158 -23.654 18.556 1.00 78.79 D O HETATM 2413 O HOH A 370 53.747 -31.792 10.174 1.00 78.98 D O HETATM 2414 O HOH A 371 53.807 -25.998 -0.111 1.00 83.53 D O HETATM 2415 O HOH A 372 37.096 4.595 -33.829 1.00 69.22 D O HETATM 2416 O HOH A 373 36.272 5.925 -36.371 1.00 81.40 D O HETATM 2417 O HOH A 374 64.715 -19.929 10.926 1.00 85.82 D O HETATM 2418 O HOH A 375 44.764 -18.726 -30.592 1.00 78.13 D O HETATM 2419 O HOH A 376 51.053 -9.618 20.577 1.00 64.72 D O HETATM 2420 O HOH A 377 54.926 -14.908 -12.731 1.00 64.25 D O HETATM 2421 O HOH A 378 56.058 -4.732 0.813 1.00 64.29 D O HETATM 2422 O HOH A 379 36.758 -3.420 -15.007 1.00 60.06 D O HETATM 2423 O HOH A 380 51.331 -14.351 -11.811 1.00 73.12 D O HETATM 2424 O HOH A 381 39.502 -12.230 8.692 1.00 61.03 D O HETATM 2425 O HOH A 382 39.930 -14.230 10.541 1.00 62.69 D O HETATM 2426 O HOH A 383 36.632 -1.789 -3.100 1.00 53.77 D O HETATM 2427 O HOH A 384 34.469 -6.044 -4.460 1.00 65.11 D O HETATM 2428 O HOH B 261 24.490 -14.266 -19.708 1.00 42.25 E O HETATM 2429 O HOH B 262 17.225 21.002 -6.416 1.00 58.34 E O HETATM 2430 O HOH B 263 31.447 6.228 -20.098 1.00 42.78 E O HETATM 2431 O HOH B 264 39.607 -1.403 -28.162 1.00 61.15 E O HETATM 2432 O HOH B 265 34.123 0.134 -20.823 1.00 53.84 E O HETATM 2433 O HOH B 266 29.405 6.989 -16.837 1.00 54.83 E O HETATM 2434 O HOH B 267 18.719 -18.659 -15.310 1.00 59.81 E O HETATM 2435 O HOH B 268 7.999 -10.906 -37.100 1.00 60.18 E O HETATM 2436 O HOH B 269 29.952 -3.894 -13.786 1.00 46.91 E O HETATM 2437 O HOH B 270 33.066 -0.160 -36.599 1.00 50.65 E O HETATM 2438 O HOH B 271 6.559 11.587 -22.084 1.00 48.93 E O HETATM 2439 O HOH B 272 32.897 -14.704 -26.546 1.00 50.80 E O HETATM 2440 O HOH B 273 18.699 -3.579 -10.336 1.00 46.89 E O HETATM 2441 O HOH B 274 31.231 14.824 -14.636 1.00 56.72 E O HETATM 2442 O HOH B 275 28.907 5.938 -33.479 1.00 52.42 E O HETATM 2443 O HOH B 276 14.196 2.157 -13.462 1.00 61.13 E O HETATM 2444 O HOH B 277 2.992 15.318 -11.755 1.00 46.51 E O HETATM 2445 O HOH B 278 21.347 0.402 -12.094 1.00 60.06 E O HETATM 2446 O HOH B 279 7.233 19.107 -18.780 1.00 49.41 E O HETATM 2447 O HOH B 280 13.222 -0.504 -13.652 1.00 44.64 E O HETATM 2448 O HOH B 281 21.443 -7.566 -10.358 1.00 54.16 E O HETATM 2449 O HOH B 282 19.342 -0.596 -10.182 1.00 58.57 E O HETATM 2450 O HOH B 283 0.104 8.931 -14.214 1.00 55.69 E O HETATM 2451 O HOH B 284 33.178 19.835 -27.454 1.00 68.60 E O HETATM 2452 O HOH B 285 22.763 -19.715 -16.729 1.00 55.03 E O HETATM 2453 O HOH B 286 7.350 -6.632 -24.696 1.00 55.24 E O HETATM 2454 O HOH B 287 32.091 -10.830 -12.627 1.00 62.33 E O HETATM 2455 O HOH B 288 17.261 11.614 -32.266 1.00 67.50 E O HETATM 2456 O HOH B 289 6.601 12.323 -8.905 1.00 75.61 E O HETATM 2457 O HOH B 290 16.215 23.830 -15.977 1.00 73.40 E O HETATM 2458 O HOH B 291 14.270 21.716 -16.354 1.00 62.21 E O HETATM 2459 O HOH B 292 11.356 22.010 -14.966 1.00 61.51 E O HETATM 2460 O HOH B 293 29.022 4.467 -16.188 1.00 55.00 E O HETATM 2461 O HOH B 294 7.591 -11.748 -29.155 1.00 55.45 E O HETATM 2462 O HOH B 295 14.529 -16.671 -16.582 1.00 46.53 E O HETATM 2463 O HOH B 296 0.296 16.866 -11.508 1.00 58.76 E O HETATM 2464 O HOH B 297 18.670 -14.183 -32.295 1.00 65.02 E O HETATM 2465 O HOH B 298 4.427 15.442 -9.313 1.00 62.18 E O HETATM 2466 O HOH B 299 30.791 -12.912 -11.884 1.00 76.14 E O HETATM 2467 O HOH B 300 21.137 -7.570 -37.002 1.00 63.89 E O HETATM 2468 O HOH B 301 -3.346 15.926 -11.386 1.00 57.30 E O HETATM 2469 O HOH B 302 17.023 17.200 -25.101 1.00 59.95 E O HETATM 2470 O HOH B 303 13.773 -16.616 -14.043 1.00 54.00 E O HETATM 2471 O HOH B 304 15.722 16.544 -27.407 1.00 69.81 E O HETATM 2472 O HOH B 305 21.510 -16.727 -13.586 1.00 58.27 E O HETATM 2473 O HOH B 306 22.232 13.213 -25.351 1.00 61.86 E O HETATM 2474 O HOH B 307 21.295 -12.476 -31.620 1.00 60.27 E O HETATM 2475 O HOH B 308 3.891 10.754 -21.148 1.00 38.43 E O HETATM 2476 O HOH B 309 9.370 -6.954 -22.129 1.00 40.99 E O HETATM 2477 O HOH B 310 23.044 8.341 -18.284 1.00 43.61 E O HETATM 2478 O HOH B 311 21.346 -0.136 -35.933 1.00 59.39 E O HETATM 2479 O HOH B 312 19.322 -5.756 -37.872 1.00 91.68 E O HETATM 2480 O HOH B 313 25.906 4.744 -15.878 1.00 46.91 E O HETATM 2481 O HOH B 314 15.326 21.403 -4.785 1.00 68.12 E O HETATM 2482 O HOH B 315 32.187 -9.695 -37.298 1.00 72.56 E O HETATM 2483 O HOH B 316 24.944 7.325 -16.497 1.00 47.32 E O HETATM 2484 O HOH B 317 23.419 7.866 -20.846 1.00 43.43 E O HETATM 2485 O HOH B 318 19.897 -2.475 -35.590 1.00 52.55 E O HETATM 2486 O HOH B 319 21.946 0.219 -38.584 1.00 74.84 E O HETATM 2487 O HOH B 320 39.027 0.421 -20.952 1.00 58.77 E O HETATM 2488 O HOH B 321 36.995 6.441 -18.458 1.00 55.77 E O HETATM 2489 O HOH B 322 16.933 -14.049 -13.529 1.00 62.01 E O HETATM 2490 O HOH B 323 7.052 5.046 -22.213 1.00 62.21 E O HETATM 2491 O HOH B 324 20.655 7.182 -25.199 1.00 49.95 E O HETATM 2492 O HOH B 325 33.165 5.684 -14.301 1.00 70.06 E O HETATM 2493 O HOH B 326 31.588 3.465 -15.003 1.00 64.46 E O HETATM 2494 O HOH B 327 33.760 1.991 -16.208 1.00 55.13 E O HETATM 2495 O HOH B 328 20.503 -10.458 -33.207 1.00 56.53 E O HETATM 2496 O HOH B 329 18.041 -9.340 -36.628 1.00 78.29 E O HETATM 2497 O HOH B 330 23.828 27.762 -5.500 1.00 84.46 E O HETATM 2498 O HOH B 331 42.728 6.289 -23.187 1.00 63.15 E O HETATM 2499 O HOH B 332 28.301 -4.541 -10.375 1.00 72.23 E O HETATM 2500 O HOH B 333 34.978 4.662 -16.280 1.00 63.23 E O HETATM 2501 O HOH B 334 17.165 -7.170 -37.334 1.00 66.97 E O HETATM 2502 O HOH B 335 35.617 8.780 -34.009 1.00 60.03 E O HETATM 2503 O HOH B 336 27.286 -2.082 -11.778 1.00 67.88 E O HETATM 2504 O HOH B 337 26.359 -4.679 -7.644 1.00 81.40 E O HETATM 2505 O HOH B 338 -1.425 17.692 -9.248 1.00 69.00 E O HETATM 2506 O HOH B 339 11.595 0.883 -22.452 1.00 60.34 E O HETATM 2507 O HOH B 340 9.551 -2.520 -22.159 1.00 65.65 E O HETATM 2508 O HOH B 341 9.006 -1.181 -15.274 1.00 75.09 E O HETATM 2509 O HOH B 342 11.097 -1.256 -23.709 1.00 73.43 E O HETATM 2510 O HOH B 343 7.807 -4.669 -22.683 1.00 60.40 E O HETATM 2511 O HOH B 344 7.954 -9.188 -29.767 1.00 63.18 E O HETATM 2512 O HOH B 345 36.827 -4.174 -11.011 1.00 47.54 E O 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 CONECT 2366 2367 CONECT 2367 2366 2368 2370 2372 CONECT 2368 2367 2369 CONECT 2369 2368 CONECT 2370 2367 2371 CONECT 2371 2370 CONECT 2372 2367 2373 CONECT 2373 2372 END A second structure was input as follows:CRYST1 173.249 173.249 99.241 90.00 90.00 120.00 H 3 9 ATOM 1 N ASP A 6 37.845 -7.152 -44.022 1.00181.97 A N ANISOU 1 N ASP A 6 21825 26992 20322 1019 797 -1354 A N ATOM 2 CA ASP A 6 37.841 -5.896 -43.274 1.00181.21 A C ANISOU 2 CA ASP A 6 21729 26814 20307 954 808 -1106 A C ATOM 3 C ASP A 6 38.294 -6.078 -41.823 1.00174.48 A C ANISOU 3 C ASP A 6 20882 25712 19702 920 799 -1080 A C ATOM 4 O ASP A 6 38.202 -7.173 -41.262 1.00173.56 A O ANISOU 4 O ASP A 6 20785 25448 19711 936 751 -1238 A O ATOM 5 CB ASP A 6 36.465 -5.213 -43.342 1.00184.76 A C ANISOU 5 CB ASP A 6 22222 27270 20707 904 724 -1002 A C ATOM 6 CG ASP A 6 35.311 -6.166 -43.040 1.00187.14 A C ANISOU 6 CG ASP A 6 22574 27453 21079 892 605 -1168 A C ATOM 7 OD1 ASP A 6 35.565 -7.307 -42.597 1.00190.83 A O ANISOU 7 OD1 ASP A 6 23048 27795 21663 914 588 -1346 A O ATOM 8 OD2 ASP A 6 34.143 -5.768 -43.248 1.00182.49 A O1- ANISOU 8 OD2 ASP A 6 22010 26894 20432 861 531 -1116 A O1- ATOM 9 N SER A 7 38.789 -4.995 -41.229 1.00164.48 A N ANISOU 9 N SER A 7 19594 24399 18501 871 847 -878 A N ATOM 10 CA SER A 7 39.338 -5.024 -39.877 1.00152.50 A C ANISOU 10 CA SER A 7 18071 22674 17198 836 845 -835 A C ATOM 11 C SER A 7 38.524 -4.120 -38.964 1.00147.64 A C ANISOU 11 C SER A 7 17499 21914 16682 752 791 -674 A C ATOM 12 O SER A 7 37.872 -3.188 -39.437 1.00147.18 A O ANISOU 12 O SER A 7 17455 21939 16527 721 790 -546 A O ATOM 13 CB SER A 7 40.799 -4.565 -39.897 1.00144.79 A C ANISOU 13 CB SER A 7 17019 21766 16227 849 957 -754 A C ATOM 14 OG SER A 7 41.326 -4.451 -38.588 1.00138.10 A O ANISOU 14 OG SER A 7 16160 20737 15574 808 950 -696 A O ATOM 15 N VAL A 8 38.563 -4.392 -37.660 1.00144.59 A N ANISOU 15 N VAL A 8 17132 21316 16488 717 749 -677 A N ATOM 16 CA VAL A 8 37.799 -3.597 -36.692 1.00137.41 A C ANISOU 16 CA VAL A 8 16267 20256 15685 636 700 -539 A C ATOM 17 C VAL A 8 38.688 -2.691 -35.838 1.00121.66 A C ANISOU 17 C VAL A 8 14240 18193 13794 583 757 -388 A C ATOM 18 O VAL A 8 39.790 -3.076 -35.449 1.00106.52 A O ANISOU 18 O VAL A 8 12276 16254 11944 604 795 -429 A O ATOM 19 CB VAL A 8 36.949 -4.478 -35.740 1.00 98.06 A C ANISOU 19 CB VAL A 8 11343 15071 10844 622 601 -641 A C ATOM 20 CG1 VAL A 8 35.878 -3.636 -35.083 1.00 86.80 A C ANISOU 20 CG1 VAL A 8 9967 13534 9478 547 551 -511 A C ATOM 21 CG2 VAL A 8 36.319 -5.641 -36.487 1.00100.00 A C ANISOU 21 CG2 VAL A 8 11610 15364 11021 678 550 -835 A C ATOM 22 N GLU A 9 38.180 -1.494 -35.546 1.00116.32 A N ANISOU 22 N GLU A 9 13583 17480 13131 513 762 -219 A N ATOM 23 CA GLU A 9 38.852 -0.509 -34.696 1.00104.26 A C ANISOU 23 CA GLU A 9 12031 15876 11708 445 811 -74 A C ATOM 24 C GLU A 9 38.980 -1.023 -33.262 1.00 98.32 A C ANISOU 24 C GLU A 9 11299 14923 11134 416 756 -122 A C ATOM 25 O GLU A 9 38.020 -1.562 -32.712 1.00101.25 A O ANISOU 25 O GLU A 9 11732 15169 11570 409 673 -182 A O ATOM 26 CB GLU A 9 38.031 0.785 -34.708 1.00110.26 A C ANISOU 26 CB GLU A 9 12822 16619 12451 380 820 99 A C ATOM 27 CG GLU A 9 38.655 1.967 -33.997 1.00120.22 A C ANISOU 27 CG GLU A 9 14057 17814 13806 301 884 255 A C ATOM 28 CD GLU A 9 39.869 2.502 -34.725 1.00137.54 A C ANISOU 28 CD GLU A 9 16172 20161 15926 312 996 321 A C ATOM 29 OE1 GLU A 9 39.885 2.453 -35.976 1.00138.43 A O ANISOU 29 OE1 GLU A 9 16265 20452 15881 368 1036 317 A O ATOM 30 OE2 GLU A 9 40.808 2.971 -34.045 1.00147.26 A O1- ANISOU 30 OE2 GLU A 9 17358 21339 17255 263 1045 374 A O1- ATOM 31 N CYS A 10 40.153 -0.860 -32.650 1.00 98.72 A N ANISOU 31 N CYS A 10 11295 14949 11264 399 801 -94 A N ATOM 32 CA CYS A 10 40.366 -1.343 -31.275 1.00 93.62 A C ANISOU 32 CA CYS A 10 10662 14131 10777 377 747 -132 A C ATOM 33 C CYS A 10 41.483 -0.626 -30.503 1.00100.56 A C ANISOU 33 C CYS A 10 11481 14987 11741 323 796 -42 A C ATOM 34 O CYS A 10 42.572 -1.171 -30.312 1.00114.85 A O ANISOU 34 O CYS A 10 13227 16824 13586 361 816 -100 A O ATOM 35 CB CYS A 10 40.617 -2.853 -31.261 1.00 75.86 A C ANISOU 35 CB CYS A 10 8409 11860 8554 462 708 -305 A C ATOM 36 SG CYS A 10 40.362 -3.563 -29.638 1.00135.17 A S ANISOU 36 SG CYS A 10 15967 19146 16244 444 622 -347 A S ATOM 37 N PRO A 11 41.194 0.589 -30.034 1.00 91.61 A N ANISOU 37 N PRO A 11 10365 13799 10646 233 814 95 A N ATOM 38 CA PRO A 11 42.077 1.540 -29.361 1.00 84.32 A C ANISOU 38 CA PRO A 11 9388 12853 9797 157 865 195 A C ATOM 39 C PRO A 11 42.600 1.096 -28.002 1.00 83.63 A C ANISOU 39 C PRO A 11 9290 12645 9841 136 814 152 A C ATOM 40 O PRO A 11 43.670 1.571 -27.621 1.00 79.32 A O ANISOU 40 O PRO A 11 8671 12127 9342 97 857 193 A O ATOM 41 CB PRO A 11 41.169 2.754 -29.150 1.00 89.16 A C ANISOU 41 CB PRO A 11 10056 13395 10427 72 875 326 A C ATOM 42 CG PRO A 11 40.130 2.623 -30.163 1.00 96.95 A C ANISOU 42 CG PRO A 11 11090 14444 11302 117 862 322 A C ATOM 43 CD PRO A 11 39.858 1.160 -30.222 1.00100.36 A C ANISOU 43 CD PRO A 11 11546 14864 11722 198 788 161 A C ATOM 44 N PHE A 12 41.870 0.251 -27.273 1.00 81.61 A N ANISOU 44 N PHE A 12 9101 12263 9644 157 725 77 A N ATOM 45 CA PHE A 12 42.306 -0.127 -25.928 1.00 68.21 A C ANISOU 45 CA PHE A 12 7398 10454 8063 138 674 52 A C ATOM 46 C PHE A 12 42.580 -1.612 -25.730 1.00 74.33 A C ANISOU 46 C PHE A 12 8167 11204 8869 233 623 -76 A C ATOM 47 O PHE A 12 42.485 -2.129 -24.610 1.00 70.85 A O ANISOU 47 O PHE A 12 7755 10643 8520 232 560 -100 A O ATOM 48 CB PHE A 12 41.296 0.295 -24.894 1.00 66.30 A C ANISOU 48 CB PHE A 12 7241 10057 7895 66 621 101 A C ATOM 49 CG PHE A 12 40.754 1.653 -25.106 1.00 73.86 A C ANISOU 49 CG PHE A 12 8221 11010 8831 -17 667 218 A C ATOM 50 CD1 PHE A 12 41.590 2.721 -25.271 1.00 65.60 A C ANISOU 50 CD1 PHE A 12 7110 10034 7782 -76 745 306 A C ATOM 51 CD2 PHE A 12 39.393 1.870 -25.099 1.00 84.37 A C ANISOU 51 CD2 PHE A 12 9638 12260 10159 -38 636 245 A C ATOM 52 CE1 PHE A 12 41.076 3.977 -25.448 1.00 63.95 A C ANISOU 52 CE1 PHE A 12 6924 9806 7568 -151 794 420 A C ATOM 53 CE2 PHE A 12 38.881 3.129 -25.268 1.00 79.02 A C ANISOU 53 CE2 PHE A 12 8980 11571 9474 -108 682 361 A C ATOM 54 CZ PHE A 12 39.726 4.179 -25.443 1.00 70.19 A C ANISOU 54 CZ PHE A 12 7801 10514 8354 -163 763 450 A C ATOM 55 N CYS A 13 42.908 -2.308 -26.807 1.00 75.01 A N ANISOU 55 N CYS A 13 8218 11400 8880 319 653 -156 A N ATOM 56 CA CYS A 13 43.363 -3.676 -26.667 1.00 79.07 A C ANISOU 56 CA CYS A 13 8713 11895 9435 413 623 -277 A C ATOM 57 C CYS A 13 44.449 -3.835 -27.675 1.00 85.88 A C ANISOU 57 C CYS A 13 9483 12921 10226 475 698 -313 A C ATOM 58 O CYS A 13 44.208 -3.718 -28.878 1.00 88.75 A O ANISOU 58 O CYS A 13 9848 13397 10478 499 744 -333 A O ATOM 59 CB CYS A 13 42.257 -4.669 -26.955 1.00 81.30 A C ANISOU 59 CB CYS A 13 9075 12106 9707 466 570 -378 A C ATOM 60 SG CYS A 13 42.392 -6.151 -25.991 1.00 79.46 A S ANISOU 60 SG CYS A 13 8860 11733 9598 539 504 -480 A S ATOM 61 N ASP A 14 45.658 -4.061 -27.180 1.00 83.92 A N ANISOU 61 N ASP A 14 9151 12696 10041 498 713 -318 A N ATOM 62 CA ASP A 14 46.802 -4.148 -28.058 1.00 82.04 A C ANISOU 62 CA ASP A 14 8811 12614 9746 553 794 -345 A C ATOM 63 C ASP A 14 47.009 -5.599 -28.434 1.00 78.88 A C ANISOU 63 C ASP A 14 8403 12216 9354 675 784 -488 A C ATOM 64 O ASP A 14 46.693 -6.498 -27.655 1.00 78.75 A O ANISOU 64 O ASP A 14 8427 12067 9426 712 716 -546 A O ATOM 65 CB ASP A 14 48.042 -3.559 -27.391 1.00 90.85 A C ANISOU 65 CB ASP A 14 9825 13767 10928 511 822 -272 A C ATOM 66 CG ASP A 14 48.069 -2.041 -27.440 1.00100.52 A C ANISOU 66 CG ASP A 14 11034 15033 12125 395 871 -141 A C ATOM 67 OD1 ASP A 14 47.169 -1.431 -28.071 1.00 98.79 A O ANISOU 67 OD1 ASP A 14 10880 14825 11830 358 891 -96 A O ATOM 68 OD2 ASP A 14 49.004 -1.458 -26.850 1.00104.50 A O1- ANISOU 68 OD2 ASP A 14 11456 15560 12688 342 892 -82 A O1- ATOM 69 N GLU A 15 47.510 -5.829 -29.641 1.00 79.02 A N ANISOU 69 N GLU A 15 8368 12378 9277 738 859 -547 A N ATOM 70 CA GLU A 15 47.823 -7.181 -30.053 1.00 81.00 A C ANISOU 70 CA GLU A 15 8601 12636 9538 856 865 -693 A C ATOM 71 C GLU A 15 49.062 -7.612 -29.286 1.00 79.44 A C ANISOU 71 C GLU A 15 8310 12424 9451 901 869 -693 A C ATOM 72 O GLU A 15 50.088 -6.919 -29.279 1.00 73.26 A O ANISOU 72 O GLU A 15 7429 11741 8667 874 923 -620 A O ATOM 73 CB GLU A 15 48.058 -7.255 -31.556 1.00 93.14 A C ANISOU 73 CB GLU A 15 10106 14346 10936 909 951 -758 A C ATOM 74 CG GLU A 15 47.371 -6.157 -32.338 1.00108.01 A C ANISOU 74 CG GLU A 15 12028 16322 12688 837 980 -674 A C ATOM 75 CD GLU A 15 47.499 -6.350 -33.835 1.00127.04 A C ANISOU 75 CD GLU A 15 14417 18909 14944 899 1057 -748 A C ATOM 76 OE1 GLU A 15 48.455 -7.030 -34.266 1.00131.78 A O ANISOU 76 OE1 GLU A 15 14944 19586 15539 982 1115 -835 A O ATOM 77 OE2 GLU A 15 46.642 -5.827 -34.579 1.00135.92 A O1- ANISOU 77 OE2 GLU A 15 15595 20098 15948 867 1060 -718 A O1- ATOM 78 N VAL A 16 48.940 -8.754 -28.622 1.00 77.38 A N ANISOU 78 N VAL A 16 8076 12035 9291 970 810 -771 A N ATOM 79 CA VAL A 16 49.997 -9.316 -27.793 1.00 74.00 A C ANISOU 79 CA VAL A 16 7566 11575 8977 1027 798 -771 A C ATOM 80 C VAL A 16 51.311 -9.557 -28.562 1.00 75.28 A C ANISOU 80 C VAL A 16 7601 11888 9113 1107 889 -814 A C ATOM 81 O VAL A 16 52.321 -9.941 -27.987 1.00 79.66 A O ANISOU 81 O VAL A 16 8066 12444 9756 1159 888 -807 A O ATOM 82 CB VAL A 16 49.527 -10.641 -27.208 1.00 62.72 A C ANISOU 82 CB VAL A 16 6197 9986 7649 1107 735 -859 A C ATOM 83 CG1 VAL A 16 49.652 -11.726 -28.260 1.00 70.41 A C ANISOU 83 CG1 VAL A 16 7161 10996 8594 1220 789 -1011 A C ATOM 84 CG2 VAL A 16 50.325 -11.001 -25.997 1.00 60.09 A C ANISOU 84 CG2 VAL A 16 5804 9586 7440 1139 693 -811 A C ATOM 85 N SER A 17 51.298 -9.331 -29.865 1.00 70.74 A N ANISOU 85 N SER A 17 7018 11447 8415 1119 968 -858 A N ATOM 86 CA SER A 17 52.493 -9.516 -30.671 1.00 71.99 A C ANISOU 86 CA SER A 17 7059 11757 8537 1192 1066 -900 A C ATOM 87 C SER A 17 53.543 -8.474 -30.324 1.00 73.38 A C ANISOU 87 C SER A 17 7123 12028 8731 1127 1104 -774 A C ATOM 88 O SER A 17 54.625 -8.463 -30.905 1.00 73.43 A O ANISOU 88 O SER A 17 7016 12168 8717 1173 1190 -787 A O ATOM 89 CB SER A 17 52.144 -9.401 -32.157 1.00 84.12 A C ANISOU 89 CB SER A 17 8620 13426 9915 1208 1142 -965 A C ATOM 90 OG SER A 17 51.683 -8.095 -32.503 1.00 80.88 A O ANISOU 90 OG SER A 17 8239 13089 9404 1099 1160 -850 A O ATOM 91 N LYS A 18 53.219 -7.583 -29.393 1.00 66.91 A N ANISOU 91 N LYS A 18 6331 11140 7952 1016 1045 -657 A N ATOM 92 CA LYS A 18 54.128 -6.496 -29.067 1.00 74.51 A C ANISOU 92 CA LYS A 18 7191 12186 8933 935 1081 -543 A C ATOM 93 C LYS A 18 55.089 -6.980 -28.016 1.00 79.10 A C ANISOU 93 C LYS A 18 7679 12732 9643 975 1037 -538 A C ATOM 94 O LYS A 18 56.040 -6.281 -27.651 1.00 83.82 A O ANISOU 94 O LYS A 18 8166 13404 10278 922 1060 -463 A O ATOM 95 CB LYS A 18 53.372 -5.255 -28.583 1.00 87.75 A C ANISOU 95 CB LYS A 18 8935 13809 10595 793 1046 -426 A C ATOM 96 CG LYS A 18 52.811 -5.316 -27.166 1.00 79.34 A C ANISOU 96 CG LYS A 18 7936 12580 9629 745 933 -393 A C ATOM 97 CD LYS A 18 52.330 -3.938 -26.778 1.00 70.67 A C ANISOU 97 CD LYS A 18 6876 11456 8518 602 926 -276 A C ATOM 98 CE LYS A 18 51.864 -3.885 -25.355 1.00 73.45 A C ANISOU 98 CE LYS A 18 7285 11662 8961 546 824 -240 A C ATOM 99 NZ LYS A 18 50.588 -3.114 -25.243 1.00 72.59 A N1+ ANISOU 99 NZ LYS A 18 7296 11467 8819 452 800 -184 A N1+ ATOM 100 N TYR A 19 54.811 -8.188 -27.534 1.00 76.99 A N ANISOU 100 N TYR A 19 7456 12350 9447 1067 974 -617 A N ATOM 101 CA TYR A 19 55.715 -8.931 -26.672 1.00 74.21 A C ANISOU 101 CA TYR A 19 7016 11968 9213 1144 935 -627 A C ATOM 102 C TYR A 19 56.291 -10.088 -27.459 1.00 83.57 A C ANISOU 102 C TYR A 19 8147 13199 10407 1292 998 -744 A C ATOM 103 O TYR A 19 55.663 -10.599 -28.383 1.00 92.45 A O ANISOU 103 O TYR A 19 9345 14318 11466 1340 1035 -840 A O ATOM 104 CB TYR A 19 54.970 -9.455 -25.449 1.00 67.89 A C ANISOU 104 CB TYR A 19 6308 10990 8498 1143 820 -615 A C ATOM 105 CG TYR A 19 54.368 -8.342 -24.643 1.00 74.70 A C ANISOU 105 CG TYR A 19 7229 11803 9352 1000 762 -510 A C ATOM 106 CD1 TYR A 19 55.129 -7.640 -23.716 1.00 75.96 A C ANISOU 106 CD1 TYR A 19 7302 11998 9562 931 731 -421 A C ATOM 107 CD2 TYR A 19 53.056 -7.958 -24.834 1.00 74.35 A C ANISOU 107 CD2 TYR A 19 7319 11682 9250 931 742 -503 A C ATOM 108 CE1 TYR A 19 54.592 -6.607 -22.985 1.00 71.80 A C ANISOU 108 CE1 TYR A 19 6828 11423 9029 797 684 -336 A C ATOM 109 CE2 TYR A 19 52.512 -6.924 -24.109 1.00 79.66 A C ANISOU 109 CE2 TYR A 19 8043 12304 9921 803 698 -409 A C ATOM 110 CZ TYR A 19 53.281 -6.254 -23.187 1.00 78.20 A C ANISOU 110 CZ TYR A 19 7777 12148 9787 736 672 -330 A C ATOM 111 OH TYR A 19 52.734 -5.226 -22.467 1.00 79.41 A O ANISOU 111 OH TYR A 19 7984 12247 9941 607 634 -249 A O ATOM 112 N GLU A 20 57.500 -10.485 -27.104 1.00 86.52 A N ANISOU 112 N GLU A 20 8388 13624 10863 1364 1012 -740 A N ATOM 113 CA GLU A 20 58.110 -11.652 -27.696 1.00 88.60 A C ANISOU 113 CA GLU A 20 8593 13913 11160 1515 1069 -850 A C ATOM 114 C GLU A 20 58.137 -12.699 -26.607 1.00 91.19 A C ANISOU 114 C GLU A 20 8930 14096 11622 1601 984 -860 A C ATOM 115 O GLU A 20 58.683 -12.457 -25.526 1.00 90.31 A O ANISOU 115 O GLU A 20 8751 13976 11586 1578 921 -770 A O ATOM 116 CB GLU A 20 59.525 -11.317 -28.149 1.00102.19 A C ANISOU 116 CB GLU A 20 10141 15808 12880 1542 1159 -829 A C ATOM 117 CG GLU A 20 60.232 -12.438 -28.882 1.00127.78 A C ANISOU 117 CG GLU A 20 13309 19093 16148 1700 1239 -946 A C ATOM 118 CD GLU A 20 61.376 -11.932 -29.741 1.00144.36 A C ANISOU 118 CD GLU A 20 15262 21389 18198 1708 1359 -938 A C ATOM 119 OE1 GLU A 20 62.064 -10.974 -29.308 1.00143.51 A O ANISOU 119 OE1 GLU A 20 15054 21367 18108 1621 1357 -829 A O ATOM 120 OE2 GLU A 20 61.574 -12.488 -30.849 1.00147.65 A O1- ANISOU 120 OE2 GLU A 20 15664 21875 18560 1797 1458 -1045 A O1- ATOM 121 N LYS A 21 57.525 -13.851 -26.862 1.00 87.60 A N ANISOU 121 N LYS A 21 8560 13526 11198 1698 981 -968 A N ATOM 122 CA LYS A 21 57.576 -14.934 -25.885 1.00 85.61 A C ANISOU 122 CA LYS A 21 8315 13129 11084 1794 913 -974 A C ATOM 123 C LYS A 21 59.018 -15.400 -25.618 1.00 88.48 A C ANISOU 123 C LYS A 21 8513 13566 11540 1904 942 -958 A C ATOM 124 O LYS A 21 59.909 -15.280 -26.478 1.00 83.52 A O ANISOU 124 O LYS A 21 7774 13083 10876 1944 1037 -996 A O ATOM 125 CB LYS A 21 56.684 -16.096 -26.317 1.00 84.04 A C ANISOU 125 CB LYS A 21 8232 12790 10910 1876 921 -1103 A C ATOM 126 CG LYS A 21 55.198 -15.734 -26.385 1.00 91.84 A C ANISOU 126 CG LYS A 21 9380 13687 11827 1772 874 -1112 A C ATOM 127 CD LYS A 21 54.324 -16.995 -26.435 1.00 98.70 A C ANISOU 127 CD LYS A 21 10357 14381 12764 1850 857 -1226 A C ATOM 128 CE LYS A 21 52.833 -16.680 -26.594 1.00 94.90 A C ANISOU 128 CE LYS A 21 10024 13819 12214 1750 814 -1247 A C ATOM 129 NZ LYS A 21 52.431 -16.275 -27.983 1.00 89.88 A N1+ ANISOU 129 NZ LYS A 21 9416 13302 11432 1713 880 -1334 A N1+ ATOM 130 N LEU A 22 59.258 -15.912 -24.417 1.00 89.52 A N ANISOU 130 N LEU A 22 8622 13605 11787 1954 860 -895 A N ATOM 131 CA LEU A 22 60.612 -16.337 -24.060 1.00 87.45 A C ANISOU 131 CA LEU A 22 8194 13414 11618 2060 873 -864 A C ATOM 132 C LEU A 22 60.677 -17.725 -23.445 1.00 93.52 A C ANISOU 132 C LEU A 22 8971 14036 12525 2212 840 -887 A C ATOM 133 O LEU A 22 61.678 -18.422 -23.605 1.00100.14 A O ANISOU 133 O LEU A 22 9689 14917 13443 2345 888 -914 A O ATOM 134 CB LEU A 22 61.291 -15.329 -23.127 1.00 72.80 A C ANISOU 134 CB LEU A 22 6238 11659 9765 1966 808 -728 A C ATOM 135 CG LEU A 22 61.591 -13.979 -23.766 1.00 75.00 A C ANISOU 135 CG LEU A 22 6462 12100 9935 1834 864 -699 A C ATOM 136 CD1 LEU A 22 62.476 -13.144 -22.865 1.00 71.91 A C ANISOU 136 CD1 LEU A 22 5940 11811 9572 1759 809 -585 A C ATOM 137 CD2 LEU A 22 62.229 -14.169 -25.139 1.00 81.13 A C ANISOU 137 CD2 LEU A 22 7158 12997 10670 1903 998 -790 A C ATOM 138 N ALA A 23 59.624 -18.125 -22.739 1.00 82.03 A N ANISOU 138 N ALA A 23 7655 12408 11106 2196 762 -871 A N ATOM 139 CA ALA A 23 59.644 -19.414 -22.071 1.00 87.67 A C ANISOU 139 CA ALA A 23 8383 12969 11959 2336 731 -873 A C ATOM 140 C ALA A 23 58.343 -19.698 -21.347 1.00100.02 A C ANISOU 140 C ALA A 23 10114 14345 13546 2291 653 -851 A C ATOM 141 O ALA A 23 57.735 -18.794 -20.789 1.00112.63 A O ANISOU 141 O ALA A 23 11775 15944 15075 2155 584 -774 A O ATOM 142 CB ALA A 23 60.802 -19.464 -21.089 1.00 90.86 A C ANISOU 142 CB ALA A 23 8640 13441 12444 2399 680 -758 A C ATOM 143 N LYS A 24 57.921 -20.957 -21.357 1.00 97.77 A N ANISOU 143 N LYS A 24 9896 13891 13364 2405 670 -920 A N ATOM 144 CA LYS A 24 56.797 -21.391 -20.542 1.00 99.63 A C ANISOU 144 CA LYS A 24 10273 13933 13650 2382 599 -887 A C ATOM 145 C LYS A 24 57.223 -21.297 -19.079 1.00 95.25 A C ANISOU 145 C LYS A 24 9671 13368 13151 2393 502 -724 A C ATOM 146 O LYS A 24 58.408 -21.357 -18.783 1.00 96.37 A O ANISOU 146 O LYS A 24 9670 13613 13334 2470 499 -666 A O ATOM 147 CB LYS A 24 56.409 -22.830 -20.902 1.00112.87 A C ANISOU 147 CB LYS A 24 12011 15429 15445 2513 652 -1000 A C ATOM 148 CG LYS A 24 54.991 -23.241 -20.496 1.00131.44 A C ANISOU 148 CG LYS A 24 14531 17579 17831 2466 608 -1014 A C ATOM 149 CD LYS A 24 54.391 -24.250 -21.483 1.00146.21 A C ANISOU 149 CD LYS A 24 16475 19325 19754 2529 688 -1192 A C ATOM 150 CE LYS A 24 54.254 -23.657 -22.895 1.00149.39 A C ANISOU 150 CE LYS A 24 16878 19867 20017 2462 756 -1324 A C ATOM 151 NZ LYS A 24 53.881 -24.661 -23.946 1.00143.81 A N1+ ANISOU 151 NZ LYS A 24 16217 19073 19352 2535 841 -1516 A N1+ ATOM 152 N ILE A 25 56.276 -21.120 -18.161 1.00 98.62 A N ANISOU 152 N ILE A 25 10214 13684 13573 2316 420 -650 A N ATOM 153 CA ILE A 25 56.614 -21.151 -16.737 1.00103.05 A C ANISOU 153 CA ILE A 25 10742 14229 14182 2337 327 -499 A C ATOM 154 C ILE A 25 55.534 -21.783 -15.844 1.00107.63 A C ANISOU 154 C ILE A 25 11463 14604 14826 2342 273 -451 A C ATOM 155 O ILE A 25 55.819 -22.160 -14.703 1.00104.93 A O ANISOU 155 O ILE A 25 11099 14222 14546 2403 208 -333 A O ATOM 156 CB ILE A 25 57.067 -19.766 -16.197 1.00 82.36 A C ANISOU 156 CB ILE A 25 8053 11783 11456 2205 264 -401 A C ATOM 157 CG1 ILE A 25 55.889 -18.827 -15.970 1.00 74.28 A C ANISOU 157 CG1 ILE A 25 7164 10723 10337 2034 222 -383 A C ATOM 158 CG2 ILE A 25 58.070 -19.109 -17.136 1.00 82.86 A C ANISOU 158 CG2 ILE A 25 7980 12042 11460 2188 328 -449 A C ATOM 159 CD1 ILE A 25 56.335 -17.412 -15.697 1.00 69.68 A C ANISOU 159 CD1 ILE A 25 6513 10310 9652 1897 185 -317 A C ATOM 160 N GLY A 26 54.314 -21.916 -16.371 1.00108.72 A N ANISOU 160 N GLY A 26 11741 14618 14949 2283 301 -541 A N ATOM 161 CA GLY A 26 53.234 -22.621 -15.689 1.00119.08 A C ANISOU 161 CA GLY A 26 13188 15721 16336 2292 269 -515 A C ATOM 162 C GLY A 26 52.233 -23.170 -16.697 1.00134.89 A C ANISOU 162 C GLY A 26 15296 17596 18361 2285 335 -668 A C ATOM 163 O GLY A 26 52.350 -22.841 -17.882 1.00134.40 A O ANISOU 163 O GLY A 26 15207 17630 18229 2257 396 -784 A O ATOM 164 N GLN A 27 51.258 -23.992 -16.284 1.00145.42 A N ANISOU 164 N GLN A 27 16745 18722 19787 2306 328 -675 A N ATOM 165 CA GLN A 27 51.026 -24.463 -14.903 1.00141.68 A C ANISOU 165 CA GLN A 27 16314 18120 19396 2343 266 -536 A C ATOM 166 C GLN A 27 50.481 -23.404 -13.940 1.00133.90 A C ANISOU 166 C GLN A 27 15385 17178 18312 2203 180 -415 A C ATOM 167 O GLN A 27 49.320 -23.465 -13.523 1.00120.32 A O ANISOU 167 O GLN A 27 13789 15324 16604 2137 158 -400 A O ATOM 168 CB GLN A 27 52.252 -25.179 -14.312 1.00141.26 A C ANISOU 168 CB GLN A 27 16145 18084 19441 2503 263 -448 A C ATOM 169 CG GLN A 27 52.447 -26.605 -14.833 1.00149.07 A C ANISOU 169 CG GLN A 27 17125 18925 20589 2663 346 -539 A C ATOM 170 CD GLN A 27 53.505 -26.708 -15.924 1.00149.08 A C ANISOU 170 CD GLN A 27 17002 19053 20587 2742 420 -646 A C ATOM 171 NE2 GLN A 27 53.074 -27.040 -17.140 1.00145.18 A N ANISOU 171 NE2 GLN A 27 16550 18515 20099 2737 501 -824 A N ATOM 172 OE1 GLN A 27 54.696 -26.501 -15.673 1.00148.20 A O ANISOU 172 OE1 GLN A 27 16757 19084 20469 2807 405 -571 A O ATOM 173 N PHE A 30 46.533 -24.548 -14.368 1.00171.87 A N ANISOU 173 N PHE A 30 20581 21481 23241 2054 224 -601 A N ATOM 174 CA PHE A 30 45.844 -23.379 -14.921 1.00175.03 A C ANISOU 174 CA PHE A 30 21022 21981 23502 1901 208 -647 A C ATOM 175 C PHE A 30 46.668 -22.092 -14.788 1.00169.49 A C ANISOU 175 C PHE A 30 20236 21498 22665 1836 170 -570 A C ATOM 176 O PHE A 30 46.862 -21.571 -13.686 1.00167.02 A O ANISOU 176 O PHE A 30 19918 21221 22323 1801 109 -433 A O ATOM 177 CB PHE A 30 44.458 -23.211 -14.280 1.00174.69 A C ANISOU 177 CB PHE A 30 21106 21805 23465 1799 172 -605 A C ATOM 178 CG PHE A 30 43.719 -21.978 -14.733 1.00171.81 A C ANISOU 178 CG PHE A 30 20781 21534 22963 1646 152 -632 A C ATOM 179 CD1 PHE A 30 42.951 -21.246 -13.838 1.00169.60 A C ANISOU 179 CD1 PHE A 30 20572 21228 22639 1540 99 -530 A C ATOM 180 CD2 PHE A 30 43.799 -21.547 -16.051 1.00172.00 A C ANISOU 180 CD2 PHE A 30 20772 21676 22905 1614 190 -754 A C ATOM 181 CE1 PHE A 30 42.271 -20.112 -14.249 1.00171.53 A C ANISOU 181 CE1 PHE A 30 20852 21552 22770 1407 86 -549 A C ATOM 182 CE2 PHE A 30 43.124 -20.414 -16.472 1.00172.76 A C ANISOU 182 CE2 PHE A 30 20904 21858 22880 1482 174 -764 A C ATOM 183 CZ PHE A 30 42.358 -19.694 -15.569 1.00174.19 A C ANISOU 183 CZ PHE A 30 21154 22003 23029 1380 123 -661 A C ATOM 184 N GLY A 31 47.148 -21.584 -15.920 1.00159.57 A N ANISOU 184 N GLY A 31 18915 20389 21327 1818 211 -661 A N ATOM 185 CA GLY A 31 46.908 -22.211 -17.207 1.00153.90 A C ANISOU 185 CA GLY A 31 18206 19639 20630 1860 282 -828 A C ATOM 186 C GLY A 31 48.176 -22.363 -18.027 1.00145.35 A C ANISOU 186 C GLY A 31 17000 18693 19535 1951 338 -890 A C ATOM 187 O GLY A 31 49.042 -23.188 -17.703 1.00134.51 A O ANISOU 187 O GLY A 31 15558 17287 18262 2082 355 -867 A O ATOM 188 N GLU A 32 48.275 -21.569 -19.095 1.00144.01 A N ANISOU 188 N GLU A 32 16800 18676 19242 1887 371 -964 A N ATOM 189 CA GLU A 32 49.464 -21.539 -19.948 1.00137.60 A C ANISOU 189 CA GLU A 32 15867 18019 18396 1957 432 -1021 A C ATOM 190 C GLU A 32 50.163 -20.172 -19.862 1.00120.57 A C ANISOU 190 C GLU A 32 13630 16064 16118 1872 410 -926 A C ATOM 191 O GLU A 32 49.689 -19.187 -20.426 1.00112.93 A O ANISOU 191 O GLU A 32 12691 15185 15031 1758 414 -940 A O ATOM 192 CB GLU A 32 49.093 -21.861 -21.397 1.00141.59 A C ANISOU 192 CB GLU A 32 16395 18544 18859 1967 505 -1200 A C ATOM 193 CG GLU A 32 50.275 -22.281 -22.256 1.00151.69 A C ANISOU 193 CG GLU A 32 17560 19931 20144 2079 586 -1285 A C ATOM 194 CD GLU A 32 49.932 -22.349 -23.734 1.00161.01 A C ANISOU 194 CD GLU A 32 18760 21178 21240 2068 656 -1457 A C ATOM 195 OE1 GLU A 32 48.842 -21.867 -24.119 1.00161.51 A O ANISOU 195 OE1 GLU A 32 18914 21236 21218 1961 634 -1495 A O ATOM 196 OE2 GLU A 32 50.759 -22.877 -24.512 1.00162.24 A O1- ANISOU 196 OE2 GLU A 32 18838 21397 21410 2168 734 -1555 A O1- ATOM 197 N VAL A 33 51.309 -20.140 -19.180 1.00111.25 A N ANISOU 197 N VAL A 33 12342 14954 14975 1931 392 -832 A N ATOM 198 CA VAL A 33 51.925 -18.899 -18.702 1.00 92.96 A C ANISOU 198 CA VAL A 33 9952 12794 12573 1842 351 -718 A C ATOM 199 C VAL A 33 53.384 -18.713 -19.143 1.00 85.24 A C ANISOU 199 C VAL A 33 8814 11991 11582 1904 396 -719 A C ATOM 200 O VAL A 33 54.246 -19.495 -18.745 1.00 78.54 A O ANISOU 200 O VAL A 33 7883 11132 10829 2029 398 -695 A O ATOM 201 CB VAL A 33 51.894 -18.891 -17.166 1.00 80.70 A C ANISOU 201 CB VAL A 33 8417 11173 11072 1832 262 -578 A C ATOM 202 CG1 VAL A 33 52.328 -17.538 -16.605 1.00 73.29 A C ANISOU 202 CG1 VAL A 33 7424 10381 10042 1714 213 -474 A C ATOM 203 CG2 VAL A 33 50.515 -19.266 -16.689 1.00 76.79 A C ANISOU 203 CG2 VAL A 33 8074 10491 10612 1793 228 -577 A C ATOM 204 N PHE A 34 53.650 -17.662 -19.929 1.00 82.03 A N ANISOU 204 N PHE A 34 8361 11745 11061 1817 434 -736 A N ATOM 205 CA PHE A 34 54.977 -17.382 -20.489 1.00 82.67 A C ANISOU 205 CA PHE A 34 8288 12002 11120 1860 491 -744 A C ATOM 206 C PHE A 34 55.660 -16.153 -19.901 1.00 82.66 A C ANISOU 206 C PHE A 34 8199 12144 11064 1759 451 -628 A C ATOM 207 O PHE A 34 55.020 -15.148 -19.625 1.00 87.08 A O ANISOU 207 O PHE A 34 8823 12712 11552 1621 415 -576 A O ATOM 208 CB PHE A 34 54.889 -17.097 -21.990 1.00101.28 A C ANISOU 208 CB PHE A 34 10644 14454 13382 1840 585 -856 A C ATOM 209 CG PHE A 34 54.038 -18.057 -22.766 1.00122.37 A C ANISOU 209 CG PHE A 34 13415 17008 16072 1899 626 -993 A C ATOM 210 CD1 PHE A 34 54.614 -19.147 -23.412 1.00128.03 A C ANISOU 210 CD1 PHE A 34 14078 17711 16855 2042 698 -1101 A C ATOM 211 CD2 PHE A 34 52.669 -17.842 -22.895 1.00123.38 A C ANISOU 211 CD2 PHE A 34 13683 17044 16150 1809 598 -1021 A C ATOM 212 CE1 PHE A 34 53.837 -20.022 -24.145 1.00131.28 A C ANISOU 212 CE1 PHE A 34 14579 18016 17285 2089 738 -1243 A C ATOM 213 CE2 PHE A 34 51.883 -18.712 -23.624 1.00126.79 A C ANISOU 213 CE2 PHE A 34 14199 17376 16599 1855 632 -1157 A C ATOM 214 CZ PHE A 34 52.469 -19.806 -24.252 1.00133.95 A C ANISOU 214 CZ PHE A 34 15055 18268 17572 1993 702 -1273 A C ATOM 215 N LYS A 35 56.976 -16.220 -19.759 1.00 88.17 A N ANISOU 215 N LYS A 35 8743 12957 11800 1827 464 -595 A N ATOM 216 CA LYS A 35 57.774 -15.015 -19.622 1.00 79.54 A C ANISOU 216 CA LYS A 35 7540 12034 10648 1730 459 -524 A C ATOM 217 C LYS A 35 57.845 -14.403 -21.010 1.00 79.73 A C ANISOU 217 C LYS A 35 7543 12172 10578 1682 560 -595 A C ATOM 218 O LYS A 35 57.866 -15.118 -22.008 1.00 84.48 A O ANISOU 218 O LYS A 35 8148 12769 11182 1774 637 -699 A O ATOM 219 CB LYS A 35 59.180 -15.355 -19.146 1.00 75.49 A C ANISOU 219 CB LYS A 35 6855 11618 10209 1826 448 -477 A C ATOM 220 CG LYS A 35 60.063 -14.141 -18.885 1.00 83.11 A C ANISOU 220 CG LYS A 35 7693 12758 11128 1721 434 -404 A C ATOM 221 CD LYS A 35 61.549 -14.535 -18.798 1.00 85.91 A C ANISOU 221 CD LYS A 35 7853 13236 11553 1831 450 -386 A C ATOM 222 CE LYS A 35 62.392 -13.472 -18.084 1.00 87.28 A C ANISOU 222 CE LYS A 35 7898 13557 11708 1727 398 -296 A C ATOM 223 NZ LYS A 35 63.818 -13.886 -17.870 1.00 90.65 A N1+ ANISOU 223 NZ LYS A 35 8127 14106 12210 1835 398 -271 A N1+ ATOM 224 N ALA A 36 57.877 -13.083 -21.087 1.00 75.34 A N ANISOU 224 N ALA A 36 6968 11717 9939 1540 564 -541 A N ATOM 225 CA ALA A 36 58.013 -12.432 -22.379 1.00 73.36 A C ANISOU 225 CA ALA A 36 6690 11586 9595 1495 664 -588 A C ATOM 226 C ALA A 36 58.649 -11.052 -22.260 1.00 76.08 A C ANISOU 226 C ALA A 36 6942 12072 9893 1367 675 -504 A C ATOM 227 O ALA A 36 58.738 -10.470 -21.177 1.00 68.35 A O ANISOU 227 O ALA A 36 5948 11084 8938 1286 597 -419 A O ATOM 228 CB ALA A 36 56.674 -12.345 -23.079 1.00 71.48 A C ANISOU 228 CB ALA A 36 6609 11269 9280 1446 683 -645 A C ATOM 229 N ARG A 37 59.100 -10.539 -23.393 1.00 76.53 A N ANISOU 229 N ARG A 37 6935 12260 9882 1348 777 -532 A N ATOM 230 CA ARG A 37 59.831 -9.292 -23.414 1.00 67.70 A C ANISOU 230 CA ARG A 37 5711 11280 8733 1235 809 -458 A C ATOM 231 C ARG A 37 59.194 -8.311 -24.371 1.00 64.85 A C ANISOU 231 C ARG A 37 5419 10961 8261 1130 881 -452 A C ATOM 232 O ARG A 37 58.885 -8.646 -25.509 1.00 77.58 A O ANISOU 232 O ARG A 37 7072 12599 9806 1183 956 -523 A O ATOM 233 CB ARG A 37 61.270 -9.552 -23.841 1.00 68.98 A C ANISOU 233 CB ARG A 37 5690 11587 8934 1319 880 -476 A C ATOM 234 CG ARG A 37 61.825 -8.472 -24.723 1.00 62.38 A C ANISOU 234 CG ARG A 37 4769 10904 8028 1232 983 -451 A C ATOM 235 CD ARG A 37 63.173 -8.842 -25.198 1.00 61.74 A C ANISOU 235 CD ARG A 37 4512 10960 7987 1326 1060 -478 A C ATOM 236 NE ARG A 37 64.144 -7.863 -24.767 1.00 74.66 A N ANISOU 236 NE ARG A 37 6001 12713 9655 1229 1063 -398 A N ATOM 237 CZ ARG A 37 64.484 -6.809 -25.489 1.00 89.85 A C ANISOU 237 CZ ARG A 37 7867 14751 11521 1131 1157 -363 A C ATOM 238 NH1 ARG A 37 63.917 -6.616 -26.677 1.00 59.81 A N1+ ANISOU 238 NH1 ARG A 37 4145 10968 7614 1125 1252 -395 A N1+ ATOM 239 NH2 ARG A 37 65.389 -5.957 -25.021 1.00 90.00 A N ANISOU 239 NH2 ARG A 37 7745 14866 11586 1038 1157 -296 A N ATOM 240 N HIS A 38 59.009 -7.087 -23.909 1.00 59.50 A N ANISOU 240 N HIS A 38 4752 10294 7563 982 858 -366 A N ATOM 241 CA HIS A 38 58.389 -6.069 -24.731 1.00 69.99 A C ANISOU 241 CA HIS A 38 6144 11654 8793 878 924 -339 A C ATOM 242 C HIS A 38 59.350 -5.677 -25.835 1.00 78.93 A C ANISOU 242 C HIS A 38 7153 12955 9881 889 1048 -342 A C ATOM 243 O HIS A 38 60.453 -5.210 -25.572 1.00 82.23 A O ANISOU 243 O HIS A 38 7427 13472 10346 856 1072 -299 A O ATOM 244 CB HIS A 38 58.036 -4.855 -23.885 1.00 81.34 A C ANISOU 244 CB HIS A 38 7614 13051 10240 720 875 -244 A C ATOM 245 CG HIS A 38 57.353 -3.771 -24.648 1.00 84.06 A C ANISOU 245 CG HIS A 38 8028 13413 10498 615 941 -201 A C ATOM 246 CD2 HIS A 38 56.053 -3.404 -24.701 1.00 91.26 A C ANISOU 246 CD2 HIS A 38 9088 14225 11361 556 917 -182 A C ATOM 247 ND1 HIS A 38 58.031 -2.912 -25.483 1.00 89.78 A N ANISOU 247 ND1 HIS A 38 8661 14271 11181 563 1049 -161 A N ATOM 248 CE1 HIS A 38 57.176 -2.063 -26.022 1.00 99.87 A C ANISOU 248 CE1 HIS A 38 10031 15530 12386 480 1089 -114 A C ATOM 249 NE2 HIS A 38 55.967 -2.341 -25.567 1.00 99.06 A N ANISOU 249 NE2 HIS A 38 10073 15289 12278 476 1008 -128 A N ATOM 250 N ARG A 39 58.918 -5.858 -27.076 1.00 79.96 A N ANISOU 250 N ARG A 39 7338 13126 9917 932 1129 -394 A N ATOM 251 CA ARG A 39 59.809 -5.695 -28.217 1.00 74.78 A C ANISOU 251 CA ARG A 39 6571 12634 9207 968 1256 -410 A C ATOM 252 C ARG A 39 60.553 -4.372 -28.267 1.00 73.26 A C ANISOU 252 C ARG A 39 6272 12551 9013 847 1320 -309 A C ATOM 253 O ARG A 39 61.586 -4.275 -28.914 1.00 89.77 A O ANISOU 253 O ARG A 39 8231 14780 11097 877 1417 -312 A O ATOM 254 CB ARG A 39 59.072 -5.953 -29.545 1.00 78.16 A C ANISOU 254 CB ARG A 39 7092 13095 9509 1016 1328 -476 A C ATOM 255 CG ARG A 39 58.769 -7.429 -29.781 1.00 83.38 A C ANISOU 255 CG ARG A 39 7806 13692 10182 1163 1305 -608 A C ATOM 256 CD ARG A 39 58.424 -7.774 -31.217 1.00 85.09 A C ANISOU 256 CD ARG A 39 8068 13991 10272 1226 1395 -696 A C ATOM 257 NE ARG A 39 57.407 -8.819 -31.216 1.00100.99 A N ANISOU 257 NE ARG A 39 10209 15876 12285 1296 1332 -802 A N ATOM 258 CZ ARG A 39 57.668 -10.120 -31.170 1.00112.28 A C ANISOU 258 CZ ARG A 39 11624 17253 13783 1427 1324 -915 A C ATOM 259 NH1 ARG A 39 58.927 -10.538 -31.153 1.00122.98 A N1+ ANISOU 259 NH1 ARG A 39 12839 18681 15205 1509 1376 -934 A N1+ ATOM 260 NH2 ARG A 39 56.672 -11.003 -31.152 1.00102.71 A N ANISOU 260 NH2 ARG A 39 10533 15914 12580 1475 1269 -1009 A N ATOM 261 N LYS A 40 60.043 -3.353 -27.593 1.00 75.61 A N ANISOU 261 N LYS A 40 6622 12783 9324 709 1273 -223 A N ATOM 262 CA LYS A 40 60.601 -2.016 -27.764 1.00 80.27 A C ANISOU 262 CA LYS A 40 7127 13461 9910 581 1347 -129 A C ATOM 263 C LYS A 40 61.462 -1.533 -26.595 1.00 81.02 A C ANISOU 263 C LYS A 40 7105 13561 10118 501 1293 -82 A C ATOM 264 O LYS A 40 62.348 -0.699 -26.778 1.00 75.08 A O ANISOU 264 O LYS A 40 6226 12910 9389 426 1368 -29 A O ATOM 265 CB LYS A 40 59.488 -1.001 -28.064 1.00 74.65 A C ANISOU 265 CB LYS A 40 6545 12692 9126 471 1365 -60 A C ATOM 266 CG LYS A 40 58.931 -1.063 -29.491 1.00 69.08 A C ANISOU 266 CG LYS A 40 5908 12052 8287 521 1457 -77 A C ATOM 267 CD LYS A 40 58.113 0.182 -29.817 1.00 79.18 A C ANISOU 267 CD LYS A 40 7273 13307 9506 401 1495 24 A C ATOM 268 CE LYS A 40 57.846 0.310 -31.312 1.00 95.87 A C ANISOU 268 CE LYS A 40 9416 15533 11479 443 1605 31 A C ATOM 269 NZ LYS A 40 58.639 1.416 -31.943 1.00107.95 A N1+ ANISOU 269 NZ LYS A 40 10842 17185 12988 368 1737 132 A N1+ ATOM 270 N THR A 41 61.210 -2.072 -25.406 1.00 82.09 A N ANISOU 270 N THR A 41 7277 13591 10322 518 1166 -102 A N ATOM 271 CA THR A 41 61.799 -1.540 -24.184 1.00 76.87 A C ANISOU 271 CA THR A 41 6531 12925 9751 427 1094 -58 A C ATOM 272 C THR A 41 62.553 -2.592 -23.384 1.00 74.97 A C ANISOU 272 C THR A 41 6198 12697 9590 534 1011 -101 A C ATOM 273 O THR A 41 63.418 -2.279 -22.548 1.00 80.16 A O ANISOU 273 O THR A 41 6730 13407 10319 484 966 -74 A O ATOM 274 CB THR A 41 60.720 -0.886 -23.302 1.00 76.21 A C ANISOU 274 CB THR A 41 6584 12703 9669 311 1011 -15 A C ATOM 275 CG2 THR A 41 60.046 0.216 -24.078 1.00 76.24 A C ANISOU 275 CG2 THR A 41 6665 12697 9607 207 1098 40 A C ATOM 276 OG1 THR A 41 59.742 -1.859 -22.900 1.00 73.98 A O ANISOU 276 OG1 THR A 41 6440 12294 9376 395 922 -60 A O ATOM 277 N GLY A 42 62.224 -3.843 -23.648 1.00 68.77 A N ANISOU 277 N GLY A 42 5472 11864 8793 682 991 -169 A N ATOM 278 CA GLY A 42 62.901 -4.934 -22.991 1.00 81.17 A C ANISOU 278 CA GLY A 42 6960 13439 10442 805 924 -204 A C ATOM 279 C GLY A 42 62.172 -5.326 -21.731 1.00 79.91 A C ANISOU 279 C GLY A 42 6904 13139 10319 803 787 -192 A C ATOM 280 O GLY A 42 62.430 -6.387 -21.157 1.00 78.43 A O ANISOU 280 O GLY A 42 6691 12917 10189 921 722 -216 A O ATOM 281 N GLN A 43 61.247 -4.479 -21.298 1.00 70.26 A N ANISOU 281 N GLN A 43 5798 11833 9064 672 750 -149 A N ATOM 282 CA GLN A 43 60.494 -4.806 -20.102 1.00 74.17 A C ANISOU 282 CA GLN A 43 6399 12196 9585 664 627 -136 A C ATOM 283 C GLN A 43 60.052 -6.263 -20.131 1.00 77.26 A C ANISOU 283 C GLN A 43 6865 12496 9996 824 592 -192 A C ATOM 284 O GLN A 43 59.424 -6.705 -21.088 1.00 75.44 A O ANISOU 284 O GLN A 43 6718 12225 9720 882 650 -245 A O ATOM 285 CB GLN A 43 59.280 -3.912 -19.970 1.00 77.44 A C ANISOU 285 CB GLN A 43 6964 12510 9949 534 617 -102 A C ATOM 286 CG GLN A 43 58.497 -4.185 -18.705 1.00 87.17 A C ANISOU 286 CG GLN A 43 8304 13610 11206 517 498 -86 A C ATOM 287 CD GLN A 43 57.114 -3.585 -18.758 1.00 91.59 A C ANISOU 287 CD GLN A 43 9032 14052 11716 426 497 -68 A C ATOM 288 NE2 GLN A 43 56.338 -3.775 -17.689 1.00 78.78 A N ANISOU 288 NE2 GLN A 43 7512 12309 10110 405 404 -53 A N ATOM 289 OE1 GLN A 43 56.743 -2.954 -19.754 1.00 95.17 A O ANISOU 289 OE1 GLN A 43 9520 14525 12116 378 583 -64 A O ATOM 290 N LYS A 44 60.397 -7.017 -19.095 1.00 77.44 A N ANISOU 290 N LYS A 44 6852 12487 10087 897 500 -182 A N ATOM 291 CA LYS A 44 59.917 -8.388 -18.992 1.00 77.71 A C ANISOU 291 CA LYS A 44 6964 12408 10154 1043 465 -226 A C ATOM 292 C LYS A 44 58.510 -8.424 -18.388 1.00 82.31 A C ANISOU 292 C LYS A 44 7731 12826 10717 995 398 -213 A C ATOM 293 O LYS A 44 58.159 -7.607 -17.529 1.00 84.54 A O ANISOU 293 O LYS A 44 8053 13082 10985 874 338 -156 A O ATOM 294 CB LYS A 44 60.873 -9.220 -18.151 1.00 68.47 A C ANISOU 294 CB LYS A 44 5676 11271 9069 1154 400 -206 A C ATOM 295 CG LYS A 44 62.314 -9.041 -18.552 1.00 69.48 A C ANISOU 295 CG LYS A 44 5604 11572 9225 1184 455 -206 A C ATOM 296 CD LYS A 44 62.681 -9.743 -19.847 1.00 65.56 A C ANISOU 296 CD LYS A 44 5064 11117 8730 1306 567 -283 A C ATOM 297 CE LYS A 44 64.186 -9.647 -20.085 1.00 82.57 A C ANISOU 297 CE LYS A 44 7003 13442 10927 1347 615 -275 A C ATOM 298 NZ LYS A 44 64.766 -8.294 -19.776 1.00 87.33 A N1+ ANISOU 298 NZ LYS A 44 7505 14164 11512 1187 611 -215 A N1+ ATOM 299 N VAL A 45 57.706 -9.378 -18.842 1.00 73.49 A N ANISOU 299 N VAL A 45 6724 11597 9602 1087 411 -272 A N ATOM 300 CA VAL A 45 56.343 -9.512 -18.359 1.00 68.09 A C ANISOU 300 CA VAL A 45 6211 10754 8907 1050 355 -266 A C ATOM 301 C VAL A 45 55.983 -10.985 -18.268 1.00 69.98 A C ANISOU 301 C VAL A 45 6509 10872 9209 1197 334 -316 A C ATOM 302 O VAL A 45 56.700 -11.836 -18.776 1.00 78.85 A O ANISOU 302 O VAL A 45 7553 12033 10376 1324 376 -366 A O ATOM 303 CB VAL A 45 55.336 -8.817 -19.309 1.00 63.65 A C ANISOU 303 CB VAL A 45 5755 10168 8261 963 415 -293 A C ATOM 304 CG1 VAL A 45 55.668 -7.336 -19.487 1.00 56.06 A C ANISOU 304 CG1 VAL A 45 4739 9315 7247 819 452 -238 A C ATOM 305 CG2 VAL A 45 55.332 -9.498 -20.642 1.00 62.35 A C ANISOU 305 CG2 VAL A 45 5590 10030 8071 1060 500 -384 A C ATOM 306 N ALA A 46 54.871 -11.286 -17.613 1.00 70.40 A N ANISOU 306 N ALA A 46 6700 10773 9275 1180 274 -302 A N ATOM 307 CA ALA A 46 54.300 -12.624 -17.666 1.00 68.29 A C ANISOU 307 CA ALA A 46 6513 10367 9069 1302 268 -358 A C ATOM 308 C ALA A 46 52.966 -12.526 -18.391 1.00 70.60 A C ANISOU 308 C ALA A 46 6947 10568 9311 1250 298 -416 A C ATOM 309 O ALA A 46 52.209 -11.587 -18.156 1.00 77.85 A O ANISOU 309 O ALA A 46 7939 11466 10174 1124 276 -375 A O ATOM 310 CB ALA A 46 54.105 -13.183 -16.261 1.00 59.50 A C ANISOU 310 CB ALA A 46 5438 9146 8023 1336 175 -288 A C ATOM 311 N LEU A 47 52.691 -13.477 -19.282 1.00 63.96 A N ANISOU 311 N LEU A 47 6137 9675 8488 1347 349 -517 A N ATOM 312 CA LEU A 47 51.411 -13.531 -19.984 1.00 60.21 A C ANISOU 312 CA LEU A 47 5791 9118 7969 1309 370 -585 A C ATOM 313 C LEU A 47 50.660 -14.805 -19.628 1.00 73.38 A C ANISOU 313 C LEU A 47 7551 10603 9726 1393 341 -633 A C ATOM 314 O LEU A 47 51.163 -15.900 -19.852 1.00 79.38 A O ANISOU 314 O LEU A 47 8269 11332 10559 1522 369 -695 A O ATOM 315 CB LEU A 47 51.617 -13.524 -21.498 1.00 54.83 A C ANISOU 315 CB LEU A 47 5075 8540 7218 1337 462 -683 A C ATOM 316 CG LEU A 47 52.623 -12.575 -22.128 1.00 62.92 A C ANISOU 316 CG LEU A 47 5981 9755 8170 1297 522 -656 A C ATOM 317 CD1 LEU A 47 52.988 -13.062 -23.505 1.00 70.52 A C ANISOU 317 CD1 LEU A 47 6901 10802 9091 1380 615 -768 A C ATOM 318 CD2 LEU A 47 52.078 -11.170 -22.198 1.00 75.02 A C ANISOU 318 CD2 LEU A 47 7555 11336 9613 1145 519 -587 A C ATOM 319 N LYS A 48 49.457 -14.660 -19.081 1.00 74.79 A N ANISOU 319 N LYS A 48 7853 10659 9906 1321 291 -606 A N ATOM 320 CA LYS A 48 48.541 -15.780 -18.912 1.00 72.38 A C ANISOU 320 CA LYS A 48 7647 10175 9680 1380 276 -661 A C ATOM 321 C LYS A 48 47.576 -15.779 -20.084 1.00 73.74 A C ANISOU 321 C LYS A 48 7893 10332 9793 1347 317 -770 A C ATOM 322 O LYS A 48 46.811 -14.833 -20.261 1.00 79.22 A O ANISOU 322 O LYS A 48 8644 11051 10407 1233 306 -744 A O ATOM 323 CB LYS A 48 47.732 -15.622 -17.624 1.00 77.95 A C ANISOU 323 CB LYS A 48 8442 10755 10419 1317 201 -568 A C ATOM 324 CG LYS A 48 48.252 -16.390 -16.427 1.00 92.09 A C ANISOU 324 CG LYS A 48 10208 12472 12309 1401 154 -495 A C ATOM 325 CD LYS A 48 47.326 -16.186 -15.224 1.00107.74 A C ANISOU 325 CD LYS A 48 12291 14337 14307 1330 88 -406 A C ATOM 326 CE LYS A 48 47.774 -16.987 -13.998 1.00117.19 A C ANISOU 326 CE LYS A 48 13472 15461 15594 1419 40 -322 A C ATOM 327 NZ LYS A 48 46.846 -16.787 -12.842 1.00123.27 A N1+ ANISOU 327 NZ LYS A 48 14345 16123 16369 1349 -17 -237 A N1+ ATOM 328 N LYS A 49 47.600 -16.827 -20.893 1.00 71.45 A N ANISOU 328 N LYS A 49 7600 10004 9542 1446 365 -894 A N ATOM 329 CA LYS A 49 46.578 -16.986 -21.919 1.00 79.43 A C ANISOU 329 CA LYS A 49 8688 10988 10502 1418 393 -1009 A C ATOM 330 C LYS A 49 45.263 -17.324 -21.228 1.00 76.29 A C ANISOU 330 C LYS A 49 8411 10408 10166 1374 338 -997 A C ATOM 331 O LYS A 49 45.262 -18.036 -20.227 1.00 81.57 A O ANISOU 331 O LYS A 49 9101 10944 10947 1423 306 -953 A O ATOM 332 CB LYS A 49 46.971 -18.115 -22.869 1.00 88.80 A C ANISOU 332 CB LYS A 49 9840 12171 11727 1539 458 -1158 A C ATOM 333 CG LYS A 49 46.207 -18.181 -24.177 1.00 89.94 A C ANISOU 333 CG LYS A 49 10034 12353 11788 1515 497 -1296 A C ATOM 334 CD LYS A 49 46.839 -19.235 -25.079 1.00104.78 A C ANISOU 334 CD LYS A 49 11861 14251 13700 1639 570 -1445 A C ATOM 335 CE LYS A 49 46.461 -19.055 -26.543 1.00111.28 A C ANISOU 335 CE LYS A 49 12696 15192 14392 1617 620 -1576 A C ATOM 336 NZ LYS A 49 47.438 -19.746 -27.441 1.00113.53 A N1+ ANISOU 336 NZ LYS A 49 12900 15560 14676 1731 706 -1698 A N1+ ATOM 337 N VAL A 50 44.151 -16.796 -21.734 1.00 77.32 A N ANISOU 337 N VAL A 50 8617 10537 10223 1283 329 -1028 A N ATOM 338 CA VAL A 50 42.832 -17.252 -21.289 1.00 85.07 A C ANISOU 338 CA VAL A 50 9708 11346 11268 1248 289 -1045 A C ATOM 339 C VAL A 50 42.347 -18.414 -22.149 1.00 97.85 A C ANISOU 339 C VAL A 50 11358 12887 12934 1314 323 -1212 A C ATOM 340 O VAL A 50 42.131 -18.266 -23.370 1.00 90.54 A O ANISOU 340 O VAL A 50 10425 12060 11916 1302 357 -1317 A O ATOM 341 CB VAL A 50 41.754 -16.144 -21.291 1.00 68.54 A C ANISOU 341 CB VAL A 50 7681 9271 9089 1115 257 -991 A C ATOM 342 CG1 VAL A 50 40.370 -16.770 -21.146 1.00 49.54 A C ANISOU 342 CG1 VAL A 50 5375 6699 6747 1091 229 -1047 A C ATOM 343 CG2 VAL A 50 41.983 -15.191 -20.151 1.00 67.32 A C ANISOU 343 CG2 VAL A 50 7523 9129 8927 1045 217 -835 A C ATOM 344 N LEU A 51 42.163 -19.553 -21.480 1.00105.24 A N ANISOU 344 N LEU A 51 12328 13644 14014 1381 314 -1232 A N ATOM 345 CA LEU A 51 41.872 -20.827 -22.121 1.00124.73 A C ANISOU 345 CA LEU A 51 14817 16008 16565 1458 352 -1392 A C ATOM 346 C LEU A 51 40.409 -20.936 -22.548 1.00129.19 A C ANISOU 346 C LEU A 51 15472 16494 17121 1381 333 -1480 A C ATOM 347 O LEU A 51 39.527 -21.146 -21.714 1.00122.83 A O ANISOU 347 O LEU A 51 14737 15534 16397 1340 294 -1430 A O ATOM 348 CB LEU A 51 42.218 -21.963 -21.159 1.00135.66 A C ANISOU 348 CB LEU A 51 16205 17219 18121 1556 354 -1360 A C ATOM 349 CG LEU A 51 43.048 -21.596 -19.922 1.00140.09 A C ANISOU 349 CG LEU A 51 16724 17796 18709 1577 319 -1184 A C ATOM 350 CD1 LEU A 51 42.947 -22.705 -18.894 1.00139.49 A C ANISOU 350 CD1 LEU A 51 16683 17519 18799 1654 310 -1139 A C ATOM 351 CD2 LEU A 51 44.514 -21.317 -20.269 1.00144.41 A C ANISOU 351 CD2 LEU A 51 17151 18513 19206 1644 352 -1167 A C ATOM 352 N MET A 52 40.160 -20.797 -23.849 1.00135.93 A N ANISOU 352 N MET A 52 16316 17459 17872 1364 360 -1609 A N ATOM 353 CA MET A 52 38.802 -20.854 -24.391 1.00142.42 A C ANISOU 353 CA MET A 52 17208 18237 18668 1290 337 -1704 A C ATOM 354 C MET A 52 38.426 -22.274 -24.809 1.00152.74 A C ANISOU 354 C MET A 52 18540 19403 20091 1353 366 -1882 A C ATOM 355 O MET A 52 37.612 -22.481 -25.717 1.00151.58 A O ANISOU 355 O MET A 52 18420 19273 19899 1318 366 -2023 A O ATOM 356 CB MET A 52 38.660 -19.900 -25.576 1.00142.28 A C ANISOU 356 CB MET A 52 17166 18428 18464 1234 344 -1743 A C ATOM 357 CG MET A 52 38.850 -18.440 -25.206 1.00146.08 A C ANISOU 357 CG MET A 52 17633 19031 18842 1156 319 -1571 A C ATOM 358 SD MET A 52 37.371 -17.696 -24.489 1.00167.72 A S ANISOU 358 SD MET A 52 20461 21682 21585 1030 249 -1470 A S ATOM 359 CE MET A 52 36.503 -17.160 -25.974 1.00 92.47 A C ANISOU 359 CE MET A 52 10938 12302 11895 972 248 -1570 A C ATOM 360 N GLU A 53 39.032 -23.250 -24.139 1.00158.78 A N ANISOU 360 N GLU A 53 19293 20028 21007 1448 393 -1874 A N ATOM 361 CA GLU A 53 38.755 -24.653 -24.405 1.00162.01 A C ANISOU 361 CA GLU A 53 19726 20273 21558 1514 431 -2033 A C ATOM 362 C GLU A 53 37.714 -25.186 -23.442 1.00159.78 A C ANISOU 362 C GLU A 53 19523 19765 21421 1475 397 -1992 A C ATOM 363 O GLU A 53 37.824 -24.989 -22.227 1.00153.61 A O ANISOU 363 O GLU A 53 18759 18906 20700 1473 369 -1824 A O ATOM 364 CB GLU A 53 40.017 -25.490 -24.259 1.00165.70 A C ANISOU 364 CB GLU A 53 20132 20703 22125 1652 489 -2048 A C ATOM 365 CG GLU A 53 39.711 -26.966 -24.110 1.00169.79 A C ANISOU 365 CG GLU A 53 20685 20991 22838 1723 528 -2162 A C ATOM 366 CD GLU A 53 40.828 -27.728 -23.439 1.00170.53 A C ANISOU 366 CD GLU A 53 20731 20995 23069 1857 570 -2097 A C ATOM 367 OE1 GLU A 53 40.560 -28.826 -22.906 1.00167.65 A O ANISOU 367 OE1 GLU A 53 20402 20409 22887 1912 593 -2119 A O ATOM 368 OE2 GLU A 53 41.972 -27.224 -23.439 1.00171.72 A O1- ANISOU 368 OE2 GLU A 53 20803 21295 23148 1908 581 -2019 A O1- ATOM 369 N ASN A 54 36.721 -25.883 -23.987 1.00161.74 A N ANISOU 369 N ASN A 54 19817 19912 21725 1445 403 -2151 A N ATOM 370 CA ASN A 54 35.610 -26.378 -23.186 1.00161.67 A C ANISOU 370 CA ASN A 54 19881 19690 21854 1395 377 -2126 A C ATOM 371 C ASN A 54 34.783 -25.195 -22.675 1.00149.52 A C ANISOU 371 C ASN A 54 18381 18208 20222 1276 310 -1987 A C ATOM 372 O ASN A 54 34.087 -25.292 -21.659 1.00140.38 A O ANISOU 372 O ASN A 54 17278 16899 19160 1235 284 -1889 A O ATOM 373 CB ASN A 54 36.123 -27.238 -22.021 1.00163.33 A C ANISOU 373 CB ASN A 54 20101 19709 22248 1485 404 -2026 A C ATOM 374 CG ASN A 54 35.380 -28.562 -21.890 1.00161.73 A C ANISOU 374 CG ASN A 54 19948 19259 22241 1504 437 -2138 A C ATOM 375 ND2 ASN A 54 35.461 -29.172 -20.708 1.00155.76 A N ANISOU 375 ND2 ASN A 54 19221 18316 21644 1553 449 -2016 A N ATOM 376 OD1 ASN A 54 34.746 -29.032 -22.837 1.00161.93 A O ANISOU 376 OD1 ASN A 54 19984 19264 22276 1474 453 -2332 A O ATOM 377 N GLU A 55 34.875 -24.076 -23.390 1.00137.20 A N ANISOU 377 N GLU A 55 16790 16863 18475 1223 288 -1976 A N ATOM 378 CA GLU A 55 34.153 -22.866 -23.023 1.00122.84 A C ANISOU 378 CA GLU A 55 15001 15112 16561 1114 232 -1848 A C ATOM 379 C GLU A 55 33.023 -22.597 -24.004 1.00110.58 A C ANISOU 379 C GLU A 55 13467 13624 14923 1032 205 -1966 A C ATOM 380 O GLU A 55 33.218 -22.032 -25.080 1.00 98.51 A O ANISOU 380 O GLU A 55 11901 12287 13242 1021 208 -2028 A O ATOM 381 CB GLU A 55 35.101 -21.672 -22.932 1.00124.69 A C ANISOU 381 CB GLU A 55 15187 15532 16658 1111 226 -1712 A C ATOM 382 CG GLU A 55 36.058 -21.741 -21.751 1.00123.60 A C ANISOU 382 CG GLU A 55 15031 15337 16595 1169 231 -1565 A C ATOM 383 CD GLU A 55 35.338 -21.808 -20.416 1.00124.60 A C ANISOU 383 CD GLU A 55 15223 15293 16825 1126 197 -1443 A C ATOM 384 OE1 GLU A 55 34.094 -21.655 -20.395 1.00128.58 A O ANISOU 384 OE1 GLU A 55 15784 15732 17338 1043 169 -1460 A O ATOM 385 OE2 GLU A 55 36.019 -22.008 -19.385 1.00119.77 A O1- ANISOU 385 OE2 GLU A 55 14604 14621 16283 1178 197 -1327 A O1- ATOM 386 N LYS A 56 31.829 -23.007 -23.610 1.00112.83 A N ANISOU 386 N LYS A 56 13808 13753 15309 974 180 -1991 A N ATOM 387 CA LYS A 56 30.698 -23.013 -24.516 1.00114.89 A C ANISOU 387 CA LYS A 56 14081 14051 15522 904 152 -2127 A C ATOM 388 C LYS A 56 29.717 -21.914 -24.144 1.00 99.14 A C ANISOU 388 C LYS A 56 12115 12094 13462 799 97 -2003 A C ATOM 389 O LYS A 56 28.609 -21.841 -24.663 1.00 97.27 A O ANISOU 389 O LYS A 56 11890 11869 13200 730 63 -2082 A O ATOM 390 CB LYS A 56 30.042 -24.400 -24.500 1.00121.95 A C ANISOU 390 CB LYS A 56 15005 14740 16592 916 171 -2279 A C ATOM 391 CG LYS A 56 30.965 -25.499 -25.042 1.00125.60 A C ANISOU 391 CG LYS A 56 15436 15169 17119 1023 233 -2428 A C ATOM 392 CD LYS A 56 30.691 -26.859 -24.419 1.00130.50 A C ANISOU 392 CD LYS A 56 16091 15523 17970 1060 269 -2489 A C ATOM 393 CE LYS A 56 31.771 -27.862 -24.821 1.00135.83 A C ANISOU 393 CE LYS A 56 16732 16160 18717 1179 340 -2606 A C ATOM 394 NZ LYS A 56 31.566 -29.208 -24.208 1.00136.62 A N1+ ANISOU 394 NZ LYS A 56 16866 15988 19057 1225 386 -2656 A N1+ ATOM 395 N GLU A 57 30.155 -21.044 -23.251 1.00 87.72 A N ANISOU 395 N GLU A 57 10674 10671 11985 787 89 -1813 A N ATOM 396 CA GLU A 57 29.309 -19.982 -22.748 1.00 71.93 A C ANISOU 396 CA GLU A 57 8704 8687 9938 694 47 -1682 A C ATOM 397 C GLU A 57 29.939 -18.603 -22.962 1.00 75.72 A C ANISOU 397 C GLU A 57 9151 9364 10254 674 42 -1563 A C ATOM 398 O GLU A 57 29.822 -17.712 -22.116 1.00 62.69 A O ANISOU 398 O GLU A 57 7521 7707 8590 625 26 -1406 A O ATOM 399 CB GLU A 57 29.032 -20.230 -21.278 1.00 54.53 A C ANISOU 399 CB GLU A 57 6552 6291 7875 681 45 -1559 A C ATOM 400 CG GLU A 57 27.799 -21.064 -21.058 1.00 85.32 A C ANISOU 400 CG GLU A 57 10494 10011 11911 642 36 -1635 A C ATOM 401 CD GLU A 57 26.506 -20.283 -21.298 1.00107.86 A C ANISOU 401 CD GLU A 57 13363 12908 14709 539 -7 -1622 A C ATOM 402 OE1 GLU A 57 26.308 -19.210 -20.653 1.00104.00 A O ANISOU 402 OE1 GLU A 57 12892 12456 14167 488 -25 -1467 A O ATOM 403 OE2 GLU A 57 25.688 -20.760 -22.124 1.00109.60 A O1- ANISOU 403 OE2 GLU A 57 13575 13125 14943 511 -22 -1771 A O1- ATOM 404 N GLY A 58 30.593 -18.430 -24.107 1.00 77.75 A N ANISOU 404 N GLY A 58 9357 9797 10389 710 60 -1643 A N ATOM 405 CA GLY A 58 31.349 -17.221 -24.364 1.00 76.90 A C ANISOU 405 CA GLY A 58 9210 9871 10137 701 70 -1535 A C ATOM 406 C GLY A 58 32.526 -17.079 -23.410 1.00 84.98 A C ANISOU 406 C GLY A 58 10216 10869 11202 744 93 -1415 A C ATOM 407 O GLY A 58 32.917 -18.040 -22.728 1.00 88.20 A O ANISOU 407 O GLY A 58 10633 11140 11738 803 107 -1430 A O ATOM 408 N PHE A 59 33.083 -15.870 -23.370 1.00 80.23 A N ANISOU 408 N PHE A 59 9586 10403 10496 714 98 -1293 A N ATOM 409 CA PHE A 59 34.207 -15.519 -22.494 1.00 69.31 A C ANISOU 409 CA PHE A 59 8174 9028 9132 739 113 -1172 A C ATOM 410 C PHE A 59 33.972 -15.915 -21.025 1.00 65.26 A C ANISOU 410 C PHE A 59 7711 8331 8754 733 90 -1088 A C ATOM 411 O PHE A 59 32.984 -15.515 -20.407 1.00 60.40 A O ANISOU 411 O PHE A 59 7150 7633 8165 660 61 -1023 A O ATOM 412 CB PHE A 59 34.505 -14.018 -22.619 1.00 55.46 A C ANISOU 412 CB PHE A 59 6393 7424 7253 676 117 -1051 A C ATOM 413 CG PHE A 59 35.727 -13.584 -21.892 1.00 64.18 A C ANISOU 413 CG PHE A 59 7454 8569 8362 693 132 -945 A C ATOM 414 CD1 PHE A 59 36.965 -13.605 -22.521 1.00 62.55 A C ANISOU 414 CD1 PHE A 59 7171 8496 8100 754 173 -974 A C ATOM 415 CD2 PHE A 59 35.647 -13.160 -20.570 1.00 75.84 A C ANISOU 415 CD2 PHE A 59 8963 9956 9896 648 107 -821 A C ATOM 416 CE1 PHE A 59 38.103 -13.209 -21.852 1.00 59.26 A C ANISOU 416 CE1 PHE A 59 6703 8123 7692 768 184 -881 A C ATOM 417 CE2 PHE A 59 36.781 -12.758 -19.887 1.00 78.92 A C ANISOU 417 CE2 PHE A 59 9306 10395 10286 660 114 -731 A C ATOM 418 CZ PHE A 59 38.013 -12.786 -20.531 1.00 77.06 A C ANISOU 418 CZ PHE A 59 8986 10291 10001 719 150 -761 A C ATOM 419 N PRO A 60 34.896 -16.703 -20.462 1.00 61.11 A N ANISOU 419 N PRO A 60 7163 7745 8312 814 106 -1084 A N ATOM 420 CA PRO A 60 34.687 -17.407 -19.189 1.00 56.20 A C ANISOU 420 CA PRO A 60 6587 6940 7828 834 91 -1026 A C ATOM 421 C PRO A 60 34.398 -16.492 -18.030 1.00 62.35 A C ANISOU 421 C PRO A 60 7402 7691 8596 759 60 -870 A C ATOM 422 O PRO A 60 35.183 -15.600 -17.741 1.00 70.31 A O ANISOU 422 O PRO A 60 8371 8809 9533 740 58 -778 A O ATOM 423 CB PRO A 60 36.013 -18.102 -18.952 1.00 49.21 A C ANISOU 423 CB PRO A 60 5646 6059 6992 941 116 -1026 A C ATOM 424 CG PRO A 60 36.619 -18.232 -20.326 1.00 61.32 A C ANISOU 424 CG PRO A 60 7118 7731 8451 989 153 -1149 A C ATOM 425 CD PRO A 60 36.201 -17.015 -21.065 1.00 61.55 A C ANISOU 425 CD PRO A 60 7142 7908 8335 901 145 -1135 A C ATOM 426 N ILE A 61 33.282 -16.735 -17.361 1.00 61.88 A N ANISOU 426 N ILE A 61 7414 7485 8614 714 41 -846 A N ATOM 427 CA ILE A 61 32.881 -15.921 -16.225 1.00 64.71 A C ANISOU 427 CA ILE A 61 7815 7804 8967 641 17 -708 A C ATOM 428 C ILE A 61 33.999 -15.766 -15.166 1.00 67.14 A C ANISOU 428 C ILE A 61 8097 8132 9279 676 11 -596 A C ATOM 429 O ILE A 61 34.246 -14.672 -14.648 1.00 65.88 A O ANISOU 429 O ILE A 61 7932 8049 9050 616 -3 -497 A O ATOM 430 CB ILE A 61 31.557 -16.449 -15.619 1.00 58.89 A C ANISOU 430 CB ILE A 61 7156 6888 8333 604 7 -708 A C ATOM 431 CG1 ILE A 61 30.856 -15.350 -14.833 1.00 67.49 A C ANISOU 431 CG1 ILE A 61 8289 7969 9385 506 -11 -593 A C ATOM 432 CG2 ILE A 61 31.806 -17.645 -14.752 1.00 72.32 A C ANISOU 432 CG2 ILE A 61 8879 8436 10163 678 16 -692 A C ATOM 433 CD1 ILE A 61 29.405 -15.623 -14.601 1.00 79.11 A C ANISOU 433 CD1 ILE A 61 9824 9303 10930 453 -16 -609 A C ATOM 434 N THR A 62 34.704 -16.848 -14.876 1.00 67.31 A N ANISOU 434 N THR A 62 8099 8093 9384 775 20 -614 A N ATOM 435 CA THR A 62 35.732 -16.803 -13.849 1.00 70.15 A C ANISOU 435 CA THR A 62 8429 8475 9751 816 7 -506 A C ATOM 436 C THR A 62 36.870 -15.893 -14.261 1.00 67.40 A C ANISOU 436 C THR A 62 7997 8317 9294 811 8 -484 A C ATOM 437 O THR A 62 37.452 -15.219 -13.427 1.00 78.46 A O ANISOU 437 O THR A 62 9378 9777 10657 784 -14 -381 A O ATOM 438 CB THR A 62 36.278 -18.188 -13.582 1.00 71.76 A C ANISOU 438 CB THR A 62 8619 8578 10069 937 21 -530 A C ATOM 439 CG2 THR A 62 35.256 -18.991 -12.812 1.00 63.80 A C ANISOU 439 CG2 THR A 62 7695 7370 9177 936 21 -508 A C ATOM 440 OG1 THR A 62 36.511 -18.827 -14.837 1.00 75.59 A O ANISOU 440 OG1 THR A 62 9064 9089 10568 996 56 -671 A O ATOM 441 N ALA A 63 37.185 -15.878 -15.550 1.00 59.82 A N ANISOU 441 N ALA A 63 6988 7457 8285 833 37 -584 A N ATOM 442 CA ALA A 63 38.178 -14.947 -16.079 1.00 58.83 A C ANISOU 442 CA ALA A 63 6783 7517 8054 818 49 -566 A C ATOM 443 C ALA A 63 37.733 -13.511 -15.849 1.00 68.33 A C ANISOU 443 C ALA A 63 8008 8784 9171 698 35 -484 A C ATOM 444 O ALA A 63 38.562 -12.642 -15.577 1.00 68.40 A O ANISOU 444 O ALA A 63 7964 8903 9122 667 33 -414 A O ATOM 445 CB ALA A 63 38.427 -15.193 -17.584 1.00 48.71 A C ANISOU 445 CB ALA A 63 5454 6330 6725 860 90 -692 A C ATOM 446 N LEU A 64 36.423 -13.274 -15.963 1.00 64.59 A N ANISOU 446 N LEU A 64 7608 8237 8698 630 28 -496 A N ATOM 447 CA LEU A 64 35.849 -11.950 -15.752 1.00 60.17 A C ANISOU 447 CA LEU A 64 7076 7713 8071 519 21 -421 A C ATOM 448 C LEU A 64 35.970 -11.570 -14.300 1.00 60.05 A C ANISOU 448 C LEU A 64 7089 7646 8083 480 -6 -310 A C ATOM 449 O LEU A 64 36.286 -10.423 -13.968 1.00 64.10 A O ANISOU 449 O LEU A 64 7583 8236 8534 410 -6 -238 A O ATOM 450 CB LEU A 64 34.376 -11.929 -16.145 1.00 58.48 A C ANISOU 450 CB LEU A 64 6931 7421 7869 468 17 -460 A C ATOM 451 CG LEU A 64 34.093 -12.018 -17.640 1.00 64.61 A C ANISOU 451 CG LEU A 64 7682 8279 8588 482 37 -565 A C ATOM 452 CD1 LEU A 64 32.598 -12.156 -17.876 1.00 71.56 A C ANISOU 452 CD1 LEU A 64 8625 9068 9495 437 22 -605 A C ATOM 453 CD2 LEU A 64 34.664 -10.812 -18.367 1.00 52.64 A C ANISOU 453 CD2 LEU A 64 6111 6934 6954 443 61 -528 A C ATOM 454 N ARG A 65 35.686 -12.542 -13.439 1.00 49.78 A N ANISOU 454 N ARG A 65 5833 6210 6872 525 -24 -298 A N ATOM 455 CA ARG A 65 35.836 -12.384 -11.999 1.00 58.00 A C ANISOU 455 CA ARG A 65 6901 7201 7935 505 -52 -195 A C ATOM 456 C ARG A 65 37.256 -11.956 -11.654 1.00 65.18 A C ANISOU 456 C ARG A 65 7729 8240 8796 524 -63 -146 A C ATOM 457 O ARG A 65 37.468 -10.929 -11.011 1.00 62.27 A O ANISOU 457 O ARG A 65 7356 7929 8374 448 -76 -75 A O ATOM 458 CB ARG A 65 35.531 -13.716 -11.315 1.00 62.03 A C ANISOU 458 CB ARG A 65 7456 7558 8552 580 -61 -195 A C ATOM 459 CG ARG A 65 35.192 -13.633 -9.835 1.00 67.89 A C ANISOU 459 CG ARG A 65 8259 8218 9319 549 -85 -89 A C ATOM 460 CD ARG A 65 34.774 -15.010 -9.368 1.00 87.05 A C ANISOU 460 CD ARG A 65 10732 10483 11860 626 -81 -92 A C ATOM 461 NE ARG A 65 35.692 -15.999 -9.929 1.00111.27 A N ANISOU 461 NE ARG A 65 13736 13566 14974 741 -71 -149 A N ATOM 462 CZ ARG A 65 35.900 -17.207 -9.418 1.00119.01 A C ANISOU 462 CZ ARG A 65 14727 14439 16054 837 -67 -131 A C ATOM 463 NH1 ARG A 65 35.247 -17.585 -8.322 1.00120.18 A N1+ ANISOU 463 NH1 ARG A 65 14947 14458 16258 831 -74 -51 A N1+ ATOM 464 NH2 ARG A 65 36.764 -18.032 -10.001 1.00114.85 A N ANISOU 464 NH2 ARG A 65 14137 13931 15572 943 -52 -188 A N ATOM 465 N GLU A 66 38.221 -12.762 -12.096 1.00 70.57 A N ANISOU 465 N GLU A 66 8344 8967 9504 625 -56 -190 A N ATOM 466 CA GLU A 66 39.632 -12.529 -11.831 1.00 67.41 A C ANISOU 466 CA GLU A 66 7850 8691 9071 659 -67 -151 A C ATOM 467 C GLU A 66 40.051 -11.163 -12.325 1.00 66.46 A C ANISOU 467 C GLU A 66 7678 8717 8856 572 -51 -139 A C ATOM 468 O GLU A 66 40.626 -10.381 -11.585 1.00 78.95 A O ANISOU 468 O GLU A 66 9228 10368 10400 520 -72 -70 A O ATOM 469 CB GLU A 66 40.487 -13.603 -12.491 1.00 65.92 A C ANISOU 469 CB GLU A 66 7593 8526 8928 785 -48 -217 A C ATOM 470 CG GLU A 66 41.961 -13.476 -12.189 1.00 75.89 A C ANISOU 470 CG GLU A 66 8748 9915 10170 832 -61 -175 A C ATOM 471 CD GLU A 66 42.779 -14.610 -12.792 1.00100.57 A C ANISOU 471 CD GLU A 66 11806 13051 13356 967 -36 -239 A C ATOM 472 OE1 GLU A 66 42.187 -15.445 -13.520 1.00102.27 A O ANISOU 472 OE1 GLU A 66 12061 13175 13621 1016 -5 -328 A O ATOM 473 OE2 GLU A 66 44.013 -14.669 -12.538 1.00110.82 A O1- ANISOU 473 OE2 GLU A 66 13007 14447 14652 1023 -46 -205 A O1- ATOM 474 N ILE A 67 39.760 -10.877 -13.583 1.00 60.39 A N ANISOU 474 N ILE A 67 6900 7997 8048 555 -13 -206 A N ATOM 475 CA ILE A 67 40.028 -9.558 -14.141 1.00 53.26 A C ANISOU 475 CA ILE A 67 5956 7220 7059 471 13 -186 A C ATOM 476 C ILE A 67 39.308 -8.451 -13.384 1.00 62.33 A C ANISOU 476 C ILE A 67 7166 8333 8185 353 1 -112 A C ATOM 477 O ILE A 67 39.747 -7.315 -13.394 1.00 68.29 A O ANISOU 477 O ILE A 67 7882 9179 8887 278 16 -71 A O ATOM 478 CB ILE A 67 39.588 -9.474 -15.606 1.00 46.49 A C ANISOU 478 CB ILE A 67 5098 6410 6158 474 55 -262 A C ATOM 479 CG1 ILE A 67 40.424 -10.411 -16.463 1.00 48.98 A C ANISOU 479 CG1 ILE A 67 5343 6785 6481 584 80 -345 A C ATOM 480 CG2 ILE A 67 39.718 -8.061 -16.126 1.00 42.02 A C ANISOU 480 CG2 ILE A 67 4501 5957 5508 383 87 -221 A C ATOM 481 CD1 ILE A 67 40.045 -10.362 -17.898 1.00 48.05 A C ANISOU 481 CD1 ILE A 67 5222 6730 6306 590 120 -426 A C ATOM 482 N LYS A 68 38.182 -8.758 -12.752 1.00 69.96 A N ANISOU 482 N LYS A 68 8226 9162 9194 333 -20 -98 A N ATOM 483 CA LYS A 68 37.496 -7.727 -11.997 1.00 68.54 A C ANISOU 483 CA LYS A 68 8102 8943 8995 225 -25 -31 A C ATOM 484 C LYS A 68 38.405 -7.409 -10.830 1.00 68.50 A C ANISOU 484 C LYS A 68 8064 8982 8982 206 -55 31 A C ATOM 485 O LYS A 68 38.771 -6.256 -10.585 1.00 73.40 A O ANISOU 485 O LYS A 68 8657 9675 9557 121 -47 70 A O ATOM 486 CB LYS A 68 36.134 -8.210 -11.495 1.00 67.93 A C ANISOU 486 CB LYS A 68 8128 8710 8974 215 -38 -29 A C ATOM 487 CG LYS A 68 35.305 -7.121 -10.786 1.00 77.67 A C ANISOU 487 CG LYS A 68 9425 9897 10191 104 -33 34 A C ATOM 488 CD LYS A 68 34.040 -7.666 -10.101 1.00 84.52 A C ANISOU 488 CD LYS A 68 10387 10607 11118 98 -44 45 A C ATOM 489 CE LYS A 68 34.367 -8.513 -8.876 1.00 85.93 A C ANISOU 489 CE LYS A 68 10587 10723 11339 148 -76 83 A C ATOM 490 NZ LYS A 68 33.445 -9.679 -8.720 1.00 86.07 A N1+ ANISOU 490 NZ LYS A 68 10669 10595 11440 199 -79 61 A N1+ ATOM 491 N ILE A 69 38.800 -8.471 -10.148 1.00 64.34 A N ANISOU 491 N ILE A 69 7533 8413 8501 290 -89 39 A N ATOM 492 CA ILE A 69 39.543 -8.387 -8.901 1.00 73.21 A C ANISOU 492 CA ILE A 69 8632 9569 9616 287 -130 102 A C ATOM 493 C ILE A 69 40.950 -7.796 -9.069 1.00 74.16 A C ANISOU 493 C ILE A 69 8636 9851 9691 278 -134 108 A C ATOM 494 O ILE A 69 41.391 -7.007 -8.231 1.00 75.92 A O ANISOU 494 O ILE A 69 8837 10132 9877 208 -157 153 A O ATOM 495 CB ILE A 69 39.595 -9.785 -8.210 1.00 62.91 A C ANISOU 495 CB ILE A 69 7349 8177 8377 396 -163 119 A C ATOM 496 CG1 ILE A 69 38.173 -10.280 -7.923 1.00 54.64 A C ANISOU 496 CG1 ILE A 69 6417 6964 7381 387 -155 121 A C ATOM 497 CG2 ILE A 69 40.408 -9.736 -6.942 1.00 61.63 A C ANISOU 497 CG2 ILE A 69 7156 8069 8194 403 -212 191 A C ATOM 498 CD1 ILE A 69 38.110 -11.629 -7.270 1.00 58.90 A C ANISOU 498 CD1 ILE A 69 6986 7398 7996 488 -175 144 A C ATOM 499 N LEU A 70 41.642 -8.162 -10.148 1.00 63.38 A N ANISOU 499 N LEU A 70 7194 8561 8328 345 -107 56 A N ATOM 500 CA LEU A 70 43.005 -7.682 -10.387 1.00 54.91 A C ANISOU 500 CA LEU A 70 6000 7644 7221 344 -103 59 A C ATOM 501 C LEU A 70 43.053 -6.205 -10.706 1.00 62.67 A C ANISOU 501 C LEU A 70 6962 8704 8148 220 -69 72 A C ATOM 502 O LEU A 70 44.088 -5.551 -10.523 1.00 78.40 A O ANISOU 502 O LEU A 70 8863 10812 10115 181 -72 91 A O ATOM 503 CB LEU A 70 43.665 -8.421 -11.536 1.00 52.67 A C ANISOU 503 CB LEU A 70 5642 7419 6952 446 -70 -3 A C ATOM 504 CG LEU A 70 43.979 -9.891 -11.339 1.00 56.69 A C ANISOU 504 CG LEU A 70 6139 7872 7528 584 -92 -22 A C ATOM 505 CD1 LEU A 70 44.508 -10.422 -12.651 1.00 62.39 A C ANISOU 505 CD1 LEU A 70 6794 8654 8257 667 -44 -101 A C ATOM 506 CD2 LEU A 70 44.989 -10.081 -10.212 1.00 52.28 A C ANISOU 506 CD2 LEU A 70 5513 7369 6981 619 -146 41 A C ATOM 507 N GLN A 71 41.938 -5.689 -11.205 1.00 50.18 A N ANISOU 507 N GLN A 71 5457 7055 6553 159 -35 64 A N ATOM 508 CA GLN A 71 41.858 -4.291 -11.574 1.00 52.15 A C ANISOU 508 CA GLN A 71 5696 7358 6760 46 7 84 A C ATOM 509 C GLN A 71 41.602 -3.484 -10.342 1.00 59.35 A C ANISOU 509 C GLN A 71 6651 8232 7669 -54 -18 134 A C ATOM 510 O GLN A 71 41.836 -2.279 -10.305 1.00 71.96 A O ANISOU 510 O GLN A 71 8222 9878 9242 -154 10 156 A O ATOM 511 CB GLN A 71 40.741 -4.081 -12.580 1.00 44.03 A C ANISOU 511 CB GLN A 71 4733 6278 5721 29 50 63 A C ATOM 512 CG GLN A 71 40.998 -4.847 -13.839 1.00 57.66 A C ANISOU 512 CG GLN A 71 6417 8055 7436 123 75 2 A C ATOM 513 CD GLN A 71 39.988 -4.607 -14.915 1.00 58.33 A C ANISOU 513 CD GLN A 71 6551 8118 7493 108 113 -22 A C ATOM 514 NE2 GLN A 71 40.472 -4.557 -16.144 1.00 55.02 A N ANISOU 514 NE2 GLN A 71 6070 7806 7028 142 156 -56 A N ATOM 515 OE1 GLN A 71 38.783 -4.496 -14.663 1.00 68.00 A O ANISOU 515 OE1 GLN A 71 7864 9238 8734 70 103 -9 A O ATOM 516 N LEU A 72 41.129 -4.176 -9.323 1.00 61.61 A N ANISOU 516 N LEU A 72 7003 8426 7981 -24 -66 150 A N ATOM 517 CA LEU A 72 40.710 -3.531 -8.095 1.00 74.08 A C ANISOU 517 CA LEU A 72 8640 9956 9551 -112 -88 191 A C ATOM 518 C LEU A 72 41.839 -3.551 -7.072 1.00 75.44 A C ANISOU 518 C LEU A 72 8743 10217 9704 -111 -141 212 A C ATOM 519 O LEU A 72 42.091 -2.560 -6.391 1.00 72.66 A O ANISOU 519 O LEU A 72 8379 9905 9323 -212 -146 228 A O ATOM 520 CB LEU A 72 39.458 -4.219 -7.531 1.00 60.71 A C ANISOU 520 CB LEU A 72 7063 8115 7890 -86 -104 203 A C ATOM 521 CG LEU A 72 39.266 -3.874 -6.065 1.00 50.01 A C ANISOU 521 CG LEU A 72 5757 6725 6519 -147 -138 246 A C ATOM 522 CD1 LEU A 72 38.636 -2.517 -5.936 1.00 55.78 A C ANISOU 522 CD1 LEU A 72 6531 7430 7230 -275 -98 255 A C ATOM 523 CD2 LEU A 72 38.450 -4.920 -5.388 1.00 55.52 A C ANISOU 523 CD2 LEU A 72 6541 7303 7251 -85 -163 266 A C ATOM 524 N LEU A 73 42.509 -4.691 -6.974 1.00 75.03 A N ANISOU 524 N LEU A 73 8644 10194 9671 3 -179 210 A N ATOM 525 CA LEU A 73 43.625 -4.852 -6.062 1.00 66.87 A C ANISOU 525 CA LEU A 73 7532 9257 8619 24 -237 236 A C ATOM 526 C LEU A 73 44.881 -4.244 -6.636 1.00 62.30 A C ANISOU 526 C LEU A 73 6819 8829 8022 0 -222 215 A C ATOM 527 O LEU A 73 45.484 -4.810 -7.531 1.00 76.95 A O ANISOU 527 O LEU A 73 8604 10736 9898 84 -203 190 A O ATOM 528 CB LEU A 73 43.854 -6.323 -5.804 1.00 62.69 A C ANISOU 528 CB LEU A 73 6996 8695 8127 168 -277 251 A C ATOM 529 CG LEU A 73 42.663 -6.943 -5.082 1.00 66.06 A C ANISOU 529 CG LEU A 73 7552 8971 8578 188 -290 281 A C ATOM 530 CD1 LEU A 73 43.065 -8.277 -4.497 1.00 67.73 A C ANISOU 530 CD1 LEU A 73 7749 9161 8824 319 -336 318 A C ATOM 531 CD2 LEU A 73 42.180 -6.020 -3.986 1.00 63.89 A C ANISOU 531 CD2 LEU A 73 7338 8681 8255 72 -307 314 A C ATOM 532 N LYS A 74 45.256 -3.077 -6.126 1.00 58.71 A N ANISOU 532 N LYS A 74 6332 8442 7534 -119 -225 222 A N ATOM 533 CA LYS A 74 46.468 -2.392 -6.558 1.00 61.16 A C ANISOU 533 CA LYS A 74 6509 8895 7833 -161 -209 204 A C ATOM 534 C LYS A 74 47.349 -2.086 -5.359 1.00 65.51 A C ANISOU 534 C LYS A 74 6990 9545 8355 -206 -277 218 A C ATOM 535 O LYS A 74 47.053 -1.191 -4.576 1.00 59.41 A O ANISOU 535 O LYS A 74 6257 8760 7556 -322 -286 219 A O ATOM 536 CB LYS A 74 46.131 -1.120 -7.322 1.00 47.84 A C ANISOU 536 CB LYS A 74 4832 7203 6142 -278 -132 190 A C ATOM 537 CG LYS A 74 45.396 -1.398 -8.643 1.00 69.86 A C ANISOU 537 CG LYS A 74 7669 9928 8946 -228 -68 176 A C ATOM 538 CD LYS A 74 46.132 -2.408 -9.516 1.00 77.29 A C ANISOU 538 CD LYS A 74 8530 10937 9900 -99 -63 152 A C ATOM 539 CE LYS A 74 45.501 -2.537 -10.894 1.00 81.47 A C ANISOU 539 CE LYS A 74 9095 11432 10428 -65 3 127 A C ATOM 540 NZ LYS A 74 46.523 -2.920 -11.911 1.00 88.45 A N1+ ANISOU 540 NZ LYS A 74 9867 12431 11310 11 36 97 A N1+ ATOM 541 N HIS A 75 48.440 -2.834 -5.225 1.00 61.56 A N ANISOU 541 N HIS A 75 6382 9148 7861 -113 -325 225 A N ATOM 542 CA HIS A 75 49.185 -2.812 -3.982 1.00 54.99 A C ANISOU 542 CA HIS A 75 5489 8409 6995 -129 -408 245 A C ATOM 543 C HIS A 75 50.531 -3.547 -4.115 1.00 66.49 A C ANISOU 543 C HIS A 75 6796 10000 8468 -21 -449 253 A C ATOM 544 O HIS A 75 50.644 -4.538 -4.841 1.00 68.01 A O ANISOU 544 O HIS A 75 6972 10168 8701 108 -429 255 A O ATOM 545 CB HIS A 75 48.303 -3.392 -2.873 1.00 44.45 A C ANISOU 545 CB HIS A 75 4276 6976 5637 -99 -459 285 A C ATOM 546 CG HIS A 75 48.977 -3.488 -1.541 1.00 57.65 A C ANISOU 546 CG HIS A 75 5899 8748 7259 -100 -552 314 A C ATOM 547 CD2 HIS A 75 48.679 -2.917 -0.352 1.00 56.94 A C ANISOU 547 CD2 HIS A 75 5860 8666 7109 -191 -594 322 A C ATOM 548 ND1 HIS A 75 50.082 -4.277 -1.321 1.00 65.27 A N ANISOU 548 ND1 HIS A 75 6746 9827 8227 8 -613 341 A N ATOM 549 CE1 HIS A 75 50.452 -4.171 -0.057 1.00 60.40 A C ANISOU 549 CE1 HIS A 75 6108 9294 7549 -18 -696 368 A C ATOM 550 NE2 HIS A 75 49.620 -3.347 0.551 1.00 53.12 A N ANISOU 550 NE2 HIS A 75 5288 8311 6583 -141 -685 352 A N ATOM 551 N GLU A 76 51.543 -3.041 -3.408 1.00 67.67 A N ANISOU 551 N GLU A 76 6834 10290 8588 -77 -504 252 A N ATOM 552 CA GLU A 76 52.937 -3.443 -3.603 1.00 64.13 A C ANISOU 552 CA GLU A 76 6215 9993 8157 -3 -535 253 A C ATOM 553 C GLU A 76 53.187 -4.912 -3.333 1.00 69.64 A C ANISOU 553 C GLU A 76 6898 10684 8877 176 -588 301 A C ATOM 554 O GLU A 76 54.213 -5.466 -3.740 1.00 72.99 A O ANISOU 554 O GLU A 76 7193 11206 9336 273 -595 304 A O ATOM 555 CB GLU A 76 53.874 -2.610 -2.727 1.00 63.56 A C ANISOU 555 CB GLU A 76 6030 10073 8045 -107 -597 241 A C ATOM 556 CG GLU A 76 55.217 -2.311 -3.401 1.00 88.08 A C ANISOU 556 CG GLU A 76 8951 13332 11184 -113 -578 214 A C ATOM 557 CD GLU A 76 56.313 -1.942 -2.404 1.00118.79 A C ANISOU 557 CD GLU A 76 12702 17393 15040 -166 -669 210 A C ATOM 558 OE1 GLU A 76 56.028 -1.133 -1.489 1.00131.12 A O ANISOU 558 OE1 GLU A 76 14306 18962 16551 -294 -707 190 A O ATOM 559 OE2 GLU A 76 57.454 -2.462 -2.534 1.00120.19 A O1- ANISOU 559 OE2 GLU A 76 12724 17701 15241 -79 -704 222 A O1- ATOM 560 N ASN A 77 52.252 -5.533 -2.631 1.00 72.38 A N ANISOU 560 N ASN A 77 7376 10914 9210 222 -619 341 A N ATOM 561 CA ASN A 77 52.343 -6.945 -2.296 1.00 71.94 A C ANISOU 561 CA ASN A 77 7326 10825 9184 391 -662 397 A C ATOM 562 C ASN A 77 51.324 -7.808 -3.049 1.00 70.77 A C ANISOU 562 C ASN A 77 7297 10500 9094 478 -598 392 A C ATOM 563 O ASN A 77 51.137 -8.985 -2.770 1.00 70.18 A O ANISOU 563 O ASN A 77 7258 10352 9056 609 -619 437 A O ATOM 564 CB ASN A 77 52.191 -7.103 -0.796 1.00 68.70 A C ANISOU 564 CB ASN A 77 6958 10432 8713 388 -752 459 A C ATOM 565 CG ASN A 77 53.374 -6.568 -0.057 1.00 81.36 A C ANISOU 565 CG ASN A 77 8419 12229 10263 341 -830 464 A C ATOM 566 ND2 ASN A 77 54.558 -6.847 -0.582 1.00 84.72 A N ANISOU 566 ND2 ASN A 77 8686 12775 10727 412 -837 458 A N ATOM 567 OD1 ASN A 77 53.240 -5.903 0.969 1.00 90.32 A O ANISOU 567 OD1 ASN A 77 9581 13412 11323 240 -883 468 A O ATOM 568 N VAL A 78 50.662 -7.209 -4.018 1.00 67.78 A N ANISOU 568 N VAL A 78 6975 10054 8726 403 -519 337 A N ATOM 569 CA VAL A 78 49.766 -7.965 -4.849 1.00 62.87 A C ANISOU 569 CA VAL A 78 6448 9285 8155 476 -460 316 A C ATOM 570 C VAL A 78 50.219 -7.871 -6.286 1.00 75.30 A C ANISOU 570 C VAL A 78 7948 10905 9758 497 -388 256 A C ATOM 571 O VAL A 78 50.506 -6.789 -6.811 1.00 75.57 A O ANISOU 571 O VAL A 78 7932 11016 9764 391 -350 224 A O ATOM 572 CB VAL A 78 48.337 -7.459 -4.730 1.00 55.53 A C ANISOU 572 CB VAL A 78 5672 8219 7206 380 -431 309 A C ATOM 573 CG1 VAL A 78 47.437 -8.164 -5.751 1.00 48.65 A C ANISOU 573 CG1 VAL A 78 4883 7212 6388 445 -369 273 A C ATOM 574 CG2 VAL A 78 47.849 -7.680 -3.320 1.00 45.93 A C ANISOU 574 CG2 VAL A 78 4536 6952 5962 374 -494 371 A C ATOM 575 N VAL A 79 50.303 -9.036 -6.903 1.00 79.33 A N ANISOU 575 N VAL A 79 8449 11366 10327 637 -365 241 A N ATOM 576 CA VAL A 79 50.675 -9.145 -8.291 1.00 71.23 A C ANISOU 576 CA VAL A 79 7362 10377 9324 678 -292 178 A C ATOM 577 C VAL A 79 49.919 -8.067 -9.062 1.00 67.94 A C ANISOU 577 C VAL A 79 7008 9937 8868 550 -230 138 A C ATOM 578 O VAL A 79 48.843 -7.651 -8.649 1.00 69.01 A O ANISOU 578 O VAL A 79 7261 9975 8983 470 -236 152 A O ATOM 579 CB VAL A 79 50.385 -10.572 -8.792 1.00 68.54 A C ANISOU 579 CB VAL A 79 7059 9929 9054 831 -269 153 A C ATOM 580 CG1 VAL A 79 49.167 -10.600 -9.691 1.00 54.37 A C ANISOU 580 CG1 VAL A 79 5382 8013 7263 803 -208 95 A C ATOM 581 CG2 VAL A 79 51.623 -11.160 -9.454 1.00 76.71 A C ANISOU 581 CG2 VAL A 79 7952 11066 10128 945 -245 126 A C ATOM 582 N ASN A 80 50.507 -7.591 -10.156 1.00 76.32 A N ANISOU 582 N ASN A 80 7987 11095 9919 532 -168 97 A N ATOM 583 CA ASN A 80 50.002 -6.422 -10.880 1.00 72.93 A C ANISOU 583 CA ASN A 80 7591 10672 9446 408 -107 76 A C ATOM 584 C ASN A 80 49.607 -6.701 -12.328 1.00 78.90 A C ANISOU 584 C ASN A 80 8371 11406 10200 454 -29 19 A C ATOM 585 O ASN A 80 50.453 -7.012 -13.178 1.00 73.63 A O ANISOU 585 O ASN A 80 7606 10831 9540 523 13 -15 A O ATOM 586 CB ASN A 80 51.043 -5.298 -10.852 1.00 72.17 A C ANISOU 586 CB ASN A 80 7372 10724 9324 312 -95 89 A C ATOM 587 CG ASN A 80 50.589 -4.060 -11.601 1.00 72.54 A C ANISOU 587 CG ASN A 80 7449 10775 9337 187 -23 80 A C ATOM 588 ND2 ASN A 80 51.142 -3.858 -12.799 1.00 65.55 A N ANISOU 588 ND2 ASN A 80 6486 9977 8444 203 51 54 A N ATOM 589 OD1 ASN A 80 49.754 -3.287 -11.107 1.00 71.26 A O ANISOU 589 OD1 ASN A 80 7378 10541 9157 81 -30 102 A O ATOM 590 N LEU A 81 48.317 -6.572 -12.613 1.00 81.62 A N ANISOU 590 N LEU A 81 8842 11637 10531 415 -9 7 A N ATOM 591 CA LEU A 81 47.849 -6.759 -13.976 1.00 73.86 A C ANISOU 591 CA LEU A 81 7888 10645 9532 447 58 -49 A C ATOM 592 C LEU A 81 48.080 -5.476 -14.750 1.00 65.99 A C ANISOU 592 C LEU A 81 6846 9746 8481 346 121 -39 A C ATOM 593 O LEU A 81 47.416 -4.484 -14.486 1.00 73.08 A O ANISOU 593 O LEU A 81 7804 10606 9356 233 126 -3 A O ATOM 594 CB LEU A 81 46.367 -7.127 -13.992 1.00 58.85 A C ANISOU 594 CB LEU A 81 6129 8591 7638 445 50 -65 A C ATOM 595 CG LEU A 81 45.799 -7.226 -15.397 1.00 46.08 A C ANISOU 595 CG LEU A 81 4542 6976 5991 466 111 -126 A C ATOM 596 CD1 LEU A 81 46.201 -8.548 -16.022 1.00 52.69 A C ANISOU 596 CD1 LEU A 81 5344 7814 6863 605 125 -200 A C ATOM 597 CD2 LEU A 81 44.313 -7.100 -15.333 1.00 50.48 A C ANISOU 597 CD2 LEU A 81 5229 7407 6545 415 102 -125 A C ATOM 598 N ILE A 82 49.033 -5.499 -15.683 1.00 64.49 A N ANISOU 598 N ILE A 82 6549 9678 8276 390 174 -67 A N ATOM 599 CA ILE A 82 49.401 -4.320 -16.477 1.00 65.03 A C ANISOU 599 CA ILE A 82 6561 9851 8297 303 246 -49 A C ATOM 600 C ILE A 82 48.358 -3.957 -17.514 1.00 61.69 A C ANISOU 600 C ILE A 82 6223 9392 7822 274 301 -62 A C ATOM 601 O ILE A 82 48.004 -2.793 -17.684 1.00 62.29 A O ANISOU 601 O ILE A 82 6322 9477 7868 167 336 -16 A O ATOM 602 CB ILE A 82 50.663 -4.562 -17.292 1.00 56.48 A C ANISOU 602 CB ILE A 82 5340 8909 7209 370 298 -78 A C ATOM 603 CG1 ILE A 82 51.844 -4.845 -16.397 1.00 56.61 A C ANISOU 603 CG1 ILE A 82 5245 8991 7275 401 249 -61 A C ATOM 604 CG2 ILE A 82 50.987 -3.356 -18.111 1.00 46.02 A C ANISOU 604 CG2 ILE A 82 3963 7685 5837 279 380 -50 A C ATOM 605 CD1 ILE A 82 53.013 -5.325 -17.201 1.00 62.40 A C ANISOU 605 CD1 ILE A 82 5845 9849 8014 493 300 -97 A C ATOM 606 N GLU A 83 47.911 -4.965 -18.246 1.00 66.94 A N ANISOU 606 N GLU A 83 6929 10025 8480 375 310 -126 A N ATOM 607 CA GLU A 83 46.927 -4.770 -19.293 1.00 68.89 A C ANISOU 607 CA GLU A 83 7250 10254 8669 363 353 -149 A C ATOM 608 C GLU A 83 46.398 -6.108 -19.801 1.00 78.58 A C ANISOU 608 C GLU A 83 8529 11421 9907 478 341 -238 A C ATOM 609 O GLU A 83 46.826 -7.169 -19.350 1.00 77.61 A O ANISOU 609 O GLU A 83 8383 11262 9843 568 308 -276 A O ATOM 610 CB GLU A 83 47.529 -3.970 -20.439 1.00 55.72 A C ANISOU 610 CB GLU A 83 5506 8729 6935 336 440 -136 A C ATOM 611 CG GLU A 83 48.693 -4.637 -21.133 1.00 71.89 A C ANISOU 611 CG GLU A 83 7443 10895 8976 434 482 -190 A C ATOM 612 CD GLU A 83 48.950 -4.040 -22.515 1.00 90.20 A C ANISOU 612 CD GLU A 83 9717 13344 11210 424 576 -189 A C ATOM 613 OE1 GLU A 83 47.975 -3.621 -23.194 1.00101.42 A O ANISOU 613 OE1 GLU A 83 11217 14750 12568 390 600 -180 A O ATOM 614 OE2 GLU A 83 50.125 -3.998 -22.924 1.00 76.59 A O1- ANISOU 614 OE2 GLU A 83 7878 11744 9481 454 628 -194 A O1- ATOM 615 N ILE A 84 45.445 -6.053 -20.723 1.00 81.72 A N ANISOU 615 N ILE A 84 8994 11806 10251 472 368 -271 A N ATOM 616 CA ILE A 84 44.949 -7.264 -21.355 1.00 70.81 A C ANISOU 616 CA ILE A 84 7653 10380 8872 571 364 -373 A C ATOM 617 C ILE A 84 45.122 -7.126 -22.853 1.00 71.55 A C ANISOU 617 C ILE A 84 7709 10603 8872 599 436 -423 A C ATOM 618 O ILE A 84 44.936 -6.039 -23.407 1.00 85.27 A O ANISOU 618 O ILE A 84 9445 12416 10536 525 476 -366 A O ATOM 619 CB ILE A 84 43.495 -7.546 -20.974 1.00 59.33 A C ANISOU 619 CB ILE A 84 6322 8776 7443 545 315 -384 A C ATOM 620 CG1 ILE A 84 43.444 -8.045 -19.537 1.00 56.83 A C ANISOU 620 CG1 ILE A 84 6038 8333 7222 552 250 -352 A C ATOM 621 CG2 ILE A 84 42.907 -8.604 -21.870 1.00 62.13 A C ANISOU 621 CG2 ILE A 84 6714 9103 7788 626 322 -498 A C ATOM 622 CD1 ILE A 84 42.119 -7.811 -18.859 1.00 60.50 A C ANISOU 622 CD1 ILE A 84 6613 8663 7711 483 207 -317 A C ATOM 623 N CYS A 85 45.517 -8.224 -23.492 1.00 58.15 A N ANISOU 623 N CYS A 85 5981 8934 7178 709 456 -525 A N ATOM 624 CA CYS A 85 45.894 -8.217 -24.896 1.00 64.75 A C ANISOU 624 CA CYS A 85 6768 9914 7921 751 530 -585 A C ATOM 625 C CYS A 85 45.152 -9.289 -25.666 1.00 72.11 A C ANISOU 625 C CYS A 85 7758 10807 8835 825 527 -714 A C ATOM 626 O CYS A 85 44.712 -10.296 -25.097 1.00 65.56 A O ANISOU 626 O CYS A 85 6979 9840 8093 872 479 -772 A O ATOM 627 CB CYS A 85 47.397 -8.469 -25.059 1.00 74.78 A C ANISOU 627 CB CYS A 85 7913 11293 9208 817 579 -599 A C ATOM 628 SG CYS A 85 48.476 -7.126 -24.561 1.00 81.30 A S ANISOU 628 SG CYS A 85 8638 12221 10032 727 607 -468 A S ATOM 629 N ARG A 86 45.055 -9.069 -26.975 1.00 75.67 A N ANISOU 629 N ARG A 86 8197 11384 9171 836 583 -760 A N ATOM 630 CA ARG A 86 44.412 -9.994 -27.891 1.00 80.36 A C ANISOU 630 CA ARG A 86 8835 11975 9724 900 588 -899 A C ATOM 631 C ARG A 86 45.401 -10.510 -28.926 1.00 81.75 A C ANISOU 631 C ARG A 86 8929 12289 9843 992 665 -992 A C ATOM 632 O ARG A 86 46.538 -10.058 -28.995 1.00 87.57 A O ANISOU 632 O ARG A 86 9574 13132 10567 1000 718 -938 A O ATOM 633 CB ARG A 86 43.271 -9.276 -28.610 1.00 86.07 A C ANISOU 633 CB ARG A 86 9623 12742 10338 832 582 -879 A C ATOM 634 CG ARG A 86 43.729 -8.047 -29.350 1.00 90.18 A C ANISOU 634 CG ARG A 86 10091 13432 10740 785 647 -786 A C ATOM 635 CD ARG A 86 42.592 -7.140 -29.750 1.00 97.33 A C ANISOU 635 CD ARG A 86 11060 14358 11561 707 632 -719 A C ATOM 636 NE ARG A 86 43.120 -5.993 -30.479 1.00108.06 A N ANISOU 636 NE ARG A 86 12365 15877 12815 670 706 -621 A N ATOM 637 CZ ARG A 86 43.281 -5.959 -31.798 1.00106.20 A C ANISOU 637 CZ ARG A 86 12101 15806 12443 711 766 -662 A C ATOM 638 NH1 ARG A 86 42.923 -7.015 -32.525 1.00100.55 A N1+ ANISOU 638 NH1 ARG A 86 11408 15116 11679 785 754 -814 A N1+ ATOM 639 NH2 ARG A 86 43.789 -4.872 -32.384 1.00 98.11 A N ANISOU 639 NH2 ARG A 86 11026 14920 11331 674 841 -554 A N ATOM 640 N THR A 87 44.953 -11.459 -29.732 1.00 86.09 A N ANISOU 640 N THR A 87 9510 12837 10362 1058 673 -1139 A N ATOM 641 CA THR A 87 45.678 -11.879 -30.920 1.00 95.27 A C ANISOU 641 CA THR A 87 10610 14146 11441 1138 753 -1244 A C ATOM 642 C THR A 87 44.945 -11.294 -32.121 1.00111.02 A C ANISOU 642 C THR A 87 12640 16275 13269 1099 775 -1262 A C ATOM 643 O THR A 87 43.840 -10.769 -31.976 1.00121.63 A O ANISOU 643 O THR A 87 14057 17572 14586 1024 721 -1210 A O ATOM 644 CB THR A 87 45.704 -13.400 -31.005 1.00 95.89 A C ANISOU 644 CB THR A 87 10700 14130 11602 1243 751 -1410 A C ATOM 645 CG2 THR A 87 47.005 -13.947 -30.428 1.00 99.03 A C ANISOU 645 CG2 THR A 87 11010 14505 12111 1324 782 -1405 A C ATOM 646 OG1 THR A 87 44.615 -13.927 -30.234 1.00 97.80 A O ANISOU 646 OG1 THR A 87 11034 14182 11942 1218 670 -1431 A O ATOM 647 N LYS A 88 45.537 -11.367 -33.305 1.00119.72 A N ANISOU 647 N LYS A 88 13688 17547 14253 1152 854 -1332 A N ATOM 648 CA LYS A 88 44.870 -10.812 -34.487 1.00135.93 A C ANISOU 648 CA LYS A 88 15770 19747 16130 1122 875 -1343 A C ATOM 649 C LYS A 88 44.344 -11.893 -35.438 1.00137.20 A C ANISOU 649 C LYS A 88 15966 19937 16227 1190 876 -1543 A C ATOM 650 O LYS A 88 43.318 -11.713 -36.104 1.00129.93 A O ANISOU 650 O LYS A 88 15102 19069 15197 1157 845 -1577 A O ATOM 651 CB LYS A 88 45.783 -9.827 -35.231 1.00146.88 A C ANISOU 651 CB LYS A 88 17077 21335 17395 1112 969 -1248 A C ATOM 652 CG LYS A 88 47.123 -10.406 -35.680 1.00155.37 A C ANISOU 652 CG LYS A 88 18056 22506 18471 1205 1058 -1327 A C ATOM 653 CD LYS A 88 48.072 -10.628 -34.503 1.00160.68 A C ANISOU 653 CD LYS A 88 18668 23069 19315 1223 1051 -1276 A C ATOM 654 CE LYS A 88 49.405 -11.191 -34.973 1.00164.86 A C ANISOU 654 CE LYS A 88 19092 23699 19850 1321 1142 -1350 A C ATOM 655 NZ LYS A 88 50.288 -11.555 -33.835 1.00160.99 A N1+ ANISOU 655 NZ LYS A 88 18537 23102 19529 1352 1124 -1313 A N1+ ATOM 656 N GLY A 97 40.693 -17.300 -32.084 1.00 98.49 A N ANISOU 656 N GLY A 97 11377 13987 12058 1266 569 -2030 A N ATOM 657 CA GLY A 97 41.288 -16.129 -31.459 1.00115.01 A C ANISOU 657 CA GLY A 97 13434 16137 14127 1222 570 -1829 A C ATOM 658 C GLY A 97 41.122 -16.081 -29.943 1.00129.84 A C ANISOU 658 C GLY A 97 15343 17831 16158 1189 514 -1703 A C ATOM 659 O GLY A 97 40.059 -16.433 -29.415 1.00128.05 A O ANISOU 659 O GLY A 97 15189 17453 16009 1150 456 -1719 A O ATOM 660 N SER A 98 42.170 -15.633 -29.242 1.00132.03 A N ANISOU 660 N SER A 98 15563 18127 16475 1201 533 -1579 A N ATOM 661 CA SER A 98 42.185 -15.635 -27.768 1.00117.70 A C ANISOU 661 CA SER A 98 13769 16155 14797 1180 483 -1462 A C ATOM 662 C SER A 98 42.676 -14.337 -27.102 1.00100.04 A C ANISOU 662 C SER A 98 11498 13985 12527 1109 474 -1279 A C ATOM 663 O SER A 98 42.794 -13.289 -27.736 1.00 97.17 A O ANISOU 663 O SER A 98 11107 13772 12039 1056 501 -1224 A O ATOM 664 CB SER A 98 42.990 -16.824 -27.237 1.00110.84 A C ANISOU 664 CB SER A 98 12865 15179 14069 1288 502 -1516 A C ATOM 665 OG SER A 98 44.300 -16.820 -27.780 1.00107.43 A O ANISOU 665 OG SER A 98 12334 14886 13597 1359 570 -1534 A O ATOM 666 N ILE A 99 42.982 -14.437 -25.814 1.00 82.91 A N ANISOU 666 N ILE A 99 9328 11703 10472 1109 438 -1189 A N ATOM 667 CA ILE A 99 43.139 -13.270 -24.961 1.00 73.36 A C ANISOU 667 CA ILE A 99 8110 10513 9252 1023 411 -1027 A C ATOM 668 C ILE A 99 44.188 -13.510 -23.867 1.00 78.00 A C ANISOU 668 C ILE A 99 8639 11060 9937 1066 399 -955 A C ATOM 669 O ILE A 99 44.158 -14.532 -23.183 1.00 78.05 A O ANISOU 669 O ILE A 99 8667 10932 10058 1130 372 -983 A O ATOM 670 CB ILE A 99 41.754 -12.912 -24.349 1.00 58.99 A C ANISOU 670 CB ILE A 99 6392 8570 7451 933 349 -977 A C ATOM 671 CG1 ILE A 99 41.007 -11.986 -25.291 1.00 64.88 A C ANISOU 671 CG1 ILE A 99 7164 9420 8070 860 361 -970 A C ATOM 672 CG2 ILE A 99 41.854 -12.306 -22.952 1.00 60.80 A C ANISOU 672 CG2 ILE A 99 6633 8727 7741 873 306 -836 A C ATOM 673 CD1 ILE A 99 41.810 -10.810 -25.707 1.00 79.68 A C ANISOU 673 CD1 ILE A 99 8969 11460 9846 821 408 -882 A C ATOM 674 N TYR A 100 45.119 -12.572 -23.709 1.00 78.86 A N ANISOU 674 N TYR A 100 8670 11290 10003 1031 418 -861 A N ATOM 675 CA TYR A 100 46.198 -12.717 -22.729 1.00 75.24 A C ANISOU 675 CA TYR A 100 8139 10826 9624 1068 403 -793 A C ATOM 676 C TYR A 100 46.146 -11.669 -21.607 1.00 71.94 A C ANISOU 676 C TYR A 100 7731 10392 9210 964 354 -655 A C ATOM 677 O TYR A 100 46.052 -10.472 -21.866 1.00 69.38 A O ANISOU 677 O TYR A 100 7401 10153 8808 869 371 -594 A O ATOM 678 CB TYR A 100 47.567 -12.627 -23.415 1.00 76.94 A C ANISOU 678 CB TYR A 100 8229 11203 9803 1126 470 -812 A C ATOM 679 CG TYR A 100 47.871 -13.709 -24.440 1.00 86.14 A C ANISOU 679 CG TYR A 100 9366 12393 10970 1242 527 -953 A C ATOM 680 CD1 TYR A 100 48.241 -14.988 -24.046 1.00 92.83 A C ANISOU 680 CD1 TYR A 100 10198 13140 11934 1357 521 -1012 A C ATOM 681 CD2 TYR A 100 47.823 -13.437 -25.801 1.00 86.51 A C ANISOU 681 CD2 TYR A 100 9400 12568 10902 1240 592 -1026 A C ATOM 682 CE1 TYR A 100 48.536 -15.973 -24.978 1.00 95.64 A C ANISOU 682 CE1 TYR A 100 10527 13511 12300 1463 581 -1150 A C ATOM 683 CE2 TYR A 100 48.114 -14.413 -26.740 1.00 93.61 A C ANISOU 683 CE2 TYR A 100 10274 13497 11796 1344 649 -1167 A C ATOM 684 CZ TYR A 100 48.470 -15.680 -26.324 1.00100.14 A C ANISOU 684 CZ TYR A 100 11087 14212 12749 1454 645 -1234 A C ATOM 685 OH TYR A 100 48.761 -16.652 -27.260 1.00104.15 A O ANISOU 685 OH TYR A 100 11571 14742 13260 1558 708 -1384 A O ATOM 686 N LEU A 101 46.211 -12.132 -20.362 1.00 68.34 A N ANISOU 686 N LEU A 101 7290 9827 8848 985 298 -606 A N ATOM 687 CA LEU A 101 46.449 -11.263 -19.215 1.00 59.46 A C ANISOU 687 CA LEU A 101 6155 8707 7731 903 253 -486 A C ATOM 688 C LEU A 101 47.938 -10.940 -19.141 1.00 66.64 A C ANISOU 688 C LEU A 101 6928 9756 8636 926 274 -449 A C ATOM 689 O LEU A 101 48.774 -11.824 -19.311 1.00 72.95 A O ANISOU 689 O LEU A 101 7655 10580 9481 1038 291 -494 A O ATOM 690 CB LEU A 101 45.992 -11.951 -17.928 1.00 60.72 A C ANISOU 690 CB LEU A 101 6378 8711 7981 925 185 -448 A C ATOM 691 CG LEU A 101 44.535 -11.674 -17.507 1.00 70.28 A C ANISOU 691 CG LEU A 101 7717 9795 9191 842 151 -426 A C ATOM 692 CD1 LEU A 101 43.573 -11.828 -18.668 1.00 71.17 A C ANISOU 692 CD1 LEU A 101 7888 9887 9264 836 185 -515 A C ATOM 693 CD2 LEU A 101 44.081 -12.543 -16.341 1.00 64.24 A C ANISOU 693 CD2 LEU A 101 7017 8873 8520 882 98 -397 A C ATOM 694 N VAL A 102 48.282 -9.680 -18.899 1.00 64.43 A N ANISOU 694 N VAL A 102 6608 9565 8307 821 276 -372 A N ATOM 695 CA VAL A 102 49.687 -9.290 -18.895 1.00 56.86 A C ANISOU 695 CA VAL A 102 5511 8749 7345 830 300 -341 A C ATOM 696 C VAL A 102 50.120 -8.707 -17.557 1.00 64.89 A C ANISOU 696 C VAL A 102 6494 9769 8390 763 237 -249 A C ATOM 697 O VAL A 102 49.656 -7.644 -17.164 1.00 68.16 A O ANISOU 697 O VAL A 102 6951 10175 8772 641 224 -194 A O ATOM 698 CB VAL A 102 49.992 -8.271 -19.993 1.00 58.82 A C ANISOU 698 CB VAL A 102 5708 9135 7508 766 377 -340 A C ATOM 699 CG1 VAL A 102 51.471 -8.041 -20.078 1.00 71.94 A C ANISOU 699 CG1 VAL A 102 7216 10939 9177 788 411 -321 A C ATOM 700 CG2 VAL A 102 49.490 -8.763 -21.320 1.00 58.48 A C ANISOU 700 CG2 VAL A 102 5703 9103 7412 823 434 -430 A C ATOM 701 N PHE A 103 51.021 -9.404 -16.867 1.00 68.11 A N ANISOU 701 N PHE A 103 6824 10194 8860 846 200 -236 A N ATOM 702 CA PHE A 103 51.537 -8.954 -15.572 1.00 69.41 A C ANISOU 702 CA PHE A 103 6944 10382 9046 794 132 -156 A C ATOM 703 C PHE A 103 52.987 -8.462 -15.628 1.00 74.31 A C ANISOU 703 C PHE A 103 7400 11171 9664 787 150 -135 A C ATOM 704 O PHE A 103 53.708 -8.713 -16.597 1.00 75.97 A O ANISOU 704 O PHE A 103 7522 11471 9872 852 214 -180 A O ATOM 705 CB PHE A 103 51.474 -10.098 -14.569 1.00 61.57 A C ANISOU 705 CB PHE A 103 5980 9291 8124 893 63 -138 A C ATOM 706 CG PHE A 103 50.129 -10.684 -14.424 1.00 63.32 A C ANISOU 706 CG PHE A 103 6351 9343 8365 906 46 -156 A C ATOM 707 CD1 PHE A 103 49.267 -10.223 -13.450 1.00 62.77 A C ANISOU 707 CD1 PHE A 103 6378 9187 8284 817 -6 -101 A C ATOM 708 CD2 PHE A 103 49.710 -11.685 -15.269 1.00 71.54 A C ANISOU 708 CD2 PHE A 103 7433 10311 9438 1002 87 -236 A C ATOM 709 CE1 PHE A 103 48.014 -10.758 -13.312 1.00 60.44 A C ANISOU 709 CE1 PHE A 103 6215 8736 8013 825 -17 -116 A C ATOM 710 CE2 PHE A 103 48.454 -12.228 -15.140 1.00 75.91 A C ANISOU 710 CE2 PHE A 103 8118 10707 10018 1006 73 -259 A C ATOM 711 CZ PHE A 103 47.606 -11.764 -14.157 1.00 71.67 A C ANISOU 711 CZ PHE A 103 7673 10085 9473 918 21 -194 A C ATOM 712 N ASP A 104 53.413 -7.767 -14.579 1.00 64.77 A N ANISOU 712 N ASP A 104 6147 10006 8456 706 93 -72 A N ATOM 713 CA ASP A 104 54.826 -7.526 -14.369 1.00 78.28 A C ANISOU 713 CA ASP A 104 7693 11868 10184 714 87 -51 A C ATOM 714 C ASP A 104 55.425 -8.912 -14.172 1.00 83.70 A C ANISOU 714 C ASP A 104 8322 12547 10935 882 59 -64 A C ATOM 715 O ASP A 104 54.747 -9.808 -13.683 1.00 81.00 A O ANISOU 715 O ASP A 104 8074 12077 10626 954 17 -60 A O ATOM 716 CB ASP A 104 55.040 -6.697 -13.101 1.00 98.10 A C ANISOU 716 CB ASP A 104 10179 14408 12684 602 12 10 A C ATOM 717 CG ASP A 104 54.637 -5.245 -13.268 1.00106.21 A C ANISOU 717 CG ASP A 104 11240 15449 13664 432 49 23 A C ATOM 718 OD1 ASP A 104 54.913 -4.667 -14.345 1.00108.07 A O ANISOU 718 OD1 ASP A 104 11429 15755 13879 397 135 3 A O ATOM 719 OD2 ASP A 104 54.062 -4.679 -12.309 1.00103.60 A O1- ANISOU 719 OD2 ASP A 104 10983 15061 13319 336 -4 56 A O1- ATOM 720 N PHE A 105 56.684 -9.110 -14.536 1.00 88.04 A N ANISOU 720 N PHE A 105 8715 13226 11511 949 87 -74 A N ATOM 721 CA PHE A 105 57.284 -10.423 -14.342 1.00 80.78 A C ANISOU 721 CA PHE A 105 7734 12295 10663 1118 65 -81 A C ATOM 722 C PHE A 105 57.973 -10.488 -12.997 1.00 80.03 A C ANISOU 722 C PHE A 105 7559 12252 10596 1129 -35 -6 A C ATOM 723 O PHE A 105 58.714 -9.571 -12.645 1.00 85.79 A O ANISOU 723 O PHE A 105 8183 13111 11302 1037 -57 24 A O ATOM 724 CB PHE A 105 58.290 -10.710 -15.440 1.00 85.93 A C ANISOU 724 CB PHE A 105 8254 13061 11335 1202 150 -133 A C ATOM 725 CG PHE A 105 59.038 -11.984 -15.247 1.00 93.04 A C ANISOU 725 CG PHE A 105 9072 13961 12319 1378 135 -137 A C ATOM 726 CD1 PHE A 105 58.449 -13.200 -15.550 1.00 99.45 A C ANISOU 726 CD1 PHE A 105 9973 14634 13180 1503 156 -184 A C ATOM 727 CD2 PHE A 105 60.335 -11.975 -14.773 1.00 88.54 A C ANISOU 727 CD2 PHE A 105 8329 13525 11786 1418 104 -94 A C ATOM 728 CE1 PHE A 105 59.140 -14.383 -15.380 1.00 92.87 A C ANISOU 728 CE1 PHE A 105 9063 13786 12437 1671 151 -185 A C ATOM 729 CE2 PHE A 105 61.029 -13.157 -14.598 1.00 81.63 A C ANISOU 729 CE2 PHE A 105 7373 12648 10996 1591 93 -89 A C ATOM 730 CZ PHE A 105 60.430 -14.359 -14.901 1.00 82.65 A C ANISOU 730 CZ PHE A 105 7597 12628 11179 1719 120 -132 A C ATOM 731 N CYS A 106 57.724 -11.565 -12.249 1.00 79.69 A N ANISOU 731 N CYS A 106 7564 12111 10604 1241 -94 25 A N ATOM 732 CA CYS A 106 58.413 -11.816 -10.971 1.00 83.53 A C ANISOU 732 CA CYS A 106 7971 12654 11115 1282 -193 105 A C ATOM 733 C CYS A 106 59.479 -12.899 -11.076 1.00 83.68 A C ANISOU 733 C CYS A 106 7856 12725 11213 1459 -190 113 A C ATOM 734 O CYS A 106 59.220 -14.002 -11.564 1.00 93.70 A O ANISOU 734 O CYS A 106 9169 13887 12544 1593 -146 79 A O ATOM 735 CB CYS A 106 57.426 -12.171 -9.868 1.00 81.55 A C ANISOU 735 CB CYS A 106 7861 12266 10858 1278 -269 160 A C ATOM 736 SG CYS A 106 56.425 -10.783 -9.381 1.00 97.11 A S ANISOU 736 SG CYS A 106 9953 14208 12738 1066 -293 170 A S ATOM 737 N GLU A 107 60.674 -12.576 -10.593 1.00 77.10 A N ANISOU 737 N GLU A 107 6855 12056 10384 1460 -236 155 A N ATOM 738 CA GLU A 107 61.874 -13.358 -10.913 1.00 90.34 A C ANISOU 738 CA GLU A 107 8368 13822 12135 1613 -214 155 A C ATOM 739 C GLU A 107 61.911 -14.699 -10.188 1.00 90.80 A C ANISOU 739 C GLU A 107 8438 13792 12268 1787 -268 215 A C ATOM 740 O GLU A 107 62.525 -15.643 -10.670 1.00 97.40 A O ANISOU 740 O GLU A 107 9194 14627 13187 1944 -223 198 A O ATOM 741 CB GLU A 107 63.166 -12.548 -10.654 1.00 85.51 A C ANISOU 741 CB GLU A 107 7558 13424 11508 1552 -246 180 A C ATOM 742 CG GLU A 107 63.228 -11.160 -11.358 1.00157.76 A C ANISOU 742 CG GLU A 107 16682 22663 20596 1374 -184 130 A C ATOM 743 CD GLU A 107 62.275 -10.093 -10.768 1.00152.46 A C ANISOU 743 CD GLU A 107 16141 21941 19846 1191 -226 144 A C ATOM 744 OE1 GLU A 107 61.522 -10.401 -9.825 1.00153.85 A O ANISOU 744 OE1 GLU A 107 16433 22015 20006 1195 -303 187 A O ATOM 745 OE2 GLU A 107 62.272 -8.936 -11.249 1.00142.78 A O1- ANISOU 745 OE2 GLU A 107 14902 20771 18577 1043 -177 113 A O1- ATOM 746 N HIS A 108 61.233 -14.778 -9.044 1.00 83.19 A N ANISOU 746 N HIS A 108 7578 12752 11279 1761 -357 286 A N ATOM 747 CA HIS A 108 61.263 -15.972 -8.205 1.00 85.99 A C ANISOU 747 CA HIS A 108 7945 13029 11700 1918 -415 367 A C ATOM 748 C HIS A 108 59.883 -16.357 -7.741 1.00 91.79 A C ANISOU 748 C HIS A 108 8883 13567 12427 1903 -430 388 A C ATOM 749 O HIS A 108 58.970 -15.546 -7.785 1.00104.13 A O ANISOU 749 O HIS A 108 10564 15082 13919 1755 -423 356 A O ATOM 750 CB HIS A 108 62.131 -15.734 -6.968 1.00 85.46 A C ANISOU 750 CB HIS A 108 7753 13115 11604 1921 -532 468 A C ATOM 751 CG HIS A 108 63.571 -15.511 -7.290 1.00 94.08 A C ANISOU 751 CG HIS A 108 8624 14403 12721 1956 -529 460 A C ATOM 752 CD2 HIS A 108 64.536 -16.370 -7.692 1.00 93.59 A C ANISOU 752 CD2 HIS A 108 8422 14388 12751 2125 -496 467 A C ATOM 753 ND1 HIS A 108 64.156 -14.263 -7.258 1.00101.62 A N ANISOU 753 ND1 HIS A 108 9474 15530 13609 1804 -551 438 A N ATOM 754 CE1 HIS A 108 65.425 -14.364 -7.607 1.00105.13 A C ANISOU 754 CE1 HIS A 108 9719 16124 14101 1874 -537 435 A C ATOM 755 NE2 HIS A 108 65.680 -15.632 -7.880 1.00108.14 A N ANISOU 755 NE2 HIS A 108 10075 16436 14578 2072 -503 452 A N ATOM 756 N ASP A 109 59.725 -17.597 -7.294 1.00 83.62 A N ANISOU 756 N ASP A 109 10282 10715 10776 1296 -2614 1106 A N ATOM 757 CA ASP A 109 58.585 -17.906 -6.449 1.00 90.91 A C ANISOU 757 CA ASP A 109 11385 11400 11756 1097 -2580 1108 A C ATOM 758 C ASP A 109 58.960 -18.770 -5.258 1.00 94.43 A C ANISOU 758 C ASP A 109 12009 11682 12190 1049 -2684 1188 A C ATOM 759 O ASP A 109 59.807 -19.657 -5.338 1.00103.36 A O ANISOU 759 O ASP A 109 13160 12804 13309 1228 -2820 1189 A O ATOM 760 CB ASP A 109 57.391 -18.448 -7.228 1.00101.63 A C ANISOU 760 CB ASP A 109 12766 12640 13210 1128 -2560 970 A C ATOM 761 CG ASP A 109 57.572 -19.860 -7.659 1.00113.63 A C ANISOU 761 CG ASP A 109 14349 14041 14786 1313 -2702 883 A C ATOM 762 OD1 ASP A 109 57.554 -20.102 -8.885 1.00121.89 A O ANISOU 762 OD1 ASP A 109 15285 15174 15852 1506 -2731 761 A O ATOM 763 OD2 ASP A 109 57.714 -20.722 -6.771 1.00117.66 A O1- ANISOU 763 OD2 ASP A 109 15025 14365 15316 1270 -2783 936 A O1- ATOM 764 N LEU A 110 58.316 -18.459 -4.146 1.00 92.19 A N ANISOU 764 N LEU A 110 11854 11277 11899 812 -2613 1259 A N ATOM 765 CA LEU A 110 58.685 -18.948 -2.835 1.00 87.06 A C ANISOU 765 CA LEU A 110 11373 10507 11199 729 -2682 1369 A C ATOM 766 C LEU A 110 58.805 -20.458 -2.767 1.00 97.40 A C ANISOU 766 C LEU A 110 12830 11623 12555 860 -2818 1355 A C ATOM 767 O LEU A 110 59.512 -20.984 -1.918 1.00109.01 A O ANISOU 767 O LEU A 110 14414 13040 13966 892 -2918 1450 A O ATOM 768 CB LEU A 110 57.644 -18.480 -1.833 1.00 85.12 A C ANISOU 768 CB LEU A 110 11251 10140 10950 458 -2561 1418 A C ATOM 769 CG LEU A 110 57.976 -18.764 -0.387 1.00 92.11 A C ANISOU 769 CG LEU A 110 12312 10932 11754 350 -2607 1546 A C ATOM 770 CD1 LEU A 110 59.139 -17.880 0.036 1.00 86.31 A C ANISOU 770 CD1 LEU A 110 11477 10410 10906 359 -2637 1617 A C ATOM 771 CD2 LEU A 110 56.740 -18.525 0.465 1.00 94.15 A C ANISOU 771 CD2 LEU A 110 12703 11045 12023 98 -2477 1572 A C ATOM 772 N ALA A 111 58.097 -21.165 -3.639 1.00 99.57 A N ANISOU 772 N ALA A 111 13111 11784 12936 938 -2827 1235 A N ATOM 773 CA ALA A 111 58.201 -22.620 -3.658 1.00100.82 A C ANISOU 773 CA ALA A 111 13416 11735 13157 1069 -2957 1207 A C ATOM 774 C ALA A 111 59.599 -23.032 -4.136 1.00107.83 A C ANISOU 774 C ALA A 111 14220 12759 13991 1350 -3105 1204 A C ATOM 775 O ALA A 111 60.312 -23.784 -3.456 1.00 98.00 A O ANISOU 775 O ALA A 111 13102 11427 12708 1434 -3224 1283 A O ATOM 776 CB ALA A 111 57.120 -23.219 -4.545 1.00 90.22 A C ANISOU 776 CB ALA A 111 12079 10251 11948 1082 -2935 1054 A C ATOM 777 N GLY A 112 59.980 -22.513 -5.303 1.00109.63 A N ANISOU 777 N GLY A 112 14233 13213 14208 1502 -3091 1114 A N ATOM 778 CA GLY A 112 61.267 -22.797 -5.908 1.00110.10 A C ANISOU 778 CA GLY A 112 14172 13445 14215 1774 -3208 1093 A C ATOM 779 C GLY A 112 62.439 -22.270 -5.109 1.00112.65 A C ANISOU 779 C GLY A 112 14445 13934 14424 1771 -3246 1224 A C ATOM 780 O GLY A 112 63.588 -22.656 -5.344 1.00116.18 A O ANISOU 780 O GLY A 112 14815 14506 14823 1992 -3363 1224 A O ATOM 781 N LEU A 113 62.153 -21.379 -4.166 1.00109.09 A N ANISOU 781 N LEU A 113 14028 13495 13927 1525 -3151 1323 A N ATOM 782 CA LEU A 113 63.175 -20.887 -3.250 1.00106.53 A C ANISOU 782 CA LEU A 113 13674 13308 13495 1489 -3194 1439 A C ATOM 783 C LEU A 113 63.351 -21.827 -2.073 1.00105.24 A C ANISOU 783 C LEU A 113 13738 12951 13298 1484 -3309 1531 A C ATOM 784 O LEU A 113 64.449 -21.978 -1.547 1.00115.01 A O ANISOU 784 O LEU A 113 14960 14290 14450 1588 -3423 1596 A O ATOM 785 CB LEU A 113 62.814 -19.503 -2.723 1.00103.65 A C ANISOU 785 CB LEU A 113 13255 13038 13090 1233 -3048 1495 A C ATOM 786 CG LEU A 113 62.918 -18.372 -3.729 1.00107.40 A C ANISOU 786 CG LEU A 113 13499 13738 13570 1237 -2936 1444 A C ATOM 787 CD1 LEU A 113 63.178 -17.104 -2.975 1.00102.08 A C ANISOU 787 CD1 LEU A 113 12769 13186 12831 1034 -2853 1524 A C ATOM 788 CD2 LEU A 113 64.045 -18.647 -4.715 1.00115.05 A C ANISOU 788 CD2 LEU A 113 14286 14907 14520 1504 -3021 1398 A C ATOM 789 N LEU A 114 62.258 -22.451 -1.656 1.00100.41 A N ANISOU 789 N LEU A 114 13336 12064 12751 1361 -3275 1538 A N ATOM 790 CA LEU A 114 62.282 -23.297 -0.479 1.00107.54 A C ANISOU 790 CA LEU A 114 14483 12759 13618 1327 -3357 1647 A C ATOM 791 C LEU A 114 62.795 -24.694 -0.804 1.00109.71 A C ANISOU 791 C LEU A 114 14856 12896 13932 1588 -3521 1620 A C ATOM 792 O LEU A 114 63.234 -25.415 0.085 1.00109.52 A O ANISOU 792 O LEU A 114 15010 12752 13852 1643 -3628 1722 A O ATOM 793 CB LEU A 114 60.901 -23.359 0.176 1.00110.12 A C ANISOU 793 CB LEU A 114 14996 12850 13995 1067 -3235 1680 A C ATOM 794 CG LEU A 114 60.469 -22.115 0.956 1.00105.25 A C ANISOU 794 CG LEU A 114 14354 12330 13308 806 -3095 1742 A C ATOM 795 CD1 LEU A 114 59.153 -22.367 1.683 1.00102.19 A C ANISOU 795 CD1 LEU A 114 14165 11702 12961 572 -2984 1782 A C ATOM 796 CD2 LEU A 114 61.554 -21.670 1.937 1.00100.91 A C ANISOU 796 CD2 LEU A 114 13800 11935 12607 811 -3169 1854 A C ATOM 797 N SER A 115 62.743 -25.067 -2.079 1.00111.73 A N ANISOU 797 N SER A 115 15005 13171 14278 1759 -3543 1480 A N ATOM 798 CA SER A 115 63.254 -26.360 -2.520 1.00117.78 A C ANISOU 798 CA SER A 115 15848 13815 15087 2031 -3701 1427 A C ATOM 799 C SER A 115 64.761 -26.288 -2.755 1.00127.51 A C ANISOU 799 C SER A 115 16917 15308 16223 2288 -3825 1433 A C ATOM 800 O SER A 115 65.525 -27.080 -2.200 1.00131.07 A O ANISOU 800 O SER A 115 17482 15694 16626 2450 -3972 1498 A O ATOM 801 CB SER A 115 62.553 -26.803 -3.799 1.00119.09 A C ANISOU 801 CB SER A 115 15965 13901 15384 2115 -3678 1254 A C ATOM 802 OG SER A 115 62.795 -25.879 -4.846 1.00120.16 A O ANISOU 802 OG SER A 115 15829 14328 15496 2179 -3612 1162 A O ATOM 803 N ASN A 116 65.182 -25.340 -3.589 1.00129.65 A N ANISOU 803 N ASN A 116 16918 15878 16466 2329 -3764 1368 A N ATOM 804 CA ASN A 116 66.602 -25.095 -3.818 1.00130.10 A C ANISOU 804 CA ASN A 116 16776 16224 16430 2536 -3853 1375 A C ATOM 805 C ASN A 116 67.338 -24.978 -2.481 1.00129.79 A C ANISOU 805 C ASN A 116 16809 16223 16281 2485 -3932 1518 A C ATOM 806 O ASN A 116 66.939 -24.200 -1.609 1.00124.32 A O ANISOU 806 O ASN A 116 16164 15527 15546 2227 -3843 1606 A O ATOM 807 CB ASN A 116 66.790 -23.830 -4.659 1.00125.78 A C ANISOU 807 CB ASN A 116 15946 15981 15863 2489 -3727 1326 A C ATOM 808 CG ASN A 116 68.226 -23.624 -5.093 1.00127.31 A C ANISOU 808 CG ASN A 116 15905 16487 15979 2709 -3803 1313 A C ATOM 809 ND2 ASN A 116 68.438 -23.536 -6.399 1.00122.03 A N ANISOU 809 ND2 ASN A 116 15049 15986 15331 2879 -3772 1203 A N ATOM 810 OD1 ASN A 116 69.134 -23.543 -4.267 1.00132.38 A O ANISOU 810 OD1 ASN A 116 16526 17232 16538 2729 -3889 1397 A O ATOM 811 N VAL A 117 68.408 -25.754 -2.319 1.00128.99 A N ANISOU 811 N VAL A 117 16716 16166 16127 2742 -4104 1534 A N ATOM 812 CA VAL A 117 69.035 -25.893 -1.004 1.00125.39 A C ANISOU 812 CA VAL A 117 16375 15705 15562 2729 -4208 1667 A C ATOM 813 C VAL A 117 70.172 -24.905 -0.726 1.00132.37 A C ANISOU 813 C VAL A 117 17012 16946 16334 2727 -4229 1698 A C ATOM 814 O VAL A 117 70.595 -24.753 0.423 1.00126.95 A O ANISOU 814 O VAL A 117 16397 16292 15547 2661 -4295 1801 A O ATOM 815 CB VAL A 117 69.506 -27.339 -0.724 1.00115.04 A C ANISOU 815 CB VAL A 117 15260 14205 14244 2999 -4398 1691 A C ATOM 816 CG1 VAL A 117 69.225 -27.696 0.730 1.00111.67 A C ANISOU 816 CG1 VAL A 117 15115 13564 13749 2871 -4440 1849 A C ATOM 817 CG2 VAL A 117 68.818 -28.336 -1.659 1.00109.48 A C ANISOU 817 CG2 VAL A 117 14666 13253 13677 3123 -4404 1581 A C ATOM 818 N LEU A 118 70.657 -24.231 -1.768 1.00143.99 A N ANISOU 818 N LEU A 118 18197 18688 17823 2792 -4171 1608 A N ATOM 819 CA LEU A 118 71.665 -23.182 -1.592 1.00149.55 A C ANISOU 819 CA LEU A 118 18644 19733 18446 2747 -4162 1629 A C ATOM 820 C LEU A 118 71.031 -21.914 -1.022 1.00144.54 A C ANISOU 820 C LEU A 118 18001 19119 17800 2397 -4004 1683 A C ATOM 821 O LEU A 118 71.678 -21.142 -0.316 1.00146.13 A O ANISOU 821 O LEU A 118 18098 19502 17922 2287 -4017 1731 A O ATOM 822 CB LEU A 118 72.372 -22.853 -2.912 1.00154.23 A C ANISOU 822 CB LEU A 118 18934 20607 19061 2918 -4129 1527 A C ATOM 823 CG LEU A 118 73.179 -23.933 -3.635 1.00152.04 A C ANISOU 823 CG LEU A 118 18594 20391 18784 3292 -4274 1448 A C ATOM 824 CD1 LEU A 118 72.269 -24.751 -4.552 1.00149.80 A C ANISOU 824 CD1 LEU A 118 18444 19874 18600 3399 -4249 1357 A C ATOM 825 CD2 LEU A 118 74.326 -23.304 -4.425 1.00143.10 A C ANISOU 825 CD2 LEU A 118 17107 19651 17614 3418 -4257 1394 A C ATOM 826 N VAL A 119 69.763 -21.699 -1.345 1.00136.31 A N ANISOU 826 N VAL A 119 17062 17892 16839 2227 -3860 1662 A N ATOM 827 CA VAL A 119 69.027 -20.565 -0.816 1.00129.88 A C ANISOU 827 CA VAL A 119 16266 17063 16020 1908 -3707 1705 A C ATOM 828 C VAL A 119 68.936 -20.707 0.692 1.00125.24 A C ANISOU 828 C VAL A 119 15887 16352 15348 1776 -3768 1811 A C ATOM 829 O VAL A 119 68.595 -21.774 1.193 1.00124.54 A O ANISOU 829 O VAL A 119 16035 16030 15256 1845 -3851 1855 A O ATOM 830 CB VAL A 119 67.606 -20.523 -1.382 1.00128.10 A C ANISOU 830 CB VAL A 119 16140 16636 15896 1783 -3562 1659 A C ATOM 831 CG1 VAL A 119 67.077 -19.096 -1.353 1.00130.55 A C ANISOU 831 CG1 VAL A 119 16355 17036 16212 1519 -3384 1666 A C ATOM 832 CG2 VAL A 119 67.584 -21.081 -2.800 1.00119.87 A C ANISOU 832 CG2 VAL A 119 14999 15614 14931 2007 -3569 1547 A C ATOM 833 N LYS A 120 69.244 -19.641 1.420 1.00122.25 A N ANISOU 833 N LYS A 120 15428 16125 14897 1588 -3727 1852 A N ATOM 834 CA LYS A 120 69.201 -19.703 2.882 1.00125.42 A C ANISOU 834 CA LYS A 120 16019 16442 15194 1468 -3788 1948 A C ATOM 835 C LYS A 120 68.627 -18.424 3.495 1.00118.89 A C ANISOU 835 C LYS A 120 15186 15645 14342 1157 -3643 1965 A C ATOM 836 O LYS A 120 68.882 -17.312 3.008 1.00108.52 A O ANISOU 836 O LYS A 120 13657 14519 13057 1060 -3550 1916 A O ATOM 837 CB LYS A 120 70.589 -20.016 3.466 1.00128.76 A C ANISOU 837 CB LYS A 120 16368 17050 15505 1644 -3981 1979 A C ATOM 838 CG LYS A 120 71.130 -21.405 3.125 1.00129.35 A C ANISOU 838 CG LYS A 120 16506 17058 15584 1968 -4146 1976 A C ATOM 839 CD LYS A 120 72.603 -21.556 3.523 1.00133.26 A C ANISOU 839 CD LYS A 120 16860 17802 15973 2163 -4333 1985 A C ATOM 840 CE LYS A 120 72.813 -21.367 5.031 1.00132.50 A C ANISOU 840 CE LYS A 120 16897 17714 15732 2052 -4414 2078 A C ATOM 841 NZ LYS A 120 74.211 -21.645 5.510 1.00117.97 A N1+ ANISOU 841 NZ LYS A 120 14940 16106 13776 2265 -4621 2085 A N1+ ATOM 842 N PHE A 121 67.852 -18.594 4.566 1.00113.79 A N ANISOU 842 N PHE A 121 14785 14808 13641 1006 -3619 2038 A N ATOM 843 CA PHE A 121 67.123 -17.483 5.172 1.00109.58 A C ANISOU 843 CA PHE A 121 14284 14266 13087 718 -3473 2047 A C ATOM 844 C PHE A 121 67.596 -17.160 6.583 1.00103.72 A C ANISOU 844 C PHE A 121 13621 13597 12191 622 -3551 2110 A C ATOM 845 O PHE A 121 67.644 -18.032 7.458 1.00103.09 A O ANISOU 845 O PHE A 121 13746 13406 12017 692 -3658 2194 A O ATOM 846 CB PHE A 121 65.611 -17.776 5.212 1.00118.07 A C ANISOU 846 CB PHE A 121 15565 15070 14227 582 -3338 2061 A C ATOM 847 CG PHE A 121 64.927 -17.717 3.861 1.00124.46 A C ANISOU 847 CG PHE A 121 16275 15830 15183 607 -3224 1975 A C ATOM 848 CD1 PHE A 121 64.694 -16.494 3.232 1.00123.26 A C ANISOU 848 CD1 PHE A 121 15945 15805 15084 486 -3084 1912 A C ATOM 849 CD2 PHE A 121 64.491 -18.884 3.235 1.00123.21 A C ANISOU 849 CD2 PHE A 121 16213 15491 15109 754 -3258 1955 A C ATOM 850 CE1 PHE A 121 64.065 -16.437 1.999 1.00114.69 A C ANISOU 850 CE1 PHE A 121 14773 14688 14115 526 -2986 1836 A C ATOM 851 CE2 PHE A 121 63.859 -18.836 2.001 1.00120.16 A C ANISOU 851 CE2 PHE A 121 15733 15075 14846 786 -3166 1862 A C ATOM 852 CZ PHE A 121 63.645 -17.611 1.382 1.00116.63 A C ANISOU 852 CZ PHE A 121 15104 14775 14434 679 -3031 1805 A C ATOM 853 N THR A 122 67.931 -15.895 6.805 1.00 98.11 A N ANISOU 853 N THR A 122 12755 13071 11453 463 -3497 2070 A N ATOM 854 CA THR A 122 68.179 -15.415 8.155 1.00103.92 A C ANISOU 854 CA THR A 122 13570 13870 12045 330 -3546 2106 A C ATOM 855 C THR A 122 66.839 -15.115 8.827 1.00109.26 A C ANISOU 855 C THR A 122 14460 14353 12702 107 -3397 2138 A C ATOM 856 O THR A 122 65.816 -14.996 8.159 1.00109.98 A O ANISOU 856 O THR A 122 14574 14307 12906 29 -3245 2112 A O ATOM 857 CB THR A 122 69.076 -14.165 8.143 1.00104.64 A C ANISOU 857 CB THR A 122 13408 14227 12124 234 -3549 2034 A C ATOM 858 CG2 THR A 122 69.462 -13.807 6.717 1.00 99.51 A C ANISOU 858 CG2 THR A 122 12502 13695 11613 308 -3488 1966 A C ATOM 859 OG1 THR A 122 68.385 -13.061 8.738 1.00114.19 A O ANISOU 859 OG1 THR A 122 14667 15406 13313 -31 -3415 2011 A O ATOM 860 N LEU A 123 66.834 -15.007 10.146 1.00108.84 A N ANISOU 860 N LEU A 123 14557 14298 12498 12 -3441 2190 A N ATOM 861 CA LEU A 123 65.606 -14.659 10.846 1.00108.33 A C ANISOU 861 CA LEU A 123 14681 14079 12399 -201 -3293 2216 A C ATOM 862 C LEU A 123 65.058 -13.308 10.386 1.00113.89 A C ANISOU 862 C LEU A 123 15249 14830 13195 -401 -3117 2122 A C ATOM 863 O LEU A 123 63.850 -13.127 10.287 1.00113.14 A O ANISOU 863 O LEU A 123 15249 14583 13156 -529 -2957 2117 A O ATOM 864 CB LEU A 123 65.837 -14.618 12.351 1.00103.14 A C ANISOU 864 CB LEU A 123 14182 13464 11541 -263 -3374 2275 A C ATOM 865 CG LEU A 123 64.541 -14.780 13.134 1.00 99.78 A C ANISOU 865 CG LEU A 123 14014 12840 11058 -419 -3241 2341 A C ATOM 866 CD1 LEU A 123 63.941 -16.153 12.843 1.00 91.86 A C ANISOU 866 CD1 LEU A 123 13191 11601 10112 -305 -3238 2433 A C ATOM 867 CD2 LEU A 123 64.770 -14.588 14.618 1.00101.90 A C ANISOU 867 CD2 LEU A 123 14428 13180 11108 -486 -3308 2390 A C ATOM 868 N SER A 124 65.950 -12.357 10.123 1.00118.19 A N ANISOU 868 N SER A 124 15569 15583 13755 -427 -3146 2049 A N ATOM 869 CA SER A 124 65.546 -11.023 9.695 1.00112.20 A C ANISOU 869 CA SER A 124 14685 14865 13083 -608 -2987 1967 A C ATOM 870 C SER A 124 64.864 -11.066 8.343 1.00112.86 A C ANISOU 870 C SER A 124 14694 14857 13331 -567 -2858 1941 A C ATOM 871 O SER A 124 63.890 -10.348 8.105 1.00105.94 A O ANISOU 871 O SER A 124 13836 13898 12518 -709 -2692 1906 A O ATOM 872 CB SER A 124 66.755 -10.096 9.620 1.00116.83 A C ANISOU 872 CB SER A 124 15039 15685 13666 -636 -3053 1901 A C ATOM 873 OG SER A 124 67.215 -9.760 10.914 1.00128.44 A O ANISOU 873 OG SER A 124 16569 17245 14986 -724 -3146 1894 A O ATOM 874 N GLU A 125 65.389 -11.905 7.454 1.00119.91 A N ANISOU 874 N GLU A 125 15500 15776 14285 -359 -2940 1952 A N ATOM 875 CA GLU A 125 64.809 -12.070 6.126 1.00121.30 A C ANISOU 875 CA GLU A 125 15605 15882 14603 -286 -2841 1920 A C ATOM 876 C GLU A 125 63.432 -12.731 6.210 1.00111.75 A C ANISOU 876 C GLU A 125 14602 14432 13425 -326 -2753 1944 A C ATOM 877 O GLU A 125 62.507 -12.336 5.510 1.00110.80 A O ANISOU 877 O GLU A 125 14457 14241 13402 -389 -2610 1899 A O ATOM 878 CB GLU A 125 65.752 -12.864 5.210 1.00132.44 A C ANISOU 878 CB GLU A 125 16878 17390 16055 -39 -2962 1916 A C ATOM 879 CG GLU A 125 67.071 -12.149 4.898 1.00143.53 A C ANISOU 879 CG GLU A 125 18030 19052 17454 -4 -3018 1882 A C ATOM 880 CD GLU A 125 67.866 -12.811 3.777 1.00150.75 A C ANISOU 880 CD GLU A 125 18779 20077 18424 241 -3096 1863 A C ATOM 881 OE1 GLU A 125 68.005 -14.055 3.786 1.00150.09 A O ANISOU 881 OE1 GLU A 125 18791 19918 18318 431 -3217 1890 A O ATOM 882 OE2 GLU A 125 68.361 -12.081 2.888 1.00152.38 A O1- ANISOU 882 OE2 GLU A 125 18763 20443 18692 248 -3033 1823 A O1- ATOM 883 N ILE A 126 63.297 -13.724 7.081 1.00106.49 A N ANISOU 883 N ILE A 126 14138 13647 12677 -291 -2839 2015 A N ATOM 884 CA ILE A 126 62.022 -14.412 7.273 1.00 99.26 A C ANISOU 884 CA ILE A 126 13423 12498 11791 -350 -2754 2047 A C ATOM 885 C ILE A 126 60.946 -13.508 7.871 1.00 94.13 A C ANISOU 885 C ILE A 126 12849 11793 11122 -588 -2587 2029 A C ATOM 886 O ILE A 126 59.816 -13.488 7.402 1.00 90.18 A O ANISOU 886 O ILE A 126 12378 11173 10715 -656 -2454 1995 A O ATOM 887 CB ILE A 126 62.171 -15.652 8.176 1.00 97.78 A C ANISOU 887 CB ILE A 126 13456 12188 11509 -270 -2876 2149 A C ATOM 888 CG1 ILE A 126 62.962 -16.744 7.462 1.00103.72 A C ANISOU 888 CG1 ILE A 126 14167 12936 12307 -13 -3027 2158 A C ATOM 889 CG2 ILE A 126 60.810 -16.184 8.576 1.00 85.82 A C ANISOU 889 CG2 ILE A 126 12153 10438 10015 -391 -2761 2190 A C ATOM 890 CD1 ILE A 126 63.122 -17.993 8.276 1.00109.21 A C ANISOU 890 CD1 ILE A 126 15090 13487 12917 87 -3150 2265 A C ATOM 891 N LYS A 127 61.286 -12.775 8.922 1.00 94.61 A N ANISOU 891 N LYS A 127 12941 11947 11059 -707 -2598 2044 A N ATOM 892 CA LYS A 127 60.329 -11.856 9.508 1.00 87.67 A C ANISOU 892 CA LYS A 127 12127 11030 10154 -920 -2443 2015 A C ATOM 893 C LYS A 127 59.757 -10.975 8.403 1.00 91.03 A C ANISOU 893 C LYS A 127 12397 11469 10721 -966 -2300 1925 A C ATOM 894 O LYS A 127 58.563 -10.659 8.401 1.00 92.65 A O ANISOU 894 O LYS A 127 12662 11573 10967 -1082 -2150 1896 A O ATOM 895 CB LYS A 127 60.984 -10.995 10.592 1.00 86.23 A C ANISOU 895 CB LYS A 127 11947 10987 9830 -1024 -2489 2008 A C ATOM 896 CG LYS A 127 61.470 -11.776 11.796 1.00 94.48 A C ANISOU 896 CG LYS A 127 13162 12033 10705 -980 -2626 2098 A C ATOM 897 CD LYS A 127 61.704 -10.884 13.019 1.00 97.96 A C ANISOU 897 CD LYS A 127 13649 12581 10990 -1122 -2634 2076 A C ATOM 898 CE LYS A 127 62.167 -11.728 14.207 1.00 97.93 A C ANISOU 898 CE LYS A 127 13826 12586 10796 -1054 -2777 2176 A C ATOM 899 NZ LYS A 127 62.234 -10.983 15.493 1.00101.46 A N1+ ANISOU 899 NZ LYS A 127 14356 13127 11066 -1187 -2781 2155 A N1+ ATOM 900 N ARG A 128 60.616 -10.594 7.459 1.00 87.94 A N ANISOU 900 N ARG A 128 11804 11210 10397 -867 -2345 1886 A N ATOM 901 CA ARG A 128 60.243 -9.652 6.405 1.00 85.57 A C ANISOU 901 CA ARG A 128 11352 10946 10213 -897 -2216 1815 A C ATOM 902 C ARG A 128 59.249 -10.265 5.440 1.00 87.23 A C ANISOU 902 C ARG A 128 11574 11032 10535 -823 -2141 1791 A C ATOM 903 O ARG A 128 58.173 -9.725 5.201 1.00 92.72 A O ANISOU 903 O ARG A 128 12283 11662 11286 -916 -1997 1747 A O ATOM 904 CB ARG A 128 61.466 -9.216 5.621 1.00 80.09 A C ANISOU 904 CB ARG A 128 10444 10429 9557 -799 -2281 1795 A C ATOM 905 CG ARG A 128 61.167 -8.138 4.629 1.00 75.67 A C ANISOU 905 CG ARG A 128 9742 9912 9097 -838 -2143 1742 A C ATOM 906 CD ARG A 128 60.961 -6.824 5.342 1.00 86.56 A C ANISOU 906 CD ARG A 128 11140 11305 10444 -1040 -2049 1712 A C ATOM 907 NE ARG A 128 60.417 -5.833 4.427 1.00102.86 A N ANISOU 907 NE ARG A 128 13114 13362 12606 -1076 -1898 1670 A N ATOM 908 CZ ARG A 128 59.165 -5.393 4.465 1.00 99.63 A C ANISOU 908 CZ ARG A 128 12790 12838 12225 -1162 -1760 1638 A C ATOM 909 NH1 ARG A 128 58.336 -5.845 5.395 1.00 94.02 A N1+ ANISOU 909 NH1 ARG A 128 12252 12018 11455 -1238 -1745 1640 A N1+ ATOM 910 NH2 ARG A 128 58.752 -4.491 3.582 1.00 96.58 A N ANISOU 910 NH2 ARG A 128 12320 12455 11922 -1168 -1634 1606 A N ATOM 911 N VAL A 129 59.632 -11.393 4.870 1.00 78.80 A N ANISOU 911 N VAL A 129 10497 9942 9503 -646 -2247 1811 A N ATOM 912 CA VAL A 129 58.741 -12.142 4.014 1.00 76.32 A C ANISOU 912 CA VAL A 129 10204 9502 9291 -569 -2203 1777 A C ATOM 913 C VAL A 129 57.342 -12.249 4.594 1.00 83.07 A C ANISOU 913 C VAL A 129 11215 10194 10155 -723 -2085 1772 A C ATOM 914 O VAL A 129 56.360 -11.929 3.920 1.00 90.24 A O ANISOU 914 O VAL A 129 12078 11060 11151 -756 -1966 1706 A O ATOM 915 CB VAL A 129 59.271 -13.542 3.784 1.00 72.99 A C ANISOU 915 CB VAL A 129 9830 9026 8879 -385 -2351 1808 A C ATOM 916 CG1 VAL A 129 58.125 -14.522 3.659 1.00 61.91 A C ANISOU 916 CG1 VAL A 129 8562 7413 7546 -392 -2312 1795 A C ATOM 917 CG2 VAL A 129 60.153 -13.565 2.558 1.00 83.85 A C ANISOU 917 CG2 VAL A 129 11009 10542 10309 -191 -2415 1767 A C ATOM 918 N MET A 130 57.258 -12.718 5.835 1.00 79.92 A N ANISOU 918 N MET A 130 10993 9712 9659 -809 -2117 1843 A N ATOM 919 CA MET A 130 55.974 -12.894 6.505 1.00 78.70 A C ANISOU 919 CA MET A 130 10993 9411 9499 -963 -2000 1852 A C ATOM 920 C MET A 130 55.256 -11.569 6.652 1.00 77.01 A C ANISOU 920 C MET A 130 10728 9249 9283 -1119 -1844 1793 A C ATOM 921 O MET A 130 54.029 -11.482 6.514 1.00 75.78 A O ANISOU 921 O MET A 130 10596 9009 9187 -1204 -1713 1747 A O ATOM 922 CB MET A 130 56.165 -13.514 7.882 1.00 74.37 A C ANISOU 922 CB MET A 130 10646 8795 8816 -1023 -2060 1957 A C ATOM 923 CG MET A 130 56.568 -14.958 7.825 1.00 86.90 A C ANISOU 923 CG MET A 130 12334 10269 10414 -881 -2192 2025 A C ATOM 924 SD MET A 130 55.455 -15.921 6.793 1.00 89.24 A S ANISOU 924 SD MET A 130 12641 10377 10889 -844 -2131 1968 A S ATOM 925 CE MET A 130 53.913 -15.714 7.685 1.00 85.06 A C ANISOU 925 CE MET A 130 12251 9726 10344 -1096 -1939 1980 A C ATOM 926 N GLN A 131 56.030 -10.534 6.933 1.00 66.33 A N ANISOU 926 N GLN A 131 9301 8036 7865 -1153 -1860 1786 A N ATOM 927 CA GLN A 131 55.449 -9.236 7.123 1.00 66.65 A C ANISOU 927 CA GLN A 131 9307 8115 7902 -1291 -1722 1728 A C ATOM 928 C GLN A 131 54.790 -8.778 5.827 1.00 69.13 A C ANISOU 928 C GLN A 131 9487 8431 8351 -1241 -1621 1650 A C ATOM 929 O GLN A 131 53.625 -8.408 5.828 1.00 69.57 A O ANISOU 929 O GLN A 131 9566 8425 8441 -1326 -1488 1601 A O ATOM 930 CB GLN A 131 56.495 -8.245 7.609 1.00 74.41 A C ANISOU 930 CB GLN A 131 10232 9236 8806 -1336 -1771 1727 A C ATOM 931 CG GLN A 131 55.900 -6.893 7.873 1.00 87.72 A C ANISOU 931 CG GLN A 131 11904 10938 10488 -1480 -1631 1662 A C ATOM 932 CD GLN A 131 56.748 -6.061 8.784 1.00 89.02 A C ANISOU 932 CD GLN A 131 12074 11199 10548 -1573 -1680 1657 A C ATOM 933 NE2 GLN A 131 56.179 -5.686 9.939 1.00 96.23 A N ANISOU 933 NE2 GLN A 131 13123 12080 11359 -1712 -1619 1642 A N ATOM 934 OE1 GLN A 131 57.903 -5.747 8.463 1.00 70.05 A O ANISOU 934 OE1 GLN A 131 9550 8909 8156 -1522 -1772 1657 A O ATOM 935 N MET A 132 55.527 -8.823 4.721 1.00 75.06 A N ANISOU 935 N MET A 132 10092 9261 9168 -1091 -1685 1639 A N ATOM 936 CA MET A 132 54.974 -8.470 3.414 1.00 70.61 A C ANISOU 936 CA MET A 132 9401 8712 8716 -1012 -1604 1573 A C ATOM 937 C MET A 132 53.743 -9.307 3.083 1.00 77.31 A C ANISOU 937 C MET A 132 10305 9435 9635 -998 -1555 1531 A C ATOM 938 O MET A 132 52.775 -8.812 2.517 1.00 79.23 A O ANISOU 938 O MET A 132 10496 9665 9941 -1013 -1442 1463 A O ATOM 939 CB MET A 132 56.013 -8.664 2.313 1.00 63.24 A C ANISOU 939 CB MET A 132 8318 7887 7824 -832 -1695 1578 A C ATOM 940 CG MET A 132 57.217 -7.761 2.410 1.00 68.79 A C ANISOU 940 CG MET A 132 8922 8733 8484 -847 -1727 1607 A C ATOM 941 SD MET A 132 58.307 -7.965 0.992 1.00 82.01 A S ANISOU 941 SD MET A 132 10398 10551 10211 -633 -1800 1610 A S ATOM 942 CE MET A 132 59.077 -9.523 1.399 1.00118.93 A C ANISOU 942 CE MET A 132 15139 15208 14842 -509 -1990 1652 A C ATOM 943 N LEU A 133 53.781 -10.585 3.429 1.00 75.64 A N ANISOU 943 N LEU A 133 10196 9128 9416 -966 -1643 1569 A N ATOM 944 CA LEU A 133 52.682 -11.477 3.099 1.00 69.73 A C ANISOU 944 CA LEU A 133 9495 8248 8751 -964 -1606 1524 A C ATOM 945 C LEU A 133 51.440 -11.222 3.936 1.00 69.49 A C ANISOU 945 C LEU A 133 9564 8134 8706 -1150 -1469 1509 A C ATOM 946 O LEU A 133 50.337 -11.212 3.406 1.00 73.03 A O ANISOU 946 O LEU A 133 9967 8542 9239 -1170 -1377 1429 A O ATOM 947 CB LEU A 133 53.123 -12.925 3.216 1.00 76.46 A C ANISOU 947 CB LEU A 133 10442 8999 9611 -877 -1738 1574 A C ATOM 948 CG LEU A 133 52.007 -13.945 3.076 1.00 73.48 A C ANISOU 948 CG LEU A 133 10142 8454 9324 -911 -1703 1534 A C ATOM 949 CD1 LEU A 133 52.469 -15.129 2.248 1.00 78.64 A C ANISOU 949 CD1 LEU A 133 10781 9046 10052 -730 -1836 1514 A C ATOM 950 CD2 LEU A 133 51.592 -14.379 4.450 1.00 75.77 A C ANISOU 950 CD2 LEU A 133 10625 8622 9543 -1077 -1667 1619 A C ATOM 951 N LEU A 134 51.614 -11.013 5.238 1.00 71.91 A N ANISOU 951 N LEU A 134 9996 8430 8898 -1280 -1456 1579 A N ATOM 952 CA LEU A 134 50.494 -10.607 6.097 1.00 71.10 A C ANISOU 952 CA LEU A 134 9978 8278 8758 -1457 -1312 1564 A C ATOM 953 C LEU A 134 49.925 -9.224 5.727 1.00 69.23 A C ANISOU 953 C LEU A 134 9631 8126 8546 -1496 -1186 1477 A C ATOM 954 O LEU A 134 48.749 -8.944 5.914 1.00 69.26 A O ANISOU 954 O LEU A 134 9646 8097 8573 -1591 -1055 1421 A O ATOM 955 CB LEU A 134 50.884 -10.673 7.578 1.00 58.43 A C ANISOU 955 CB LEU A 134 8537 6661 7002 -1569 -1333 1658 A C ATOM 956 CG LEU A 134 51.039 -12.131 8.036 1.00 71.68 A C ANISOU 956 CG LEU A 134 10363 8214 8660 -1550 -1420 1751 A C ATOM 957 CD1 LEU A 134 51.592 -12.273 9.448 1.00 61.49 A C ANISOU 957 CD1 LEU A 134 9240 6926 7197 -1622 -1467 1860 A C ATOM 958 CD2 LEU A 134 49.697 -12.865 7.908 1.00 79.24 A C ANISOU 958 CD2 LEU A 134 11367 9031 9712 -1631 -1314 1722 A C ATOM 959 N ASN A 135 50.766 -8.359 5.192 1.00 63.48 A N ANISOU 959 N ASN A 135 8796 7506 7816 -1419 -1221 1466 A N ATOM 960 CA ASN A 135 50.304 -7.068 4.738 1.00 66.88 A C ANISOU 960 CA ASN A 135 9134 7998 8279 -1434 -1109 1395 A C ATOM 961 C ASN A 135 49.481 -7.239 3.464 1.00 71.29 A C ANISOU 961 C ASN A 135 9580 8550 8958 -1328 -1062 1317 A C ATOM 962 O ASN A 135 48.388 -6.691 3.327 1.00 67.31 A O ANISOU 962 O ASN A 135 9048 8038 8489 -1369 -942 1245 A O ATOM 963 CB ASN A 135 51.502 -6.158 4.480 1.00 68.91 A C ANISOU 963 CB ASN A 135 9312 8361 8511 -1387 -1160 1418 A C ATOM 964 CG ASN A 135 51.174 -4.706 4.666 1.00 72.90 A C ANISOU 964 CG ASN A 135 9798 8898 9003 -1469 -1043 1372 A C ATOM 965 ND2 ASN A 135 51.580 -3.883 3.716 1.00 74.25 A N ANISOU 965 ND2 ASN A 135 9850 9134 9229 -1388 -1024 1358 A N ATOM 966 OD1 ASN A 135 50.553 -4.324 5.652 1.00 82.22 A O ANISOU 966 OD1 ASN A 135 11076 10043 10123 -1600 -965 1351 A O ATOM 967 N GLY A 136 50.024 -8.004 2.528 1.00 80.68 A N ANISOU 967 N GLY A 136 10699 9751 10204 -1179 -1166 1323 A N ATOM 968 CA GLY A 136 49.323 -8.317 1.301 1.00 82.12 A C ANISOU 968 CA GLY A 136 10777 9935 10490 -1061 -1148 1240 A C ATOM 969 C GLY A 136 47.934 -8.838 1.594 1.00 77.09 A C ANISOU 969 C GLY A 136 10186 9203 9901 -1155 -1067 1176 A C ATOM 970 O GLY A 136 46.972 -8.445 0.935 1.00 75.85 A O ANISOU 970 O GLY A 136 9942 9072 9805 -1126 -985 1084 A O ATOM 971 N LEU A 137 47.823 -9.718 2.587 1.00 64.22 A N ANISOU 971 N LEU A 137 8691 7469 8240 -1268 -1088 1228 A N ATOM 972 CA LEU A 137 46.513 -10.219 3.000 1.00 61.06 A C ANISOU 972 CA LEU A 137 8339 6978 7884 -1392 -994 1179 A C ATOM 973 C LEU A 137 45.597 -9.126 3.564 1.00 64.17 A C ANISOU 973 C LEU A 137 8726 7414 8240 -1512 -838 1135 A C ATOM 974 O LEU A 137 44.512 -8.909 3.048 1.00 76.23 A O ANISOU 974 O LEU A 137 10164 8959 9841 -1509 -751 1034 A O ATOM 975 CB LEU A 137 46.647 -11.387 3.976 1.00 46.05 A C ANISOU 975 CB LEU A 137 6601 4947 5949 -1490 -1040 1267 A C ATOM 976 CG LEU A 137 47.058 -12.722 3.343 1.00 51.14 A C ANISOU 976 CG LEU A 137 7259 5501 6673 -1379 -1171 1275 A C ATOM 977 CD1 LEU A 137 47.204 -13.806 4.398 1.00 49.86 A C ANISOU 977 CD1 LEU A 137 7284 5192 6467 -1477 -1208 1382 A C ATOM 978 CD2 LEU A 137 46.078 -13.174 2.258 1.00 52.28 A C ANISOU 978 CD2 LEU A 137 7289 5614 6961 -1328 -1148 1143 A C ATOM 979 N TYR A 138 46.041 -8.433 4.606 1.00 64.52 A N ANISOU 979 N TYR A 138 8860 7484 8169 -1606 -808 1200 A N ATOM 980 CA TYR A 138 45.292 -7.312 5.169 1.00 60.37 A C ANISOU 980 CA TYR A 138 8337 7002 7597 -1704 -667 1152 A C ATOM 981 C TYR A 138 44.674 -6.465 4.062 1.00 63.94 A C ANISOU 981 C TYR A 138 8639 7525 8132 -1600 -603 1047 A C ATOM 982 O TYR A 138 43.529 -6.041 4.146 1.00 67.34 A O ANISOU 982 O TYR A 138 9033 7967 8584 -1648 -482 966 A O ATOM 983 CB TYR A 138 46.218 -6.444 6.025 1.00 61.05 A C ANISOU 983 CB TYR A 138 8500 7135 7561 -1755 -685 1214 A C ATOM 984 CG TYR A 138 45.575 -5.186 6.570 1.00 77.16 A C ANISOU 984 CG TYR A 138 10549 9216 9552 -1837 -550 1154 A C ATOM 985 CD1 TYR A 138 44.958 -5.183 7.815 1.00 82.36 A C ANISOU 985 CD1 TYR A 138 11321 9854 10119 -1987 -460 1159 A C ATOM 986 CD2 TYR A 138 45.593 -3.996 5.846 1.00 80.75 A C ANISOU 986 CD2 TYR A 138 10907 9729 10046 -1757 -510 1096 A C ATOM 987 CE1 TYR A 138 44.374 -4.031 8.334 1.00 79.86 A C ANISOU 987 CE1 TYR A 138 11015 9577 9752 -2049 -338 1091 A C ATOM 988 CE2 TYR A 138 45.000 -2.840 6.350 1.00 79.85 A C ANISOU 988 CE2 TYR A 138 10813 9635 9891 -1820 -390 1035 A C ATOM 989 CZ TYR A 138 44.389 -2.866 7.596 1.00 82.03 A C ANISOU 989 CZ TYR A 138 11197 9895 10078 -1963 -307 1025 A C ATOM 990 OH TYR A 138 43.789 -1.734 8.111 1.00 84.14 A O ANISOU 990 OH TYR A 138 11485 10185 10299 -2013 -188 951 A O ATOM 991 N TYR A 139 45.439 -6.219 3.013 1.00 62.23 A N ANISOU 991 N TYR A 139 8332 7361 7953 -1447 -683 1051 A N ATOM 992 CA TYR A 139 44.981 -5.322 1.977 1.00 60.45 A C ANISOU 992 CA TYR A 139 7981 7207 7782 -1331 -625 974 A C ATOM 993 C TYR A 139 43.770 -5.864 1.276 1.00 61.64 A C ANISOU 993 C TYR A 139 8042 7353 8024 -1285 -587 868 A C ATOM 994 O TYR A 139 42.782 -5.152 1.093 1.00 62.48 A O ANISOU 994 O TYR A 139 8088 7499 8152 -1276 -483 785 A O ATOM 995 CB TYR A 139 46.080 -5.068 0.951 1.00 61.45 A C ANISOU 995 CB TYR A 139 8029 7397 7922 -1172 -715 1014 A C ATOM 996 CG TYR A 139 45.590 -4.299 -0.247 1.00 52.22 A C ANISOU 996 CG TYR A 139 6737 6299 6805 -1028 -661 947 A C ATOM 997 CD1 TYR A 139 45.309 -2.949 -0.151 1.00 46.44 A C ANISOU 997 CD1 TYR A 139 6003 5593 6049 -1039 -557 933 A C ATOM 998 CD2 TYR A 139 45.406 -4.926 -1.475 1.00 55.23 A C ANISOU 998 CD2 TYR A 139 7013 6720 7252 -868 -718 896 A C ATOM 999 CE1 TYR A 139 44.852 -2.241 -1.239 1.00 56.07 A C ANISOU 999 CE1 TYR A 139 7126 6872 7305 -892 -509 885 A C ATOM 1000 CE2 TYR A 139 44.965 -4.222 -2.576 1.00 59.75 A C ANISOU 1000 CE2 TYR A 139 7479 7370 7852 -718 -674 841 A C ATOM 1001 CZ TYR A 139 44.686 -2.880 -2.449 1.00 61.55 A C ANISOU 1001 CZ TYR A 139 7715 7620 8052 -729 -567 843 A C ATOM 1002 OH TYR A 139 44.230 -2.163 -3.526 1.00 61.87 A O ANISOU 1002 OH TYR A 139 7665 7732 8111 -566 -522 801 A O ATOM 1003 N ILE A 140 43.853 -7.127 0.868 1.00 70.67 A N ANISOU 1003 N ILE A 140 9174 8451 9228 -1247 -678 863 A N ATOM 1004 CA ILE A 140 42.817 -7.715 0.023 1.00 68.69 A C ANISOU 1004 CA ILE A 140 8817 8203 9079 -1186 -669 745 A C ATOM 1005 C ILE A 140 41.565 -8.007 0.832 1.00 62.87 A C ANISOU 1005 C ILE A 140 8108 7415 8366 -1356 -560 689 A C ATOM 1006 O ILE A 140 40.451 -7.782 0.378 1.00 66.39 A O ANISOU 1006 O ILE A 140 8446 7909 8871 -1335 -488 571 A O ATOM 1007 CB ILE A 140 43.316 -8.963 -0.758 1.00 59.09 A C ANISOU 1007 CB ILE A 140 7576 6946 7929 -1082 -808 737 A C ATOM 1008 CG1 ILE A 140 43.148 -10.237 0.025 1.00 71.34 A C ANISOU 1008 CG1 ILE A 140 9238 8360 9510 -1220 -836 767 A C ATOM 1009 CG2 ILE A 140 44.785 -8.876 -1.087 1.00 58.77 A C ANISOU 1009 CG2 ILE A 140 7552 6942 7837 -966 -916 832 A C ATOM 1010 CD1 ILE A 140 43.897 -11.363 -0.648 1.00 76.62 A C ANISOU 1010 CD1 ILE A 140 9909 8974 10228 -1102 -986 776 A C ATOM 1011 N HIS A 141 41.762 -8.484 2.051 1.00 61.63 A N ANISOU 1011 N HIS A 141 8092 7171 8153 -1519 -544 775 A N ATOM 1012 CA HIS A 141 40.669 -8.651 2.989 1.00 57.95 A C ANISOU 1012 CA HIS A 141 7668 6667 7684 -1699 -418 747 A C ATOM 1013 C HIS A 141 39.942 -7.341 3.246 1.00 61.26 A C ANISOU 1013 C HIS A 141 8037 7179 8059 -1718 -283 683 A C ATOM 1014 O HIS A 141 38.713 -7.306 3.274 1.00 76.04 A O ANISOU 1014 O HIS A 141 9832 9080 9980 -1774 -179 583 A O ATOM 1015 CB HIS A 141 41.199 -9.212 4.294 1.00 60.15 A C ANISOU 1015 CB HIS A 141 8128 6853 7872 -1849 -425 877 A C ATOM 1016 CG HIS A 141 41.621 -10.640 4.195 1.00 67.63 A C ANISOU 1016 CG HIS A 141 9144 7680 8873 -1853 -533 933 A C ATOM 1017 CD2 HIS A 141 41.463 -11.546 3.200 1.00 69.74 A C ANISOU 1017 CD2 HIS A 141 9335 7897 9266 -1769 -613 867 A C ATOM 1018 ND1 HIS A 141 42.296 -11.289 5.207 1.00 74.66 A N ANISOU 1018 ND1 HIS A 141 10208 8479 9681 -1941 -576 1068 A N ATOM 1019 CE1 HIS A 141 42.530 -12.537 4.839 1.00 86.61 A C ANISOU 1019 CE1 HIS A 141 11756 9878 11273 -1910 -673 1090 A C ATOM 1020 NE2 HIS A 141 42.034 -12.718 3.626 1.00 78.77 A N ANISOU 1020 NE2 HIS A 141 10613 8905 10410 -1810 -698 963 A N ATOM 1021 N ARG A 142 40.708 -6.274 3.439 1.00 51.82 A N ANISOU 1021 N ARG A 142 6882 6029 6777 -1672 -287 736 A N ATOM 1022 CA ARG A 142 40.171 -4.919 3.619 1.00 51.10 A C ANISOU 1022 CA ARG A 142 6759 6010 6645 -1664 -172 677 A C ATOM 1023 C ARG A 142 39.354 -4.514 2.412 1.00 59.88 A C ANISOU 1023 C ARG A 142 7708 7199 7846 -1515 -146 557 A C ATOM 1024 O ARG A 142 38.444 -3.696 2.516 1.00 65.98 A O ANISOU 1024 O ARG A 142 8431 8027 8613 -1510 -35 475 A O ATOM 1025 CB ARG A 142 41.327 -3.930 3.825 1.00 53.79 A C ANISOU 1025 CB ARG A 142 7169 6367 6903 -1626 -210 755 A C ATOM 1026 CG ARG A 142 40.974 -2.458 3.900 1.00 65.96 A C ANISOU 1026 CG ARG A 142 8694 7957 8411 -1596 -109 702 A C ATOM 1027 CD ARG A 142 42.157 -1.627 3.376 1.00 96.11 A C ANISOU 1027 CD ARG A 142 12516 11788 12213 -1496 -177 763 A C ATOM 1028 NE ARG A 142 42.076 -0.219 3.741 1.00120.91 A N ANISOU 1028 NE ARG A 142 15694 14936 15309 -1506 -89 736 A N ATOM 1029 CZ ARG A 142 42.483 0.267 4.912 1.00143.93 A C ANISOU 1029 CZ ARG A 142 18730 17824 18134 -1635 -65 764 A C ATOM 1030 NH1 ARG A 142 42.990 -0.548 5.827 1.00146.95 A N1+ ANISOU 1030 NH1 ARG A 142 19204 18182 18450 -1757 -121 829 A N1+ ATOM 1031 NH2 ARG A 142 42.380 1.564 5.175 1.00154.50 A N ANISOU 1031 NH2 ARG A 142 20103 19156 19444 -1635 12 724 A N ATOM 1032 N ASN A 143 39.694 -5.097 1.265 1.00 66.42 A N ANISOU 1032 N ASN A 143 8454 8037 8747 -1378 -253 544 A N ATOM 1033 CA ASN A 143 39.003 -4.826 0.016 1.00 64.71 A C ANISOU 1033 CA ASN A 143 8081 7904 8601 -1211 -253 431 A C ATOM 1034 C ASN A 143 37.980 -5.892 -0.296 1.00 73.50 A C ANISOU 1034 C ASN A 143 9100 9012 9814 -1245 -256 320 A C ATOM 1035 O ASN A 143 37.583 -6.075 -1.450 1.00 85.76 A O ANISOU 1035 O ASN A 143 10521 10629 11435 -1098 -305 222 A O ATOM 1036 CB ASN A 143 39.996 -4.741 -1.127 1.00 70.00 A C ANISOU 1036 CB ASN A 143 8709 8609 9279 -1023 -366 473 A C ATOM 1037 CG ASN A 143 40.469 -3.344 -1.366 1.00 76.66 A C ANISOU 1037 CG ASN A 143 9561 9501 10063 -929 -326 518 A C ATOM 1038 ND2 ASN A 143 41.440 -2.909 -0.565 1.00 61.70 A N ANISOU 1038 ND2 ASN A 143 7783 7561 8099 -1019 -328 627 A N ATOM 1039 OD1 ASN A 143 39.963 -2.647 -2.259 1.00 82.70 A O ANISOU 1039 OD1 ASN A 143 10233 10343 10846 -776 -294 456 A O ATOM 1040 N LYS A 144 37.569 -6.612 0.738 1.00 72.40 A N ANISOU 1040 N LYS A 144 9032 8797 9679 -1443 -203 335 A N ATOM 1041 CA LYS A 144 36.467 -7.547 0.620 1.00 73.99 A C ANISOU 1041 CA LYS A 144 9145 8984 9983 -1523 -175 226 A C ATOM 1042 C LYS A 144 36.772 -8.687 -0.326 1.00 72.34 A C ANISOU 1042 C LYS A 144 8888 8728 9870 -1444 -313 192 A C ATOM 1043 O LYS A 144 35.854 -9.304 -0.847 1.00 79.62 A O ANISOU 1043 O LYS A 144 9691 9665 10897 -1451 -313 61 A O ATOM 1044 CB LYS A 144 35.213 -6.820 0.142 1.00 79.50 A C ANISOU 1044 CB LYS A 144 9679 9808 10718 -1455 -85 74 A C ATOM 1045 CG LYS A 144 34.748 -5.730 1.075 1.00 86.30 A C ANISOU 1045 CG LYS A 144 10579 10717 11495 -1526 60 80 A C ATOM 1046 CD LYS A 144 34.624 -6.264 2.498 1.00100.79 A C ANISOU 1046 CD LYS A 144 12540 12469 13286 -1769 145 153 A C ATOM 1047 CE LYS A 144 33.992 -5.209 3.373 1.00117.26 A C ANISOU 1047 CE LYS A 144 14642 14623 15289 -1829 297 126 A C ATOM 1048 NZ LYS A 144 33.019 -4.398 2.566 1.00126.43 A N1+ ANISOU 1048 NZ LYS A 144 15628 15913 16496 -1678 345 -25 A N1+ ATOM 1049 N ILE A 145 38.050 -8.978 -0.551 1.00 67.11 A N ANISOU 1049 N ILE A 145 8312 8014 9173 -1367 -431 297 A N ATOM 1050 CA ILE A 145 38.405 -10.120 -1.386 1.00 68.36 A C ANISOU 1050 CA ILE A 145 8440 8117 9415 -1285 -566 264 A C ATOM 1051 C ILE A 145 38.970 -11.265 -0.557 1.00 73.09 A C ANISOU 1051 C ILE A 145 9197 8554 10021 -1426 -614 370 A C ATOM 1052 O ILE A 145 39.747 -11.019 0.365 1.00 72.94 A O ANISOU 1052 O ILE A 145 9318 8495 9902 -1495 -604 510 A O ATOM 1053 CB ILE A 145 39.415 -9.750 -2.479 1.00 62.28 A C ANISOU 1053 CB ILE A 145 7629 7423 8614 -1052 -678 286 A C ATOM 1054 CG1 ILE A 145 38.833 -8.688 -3.396 1.00 63.71 A C ANISOU 1054 CG1 ILE A 145 7665 7757 8787 -892 -635 190 A C ATOM 1055 CG2 ILE A 145 39.741 -10.959 -3.321 1.00 68.87 A C ANISOU 1055 CG2 ILE A 145 8433 8206 9528 -958 -817 235 A C ATOM 1056 CD1 ILE A 145 37.469 -9.042 -3.897 1.00 73.09 A C ANISOU 1056 CD1 ILE A 145 8708 8991 10071 -891 -607 13 A C ATOM 1057 N LEU A 146 38.551 -12.498 -0.878 1.00 68.70 A N ANISOU 1057 N LEU A 146 8620 7902 9581 -1466 -667 298 A N ATOM 1058 CA LEU A 146 39.175 -13.722 -0.354 1.00 69.91 A C ANISOU 1058 CA LEU A 146 8927 7880 9756 -1551 -742 395 A C ATOM 1059 C LEU A 146 40.058 -14.372 -1.422 1.00 77.02 A C ANISOU 1059 C LEU A 146 9807 8759 10698 -1354 -913 371 A C ATOM 1060 O LEU A 146 39.611 -14.598 -2.544 1.00 85.04 A O ANISOU 1060 O LEU A 146 10683 9827 11802 -1236 -967 222 A O ATOM 1061 CB LEU A 146 38.117 -14.736 0.075 1.00 67.85 A C ANISOU 1061 CB LEU A 146 8678 7492 9610 -1749 -678 336 A C ATOM 1062 CG LEU A 146 37.179 -14.443 1.241 1.00 62.82 A C ANISOU 1062 CG LEU A 146 8074 6850 8944 -1977 -500 363 A C ATOM 1063 CD1 LEU A 146 36.383 -15.672 1.500 1.00 55.53 A C ANISOU 1063 CD1 LEU A 146 7171 5776 8151 -2159 -464 322 A C ATOM 1064 CD2 LEU A 146 37.935 -14.078 2.475 1.00 57.40 A C ANISOU 1064 CD2 LEU A 146 7572 6133 8106 -2058 -459 549 A C ATOM 1065 N HIS A 147 41.304 -14.688 -1.083 1.00 72.68 A N ANISOU 1065 N HIS A 147 9390 8145 10081 -1309 -1004 509 A N ATOM 1066 CA HIS A 147 42.226 -15.215 -2.090 1.00 69.52 A C ANISOU 1066 CA HIS A 147 8963 7748 9703 -1101 -1162 488 A C ATOM 1067 C HIS A 147 41.930 -16.665 -2.445 1.00 67.00 A C ANISOU 1067 C HIS A 147 8671 7269 9518 -1114 -1247 407 A C ATOM 1068 O HIS A 147 41.980 -17.049 -3.620 1.00 71.16 A O ANISOU 1068 O HIS A 147 9095 7830 10111 -947 -1346 283 A O ATOM 1069 CB HIS A 147 43.673 -15.074 -1.627 1.00 71.90 A C ANISOU 1069 CB HIS A 147 9377 8049 9891 -1038 -1236 651 A C ATOM 1070 CG HIS A 147 44.674 -15.627 -2.592 1.00 72.47 A C ANISOU 1070 CG HIS A 147 9420 8138 9978 -821 -1392 636 A C ATOM 1071 CD2 HIS A 147 45.454 -15.019 -3.514 1.00 76.11 A C ANISOU 1071 CD2 HIS A 147 9776 8753 10388 -618 -1450 626 A C ATOM 1072 ND1 HIS A 147 44.967 -16.970 -2.674 1.00 73.99 A N ANISOU 1072 ND1 HIS A 147 9697 8175 10241 -793 -1503 629 A N ATOM 1073 CE1 HIS A 147 45.882 -17.166 -3.602 1.00 75.66 A C ANISOU 1073 CE1 HIS A 147 9852 8454 10442 -572 -1627 606 A C ATOM 1074 NE2 HIS A 147 46.197 -15.997 -4.128 1.00 77.63 A N ANISOU 1074 NE2 HIS A 147 9983 8898 10615 -467 -1593 608 A N ATOM 1075 N ARG A 148 41.668 -17.462 -1.413 1.00 61.75 A N ANISOU 1075 N ARG A 148 8154 6424 8884 -1310 -1207 483 A N ATOM 1076 CA ARG A 148 41.179 -18.831 -1.559 1.00 74.47 A C ANISOU 1076 CA ARG A 148 9812 7844 10641 -1383 -1254 411 A C ATOM 1077 C ARG A 148 42.160 -19.790 -2.202 1.00 72.76 A C ANISOU 1077 C ARG A 148 9654 7531 10461 -1206 -1430 408 A C ATOM 1078 O ARG A 148 41.777 -20.893 -2.604 1.00 73.27 A O ANISOU 1078 O ARG A 148 9734 7443 10663 -1223 -1491 309 A O ATOM 1079 CB ARG A 148 39.890 -18.860 -2.377 1.00 75.38 A C ANISOU 1079 CB ARG A 148 9742 8011 10886 -1408 -1211 198 A C ATOM 1080 CG ARG A 148 38.705 -18.213 -1.737 1.00 64.53 A C ANISOU 1080 CG ARG A 148 8304 6700 9515 -1603 -1035 171 A C ATOM 1081 CD ARG A 148 37.679 -17.995 -2.805 1.00 72.37 A C ANISOU 1081 CD ARG A 148 9074 7817 10607 -1540 -1029 -51 A C ATOM 1082 NE ARG A 148 36.587 -18.954 -2.759 1.00 80.28 A N ANISOU 1082 NE ARG A 148 10036 8692 11773 -1720 -992 -174 A N ATOM 1083 CZ ARG A 148 35.645 -19.038 -3.693 1.00 98.51 A C ANISOU 1083 CZ ARG A 148 12148 11085 14196 -1683 -1009 -394 A C ATOM 1084 NH1 ARG A 148 35.685 -18.239 -4.750 1.00102.96 A N1+ ANISOU 1084 NH1 ARG A 148 12553 11857 14710 -1454 -1066 -501 A N1+ ATOM 1085 NH2 ARG A 148 34.666 -19.924 -3.579 1.00105.49 A N ANISOU 1085 NH2 ARG A 148 12992 11848 15240 -1874 -971 -506 A N ATOM 1086 N ASP A 149 43.410 -19.375 -2.324 1.00 70.32 A N ANISOU 1086 N ASP A 149 9371 7313 10036 -1036 -1513 505 A N ATOM 1087 CA ASP A 149 44.414 -20.268 -2.863 1.00 80.65 A C ANISOU 1087 CA ASP A 149 10736 8545 11364 -855 -1679 509 A C ATOM 1088 C ASP A 149 45.785 -20.036 -2.238 1.00 85.19 A C ANISOU 1088 C ASP A 149 11420 9149 11798 -778 -1738 691 A C ATOM 1089 O ASP A 149 46.800 -19.971 -2.935 1.00 82.38 A O ANISOU 1089 O ASP A 149 11012 8891 11397 -563 -1849 689 A O ATOM 1090 CB ASP A 149 44.475 -20.174 -4.385 1.00 83.37 A C ANISOU 1090 CB ASP A 149 10901 9025 11750 -625 -1767 338 A C ATOM 1091 CG ASP A 149 45.073 -21.421 -5.016 1.00 95.12 A C ANISOU 1091 CG ASP A 149 12443 10384 13313 -470 -1929 278 A C ATOM 1092 OD1 ASP A 149 45.318 -22.400 -4.269 1.00 98.53 A O ANISOU 1092 OD1 ASP A 149 13057 10596 13784 -555 -1969 364 A O ATOM 1093 OD2 ASP A 149 45.293 -21.422 -6.250 1.00 97.08 A O1- ANISOU 1093 OD2 ASP A 149 12561 10751 13575 -255 -2016 145 A O1- ATOM 1094 N MET A 150 45.812 -19.926 -0.916 1.00 85.44 A N ANISOU 1094 N MET A 150 11600 9109 11757 -954 -1663 844 A N ATOM 1095 CA MET A 150 47.076 -19.765 -0.222 1.00 87.47 A C ANISOU 1095 CA MET A 150 11964 9393 11878 -894 -1728 1009 A C ATOM 1096 C MET A 150 47.956 -20.978 -0.429 1.00 92.89 A C ANISOU 1096 C MET A 150 12756 9941 12596 -747 -1891 1040 A C ATOM 1097 O MET A 150 47.519 -22.108 -0.237 1.00113.95 A O ANISOU 1097 O MET A 150 15546 12388 15363 -816 -1912 1031 A O ATOM 1098 CB MET A 150 46.837 -19.543 1.265 1.00102.65 A C ANISOU 1098 CB MET A 150 14038 11253 13711 -1110 -1622 1155 A C ATOM 1099 CG MET A 150 46.467 -18.115 1.605 1.00106.39 A C ANISOU 1099 CG MET A 150 14421 11905 14097 -1201 -1490 1157 A C ATOM 1100 SD MET A 150 47.756 -16.971 1.081 1.00 84.91 A S ANISOU 1100 SD MET A 150 11580 9418 11266 -1007 -1562 1181 A S ATOM 1101 CE MET A 150 47.128 -16.430 -0.506 1.00124.90 A C ANISOU 1101 CE MET A 150 16413 14616 16428 -876 -1538 995 A C ATOM 1102 N LYS A 151 49.190 -20.737 -0.850 1.00 87.35 A N ANISOU 1102 N LYS A 151 12004 9368 11816 -542 -2002 1072 A N ATOM 1103 CA LYS A 151 50.208 -21.782 -0.947 1.00 88.96 A C ANISOU 1103 CA LYS A 151 12308 9472 12022 -374 -2164 1116 A C ATOM 1104 C LYS A 151 51.499 -21.151 -1.432 1.00 85.39 A C ANISOU 1104 C LYS A 151 11739 9238 11467 -166 -2250 1141 A C ATOM 1105 O LYS A 151 51.480 -20.234 -2.247 1.00 86.59 A O ANISOU 1105 O LYS A 151 11708 9585 11605 -97 -2209 1064 A O ATOM 1106 CB LYS A 151 49.780 -22.922 -1.881 1.00 85.88 A C ANISOU 1106 CB LYS A 151 11915 8928 11789 -282 -2242 970 A C ATOM 1107 CG LYS A 151 49.587 -22.526 -3.338 1.00 82.17 A C ANISOU 1107 CG LYS A 151 11227 8624 11369 -123 -2261 789 A C ATOM 1108 CD LYS A 151 49.312 -23.746 -4.204 1.00 83.95 A C ANISOU 1108 CD LYS A 151 11465 8693 11737 -14 -2365 636 A C ATOM 1109 CE LYS A 151 49.112 -23.364 -5.663 1.00 90.12 A C ANISOU 1109 CE LYS A 151 12033 9659 12551 160 -2390 449 A C ATOM 1110 NZ LYS A 151 49.078 -24.541 -6.588 1.00 93.47 A N1+ ANISOU 1110 NZ LYS A 151 12463 9959 13093 315 -2520 287 A N1+ ATOM 1111 N ALA A 152 52.624 -21.628 -0.922 1.00 86.40 A N ANISOU 1111 N ALA A 152 11969 9339 11520 -65 -2365 1254 A N ATOM 1112 CA ALA A 152 53.903 -21.019 -1.258 1.00 92.63 A C ANISOU 1112 CA ALA A 152 12638 10349 12209 111 -2440 1286 A C ATOM 1113 C ALA A 152 54.064 -20.815 -2.765 1.00 91.36 A C ANISOU 1113 C ALA A 152 12276 10339 12098 308 -2472 1143 A C ATOM 1114 O ALA A 152 54.665 -19.839 -3.213 1.00 94.16 A O ANISOU 1114 O ALA A 152 12474 10918 12383 384 -2452 1146 A O ATOM 1115 CB ALA A 152 55.046 -21.850 -0.706 1.00 95.23 A C ANISOU 1115 CB ALA A 152 13093 10612 12476 239 -2589 1391 A C ATOM 1116 N ALA A 153 53.518 -21.730 -3.551 1.00 83.98 A N ANISOU 1116 N ALA A 153 11349 9279 11282 388 -2518 1016 A N ATOM 1117 CA ALA A 153 53.720 -21.672 -4.989 1.00 80.90 A C ANISOU 1117 CA ALA A 153 10783 9032 10922 604 -2565 875 A C ATOM 1118 C ALA A 153 53.089 -20.417 -5.619 1.00 80.99 A C ANISOU 1118 C ALA A 153 10618 9235 10918 555 -2436 811 A C ATOM 1119 O ALA A 153 53.399 -20.063 -6.760 1.00 82.29 A O ANISOU 1119 O ALA A 153 10622 9577 11066 736 -2454 728 A O ATOM 1120 CB ALA A 153 53.208 -22.954 -5.638 1.00 81.94 A C ANISOU 1120 CB ALA A 153 10973 8975 11187 690 -2650 734 A C ATOM 1121 N ASN A 154 52.223 -19.746 -4.856 1.00 77.99 A N ANISOU 1121 N ASN A 154 10276 8821 10535 321 -2303 855 A N ATOM 1122 CA ASN A 154 51.479 -18.569 -5.318 1.00 75.29 A C ANISOU 1122 CA ASN A 154 9795 8628 10186 261 -2174 799 A C ATOM 1123 C ASN A 154 52.005 -17.272 -4.698 1.00 84.94 A C ANISOU 1123 C ASN A 154 10983 9997 11293 179 -2091 924 A C ATOM 1124 O ASN A 154 51.392 -16.199 -4.785 1.00 80.41 A O ANISOU 1124 O ASN A 154 10332 9517 10703 94 -1969 908 A O ATOM 1125 CB ASN A 154 49.989 -18.729 -5.009 1.00 71.37 A C ANISOU 1125 CB ASN A 154 9343 7992 9781 66 -2077 726 A C ATOM 1126 CG ASN A 154 49.271 -19.578 -6.031 1.00 85.22 A C ANISOU 1126 CG ASN A 154 11044 9677 11657 157 -2131 546 A C ATOM 1127 ND2 ASN A 154 48.045 -19.965 -5.716 1.00 89.92 A N ANISOU 1127 ND2 ASN A 154 11684 10127 12353 -20 -2067 476 A N ATOM 1128 OD1 ASN A 154 49.807 -19.877 -7.098 1.00 95.98 A O ANISOU 1128 OD1 ASN A 154 12320 11125 13023 382 -2228 462 A O ATOM 1129 N VAL A 155 53.164 -17.389 -4.074 1.00 88.04 A N ANISOU 1129 N VAL A 155 11433 10408 11608 211 -2166 1041 A N ATOM 1130 CA VAL A 155 53.786 -16.280 -3.385 1.00 77.01 A C ANISOU 1130 CA VAL A 155 10015 9136 10107 125 -2111 1154 A C ATOM 1131 C VAL A 155 55.079 -15.967 -4.127 1.00 73.84 A C ANISOU 1131 C VAL A 155 9476 8928 9651 322 -2182 1172 A C ATOM 1132 O VAL A 155 56.080 -16.635 -3.939 1.00 85.36 A O ANISOU 1132 O VAL A 155 10966 10388 11078 431 -2303 1219 A O ATOM 1133 CB VAL A 155 54.069 -16.706 -1.939 1.00 69.30 A C ANISOU 1133 CB VAL A 155 9220 8033 9078 -11 -2144 1274 A C ATOM 1134 CG1 VAL A 155 54.794 -15.650 -1.188 1.00 58.42 A C ANISOU 1134 CG1 VAL A 155 7822 6784 7590 -93 -2112 1373 A C ATOM 1135 CG2 VAL A 155 52.766 -17.049 -1.241 1.00 71.58 A C ANISOU 1135 CG2 VAL A 155 9640 8138 9420 -210 -2056 1261 A C ATOM 1136 N LEU A 156 55.050 -14.976 -5.003 1.00 69.55 A N ANISOU 1136 N LEU A 156 8778 8553 9096 379 -2104 1135 A N ATOM 1137 CA LEU A 156 56.219 -14.683 -5.819 1.00 70.75 A C ANISOU 1137 CA LEU A 156 8784 8899 9200 565 -2152 1151 A C ATOM 1138 C LEU A 156 57.095 -13.680 -5.114 1.00 78.10 A C ANISOU 1138 C LEU A 156 9681 9942 10050 466 -2117 1265 A C ATOM 1139 O LEU A 156 56.607 -12.881 -4.321 1.00 77.15 A O ANISOU 1139 O LEU A 156 9616 9784 9913 271 -2022 1307 A O ATOM 1140 CB LEU A 156 55.807 -14.095 -7.167 1.00 63.25 A C ANISOU 1140 CB LEU A 156 7685 8081 8266 685 -2079 1068 A C ATOM 1141 CG LEU A 156 54.686 -14.841 -7.880 1.00 63.67 A C ANISOU 1141 CG LEU A 156 7753 8038 8401 750 -2092 929 A C ATOM 1142 CD1 LEU A 156 54.503 -14.313 -9.296 1.00 59.74 A C ANISOU 1142 CD1 LEU A 156 7098 7710 7890 921 -2046 851 A C ATOM 1143 CD2 LEU A 156 54.995 -16.318 -7.878 1.00 61.99 A C ANISOU 1143 CD2 LEU A 156 7619 7701 8232 859 -2240 881 A C ATOM 1144 N ILE A 157 58.390 -13.713 -5.409 1.00 84.57 A N ANISOU 1144 N ILE A 157 10403 10909 10823 601 -2194 1305 A N ATOM 1145 CA ILE A 157 59.272 -12.633 -4.987 1.00 80.30 A C ANISOU 1145 CA ILE A 157 9782 10511 10218 517 -2153 1393 A C ATOM 1146 C ILE A 157 60.012 -12.000 -6.148 1.00 82.10 A C ANISOU 1146 C ILE A 157 9813 10952 10428 660 -2115 1392 A C ATOM 1147 O ILE A 157 60.357 -12.672 -7.113 1.00 90.10 A O ANISOU 1147 O ILE A 157 10747 12038 11448 873 -2179 1340 A O ATOM 1148 CB ILE A 157 60.262 -13.081 -3.945 1.00 70.89 A C ANISOU 1148 CB ILE A 157 8649 9316 8971 493 -2270 1465 A C ATOM 1149 CG1 ILE A 157 59.536 -13.923 -2.888 1.00 68.68 A C ANISOU 1149 CG1 ILE A 157 8581 8813 8700 386 -2314 1476 A C ATOM 1150 CG2 ILE A 157 60.914 -11.858 -3.328 1.00 70.14 A C ANISOU 1150 CG2 ILE A 157 8489 9340 8822 345 -2214 1536 A C ATOM 1151 CD1 ILE A 157 60.278 -14.047 -1.569 1.00 60.10 A C ANISOU 1151 CD1 ILE A 157 7588 7715 7534 301 -2397 1565 A C ATOM 1152 N THR A 158 60.230 -10.694 -6.052 1.00 78.86 A N ANISOU 1152 N THR A 158 9330 10638 9995 539 -2005 1448 A N ATOM 1153 CA THR A 158 60.891 -9.947 -7.110 1.00 85.41 A C ANISOU 1153 CA THR A 158 9980 11665 10808 643 -1939 1469 A C ATOM 1154 C THR A 158 62.381 -9.754 -6.829 1.00 99.53 A C ANISOU 1154 C THR A 158 11654 13611 12552 652 -1997 1536 A C ATOM 1155 O THR A 158 62.801 -9.744 -5.674 1.00102.57 A O ANISOU 1155 O THR A 158 12100 13956 12915 520 -2056 1575 A O ATOM 1156 CB THR A 158 60.208 -8.583 -7.355 1.00 78.25 A C ANISOU 1156 CB THR A 158 9055 10763 9913 520 -1769 1491 A C ATOM 1157 CG2 THR A 158 58.726 -8.780 -7.475 1.00 71.04 A C ANISOU 1157 CG2 THR A 158 8249 9704 9041 500 -1722 1417 A C ATOM 1158 OG1 THR A 158 60.485 -7.674 -6.275 1.00 79.40 A O ANISOU 1158 OG1 THR A 158 9239 10883 10046 298 -1724 1556 A O ATOM 1159 N ARG A 159 63.166 -9.613 -7.897 1.00100.44 A N ANISOU 1159 N ARG A 159 11596 13917 12649 813 -1981 1544 A N ATOM 1160 CA ARG A 159 64.606 -9.396 -7.805 1.00100.26 A C ANISOU 1160 CA ARG A 159 11422 14080 12591 835 -2022 1598 A C ATOM 1161 C ARG A 159 64.978 -8.366 -6.723 1.00 94.18 A C ANISOU 1161 C ARG A 159 10660 13306 11818 582 -1979 1663 A C ATOM 1162 O ARG A 159 65.888 -8.600 -5.918 1.00 93.33 A O ANISOU 1162 O ARG A 159 10524 13253 11682 544 -2084 1683 A O ATOM 1163 CB ARG A 159 65.154 -8.970 -9.172 1.00109.55 A C ANISOU 1163 CB ARG A 159 12407 15467 13751 988 -1938 1614 A C ATOM 1164 CG ARG A 159 66.685 -8.931 -9.287 1.00123.14 A C ANISOU 1164 CG ARG A 159 13935 17413 15438 1053 -1983 1655 A C ATOM 1165 CD ARG A 159 67.137 -8.534 -10.699 1.00130.82 A C ANISOU 1165 CD ARG A 159 14724 18597 16386 1209 -1878 1677 A C ATOM 1166 NE ARG A 159 66.621 -7.221 -11.093 1.00144.25 A N ANISOU 1166 NE ARG A 159 16417 20287 18103 1074 -1692 1740 A N ATOM 1167 CZ ARG A 159 65.540 -7.023 -11.849 1.00149.11 A C ANISOU 1167 CZ ARG A 159 17103 20833 18719 1136 -1603 1719 A C ATOM 1168 NH1 ARG A 159 64.849 -8.057 -12.316 1.00152.98 A N1+ ANISOU 1168 NH1 ARG A 159 17665 21262 19200 1319 -1683 1624 A N1+ ATOM 1169 NH2 ARG A 159 65.148 -5.787 -12.145 1.00141.79 A N ANISOU 1169 NH2 ARG A 159 16175 19895 17804 1020 -1437 1788 A N ATOM 1170 N ASP A 160 64.278 -7.233 -6.693 1.00 72.21 A N ANISOU 1170 N ASP A 160 7915 10459 9061 419 -1833 1688 A N ATOM 1171 CA ASP A 160 64.567 -6.206 -5.694 1.00 72.40 A C ANISOU 1171 CA ASP A 160 7956 10464 9089 176 -1788 1732 A C ATOM 1172 C ASP A 160 64.001 -6.564 -4.318 1.00 77.01 A C ANISOU 1172 C ASP A 160 8728 10875 9657 36 -1861 1709 A C ATOM 1173 O ASP A 160 63.945 -5.709 -3.424 1.00 78.92 A O ANISOU 1173 O ASP A 160 9023 11067 9896 -171 -1817 1726 A O ATOM 1174 CB ASP A 160 64.060 -4.828 -6.138 1.00 94.35 A C ANISOU 1174 CB ASP A 160 10720 13225 11905 59 -1604 1766 A C ATOM 1175 CG ASP A 160 64.472 -4.472 -7.568 1.00116.48 A C ANISOU 1175 CG ASP A 160 13359 16188 14710 207 -1511 1804 A C ATOM 1176 OD1 ASP A 160 65.386 -5.125 -8.114 1.00123.44 A O ANISOU 1176 OD1 ASP A 160 14105 17231 15565 370 -1583 1805 A O ATOM 1177 OD2 ASP A 160 63.878 -3.534 -8.150 1.00120.58 A O1- ANISOU 1177 OD2 ASP A 160 13889 16676 15251 172 -1361 1835 A O1- ATOM 1178 N GLY A 161 63.564 -7.816 -4.165 1.00 77.94 A N ANISOU 1178 N GLY A 161 8954 10897 9764 149 -1966 1671 A N ATOM 1179 CA GLY A 161 63.168 -8.365 -2.871 1.00 91.13 A C ANISOU 1179 CA GLY A 161 10803 12417 11404 44 -2047 1667 A C ATOM 1180 C GLY A 161 61.776 -8.076 -2.309 1.00 92.03 A C ANISOU 1180 C GLY A 161 11088 12343 11535 -109 -1957 1646 A C ATOM 1181 O GLY A 161 61.565 -8.160 -1.093 1.00 91.69 A O ANISOU 1181 O GLY A 161 11181 12206 11453 -247 -1991 1658 A O ATOM 1182 N VAL A 162 60.828 -7.747 -3.183 1.00 78.27 A N ANISOU 1182 N VAL A 162 9338 10560 9843 -75 -1842 1611 A N ATOM 1183 CA VAL A 162 59.473 -7.425 -2.759 1.00 71.26 A C ANISOU 1183 CA VAL A 162 8584 9516 8976 -204 -1746 1581 A C ATOM 1184 C VAL A 162 58.567 -8.595 -3.048 1.00 79.66 A C ANISOU 1184 C VAL A 162 9732 10463 10072 -105 -1788 1524 A C ATOM 1185 O VAL A 162 58.620 -9.166 -4.134 1.00 84.45 A O ANISOU 1185 O VAL A 162 10260 11119 10707 80 -1819 1487 A O ATOM 1186 CB VAL A 162 58.892 -6.242 -3.541 1.00 76.89 A C ANISOU 1186 CB VAL A 162 9235 10255 9726 -228 -1589 1571 A C ATOM 1187 CG1 VAL A 162 57.689 -5.679 -2.808 1.00 74.46 A C ANISOU 1187 CG1 VAL A 162 9058 9807 9427 -394 -1491 1543 A C ATOM 1188 CG2 VAL A 162 59.932 -5.161 -3.768 1.00 80.86 A C ANISOU 1188 CG2 VAL A 162 9609 10893 10221 -271 -1540 1628 A C ATOM 1189 N LEU A 163 57.711 -8.927 -2.090 1.00 82.01 A N ANISOU 1189 N LEU A 163 10188 10608 10366 -233 -1780 1513 A N ATOM 1190 CA LEU A 163 56.800 -10.062 -2.219 1.00 78.05 A C ANISOU 1190 CA LEU A 163 9777 9971 9907 -180 -1814 1459 A C ATOM 1191 C LEU A 163 55.455 -9.740 -2.896 1.00 76.17 A C ANISOU 1191 C LEU A 163 9528 9683 9732 -186 -1696 1381 A C ATOM 1192 O LEU A 163 54.841 -8.701 -2.650 1.00 81.45 A O ANISOU 1192 O LEU A 163 10204 10345 10397 -308 -1576 1378 A O ATOM 1193 CB LEU A 163 56.507 -10.622 -0.843 1.00 76.57 A C ANISOU 1193 CB LEU A 163 9766 9644 9682 -322 -1851 1494 A C ATOM 1194 CG LEU A 163 55.445 -11.702 -0.878 1.00 74.27 A C ANISOU 1194 CG LEU A 163 9580 9190 9450 -314 -1858 1444 A C ATOM 1195 CD1 LEU A 163 56.210 -12.963 -1.048 1.00 86.46 A C ANISOU 1195 CD1 LEU A 163 11148 10707 10996 -159 -2012 1460 A C ATOM 1196 CD2 LEU A 163 54.677 -11.724 0.408 1.00 68.83 A C ANISOU 1196 CD2 LEU A 163 9053 8371 8727 -514 -1802 1474 A C ATOM 1197 N LYS A 164 54.985 -10.648 -3.734 1.00 62.26 A N ANISOU 1197 N LYS A 164 7746 7884 8026 -48 -1739 1309 A N ATOM 1198 CA LYS A 164 53.698 -10.459 -4.367 1.00 62.13 A C ANISOU 1198 CA LYS A 164 7709 7831 8068 -43 -1648 1219 A C ATOM 1199 C LYS A 164 52.852 -11.725 -4.217 1.00 69.34 A C ANISOU 1199 C LYS A 164 8714 8588 9044 -51 -1699 1149 A C ATOM 1200 O LYS A 164 53.386 -12.834 -4.273 1.00 79.55 A O ANISOU 1200 O LYS A 164 10043 9832 10350 42 -1821 1149 A O ATOM 1201 CB LYS A 164 53.865 -10.124 -5.853 1.00 51.71 A C ANISOU 1201 CB LYS A 164 6235 6655 6759 154 -1632 1174 A C ATOM 1202 CG LYS A 164 54.917 -9.077 -6.207 1.00 42.18 A C ANISOU 1202 CG LYS A 164 4922 5608 5498 194 -1593 1255 A C ATOM 1203 CD LYS A 164 54.800 -7.779 -5.426 1.00 80.33 A C ANISOU 1203 CD LYS A 164 9788 10430 10304 6 -1480 1315 A C ATOM 1204 CE LYS A 164 55.334 -6.577 -6.226 1.00 64.64 A C ANISOU 1204 CE LYS A 164 7681 8583 8296 63 -1393 1364 A C ATOM 1205 NZ LYS A 164 54.511 -6.370 -7.472 1.00 71.83 A N1+ ANISOU 1205 NZ LYS A 164 8525 9540 9227 212 -1328 1303 A N1+ ATOM 1206 N LEU A 165 51.540 -11.558 -4.027 1.00 60.33 A N ANISOU 1206 N LEU A 165 7609 7366 7947 -164 -1605 1087 A N ATOM 1207 CA LEU A 165 50.614 -12.691 -4.012 1.00 62.91 A C ANISOU 1207 CA LEU A 165 8000 7549 8354 -188 -1635 1004 A C ATOM 1208 C LEU A 165 50.044 -12.884 -5.416 1.00 70.78 A C ANISOU 1208 C LEU A 165 8872 8606 9415 -22 -1645 872 A C ATOM 1209 O LEU A 165 49.896 -11.915 -6.160 1.00 71.15 A O ANISOU 1209 O LEU A 165 8807 8787 9439 53 -1577 848 A O ATOM 1210 CB LEU A 165 49.483 -12.482 -2.998 1.00 60.73 A C ANISOU 1210 CB LEU A 165 7817 7164 8092 -409 -1526 1001 A C ATOM 1211 CG LEU A 165 49.875 -12.117 -1.562 1.00 70.04 A C ANISOU 1211 CG LEU A 165 9123 8302 9188 -583 -1495 1120 A C ATOM 1212 CD1 LEU A 165 48.655 -11.846 -0.719 1.00 69.84 A C ANISOU 1212 CD1 LEU A 165 9168 8198 9171 -779 -1369 1099 A C ATOM 1213 CD2 LEU A 165 50.709 -13.204 -0.930 1.00 84.77 A C ANISOU 1213 CD2 LEU A 165 11107 10075 11027 -573 -1618 1200 A C ATOM 1214 N ALA A 166 49.730 -14.125 -5.787 1.00 65.03 A N ANISOU 1214 N ALA A 166 8167 7777 8763 41 -1732 785 A N ATOM 1215 CA ALA A 166 49.342 -14.393 -7.166 1.00 69.18 A C ANISOU 1215 CA ALA A 166 8570 8377 9338 225 -1769 646 A C ATOM 1216 C ALA A 166 48.226 -15.429 -7.325 1.00 81.25 A C ANISOU 1216 C ALA A 166 10126 9762 10982 181 -1796 507 A C ATOM 1217 O ALA A 166 47.778 -16.041 -6.354 1.00 76.95 A O ANISOU 1217 O ALA A 166 9706 9045 10488 3 -1784 531 A O ATOM 1218 CB ALA A 166 50.567 -14.792 -7.979 1.00 79.70 A C ANISOU 1218 CB ALA A 166 9845 9806 10632 451 -1884 657 A C ATOM 1219 N ASP A 167 47.801 -15.624 -8.572 1.00 93.83 A N ANISOU 1219 N ASP A 167 11601 11436 12615 347 -1834 360 A N ATOM 1220 CA ASP A 167 46.675 -16.492 -8.904 1.00101.79 A C ANISOU 1220 CA ASP A 167 12596 12337 13741 314 -1861 194 A C ATOM 1221 C ASP A 167 45.421 -16.061 -8.161 1.00 96.80 A C ANISOU 1221 C ASP A 167 11978 11646 13154 87 -1733 175 A C ATOM 1222 O ASP A 167 45.068 -16.612 -7.104 1.00 89.06 A O ANISOU 1222 O ASP A 167 11121 10493 12226 -116 -1704 219 A O ATOM 1223 CB ASP A 167 46.972 -17.975 -8.638 1.00110.23 A C ANISOU 1223 CB ASP A 167 13784 13207 14892 304 -1981 170 A C ATOM 1224 CG ASP A 167 46.108 -18.908 -9.492 1.00123.95 A C ANISOU 1224 CG ASP A 167 15466 14878 16752 363 -2050 -41 A C ATOM 1225 OD1 ASP A 167 45.282 -19.663 -8.929 1.00129.67 A O ANISOU 1225 OD1 ASP A 167 16267 15410 17590 182 -2037 -92 A O ATOM 1226 OD2 ASP A 167 46.250 -18.880 -10.734 1.00126.39 A O1- ANISOU 1226 OD2 ASP A 167 15651 15329 17040 587 -2116 -158 A O1- ATOM 1227 N PHE A 168 44.752 -15.059 -8.717 1.00 86.24 A N ANISOU 1227 N PHE A 168 10517 10462 11790 132 -1651 114 A N ATOM 1228 CA PHE A 168 43.443 -14.686 -8.213 1.00 75.77 A C ANISOU 1228 CA PHE A 168 9168 9107 10513 -45 -1536 57 A C ATOM 1229 C PHE A 168 42.380 -15.375 -9.039 1.00 79.92 A C ANISOU 1229 C PHE A 168 9590 9629 11149 -1 -1580 -154 A C ATOM 1230 O PHE A 168 41.251 -14.893 -9.190 1.00 82.12 A O ANISOU 1230 O PHE A 168 9769 9975 11458 -47 -1503 -256 A O ATOM 1231 CB PHE A 168 43.306 -13.175 -8.178 1.00 68.70 A C ANISOU 1231 CB PHE A 168 8215 8361 9525 -33 -1417 118 A C ATOM 1232 CG PHE A 168 44.101 -12.552 -7.076 1.00 77.57 A C ANISOU 1232 CG PHE A 168 9454 9452 10567 -153 -1359 304 A C ATOM 1233 CD1 PHE A 168 43.510 -12.235 -5.870 1.00 68.01 A C ANISOU 1233 CD1 PHE A 168 8323 8161 9356 -376 -1251 353 A C ATOM 1234 CD2 PHE A 168 45.456 -12.351 -7.216 1.00 92.92 A C ANISOU 1234 CD2 PHE A 168 11424 11448 12433 -46 -1417 419 A C ATOM 1235 CE1 PHE A 168 44.241 -11.699 -4.845 1.00 59.23 A C ANISOU 1235 CE1 PHE A 168 7319 7023 8162 -482 -1209 507 A C ATOM 1236 CE2 PHE A 168 46.193 -11.802 -6.182 1.00 85.94 A C ANISOU 1236 CE2 PHE A 168 10637 10539 11476 -163 -1375 573 A C ATOM 1237 CZ PHE A 168 45.576 -11.480 -4.998 1.00 69.04 A C ANISOU 1237 CZ PHE A 168 8582 8318 9332 -379 -1276 612 A C ATOM 1238 N GLY A 169 42.775 -16.535 -9.559 1.00 80.79 A N ANISOU 1238 N GLY A 169 9721 9657 11319 93 -1713 -228 A N ATOM 1239 CA GLY A 169 41.924 -17.343 -10.399 1.00 81.68 A C ANISOU 1239 CA GLY A 169 9740 9751 11544 146 -1786 -446 A C ATOM 1240 C GLY A 169 40.818 -17.931 -9.567 1.00 85.37 A C ANISOU 1240 C GLY A 169 10247 10048 12140 -119 -1723 -504 A C ATOM 1241 O GLY A 169 39.723 -18.183 -10.072 1.00 89.89 A O ANISOU 1241 O GLY A 169 10702 10645 12808 -142 -1725 -692 A O ATOM 1242 N LEU A 170 41.104 -18.141 -8.285 1.00 84.13 A N ANISOU 1242 N LEU A 170 10252 9731 11983 -320 -1665 -342 A N ATOM 1243 CA LEU A 170 40.111 -18.698 -7.378 1.00 90.06 A C ANISOU 1243 CA LEU A 170 11058 10314 12845 -591 -1583 -364 A C ATOM 1244 C LEU A 170 39.536 -17.660 -6.435 1.00 83.37 A C ANISOU 1244 C LEU A 170 10210 9531 11936 -762 -1414 -273 A C ATOM 1245 O LEU A 170 38.543 -17.920 -5.754 1.00 81.91 A O ANISOU 1245 O LEU A 170 10031 9261 11832 -983 -1318 -306 A O ATOM 1246 CB LEU A 170 40.691 -19.853 -6.571 1.00102.20 A C ANISOU 1246 CB LEU A 170 12797 11602 14433 -706 -1634 -257 A C ATOM 1247 CG LEU A 170 40.945 -21.142 -7.338 1.00 98.82 A C ANISOU 1247 CG LEU A 170 12390 11041 14114 -595 -1790 -380 A C ATOM 1248 CD1 LEU A 170 41.248 -22.251 -6.347 1.00 99.88 A C ANISOU 1248 CD1 LEU A 170 12741 10894 14313 -756 -1808 -264 A C ATOM 1249 CD2 LEU A 170 39.722 -21.463 -8.160 1.00 95.27 A C ANISOU 1249 CD2 LEU A 170 11779 10620 13799 -614 -1801 -628 A C ATOM 1250 N ALA A 171 40.165 -16.492 -6.383 1.00 78.66 A N ANISOU 1250 N ALA A 171 9605 9082 11200 -664 -1374 -160 A N ATOM 1251 CA ALA A 171 39.670 -15.409 -5.544 1.00 69.68 A C ANISOU 1251 CA ALA A 171 8467 8012 9995 -800 -1220 -85 A C ATOM 1252 C ALA A 171 38.201 -15.121 -5.833 1.00 65.57 A C ANISOU 1252 C ALA A 171 7791 7574 9550 -859 -1135 -254 A C ATOM 1253 O ALA A 171 37.730 -15.358 -6.927 1.00 67.15 A O ANISOU 1253 O ALA A 171 7851 7851 9813 -727 -1204 -425 A O ATOM 1254 CB ALA A 171 40.495 -14.161 -5.768 1.00 62.70 A C ANISOU 1254 CB ALA A 171 7567 7284 8972 -650 -1205 17 A C ATOM 1255 N ARG A 172 37.492 -14.603 -4.838 1.00 72.80 A N ANISOU 1255 N ARG A 172 8727 8485 10450 -1050 -989 -212 A N ATOM 1256 CA ARG A 172 36.113 -14.151 -4.976 1.00 73.17 A C ANISOU 1256 CA ARG A 172 8617 8636 10548 -1107 -890 -359 A C ATOM 1257 C ARG A 172 35.881 -13.051 -3.930 1.00 78.07 A C ANISOU 1257 C ARG A 172 9283 9308 11070 -1222 -734 -253 A C ATOM 1258 O ARG A 172 36.602 -12.977 -2.915 1.00 67.05 A O ANISOU 1258 O ARG A 172 8055 7823 9596 -1326 -699 -81 A O ATOM 1259 CB ARG A 172 35.141 -15.308 -4.717 1.00 65.74 A C ANISOU 1259 CB ARG A 172 7647 7568 9763 -1306 -871 -473 A C ATOM 1260 CG ARG A 172 34.410 -15.178 -3.396 1.00 72.37 A C ANISOU 1260 CG ARG A 172 8541 8351 10604 -1573 -702 -408 A C ATOM 1261 CD ARG A 172 33.680 -16.436 -2.959 1.00 94.34 A C ANISOU 1261 CD ARG A 172 11344 10965 13538 -1806 -671 -466 A C ATOM 1262 NE ARG A 172 32.441 -16.707 -3.691 1.00113.11 A N ANISOU 1262 NE ARG A 172 13504 13419 16055 -1827 -667 -702 A N ATOM 1263 CZ ARG A 172 31.408 -15.871 -3.781 1.00116.07 A C ANISOU 1263 CZ ARG A 172 13701 13976 16423 -1830 -567 -816 A C ATOM 1264 NH1 ARG A 172 31.465 -14.682 -3.202 1.00122.77 A N1+ ANISOU 1264 NH1 ARG A 172 14575 14937 17135 -1807 -459 -716 A N1+ ATOM 1265 NH2 ARG A 172 30.320 -16.218 -4.466 1.00110.20 A N ANISOU 1265 NH2 ARG A 172 12752 13307 15813 -1846 -581 -1042 A N ATOM 1266 N ALA A 173 34.878 -12.204 -4.153 1.00 70.11 A N ANISOU 1266 N ALA A 173 8130 8448 10060 -1194 -645 -362 A N ATOM 1267 CA ALA A 173 34.558 -11.175 -3.164 1.00 60.94 A C ANISOU 1267 CA ALA A 173 7009 7333 8812 -1297 -493 -286 A C ATOM 1268 C ALA A 173 33.708 -11.737 -2.026 1.00 68.88 A C ANISOU 1268 C ALA A 173 8050 8248 9873 -1573 -371 -288 A C ATOM 1269 O ALA A 173 33.073 -12.773 -2.182 1.00 76.58 A O ANISOU 1269 O ALA A 173 8966 9154 10975 -1677 -388 -388 A O ATOM 1270 CB ALA A 173 33.868 -10.014 -3.814 1.00 55.77 A C ANISOU 1270 CB ALA A 173 6200 6865 8125 -1140 -445 -391 A C ATOM 1271 N PHE A 174 33.711 -11.069 -0.876 1.00 69.63 A N ANISOU 1271 N PHE A 174 8245 8340 9870 -1696 -245 -178 A N ATOM 1272 CA PHE A 174 32.895 -11.515 0.251 1.00 75.23 A C ANISOU 1272 CA PHE A 174 8990 8986 10609 -1955 -108 -167 A C ATOM 1273 C PHE A 174 32.206 -10.351 0.957 1.00 96.39 A C ANISOU 1273 C PHE A 174 11634 11789 13203 -2000 53 -180 A C ATOM 1274 O PHE A 174 32.603 -9.192 0.801 1.00 91.76 A O ANISOU 1274 O PHE A 174 11054 11292 12517 -1852 55 -152 A O ATOM 1275 CB PHE A 174 33.710 -12.347 1.240 1.00 70.06 A C ANISOU 1275 CB PHE A 174 8557 8147 9916 -2111 -121 12 A C ATOM 1276 CG PHE A 174 34.601 -11.536 2.138 1.00 84.58 A C ANISOU 1276 CG PHE A 174 10559 9989 11588 -2111 -89 179 A C ATOM 1277 CD1 PHE A 174 35.880 -11.186 1.740 1.00 90.08 A C ANISOU 1277 CD1 PHE A 174 11327 10686 12213 -1945 -212 267 A C ATOM 1278 CD2 PHE A 174 34.167 -11.140 3.397 1.00 85.55 A C ANISOU 1278 CD2 PHE A 174 10759 10123 11625 -2283 65 241 A C ATOM 1279 CE1 PHE A 174 36.706 -10.440 2.580 1.00 89.42 A C ANISOU 1279 CE1 PHE A 174 11382 10609 11984 -1958 -189 405 A C ATOM 1280 CE2 PHE A 174 34.994 -10.399 4.244 1.00 79.39 A C ANISOU 1280 CE2 PHE A 174 10129 9349 10687 -2284 84 378 A C ATOM 1281 CZ PHE A 174 36.260 -10.053 3.834 1.00 79.31 A C ANISOU 1281 CZ PHE A 174 10183 9335 10618 -2127 -47 455 A C ATOM 1282 N SER A 175 31.160 -10.669 1.720 1.00116.58 A N ANISOU 1282 N SER A 175 14149 14345 15800 -2206 194 -225 A N ATOM 1283 CA SER A 175 30.341 -9.655 2.387 1.00122.05 A C ANISOU 1283 CA SER A 175 14785 15167 16422 -2251 357 -266 A C ATOM 1284 C SER A 175 29.808 -10.148 3.727 1.00128.05 A C ANISOU 1284 C SER A 175 15625 15867 17161 -2524 515 -200 A C ATOM 1285 O SER A 175 30.221 -11.195 4.225 1.00125.42 A O ANISOU 1285 O SER A 175 15430 15375 16850 -2674 495 -88 A O ATOM 1286 CB SER A 175 29.181 -9.222 1.486 1.00119.31 A C ANISOU 1286 CB SER A 175 14183 14991 16160 -2137 379 -479 A C ATOM 1287 OG SER A 175 28.490 -10.346 0.967 1.00121.16 A O ANISOU 1287 OG SER A 175 14284 15197 16555 -2224 345 -603 A O ATOM 1288 N LEU A 176 28.883 -9.390 4.304 1.00142.36 A N ANISOU 1288 N LEU A 176 17355 17809 18926 -2579 675 -266 A N ATOM 1289 CA LEU A 176 28.343 -9.714 5.621 1.00153.14 A C ANISOU 1289 CA LEU A 176 18792 19149 20245 -2827 848 -201 A C ATOM 1290 C LEU A 176 26.864 -10.104 5.552 1.00159.29 A C ANISOU 1290 C LEU A 176 19352 20021 21150 -2959 974 -364 A C ATOM 1291 O LEU A 176 26.171 -10.143 6.570 1.00161.52 A O ANISOU 1291 O LEU A 176 19638 20340 21390 -3148 1152 -344 A O ATOM 1292 CB LEU A 176 28.557 -8.530 6.565 1.00156.56 A C ANISOU 1292 CB LEU A 176 19333 19658 20496 -2805 948 -132 A C ATOM 1293 CG LEU A 176 29.992 -7.990 6.464 1.00162.20 A C ANISOU 1293 CG LEU A 176 20220 20305 21103 -2655 812 -5 A C ATOM 1294 CD1 LEU A 176 30.140 -6.616 7.115 1.00162.49 A C ANISOU 1294 CD1 LEU A 176 20323 20431 20985 -2588 889 10 A C ATOM 1295 CD2 LEU A 176 30.993 -8.993 7.041 1.00160.60 A C ANISOU 1295 CD2 LEU A 176 20230 19927 20864 -2772 742 177 A C ATOM 1296 N ALA A 177 26.395 -10.404 4.342 1.00158.21 A N ANISOU 1296 N ALA A 177 19016 19933 21162 -2859 879 -529 A N ATOM 1297 CA ALA A 177 25.013 -10.817 4.124 1.00159.93 A C ANISOU 1297 CA ALA A 177 18994 20252 21522 -2974 972 -711 A C ATOM 1298 C ALA A 177 24.620 -11.974 5.039 1.00161.16 A C ANISOU 1298 C ALA A 177 19213 20280 21742 -3294 1094 -636 A C ATOM 1299 O ALA A 177 24.057 -12.974 4.587 1.00160.15 A O ANISOU 1299 O ALA A 177 18965 20098 21788 -3414 1075 -734 A O ATOM 1300 CB ALA A 177 24.795 -11.193 2.662 1.00155.04 A C ANISOU 1300 CB ALA A 177 18187 19668 21053 -2824 811 -885 A C ATOM 1301 N PRO A 182 22.544 -15.794 5.922 1.00146.88 A N ANISOU 1301 N PRO A 182 17271 18126 20409 -4162 1359 -686 A N ATOM 1302 CA PRO A 182 23.967 -16.154 5.921 1.00154.85 A C ANISOU 1302 CA PRO A 182 18566 18925 21346 -4067 1202 -496 A C ATOM 1303 C PRO A 182 24.452 -16.511 4.520 1.00165.56 A C ANISOU 1303 C PRO A 182 19857 20224 22823 -3868 963 -616 A C ATOM 1304 O PRO A 182 23.643 -16.865 3.659 1.00172.51 A O ANISOU 1304 O PRO A 182 20503 21165 23878 -3879 924 -831 A O ATOM 1305 CB PRO A 182 24.005 -17.392 6.814 1.00149.44 A C ANISOU 1305 CB PRO A 182 18066 18004 20712 -4362 1300 -328 A C ATOM 1306 CG PRO A 182 22.685 -18.025 6.581 1.00150.35 A C ANISOU 1306 CG PRO A 182 17938 18154 21034 -4577 1408 -505 A C ATOM 1307 CD PRO A 182 21.711 -16.876 6.470 1.00146.71 A C ANISOU 1307 CD PRO A 182 17208 18006 20531 -4496 1512 -684 A C ATOM 1308 N ASN A 183 25.763 -16.427 4.307 1.00161.64 A N ANISOU 1308 N ASN A 183 19561 19623 22231 -3689 805 -484 A N ATOM 1309 CA ASN A 183 26.358 -16.645 2.992 1.00151.69 A C ANISOU 1309 CA ASN A 183 18255 18331 21049 -3464 579 -583 A C ATOM 1310 C ASN A 183 26.283 -18.097 2.535 1.00145.56 A C ANISOU 1310 C ASN A 183 17489 17345 20472 -3591 494 -637 A C ATOM 1311 O ASN A 183 26.017 -18.999 3.332 1.00144.73 A O ANISOU 1311 O ASN A 183 17490 17068 20434 -3856 600 -544 A O ATOM 1312 CB ASN A 183 27.821 -16.192 2.989 1.00147.48 A C ANISOU 1312 CB ASN A 183 17936 17744 20355 -3258 450 -413 A C ATOM 1313 CG ASN A 183 28.011 -14.814 3.596 1.00148.53 A C ANISOU 1313 CG ASN A 183 18105 18039 20292 -3164 538 -336 A C ATOM 1314 ND2 ASN A 183 29.118 -14.630 4.320 1.00144.99 A N ANISOU 1314 ND2 ASN A 183 17897 17502 19690 -3142 515 -128 A N ATOM 1315 OD1 ASN A 183 27.180 -13.923 3.414 1.00149.30 A O ANISOU 1315 OD1 ASN A 183 18015 18337 20375 -3106 618 -470 A O ATOM 1316 N ARG A 184 26.526 -18.312 1.245 1.00134.20 A N ANISOU 1316 N ARG A 184 15948 15917 19124 -3396 303 -788 A N ATOM 1317 CA ARG A 184 26.575 -19.654 0.690 1.00127.44 A C ANISOU 1317 CA ARG A 184 15112 14855 18456 -3475 191 -860 A C ATOM 1318 C ARG A 184 27.721 -19.772 -0.319 1.00118.30 A C ANISOU 1318 C ARG A 184 14030 13648 17272 -3194 -42 -866 A C ATOM 1319 O ARG A 184 27.493 -20.037 -1.498 1.00121.61 A O ANISOU 1319 O ARG A 184 14286 14116 17802 -3064 -179 -1072 A O ATOM 1320 CB ARG A 184 25.229 -20.007 0.044 1.00133.28 A C ANISOU 1320 CB ARG A 184 15559 15688 19394 -3582 217 -1133 A C ATOM 1321 CG ARG A 184 25.031 -21.500 -0.253 1.00143.12 A C ANISOU 1321 CG ARG A 184 16826 16689 20865 -3763 153 -1213 A C ATOM 1322 CD ARG A 184 23.620 -21.813 -0.774 1.00147.81 A C ANISOU 1322 CD ARG A 184 17111 17390 21661 -3907 198 -1493 A C ATOM 1323 NE ARG A 184 22.630 -21.941 0.297 1.00150.10 A N ANISOU 1323 NE ARG A 184 17347 17682 22001 -4234 441 -1451 A N ATOM 1324 CZ ARG A 184 21.963 -20.924 0.843 1.00146.87 A C ANISOU 1324 CZ ARG A 184 16806 17514 21483 -4254 607 -1453 A C ATOM 1325 NH1 ARG A 184 22.174 -19.679 0.429 1.00145.59 A N1+ ANISOU 1325 NH1 ARG A 184 16564 17592 21161 -3965 553 -1490 A N1+ ATOM 1326 NH2 ARG A 184 21.084 -21.151 1.814 1.00138.24 A N ANISOU 1326 NH2 ARG A 184 15667 16417 20440 -4560 833 -1414 A N ATOM 1327 N TYR A 185 28.953 -19.569 0.144 1.00114.32 A N ANISOU 1327 N TYR A 185 13762 13060 16614 -3096 -88 -645 A N ATOM 1328 CA TYR A 185 30.126 -19.626 -0.738 1.00109.40 A C ANISOU 1328 CA TYR A 185 13213 12407 15949 -2827 -295 -631 A C ATOM 1329 C TYR A 185 30.528 -21.073 -0.977 1.00112.11 A C ANISOU 1329 C TYR A 185 13682 12483 16434 -2888 -411 -629 A C ATOM 1330 O TYR A 185 30.263 -21.941 -0.149 1.00115.32 A O ANISOU 1330 O TYR A 185 14214 12686 16918 -3139 -322 -540 A O ATOM 1331 CB TYR A 185 31.333 -18.839 -0.179 1.00103.27 A C ANISOU 1331 CB TYR A 185 12623 11656 14959 -2694 -308 -408 A C ATOM 1332 CG TYR A 185 31.069 -17.381 0.164 1.00 96.95 A C ANISOU 1332 CG TYR A 185 11743 11084 14011 -2634 -194 -389 A C ATOM 1333 CD1 TYR A 185 30.388 -16.552 -0.713 1.00 98.68 A C ANISOU 1333 CD1 TYR A 185 11726 11525 14243 -2486 -200 -575 A C ATOM 1334 CD2 TYR A 185 31.514 -16.838 1.362 1.00100.39 A C ANISOU 1334 CD2 TYR A 185 12347 11509 14287 -2714 -89 -189 A C ATOM 1335 CE1 TYR A 185 30.136 -15.226 -0.401 1.00107.23 A C ANISOU 1335 CE1 TYR A 185 12750 12794 15197 -2422 -97 -559 A C ATOM 1336 CE2 TYR A 185 31.270 -15.510 1.688 1.00107.62 A C ANISOU 1336 CE2 TYR A 185 13199 12615 15074 -2659 13 -184 A C ATOM 1337 CZ TYR A 185 30.582 -14.705 0.799 1.00114.94 A C ANISOU 1337 CZ TYR A 185 13900 13744 16030 -2512 10 -367 A C ATOM 1338 OH TYR A 185 30.333 -13.378 1.101 1.00116.55 A O ANISOU 1338 OH TYR A 185 14052 14121 16112 -2443 108 -366 A O HETATM 1339 N TPO A 186 31.160 -21.304 -2.118 1.00110.66 A N ANISOU 1339 N TPO A 186 13471 12300 16276 -2651 -605 -724 A N HETATM 1340 CA TPO A 186 31.701 -22.616 -2.561 1.00101.07 A C ANISOU 1340 CA TPO A 186 12356 10838 15206 -2659 -745 -767 A C HETATM 1341 C TPO A 186 32.587 -23.278 -1.567 1.00108.94 A C ANISOU 1341 C TPO A 186 13653 11598 16139 -2698 -770 -519 A C HETATM 1342 O TPO A 186 33.366 -22.582 -0.953 1.00111.24 A O ANISOU 1342 O TPO A 186 14060 11954 16253 -2562 -788 -348 A O HETATM 1343 CB TPO A 186 32.629 -22.192 -3.670 1.00 89.83 A C ANISOU 1343 CB TPO A 186 10799 9550 13781 -2349 -934 -940 A C HETATM 1344 CG2 TPO A 186 32.546 -23.056 -4.898 1.00 77.36 A C ANISOU 1344 CG2 TPO A 186 9400 7800 12193 -2186 -1108 -869 A C HETATM 1345 OG1 TPO A 186 32.374 -20.839 -4.008 1.00 98.93 A O ANISOU 1345 OG1 TPO A 186 11858 10970 14760 -2168 -902 -909 A O HETATM 1346 P TPO A 186 32.104 -20.367 -5.488 1.00111.92 A P ANISOU 1346 P TPO A 186 13300 12863 16363 -1854 -1029 -1093 A P HETATM 1347 O1P TPO A 186 33.449 -20.262 -6.094 1.00100.27 A O ANISOU 1347 O1P TPO A 186 11962 11350 14787 -1617 -1176 -984 A O HETATM 1348 O2P TPO A 186 31.305 -21.483 -6.024 1.00121.69 A O1- ANISOU 1348 O2P TPO A 186 14368 14076 17795 -1901 -1100 -1361 A O1- HETATM 1349 O3P TPO A 186 31.364 -19.088 -5.355 1.00 84.74 A O ANISOU 1349 O3P TPO A 186 9742 9652 12801 -1832 -896 -1071 A O ATOM 1350 N ASN A 187 32.519 -24.597 -1.400 1.00126.05 A N ANISOU 1350 N ASN A 187 15952 13486 18456 -2881 -773 -498 A N ATOM 1351 CA ASN A 187 33.423 -25.264 -0.459 1.00130.32 A C ANISOU 1351 CA ASN A 187 16795 13783 18939 -2943 -777 -246 A C ATOM 1352 C ASN A 187 34.688 -25.879 -1.069 1.00128.67 A C ANISOU 1352 C ASN A 187 16725 13446 18717 -2702 -989 -216 A C ATOM 1353 O ASN A 187 35.697 -26.040 -0.388 1.00119.41 A O ANISOU 1353 O ASN A 187 15777 12166 17428 -2653 -1020 2 A O ATOM 1354 CB ASN A 187 32.662 -26.328 0.332 1.00135.45 A C ANISOU 1354 CB ASN A 187 17553 14171 19741 -3271 -653 -198 A C ATOM 1355 CG ASN A 187 33.486 -26.916 1.459 1.00139.45 A C ANISOU 1355 CG ASN A 187 18383 14442 20160 -3346 -628 90 A C ATOM 1356 ND2 ASN A 187 33.141 -26.567 2.689 1.00142.97 A N ANISOU 1356 ND2 ASN A 187 18915 14906 20503 -3547 -437 266 A N ATOM 1357 OD1 ASN A 187 34.423 -27.674 1.225 1.00141.04 A O ANISOU 1357 OD1 ASN A 187 18756 14455 20378 -3213 -781 150 A O ATOM 1358 N ARG A 188 34.627 -26.214 -2.353 1.00139.97 A N ANISOU 1358 N ARG A 188 18015 14905 20263 -2541 -1138 -444 A N ATOM 1359 CA ARG A 188 35.714 -26.916 -3.036 1.00142.17 A C ANISOU 1359 CA ARG A 188 18405 15060 20554 -2310 -1341 -455 A C ATOM 1360 C ARG A 188 36.954 -26.049 -3.302 1.00130.91 A C ANISOU 1360 C ARG A 188 16996 13826 18919 -2017 -1432 -351 A C ATOM 1361 O ARG A 188 37.560 -26.143 -4.372 1.00127.80 A O ANISOU 1361 O ARG A 188 16538 13498 18521 -1760 -1593 -465 A O ATOM 1362 CB ARG A 188 35.192 -27.494 -4.360 1.00152.58 A C ANISOU 1362 CB ARG A 188 19550 16376 22050 -2225 -1468 -755 A C ATOM 1363 CG ARG A 188 33.860 -28.239 -4.226 1.00163.64 A C ANISOU 1363 CG ARG A 188 20877 17625 23674 -2525 -1377 -903 A C ATOM 1364 CD ARG A 188 33.333 -28.769 -5.564 1.00165.27 A C ANISOU 1364 CD ARG A 188 20894 17850 24053 -2435 -1517 -1228 A C ATOM 1365 NE ARG A 188 32.488 -29.954 -5.390 1.00162.10 A N ANISOU 1365 NE ARG A 188 20522 17170 23899 -2713 -1484 -1336 A N ATOM 1366 CZ ARG A 188 31.838 -30.570 -6.375 1.00156.34 A C ANISOU 1366 CZ ARG A 188 19635 16410 23358 -2716 -1586 -1633 A C ATOM 1367 NH1 ARG A 188 31.922 -30.114 -7.617 1.00151.07 A N1+ ANISOU 1367 NH1 ARG A 188 18769 15986 22644 -2439 -1730 -1850 A N1+ ATOM 1368 NH2 ARG A 188 31.099 -31.642 -6.118 1.00157.15 A N ANISOU 1368 NH2 ARG A 188 19778 16238 23695 -3000 -1543 -1716 A N ATOM 1369 N VAL A 189 37.345 -25.216 -2.339 1.00121.56 A N ANISOU 1369 N VAL A 189 15893 12733 17560 -2056 -1330 -140 A N ATOM 1370 CA VAL A 189 38.470 -24.304 -2.564 1.00126.29 A C ANISOU 1370 CA VAL A 189 16487 13526 17971 -1806 -1402 -48 A C ATOM 1371 C VAL A 189 39.719 -24.597 -1.733 1.00128.56 A C ANISOU 1371 C VAL A 189 17018 13689 18139 -1758 -1453 192 A C ATOM 1372 O VAL A 189 39.652 -25.242 -0.684 1.00131.19 A O ANISOU 1372 O VAL A 189 17545 13815 18486 -1944 -1388 340 A O ATOM 1373 CB VAL A 189 38.078 -22.813 -2.373 1.00102.40 A C ANISOU 1373 CB VAL A 189 13315 10775 14816 -1814 -1274 -35 A C ATOM 1374 CG1 VAL A 189 37.431 -22.256 -3.639 1.00104.78 A C ANISOU 1374 CG1 VAL A 189 13357 11288 15168 -1677 -1306 -271 A C ATOM 1375 CG2 VAL A 189 37.185 -22.631 -1.150 1.00 92.20 A C ANISOU 1375 CG2 VAL A 189 12071 9439 13521 -2107 -1078 56 A C ATOM 1376 N VAL A 190 40.853 -24.098 -2.223 1.00119.03 A N ANISOU 1376 N VAL A 190 15792 12623 16809 -1501 -1566 229 A N ATOM 1377 CA VAL A 190 42.152 -24.248 -1.567 1.00109.20 A C ANISOU 1377 CA VAL A 190 14737 11317 15436 -1410 -1637 436 A C ATOM 1378 C VAL A 190 42.770 -25.639 -1.732 1.00108.49 A C ANISOU 1378 C VAL A 190 14812 10975 15435 -1326 -1783 449 A C ATOM 1379 O VAL A 190 42.168 -26.647 -1.344 1.00 93.85 A O ANISOU 1379 O VAL A 190 13078 8869 13713 -1499 -1754 447 A O ATOM 1380 CB VAL A 190 42.095 -23.926 -0.057 1.00 97.67 A C ANISOU 1380 CB VAL A 190 13432 9812 13864 -1618 -1501 650 A C ATOM 1381 CG1 VAL A 190 43.504 -23.695 0.477 1.00 94.98 A C ANISOU 1381 CG1 VAL A 190 13224 9510 13353 -1477 -1584 836 A C ATOM 1382 CG2 VAL A 190 41.212 -22.725 0.205 1.00 89.02 A C ANISOU 1382 CG2 VAL A 190 12192 8916 12716 -1746 -1335 615 A C ATOM 1383 N THR A 191 43.975 -25.671 -2.306 1.00111.17 A N ANISOU 1383 N THR A 191 15154 11383 15702 -1059 -1935 462 A N ATOM 1384 CA THR A 191 44.834 -26.850 -2.306 1.00103.50 A C ANISOU 1384 CA THR A 191 14360 10196 14767 -935 -2083 513 A C ATOM 1385 C THR A 191 44.667 -27.600 -0.992 1.00103.62 A C ANISOU 1385 C THR A 191 14629 9945 14798 -1148 -2018 696 A C ATOM 1386 O THR A 191 44.632 -26.994 0.080 1.00103.50 A O ANISOU 1386 O THR A 191 14682 9984 14661 -1290 -1903 863 A O ATOM 1387 CB THR A 191 46.311 -26.433 -2.413 1.00111.87 A C ANISOU 1387 CB THR A 191 15428 11412 15665 -680 -2197 616 A C ATOM 1388 CG2 THR A 191 47.224 -27.646 -2.541 1.00115.71 A C ANISOU 1388 CG2 THR A 191 16076 11699 16189 -508 -2364 645 A C ATOM 1389 OG1 THR A 191 46.487 -25.570 -3.540 1.00116.60 A O ANISOU 1389 OG1 THR A 191 15795 12284 16223 -498 -2227 481 A O ATOM 1390 N LEU A 192 44.575 -28.920 -1.063 1.00105.95 A N ANISOU 1390 N LEU A 192 15073 9947 15237 -1166 -2090 668 A N ATOM 1391 CA LEU A 192 44.370 -29.713 0.143 1.00108.60 A C ANISOU 1391 CA LEU A 192 15667 10003 15596 -1371 -2021 852 A C ATOM 1392 C LEU A 192 45.347 -29.368 1.291 1.00109.73 A C ANISOU 1392 C LEU A 192 15977 10188 15526 -1333 -2019 1115 A C ATOM 1393 O LEU A 192 44.913 -29.011 2.388 1.00107.79 A O ANISOU 1393 O LEU A 192 15815 9940 15200 -1545 -1872 1263 A O ATOM 1394 CB LEU A 192 44.399 -31.208 -0.189 1.00105.89 A C ANISOU 1394 CB LEU A 192 15482 9321 15430 -1338 -2132 793 A C ATOM 1395 CG LEU A 192 44.081 -32.199 0.933 1.00102.32 A C ANISOU 1395 CG LEU A 192 15314 8525 15037 -1557 -2058 973 A C ATOM 1396 CD1 LEU A 192 42.765 -31.838 1.617 1.00 98.52 A C ANISOU 1396 CD1 LEU A 192 14790 8044 14598 -1903 -1834 998 A C ATOM 1397 CD2 LEU A 192 44.051 -33.622 0.391 1.00 96.29 A C ANISOU 1397 CD2 LEU A 192 14682 7423 14479 -1511 -2176 872 A C ATOM 1398 N TRP A 193 46.654 -29.453 1.047 1.00109.10 A N ANISOU 1398 N TRP A 193 15937 10167 15350 -1062 -2182 1164 A N ATOM 1399 CA TRP A 193 47.627 -29.276 2.134 1.00111.49 A C ANISOU 1399 CA TRP A 193 16406 10495 15460 -1013 -2207 1402 A C ATOM 1400 C TRP A 193 47.525 -27.940 2.872 1.00101.13 A C ANISOU 1400 C TRP A 193 15010 9436 13977 -1131 -2076 1495 A C ATOM 1401 O TRP A 193 48.100 -27.781 3.948 1.00 86.80 A O ANISOU 1401 O TRP A 193 13344 7633 12003 -1151 -2068 1690 A O ATOM 1402 CB TRP A 193 49.063 -29.465 1.646 1.00111.81 A C ANISOU 1402 CB TRP A 193 16448 10611 15424 -687 -2407 1411 A C ATOM 1403 CG TRP A 193 49.329 -30.779 1.014 1.00116.80 A C ANISOU 1403 CG TRP A 193 17187 10993 16200 -534 -2551 1332 A C ATOM 1404 CD1 TRP A 193 48.599 -31.922 1.147 1.00119.93 A C ANISOU 1404 CD1 TRP A 193 17752 11051 16765 -672 -2530 1317 A C ATOM 1405 CD2 TRP A 193 50.420 -31.097 0.147 1.00124.80 A C ANISOU 1405 CD2 TRP A 193 18148 12070 17202 -211 -2739 1252 A C ATOM 1406 CE2 TRP A 193 50.286 -32.447 -0.216 1.00117.99 A C ANISOU 1406 CE2 TRP A 193 17436 10892 16505 -155 -2832 1181 A C ATOM 1407 CE3 TRP A 193 51.499 -30.365 -0.363 1.00132.06 A C ANISOU 1407 CE3 TRP A 193 18904 13284 17990 33 -2832 1231 A C ATOM 1408 NE1 TRP A 193 49.165 -32.931 0.406 1.00120.30 A N ANISOU 1408 NE1 TRP A 193 17864 10932 16911 -448 -2701 1224 A N ATOM 1409 CZ2 TRP A 193 51.184 -33.080 -1.064 1.00116.15 A C ANISOU 1409 CZ2 TRP A 193 17195 10636 16300 151 -3018 1082 A C ATOM 1410 CZ3 TRP A 193 52.391 -30.999 -1.208 1.00125.68 A C ANISOU 1410 CZ3 TRP A 193 18077 12466 17209 330 -3008 1140 A C ATOM 1411 CH2 TRP A 193 52.226 -32.340 -1.551 1.00116.97 A C ANISOU 1411 CH2 TRP A 193 17127 11053 16263 395 -3102 1063 A C ATOM 1412 N TYR A 194 46.810 -26.984 2.287 1.00 99.09 A N ANISOU 1412 N TYR A 194 14521 9382 13748 -1195 -1981 1349 A N ATOM 1413 CA TYR A 194 46.665 -25.672 2.896 1.00 97.16 A C ANISOU 1413 CA TYR A 194 14190 9371 13356 -1297 -1857 1412 A C ATOM 1414 C TYR A 194 45.221 -25.346 3.242 1.00105.88 A C ANISOU 1414 C TYR A 194 15241 10462 14526 -1572 -1661 1364 A C ATOM 1415 O TYR A 194 44.931 -24.249 3.726 1.00107.28 A O ANISOU 1415 O TYR A 194 15342 10824 14595 -1667 -1542 1393 A O ATOM 1416 CB TYR A 194 47.183 -24.596 1.964 1.00 89.86 A C ANISOU 1416 CB TYR A 194 13031 8735 12376 -1113 -1908 1301 A C ATOM 1417 CG TYR A 194 48.642 -24.705 1.621 1.00 93.14 A C ANISOU 1417 CG TYR A 194 13455 9227 12709 -845 -2083 1345 A C ATOM 1418 CD1 TYR A 194 49.602 -24.051 2.381 1.00 94.06 A C ANISOU 1418 CD1 TYR A 194 13612 9482 12645 -800 -2107 1492 A C ATOM 1419 CD2 TYR A 194 49.060 -25.431 0.512 1.00 95.55 A C ANISOU 1419 CD2 TYR A 194 13709 9483 13114 -634 -2226 1223 A C ATOM 1420 CE1 TYR A 194 50.941 -24.128 2.054 1.00103.49 A C ANISOU 1420 CE1 TYR A 194 14786 10769 13767 -558 -2265 1522 A C ATOM 1421 CE2 TYR A 194 50.392 -25.520 0.179 1.00 98.18 A C ANISOU 1421 CE2 TYR A 194 14031 9907 13368 -381 -2379 1255 A C ATOM 1422 CZ TYR A 194 51.331 -24.867 0.950 1.00108.75 A C ANISOU 1422 CZ TYR A 194 15398 11389 14534 -347 -2396 1407 A C ATOM 1423 OH TYR A 194 52.666 -24.954 0.615 1.00115.88 A O ANISOU 1423 OH TYR A 194 16266 12399 15362 -98 -2548 1431 A O ATOM 1424 N ARG A 195 44.311 -26.279 2.977 1.00107.91 A N ANISOU 1424 N ARG A 195 15529 10507 14965 -1697 -1625 1278 A N ATOM 1425 CA ARG A 195 42.909 -26.047 3.296 1.00102.06 A C ANISOU 1425 CA ARG A 195 14719 9758 14299 -1965 -1435 1222 A C ATOM 1426 C ARG A 195 42.757 -26.058 4.795 1.00101.36 A C ANISOU 1426 C ARG A 195 14830 9592 14091 -2166 -1304 1441 A C ATOM 1427 O ARG A 195 43.395 -26.857 5.475 1.00108.59 A O ANISOU 1427 O ARG A 195 15981 10320 14956 -2147 -1362 1611 A O ATOM 1428 CB ARG A 195 41.992 -27.101 2.676 1.00 98.88 A C ANISOU 1428 CB ARG A 195 14298 9140 14134 -2068 -1432 1072 A C ATOM 1429 CG ARG A 195 40.630 -26.543 2.276 1.00103.78 A C ANISOU 1429 CG ARG A 195 14692 9884 14855 -2233 -1292 893 A C ATOM 1430 CD ARG A 195 39.561 -27.613 2.129 1.00113.80 A C ANISOU 1430 CD ARG A 195 15978 10915 16348 -2437 -1236 791 A C ATOM 1431 NE ARG A 195 40.033 -28.799 1.421 1.00123.47 A N ANISOU 1431 NE ARG A 195 17291 11911 17711 -2309 -1406 719 A N ATOM 1432 CZ ARG A 195 40.150 -28.886 0.102 1.00123.89 A C ANISOU 1432 CZ ARG A 195 17181 12033 17857 -2115 -1545 501 A C ATOM 1433 NH1 ARG A 195 39.838 -27.850 -0.657 1.00117.56 A N1+ ANISOU 1433 NH1 ARG A 195 16124 11522 17019 -2024 -1533 347 A N1+ ATOM 1434 NH2 ARG A 195 40.588 -30.007 -0.454 1.00129.36 A N ANISOU 1434 NH2 ARG A 195 17977 12504 18670 -2000 -1697 438 A N ATOM 1435 N PRO A 196 41.928 -25.150 5.317 1.00 98.38 A N ANISOU 1435 N PRO A 196 14360 9366 13653 -2341 -1127 1436 A N ATOM 1436 CA PRO A 196 41.644 -25.047 6.750 1.00105.73 A C ANISOU 1436 CA PRO A 196 15459 10260 14455 -2543 -976 1627 A C ATOM 1437 C PRO A 196 40.717 -26.168 7.188 1.00118.48 A C ANISOU 1437 C PRO A 196 17204 11606 16209 -2781 -865 1670 A C ATOM 1438 O PRO A 196 40.123 -26.828 6.328 1.00114.24 A O ANISOU 1438 O PRO A 196 16577 10946 15882 -2814 -889 1512 A O ATOM 1439 CB PRO A 196 40.903 -23.709 6.870 1.00 98.22 A C ANISOU 1439 CB PRO A 196 14315 9569 13436 -2635 -826 1544 A C ATOM 1440 CG PRO A 196 41.096 -23.018 5.576 1.00 92.50 A C ANISOU 1440 CG PRO A 196 13352 9027 12766 -2439 -923 1352 A C ATOM 1441 CD PRO A 196 41.291 -24.074 4.548 1.00 92.05 A C ANISOU 1441 CD PRO A 196 13286 8808 12882 -2323 -1069 1249 A C ATOM 1442 N PRO A 197 40.589 -26.378 8.510 1.00125.44 A N ANISOU 1442 N PRO A 197 18293 12399 16970 -2950 -743 1879 A N ATOM 1443 CA PRO A 197 39.629 -27.346 9.052 1.00119.54 A C ANISOU 1443 CA PRO A 197 17670 11407 16341 -3214 -596 1945 A C ATOM 1444 C PRO A 197 38.231 -26.944 8.627 1.00120.24 A C ANISOU 1444 C PRO A 197 17513 11597 16574 -3405 -436 1751 A C ATOM 1445 O PRO A 197 37.547 -27.692 7.940 1.00128.13 A O ANISOU 1445 O PRO A 197 18440 12444 17800 -3495 -435 1614 A O ATOM 1446 CB PRO A 197 39.772 -27.171 10.565 1.00116.64 A C ANISOU 1446 CB PRO A 197 17519 11049 15751 -3330 -473 2196 A C ATOM 1447 CG PRO A 197 41.123 -26.569 10.757 1.00122.52 A C ANISOU 1447 CG PRO A 197 18322 11944 16287 -3080 -630 2282 A C ATOM 1448 CD PRO A 197 41.334 -25.682 9.573 1.00122.71 A C ANISOU 1448 CD PRO A 197 18070 12191 16364 -2904 -731 2062 A C ATOM 1449 N GLU A 198 37.830 -25.750 9.040 1.00117.31 A N ANISOU 1449 N GLU A 198 17014 11488 16071 -3458 -309 1732 A N ATOM 1450 CA GLU A 198 36.555 -25.147 8.666 1.00113.81 A C ANISOU 1450 CA GLU A 198 16313 11201 15730 -3602 -161 1543 A C ATOM 1451 C GLU A 198 36.003 -25.650 7.339 1.00113.29 A C ANISOU 1451 C GLU A 198 16055 11071 15919 -3579 -238 1303 A C ATOM 1452 O GLU A 198 34.841 -26.055 7.247 1.00112.16 A O ANISOU 1452 O GLU A 198 15811 10864 15940 -3794 -112 1201 A O ATOM 1453 CB GLU A 198 36.747 -23.639 8.590 1.00107.22 A C ANISOU 1453 CB GLU A 198 15316 10685 14738 -3471 -153 1477 A C ATOM 1454 CG GLU A 198 38.099 -23.224 9.120 1.00113.12 A C ANISOU 1454 CG GLU A 198 16225 11490 15267 -3292 -267 1643 A C ATOM 1455 CD GLU A 198 38.498 -21.851 8.658 1.00126.88 A C ANISOU 1455 CD GLU A 198 17793 13508 16908 -3116 -318 1542 A C ATOM 1456 OE1 GLU A 198 37.610 -21.076 8.239 1.00122.12 A O ANISOU 1456 OE1 GLU A 198 16974 13069 16358 -3159 -220 1382 A O ATOM 1457 OE2 GLU A 198 39.707 -21.545 8.717 1.00141.02 A O1- ANISOU 1457 OE2 GLU A 198 19662 15350 18568 -2932 -456 1625 A O1- ATOM 1458 N LEU A 199 36.843 -25.612 6.310 1.00109.28 A N ANISOU 1458 N LEU A 199 15488 10596 15439 -3316 -445 1205 A N ATOM 1459 CA LEU A 199 36.431 -26.013 4.972 1.00103.90 A C ANISOU 1459 CA LEU A 199 14620 9886 14970 -3249 -544 962 A C ATOM 1460 C LEU A 199 36.183 -27.512 4.860 1.00100.08 A C ANISOU 1460 C LEU A 199 14269 9069 14688 -3372 -576 958 A C ATOM 1461 O LEU A 199 35.179 -27.945 4.303 1.00102.14 A O ANISOU 1461 O LEU A 199 14385 9271 15151 -3511 -531 777 A O ATOM 1462 CB LEU A 199 37.477 -25.581 3.949 1.00100.12 A C ANISOU 1462 CB LEU A 199 14061 9538 14443 -2923 -751 878 A C ATOM 1463 CG LEU A 199 37.432 -24.100 3.593 1.00 99.84 A C ANISOU 1463 CG LEU A 199 13814 9831 14289 -2803 -724 791 A C ATOM 1464 CD1 LEU A 199 38.398 -23.806 2.446 1.00106.93 A C ANISOU 1464 CD1 LEU A 199 14622 10840 15166 -2494 -921 699 A C ATOM 1465 CD2 LEU A 199 36.016 -23.706 3.226 1.00 93.46 A C ANISOU 1465 CD2 LEU A 199 12768 9144 13596 -2948 -591 599 A C ATOM 1466 N LEU A 200 37.111 -28.297 5.387 1.00 95.86 A N ANISOU 1466 N LEU A 200 14010 8314 14098 -3316 -659 1153 A N ATOM 1467 CA LEU A 200 37.003 -29.745 5.348 1.00 98.85 A C ANISOU 1467 CA LEU A 200 14561 8339 14659 -3416 -698 1177 A C ATOM 1468 C LEU A 200 35.725 -30.244 6.005 1.00107.11 A C ANISOU 1468 C LEU A 200 15626 9240 15831 -3775 -479 1202 A C ATOM 1469 O LEU A 200 35.236 -31.313 5.656 1.00104.33 A O ANISOU 1469 O LEU A 200 15309 8629 15701 -3904 -488 1122 A O ATOM 1470 CB LEU A 200 38.215 -30.377 6.018 1.00100.31 A C ANISOU 1470 CB LEU A 200 15062 8330 14722 -3292 -802 1423 A C ATOM 1471 CG LEU A 200 39.542 -29.996 5.369 1.00 99.31 A C ANISOU 1471 CG LEU A 200 14914 8336 14482 -2938 -1022 1400 A C ATOM 1472 CD1 LEU A 200 40.719 -30.427 6.231 1.00108.22 A C ANISOU 1472 CD1 LEU A 200 16337 9334 15447 -2820 -1105 1659 A C ATOM 1473 CD2 LEU A 200 39.644 -30.587 3.971 1.00 95.12 A C ANISOU 1473 CD2 LEU A 200 14269 7728 14145 -2776 -1194 1166 A C ATOM 1474 N LEU A 201 35.191 -29.474 6.954 1.00117.94 A N ANISOU 1474 N LEU A 201 16972 10778 17063 -3939 -281 1307 A N ATOM 1475 CA LEU A 201 33.921 -29.819 7.600 1.00126.95 A C ANISOU 1475 CA LEU A 201 18096 11833 18308 -4288 -47 1327 A C ATOM 1476 C LEU A 201 32.715 -29.255 6.845 1.00129.21 A C ANISOU 1476 C LEU A 201 18030 12327 18737 -4387 34 1047 A C ATOM 1477 O LEU A 201 31.647 -29.068 7.429 1.00134.48 A O ANISOU 1477 O LEU A 201 18609 13059 19430 -4646 251 1047 A O ATOM 1478 CB LEU A 201 33.879 -29.355 9.063 1.00120.55 A C ANISOU 1478 CB LEU A 201 17439 11095 17269 -4425 143 1581 A C ATOM 1479 CG LEU A 201 34.975 -29.810 10.030 1.00113.27 A C ANISOU 1479 CG LEU A 201 16870 10007 16161 -4345 92 1882 A C ATOM 1480 CD1 LEU A 201 34.456 -29.816 11.456 1.00113.80 A C ANISOU 1480 CD1 LEU A 201 17096 10052 16091 -4596 334 2110 A C ATOM 1481 CD2 LEU A 201 35.493 -31.174 9.666 1.00107.61 A C ANISOU 1481 CD2 LEU A 201 16357 8929 15599 -4295 -53 1927 A C ATOM 1482 N GLY A 202 32.898 -28.980 5.555 1.00119.22 A N ANISOU 1482 N GLY A 202 16563 11180 17554 -4170 -140 812 A N ATOM 1483 CA GLY A 202 31.805 -28.595 4.677 1.00114.74 A C ANISOU 1483 CA GLY A 202 15666 10790 17141 -4227 -104 525 A C ATOM 1484 C GLY A 202 31.237 -27.207 4.914 1.00112.84 A C ANISOU 1484 C GLY A 202 15215 10900 16759 -4230 30 476 A C ATOM 1485 O GLY A 202 30.084 -26.932 4.576 1.00110.89 A O ANISOU 1485 O GLY A 202 14715 10791 16628 -4359 130 284 A O ATOM 1486 N GLU A 203 32.045 -26.319 5.482 1.00109.63 A N ANISOU 1486 N GLU A 203 14906 10642 16107 -4080 25 638 A N ATOM 1487 CA GLU A 203 31.595 -24.956 5.724 1.00107.99 A C ANISOU 1487 CA GLU A 203 14522 10752 15758 -4061 142 595 A C ATOM 1488 C GLU A 203 31.428 -24.141 4.430 1.00107.23 A C ANISOU 1488 C GLU A 203 14142 10897 15705 -3842 30 341 A C ATOM 1489 O GLU A 203 32.298 -24.143 3.561 1.00 98.35 A O ANISOU 1489 O GLU A 203 13021 9774 14574 -3592 -167 290 A O ATOM 1490 CB GLU A 203 32.536 -24.249 6.694 1.00102.55 A C ANISOU 1490 CB GLU A 203 14023 10139 14800 -3967 160 828 A C ATOM 1491 CG GLU A 203 32.192 -22.789 6.911 1.00107.22 A C ANISOU 1491 CG GLU A 203 14454 11045 15241 -3917 261 778 A C ATOM 1492 CD GLU A 203 30.880 -22.601 7.639 1.00119.23 A C ANISOU 1492 CD GLU A 203 15874 12645 16783 -4185 508 754 A C ATOM 1493 OE1 GLU A 203 30.888 -22.651 8.887 1.00121.62 A O ANISOU 1493 OE1 GLU A 203 16356 12905 16950 -4337 652 954 A O ATOM 1494 OE2 GLU A 203 29.843 -22.399 6.969 1.00125.34 A O1- ANISOU 1494 OE2 GLU A 203 16385 13539 17700 -4236 559 534 A O1- ATOM 1495 N ARG A 204 30.297 -23.452 4.310 1.00112.41 A N ANISOU 1495 N ARG A 204 14553 11762 16397 -3932 161 186 A N ATOM 1496 CA ARG A 204 30.015 -22.628 3.141 1.00113.74 A C ANISOU 1496 CA ARG A 204 14452 12173 16593 -3727 73 -48 A C ATOM 1497 C ARG A 204 29.826 -21.159 3.524 1.00112.11 A C ANISOU 1497 C ARG A 204 14146 12246 16205 -3653 179 -33 A C ATOM 1498 O ARG A 204 29.577 -20.311 2.672 1.00114.62 A O ANISOU 1498 O ARG A 204 14255 12780 16515 -3476 128 -200 A O ATOM 1499 CB ARG A 204 28.777 -23.146 2.395 1.00116.16 A C ANISOU 1499 CB ARG A 204 14513 12489 17133 -3856 95 -305 A C ATOM 1500 CG ARG A 204 28.975 -24.477 1.689 1.00120.70 A C ANISOU 1500 CG ARG A 204 15143 12811 17908 -3871 -53 -389 A C ATOM 1501 CD ARG A 204 27.723 -24.914 0.930 1.00131.90 A C ANISOU 1501 CD ARG A 204 16295 14263 19559 -4001 -38 -671 A C ATOM 1502 NE ARG A 204 27.357 -23.990 -0.145 1.00135.98 A N ANISOU 1502 NE ARG A 204 16530 15077 20058 -3779 -119 -903 A N ATOM 1503 CZ ARG A 204 27.800 -24.079 -1.397 1.00136.37 A C ANISOU 1503 CZ ARG A 204 16501 15165 20147 -3525 -329 -1062 A C ATOM 1504 NH1 ARG A 204 28.639 -25.053 -1.740 1.00137.34 A N1+ ANISOU 1504 NH1 ARG A 204 16800 15048 20334 -3457 -483 -1027 A N1+ ATOM 1505 NH2 ARG A 204 27.408 -23.192 -2.308 1.00128.45 A N ANISOU 1505 NH2 ARG A 204 15250 14445 19110 -3325 -384 -1255 A N ATOM 1506 N ASP A 205 29.929 -20.865 4.812 1.00108.23 A N ANISOU 1506 N ASP A 205 13813 11747 15562 -3784 328 166 A N ATOM 1507 CA ASP A 205 29.875 -19.487 5.281 1.00115.38 A C ANISOU 1507 CA ASP A 205 14665 12891 16282 -3710 422 194 A C ATOM 1508 C ASP A 205 31.161 -19.144 6.023 1.00113.38 A C ANISOU 1508 C ASP A 205 14664 12596 15820 -3610 371 423 A C ATOM 1509 O ASP A 205 31.191 -19.083 7.254 1.00120.39 A O ANISOU 1509 O ASP A 205 15710 13455 16577 -3754 503 593 A O ATOM 1510 CB ASP A 205 28.669 -19.263 6.193 1.00126.03 A C ANISOU 1510 CB ASP A 205 15934 14329 17624 -3957 667 186 A C ATOM 1511 CG ASP A 205 28.695 -17.903 6.866 1.00130.06 A C ANISOU 1511 CG ASP A 205 16439 15053 17924 -3888 770 238 A C ATOM 1512 OD1 ASP A 205 28.911 -16.895 6.156 1.00137.72 A O ANISOU 1512 OD1 ASP A 205 17288 16195 18844 -3659 686 134 A O ATOM 1513 OD2 ASP A 205 28.511 -17.845 8.101 1.00122.04 A O1- ANISOU 1513 OD2 ASP A 205 15549 14029 16790 -4058 937 383 A O1- ATOM 1514 N TYR A 206 32.228 -18.935 5.265 1.00 98.74 A N ANISOU 1514 N TYR A 206 12840 10748 13929 -3362 179 423 A N ATOM 1515 CA TYR A 206 33.523 -18.624 5.847 1.00 93.01 A C ANISOU 1515 CA TYR A 206 12325 9995 13019 -3251 106 618 A C ATOM 1516 C TYR A 206 33.985 -17.236 5.416 1.00 92.75 A C ANISOU 1516 C TYR A 206 12193 10181 12866 -3033 56 568 A C ATOM 1517 O TYR A 206 33.239 -16.482 4.778 1.00 93.94 A O ANISOU 1517 O TYR A 206 12130 10503 13061 -2972 96 400 A O ATOM 1518 CB TYR A 206 34.547 -19.660 5.412 1.00 91.83 A C ANISOU 1518 CB TYR A 206 12321 9645 12926 -3150 -80 687 A C ATOM 1519 CG TYR A 206 34.543 -19.875 3.919 1.00 97.02 A C ANISOU 1519 CG TYR A 206 12805 10325 13734 -2976 -231 492 A C ATOM 1520 CD1 TYR A 206 34.109 -21.078 3.363 1.00 97.53 A C ANISOU 1520 CD1 TYR A 206 12847 10215 13997 -3050 -282 393 A C ATOM 1521 CD2 TYR A 206 34.946 -18.866 3.061 1.00 90.33 A C ANISOU 1521 CD2 TYR A 206 11819 9673 12828 -2739 -319 400 A C ATOM 1522 CE1 TYR A 206 34.098 -21.271 1.992 1.00 88.67 A C ANISOU 1522 CE1 TYR A 206 11564 9127 12999 -2880 -427 199 A C ATOM 1523 CE2 TYR A 206 34.931 -19.045 1.695 1.00 90.02 A C ANISOU 1523 CE2 TYR A 206 11625 9674 12904 -2568 -452 225 A C ATOM 1524 CZ TYR A 206 34.509 -20.245 1.164 1.00 88.56 A C ANISOU 1524 CZ TYR A 206 11416 9330 12904 -2633 -510 118 A C ATOM 1525 OH TYR A 206 34.512 -20.402 -0.202 1.00 83.60 A O ANISOU 1525 OH TYR A 206 10633 8756 12374 -2447 -651 -69 A O ATOM 1526 N GLY A 207 35.222 -16.908 5.770 1.00 87.24 A N ANISOU 1526 N GLY A 207 11652 9476 12019 -2916 -34 715 A N ATOM 1527 CA GLY A 207 35.800 -15.622 5.432 1.00 74.29 A C ANISOU 1527 CA GLY A 207 9946 8014 10266 -2726 -81 692 A C ATOM 1528 C GLY A 207 37.310 -15.610 5.569 1.00 75.51 A C ANISOU 1528 C GLY A 207 10259 8124 10306 -2589 -227 838 A C ATOM 1529 O GLY A 207 37.975 -16.645 5.480 1.00 72.90 A O ANISOU 1529 O GLY A 207 10045 7636 10015 -2565 -341 913 A O ATOM 1530 N PRO A 208 37.870 -14.422 5.795 1.00 78.87 A N ANISOU 1530 N PRO A 208 10686 8689 10593 -2497 -225 872 A N ATOM 1531 CA PRO A 208 39.322 -14.238 5.859 1.00 73.81 A C ANISOU 1531 CA PRO A 208 10155 8044 9844 -2361 -364 989 A C ATOM 1532 C PRO A 208 40.081 -15.327 6.596 1.00 79.90 A C ANISOU 1532 C PRO A 208 11139 8649 10570 -2415 -437 1153 A C ATOM 1533 O PRO A 208 41.124 -15.739 6.106 1.00 86.00 A O ANISOU 1533 O PRO A 208 11950 9376 11349 -2268 -596 1194 A O ATOM 1534 CB PRO A 208 39.450 -12.908 6.566 1.00 68.97 A C ANISOU 1534 CB PRO A 208 9556 7570 9079 -2374 -280 1019 A C ATOM 1535 CG PRO A 208 38.265 -12.139 5.990 1.00 69.80 A C ANISOU 1535 CG PRO A 208 9467 7797 9259 -2369 -168 852 A C ATOM 1536 CD PRO A 208 37.154 -13.137 5.870 1.00 72.77 A C ANISOU 1536 CD PRO A 208 9789 8090 9772 -2500 -100 781 A C ATOM 1537 N PRO A 209 39.565 -15.815 7.730 1.00 83.79 A N ANISOU 1537 N PRO A 209 11768 9053 11016 -2612 -321 1247 A N ATOM 1538 CA PRO A 209 40.447 -16.703 8.493 1.00 89.22 A C ANISOU 1538 CA PRO A 209 12682 9595 11623 -2631 -401 1427 A C ATOM 1539 C PRO A 209 40.920 -17.932 7.719 1.00 89.21 A C ANISOU 1539 C PRO A 209 12716 9425 11754 -2536 -553 1429 A C ATOM 1540 O PRO A 209 41.825 -18.616 8.198 1.00 94.29 A O ANISOU 1540 O PRO A 209 13540 9957 12331 -2496 -652 1573 A O ATOM 1541 CB PRO A 209 39.592 -17.098 9.698 1.00 83.92 A C ANISOU 1541 CB PRO A 209 12136 8851 10900 -2867 -228 1516 A C ATOM 1542 CG PRO A 209 38.627 -15.984 9.847 1.00 81.35 A C ANISOU 1542 CG PRO A 209 11665 8697 10547 -2943 -65 1406 A C ATOM 1543 CD PRO A 209 38.308 -15.545 8.444 1.00 77.16 A C ANISOU 1543 CD PRO A 209 10900 8253 10165 -2810 -117 1215 A C ATOM 1544 N ILE A 210 40.345 -18.202 6.549 1.00 82.42 A N ANISOU 1544 N ILE A 210 11691 8554 11072 -2487 -578 1267 A N ATOM 1545 CA ILE A 210 40.819 -19.327 5.743 1.00 81.85 A C ANISOU 1545 CA ILE A 210 11646 8328 11126 -2377 -732 1244 A C ATOM 1546 C ILE A 210 42.153 -19.006 5.078 1.00 85.54 A C ANISOU 1546 C ILE A 210 12087 8879 11535 -2126 -909 1254 A C ATOM 1547 O ILE A 210 42.989 -19.897 4.849 1.00 85.10 A O ANISOU 1547 O ILE A 210 12131 8700 11504 -2015 -1054 1309 A O ATOM 1548 CB ILE A 210 39.825 -19.738 4.645 1.00 73.88 A C ANISOU 1548 CB ILE A 210 10460 7290 10321 -2390 -721 1046 A C ATOM 1549 CG1 ILE A 210 39.842 -18.726 3.496 1.00 74.94 A C ANISOU 1549 CG1 ILE A 210 10368 7636 10469 -2207 -767 888 A C ATOM 1550 CG2 ILE A 210 38.442 -19.916 5.222 1.00 76.65 A C ANISOU 1550 CG2 ILE A 210 10786 7597 10739 -2643 -533 1011 A C ATOM 1551 CD1 ILE A 210 39.105 -19.199 2.249 1.00 71.11 A C ANISOU 1551 CD1 ILE A 210 9710 7139 10170 -2156 -809 683 A C ATOM 1552 N ASP A 211 42.345 -17.732 4.750 1.00 81.95 A N ANISOU 1552 N ASP A 211 11496 8632 11007 -2035 -895 1198 A N ATOM 1553 CA ASP A 211 43.583 -17.318 4.108 1.00 81.35 A C ANISOU 1553 CA ASP A 211 11374 8657 10877 -1814 -1040 1208 A C ATOM 1554 C ASP A 211 44.698 -17.267 5.147 1.00 84.17 A C ANISOU 1554 C ASP A 211 11902 9007 11070 -1808 -1097 1385 A C ATOM 1555 O ASP A 211 45.867 -17.473 4.831 1.00 82.27 A O ANISOU 1555 O ASP A 211 11682 8780 10795 -1643 -1245 1431 A O ATOM 1556 CB ASP A 211 43.414 -15.975 3.395 1.00 69.64 A C ANISOU 1556 CB ASP A 211 9699 7383 9378 -1727 -998 1100 A C ATOM 1557 CG ASP A 211 42.698 -16.102 2.061 1.00 74.80 A C ANISOU 1557 CG ASP A 211 10171 8072 10179 -1637 -1012 921 A C ATOM 1558 OD1 ASP A 211 42.518 -17.248 1.585 1.00 74.55 A O ANISOU 1558 OD1 ASP A 211 10155 7906 10266 -1620 -1082 869 A O ATOM 1559 OD2 ASP A 211 42.325 -15.049 1.484 1.00 75.08 A O1- ANISOU 1559 OD2 ASP A 211 10055 8266 10208 -1575 -957 829 A O1- ATOM 1560 N LEU A 212 44.321 -17.022 6.396 1.00 84.96 A N ANISOU 1560 N LEU A 212 12120 9094 11066 -1983 -980 1479 A N ATOM 1561 CA LEU A 212 45.297 -16.858 7.459 1.00 86.58 A C ANISOU 1561 CA LEU A 212 12481 9320 11095 -1983 -1028 1635 A C ATOM 1562 C LEU A 212 45.803 -18.199 7.926 1.00 84.49 A C ANISOU 1562 C LEU A 212 12413 8867 10823 -1973 -1122 1765 A C ATOM 1563 O LEU A 212 46.896 -18.293 8.475 1.00 87.54 A O ANISOU 1563 O LEU A 212 12910 9267 11083 -1891 -1230 1882 A O ATOM 1564 CB LEU A 212 44.695 -16.088 8.621 1.00 91.28 A C ANISOU 1564 CB LEU A 212 13134 9983 11563 -2160 -869 1678 A C ATOM 1565 CG LEU A 212 44.675 -14.591 8.381 1.00 90.79 A C ANISOU 1565 CG LEU A 212 12924 10118 11454 -2127 -816 1586 A C ATOM 1566 CD1 LEU A 212 43.610 -13.957 9.245 1.00115.13 A C ANISOU 1566 CD1 LEU A 212 16024 13248 14473 -2307 -627 1568 A C ATOM 1567 CD2 LEU A 212 46.028 -14.063 8.728 1.00 85.83 A C ANISOU 1567 CD2 LEU A 212 12340 9580 10689 -2027 -933 1664 A C ATOM 1568 N TRP A 213 44.997 -19.233 7.714 1.00 84.76 A N ANISOU 1568 N TRP A 213 12488 8721 10994 -2056 -1082 1741 A N ATOM 1569 CA TRP A 213 45.438 -20.604 7.934 1.00 85.26 A C ANISOU 1569 CA TRP A 213 12737 8567 11089 -2025 -1181 1848 A C ATOM 1570 C TRP A 213 46.544 -20.923 6.937 1.00 88.11 A C ANISOU 1570 C TRP A 213 13039 8941 11498 -1773 -1381 1806 A C ATOM 1571 O TRP A 213 47.622 -21.359 7.322 1.00 91.63 A O ANISOU 1571 O TRP A 213 13614 9350 11853 -1657 -1510 1924 A O ATOM 1572 CB TRP A 213 44.277 -21.576 7.762 1.00 80.54 A C ANISOU 1572 CB TRP A 213 12169 7770 10662 -2177 -1090 1802 A C ATOM 1573 CG TRP A 213 44.660 -22.980 7.989 1.00 84.77 A C ANISOU 1573 CG TRP A 213 12912 8052 11245 -2156 -1181 1913 A C ATOM 1574 CD1 TRP A 213 45.111 -23.861 7.057 1.00 90.01 A C ANISOU 1574 CD1 TRP A 213 13571 8588 12041 -1998 -1332 1850 A C ATOM 1575 CD2 TRP A 213 44.631 -23.687 9.234 1.00 98.21 A C ANISOU 1575 CD2 TRP A 213 14870 9587 12857 -2286 -1125 2111 A C ATOM 1576 CE2 TRP A 213 45.085 -24.999 8.978 1.00100.01 A C ANISOU 1576 CE2 TRP A 213 15248 9572 13179 -2196 -1252 2165 A C ATOM 1577 CE3 TRP A 213 44.271 -23.338 10.541 1.00100.03 A C ANISOU 1577 CE3 TRP A 213 15226 9852 12928 -2459 -979 2249 A C ATOM 1578 NE1 TRP A 213 45.375 -25.078 7.641 1.00 95.53 A N ANISOU 1578 NE1 TRP A 213 14513 9034 12748 -2019 -1379 1995 A N ATOM 1579 CZ2 TRP A 213 45.187 -25.966 9.980 1.00 97.93 A C ANISOU 1579 CZ2 TRP A 213 15263 9087 12858 -2275 -1236 2366 A C ATOM 1580 CZ3 TRP A 213 44.374 -24.296 11.537 1.00103.44 A C ANISOU 1580 CZ3 TRP A 213 15928 10083 13291 -2538 -960 2449 A C ATOM 1581 CH2 TRP A 213 44.827 -25.598 11.249 1.00104.55 A C ANISOU 1581 CH2 TRP A 213 16221 9970 13532 -2447 -1087 2512 A C ATOM 1582 N GLY A 214 46.281 -20.696 5.655 1.00 84.49 A N ANISOU 1582 N GLY A 214 12380 8551 11170 -1678 -1407 1634 A N ATOM 1583 CA GLY A 214 47.321 -20.832 4.656 1.00 85.38 A C ANISOU 1583 CA GLY A 214 12409 8722 11310 -1431 -1579 1582 A C ATOM 1584 C GLY A 214 48.627 -20.201 5.122 1.00 87.32 A C ANISOU 1584 C GLY A 214 12677 9115 11384 -1316 -1667 1688 A C ATOM 1585 O GLY A 214 49.667 -20.849 5.164 1.00 93.42 A O ANISOU 1585 O GLY A 214 13537 9839 12120 -1169 -1814 1762 A O ATOM 1586 N ALA A 215 48.576 -18.927 5.481 1.00 85.32 A N ANISOU 1586 N ALA A 215 12343 9043 11031 -1382 -1580 1687 A N ATOM 1587 CA ALA A 215 49.775 -18.212 5.899 1.00 84.84 A C ANISOU 1587 CA ALA A 215 12279 9138 10820 -1295 -1657 1764 A C ATOM 1588 C ALA A 215 50.512 -18.926 7.030 1.00 92.98 A C ANISOU 1588 C ALA A 215 13526 10076 11727 -1295 -1741 1931 A C ATOM 1589 O ALA A 215 51.740 -18.941 7.061 1.00 97.13 A O ANISOU 1589 O ALA A 215 14053 10679 12173 -1144 -1882 1984 A O ATOM 1590 CB ALA A 215 49.431 -16.787 6.307 1.00 77.79 A C ANISOU 1590 CB ALA A 215 11304 8410 9843 -1409 -1531 1739 A C ATOM 1591 N GLY A 216 49.766 -19.505 7.964 1.00 88.40 A N ANISOU 1591 N GLY A 216 13122 9340 11124 -1461 -1651 2016 A N ATOM 1592 CA GLY A 216 50.372 -20.299 9.017 1.00 88.18 A C ANISOU 1592 CA GLY A 216 13324 9204 10978 -1451 -1726 2187 A C ATOM 1593 C GLY A 216 51.225 -21.418 8.438 1.00 91.68 A C ANISOU 1593 C GLY A 216 13820 9530 11486 -1245 -1907 2210 A C ATOM 1594 O GLY A 216 52.366 -21.612 8.840 1.00 96.54 A O ANISOU 1594 O GLY A 216 14507 10187 11985 -1108 -2046 2304 A O ATOM 1595 N CYS A 217 50.672 -22.149 7.476 1.00 92.21 A N ANISOU 1595 N CYS A 217 13842 9456 11737 -1215 -1910 2112 A N ATOM 1596 CA CYS A 217 51.370 -23.274 6.864 1.00 96.71 A C ANISOU 1596 CA CYS A 217 14468 9892 12387 -1016 -2076 2112 A C ATOM 1597 C CYS A 217 52.621 -22.827 6.148 1.00 95.89 A C ANISOU 1597 C CYS A 217 14207 9986 12240 -778 -2226 2061 A C ATOM 1598 O CYS A 217 53.656 -23.492 6.193 1.00107.87 A O ANISOU 1598 O CYS A 217 15802 11470 13715 -594 -2385 2126 A O ATOM 1599 CB CYS A 217 50.468 -23.967 5.853 1.00 93.62 A C ANISOU 1599 CB CYS A 217 14020 9342 12208 -1036 -2046 1974 A C ATOM 1600 SG CYS A 217 48.892 -24.404 6.527 1.00103.39 A S ANISOU 1600 SG CYS A 217 15383 10372 13528 -1341 -1849 2002 A S ATOM 1601 N ILE A 218 52.507 -21.710 5.452 1.00 83.57 A N ANISOU 1601 N ILE A 218 12424 8633 10697 -777 -2170 1943 A N ATOM 1602 CA ILE A 218 53.624 -21.188 4.700 1.00 86.62 A C ANISOU 1602 CA ILE A 218 12639 9223 11052 -573 -2284 1891 A C ATOM 1603 C ILE A 218 54.675 -20.674 5.671 1.00 92.97 A C ANISOU 1603 C ILE A 218 13487 10163 11675 -551 -2348 2012 A C ATOM 1604 O ILE A 218 55.868 -20.862 5.460 1.00 99.99 A O ANISOU 1604 O ILE A 218 14335 11141 12516 -359 -2497 2033 A O ATOM 1605 CB ILE A 218 53.163 -20.094 3.735 1.00 83.17 A C ANISOU 1605 CB ILE A 218 11968 8957 10676 -590 -2190 1750 A C ATOM 1606 CG1 ILE A 218 52.048 -20.649 2.840 1.00 87.73 A C ANISOU 1606 CG1 ILE A 218 12503 9404 11424 -615 -2135 1621 A C ATOM 1607 CG2 ILE A 218 54.336 -19.569 2.909 1.00 65.97 A C ANISOU 1607 CG2 ILE A 218 9610 6989 8468 -384 -2293 1708 A C ATOM 1608 CD1 ILE A 218 51.249 -19.592 2.139 1.00 83.84 A C ANISOU 1608 CD1 ILE A 218 11823 9052 10982 -677 -2010 1498 A C ATOM 1609 N MET A 219 54.232 -20.055 6.758 1.00 92.92 A N ANISOU 1609 N MET A 219 13563 10181 11564 -744 -2239 2083 A N ATOM 1610 CA MET A 219 55.168 -19.574 7.767 1.00 88.27 A C ANISOU 1610 CA MET A 219 13026 9722 10793 -736 -2304 2186 A C ATOM 1611 C MET A 219 56.033 -20.714 8.292 1.00 83.30 A C ANISOU 1611 C MET A 219 12570 8988 10093 -591 -2467 2307 A C ATOM 1612 O MET A 219 57.229 -20.554 8.509 1.00 88.31 A O ANISOU 1612 O MET A 219 13166 9764 10623 -454 -2602 2345 A O ATOM 1613 CB MET A 219 54.438 -18.896 8.925 1.00 83.48 A C ANISOU 1613 CB MET A 219 12515 9128 10078 -965 -2159 2241 A C ATOM 1614 CG MET A 219 55.329 -17.962 9.725 1.00 74.75 A C ANISOU 1614 CG MET A 219 11383 8220 8797 -972 -2207 2283 A C ATOM 1615 SD MET A 219 54.566 -17.422 11.254 1.00128.72 A S ANISOU 1615 SD MET A 219 18384 15051 15471 -1210 -2064 2361 A S ATOM 1616 CE MET A 219 55.947 -16.596 12.034 1.00102.27 A C ANISOU 1616 CE MET A 219 15000 11932 11927 -1149 -2195 2393 A C ATOM 1617 N ALA A 220 55.426 -21.871 8.495 1.00 82.47 A N ANISOU 1617 N ALA A 220 12654 8633 10049 -619 -2454 2367 A N ATOM 1618 CA ALA A 220 56.183 -23.034 8.923 1.00 91.94 A C ANISOU 1618 CA ALA A 220 14039 9699 11196 -463 -2607 2486 A C ATOM 1619 C ALA A 220 57.101 -23.494 7.792 1.00 97.56 A C ANISOU 1619 C ALA A 220 14623 10451 11994 -199 -2769 2403 A C ATOM 1620 O ALA A 220 58.287 -23.737 7.985 1.00101.54 A O ANISOU 1620 O ALA A 220 15136 11040 12405 -9 -2930 2457 A O ATOM 1621 CB ALA A 220 55.241 -24.142 9.332 1.00 88.50 A C ANISOU 1621 CB ALA A 220 13838 8959 10827 -573 -2537 2567 A C ATOM 1622 N GLU A 221 56.537 -23.599 6.602 1.00101.24 A N ANISOU 1622 N GLU A 221 14961 10873 12633 -180 -2726 2262 A N ATOM 1623 CA GLU A 221 57.273 -24.057 5.437 1.00107.53 A C ANISOU 1623 CA GLU A 221 15632 11706 13517 70 -2861 2165 A C ATOM 1624 C GLU A 221 58.562 -23.263 5.239 1.00114.00 A C ANISOU 1624 C GLU A 221 16264 12818 14233 223 -2960 2150 A C ATOM 1625 O GLU A 221 59.377 -23.606 4.392 1.00120.14 A O ANISOU 1625 O GLU A 221 16932 13667 15048 452 -3083 2087 A O ATOM 1626 CB GLU A 221 56.370 -23.930 4.211 1.00105.49 A C ANISOU 1626 CB GLU A 221 15226 11425 13432 35 -2771 1998 A C ATOM 1627 CG GLU A 221 56.799 -24.674 2.972 1.00103.39 A C ANISOU 1627 CG GLU A 221 14877 11128 13280 275 -2892 1882 A C ATOM 1628 CD GLU A 221 55.595 -25.056 2.142 1.00114.14 A C ANISOU 1628 CD GLU A 221 16214 12337 14816 196 -2808 1747 A C ATOM 1629 OE1 GLU A 221 54.557 -25.378 2.762 1.00118.44 A O ANISOU 1629 OE1 GLU A 221 16906 12687 15409 -14 -2702 1789 A O ATOM 1630 OE2 GLU A 221 55.672 -25.025 0.892 1.00115.06 A O1- ANISOU 1630 OE2 GLU A 221 16160 12539 15018 341 -2843 1598 A O1- ATOM 1631 N MET A 222 58.738 -22.199 6.020 1.00117.51 A N ANISOU 1631 N MET A 222 16666 13433 14548 93 -2904 2200 A N ATOM 1632 CA MET A 222 59.919 -21.336 5.909 1.00118.13 A C ANISOU 1632 CA MET A 222 16556 13793 14536 194 -2983 2182 A C ATOM 1633 C MET A 222 61.123 -21.917 6.654 1.00123.47 A C ANISOU 1633 C MET A 222 17325 14507 15080 360 -3164 2288 A C ATOM 1634 O MET A 222 62.274 -21.593 6.353 1.00124.38 A O ANISOU 1634 O MET A 222 17275 14835 15148 514 -3274 2259 A O ATOM 1635 CB MET A 222 59.616 -19.925 6.436 1.00108.14 A C ANISOU 1635 CB MET A 222 15207 12685 13196 -18 -2853 2175 A C ATOM 1636 CG MET A 222 58.581 -19.137 5.625 1.00101.43 A C ANISOU 1636 CG MET A 222 14224 11852 12462 -149 -2684 2062 A C ATOM 1637 SD MET A 222 59.208 -18.428 4.079 1.00 91.79 A S ANISOU 1637 SD MET A 222 12700 10851 11326 6 -2699 1932 A S ATOM 1638 CE MET A 222 60.603 -17.485 4.692 1.00209.40 A C ANISOU 1638 CE MET A 222 27480 26006 26076 24 -2780 1980 A C ATOM 1639 N TRP A 223 60.851 -22.774 7.631 1.00120.63 A N ANISOU 1639 N TRP A 223 17229 13946 14658 328 -3191 2413 A N ATOM 1640 CA TRP A 223 61.910 -23.398 8.408 1.00112.06 A C ANISOU 1640 CA TRP A 223 16263 12878 13435 497 -3366 2526 A C ATOM 1641 C TRP A 223 62.046 -24.861 8.052 1.00115.17 A C ANISOU 1641 C TRP A 223 16810 13041 13906 699 -3479 2557 A C ATOM 1642 O TRP A 223 62.974 -25.525 8.502 1.00126.02 A O ANISOU 1642 O TRP A 223 18280 14415 15186 895 -3645 2640 A O ATOM 1643 CB TRP A 223 61.634 -23.262 9.905 1.00108.35 A C ANISOU 1643 CB TRP A 223 16003 12367 12798 338 -3327 2667 A C ATOM 1644 CG TRP A 223 62.006 -21.922 10.428 1.00118.81 A C ANISOU 1644 CG TRP A 223 17184 13958 14000 222 -3296 2641 A C ATOM 1645 CD1 TRP A 223 63.256 -21.497 10.778 1.00122.90 A C ANISOU 1645 CD1 TRP A 223 17592 14715 14391 339 -3439 2645 A C ATOM 1646 CD2 TRP A 223 61.128 -20.810 10.642 1.00117.25 A C ANISOU 1646 CD2 TRP A 223 16929 13816 13803 -35 -3112 2593 A C ATOM 1647 CE2 TRP A 223 61.914 -19.745 11.128 1.00111.02 A C ANISOU 1647 CE2 TRP A 223 16009 13286 12889 -64 -3156 2570 A C ATOM 1648 CE3 TRP A 223 59.754 -20.613 10.469 1.00109.28 A C ANISOU 1648 CE3 TRP A 223 15961 12668 12894 -237 -2919 2560 A C ATOM 1649 NE1 TRP A 223 63.208 -20.190 11.203 1.00119.56 A N ANISOU 1649 NE1 TRP A 223 17053 14480 13896 159 -3356 2600 A N ATOM 1650 CZ2 TRP A 223 61.372 -18.502 11.443 1.00 98.95 A C ANISOU 1650 CZ2 TRP A 223 14407 11858 11331 -284 -3012 2516 A C ATOM 1651 CZ3 TRP A 223 59.220 -19.384 10.788 1.00105.10 A C ANISOU 1651 CZ3 TRP A 223 15352 12256 12327 -442 -2778 2510 A C ATOM 1652 CH2 TRP A 223 60.028 -18.342 11.271 1.00101.00 A C ANISOU 1652 CH2 TRP A 223 14719 11974 11682 -461 -2825 2489 A C ATOM 1653 N THR A 224 61.120 -25.363 7.244 1.00104.77 A N ANISOU 1653 N THR A 224 15518 11528 12764 656 -3396 2482 A N ATOM 1654 CA THR A 224 61.046 -26.795 7.005 1.00106.72 A C ANISOU 1654 CA THR A 224 15952 11496 13101 804 -3483 2511 A C ATOM 1655 C THR A 224 61.254 -27.131 5.543 1.00105.75 A C ANISOU 1655 C THR A 224 15660 11388 13132 991 -3541 2348 A C ATOM 1656 O THR A 224 61.292 -28.300 5.169 1.00112.24 A O ANISOU 1656 O THR A 224 16610 11993 14044 1147 -3630 2336 A O ATOM 1657 CB THR A 224 59.695 -27.394 7.477 1.00 92.64 A C ANISOU 1657 CB THR A 224 14407 9398 11394 582 -3344 2576 A C ATOM 1658 CG2 THR A 224 59.393 -27.009 8.918 1.00 77.60 A C ANISOU 1658 CG2 THR A 224 12668 7495 9324 386 -3262 2736 A C ATOM 1659 OG1 THR A 224 58.634 -26.936 6.632 1.00 97.31 A O ANISOU 1659 OG1 THR A 224 14857 9977 12138 421 -3192 2434 A O ATOM 1660 N ARG A 225 61.381 -26.108 4.714 1.00102.64 A N ANISOU 1660 N ARG A 225 14988 11244 12766 980 -3487 2221 A N ATOM 1661 CA ARG A 225 61.503 -26.321 3.273 1.00109.37 A C ANISOU 1661 CA ARG A 225 15666 12140 13750 1151 -3522 2060 A C ATOM 1662 C ARG A 225 60.404 -27.219 2.670 1.00110.79 A C ANISOU 1662 C ARG A 225 15962 12027 14105 1108 -3471 1981 A C ATOM 1663 O ARG A 225 60.400 -27.473 1.464 1.00112.47 A O ANISOU 1663 O ARG A 225 16048 12258 14428 1249 -3501 1834 A O ATOM 1664 CB ARG A 225 62.888 -26.885 2.936 1.00109.00 A C ANISOU 1664 CB ARG A 225 15560 12199 13656 1476 -3719 2051 A C ATOM 1665 CG ARG A 225 64.025 -25.979 3.365 1.00106.80 A C ANISOU 1665 CG ARG A 225 15115 12240 13224 1525 -3777 2097 A C ATOM 1666 CD ARG A 225 63.719 -24.555 2.984 1.00107.74 A C ANISOU 1666 CD ARG A 225 15004 12584 13347 1343 -3628 2027 A C ATOM 1667 NE ARG A 225 64.805 -23.640 3.305 1.00112.65 A N ANISOU 1667 NE ARG A 225 15448 13510 13845 1371 -3676 2052 A N ATOM 1668 CZ ARG A 225 65.601 -23.075 2.402 1.00121.32 A C ANISOU 1668 CZ ARG A 225 16277 14866 14953 1497 -3698 1964 A C ATOM 1669 NH1 ARG A 225 65.439 -23.331 1.108 1.00119.46 A N1+ ANISOU 1669 NH1 ARG A 225 15927 14634 14830 1625 -3679 1847 A N1+ ATOM 1670 NH2 ARG A 225 66.562 -22.248 2.796 1.00125.26 A N ANISOU 1670 NH2 ARG A 225 16619 15628 15347 1491 -3736 1989 A N ATOM 1671 N SER A 226 59.469 -27.686 3.495 1.00106.78 A N ANISOU 1671 N SER A 226 15688 11262 13622 909 -3390 2073 A N ATOM 1672 CA SER A 226 58.453 -28.623 3.025 1.00116.22 A C ANISOU 1672 CA SER A 226 17005 12161 14993 851 -3348 2003 A C ATOM 1673 C SER A 226 57.062 -28.355 3.626 1.00116.42 A C ANISOU 1673 C SER A 226 17124 12047 15061 519 -3156 2040 A C ATOM 1674 O SER A 226 56.948 -28.044 4.814 1.00118.63 A O ANISOU 1674 O SER A 226 17531 12324 15221 364 -3093 2192 A O ATOM 1675 CB SER A 226 58.905 -30.060 3.327 1.00127.60 A C ANISOU 1675 CB SER A 226 18696 13329 16458 1026 -3495 2082 A C ATOM 1676 OG SER A 226 58.040 -31.031 2.751 1.00131.60 A O ANISOU 1676 OG SER A 226 19310 13539 17154 993 -3475 1990 A O ATOM 1677 N PRO A 227 56.001 -28.483 2.800 1.00107.31 A N ANISOU 1677 N PRO A 227 15903 10792 14076 418 -3066 1894 A N ATOM 1678 CA PRO A 227 54.605 -28.402 3.255 1.00 99.95 A C ANISOU 1678 CA PRO A 227 15050 9709 13216 113 -2887 1906 A C ATOM 1679 C PRO A 227 54.398 -29.328 4.445 1.00114.51 A C ANISOU 1679 C PRO A 227 17206 11269 15033 8 -2878 2090 A C ATOM 1680 O PRO A 227 54.672 -30.526 4.351 1.00122.84 A O ANISOU 1680 O PRO A 227 18432 12082 16160 138 -2988 2115 A O ATOM 1681 CB PRO A 227 53.812 -28.935 2.062 1.00 91.60 A C ANISOU 1681 CB PRO A 227 13912 8526 12365 123 -2877 1709 A C ATOM 1682 CG PRO A 227 54.685 -28.711 0.892 1.00 97.30 A C ANISOU 1682 CG PRO A 227 14429 9454 13087 397 -2999 1575 A C ATOM 1683 CD PRO A 227 56.097 -28.835 1.373 1.00103.00 A C ANISOU 1683 CD PRO A 227 15208 10265 13662 607 -3143 1700 A C ATOM 1684 N ILE A 228 53.901 -28.781 5.545 1.00117.08 A N ANISOU 1684 N ILE A 228 17613 11619 15253 -220 -2743 2219 A N ATOM 1685 CA ILE A 228 53.903 -29.492 6.822 1.00113.87 A C ANISOU 1685 CA ILE A 228 17505 11002 14760 -299 -2734 2432 A C ATOM 1686 C ILE A 228 52.803 -30.547 7.021 1.00120.55 A C ANISOU 1686 C ILE A 228 18555 11491 15760 -482 -2638 2465 A C ATOM 1687 O ILE A 228 52.915 -31.391 7.913 1.00125.68 A O ANISOU 1687 O ILE A 228 19480 11914 16359 -499 -2656 2646 A O ATOM 1688 CB ILE A 228 53.888 -28.495 7.994 1.00110.20 A C ANISOU 1688 CB ILE A 228 17058 10721 14093 -455 -2632 2563 A C ATOM 1689 CG1 ILE A 228 52.675 -27.564 7.881 1.00111.34 A C ANISOU 1689 CG1 ILE A 228 17050 10962 14291 -716 -2426 2467 A C ATOM 1690 CG2 ILE A 228 55.192 -27.698 8.014 1.00104.91 A C ANISOU 1690 CG2 ILE A 228 16247 10352 13260 -259 -2761 2569 A C ATOM 1691 CD1 ILE A 228 52.393 -26.748 9.127 1.00105.27 A C ANISOU 1691 CD1 ILE A 228 16344 10311 13343 -908 -2297 2593 A C ATOM 1692 N MET A 229 51.756 -30.510 6.198 1.00123.06 A N ANISOU 1692 N MET A 229 18737 11757 16262 -618 -2539 2292 A N ATOM 1693 CA MET A 229 50.663 -31.485 6.296 1.00120.86 A C ANISOU 1693 CA MET A 229 18618 11147 16157 -815 -2442 2295 A C ATOM 1694 C MET A 229 50.257 -32.045 4.936 1.00120.24 A C ANISOU 1694 C MET A 229 18416 10958 16311 -748 -2498 2063 A C ATOM 1695 O MET A 229 49.283 -31.584 4.338 1.00115.70 A O ANISOU 1695 O MET A 229 17655 10457 15850 -898 -2388 1900 A O ATOM 1696 CB MET A 229 49.431 -30.857 6.950 1.00106.98 A C ANISOU 1696 CB MET A 229 16832 9425 14390 -1146 -2210 2326 A C ATOM 1697 CG MET A 229 49.644 -30.340 8.353 1.00 95.34 A C ANISOU 1697 CG MET A 229 15494 8045 12686 -1244 -2131 2545 A C ATOM 1698 SD MET A 229 48.131 -29.556 8.925 1.00166.11 A S ANISOU 1698 SD MET A 229 24380 17079 21656 -1613 -1853 2533 A S ATOM 1699 CE MET A 229 48.736 -28.618 10.322 1.00121.78 A C ANISOU 1699 CE MET A 229 18850 11691 15729 -1630 -1814 2732 A C ATOM 1700 N GLN A 230 50.984 -33.050 4.460 1.00122.92 A N ANISOU 1700 N GLN A 230 18863 11123 16719 -516 -2672 2040 A N ATOM 1701 CA GLN A 230 50.751 -33.579 3.117 1.00126.15 A C ANISOU 1701 CA GLN A 230 19153 11450 17330 -408 -2753 1802 A C ATOM 1702 C GLN A 230 49.797 -34.776 3.099 1.00126.37 A C ANISOU 1702 C GLN A 230 19358 11081 17575 -581 -2705 1768 A C ATOM 1703 O GLN A 230 50.227 -35.917 3.205 1.00125.72 A O ANISOU 1703 O GLN A 230 19504 10711 17555 -464 -2815 1830 A O ATOM 1704 CB GLN A 230 52.086 -33.936 2.456 1.00123.61 A C ANISOU 1704 CB GLN A 230 18810 11189 16966 -36 -2974 1755 A C ATOM 1705 CG GLN A 230 53.080 -32.785 2.472 1.00119.34 A C ANISOU 1705 CG GLN A 230 18086 11036 16221 124 -3020 1788 A C ATOM 1706 CD GLN A 230 54.450 -33.180 1.981 1.00118.21 A C ANISOU 1706 CD GLN A 230 17932 10960 16021 484 -3229 1769 A C ATOM 1707 NE2 GLN A 230 54.939 -32.485 0.963 1.00117.82 A N ANISOU 1707 NE2 GLN A 230 17614 11203 15950 656 -3283 1614 A N ATOM 1708 OE1 GLN A 230 55.070 -34.092 2.517 1.00121.53 A O ANISOU 1708 OE1 GLN A 230 18584 11180 16413 612 -3338 1896 A O ATOM 1709 N GLY A 231 48.502 -34.506 2.950 1.00129.47 A N ANISOU 1709 N GLY A 231 19641 11461 18091 -857 -2541 1664 A N ATOM 1710 CA GLY A 231 47.495 -35.553 2.975 1.00133.27 A C ANISOU 1710 CA GLY A 231 20263 11582 18791 -1071 -2470 1625 A C ATOM 1711 C GLY A 231 47.086 -36.050 1.599 1.00139.16 A C ANISOU 1711 C GLY A 231 20863 12252 19760 -1000 -2555 1333 A C ATOM 1712 O GLY A 231 47.177 -35.314 0.613 1.00139.41 A O ANISOU 1712 O GLY A 231 20623 12567 19778 -866 -2603 1140 A O ATOM 1713 N ASN A 232 46.632 -37.301 1.538 1.00143.25 A N ANISOU 1713 N ASN A 232 21567 12382 20481 -1091 -2573 1300 A N ATOM 1714 CA ASN A 232 46.191 -37.915 0.286 1.00148.42 A C ANISOU 1714 CA ASN A 232 22110 12919 21364 -1041 -2661 1009 A C ATOM 1715 C ASN A 232 44.736 -37.598 -0.028 1.00147.61 A C ANISOU 1715 C ASN A 232 21813 12857 21416 -1345 -2502 837 A C ATOM 1716 O ASN A 232 44.353 -37.521 -1.196 1.00147.56 A O ANISOU 1716 O ASN A 232 21587 12950 21529 -1281 -2563 558 A O ATOM 1717 CB ASN A 232 46.386 -39.435 0.312 1.00161.40 A C ANISOU 1717 CB ASN A 232 24044 14107 23173 -993 -2766 1029 A C ATOM 1718 CG ASN A 232 47.853 -39.844 0.319 1.00170.97 A C ANISOU 1718 CG ASN A 232 25412 15290 24260 -624 -2964 1130 A C ATOM 1719 ND2 ASN A 232 48.124 -41.071 -0.120 1.00176.94 A N ANISOU 1719 ND2 ASN A 232 26345 15710 25172 -485 -3105 1049 A N ATOM 1720 OD1 ASN A 232 48.728 -39.076 0.722 1.00170.25 A O ANISOU 1720 OD1 ASN A 232 25280 15472 23938 -467 -2992 1272 A O ATOM 1721 N THR A 233 43.928 -37.434 1.018 1.00147.23 A N ANISOU 1721 N THR A 233 21843 12738 21359 -1668 -2301 999 A N ATOM 1722 CA THR A 233 42.537 -37.001 0.868 1.00145.41 A C ANISOU 1722 CA THR A 233 21408 12593 21249 -1969 -2129 857 A C ATOM 1723 C THR A 233 42.036 -36.304 2.123 1.00140.80 A C ANISOU 1723 C THR A 233 20861 12109 20529 -2228 -1911 1080 A C ATOM 1724 O THR A 233 42.662 -36.385 3.178 1.00140.92 A O ANISOU 1724 O THR A 233 21107 12052 20384 -2213 -1888 1352 A O ATOM 1725 CB THR A 233 41.588 -38.173 0.583 1.00146.15 A C ANISOU 1725 CB THR A 233 21576 12318 21635 -2187 -2102 720 A C ATOM 1726 CG2 THR A 233 41.749 -38.666 -0.849 1.00143.39 A C ANISOU 1726 CG2 THR A 233 21102 11937 21443 -1970 -2297 411 A C ATOM 1727 OG1 THR A 233 41.860 -39.239 1.503 1.00150.80 A O ANISOU 1727 OG1 THR A 233 22525 12513 22261 -2269 -2088 954 A O ATOM 1728 N GLU A 234 40.894 -35.635 1.995 1.00133.13 A N ANISOU 1728 N GLU A 234 19660 11310 19615 -2453 -1755 954 A N ATOM 1729 CA GLU A 234 40.262 -34.939 3.111 1.00134.45 A C ANISOU 1729 CA GLU A 234 19829 11590 19665 -2711 -1532 1126 A C ATOM 1730 C GLU A 234 40.365 -35.709 4.430 1.00145.79 A C ANISOU 1730 C GLU A 234 21607 12727 21060 -2875 -1437 1425 A C ATOM 1731 O GLU A 234 40.924 -35.201 5.407 1.00144.32 A O ANISOU 1731 O GLU A 234 21543 12650 20642 -2842 -1390 1660 A O ATOM 1732 CB GLU A 234 38.803 -34.637 2.775 1.00135.95 A C ANISOU 1732 CB GLU A 234 19775 11866 20015 -2981 -1376 928 A C ATOM 1733 CG GLU A 234 38.640 -33.730 1.564 1.00145.93 A C ANISOU 1733 CG GLU A 234 20699 13465 21284 -2816 -1452 655 A C ATOM 1734 CD GLU A 234 37.191 -33.555 1.137 1.00157.05 A C ANISOU 1734 CD GLU A 234 21859 14945 22867 -3058 -1326 432 A C ATOM 1735 OE1 GLU A 234 36.592 -34.536 0.634 1.00166.09 A O ANISOU 1735 OE1 GLU A 234 23003 15850 24253 -3175 -1356 271 A O ATOM 1736 OE2 GLU A 234 36.656 -32.433 1.299 1.00150.30 A O1- ANISOU 1736 OE2 GLU A 234 20808 14388 21911 -3125 -1201 408 A O1- ATOM 1737 N GLN A 235 39.819 -36.926 4.452 1.00151.88 A N ANISOU 1737 N GLN A 235 22535 13120 22052 -3052 -1410 1414 A N ATOM 1738 CA GLN A 235 39.945 -37.828 5.597 1.00148.57 A C ANISOU 1738 CA GLN A 235 22473 12361 21615 -3190 -1333 1701 A C ATOM 1739 C GLN A 235 41.357 -37.790 6.173 1.00141.17 A C ANISOU 1739 C GLN A 235 21759 11444 20436 -2905 -1465 1935 A C ATOM 1740 O GLN A 235 41.553 -37.501 7.358 1.00130.71 A O ANISOU 1740 O GLN A 235 20596 10159 18910 -2975 -1358 2200 A O ATOM 1741 CB GLN A 235 39.624 -39.266 5.176 1.00155.17 A C ANISOU 1741 CB GLN A 235 23469 12754 22736 -3280 -1387 1620 A C ATOM 1742 CG GLN A 235 38.150 -39.648 5.235 1.00162.79 A C ANISOU 1742 CG GLN A 235 24353 13564 23938 -3682 -1188 1522 A C ATOM 1743 CD GLN A 235 37.750 -40.242 6.577 1.00166.60 A C ANISOU 1743 CD GLN A 235 25126 13769 24404 -3972 -984 1828 A C ATOM 1744 NE2 GLN A 235 37.137 -41.423 6.543 1.00160.33 A N ANISOU 1744 NE2 GLN A 235 24480 12566 23872 -4198 -933 1808 A N ATOM 1745 OE1 GLN A 235 37.986 -39.646 7.630 1.00170.90 A O ANISOU 1745 OE1 GLN A 235 25767 14467 24702 -3996 -871 2078 A O ATOM 1746 N HIS A 236 42.332 -38.093 5.317 1.00139.47 A N ANISOU 1746 N HIS A 236 21543 11212 20238 -2578 -1701 1826 A N ATOM 1747 CA HIS A 236 43.732 -38.167 5.715 1.00135.95 A C ANISOU 1747 CA HIS A 236 21287 10780 19589 -2275 -1858 2013 A C ATOM 1748 C HIS A 236 44.209 -36.834 6.250 1.00137.97 A C ANISOU 1748 C HIS A 236 21419 11438 19563 -2198 -1819 2116 A C ATOM 1749 O HIS A 236 44.802 -36.763 7.326 1.00140.46 A O ANISOU 1749 O HIS A 236 21939 11756 19675 -2165 -1802 2376 A O ATOM 1750 CB HIS A 236 44.606 -38.595 4.532 1.00135.67 A C ANISOU 1750 CB HIS A 236 21199 10719 19631 -1933 -2109 1824 A C ATOM 1751 CG HIS A 236 46.052 -38.782 4.884 1.00140.76 A C ANISOU 1751 CG HIS A 236 22029 11366 20087 -1609 -2282 1998 A C ATOM 1752 CD2 HIS A 236 46.648 -39.161 6.040 1.00141.68 A C ANISOU 1752 CD2 HIS A 236 22445 11339 20049 -1578 -2279 2297 A C ATOM 1753 ND1 HIS A 236 47.074 -38.563 3.983 1.00140.06 A N ANISOU 1753 ND1 HIS A 236 21807 11463 19945 -1257 -2487 1862 A N ATOM 1754 CE1 HIS A 236 48.235 -38.804 4.566 1.00135.47 A C ANISOU 1754 CE1 HIS A 236 21424 10855 19195 -1027 -2607 2059 A C ATOM 1755 NE2 HIS A 236 48.006 -39.167 5.815 1.00137.51 A N ANISOU 1755 NE2 HIS A 236 21949 10915 19385 -1208 -2491 2324 A N ATOM 1756 N GLN A 237 43.951 -35.779 5.482 1.00138.33 A N ANISOU 1756 N GLN A 237 21137 11823 19600 -2165 -1811 1908 A N ATOM 1757 CA GLN A 237 44.353 -34.431 5.856 1.00129.49 A C ANISOU 1757 CA GLN A 237 19873 11089 18240 -2098 -1775 1968 A C ATOM 1758 C GLN A 237 43.817 -34.098 7.236 1.00123.92 A C ANISOU 1758 C GLN A 237 19294 10392 17398 -2358 -1567 2193 A C ATOM 1759 O GLN A 237 44.577 -34.007 8.193 1.00125.53 A O ANISOU 1759 O GLN A 237 19685 10617 17392 -2281 -1587 2422 A O ATOM 1760 CB GLN A 237 43.828 -33.415 4.842 1.00127.86 A C ANISOU 1760 CB GLN A 237 19306 11192 18085 -2091 -1751 1708 A C ATOM 1761 CG GLN A 237 44.200 -31.970 5.145 1.00122.36 A C ANISOU 1761 CG GLN A 237 18452 10879 17160 -2028 -1710 1752 A C ATOM 1762 CD GLN A 237 45.567 -31.597 4.617 1.00121.73 A C ANISOU 1762 CD GLN A 237 18314 10982 16956 -1686 -1908 1735 A C ATOM 1763 NE2 GLN A 237 45.928 -30.324 4.754 1.00121.70 A N ANISOU 1763 NE2 GLN A 237 18157 11307 16777 -1627 -1882 1750 A N ATOM 1764 OE1 GLN A 237 46.291 -32.440 4.087 1.00121.49 A O ANISOU 1764 OE1 GLN A 237 18372 10799 16990 -1478 -2078 1704 A O ATOM 1765 N LEU A 238 42.503 -33.927 7.333 1.00117.61 A N ANISOU 1765 N LEU A 238 18386 9588 16712 -2659 -1369 2120 A N ATOM 1766 CA LEU A 238 41.869 -33.574 8.598 1.00120.01 A C ANISOU 1766 CA LEU A 238 18784 9925 16891 -2921 -1148 2312 A C ATOM 1767 C LEU A 238 42.511 -34.299 9.777 1.00119.05 A C ANISOU 1767 C LEU A 238 19027 9581 16626 -2907 -1153 2622 A C ATOM 1768 O LEU A 238 42.640 -33.748 10.863 1.00117.01 A O ANISOU 1768 O LEU A 238 18861 9454 16142 -2965 -1054 2814 A O ATOM 1769 CB LEU A 238 40.374 -33.890 8.551 1.00126.37 A C ANISOU 1769 CB LEU A 238 19505 10606 17905 -3261 -948 2214 A C ATOM 1770 CG LEU A 238 39.376 -32.769 8.865 1.00121.75 A C ANISOU 1770 CG LEU A 238 18693 10308 17259 -3470 -739 2152 A C ATOM 1771 CD1 LEU A 238 37.958 -33.289 8.679 1.00128.40 A C ANISOU 1771 CD1 LEU A 238 19443 10998 18344 -3787 -570 2032 A C ATOM 1772 CD2 LEU A 238 39.564 -32.185 10.269 1.00107.86 A C ANISOU 1772 CD2 LEU A 238 17082 8671 15227 -3544 -606 2410 A C ATOM 1773 N ALA A 239 42.910 -35.542 9.558 1.00126.43 A N ANISOU 1773 N ALA A 239 20175 10175 17687 -2818 -1273 2667 A N ATOM 1774 CA ALA A 239 43.519 -36.334 10.613 1.00128.48 A C ANISOU 1774 CA ALA A 239 20802 10192 17822 -2781 -1292 2965 A C ATOM 1775 C ALA A 239 44.908 -35.809 10.990 1.00126.82 A C ANISOU 1775 C ALA A 239 20652 10194 17341 -2471 -1457 3088 A C ATOM 1776 O ALA A 239 45.274 -35.811 12.162 1.00130.68 A O ANISOU 1776 O ALA A 239 21361 10675 17614 -2479 -1413 3345 A O ATOM 1777 CB ALA A 239 43.582 -37.789 10.200 1.00134.04 A C ANISOU 1777 CB ALA A 239 21716 10463 18748 -2750 -1386 2963 A C ATOM 1778 N LEU A 240 45.676 -35.362 9.997 1.00122.08 A N ANISOU 1778 N LEU A 240 19848 9791 16744 -2200 -1645 2904 A N ATOM 1779 CA LEU A 240 46.991 -34.765 10.244 1.00118.98 A C ANISOU 1779 CA LEU A 240 19455 9640 16111 -1914 -1803 2985 A C ATOM 1780 C LEU A 240 46.877 -33.499 11.072 1.00119.27 A C ANISOU 1780 C LEU A 240 19395 10004 15919 -2019 -1676 3063 A C ATOM 1781 O LEU A 240 47.710 -33.234 11.935 1.00116.70 A O ANISOU 1781 O LEU A 240 19199 9786 15355 -1902 -1732 3243 A O ATOM 1782 CB LEU A 240 47.686 -34.417 8.933 1.00115.88 A C ANISOU 1782 CB LEU A 240 18816 9428 15784 -1643 -1992 2749 A C ATOM 1783 CG LEU A 240 48.705 -35.404 8.386 1.00122.47 A C ANISOU 1783 CG LEU A 240 19780 10074 16679 -1343 -2222 2739 A C ATOM 1784 CD1 LEU A 240 48.007 -36.695 7.986 1.00125.58 A C ANISOU 1784 CD1 LEU A 240 20322 10058 17335 -1452 -2207 2684 A C ATOM 1785 CD2 LEU A 240 49.436 -34.781 7.203 1.00121.00 A C ANISOU 1785 CD2 LEU A 240 19313 10163 16498 -1078 -2381 2521 A C ATOM 1786 N ILE A 241 45.846 -32.712 10.771 1.00123.86 A N ANISOU 1786 N ILE A 241 19740 10749 16573 -2227 -1515 2911 A N ATOM 1787 CA ILE A 241 45.562 -31.463 11.467 1.00116.52 A C ANISOU 1787 CA ILE A 241 18696 10122 15455 -2346 -1376 2947 A C ATOM 1788 C ILE A 241 45.201 -31.721 12.917 1.00120.26 A C ANISOU 1788 C ILE A 241 19428 10490 15775 -2541 -1215 3205 A C ATOM 1789 O ILE A 241 45.741 -31.079 13.814 1.00120.75 A O ANISOU 1789 O ILE A 241 19556 10739 15585 -2490 -1213 3342 A O ATOM 1790 CB ILE A 241 44.377 -30.717 10.825 1.00113.81 A C ANISOU 1790 CB ILE A 241 18063 9931 15250 -2537 -1224 2727 A C ATOM 1791 CG1 ILE A 241 44.645 -30.442 9.344 1.00114.54 A C ANISOU 1791 CG1 ILE A 241 17895 10139 15486 -2347 -1370 2468 A C ATOM 1792 CG2 ILE A 241 44.085 -29.425 11.580 1.00115.11 A C ANISOU 1792 CG2 ILE A 241 18125 10394 15217 -2648 -1079 2763 A C ATOM 1793 CD1 ILE A 241 43.525 -29.676 8.656 1.00116.36 A C ANISOU 1793 CD1 ILE A 241 17835 10537 15840 -2498 -1241 2247 A C ATOM 1794 N SER A 242 44.276 -32.654 13.141 1.00123.72 A N ANISOU 1794 N SER A 242 20010 10633 16366 -2769 -1077 3268 A N ATOM 1795 CA SER A 242 43.853 -32.997 14.498 1.00124.25 A C ANISOU 1795 CA SER A 242 20336 10576 16296 -2970 -902 3528 A C ATOM 1796 C SER A 242 44.994 -33.658 15.260 1.00124.71 A C ANISOU 1796 C SER A 242 20715 10498 16172 -2766 -1045 3779 A C ATOM 1797 O SER A 242 44.933 -33.814 16.475 1.00131.24 A O ANISOU 1797 O SER A 242 21777 11279 16811 -2861 -936 4022 A O ATOM 1798 CB SER A 242 42.576 -33.862 14.513 1.00121.38 A C ANISOU 1798 CB SER A 242 20041 9920 16159 -3281 -708 3535 A C ATOM 1799 OG SER A 242 42.468 -34.701 13.373 1.00116.65 A O ANISOU 1799 OG SER A 242 19391 9085 15846 -3236 -817 3365 A O ATOM 1800 N GLN A 243 46.045 -34.014 14.531 1.00121.64 A N ANISOU 1800 N GLN A 243 20326 10065 15826 -2470 -1291 3714 A N ATOM 1801 CA GLN A 243 47.219 -34.651 15.112 1.00129.72 A C ANISOU 1801 CA GLN A 243 21627 10975 16688 -2227 -1461 3924 A C ATOM 1802 C GLN A 243 48.246 -33.622 15.590 1.00124.82 A C ANISOU 1802 C GLN A 243 20932 10712 15780 -2028 -1573 3963 A C ATOM 1803 O GLN A 243 49.015 -33.879 16.517 1.00123.47 A O ANISOU 1803 O GLN A 243 20996 10526 15390 -1897 -1649 4180 A O ATOM 1804 CB GLN A 243 47.846 -35.582 14.077 1.00137.27 A C ANISOU 1804 CB GLN A 243 22612 11708 17838 -1995 -1674 3821 A C ATOM 1805 CG GLN A 243 48.882 -36.532 14.626 1.00143.42 A C ANISOU 1805 CG GLN A 243 23715 12275 18503 -1759 -1838 4041 A C ATOM 1806 CD GLN A 243 49.127 -37.701 13.696 1.00145.58 A C ANISOU 1806 CD GLN A 243 24073 12221 19019 -1610 -1986 3953 A C ATOM 1807 NE2 GLN A 243 49.911 -38.671 14.157 1.00153.36 A N ANISOU 1807 NE2 GLN A 243 25371 12963 19938 -1412 -2119 4148 A N ATOM 1808 OE1 GLN A 243 48.610 -37.737 12.579 1.00136.79 A O ANISOU 1808 OE1 GLN A 243 22751 11073 18147 -1664 -1986 3707 A O ATOM 1809 N LEU A 244 48.245 -32.457 14.946 1.00126.47 A N ANISOU 1809 N LEU A 244 20816 11241 15996 -2006 -1583 3748 A N ATOM 1810 CA LEU A 244 49.165 -31.372 15.275 1.00123.61 A C ANISOU 1810 CA LEU A 244 20342 11229 15397 -1843 -1681 3745 A C ATOM 1811 C LEU A 244 48.505 -30.317 16.170 1.00128.89 A C ANISOU 1811 C LEU A 244 20954 12126 15894 -2061 -1483 3784 A C ATOM 1812 O LEU A 244 49.170 -29.683 16.991 1.00132.26 A O ANISOU 1812 O LEU A 244 21424 12763 16067 -1981 -1528 3879 A O ATOM 1813 CB LEU A 244 49.686 -30.712 13.995 1.00115.51 A C ANISOU 1813 CB LEU A 244 19002 10411 14476 -1664 -1822 3494 A C ATOM 1814 CG LEU A 244 50.806 -29.678 14.165 1.00111.72 A C ANISOU 1814 CG LEU A 244 18391 10270 13786 -1471 -1955 3475 A C ATOM 1815 CD1 LEU A 244 52.169 -30.354 14.074 1.00113.79 A C ANISOU 1815 CD1 LEU A 244 18768 10482 13986 -1156 -2203 3549 A C ATOM 1816 CD2 LEU A 244 50.701 -28.542 13.148 1.00 94.47 A C ANISOU 1816 CD2 LEU A 244 15855 8351 11688 -1462 -1949 3230 A C ATOM 1817 N CYS A 245 47.196 -30.137 16.017 1.00127.52 A N ANISOU 1817 N CYS A 245 20678 11915 15857 -2333 -1268 3699 A N ATOM 1818 CA CYS A 245 46.479 -29.098 16.754 1.00125.99 A C ANISOU 1818 CA CYS A 245 20401 11946 15522 -2535 -1071 3701 A C ATOM 1819 C CYS A 245 45.444 -29.642 17.745 1.00131.89 A C ANISOU 1819 C CYS A 245 21356 12519 16237 -2809 -836 3879 A C ATOM 1820 O CYS A 245 44.614 -28.892 18.259 1.00130.19 A O ANISOU 1820 O CYS A 245 21056 12463 15946 -3009 -638 3859 A O ATOM 1821 CB CYS A 245 45.807 -28.132 15.776 1.00120.27 A C ANISOU 1821 CB CYS A 245 19331 11414 14951 -2612 -1002 3433 A C ATOM 1822 SG CYS A 245 46.910 -27.511 14.491 1.00130.65 A S ANISOU 1822 SG CYS A 245 20391 12924 16326 -2313 -1247 3225 A S ATOM 1823 N GLY A 246 45.495 -30.943 18.013 1.00140.52 A N ANISOU 1823 N GLY A 246 22722 13283 17385 -2816 -852 4054 A N ATOM 1824 CA GLY A 246 44.564 -31.563 18.941 1.00143.90 A C ANISOU 1824 CA GLY A 246 23368 13517 17789 -3078 -624 4247 A C ATOM 1825 C GLY A 246 43.289 -32.017 18.259 1.00140.52 A C ANISOU 1825 C GLY A 246 22824 12903 17664 -3333 -459 4118 A C ATOM 1826 O GLY A 246 43.134 -31.856 17.053 1.00135.07 A O ANISOU 1826 O GLY A 246 21888 12238 17194 -3291 -533 3873 A O ATOM 1827 N SER A 247 42.373 -32.593 19.025 1.00145.34 A N ANISOU 1827 N SER A 247 23606 13334 18282 -3599 -233 4281 A N ATOM 1828 CA SER A 247 41.120 -33.066 18.453 1.00149.73 A C ANISOU 1828 CA SER A 247 24048 13711 19131 -3870 -65 4161 A C ATOM 1829 C SER A 247 40.146 -31.912 18.331 1.00145.29 A C ANISOU 1829 C SER A 247 23172 13452 18578 -4049 113 3972 A C ATOM 1830 O SER A 247 40.312 -30.875 18.982 1.00139.87 A O ANISOU 1830 O SER A 247 22433 13064 17648 -4015 158 3997 A O ATOM 1831 CB SER A 247 40.511 -34.183 19.304 1.00155.36 A C ANISOU 1831 CB SER A 247 25066 14096 19867 -4102 120 4416 A C ATOM 1832 OG SER A 247 41.356 -35.319 19.329 1.00155.52 A O ANISOU 1832 OG SER A 247 25385 13797 19910 -3930 -47 4582 A O ATOM 1833 N ILE A 248 39.138 -32.089 17.486 1.00143.66 A N ANISOU 1833 N ILE A 248 22758 13172 18655 -4229 205 3772 A N ATOM 1834 CA ILE A 248 38.109 -31.074 17.340 1.00139.17 A C ANISOU 1834 CA ILE A 248 21888 12875 18115 -4402 381 3588 A C ATOM 1835 C ILE A 248 36.974 -31.337 18.321 1.00145.52 A C ANISOU 1835 C ILE A 248 22782 13618 18892 -4736 684 3733 A C ATOM 1836 O ILE A 248 36.110 -32.181 18.088 1.00149.71 A O ANISOU 1836 O ILE A 248 23315 13911 19656 -4965 807 3716 A O ATOM 1837 CB ILE A 248 37.555 -30.986 15.901 1.00126.04 A C ANISOU 1837 CB ILE A 248 19911 11226 16754 -4412 324 3271 A C ATOM 1838 CG1 ILE A 248 38.610 -30.440 14.935 1.00101.35 A C ANISOU 1838 CG1 ILE A 248 16645 8248 13617 -4083 55 3111 A C ATOM 1839 CG2 ILE A 248 36.332 -30.092 15.864 1.00125.05 A C ANISOU 1839 CG2 ILE A 248 19501 11346 16667 -4620 535 3106 A C ATOM 1840 CD1 ILE A 248 39.513 -31.495 14.331 1.00 94.10 A C ANISOU 1840 CD1 ILE A 248 15885 7056 12813 -3886 -172 3138 A C ATOM 1841 N THR A 249 37.000 -30.608 19.428 1.00145.80 A N ANISOU 1841 N THR A 249 22888 13873 18637 -4762 805 3871 A N ATOM 1842 CA THR A 249 35.988 -30.718 20.460 1.00145.50 A C ANISOU 1842 CA THR A 249 22930 13834 18518 -5057 1105 4020 A C ATOM 1843 C THR A 249 35.407 -29.330 20.678 1.00142.06 A C ANISOU 1843 C THR A 249 22235 13788 17954 -5106 1238 3870 A C ATOM 1844 O THR A 249 36.098 -28.333 20.491 1.00132.05 A O ANISOU 1844 O THR A 249 20858 12767 16549 -4885 1091 3766 A O ATOM 1845 CB THR A 249 36.603 -31.222 21.771 1.00144.51 A C ANISOU 1845 CB THR A 249 23192 13600 18114 -5026 1136 4367 A C ATOM 1846 CG2 THR A 249 37.272 -32.570 21.562 1.00144.26 A C ANISOU 1846 CG2 THR A 249 23439 13177 18198 -4936 984 4522 A C ATOM 1847 OG1 THR A 249 37.590 -30.287 22.216 1.00142.43 A O ANISOU 1847 OG1 THR A 249 22954 13609 17556 -4775 994 4392 A O ATOM 1848 N PRO A 250 34.127 -29.259 21.055 1.00145.18 A N ANISOU 1848 N PRO A 250 22525 14236 18402 -5398 1518 3852 A N ATOM 1849 CA PRO A 250 33.477 -27.977 21.340 1.00143.62 A C ANISOU 1849 CA PRO A 250 22090 14400 18078 -5453 1668 3714 A C ATOM 1850 C PRO A 250 34.072 -27.249 22.548 1.00142.27 A C ANISOU 1850 C PRO A 250 22090 14442 17524 -5346 1693 3881 A C ATOM 1851 O PRO A 250 33.719 -26.096 22.789 1.00135.31 A O ANISOU 1851 O PRO A 250 21032 13867 16514 -5342 1781 3759 A O ATOM 1852 CB PRO A 250 32.025 -28.376 21.614 1.00146.74 A C ANISOU 1852 CB PRO A 250 22395 14746 18613 -5805 1974 3713 A C ATOM 1853 CG PRO A 250 31.848 -29.656 20.883 1.00148.55 A C ANISOU 1853 CG PRO A 250 22673 14616 19153 -5910 1923 3709 A C ATOM 1854 CD PRO A 250 33.163 -30.368 21.010 1.00148.13 A C ANISOU 1854 CD PRO A 250 22943 14329 19012 -5692 1697 3907 A C ATOM 1855 N GLU A 251 34.952 -27.904 23.298 1.00153.13 A N ANISOU 1855 N GLU A 251 23805 15661 18718 -5254 1613 4149 A N ATOM 1856 CA GLU A 251 35.651 -27.224 24.386 1.00162.98 A C ANISOU 1856 CA GLU A 251 25213 17118 19592 -5116 1592 4291 A C ATOM 1857 C GLU A 251 36.763 -26.359 23.800 1.00157.82 A C ANISOU 1857 C GLU A 251 24448 16639 18879 -4811 1311 4135 A C ATOM 1858 O GLU A 251 37.105 -25.302 24.335 1.00151.66 A O ANISOU 1858 O GLU A 251 23632 16133 17858 -4709 1294 4100 A O ATOM 1859 CB GLU A 251 36.226 -28.226 25.392 1.00174.35 A C ANISOU 1859 CB GLU A 251 27057 18343 20845 -5104 1593 4634 A C ATOM 1860 CG GLU A 251 37.277 -29.163 24.818 1.00182.11 A C ANISOU 1860 CG GLU A 251 28211 19043 21939 -4906 1327 4710 A C ATOM 1861 CD GLU A 251 37.966 -29.999 25.880 1.00189.58 A C ANISOU 1861 CD GLU A 251 29565 19817 22651 -4839 1302 5052 A C ATOM 1862 OE1 GLU A 251 37.861 -31.246 25.825 1.00191.03 A O ANISOU 1862 OE1 GLU A 251 29954 19650 22979 -4923 1327 5214 A O ATOM 1863 OE2 GLU A 251 38.612 -29.406 26.769 1.00190.22 A O1- ANISOU 1863 OE2 GLU A 251 29765 20110 22400 -4696 1255 5155 A O1- ATOM 1864 N VAL A 252 37.312 -26.830 22.685 1.00153.94 A N ANISOU 1864 N VAL A 252 23897 15980 18612 -4673 1095 4036 A N ATOM 1865 CA VAL A 252 38.366 -26.139 21.958 1.00141.92 A C ANISOU 1865 CA VAL A 252 22252 14593 17079 -4392 828 3885 A C ATOM 1866 C VAL A 252 37.737 -25.246 20.890 1.00140.61 A C ANISOU 1866 C VAL A 252 21717 14601 17107 -4409 844 3577 A C ATOM 1867 O VAL A 252 38.026 -24.049 20.804 1.00135.36 A O ANISOU 1867 O VAL A 252 20897 14202 16333 -4291 790 3442 A O ATOM 1868 CB VAL A 252 39.309 -27.165 21.295 1.00130.69 A C ANISOU 1868 CB VAL A 252 20963 12903 15789 -4216 588 3944 A C ATOM 1869 CG1 VAL A 252 40.326 -26.483 20.431 1.00117.01 A C ANISOU 1869 CG1 VAL A 252 19069 11318 14073 -3942 330 3774 A C ATOM 1870 CG2 VAL A 252 39.998 -28.013 22.353 1.00136.31 A C ANISOU 1870 CG2 VAL A 252 22051 13449 16293 -4163 553 4255 A C ATOM 1871 N TRP A 253 36.858 -25.840 20.093 1.00141.94 A N ANISOU 1871 N TRP A 253 21752 14614 17565 -4560 921 3466 A N ATOM 1872 CA TRP A 253 36.186 -25.138 19.005 1.00140.33 A C ANISOU 1872 CA TRP A 253 21201 14553 17563 -4573 932 3175 A C ATOM 1873 C TRP A 253 34.669 -25.178 19.193 1.00142.50 A C ANISOU 1873 C TRP A 253 21339 14854 17950 -4868 1213 3112 A C ATOM 1874 O TRP A 253 33.989 -26.040 18.636 1.00147.01 A O ANISOU 1874 O TRP A 253 21856 15228 18774 -5020 1266 3062 A O ATOM 1875 CB TRP A 253 36.578 -25.779 17.670 1.00137.71 A C ANISOU 1875 CB TRP A 253 20788 14042 17494 -4447 726 3047 A C ATOM 1876 CG TRP A 253 35.900 -25.210 16.451 1.00133.24 A C ANISOU 1876 CG TRP A 253 19879 13600 17147 -4444 719 2751 A C ATOM 1877 CD1 TRP A 253 34.876 -24.298 16.413 1.00136.50 A C ANISOU 1877 CD1 TRP A 253 20050 14239 17575 -4561 889 2593 A C ATOM 1878 CD2 TRP A 253 36.203 -25.525 15.090 1.00123.75 A C ANISOU 1878 CD2 TRP A 253 18540 12310 16170 -4300 529 2578 A C ATOM 1879 CE2 TRP A 253 35.323 -24.772 14.278 1.00126.53 A C ANISOU 1879 CE2 TRP A 253 18572 12847 16657 -4337 592 2323 A C ATOM 1880 CE3 TRP A 253 37.132 -26.371 14.477 1.00116.35 A C ANISOU 1880 CE3 TRP A 253 17720 11165 15323 -4129 310 2609 A C ATOM 1881 NE1 TRP A 253 34.526 -24.029 15.108 1.00129.23 A N ANISOU 1881 NE1 TRP A 253 18854 13375 16870 -4494 810 2337 A N ATOM 1882 CZ2 TRP A 253 35.344 -24.845 12.887 1.00122.73 A C ANISOU 1882 CZ2 TRP A 253 17892 12351 16387 -4213 443 2107 A C ATOM 1883 CZ3 TRP A 253 37.154 -26.442 13.096 1.00119.06 A C ANISOU 1883 CZ3 TRP A 253 17862 11495 15881 -4010 167 2387 A C ATOM 1884 CH2 TRP A 253 36.264 -25.687 12.316 1.00121.97 A C ANISOU 1884 CH2 TRP A 253 17919 12054 16371 -4054 235 2141 A C ATOM 1885 N PRO A 254 34.132 -24.239 19.985 1.00134.80 A N ANISOU 1885 N PRO A 254 20299 14129 16788 -4950 1392 3105 A N ATOM 1886 CA PRO A 254 32.698 -24.198 20.290 1.00130.73 A C ANISOU 1886 CA PRO A 254 19645 13680 16345 -5225 1676 3052 A C ATOM 1887 C PRO A 254 31.814 -24.224 19.046 1.00132.27 A C ANISOU 1887 C PRO A 254 19526 13872 16858 -5297 1687 2787 A C ATOM 1888 O PRO A 254 32.016 -23.422 18.139 1.00130.17 A O ANISOU 1888 O PRO A 254 19046 13757 16656 -5121 1548 2575 A O ATOM 1889 CB PRO A 254 32.544 -22.868 21.028 1.00123.83 A C ANISOU 1889 CB PRO A 254 18699 13134 15218 -5187 1782 3009 A C ATOM 1890 CG PRO A 254 33.861 -22.672 21.694 1.00126.87 A C ANISOU 1890 CG PRO A 254 19331 13539 15337 -4987 1620 3175 A C ATOM 1891 CD PRO A 254 34.882 -23.207 20.722 1.00129.99 A C ANISOU 1891 CD PRO A 254 19761 13752 15877 -4790 1339 3154 A C ATOM 1892 N ASN A 255 30.855 -25.146 19.018 1.00143.31 A N ANISOU 1892 N ASN A 255 20903 15098 18450 -5555 1849 2804 A N ATOM 1893 CA ASN A 255 29.861 -25.251 17.942 1.00148.58 A C ANISOU 1893 CA ASN A 255 21263 15770 19420 -5663 1885 2549 A C ATOM 1894 C ASN A 255 30.296 -26.047 16.710 1.00143.03 A C ANISOU 1894 C ASN A 255 20534 14836 18976 -5561 1657 2443 A C ATOM 1895 O ASN A 255 29.681 -25.939 15.648 1.00138.15 A O ANISOU 1895 O ASN A 255 19640 14267 18583 -5571 1622 2191 A O ATOM 1896 CB ASN A 255 29.315 -23.873 17.531 1.00149.17 A C ANISOU 1896 CB ASN A 255 21019 16189 19470 -5581 1921 2300 A C ATOM 1897 CG ASN A 255 27.966 -23.563 18.166 1.00152.96 A C ANISOU 1897 CG ASN A 255 21346 16836 19935 -5833 2224 2260 A C ATOM 1898 ND2 ASN A 255 26.983 -23.220 17.338 1.00151.79 A N ANISOU 1898 ND2 ASN A 255 20866 16821 19988 -5889 2274 1998 A N ATOM 1899 OD1 ASN A 255 27.812 -23.631 19.385 1.00154.38 A O ANISOU 1899 OD1 ASN A 255 21700 17039 19918 -5966 2409 2459 A O ATOM 1900 N VAL A 256 31.348 -26.844 16.855 1.00140.20 A N ANISOU 1900 N VAL A 256 20460 14234 18575 -5452 1501 2628 A N ATOM 1901 CA VAL A 256 31.730 -27.771 15.799 1.00141.41 A C ANISOU 1901 CA VAL A 256 20626 14130 18972 -5375 1304 2549 A C ATOM 1902 C VAL A 256 30.651 -28.829 15.600 1.00165.85 A C ANISOU 1902 C VAL A 256 23678 16997 22340 -5673 1451 2510 A C ATOM 1903 O VAL A 256 30.346 -29.221 14.470 1.00170.75 A O ANISOU 1903 O VAL A 256 24124 17529 23225 -5671 1351 2296 A O ATOM 1904 CB VAL A 256 33.040 -28.492 16.120 1.00127.02 A C ANISOU 1904 CB VAL A 256 19140 12080 17042 -5205 1125 2775 A C ATOM 1905 CG1 VAL A 256 34.169 -27.820 15.418 1.00121.58 A C ANISOU 1905 CG1 VAL A 256 18390 11528 16278 -4868 863 2676 A C ATOM 1906 CG2 VAL A 256 33.273 -28.554 17.627 1.00122.81 A C ANISOU 1906 CG2 VAL A 256 18894 11538 16230 -5283 1266 3078 A C ATOM 1907 N ASP A 257 30.082 -29.297 16.709 1.00180.78 A N ANISOU 1907 N ASP A 257 25730 18796 24162 -5933 1692 2718 A N ATOM 1908 CA ASP A 257 29.028 -30.308 16.669 1.00184.01 A C ANISOU 1908 CA ASP A 257 26111 18980 24824 -6259 1866 2709 A C ATOM 1909 C ASP A 257 27.898 -29.910 15.716 1.00182.03 A C ANISOU 1909 C ASP A 257 25452 18899 24811 -6368 1921 2376 A C ATOM 1910 O ASP A 257 27.191 -30.764 15.181 1.00185.79 A O ANISOU 1910 O ASP A 257 25840 19181 25572 -6569 1961 2269 A O ATOM 1911 CB ASP A 257 28.496 -30.626 18.083 1.00185.83 A C ANISOU 1911 CB ASP A 257 26539 19163 24905 -6529 2159 2982 A C ATOM 1912 CG ASP A 257 28.296 -29.378 18.952 1.00184.72 A C ANISOU 1912 CG ASP A 257 26323 19395 24466 -6501 2309 3016 A C ATOM 1913 OD1 ASP A 257 28.279 -28.248 18.419 1.00185.76 A O ANISOU 1913 OD1 ASP A 257 26199 19823 24557 -6333 2230 2796 A O ATOM 1914 OD2 ASP A 257 28.147 -29.538 20.183 1.00179.29 A O1- ANISOU 1914 OD2 ASP A 257 25844 18698 23580 -6645 2511 3268 A O1- ATOM 1915 N ASN A 258 27.753 -28.608 15.492 1.00171.97 A N ANISOU 1915 N ASN A 258 23934 17986 23421 -6224 1911 2209 A N ATOM 1916 CA ASN A 258 26.709 -28.081 14.624 1.00163.62 A C ANISOU 1916 CA ASN A 258 22482 17136 22549 -6285 1955 1894 A C ATOM 1917 C ASN A 258 26.831 -28.524 13.161 1.00149.65 A C ANISOU 1917 C ASN A 258 20560 15250 21050 -6167 1724 1651 A C ATOM 1918 O ASN A 258 25.902 -28.345 12.372 1.00140.72 A O ANISOU 1918 O ASN A 258 19112 14242 20113 -6242 1750 1384 A O ATOM 1919 CB ASN A 258 26.681 -26.552 14.713 1.00164.40 A C ANISOU 1919 CB ASN A 258 22396 17628 22442 -6108 1971 1788 A C ATOM 1920 CG ASN A 258 25.453 -26.031 15.431 1.00164.53 A C ANISOU 1920 CG ASN A 258 22238 17868 22406 -6339 2266 1757 A C ATOM 1921 ND2 ASN A 258 25.393 -24.716 15.626 1.00158.90 A N ANISOU 1921 ND2 ASN A 258 21390 17480 21505 -6195 2299 1678 A N ATOM 1922 OD1 ASN A 258 24.564 -26.800 15.798 1.00169.29 A O ANISOU 1922 OD1 ASN A 258 22826 18353 23144 -6646 2467 1800 A O ATOM 1923 N TYR A 259 27.976 -29.094 12.798 1.00143.55 A N ANISOU 1923 N TYR A 259 20006 14256 20281 -5970 1494 1733 A N ATOM 1924 CA TYR A 259 28.197 -29.510 11.418 1.00144.58 A C ANISOU 1924 CA TYR A 259 20012 14283 20640 -5826 1263 1506 A C ATOM 1925 C TYR A 259 27.833 -30.969 11.256 1.00152.66 A C ANISOU 1925 C TYR A 259 21146 14930 21926 -6053 1284 1523 A C ATOM 1926 O TYR A 259 28.109 -31.784 12.133 1.00157.43 A O ANISOU 1926 O TYR A 259 22057 15271 22487 -6184 1364 1788 A O ATOM 1927 CB TYR A 259 29.654 -29.309 11.000 1.00146.80 A C ANISOU 1927 CB TYR A 259 20442 14545 20791 -5468 993 1557 A C ATOM 1928 CG TYR A 259 30.147 -27.875 11.008 1.00144.57 A C ANISOU 1928 CG TYR A 259 20051 14607 20271 -5224 938 1522 A C ATOM 1929 CD1 TYR A 259 29.258 -26.798 11.030 1.00141.63 A C ANISOU 1929 CD1 TYR A 259 19409 14549 19855 -5278 1080 1377 A C ATOM 1930 CD2 TYR A 259 31.507 -27.602 10.983 1.00139.21 A C ANISOU 1930 CD2 TYR A 259 19538 13935 19420 -4937 742 1630 A C ATOM 1931 CE1 TYR A 259 29.719 -25.493 11.038 1.00134.51 A C ANISOU 1931 CE1 TYR A 259 18427 13933 18748 -5057 1030 1347 A C ATOM 1932 CE2 TYR A 259 31.974 -26.310 10.986 1.00139.70 A C ANISOU 1932 CE2 TYR A 259 19506 14291 19282 -4733 694 1598 A C ATOM 1933 CZ TYR A 259 31.085 -25.258 11.012 1.00137.96 A C ANISOU 1933 CZ TYR A 259 19038 14355 19027 -4794 838 1459 A C ATOM 1934 OH TYR A 259 31.588 -23.973 11.014 1.00132.66 A O ANISOU 1934 OH TYR A 259 18294 13948 18164 -4588 786 1431 A O ATOM 1935 N GLU A 260 27.221 -31.303 10.127 1.00162.22 A N ANISOU 1935 N GLU A 260 22115 16112 23410 -6094 1206 1239 A N ATOM 1936 CA GLU A 260 26.764 -32.668 9.902 1.00174.43 A C ANISOU 1936 CA GLU A 260 23734 17300 25240 -6334 1228 1212 A C ATOM 1937 C GLU A 260 27.930 -33.610 9.612 1.00175.50 A C ANISOU 1937 C GLU A 260 24174 17095 25413 -6155 1004 1321 A C ATOM 1938 O GLU A 260 27.944 -34.760 10.062 1.00182.45 A O ANISOU 1938 O GLU A 260 25307 17611 26405 -6338 1059 1485 A O ATOM 1939 CB GLU A 260 25.710 -32.725 8.785 1.00181.13 A C ANISOU 1939 CB GLU A 260 24213 18239 26371 -6437 1207 848 A C ATOM 1940 CG GLU A 260 26.100 -32.027 7.482 1.00183.13 A C ANISOU 1940 CG GLU A 260 24237 18716 26628 -6099 956 574 A C ATOM 1941 CD GLU A 260 25.027 -32.160 6.407 1.00181.39 A C ANISOU 1941 CD GLU A 260 23660 18582 26680 -6202 930 214 A C ATOM 1942 OE1 GLU A 260 24.083 -32.954 6.609 1.00180.48 A O ANISOU 1942 OE1 GLU A 260 23493 18298 26783 -6541 1080 170 A O ATOM 1943 OE2 GLU A 260 25.127 -31.472 5.365 1.00177.74 A O1- ANISOU 1943 OE2 GLU A 260 22967 18357 26209 -5947 762 -23 A O1- ATOM 1944 N LEU A 261 28.912 -33.115 8.868 1.00162.95 A N ANISOU 1944 N LEU A 261 22562 15625 23728 -5793 756 1236 A N ATOM 1945 CA LEU A 261 30.066 -33.928 8.515 1.00156.30 A C ANISOU 1945 CA LEU A 261 21977 14501 22908 -5581 528 1314 A C ATOM 1946 C LEU A 261 30.917 -34.170 9.761 1.00148.95 A C ANISOU 1946 C LEU A 261 21424 13422 21748 -5554 576 1687 A C ATOM 1947 O LEU A 261 31.890 -34.924 9.726 1.00147.96 A O ANISOU 1947 O LEU A 261 21565 13038 21617 -5397 414 1812 A O ATOM 1948 CB LEU A 261 30.872 -33.252 7.396 1.00152.71 A C ANISOU 1948 CB LEU A 261 21372 14256 22396 -5200 269 1124 A C ATOM 1949 CG LEU A 261 31.856 -34.096 6.580 1.00152.80 A C ANISOU 1949 CG LEU A 261 21532 14021 22505 -4963 5 1076 A C ATOM 1950 CD1 LEU A 261 33.219 -34.127 7.242 1.00155.73 A C ANISOU 1950 CD1 LEU A 261 22213 14316 22640 -4740 -95 1355 A C ATOM 1951 CD2 LEU A 261 31.328 -35.509 6.389 1.00153.66 A C ANISOU 1951 CD2 LEU A 261 21747 13730 22906 -5192 20 1026 A C ATOM 1952 N TYR A 262 30.527 -33.541 10.868 1.00143.72 A N ANISOU 1952 N TYR A 262 20783 12932 20892 -5702 797 1859 A N ATOM 1953 CA TYR A 262 31.267 -33.654 12.122 1.00152.14 A C ANISOU 1953 CA TYR A 262 22192 13910 21705 -5676 856 2209 A C ATOM 1954 C TYR A 262 31.400 -35.100 12.576 1.00158.06 A C ANISOU 1954 C TYR A 262 23276 14207 22572 -5827 884 2418 A C ATOM 1955 O TYR A 262 32.501 -35.656 12.585 1.00156.84 A O ANISOU 1955 O TYR A 262 23385 13847 22358 -5613 701 2555 A O ATOM 1956 CB TYR A 262 30.610 -32.813 13.220 1.00162.99 A C ANISOU 1956 CB TYR A 262 23513 15540 22876 -5853 1119 2330 A C ATOM 1957 CG TYR A 262 31.252 -32.963 14.586 1.00173.11 A C ANISOU 1957 CG TYR A 262 25148 16740 23885 -5852 1200 2692 A C ATOM 1958 CD1 TYR A 262 32.619 -32.787 14.758 1.00173.79 A C ANISOU 1958 CD1 TYR A 262 25439 16834 23760 -5540 997 2829 A C ATOM 1959 CD2 TYR A 262 30.489 -33.267 15.706 1.00181.06 A C ANISOU 1959 CD2 TYR A 262 26276 17681 24837 -6158 1482 2892 A C ATOM 1960 CE1 TYR A 262 33.210 -32.919 16.004 1.00177.14 A C ANISOU 1960 CE1 TYR A 262 26181 17202 23923 -5523 1057 3150 A C ATOM 1961 CE2 TYR A 262 31.071 -33.400 16.957 1.00184.17 A C ANISOU 1961 CE2 TYR A 262 27000 18015 24961 -6142 1555 3225 A C ATOM 1962 CZ TYR A 262 32.431 -33.225 17.100 1.00182.05 A C ANISOU 1962 CZ TYR A 262 26931 17757 24482 -5819 1334 3348 A C ATOM 1963 OH TYR A 262 33.013 -33.358 18.341 1.00182.90 A O ANISOU 1963 OH TYR A 262 27363 17821 24311 -5789 1393 3670 A O ATOM 1964 N GLU A 263 30.276 -35.703 12.953 1.00166.63 A N ANISOU 1964 N GLU A 263 24349 15137 23827 -6195 1116 2442 A N ATOM 1965 CA GLU A 263 30.269 -37.088 13.411 1.00173.17 A C ANISOU 1965 CA GLU A 263 25496 15510 24789 -6382 1176 2647 A C ATOM 1966 C GLU A 263 30.360 -38.061 12.242 1.00171.65 A C ANISOU 1966 C GLU A 263 25288 15015 24916 -6340 981 2439 A C ATOM 1967 O GLU A 263 30.922 -39.149 12.370 1.00174.05 A O ANISOU 1967 O GLU A 263 25909 14930 25293 -6314 898 2595 A O ATOM 1968 CB GLU A 263 29.028 -37.375 14.260 1.00181.59 A C ANISOU 1968 CB GLU A 263 26553 16520 25924 -6810 1514 2757 A C ATOM 1969 CG GLU A 263 29.321 -37.530 15.751 1.00189.13 A C ANISOU 1969 CG GLU A 263 27854 17397 26611 -6890 1691 3160 A C ATOM 1970 CD GLU A 263 30.170 -38.757 16.065 1.00196.93 A C ANISOU 1970 CD GLU A 263 29274 17933 27615 -6822 1588 3418 A C ATOM 1971 OE1 GLU A 263 30.022 -39.788 15.373 1.00200.32 A O ANISOU 1971 OE1 GLU A 263 29751 18014 28347 -6906 1508 3318 A O ATOM 1972 OE2 GLU A 263 30.982 -38.691 17.012 1.00197.44 A O1- ANISOU 1972 OE2 GLU A 263 29636 17993 27390 -6677 1582 3716 A O1- ATOM 1973 N LYS A 264 29.812 -37.661 11.100 1.00169.17 A N ANISOU 1973 N LYS A 264 24611 14883 24783 -6320 901 2083 A N ATOM 1974 CA LYS A 264 29.877 -38.486 9.900 1.00173.51 A C ANISOU 1974 CA LYS A 264 25110 15193 25625 -6258 700 1841 A C ATOM 1975 C LYS A 264 31.310 -38.601 9.378 1.00178.13 A C ANISOU 1975 C LYS A 264 25863 15710 26108 -5842 398 1860 A C ATOM 1976 O LYS A 264 31.535 -38.759 8.179 1.00179.83 A O ANISOU 1976 O LYS A 264 25938 15915 26477 -5663 186 1594 A O ATOM 1977 CB LYS A 264 28.954 -37.924 8.813 1.00167.38 A C ANISOU 1977 CB LYS A 264 23887 14681 25027 -6308 681 1449 A C ATOM 1978 CG LYS A 264 28.899 -38.766 7.539 1.00165.84 A C ANISOU 1978 CG LYS A 264 23611 14261 25140 -6262 479 1162 A C ATOM 1979 CD LYS A 264 28.725 -40.253 7.863 1.00163.64 A C ANISOU 1979 CD LYS A 264 23620 13463 25093 -6512 536 1285 A C ATOM 1980 CE LYS A 264 28.763 -41.121 6.607 1.00150.73 A C ANISOU 1980 CE LYS A 264 21931 11582 23757 -6444 315 993 A C ATOM 1981 NZ LYS A 264 28.474 -42.550 6.906 1.00142.70 A N1+ ANISOU 1981 NZ LYS A 264 21180 10044 22997 -6722 386 1090 A N1+ ATOM 1982 N LEU A 265 32.284 -38.520 10.277 1.00177.57 A N ANISOU 1982 N LEU A 265 26087 15610 25770 -5682 378 2168 A N ATOM 1983 CA LEU A 265 33.680 -38.603 9.867 1.00172.86 A C ANISOU 1983 CA LEU A 265 25644 14975 25061 -5286 100 2200 A C ATOM 1984 C LEU A 265 34.611 -39.068 10.983 1.00168.36 A C ANISOU 1984 C LEU A 265 25486 14203 24278 -5194 97 2575 A C ATOM 1985 O LEU A 265 34.411 -38.766 12.162 1.00157.77 A O ANISOU 1985 O LEU A 265 24269 12934 22743 -5340 294 2824 A O ATOM 1986 CB LEU A 265 34.155 -37.270 9.270 1.00172.09 A C ANISOU 1986 CB LEU A 265 25272 15326 24788 -4998 -30 2033 A C ATOM 1987 CG LEU A 265 35.586 -37.225 8.718 1.00173.57 A C ANISOU 1987 CG LEU A 265 25551 15536 24862 -4580 -316 2028 A C ATOM 1988 CD1 LEU A 265 35.688 -36.358 7.463 1.00165.44 A C ANISOU 1988 CD1 LEU A 265 24174 14828 23855 -4359 -469 1715 A C ATOM 1989 CD2 LEU A 265 36.564 -36.753 9.785 1.00175.46 A C ANISOU 1989 CD2 LEU A 265 26010 15885 24772 -4422 -320 2328 A C ATOM 1990 N GLU A 266 35.631 -39.814 10.581 1.00177.41 A N ANISOU 1990 N GLU A 266 26843 15105 25459 -4936 -134 2606 A N ATOM 1991 CA GLU A 266 36.604 -40.364 11.504 1.00186.60 A C ANISOU 1991 CA GLU A 266 28405 16056 26437 -4799 -181 2941 A C ATOM 1992 C GLU A 266 37.525 -39.261 11.984 1.00193.41 A C ANISOU 1992 C GLU A 266 29248 17288 26949 -4534 -252 3056 A C ATOM 1993 O GLU A 266 38.243 -38.648 11.195 1.00192.34 A O ANISOU 1993 O GLU A 266 28938 17386 26757 -4240 -454 2885 A O ATOM 1994 CB GLU A 266 37.421 -41.453 10.809 1.00187.39 A C ANISOU 1994 CB GLU A 266 28702 15806 26692 -4570 -426 2897 A C ATOM 1995 CG GLU A 266 37.843 -42.600 11.709 1.00192.51 A C ANISOU 1995 CG GLU A 266 29805 16025 27316 -4598 -403 3225 A C ATOM 1996 CD GLU A 266 38.440 -43.751 10.922 1.00195.70 A C ANISOU 1996 CD GLU A 266 30382 16044 27929 -4409 -628 3136 A C ATOM 1997 OE1 GLU A 266 39.345 -43.493 10.099 1.00191.92 A O ANISOU 1997 OE1 GLU A 266 29800 15712 27408 -4055 -878 2975 A O ATOM 1998 OE2 GLU A 266 38.003 -44.908 11.123 1.00198.29 A O1- ANISOU 1998 OE2 GLU A 266 30949 15924 28467 -4615 -552 3226 A O1- ATOM 1999 N LEU A 267 37.490 -38.999 13.283 1.00204.83 A N ANISOU 1999 N LEU A 267 30871 18795 28160 -4645 -81 3343 A N ATOM 2000 CA LEU A 267 38.433 -38.074 13.894 1.00211.06 A C ANISOU 2000 CA LEU A 267 31695 19892 28606 -4401 -154 3481 A C ATOM 2001 C LEU A 267 38.851 -38.597 15.265 1.00213.81 A C ANISOU 2001 C LEU A 267 32440 20061 28739 -4425 -73 3864 A C ATOM 2002 O LEU A 267 38.013 -39.039 16.054 1.00218.39 A O ANISOU 2002 O LEU A 267 33159 20475 29344 -4731 166 4033 A O ATOM 2003 CB LEU A 267 37.842 -36.660 13.980 1.00214.82 A C ANISOU 2003 CB LEU A 267 31850 20813 28958 -4489 -20 3354 A C ATOM 2004 CG LEU A 267 36.428 -36.496 14.545 1.00223.00 A C ANISOU 2004 CG LEU A 267 32789 21888 30053 -4883 291 3369 A C ATOM 2005 CD1 LEU A 267 36.424 -36.557 16.070 1.00230.20 A C ANISOU 2005 CD1 LEU A 267 33982 22772 30712 -5010 478 3715 A C ATOM 2006 CD2 LEU A 267 35.826 -35.186 14.067 1.00214.77 A C ANISOU 2006 CD2 LEU A 267 31351 21260 28993 -4908 350 3118 A C ATOM 2007 N VAL A 268 40.152 -38.571 15.531 1.00205.61 A N ANISOU 2007 N VAL A 268 31578 19057 27486 -4098 -274 4002 A N ATOM 2008 CA VAL A 268 40.670 -39.033 16.810 1.00201.61 A C ANISOU 2008 CA VAL A 268 31452 18408 26743 -4066 -232 4364 A C ATOM 2009 C VAL A 268 39.986 -38.255 17.927 1.00193.08 A C ANISOU 2009 C VAL A 268 30349 17569 25443 -4297 30 4508 A C ATOM 2010 O VAL A 268 39.309 -37.260 17.674 1.00194.26 A O ANISOU 2010 O VAL A 268 30182 18027 25602 -4420 138 4317 A O ATOM 2011 CB VAL A 268 42.195 -38.847 16.897 1.00202.07 A C ANISOU 2011 CB VAL A 268 31625 18580 26572 -3653 -500 4446 A C ATOM 2012 CG1 VAL A 268 42.765 -39.620 18.084 1.00205.18 A C ANISOU 2012 CG1 VAL A 268 32452 18744 26764 -3588 -495 4816 A C ATOM 2013 CG2 VAL A 268 42.851 -39.299 15.603 1.00199.67 A C ANISOU 2013 CG2 VAL A 268 31233 18157 26475 -3398 -762 4226 A C ATOM 2014 N LYS A 269 40.153 -38.705 19.163 1.00181.08 A N ANISOU 2014 N LYS A 269 29170 15916 23718 -4345 132 4843 A N ATOM 2015 CA LYS A 269 39.507 -38.038 20.280 1.00172.06 A C ANISOU 2015 CA LYS A 269 28031 14995 22350 -4559 389 4992 A C ATOM 2016 C LYS A 269 40.493 -37.730 21.408 1.00170.51 A C ANISOU 2016 C LYS A 269 28079 14947 21759 -4341 321 5258 A C ATOM 2017 O LYS A 269 40.223 -36.876 22.250 1.00171.34 A O ANISOU 2017 O LYS A 269 28139 15344 21619 -4425 470 5329 A O ATOM 2018 CB LYS A 269 38.334 -38.881 20.789 1.00174.41 A C ANISOU 2018 CB LYS A 269 28477 14997 22795 -4945 677 5143 A C ATOM 2019 CG LYS A 269 37.381 -39.357 19.686 1.00166.89 A C ANISOU 2019 CG LYS A 269 27306 13851 22253 -5168 730 4883 A C ATOM 2020 CD LYS A 269 36.494 -40.507 20.171 1.00160.18 A C ANISOU 2020 CD LYS A 269 26686 12598 21576 -5514 965 5073 A C ATOM 2021 CE LYS A 269 35.703 -41.136 19.032 1.00150.16 A C ANISOU 2021 CE LYS A 269 25232 11090 20734 -5708 970 4807 A C ATOM 2022 NZ LYS A 269 34.893 -42.291 19.506 1.00150.56 A N1+ ANISOU 2022 NZ LYS A 269 25517 10721 20967 -6054 1195 4996 A N1+ ATOM 2023 N GLY A 270 41.637 -38.413 21.413 1.00168.81 A N ANISOU 2023 N GLY A 270 28117 14543 21482 -4051 88 5389 A N ATOM 2024 CA GLY A 270 42.647 -38.203 22.440 1.00169.11 A C ANISOU 2024 CA GLY A 270 28390 14715 21149 -3816 -10 5632 A C ATOM 2025 C GLY A 270 43.840 -37.357 22.011 1.00164.42 A C ANISOU 2025 C GLY A 270 27622 14438 20413 -3461 -289 5478 A C ATOM 2026 O GLY A 270 44.964 -37.581 22.460 1.00159.41 A O ANISOU 2026 O GLY A 270 27196 13802 19571 -3178 -477 5637 A O ATOM 2027 N GLN A 271 43.596 -36.368 21.155 1.00163.64 A N ANISOU 2027 N GLN A 271 27136 14620 20420 -3475 -312 5171 A N ATOM 2028 CA GLN A 271 44.676 -35.571 20.574 1.00155.51 A C ANISOU 2028 CA GLN A 271 25908 13875 19305 -3161 -567 4999 A C ATOM 2029 C GLN A 271 44.938 -34.247 21.292 1.00159.65 A C ANISOU 2029 C GLN A 271 26311 14825 19523 -3121 -539 4997 A C ATOM 2030 O GLN A 271 44.012 -33.489 21.582 1.00161.85 A O ANISOU 2030 O GLN A 271 26435 15289 19771 -3355 -325 4933 A O ATOM 2031 CB GLN A 271 44.420 -35.332 19.085 1.00143.66 A C ANISOU 2031 CB GLN A 271 24072 12406 18106 -3149 -646 4663 A C ATOM 2032 CG GLN A 271 45.002 -36.415 18.205 1.00141.86 A C ANISOU 2032 CG GLN A 271 23941 11867 18092 -2961 -851 4617 A C ATOM 2033 CD GLN A 271 46.378 -36.838 18.686 1.00147.18 A C ANISOU 2033 CD GLN A 271 24869 12494 18559 -2632 -1075 4807 A C ATOM 2034 NE2 GLN A 271 47.333 -35.912 18.650 1.00144.10 A N ANISOU 2034 NE2 GLN A 271 24327 12448 17976 -2392 -1238 4735 A N ATOM 2035 OE1 GLN A 271 46.574 -37.975 19.110 1.00151.78 A O ANISOU 2035 OE1 GLN A 271 25781 12736 19152 -2596 -1097 5021 A O ATOM 2036 N LYS A 272 46.212 -33.975 21.568 1.00159.24 A N ANISOU 2036 N LYS A 272 26325 14928 19249 -2820 -761 5056 A N ATOM 2037 CA LYS A 272 46.608 -32.754 22.266 1.00154.13 A C ANISOU 2037 CA LYS A 272 25581 14674 18307 -2757 -768 5049 A C ATOM 2038 C LYS A 272 47.486 -31.873 21.386 1.00148.41 A C ANISOU 2038 C LYS A 272 24566 14219 17604 -2525 -989 4806 A C ATOM 2039 O LYS A 272 48.295 -32.378 20.607 1.00148.72 A O ANISOU 2039 O LYS A 272 24595 14152 17761 -2297 -1206 4746 A O ATOM 2040 CB LYS A 272 47.325 -33.095 23.573 1.00155.63 A C ANISOU 2040 CB LYS A 272 26106 14858 18167 -2627 -818 5347 A C ATOM 2041 CG LYS A 272 46.425 -33.786 24.579 1.00160.12 A C ANISOU 2041 CG LYS A 272 26960 15215 18663 -2873 -566 5607 A C ATOM 2042 CD LYS A 272 47.176 -34.222 25.826 1.00159.84 A C ANISOU 2042 CD LYS A 272 27283 15155 18294 -2713 -630 5917 A C ATOM 2043 CE LYS A 272 46.212 -34.789 26.864 1.00157.16 A C ANISOU 2043 CE LYS A 272 27216 14640 17859 -2978 -345 6183 A C ATOM 2044 NZ LYS A 272 45.314 -35.838 26.291 1.00152.19 A N1+ ANISOU 2044 NZ LYS A 272 26655 13608 17563 -3199 -200 6206 A N1+ ATOM 2045 N ARG A 273 47.319 -30.559 21.521 1.00147.21 A N ANISOU 2045 N ARG A 273 24185 14411 17338 -2583 -927 4670 A N ATOM 2046 CA ARG A 273 47.983 -29.583 20.655 1.00153.73 A C ANISOU 2046 CA ARG A 273 24707 15501 18203 -2414 -1091 4429 A C ATOM 2047 C ARG A 273 49.502 -29.642 20.755 1.00143.80 A C ANISOU 2047 C ARG A 273 23517 14333 16786 -2090 -1367 4484 A C ATOM 2048 O ARG A 273 50.083 -29.171 21.730 1.00140.56 A O ANISOU 2048 O ARG A 273 23200 14113 16093 -2014 -1412 4592 A O ATOM 2049 CB ARG A 273 47.498 -28.162 20.975 1.00169.01 A C ANISOU 2049 CB ARG A 273 26431 17766 20018 -2550 -955 4305 A C ATOM 2050 CG ARG A 273 45.979 -27.988 20.909 1.00180.40 A C ANISOU 2050 CG ARG A 273 27774 19169 21601 -2861 -677 4234 A C ATOM 2051 CD ARG A 273 45.520 -26.687 21.568 1.00183.73 A C ANISOU 2051 CD ARG A 273 28069 19900 21840 -2983 -528 4170 A C ATOM 2052 NE ARG A 273 44.081 -26.680 21.839 1.00183.20 A N ANISOU 2052 NE ARG A 273 27974 19788 21846 -3279 -244 4167 A N ATOM 2053 CZ ARG A 273 43.486 -25.880 22.722 1.00180.88 A C ANISOU 2053 CZ ARG A 273 27665 19695 21367 -3424 -60 4183 A C ATOM 2054 NH1 ARG A 273 44.203 -25.017 23.430 1.00179.50 A N1+ ANISOU 2054 NH1 ARG A 273 27512 19770 20921 -3304 -137 4200 A N1+ ATOM 2055 NH2 ARG A 273 42.173 -25.947 22.902 1.00178.54 A N ANISOU 2055 NH2 ARG A 273 27327 19356 21155 -3688 200 4174 A N ATOM 2056 N LYS A 274 50.138 -30.210 19.734 1.00138.95 A N ANISOU 2056 N LYS A 274 22846 13596 16353 -1894 -1555 4395 A N ATOM 2057 CA LYS A 274 51.593 -30.326 19.702 1.00141.98 A C ANISOU 2057 CA LYS A 274 23264 14068 16616 -1571 -1825 4427 A C ATOM 2058 C LYS A 274 52.197 -29.333 18.708 1.00137.59 A C ANISOU 2058 C LYS A 274 22363 13787 16129 -1440 -1954 4176 A C ATOM 2059 O LYS A 274 53.275 -29.573 18.151 1.00130.77 A O ANISOU 2059 O LYS A 274 21448 12953 15287 -1177 -2176 4130 A O ATOM 2060 CB LYS A 274 52.019 -31.756 19.336 1.00147.08 A C ANISOU 2060 CB LYS A 274 24121 14375 17389 -1404 -1960 4528 A C ATOM 2061 CG LYS A 274 51.247 -32.864 20.058 1.00149.29 A C ANISOU 2061 CG LYS A 274 24735 14306 17683 -1569 -1806 4760 A C ATOM 2062 CD LYS A 274 52.139 -34.066 20.391 1.00150.13 A C ANISOU 2062 CD LYS A 274 25154 14166 17723 -1321 -1986 4966 A C ATOM 2063 CE LYS A 274 53.029 -33.807 21.621 1.00142.52 A C ANISOU 2063 CE LYS A 274 24363 13394 16396 -1157 -2085 5162 A C ATOM 2064 NZ LYS A 274 53.908 -34.964 21.975 1.00128.39 A N1+ ANISOU 2064 NZ LYS A 274 22884 11375 14524 -890 -2268 5369 A N1+ ATOM 2065 N VAL A 275 51.502 -28.218 18.493 1.00137.79 A N ANISOU 2065 N VAL A 275 22153 14014 16187 -1619 -1809 4018 A N ATOM 2066 CA VAL A 275 51.919 -27.241 17.491 1.00132.14 A C ANISOU 2066 CA VAL A 275 21111 13539 15559 -1526 -1896 3783 A C ATOM 2067 C VAL A 275 53.321 -26.721 17.790 1.00133.89 A C ANISOU 2067 C VAL A 275 21289 14002 15581 -1292 -2104 3795 A C ATOM 2068 O VAL A 275 54.195 -26.736 16.920 1.00130.99 A O ANISOU 2068 O VAL A 275 20775 13698 15296 -1083 -2282 3690 A O ATOM 2069 CB VAL A 275 50.942 -26.052 17.394 1.00125.40 A C ANISOU 2069 CB VAL A 275 20044 12867 14734 -1753 -1699 3636 A C ATOM 2070 CG1 VAL A 275 51.052 -25.410 16.033 1.00113.08 A C ANISOU 2070 CG1 VAL A 275 18171 11433 13361 -1681 -1756 3396 A C ATOM 2071 CG2 VAL A 275 49.505 -26.499 17.654 1.00130.16 A C ANISOU 2071 CG2 VAL A 275 20742 13276 15439 -2024 -1459 3683 A C ATOM 2072 N LYS A 276 53.532 -26.269 19.024 1.00134.30 A N ANISOU 2072 N LYS A 276 21461 14197 15368 -1328 -2082 3917 A N ATOM 2073 CA LYS A 276 54.834 -25.757 19.437 1.00130.48 A C ANISOU 2073 CA LYS A 276 20939 13958 14681 -1126 -2279 3925 A C ATOM 2074 C LYS A 276 55.852 -26.877 19.646 1.00136.37 A C ANISOU 2074 C LYS A 276 21885 14574 15355 -867 -2489 4077 A C ATOM 2075 O LYS A 276 57.037 -26.695 19.376 1.00140.26 A O ANISOU 2075 O LYS A 276 22267 15229 15798 -639 -2698 4022 A O ATOM 2076 CB LYS A 276 54.716 -24.909 20.706 1.00121.97 A C ANISOU 2076 CB LYS A 276 19927 13084 13332 -1243 -2196 3989 A C ATOM 2077 CG LYS A 276 54.146 -23.521 20.496 1.00108.65 A C ANISOU 2077 CG LYS A 276 17994 11612 11674 -1418 -2059 3803 A C ATOM 2078 CD LYS A 276 54.410 -22.622 21.702 1.00117.35 A C ANISOU 2078 CD LYS A 276 19141 12957 12489 -1461 -2049 3835 A C ATOM 2079 CE LYS A 276 54.092 -21.149 21.383 1.00126.13 A C ANISOU 2079 CE LYS A 276 19988 14295 13640 -1587 -1958 3624 A C ATOM 2080 NZ LYS A 276 54.907 -20.138 22.155 1.00119.84 A N1+ ANISOU 2080 NZ LYS A 276 19143 13779 12610 -1539 -2058 3579 A N1+ ATOM 2081 N ASP A 277 55.392 -28.031 20.121 1.00138.79 A N ANISOU 2081 N ASP A 277 22485 14587 15661 -901 -2431 4268 A N ATOM 2082 CA ASP A 277 56.281 -29.176 20.352 1.00149.21 A C ANISOU 2082 CA ASP A 277 24033 15744 16918 -647 -2622 4429 A C ATOM 2083 C ASP A 277 56.986 -29.663 19.080 1.00143.26 A C ANISOU 2083 C ASP A 277 23136 14922 16373 -420 -2803 4299 A C ATOM 2084 O ASP A 277 58.214 -29.754 19.038 1.00138.63 A O ANISOU 2084 O ASP A 277 22517 14461 15693 -149 -3027 4300 A O ATOM 2085 CB ASP A 277 55.524 -30.352 20.989 1.00156.42 A C ANISOU 2085 CB ASP A 277 25296 16307 17831 -752 -2497 4658 A C ATOM 2086 CG ASP A 277 55.013 -30.042 22.385 1.00158.30 A C ANISOU 2086 CG ASP A 277 25725 16614 17809 -922 -2342 4832 A C ATOM 2087 OD1 ASP A 277 54.893 -28.845 22.727 1.00164.24 A O ANISOU 2087 OD1 ASP A 277 26309 17659 18438 -1029 -2275 4733 A O ATOM 2088 OD2 ASP A 277 54.725 -31.001 23.136 1.00153.83 A O1- ANISOU 2088 OD2 ASP A 277 25483 15804 17160 -947 -2281 5069 A O1- ATOM 2089 N ARG A 278 56.205 -29.981 18.051 1.00138.76 A N ANISOU 2089 N ARG A 278 22476 14167 16081 -525 -2707 4180 A N ATOM 2090 CA ARG A 278 56.747 -30.613 16.852 1.00135.92 A C ANISOU 2090 CA ARG A 278 22020 13700 15925 -313 -2862 4065 A C ATOM 2091 C ARG A 278 57.679 -29.701 16.062 1.00125.95 A C ANISOU 2091 C ARG A 278 20429 12759 14669 -148 -3004 3869 A C ATOM 2092 O ARG A 278 58.535 -30.182 15.324 1.00121.58 A O ANISOU 2092 O ARG A 278 19812 12194 14191 106 -3185 3807 A O ATOM 2093 CB ARG A 278 55.622 -31.152 15.954 1.00142.93 A C ANISOU 2093 CB ARG A 278 22886 14320 17102 -479 -2722 3968 A C ATOM 2094 CG ARG A 278 55.574 -32.691 15.864 1.00152.61 A C ANISOU 2094 CG ARG A 278 24392 15147 18447 -386 -2778 4089 A C ATOM 2095 CD ARG A 278 54.368 -33.222 15.063 1.00159.67 A C ANISOU 2095 CD ARG A 278 25268 15768 19631 -589 -2629 3985 A C ATOM 2096 NE ARG A 278 54.418 -32.864 13.641 1.00164.91 A N ANISOU 2096 NE ARG A 278 25625 16538 20496 -516 -2686 3718 A N ATOM 2097 CZ ARG A 278 53.510 -33.221 12.731 1.00157.07 A C ANISOU 2097 CZ ARG A 278 24553 15367 19760 -645 -2598 3571 A C ATOM 2098 NH1 ARG A 278 52.461 -33.959 13.080 1.00155.31 A N1+ ANISOU 2098 NH1 ARG A 278 24525 14839 19647 -874 -2442 3659 A N1+ ATOM 2099 NH2 ARG A 278 53.653 -32.839 11.465 1.00143.11 A N ANISOU 2099 NH2 ARG A 278 22506 13733 18137 -547 -2664 3333 A N ATOM 2100 N LEU A 279 57.530 -28.392 16.238 1.00126.79 A N ANISOU 2100 N LEU A 279 20333 13149 14691 -288 -2919 3775 A N ATOM 2101 CA LEU A 279 58.265 -27.419 15.423 1.00129.14 A C ANISOU 2101 CA LEU A 279 20303 13742 15021 -182 -3014 3583 A C ATOM 2102 C LEU A 279 59.489 -26.753 16.064 1.00132.50 A C ANISOU 2102 C LEU A 279 20657 14467 15218 -34 -3171 3606 A C ATOM 2103 O LEU A 279 60.188 -25.977 15.400 1.00116.70 A O ANISOU 2103 O LEU A 279 18385 12710 13247 55 -3254 3456 A O ATOM 2104 CB LEU A 279 57.316 -26.342 14.905 1.00123.01 A C ANISOU 2104 CB LEU A 279 19303 13079 14356 -420 -2824 3422 A C ATOM 2105 CG LEU A 279 56.553 -26.770 13.655 1.00117.03 A C ANISOU 2105 CG LEU A 279 18448 12143 13873 -463 -2752 3290 A C ATOM 2106 CD1 LEU A 279 55.535 -25.718 13.232 1.00 99.88 A C ANISOU 2106 CD1 LEU A 279 16074 10082 11794 -694 -2560 3145 A C ATOM 2107 CD2 LEU A 279 57.543 -27.053 12.535 1.00120.35 A C ANISOU 2107 CD2 LEU A 279 18710 12620 14396 -191 -2941 3177 A C ATOM 2108 N LYS A 280 59.744 -27.050 17.338 1.00142.18 A N ANISOU 2108 N LYS A 280 22124 15682 16217 -10 -3212 3791 A N ATOM 2109 CA LYS A 280 60.898 -26.491 18.040 1.00140.00 A C ANISOU 2109 CA LYS A 280 21796 15690 15709 133 -3376 3812 A C ATOM 2110 C LYS A 280 62.187 -26.816 17.296 1.00139.76 A C ANISOU 2110 C LYS A 280 21618 15758 15725 439 -3611 3740 A C ATOM 2111 O LYS A 280 63.107 -26.001 17.248 1.00141.17 A O ANISOU 2111 O LYS A 280 21577 16237 15823 525 -3725 3642 A O ATOM 2112 CB LYS A 280 60.982 -27.022 19.476 1.00143.96 A C ANISOU 2112 CB LYS A 280 22618 16126 15955 158 -3404 4039 A C ATOM 2113 CG LYS A 280 59.884 -26.529 20.417 1.00137.52 A C ANISOU 2113 CG LYS A 280 21931 15295 15025 -130 -3180 4113 A C ATOM 2114 CD LYS A 280 60.035 -27.110 21.834 1.00128.12 A C ANISOU 2114 CD LYS A 280 21072 14051 13558 -78 -3214 4354 A C ATOM 2115 CE LYS A 280 59.960 -28.639 21.849 1.00115.34 A C ANISOU 2115 CE LYS A 280 19749 12081 11995 50 -3254 4543 A C ATOM 2116 NZ LYS A 280 59.836 -29.180 23.230 1.00107.84 A N1+ ANISOU 2116 NZ LYS A 280 19148 11045 10783 50 -3228 4799 A N1+ ATOM 2117 N ALA A 281 62.243 -28.014 16.721 1.00139.56 A N ANISOU 2117 N ALA A 281 21713 15480 15835 600 -3680 3783 A N ATOM 2118 CA ALA A 281 63.393 -28.452 15.932 1.00136.33 A C ANISOU 2118 CA ALA A 281 21174 15139 15487 908 -3894 3710 A C ATOM 2119 C ALA A 281 63.885 -27.390 14.939 1.00133.32 A C ANISOU 2119 C ALA A 281 20404 15052 15199 920 -3915 3490 A C ATOM 2120 O ALA A 281 65.019 -26.913 15.038 1.00129.82 A O ANISOU 2120 O ALA A 281 19795 14887 14645 1074 -4070 3444 A O ATOM 2121 CB ALA A 281 63.061 -29.751 15.193 1.00130.09 A C ANISOU 2121 CB ALA A 281 20531 14004 14893 1018 -3910 3732 A C ATOM 2122 N TYR A 282 63.027 -27.022 13.990 1.00121.93 A N ANISOU 2122 N TYR A 282 18817 13551 13960 756 -3758 3358 A N ATOM 2123 CA TYR A 282 63.432 -26.157 12.893 1.00111.55 A C ANISOU 2123 CA TYR A 282 17157 12471 12755 786 -3767 3163 A C ATOM 2124 C TYR A 282 63.286 -24.691 13.251 1.00115.68 A C ANISOU 2124 C TYR A 282 17506 13251 13197 574 -3662 3096 A C ATOM 2125 O TYR A 282 64.082 -23.850 12.824 1.00112.20 A O ANISOU 2125 O TYR A 282 16802 13081 12748 631 -3725 2984 A O ATOM 2126 CB TYR A 282 62.592 -26.438 11.659 1.00110.86 A C ANISOU 2126 CB TYR A 282 16996 12212 12915 731 -3657 3047 A C ATOM 2127 CG TYR A 282 62.099 -27.854 11.543 1.00121.65 A C ANISOU 2127 CG TYR A 282 18617 13219 14385 799 -3670 3126 A C ATOM 2128 CD1 TYR A 282 61.088 -28.323 12.369 1.00124.86 A C ANISOU 2128 CD1 TYR A 282 19296 13375 14771 606 -3541 3263 A C ATOM 2129 CD2 TYR A 282 62.623 -28.717 10.587 1.00126.34 A C ANISOU 2129 CD2 TYR A 282 19177 13721 15105 1050 -3801 3058 A C ATOM 2130 CE1 TYR A 282 60.624 -29.614 12.259 1.00130.53 A C ANISOU 2130 CE1 TYR A 282 20251 13743 15600 647 -3544 3336 A C ATOM 2131 CE2 TYR A 282 62.161 -30.011 10.467 1.00129.14 A C ANISOU 2131 CE2 TYR A 282 19774 13724 15570 1105 -3814 3119 A C ATOM 2132 CZ TYR A 282 61.160 -30.453 11.306 1.00133.08 A C ANISOU 2132 CZ TYR A 282 20546 13962 16057 895 -3684 3260 A C ATOM 2133 OH TYR A 282 60.689 -31.740 11.195 1.00137.68 A O ANISOU 2133 OH TYR A 282 21375 14175 16764 929 -3689 3324 A O ATOM 2134 N VAL A 283 62.249 -24.385 14.017 1.00124.12 A N ANISOU 2134 N VAL A 283 18721 14228 14213 324 -3493 3161 A N ATOM 2135 CA VAL A 283 61.990 -23.008 14.413 1.00123.48 A C ANISOU 2135 CA VAL A 283 18502 14358 14055 115 -3381 3093 A C ATOM 2136 C VAL A 283 62.561 -22.776 15.805 1.00118.45 A C ANISOU 2136 C VAL A 283 17993 13856 13157 123 -3465 3203 A C ATOM 2137 O VAL A 283 62.209 -23.465 16.766 1.00103.74 A O ANISOU 2137 O VAL A 283 16409 11838 11170 102 -3451 3363 A O ATOM 2138 CB VAL A 283 60.476 -22.675 14.376 1.00110.55 A C ANISOU 2138 CB VAL A 283 16914 12576 12512 -161 -3136 3070 A C ATOM 2139 CG1 VAL A 283 60.237 -21.220 14.724 1.00105.34 A C ANISOU 2139 CG1 VAL A 283 16110 12134 11783 -355 -3026 2986 A C ATOM 2140 CG2 VAL A 283 59.897 -22.994 13.008 1.00105.94 A C ANISOU 2140 CG2 VAL A 283 16214 11859 12179 -153 -3070 2958 A C ATOM 2141 N ARG A 284 63.458 -21.810 15.911 1.00129.67 A N ANISOU 2141 N ARG A 284 19207 15569 14491 154 -3554 3115 A N ATOM 2142 CA ARG A 284 64.096 -21.551 17.185 1.00145.00 A C ANISOU 2142 CA ARG A 284 21241 17672 16181 178 -3659 3190 A C ATOM 2143 C ARG A 284 63.400 -20.416 17.929 1.00147.01 A C ANISOU 2143 C ARG A 284 21496 18022 16339 -87 -3502 3153 A C ATOM 2144 O ARG A 284 62.937 -20.601 19.061 1.00143.66 A O ANISOU 2144 O ARG A 284 21307 17537 15741 -170 -3453 3273 A O ATOM 2145 CB ARG A 284 65.584 -21.290 16.974 1.00151.99 A C ANISOU 2145 CB ARG A 284 21912 18823 17016 385 -3877 3116 A C ATOM 2146 CG ARG A 284 66.294 -22.531 16.475 1.00160.73 A C ANISOU 2146 CG ARG A 284 23067 19833 18172 678 -4047 3174 A C ATOM 2147 CD ARG A 284 67.553 -22.226 15.698 1.00170.92 A C ANISOU 2147 CD ARG A 284 24056 21371 19515 864 -4206 3049 A C ATOM 2148 NE ARG A 284 68.195 -23.466 15.265 1.00182.93 A N ANISOU 2148 NE ARG A 284 25639 22792 21074 1163 -4368 3103 A N ATOM 2149 CZ ARG A 284 68.028 -24.022 14.069 1.00184.80 A C ANISOU 2149 CZ ARG A 284 25809 22894 21512 1260 -4344 3046 A C ATOM 2150 NH1 ARG A 284 67.247 -23.438 13.167 1.00184.17 A N1+ ANISOU 2150 NH1 ARG A 284 25591 22776 21610 1084 -4167 2937 A N1+ ATOM 2151 NH2 ARG A 284 68.652 -25.157 13.771 1.00182.15 A N ANISOU 2151 NH2 ARG A 284 25547 22467 21195 1546 -4503 3091 A N ATOM 2152 N ASP A 285 63.302 -19.259 17.277 1.00142.14 A N ANISOU 2152 N ASP A 285 20625 17547 15833 -214 -3418 2991 A N ATOM 2153 CA ASP A 285 62.656 -18.089 17.870 1.00138.33 A C ANISOU 2153 CA ASP A 285 20122 17156 15281 -455 -3269 2929 A C ATOM 2154 C ASP A 285 61.312 -18.446 18.511 1.00134.87 A C ANISOU 2154 C ASP A 285 19933 16509 14802 -623 -3082 3031 A C ATOM 2155 O ASP A 285 60.423 -18.982 17.848 1.00133.66 A O ANISOU 2155 O ASP A 285 19822 16147 14816 -672 -2959 3046 A O ATOM 2156 CB ASP A 285 62.474 -16.989 16.817 1.00138.45 A C ANISOU 2156 CB ASP A 285 19861 17263 15481 -563 -3166 2756 A C ATOM 2157 CG ASP A 285 62.044 -15.661 17.423 1.00141.92 A C ANISOU 2157 CG ASP A 285 20254 17824 15844 -782 -3046 2671 A C ATOM 2158 OD1 ASP A 285 60.944 -15.600 18.008 1.00142.16 A O ANISOU 2158 OD1 ASP A 285 20446 17742 15826 -941 -2886 2713 A O ATOM 2159 OD2 ASP A 285 62.803 -14.672 17.306 1.00143.82 A O1- ANISOU 2159 OD2 ASP A 285 20294 18272 16077 -798 -3108 2557 A O1- ATOM 2160 N PRO A 286 61.166 -18.148 19.810 1.00128.84 A N ANISOU 2160 N PRO A 286 19327 15814 13812 -712 -3060 3096 A N ATOM 2161 CA PRO A 286 59.948 -18.435 20.580 1.00131.99 A C ANISOU 2161 CA PRO A 286 19965 16052 14134 -876 -2877 3203 A C ATOM 2162 C PRO A 286 58.777 -17.535 20.191 1.00135.03 A C ANISOU 2162 C PRO A 286 20244 16414 14648 -1109 -2645 3086 A C ATOM 2163 O PRO A 286 57.632 -17.987 20.231 1.00143.33 A O ANISOU 2163 O PRO A 286 21425 17278 15758 -1230 -2473 3149 A O ATOM 2164 CB PRO A 286 60.372 -18.156 22.022 1.00131.09 A C ANISOU 2164 CB PRO A 286 19997 16095 13718 -875 -2948 3272 A C ATOM 2165 CG PRO A 286 61.489 -17.187 21.899 1.00128.04 A C ANISOU 2165 CG PRO A 286 19374 15978 13299 -813 -3102 3123 A C ATOM 2166 CD PRO A 286 62.213 -17.524 20.634 1.00122.15 A C ANISOU 2166 CD PRO A 286 18430 15222 12758 -653 -3218 3064 A C ATOM 2167 N TYR A 287 59.062 -16.283 19.838 1.00131.00 A N ANISOU 2167 N TYR A 287 19504 16089 14181 -1169 -2640 2919 A N ATOM 2168 CA TYR A 287 58.044 -15.376 19.316 1.00122.75 A C ANISOU 2168 CA TYR A 287 18336 15028 13276 -1354 -2438 2794 A C ATOM 2169 C TYR A 287 57.480 -15.934 18.011 1.00113.77 A C ANISOU 2169 C TYR A 287 17115 13718 12395 -1331 -2369 2769 A C ATOM 2170 O TYR A 287 56.271 -15.916 17.791 1.00114.81 A O ANISOU 2170 O TYR A 287 17272 13727 12625 -1470 -2183 2752 A O ATOM 2171 CB TYR A 287 58.632 -13.986 19.054 1.00124.69 A C ANISOU 2171 CB TYR A 287 18350 15486 13540 -1392 -2472 2627 A C ATOM 2172 CG TYR A 287 58.996 -13.180 20.286 1.00128.14 A C ANISOU 2172 CG TYR A 287 18841 16099 13746 -1461 -2510 2598 A C ATOM 2173 CD1 TYR A 287 58.024 -12.790 21.199 1.00128.82 A C ANISOU 2173 CD1 TYR A 287 19071 16168 13707 -1623 -2350 2608 A C ATOM 2174 CD2 TYR A 287 60.310 -12.774 20.513 1.00128.75 A C ANISOU 2174 CD2 TYR A 287 18811 16375 13734 -1364 -2706 2546 A C ATOM 2175 CE1 TYR A 287 58.353 -12.034 22.318 1.00133.62 A C ANISOU 2175 CE1 TYR A 287 19730 16945 14096 -1678 -2389 2564 A C ATOM 2176 CE2 TYR A 287 60.652 -12.017 21.628 1.00129.93 A C ANISOU 2176 CE2 TYR A 287 19001 16693 13674 -1428 -2752 2497 A C ATOM 2177 CZ TYR A 287 59.669 -11.649 22.529 1.00133.00 A C ANISOU 2177 CZ TYR A 287 19547 17053 13932 -1581 -2596 2505 A C ATOM 2178 OH TYR A 287 59.995 -10.900 23.644 1.00128.39 A O ANISOU 2178 OH TYR A 287 19010 16641 13130 -1637 -2645 2443 A O ATOM 2179 N ALA A 288 58.368 -16.420 17.146 1.00105.64 A N ANISOU 2179 N ALA A 288 15974 12694 11469 -1147 -2523 2757 A N ATOM 2180 CA ALA A 288 57.963 -17.024 15.881 1.00100.94 A C ANISOU 2180 CA ALA A 288 15300 11949 11105 -1092 -2487 2724 A C ATOM 2181 C ALA A 288 57.020 -18.189 16.122 1.00111.97 A C ANISOU 2181 C ALA A 288 16920 13092 12531 -1136 -2399 2843 A C ATOM 2182 O ALA A 288 56.031 -18.351 15.410 1.00123.34 A O ANISOU 2182 O ALA A 288 18322 14398 14142 -1222 -2264 2793 A O ATOM 2183 CB ALA A 288 59.175 -17.484 15.091 1.00 92.74 A C ANISOU 2183 CB ALA A 288 14138 10967 10130 -861 -2683 2707 A C ATOM 2184 N LEU A 289 57.333 -19.003 17.125 1.00109.51 A N ANISOU 2184 N LEU A 289 16841 12715 12054 -1079 -2476 3002 A N ATOM 2185 CA LEU A 289 56.475 -20.124 17.485 1.00103.59 A C ANISOU 2185 CA LEU A 289 16330 11711 11318 -1137 -2385 3140 A C ATOM 2186 C LEU A 289 55.121 -19.627 17.949 1.00109.31 A C ANISOU 2186 C LEU A 289 17103 12396 12034 -1389 -2145 3128 A C ATOM 2187 O LEU A 289 54.090 -20.035 17.424 1.00115.22 A O ANISOU 2187 O LEU A 289 17857 12974 12948 -1493 -2006 3109 A O ATOM 2188 CB LEU A 289 57.126 -20.981 18.562 1.00102.29 A C ANISOU 2188 CB LEU A 289 16418 11502 10946 -1019 -2513 3328 A C ATOM 2189 CG LEU A 289 57.986 -22.104 17.983 1.00113.34 A C ANISOU 2189 CG LEU A 289 17857 12787 12421 -773 -2704 3384 A C ATOM 2190 CD1 LEU A 289 58.810 -22.791 19.056 1.00123.99 A C ANISOU 2190 CD1 LEU A 289 19433 14138 13540 -618 -2859 3560 A C ATOM 2191 CD2 LEU A 289 57.113 -23.110 17.263 1.00113.09 A C ANISOU 2191 CD2 LEU A 289 17906 12462 12602 -810 -2611 3408 A C ATOM 2192 N ASP A 290 55.127 -18.728 18.924 1.00112.99 A N ANISOU 2192 N ASP A 290 17593 13032 12308 -1484 -2099 3123 A N ATOM 2193 CA ASP A 290 53.889 -18.158 19.434 1.00119.67 A C ANISOU 2193 CA ASP A 290 18474 13874 13123 -1711 -1871 3100 A C ATOM 2194 C ASP A 290 53.002 -17.626 18.308 1.00124.03 A C ANISOU 2194 C ASP A 290 18817 14397 13913 -1811 -1732 2939 A C ATOM 2195 O ASP A 290 51.775 -17.699 18.397 1.00131.87 A O ANISOU 2195 O ASP A 290 19848 15292 14964 -1976 -1539 2938 A O ATOM 2196 CB ASP A 290 54.182 -17.047 20.443 1.00123.53 A C ANISOU 2196 CB ASP A 290 18962 14588 13387 -1769 -1868 3063 A C ATOM 2197 CG ASP A 290 52.957 -16.648 21.243 1.00129.94 A C ANISOU 2197 CG ASP A 290 19869 15393 14109 -1980 -1639 3075 A C ATOM 2198 OD1 ASP A 290 52.397 -17.508 21.964 1.00130.71 A O ANISOU 2198 OD1 ASP A 290 20189 15357 14117 -2040 -1553 3234 A O ATOM 2199 OD2 ASP A 290 52.562 -15.467 21.157 1.00130.43 A O1- ANISOU 2199 OD2 ASP A 290 19786 15584 14189 -2082 -1542 2927 A O1- ATOM 2200 N LEU A 291 53.611 -17.093 17.250 1.00115.63 A N ANISOU 2200 N LEU A 291 17527 13427 12980 -1707 -1827 2806 A N ATOM 2201 CA LEU A 291 52.823 -16.560 16.140 1.00105.05 A C ANISOU 2201 CA LEU A 291 15989 12075 11851 -1775 -1708 2656 A C ATOM 2202 C LEU A 291 52.175 -17.663 15.312 1.00106.25 A C ANISOU 2202 C LEU A 291 16162 12011 12199 -1762 -1672 2671 A C ATOM 2203 O LEU A 291 50.976 -17.615 15.040 1.00105.43 A O ANISOU 2203 O LEU A 291 16024 11828 12205 -1902 -1503 2616 A O ATOM 2204 CB LEU A 291 53.649 -15.641 15.237 1.00 92.10 A C ANISOU 2204 CB LEU A 291 14108 10600 10285 -1671 -1805 2521 A C ATOM 2205 CG LEU A 291 52.853 -15.158 14.010 1.00 86.53 A C ANISOU 2205 CG LEU A 291 13209 9877 9792 -1711 -1691 2378 A C ATOM 2206 CD1 LEU A 291 51.474 -14.635 14.401 1.00 87.44 A C ANISOU 2206 CD1 LEU A 291 13346 9968 9909 -1909 -1474 2334 A C ATOM 2207 CD2 LEU A 291 53.607 -14.114 13.194 1.00 74.41 A C ANISOU 2207 CD2 LEU A 291 11449 8510 8312 -1629 -1757 2259 A C ATOM 2208 N ILE A 292 52.976 -18.646 14.908 1.00105.73 A N ANISOU 2208 N ILE A 292 16143 11853 12177 -1588 -1837 2732 A N ATOM 2209 CA ILE A 292 52.479 -19.791 14.154 1.00104.37 A C ANISOU 2209 CA ILE A 292 16012 11457 12189 -1559 -1829 2743 A C ATOM 2210 C ILE A 292 51.302 -20.445 14.869 1.00109.76 A C ANISOU 2210 C ILE A 292 16885 11953 12865 -1747 -1661 2841 A C ATOM 2211 O ILE A 292 50.318 -20.860 14.247 1.00112.53 A O ANISOU 2211 O ILE A 292 17198 12163 13396 -1839 -1553 2782 A O ATOM 2212 CB ILE A 292 53.574 -20.849 13.962 1.00 93.07 A C ANISOU 2212 CB ILE A 292 14669 9938 10753 -1338 -2037 2828 A C ATOM 2213 CG1 ILE A 292 54.715 -20.274 13.126 1.00 88.08 A C ANISOU 2213 CG1 ILE A 292 13820 9496 10149 -1151 -2192 2722 A C ATOM 2214 CG2 ILE A 292 52.995 -22.103 13.322 1.00 87.50 A C ANISOU 2214 CG2 ILE A 292 14047 8967 10233 -1324 -2023 2843 A C ATOM 2215 CD1 ILE A 292 55.470 -21.308 12.325 1.00 88.59 A C ANISOU 2215 CD1 ILE A 292 13885 9462 10315 -927 -2361 2729 A C ATOM 2216 N ASP A 293 51.414 -20.520 16.187 1.00102.62 A N ANISOU 2216 N ASP A 293 16180 11062 11749 -1805 -1639 2988 A N ATOM 2217 CA ASP A 293 50.406 -21.162 17.003 1.00109.63 A C ANISOU 2217 CA ASP A 293 17271 11785 12598 -1982 -1475 3112 A C ATOM 2218 C ASP A 293 49.081 -20.407 16.965 1.00114.37 A C ANISOU 2218 C ASP A 293 17757 12437 13263 -2201 -1245 3005 A C ATOM 2219 O ASP A 293 48.029 -20.998 17.189 1.00125.04 A O ANISOU 2219 O ASP A 293 19200 13632 14679 -2363 -1087 3056 A O ATOM 2220 CB ASP A 293 50.910 -21.296 18.440 1.00121.17 A C ANISOU 2220 CB ASP A 293 18966 13290 13782 -1972 -1509 3294 A C ATOM 2221 CG ASP A 293 49.967 -22.083 19.319 1.00129.36 A C ANISOU 2221 CG ASP A 293 20242 14146 14763 -2140 -1341 3458 A C ATOM 2222 OD1 ASP A 293 49.993 -23.332 19.250 1.00139.44 A O ANISOU 2222 OD1 ASP A 293 21689 15182 16109 -2098 -1381 3583 A O ATOM 2223 OD2 ASP A 293 49.206 -21.451 20.085 1.00126.35 A O1- ANISOU 2223 OD2 ASP A 293 19882 13859 14266 -2315 -1164 3462 A O1- ATOM 2224 N LYS A 294 49.121 -19.107 16.685 1.00110.40 A N ANISOU 2224 N LYS A 294 17052 12146 12747 -2208 -1223 2856 A N ATOM 2225 CA LYS A 294 47.885 -18.328 16.608 1.00105.64 A C ANISOU 2225 CA LYS A 294 16330 11604 12205 -2388 -1014 2741 A C ATOM 2226 C LYS A 294 47.329 -18.312 15.199 1.00104.04 A C ANISOU 2226 C LYS A 294 15915 11354 12259 -2374 -990 2580 A C ATOM 2227 O LYS A 294 46.186 -17.913 14.983 1.00107.70 A O ANISOU 2227 O LYS A 294 16277 11833 12812 -2513 -821 2483 A O ATOM 2228 CB LYS A 294 48.083 -16.911 17.140 1.00 99.19 A C ANISOU 2228 CB LYS A 294 15433 11022 11232 -2415 -982 2666 A C ATOM 2229 CG LYS A 294 48.069 -16.852 18.650 1.00104.68 A C ANISOU 2229 CG LYS A 294 16334 11769 11672 -2500 -921 2798 A C ATOM 2230 CD LYS A 294 49.124 -15.922 19.210 1.00107.48 A C ANISOU 2230 CD LYS A 294 16677 12326 11837 -2412 -1045 2774 A C ATOM 2231 CE LYS A 294 49.170 -16.012 20.732 1.00115.79 A C ANISOU 2231 CE LYS A 294 17956 13428 12613 -2472 -1006 2913 A C ATOM 2232 NZ LYS A 294 50.007 -14.937 21.342 1.00121.40 A N1+ ANISOU 2232 NZ LYS A 294 18635 14357 13136 -2421 -1101 2851 A N1+ ATOM 2233 N LEU A 295 48.148 -18.762 14.253 1.00 95.77 A N ANISOU 2233 N LEU A 295 14803 10264 11322 -2195 -1164 2550 A N ATOM 2234 CA LEU A 295 47.741 -18.888 12.863 1.00 79.11 A C ANISOU 2234 CA LEU A 295 12508 8107 9443 -2148 -1169 2402 A C ATOM 2235 C LEU A 295 47.122 -20.240 12.634 1.00 82.07 A C ANISOU 2235 C LEU A 295 12989 8234 9962 -2201 -1143 2447 A C ATOM 2236 O LEU A 295 46.114 -20.347 11.945 1.00 90.76 A O ANISOU 2236 O LEU A 295 13975 9276 11233 -2289 -1042 2333 A O ATOM 2237 CB LEU A 295 48.933 -18.731 11.931 1.00 71.05 A C ANISOU 2237 CB LEU A 295 11362 7170 8465 -1921 -1363 2342 A C ATOM 2238 CG LEU A 295 49.429 -17.297 11.769 1.00 79.11 A C ANISOU 2238 CG LEU A 295 12215 8428 9415 -1878 -1376 2251 A C ATOM 2239 CD1 LEU A 295 50.730 -17.292 11.010 1.00 87.24 A C ANISOU 2239 CD1 LEU A 295 13147 9537 10465 -1662 -1568 2228 A C ATOM 2240 CD2 LEU A 295 48.397 -16.454 11.062 1.00 73.49 A C ANISOU 2240 CD2 LEU A 295 11318 7783 8820 -1961 -1232 2097 A C ATOM 2241 N LEU A 296 47.735 -21.277 13.199 1.00 78.21 A N ANISOU 2241 N LEU A 296 12717 7593 9406 -2143 -1239 2609 A N ATOM 2242 CA LEU A 296 47.196 -22.633 13.081 1.00 82.49 A C ANISOU 2242 CA LEU A 296 13398 7861 10084 -2202 -1214 2672 A C ATOM 2243 C LEU A 296 46.290 -22.956 14.261 1.00 92.85 A C ANISOU 2243 C LEU A 296 14895 9072 11311 -2432 -1027 2809 A C ATOM 2244 O LEU A 296 46.592 -23.808 15.095 1.00 95.06 A O ANISOU 2244 O LEU A 296 15423 9202 11492 -2436 -1051 2998 A O ATOM 2245 CB LEU A 296 48.316 -23.653 12.949 1.00 79.94 A C ANISOU 2245 CB LEU A 296 13219 7400 9756 -1998 -1420 2771 A C ATOM 2246 CG LEU A 296 49.182 -23.319 11.741 1.00 92.16 A C ANISOU 2246 CG LEU A 296 14562 9068 11386 -1773 -1589 2628 A C ATOM 2247 CD1 LEU A 296 50.483 -24.102 11.751 1.00 95.31 A C ANISOU 2247 CD1 LEU A 296 15084 9400 11730 -1541 -1804 2725 A C ATOM 2248 CD2 LEU A 296 48.398 -23.545 10.450 1.00 88.83 A C ANISOU 2248 CD2 LEU A 296 13971 8572 11210 -1791 -1552 2448 A C ATOM 2249 N VAL A 297 45.179 -22.236 14.318 1.00 98.94 A N ANISOU 2249 N VAL A 297 15539 9939 12114 -2613 -837 2713 A N ATOM 2250 CA VAL A 297 44.192 -22.382 15.365 1.00 99.01 A C ANISOU 2250 CA VAL A 297 15676 9897 12047 -2846 -627 2815 A C ATOM 2251 C VAL A 297 42.979 -23.000 14.711 1.00105.43 A C ANISOU 2251 C VAL A 297 16405 10552 13102 -3004 -501 2722 A C ATOM 2252 O VAL A 297 42.549 -22.543 13.654 1.00111.21 A O ANISOU 2252 O VAL A 297 16897 11361 13995 -2983 -500 2522 A O ATOM 2253 CB VAL A 297 43.809 -21.007 15.936 1.00 94.07 A C ANISOU 2253 CB VAL A 297 14944 9527 11272 -2930 -498 2752 A C ATOM 2254 CG1 VAL A 297 42.692 -21.126 16.957 1.00 84.35 A C ANISOU 2254 CG1 VAL A 297 13818 8266 9967 -3172 -260 2839 A C ATOM 2255 CG2 VAL A 297 45.025 -20.330 16.540 1.00 95.94 A C ANISOU 2255 CG2 VAL A 297 15242 9929 11281 -2781 -633 2815 A C ATOM 2256 N LEU A 298 42.429 -24.038 15.333 1.00108.25 A N ANISOU 2256 N LEU A 298 16956 10690 13483 -3162 -396 2866 A N ATOM 2257 CA LEU A 298 41.319 -24.784 14.745 1.00110.07 A C ANISOU 2257 CA LEU A 298 17122 10740 13961 -3329 -286 2783 A C ATOM 2258 C LEU A 298 40.091 -23.906 14.491 1.00111.85 A C ANISOU 2258 C LEU A 298 17100 11138 14260 -3492 -100 2606 A C ATOM 2259 O LEU A 298 39.591 -23.825 13.362 1.00106.80 A O ANISOU 2259 O LEU A 298 16240 10512 13826 -3480 -118 2404 A O ATOM 2260 CB LEU A 298 40.964 -25.981 15.629 1.00112.51 A C ANISOU 2260 CB LEU A 298 17705 10783 14259 -3496 -182 2998 A C ATOM 2261 CG LEU A 298 42.077 -27.030 15.797 1.00114.15 A C ANISOU 2261 CG LEU A 298 18173 10770 14427 -3328 -368 3172 A C ATOM 2262 CD1 LEU A 298 41.844 -27.908 17.020 1.00127.77 A C ANISOU 2262 CD1 LEU A 298 20212 12294 16043 -3479 -245 3438 A C ATOM 2263 CD2 LEU A 298 42.254 -27.893 14.547 1.00 97.51 A C ANISOU 2263 CD2 LEU A 298 16009 8458 12580 -3222 -518 3051 A C ATOM 2264 N ASP A 299 39.625 -23.243 15.545 1.00112.62 A N ANISOU 2264 N ASP A 299 17234 11378 14178 -3626 72 2677 A N ATOM 2265 CA ASP A 299 38.468 -22.358 15.463 1.00106.62 A C ANISOU 2265 CA ASP A 299 16253 10799 13457 -3770 259 2521 A C ATOM 2266 C ASP A 299 38.779 -21.026 14.760 1.00102.84 A C ANISOU 2266 C ASP A 299 15544 10573 12958 -3604 176 2335 A C ATOM 2267 O ASP A 299 39.483 -20.169 15.299 1.00 97.70 A O ANISOU 2267 O ASP A 299 14934 10082 12105 -3505 130 2378 A O ATOM 2268 CB ASP A 299 37.918 -22.106 16.865 1.00111.87 A C ANISOU 2268 CB ASP A 299 17047 11537 13920 -3952 471 2662 A C ATOM 2269 CG ASP A 299 36.657 -21.279 16.851 1.00121.35 A C ANISOU 2269 CG ASP A 299 18027 12919 15161 -4105 679 2506 A C ATOM 2270 OD1 ASP A 299 36.091 -21.078 15.755 1.00119.92 A O ANISOU 2270 OD1 ASP A 299 17604 12773 15189 -4094 668 2299 A O ATOM 2271 OD2 ASP A 299 36.234 -20.832 17.937 1.00128.57 A O1- ANISOU 2271 OD2 ASP A 299 19009 13950 15890 -4224 851 2586 A O1- ATOM 2272 N PRO A 300 38.246 -20.851 13.546 1.00102.29 A N ANISOU 2272 N PRO A 300 15235 10534 13098 -3573 156 2126 A N ATOM 2273 CA PRO A 300 38.401 -19.657 12.703 1.00102.20 A C ANISOU 2273 CA PRO A 300 14993 10737 13101 -3419 90 1943 A C ATOM 2274 C PRO A 300 38.159 -18.353 13.442 1.00104.72 A C ANISOU 2274 C PRO A 300 15266 11284 13240 -3453 211 1925 A C ATOM 2275 O PRO A 300 38.866 -17.375 13.207 1.00106.69 A O ANISOU 2275 O PRO A 300 15451 11683 13404 -3295 117 1873 A O ATOM 2276 CB PRO A 300 37.308 -19.838 11.654 1.00 98.11 A C ANISOU 2276 CB PRO A 300 14249 10206 12823 -3482 147 1744 A C ATOM 2277 CG PRO A 300 37.189 -21.314 11.527 1.00101.32 A C ANISOU 2277 CG PRO A 300 14776 10343 13377 -3569 119 1811 A C ATOM 2278 CD PRO A 300 37.436 -21.888 12.890 1.00100.35 A C ANISOU 2278 CD PRO A 300 14933 10099 13096 -3691 194 2056 A C ATOM 2279 N ALA A 301 37.161 -18.345 14.316 1.00106.23 A N ANISOU 2279 N ALA A 301 15487 11498 13377 -3659 424 1962 A N ATOM 2280 CA ALA A 301 36.791 -17.143 15.043 1.00105.96 A C ANISOU 2280 CA ALA A 301 15407 11677 13176 -3699 557 1927 A C ATOM 2281 C ALA A 301 37.738 -16.875 16.204 1.00105.61 A C ANISOU 2281 C ALA A 301 15585 11675 12869 -3658 517 2098 A C ATOM 2282 O ALA A 301 37.625 -15.851 16.876 1.00 99.63 A O ANISOU 2282 O ALA A 301 14817 11091 11946 -3669 600 2072 A O ATOM 2283 CB ALA A 301 35.376 -17.254 15.540 1.00108.43 A C ANISOU 2283 CB ALA A 301 15659 12018 13524 -3926 804 1897 A C ATOM 2284 N GLN A 302 38.655 -17.809 16.445 1.00107.91 A N ANISOU 2284 N GLN A 302 16077 11807 13117 -3604 384 2263 A N ATOM 2285 CA GLN A 302 39.704 -17.620 17.443 1.00105.71 A C ANISOU 2285 CA GLN A 302 16002 11573 12590 -3529 301 2418 A C ATOM 2286 C GLN A 302 41.071 -17.540 16.783 1.00109.00 A C ANISOU 2286 C GLN A 302 16412 11987 13015 -3301 48 2409 A C ATOM 2287 O GLN A 302 42.075 -17.314 17.455 1.00110.46 A O ANISOU 2287 O GLN A 302 16731 12231 13010 -3209 -58 2509 A O ATOM 2288 CB GLN A 302 39.697 -18.746 18.474 1.00106.31 A C ANISOU 2288 CB GLN A 302 16345 11487 12561 -3644 362 2647 A C ATOM 2289 CG GLN A 302 38.602 -18.614 19.521 1.00118.30 A C ANISOU 2289 CG GLN A 302 17916 13067 13966 -3860 621 2700 A C ATOM 2290 CD GLN A 302 38.593 -19.762 20.517 1.00128.47 A C ANISOU 2290 CD GLN A 302 19482 14183 15147 -3974 692 2948 A C ATOM 2291 NE2 GLN A 302 39.193 -19.537 21.684 1.00127.50 A N ANISOU 2291 NE2 GLN A 302 19559 14144 14740 -3938 684 3097 A N ATOM 2292 OE1 GLN A 302 38.048 -20.836 20.243 1.00134.30 A O ANISOU 2292 OE1 GLN A 302 20260 14714 16056 -4093 755 3003 A O ATOM 2293 N ARG A 303 41.101 -17.725 15.465 1.00107.83 A N ANISOU 2293 N ARG A 303 16100 11785 13084 -3208 -48 2283 A N ATOM 2294 CA ARG A 303 42.345 -17.656 14.706 1.00 94.76 A C ANISOU 2294 CA ARG A 303 14408 10141 11455 -2988 -276 2260 A C ATOM 2295 C ARG A 303 42.716 -16.208 14.427 1.00 88.34 A C ANISOU 2295 C ARG A 303 13438 9548 10581 -2890 -308 2136 A C ATOM 2296 O ARG A 303 41.888 -15.425 13.948 1.00 87.97 A O ANISOU 2296 O ARG A 303 13212 9598 10613 -2931 -201 1986 A O ATOM 2297 CB ARG A 303 42.237 -18.437 13.391 1.00 92.79 A C ANISOU 2297 CB ARG A 303 14051 9756 11450 -2916 -363 2171 A C ATOM 2298 CG ARG A 303 43.586 -18.691 12.718 1.00 94.11 A C ANISOU 2298 CG ARG A 303 14224 9902 11633 -2688 -598 2186 A C ATOM 2299 CD ARG A 303 43.455 -19.208 11.285 1.00 90.35 A C ANISOU 2299 CD ARG A 303 13599 9343 11389 -2592 -683 2053 A C ATOM 2300 NE ARG A 303 42.938 -20.571 11.232 1.00 90.48 A N ANISOU 2300 NE ARG A 303 13724 9118 11538 -2681 -662 2101 A N ATOM 2301 CZ ARG A 303 41.666 -20.860 11.007 1.00 91.19 A C ANISOU 2301 CZ ARG A 303 13737 9140 11773 -2850 -515 2015 A C ATOM 2302 NH1 ARG A 303 40.811 -19.875 10.817 1.00 94.28 A N1+ ANISOU 2302 NH1 ARG A 303 13940 9699 12181 -2923 -386 1880 A N1+ ATOM 2303 NH2 ARG A 303 41.246 -22.118 10.971 1.00 95.47 A N ANISOU 2303 NH2 ARG A 303 14383 9444 12446 -2944 -500 2060 A N ATOM 2304 N ILE A 304 43.978 -15.885 14.706 1.00 84.29 A N ANISOU 2304 N ILE A 304 12991 9103 9931 -2757 -461 2198 A N ATOM 2305 CA ILE A 304 44.529 -14.529 14.618 1.00 77.10 A C ANISOU 2305 CA ILE A 304 11969 8385 8942 -2676 -504 2106 A C ATOM 2306 C ILE A 304 44.208 -13.757 13.342 1.00 78.51 A C ANISOU 2306 C ILE A 304 11905 8639 9286 -2605 -497 1926 A C ATOM 2307 O ILE A 304 44.301 -14.287 12.227 1.00 69.42 A O ANISOU 2307 O ILE A 304 10659 7418 8301 -2510 -579 1875 A O ATOM 2308 CB ILE A 304 46.072 -14.547 14.812 1.00 84.75 A C ANISOU 2308 CB ILE A 304 13013 9393 9795 -2523 -710 2188 A C ATOM 2309 CG1 ILE A 304 46.584 -13.176 15.251 1.00 78.76 A C ANISOU 2309 CG1 ILE A 304 12204 8824 8897 -2505 -722 2129 A C ATOM 2310 CG2 ILE A 304 46.776 -15.004 13.547 1.00 81.21 A C ANISOU 2310 CG2 ILE A 304 12457 8894 9506 -2353 -872 2147 A C ATOM 2311 CD1 ILE A 304 47.962 -13.211 15.855 1.00 74.37 A C ANISOU 2311 CD1 ILE A 304 11751 8325 8180 -2406 -896 2223 A C ATOM 2312 N ASP A 305 43.832 -12.492 13.545 1.00 84.07 A N ANISOU 2312 N ASP A 305 12523 9486 9932 -2643 -400 1831 A N ATOM 2313 CA ASP A 305 43.598 -11.504 12.491 1.00 77.17 A C ANISOU 2313 CA ASP A 305 11441 8707 9173 -2565 -386 1673 A C ATOM 2314 C ASP A 305 44.896 -11.228 11.759 1.00 83.40 A C ANISOU 2314 C ASP A 305 12168 9538 9981 -2392 -568 1669 A C ATOM 2315 O ASP A 305 45.970 -11.324 12.358 1.00 90.29 A O ANISOU 2315 O ASP A 305 13148 10428 10731 -2353 -682 1765 A O ATOM 2316 CB ASP A 305 43.164 -10.200 13.153 1.00 87.35 A C ANISOU 2316 CB ASP A 305 12710 10127 10351 -2634 -261 1604 A C ATOM 2317 CG ASP A 305 42.047 -9.512 12.416 1.00110.45 A C ANISOU 2317 CG ASP A 305 15459 13106 13401 -2641 -135 1450 A C ATOM 2318 OD1 ASP A 305 40.975 -10.139 12.277 1.00125.03 A O ANISOU 2318 OD1 ASP A 305 17268 14898 15339 -2725 -29 1421 A O ATOM 2319 OD2 ASP A 305 42.226 -8.346 11.990 1.00109.74 A O1- ANISOU 2319 OD2 ASP A 305 15268 13110 13317 -2564 -139 1358 A O1- ATOM 2320 N SER A 306 44.819 -10.854 10.482 1.00 82.78 A N ANISOU 2320 N SER A 306 11912 9494 10048 -2285 -594 1560 A N ATOM 2321 CA SER A 306 46.027 -10.399 9.770 1.00 89.18 A C ANISOU 2321 CA SER A 306 12643 10372 10869 -2128 -740 1552 A C ATOM 2322 C SER A 306 46.586 -9.073 10.333 1.00 84.69 A C ANISOU 2322 C SER A 306 12075 9926 10178 -2143 -731 1537 A C ATOM 2323 O SER A 306 47.761 -8.761 10.167 1.00 78.58 A O ANISOU 2323 O SER A 306 11278 9209 9369 -2056 -854 1564 A O ATOM 2324 CB SER A 306 45.768 -10.251 8.272 1.00 82.47 A C ANISOU 2324 CB SER A 306 11609 9542 10185 -2006 -755 1443 A C ATOM 2325 OG SER A 306 45.338 -8.934 7.978 1.00 87.28 A O ANISOU 2325 OG SER A 306 12109 10253 10802 -2002 -661 1346 A O ATOM 2326 N ASP A 307 45.727 -8.298 10.985 1.00 86.54 A N ANISOU 2326 N ASP A 307 12327 10200 10354 -2257 -583 1484 A N ATOM 2327 CA ASP A 307 46.133 -7.075 11.663 1.00 89.73 A C ANISOU 2327 CA ASP A 307 12756 10699 10638 -2291 -563 1457 A C ATOM 2328 C ASP A 307 46.860 -7.425 12.953 1.00 80.15 A C ANISOU 2328 C ASP A 307 11714 9493 9245 -2352 -631 1564 A C ATOM 2329 O ASP A 307 47.991 -7.014 13.182 1.00 89.88 A O ANISOU 2329 O ASP A 307 12960 10788 10403 -2309 -747 1586 A O ATOM 2330 CB ASP A 307 44.896 -6.233 11.993 1.00101.77 A C ANISOU 2330 CB ASP A 307 14257 12259 12153 -2382 -380 1358 A C ATOM 2331 CG ASP A 307 45.177 -4.737 12.012 1.00111.92 A C ANISOU 2331 CG ASP A 307 15495 13627 13405 -2364 -356 1275 A C ATOM 2332 OD1 ASP A 307 46.193 -4.283 11.421 1.00123.50 A O ANISOU 2332 OD1 ASP A 307 16898 15120 14905 -2275 -466 1276 A O ATOM 2333 OD2 ASP A 307 44.354 -4.015 12.615 1.00101.01 A O1- ANISOU 2333 OD2 ASP A 307 14136 12277 11965 -2440 -221 1204 A O1- ATOM 2334 N ASP A 308 46.209 -8.200 13.798 1.00 73.99 A N ANISOU 2334 N ASP A 308 11065 8656 8391 -2453 -556 1631 A N ATOM 2335 CA ASP A 308 46.775 -8.516 15.093 1.00 86.88 A C ANISOU 2335 CA ASP A 308 12878 10305 9828 -2506 -605 1738 A C ATOM 2336 C ASP A 308 48.090 -9.274 14.962 1.00 86.96 A C ANISOU 2336 C ASP A 308 12932 10292 9818 -2395 -806 1840 A C ATOM 2337 O ASP A 308 48.885 -9.317 15.904 1.00 92.89 A O ANISOU 2337 O ASP A 308 13802 11093 10400 -2395 -894 1913 A O ATOM 2338 CB ASP A 308 45.772 -9.316 15.921 1.00 99.65 A C ANISOU 2338 CB ASP A 308 14629 11853 11382 -2632 -472 1811 A C ATOM 2339 CG ASP A 308 44.496 -8.540 16.198 1.00108.38 A C ANISOU 2339 CG ASP A 308 15687 13009 12482 -2742 -267 1707 A C ATOM 2340 OD1 ASP A 308 44.510 -7.701 17.127 1.00107.97 A O ANISOU 2340 OD1 ASP A 308 15699 13052 12271 -2795 -216 1677 A O ATOM 2341 OD2 ASP A 308 43.483 -8.767 15.491 1.00107.28 A O1- ANISOU 2341 OD2 ASP A 308 15443 12823 12495 -2767 -164 1646 A O1- ATOM 2342 N ALA A 309 48.321 -9.859 13.791 1.00 76.92 A N ANISOU 2342 N ALA A 309 11560 8958 8709 -2287 -884 1835 A N ATOM 2343 CA ALA A 309 49.500 -10.693 13.583 1.00 79.49 A C ANISOU 2343 CA ALA A 309 11918 9256 9028 -2163 -1071 1925 A C ATOM 2344 C ALA A 309 50.710 -9.856 13.225 1.00 83.83 A C ANISOU 2344 C ALA A 309 12356 9932 9564 -2066 -1197 1881 A C ATOM 2345 O ALA A 309 51.826 -10.158 13.622 1.00 85.73 A O ANISOU 2345 O ALA A 309 12647 10215 9711 -1997 -1347 1951 A O ATOM 2346 CB ALA A 309 49.239 -11.711 12.505 1.00 82.84 A C ANISOU 2346 CB ALA A 309 12286 9561 9626 -2082 -1102 1928 A C ATOM 2347 N LEU A 310 50.476 -8.802 12.456 1.00 89.11 A N ANISOU 2347 N LEU A 310 12868 10660 10329 -2061 -1133 1766 A N ATOM 2348 CA LEU A 310 51.520 -7.862 12.079 1.00 85.92 A C ANISOU 2348 CA LEU A 310 12347 10369 9928 -1998 -1219 1719 A C ATOM 2349 C LEU A 310 51.966 -7.066 13.294 1.00 87.68 A C ANISOU 2349 C LEU A 310 12652 10681 9982 -2089 -1231 1713 A C ATOM 2350 O LEU A 310 53.020 -6.426 13.295 1.00 96.80 A O ANISOU 2350 O LEU A 310 13741 11932 11108 -2059 -1330 1689 A O ATOM 2351 CB LEU A 310 50.976 -6.898 11.033 1.00 77.49 A C ANISOU 2351 CB LEU A 310 11121 9322 8998 -1984 -1118 1608 A C ATOM 2352 CG LEU A 310 50.764 -7.363 9.600 1.00 63.11 A C ANISOU 2352 CG LEU A 310 9170 7462 7346 -1863 -1127 1583 A C ATOM 2353 CD1 LEU A 310 49.896 -6.350 8.905 1.00 67.95 A C ANISOU 2353 CD1 LEU A 310 9674 8092 8050 -1875 -991 1478 A C ATOM 2354 CD2 LEU A 310 52.094 -7.480 8.890 1.00 67.15 A C ANISOU 2354 CD2 LEU A 310 9583 8039 7891 -1727 -1279 1611 A C ATOM 2355 N ASN A 311 51.130 -7.111 14.319 1.00 84.76 A N ANISOU 2355 N ASN A 311 12420 10283 9501 -2204 -1125 1726 A N ATOM 2356 CA ASN A 311 51.330 -6.365 15.541 1.00 95.68 A C ANISOU 2356 CA ASN A 311 13898 11750 10708 -2296 -1115 1704 A C ATOM 2357 C ASN A 311 51.995 -7.250 16.579 1.00 93.57 A C ANISOU 2357 C ASN A 311 13791 11498 10265 -2282 -1233 1824 A C ATOM 2358 O ASN A 311 52.236 -6.837 17.711 1.00 93.59 A O ANISOU 2358 O ASN A 311 13896 11579 10087 -2344 -1249 1821 A O ATOM 2359 CB ASN A 311 49.971 -5.897 16.045 1.00109.32 A C ANISOU 2359 CB ASN A 311 15681 13453 12402 -2416 -917 1645 A C ATOM 2360 CG ASN A 311 50.078 -4.947 17.201 1.00115.66 A C ANISOU 2360 CG ASN A 311 16566 14348 13033 -2504 -890 1588 A C ATOM 2361 ND2 ASN A 311 48.934 -4.507 17.707 1.00114.88 A N ANISOU 2361 ND2 ASN A 311 16516 14244 12889 -2598 -717 1530 A N ATOM 2362 OD1 ASN A 311 51.175 -4.601 17.636 1.00120.33 A O ANISOU 2362 OD1 ASN A 311 17168 15020 13531 -2486 -1024 1584 A O ATOM 2363 N HIS A 312 52.294 -8.476 16.172 1.00 95.62 A N ANISOU 2363 N HIS A 312 14077 11681 10575 -2188 -1322 1927 A N ATOM 2364 CA HIS A 312 52.868 -9.490 17.050 1.00 97.40 A C ANISOU 2364 CA HIS A 312 14469 11892 10646 -2147 -1436 2062 A C ATOM 2365 C HIS A 312 54.332 -9.195 17.366 1.00 95.43 A C ANISOU 2365 C HIS A 312 14186 11777 10295 -2064 -1631 2063 A C ATOM 2366 O HIS A 312 55.074 -8.720 16.509 1.00102.54 A O ANISOU 2366 O HIS A 312 14913 12740 11306 -1994 -1711 1996 A O ATOM 2367 CB HIS A 312 52.739 -10.854 16.373 1.00 95.23 A C ANISOU 2367 CB HIS A 312 14223 11474 10487 -2059 -1474 2156 A C ATOM 2368 CG HIS A 312 53.022 -12.019 17.268 1.00 96.44 A C ANISOU 2368 CG HIS A 312 14585 11562 10497 -2026 -1551 2315 A C ATOM 2369 CD2 HIS A 312 52.189 -12.818 17.977 1.00 99.40 A C ANISOU 2369 CD2 HIS A 312 15146 11820 10801 -2107 -1450 2422 A C ATOM 2370 ND1 HIS A 312 54.293 -12.510 17.472 1.00 91.75 A N ANISOU 2370 ND1 HIS A 312 14025 11018 9819 -1887 -1754 2387 A N ATOM 2371 CE1 HIS A 312 54.233 -13.553 18.281 1.00 96.58 A C ANISOU 2371 CE1 HIS A 312 14849 11539 10307 -1872 -1780 2537 A C ATOM 2372 NE2 HIS A 312 52.969 -13.760 18.603 1.00 98.86 A N ANISOU 2372 NE2 HIS A 312 15238 11721 10603 -2012 -1592 2566 A N ATOM 2373 N ASP A 313 54.747 -9.494 18.591 1.00 93.87 A N ANISOU 2373 N ASP A 313 14150 11634 9884 -2070 -1706 2140 A N ATOM 2374 CA ASP A 313 56.102 -9.175 19.045 1.00100.19 A C ANISOU 2374 CA ASP A 313 14918 12586 10565 -2000 -1896 2126 A C ATOM 2375 C ASP A 313 57.186 -9.818 18.180 1.00102.16 A C ANISOU 2375 C ASP A 313 15053 12847 10915 -1832 -2071 2163 A C ATOM 2376 O ASP A 313 58.358 -9.475 18.282 1.00104.36 A O ANISOU 2376 O ASP A 313 15242 13267 11144 -1767 -2228 2127 A O ATOM 2377 CB ASP A 313 56.288 -9.568 20.514 1.00105.04 A C ANISOU 2377 CB ASP A 313 15744 13253 10913 -2010 -1952 2217 A C ATOM 2378 CG ASP A 313 55.317 -8.853 21.438 1.00120.04 A C ANISOU 2378 CG ASP A 313 17748 15175 12685 -2167 -1784 2167 A C ATOM 2379 OD1 ASP A 313 55.730 -7.880 22.110 1.00119.36 A O ANISOU 2379 OD1 ASP A 313 17646 15230 12475 -2216 -1823 2067 A O ATOM 2380 OD2 ASP A 313 54.135 -9.264 21.489 1.00131.29 A O1- ANISOU 2380 OD2 ASP A 313 19266 16481 14137 -2241 -1612 2218 A O1- ATOM 2381 N PHE A 314 56.788 -10.754 17.331 1.00101.69 A N ANISOU 2381 N PHE A 314 14992 12646 11000 -1760 -2044 2224 A N ATOM 2382 CA PHE A 314 57.706 -11.379 16.393 1.00 97.24 A C ANISOU 2382 CA PHE A 314 14314 12086 10547 -1589 -2193 2246 A C ATOM 2383 C PHE A 314 58.243 -10.343 15.410 1.00 90.44 A C ANISOU 2383 C PHE A 314 13205 11337 9822 -1579 -2204 2118 A C ATOM 2384 O PHE A 314 59.417 -10.356 15.037 1.00 88.73 A O ANISOU 2384 O PHE A 314 12863 11230 9621 -1463 -2356 2106 A O ATOM 2385 CB PHE A 314 56.973 -12.499 15.653 1.00100.83 A C ANISOU 2385 CB PHE A 314 14821 12349 11141 -1537 -2135 2310 A C ATOM 2386 CG PHE A 314 57.701 -13.028 14.449 1.00103.01 A C ANISOU 2386 CG PHE A 314 14955 12619 11565 -1363 -2252 2298 A C ATOM 2387 CD1 PHE A 314 58.960 -13.581 14.564 1.00104.97 A C ANISOU 2387 CD1 PHE A 314 15195 12943 11745 -1198 -2452 2352 A C ATOM 2388 CD2 PHE A 314 57.102 -13.005 13.202 1.00105.98 A C ANISOU 2388 CD2 PHE A 314 15204 12922 12141 -1352 -2163 2229 A C ATOM 2389 CE1 PHE A 314 59.619 -14.080 13.458 1.00103.25 A C ANISOU 2389 CE1 PHE A 314 14842 12730 11657 -1028 -2553 2334 A C ATOM 2390 CE2 PHE A 314 57.757 -13.504 12.093 1.00104.35 A C ANISOU 2390 CE2 PHE A 314 14871 12721 12057 -1182 -2266 2212 A C ATOM 2391 CZ PHE A 314 59.017 -14.041 12.223 1.00101.16 A C ANISOU 2391 CZ PHE A 314 14458 12393 11584 -1021 -2457 2264 A C ATOM 2392 N PHE A 315 57.376 -9.431 14.999 1.00 86.68 A N ANISOU 2392 N PHE A 315 12657 10836 9443 -1697 -2038 2025 A N ATOM 2393 CA PHE A 315 57.766 -8.412 14.040 1.00 91.14 A C ANISOU 2393 CA PHE A 315 13005 11483 10139 -1696 -2022 1918 A C ATOM 2394 C PHE A 315 58.426 -7.224 14.720 1.00 93.08 A C ANISOU 2394 C PHE A 315 13201 11872 10291 -1787 -2059 1839 A C ATOM 2395 O PHE A 315 59.053 -6.387 14.065 1.00 81.80 A O ANISOU 2395 O PHE A 315 11597 10529 8955 -1787 -2078 1763 A O ATOM 2396 CB PHE A 315 56.546 -7.963 13.245 1.00 93.26 A C ANISOU 2396 CB PHE A 315 13223 11656 10554 -1762 -1835 1855 A C ATOM 2397 CG PHE A 315 55.957 -9.048 12.410 1.00 90.60 A C ANISOU 2397 CG PHE A 315 12897 11191 10337 -1673 -1809 1901 A C ATOM 2398 CD1 PHE A 315 54.781 -9.665 12.785 1.00 87.10 A C ANISOU 2398 CD1 PHE A 315 12595 10615 9884 -1743 -1698 1940 A C ATOM 2399 CD2 PHE A 315 56.596 -9.470 11.258 1.00 89.64 A C ANISOU 2399 CD2 PHE A 315 12638 11086 10335 -1523 -1897 1901 A C ATOM 2400 CE1 PHE A 315 54.243 -10.666 12.016 1.00 83.36 A C ANISOU 2400 CE1 PHE A 315 12125 10016 9531 -1675 -1681 1967 A C ATOM 2401 CE2 PHE A 315 56.062 -10.473 10.489 1.00 87.21 A C ANISOU 2401 CE2 PHE A 315 12342 10658 10137 -1438 -1883 1925 A C ATOM 2402 CZ PHE A 315 54.885 -11.075 10.872 1.00 82.71 A C ANISOU 2402 CZ PHE A 315 11914 9944 9567 -1519 -1779 1955 A C ATOM 2403 N TRP A 316 58.283 -7.174 16.042 1.00105.69 A N ANISOU 2403 N TRP A 316 14959 13494 11702 -1866 -2067 1856 A N ATOM 2404 CA TRP A 316 58.810 -6.079 16.853 1.00110.05 A C ANISOU 2404 CA TRP A 316 15492 14176 12144 -1963 -2105 1765 A C ATOM 2405 C TRP A 316 59.758 -6.557 17.954 1.00114.44 A C ANISOU 2405 C TRP A 316 16138 14847 12495 -1910 -2288 1816 A C ATOM 2406 O TRP A 316 59.537 -6.293 19.135 1.00124.83 A O ANISOU 2406 O TRP A 316 17595 16205 13631 -1990 -2278 1803 A O ATOM 2407 CB TRP A 316 57.653 -5.295 17.461 1.00102.85 A C ANISOU 2407 CB TRP A 316 14682 13214 11184 -2116 -1927 1699 A C ATOM 2408 CG TRP A 316 56.667 -4.899 16.434 1.00 95.72 A C ANISOU 2408 CG TRP A 316 13699 12203 10466 -2147 -1756 1654 A C ATOM 2409 CD1 TRP A 316 55.475 -5.490 16.178 1.00 95.02 A C ANISOU 2409 CD1 TRP A 316 13684 11990 10431 -2154 -1622 1698 A C ATOM 2410 CD2 TRP A 316 56.802 -3.836 15.488 1.00 98.92 A C ANISOU 2410 CD2 TRP A 316 13932 12623 11031 -2170 -1703 1556 A C ATOM 2411 CE2 TRP A 316 55.643 -3.832 14.703 1.00 94.17 A C ANISOU 2411 CE2 TRP A 316 13312 11909 10559 -2172 -1543 1546 A C ATOM 2412 CE3 TRP A 316 57.791 -2.883 15.236 1.00103.10 A C ANISOU 2412 CE3 TRP A 316 14320 13248 11606 -2193 -1773 1479 A C ATOM 2413 NE1 TRP A 316 54.845 -4.851 15.143 1.00 94.46 A N ANISOU 2413 NE1 TRP A 316 13492 11867 10533 -2168 -1498 1625 A N ATOM 2414 CZ2 TRP A 316 55.447 -2.912 13.683 1.00 94.77 A C ANISOU 2414 CZ2 TRP A 316 13249 11967 10794 -2177 -1455 1470 A C ATOM 2415 CZ3 TRP A 316 57.588 -1.971 14.224 1.00 96.22 A C ANISOU 2415 CZ3 TRP A 316 13315 12343 10901 -2215 -1672 1412 A C ATOM 2416 CH2 TRP A 316 56.430 -1.990 13.462 1.00 93.40 A C ANISOU 2416 CH2 TRP A 316 12958 11875 10657 -2198 -1518 1413 A C ATOM 2417 N SER A 317 60.809 -7.262 17.551 1.00107.17 A N ANISOU 2417 N SER A 317 15136 13988 11596 -1762 -2456 1871 A N ATOM 2418 CA SER A 317 61.835 -7.748 18.464 1.00111.06 A C ANISOU 2418 CA SER A 317 15686 14608 11903 -1676 -2655 1917 A C ATOM 2419 C SER A 317 63.024 -8.159 17.609 1.00117.03 A C ANISOU 2419 C SER A 317 16257 15452 12758 -1519 -2813 1927 A C ATOM 2420 O SER A 317 62.884 -8.317 16.394 1.00118.65 A O ANISOU 2420 O SER A 317 16342 15588 13150 -1467 -2755 1928 A O ATOM 2421 CB SER A 317 61.327 -8.941 19.267 1.00108.59 A C ANISOU 2421 CB SER A 317 15624 14200 11438 -1615 -2663 2064 A C ATOM 2422 OG SER A 317 61.212 -10.089 18.445 1.00108.10 A O ANISOU 2422 OG SER A 317 15574 14009 11491 -1481 -2676 2167 A O ATOM 2423 N ASP A 318 64.191 -8.330 18.221 1.00113.93 A N ANISOU 2423 N ASP A 318 15831 15223 12233 -1435 -3012 1928 A N ATOM 2424 CA ASP A 318 65.380 -8.629 17.430 1.00112.28 A C ANISOU 2424 CA ASP A 318 15418 15128 12114 -1286 -3161 1920 A C ATOM 2425 C ASP A 318 65.487 -10.100 17.075 1.00109.24 A C ANISOU 2425 C ASP A 318 15116 14655 11735 -1077 -3243 2055 A C ATOM 2426 O ASP A 318 65.074 -10.956 17.851 1.00106.07 A O ANISOU 2426 O ASP A 318 14945 14161 11196 -1028 -3265 2165 A O ATOM 2427 CB ASP A 318 66.649 -8.121 18.114 1.00120.61 A C ANISOU 2427 CB ASP A 318 16355 16419 13051 -1282 -3347 1840 A C ATOM 2428 CG ASP A 318 66.847 -6.623 17.925 1.00127.22 A C ANISOU 2428 CG ASP A 318 17014 17345 13980 -1469 -3278 1683 A C ATOM 2429 OD1 ASP A 318 67.027 -6.174 16.766 1.00122.17 A O ANISOU 2429 OD1 ASP A 318 16178 16703 13539 -1487 -3210 1639 A O ATOM 2430 OD2 ASP A 318 66.809 -5.894 18.938 1.00131.90 A O1- ANISOU 2430 OD2 ASP A 318 17671 18003 14442 -1598 -3290 1603 A O1- ATOM 2431 N PRO A 319 66.004 -10.393 15.870 1.00113.25 A N ANISOU 2431 N PRO A 319 15443 15182 12407 -955 -3277 2047 A N ATOM 2432 CA PRO A 319 66.393 -9.377 14.881 1.00110.32 A C ANISOU 2432 CA PRO A 319 14808 14905 12202 -1022 -3220 1934 A C ATOM 2433 C PRO A 319 65.179 -8.722 14.232 1.00100.27 A C ANISOU 2433 C PRO A 319 13545 13482 11070 -1168 -2991 1897 A C ATOM 2434 O PRO A 319 64.172 -9.385 14.002 1.00101.02 A O ANISOU 2434 O PRO A 319 13782 13398 11203 -1148 -2893 1963 A O ATOM 2435 CB PRO A 319 67.158 -10.187 13.818 1.00110.49 A C ANISOU 2435 CB PRO A 319 14682 14971 12329 -809 -3318 1967 A C ATOM 2436 CG PRO A 319 67.422 -11.526 14.428 1.00111.87 A C ANISOU 2436 CG PRO A 319 15028 15106 12371 -624 -3471 2079 A C ATOM 2437 CD PRO A 319 66.309 -11.754 15.402 1.00113.74 A C ANISOU 2437 CD PRO A 319 15547 15177 12493 -730 -3380 2148 A C ATOM 2438 N MET A 320 65.265 -7.433 13.936 1.00 98.14 A N ANISOU 2438 N MET A 320 13126 13281 10882 -1313 -2907 1792 A N ATOM 2439 CA MET A 320 64.175 -6.779 13.228 1.00 99.05 A C ANISOU 2439 CA MET A 320 13238 13264 11134 -1423 -2698 1756 A C ATOM 2440 C MET A 320 64.131 -7.294 11.803 1.00109.34 A C ANISOU 2440 C MET A 320 14423 14520 12601 -1289 -2661 1787 A C ATOM 2441 O MET A 320 65.137 -7.807 11.296 1.00112.81 A O ANISOU 2441 O MET A 320 14730 15066 13066 -1140 -2788 1806 A O ATOM 2442 CB MET A 320 64.343 -5.268 13.238 1.00 93.09 A C ANISOU 2442 CB MET A 320 12361 12579 10429 -1598 -2623 1642 A C ATOM 2443 CG MET A 320 64.144 -4.669 14.593 1.00 92.48 A C ANISOU 2443 CG MET A 320 12417 12523 10198 -1743 -2629 1588 A C ATOM 2444 SD MET A 320 62.482 -4.991 15.165 1.00104.14 A S ANISOU 2444 SD MET A 320 14156 13804 11607 -1806 -2468 1634 A S ATOM 2445 CE MET A 320 61.606 -3.586 14.496 1.00 73.16 A C ANISOU 2445 CE MET A 320 10163 9796 7840 -1960 -2251 1531 A C ATOM 2446 N PRO A 321 62.961 -7.173 11.153 1.00107.53 A N ANISOU 2446 N PRO A 321 14237 14142 12477 -1330 -2491 1784 A N ATOM 2447 CA PRO A 321 62.822 -7.673 9.782 1.00101.59 A C ANISOU 2447 CA PRO A 321 13383 13346 11871 -1196 -2455 1801 A C ATOM 2448 C PRO A 321 63.755 -6.889 8.870 1.00 94.60 A C ANISOU 2448 C PRO A 321 12253 12609 11083 -1175 -2462 1751 A C ATOM 2449 O PRO A 321 63.836 -5.670 9.025 1.00 83.22 A O ANISOU 2449 O PRO A 321 10745 11215 9659 -1325 -2391 1690 A O ATOM 2450 CB PRO A 321 61.359 -7.372 9.447 1.00 97.44 A C ANISOU 2450 CB PRO A 321 12941 12662 11420 -1285 -2264 1781 A C ATOM 2451 CG PRO A 321 60.681 -7.156 10.785 1.00 97.66 A C ANISOU 2451 CG PRO A 321 13159 12628 11320 -1433 -2220 1782 A C ATOM 2452 CD PRO A 321 61.724 -6.543 11.647 1.00100.70 A C ANISOU 2452 CD PRO A 321 13505 13160 11595 -1493 -2329 1752 A C ATOM 2453 N SER A 322 64.446 -7.569 7.956 1.00 95.12 A N ANISOU 2453 N SER A 322 12190 12744 11208 -996 -2541 1776 A N ATOM 2454 CA SER A 322 65.417 -6.918 7.080 1.00 97.72 A C ANISOU 2454 CA SER A 322 12275 13235 11620 -966 -2546 1742 A C ATOM 2455 C SER A 322 65.082 -7.125 5.613 1.00 88.61 A C ANISOU 2455 C SER A 322 11024 12050 10594 -845 -2458 1747 A C ATOM 2456 O SER A 322 64.310 -8.005 5.280 1.00 97.59 A O ANISOU 2456 O SER A 322 12267 13060 11752 -747 -2441 1771 A O ATOM 2457 CB SER A 322 66.820 -7.462 7.354 1.00111.36 A C ANISOU 2457 CB SER A 322 13893 15139 13281 -846 -2741 1754 A C ATOM 2458 OG SER A 322 66.926 -8.818 6.952 1.00116.46 A O ANISOU 2458 OG SER A 322 14577 15751 13921 -626 -2837 1807 A O ATOM 2459 N ASP A 323 65.679 -6.326 4.736 1.00 90.90 A N ANISOU 2459 N ASP A 323 11110 12462 10966 -850 -2402 1723 A N ATOM 2460 CA ASP A 323 65.496 -6.497 3.295 1.00100.65 A C ANISOU 2460 CA ASP A 323 12236 13705 12302 -714 -2325 1730 A C ATOM 2461 C ASP A 323 66.062 -7.814 2.744 1.00101.56 A C ANISOU 2461 C ASP A 323 12302 13876 12409 -471 -2456 1753 A C ATOM 2462 O ASP A 323 66.665 -8.607 3.478 1.00100.33 A O ANISOU 2462 O ASP A 323 12193 13754 12172 -399 -2613 1773 A O ATOM 2463 CB ASP A 323 66.062 -5.298 2.535 1.00114.62 A C ANISOU 2463 CB ASP A 323 13806 15596 14147 -783 -2226 1715 A C ATOM 2464 CG ASP A 323 65.069 -4.148 2.451 1.00136.02 A C ANISOU 2464 CG ASP A 323 16582 18187 16910 -948 -2046 1696 A C ATOM 2465 OD1 ASP A 323 65.491 -3.015 2.124 1.00141.96 A O ANISOU 2465 OD1 ASP A 323 17215 19005 17718 -1053 -1960 1688 A O ATOM 2466 OD2 ASP A 323 63.863 -4.381 2.711 1.00139.91 A O1- ANISOU 2466 OD2 ASP A 323 17247 18518 17394 -971 -1989 1687 A O1- ATOM 2467 N LEU A 324 65.848 -8.055 1.453 1.00101.91 A N ANISOU 2467 N LEU A 324 12260 13929 12530 -331 -2395 1748 A N ATOM 2468 CA LEU A 324 66.288 -9.308 0.845 1.00105.06 A C ANISOU 2468 CA LEU A 324 12622 14367 12929 -87 -2510 1754 A C ATOM 2469 C LEU A 324 67.299 -9.112 -0.283 1.00121.87 A C ANISOU 2469 C LEU A 324 14504 16705 15097 48 -2509 1746 A C ATOM 2470 O LEU A 324 67.059 -8.411 -1.276 1.00110.64 A O ANISOU 2470 O LEU A 324 12979 15323 13738 40 -2372 1739 A O ATOM 2471 CB LEU A 324 65.110 -10.165 0.385 1.00 99.04 A C ANISOU 2471 CB LEU A 324 12006 13419 12207 3 -2477 1741 A C ATOM 2472 CG LEU A 324 64.092 -10.558 1.458 1.00 94.03 A C ANISOU 2472 CG LEU A 324 11614 12577 11535 -115 -2475 1755 A C ATOM 2473 CD1 LEU A 324 63.239 -9.353 1.832 1.00108.36 A C ANISOU 2473 CD1 LEU A 324 13478 14331 13363 -340 -2319 1742 A C ATOM 2474 CD2 LEU A 324 63.201 -11.693 0.983 1.00 70.06 A C ANISOU 2474 CD2 LEU A 324 8697 9375 8546 4 -2483 1739 A C ATOM 2475 N LYS A 325 68.449 -9.742 -0.073 1.00143.27 A N ANISOU 2475 N LYS A 325 17122 19555 17759 178 -2663 1751 A N ATOM 2476 CA LYS A 325 69.575 -9.730 -0.987 1.00143.93 A C ANISOU 2476 CA LYS A 325 16959 19867 17861 325 -2688 1742 A C ATOM 2477 C LYS A 325 70.230 -11.094 -0.785 1.00141.91 A C ANISOU 2477 C LYS A 325 16722 19647 17550 556 -2882 1738 A C ATOM 2478 O LYS A 325 71.118 -11.497 -1.539 1.00138.85 A O ANISOU 2478 O LYS A 325 16158 19433 17166 750 -2939 1722 A O ATOM 2479 CB LYS A 325 70.526 -8.577 -0.645 1.00143.37 A C ANISOU 2479 CB LYS A 325 16708 19978 17789 158 -2661 1745 A C ATOM 2480 CG LYS A 325 69.858 -7.189 -0.681 1.00142.08 A C ANISOU 2480 CG LYS A 325 16563 19741 17681 -86 -2475 1752 A C ATOM 2481 CD LYS A 325 70.670 -6.114 0.061 1.00141.20 A C ANISOU 2481 CD LYS A 325 16339 19746 17566 -299 -2476 1741 A C ATOM 2482 CE LYS A 325 71.925 -5.673 -0.712 1.00133.22 A C ANISOU 2482 CE LYS A 325 15035 18986 16595 -264 -2456 1744 A C ATOM 2483 NZ LYS A 325 72.813 -4.733 0.058 1.00120.46 A N1+ ANISOU 2483 NZ LYS A 325 13291 17493 14983 -474 -2480 1718 A N1+ ATOM 2484 N GLY A 326 69.771 -11.789 0.258 1.00139.03 A N ANISOU 2484 N GLY A 326 16581 19114 17131 536 -2978 1757 A N ATOM 2485 CA GLY A 326 69.972 -13.222 0.404 1.00141.03 A C ANISOU 2485 CA GLY A 326 16937 19301 17345 761 -3140 1764 A C ATOM 2486 C GLY A 326 69.085 -13.908 -0.620 1.00138.37 A C ANISOU 2486 C GLY A 326 16675 18818 17081 893 -3081 1735 A C ATOM 2487 O GLY A 326 68.053 -14.514 -0.290 1.00122.10 A O ANISOU 2487 O GLY A 326 14836 16522 15033 865 -3074 1744 A O ATOM 2488 N MET A 327 69.521 -13.800 -1.874 1.00152.42 A N ANISOU 2488 N MET A 327 18256 20751 18905 1035 -3038 1696 A N ATOM 2489 CA MET A 327 68.723 -14.085 -3.064 1.00157.45 A C ANISOU 2489 CA MET A 327 18903 21310 19611 1140 -2949 1651 A C ATOM 2490 C MET A 327 68.778 -15.551 -3.496 1.00153.70 A C ANISOU 2490 C MET A 327 18500 20756 19143 1409 -3081 1609 A C ATOM 2491 O MET A 327 68.503 -15.878 -4.656 1.00145.39 A O ANISOU 2491 O MET A 327 17392 19714 18136 1562 -3043 1549 A O ATOM 2492 CB MET A 327 69.226 -13.197 -4.205 1.00163.38 A C ANISOU 2492 CB MET A 327 19404 22286 20388 1169 -2832 1635 A C ATOM 2493 CG MET A 327 70.747 -13.282 -4.394 1.00172.14 A C ANISOU 2493 CG MET A 327 20286 23664 21457 1311 -2925 1636 A C ATOM 2494 SD MET A 327 71.484 -12.085 -5.532 1.00229.35 A S ANISOU 2494 SD MET A 327 27224 31194 28725 1291 -2768 1645 A S ATOM 2495 CE MET A 327 71.599 -10.618 -4.508 1.00100.41 A C ANISOU 2495 CE MET A 327 10871 14878 12401 939 -2681 1698 A C TER HETATM 2496 CA' SLQ A 331 58.725 -17.063 -11.009 0.99103.45 C C HETATM 2497 C6' SLQ A 331 59.125 -19.207 -12.289 0.99104.00 C C HETATM 2498 C5' SLQ A 331 59.706 -19.863 -13.383 0.99114.93 C C HETATM 2499 C4' SLQ A 331 60.515 -19.137 -14.284 0.99118.84 C C HETATM 2500 C3' SLQ A 331 60.736 -17.767 -14.095 0.99106.37 C C HETATM 2501 C2' SLQ A 331 60.165 -17.110 -13.012 0.99 97.65 C C HETATM 2502 C1' SLQ A 331 59.382 -17.839 -12.121 0.99102.38 C C HETATM 2503 C1B SLQ A 331 61.102 -19.734 -15.393 0.99125.95 C C HETATM 2504 N1 SLQ A 331 55.336 -17.504 -11.365 0.99 90.63 C N HETATM 2505 N1B SLQ A 331 61.824 -18.944 -16.267 0.99118.45 C N HETATM 2506 O1 SLQ A 331 52.564 -20.630 -12.495 0.99115.37 C O HETATM 2507 C2 SLQ A 331 53.986 -17.467 -11.485 0.99 91.04 C C HETATM 2508 C2B SLQ A 331 60.934 -21.108 -15.634 0.99127.96 C C HETATM 2509 N2 SLQ A 331 53.185 -18.583 -11.030 0.99 96.76 C N HETATM 2510 C3B SLQ A 331 61.513 -21.667 -16.746 0.99129.35 C C HETATM 2511 N3 SLQ A 331 53.386 -16.335 -11.937 0.99 97.59 C N HETATM 2512 C4 SLQ A 331 54.122 -15.261 -12.274 0.99 93.44 C C HETATM 2513 C4B SLQ A 331 62.237 -20.874 -17.609 0.99128.52 C C HETATM 2514 C5 SLQ A 331 55.473 -15.304 -12.161 0.99 91.42 C C HETATM 2515 C5B SLQ A 331 62.399 -19.498 -17.376 0.99117.02 C C HETATM 2516 C6 SLQ A 331 56.067 -16.441 -11.700 0.99 93.26 C C HETATM 2517 N6 SLQ A 331 57.489 -16.504 -11.496 0.99 98.72 C N HETATM 2518 N7 SLQ A 331 55.961 -14.132 -12.560 0.99 88.25 C N HETATM 2519 C8 SLQ A 331 54.916 -13.357 -12.926 0.99 85.52 C C HETATM 2520 C9 SLQ A 331 52.420 -13.606 -12.980 0.99 86.45 C C HETATM 2521 N9 SLQ A 331 53.781 -14.061 -12.744 0.99 85.43 C N HETATM 2522 C10 SLQ A 331 51.679 -14.328 -14.104 0.99 88.90 C C HETATM 2523 C11 SLQ A 331 51.593 -13.467 -11.705 0.99 79.25 C C HETATM 2524 C12 SLQ A 331 52.057 -19.299 -10.465 0.99109.34 C C HETATM 2525 C13 SLQ A 331 50.789 -18.439 -10.557 0.99108.99 C C HETATM 2526 C14 SLQ A 331 49.479 -19.114 -10.156 0.99110.16 C C HETATM 2527 C15 SLQ A 331 51.879 -20.558 -11.275 0.99117.92 C C HETATM 2528 O HOH A 332 62.355 -6.104 0.809 1.00 72.90 D O HETATM 2529 O HOH A 333 42.660 -10.598 8.086 1.00 43.58 D O HETATM 2530 O HOH A 334 33.431 -12.365 -6.796 1.00 49.80 D O HETATM 2531 O HOH A 335 66.983 -19.127 9.823 1.00 69.78 D O HETATM 2532 O HOH A 336 48.644 -14.349 -10.831 1.00 55.67 D O HETATM 2533 O HOH B 260 25.616 11.020 -30.075 1.00 62.00 E O HETATM 2534 O HOH B 261 31.830 3.562 -14.505 1.00 82.88 E O HETATM 2535 O HOH B 262 8.048 -9.910 -28.664 1.00 75.16 E O HETATM 2536 O HOH B 263 9.061 -15.394 -31.342 1.00 68.43 E O CONECT 1329 1339 CONECT 1339 1329 1340 CONECT 1340 1339 1341 1343 CONECT 1341 1340 1342 1350 CONECT 1342 1341 CONECT 1343 1340 1344 1345 CONECT 1344 1343 CONECT 1345 1343 1346 CONECT 1346 1345 1347 1348 1349 CONECT 1347 1346 CONECT 1348 1346 CONECT 1349 1346 CONECT 1350 1341 CONECT 2496 2502 2517 CONECT 2497 2498 2502 CONECT 2498 2497 2499 CONECT 2499 2498 2500 2503 CONECT 2500 2499 2501 CONECT 2501 2500 2502 CONECT 2502 2496 2497 2501 CONECT 2503 2499 2505 2508 CONECT 2504 2507 2516 CONECT 2505 2503 2515 CONECT 2506 2527 CONECT 2507 2504 2509 2511 CONECT 2508 2503 2510 CONECT 2509 2507 2524 CONECT 2510 2508 2513 CONECT 2511 2507 2512 CONECT 2512 2511 2514 2521 CONECT 2513 2510 2515 CONECT 2514 2512 2516 2518 CONECT 2515 2505 2513 CONECT 2516 2504 2514 2517 CONECT 2517 2516 2496 CONECT 2518 2514 2519 CONECT 2519 2518 2521 CONECT 2520 2521 2522 2523 CONECT 2521 2512 2519 2520 CONECT 2522 2520 CONECT 2523 2520 CONECT 2524 2509 2525 2527 CONECT 2525 2524 2526 CONECT 2526 2525 CONECT 2527 2506 2524 END If you find results from this site helpful for your research, please cite one of our papers:
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