ATOM 1 N THR A 3 -28.726 29.519 29.425 1.00 75.39 N1+ ANISOU 1 N THR A 3 11263 10585 6798 640 -574 -144 N1+ ATOM 2 CA THR A 3 -27.475 28.877 28.888 1.00 75.90 C ANISOU 2 CA THR A 3 11321 10776 6740 857 -720 -91 C ATOM 3 C THR A 3 -27.875 27.657 28.019 1.00 75.91 C ANISOU 3 C THR A 3 11533 10589 6721 978 -642 70 C ATOM 4 O THR A 3 -27.235 27.450 26.991 1.00 74.23 O ANISOU 4 O THR A 3 11265 10386 6555 1091 -700 115 O ATOM 5 CB THR A 3 -26.434 28.449 29.962 1.00 77.44 C ANISOU 5 CB THR A 3 11570 11188 6665 1004 -861 -134 C ATOM 6 CG2 THR A 3 -25.858 29.646 30.734 1.00 76.98 C ANISOU 6 CG2 THR A 3 11279 11336 6633 870 -958 -319 C ATOM 7 OG1 THR A 3 -26.986 27.556 30.918 1.00 78.83 O ANISOU 7 OG1 THR A 3 12016 11259 6677 1022 -762 -73 O ATOM 8 N ASN A 4 -28.882 26.862 28.435 1.00 76.47 N ANISOU 8 N ASN A 4 11851 10481 6721 947 -498 153 N ATOM 9 CA ASN A 4 -29.289 25.597 27.802 1.00 77.68 C ANISOU 9 CA ASN A 4 12222 10418 6874 1007 -394 295 C ATOM 10 C ASN A 4 -29.844 25.742 26.371 1.00 74.64 C ANISOU 10 C ASN A 4 11710 9902 6747 867 -316 292 C ATOM 11 O ASN A 4 -29.778 24.771 25.620 1.00 74.54 O ANISOU 11 O ASN A 4 11821 9745 6756 928 -273 379 O ATOM 12 CB ASN A 4 -30.314 24.868 28.706 1.00 79.91 C ANISOU 12 CB ASN A 4 12775 10543 7044 946 -227 370 C ATOM 13 CG ASN A 4 -29.749 24.457 30.072 1.00 85.70 C ANISOU 13 CG ASN A 4 13723 11367 7473 1141 -295 424 C ATOM 14 ND2 ASN A 4 -29.673 23.152 30.336 1.00 87.24 N ANISOU 14 ND2 ASN A 4 13785 11812 7552 1291 -496 355 N ATOM 15 OD1 ASN A 4 -29.398 25.309 30.887 1.00 87.75 O ANISOU 15 OD1 ASN A 4 14264 11483 7593 1154 -166 529 O ATOM 16 N SER A 5 -30.364 26.931 26.059 1.00 70.74 N ANISOU 16 N SER A 5 10985 9453 6438 687 -297 192 N ATOM 17 CA SER A 5 -30.868 27.364 24.764 1.00 65.20 C ANISOU 17 CA SER A 5 10147 8656 5970 556 -233 185 C ATOM 18 C SER A 5 -29.761 27.508 23.705 1.00 64.67 C ANISOU 18 C SER A 5 9888 8705 5979 631 -360 155 C ATOM 19 O SER A 5 -30.015 27.261 22.528 1.00 66.49 O ANISOU 19 O SER A 5 10111 8847 6307 634 -334 197 O ATOM 20 CB SER A 5 -31.610 28.691 25.022 1.00 0.00 C ATOM 21 OG SER A 5 -30.847 29.551 25.869 1.00 0.00 O ATOM 22 N SER A 6 -28.548 27.860 24.145 1.00 63.07 N ANISOU 22 N SER A 6 9527 8710 5728 680 -493 74 N ATOM 23 CA SER A 6 -27.368 27.964 23.298 1.00 66.34 C ANISOU 23 CA SER A 6 9740 9264 6201 747 -604 41 C ATOM 24 C SER A 6 -26.583 26.638 23.241 1.00 67.41 C ANISOU 24 C SER A 6 9979 9435 6199 993 -685 111 C ATOM 25 O SER A 6 -25.547 26.612 22.587 1.00 66.94 O ANISOU 25 O SER A 6 9793 9441 6201 1062 -736 107 O ATOM 26 CB SER A 6 -26.482 29.120 23.811 1.00 73.70 C ANISOU 26 CB SER A 6 10462 10418 7122 696 -711 -81 C ATOM 27 OG SER A 6 -27.120 30.372 23.604 1.00 78.95 O ANISOU 27 OG SER A 6 11073 11023 7899 489 -629 -149 O ATOM 28 N LEU A 7 -27.040 25.565 23.903 1.00 71.40 N ANISOU 28 N LEU A 7 10721 9896 6510 1139 -688 181 N ATOM 29 CA LEU A 7 -26.352 24.274 23.921 1.00 73.94 C ANISOU 29 CA LEU A 7 11188 10220 6687 1406 -754 264 C ATOM 30 C LEU A 7 -27.131 23.290 23.023 1.00 75.59 C ANISOU 30 C LEU A 7 11589 10159 6972 1395 -626 355 C ATOM 31 O LEU A 7 -28.276 22.986 23.364 1.00 72.26 O ANISOU 31 O LEU A 7 11384 9531 6543 1294 -491 416 O ATOM 32 CB LEU A 7 -26.309 23.762 25.381 1.00 0.00 C ATOM 33 CG LEU A 7 -25.375 24.571 26.312 1.00 0.00 C ATOM 34 CD1 LEU A 7 -25.591 24.192 27.794 1.00 0.00 C ATOM 35 CD2 LEU A 7 -23.891 24.472 25.892 1.00 0.00 C ATOM 36 N PRO A 8 -26.545 22.808 21.899 1.00 78.50 N ANISOU 36 N PRO A 8 11885 10529 7413 1483 -657 356 N ATOM 37 CA PRO A 8 -27.190 21.760 21.091 1.00 82.05 C ANISOU 37 CA PRO A 8 12530 10720 7928 1463 -540 422 C ATOM 38 C PRO A 8 -27.289 20.440 21.872 1.00 89.09 C ANISOU 38 C PRO A 8 13776 11443 8633 1660 -506 536 C ATOM 39 O PRO A 8 -26.300 20.008 22.465 1.00 92.79 O ANISOU 39 O PRO A 8 14303 12032 8920 1919 -616 570 O ATOM 40 CB PRO A 8 -26.298 21.639 19.845 1.00 81.07 C ANISOU 40 CB PRO A 8 12225 10687 7891 1545 -603 379 C ATOM 41 CG PRO A 8 -24.926 22.101 20.300 1.00 80.85 C ANISOU 41 CG PRO A 8 12003 10953 7764 1722 -763 332 C ATOM 42 CD PRO A 8 -25.253 23.187 21.321 1.00 80.56 C ANISOU 42 CD PRO A 8 11883 11035 7692 1598 -792 287 C ATOM 43 N THR A 9 -28.492 19.862 21.897 1.00 94.45 N ANISOU 43 N THR A 9 14691 11842 9352 1535 -349 594 N ATOM 44 CA THR A 9 -28.781 18.596 22.580 1.00102.53 C ANISOU 44 CA THR A 9 16099 12651 10208 1677 -277 714 C ATOM 45 C THR A 9 -27.912 17.417 22.085 1.00106.44 C ANISOU 45 C THR A 9 16723 13068 10651 1933 -322 750 C ATOM 46 O THR A 9 -27.917 17.097 20.896 1.00105.91 O ANISOU 46 O THR A 9 16609 12909 10723 1859 -281 706 O ATOM 47 CB THR A 9 -30.296 18.236 22.525 1.00 0.00 C ATOM 48 CG2 THR A 9 -30.919 18.152 21.119 1.00 0.00 C ATOM 49 OG1 THR A 9 -30.558 16.999 23.166 1.00 0.00 O ATOM 50 N ASN A 10 -27.170 16.812 23.029 1.00104.46 N ANISOU 50 N ASN A 10 16637 12862 10189 2250 -408 828 N ATOM 51 CA ASN A 10 -26.264 15.692 22.786 1.00103.95 C ANISOU 51 CA ASN A 10 16709 12739 10047 2559 -458 869 C ATOM 52 C ASN A 10 -27.042 14.371 22.910 1.00102.64 C ANISOU 52 C ASN A 10 16984 12174 9841 2555 -289 972 C ATOM 53 O ASN A 10 -26.901 13.652 23.900 1.00106.21 O ANISOU 53 O ASN A 10 17762 12487 10104 2705 -250 1097 O ATOM 54 CB ASN A 10 -25.054 15.793 23.751 1.00108.45 C ANISOU 54 CB ASN A 10 17260 13546 10398 2921 -628 911 C ATOM 55 CG ASN A 10 -23.814 15.050 23.236 1.00113.42 C ANISOU 55 CG ASN A 10 18001 14149 10943 3287 -689 948 C ATOM 56 ND2 ASN A 10 -22.710 15.773 23.037 1.00114.76 N ANISOU 56 ND2 ASN A 10 17832 14631 11140 3435 -837 856 N ATOM 57 OD1 ASN A 10 -23.850 13.841 23.017 1.00116.40 O ANISOU 57 OD1 ASN A 10 18772 14227 11227 3436 -596 1057 O ATOM 58 N ILE A 11 -27.862 14.087 21.885 1.00 99.14 N ANISOU 58 N ILE A 11 16565 11542 9564 2378 -186 919 N ATOM 59 CA ILE A 11 -28.667 12.870 21.776 1.00100.69 C ANISOU 59 CA ILE A 11 17172 11344 9741 2320 -12 992 C ATOM 60 C ILE A 11 -27.820 11.602 21.510 1.00105.11 C ANISOU 60 C ILE A 11 18033 11747 10157 2693 -34 1067 C ATOM 61 O ILE A 11 -28.283 10.505 21.819 1.00107.56 O ANISOU 61 O ILE A 11 18735 11696 10435 2670 116 1131 O ATOM 62 CB ILE A 11 -29.763 13.029 20.682 1.00 0.00 C ATOM 63 CG1 ILE A 11 -30.871 11.955 20.768 1.00 0.00 C ATOM 64 CG2 ILE A 11 -29.201 13.104 19.246 1.00 0.00 C ATOM 65 CD1 ILE A 11 -31.631 11.943 22.104 1.00 0.00 C ATOM 66 N SER A 12 -26.579 11.776 21.018 1.00107.74 N ANISOU 66 N SER A 12 18193 12340 10401 3034 -209 1055 N ATOM 67 CA SER A 12 -25.576 10.722 20.833 1.00111.23 C ANISOU 67 CA SER A 12 18926 12664 10673 3454 -242 1143 C ATOM 68 C SER A 12 -25.196 10.006 22.148 1.00116.35 C ANISOU 68 C SER A 12 19878 13252 11077 3679 -251 1306 C ATOM 69 O SER A 12 -24.898 8.813 22.112 1.00122.24 O ANISOU 69 O SER A 12 20988 13794 11666 4005 -230 1417 O ATOM 70 CB SER A 12 -24.323 11.339 20.179 1.00 0.00 C ATOM 71 OG SER A 12 -24.624 11.878 18.907 1.00 0.00 O ATOM 72 N GLY A 13 -25.251 10.738 23.276 1.00115.59 N ANISOU 72 N GLY A 13 19659 13325 10936 3523 -279 1323 N ATOM 73 CA GLY A 13 -25.071 10.220 24.633 1.00119.98 C ANISOU 73 CA GLY A 13 20502 13844 11243 3708 -284 1475 C ATOM 74 C GLY A 13 -26.370 10.328 25.454 1.00118.77 C ANISOU 74 C GLY A 13 20612 13427 11090 3380 -82 1547 C ATOM 75 O GLY A 13 -26.319 10.141 26.669 1.00121.53 O ANISOU 75 O GLY A 13 21228 13664 11286 3482 -24 1654 O ATOM 76 N GLY A 14 -27.515 10.653 24.822 1.00113.17 N ANISOU 76 N GLY A 14 19743 12649 10607 2955 36 1446 N ATOM 77 CA GLY A 14 -28.797 10.890 25.483 1.00112.75 C ANISOU 77 CA GLY A 14 19900 12373 10564 2630 240 1500 C ATOM 78 C GLY A 14 -29.460 9.567 25.888 1.00113.95 C ANISOU 78 C GLY A 14 20574 12073 10649 2646 435 1624 C ATOM 79 O GLY A 14 -29.407 8.584 25.148 1.00116.15 O ANISOU 79 O GLY A 14 20974 12162 10996 2730 460 1599 O ATOM 80 N THR A 15 -30.123 9.576 27.059 1.00113.26 N ANISOU 80 N THR A 15 20809 11806 10420 2556 587 1754 N ATOM 81 CA THR A 15 -30.772 8.412 27.664 1.00113.30 C ANISOU 81 CA THR A 15 21231 11404 10415 2516 790 1820 C ATOM 82 C THR A 15 -32.007 7.793 26.943 1.00111.87 C ANISOU 82 C THR A 15 21161 10936 10410 2099 998 1775 C ATOM 83 O THR A 15 -32.138 6.571 27.034 1.00114.31 O ANISOU 83 O THR A 15 21762 10910 10761 2066 1131 1775 O ATOM 84 CB THR A 15 -31.053 8.625 29.183 1.00 0.00 C ATOM 85 CG2 THR A 15 -32.071 9.729 29.507 1.00 0.00 C ATOM 86 OG1 THR A 15 -31.525 7.448 29.811 1.00 0.00 O ATOM 87 N PRO A 16 -32.835 8.544 26.164 1.00108.92 N ANISOU 87 N PRO A 16 20438 10744 10205 1747 1018 1661 N ATOM 88 CA PRO A 16 -33.916 7.901 25.386 1.00108.81 C ANISOU 88 CA PRO A 16 20388 10549 10407 1317 1196 1558 C ATOM 89 C PRO A 16 -33.458 7.303 24.037 1.00104.56 C ANISOU 89 C PRO A 16 19757 9940 10031 1323 1141 1432 C ATOM 90 O PRO A 16 -34.241 6.586 23.415 1.00102.43 O ANISOU 90 O PRO A 16 19549 9464 9907 1003 1291 1352 O ATOM 91 CB PRO A 16 -34.935 9.033 25.193 1.00 0.00 C ATOM 92 CG PRO A 16 -34.081 10.283 25.095 1.00 0.00 C ATOM 93 CD PRO A 16 -32.941 10.008 26.070 1.00 0.00 C ATOM 94 N ALA A 17 -32.219 7.612 23.616 1.00104.99 N ANISOU 94 N ALA A 17 19655 10177 10057 1669 934 1403 N ATOM 95 CA ALA A 17 -31.649 7.236 22.324 1.00106.59 C ANISOU 95 CA ALA A 17 19772 10340 10388 1718 877 1285 C ATOM 96 C ALA A 17 -30.607 6.108 22.403 1.00111.51 C ANISOU 96 C ALA A 17 20713 10808 10849 2164 818 1374 C ATOM 97 O ALA A 17 -29.985 5.806 21.385 1.00110.77 O ANISOU 97 O ALA A 17 20439 10860 10788 2397 675 1298 O ATOM 98 CB ALA A 17 -31.060 8.496 21.681 1.00 0.00 C ATOM 99 N VAL A 18 -30.451 5.483 23.584 1.00117.30 N ANISOU 99 N VAL A 18 21929 11242 11396 2301 939 1543 N ATOM 100 CA VAL A 18 -29.565 4.337 23.822 1.00119.64 C ANISOU 100 CA VAL A 18 22529 11392 11538 2741 897 1623 C ATOM 101 C VAL A 18 -29.979 3.049 23.073 1.00120.04 C ANISOU 101 C VAL A 18 22890 11053 11664 2676 1044 1558 C ATOM 102 O VAL A 18 -29.139 2.164 22.905 1.00122.32 O ANISOU 102 O VAL A 18 23283 11301 11891 3028 981 1544 O ATOM 103 CB VAL A 18 -29.466 4.003 25.337 1.00 0.00 C ATOM 104 CG1 VAL A 18 -28.850 5.169 26.127 1.00 0.00 C ATOM 105 CG2 VAL A 18 -30.788 3.533 25.979 1.00 0.00 C ATOM 106 N SER A 19 -31.244 2.978 22.620 1.00113.88 N ANISOU 106 N SER A 19 22238 10012 11017 2225 1240 1504 N ATOM 107 CA SER A 19 -31.774 1.919 21.762 1.00112.76 C ANISOU 107 CA SER A 19 22402 9495 10945 2089 1401 1421 C ATOM 108 C SER A 19 -31.166 1.961 20.347 1.00105.08 C ANISOU 108 C SER A 19 21368 8529 10027 2329 1285 1317 C ATOM 109 O SER A 19 -30.773 3.029 19.872 1.00104.60 O ANISOU 109 O SER A 19 20885 8826 10033 2432 1096 1243 O ATOM 110 CB SER A 19 -33.315 2.024 21.749 1.00116.84 C ANISOU 110 CB SER A 19 22926 9841 11628 1519 1589 1336 C ATOM 111 OG SER A 19 -33.787 3.126 20.995 1.00116.84 O ANISOU 111 OG SER A 19 22440 10146 11809 1315 1473 1183 O ATOM 112 N ALA A 20 -31.127 0.785 19.698 1.00 97.13 N ANISOU 112 N ALA A 20 20678 7220 9007 2383 1395 1260 N ATOM 113 CA ALA A 20 -30.577 0.582 18.356 1.00 99.48 C ANISOU 113 CA ALA A 20 20939 7514 9343 2626 1303 1149 C ATOM 114 C ALA A 20 -31.254 1.407 17.246 1.00 93.48 C ANISOU 114 C ALA A 20 19878 6851 8789 2313 1266 973 C ATOM 115 O ALA A 20 -30.581 1.741 16.274 1.00 93.27 O ANISOU 115 O ALA A 20 19571 7060 8808 2505 1121 860 O ATOM 116 CB ALA A 20 -30.623 -0.916 18.019 1.00107.55 C ANISOU 116 CB ALA A 20 22373 8184 10307 2686 1456 1112 C ATOM 117 N GLY A 21 -32.548 1.741 17.415 1.00 87.71 N ANISOU 117 N GLY A 21 19068 6070 8187 1795 1389 905 N ATOM 118 CA GLY A 21 -33.344 2.519 16.465 1.00 82.02 C ANISOU 118 CA GLY A 21 17901 5603 7661 1465 1329 701 C ATOM 119 C GLY A 21 -32.786 3.939 16.304 1.00 75.13 C ANISOU 119 C GLY A 21 16459 5255 6832 1559 1117 689 C ATOM 120 O GLY A 21 -32.393 4.311 15.200 1.00 72.93 O ANISOU 120 O GLY A 21 15841 5229 6639 1599 989 556 O ATOM 121 N TYR A 22 -32.715 4.707 17.407 1.00 77.98 N ANISOU 121 N TYR A 22 16724 5779 7125 1591 1086 824 N ATOM 122 CA TYR A 22 -32.166 6.068 17.432 1.00 79.14 C ANISOU 122 CA TYR A 22 16362 6400 7307 1673 894 810 C ATOM 123 C TYR A 22 -30.651 6.132 17.178 1.00 81.27 C ANISOU 123 C TYR A 22 16512 6877 7490 2143 712 820 C ATOM 124 O TYR A 22 -30.193 7.117 16.599 1.00 68.22 O ANISOU 124 O TYR A 22 14411 5603 5907 2181 557 747 O ATOM 125 CB TYR A 22 -32.502 6.741 18.772 1.00 80.84 C ANISOU 125 CB TYR A 22 16551 6719 7445 1622 908 944 C ATOM 126 CG TYR A 22 -33.959 7.118 18.956 1.00 83.00 C ANISOU 126 CG TYR A 22 16612 7065 7858 1154 1000 883 C ATOM 127 CD1 TYR A 22 -34.524 8.144 18.167 1.00 81.68 C ANISOU 127 CD1 TYR A 22 15951 7235 7848 983 892 758 C ATOM 128 CD2 TYR A 22 -34.749 6.473 19.930 1.00 86.09 C ANISOU 128 CD2 TYR A 22 17295 7195 8220 896 1202 957 C ATOM 129 CE1 TYR A 22 -35.870 8.516 18.347 1.00 83.51 C ANISOU 129 CE1 TYR A 22 15981 7546 8203 593 971 703 C ATOM 130 CE2 TYR A 22 -36.094 6.847 20.112 1.00 87.65 C ANISOU 130 CE2 TYR A 22 17271 7487 8543 484 1289 894 C ATOM 131 CZ TYR A 22 -36.656 7.869 19.320 1.00 87.60 C ANISOU 131 CZ TYR A 22 16766 7824 8692 348 1168 766 C ATOM 132 OH TYR A 22 -37.958 8.235 19.495 1.00 89.76 O ANISOU 132 OH TYR A 22 16813 8204 9087 -25 1251 705 O ATOM 133 N LEU A 23 -29.910 5.088 17.590 1.00 85.26 N ANISOU 133 N LEU A 23 17410 7141 7844 2507 737 913 N ATOM 134 CA LEU A 23 -28.469 4.956 17.370 1.00 83.48 C ANISOU 134 CA LEU A 23 17060 7134 7522 2983 568 925 C ATOM 135 C LEU A 23 -28.115 4.826 15.877 1.00 83.99 C ANISOU 135 C LEU A 23 16915 7296 7700 2994 518 750 C ATOM 136 O LEU A 23 -27.202 5.515 15.422 1.00 81.91 O ANISOU 136 O LEU A 23 16261 7409 7455 3172 357 695 O ATOM 137 CB LEU A 23 -27.940 3.777 18.217 1.00 0.00 C ATOM 138 CG LEU A 23 -26.419 3.506 18.138 1.00 0.00 C ATOM 139 CD1 LEU A 23 -25.581 4.729 18.568 1.00 0.00 C ATOM 140 CD2 LEU A 23 -26.052 2.234 18.932 1.00 0.00 C ATOM 141 N PHE A 24 -28.865 3.991 15.137 1.00 83.82 N ANISOU 141 N PHE A 24 17153 6945 7751 2792 661 653 N ATOM 142 CA PHE A 24 -28.710 3.835 13.689 1.00 82.51 C ANISOU 142 CA PHE A 24 16810 6865 7674 2794 621 478 C ATOM 143 C PHE A 24 -29.223 5.041 12.884 1.00 82.35 C ANISOU 143 C PHE A 24 16297 7173 7819 2434 553 358 C ATOM 144 O PHE A 24 -28.642 5.322 11.841 1.00 82.69 O ANISOU 144 O PHE A 24 16042 7460 7917 2495 460 243 O ATOM 145 CB PHE A 24 -29.365 2.523 13.203 1.00 0.00 C ATOM 146 CG PHE A 24 -28.758 1.220 13.709 1.00 0.00 C ATOM 147 CD1 PHE A 24 -27.361 1.060 13.870 1.00 0.00 C ATOM 148 CD2 PHE A 24 -29.587 0.086 13.857 1.00 0.00 C ATOM 149 CE1 PHE A 24 -26.840 -0.167 14.256 1.00 0.00 C ATOM 150 CE2 PHE A 24 -29.045 -1.133 14.243 1.00 0.00 C ATOM 151 CZ PHE A 24 -27.679 -1.256 14.451 1.00 0.00 C ATOM 152 N LEU A 25 -30.248 5.755 13.386 1.00 81.85 N ANISOU 152 N LEU A 25 16141 7127 7831 2069 604 386 N ATOM 153 CA LEU A 25 -30.753 6.997 12.787 1.00 81.60 C ANISOU 153 CA LEU A 25 15645 7412 7947 1766 535 291 C ATOM 154 C LEU A 25 -29.742 8.156 12.856 1.00 80.84 C ANISOU 154 C LEU A 25 15135 7739 7840 1954 363 333 C ATOM 155 O LEU A 25 -29.688 8.938 11.908 1.00 78.89 O ANISOU 155 O LEU A 25 14500 7768 7708 1768 293 255 O ATOM 156 CB LEU A 25 -32.091 7.402 13.443 1.00 82.24 C ANISOU 156 CB LEU A 25 15745 7395 8109 1345 648 305 C ATOM 157 CG LEU A 25 -33.304 6.570 12.971 1.00 86.96 C ANISOU 157 CG LEU A 25 16648 7636 8758 1036 820 217 C ATOM 158 CD1 LEU A 25 -34.508 6.750 13.923 1.00 86.42 C ANISOU 158 CD1 LEU A 25 16526 7539 8770 624 926 230 C ATOM 159 CD2 LEU A 25 -33.663 6.854 11.494 1.00 87.12 C ANISOU 159 CD2 LEU A 25 16522 7715 8863 936 784 32 C ATOM 160 N ASP A 26 -28.947 8.220 13.940 1.00 83.64 N ANISOU 160 N ASP A 26 15568 8154 8057 2310 294 453 N ATOM 161 CA ASP A 26 -27.846 9.169 14.139 1.00 81.19 C ANISOU 161 CA ASP A 26 14862 8256 7729 2505 125 463 C ATOM 162 C ASP A 26 -26.705 8.914 13.128 1.00 82.92 C ANISOU 162 C ASP A 26 14956 8624 7925 2798 43 386 C ATOM 163 O ASP A 26 -26.234 9.854 12.487 1.00 82.90 O ANISOU 163 O ASP A 26 14551 8978 7969 2829 -73 334 O ATOM 164 CB ASP A 26 -27.351 9.117 15.609 1.00 0.00 C ATOM 165 CG ASP A 26 -26.321 10.178 16.020 1.00 0.00 C ATOM 166 OD1 ASP A 26 -26.219 11.211 15.322 1.00 0.00 O ATOM 167 OD2 ASP A 26 -25.692 9.962 17.079 1.00 0.00 O1- ATOM 168 N ILE A 27 -26.326 7.633 12.973 1.00 83.48 N ANISOU 168 N ILE A 27 15377 8420 7923 3010 112 375 N ATOM 169 CA ILE A 27 -25.313 7.160 12.025 1.00 83.20 C ANISOU 169 CA ILE A 27 15245 8507 7858 3297 56 290 C ATOM 170 C ILE A 27 -25.735 7.304 10.545 1.00 79.94 C ANISOU 170 C ILE A 27 14656 8142 7578 3026 88 131 C ATOM 171 O ILE A 27 -24.869 7.563 9.710 1.00 64.52 O ANISOU 171 O ILE A 27 12439 6443 5634 3166 17 50 O ATOM 172 CB ILE A 27 -24.907 5.686 12.346 1.00 89.97 C ANISOU 172 CB ILE A 27 16570 9034 8581 3652 127 334 C ATOM 173 CG1 ILE A 27 -24.177 5.583 13.708 1.00 92.56 C ANISOU 173 CG1 ILE A 27 17087 9324 8757 3929 91 511 C ATOM 174 CG2 ILE A 27 -24.107 4.943 11.250 1.00 91.18 C ANISOU 174 CG2 ILE A 27 16617 9335 8692 3994 74 245 C ATOM 175 CD1 ILE A 27 -22.847 6.348 13.804 1.00 92.36 C ANISOU 175 CD1 ILE A 27 16663 9760 8670 4186 -91 548 C ATOM 176 N ILE A 28 -27.042 7.201 10.249 1.00 78.31 N ANISOU 176 N ILE A 28 14576 7715 7464 2638 191 82 N ATOM 177 CA ILE A 28 -27.622 7.445 8.922 1.00 75.53 C ANISOU 177 CA ILE A 28 14079 7403 7216 2383 214 -72 C ATOM 178 C ILE A 28 -27.424 8.891 8.424 1.00 69.77 C ANISOU 178 C ILE A 28 12847 7101 6562 2310 98 -114 C ATOM 179 O ILE A 28 -27.191 9.067 7.230 1.00 69.29 O ANISOU 179 O ILE A 28 12648 7175 6504 2383 71 -217 O ATOM 180 CB ILE A 28 -29.127 7.025 8.865 1.00 0.00 C ATOM 181 CG1 ILE A 28 -29.240 5.491 8.704 1.00 0.00 C ATOM 182 CG2 ILE A 28 -30.009 7.722 7.800 1.00 0.00 C ATOM 183 CD1 ILE A 28 -30.601 4.909 9.125 1.00 0.00 C ATOM 184 N THR A 29 -27.453 9.885 9.335 1.00 66.62 N ANISOU 184 N THR A 29 12178 6918 6219 2170 35 -43 N ATOM 185 CA THR A 29 -27.140 11.281 9.009 1.00 64.95 C ANISOU 185 CA THR A 29 11519 7084 6076 2113 -63 -80 C ATOM 186 C THR A 29 -25.680 11.458 8.540 1.00 64.74 C ANISOU 186 C THR A 29 11320 7308 5972 2466 -148 -77 C ATOM 187 O THR A 29 -25.462 12.131 7.535 1.00 67.31 O ANISOU 187 O THR A 29 11348 7892 6336 2448 -194 -141 O ATOM 188 CB THR A 29 -27.463 12.286 10.161 1.00 0.00 C ATOM 189 CG2 THR A 29 -28.719 11.928 10.965 1.00 0.00 C ATOM 190 OG1 THR A 29 -26.404 12.549 11.067 1.00 0.00 O ATOM 191 N TYR A 30 -24.737 10.791 9.233 1.00 63.34 N ANISOU 191 N TYR A 30 11316 7074 5678 2791 -170 -2 N ATOM 192 CA TYR A 30 -23.301 10.789 8.946 1.00 62.83 C ANISOU 192 CA TYR A 30 11076 7266 5531 3151 -251 -11 C ATOM 193 C TYR A 30 -22.957 10.165 7.582 1.00 64.99 C ANISOU 193 C TYR A 30 11412 7500 5782 3288 -204 -123 C ATOM 194 O TYR A 30 -22.116 10.712 6.869 1.00 64.85 O ANISOU 194 O TYR A 30 11101 7781 5757 3412 -254 -178 O ATOM 195 CB TYR A 30 -22.561 10.093 10.107 1.00 0.00 C ATOM 196 CG TYR A 30 -21.045 10.176 10.062 1.00 0.00 C ATOM 197 CD1 TYR A 30 -20.286 9.180 9.410 1.00 0.00 C ATOM 198 CD2 TYR A 30 -20.390 11.255 10.684 1.00 0.00 C ATOM 199 CE1 TYR A 30 -18.880 9.272 9.380 1.00 0.00 C ATOM 200 CE2 TYR A 30 -18.985 11.341 10.666 1.00 0.00 C ATOM 201 CZ TYR A 30 -18.229 10.350 10.011 1.00 0.00 C ATOM 202 OH TYR A 30 -16.867 10.429 9.992 1.00 0.00 O ATOM 203 N LEU A 31 -23.634 9.055 7.240 1.00 67.75 N ANISOU 203 N LEU A 31 12147 7483 6114 3255 -100 -165 N ATOM 204 CA LEU A 31 -23.494 8.351 5.964 1.00 69.77 C ANISOU 204 CA LEU A 31 12492 7677 6341 3367 -46 -292 C ATOM 205 C LEU A 31 -24.003 9.178 4.773 1.00 66.24 C ANISOU 205 C LEU A 31 11772 7406 5989 3057 -49 -396 C ATOM 206 O LEU A 31 -23.356 9.164 3.726 1.00 65.51 O ANISOU 206 O LEU A 31 11510 7511 5869 3174 -57 -482 O ATOM 207 CB LEU A 31 -24.234 6.996 6.026 1.00 0.00 C ATOM 208 CG LEU A 31 -23.603 5.957 6.977 1.00 0.00 C ATOM 209 CD1 LEU A 31 -24.578 4.786 7.215 1.00 0.00 C ATOM 210 CD2 LEU A 31 -22.220 5.477 6.484 1.00 0.00 C ATOM 211 N VAL A 32 -25.125 9.899 4.955 1.00 64.96 N ANISOU 211 N VAL A 32 11562 7191 5928 2672 -38 -385 N ATOM 212 CA VAL A 32 -25.698 10.770 3.928 1.00 60.60 C ANISOU 212 CA VAL A 32 10749 6818 5456 2391 -51 -466 C ATOM 213 C VAL A 32 -24.850 12.043 3.695 1.00 57.12 C ANISOU 213 C VAL A 32 9887 6785 5030 2467 -135 -436 C ATOM 214 O VAL A 32 -24.727 12.454 2.542 1.00 58.78 O ANISOU 214 O VAL A 32 9913 7182 5239 2438 -138 -512 O ATOM 215 CB VAL A 32 -27.186 11.125 4.206 1.00 60.06 C ANISOU 215 CB VAL A 32 10689 6639 5491 1999 -30 -446 C ATOM 216 CG1 VAL A 32 -27.781 12.187 3.255 1.00 56.12 C ANISOU 216 CG1 VAL A 32 9892 6364 5066 1745 -65 -506 C ATOM 217 CG2 VAL A 32 -28.069 9.865 4.121 1.00 61.75 C ANISOU 217 CG2 VAL A 32 11309 6459 5694 1878 72 -501 C ATOM 218 N PHE A 33 -24.221 12.596 4.752 1.00 55.64 N ANISOU 218 N PHE A 33 9549 6745 4847 2557 -199 -331 N ATOM 219 CA PHE A 33 -23.250 13.698 4.646 1.00 57.65 C ANISOU 219 CA PHE A 33 9416 7379 5111 2630 -270 -313 C ATOM 220 C PHE A 33 -21.985 13.301 3.855 1.00 64.47 C ANISOU 220 C PHE A 33 10229 8392 5875 2975 -271 -368 C ATOM 221 O PHE A 33 -21.468 14.127 3.103 1.00 66.32 O ANISOU 221 O PHE A 33 10152 8933 6114 2993 -291 -397 O ATOM 222 CB PHE A 33 -22.816 14.196 6.046 1.00 0.00 C ATOM 223 CG PHE A 33 -23.886 14.700 7.005 1.00 0.00 C ATOM 224 CD1 PHE A 33 -23.681 14.563 8.394 1.00 0.00 C ATOM 225 CD2 PHE A 33 -24.995 15.447 6.560 1.00 0.00 C ATOM 226 CE1 PHE A 33 -24.595 15.082 9.299 1.00 0.00 C ATOM 227 CE2 PHE A 33 -25.895 15.971 7.483 1.00 0.00 C ATOM 228 CZ PHE A 33 -25.702 15.782 8.844 1.00 0.00 C ATOM 229 N ALA A 34 -21.524 12.051 4.043 1.00 66.44 N ANISOU 229 N ALA A 34 10785 8427 6031 3254 -238 -379 N ATOM 230 CA ALA A 34 -20.317 11.496 3.430 1.00 69.41 C ANISOU 230 CA ALA A 34 11126 8939 6308 3613 -228 -439 C ATOM 231 C ALA A 34 -20.455 11.217 1.923 1.00 70.74 C ANISOU 231 C ALA A 34 11264 9142 6470 3547 -162 -564 C ATOM 232 O ALA A 34 -19.511 11.505 1.186 1.00 71.94 O ANISOU 232 O ALA A 34 11138 9602 6592 3659 -168 -608 O ATOM 233 CB ALA A 34 -19.903 10.227 4.191 1.00 0.00 C ATOM 234 N VAL A 35 -21.617 10.697 1.482 1.00 69.66 N ANISOU 234 N VAL A 35 11414 8703 6352 3355 -96 -630 N ATOM 235 CA VAL A 35 -21.895 10.478 0.056 1.00 72.14 C ANISOU 235 CA VAL A 35 11719 9050 6643 3277 -41 -759 C ATOM 236 C VAL A 35 -22.218 11.790 -0.689 1.00 72.10 C ANISOU 236 C VAL A 35 11348 9340 6705 3001 -78 -750 C ATOM 237 O VAL A 35 -21.859 11.903 -1.860 1.00 74.71 O ANISOU 237 O VAL A 35 11523 9873 6990 3030 -51 -824 O ATOM 238 CB VAL A 35 -23.031 9.453 -0.212 1.00 75.49 C ANISOU 238 CB VAL A 35 12536 9081 7065 3115 31 -848 C ATOM 239 CG1 VAL A 35 -22.677 8.061 0.336 1.00 77.87 C ANISOU 239 CG1 VAL A 35 13237 9057 7291 3407 84 -848 C ATOM 240 CG2 VAL A 35 -24.431 9.893 0.247 1.00 76.16 C ANISOU 240 CG2 VAL A 35 12630 9049 7260 2720 12 -798 C ATOM 241 N THR A 36 -22.824 12.771 0.006 1.00 69.82 N ANISOU 241 N THR A 36 10928 9083 6518 2745 -128 -655 N ATOM 242 CA THR A 36 -23.077 14.115 -0.523 1.00 67.96 C ANISOU 242 CA THR A 36 10363 9113 6348 2510 -159 -629 C ATOM 243 C THR A 36 -21.781 14.939 -0.680 1.00 68.95 C ANISOU 243 C THR A 36 10161 9592 6447 2678 -181 -598 C ATOM 244 O THR A 36 -21.712 15.759 -1.594 1.00 65.79 O ANISOU 244 O THR A 36 9518 9424 6057 2558 -171 -603 O ATOM 245 CB THR A 36 -24.071 14.907 0.365 1.00 66.54 C ANISOU 245 CB THR A 36 10134 8868 6280 2231 -201 -538 C ATOM 246 CG2 THR A 36 -24.393 16.337 -0.096 1.00 63.00 C ANISOU 246 CG2 THR A 36 9390 8651 5897 1996 -223 -509 C ATOM 247 OG1 THR A 36 -25.303 14.216 0.416 1.00 68.14 O ANISOU 247 OG1 THR A 36 10624 8759 6506 2064 -168 -575 O ATOM 248 N PHE A 37 -20.770 14.672 0.168 1.00 72.48 N ANISOU 248 N PHE A 37 10595 10094 6850 2956 -208 -565 N ATOM 249 CA PHE A 37 -19.408 15.189 0.034 1.00 71.39 C ANISOU 249 CA PHE A 37 10128 10316 6680 3123 -225 -557 C ATOM 250 C PHE A 37 -18.732 14.762 -1.279 1.00 75.25 C ANISOU 250 C PHE A 37 10585 10934 7072 3316 -154 -659 C ATOM 251 O PHE A 37 -18.418 15.630 -2.091 1.00 76.97 O ANISOU 251 O PHE A 37 10531 11427 7286 3237 -125 -675 O ATOM 252 CB PHE A 37 -18.575 14.891 1.310 1.00 66.96 C ANISOU 252 CB PHE A 37 9553 9804 6084 3385 -289 -504 C ATOM 253 CG PHE A 37 -17.059 14.862 1.152 1.00 65.93 C ANISOU 253 CG PHE A 37 9091 10058 5904 3599 -307 -523 C ATOM 254 CD1 PHE A 37 -16.340 16.052 0.910 1.00 61.54 C ANISOU 254 CD1 PHE A 37 8170 9800 5412 3402 -331 -494 C ATOM 255 CD2 PHE A 37 -16.374 13.628 1.096 1.00 65.67 C ANISOU 255 CD2 PHE A 37 9107 10086 5760 3995 -292 -575 C ATOM 256 CE1 PHE A 37 -14.975 16.006 0.669 1.00 65.34 C ANISOU 256 CE1 PHE A 37 8326 10650 5849 3564 -337 -523 C ATOM 257 CE2 PHE A 37 -15.007 13.603 0.852 1.00 63.62 C ANISOU 257 CE2 PHE A 37 8505 10215 5454 4188 -307 -602 C ATOM 258 CZ PHE A 37 -14.311 14.787 0.644 1.00 62.37 C ANISOU 258 CZ PHE A 37 7967 10367 5363 3957 -328 -580 C ATOM 259 N VAL A 38 -18.523 13.445 -1.454 1.00 75.66 N ANISOU 259 N VAL A 38 10929 10781 7039 3572 -114 -730 N ATOM 260 CA VAL A 38 -17.749 12.882 -2.563 1.00 76.25 C ANISOU 260 CA VAL A 38 10987 10977 7009 3799 -39 -839 C ATOM 261 C VAL A 38 -18.426 13.040 -3.942 1.00 75.34 C ANISOU 261 C VAL A 38 10874 10865 6886 3549 18 -911 C ATOM 262 O VAL A 38 -17.729 13.362 -4.902 1.00 78.63 O ANISOU 262 O VAL A 38 11068 11558 7249 3577 68 -954 O ATOM 263 CB VAL A 38 -17.369 11.395 -2.300 1.00 77.53 C ANISOU 263 CB VAL A 38 11503 10875 7080 4144 -3 -901 C ATOM 264 CG1 VAL A 38 -18.566 10.427 -2.292 1.00 77.75 C ANISOU 264 CG1 VAL A 38 11938 10459 7145 3980 4 -900 C ATOM 265 CG2 VAL A 38 -16.286 10.875 -3.260 1.00 78.02 C ANISOU 265 CG2 VAL A 38 11594 11017 7031 4353 90 -1036 C ATOM 266 N LEU A 39 -19.762 12.890 -4.006 1.00 71.51 N ANISOU 266 N LEU A 39 10630 10094 6445 3298 13 -925 N ATOM 267 CA LEU A 39 -20.556 13.133 -5.216 1.00 69.72 C ANISOU 267 CA LEU A 39 10399 9893 6198 3062 45 -994 C ATOM 268 C LEU A 39 -20.749 14.632 -5.505 1.00 71.73 C ANISOU 268 C LEU A 39 10311 10430 6514 2822 18 -904 C ATOM 269 O LEU A 39 -21.017 14.986 -6.652 1.00 74.23 O ANISOU 269 O LEU A 39 10506 10926 6770 2746 58 -942 O ATOM 270 CB LEU A 39 -21.936 12.446 -5.090 1.00 67.09 C ANISOU 270 CB LEU A 39 10378 9213 5899 2840 37 -1040 C ATOM 271 CG LEU A 39 -21.896 10.905 -4.990 1.00 70.81 C ANISOU 271 CG LEU A 39 11254 9339 6313 3015 85 -1138 C ATOM 272 CD1 LEU A 39 -23.292 10.343 -4.646 1.00 72.21 C ANISOU 272 CD1 LEU A 39 11686 9226 6525 2714 88 -1206 C ATOM 273 CD2 LEU A 39 -21.291 10.249 -6.249 1.00 73.38 C ANISOU 273 CD2 LEU A 39 11648 9731 6503 3304 161 -1267 C ATOM 274 N GLY A 40 -20.619 15.480 -4.471 1.00 73.20 N ANISOU 274 N GLY A 40 10353 10651 6808 2707 -46 -784 N ATOM 275 CA GLY A 40 -20.781 16.923 -4.565 1.00 74.04 C ANISOU 275 CA GLY A 40 10176 10973 6982 2468 -64 -697 C ATOM 276 C GLY A 40 -19.527 17.559 -5.164 1.00 75.43 C ANISOU 276 C GLY A 40 10051 11499 7111 2572 -18 -687 C ATOM 277 O GLY A 40 -19.627 18.235 -6.185 1.00 74.94 O ANISOU 277 O GLY A 40 9834 11607 7034 2417 21 -665 O ATOM 278 N VAL A 41 -18.358 17.337 -4.540 1.00 78.75 N ANISOU 278 N VAL A 41 10380 12042 7502 2837 -16 -699 N ATOM 279 CA VAL A 41 -17.091 17.953 -4.946 1.00 80.56 C ANISOU 279 CA VAL A 41 10284 12633 7691 2921 35 -697 C ATOM 280 C VAL A 41 -16.544 17.422 -6.289 1.00 82.32 C ANISOU 280 C VAL A 41 10525 12966 7785 3039 135 -794 C ATOM 281 O VAL A 41 -15.897 18.188 -7.001 1.00 81.95 O ANISOU 281 O VAL A 41 10232 13202 7703 2980 206 -783 O ATOM 282 CB VAL A 41 -15.989 17.818 -3.858 1.00 82.02 C ANISOU 282 CB VAL A 41 10334 12957 7872 3180 -4 -694 C ATOM 283 CG1 VAL A 41 -16.414 18.479 -2.534 1.00 80.71 C ANISOU 283 CG1 VAL A 41 10147 12703 7815 3047 -104 -602 C ATOM 284 CG2 VAL A 41 -15.454 16.388 -3.633 1.00 84.65 C ANISOU 284 CG2 VAL A 41 10908 13145 8109 3540 5 -779 C ATOM 285 N LEU A 42 -16.838 16.154 -6.633 1.00 81.34 N ANISOU 285 N LEU A 42 10704 12618 7585 3194 155 -894 N ATOM 286 CA LEU A 42 -16.459 15.563 -7.917 1.00 82.30 C ANISOU 286 CA LEU A 42 10870 12832 7568 3314 252 -1005 C ATOM 287 C LEU A 42 -17.491 15.864 -9.012 1.00 77.65 C ANISOU 287 C LEU A 42 10335 12214 6954 3029 269 -1007 C ATOM 288 O LEU A 42 -17.081 16.170 -10.129 1.00 78.58 O ANISOU 288 O LEU A 42 10298 12573 6987 2992 346 -1017 O ATOM 289 CB LEU A 42 -16.246 14.040 -7.781 1.00 86.66 C ANISOU 289 CB LEU A 42 11745 13142 8041 3600 273 -1127 C ATOM 290 CG LEU A 42 -15.072 13.631 -6.861 1.00 91.26 C ANISOU 290 CG LEU A 42 12312 13755 8610 3965 262 -1134 C ATOM 291 CD1 LEU A 42 -15.029 12.102 -6.671 1.00 94.34 C ANISOU 291 CD1 LEU A 42 13075 13859 8911 4245 301 -1254 C ATOM 292 CD2 LEU A 42 -13.714 14.185 -7.341 1.00 92.99 C ANISOU 292 CD2 LEU A 42 12151 14401 8781 4136 317 -1135 C ATOM 293 N GLY A 43 -18.795 15.788 -8.691 1.00 74.14 N ANISOU 293 N GLY A 43 10105 11491 6574 2828 198 -996 N ATOM 294 CA GLY A 43 -19.879 15.965 -9.661 1.00 73.30 C ANISOU 294 CA GLY A 43 10050 11368 6433 2577 193 -1005 C ATOM 295 C GLY A 43 -19.980 17.421 -10.132 1.00 73.88 C ANISOU 295 C GLY A 43 9841 11692 6537 2377 203 -879 C ATOM 296 O GLY A 43 -20.085 17.660 -11.333 1.00 78.40 O ANISOU 296 O GLY A 43 10350 12435 7002 2324 260 -890 O ATOM 297 N ASN A 44 -19.912 18.384 -9.196 1.00 71.05 N ANISOU 297 N ASN A 44 9330 11349 6318 2263 153 -754 N ATOM 298 CA ASN A 44 -19.909 19.821 -9.491 1.00 69.63 C ANISOU 298 CA ASN A 44 8906 11371 6178 2069 173 -631 C ATOM 299 C ASN A 44 -18.518 20.330 -9.904 1.00 69.54 C ANISOU 299 C ASN A 44 8656 11673 6093 2184 279 -628 C ATOM 300 O ASN A 44 -18.451 21.370 -10.554 1.00 70.36 O ANISOU 300 O ASN A 44 8624 11954 6155 2048 343 -560 O ATOM 301 CB ASN A 44 -20.445 20.614 -8.283 1.00 67.94 C ANISOU 301 CB ASN A 44 8606 11079 6129 1924 102 -520 C ATOM 302 CG ASN A 44 -21.918 20.324 -8.001 1.00 65.91 C ANISOU 302 CG ASN A 44 8550 10545 5947 1778 14 -511 C ATOM 303 ND2 ASN A 44 -22.200 19.529 -6.969 1.00 63.70 N ANISOU 303 ND2 ASN A 44 8403 10071 5729 1858 -37 -537 N ATOM 304 OD1 ASN A 44 -22.794 20.820 -8.705 1.00 66.18 O ANISOU 304 OD1 ASN A 44 8617 10553 5977 1598 -4 -479 O ATOM 305 N GLY A 45 -17.446 19.582 -9.582 1.00 68.40 N ANISOU 305 N GLY A 45 8458 11606 5926 2438 304 -696 N ATOM 306 CA GLY A 45 -16.094 19.840 -10.080 1.00 67.02 C ANISOU 306 CA GLY A 45 8037 11755 5671 2561 415 -716 C ATOM 307 C GLY A 45 -15.998 19.538 -11.586 1.00 68.80 C ANISOU 307 C GLY A 45 8325 12088 5729 2614 517 -789 C ATOM 308 O GLY A 45 -15.296 20.252 -12.303 1.00 68.95 O ANISOU 308 O GLY A 45 8143 12375 5681 2559 624 -753 O ATOM 309 N LEU A 46 -16.746 18.527 -12.068 1.00 69.88 N ANISOU 309 N LEU A 46 8752 12014 5787 2705 491 -897 N ATOM 310 CA LEU A 46 -16.900 18.198 -13.485 1.00 72.16 C ANISOU 310 CA LEU A 46 9131 12390 5898 2739 577 -981 C ATOM 311 C LEU A 46 -17.764 19.223 -14.240 1.00 70.04 C ANISOU 311 C LEU A 46 8813 12195 5602 2457 581 -876 C ATOM 312 O LEU A 46 -17.483 19.453 -15.413 1.00 71.50 O ANISOU 312 O LEU A 46 8902 12612 5654 2447 689 -866 O ATOM 313 CB LEU A 46 -17.476 16.773 -13.638 1.00 74.46 C ANISOU 313 CB LEU A 46 9762 12407 6121 2855 536 -1133 C ATOM 314 CG LEU A 46 -16.479 15.639 -13.300 1.00 76.86 C ANISOU 314 CG LEU A 46 10179 12634 6390 3197 569 -1259 C ATOM 315 CD1 LEU A 46 -17.212 14.293 -13.112 1.00 78.72 C ANISOU 315 CD1 LEU A 46 10797 12529 6586 3239 527 -1395 C ATOM 316 CD2 LEU A 46 -15.326 15.542 -14.319 1.00 76.88 C ANISOU 316 CD2 LEU A 46 10029 12937 6246 3424 711 -1334 C ATOM 317 N VAL A 47 -18.765 19.843 -13.582 1.00 67.61 N ANISOU 317 N VAL A 47 8575 11700 5412 2241 471 -788 N ATOM 318 CA VAL A 47 -19.548 20.942 -14.167 1.00 67.62 C ANISOU 318 CA VAL A 47 8537 11762 5392 2001 464 -673 C ATOM 319 C VAL A 47 -18.712 22.228 -14.296 1.00 67.39 C ANISOU 319 C VAL A 47 8237 11971 5397 1908 555 -533 C ATOM 320 O VAL A 47 -18.777 22.874 -15.338 1.00 67.77 O ANISOU 320 O VAL A 47 8231 12177 5339 1811 632 -459 O ATOM 321 CB VAL A 47 -20.834 21.286 -13.359 1.00 68.07 C ANISOU 321 CB VAL A 47 8710 11571 5580 1816 326 -618 C ATOM 322 CG1 VAL A 47 -21.569 22.554 -13.858 1.00 66.75 C ANISOU 322 CG1 VAL A 47 8490 11476 5396 1602 314 -483 C ATOM 323 CG2 VAL A 47 -21.816 20.105 -13.317 1.00 69.14 C ANISOU 323 CG2 VAL A 47 9115 11483 5672 1866 255 -768 C ATOM 324 N ILE A 48 -17.926 22.560 -13.256 1.00 68.88 N ANISOU 324 N ILE A 48 8258 12189 5724 1929 554 -494 N ATOM 325 CA ILE A 48 -17.003 23.700 -13.241 1.00 70.72 C ANISOU 325 CA ILE A 48 8223 12656 5993 1827 652 -388 C ATOM 326 C ILE A 48 -15.922 23.611 -14.341 1.00 72.88 C ANISOU 326 C ILE A 48 8381 13213 6099 1946 810 -439 C ATOM 327 O ILE A 48 -15.552 24.642 -14.900 1.00 73.70 O ANISOU 327 O ILE A 48 8349 13501 6152 1806 925 -342 O ATOM 328 CB ILE A 48 -16.363 23.886 -11.829 1.00 70.75 C ANISOU 328 CB ILE A 48 8063 12662 6155 1850 609 -379 C ATOM 329 CG1 ILE A 48 -17.418 24.438 -10.841 1.00 71.02 C ANISOU 329 CG1 ILE A 48 8183 12450 6350 1677 482 -297 C ATOM 330 CG2 ILE A 48 -15.090 24.762 -11.770 1.00 70.65 C ANISOU 330 CG2 ILE A 48 7748 12937 6159 1770 729 -322 C ATOM 331 CD1 ILE A 48 -17.065 24.232 -9.361 1.00 71.63 C ANISOU 331 CD1 ILE A 48 8144 12510 6563 1714 418 -304 C ATOM 332 N TRP A 49 -15.495 22.380 -14.665 1.00 75.07 N ANISOU 332 N TRP A 49 8724 13519 6281 2210 831 -593 N ATOM 333 CA TRP A 49 -14.615 22.064 -15.782 1.00 80.63 C ANISOU 333 CA TRP A 49 9313 14504 6819 2354 990 -660 C ATOM 334 C TRP A 49 -15.332 22.163 -17.141 1.00 83.01 C ANISOU 334 C TRP A 49 9774 14835 6934 2300 1047 -664 C ATOM 335 O TRP A 49 -14.885 22.930 -17.992 1.00 85.75 O ANISOU 335 O TRP A 49 9992 15423 7165 2234 1192 -605 O ATOM 336 CB TRP A 49 -14.000 20.673 -15.542 1.00 84.53 C ANISOU 336 CB TRP A 49 9838 15006 7273 2688 992 -827 C ATOM 337 CG TRP A 49 -13.052 20.138 -16.576 1.00 90.82 C ANISOU 337 CG TRP A 49 10500 16104 7905 2875 1162 -914 C ATOM 338 CD1 TRP A 49 -11.980 20.789 -17.085 1.00 94.76 C ANISOU 338 CD1 TRP A 49 10684 16939 8380 2824 1307 -863 C ATOM 339 CD2 TRP A 49 -13.025 18.805 -17.167 1.00 95.43 C ANISOU 339 CD2 TRP A 49 11257 16683 8320 3140 1217 -1079 C ATOM 340 CE2 TRP A 49 -11.878 18.704 -18.012 1.00 99.94 C ANISOU 340 CE2 TRP A 49 11597 17611 8768 3256 1398 -1116 C ATOM 341 CE3 TRP A 49 -13.847 17.661 -17.062 1.00 96.07 C ANISOU 341 CE3 TRP A 49 11673 16487 8342 3279 1140 -1208 C ATOM 342 NE1 TRP A 49 -11.289 19.950 -17.936 1.00 99.37 N ANISOU 342 NE1 TRP A 49 11221 17747 8789 3048 1452 -980 N ATOM 343 CZ2 TRP A 49 -11.549 17.517 -18.690 1.00102.79 C ANISOU 343 CZ2 TRP A 49 12050 18061 8944 3529 1502 -1277 C ATOM 344 CZ3 TRP A 49 -13.530 16.464 -17.735 1.00 98.37 C ANISOU 344 CZ3 TRP A 49 12074 16849 8454 3537 1240 -1372 C ATOM 345 CH2 TRP A 49 -12.375 16.389 -18.535 1.00101.69 C ANISOU 345 CH2 TRP A 49 12259 17629 8749 3671 1418 -1405 C ATOM 346 N VAL A 50 -16.413 21.384 -17.330 1.00 82.10 N ANISOU 346 N VAL A 50 9937 14483 6773 2316 940 -735 N ATOM 347 CA VAL A 50 -17.119 21.253 -18.609 1.00 80.68 C ANISOU 347 CA VAL A 50 9916 14347 6391 2285 973 -768 C ATOM 348 C VAL A 50 -17.878 22.532 -19.009 1.00 79.25 C ANISOU 348 C VAL A 50 9716 14184 6212 2022 954 -586 C ATOM 349 O VAL A 50 -17.525 23.124 -20.023 1.00 82.46 O ANISOU 349 O VAL A 50 10046 14805 6479 1962 1078 -503 O ATOM 350 CB VAL A 50 -18.060 20.013 -18.664 1.00 77.73 C ANISOU 350 CB VAL A 50 9841 13727 5967 2378 862 -930 C ATOM 351 CG1 VAL A 50 -18.988 19.950 -19.899 1.00 78.17 C ANISOU 351 CG1 VAL A 50 10053 13845 5804 2323 874 -974 C ATOM 352 CG2 VAL A 50 -17.240 18.713 -18.603 1.00 78.09 C ANISOU 352 CG2 VAL A 50 9942 13741 5989 2670 905 -1105 C ATOM 353 N ALA A 51 -18.872 22.951 -18.210 1.00 74.97 N ANISOU 353 N ALA A 51 9252 13415 5818 1872 807 -514 N ATOM 354 CA ALA A 51 -19.672 24.156 -18.457 1.00 75.70 C ANISOU 354 CA ALA A 51 9349 13503 5910 1656 776 -342 C ATOM 355 C ALA A 51 -18.876 25.471 -18.345 1.00 78.54 C ANISOU 355 C ALA A 51 9490 14015 6335 1530 896 -170 C ATOM 356 O ALA A 51 -19.270 26.452 -18.971 1.00 79.51 O ANISOU 356 O ALA A 51 9615 14219 6376 1401 952 -26 O ATOM 357 CB ALA A 51 -20.886 24.177 -17.513 1.00 70.92 C ANISOU 357 CB ALA A 51 8850 12631 5464 1542 600 -315 C ATOM 358 N GLY A 52 -17.780 25.472 -17.566 1.00 78.46 N ANISOU 358 N GLY A 52 9298 14049 6465 1564 941 -185 N ATOM 359 CA GLY A 52 -16.988 26.669 -17.301 1.00 76.76 C ANISOU 359 CA GLY A 52 8869 13966 6331 1410 1052 -45 C ATOM 360 C GLY A 52 -15.831 26.877 -18.289 1.00 76.41 C ANISOU 360 C GLY A 52 8678 14224 6131 1439 1257 -37 C ATOM 361 O GLY A 52 -15.366 28.013 -18.390 1.00 77.63 O ANISOU 361 O GLY A 52 8748 14479 6269 1259 1375 114 O ATOM 362 N PHE A 53 -15.346 25.831 -18.990 1.00 78.54 N ANISOU 362 N PHE A 53 8928 14634 6283 1664 1314 -198 N ATOM 363 CA PHE A 53 -14.153 25.921 -19.849 1.00 85.87 C ANISOU 363 CA PHE A 53 9675 15879 7073 1712 1524 -211 C ATOM 364 C PHE A 53 -14.291 25.160 -21.175 1.00 89.33 C ANISOU 364 C PHE A 53 10252 16436 7253 1879 1601 -313 C ATOM 365 O PHE A 53 -13.949 25.729 -22.212 1.00 92.05 O ANISOU 365 O PHE A 53 10481 17046 7450 1871 1793 -285 O ATOM 366 CB PHE A 53 -12.876 25.463 -19.101 1.00 70.84 C ANISOU 366 CB PHE A 53 7517 14127 5272 1845 1567 -315 C ATOM 367 CG PHE A 53 -12.508 26.277 -17.874 1.00 69.38 C ANISOU 367 CG PHE A 53 7164 13879 5317 1676 1507 -232 C ATOM 368 CD1 PHE A 53 -11.876 27.530 -18.009 1.00 70.28 C ANISOU 368 CD1 PHE A 53 7063 14160 5479 1445 1643 -113 C ATOM 369 CD2 PHE A 53 -12.944 25.864 -16.596 1.00 74.00 C ANISOU 369 CD2 PHE A 53 7822 14234 6062 1736 1321 -279 C ATOM 370 CE1 PHE A 53 -11.639 28.312 -16.886 1.00107.16 C ANISOU 370 CE1 PHE A 53 11591 18769 10356 1276 1587 -58 C ATOM 371 CE2 PHE A 53 -12.702 26.661 -15.486 1.00 66.10 C ANISOU 371 CE2 PHE A 53 6676 13185 5256 1582 1264 -215 C ATOM 372 CZ PHE A 53 -12.046 27.877 -15.630 1.00 67.02 C ANISOU 372 CZ PHE A 53 6575 13470 5419 1351 1392 -112 C ATOM 373 N ARG A 54 -14.749 23.894 -21.138 1.00 87.72 N ANISOU 373 N ARG A 54 10291 16052 6986 2016 1469 -438 N ATOM 374 CA ARG A 54 -14.858 23.043 -22.333 1.00 88.57 C ANISOU 374 CA ARG A 54 10553 16261 6839 2165 1533 -557 C ATOM 375 C ARG A 54 -16.003 23.456 -23.277 1.00 86.43 C ANISOU 375 C ARG A 54 10479 15944 6417 2026 1485 -464 C ATOM 376 O ARG A 54 -15.855 23.314 -24.489 1.00 87.91 O ANISOU 376 O ARG A 54 10717 16324 6363 2062 1604 -472 O ATOM 377 CB ARG A 54 -14.983 21.550 -21.950 1.00 89.59 C ANISOU 377 CB ARG A 54 10850 16227 6964 2404 1432 -776 C ATOM 378 CG ARG A 54 -13.937 21.027 -20.942 1.00 92.63 C ANISOU 378 CG ARG A 54 11067 16656 7470 2603 1465 -873 C ATOM 379 CD ARG A 54 -12.494 20.984 -21.470 1.00 97.86 C ANISOU 379 CD ARG A 54 11549 17653 7982 2776 1676 -946 C ATOM 380 NE ARG A 54 -12.328 19.973 -22.523 1.00104.62 N ANISOU 380 NE ARG A 54 12611 18530 8609 2977 1727 -1118 N ATOM 381 CZ ARG A 54 -11.231 19.790 -23.276 1.00110.87 C ANISOU 381 CZ ARG A 54 13305 19564 9255 3207 1894 -1241 C ATOM 382 NH1 ARG A 54 -10.145 20.562 -23.126 1.00114.01 N1+ ANISOU 382 NH1 ARG A 54 13381 20200 9738 3250 2012 -1203 N1+ ATOM 383 NH2 ARG A 54 -11.221 18.816 -24.194 1.00112.40 N1+ ANISOU 383 NH2 ARG A 54 13723 19683 9300 3343 1904 -1388 N1+ ATOM 384 N MET A 55 -17.101 23.967 -22.701 1.00 83.64 N ANISOU 384 N MET A 55 10234 15359 6188 1880 1313 -379 N ATOM 385 CA MET A 55 -18.253 24.537 -23.396 1.00 84.73 C ANISOU 385 CA MET A 55 10537 15466 6190 1764 1244 -285 C ATOM 386 C MET A 55 -18.049 26.046 -23.601 1.00 85.22 C ANISOU 386 C MET A 55 10500 15670 6211 1595 1371 -47 C ATOM 387 O MET A 55 -17.385 26.696 -22.790 1.00 86.65 O ANISOU 387 O MET A 55 10481 15933 6510 1520 1497 44 O ATOM 388 CB MET A 55 -19.518 24.290 -22.546 1.00 86.31 C ANISOU 388 CB MET A 55 10861 15388 6546 1676 1022 -279 C ATOM 389 CG MET A 55 -19.905 22.808 -22.379 1.00 91.59 C ANISOU 389 CG MET A 55 11648 15870 7281 1806 904 -497 C ATOM 390 SD MET A 55 -20.569 22.014 -23.868 1.00101.46 S ANISOU 390 SD MET A 55 13145 17150 8255 1927 866 -714 S ATOM 391 CE MET A 55 -22.257 22.676 -23.863 1.00102.17 C ANISOU 391 CE MET A 55 13343 17207 8270 1739 712 -592 C ATOM 392 N THR A 56 -18.665 26.577 -24.670 1.00 84.55 N ANISOU 392 N THR A 56 10564 15613 5949 1533 1337 53 N ATOM 393 CA THR A 56 -18.678 28.000 -25.018 1.00 83.29 C ANISOU 393 CA THR A 56 10374 15536 5737 1378 1443 302 C ATOM 394 C THR A 56 -19.441 28.845 -23.977 1.00 80.55 C ANISOU 394 C THR A 56 10037 14958 5613 1227 1309 453 C ATOM 395 O THR A 56 -20.458 28.391 -23.452 1.00 79.66 O ANISOU 395 O THR A 56 10035 14675 5559 1241 1108 398 O ATOM 396 CB THR A 56 -19.362 28.209 -26.399 1.00 85.01 C ANISOU 396 CB THR A 56 10763 15904 5634 1414 1466 351 C ATOM 397 CG2 THR A 56 -19.478 29.667 -26.890 1.00 83.71 C ANISOU 397 CG2 THR A 56 10616 15776 5415 1264 1561 637 C ATOM 398 OG1 THR A 56 -18.649 27.480 -27.379 1.00 89.37 O ANISOU 398 OG1 THR A 56 11298 16690 5968 1547 1628 222 O ATOM 399 N HIS A 57 -18.941 30.067 -23.723 1.00 79.20 N ANISOU 399 N HIS A 57 9746 14783 5564 1075 1431 635 N ATOM 400 CA HIS A 57 -19.553 31.068 -22.848 1.00 76.96 C ANISOU 400 CA HIS A 57 9467 14274 5502 935 1330 774 C ATOM 401 C HIS A 57 -20.906 31.557 -23.402 1.00 76.33 C ANISOU 401 C HIS A 57 9575 14108 5318 926 1197 896 C ATOM 402 O HIS A 57 -20.945 32.280 -24.398 1.00 77.94 O ANISOU 402 O HIS A 57 9864 14405 5347 890 1292 1072 O ATOM 403 CB HIS A 57 -18.568 32.232 -22.592 1.00 0.00 C ATOM 404 CG HIS A 57 -17.984 32.904 -23.815 1.00 0.00 C ATOM 405 CD2 HIS A 57 -18.276 34.148 -24.337 1.00 0.00 C ATOM 406 ND1 HIS A 57 -17.006 32.299 -24.615 1.00 0.00 N ATOM 407 CE1 HIS A 57 -16.759 33.180 -25.576 1.00 0.00 C ATOM 408 NE2 HIS A 57 -17.483 34.294 -25.462 1.00 0.00 N ATOM 409 N THR A 58 -21.986 31.119 -22.745 1.00 75.94 N ANISOU 409 N THR A 58 9591 13893 5369 963 982 805 N ATOM 410 CA THR A 58 -23.376 31.456 -23.050 1.00 74.01 C ANISOU 410 CA THR A 58 9481 13565 5076 955 828 906 C ATOM 411 C THR A 58 -24.137 31.603 -21.720 1.00 71.53 C ANISOU 411 C THR A 58 9125 13007 5047 875 705 935 C ATOM 412 O THR A 58 -23.650 31.155 -20.683 1.00 69.84 O ANISOU 412 O THR A 58 8796 12697 5043 831 729 865 O ATOM 413 CB THR A 58 -24.072 30.351 -23.899 1.00 74.59 C ANISOU 413 CB THR A 58 9671 13716 4954 1073 681 736 C ATOM 414 CG2 THR A 58 -23.351 30.010 -25.213 1.00 75.27 C ANISOU 414 CG2 THR A 58 9811 14049 4738 1160 810 699 C ATOM 415 OG1 THR A 58 -24.296 29.155 -23.173 1.00 74.57 O ANISOU 415 OG1 THR A 58 9640 13602 5090 1114 582 507 O ATOM 416 N VAL A 59 -25.334 32.209 -21.771 1.00 71.62 N ANISOU 416 N VAL A 59 9224 12936 5053 867 568 1036 N ATOM 417 CA VAL A 59 -26.206 32.419 -20.608 1.00 67.38 C ANISOU 417 CA VAL A 59 8654 12179 4770 806 447 1050 C ATOM 418 C VAL A 59 -26.628 31.105 -19.907 1.00 67.46 C ANISOU 418 C VAL A 59 8629 12107 4897 837 327 813 C ATOM 419 O VAL A 59 -26.721 31.085 -18.679 1.00 68.93 O ANISOU 419 O VAL A 59 8746 12126 5316 779 297 782 O ATOM 420 CB VAL A 59 -27.480 33.215 -21.009 1.00 60.84 C ANISOU 420 CB VAL A 59 7916 11315 3886 829 319 1187 C ATOM 421 CG1 VAL A 59 -28.460 33.473 -19.844 1.00 58.68 C ANISOU 421 CG1 VAL A 59 7600 10829 3866 779 195 1179 C ATOM 422 CG2 VAL A 59 -27.103 34.537 -21.701 1.00 62.60 C ANISOU 422 CG2 VAL A 59 8206 11576 4002 810 452 1446 C ATOM 423 N THR A 60 -26.813 30.033 -20.697 1.00 67.82 N ANISOU 423 N THR A 60 8738 12258 4773 925 267 642 N ATOM 424 CA THR A 60 -27.130 28.680 -20.237 1.00 64.59 C ANISOU 424 CA THR A 60 8338 11746 4457 951 165 417 C ATOM 425 C THR A 60 -25.975 28.037 -19.439 1.00 63.88 C ANISOU 425 C THR A 60 8164 11613 4496 973 273 334 C ATOM 426 O THR A 60 -26.213 27.549 -18.334 1.00 61.46 O ANISOU 426 O THR A 60 7825 11138 4392 948 215 267 O ATOM 427 CB THR A 60 -27.465 27.752 -21.439 1.00 64.86 C ANISOU 427 CB THR A 60 8482 11898 4262 1031 95 245 C ATOM 428 CG2 THR A 60 -27.811 26.295 -21.083 1.00 62.55 C ANISOU 428 CG2 THR A 60 8238 11458 4072 1037 -8 20 C ATOM 429 OG1 THR A 60 -28.552 28.293 -22.168 1.00 67.38 O ANISOU 429 OG1 THR A 60 8859 12303 4440 1020 -17 326 O ATOM 430 N THR A 61 -24.754 28.068 -20.002 1.00 67.97 N ANISOU 430 N THR A 61 8637 12298 4892 1027 431 337 N ATOM 431 CA THR A 61 -23.548 27.493 -19.395 1.00 70.13 C ANISOU 431 CA THR A 61 8801 12577 5269 1073 529 252 C ATOM 432 C THR A 61 -23.032 28.309 -18.189 1.00 71.24 C ANISOU 432 C THR A 61 8809 12617 5641 961 565 373 C ATOM 433 O THR A 61 -22.488 27.704 -17.268 1.00 72.77 O ANISOU 433 O THR A 61 8915 12755 5977 990 570 287 O ATOM 434 CB THR A 61 -22.396 27.349 -20.428 1.00 69.32 C ANISOU 434 CB THR A 61 8651 12711 4976 1152 704 233 C ATOM 435 CG2 THR A 61 -22.744 26.486 -21.650 1.00 69.78 C ANISOU 435 CG2 THR A 61 8853 12862 4796 1273 669 83 C ATOM 436 OG1 THR A 61 -21.877 28.591 -20.867 1.00 69.67 O ANISOU 436 OG1 THR A 61 8655 12865 4951 1052 823 441 O ATOM 437 N ILE A 62 -23.251 29.637 -18.187 1.00 67.31 N ANISOU 437 N ILE A 62 8307 12091 5177 840 588 568 N ATOM 438 CA ILE A 62 -22.942 30.548 -17.079 1.00 65.22 C ANISOU 438 CA ILE A 62 7944 11702 5134 716 613 669 C ATOM 439 C ILE A 62 -23.856 30.323 -15.859 1.00 66.47 C ANISOU 439 C ILE A 62 8131 11649 5477 707 451 597 C ATOM 440 O ILE A 62 -23.365 30.373 -14.731 1.00 69.25 O ANISOU 440 O ILE A 62 8392 11917 6004 671 452 562 O ATOM 441 CB ILE A 62 -22.999 32.040 -17.538 1.00 64.25 C ANISOU 441 CB ILE A 62 7853 11568 4991 601 685 895 C ATOM 442 CG1 ILE A 62 -21.771 32.363 -18.420 1.00 65.53 C ANISOU 442 CG1 ILE A 62 7964 11928 5007 570 889 977 C ATOM 443 CG2 ILE A 62 -23.130 33.101 -16.417 1.00 64.00 C ANISOU 443 CG2 ILE A 62 7769 11351 5197 470 674 982 C ATOM 444 CD1 ILE A 62 -21.925 33.637 -19.262 1.00 68.56 C ANISOU 444 CD1 ILE A 62 8422 12282 5347 460 982 1213 C ATOM 445 N SER A 63 -25.149 30.047 -16.102 1.00 64.96 N ANISOU 445 N SER A 63 8056 11384 5240 734 314 568 N ATOM 446 CA SER A 63 -26.127 29.726 -15.060 1.00 63.07 C ANISOU 446 CA SER A 63 7846 10953 5166 712 176 499 C ATOM 447 C SER A 63 -25.826 28.392 -14.352 1.00 62.09 C ANISOU 447 C SER A 63 7719 10780 5091 791 152 314 C ATOM 448 O SER A 63 -25.991 28.305 -13.136 1.00 62.07 O ANISOU 448 O SER A 63 7681 10640 5262 764 117 287 O ATOM 449 CB SER A 63 -27.548 29.735 -15.652 1.00 0.00 C ATOM 450 OG SER A 63 -27.958 31.056 -15.937 1.00 0.00 O ATOM 451 N TYR A 64 -25.346 27.402 -15.125 1.00 63.15 N ANISOU 451 N TYR A 64 7909 11020 5065 902 175 185 N ATOM 452 CA TYR A 64 -24.928 26.083 -14.642 1.00 63.38 C ANISOU 452 CA TYR A 64 7972 10982 5125 1008 159 13 C ATOM 453 C TYR A 64 -23.565 26.112 -13.930 1.00 59.79 C ANISOU 453 C TYR A 64 7375 10572 4770 1048 251 24 C ATOM 454 O TYR A 64 -23.365 25.324 -13.006 1.00 60.57 O ANISOU 454 O TYR A 64 7477 10553 4983 1100 208 -53 O ATOM 455 CB TYR A 64 -24.896 25.098 -15.828 1.00 70.02 C ANISOU 455 CB TYR A 64 8918 11925 5762 1129 180 -132 C ATOM 456 CG TYR A 64 -26.210 24.816 -16.551 1.00 74.83 C ANISOU 456 CG TYR A 64 9670 12495 6269 1088 66 -195 C ATOM 457 CD1 TYR A 64 -27.465 25.241 -16.051 1.00 75.16 C ANISOU 457 CD1 TYR A 64 9734 12398 6427 971 -55 -154 C ATOM 458 CD2 TYR A 64 -26.165 24.109 -17.769 1.00 79.23 C ANISOU 458 CD2 TYR A 64 10325 13172 6605 1164 80 -309 C ATOM 459 CE1 TYR A 64 -28.644 24.998 -16.781 1.00 79.71 C ANISOU 459 CE1 TYR A 64 10405 12973 6907 925 -165 -225 C ATOM 460 CE2 TYR A 64 -27.344 23.855 -18.495 1.00 82.11 C ANISOU 460 CE2 TYR A 64 10804 13527 6867 1113 -35 -386 C ATOM 461 CZ TYR A 64 -28.583 24.311 -18.009 1.00 84.22 C ANISOU 461 CZ TYR A 64 11069 13673 7257 989 -161 -344 C ATOM 462 OH TYR A 64 -29.723 24.081 -18.724 1.00 88.54 O ANISOU 462 OH TYR A 64 11697 14246 7699 930 -282 -434 O ATOM 463 N LEU A 65 -22.668 27.022 -14.350 1.00 59.15 N ANISOU 463 N LEU A 65 7165 10671 4637 1021 379 119 N ATOM 464 CA LEU A 65 -21.360 27.255 -13.737 1.00 61.40 C ANISOU 464 CA LEU A 65 7277 11040 5014 1035 464 122 C ATOM 465 C LEU A 65 -21.494 27.834 -12.318 1.00 64.48 C ANISOU 465 C LEU A 65 7608 11277 5613 918 403 189 C ATOM 466 O LEU A 65 -20.890 27.283 -11.402 1.00 67.18 O ANISOU 466 O LEU A 65 7878 11594 6055 974 379 120 O ATOM 467 CB LEU A 65 -20.503 28.143 -14.673 1.00 63.00 C ANISOU 467 CB LEU A 65 7348 11468 5122 981 627 215 C ATOM 468 CG LEU A 65 -19.099 28.532 -14.151 1.00 65.18 C ANISOU 468 CG LEU A 65 7403 11871 5491 955 724 216 C ATOM 469 CD1 LEU A 65 -18.227 27.292 -13.876 1.00 65.86 C ANISOU 469 CD1 LEU A 65 7425 12059 5540 1168 730 48 C ATOM 470 CD2 LEU A 65 -18.412 29.528 -15.111 1.00 68.52 C ANISOU 470 CD2 LEU A 65 7708 12485 5839 832 898 334 C ATOM 471 N ASN A 66 -22.303 28.898 -12.159 1.00 62.87 N ANISOU 471 N ASN A 66 7441 10978 5468 769 376 321 N ATOM 472 CA ASN A 66 -22.583 29.547 -10.870 1.00 59.19 C ANISOU 472 CA ASN A 66 6943 10352 5193 660 319 375 C ATOM 473 C ASN A 66 -23.366 28.641 -9.903 1.00 56.67 C ANISOU 473 C ASN A 66 6715 9863 4953 729 191 265 C ATOM 474 O ASN A 66 -23.077 28.686 -8.707 1.00 58.11 O ANISOU 474 O ASN A 66 6841 9979 5260 724 162 237 O ATOM 475 CB ASN A 66 -23.322 30.880 -11.113 1.00 59.68 C ANISOU 475 CB ASN A 66 7062 10326 5289 526 312 529 C ATOM 476 CG ASN A 66 -22.388 32.025 -11.512 1.00 62.08 C ANISOU 476 CG ASN A 66 7268 10703 5616 396 446 661 C ATOM 477 ND2 ASN A 66 -22.121 32.187 -12.808 1.00 66.90 N ANISOU 477 ND2 ASN A 66 7875 11471 6073 400 557 723 N ATOM 478 OD1 ASN A 66 -21.920 32.768 -10.652 1.00 58.58 O ANISOU 478 OD1 ASN A 66 6763 10171 5323 285 459 702 O ATOM 479 N LEU A 67 -24.291 27.810 -10.424 1.00 55.22 N ANISOU 479 N LEU A 67 6678 9614 4692 786 117 199 N ATOM 480 CA LEU A 67 -24.984 26.756 -9.673 1.00 53.64 C ANISOU 480 CA LEU A 67 6586 9239 4557 832 17 94 C ATOM 481 C LEU A 67 -23.993 25.763 -9.043 1.00 53.96 C ANISOU 481 C LEU A 67 6619 9299 4584 987 38 -23 C ATOM 482 O LEU A 67 -24.039 25.555 -7.832 1.00 53.24 O ANISOU 482 O LEU A 67 6560 9076 4591 1016 -15 -63 O ATOM 483 CB LEU A 67 -26.021 26.058 -10.590 1.00 50.19 C ANISOU 483 CB LEU A 67 6297 8746 4026 834 -55 30 C ATOM 484 CG LEU A 67 -26.701 24.787 -10.020 1.00 48.31 C ANISOU 484 CG LEU A 67 6196 8318 3840 855 -138 -91 C ATOM 485 CD1 LEU A 67 -27.454 25.064 -8.708 1.00 48.43 C ANISOU 485 CD1 LEU A 67 6189 8180 4032 759 -187 -32 C ATOM 486 CD2 LEU A 67 -27.608 24.115 -11.072 1.00 47.86 C ANISOU 486 CD2 LEU A 67 6262 8240 3682 822 -202 -171 C ATOM 487 N ALA A 68 -23.098 25.208 -9.876 1.00 55.22 N ANISOU 487 N ALA A 68 6742 9629 4611 1103 117 -77 N ATOM 488 CA ALA A 68 -22.073 24.258 -9.460 1.00 56.36 C ANISOU 488 CA ALA A 68 6869 9814 4732 1290 141 -186 C ATOM 489 C ALA A 68 -20.995 24.844 -8.542 1.00 55.73 C ANISOU 489 C ALA A 68 6602 9812 4762 1284 162 -141 C ATOM 490 O ALA A 68 -20.509 24.110 -7.691 1.00 56.80 O ANISOU 490 O ALA A 68 6748 9893 4940 1411 122 -206 O ATOM 491 CB ALA A 68 -21.445 23.618 -10.695 1.00 57.66 C ANISOU 491 CB ALA A 68 7020 10167 4723 1425 235 -257 C ATOM 492 N VAL A 69 -20.663 26.140 -8.685 1.00 56.78 N ANISOU 492 N VAL A 69 6573 10068 4933 1136 227 -32 N ATOM 493 CA VAL A 69 -19.768 26.864 -7.775 1.00 60.74 C ANISOU 493 CA VAL A 69 6885 10656 5537 1091 245 -6 C ATOM 494 C VAL A 69 -20.344 26.972 -6.348 1.00 63.63 C ANISOU 494 C VAL A 69 7312 10821 6043 1036 137 5 C ATOM 495 O VAL A 69 -19.580 26.813 -5.397 1.00 64.62 O ANISOU 495 O VAL A 69 7347 10984 6223 1100 106 -35 O ATOM 496 CB VAL A 69 -19.389 28.270 -8.335 1.00 0.00 C ATOM 497 CG1 VAL A 69 -18.870 29.303 -7.308 1.00 0.00 C ATOM 498 CG2 VAL A 69 -18.352 28.135 -9.464 1.00 0.00 C ATOM 499 N ALA A 70 -21.672 27.163 -6.224 1.00 62.08 N ANISOU 499 N ALA A 70 7260 10430 5896 926 80 58 N ATOM 500 CA ALA A 70 -22.387 27.134 -4.947 1.00 58.93 C ANISOU 500 CA ALA A 70 6928 9842 5620 873 -8 66 C ATOM 501 C ALA A 70 -22.330 25.742 -4.302 1.00 61.36 C ANISOU 501 C ALA A 70 7366 10042 5906 1044 -73 -36 C ATOM 502 O ALA A 70 -21.812 25.602 -3.197 1.00 63.05 O ANISOU 502 O ALA A 70 7557 10221 6178 1092 -117 -55 O ATOM 503 CB ALA A 70 -23.836 27.623 -5.134 1.00 59.13 C ANISOU 503 CB ALA A 70 7060 9712 5695 730 -44 140 C ATOM 504 N ASP A 71 -22.799 24.730 -5.044 1.00 64.00 N ANISOU 504 N ASP A 71 7853 10315 6147 1137 -79 -103 N ATOM 505 CA ASP A 71 -22.830 23.321 -4.647 1.00 66.50 C ANISOU 505 CA ASP A 71 8338 10489 6439 1292 -124 -196 C ATOM 506 C ASP A 71 -21.456 22.730 -4.278 1.00 66.92 C ANISOU 506 C ASP A 71 8309 10675 6443 1510 -100 -253 C ATOM 507 O ASP A 71 -21.366 22.033 -3.270 1.00 68.42 O ANISOU 507 O ASP A 71 8597 10753 6645 1641 -146 -290 O ATOM 508 CB ASP A 71 -23.515 22.458 -5.720 1.00 72.08 C ANISOU 508 CB ASP A 71 9233 11100 7053 1322 -124 -274 C ATOM 509 CG ASP A 71 -24.922 22.919 -6.106 1.00 78.36 C ANISOU 509 CG ASP A 71 10130 11738 7903 1136 -176 -246 C ATOM 510 OD1 ASP A 71 -25.658 23.380 -5.206 1.00 79.69 O ANISOU 510 OD1 ASP A 71 10286 11806 8190 1033 -215 -185 O ATOM 511 OD2 ASP A 71 -25.279 22.715 -7.286 1.00 80.54 O1- ANISOU 511 OD2 ASP A 71 10491 12009 8100 1098 -180 -293 O1- ATOM 512 N PHE A 72 -20.412 23.046 -5.062 1.00 65.51 N ANISOU 512 N PHE A 72 7948 10743 6200 1559 -26 -257 N ATOM 513 CA PHE A 72 -19.021 22.652 -4.820 1.00 67.86 C ANISOU 513 CA PHE A 72 8124 11212 6450 1777 -5 -316 C ATOM 514 C PHE A 72 -18.459 23.217 -3.504 1.00 67.11 C ANISOU 514 C PHE A 72 7868 11181 6447 1742 -54 -277 C ATOM 515 O PHE A 72 -17.898 22.454 -2.718 1.00 66.43 O ANISOU 515 O PHE A 72 7786 11111 6344 1939 -102 -323 O ATOM 516 CB PHE A 72 -18.158 23.042 -6.043 1.00 68.10 C ANISOU 516 CB PHE A 72 7975 11515 6386 1817 103 -335 C ATOM 517 CG PHE A 72 -16.666 22.775 -5.940 1.00 69.36 C ANISOU 517 CG PHE A 72 7986 11884 6482 2068 133 -411 C ATOM 518 CD1 PHE A 72 -16.158 21.493 -6.236 1.00 71.33 C ANISOU 518 CD1 PHE A 72 8374 12104 6623 2335 150 -512 C ATOM 519 CD2 PHE A 72 -15.798 23.749 -5.403 1.00 69.75 C ANISOU 519 CD2 PHE A 72 7756 12166 6580 2039 142 -391 C ATOM 520 CE1 PHE A 72 -14.810 21.220 -6.044 1.00 72.53 C ANISOU 520 CE1 PHE A 72 8382 12463 6712 2602 177 -582 C ATOM 521 CE2 PHE A 72 -14.454 23.456 -5.216 1.00 70.60 C ANISOU 521 CE2 PHE A 72 7694 12505 6625 2282 160 -468 C ATOM 522 CZ PHE A 72 -13.963 22.198 -5.539 1.00 71.60 C ANISOU 522 CZ PHE A 72 7955 12608 6641 2580 178 -558 C ATOM 523 N CYS A 73 -18.636 24.534 -3.295 1.00 66.96 N ANISOU 523 N CYS A 73 7722 11201 6519 1501 -45 -195 N ATOM 524 CA CYS A 73 -18.154 25.267 -2.121 1.00 67.90 C ANISOU 524 CA CYS A 73 7696 11381 6722 1438 -93 -176 C ATOM 525 C CYS A 73 -18.878 24.872 -0.823 1.00 67.18 C ANISOU 525 C CYS A 73 7788 11063 6674 1491 -194 -179 C ATOM 526 O CYS A 73 -18.224 24.845 0.219 1.00 66.49 O ANISOU 526 O CYS A 73 7635 11040 6589 1596 -254 -204 O ATOM 527 CB CYS A 73 -18.225 26.792 -2.323 1.00 0.00 C ATOM 528 SG CYS A 73 -16.934 27.327 -3.479 1.00 0.00 S ATOM 529 N PHE A 74 -20.183 24.548 -0.891 1.00 65.37 N ANISOU 529 N PHE A 74 7783 10584 6470 1417 -212 -154 N ATOM 530 CA PHE A 74 -20.895 23.957 0.246 1.00 64.51 C ANISOU 530 CA PHE A 74 7863 10251 6397 1446 -286 -152 C ATOM 531 C PHE A 74 -20.369 22.556 0.603 1.00 65.24 C ANISOU 531 C PHE A 74 8095 10294 6401 1721 -312 -216 C ATOM 532 O PHE A 74 -19.882 22.359 1.720 1.00 68.64 O ANISOU 532 O PHE A 74 8546 10709 6824 1838 -370 -217 O ATOM 533 CB PHE A 74 -22.445 24.014 0.128 1.00 64.69 C ANISOU 533 CB PHE A 74 8066 10048 6467 1286 -286 -120 C ATOM 534 CG PHE A 74 -23.153 22.976 0.987 1.00 67.03 C ANISOU 534 CG PHE A 74 8598 10103 6768 1338 -329 -139 C ATOM 535 CD1 PHE A 74 -23.006 23.014 2.392 1.00 67.65 C ANISOU 535 CD1 PHE A 74 8699 10100 6903 1299 -375 -105 C ATOM 536 CD2 PHE A 74 -23.746 21.845 0.386 1.00 68.84 C ANISOU 536 CD2 PHE A 74 9038 10182 6936 1417 -316 -196 C ATOM 537 CE1 PHE A 74 -23.376 21.919 3.155 1.00 69.15 C ANISOU 537 CE1 PHE A 74 9119 10066 7088 1339 -397 -111 C ATOM 538 CE2 PHE A 74 -24.128 20.767 1.170 1.00 71.02 C ANISOU 538 CE2 PHE A 74 9547 10220 7217 1440 -336 -211 C ATOM 539 CZ PHE A 74 -23.908 20.794 2.540 1.00 70.77 C ANISOU 539 CZ PHE A 74 9536 10112 7240 1403 -372 -161 C ATOM 540 N THR A 75 -20.484 21.610 -0.342 1.00 63.60 N ANISOU 540 N THR A 75 8001 10052 6112 1839 -268 -272 N ATOM 541 CA THR A 75 -20.170 20.195 -0.100 1.00 64.06 C ANISOU 541 CA THR A 75 8238 10019 6083 2114 -277 -335 C ATOM 542 C THR A 75 -18.690 19.933 0.259 1.00 63.70 C ANISOU 542 C THR A 75 8015 10207 5982 2355 -297 -358 C ATOM 543 O THR A 75 -18.411 18.885 0.837 1.00 65.82 O ANISOU 543 O THR A 75 8428 10393 6189 2605 -330 -383 O ATOM 544 CB THR A 75 -20.560 19.295 -1.302 1.00 64.91 C ANISOU 544 CB THR A 75 8489 10067 6108 2185 -216 -409 C ATOM 545 CG2 THR A 75 -22.070 19.318 -1.599 1.00 61.29 C ANISOU 545 CG2 THR A 75 8241 9358 5687 1980 -218 -408 C ATOM 546 OG1 THR A 75 -19.838 19.642 -2.469 1.00 66.81 O ANISOU 546 OG1 THR A 75 8509 10565 6311 2151 -155 -419 O ATOM 547 N SER A 76 -17.795 20.904 0.002 1.00 61.41 N ANISOU 547 N SER A 76 7415 10210 5708 2287 -275 -351 N ATOM 548 CA SER A 76 -16.413 20.927 0.490 1.00 63.21 C ANISOU 548 CA SER A 76 7423 10706 5886 2494 -302 -385 C ATOM 549 C SER A 76 -16.290 21.081 2.023 1.00 65.01 C ANISOU 549 C SER A 76 7639 10917 6146 2514 -406 -352 C ATOM 550 O SER A 76 -15.256 20.694 2.567 1.00 69.02 O ANISOU 550 O SER A 76 8025 11611 6589 2749 -458 -385 O ATOM 551 CB SER A 76 -15.642 22.055 -0.226 1.00 0.00 C ATOM 552 OG SER A 76 -15.315 21.680 -1.547 1.00 0.00 O ATOM 553 N THR A 77 -17.330 21.619 2.689 1.00 62.50 N ANISOU 553 N THR A 77 7435 10397 5914 2287 -438 -293 N ATOM 554 CA THR A 77 -17.387 21.799 4.144 1.00 63.17 C ANISOU 554 CA THR A 77 7531 10454 6018 2290 -529 -264 C ATOM 555 C THR A 77 -18.079 20.634 4.888 1.00 63.89 C ANISOU 555 C THR A 77 7950 10270 6056 2464 -570 -243 C ATOM 556 O THR A 77 -18.052 20.632 6.118 1.00 66.39 O ANISOU 556 O THR A 77 8306 10568 6353 2519 -646 -215 O ATOM 557 CB THR A 77 -18.108 23.117 4.548 1.00 62.80 C ANISOU 557 CB THR A 77 7436 10339 6088 1956 -530 -214 C ATOM 558 CG2 THR A 77 -17.616 24.362 3.802 1.00 63.15 C ANISOU 558 CG2 THR A 77 7237 10570 6188 1751 -460 -216 C ATOM 559 OG1 THR A 77 -19.523 23.048 4.481 1.00 62.47 O ANISOU 559 OG1 THR A 77 7660 9985 6090 1839 -507 -173 O ATOM 560 N LEU A 78 -18.663 19.663 4.169 1.00 63.24 N ANISOU 560 N LEU A 78 8114 9972 5944 2541 -514 -257 N ATOM 561 CA LEU A 78 -19.271 18.480 4.783 1.00 66.65 C ANISOU 561 CA LEU A 78 8893 10098 6335 2659 -528 -234 C ATOM 562 C LEU A 78 -18.346 17.576 5.633 1.00 73.02 C ANISOU 562 C LEU A 78 9764 10949 7032 2997 -593 -226 C ATOM 563 O LEU A 78 -18.855 17.067 6.633 1.00 74.51 O ANISOU 563 O LEU A 78 10188 10924 7199 3029 -623 -171 O ATOM 564 CB LEU A 78 -20.115 17.677 3.772 1.00 66.24 C ANISOU 564 CB LEU A 78 9079 9830 6261 2677 -449 -278 C ATOM 565 CG LEU A 78 -21.519 18.268 3.519 1.00 63.88 C ANISOU 565 CG LEU A 78 8781 9439 6052 2353 -401 -278 C ATOM 566 CD1 LEU A 78 -22.187 17.597 2.304 1.00 65.87 C ANISOU 566 CD1 LEU A 78 9271 9495 6262 2378 -339 -344 C ATOM 567 CD2 LEU A 78 -22.417 18.210 4.778 1.00 61.84 C ANISOU 567 CD2 LEU A 78 8596 9019 5881 2119 -428 -213 C ATOM 568 N PRO A 79 -17.013 17.484 5.377 1.00 76.05 N ANISOU 568 N PRO A 79 9960 11598 7336 3264 -615 -272 N ATOM 569 CA PRO A 79 -16.095 16.877 6.365 1.00 78.05 C ANISOU 569 CA PRO A 79 10265 11914 7475 3608 -696 -254 C ATOM 570 C PRO A 79 -16.052 17.557 7.750 1.00 77.81 C ANISOU 570 C PRO A 79 10131 11983 7450 3527 -797 -204 C ATOM 571 O PRO A 79 -15.869 16.850 8.739 1.00 78.78 O ANISOU 571 O PRO A 79 10439 12015 7479 3745 -862 -155 O ATOM 572 CB PRO A 79 -14.719 16.868 5.673 1.00 80.47 C ANISOU 572 CB PRO A 79 10290 12571 7715 3860 -697 -328 C ATOM 573 CG PRO A 79 -14.846 17.857 4.527 1.00 80.40 C ANISOU 573 CG PRO A 79 10021 12731 7797 3574 -625 -370 C ATOM 574 CD PRO A 79 -16.301 17.698 4.117 1.00 77.28 C ANISOU 574 CD PRO A 79 9878 12001 7482 3304 -557 -343 C ATOM 575 N PHE A 80 -16.258 18.885 7.809 1.00 76.58 N ANISOU 575 N PHE A 80 9705 12002 7389 3225 -810 -215 N ATOM 576 CA PHE A 80 -16.387 19.640 9.062 1.00 75.70 C ANISOU 576 CA PHE A 80 9513 11971 7280 3125 -902 -186 C ATOM 577 C PHE A 80 -17.771 19.452 9.711 1.00 74.42 C ANISOU 577 C PHE A 80 9663 11459 7153 2962 -884 -113 C ATOM 578 O PHE A 80 -17.862 19.424 10.939 1.00 78.68 O ANISOU 578 O PHE A 80 10274 11984 7638 3000 -957 -74 O ATOM 579 CB PHE A 80 -16.147 21.149 8.822 1.00 74.69 C ANISOU 579 CB PHE A 80 9024 12109 7246 2841 -905 -231 C ATOM 580 CG PHE A 80 -14.759 21.555 8.363 1.00 78.81 C ANISOU 580 CG PHE A 80 9199 13015 7730 2967 -919 -308 C ATOM 581 CD1 PHE A 80 -14.367 21.379 7.019 1.00 80.34 C ANISOU 581 CD1 PHE A 80 9295 13274 7956 2943 -817 -342 C ATOM 582 CD2 PHE A 80 -13.809 22.019 9.298 1.00 80.82 C ANISOU 582 CD2 PHE A 80 9213 13587 7907 3104 -1030 -351 C ATOM 583 CE1 PHE A 80 -13.078 21.707 6.623 1.00 83.38 C ANISOU 583 CE1 PHE A 80 9349 14028 8304 3050 -811 -415 C ATOM 584 CE2 PHE A 80 -12.526 22.344 8.881 1.00 84.01 C ANISOU 584 CE2 PHE A 80 9266 14376 8279 3207 -1036 -433 C ATOM 585 CZ PHE A 80 -12.163 22.191 7.550 1.00 85.22 C ANISOU 585 CZ PHE A 80 9324 14584 8472 3178 -918 -462 C ATOM 586 N PHE A 81 -18.813 19.366 8.875 1.00 70.43 N ANISOU 586 N PHE A 81 9339 10691 6731 2781 -786 -98 N ATOM 587 CA PHE A 81 -20.199 19.309 9.328 1.00 67.97 C ANISOU 587 CA PHE A 81 9301 10066 6459 2611 -753 -39 C ATOM 588 C PHE A 81 -20.611 17.900 9.789 1.00 71.42 C ANISOU 588 C PHE A 81 10112 10225 6799 2834 -732 4 C ATOM 589 O PHE A 81 -21.465 17.803 10.664 1.00 74.18 O ANISOU 589 O PHE A 81 10692 10349 7146 2743 -716 63 O ATOM 590 CB PHE A 81 -21.143 19.881 8.244 1.00 0.00 C ATOM 591 CG PHE A 81 -22.042 20.987 8.773 1.00 0.00 C ATOM 592 CD1 PHE A 81 -21.525 22.288 8.956 1.00 0.00 C ATOM 593 CD2 PHE A 81 -23.338 20.691 9.250 1.00 0.00 C ATOM 594 CE1 PHE A 81 -22.311 23.272 9.540 1.00 0.00 C ATOM 595 CE2 PHE A 81 -24.116 21.697 9.810 1.00 0.00 C ATOM 596 CZ PHE A 81 -23.606 22.983 9.949 1.00 0.00 C ATOM 597 N MET A 82 -19.988 16.836 9.264 1.00 73.08 N ANISOU 597 N MET A 82 10403 10437 6926 3123 -720 -23 N ATOM 598 CA MET A 82 -20.327 15.458 9.633 1.00 78.72 C ANISOU 598 CA MET A 82 11519 10838 7554 3326 -680 18 C ATOM 599 C MET A 82 -19.735 15.058 10.994 1.00 79.49 C ANISOU 599 C MET A 82 11709 10981 7510 3624 -767 86 C ATOM 600 O MET A 82 -20.440 14.430 11.783 1.00 78.39 O ANISOU 600 O MET A 82 11911 10562 7311 3671 -740 163 O ATOM 601 CB MET A 82 -19.962 14.482 8.491 1.00 0.00 C ATOM 602 CG MET A 82 -18.471 14.162 8.299 1.00 0.00 C ATOM 603 SD MET A 82 -18.132 13.212 6.793 1.00 0.00 S ATOM 604 CE MET A 82 -16.385 12.816 7.070 1.00 0.00 C ATOM 605 N VAL A 83 -18.474 15.445 11.260 1.00 81.09 N ANISOU 605 N VAL A 83 11614 11549 7649 3824 -872 59 N ATOM 606 CA VAL A 83 -17.759 15.087 12.487 1.00 80.21 C ANISOU 606 CA VAL A 83 11556 11534 7388 4109 -979 120 C ATOM 607 C VAL A 83 -18.290 15.798 13.747 1.00 75.55 C ANISOU 607 C VAL A 83 10931 10963 6811 3875 -1029 166 C ATOM 608 O VAL A 83 -18.143 15.240 14.832 1.00 76.32 O ANISOU 608 O VAL A 83 11190 11033 6775 4058 -1095 239 O ATOM 609 CB VAL A 83 -16.231 15.345 12.377 1.00 81.09 C ANISOU 609 CB VAL A 83 11327 12068 7415 4405 -1085 62 C ATOM 610 CG1 VAL A 83 -15.593 14.470 11.284 1.00 82.23 C ANISOU 610 CG1 VAL A 83 11386 12267 7589 4529 -1013 -15 C ATOM 611 CG2 VAL A 83 -15.832 16.825 12.218 1.00 78.64 C ANISOU 611 CG2 VAL A 83 10598 12122 7160 4180 -1171 8 C ATOM 612 N ARG A 84 -18.935 16.969 13.604 1.00 72.05 N ANISOU 612 N ARG A 84 10296 10564 6515 3490 -997 124 N ATOM 613 CA ARG A 84 -19.571 17.647 14.740 1.00 72.10 C ANISOU 613 CA ARG A 84 10314 10536 6544 3253 -1019 160 C ATOM 614 C ARG A 84 -20.879 16.948 15.169 1.00 76.16 C ANISOU 614 C ARG A 84 11215 10645 7079 3121 -914 237 C ATOM 615 O ARG A 84 -21.172 16.872 16.363 1.00 79.91 O ANISOU 615 O ARG A 84 11855 11028 7478 3111 -929 303 O ATOM 616 CB ARG A 84 -19.798 19.151 14.448 1.00 0.00 C ATOM 617 CG ARG A 84 -20.668 19.456 13.210 1.00 0.00 C ATOM 618 CD ARG A 84 -21.204 20.890 13.098 1.00 0.00 C ATOM 619 NE ARG A 84 -21.969 21.283 14.295 1.00 0.00 N ATOM 620 CZ ARG A 84 -23.118 21.979 14.331 1.00 0.00 C ATOM 621 NH1 ARG A 84 -23.753 22.342 13.210 1.00 0.00 N1+ ATOM 622 NH2 ARG A 84 -23.639 22.302 15.519 1.00 0.00 N1+ ATOM 623 N LYS A 85 -21.652 16.430 14.203 1.00 76.39 N ANISOU 623 N LYS A 85 11385 10441 7197 3011 -802 222 N ATOM 624 CA LYS A 85 -22.918 15.746 14.481 1.00 77.75 C ANISOU 624 CA LYS A 85 11918 10236 7387 2877 -692 279 C ATOM 625 C LYS A 85 -22.678 14.369 15.128 1.00 81.33 C ANISOU 625 C LYS A 85 12740 10483 7679 3183 -682 364 C ATOM 626 O LYS A 85 -23.427 13.993 16.024 1.00 82.05 O ANISOU 626 O LYS A 85 13113 10334 7730 3107 -622 443 O ATOM 627 CB LYS A 85 -23.775 15.639 13.204 1.00 0.00 C ATOM 628 CG LYS A 85 -24.166 16.982 12.549 1.00 0.00 C ATOM 629 CD LYS A 85 -24.996 17.950 13.411 1.00 0.00 C ATOM 630 CE LYS A 85 -25.559 19.118 12.577 1.00 0.00 C ATOM 631 NZ LYS A 85 -26.472 19.971 13.357 1.00 0.00 N1+ ATOM 632 N ALA A 86 -21.574 13.700 14.754 1.00 83.75 N ANISOU 632 N ALA A 86 13057 10876 7887 3539 -731 353 N ATOM 633 CA ALA A 86 -21.105 12.456 15.369 1.00 83.09 C ANISOU 633 CA ALA A 86 13338 10595 7638 3881 -725 444 C ATOM 634 C ALA A 86 -20.704 12.616 16.851 1.00 82.14 C ANISOU 634 C ALA A 86 13225 10620 7365 4054 -833 530 C ATOM 635 O ALA A 86 -20.726 11.626 17.582 1.00 85.67 O ANISOU 635 O ALA A 86 14021 10869 7659 4311 -821 634 O ATOM 636 CB ALA A 86 -19.925 11.917 14.549 1.00 84.55 C ANISOU 636 CB ALA A 86 13514 10854 7759 4245 -748 401 C ATOM 637 N MET A 87 -20.375 13.852 17.262 1.00 77.14 N ANISOU 637 N MET A 87 12232 10319 6759 3922 -937 486 N ATOM 638 CA MET A 87 -20.073 14.242 18.641 1.00 78.13 C ANISOU 638 CA MET A 87 12332 10621 6733 4055 -1053 543 C ATOM 639 C MET A 87 -21.287 14.889 19.352 1.00 77.07 C ANISOU 639 C MET A 87 12288 10359 6634 3728 -1000 582 C ATOM 640 O MET A 87 -21.111 15.431 20.443 1.00 79.10 O ANISOU 640 O MET A 87 12429 10825 6800 3735 -1099 589 O ATOM 641 CB MET A 87 -18.847 15.180 18.644 1.00 78.67 C ANISOU 641 CB MET A 87 11937 11169 6784 4141 -1210 450 C ATOM 642 CG MET A 87 -17.560 14.561 18.077 1.00 83.63 C ANISOU 642 CG MET A 87 12480 12000 7299 4574 -1297 435 C ATOM 643 SD MET A 87 -16.194 15.741 17.896 1.00 85.93 S ANISOU 643 SD MET A 87 12175 12883 7590 4599 -1464 302 S ATOM 644 CE MET A 87 -15.708 15.941 19.632 1.00 86.01 C ANISOU 644 CE MET A 87 12158 13040 7482 4504 -1584 330 C ATOM 645 N GLY A 88 -22.490 14.810 18.751 1.00 74.84 N ANISOU 645 N GLY A 88 12204 9756 6475 3446 -847 596 N ATOM 646 CA GLY A 88 -23.748 15.264 19.349 1.00 74.84 C ANISOU 646 CA GLY A 88 12262 9651 6520 3133 -781 621 C ATOM 647 C GLY A 88 -23.944 16.788 19.267 1.00 72.91 C ANISOU 647 C GLY A 88 11626 9673 6403 2865 -835 524 C ATOM 648 O GLY A 88 -24.626 17.352 20.122 1.00 74.37 O ANISOU 648 O GLY A 88 11771 9943 6544 2758 -865 533 O ATOM 649 N GLY A 89 -23.320 17.443 18.278 1.00 70.80 N ANISOU 649 N GLY A 89 11085 9532 6283 2761 -840 431 N ATOM 650 CA GLY A 89 -23.454 18.876 18.012 1.00 70.57 C ANISOU 650 CA GLY A 89 10703 9716 6395 2496 -868 342 C ATOM 651 C GLY A 89 -22.222 19.657 18.490 1.00 67.02 C ANISOU 651 C GLY A 89 9973 9624 5865 2593 -1016 291 C ATOM 652 O GLY A 89 -22.096 20.836 18.148 1.00 61.97 O ANISOU 652 O GLY A 89 9079 9140 5325 2360 -1035 219 O ATOM 653 N HIS A 90 -21.313 19.012 19.240 1.00 71.49 N ANISOU 653 N HIS A 90 10580 10329 6253 2930 -1122 319 N ATOM 654 CA HIS A 90 -20.024 19.550 19.685 1.00 73.69 C ANISOU 654 CA HIS A 90 10549 10996 6452 3022 -1276 246 C ATOM 655 C HIS A 90 -19.131 19.889 18.478 1.00 73.98 C ANISOU 655 C HIS A 90 10235 11280 6596 3006 -1305 148 C ATOM 656 O HIS A 90 -19.019 19.068 17.572 1.00 75.07 O ANISOU 656 O HIS A 90 10409 11308 6806 3053 -1231 151 O ATOM 657 CB HIS A 90 -19.363 18.490 20.594 1.00 0.00 C ATOM 658 CG HIS A 90 -18.049 18.854 21.250 1.00 0.00 C ATOM 659 CD2 HIS A 90 -17.771 18.965 22.597 1.00 0.00 C ATOM 660 ND1 HIS A 90 -16.868 19.090 20.535 1.00 0.00 N ATOM 661 CE1 HIS A 90 -15.951 19.356 21.455 1.00 0.00 C ATOM 662 NE2 HIS A 90 -16.429 19.289 22.697 1.00 0.00 N ATOM 663 N TRP A 91 -18.497 21.069 18.510 1.00 74.24 N ANISOU 663 N TRP A 91 9928 11650 6630 2926 -1405 52 N ATOM 664 CA TRP A 91 -17.611 21.564 17.460 1.00 74.54 C ANISOU 664 CA TRP A 91 9607 11950 6766 2867 -1420 -46 C ATOM 665 C TRP A 91 -16.141 21.407 17.907 1.00 76.87 C ANISOU 665 C TRP A 91 9655 12638 6913 3146 -1575 -105 C ATOM 666 O TRP A 91 -15.727 22.144 18.804 1.00 76.84 O ANISOU 666 O TRP A 91 9438 12898 6858 3062 -1681 -181 O ATOM 667 CB TRP A 91 -17.969 23.039 17.205 1.00 75.24 C ANISOU 667 CB TRP A 91 9481 12090 7015 2468 -1378 -122 C ATOM 668 CG TRP A 91 -17.168 23.728 16.144 1.00 78.98 C ANISOU 668 CG TRP A 91 9653 12746 7611 2356 -1342 -196 C ATOM 669 CD1 TRP A 91 -16.196 24.642 16.357 1.00 82.33 C ANISOU 669 CD1 TRP A 91 9717 13521 8042 2284 -1409 -302 C ATOM 670 CD2 TRP A 91 -17.209 23.522 14.701 1.00 80.36 C ANISOU 670 CD2 TRP A 91 9863 12768 7904 2292 -1222 -172 C ATOM 671 CE2 TRP A 91 -16.268 24.400 14.090 1.00 82.15 C ANISOU 671 CE2 TRP A 91 9752 13263 8199 2193 -1215 -252 C ATOM 672 CE3 TRP A 91 -17.940 22.670 13.843 1.00 80.10 C ANISOU 672 CE3 TRP A 91 10111 12407 7917 2297 -1118 -96 C ATOM 673 NE1 TRP A 91 -15.680 25.060 15.150 1.00 83.49 N ANISOU 673 NE1 TRP A 91 9681 13735 8308 2179 -1326 -333 N ATOM 674 CZ2 TRP A 91 -16.079 24.444 12.698 1.00 81.71 C ANISOU 674 CZ2 TRP A 91 9645 13157 8243 2119 -1109 -249 C ATOM 675 CZ3 TRP A 91 -17.767 22.711 12.444 1.00 80.27 C ANISOU 675 CZ3 TRP A 91 10070 12390 8040 2221 -1028 -108 C ATOM 676 CH2 TRP A 91 -16.843 23.605 11.872 1.00 80.28 C ANISOU 676 CH2 TRP A 91 9745 12662 8094 2143 -1025 -178 C ATOM 677 N PRO A 92 -15.378 20.465 17.304 1.00 79.21 N ANISOU 677 N PRO A 92 9964 12999 7131 3483 -1594 -83 N ATOM 678 CA PRO A 92 -13.988 20.207 17.723 1.00 81.24 C ANISOU 678 CA PRO A 92 9957 13669 7244 3782 -1746 -144 C ATOM 679 C PRO A 92 -12.940 21.225 17.220 1.00 82.57 C ANISOU 679 C PRO A 92 9656 14211 7506 3617 -1767 -281 C ATOM 680 O PRO A 92 -11.831 21.224 17.752 1.00 86.26 O ANISOU 680 O PRO A 92 9833 15080 7863 3800 -1901 -358 O ATOM 681 CB PRO A 92 -13.717 18.796 17.177 1.00 83.19 C ANISOU 681 CB PRO A 92 10412 13800 7395 4196 -1727 -69 C ATOM 682 CG PRO A 92 -14.554 18.716 15.912 1.00 81.87 C ANISOU 682 CG PRO A 92 10429 13288 7390 4014 -1551 -39 C ATOM 683 CD PRO A 92 -15.803 19.517 16.269 1.00 80.26 C ANISOU 683 CD PRO A 92 10359 12835 7301 3616 -1478 -14 C ATOM 684 N PHE A 93 -13.284 22.055 16.218 1.00 82.21 N ANISOU 684 N PHE A 93 9525 14058 7652 3281 -1638 -313 N ATOM 685 CA PHE A 93 -12.370 23.020 15.593 1.00 78.92 C ANISOU 685 CA PHE A 93 8696 13961 7330 3097 -1625 -428 C ATOM 686 C PHE A 93 -12.353 24.367 16.351 1.00 85.27 C ANISOU 686 C PHE A 93 9309 14906 8184 2756 -1672 -513 C ATOM 687 O PHE A 93 -13.088 24.547 17.323 1.00 88.96 O ANISOU 687 O PHE A 93 9966 15221 8613 2672 -1711 -484 O ATOM 688 CB PHE A 93 -12.767 23.228 14.114 1.00 69.66 C ANISOU 688 CB PHE A 93 7551 12602 6316 2929 -1458 -408 C ATOM 689 CG PHE A 93 -12.927 21.976 13.269 1.00 65.29 C ANISOU 689 CG PHE A 93 7281 11805 5721 3208 -1396 -328 C ATOM 690 CD1 PHE A 93 -11.801 21.350 12.695 1.00 63.77 C ANISOU 690 CD1 PHE A 93 7001 11809 5419 3583 -1435 -347 C ATOM 691 CD2 PHE A 93 -14.189 21.350 13.159 1.00 58.84 C ANISOU 691 CD2 PHE A 93 6817 10566 4972 3096 -1294 -242 C ATOM 692 CE1 PHE A 93 -11.956 20.176 11.971 1.00 63.78 C ANISOU 692 CE1 PHE A 93 7294 11561 5381 3840 -1369 -285 C ATOM 693 CE2 PHE A 93 -14.324 20.179 12.428 1.00 59.13 C ANISOU 693 CE2 PHE A 93 7127 10368 4970 3324 -1232 -185 C ATOM 694 CZ PHE A 93 -13.212 19.597 11.831 1.00 62.40 C ANISOU 694 CZ PHE A 93 7482 10951 5277 3696 -1265 -207 C ATOM 695 N GLY A 94 -11.499 25.295 15.882 1.00 87.01 N ANISOU 695 N GLY A 94 9160 15415 8485 2549 -1657 -624 N ATOM 696 CA GLY A 94 -11.279 26.612 16.485 1.00 89.95 C ANISOU 696 CA GLY A 94 9336 15940 8899 2227 -1701 -728 C ATOM 697 C GLY A 94 -12.413 27.612 16.196 1.00 90.09 C ANISOU 697 C GLY A 94 9543 15610 9075 1861 -1579 -691 C ATOM 698 O GLY A 94 -13.344 27.338 15.434 1.00 90.66 O ANISOU 698 O GLY A 94 9851 15355 9240 1824 -1457 -591 O ATOM 699 N TRP A 95 -12.297 28.796 16.827 1.00 87.00 N ANISOU 699 N TRP A 95 9045 15302 8707 1591 -1619 -784 N ATOM 700 CA TRP A 95 -13.242 29.917 16.747 1.00 83.52 C ANISOU 700 CA TRP A 95 8734 14575 8425 1234 -1500 -770 C ATOM 701 C TRP A 95 -13.342 30.566 15.355 1.00 82.56 C ANISOU 701 C TRP A 95 8494 14405 8470 1026 -1348 -759 C ATOM 702 O TRP A 95 -14.439 30.974 14.969 1.00 80.39 O ANISOU 702 O TRP A 95 8404 13818 8321 851 -1226 -685 O ATOM 703 CB TRP A 95 -12.894 30.959 17.831 1.00 86.93 C ANISOU 703 CB TRP A 95 9051 15138 8843 992 -1570 -898 C ATOM 704 CG TRP A 95 -13.778 32.173 17.899 1.00 89.51 C ANISOU 704 CG TRP A 95 9394 15267 9349 597 -1438 -927 C ATOM 705 CD1 TRP A 95 -14.922 32.257 18.612 1.00 89.18 C ANISOU 705 CD1 TRP A 95 9620 14888 9377 450 -1367 -877 C ATOM 706 CD2 TRP A 95 -13.669 33.437 17.170 1.00 92.39 C ANISOU 706 CD2 TRP A 95 9508 15756 9840 308 -1353 -1007 C ATOM 707 CE2 TRP A 95 -14.786 34.258 17.521 1.00 91.14 C ANISOU 707 CE2 TRP A 95 9506 15301 9824 12 -1235 -993 C ATOM 708 CE3 TRP A 95 -12.747 33.977 16.242 1.00 95.18 C ANISOU 708 CE3 TRP A 95 9522 16443 10199 274 -1354 -1089 C ATOM 709 NE1 TRP A 95 -15.510 33.486 18.404 1.00 89.10 N ANISOU 709 NE1 TRP A 95 9549 14775 9527 114 -1250 -917 N ATOM 710 CZ2 TRP A 95 -14.970 35.547 16.991 1.00 91.11 C ANISOU 710 CZ2 TRP A 95 9362 15295 9961 -312 -1119 -1046 C ATOM 711 CZ3 TRP A 95 -12.926 35.265 15.695 1.00 95.26 C ANISOU 711 CZ3 TRP A 95 9378 16464 10351 -74 -1230 -1145 C ATOM 712 CH2 TRP A 95 -14.034 36.050 16.070 1.00 93.23 C ANISOU 712 CH2 TRP A 95 9315 15880 10230 -361 -1113 -1118 C ATOM 713 N PHE A 96 -12.214 30.645 14.628 1.00 84.63 N ANISOU 713 N PHE A 96 8441 14989 8725 1053 -1353 -829 N ATOM 714 CA PHE A 96 -12.182 31.132 13.248 1.00 82.98 C ANISOU 714 CA PHE A 96 8119 14761 8650 866 -1201 -812 C ATOM 715 C PHE A 96 -12.979 30.226 12.298 1.00 79.27 C ANISOU 715 C PHE A 96 7877 14039 8202 1042 -1111 -680 C ATOM 716 O PHE A 96 -13.831 30.730 11.569 1.00 77.95 O ANISOU 716 O PHE A 96 7816 13646 8156 855 -981 -615 O ATOM 717 CB PHE A 96 -10.728 31.379 12.780 1.00 84.48 C ANISOU 717 CB PHE A 96 7906 15386 8805 871 -1221 -925 C ATOM 718 CG PHE A 96 -10.566 31.661 11.293 1.00 84.43 C ANISOU 718 CG PHE A 96 7779 15394 8908 715 -1055 -901 C ATOM 719 CD1 PHE A 96 -10.911 32.928 10.774 1.00 84.46 C ANISOU 719 CD1 PHE A 96 7744 15299 9049 324 -932 -915 C ATOM 720 CD2 PHE A 96 -10.261 30.614 10.395 1.00 86.63 C ANISOU 720 CD2 PHE A 96 7997 15782 9138 968 -1016 -861 C ATOM 721 CE1 PHE A 96 -10.899 33.142 9.401 1.00 85.78 C ANISOU 721 CE1 PHE A 96 7819 15476 9296 186 -772 -877 C ATOM 722 CE2 PHE A 96 -10.260 30.848 9.027 1.00 86.85 C ANISOU 722 CE2 PHE A 96 7920 15837 9244 828 -858 -838 C ATOM 723 CZ PHE A 96 -10.573 32.107 8.532 1.00 86.40 C ANISOU 723 CZ PHE A 96 7828 15684 9316 435 -736 -839 C ATOM 724 N LEU A 97 -12.707 28.910 12.369 1.00 77.48 N ANISOU 724 N LEU A 97 7741 13844 7854 1405 -1183 -642 N ATOM 725 CA LEU A 97 -13.359 27.879 11.564 1.00 73.28 C ANISOU 725 CA LEU A 97 7445 13064 7333 1566 -1101 -537 C ATOM 726 C LEU A 97 -14.863 27.742 11.846 1.00 72.96 C ANISOU 726 C LEU A 97 7755 12618 7346 1478 -1063 -444 C ATOM 727 O LEU A 97 -15.589 27.403 10.916 1.00 75.55 O ANISOU 727 O LEU A 97 8250 12715 7742 1445 -962 -372 O ATOM 728 CB LEU A 97 -12.637 26.525 11.743 1.00 73.44 C ANISOU 728 CB LEU A 97 7494 13203 7207 1983 -1179 -529 C ATOM 729 CG LEU A 97 -11.211 26.488 11.150 1.00 74.38 C ANISOU 729 CG LEU A 97 7262 13726 7273 2124 -1194 -614 C ATOM 730 CD1 LEU A 97 -10.479 25.200 11.565 1.00 75.81 C ANISOU 730 CD1 LEU A 97 7527 13968 7310 2578 -1259 -592 C ATOM 731 CD2 LEU A 97 -11.214 26.662 9.614 1.00 72.63 C ANISOU 731 CD2 LEU A 97 6911 13521 7161 1924 -1039 -616 C ATOM 732 N CYS A 98 -15.314 28.020 13.077 1.00 72.06 N ANISOU 732 N CYS A 98 7750 12434 7196 1440 -1139 -451 N ATOM 733 CA CYS A 98 -16.737 28.067 13.440 1.00 73.21 C ANISOU 733 CA CYS A 98 8199 12222 7396 1334 -1089 -373 C ATOM 734 C CYS A 98 -17.515 29.050 12.546 1.00 72.20 C ANISOU 734 C CYS A 98 8058 11943 7433 1015 -969 -358 C ATOM 735 O CYS A 98 -18.373 28.647 11.764 1.00 71.14 O ANISOU 735 O CYS A 98 8140 11525 7364 955 -895 -280 O ATOM 736 CB CYS A 98 -16.864 28.361 14.958 1.00 76.55 C ANISOU 736 CB CYS A 98 8709 12640 7735 1341 -1185 -397 C ATOM 737 SG CYS A 98 -18.422 29.007 15.638 1.00 79.68 S ANISOU 737 SG CYS A 98 9359 12690 8226 1092 -1109 -350 S ATOM 738 N LYS A 99 -17.132 30.325 12.611 1.00 71.35 N ANISOU 738 N LYS A 99 7698 12023 7390 808 -945 -429 N ATOM 739 CA LYS A 99 -17.804 31.402 11.891 1.00 66.36 C ANISOU 739 CA LYS A 99 7062 11246 6905 526 -823 -402 C ATOM 740 C LYS A 99 -17.576 31.327 10.372 1.00 64.79 C ANISOU 740 C LYS A 99 6776 11095 6745 532 -729 -362 C ATOM 741 O LYS A 99 -18.504 31.627 9.625 1.00 64.28 O ANISOU 741 O LYS A 99 6815 10836 6773 400 -630 -291 O ATOM 742 CB LYS A 99 -17.346 32.755 12.466 1.00 66.74 C ANISOU 742 CB LYS A 99 6931 11421 7006 263 -824 -496 C ATOM 743 CG LYS A 99 -17.700 32.925 13.957 1.00 68.02 C ANISOU 743 CG LYS A 99 7180 11543 7121 234 -911 -553 C ATOM 744 CD LYS A 99 -17.198 34.243 14.571 1.00 70.68 C ANISOU 744 CD LYS A 99 7357 11982 7515 -54 -901 -666 C ATOM 745 CE LYS A 99 -17.838 35.519 14.000 1.00 70.72 C ANISOU 745 CE LYS A 99 7503 11697 7670 -304 -772 -619 C ATOM 746 NZ LYS A 99 -19.300 35.529 14.171 1.00 69.65 N1+ ANISOU 746 NZ LYS A 99 7624 11308 7531 -273 -782 -583 N1+ ATOM 747 N PHE A 100 -16.371 30.904 9.953 1.00 62.89 N ANISOU 747 N PHE A 100 6346 11123 6426 696 -757 -407 N ATOM 748 CA PHE A 100 -15.956 30.768 8.555 1.00 61.55 C ANISOU 748 CA PHE A 100 6096 11015 6276 712 -658 -376 C ATOM 749 C PHE A 100 -16.725 29.676 7.788 1.00 59.88 C ANISOU 749 C PHE A 100 6137 10572 6042 885 -630 -291 C ATOM 750 O PHE A 100 -17.242 29.965 6.709 1.00 57.71 O ANISOU 750 O PHE A 100 5936 10166 5827 783 -534 -231 O ATOM 751 CB PHE A 100 -14.422 30.590 8.510 1.00 0.00 C ATOM 752 CG PHE A 100 -13.775 30.368 7.154 1.00 0.00 C ATOM 753 CD1 PHE A 100 -13.579 31.456 6.277 1.00 0.00 C ATOM 754 CD2 PHE A 100 -13.455 29.065 6.718 1.00 0.00 C ATOM 755 CE1 PHE A 100 -13.005 31.244 5.030 1.00 0.00 C ATOM 756 CE2 PHE A 100 -12.880 28.875 5.469 1.00 0.00 C ATOM 757 CZ PHE A 100 -12.646 29.961 4.634 1.00 0.00 C ATOM 758 N VAL A 101 -16.843 28.477 8.388 1.00 59.93 N ANISOU 758 N VAL A 101 6291 10525 5955 1144 -713 -289 N ATOM 759 CA VAL A 101 -17.579 27.349 7.812 1.00 56.12 C ANISOU 759 CA VAL A 101 6046 9838 5441 1312 -683 -231 C ATOM 760 C VAL A 101 -19.094 27.612 7.775 1.00 53.20 C ANISOU 760 C VAL A 101 5900 9155 5159 1137 -633 -162 C ATOM 761 O VAL A 101 -19.707 27.421 6.727 1.00 52.03 O ANISOU 761 O VAL A 101 5844 8885 5040 1105 -562 -123 O ATOM 762 CB VAL A 101 -17.288 26.006 8.558 1.00 0.00 C ATOM 763 CG1 VAL A 101 -18.275 24.850 8.277 1.00 0.00 C ATOM 764 CG2 VAL A 101 -15.848 25.535 8.280 1.00 0.00 C ATOM 765 N PHE A 102 -19.680 28.067 8.891 1.00 51.86 N ANISOU 765 N PHE A 102 5810 8870 5025 1025 -669 -152 N ATOM 766 CA PHE A 102 -21.132 28.248 8.984 1.00 56.60 C ANISOU 766 CA PHE A 102 6606 9194 5706 880 -621 -92 C ATOM 767 C PHE A 102 -21.661 29.378 8.075 1.00 56.90 C ANISOU 767 C PHE A 102 6557 9208 5857 642 -538 -65 C ATOM 768 O PHE A 102 -22.756 29.249 7.529 1.00 52.57 O ANISOU 768 O PHE A 102 6141 8465 5367 558 -490 -10 O ATOM 769 CB PHE A 102 -21.580 28.374 10.453 1.00 0.00 C ATOM 770 CG PHE A 102 -21.585 27.078 11.264 1.00 0.00 C ATOM 771 CD1 PHE A 102 -20.406 26.328 11.481 1.00 0.00 C ATOM 772 CD2 PHE A 102 -22.780 26.637 11.870 1.00 0.00 C ATOM 773 CE1 PHE A 102 -20.424 25.221 12.316 1.00 0.00 C ATOM 774 CE2 PHE A 102 -22.777 25.529 12.703 1.00 0.00 C ATOM 775 CZ PHE A 102 -21.600 24.831 12.936 1.00 0.00 C ATOM 776 N THR A 103 -20.844 30.418 7.841 1.00 57.96 N ANISOU 776 N THR A 103 6471 9536 6017 532 -515 -98 N ATOM 777 CA THR A 103 -21.113 31.444 6.828 1.00 55.94 C ANISOU 777 CA THR A 103 6155 9250 5850 332 -419 -55 C ATOM 778 C THR A 103 -21.112 30.862 5.392 1.00 54.67 C ANISOU 778 C THR A 103 5994 9125 5651 413 -363 -18 C ATOM 779 O THR A 103 -21.991 31.198 4.596 1.00 54.31 O ANISOU 779 O THR A 103 6037 8949 5649 332 -304 50 O ATOM 780 CB THR A 103 -20.066 32.593 6.910 1.00 0.00 C ATOM 781 CG2 THR A 103 -20.179 33.716 5.866 1.00 0.00 C ATOM 782 OG1 THR A 103 -20.141 33.204 8.186 1.00 0.00 O ATOM 783 N ILE A 104 -20.156 29.966 5.098 1.00 52.66 N ANISOU 783 N ILE A 104 5642 9060 5306 590 -383 -65 N ATOM 784 CA ILE A 104 -20.052 29.264 3.818 1.00 51.66 C ANISOU 784 CA ILE A 104 5532 8972 5125 693 -328 -48 C ATOM 785 C ILE A 104 -21.230 28.295 3.575 1.00 51.83 C ANISOU 785 C ILE A 104 5803 8760 5131 777 -344 -15 C ATOM 786 O ILE A 104 -21.637 28.149 2.423 1.00 50.27 O ANISOU 786 O ILE A 104 5665 8512 4922 755 -290 18 O ATOM 787 CB ILE A 104 -18.674 28.534 3.681 1.00 0.00 C ATOM 788 CG1 ILE A 104 -17.533 29.569 3.550 1.00 0.00 C ATOM 789 CG2 ILE A 104 -18.541 27.496 2.543 1.00 0.00 C ATOM 790 CD1 ILE A 104 -16.139 28.996 3.839 1.00 0.00 C ATOM 791 N VAL A 105 -21.785 27.692 4.638 1.00 53.33 N ANISOU 791 N VAL A 105 6143 8807 5312 859 -412 -27 N ATOM 792 CA VAL A 105 -22.999 26.878 4.566 1.00 54.38 C ANISOU 792 CA VAL A 105 6513 8711 5439 899 -415 -5 C ATOM 793 C VAL A 105 -24.219 27.718 4.126 1.00 57.59 C ANISOU 793 C VAL A 105 6969 8975 5938 694 -378 53 C ATOM 794 O VAL A 105 -24.745 27.435 3.049 1.00 59.17 O ANISOU 794 O VAL A 105 7250 9099 6131 674 -350 72 O ATOM 795 CB VAL A 105 -23.281 26.090 5.881 1.00 52.17 C ANISOU 795 CB VAL A 105 6391 8311 5121 1020 -479 -21 C ATOM 796 CG1 VAL A 105 -24.669 25.413 5.961 1.00 51.15 C ANISOU 796 CG1 VAL A 105 6494 7926 5015 974 -464 3 C ATOM 797 CG2 VAL A 105 -22.195 25.022 6.113 1.00 50.45 C ANISOU 797 CG2 VAL A 105 6179 8198 4791 1283 -514 -67 C ATOM 798 N ASP A 106 -24.597 28.763 4.893 1.00 59.29 N ANISOU 798 N ASP A 106 7134 9161 6233 550 -381 76 N ATOM 799 CA ASP A 106 -25.720 29.660 4.555 1.00 61.28 C ANISOU 799 CA ASP A 106 7440 9272 6574 389 -347 132 C ATOM 800 C ASP A 106 -25.648 30.213 3.124 1.00 62.41 C ANISOU 800 C ASP A 106 7502 9479 6731 309 -285 183 C ATOM 801 O ASP A 106 -26.596 30.017 2.361 1.00 60.76 O ANISOU 801 O ASP A 106 7367 9175 6542 265 -269 228 O ATOM 802 CB ASP A 106 -25.961 30.860 5.511 1.00 63.92 C ANISOU 802 CB ASP A 106 7743 9562 6982 270 -353 134 C ATOM 803 CG ASP A 106 -26.469 30.563 6.921 1.00 67.73 C ANISOU 803 CG ASP A 106 8369 9902 7464 303 -393 118 C ATOM 804 OD1 ASP A 106 -26.606 29.378 7.281 1.00 69.65 O ANISOU 804 OD1 ASP A 106 8685 10153 7625 447 -437 85 O ATOM 805 OD2 ASP A 106 -26.802 31.550 7.618 1.00 68.45 O1- ANISOU 805 OD2 ASP A 106 8510 9871 7628 193 -371 142 O1- ATOM 806 N ILE A 107 -24.528 30.863 2.774 1.00 62.73 N ANISOU 806 N ILE A 107 7388 9694 6753 288 -249 178 N ATOM 807 CA ILE A 107 -24.367 31.549 1.490 1.00 59.13 C ANISOU 807 CA ILE A 107 6870 9299 6299 204 -172 242 C ATOM 808 C ILE A 107 -24.549 30.619 0.276 1.00 57.58 C ANISOU 808 C ILE A 107 6743 9120 6014 311 -167 246 C ATOM 809 O ILE A 107 -25.230 30.989 -0.678 1.00 62.91 O ANISOU 809 O ILE A 107 7472 9743 6688 261 -142 309 O ATOM 810 CB ILE A 107 -23.013 32.322 1.381 1.00 60.05 C ANISOU 810 CB ILE A 107 6799 9610 6407 142 -117 225 C ATOM 811 CG1 ILE A 107 -23.035 33.516 2.356 1.00 62.02 C ANISOU 811 CG1 ILE A 107 6996 9815 6754 -29 -104 225 C ATOM 812 CG2 ILE A 107 -22.644 32.819 -0.040 1.00 60.57 C ANISOU 812 CG2 ILE A 107 6819 9767 6431 99 -25 288 C ATOM 813 CD1 ILE A 107 -21.711 34.280 2.495 1.00 65.66 C ANISOU 813 CD1 ILE A 107 7262 10467 7216 -139 -41 195 C ATOM 814 N ASN A 108 -23.967 29.420 0.346 1.00 50.96 N ANISOU 814 N ASN A 108 5914 8358 5092 472 -195 173 N ATOM 815 CA ASN A 108 -24.004 28.456 -0.748 1.00 48.53 C ANISOU 815 CA ASN A 108 5675 8076 4688 575 -181 153 C ATOM 816 C ASN A 108 -25.306 27.653 -0.794 1.00 51.14 C ANISOU 816 C ASN A 108 6192 8221 5019 592 -231 138 C ATOM 817 O ASN A 108 -25.741 27.333 -1.899 1.00 53.56 O ANISOU 817 O ASN A 108 6561 8525 5264 603 -222 134 O ATOM 818 CB ASN A 108 -22.771 27.560 -0.641 1.00 49.57 C ANISOU 818 CB ASN A 108 5752 8353 4729 757 -179 74 C ATOM 819 CG ASN A 108 -21.511 28.336 -1.009 1.00 51.65 C ANISOU 819 CG ASN A 108 5795 8848 4981 727 -118 78 C ATOM 820 ND2 ASN A 108 -20.531 28.393 -0.121 1.00 51.34 N ANISOU 820 ND2 ASN A 108 5640 8883 4985 719 -149 49 N ATOM 821 OD1 ASN A 108 -21.435 28.935 -2.070 1.00 56.18 O ANISOU 821 OD1 ASN A 108 6301 9545 5500 702 -41 103 O ATOM 822 N LEU A 109 -25.951 27.391 0.353 1.00 53.18 N ANISOU 822 N LEU A 109 6538 8334 5335 582 -279 122 N ATOM 823 CA LEU A 109 -27.298 26.809 0.379 1.00 54.65 C ANISOU 823 CA LEU A 109 6883 8349 5534 555 -308 107 C ATOM 824 C LEU A 109 -28.333 27.800 -0.197 1.00 54.92 C ANISOU 824 C LEU A 109 6893 8346 5630 411 -300 175 C ATOM 825 O LEU A 109 -29.148 27.397 -1.028 1.00 56.48 O ANISOU 825 O LEU A 109 7156 8504 5798 388 -315 163 O ATOM 826 CB LEU A 109 -27.676 26.330 1.803 1.00 52.00 C ANISOU 826 CB LEU A 109 6652 7874 5233 578 -343 81 C ATOM 827 CG LEU A 109 -27.433 24.828 2.080 1.00 51.70 C ANISOU 827 CG LEU A 109 6713 7817 5111 757 -360 17 C ATOM 828 CD1 LEU A 109 -25.959 24.409 2.025 1.00 51.19 C ANISOU 828 CD1 LEU A 109 6797 7584 5067 768 -384 10 C ATOM 829 CD2 LEU A 109 -28.096 24.384 3.395 1.00 50.88 C ANISOU 829 CD2 LEU A 109 6715 7690 4925 832 -345 -41 C ATOM 830 N PHE A 110 -28.231 29.086 0.183 1.00 51.55 N ANISOU 830 N PHE A 110 6373 7931 5283 319 -279 241 N ATOM 831 CA PHE A 110 -29.000 30.178 -0.420 1.00 52.02 C ANISOU 831 CA PHE A 110 6406 7969 5389 223 -261 322 C ATOM 832 C PHE A 110 -28.712 30.316 -1.922 1.00 52.33 C ANISOU 832 C PHE A 110 6405 8135 5343 243 -231 361 C ATOM 833 O PHE A 110 -29.644 30.372 -2.720 1.00 51.89 O ANISOU 833 O PHE A 110 6378 8075 5265 223 -245 401 O ATOM 834 CB PHE A 110 -28.743 31.522 0.289 1.00 51.95 C ANISOU 834 CB PHE A 110 6332 7927 5477 130 -229 378 C ATOM 835 CG PHE A 110 -29.530 31.815 1.553 1.00 47.96 C ANISOU 835 CG PHE A 110 5883 7278 5061 82 -251 370 C ATOM 836 CD1 PHE A 110 -30.942 31.783 1.542 1.00 45.17 C ANISOU 836 CD1 PHE A 110 5580 6848 4736 60 -268 389 C ATOM 837 CD2 PHE A 110 -28.861 32.230 2.724 1.00 47.35 C ANISOU 837 CD2 PHE A 110 5796 7166 5027 60 -252 336 C ATOM 838 CE1 PHE A 110 -31.650 32.113 2.691 1.00 45.27 C ANISOU 838 CE1 PHE A 110 5630 6744 4825 17 -273 377 C ATOM 839 CE2 PHE A 110 -29.586 32.537 3.864 1.00 46.96 C ANISOU 839 CE2 PHE A 110 5806 6993 5044 18 -261 326 C ATOM 840 CZ PHE A 110 -30.973 32.479 3.846 1.00 45.60 C ANISOU 840 CZ PHE A 110 5682 6739 4906 -3 -263 348 C ATOM 841 N GLY A 111 -27.419 30.317 -2.277 1.00 49.99 N ANISOU 841 N GLY A 111 6035 7971 4989 287 -188 349 N ATOM 842 CA GLY A 111 -26.912 30.340 -3.645 1.00 50.86 C ANISOU 842 CA GLY A 111 6113 8212 4998 310 -143 385 C ATOM 843 C GLY A 111 -27.553 29.226 -4.479 1.00 53.98 C ANISOU 843 C GLY A 111 6603 8620 5289 392 -184 320 C ATOM 844 O GLY A 111 -28.095 29.522 -5.536 1.00 57.51 O ANISOU 844 O GLY A 111 7068 9120 5663 383 -182 362 O ATOM 845 N SER A 112 -27.576 27.985 -3.972 1.00 53.69 N ANISOU 845 N SER A 112 6640 8525 5233 475 -221 216 N ATOM 846 CA SER A 112 -28.199 26.826 -4.614 1.00 54.13 C ANISOU 846 CA SER A 112 6810 8567 5191 539 -252 130 C ATOM 847 C SER A 112 -29.690 27.062 -4.944 1.00 52.46 C ANISOU 847 C SER A 112 6652 8289 4993 448 -304 144 C ATOM 848 O SER A 112 -30.042 27.042 -6.125 1.00 56.72 O ANISOU 848 O SER A 112 7219 8901 5429 456 -320 121 O ATOM 849 CB SER A 112 -27.949 25.562 -3.759 1.00 54.50 C ANISOU 849 CB SER A 112 6965 8509 5235 634 -274 26 C ATOM 850 OG SER A 112 -28.177 24.364 -4.480 1.00 52.81 O ANISOU 850 OG SER A 112 6889 8237 4938 667 -297 -69 O ATOM 851 N VAL A 113 -30.527 27.376 -3.937 1.00 51.28 N ANISOU 851 N VAL A 113 6504 8021 4961 366 -332 176 N ATOM 852 CA VAL A 113 -31.966 27.592 -4.150 1.00 54.46 C ANISOU 852 CA VAL A 113 6925 8385 5381 288 -383 180 C ATOM 853 C VAL A 113 -32.272 28.793 -5.072 1.00 53.99 C ANISOU 853 C VAL A 113 6780 8425 5309 264 -378 297 C ATOM 854 O VAL A 113 -33.146 28.693 -5.935 1.00 53.47 O ANISOU 854 O VAL A 113 6714 8419 5184 250 -427 296 O ATOM 855 CB VAL A 113 -32.783 27.737 -2.829 1.00 53.36 C ANISOU 855 CB VAL A 113 6816 8094 5364 218 -400 166 C ATOM 856 CG1 VAL A 113 -32.681 26.482 -1.951 1.00 52.12 C ANISOU 856 CG1 VAL A 113 6786 7823 5194 247 -401 59 C ATOM 857 CG2 VAL A 113 -32.470 28.971 -1.967 1.00 52.39 C ANISOU 857 CG2 VAL A 113 6624 7940 5344 198 -363 252 C ATOM 858 N PHE A 114 -31.510 29.885 -4.929 1.00 51.61 N ANISOU 858 N PHE A 114 6412 8142 5056 257 -319 397 N ATOM 859 CA PHE A 114 -31.666 31.081 -5.751 1.00 52.29 C ANISOU 859 CA PHE A 114 6452 8289 5125 242 -298 526 C ATOM 860 C PHE A 114 -31.186 30.873 -7.200 1.00 56.58 C ANISOU 860 C PHE A 114 7002 8988 5507 297 -284 543 C ATOM 861 O PHE A 114 -31.826 31.381 -8.118 1.00 57.05 O ANISOU 861 O PHE A 114 7063 9115 5498 310 -307 621 O ATOM 862 CB PHE A 114 -30.971 32.285 -5.082 1.00 51.93 C ANISOU 862 CB PHE A 114 6359 8200 5173 195 -221 618 C ATOM 863 CG PHE A 114 -31.491 32.719 -3.714 1.00 51.23 C ANISOU 863 CG PHE A 114 6270 7965 5229 140 -233 615 C ATOM 864 CD1 PHE A 114 -32.866 32.683 -3.394 1.00 50.89 C ANISOU 864 CD1 PHE A 114 6256 7852 5229 135 -297 572 C ATOM 865 CD2 PHE A 114 -30.603 33.324 -2.795 1.00 51.39 C ANISOU 865 CD2 PHE A 114 6259 7931 5337 84 -174 645 C ATOM 866 CE1 PHE A 114 -33.307 33.144 -2.163 1.00 51.93 C ANISOU 866 CE1 PHE A 114 6389 7860 5482 90 -293 568 C ATOM 867 CE2 PHE A 114 -31.066 33.782 -1.570 1.00 53.54 C ANISOU 867 CE2 PHE A 114 6542 8073 5727 38 -182 632 C ATOM 868 CZ PHE A 114 -32.410 33.678 -1.248 1.00 53.39 C ANISOU 868 CZ PHE A 114 6558 7984 5744 49 -237 598 C ATOM 869 N LEU A 115 -30.109 30.102 -7.404 1.00 57.02 N ANISOU 869 N LEU A 115 7062 9115 5488 345 -245 472 N ATOM 870 CA LEU A 115 -29.567 29.811 -8.736 1.00 50.41 C ANISOU 870 CA LEU A 115 6239 8434 4482 404 -221 470 C ATOM 871 C LEU A 115 -30.387 28.744 -9.483 1.00 51.33 C ANISOU 871 C LEU A 115 6429 8578 4496 432 -309 367 C ATOM 872 O LEU A 115 -30.459 28.820 -10.708 1.00 53.54 O ANISOU 872 O LEU A 115 6725 8989 4629 464 -322 389 O ATOM 873 CB LEU A 115 -28.072 29.434 -8.627 1.00 44.51 C ANISOU 873 CB LEU A 115 5460 7766 3684 462 -145 413 C ATOM 874 CG LEU A 115 -27.171 30.652 -8.291 1.00 44.49 C ANISOU 874 CG LEU A 115 5357 7788 3760 413 -51 498 C ATOM 875 CD1 LEU A 115 -25.812 30.238 -7.689 1.00 45.24 C ANISOU 875 CD1 LEU A 115 5388 8000 3800 485 12 419 C ATOM 876 CD2 LEU A 115 -27.023 31.605 -9.495 1.00 45.31 C ANISOU 876 CD2 LEU A 115 5441 7949 3826 353 16 654 C ATOM 877 N ILE A 116 -31.041 27.821 -8.754 1.00 51.09 N ANISOU 877 N ILE A 116 6451 8430 4532 409 -367 251 N ATOM 878 CA ILE A 116 -32.029 26.880 -9.298 1.00 52.97 C ANISOU 878 CA ILE A 116 6756 8681 4689 392 -449 137 C ATOM 879 C ILE A 116 -33.332 27.586 -9.731 1.00 57.60 C ANISOU 879 C ILE A 116 7288 9333 5263 350 -520 212 C ATOM 880 O ILE A 116 -33.878 27.248 -10.782 1.00 62.05 O ANISOU 880 O ILE A 116 7865 10025 5686 362 -578 174 O ATOM 881 CB ILE A 116 -32.346 25.733 -8.290 1.00 49.33 C ANISOU 881 CB ILE A 116 6375 8052 4314 351 -476 9 C ATOM 882 CG1 ILE A 116 -31.144 24.769 -8.202 1.00 48.17 C ANISOU 882 CG1 ILE A 116 6324 7871 4106 441 -428 -97 C ATOM 883 CG2 ILE A 116 -33.637 24.935 -8.575 1.00 51.01 C ANISOU 883 CG2 ILE A 116 6623 8258 4499 266 -560 -87 C ATOM 884 CD1 ILE A 116 -31.155 23.854 -6.968 1.00 45.45 C ANISOU 884 CD1 ILE A 116 6107 7340 3822 414 -443 -216 C ATOM 885 N ALA A 117 -33.774 28.577 -8.937 1.00 58.47 N ANISOU 885 N ALA A 117 7336 9368 5511 311 -518 315 N ATOM 886 CA ALA A 117 -34.907 29.447 -9.249 1.00 60.52 C ANISOU 886 CA ALA A 117 7537 9698 5761 311 -577 407 C ATOM 887 C ALA A 117 -34.629 30.394 -10.431 1.00 61.67 C ANISOU 887 C ALA A 117 7674 9977 5781 384 -546 546 C ATOM 888 O ALA A 117 -35.544 30.648 -11.212 1.00 63.12 O ANISOU 888 O ALA A 117 7834 10276 5872 424 -616 602 O ATOM 889 CB ALA A 117 -35.304 30.222 -7.984 1.00 0.00 C ATOM 890 N LEU A 118 -33.372 30.851 -10.575 1.00 62.30 N ANISOU 890 N LEU A 118 7770 10054 5849 404 -441 608 N ATOM 891 CA LEU A 118 -32.906 31.650 -11.710 1.00 62.57 C ANISOU 891 CA LEU A 118 7815 10208 5751 456 -385 745 C ATOM 892 C LEU A 118 -32.856 30.837 -13.017 1.00 65.04 C ANISOU 892 C LEU A 118 8169 10694 5848 512 -421 667 C ATOM 893 O LEU A 118 -33.235 31.377 -14.054 1.00 65.83 O ANISOU 893 O LEU A 118 8286 10927 5800 567 -444 761 O ATOM 894 CB LEU A 118 -31.543 32.296 -11.365 1.00 0.00 C ATOM 895 CG LEU A 118 -30.961 33.258 -12.428 1.00 0.00 C ATOM 896 CD1 LEU A 118 -31.902 34.440 -12.743 1.00 0.00 C ATOM 897 CD2 LEU A 118 -29.554 33.739 -12.021 1.00 0.00 C ATOM 898 N ILE A 119 -32.444 29.557 -12.941 1.00 65.43 N ANISOU 898 N ILE A 119 8251 10743 5865 509 -426 496 N ATOM 899 CA ILE A 119 -32.461 28.608 -14.062 1.00 58.32 C ANISOU 899 CA ILE A 119 7407 9992 4759 557 -461 388 C ATOM 900 C ILE A 119 -33.890 28.286 -14.549 1.00 55.42 C ANISOU 900 C ILE A 119 7039 9703 4318 542 -602 339 C ATOM 901 O ILE A 119 -34.087 28.164 -15.757 1.00 58.90 O ANISOU 901 O ILE A 119 7501 10320 4558 592 -645 343 O ATOM 902 CB ILE A 119 -31.686 27.294 -13.721 1.00 57.23 C ANISOU 902 CB ILE A 119 7328 9794 4625 566 -433 205 C ATOM 903 CG1 ILE A 119 -30.164 27.560 -13.706 1.00 58.93 C ANISOU 903 CG1 ILE A 119 7513 10008 4870 611 -299 252 C ATOM 904 CG2 ILE A 119 -31.978 26.077 -14.631 1.00 50.90 C ANISOU 904 CG2 ILE A 119 6607 9111 3621 603 -480 56 C ATOM 905 CD1 ILE A 119 -29.358 26.530 -12.905 1.00 58.05 C ANISOU 905 CD1 ILE A 119 7452 9824 4780 660 -271 91 C ATOM 906 N ALA A 120 -34.860 28.205 -13.620 1.00 53.50 N ANISOU 906 N ALA A 120 6754 9349 4222 470 -676 287 N ATOM 907 CA ALA A 120 -36.280 28.016 -13.928 1.00 58.02 C ANISOU 907 CA ALA A 120 7286 10022 4735 441 -812 224 C ATOM 908 C ALA A 120 -36.875 29.180 -14.737 1.00 61.63 C ANISOU 908 C ALA A 120 7686 10621 5109 523 -857 404 C ATOM 909 O ALA A 120 -37.592 28.927 -15.706 1.00 66.46 O ANISOU 909 O ALA A 120 8282 11423 5547 559 -960 372 O ATOM 910 CB ALA A 120 -37.067 27.782 -12.629 1.00 57.53 C ANISOU 910 CB ALA A 120 7179 9818 4864 338 -855 143 C ATOM 911 N LEU A 121 -36.522 30.420 -14.352 1.00 60.86 N ANISOU 911 N LEU A 121 7569 10432 5124 559 -779 591 N ATOM 912 CA LEU A 121 -36.890 31.656 -15.043 1.00 64.68 C ANISOU 912 CA LEU A 121 8035 11013 5529 660 -803 785 C ATOM 913 C LEU A 121 -36.189 31.812 -16.402 1.00 67.35 C ANISOU 913 C LEU A 121 8445 11524 5621 742 -777 853 C ATOM 914 O LEU A 121 -36.828 32.280 -17.342 1.00 69.19 O ANISOU 914 O LEU A 121 8672 11930 5688 833 -867 922 O ATOM 915 CB LEU A 121 -36.572 32.870 -14.143 1.00 67.14 C ANISOU 915 CB LEU A 121 8348 11150 6012 667 -699 960 C ATOM 916 CG LEU A 121 -37.446 32.974 -12.874 1.00 69.43 C ANISOU 916 CG LEU A 121 8567 11299 6516 626 -732 944 C ATOM 917 CD1 LEU A 121 -36.854 33.999 -11.881 1.00 69.29 C ANISOU 917 CD1 LEU A 121 8580 11093 6652 618 -608 1091 C ATOM 918 CD2 LEU A 121 -38.928 33.253 -13.208 1.00 72.95 C ANISOU 918 CD2 LEU A 121 8931 11872 6915 705 -864 972 C ATOM 919 N ASP A 122 -34.907 31.412 -16.484 1.00 68.79 N ANISOU 919 N ASP A 122 8689 11681 5767 721 -653 834 N ATOM 920 CA ASP A 122 -34.058 31.507 -17.676 1.00 70.26 C ANISOU 920 CA ASP A 122 8946 12036 5714 794 -601 900 C ATOM 921 C ASP A 122 -34.603 30.653 -18.840 1.00 68.90 C ANISOU 921 C ASP A 122 8793 12059 5327 821 -725 737 C ATOM 922 O ASP A 122 -34.729 31.159 -19.956 1.00 70.85 O ANISOU 922 O ASP A 122 9077 12496 5348 910 -767 816 O ATOM 923 CB ASP A 122 -32.592 31.130 -17.339 1.00 72.25 C ANISOU 923 CB ASP A 122 9230 12236 5987 760 -434 891 C ATOM 924 CG ASP A 122 -31.590 31.415 -18.460 1.00 78.86 C ANISOU 924 CG ASP A 122 10134 13243 6585 826 -342 987 C ATOM 925 OD1 ASP A 122 -31.710 32.495 -19.079 1.00 79.86 O ANISOU 925 OD1 ASP A 122 10296 13371 6676 855 -266 1203 O ATOM 926 OD2 ASP A 122 -30.674 30.585 -18.644 1.00 80.27 O1- ANISOU 926 OD2 ASP A 122 10347 13545 6607 849 -336 844 O1- ATOM 927 N ARG A 123 -34.950 29.391 -18.537 1.00 64.55 N ANISOU 927 N ARG A 123 8231 11461 4834 743 -782 507 N ATOM 928 CA ARG A 123 -35.558 28.438 -19.467 1.00 63.27 C ANISOU 928 CA ARG A 123 8093 11466 4482 738 -903 321 C ATOM 929 C ARG A 123 -36.980 28.841 -19.888 1.00 67.67 C ANISOU 929 C ARG A 123 8568 12170 4975 760 -1072 349 C ATOM 930 O ARG A 123 -37.336 28.631 -21.045 1.00 72.14 O ANISOU 930 O ARG A 123 9148 12961 5302 809 -1172 299 O ATOM 931 CB ARG A 123 -35.576 27.037 -18.827 1.00 58.53 C ANISOU 931 CB ARG A 123 7521 10734 3984 631 -914 75 C ATOM 932 CG ARG A 123 -34.188 26.429 -18.574 1.00 56.60 C ANISOU 932 CG ARG A 123 7364 10398 3745 651 -772 10 C ATOM 933 CD ARG A 123 -34.283 25.191 -17.675 1.00 56.49 C ANISOU 933 CD ARG A 123 7395 10199 3869 567 -777 -193 C ATOM 934 NE ARG A 123 -33.002 24.488 -17.560 1.00 59.52 N ANISOU 934 NE ARG A 123 7878 10539 4197 623 -669 -298 N ATOM 935 CZ ARG A 123 -32.762 23.465 -16.725 1.00 62.54 C ANISOU 935 CZ ARG A 123 8338 10741 4682 593 -642 -455 C ATOM 936 NH1 ARG A 123 -33.712 22.989 -15.907 1.00 61.07 N1+ ANISOU 936 NH1 ARG A 123 8148 10398 4658 483 -706 -519 N1+ ATOM 937 NH2 ARG A 123 -31.547 22.911 -16.709 1.00 65.13 N1+ ANISOU 937 NH2 ARG A 123 8753 11048 4944 684 -543 -540 N1+ ATOM 938 N CYS A 124 -37.761 29.417 -18.958 1.00 67.84 N ANISOU 938 N CYS A 124 8494 12083 5198 734 -1109 422 N ATOM 939 CA CYS A 124 -39.119 29.907 -19.201 1.00 68.16 C ANISOU 939 CA CYS A 124 8426 12280 5194 776 -1268 449 C ATOM 940 C CYS A 124 -39.142 31.110 -20.159 1.00 71.56 C ANISOU 940 C CYS A 124 8882 12879 5428 948 -1288 672 C ATOM 941 O CYS A 124 -39.957 31.129 -21.077 1.00 74.59 O ANISOU 941 O CYS A 124 9204 13496 5641 1021 -1442 659 O ATOM 942 CB CYS A 124 -39.840 30.189 -17.873 1.00 65.43 C ANISOU 942 CB CYS A 124 7977 11773 5113 729 -1274 488 C ATOM 943 SG CYS A 124 -41.549 30.765 -18.068 1.00 70.56 S ANISOU 943 SG CYS A 124 8450 12624 5734 797 -1462 512 S ATOM 944 N VAL A 125 -38.202 32.048 -19.969 1.00 69.68 N ANISOU 944 N VAL A 125 8735 12533 5205 1011 -1133 877 N ATOM 945 CA VAL A 125 -37.978 33.200 -20.841 1.00 72.80 C ANISOU 945 CA VAL A 125 9193 13051 5416 1172 -1124 1114 C ATOM 946 C VAL A 125 -37.562 32.813 -22.280 1.00 76.54 C ANISOU 946 C VAL A 125 9751 13758 5572 1224 -1146 1070 C ATOM 947 O VAL A 125 -37.948 33.516 -23.211 1.00 79.92 O ANISOU 947 O VAL A 125 10201 14395 5772 1363 -1239 1181 O ATOM 948 CB VAL A 125 -36.965 34.181 -20.173 1.00 0.00 C ATOM 949 CG1 VAL A 125 -36.194 35.132 -21.105 1.00 0.00 C ATOM 950 CG2 VAL A 125 -37.663 34.999 -19.072 1.00 0.00 C ATOM 951 N CYS A 126 -36.857 31.680 -22.453 1.00 75.74 N ANISOU 951 N CYS A 126 9704 13635 5441 1132 -1066 903 N ATOM 952 CA CYS A 126 -36.533 31.104 -23.764 1.00 77.28 C ANISOU 952 CA CYS A 126 9986 14048 5328 1181 -1072 836 C ATOM 953 C CYS A 126 -37.756 30.470 -24.453 1.00 80.87 C ANISOU 953 C CYS A 126 10384 14744 5597 1198 -1292 669 C ATOM 954 O CYS A 126 -37.938 30.682 -25.650 1.00 87.79 O ANISOU 954 O CYS A 126 11310 15865 6179 1309 -1360 723 O ATOM 955 CB CYS A 126 -35.401 30.061 -23.678 1.00 76.44 C ANISOU 955 CB CYS A 126 9938 13856 5250 1092 -942 663 C ATOM 956 SG CYS A 126 -33.830 30.863 -23.268 1.00 80.60 S ANISOU 956 SG CYS A 126 10514 14202 5908 1082 -680 845 S ATOM 957 N VAL A 127 -38.548 29.693 -23.696 1.00 77.71 N ANISOU 957 N VAL A 127 9878 14290 5356 1077 -1403 461 N ATOM 958 CA VAL A 127 -39.663 28.893 -24.212 1.00 79.41 C ANISOU 958 CA VAL A 127 10022 14741 5411 1046 -1608 260 C ATOM 959 C VAL A 127 -40.918 29.730 -24.535 1.00 82.28 C ANISOU 959 C VAL A 127 10266 15294 5702 1173 -1767 409 C ATOM 960 O VAL A 127 -41.534 29.497 -25.576 1.00 88.10 O ANISOU 960 O VAL A 127 10980 16215 6279 1214 -1890 347 O ATOM 961 CB VAL A 127 -40.015 27.743 -23.222 1.00 79.01 C ANISOU 961 CB VAL A 127 9909 14553 5559 849 -1650 -15 C ATOM 962 CG1 VAL A 127 -41.351 27.017 -23.480 1.00 69.78 C ANISOU 962 CG1 VAL A 127 8667 13629 4219 773 -1849 -255 C ATOM 963 CG2 VAL A 127 -38.888 26.698 -23.190 1.00 79.06 C ANISOU 963 CG2 VAL A 127 10049 14352 5639 768 -1486 -136 C ATOM 964 N LEU A 128 -41.263 30.685 -23.657 1.00 77.55 N ANISOU 964 N LEU A 128 9601 14538 5328 1221 -1728 595 N ATOM 965 CA LEU A 128 -42.423 31.564 -23.813 1.00 78.65 C ANISOU 965 CA LEU A 128 9615 14839 5430 1362 -1878 725 C ATOM 966 C LEU A 128 -42.114 32.786 -24.694 1.00 81.09 C ANISOU 966 C LEU A 128 10044 15165 5602 1562 -1820 1000 C ATOM 967 O LEU A 128 -43.034 33.267 -25.358 1.00 81.30 O ANISOU 967 O LEU A 128 10017 15342 5532 1683 -1944 1047 O ATOM 968 CB LEU A 128 -42.956 32.021 -22.431 1.00 75.88 C ANISOU 968 CB LEU A 128 9154 14275 5403 1328 -1846 785 C ATOM 969 CG LEU A 128 -43.865 31.004 -21.696 1.00 73.51 C ANISOU 969 CG LEU A 128 8672 13988 5268 1162 -1957 536 C ATOM 970 CD1 LEU A 128 -43.149 29.719 -21.231 1.00 66.73 C ANISOU 970 CD1 LEU A 128 7873 13028 4453 938 -1907 266 C ATOM 971 CD2 LEU A 128 -44.617 31.684 -20.534 1.00 73.73 C ANISOU 971 CD2 LEU A 128 8614 13799 5600 1156 -1893 633 C ATOM 972 N HIS A 129 -40.857 33.271 -24.684 1.00 81.57 N ANISOU 972 N HIS A 129 10265 15079 5650 1594 -1627 1184 N ATOM 973 CA HIS A 129 -40.446 34.517 -25.345 1.00 82.49 C ANISOU 973 CA HIS A 129 10527 15175 5642 1755 -1535 1457 C ATOM 974 C HIS A 129 -39.157 34.341 -26.185 1.00 83.11 C ANISOU 974 C HIS A 129 10765 15250 5563 1708 -1377 1455 C ATOM 975 O HIS A 129 -38.190 35.063 -25.940 1.00 81.55 O ANISOU 975 O HIS A 129 10671 14901 5415 1690 -1181 1612 O ATOM 976 CB HIS A 129 -40.324 35.655 -24.294 1.00 81.28 C ANISOU 976 CB HIS A 129 10413 14815 5654 1841 -1426 1728 C ATOM 977 CG HIS A 129 -41.467 35.777 -23.313 1.00 80.28 C ANISOU 977 CG HIS A 129 10118 14659 5727 1860 -1544 1699 C ATOM 978 CD2 HIS A 129 -41.517 35.591 -21.949 1.00 79.57 C ANISOU 978 CD2 HIS A 129 9973 14312 5948 1758 -1462 1683 C ATOM 979 ND1 HIS A 129 -42.759 36.100 -23.692 1.00 83.84 N ANISOU 979 ND1 HIS A 129 10426 15273 6156 1952 -1735 1637 N ATOM 980 CE1 HIS A 129 -43.508 36.088 -22.587 1.00 81.79 C ANISOU 980 CE1 HIS A 129 10020 14957 6099 1947 -1789 1617 C ATOM 981 NE2 HIS A 129 -42.823 35.784 -21.492 1.00 79.97 N ANISOU 981 NE2 HIS A 129 9851 14438 6096 1819 -1615 1637 N ATOM 982 N PRO A 130 -39.137 33.408 -27.172 1.00 85.88 N ANISOU 982 N PRO A 130 11136 15774 5721 1682 -1449 1273 N ATOM 983 CA PRO A 130 -37.959 33.208 -28.045 1.00 87.19 C ANISOU 983 CA PRO A 130 11448 15951 5728 1651 -1290 1262 C ATOM 984 C PRO A 130 -37.608 34.415 -28.943 1.00 89.35 C ANISOU 984 C PRO A 130 11875 16208 5866 1775 -1160 1546 C ATOM 985 O PRO A 130 -36.438 34.589 -29.285 1.00 88.88 O ANISOU 985 O PRO A 130 11925 16083 5761 1737 -958 1623 O ATOM 986 CB PRO A 130 -38.327 31.970 -28.878 1.00 88.74 C ANISOU 986 CB PRO A 130 11623 16338 5755 1600 -1427 983 C ATOM 987 CG PRO A 130 -39.845 32.002 -28.953 1.00 91.10 C ANISOU 987 CG PRO A 130 11798 16768 6046 1664 -1648 962 C ATOM 988 CD PRO A 130 -40.243 32.539 -27.584 1.00 89.62 C ANISOU 988 CD PRO A 130 11495 16448 6109 1673 -1670 1065 C ATOM 989 N VAL A 131 -38.620 35.239 -29.267 1.00 91.60 N ANISOU 989 N VAL A 131 12170 16553 6083 1922 -1266 1702 N ATOM 990 CA VAL A 131 -38.502 36.489 -30.020 1.00 94.58 C ANISOU 990 CA VAL A 131 12719 16886 6328 2041 -1138 1987 C ATOM 991 C VAL A 131 -37.775 37.602 -29.229 1.00 95.29 C ANISOU 991 C VAL A 131 12884 16726 6596 2023 -939 2222 C ATOM 992 O VAL A 131 -37.163 38.472 -29.848 1.00 96.24 O ANISOU 992 O VAL A 131 13160 16765 6644 2009 -733 2393 O ATOM 993 CB VAL A 131 -39.913 36.992 -30.456 1.00 93.59 C ANISOU 993 CB VAL A 131 12588 16880 6090 2222 -1309 2093 C ATOM 994 CG1 VAL A 131 -39.945 38.383 -31.126 1.00 92.83 C ANISOU 994 CG1 VAL A 131 12700 16705 5866 2351 -1170 2406 C ATOM 995 CG2 VAL A 131 -40.597 35.971 -31.387 1.00 92.83 C ANISOU 995 CG2 VAL A 131 12424 17049 5797 2219 -1494 1856 C ATOM 996 N TRP A 132 -37.819 37.536 -27.886 1.00 96.91 N ANISOU 996 N TRP A 132 12978 16807 7035 2009 -988 2228 N ATOM 997 CA TRP A 132 -37.114 38.452 -26.994 1.00 94.49 C ANISOU 997 CA TRP A 132 12739 16255 6909 1971 -801 2427 C ATOM 998 C TRP A 132 -35.645 38.035 -26.793 1.00 93.72 C ANISOU 998 C TRP A 132 12650 16102 6856 1798 -616 2346 C ATOM 999 O TRP A 132 -34.769 38.896 -26.876 1.00 93.99 O ANISOU 999 O TRP A 132 12786 15979 6946 1746 -402 2530 O ATOM 1000 CB TRP A 132 -37.884 38.552 -25.660 1.00 91.08 C ANISOU 1000 CB TRP A 132 12179 15718 6710 1998 -905 2429 C ATOM 1001 CG TRP A 132 -37.362 39.532 -24.649 1.00 90.01 C ANISOU 1001 CG TRP A 132 12121 15317 6761 1965 -723 2636 C ATOM 1002 CD1 TRP A 132 -37.694 40.841 -24.588 1.00 91.07 C ANISOU 1002 CD1 TRP A 132 12381 15272 6950 2085 -652 2898 C ATOM 1003 CD2 TRP A 132 -36.362 39.326 -23.603 1.00 88.06 C ANISOU 1003 CD2 TRP A 132 11830 14871 6757 1760 -575 2537 C ATOM 1004 CE2 TRP A 132 -36.154 40.565 -22.925 1.00 86.96 C ANISOU 1004 CE2 TRP A 132 11787 14450 6803 1749 -423 2745 C ATOM 1005 CE3 TRP A 132 -35.602 38.219 -23.160 1.00 87.76 C ANISOU 1005 CE3 TRP A 132 11687 14838 6820 1581 -554 2277 C ATOM 1006 NE1 TRP A 132 -36.994 41.451 -23.566 1.00 88.75 N ANISOU 1006 NE1 TRP A 132 12134 14708 6879 1966 -470 2987 N ATOM 1007 CZ2 TRP A 132 -35.242 40.698 -21.862 1.00 88.17 C ANISOU 1007 CZ2 TRP A 132 11915 14358 7228 1553 -264 2689 C ATOM 1008 CZ3 TRP A 132 -34.676 38.340 -22.104 1.00 87.49 C ANISOU 1008 CZ3 TRP A 132 11628 14562 7052 1415 -399 2239 C ATOM 1009 CH2 TRP A 132 -34.497 39.575 -21.454 1.00 87.86 C ANISOU 1009 CH2 TRP A 132 11752 14361 7272 1396 -262 2439 C ATOM 1010 N THR A 133 -35.397 36.739 -26.532 1.00 93.73 N ANISOU 1010 N THR A 133 12549 16230 6835 1705 -689 2067 N ATOM 1011 CA THR A 133 -34.074 36.203 -26.186 1.00 95.62 C ANISOU 1011 CA THR A 133 12780 16424 7128 1564 -525 1965 C ATOM 1012 C THR A 133 -33.044 36.220 -27.331 1.00101.13 C ANISOU 1012 C THR A 133 13610 17166 7647 1555 -323 2068 C ATOM 1013 O THR A 133 -31.852 36.313 -27.037 1.00101.03 O ANISOU 1013 O THR A 133 13625 17043 7717 1465 -109 2162 O ATOM 1014 CB THR A 133 -34.159 34.749 -25.664 1.00 0.00 C ATOM 1015 CG2 THR A 133 -34.952 34.638 -24.364 1.00 0.00 C ATOM 1016 OG1 THR A 133 -34.692 33.858 -26.626 1.00 0.00 O ATOM 1017 N GLN A 134 -33.496 36.187 -28.595 1.00103.79 N ANISOU 1017 N GLN A 134 14020 17658 7757 1632 -382 2039 N ATOM 1018 CA GLN A 134 -32.635 36.310 -29.777 1.00106.79 C ANISOU 1018 CA GLN A 134 14526 18094 7955 1620 -190 2120 C ATOM 1019 C GLN A 134 -31.975 37.700 -29.937 1.00108.45 C ANISOU 1019 C GLN A 134 14876 18162 8167 1642 -15 2447 C ATOM 1020 O GLN A 134 -31.050 37.819 -30.740 1.00111.05 O ANISOU 1020 O GLN A 134 15298 18497 8401 1584 200 2537 O ATOM 1021 CB GLN A 134 -33.431 35.890 -31.032 1.00110.76 C ANISOU 1021 CB GLN A 134 15079 18802 8201 1699 -309 2002 C ATOM 1022 CG GLN A 134 -34.623 36.810 -31.363 1.00116.56 C ANISOU 1022 CG GLN A 134 15858 19584 8845 1841 -483 2128 C ATOM 1023 CD GLN A 134 -35.445 36.364 -32.572 1.00119.94 C ANISOU 1023 CD GLN A 134 16266 20238 9070 1894 -675 1925 C ATOM 1024 NE2 GLN A 134 -36.317 37.251 -33.052 1.00122.06 N ANISOU 1024 NE2 GLN A 134 16615 20599 9163 2027 -765 2060 N ATOM 1025 OE1 GLN A 134 -35.319 35.242 -33.060 1.00119.97 O ANISOU 1025 OE1 GLN A 134 16191 20325 9067 1814 -739 1648 O ATOM 1026 N ASN A 135 -32.449 38.708 -29.179 1.00109.23 N ANISOU 1026 N ASN A 135 14998 18126 8377 1720 -92 2620 N ATOM 1027 CA ASN A 135 -31.930 40.078 -29.182 1.00113.19 C ANISOU 1027 CA ASN A 135 15669 18454 8886 1746 69 2930 C ATOM 1028 C ASN A 135 -31.360 40.478 -27.809 1.00111.60 C ANISOU 1028 C ASN A 135 15453 18010 8940 1643 211 3052 C ATOM 1029 O ASN A 135 -30.332 41.154 -27.780 1.00115.19 O ANISOU 1029 O ASN A 135 16062 18288 9419 1612 399 3292 O ATOM 1030 CB ASN A 135 -33.042 41.076 -29.590 1.00118.38 C ANISOU 1030 CB ASN A 135 16404 19114 9461 1939 -99 3067 C ATOM 1031 CG ASN A 135 -33.661 40.802 -30.963 1.00121.90 C ANISOU 1031 CG ASN A 135 16945 19758 9614 2032 -152 3062 C ATOM 1032 ND2 ASN A 135 -32.907 41.054 -32.036 1.00124.07 N ANISOU 1032 ND2 ASN A 135 17422 19960 9757 2045 25 3293 N ATOM 1033 OD1 ASN A 135 -34.808 40.373 -31.056 1.00122.17 O ANISOU 1033 OD1 ASN A 135 16878 20002 9538 2077 -344 2849 O ATOM 1034 N HIS A 136 -32.041 40.101 -26.710 1.00105.75 N ANISOU 1034 N HIS A 136 14546 17248 8387 1581 134 2893 N ATOM 1035 CA HIS A 136 -31.781 40.643 -25.371 1.00103.92 C ANISOU 1035 CA HIS A 136 14288 16749 8446 1464 250 2969 C ATOM 1036 C HIS A 136 -30.959 39.719 -24.460 1.00 96.77 C ANISOU 1036 C HIS A 136 13201 15777 7789 1282 272 2703 C ATOM 1037 O HIS A 136 -30.167 40.242 -23.675 1.00 94.33 O ANISOU 1037 O HIS A 136 12870 15253 7718 1133 422 2733 O ATOM 1038 CB HIS A 136 -33.112 40.992 -24.678 1.00108.10 C ANISOU 1038 CB HIS A 136 14816 17138 9120 1587 99 3055 C ATOM 1039 CG HIS A 136 -33.936 42.056 -25.361 1.00117.02 C ANISOU 1039 CG HIS A 136 16125 18259 10080 1777 73 3304 C ATOM 1040 CD2 HIS A 136 -34.037 43.413 -25.146 1.00120.39 C ANISOU 1040 CD2 HIS A 136 16741 18449 10551 1811 216 3570 C ATOM 1041 ND1 HIS A 136 -34.831 41.777 -26.377 1.00120.58 N ANISOU 1041 ND1 HIS A 136 16567 18906 10342 1931 -119 3242 N ATOM 1042 CE1 HIS A 136 -35.403 42.929 -26.733 1.00123.47 C ANISOU 1042 CE1 HIS A 136 17102 19176 10634 2072 -101 3468 C ATOM 1043 NE2 HIS A 136 -34.969 43.966 -26.026 1.00123.29 N ANISOU 1043 NE2 HIS A 136 17215 18880 10752 2004 104 3669 N ATOM 1044 N ARG A 137 -31.161 38.390 -24.547 1.00 90.15 N ANISOU 1044 N ARG A 137 12241 15109 6902 1287 132 2443 N ATOM 1045 CA ARG A 137 -30.511 37.405 -23.675 1.00 82.37 C ANISOU 1045 CA ARG A 137 11108 14057 6132 1144 151 2198 C ATOM 1046 C ARG A 137 -29.059 37.157 -24.120 1.00 82.37 C ANISOU 1046 C ARG A 137 11117 14133 6048 1053 364 2177 C ATOM 1047 O ARG A 137 -28.809 36.300 -24.967 1.00 83.84 O ANISOU 1047 O ARG A 137 11307 14530 6020 1095 358 2058 O ATOM 1048 CB ARG A 137 -31.367 36.120 -23.618 1.00 77.29 C ANISOU 1048 CB ARG A 137 10366 13539 5462 1185 -65 1937 C ATOM 1049 CG ARG A 137 -30.841 35.027 -22.670 1.00 74.05 C ANISOU 1049 CG ARG A 137 9839 13062 5233 1068 -49 1685 C ATOM 1050 CD ARG A 137 -31.826 33.860 -22.527 1.00 73.29 C ANISOU 1050 CD ARG A 137 9695 13089 5064 1104 -243 1438 C ATOM 1051 NE ARG A 137 -31.256 32.728 -21.787 1.00 72.00 N ANISOU 1051 NE ARG A 137 9455 12837 5066 1014 -232 1206 N ATOM 1052 CZ ARG A 137 -30.517 31.728 -22.292 1.00 75.27 C ANISOU 1052 CZ ARG A 137 9881 13341 5378 1009 -151 1060 C ATOM 1053 NH1 ARG A 137 -30.188 31.687 -23.590 1.00 79.79 N1+ ANISOU 1053 NH1 ARG A 137 10530 14103 5684 1073 -67 1115 N1+ ATOM 1054 NH2 ARG A 137 -30.105 30.750 -21.475 1.00 73.33 N1+ ANISOU 1054 NH2 ARG A 137 9580 12992 5289 955 -148 864 N1+ ATOM 1055 N THR A 138 -28.145 37.947 -23.539 1.00 81.61 N ANISOU 1055 N THR A 138 11015 13873 6122 919 556 2281 N ATOM 1056 CA THR A 138 -26.714 37.959 -23.834 1.00 81.84 C ANISOU 1056 CA THR A 138 11027 13981 6088 815 783 2286 C ATOM 1057 C THR A 138 -25.912 37.658 -22.555 1.00 78.39 C ANISOU 1057 C THR A 138 10420 13454 5913 679 837 2106 C ATOM 1058 O THR A 138 -26.434 37.794 -21.447 1.00 74.38 O ANISOU 1058 O THR A 138 9838 12781 5643 647 726 2021 O ATOM 1059 CB THR A 138 -26.280 39.363 -24.351 1.00 85.79 C ANISOU 1059 CB THR A 138 11666 14396 6533 751 993 2573 C ATOM 1060 CG2 THR A 138 -27.014 39.794 -25.631 1.00 88.51 C ANISOU 1060 CG2 THR A 138 12201 14829 6602 919 935 2775 C ATOM 1061 OG1 THR A 138 -26.434 40.378 -23.372 1.00 84.75 O ANISOU 1061 OG1 THR A 138 11531 13989 6681 647 1026 2658 O ATOM 1062 N VAL A 139 -24.638 37.272 -22.745 1.00 79.83 N ANISOU 1062 N VAL A 139 10534 13764 6033 609 1012 2049 N ATOM 1063 CA VAL A 139 -23.647 37.039 -21.687 1.00 76.76 C ANISOU 1063 CA VAL A 139 9971 13326 5867 493 1079 1896 C ATOM 1064 C VAL A 139 -23.402 38.281 -20.799 1.00 74.09 C ANISOU 1064 C VAL A 139 9616 12775 5760 328 1185 2029 C ATOM 1065 O VAL A 139 -23.205 38.127 -19.594 1.00 69.73 O ANISOU 1065 O VAL A 139 8950 12096 5450 257 1131 1918 O ATOM 1066 CB VAL A 139 -22.301 36.552 -22.307 1.00 77.62 C ANISOU 1066 CB VAL A 139 9997 13662 5834 482 1246 1804 C ATOM 1067 CG1 VAL A 139 -21.062 36.610 -21.385 1.00 77.03 C ANISOU 1067 CG1 VAL A 139 9734 13559 5974 343 1368 1719 C ATOM 1068 CG2 VAL A 139 -22.452 35.130 -22.876 1.00 75.81 C ANISOU 1068 CG2 VAL A 139 9759 13591 5454 640 1117 1588 C ATOM 1069 N SER A 140 -23.470 39.481 -21.406 1.00 77.82 N ANISOU 1069 N SER A 140 10218 13198 6151 261 1339 2267 N ATOM 1070 CA SER A 140 -23.367 40.775 -20.732 1.00 79.70 C ANISOU 1070 CA SER A 140 10475 13207 6599 87 1454 2393 C ATOM 1071 C SER A 140 -24.529 41.050 -19.761 1.00 79.67 C ANISOU 1071 C SER A 140 10501 12971 6797 130 1273 2386 C ATOM 1072 O SER A 140 -24.280 41.581 -18.680 1.00 79.62 O ANISOU 1072 O SER A 140 10414 12804 7033 0 1289 2331 O ATOM 1073 CB SER A 140 -23.264 41.893 -21.788 1.00 83.65 C ANISOU 1073 CB SER A 140 11166 13664 6952 30 1649 2668 C ATOM 1074 OG SER A 140 -21.969 41.913 -22.352 1.00 88.06 O ANISOU 1074 OG SER A 140 11705 14460 7295 -1 1823 2682 O ATOM 1075 N LEU A 141 -25.761 40.664 -20.144 1.00 77.44 N ANISOU 1075 N LEU A 141 10323 12692 6410 312 1096 2429 N ATOM 1076 CA LEU A 141 -26.953 40.751 -19.296 1.00 74.90 C ANISOU 1076 CA LEU A 141 10008 12182 6269 366 926 2409 C ATOM 1077 C LEU A 141 -26.927 39.712 -18.161 1.00 77.02 C ANISOU 1077 C LEU A 141 10101 12458 6704 351 791 2151 C ATOM 1078 O LEU A 141 -27.235 40.064 -17.024 1.00 77.75 O ANISOU 1078 O LEU A 141 10152 12369 7022 297 737 2108 O ATOM 1079 CB LEU A 141 -28.225 40.615 -20.171 1.00 72.22 C ANISOU 1079 CB LEU A 141 9789 11894 5759 570 767 2508 C ATOM 1080 CG LEU A 141 -29.570 40.773 -19.417 1.00 68.04 C ANISOU 1080 CG LEU A 141 9271 11192 5390 650 606 2523 C ATOM 1081 CD1 LEU A 141 -29.736 42.172 -18.788 1.00 69.76 C ANISOU 1081 CD1 LEU A 141 9613 11145 5749 582 736 2720 C ATOM 1082 CD2 LEU A 141 -30.766 40.398 -20.314 1.00 65.56 C ANISOU 1082 CD2 LEU A 141 9009 11018 4883 861 419 2561 C ATOM 1083 N ALA A 142 -26.551 38.464 -18.497 1.00 78.47 N ANISOU 1083 N ALA A 142 10201 12843 6772 405 744 1980 N ATOM 1084 CA ALA A 142 -26.497 37.316 -17.590 1.00 75.60 C ANISOU 1084 CA ALA A 142 9703 12471 6549 406 629 1745 C ATOM 1085 C ALA A 142 -25.541 37.501 -16.404 1.00 78.36 C ANISOU 1085 C ALA A 142 9932 12738 7102 256 737 1682 C ATOM 1086 O ALA A 142 -25.902 37.143 -15.285 1.00 77.57 O ANISOU 1086 O ALA A 142 9759 12526 7188 233 644 1563 O ATOM 1087 CB ALA A 142 -26.123 36.065 -18.391 1.00 73.98 C ANISOU 1087 CB ALA A 142 9468 12480 6162 502 579 1580 C ATOM 1088 N LYS A 143 -24.363 38.090 -16.670 1.00 81.32 N ANISOU 1088 N LYS A 143 10278 13184 7434 148 934 1755 N ATOM 1089 CA LYS A 143 -23.338 38.400 -15.673 1.00 82.40 C ANISOU 1089 CA LYS A 143 10278 13271 7757 -11 1036 1695 C ATOM 1090 C LYS A 143 -23.760 39.507 -14.681 1.00 80.46 C ANISOU 1090 C LYS A 143 10079 12771 7723 -112 1015 1770 C ATOM 1091 O LYS A 143 -23.291 39.497 -13.543 1.00 77.41 O ANISOU 1091 O LYS A 143 9584 12308 7520 -184 978 1651 O ATOM 1092 CB LYS A 143 -22.034 38.737 -16.429 1.00 0.00 C ATOM 1093 CG LYS A 143 -20.801 38.954 -15.533 1.00 0.00 C ATOM 1094 CD LYS A 143 -19.501 39.055 -16.344 1.00 0.00 C ATOM 1095 CE LYS A 143 -18.263 39.227 -15.452 1.00 0.00 C ATOM 1096 NZ LYS A 143 -17.030 39.291 -16.254 1.00 0.00 N1+ ATOM 1097 N LYS A 144 -24.647 40.418 -15.117 1.00 83.44 N ANISOU 1097 N LYS A 144 10625 13012 8064 -100 1038 1965 N ATOM 1098 CA LYS A 144 -25.146 41.548 -14.330 1.00 82.39 C ANISOU 1098 CA LYS A 144 10563 12621 8122 -187 1046 2046 C ATOM 1099 C LYS A 144 -26.351 41.211 -13.431 1.00 79.32 C ANISOU 1099 C LYS A 144 10147 12127 7865 -90 845 1934 C ATOM 1100 O LYS A 144 -26.619 41.995 -12.520 1.00 79.47 O ANISOU 1100 O LYS A 144 10092 12027 8074 -181 825 1838 O ATOM 1101 CB LYS A 144 -25.491 42.709 -15.286 1.00 84.69 C ANISOU 1101 CB LYS A 144 11066 12789 8321 -161 1129 2296 C ATOM 1102 CG LYS A 144 -24.254 43.358 -15.926 1.00 89.09 C ANISOU 1102 CG LYS A 144 11685 13390 8773 -301 1367 2437 C ATOM 1103 CD LYS A 144 -24.627 44.424 -16.965 1.00 93.68 C ANISOU 1103 CD LYS A 144 12520 13809 9266 -250 1444 2703 C ATOM 1104 CE LYS A 144 -23.401 44.997 -17.688 1.00 98.52 C ANISOU 1104 CE LYS A 144 13223 14403 9807 -436 1713 2858 C ATOM 1105 NZ LYS A 144 -23.792 46.019 -18.673 1.00101.82 N1+ ANISOU 1105 NZ LYS A 144 13927 14615 10145 -380 1799 3133 N1+ ATOM 1106 N VAL A 145 -27.051 40.089 -13.683 1.00 76.95 N ANISOU 1106 N VAL A 145 9901 11881 7456 85 697 1939 N ATOM 1107 CA VAL A 145 -28.236 39.679 -12.918 1.00 76.31 C ANISOU 1107 CA VAL A 145 9808 11693 7495 165 526 1865 C ATOM 1108 C VAL A 145 -27.980 38.460 -12.008 1.00 76.40 C ANISOU 1108 C VAL A 145 9680 11749 7599 150 433 1639 C ATOM 1109 O VAL A 145 -28.693 38.311 -11.015 1.00 77.33 O ANISOU 1109 O VAL A 145 9775 11748 7858 159 333 1567 O ATOM 1110 CB VAL A 145 -29.446 39.352 -13.842 1.00 77.59 C ANISOU 1110 CB VAL A 145 10046 11931 7505 343 396 1930 C ATOM 1111 CG1 VAL A 145 -29.898 40.590 -14.637 1.00 80.07 C ANISOU 1111 CG1 VAL A 145 10521 12179 7725 392 481 2175 C ATOM 1112 CG2 VAL A 145 -29.251 38.140 -14.773 1.00 78.92 C ANISOU 1112 CG2 VAL A 145 10171 12337 7478 416 338 1823 C ATOM 1113 N ILE A 146 -26.968 37.629 -12.328 1.00 76.19 N ANISOU 1113 N ILE A 146 9569 11889 7491 138 469 1528 N ATOM 1114 CA ILE A 146 -26.620 36.426 -11.560 1.00 72.51 C ANISOU 1114 CA ILE A 146 8999 11451 7102 151 385 1326 C ATOM 1115 C ILE A 146 -25.892 36.723 -10.228 1.00 68.06 C ANISOU 1115 C ILE A 146 8348 10789 6721 27 439 1272 C ATOM 1116 O ILE A 146 -25.810 35.836 -9.378 1.00 64.75 O ANISOU 1116 O ILE A 146 7860 10361 6380 46 361 1124 O ATOM 1117 CB ILE A 146 -25.786 35.436 -12.421 1.00 74.66 C ANISOU 1117 CB ILE A 146 9223 11931 7215 218 403 1219 C ATOM 1118 CG1 ILE A 146 -25.813 33.994 -11.866 1.00 72.94 C ANISOU 1118 CG1 ILE A 146 8975 11712 7025 298 270 1029 C ATOM 1119 CG2 ILE A 146 -24.335 35.887 -12.693 1.00 76.44 C ANISOU 1119 CG2 ILE A 146 9345 12255 7446 127 560 1213 C ATOM 1120 CD1 ILE A 146 -25.755 32.922 -12.958 1.00 74.05 C ANISOU 1120 CD1 ILE A 146 9097 12028 7010 389 285 909 C ATOM 1121 N ILE A 147 -25.446 37.977 -10.042 1.00 66.23 N ANISOU 1121 N ILE A 147 8130 10482 6554 -104 569 1386 N ATOM 1122 CA ILE A 147 -24.950 38.524 -8.779 1.00 65.49 C ANISOU 1122 CA ILE A 147 7953 10297 6631 -241 609 1323 C ATOM 1123 C ILE A 147 -26.054 38.750 -7.721 1.00 65.11 C ANISOU 1123 C ILE A 147 7957 10051 6730 -228 503 1300 C ATOM 1124 O ILE A 147 -25.720 38.828 -6.540 1.00 65.31 O ANISOU 1124 O ILE A 147 7912 10023 6881 -292 476 1194 O ATOM 1125 CB ILE A 147 -24.201 39.868 -9.005 1.00 0.00 C ATOM 1126 CG1 ILE A 147 -25.073 40.968 -9.663 1.00 0.00 C ATOM 1127 CG2 ILE A 147 -22.900 39.631 -9.795 1.00 0.00 C ATOM 1128 CD1 ILE A 147 -24.388 42.337 -9.769 1.00 0.00 C ATOM 1129 N GLY A 148 -27.332 38.833 -8.142 1.00 64.16 N ANISOU 1129 N GLY A 148 7951 9839 6586 -137 440 1394 N ATOM 1130 CA GLY A 148 -28.497 39.035 -7.276 1.00 56.98 C ANISOU 1130 CA GLY A 148 7083 8764 5804 -106 349 1377 C ATOM 1131 C GLY A 148 -28.684 37.878 -6.273 1.00 52.41 C ANISOU 1131 C GLY A 148 6426 8197 5291 -78 238 1202 C ATOM 1132 O GLY A 148 -28.714 38.158 -5.076 1.00 51.86 O ANISOU 1132 O GLY A 148 6337 8010 5356 -142 228 1144 O ATOM 1133 N PRO A 149 -28.729 36.601 -6.723 1.00 50.81 N ANISOU 1133 N PRO A 149 6195 8124 4985 18 155 1116 N ATOM 1134 CA PRO A 149 -28.608 35.398 -5.872 1.00 48.53 C ANISOU 1134 CA PRO A 149 5863 7828 4749 46 65 959 C ATOM 1135 C PRO A 149 -27.472 35.382 -4.832 1.00 49.34 C ANISOU 1135 C PRO A 149 5885 7931 4930 -29 105 876 C ATOM 1136 O PRO A 149 -27.732 35.000 -3.692 1.00 49.80 O ANISOU 1136 O PRO A 149 5938 7905 5080 -35 48 793 O ATOM 1137 CB PRO A 149 -28.461 34.266 -6.901 1.00 47.09 C ANISOU 1137 CB PRO A 149 5684 7790 4419 142 13 889 C ATOM 1138 CG PRO A 149 -29.335 34.725 -8.054 1.00 47.06 C ANISOU 1138 CG PRO A 149 5737 7841 4303 187 15 1007 C ATOM 1139 CD PRO A 149 -29.072 36.225 -8.098 1.00 49.35 C ANISOU 1139 CD PRO A 149 6044 8077 4627 112 133 1159 C ATOM 1140 N TRP A 150 -26.257 35.812 -5.217 1.00 51.43 N ANISOU 1140 N TRP A 150 6081 8306 5153 -86 203 894 N ATOM 1141 CA TRP A 150 -25.094 35.873 -4.324 1.00 53.44 C ANISOU 1141 CA TRP A 150 6227 8606 5472 -154 231 804 C ATOM 1142 C TRP A 150 -25.184 36.974 -3.250 1.00 57.71 C ANISOU 1142 C TRP A 150 6777 8995 6154 -286 259 827 C ATOM 1143 O TRP A 150 -24.818 36.718 -2.103 1.00 57.71 O ANISOU 1143 O TRP A 150 6726 8973 6227 -311 215 729 O ATOM 1144 CB TRP A 150 -23.797 36.018 -5.141 1.00 52.56 C ANISOU 1144 CB TRP A 150 6009 8684 5277 -191 337 807 C ATOM 1145 CG TRP A 150 -23.434 34.857 -6.020 1.00 50.47 C ANISOU 1145 CG TRP A 150 5723 8579 4875 -46 312 743 C ATOM 1146 CD1 TRP A 150 -23.391 34.863 -7.372 1.00 49.39 C ANISOU 1146 CD1 TRP A 150 5634 8533 4600 11 352 803 C ATOM 1147 CD2 TRP A 150 -23.047 33.509 -5.616 1.00 54.57 C ANISOU 1147 CD2 TRP A 150 6187 9179 5369 73 243 603 C ATOM 1148 CE2 TRP A 150 -22.742 32.756 -6.791 1.00 53.42 C ANISOU 1148 CE2 TRP A 150 6064 9156 5078 194 253 575 C ATOM 1149 CE3 TRP A 150 -22.907 32.846 -4.372 1.00 53.55 C ANISOU 1149 CE3 TRP A 150 6006 9025 5314 100 177 501 C ATOM 1150 NE1 TRP A 150 -22.978 33.630 -7.831 1.00 52.66 N ANISOU 1150 NE1 TRP A 150 6024 9073 4909 148 317 694 N ATOM 1151 CZ2 TRP A 150 -22.291 31.426 -6.735 1.00 46.28 C ANISOU 1151 CZ2 TRP A 150 5143 8328 4113 345 206 448 C ATOM 1152 CZ3 TRP A 150 -22.464 31.511 -4.303 1.00 44.94 C ANISOU 1152 CZ3 TRP A 150 4899 8018 4158 260 125 390 C ATOM 1153 CH2 TRP A 150 -22.143 30.809 -5.480 1.00 45.65 C ANISOU 1153 CH2 TRP A 150 5023 8209 4115 382 144 363 C ATOM 1154 N VAL A 151 -25.677 38.165 -3.632 1.00 57.55 N ANISOU 1154 N VAL A 151 6836 8863 6166 -363 336 956 N ATOM 1155 CA VAL A 151 -25.871 39.311 -2.739 1.00 57.91 C ANISOU 1155 CA VAL A 151 6921 8736 6344 -488 375 972 C ATOM 1156 C VAL A 151 -27.012 39.079 -1.728 1.00 58.49 C ANISOU 1156 C VAL A 151 7049 8675 6496 -421 270 919 C ATOM 1157 O VAL A 151 -26.839 39.402 -0.553 1.00 59.99 O ANISOU 1157 O VAL A 151 7221 8794 6778 -493 259 840 O ATOM 1158 CB VAL A 151 -26.121 40.619 -3.552 1.00 0.00 C ATOM 1159 CG1 VAL A 151 -26.715 41.805 -2.759 1.00 0.00 C ATOM 1160 CG2 VAL A 151 -24.825 41.077 -4.244 1.00 0.00 C ATOM 1161 N MET A 152 -28.127 38.489 -2.194 1.00 59.25 N ANISOU 1161 N MET A 152 7209 8753 6552 -291 196 952 N ATOM 1162 CA MET A 152 -29.280 38.108 -1.376 1.00 59.50 C ANISOU 1162 CA MET A 152 7275 8683 6651 -236 109 896 C ATOM 1163 C MET A 152 -28.946 36.999 -0.363 1.00 61.40 C ANISOU 1163 C MET A 152 7455 8981 6893 -221 43 753 C ATOM 1164 O MET A 152 -29.442 37.049 0.761 1.00 61.59 O ANISOU 1164 O MET A 152 7496 8911 6996 -246 14 693 O ATOM 1165 CB MET A 152 -30.450 37.719 -2.304 1.00 0.00 C ATOM 1166 CG MET A 152 -31.776 37.427 -1.579 1.00 0.00 C ATOM 1167 SD MET A 152 -33.164 37.001 -2.667 1.00 0.00 S ATOM 1168 CE MET A 152 -33.489 38.606 -3.445 1.00 0.00 C ATOM 1169 N ALA A 153 -28.088 36.049 -0.761 1.00 61.79 N ANISOU 1169 N ALA A 153 7449 9182 6847 -167 23 702 N ATOM 1170 CA ALA A 153 -27.571 34.993 0.103 1.00 59.12 C ANISOU 1170 CA ALA A 153 7070 8896 6498 -124 -35 581 C ATOM 1171 C ALA A 153 -26.737 35.541 1.274 1.00 59.69 C ANISOU 1171 C ALA A 153 7065 8988 6628 -219 -5 530 C ATOM 1172 O ALA A 153 -26.987 35.206 2.433 1.00 62.11 O ANISOU 1172 O ALA A 153 7367 9278 6955 -196 -62 446 O ATOM 1173 CB ALA A 153 -26.733 34.035 -0.756 1.00 58.56 C ANISOU 1173 CB ALA A 153 6963 8979 6307 -25 -48 538 C ATOM 1174 N LEU A 154 -25.776 36.412 0.950 1.00 57.00 N ANISOU 1174 N LEU A 154 6667 8685 6305 -334 85 579 N ATOM 1175 CA LEU A 154 -24.871 37.049 1.911 1.00 59.75 C ANISOU 1175 CA LEU A 154 6925 9072 6706 -457 115 514 C ATOM 1176 C LEU A 154 -25.592 37.990 2.895 1.00 57.60 C ANISOU 1176 C LEU A 154 6730 8616 6538 -537 106 499 C ATOM 1177 O LEU A 154 -25.194 38.046 4.059 1.00 58.31 O ANISOU 1177 O LEU A 154 6776 8725 6651 -569 61 400 O ATOM 1178 CB LEU A 154 -23.722 37.719 1.121 1.00 66.65 C ANISOU 1178 CB LEU A 154 7724 10028 7572 -591 235 568 C ATOM 1179 CG LEU A 154 -22.559 38.305 1.965 1.00 71.50 C ANISOU 1179 CG LEU A 154 8173 10794 8200 -722 271 475 C ATOM 1180 CD1 LEU A 154 -21.225 38.275 1.183 1.00 74.85 C ANISOU 1180 CD1 LEU A 154 8512 11351 8577 -817 397 533 C ATOM 1181 CD2 LEU A 154 -22.869 39.715 2.522 1.00 72.37 C ANISOU 1181 CD2 LEU A 154 8310 10769 8418 -889 289 433 C ATOM 1182 N LEU A 155 -26.652 38.672 2.427 1.00 53.27 N ANISOU 1182 N LEU A 155 6298 7899 6043 -554 147 596 N ATOM 1183 CA LEU A 155 -27.518 39.543 3.227 1.00 51.71 C ANISOU 1183 CA LEU A 155 6184 7519 5944 -614 155 580 C ATOM 1184 C LEU A 155 -28.261 38.789 4.348 1.00 52.95 C ANISOU 1184 C LEU A 155 6369 7647 6103 -518 59 503 C ATOM 1185 O LEU A 155 -28.386 39.318 5.451 1.00 52.93 O ANISOU 1185 O LEU A 155 6376 7592 6140 -570 43 422 O ATOM 1186 CB LEU A 155 -28.483 40.278 2.265 1.00 0.00 C ATOM 1187 CG LEU A 155 -29.506 41.246 2.907 1.00 0.00 C ATOM 1188 CD1 LEU A 155 -28.825 42.374 3.710 1.00 0.00 C ATOM 1189 CD2 LEU A 155 -30.480 41.793 1.841 1.00 0.00 C ATOM 1190 N LEU A 156 -28.712 37.570 4.040 1.00 53.19 N ANISOU 1190 N LEU A 156 6422 7711 6078 -388 1 522 N ATOM 1191 CA LEU A 156 -29.455 36.714 4.957 1.00 49.43 C ANISOU 1191 CA LEU A 156 5990 7191 5598 -314 -70 459 C ATOM 1192 C LEU A 156 -28.528 35.896 5.885 1.00 50.72 C ANISOU 1192 C LEU A 156 6110 7447 5714 -296 -124 356 C ATOM 1193 O LEU A 156 -29.014 35.276 6.830 1.00 56.61 O ANISOU 1193 O LEU A 156 6912 8139 6457 -256 -166 306 O ATOM 1194 CB LEU A 156 -30.374 35.804 4.117 1.00 49.87 C ANISOU 1194 CB LEU A 156 6079 7266 5603 -209 -112 490 C ATOM 1195 CG LEU A 156 -31.458 36.539 3.290 1.00 50.86 C ANISOU 1195 CG LEU A 156 6241 7324 5759 -191 -89 585 C ATOM 1196 CD1 LEU A 156 -32.089 35.598 2.249 1.00 49.38 C ANISOU 1196 CD1 LEU A 156 6060 7199 5503 -107 -144 586 C ATOM 1197 CD2 LEU A 156 -32.522 37.241 4.154 1.00 50.84 C ANISOU 1197 CD2 LEU A 156 6288 7178 5851 -212 -68 586 C ATOM 1198 N THR A 157 -27.213 35.923 5.623 1.00 51.92 N ANISOU 1198 N THR A 157 6158 7748 5820 -314 -119 328 N ATOM 1199 CA THR A 157 -26.190 35.240 6.420 1.00 53.27 C ANISOU 1199 CA THR A 157 6265 8041 5934 -270 -179 233 C ATOM 1200 C THR A 157 -25.614 36.129 7.553 1.00 57.17 C ANISOU 1200 C THR A 157 6713 8541 6470 -390 -176 163 C ATOM 1201 O THR A 157 -24.962 35.622 8.469 1.00 60.49 O ANISOU 1201 O THR A 157 7099 9048 6836 -342 -245 81 O ATOM 1202 CB THR A 157 -25.035 34.760 5.503 1.00 54.52 C ANISOU 1202 CB THR A 157 6307 8394 6014 -210 -179 221 C ATOM 1203 CG2 THR A 157 -23.951 33.935 6.217 1.00 53.63 C ANISOU 1203 CG2 THR A 157 6133 8420 5825 -100 -256 130 C ATOM 1204 OG1 THR A 157 -25.572 33.954 4.467 1.00 59.48 O ANISOU 1204 OG1 THR A 157 6995 9008 6597 -112 -175 275 O ATOM 1205 N LEU A 158 -25.928 37.435 7.542 1.00 59.20 N ANISOU 1205 N LEU A 158 6984 8698 6812 -538 -100 192 N ATOM 1206 CA LEU A 158 -25.469 38.419 8.529 1.00 60.36 C ANISOU 1206 CA LEU A 158 7100 8836 7000 -681 -89 109 C ATOM 1207 C LEU A 158 -25.686 38.113 10.036 1.00 58.11 C ANISOU 1207 C LEU A 158 6873 8520 6687 -633 -164 25 C ATOM 1208 O LEU A 158 -24.838 38.563 10.810 1.00 58.95 O ANISOU 1208 O LEU A 158 6899 8737 6762 -697 -205 -79 O ATOM 1209 CB LEU A 158 -25.973 39.836 8.172 1.00 62.83 C ANISOU 1209 CB LEU A 158 7492 8965 7415 -823 16 164 C ATOM 1210 CG LEU A 158 -25.441 40.406 6.835 1.00 66.56 C ANISOU 1210 CG LEU A 158 7907 9473 7909 -937 113 229 C ATOM 1211 CD1 LEU A 158 -26.124 41.748 6.503 1.00 66.57 C ANISOU 1211 CD1 LEU A 158 8043 9244 8006 -1039 220 305 C ATOM 1212 CD2 LEU A 158 -23.902 40.519 6.788 1.00 66.39 C ANISOU 1212 CD2 LEU A 158 7719 9644 7863 -1072 115 125 C ATOM 1213 N PRO A 159 -26.699 37.312 10.461 1.00 56.45 N ANISOU 1213 N PRO A 159 6788 8181 6478 -534 -181 57 N ATOM 1214 CA PRO A 159 -26.746 36.811 11.849 1.00 57.20 C ANISOU 1214 CA PRO A 159 6943 8269 6520 -484 -244 -17 C ATOM 1215 C PRO A 159 -25.540 35.949 12.260 1.00 59.92 C ANISOU 1215 C PRO A 159 7215 8804 6749 -380 -338 -75 C ATOM 1216 O PRO A 159 -25.011 36.155 13.352 1.00 64.15 O ANISOU 1216 O PRO A 159 7744 9404 7227 -384 -394 -160 O ATOM 1217 CB PRO A 159 -28.074 36.033 11.930 1.00 55.68 C ANISOU 1217 CB PRO A 159 6881 7933 6344 -396 -228 46 C ATOM 1218 CG PRO A 159 -28.945 36.672 10.860 1.00 55.82 C ANISOU 1218 CG PRO A 159 6911 7845 6456 -446 -152 129 C ATOM 1219 CD PRO A 159 -27.943 36.987 9.756 1.00 56.04 C ANISOU 1219 CD PRO A 159 6830 7985 6477 -488 -136 156 C ATOM 1220 N VAL A 160 -25.106 35.026 11.389 1.00 57.42 N ANISOU 1220 N VAL A 160 6847 8585 6385 -271 -359 -35 N ATOM 1221 CA VAL A 160 -23.972 34.139 11.657 1.00 57.84 C ANISOU 1221 CA VAL A 160 6827 8824 6326 -137 -444 -86 C ATOM 1222 C VAL A 160 -22.653 34.927 11.735 1.00 62.78 C ANISOU 1222 C VAL A 160 7263 9651 6938 -232 -467 -172 C ATOM 1223 O VAL A 160 -21.835 34.663 12.616 1.00 66.82 O ANISOU 1223 O VAL A 160 7713 10314 7360 -165 -555 -250 O ATOM 1224 CB VAL A 160 -23.831 33.017 10.585 1.00 56.02 C ANISOU 1224 CB VAL A 160 6598 8634 6051 6 -445 -32 C ATOM 1225 CG1 VAL A 160 -22.603 32.099 10.766 1.00 55.98 C ANISOU 1225 CG1 VAL A 160 6513 8827 5931 173 -526 -84 C ATOM 1226 CG2 VAL A 160 -25.097 32.148 10.524 1.00 54.69 C ANISOU 1226 CG2 VAL A 160 6613 8278 5888 76 -431 27 C ATOM 1227 N ILE A 161 -22.510 35.929 10.856 1.00 65.37 N ANISOU 1227 N ILE A 161 7497 9994 7346 -392 -387 -158 N ATOM 1228 CA ILE A 161 -21.302 36.746 10.745 1.00 67.52 C ANISOU 1228 CA ILE A 161 7575 10465 7616 -525 -388 -247 C ATOM 1229 C ILE A 161 -20.980 37.573 12.012 1.00 68.97 C ANISOU 1229 C ILE A 161 7761 10639 7805 -654 -424 -354 C ATOM 1230 O ILE A 161 -19.799 37.830 12.249 1.00 68.19 O ANISOU 1230 O ILE A 161 7492 10760 7656 -712 -481 -465 O ATOM 1231 CB ILE A 161 -21.365 37.641 9.463 1.00 0.00 C ATOM 1232 CG1 ILE A 161 -21.221 36.755 8.199 1.00 0.00 C ATOM 1233 CG2 ILE A 161 -20.361 38.816 9.402 1.00 0.00 C ATOM 1234 CD1 ILE A 161 -21.765 37.376 6.903 1.00 0.00 C ATOM 1235 N ILE A 162 -21.997 37.923 12.825 1.00 69.84 N ANISOU 1235 N ILE A 162 8051 10517 7967 -697 -394 -334 N ATOM 1236 CA ILE A 162 -21.834 38.810 13.984 1.00 71.65 C ANISOU 1236 CA ILE A 162 8311 10707 8206 -834 -408 -442 C ATOM 1237 C ILE A 162 -22.231 38.179 15.341 1.00 77.82 C ANISOU 1237 C ILE A 162 9167 11529 8872 -694 -514 -494 C ATOM 1238 O ILE A 162 -21.722 38.657 16.354 1.00 81.01 O ANISOU 1238 O ILE A 162 9503 12067 9209 -755 -584 -618 O ATOM 1239 CB ILE A 162 -22.615 40.149 13.790 1.00 0.00 C ATOM 1240 CG1 ILE A 162 -24.155 40.024 13.921 1.00 0.00 C ATOM 1241 CG2 ILE A 162 -22.189 40.838 12.475 1.00 0.00 C ATOM 1242 CD1 ILE A 162 -24.948 41.284 13.547 1.00 0.00 C ATOM 1243 N ARG A 163 -23.090 37.139 15.363 1.00 78.77 N ANISOU 1243 N ARG A 163 9432 11539 8958 -518 -524 -405 N ATOM 1244 CA ARG A 163 -23.631 36.573 16.613 1.00 79.01 C ANISOU 1244 CA ARG A 163 9591 11541 8889 -410 -587 -432 C ATOM 1245 C ARG A 163 -23.077 35.189 16.997 1.00 77.82 C ANISOU 1245 C ARG A 163 9454 11512 8602 -178 -680 -399 C ATOM 1246 O ARG A 163 -23.151 34.844 18.178 1.00 78.90 O ANISOU 1246 O ARG A 163 9714 11631 8634 -76 -729 -409 O ATOM 1247 CB ARG A 163 -25.168 36.441 16.539 1.00 0.00 C ATOM 1248 CG ARG A 163 -25.931 37.714 16.151 1.00 0.00 C ATOM 1249 CD ARG A 163 -27.450 37.503 16.113 1.00 0.00 C ATOM 1250 NE ARG A 163 -28.173 38.775 15.985 1.00 0.00 N ATOM 1251 CZ ARG A 163 -28.399 39.661 16.969 1.00 0.00 C ATOM 1252 NH1 ARG A 163 -27.971 39.447 18.218 1.00 0.00 N1+ ATOM 1253 NH2 ARG A 163 -29.066 40.784 16.692 1.00 0.00 N1+ ATOM 1254 N VAL A 164 -22.630 34.386 16.023 1.00 72.81 N ANISOU 1254 N VAL A 164 8716 10992 7957 -80 -696 -359 N ATOM 1255 CA VAL A 164 -22.236 32.995 16.273 1.00 68.67 C ANISOU 1255 CA VAL A 164 8223 10566 7302 163 -778 -330 C ATOM 1256 C VAL A 164 -20.790 32.918 16.802 1.00 67.32 C ANISOU 1256 C VAL A 164 7863 10694 7022 228 -892 -427 C ATOM 1257 O VAL A 164 -19.951 33.732 16.415 1.00 66.77 O ANISOU 1257 O VAL A 164 7577 10803 6992 145 -889 -477 O ATOM 1258 CB VAL A 164 -22.422 32.130 14.993 1.00 0.00 C ATOM 1259 CG1 VAL A 164 -21.743 30.747 14.987 1.00 0.00 C ATOM 1260 CG2 VAL A 164 -23.922 31.952 14.715 1.00 0.00 C ATOM 1261 N THR A 165 -20.529 31.956 17.690 1.00 68.03 N ANISOU 1261 N THR A 165 8030 10852 6965 378 -990 -452 N ATOM 1262 CA THR A 165 -19.249 31.776 18.356 1.00 70.42 C ANISOU 1262 CA THR A 165 8153 11466 7137 470 -1123 -548 C ATOM 1263 C THR A 165 -19.199 30.362 18.972 1.00 71.00 C ANISOU 1263 C THR A 165 8372 11570 7034 776 -1215 -493 C ATOM 1264 O THR A 165 -20.243 29.741 19.175 1.00 69.01 O ANISOU 1264 O THR A 165 8370 11079 6772 874 -1161 -389 O ATOM 1265 CB THR A 165 -19.052 32.881 19.447 1.00 70.93 C ANISOU 1265 CB THR A 165 8138 11619 7192 266 -1162 -677 C ATOM 1266 CG2 THR A 165 -20.128 32.889 20.549 1.00 65.67 C ANISOU 1266 CG2 THR A 165 7722 10756 6471 268 -1151 -657 C ATOM 1267 OG1 THR A 165 -17.803 32.797 20.113 1.00 76.24 O ANISOU 1267 OG1 THR A 165 8600 12638 7730 352 -1305 -785 O ATOM 1268 N THR A 166 -17.998 29.859 19.269 1.00 70.58 N ANISOU 1268 N THR A 166 8163 11817 6836 925 -1353 -565 N ATOM 1269 CA THR A 166 -17.800 28.633 20.045 1.00 71.62 C ANISOU 1269 CA THR A 166 8432 12005 6775 1247 -1455 -512 C ATOM 1270 C THR A 166 -18.149 28.901 21.524 1.00 75.34 C ANISOU 1270 C THR A 166 9013 12499 7114 1230 -1531 -555 C ATOM 1271 O THR A 166 -17.492 29.720 22.169 1.00 78.04 O ANISOU 1271 O THR A 166 9164 13063 7425 1091 -1608 -690 O ATOM 1272 CB THR A 166 -16.341 28.122 19.915 1.00 72.00 C ANISOU 1272 CB THR A 166 8241 12394 6720 1474 -1572 -557 C ATOM 1273 CG2 THR A 166 -15.996 27.735 18.472 1.00 70.56 C ANISOU 1273 CG2 THR A 166 8047 12148 6617 1590 -1492 -485 C ATOM 1274 OG1 THR A 166 -15.382 29.058 20.370 1.00 73.54 O ANISOU 1274 OG1 THR A 166 8105 12888 6945 1280 -1627 -707 O ATOM 1275 N VAL A 167 -19.225 28.271 21.998 1.00 74.83 N ANISOU 1275 N VAL A 167 9258 12208 6965 1356 -1499 -449 N ATOM 1276 CA VAL A 167 -19.834 28.511 23.298 1.00 73.00 C ANISOU 1276 CA VAL A 167 9174 11985 6579 1370 -1558 -471 C ATOM 1277 C VAL A 167 -19.259 27.476 24.295 1.00 73.23 C ANISOU 1277 C VAL A 167 9321 12132 6371 1731 -1678 -401 C ATOM 1278 O VAL A 167 -19.419 26.273 24.064 1.00 72.65 O ANISOU 1278 O VAL A 167 9353 11974 6278 1956 -1659 -294 O ATOM 1279 CB VAL A 167 -21.394 28.406 23.195 1.00 70.90 C ANISOU 1279 CB VAL A 167 9180 11373 6386 1219 -1410 -402 C ATOM 1280 CG1 VAL A 167 -21.914 29.162 21.962 1.00 68.53 C ANISOU 1280 CG1 VAL A 167 8772 10948 6320 911 -1291 -453 C ATOM 1281 CG2 VAL A 167 -22.054 27.012 23.247 1.00 70.61 C ANISOU 1281 CG2 VAL A 167 9414 11082 6334 1390 -1327 -242 C ATOM 1282 N PRO A 168 -18.513 27.927 25.326 1.00 74.20 N ANISOU 1282 N PRO A 168 9438 12454 6302 1794 -1806 -466 N ATOM 1283 CA PRO A 168 -17.982 27.008 26.346 1.00 76.96 C ANISOU 1283 CA PRO A 168 9921 12930 6392 2153 -1933 -392 C ATOM 1284 C PRO A 168 -19.060 26.619 27.373 1.00 78.49 C ANISOU 1284 C PRO A 168 10443 12933 6447 2154 -1891 -324 C ATOM 1285 O PRO A 168 -19.752 27.495 27.895 1.00 81.80 O ANISOU 1285 O PRO A 168 10822 13456 6802 1996 -1932 -431 O ATOM 1286 CB PRO A 168 -16.837 27.813 26.977 1.00 0.00 C ATOM 1287 CG PRO A 168 -17.280 29.264 26.874 1.00 0.00 C ATOM 1288 CD PRO A 168 -18.060 29.303 25.564 1.00 0.00 C ATOM 1289 N GLY A 169 -19.170 25.311 27.653 1.00 79.29 N ANISOU 1289 N GLY A 169 10873 12752 6501 2322 -1797 -153 N ATOM 1290 CA GLY A 169 -20.018 24.786 28.723 1.00 81.67 C ANISOU 1290 CA GLY A 169 11523 12850 6661 2343 -1727 -58 C ATOM 1291 C GLY A 169 -19.312 24.926 30.083 1.00 81.99 C ANISOU 1291 C GLY A 169 11576 13178 6398 2561 -1910 -86 C ATOM 1292 O GLY A 169 -18.138 25.292 30.160 1.00 79.84 O ANISOU 1292 O GLY A 169 11069 13235 6032 2750 -2087 -150 O ATOM 1293 N LYS A 170 -20.034 24.581 31.162 1.00 84.67 N ANISOU 1293 N LYS A 170 12158 13440 6572 2539 -1880 -53 N ATOM 1294 CA LYS A 170 -19.463 24.409 32.507 1.00 90.04 C ANISOU 1294 CA LYS A 170 12871 14409 6930 2775 -2065 -70 C ATOM 1295 C LYS A 170 -18.632 23.113 32.614 1.00 96.15 C ANISOU 1295 C LYS A 170 13657 15238 7638 3129 -2140 41 C ATOM 1296 O LYS A 170 -17.653 23.081 33.358 1.00 97.50 O ANISOU 1296 O LYS A 170 13599 15712 7733 3243 -2296 -44 O ATOM 1297 CB LYS A 170 -20.586 24.454 33.561 1.00 0.00 C ATOM 1298 CG LYS A 170 -21.266 25.832 33.650 1.00 0.00 C ATOM 1299 CD LYS A 170 -22.328 25.906 34.756 1.00 0.00 C ATOM 1300 CE LYS A 170 -22.994 27.287 34.835 1.00 0.00 C ATOM 1301 NZ LYS A 170 -23.997 27.340 35.912 1.00 0.00 N1+ ATOM 1302 N THR A 171 -19.010 22.101 31.815 1.00103.24 N ANISOU 1302 N THR A 171 14813 15846 8566 3300 -2028 215 N ATOM 1303 CA THR A 171 -18.214 20.924 31.473 1.00112.70 C ANISOU 1303 CA THR A 171 16020 17080 9720 3646 -2084 301 C ATOM 1304 C THR A 171 -17.276 21.245 30.283 1.00120.86 C ANISOU 1304 C THR A 171 16724 18285 10913 3685 -2145 215 C ATOM 1305 O THR A 171 -17.415 22.292 29.650 1.00118.75 O ANISOU 1305 O THR A 171 16237 18094 10789 3437 -2140 104 O ATOM 1306 CB THR A 171 -19.162 19.764 31.056 1.00 0.00 C ATOM 1307 CG2 THR A 171 -20.057 19.288 32.210 1.00 0.00 C ATOM 1308 OG1 THR A 171 -20.007 20.127 29.976 1.00 0.00 O ATOM 1309 N GLY A 172 -16.338 20.325 29.990 1.00133.07 N ANISOU 1309 N GLY A 172 18235 19900 12427 4005 -2195 265 N ATOM 1310 CA GLY A 172 -15.310 20.459 28.947 1.00134.58 C ANISOU 1310 CA GLY A 172 18092 20296 12746 4068 -2251 175 C ATOM 1311 C GLY A 172 -15.841 20.488 27.497 1.00132.92 C ANISOU 1311 C GLY A 172 17972 19838 12696 4015 -2126 230 C ATOM 1312 O GLY A 172 -15.039 20.601 26.570 1.00135.02 O ANISOU 1312 O GLY A 172 18312 20011 12979 4269 -2091 299 O ATOM 1313 N THR A 173 -17.164 20.388 27.294 1.00118.72 N ANISOU 1313 N THR A 173 16169 17935 11003 3695 -2056 192 N ATOM 1314 CA THR A 173 -17.852 20.512 26.010 1.00108.00 C ANISOU 1314 CA THR A 173 14874 16322 9839 3578 -1914 230 C ATOM 1315 C THR A 173 -17.816 21.953 25.454 1.00 98.22 C ANISOU 1315 C THR A 173 13317 15159 8842 3173 -1865 82 C ATOM 1316 O THR A 173 -17.787 22.919 26.221 1.00 99.29 O ANISOU 1316 O THR A 173 13417 15305 9003 2909 -1851 15 O ATOM 1317 CB THR A 173 -19.342 20.097 26.152 1.00 0.00 C ATOM 1318 CG2 THR A 173 -19.527 18.660 26.665 1.00 0.00 C ATOM 1319 OG1 THR A 173 -20.069 20.978 26.992 1.00 0.00 O ATOM 1320 N VAL A 174 -17.861 22.051 24.119 1.00 85.57 N ANISOU 1320 N VAL A 174 11507 13596 7410 3136 -1829 37 N ATOM 1321 CA VAL A 174 -17.892 23.303 23.368 1.00 78.55 C ANISOU 1321 CA VAL A 174 10326 12773 6747 2782 -1773 -85 C ATOM 1322 C VAL A 174 -18.602 23.073 22.020 1.00 75.40 C ANISOU 1322 C VAL A 174 10076 12019 6552 2601 -1586 -22 C ATOM 1323 O VAL A 174 -18.398 22.030 21.399 1.00 72.05 O ANISOU 1323 O VAL A 174 9828 11420 6127 2785 -1528 67 O ATOM 1324 CB VAL A 174 -16.462 23.888 23.160 1.00 0.00 C ATOM 1325 CG1 VAL A 174 -15.488 22.940 22.431 1.00 0.00 C ATOM 1326 CG2 VAL A 174 -16.462 25.260 22.464 1.00 0.00 C ATOM 1327 N ALA A 175 -19.435 24.022 21.580 1.00 72.38 N ANISOU 1327 N ALA A 175 9628 11534 6340 2248 -1495 -75 N ATOM 1328 CA ALA A 175 -20.156 23.948 20.309 1.00 70.95 C ANISOU 1328 CA ALA A 175 9555 11054 6349 2058 -1332 -27 C ATOM 1329 C ALA A 175 -20.156 25.324 19.640 1.00 72.75 C ANISOU 1329 C ALA A 175 9501 11370 6770 1768 -1292 -123 C ATOM 1330 O ALA A 175 -20.125 26.321 20.350 1.00 76.40 O ANISOU 1330 O ALA A 175 9809 11969 7249 1588 -1330 -214 O ATOM 1331 CB ALA A 175 -21.588 23.460 20.562 1.00 0.00 C ATOM 1332 N CYS A 176 -20.212 25.366 18.304 1.00 73.85 N ANISOU 1332 N CYS A 176 9594 11423 7045 1723 -1210 -104 N ATOM 1333 CA CYS A 176 -20.364 26.592 17.513 1.00 72.68 C ANISOU 1333 CA CYS A 176 9222 11316 7075 1462 -1149 -166 C ATOM 1334 C CYS A 176 -21.854 26.944 17.480 1.00 67.12 C ANISOU 1334 C CYS A 176 8684 10316 6504 1241 -1019 -118 C ATOM 1335 O CYS A 176 -22.614 26.135 16.950 1.00 66.70 O ANISOU 1335 O CYS A 176 8781 10059 6502 1264 -937 -49 O ATOM 1336 CB CYS A 176 -19.814 26.334 16.096 1.00 75.56 C ANISOU 1336 CB CYS A 176 9438 11786 7487 1556 -1136 -171 C ATOM 1337 SG CYS A 176 -19.853 27.735 14.952 1.00 78.78 S ANISOU 1337 SG CYS A 176 9640 12193 8100 1264 -1030 -205 S ATOM 1338 N THR A 177 -22.269 28.045 18.124 1.00 64.75 N ANISOU 1338 N THR A 177 8351 9997 6256 1031 -1000 -163 N ATOM 1339 CA THR A 177 -23.678 28.385 18.320 1.00 66.82 C ANISOU 1339 CA THR A 177 8760 10002 6626 850 -883 -123 C ATOM 1340 C THR A 177 -23.914 29.904 18.470 1.00 66.85 C ANISOU 1340 C THR A 177 8633 10045 6719 616 -864 -204 C ATOM 1341 O THR A 177 -22.967 30.669 18.671 1.00 67.58 O ANISOU 1341 O THR A 177 8523 10350 6805 563 -931 -291 O ATOM 1342 CB THR A 177 -24.376 27.556 19.466 1.00 71.77 C ANISOU 1342 CB THR A 177 9665 10459 7145 941 -859 -57 C ATOM 1343 CG2 THR A 177 -23.653 26.294 19.962 1.00 73.74 C ANISOU 1343 CG2 THR A 177 9930 10857 7232 1017 -956 -103 C ATOM 1344 OG1 THR A 177 -24.809 28.281 20.601 1.00 72.13 O ANISOU 1344 OG1 THR A 177 9815 10291 7301 756 -739 -31 O ATOM 1345 N PHE A 178 -25.188 30.314 18.373 1.00 67.02 N ANISOU 1345 N PHE A 178 8774 9865 6827 472 -765 -181 N ATOM 1346 CA PHE A 178 -25.688 31.614 18.809 1.00 70.30 C ANISOU 1346 CA PHE A 178 9122 10268 7318 271 -732 -254 C ATOM 1347 C PHE A 178 -25.690 31.661 20.349 1.00 79.82 C ANISOU 1347 C PHE A 178 10409 11539 8381 300 -790 -314 C ATOM 1348 O PHE A 178 -26.646 31.197 20.978 1.00 78.67 O ANISOU 1348 O PHE A 178 10463 11283 8145 383 -763 -260 O ATOM 1349 CB PHE A 178 -27.116 31.841 18.257 1.00 68.08 C ANISOU 1349 CB PHE A 178 8928 9760 7178 142 -603 -205 C ATOM 1350 CG PHE A 178 -27.235 32.062 16.756 1.00 66.26 C ANISOU 1350 CG PHE A 178 8632 9474 7069 119 -553 -144 C ATOM 1351 CD1 PHE A 178 -27.102 33.359 16.219 1.00 66.01 C ANISOU 1351 CD1 PHE A 178 8417 9566 7096 70 -574 -170 C ATOM 1352 CD2 PHE A 178 -27.353 30.968 15.871 1.00 64.11 C ANISOU 1352 CD2 PHE A 178 8479 9038 6843 137 -481 -68 C ATOM 1353 CE1 PHE A 178 -27.169 33.557 14.845 1.00 63.99 C ANISOU 1353 CE1 PHE A 178 8114 9269 6929 56 -526 -111 C ATOM 1354 CE2 PHE A 178 -27.410 31.188 14.500 1.00 62.89 C ANISOU 1354 CE2 PHE A 178 8264 8851 6779 118 -447 -22 C ATOM 1355 CZ PHE A 178 -27.324 32.476 13.989 1.00 62.24 C ANISOU 1355 CZ PHE A 178 8015 8890 6741 87 -469 -39 C ATOM 1356 N ASN A 179 -24.605 32.175 20.938 1.00 89.97 N ANISOU 1356 N ASN A 179 11543 13006 9635 219 -863 -431 N ATOM 1357 CA ASN A 179 -24.470 32.309 22.388 1.00 96.18 C ANISOU 1357 CA ASN A 179 12387 13893 10266 239 -937 -511 C ATOM 1358 C ASN A 179 -25.291 33.509 22.875 1.00 97.45 C ANISOU 1358 C ASN A 179 12661 13875 10491 68 -832 -550 C ATOM 1359 O ASN A 179 -24.831 34.637 22.721 1.00 99.21 O ANISOU 1359 O ASN A 179 12803 14140 10752 -97 -833 -670 O ATOM 1360 CB ASN A 179 -22.987 32.476 22.795 1.00 99.81 C ANISOU 1360 CB ASN A 179 12621 14641 10661 205 -1065 -641 C ATOM 1361 CG ASN A 179 -22.704 32.049 24.241 1.00103.36 C ANISOU 1361 CG ASN A 179 13117 15260 10894 297 -1184 -716 C ATOM 1362 ND2 ASN A 179 -21.433 31.900 24.597 1.00105.59 N ANISOU 1362 ND2 ASN A 179 13202 15847 11068 367 -1331 -802 N ATOM 1363 OD1 ASN A 179 -23.610 31.886 25.055 1.00104.16 O ANISOU 1363 OD1 ASN A 179 13422 15237 10916 309 -1145 -699 O ATOM 1364 N PHE A 180 -26.479 33.266 23.436 1.00 94.20 N ANISOU 1364 N PHE A 180 12443 13259 10090 112 -732 -453 N ATOM 1365 CA PHE A 180 -27.418 34.320 23.834 1.00 92.70 C ANISOU 1365 CA PHE A 180 12351 12895 9976 -26 -613 -479 C ATOM 1366 C PHE A 180 -27.030 35.016 25.155 1.00 97.65 C ANISOU 1366 C PHE A 180 13031 13603 10467 -66 -651 -598 C ATOM 1367 O PHE A 180 -27.424 36.158 25.390 1.00 99.48 O ANISOU 1367 O PHE A 180 13253 13766 10777 -220 -588 -689 O ATOM 1368 CB PHE A 180 -28.833 33.714 23.950 1.00 90.35 C ANISOU 1368 CB PHE A 180 12231 12409 9690 34 -503 -361 C ATOM 1369 CG PHE A 180 -29.375 33.072 22.680 1.00 88.05 C ANISOU 1369 CG PHE A 180 11890 12011 9552 25 -444 -271 C ATOM 1370 CD1 PHE A 180 -29.497 33.831 21.500 1.00 86.03 C ANISOU 1370 CD1 PHE A 180 11536 11672 9478 -107 -372 -283 C ATOM 1371 CD2 PHE A 180 -29.789 31.723 22.669 1.00 86.12 C ANISOU 1371 CD2 PHE A 180 11715 11746 9261 155 -462 -175 C ATOM 1372 CE1 PHE A 180 -30.009 33.253 20.346 1.00 83.28 C ANISOU 1372 CE1 PHE A 180 11143 11251 9249 -107 -330 -202 C ATOM 1373 CE2 PHE A 180 -30.287 31.158 21.502 1.00 83.54 C ANISOU 1373 CE2 PHE A 180 11346 11334 9060 138 -413 -111 C ATOM 1374 CZ PHE A 180 -30.398 31.921 20.345 1.00 82.14 C ANISOU 1374 CZ PHE A 180 11056 11103 9052 7 -353 -124 C ATOM 1375 N SER A 181 -26.282 34.317 26.017 1.00 99.32 N ANISOU 1375 N SER A 181 13313 13961 10464 82 -755 -599 N ATOM 1376 CA SER A 181 -25.878 34.786 27.344 1.00 99.46 C ANISOU 1376 CA SER A 181 13397 14077 10318 59 -803 -711 C ATOM 1377 C SER A 181 -24.947 36.030 27.375 1.00101.13 C ANISOU 1377 C SER A 181 13419 14461 10544 -85 -894 -886 C ATOM 1378 O SER A 181 -25.224 36.913 28.185 1.00104.66 O ANISOU 1378 O SER A 181 13908 14990 10867 -141 -931 -1013 O ATOM 1379 CB SER A 181 -25.323 33.585 28.144 1.00 0.00 C ATOM 1380 OG SER A 181 -25.031 33.918 29.487 1.00 0.00 O ATOM 1381 N PRO A 182 -23.897 36.131 26.519 1.00 99.02 N ANISOU 1381 N PRO A 182 12949 14253 10420 -161 -920 -904 N ATOM 1382 CA PRO A 182 -23.015 37.321 26.495 1.00 99.87 C ANISOU 1382 CA PRO A 182 12863 14532 10553 -327 -995 -1070 C ATOM 1383 C PRO A 182 -23.548 38.554 25.730 1.00101.73 C ANISOU 1383 C PRO A 182 13031 14594 11030 -545 -870 -1095 C ATOM 1384 O PRO A 182 -22.805 39.530 25.625 1.00106.60 O ANISOU 1384 O PRO A 182 13458 15324 11722 -674 -905 -1171 O ATOM 1385 CB PRO A 182 -21.710 36.788 25.877 1.00 0.00 C ATOM 1386 CG PRO A 182 -22.167 35.680 24.950 1.00 0.00 C ATOM 1387 CD PRO A 182 -23.298 35.042 25.743 1.00 0.00 C ATOM 1388 N TRP A 183 -24.793 38.519 25.217 1.00100.41 N ANISOU 1388 N TRP A 183 13013 14156 10979 -582 -720 -1030 N ATOM 1389 CA TRP A 183 -25.436 39.632 24.498 1.00100.82 C ANISOU 1389 CA TRP A 183 13037 14024 11248 -752 -597 -1034 C ATOM 1390 C TRP A 183 -25.738 40.863 25.390 1.00108.76 C ANISOU 1390 C TRP A 183 14119 14938 12266 -920 -540 -1191 C ATOM 1391 O TRP A 183 -25.559 40.817 26.607 1.00112.77 O ANISOU 1391 O TRP A 183 14658 15575 12613 -935 -619 -1322 O ATOM 1392 CB TRP A 183 -26.713 39.134 23.769 1.00 94.70 C ANISOU 1392 CB TRP A 183 12355 13032 10595 -672 -476 -871 C ATOM 1393 CG TRP A 183 -26.561 38.219 22.579 1.00 90.17 C ANISOU 1393 CG TRP A 183 11685 12516 10061 -571 -510 -744 C ATOM 1394 CD1 TRP A 183 -25.422 37.627 22.151 1.00 90.53 C ANISOU 1394 CD1 TRP A 183 11589 12780 10028 -508 -629 -752 C ATOM 1395 CD2 TRP A 183 -27.596 37.780 21.644 1.00 86.60 C ANISOU 1395 CD2 TRP A 183 11263 11914 9727 -517 -425 -602 C ATOM 1396 CE2 TRP A 183 -27.011 36.909 20.676 1.00 85.45 C ANISOU 1396 CE2 TRP A 183 11012 11892 9564 -428 -494 -535 C ATOM 1397 CE3 TRP A 183 -28.981 38.029 21.517 1.00 84.94 C ANISOU 1397 CE3 TRP A 183 11149 11496 9626 -528 -300 -536 C ATOM 1398 NE1 TRP A 183 -25.685 36.859 21.035 1.00 88.45 N ANISOU 1398 NE1 TRP A 183 11286 12494 9827 -415 -614 -625 N ATOM 1399 CZ2 TRP A 183 -27.760 36.305 19.650 1.00 82.51 C ANISOU 1399 CZ2 TRP A 183 10644 11432 9276 -365 -445 -413 C ATOM 1400 CZ3 TRP A 183 -29.739 37.466 20.469 1.00 82.63 C ANISOU 1400 CZ3 TRP A 183 10839 11138 9418 -467 -263 -411 C ATOM 1401 CH2 TRP A 183 -29.130 36.602 19.537 1.00 81.18 C ANISOU 1401 CH2 TRP A 183 10566 11069 9211 -393 -335 -354 C ATOM 1402 N THR A 184 -26.178 41.956 24.753 1.00112.55 N ANISOU 1402 N THR A 184 14643 15190 12931 -1037 -403 -1181 N ATOM 1403 CA THR A 184 -26.513 43.241 25.371 1.00118.72 C ANISOU 1403 CA THR A 184 15506 15854 13751 -1206 -334 -1337 C ATOM 1404 C THR A 184 -27.789 43.183 26.244 1.00122.29 C ANISOU 1404 C THR A 184 16154 16149 14161 -1139 -240 -1353 C ATOM 1405 O THR A 184 -28.597 42.264 26.100 1.00118.46 O ANISOU 1405 O THR A 184 15739 15628 13640 -979 -207 -1230 O ATOM 1406 CB THR A 184 -26.715 44.325 24.271 1.00 0.00 C ATOM 1407 CG2 THR A 184 -25.534 44.439 23.293 1.00 0.00 C ATOM 1408 OG1 THR A 184 -27.911 44.152 23.531 1.00 0.00 O ATOM 1409 N ASN A 185 -27.938 44.204 27.111 1.00131.18 N ANISOU 1409 N ASN A 185 17371 17182 15290 -1277 -186 -1520 N ATOM 1410 CA ASN A 185 -29.074 44.466 28.013 1.00137.59 C ANISOU 1410 CA ASN A 185 18367 17848 16064 -1226 -78 -1564 C ATOM 1411 C ASN A 185 -29.173 43.457 29.179 1.00143.63 C ANISOU 1411 C ASN A 185 19198 18787 16586 -1119 -160 -1604 C ATOM 1412 O ASN A 185 -28.367 42.530 29.277 1.00145.82 O ANISOU 1412 O ASN A 185 19388 19304 16714 -1079 -314 -1613 O ATOM 1413 CB ASN A 185 -30.417 44.579 27.233 1.00 0.00 C ATOM 1414 CG ASN A 185 -30.500 45.756 26.252 1.00 0.00 C ATOM 1415 ND2 ASN A 185 -31.507 46.616 26.424 1.00 0.00 N ATOM 1416 OD1 ASN A 185 -29.691 45.876 25.335 1.00 0.00 O ATOM 1417 N ASP A 186 -30.165 43.681 30.060 1.00147.05 N ANISOU 1417 N ASP A 186 19795 19100 16976 -1058 -45 -1625 N ATOM 1418 CA ASP A 186 -30.526 42.842 31.216 1.00149.46 C ANISOU 1418 CA ASP A 186 20202 19539 17046 -947 -85 -1640 C ATOM 1419 C ASP A 186 -30.863 41.383 30.817 1.00147.28 C ANISOU 1419 C ASP A 186 19898 19340 16722 -780 -122 -1434 C ATOM 1420 O ASP A 186 -31.256 41.172 29.670 1.00146.15 O ANISOU 1420 O ASP A 186 19675 19111 16744 -746 -84 -1292 O ATOM 1421 CB ASP A 186 -31.716 43.442 32.015 1.00 0.00 C ATOM 1422 CG ASP A 186 -31.551 44.881 32.520 1.00 0.00 C ATOM 1423 OD1 ASP A 186 -30.427 45.422 32.439 1.00 0.00 O ATOM 1424 OD2 ASP A 186 -32.566 45.398 33.039 1.00 0.00 O1- ATOM 1425 N PRO A 187 -30.760 40.403 31.752 1.00145.46 N ANISOU 1425 N PRO A 187 19746 19267 16257 -670 -195 -1417 N ATOM 1426 CA PRO A 187 -31.109 38.988 31.480 1.00142.40 C ANISOU 1426 CA PRO A 187 19382 18903 15821 -512 -201 -1221 C ATOM 1427 C PRO A 187 -32.525 38.727 30.924 1.00138.60 C ANISOU 1427 C PRO A 187 18954 18218 15489 -481 -21 -1095 C ATOM 1428 O PRO A 187 -32.680 37.842 30.085 1.00138.75 O ANISOU 1428 O PRO A 187 18923 18204 15590 -417 -17 -942 O ATOM 1429 CB PRO A 187 -30.906 38.282 32.831 1.00145.40 C ANISOU 1429 CB PRO A 187 19904 19436 15906 -410 -265 -1243 C ATOM 1430 CG PRO A 187 -29.895 39.141 33.567 1.00147.67 C ANISOU 1430 CG PRO A 187 20140 19886 16080 -502 -394 -1445 C ATOM 1431 CD PRO A 187 -30.250 40.554 33.119 1.00147.43 C ANISOU 1431 CD PRO A 187 20063 19693 16260 -683 -297 -1575 C ATOM 1432 N LYS A 188 -33.506 39.532 31.368 1.00134.96 N ANISOU 1432 N LYS A 188 18583 17630 15065 -524 127 -1168 N ATOM 1433 CA LYS A 188 -34.892 39.541 30.889 1.00126.81 C ANISOU 1433 CA LYS A 188 17559 16434 14189 -496 295 -1066 C ATOM 1434 C LYS A 188 -35.009 39.946 29.401 1.00123.08 C ANISOU 1434 C LYS A 188 16938 15864 13963 -534 297 -1002 C ATOM 1435 O LYS A 188 -35.891 39.442 28.706 1.00119.69 O ANISOU 1435 O LYS A 188 16461 15375 13640 -486 356 -868 O ATOM 1436 CB LYS A 188 -35.708 40.479 31.817 1.00 0.00 C ATOM 1437 CG LYS A 188 -35.449 41.983 31.589 1.00 0.00 C ATOM 1438 CD LYS A 188 -35.765 42.898 32.776 1.00 0.00 C ATOM 1439 CE LYS A 188 -35.657 44.381 32.376 1.00 0.00 C ATOM 1440 NZ LYS A 188 -35.542 45.263 33.549 1.00 0.00 N1+ ATOM 1441 N GLU A 189 -34.111 40.840 28.951 1.00121.81 N ANISOU 1441 N GLU A 189 16707 15692 13885 -630 236 -1099 N ATOM 1442 CA GLU A 189 -34.059 41.380 27.596 1.00115.28 C ANISOU 1442 CA GLU A 189 15756 14776 13270 -666 241 -1029 C ATOM 1443 C GLU A 189 -33.176 40.548 26.655 1.00109.94 C ANISOU 1443 C GLU A 189 14969 14215 12590 -624 123 -908 C ATOM 1444 O GLU A 189 -33.415 40.591 25.452 1.00109.42 O ANISOU 1444 O GLU A 189 14822 14085 12668 -602 149 -794 O ATOM 1445 CB GLU A 189 -33.593 42.846 27.623 1.00115.08 C ANISOU 1445 CB GLU A 189 15709 14690 13326 -802 229 -1164 C ATOM 1446 CG GLU A 189 -34.510 43.765 28.449 1.00117.34 C ANISOU 1446 CG GLU A 189 16126 14823 13638 -838 360 -1292 C ATOM 1447 CD GLU A 189 -34.232 45.239 28.180 1.00119.66 C ANISOU 1447 CD GLU A 189 16430 15024 14012 -993 359 -1434 C ATOM 1448 OE1 GLU A 189 -34.889 45.778 27.262 1.00119.55 O ANISOU 1448 OE1 GLU A 189 16331 14942 14152 -1048 352 -1369 O ATOM 1449 OE2 GLU A 189 -33.359 45.798 28.879 1.00121.84 O1- ANISOU 1449 OE2 GLU A 189 16809 15292 14192 -1070 369 -1614 O1- ATOM 1450 N ARG A 190 -32.214 39.777 27.193 1.00104.03 N ANISOU 1450 N ARG A 190 14217 13642 11667 -595 -9 -931 N ATOM 1451 CA ARG A 190 -31.454 38.776 26.438 1.00100.14 C ANISOU 1451 CA ARG A 190 13637 13258 11155 -520 -113 -819 C ATOM 1452 C ARG A 190 -32.347 37.619 25.957 1.00 94.49 C ANISOU 1452 C ARG A 190 12977 12471 10453 -417 -44 -668 C ATOM 1453 O ARG A 190 -32.134 37.127 24.852 1.00 91.32 O ANISOU 1453 O ARG A 190 12502 12082 10113 -373 -81 -564 O ATOM 1454 CB ARG A 190 -30.294 38.224 27.288 1.00101.86 C ANISOU 1454 CB ARG A 190 13853 13687 11164 -469 -267 -874 C ATOM 1455 CG ARG A 190 -29.183 39.245 27.568 1.00105.22 C ANISOU 1455 CG ARG A 190 14179 14234 11564 -591 -362 -1039 C ATOM 1456 CD ARG A 190 -27.964 38.588 28.222 1.00107.09 C ANISOU 1456 CD ARG A 190 14356 14730 11602 -505 -541 -1068 C ATOM 1457 NE ARG A 190 -26.959 39.569 28.642 1.00110.48 N ANISOU 1457 NE ARG A 190 14681 15316 11982 -638 -639 -1252 N ATOM 1458 CZ ARG A 190 -26.774 40.070 29.872 1.00113.43 C ANISOU 1458 CZ ARG A 190 15128 15791 12179 -666 -691 -1395 C ATOM 1459 NH1 ARG A 190 -27.529 39.679 30.906 1.00114.32 N1+ ANISOU 1459 NH1 ARG A 190 15431 15862 12144 -558 -645 -1361 N1+ ATOM 1460 NH2 ARG A 190 -25.803 40.972 30.063 1.00115.06 N1+ ANISOU 1460 NH2 ARG A 190 15218 16149 12349 -814 -785 -1580 N1+ ATOM 1461 N ILE A 191 -33.336 37.236 26.783 1.00 92.41 N ANISOU 1461 N ILE A 191 12844 12139 10130 -391 66 -661 N ATOM 1462 CA ILE A 191 -34.319 36.193 26.494 1.00 87.88 C ANISOU 1462 CA ILE A 191 12325 11503 9562 -327 145 -531 C ATOM 1463 C ILE A 191 -35.300 36.596 25.376 1.00 87.77 C ANISOU 1463 C ILE A 191 12212 11375 9762 -361 235 -471 C ATOM 1464 O ILE A 191 -35.535 35.786 24.479 1.00 88.88 O ANISOU 1464 O ILE A 191 12316 11499 9955 -330 234 -366 O ATOM 1465 CB ILE A 191 -35.105 35.794 27.783 1.00 0.00 C ATOM 1466 CG1 ILE A 191 -34.168 35.086 28.791 1.00 0.00 C ATOM 1467 CG2 ILE A 191 -36.369 34.931 27.552 1.00 0.00 C ATOM 1468 CD1 ILE A 191 -34.695 35.079 30.234 1.00 0.00 C ATOM 1469 N LYS A 192 -35.844 37.828 25.436 1.00 85.83 N ANISOU 1469 N LYS A 192 11930 11048 9636 -414 310 -541 N ATOM 1470 CA LYS A 192 -36.856 38.308 24.487 1.00 83.84 C ANISOU 1470 CA LYS A 192 11587 10699 9569 -415 393 -480 C ATOM 1471 C LYS A 192 -36.287 38.543 23.073 1.00 80.62 C ANISOU 1471 C LYS A 192 11058 10296 9278 -432 309 -432 C ATOM 1472 O LYS A 192 -36.993 38.261 22.104 1.00 77.33 O ANISOU 1472 O LYS A 192 10562 9846 8971 -409 335 -344 O ATOM 1473 CB LYS A 192 -37.593 39.546 25.062 1.00 88.31 C ANISOU 1473 CB LYS A 192 12178 11164 10210 -428 514 -561 C ATOM 1474 CG LYS A 192 -36.901 40.905 24.848 1.00 92.97 C ANISOU 1474 CG LYS A 192 12807 11724 10795 -492 482 -689 C ATOM 1475 CD LYS A 192 -37.533 42.063 25.633 1.00 97.19 C ANISOU 1475 CD LYS A 192 13408 12137 11385 -484 620 -776 C ATOM 1476 CE LYS A 192 -36.791 43.385 25.389 1.00 99.58 C ANISOU 1476 CE LYS A 192 13768 12375 11692 -569 601 -918 C ATOM 1477 NZ LYS A 192 -37.344 44.481 26.200 1.00101.24 N1+ ANISOU 1477 NZ LYS A 192 14074 12446 11947 -544 746 -1015 N1+ ATOM 1478 N VAL A 193 -35.035 39.030 22.976 1.00 81.03 N ANISOU 1478 N VAL A 193 11085 10404 9298 -480 212 -493 N ATOM 1479 CA VAL A 193 -34.373 39.301 21.696 1.00 78.24 C ANISOU 1479 CA VAL A 193 10617 10076 9037 -503 144 -442 C ATOM 1480 C VAL A 193 -33.695 38.051 21.096 1.00 76.67 C ANISOU 1480 C VAL A 193 10378 9980 8770 -439 56 -358 C ATOM 1481 O VAL A 193 -33.515 38.019 19.880 1.00 78.03 O ANISOU 1481 O VAL A 193 10457 10173 9017 -436 19 -295 O ATOM 1482 CB VAL A 193 -33.336 40.455 21.782 1.00 78.95 C ANISOU 1482 CB VAL A 193 10672 10201 9125 -601 85 -545 C ATOM 1483 CG1 VAL A 193 -33.972 41.766 22.281 1.00 81.77 C ANISOU 1483 CG1 VAL A 193 11101 10420 9548 -670 183 -641 C ATOM 1484 CG2 VAL A 193 -32.038 40.117 22.534 1.00 79.08 C ANISOU 1484 CG2 VAL A 193 10699 10383 8966 -596 -30 -616 C ATOM 1485 N ALA A 194 -33.373 37.043 21.924 1.00 73.60 N ANISOU 1485 N ALA A 194 10079 9649 8235 -380 29 -352 N ATOM 1486 CA ALA A 194 -32.967 35.713 21.465 1.00 72.43 C ANISOU 1486 CA ALA A 194 9932 9565 8022 -299 -39 -270 C ATOM 1487 C ALA A 194 -34.122 35.023 20.729 1.00 72.66 C ANISOU 1487 C ALA A 194 9957 9510 8140 -285 34 -176 C ATOM 1488 O ALA A 194 -33.950 34.601 19.586 1.00 73.25 O ANISOU 1488 O ALA A 194 9976 9607 8247 -255 -11 -115 O ATOM 1489 CB ALA A 194 -32.496 34.866 22.654 1.00 73.46 C ANISOU 1489 CB ALA A 194 10193 9760 7959 -227 -80 -280 C ATOM 1490 N VAL A 195 -35.300 35.025 21.370 1.00 71.01 N ANISOU 1490 N VAL A 195 9798 9219 7964 -310 149 -175 N ATOM 1491 CA VAL A 195 -36.562 34.553 20.804 1.00 73.66 C ANISOU 1491 CA VAL A 195 10105 9503 8379 -315 217 -105 C ATOM 1492 C VAL A 195 -36.930 35.301 19.505 1.00 77.17 C ANISOU 1492 C VAL A 195 10410 9933 8979 -330 214 -79 C ATOM 1493 O VAL A 195 -37.285 34.644 18.531 1.00 79.14 O ANISOU 1493 O VAL A 195 10602 10196 9271 -320 191 -20 O ATOM 1494 CB VAL A 195 -37.698 34.661 21.869 1.00 0.00 C ATOM 1495 CG1 VAL A 195 -39.149 34.644 21.344 1.00 0.00 C ATOM 1496 CG2 VAL A 195 -37.537 33.561 22.935 1.00 0.00 C ATOM 1497 N ALA A 196 -36.783 36.639 19.485 1.00 78.95 N ANISOU 1497 N ALA A 196 10595 10124 9280 -351 239 -123 N ATOM 1498 CA ALA A 196 -37.051 37.476 18.311 1.00 80.68 C ANISOU 1498 CA ALA A 196 10709 10312 9634 -348 247 -81 C ATOM 1499 C ALA A 196 -36.082 37.244 17.136 1.00 79.41 C ANISOU 1499 C ALA A 196 10486 10210 9476 -350 150 -41 C ATOM 1500 O ALA A 196 -36.510 37.364 15.989 1.00 79.51 O ANISOU 1500 O ALA A 196 10422 10228 9561 -331 142 25 O ATOM 1501 CB ALA A 196 -37.052 38.956 18.716 1.00 0.00 C ATOM 1502 N MET A 197 -34.812 36.921 17.423 1.00 75.92 N ANISOU 1502 N MET A 197 10066 9833 8949 -365 77 -83 N ATOM 1503 CA MET A 197 -33.813 36.579 16.408 1.00 73.07 C ANISOU 1503 CA MET A 197 9629 9554 8581 -360 -5 -53 C ATOM 1504 C MET A 197 -34.173 35.252 15.724 1.00 70.27 C ANISOU 1504 C MET A 197 9271 9238 8189 -298 -39 12 C ATOM 1505 O MET A 197 -34.194 35.182 14.495 1.00 72.85 O ANISOU 1505 O MET A 197 9525 9594 8560 -286 -61 64 O ATOM 1506 CB MET A 197 -32.400 36.570 17.040 1.00 74.32 C ANISOU 1506 CB MET A 197 9786 9806 8647 -380 -80 -126 C ATOM 1507 CG MET A 197 -31.215 36.595 16.051 1.00 79.80 C ANISOU 1507 CG MET A 197 10368 10598 9355 -403 -141 -118 C ATOM 1508 SD MET A 197 -30.806 35.095 15.105 1.00 82.48 S ANISOU 1508 SD MET A 197 10670 11044 9625 -293 -214 -52 S ATOM 1509 CE MET A 197 -30.472 33.912 16.437 1.00 84.79 C ANISOU 1509 CE MET A 197 11059 11405 9753 -204 -282 -98 C ATOM 1510 N LEU A 198 -34.524 34.248 16.541 1.00 66.66 N ANISOU 1510 N LEU A 198 8910 8774 7643 -263 -36 7 N ATOM 1511 CA LEU A 198 -34.952 32.924 16.088 1.00 64.34 C ANISOU 1511 CA LEU A 198 8647 8484 7314 -219 -53 56 C ATOM 1512 C LEU A 198 -36.257 32.968 15.268 1.00 66.91 C ANISOU 1512 C LEU A 198 8930 8760 7731 -254 8 93 C ATOM 1513 O LEU A 198 -36.365 32.232 14.287 1.00 70.20 O ANISOU 1513 O LEU A 198 9324 9195 8152 -241 -16 125 O ATOM 1514 CB LEU A 198 -35.087 31.983 17.304 1.00 61.52 C ANISOU 1514 CB LEU A 198 8437 8107 6830 -178 -50 50 C ATOM 1515 CG LEU A 198 -33.761 31.672 18.041 1.00 57.96 C ANISOU 1515 CG LEU A 198 8023 7741 6258 -104 -139 21 C ATOM 1516 CD1 LEU A 198 -34.029 31.085 19.445 1.00 56.99 C ANISOU 1516 CD1 LEU A 198 8077 7580 5998 -47 -123 33 C ATOM 1517 CD2 LEU A 198 -32.817 30.789 17.194 1.00 51.83 C ANISOU 1517 CD2 LEU A 198 7177 7049 5469 -34 -221 40 C ATOM 1518 N THR A 199 -37.182 33.871 15.623 1.00 65.45 N ANISOU 1518 N THR A 199 8728 8528 7613 -291 88 79 N ATOM 1519 CA THR A 199 -38.401 34.157 14.859 1.00 63.79 C ANISOU 1519 CA THR A 199 8439 8309 7489 -309 135 108 C ATOM 1520 C THR A 199 -38.066 34.694 13.454 1.00 60.30 C ANISOU 1520 C THR A 199 7887 7905 7120 -285 90 151 C ATOM 1521 O THR A 199 -38.550 34.134 12.474 1.00 61.05 O ANISOU 1521 O THR A 199 7922 8040 7232 -282 69 182 O ATOM 1522 CB THR A 199 -39.318 35.201 15.560 1.00 65.19 C ANISOU 1522 CB THR A 199 8608 8445 7717 -326 233 79 C ATOM 1523 CG2 THR A 199 -40.566 35.646 14.773 1.00 67.00 C ANISOU 1523 CG2 THR A 199 8723 8704 8031 -328 273 103 C ATOM 1524 OG1 THR A 199 -39.767 34.687 16.792 1.00 65.81 O ANISOU 1524 OG1 THR A 199 8800 8495 7710 -354 288 46 O ATOM 1525 N VAL A 200 -37.237 35.751 13.393 1.00 55.18 N ANISOU 1525 N VAL A 200 7219 7244 6503 -278 79 152 N ATOM 1526 CA VAL A 200 -36.846 36.441 12.162 1.00 51.36 C ANISOU 1526 CA VAL A 200 6658 6787 6070 -259 49 208 C ATOM 1527 C VAL A 200 -35.984 35.570 11.228 1.00 55.66 C ANISOU 1527 C VAL A 200 7185 7412 6552 -245 -24 229 C ATOM 1528 O VAL A 200 -36.278 35.520 10.036 1.00 59.80 O ANISOU 1528 O VAL A 200 7649 7982 7093 -221 -48 280 O ATOM 1529 CB VAL A 200 -36.123 37.785 12.481 1.00 0.00 C ATOM 1530 CG1 VAL A 200 -35.338 38.426 11.315 1.00 0.00 C ATOM 1531 CG2 VAL A 200 -37.127 38.813 13.035 1.00 0.00 C ATOM 1532 N ARG A 201 -34.998 34.846 11.789 1.00 53.23 N ANISOU 1532 N ARG A 201 6935 7131 6161 -242 -63 190 N ATOM 1533 CA ARG A 201 -34.166 33.886 11.053 1.00 50.12 C ANISOU 1533 CA ARG A 201 6532 6812 5700 -203 -126 201 C ATOM 1534 C ARG A 201 -34.983 32.677 10.557 1.00 50.21 C ANISOU 1534 C ARG A 201 6568 6817 5692 -190 -129 212 C ATOM 1535 O ARG A 201 -34.786 32.248 9.423 1.00 49.75 O ANISOU 1535 O ARG A 201 6469 6814 5620 -166 -163 235 O ATOM 1536 CB ARG A 201 -32.927 33.475 11.892 1.00 50.38 C ANISOU 1536 CB ARG A 201 6621 6880 5641 -170 -168 156 C ATOM 1537 CG ARG A 201 -31.909 32.570 11.150 1.00 49.25 C ANISOU 1537 CG ARG A 201 6470 6819 5422 -97 -228 160 C ATOM 1538 CD ARG A 201 -30.611 32.314 11.946 1.00 50.97 C ANISOU 1538 CD ARG A 201 6713 7104 5548 -38 -279 118 C ATOM 1539 NE ARG A 201 -29.755 31.288 11.317 1.00 55.31 N ANISOU 1539 NE ARG A 201 7266 7731 6019 68 -331 119 N ATOM 1540 CZ ARG A 201 -28.822 31.452 10.360 1.00 54.82 C ANISOU 1540 CZ ARG A 201 7086 7789 5954 92 -359 117 C ATOM 1541 NH1 ARG A 201 -28.535 32.655 9.853 1.00 52.77 N1+ ANISOU 1541 NH1 ARG A 201 6711 7573 5766 -2 -336 123 N1+ ATOM 1542 NH2 ARG A 201 -28.150 30.397 9.887 1.00 55.61 N1+ ANISOU 1542 NH2 ARG A 201 7194 7959 5976 211 -397 111 N1+ ATOM 1543 N GLY A 202 -35.918 32.175 11.374 1.00 52.52 N ANISOU 1543 N GLY A 202 6930 7046 5978 -220 -86 189 N ATOM 1544 CA GLY A 202 -36.791 31.055 11.012 1.00 52.37 C ANISOU 1544 CA GLY A 202 6936 7016 5948 -246 -78 184 C ATOM 1545 C GLY A 202 -37.765 31.440 9.886 1.00 51.15 C ANISOU 1545 C GLY A 202 6660 6913 5863 -269 -77 205 C ATOM 1546 O GLY A 202 -38.019 30.641 8.981 1.00 52.15 O ANISOU 1546 O GLY A 202 6770 7079 5968 -282 -107 197 O ATOM 1547 N ILE A 203 -38.260 32.686 9.897 1.00 48.61 N ANISOU 1547 N ILE A 203 6260 6594 5618 -264 -46 229 N ATOM 1548 CA ILE A 203 -39.103 33.243 8.834 1.00 47.94 C ANISOU 1548 CA ILE A 203 6057 6571 5588 -247 -55 264 C ATOM 1549 C ILE A 203 -38.315 33.448 7.525 1.00 49.16 C ANISOU 1549 C ILE A 203 6175 6790 5714 -200 -118 312 C ATOM 1550 O ILE A 203 -38.828 33.108 6.462 1.00 51.49 O ANISOU 1550 O ILE A 203 6413 7164 5985 -192 -159 320 O ATOM 1551 CB ILE A 203 -39.777 34.573 9.300 1.00 45.59 C ANISOU 1551 CB ILE A 203 5709 6241 5373 -219 1 285 C ATOM 1552 CG1 ILE A 203 -40.937 34.257 10.273 1.00 43.34 C ANISOU 1552 CG1 ILE A 203 5440 5921 5107 -264 75 233 C ATOM 1553 CG2 ILE A 203 -40.273 35.516 8.179 1.00 43.41 C ANISOU 1553 CG2 ILE A 203 5318 6035 5139 -156 -22 342 C ATOM 1554 CD1 ILE A 203 -41.401 35.459 11.107 1.00 44.56 C ANISOU 1554 CD1 ILE A 203 5573 6026 5332 -222 145 236 C ATOM 1555 N ILE A 204 -37.074 33.951 7.626 1.00 47.28 N ANISOU 1555 N ILE A 204 5963 6533 5469 -178 -121 336 N ATOM 1556 CA ILE A 204 -36.126 34.035 6.513 1.00 45.72 C ANISOU 1556 CA ILE A 204 5730 6402 5239 -145 -158 386 C ATOM 1557 C ILE A 204 -35.855 32.650 5.892 1.00 47.79 C ANISOU 1557 C ILE A 204 6014 6728 5414 -135 -208 353 C ATOM 1558 O ILE A 204 -35.971 32.507 4.675 1.00 50.18 O ANISOU 1558 O ILE A 204 6277 7111 5679 -108 -241 381 O ATOM 1559 CB ILE A 204 -34.792 34.726 6.943 1.00 42.69 C ANISOU 1559 CB ILE A 204 5360 5992 4866 -157 -137 400 C ATOM 1560 CG1 ILE A 204 -35.002 36.250 7.092 1.00 44.87 C ANISOU 1560 CG1 ILE A 204 5634 6183 5230 -168 -80 433 C ATOM 1561 CG2 ILE A 204 -33.556 34.438 6.060 1.00 40.71 C ANISOU 1561 CG2 ILE A 204 5074 5827 4567 -140 -160 442 C ATOM 1562 CD1 ILE A 204 -33.951 36.947 7.971 1.00 45.07 C ANISOU 1562 CD1 ILE A 204 5683 6168 5274 -219 -50 423 C ATOM 1563 N ARG A 205 -35.560 31.662 6.746 1.00 45.77 N ANISOU 1563 N ARG A 205 5840 6433 5115 -145 -211 293 N ATOM 1564 CA ARG A 205 -35.299 30.275 6.383 1.00 48.15 C ANISOU 1564 CA ARG A 205 6196 6763 5334 -120 -247 255 C ATOM 1565 C ARG A 205 -36.444 29.642 5.565 1.00 49.07 C ANISOU 1565 C ARG A 205 6297 6903 5446 -159 -262 231 C ATOM 1566 O ARG A 205 -36.172 29.146 4.473 1.00 51.12 O ANISOU 1566 O ARG A 205 6560 7222 5642 -138 -298 212 O ATOM 1567 CB ARG A 205 -34.944 29.482 7.663 1.00 46.10 C ANISOU 1567 CB ARG A 205 6057 6428 5028 -106 -239 208 C ATOM 1568 CG ARG A 205 -34.667 27.980 7.460 1.00 46.22 C ANISOU 1568 CG ARG A 205 6169 6433 4962 -68 -262 165 C ATOM 1569 CD ARG A 205 -34.428 27.207 8.760 1.00 48.31 C ANISOU 1569 CD ARG A 205 6589 6591 5176 -44 -243 135 C ATOM 1570 NE ARG A 205 -33.144 27.500 9.407 1.00 53.48 N ANISOU 1570 NE ARG A 205 7247 7272 5801 34 -261 149 N ATOM 1571 CZ ARG A 205 -32.736 26.992 10.581 1.00 51.44 C ANISOU 1571 CZ ARG A 205 7011 6976 5560 9 -238 156 C ATOM 1572 NH1 ARG A 205 -33.509 26.157 11.285 1.00 50.54 N1+ ANISOU 1572 NH1 ARG A 205 6918 6787 5497 -84 -184 156 N1+ ATOM 1573 NH2 ARG A 205 -31.531 27.322 11.049 1.00 48.79 N1+ ANISOU 1573 NH2 ARG A 205 6665 6693 5182 76 -270 153 N1+ ATOM 1574 N PHE A 206 -37.678 29.675 6.091 1.00 47.00 N ANISOU 1574 N PHE A 206 6003 6610 5242 -220 -232 221 N ATOM 1575 CA PHE A 206 -38.844 29.057 5.465 1.00 53.48 C ANISOU 1575 CA PHE A 206 6783 7478 6058 -281 -248 179 C ATOM 1576 C PHE A 206 -39.375 29.823 4.244 1.00 60.83 C ANISOU 1576 C PHE A 206 7580 8534 6998 -241 -292 226 C ATOM 1577 O PHE A 206 -39.637 29.189 3.224 1.00 63.74 O ANISOU 1577 O PHE A 206 7923 8990 7305 -246 -345 197 O ATOM 1578 CB PHE A 206 -39.940 28.757 6.512 1.00 55.99 C ANISOU 1578 CB PHE A 206 7102 7741 6432 -368 -188 141 C ATOM 1579 CG PHE A 206 -41.210 28.152 5.932 1.00 56.75 C ANISOU 1579 CG PHE A 206 7145 7893 6522 -466 -196 74 C ATOM 1580 CD1 PHE A 206 -41.209 26.808 5.511 1.00 55.89 C ANISOU 1580 CD1 PHE A 206 7148 7739 6350 -534 -203 1 C ATOM 1581 CD2 PHE A 206 -42.324 28.963 5.623 1.00 58.46 C ANISOU 1581 CD2 PHE A 206 7201 8213 6797 -490 -195 73 C ATOM 1582 CE1 PHE A 206 -42.310 26.278 4.853 1.00 56.41 C ANISOU 1582 CE1 PHE A 206 7165 7858 6411 -658 -209 -82 C ATOM 1583 CE2 PHE A 206 -43.414 28.419 4.957 1.00 59.31 C ANISOU 1583 CE2 PHE A 206 7230 8407 6898 -598 -210 -6 C ATOM 1584 CZ PHE A 206 -43.409 27.082 4.578 1.00 59.05 C ANISOU 1584 CZ PHE A 206 7310 8325 6803 -699 -216 -88 C ATOM 1585 N ILE A 207 -39.551 31.150 4.368 1.00 64.35 N ANISOU 1585 N ILE A 207 7955 8984 7510 -194 -272 295 N ATOM 1586 CA ILE A 207 -40.172 31.959 3.319 1.00 64.03 C ANISOU 1586 CA ILE A 207 7805 9052 7472 -131 -310 358 C ATOM 1587 C ILE A 207 -39.161 32.311 2.217 1.00 63.04 C ANISOU 1587 C ILE A 207 7698 8978 7276 -68 -344 420 C ATOM 1588 O ILE A 207 -39.338 31.867 1.086 1.00 66.96 O ANISOU 1588 O ILE A 207 8156 9589 7696 -45 -402 421 O ATOM 1589 CB ILE A 207 -40.881 33.247 3.844 1.00 0.00 C ATOM 1590 CG1 ILE A 207 -41.979 32.870 4.868 1.00 0.00 C ATOM 1591 CG2 ILE A 207 -41.480 34.113 2.707 1.00 0.00 C ATOM 1592 CD1 ILE A 207 -42.712 34.065 5.495 1.00 0.00 C ATOM 1593 N ILE A 208 -38.127 33.095 2.559 1.00 55.72 N ANISOU 1593 N ILE A 208 6826 7980 6365 -49 -304 466 N ATOM 1594 CA ILE A 208 -37.158 33.608 1.588 1.00 53.44 C ANISOU 1594 CA ILE A 208 6545 7746 6015 -5 -311 530 C ATOM 1595 C ILE A 208 -36.192 32.505 1.099 1.00 56.15 C ANISOU 1595 C ILE A 208 6930 8144 6262 -12 -342 465 C ATOM 1596 O ILE A 208 -35.856 32.485 -0.082 1.00 62.90 O ANISOU 1596 O ILE A 208 7772 9096 7030 26 -366 492 O ATOM 1597 CB ILE A 208 -36.329 34.800 2.160 1.00 50.40 C ANISOU 1597 CB ILE A 208 6188 7277 5685 -12 -248 584 C ATOM 1598 CG1 ILE A 208 -37.195 35.863 2.880 1.00 51.98 C ANISOU 1598 CG1 ILE A 208 6375 7391 5982 4 -207 633 C ATOM 1599 CG2 ILE A 208 -35.433 35.477 1.101 1.00 46.82 C ANISOU 1599 CG2 ILE A 208 5732 6884 5172 12 -233 660 C ATOM 1600 CD1 ILE A 208 -38.210 36.593 1.985 1.00 53.07 C ANISOU 1600 CD1 ILE A 208 6468 7588 6109 88 -228 724 C ATOM 1601 N GLY A 209 -35.815 31.589 2.000 1.00 53.65 N ANISOU 1601 N GLY A 209 6677 7761 5947 -47 -336 381 N ATOM 1602 CA GLY A 209 -34.875 30.502 1.737 1.00 52.30 C ANISOU 1602 CA GLY A 209 6568 7614 5688 -25 -354 319 C ATOM 1603 C GLY A 209 -35.556 29.225 1.224 1.00 52.06 C ANISOU 1603 C GLY A 209 6576 7606 5598 -51 -393 238 C ATOM 1604 O GLY A 209 -34.860 28.226 1.049 1.00 55.00 O ANISOU 1604 O GLY A 209 7014 7997 5886 -16 -405 185 O ATOM 1605 N PHE A 210 -36.879 29.213 0.993 1.00 49.32 N ANISOU 1605 N PHE A 210 6187 7264 5289 -114 -409 216 N ATOM 1606 CA PHE A 210 -37.569 28.038 0.457 1.00 49.94 C ANISOU 1606 CA PHE A 210 6294 7368 5313 -177 -445 117 C ATOM 1607 C PHE A 210 -38.847 28.363 -0.311 1.00 49.90 C ANISOU 1607 C PHE A 210 6161 7495 5303 -201 -498 123 C ATOM 1608 O PHE A 210 -38.877 28.137 -1.520 1.00 48.21 O ANISOU 1608 O PHE A 210 5928 7395 4994 -192 -555 88 O ATOM 1609 CB PHE A 210 -37.712 26.903 1.492 1.00 51.62 C ANISOU 1609 CB PHE A 210 6604 7445 5567 -266 -403 40 C ATOM 1610 CG PHE A 210 -38.707 25.797 1.179 1.00 57.41 C ANISOU 1610 CG PHE A 210 7387 8176 6251 -366 -421 -75 C ATOM 1611 CD1 PHE A 210 -38.432 24.859 0.160 1.00 59.13 C ANISOU 1611 CD1 PHE A 210 7736 8353 6377 -344 -431 -146 C ATOM 1612 CD2 PHE A 210 -39.964 25.774 1.819 1.00 60.82 C ANISOU 1612 CD2 PHE A 210 7733 8649 6728 -487 -425 -125 C ATOM 1613 CE1 PHE A 210 -39.376 23.894 -0.164 1.00 61.64 C ANISOU 1613 CE1 PHE A 210 8123 8647 6650 -455 -441 -269 C ATOM 1614 CE2 PHE A 210 -40.891 24.797 1.483 1.00 64.44 C ANISOU 1614 CE2 PHE A 210 8232 9109 7143 -614 -439 -248 C ATOM 1615 CZ PHE A 210 -40.596 23.862 0.498 1.00 64.54 C ANISOU 1615 CZ PHE A 210 8401 9055 7066 -605 -446 -323 C ATOM 1616 N SER A 211 -39.887 28.874 0.360 1.00 48.60 N ANISOU 1616 N SER A 211 5904 7332 5229 -219 -482 163 N ATOM 1617 CA SER A 211 -41.204 29.042 -0.271 1.00 51.11 C ANISOU 1617 CA SER A 211 6077 7800 5541 -215 -539 168 C ATOM 1618 C SER A 211 -41.206 29.990 -1.489 1.00 51.13 C ANISOU 1618 C SER A 211 6036 7926 5466 -97 -591 263 C ATOM 1619 O SER A 211 -41.963 29.738 -2.424 1.00 54.26 O ANISOU 1619 O SER A 211 6351 8483 5782 -82 -670 242 O ATOM 1620 CB SER A 211 -42.286 29.372 0.784 1.00 0.00 C ATOM 1621 OG SER A 211 -42.486 30.756 0.989 1.00 0.00 O ATOM 1622 N ALA A 212 -40.334 31.014 -1.479 1.00 47.05 N ANISOU 1622 N ALA A 212 5572 7344 4961 -19 -546 368 N ATOM 1623 CA ALA A 212 -40.092 31.934 -2.589 1.00 49.81 C ANISOU 1623 CA ALA A 212 5904 7792 5229 81 -571 474 C ATOM 1624 C ALA A 212 -39.437 31.251 -3.812 1.00 56.02 C ANISOU 1624 C ALA A 212 6732 8682 5872 83 -617 419 C ATOM 1625 O ALA A 212 -40.086 31.239 -4.857 1.00 60.69 O ANISOU 1625 O ALA A 212 7267 9429 6361 128 -689 432 O ATOM 1626 CB ALA A 212 -39.324 33.168 -2.080 1.00 0.00 C ATOM 1627 N PRO A 213 -38.224 30.648 -3.690 1.00 55.89 N ANISOU 1627 N PRO A 213 6810 8599 5826 52 -583 351 N ATOM 1628 CA PRO A 213 -37.624 29.886 -4.805 1.00 54.77 C ANISOU 1628 CA PRO A 213 6714 8559 5539 69 -618 288 C ATOM 1629 C PRO A 213 -38.397 28.620 -5.235 1.00 57.88 C ANISOU 1629 C PRO A 213 7097 9019 5877 -5 -692 150 C ATOM 1630 O PRO A 213 -38.327 28.278 -6.412 1.00 60.55 O ANISOU 1630 O PRO A 213 7423 9502 6080 18 -753 118 O ATOM 1631 CB PRO A 213 -36.187 29.587 -4.344 1.00 52.31 C ANISOU 1631 CB PRO A 213 6501 8145 5230 76 -555 246 C ATOM 1632 CG PRO A 213 -36.232 29.670 -2.830 1.00 52.72 C ANISOU 1632 CG PRO A 213 6572 8045 5414 23 -517 231 C ATOM 1633 CD PRO A 213 -37.281 30.746 -2.573 1.00 53.96 C ANISOU 1633 CD PRO A 213 6638 8202 5661 23 -514 331 C ATOM 1634 N MET A 214 -39.149 27.983 -4.319 1.00 58.40 N ANISOU 1634 N MET A 214 7169 8987 6034 -110 -683 62 N ATOM 1635 CA MET A 214 -40.036 26.847 -4.604 1.00 59.51 C ANISOU 1635 CA MET A 214 7301 9182 6128 -222 -739 -85 C ATOM 1636 C MET A 214 -41.271 27.253 -5.424 1.00 58.98 C ANISOU 1636 C MET A 214 7074 9325 6011 -211 -833 -72 C ATOM 1637 O MET A 214 -41.649 26.510 -6.328 1.00 55.87 O ANISOU 1637 O MET A 214 6662 9064 5501 -256 -910 -177 O ATOM 1638 CB MET A 214 -40.422 26.147 -3.282 1.00 61.90 C ANISOU 1638 CB MET A 214 7643 9333 6543 -351 -688 -164 C ATOM 1639 CG MET A 214 -41.272 24.867 -3.387 1.00 66.91 C ANISOU 1639 CG MET A 214 8304 9980 7140 -509 -718 -336 C ATOM 1640 SD MET A 214 -40.385 23.384 -3.944 1.00 71.36 S ANISOU 1640 SD MET A 214 9098 10420 7597 -530 -693 -465 S ATOM 1641 CE MET A 214 -40.765 23.375 -5.716 1.00 71.81 C ANISOU 1641 CE MET A 214 9090 10715 7477 -474 -799 -509 C ATOM 1642 N SER A 215 -41.857 28.427 -5.125 1.00 62.88 N ANISOU 1642 N SER A 215 7453 9856 6583 -142 -834 51 N ATOM 1643 CA SER A 215 -42.967 29.005 -5.888 1.00 66.44 C ANISOU 1643 CA SER A 215 7747 10521 6975 -80 -930 86 C ATOM 1644 C SER A 215 -42.544 29.424 -7.303 1.00 64.91 C ANISOU 1644 C SER A 215 7581 10469 6612 34 -986 150 C ATOM 1645 O SER A 215 -43.301 29.184 -8.241 1.00 66.18 O ANISOU 1645 O SER A 215 7664 10835 6647 39 -1093 92 O ATOM 1646 CB SER A 215 -43.583 30.202 -5.136 1.00 67.90 C ANISOU 1646 CB SER A 215 7837 10687 7275 11 -901 219 C ATOM 1647 OG SER A 215 -44.379 29.751 -4.060 1.00 69.19 O ANISOU 1647 OG SER A 215 7961 10751 7578 -93 -847 154 O ATOM 1648 N ILE A 216 -41.329 29.988 -7.433 1.00 60.66 N ANISOU 1648 N ILE A 216 7150 9840 6059 117 -914 262 N ATOM 1649 CA ILE A 216 -40.708 30.332 -8.713 1.00 60.84 C ANISOU 1649 CA ILE A 216 7213 9991 5914 218 -941 332 C ATOM 1650 C ILE A 216 -40.448 29.083 -9.577 1.00 60.88 C ANISOU 1650 C ILE A 216 7280 10073 5778 152 -985 168 C ATOM 1651 O ILE A 216 -40.847 29.082 -10.737 1.00 61.76 O ANISOU 1651 O ILE A 216 7364 10380 5723 194 -1072 146 O ATOM 1652 CB ILE A 216 -39.388 31.141 -8.526 1.00 60.10 C ANISOU 1652 CB ILE A 216 7210 9777 5849 285 -830 472 C ATOM 1653 CG1 ILE A 216 -39.688 32.542 -7.944 1.00 58.17 C ANISOU 1653 CG1 ILE A 216 6924 9449 5729 347 -787 628 C ATOM 1654 CG2 ILE A 216 -38.531 31.284 -9.804 1.00 64.66 C ANISOU 1654 CG2 ILE A 216 7840 10485 6242 369 -833 536 C ATOM 1655 CD1 ILE A 216 -38.457 33.254 -7.359 1.00 58.63 C ANISOU 1655 CD1 ILE A 216 7063 9363 5849 361 -667 736 C ATOM 1656 N VAL A 217 -39.844 28.038 -8.985 1.00 58.89 N ANISOU 1656 N VAL A 217 7127 9665 5582 58 -927 49 N ATOM 1657 CA VAL A 217 -39.597 26.736 -9.609 1.00 57.92 C ANISOU 1657 CA VAL A 217 7100 9573 5334 5 -950 -116 C ATOM 1658 C VAL A 217 -40.891 26.057 -10.107 1.00 61.72 C ANISOU 1658 C VAL A 217 7506 10189 5757 -105 -1059 -267 C ATOM 1659 O VAL A 217 -40.969 25.725 -11.289 1.00 65.18 O ANISOU 1659 O VAL A 217 7964 10779 6023 -106 -1130 -360 O ATOM 1660 CB VAL A 217 -38.801 25.808 -8.635 1.00 56.35 C ANISOU 1660 CB VAL A 217 7041 9154 5217 -48 -859 -200 C ATOM 1661 CG1 VAL A 217 -38.911 24.285 -8.849 1.00 57.51 C ANISOU 1661 CG1 VAL A 217 7303 9290 5257 -120 -880 -396 C ATOM 1662 CG2 VAL A 217 -37.313 26.197 -8.622 1.00 45.69 C ANISOU 1662 CG2 VAL A 217 5744 7741 3873 67 -769 -84 C ATOM 1663 N ALA A 218 -41.889 25.911 -9.219 1.00 58.94 N ANISOU 1663 N ALA A 218 7057 9801 5536 -206 -1074 -301 N ATOM 1664 CA ALA A 218 -43.171 25.260 -9.501 1.00 59.53 C ANISOU 1664 CA ALA A 218 7033 10019 5568 -343 -1172 -463 C ATOM 1665 C ALA A 218 -43.996 25.938 -10.610 1.00 59.76 C ANISOU 1665 C ALA A 218 6903 10343 5461 -246 -1302 -413 C ATOM 1666 O ALA A 218 -44.511 25.237 -11.481 1.00 58.27 O ANISOU 1666 O ALA A 218 6679 10334 5129 -313 -1404 -558 O ATOM 1667 CB ALA A 218 -43.984 25.166 -8.201 1.00 58.08 C ANISOU 1667 CB ALA A 218 6765 9744 5562 -476 -1137 -504 C ATOM 1668 N VAL A 219 -44.089 27.278 -10.566 1.00 60.46 N ANISOU 1668 N VAL A 219 6909 10480 5582 -83 -1303 -210 N ATOM 1669 CA VAL A 219 -44.848 28.078 -11.529 1.00 61.64 C ANISOU 1669 CA VAL A 219 6913 10903 5602 41 -1427 -137 C ATOM 1670 C VAL A 219 -44.136 28.204 -12.889 1.00 63.56 C ANISOU 1670 C VAL A 219 7252 11275 5622 146 -1468 -102 C ATOM 1671 O VAL A 219 -44.807 28.090 -13.912 1.00 65.33 O ANISOU 1671 O VAL A 219 7397 11756 5669 171 -1600 -165 O ATOM 1672 CB VAL A 219 -45.166 29.496 -10.964 1.00 0.00 C ATOM 1673 CG1 VAL A 219 -45.684 30.529 -11.989 1.00 0.00 C ATOM 1674 CG2 VAL A 219 -46.167 29.402 -9.796 1.00 0.00 C ATOM 1675 N SER A 220 -42.813 28.437 -12.886 1.00 62.38 N ANISOU 1675 N SER A 220 7266 10971 5466 208 -1354 -9 N ATOM 1676 CA SER A 220 -42.039 28.736 -14.094 1.00 64.89 C ANISOU 1676 CA SER A 220 7674 11413 5568 315 -1366 42 C ATOM 1677 C SER A 220 -41.763 27.497 -14.972 1.00 69.67 C ANISOU 1677 C SER A 220 8327 12135 6009 215 -1437 -185 C ATOM 1678 O SER A 220 -41.755 27.635 -16.195 1.00 73.51 O ANISOU 1678 O SER A 220 8781 12867 6284 275 -1547 -207 O ATOM 1679 CB SER A 220 -40.766 29.502 -13.691 1.00 0.00 C ATOM 1680 OG SER A 220 -40.128 30.087 -14.798 1.00 0.00 O ATOM 1681 N TYR A 221 -41.615 26.307 -14.358 1.00 69.09 N ANISOU 1681 N TYR A 221 8349 11883 6019 69 -1376 -357 N ATOM 1682 CA TYR A 221 -41.606 25.022 -15.073 1.00 71.06 C ANISOU 1682 CA TYR A 221 8675 12202 6122 -37 -1430 -589 C ATOM 1683 C TYR A 221 -43.015 24.569 -15.507 1.00 73.77 C ANISOU 1683 C TYR A 221 8870 12738 6422 -167 -1579 -748 C ATOM 1684 O TYR A 221 -43.119 23.807 -16.469 1.00 76.82 O ANISOU 1684 O TYR A 221 9287 13270 6630 -236 -1662 -929 O ATOM 1685 CB TYR A 221 -40.902 23.935 -14.226 1.00 72.42 C ANISOU 1685 CB TYR A 221 9016 12102 6400 -142 -1315 -721 C ATOM 1686 CG TYR A 221 -39.397 24.105 -14.057 1.00 72.97 C ANISOU 1686 CG TYR A 221 9213 12039 6474 -9 -1183 -605 C ATOM 1687 CD1 TYR A 221 -38.566 24.285 -15.183 1.00 74.11 C ANISOU 1687 CD1 TYR A 221 9437 12304 6417 102 -1169 -598 C ATOM 1688 CD2 TYR A 221 -38.810 24.056 -12.775 1.00 72.01 C ANISOU 1688 CD2 TYR A 221 9121 11693 6546 4 -1074 -510 C ATOM 1689 CE1 TYR A 221 -37.178 24.455 -15.028 1.00 73.66 C ANISOU 1689 CE1 TYR A 221 9466 12156 6364 215 -1041 -500 C ATOM 1690 CE2 TYR A 221 -37.422 24.231 -12.615 1.00 70.72 C ANISOU 1690 CE2 TYR A 221 9042 11445 6385 118 -962 -417 C ATOM 1691 CZ TYR A 221 -36.606 24.438 -13.742 1.00 72.42 C ANISOU 1691 CZ TYR A 221 9315 11790 6410 220 -943 -413 C ATOM 1692 OH TYR A 221 -35.265 24.628 -13.594 1.00 74.50 O ANISOU 1692 OH TYR A 221 9635 11997 6677 323 -824 -330 O ATOM 1693 N GLY A 222 -44.067 25.067 -14.831 1.00 73.61 N ANISOU 1693 N GLY A 222 8680 12736 6554 -204 -1612 -696 N ATOM 1694 CA GLY A 222 -45.466 24.839 -15.200 1.00 73.10 C ANISOU 1694 CA GLY A 222 8417 12924 6433 -297 -1764 -822 C ATOM 1695 C GLY A 222 -45.872 25.697 -16.411 1.00 72.78 C ANISOU 1695 C GLY A 222 8266 13207 6179 -116 -1904 -721 C ATOM 1696 O GLY A 222 -46.672 25.244 -17.229 1.00 74.76 O ANISOU 1696 O GLY A 222 8406 13727 6274 -179 -2054 -875 O ATOM 1697 N LEU A 223 -45.293 26.905 -16.549 1.00 70.24 N ANISOU 1697 N LEU A 223 7980 12868 5840 108 -1857 -461 N ATOM 1698 CA LEU A 223 -45.449 27.801 -17.698 1.00 72.44 C ANISOU 1698 CA LEU A 223 8207 13425 5890 306 -1971 -334 C ATOM 1699 C LEU A 223 -44.807 27.235 -18.976 1.00 72.84 C ANISOU 1699 C LEU A 223 8405 13584 5688 309 -1996 -434 C ATOM 1700 O LEU A 223 -45.366 27.421 -20.057 1.00 76.51 O ANISOU 1700 O LEU A 223 8805 14351 5915 377 -2144 -470 O ATOM 1701 CB LEU A 223 -44.866 29.190 -17.361 1.00 71.75 C ANISOU 1701 CB LEU A 223 8163 13239 5859 523 -1883 -28 C ATOM 1702 CG LEU A 223 -45.796 30.087 -16.516 1.00 72.07 C ANISOU 1702 CG LEU A 223 8057 13223 6105 582 -1876 97 C ATOM 1703 CD1 LEU A 223 -45.038 31.322 -15.983 1.00 70.69 C ANISOU 1703 CD1 LEU A 223 7996 12840 6024 736 -1736 364 C ATOM 1704 CD2 LEU A 223 -47.081 30.480 -17.277 1.00 72.70 C ANISOU 1704 CD2 LEU A 223 7923 13631 6068 696 -2060 108 C ATOM 1705 N ILE A 224 -43.673 26.528 -18.826 1.00 68.70 N ANISOU 1705 N ILE A 224 8076 12829 5198 251 -1852 -482 N ATOM 1706 CA ILE A 224 -43.004 25.785 -19.896 1.00 69.74 C ANISOU 1706 CA ILE A 224 8357 13047 5096 256 -1855 -598 C ATOM 1707 C ILE A 224 -43.839 24.580 -20.378 1.00 75.16 C ANISOU 1707 C ILE A 224 9007 13868 5682 67 -1980 -906 C ATOM 1708 O ILE A 224 -43.898 24.346 -21.584 1.00 80.54 O ANISOU 1708 O ILE A 224 9699 14803 6101 96 -2091 -1002 O ATOM 1709 CB ILE A 224 -41.586 25.313 -19.446 1.00 68.22 C ANISOU 1709 CB ILE A 224 8360 12576 4984 253 -1665 -586 C ATOM 1710 CG1 ILE A 224 -40.645 26.529 -19.307 1.00 66.37 C ANISOU 1710 CG1 ILE A 224 8148 12240 4829 414 -1545 -294 C ATOM 1711 CG2 ILE A 224 -40.922 24.232 -20.332 1.00 69.00 C ANISOU 1711 CG2 ILE A 224 8613 12761 4843 260 -1656 -734 C ATOM 1712 CD1 ILE A 224 -39.345 26.237 -18.544 1.00 63.71 C ANISOU 1712 CD1 ILE A 224 7956 11660 4591 412 -1365 -280 C ATOM 1713 N ALA A 225 -44.481 23.867 -19.436 1.00 74.83 N ANISOU 1713 N ALA A 225 8931 13660 5840 -140 -1958 -1069 N ATOM 1714 CA ALA A 225 -45.312 22.691 -19.693 1.00 76.46 C ANISOU 1714 CA ALA A 225 9113 13965 5975 -365 -2059 -1375 C ATOM 1715 C ALA A 225 -46.581 22.995 -20.509 1.00 80.72 C ANISOU 1715 C ALA A 225 9412 14892 6365 -362 -2270 -1423 C ATOM 1716 O ALA A 225 -46.885 22.242 -21.433 1.00 84.97 O ANISOU 1716 O ALA A 225 9937 15627 6721 -486 -2389 -1660 O ATOM 1717 CB ALA A 225 -45.673 22.021 -18.358 1.00 73.85 C ANISOU 1717 CB ALA A 225 8796 13364 5901 -592 -1973 -1506 C ATOM 1718 N THR A 226 -47.282 24.094 -20.174 1.00 84.28 N ANISOU 1718 N THR A 226 9674 15463 6885 -212 -2321 -1208 N ATOM 1719 CA THR A 226 -48.497 24.523 -20.876 1.00 89.71 C ANISOU 1719 CA THR A 226 10120 16549 7418 -154 -2530 -1227 C ATOM 1720 C THR A 226 -48.208 25.173 -22.249 1.00 91.47 C ANISOU 1720 C THR A 226 10414 16971 7369 68 -2599 -1109 C ATOM 1721 O THR A 226 -49.030 25.031 -23.151 1.00 97.56 O ANISOU 1721 O THR A 226 11087 17955 8025 67 -2728 -1199 O ATOM 1722 CB THR A 226 -49.374 25.466 -20.003 1.00 0.00 C ATOM 1723 CG2 THR A 226 -48.729 26.815 -19.654 1.00 0.00 C ATOM 1724 OG1 THR A 226 -50.605 25.762 -20.638 1.00 0.00 O ATOM 1725 N LYS A 227 -47.034 25.813 -22.408 1.00 88.53 N ANISOU 1725 N LYS A 227 10223 16486 6926 250 -2486 -897 N ATOM 1726 CA LYS A 227 -46.550 26.352 -23.685 1.00 92.99 C ANISOU 1726 CA LYS A 227 10896 17164 7271 444 -2498 -769 C ATOM 1727 C LYS A 227 -46.173 25.240 -24.685 1.00 99.77 C ANISOU 1727 C LYS A 227 11890 18064 7953 318 -2516 -1020 C ATOM 1728 O LYS A 227 -46.467 25.381 -25.873 1.00106.28 O ANISOU 1728 O LYS A 227 12715 19075 8590 395 -2607 -1031 O ATOM 1729 CB LYS A 227 -45.400 27.346 -23.399 1.00 87.14 C ANISOU 1729 CB LYS A 227 10317 16276 6518 632 -2342 -490 C ATOM 1730 CG LYS A 227 -44.675 27.955 -24.616 1.00 85.59 C ANISOU 1730 CG LYS A 227 10242 16179 6101 826 -2324 -325 C ATOM 1731 CD LYS A 227 -45.572 28.694 -25.622 1.00 85.17 C ANISOU 1731 CD LYS A 227 10058 16292 6010 1011 -2435 -137 C ATOM 1732 CE LYS A 227 -44.742 29.401 -26.704 1.00 89.88 C ANISOU 1732 CE LYS A 227 10807 16955 6387 1207 -2395 57 C ATOM 1733 NZ LYS A 227 -45.592 29.934 -27.780 1.00 94.10 N1+ ANISOU 1733 NZ LYS A 227 11245 17633 6875 1412 -2494 252 N1+ ATOM 1734 N ILE A 228 -45.592 24.138 -24.179 1.00103.16 N ANISOU 1734 N ILE A 228 12449 18314 8432 134 -2430 -1226 N ATOM 1735 CA ILE A 228 -45.332 22.902 -24.925 1.00105.59 C ANISOU 1735 CA ILE A 228 12903 18627 8587 5 -2439 -1492 C ATOM 1736 C ILE A 228 -46.625 22.186 -25.372 1.00111.12 C ANISOU 1736 C ILE A 228 13450 19488 9282 -182 -2601 -1730 C ATOM 1737 O ILE A 228 -46.641 21.628 -26.467 1.00115.18 O ANISOU 1737 O ILE A 228 14019 20129 9615 -212 -2674 -1876 O ATOM 1738 CB ILE A 228 -44.434 21.930 -24.091 1.00102.75 C ANISOU 1738 CB ILE A 228 12737 18006 8296 -125 -2293 -1650 C ATOM 1739 CG1 ILE A 228 -42.970 22.428 -24.087 1.00 96.99 C ANISOU 1739 CG1 ILE A 228 12135 17090 7627 64 -2112 -1391 C ATOM 1740 CG2 ILE A 228 -44.480 20.437 -24.494 1.00105.64 C ANISOU 1740 CG2 ILE A 228 13286 18348 8505 -237 -2288 -1925 C ATOM 1741 CD1 ILE A 228 -42.107 21.809 -22.978 1.00 93.85 C ANISOU 1741 CD1 ILE A 228 11923 16327 7409 -23 -1928 -1484 C ATOM 1742 N HIS A 229 -47.672 22.227 -24.529 1.00113.57 N ANISOU 1742 N HIS A 229 13558 19803 9790 -316 -2653 -1776 N ATOM 1743 CA HIS A 229 -48.986 21.636 -24.795 1.00120.46 C ANISOU 1743 CA HIS A 229 14245 20847 10677 -504 -2796 -1992 C ATOM 1744 C HIS A 229 -49.817 22.462 -25.797 1.00125.84 C ANISOU 1744 C HIS A 229 14765 21837 11213 -316 -2946 -1870 C ATOM 1745 O HIS A 229 -50.521 21.875 -26.618 1.00128.58 O ANISOU 1745 O HIS A 229 15001 22368 11484 -439 -3073 -2063 O ATOM 1746 CB HIS A 229 -49.714 21.451 -23.446 1.00121.61 C ANISOU 1746 CB HIS A 229 14197 20932 11077 -680 -2791 -2043 C ATOM 1747 CG HIS A 229 -50.995 20.652 -23.493 1.00126.32 C ANISOU 1747 CG HIS A 229 14625 21651 11720 -945 -2892 -2312 C ATOM 1748 CD2 HIS A 229 -51.260 19.335 -23.184 1.00127.77 C ANISOU 1748 CD2 HIS A 229 14836 21685 12025 -1277 -2845 -2584 C ATOM 1749 ND1 HIS A 229 -52.215 21.197 -23.862 1.00130.39 N ANISOU 1749 ND1 HIS A 229 14914 22476 12152 -885 -3051 -2316 N ATOM 1750 CE1 HIS A 229 -53.125 20.223 -23.779 1.00132.65 C ANISOU 1750 CE1 HIS A 229 15076 22816 12507 -1176 -3101 -2583 C ATOM 1751 NE2 HIS A 229 -52.617 19.065 -23.372 1.00131.21 N ANISOU 1751 NE2 HIS A 229 15054 22346 12455 -1425 -2972 -2747 N ATOM 1752 N LYS A 230 -49.714 23.800 -25.714 1.00129.14 N ANISOU 1752 N LYS A 230 15176 22303 11587 -24 -2929 -1553 N ATOM 1753 CA LYS A 230 -50.392 24.767 -26.580 1.00135.91 C ANISOU 1753 CA LYS A 230 15904 23432 12303 182 -3062 -1415 C ATOM 1754 C LYS A 230 -49.822 24.805 -28.013 1.00140.83 C ANISOU 1754 C LYS A 230 16686 24170 12651 231 -3104 -1485 C ATOM 1755 O LYS A 230 -50.560 25.135 -28.941 1.00143.89 O ANISOU 1755 O LYS A 230 16975 24777 12921 154 -3248 -1659 O ATOM 1756 CB LYS A 230 -50.340 26.148 -25.886 1.00133.80 C ANISOU 1756 CB LYS A 230 15626 23132 12081 471 -3006 -1052 C ATOM 1757 CG LYS A 230 -51.030 27.301 -26.635 1.00138.24 C ANISOU 1757 CG LYS A 230 16045 23949 12533 702 -3138 -889 C ATOM 1758 CD LYS A 230 -51.083 28.591 -25.802 1.00137.25 C ANISOU 1758 CD LYS A 230 15949 23732 12467 978 -3060 -534 C ATOM 1759 CE LYS A 230 -51.778 29.741 -26.544 1.00142.58 C ANISOU 1759 CE LYS A 230 16488 24643 13045 1220 -3189 -376 C ATOM 1760 NZ LYS A 230 -51.839 30.955 -25.714 1.00142.99 N1+ ANISOU 1760 NZ LYS A 230 16613 24570 13148 1492 -3099 -26 N1+ ATOM 1761 N GLN A 231 -48.534 24.457 -28.156 1.00143.44 N ANISOU 1761 N GLN A 231 17260 24368 12873 354 -2975 -1354 N ATOM 1762 CA GLN A 231 -47.807 24.373 -29.422 1.00151.14 C ANISOU 1762 CA GLN A 231 18406 25438 13582 405 -2989 -1414 C ATOM 1763 C GLN A 231 -47.465 22.890 -29.695 1.00156.90 C ANISOU 1763 C GLN A 231 19269 26063 14284 149 -2961 -1754 C ATOM 1764 O GLN A 231 -48.006 21.998 -29.038 1.00157.51 O ANISOU 1764 O GLN A 231 19274 26035 14536 -81 -2966 -1954 O ATOM 1765 CB GLN A 231 -46.567 25.294 -29.290 1.00 0.00 C ATOM 1766 CG GLN A 231 -45.932 25.739 -30.628 1.00 0.00 C ATOM 1767 CD GLN A 231 -44.874 26.836 -30.475 1.00 0.00 C ATOM 1768 NE2 GLN A 231 -44.142 27.113 -31.555 1.00 0.00 N ATOM 1769 OE1 GLN A 231 -44.722 27.439 -29.414 1.00 0.00 O ATOM 1770 N GLY A 232 -46.588 22.640 -30.677 1.00161.66 N ANISOU 1770 N GLY A 232 20079 26679 14666 186 -2922 -1820 N ATOM 1771 CA GLY A 232 -46.036 21.318 -30.964 1.00166.36 C ANISOU 1771 CA GLY A 232 20843 27144 15221 -27 -2878 -2136 C ATOM 1772 C GLY A 232 -44.865 21.011 -30.014 1.00167.74 C ANISOU 1772 C GLY A 232 21185 27009 15539 -75 -2685 -2150 C ATOM 1773 O GLY A 232 -44.308 21.902 -29.369 1.00166.38 O ANISOU 1773 O GLY A 232 20936 26721 15561 -35 -2618 -1984 O ATOM 1774 N LEU A 233 -44.476 19.728 -29.971 1.00170.98 N ANISOU 1774 N LEU A 233 21829 27285 15849 -149 -2592 -2351 N ATOM 1775 CA LEU A 233 -43.422 19.181 -29.109 1.00171.38 C ANISOU 1775 CA LEU A 233 22060 27048 16011 -172 -2406 -2388 C ATOM 1776 C LEU A 233 -42.014 19.277 -29.751 1.00173.14 C ANISOU 1776 C LEU A 233 22465 27244 16075 43 -2253 -2238 C ATOM 1777 O LEU A 233 -41.166 18.426 -29.484 1.00174.55 O ANISOU 1777 O LEU A 233 22851 27245 16226 29 -2113 -2373 O ATOM 1778 CB LEU A 233 -43.812 17.737 -28.685 1.00 0.00 C ATOM 1779 CG LEU A 233 -44.875 17.659 -27.560 1.00 0.00 C ATOM 1780 CD1 LEU A 233 -46.276 18.132 -28.001 1.00 0.00 C ATOM 1781 CD2 LEU A 233 -44.921 16.248 -26.931 1.00 0.00 C ATOM 1782 N ILE A 234 -41.769 20.327 -30.557 1.00167.45 N ANISOU 1782 N ILE A 234 21673 26697 15252 249 -2266 -1954 N ATOM 1783 CA ILE A 234 -40.487 20.622 -31.209 1.00163.56 C ANISOU 1783 CA ILE A 234 21333 26191 14619 441 -2104 -1786 C ATOM 1784 C ILE A 234 -39.380 20.947 -30.182 1.00158.62 C ANISOU 1784 C ILE A 234 20738 25359 14173 504 -1925 -1636 C ATOM 1785 O ILE A 234 -38.290 20.382 -30.271 1.00156.09 O ANISOU 1785 O ILE A 234 20576 24928 13802 568 -1754 -1658 O ATOM 1786 CB ILE A 234 -40.608 21.786 -32.250 1.00164.24 C ANISOU 1786 CB ILE A 234 21353 26508 14543 624 -2164 -1525 C ATOM 1787 CG1 ILE A 234 -41.483 21.386 -33.465 1.00166.11 C ANISOU 1787 CG1 ILE A 234 21685 26929 14501 625 -2244 -1675 C ATOM 1788 CG2 ILE A 234 -39.251 22.305 -32.780 1.00163.72 C ANISOU 1788 CG2 ILE A 234 21354 26381 14473 812 -1978 -1222 C ATOM 1789 CD1 ILE A 234 -42.994 21.323 -33.195 1.00167.63 C ANISOU 1789 CD1 ILE A 234 21789 27226 14677 438 -2446 -1952 C ATOM 1790 N LYS A 235 -39.704 21.811 -29.201 1.00162.50 N ANISOU 1790 N LYS A 235 21070 25800 14871 491 -1958 -1490 N ATOM 1791 CA LYS A 235 -38.851 22.115 -28.048 1.00163.10 C ANISOU 1791 CA LYS A 235 21162 25680 15128 526 -1808 -1371 C ATOM 1792 C LYS A 235 -38.740 20.932 -27.067 1.00176.65 C ANISOU 1792 C LYS A 235 22938 27193 16989 353 -1780 -1632 C ATOM 1793 O LYS A 235 -37.710 20.789 -26.407 1.00178.70 O ANISOU 1793 O LYS A 235 23252 27268 17378 387 -1638 -1579 O ATOM 1794 CB LYS A 235 -39.373 23.406 -27.370 1.00151.47 C ANISOU 1794 CB LYS A 235 19513 24233 13808 595 -1847 -1093 C ATOM 1795 CG LYS A 235 -38.583 23.869 -26.126 1.00139.68 C ANISOU 1795 CG LYS A 235 18055 22632 12383 736 -1669 -824 C ATOM 1796 CD LYS A 235 -39.115 23.321 -24.784 1.00131.32 C ANISOU 1796 CD LYS A 235 17010 21302 11584 651 -1559 -874 C ATOM 1797 CE LYS A 235 -38.014 23.208 -23.719 1.00125.32 C ANISOU 1797 CE LYS A 235 16334 20393 10888 761 -1341 -697 C ATOM 1798 NZ LYS A 235 -38.548 22.709 -22.440 1.00120.69 N1+ ANISOU 1798 NZ LYS A 235 15807 19506 10543 682 -1220 -817 N1+ ATOM 1799 N SER A 236 -39.805 20.116 -26.997 1.00186.34 N ANISOU 1799 N SER A 236 24166 28427 18209 162 -1900 -1909 N ATOM 1800 CA SER A 236 -39.976 18.995 -26.074 1.00186.30 C ANISOU 1800 CA SER A 236 24257 28196 18332 -22 -1859 -2173 C ATOM 1801 C SER A 236 -39.340 17.681 -26.582 1.00187.55 C ANISOU 1801 C SER A 236 24672 28203 18383 17 -1715 -2349 C ATOM 1802 O SER A 236 -39.828 16.598 -26.254 1.00189.46 O ANISOU 1802 O SER A 236 25053 28298 18635 -147 -1716 -2640 O ATOM 1803 CB SER A 236 -41.479 18.883 -25.756 1.00188.16 C ANISOU 1803 CB SER A 236 24405 28480 18607 -266 -2022 -2406 C ATOM 1804 OG SER A 236 -41.735 18.017 -24.674 1.00 0.00 O ATOM 1805 N SER A 237 -38.225 17.794 -27.327 1.00182.14 N ANISOU 1805 N SER A 237 24062 27540 17603 232 -1576 -2179 N ATOM 1806 CA SER A 237 -37.309 16.697 -27.659 1.00180.18 C ANISOU 1806 CA SER A 237 24040 27164 17255 301 -1427 -2339 C ATOM 1807 C SER A 237 -36.635 16.103 -26.399 1.00172.94 C ANISOU 1807 C SER A 237 23230 25891 16589 263 -1294 -2415 C ATOM 1808 O SER A 237 -36.345 14.908 -26.367 1.00174.85 O ANISOU 1808 O SER A 237 23683 25965 16786 269 -1202 -2635 O ATOM 1809 CB SER A 237 -36.284 17.225 -28.685 1.00183.73 C ANISOU 1809 CB SER A 237 24508 27727 17573 528 -1294 -2116 C ATOM 1810 OG SER A 237 -35.381 16.222 -29.108 1.00 0.00 O ATOM 1811 N ARG A 238 -36.467 16.949 -25.367 1.00163.65 N ANISOU 1811 N ARG A 238 21924 24556 15698 239 -1273 -2218 N ATOM 1812 CA ARG A 238 -36.118 16.589 -23.997 1.00157.15 C ANISOU 1812 CA ARG A 238 21201 23368 15139 194 -1157 -2267 C ATOM 1813 C ARG A 238 -37.374 15.992 -23.317 1.00163.95 C ANISOU 1813 C ARG A 238 22064 24089 16141 -63 -1258 -2450 C ATOM 1814 O ARG A 238 -38.376 16.707 -23.249 1.00163.43 O ANISOU 1814 O ARG A 238 21809 24187 16099 -181 -1402 -2401 O ATOM 1815 CB ARG A 238 -35.664 17.865 -23.244 1.00146.01 C ANISOU 1815 CB ARG A 238 19667 21851 13959 302 -1064 -1970 C ATOM 1816 CG ARG A 238 -34.455 18.599 -23.861 1.00137.88 C ANISOU 1816 CG ARG A 238 18612 20955 12819 523 -946 -1776 C ATOM 1817 CD ARG A 238 -34.820 19.644 -24.934 1.00134.29 C ANISOU 1817 CD ARG A 238 17997 20801 12228 567 -1031 -1570 C ATOM 1818 NE ARG A 238 -33.631 20.168 -25.617 1.00133.68 N ANISOU 1818 NE ARG A 238 17951 20903 11937 742 -925 -1466 N ATOM 1819 CZ ARG A 238 -33.641 21.113 -26.574 1.00135.70 C ANISOU 1819 CZ ARG A 238 18153 21445 11961 804 -984 -1349 C ATOM 1820 NH1 ARG A 238 -32.480 21.522 -27.102 1.00137.16 N1+ ANISOU 1820 NH1 ARG A 238 18382 21777 11954 951 -861 -1253 N1+ ATOM 1821 NH2 ARG A 238 -34.789 21.652 -27.013 1.00136.83 N1+ ANISOU 1821 NH2 ARG A 238 18195 21739 12055 724 -1166 -1326 N1+ ATOM 1822 N PRO A 239 -37.328 14.716 -22.855 1.00170.87 N ANISOU 1822 N PRO A 239 23154 24667 17102 -150 -1179 -2662 N ATOM 1823 CA PRO A 239 -38.455 14.057 -22.153 1.00169.65 C ANISOU 1823 CA PRO A 239 23015 24345 17098 -423 -1243 -2826 C ATOM 1824 C PRO A 239 -39.060 14.850 -20.982 1.00162.33 C ANISOU 1824 C PRO A 239 21889 23356 16433 -475 -1260 -2604 C ATOM 1825 O PRO A 239 -38.315 15.465 -20.221 1.00159.53 O ANISOU 1825 O PRO A 239 21515 22868 16230 -324 -1153 -2389 O ATOM 1826 CB PRO A 239 -37.847 12.738 -21.651 1.00171.61 C ANISOU 1826 CB PRO A 239 23572 24222 17413 -434 -1100 -3015 C ATOM 1827 CG PRO A 239 -36.753 12.421 -22.649 1.00173.38 C ANISOU 1827 CG PRO A 239 23937 24513 17428 -199 -1013 -3052 C ATOM 1828 CD PRO A 239 -36.194 13.796 -22.986 1.00171.71 C ANISOU 1828 CD PRO A 239 23505 24574 17162 0 -1019 -2762 C ATOM 1829 N LEU A 240 -40.396 14.805 -20.855 1.00153.73 N ANISOU 1829 N LEU A 240 20644 22380 15389 -695 -1393 -2670 N ATOM 1830 CA LEU A 240 -41.176 15.506 -19.824 1.00141.73 C ANISOU 1830 CA LEU A 240 18919 20833 14100 -752 -1416 -2481 C ATOM 1831 C LEU A 240 -40.899 15.038 -18.380 1.00130.52 C ANISOU 1831 C LEU A 240 17638 19025 12930 -800 -1272 -2458 C ATOM 1832 O LEU A 240 -41.271 15.749 -17.448 1.00129.73 O ANISOU 1832 O LEU A 240 17397 18865 13029 -829 -1263 -2293 O ATOM 1833 CB LEU A 240 -42.688 15.412 -20.149 1.00143.96 C ANISOU 1833 CB LEU A 240 18999 21328 14370 -982 -1581 -2594 C ATOM 1834 CG LEU A 240 -43.148 16.153 -21.428 1.00144.98 C ANISOU 1834 CG LEU A 240 18968 21881 14237 -944 -1759 -2629 C ATOM 1835 CD1 LEU A 240 -42.786 17.651 -21.417 1.00142.89 C ANISOU 1835 CD1 LEU A 240 18658 21783 13848 -643 -1740 -2365 C ATOM 1836 CD2 LEU A 240 -42.736 15.441 -22.731 1.00147.37 C ANISOU 1836 CD2 LEU A 240 19431 22244 14318 -1085 -1813 -2960 C ATOM 1837 N ARG A 241 -40.209 13.894 -18.215 1.00122.62 N ANISOU 1837 N ARG A 241 16921 17757 11911 -790 -1159 -2616 N ATOM 1838 CA ARG A 241 -39.671 13.418 -16.942 1.00114.72 C ANISOU 1838 CA ARG A 241 16077 16395 11117 -757 -1014 -2552 C ATOM 1839 C ARG A 241 -38.601 14.367 -16.369 1.00107.44 C ANISOU 1839 C ARG A 241 15043 15490 10287 -511 -951 -2258 C ATOM 1840 O ARG A 241 -38.591 14.564 -15.158 1.00105.34 O ANISOU 1840 O ARG A 241 14798 15011 10218 -498 -874 -2140 O ATOM 1841 CB ARG A 241 -39.111 11.985 -17.086 1.00114.81 C ANISOU 1841 CB ARG A 241 16427 16138 11057 -715 -902 -2752 C ATOM 1842 CG ARG A 241 -40.174 10.899 -17.353 1.00116.63 C ANISOU 1842 CG ARG A 241 16866 16084 11364 -985 -868 -2985 C ATOM 1843 CD ARG A 241 -40.553 10.657 -18.826 1.00120.19 C ANISOU 1843 CD ARG A 241 17320 16702 11647 -1222 -980 -3261 C ATOM 1844 NE ARG A 241 -39.468 10.001 -19.572 1.00125.01 N ANISOU 1844 NE ARG A 241 18136 17331 12031 -1103 -956 -3441 N ATOM 1845 CZ ARG A 241 -39.503 9.668 -20.874 1.00130.26 C ANISOU 1845 CZ ARG A 241 18942 18004 12548 -1303 -1003 -3747 C ATOM 1846 NH1 ARG A 241 -38.438 9.073 -21.427 1.00133.20 N1+ ANISOU 1846 NH1 ARG A 241 19510 18391 12708 -1168 -971 -3903 N1+ ATOM 1847 NH2 ARG A 241 -40.583 9.916 -21.629 1.00131.86 N1+ ANISOU 1847 NH2 ARG A 241 19086 18205 12810 -1649 -1077 -3910 N1+ ATOM 1848 N VAL A 242 -37.771 14.978 -17.237 1.00103.81 N ANISOU 1848 N VAL A 242 14475 15288 9681 -328 -978 -2141 N ATOM 1849 CA VAL A 242 -36.793 16.014 -16.880 1.00100.06 C ANISOU 1849 CA VAL A 242 13879 14851 9287 -127 -916 -1871 C ATOM 1850 C VAL A 242 -37.463 17.261 -16.276 1.00 95.88 C ANISOU 1850 C VAL A 242 13114 14409 8907 -202 -986 -1686 C ATOM 1851 O VAL A 242 -37.004 17.736 -15.240 1.00 95.77 O ANISOU 1851 O VAL A 242 13045 14278 9065 -136 -921 -1510 O ATOM 1852 CB VAL A 242 -35.947 16.463 -18.110 1.00101.61 C ANISOU 1852 CB VAL A 242 14041 15293 9273 65 -905 -1805 C ATOM 1853 CG1 VAL A 242 -35.116 17.749 -17.910 1.00100.22 C ANISOU 1853 CG1 VAL A 242 13734 15159 9185 234 -831 -1531 C ATOM 1854 CG2 VAL A 242 -35.046 15.322 -18.612 1.00102.26 C ANISOU 1854 CG2 VAL A 242 14358 15290 9206 159 -821 -1997 C ATOM 1855 N LEU A 243 -38.538 17.736 -16.931 1.00 94.09 N ANISOU 1855 N LEU A 243 12743 14397 8611 -332 -1122 -1734 N ATOM 1856 CA LEU A 243 -39.339 18.893 -16.523 1.00 89.93 C ANISOU 1856 CA LEU A 243 11981 13983 8203 -362 -1191 -1557 C ATOM 1857 C LEU A 243 -40.036 18.693 -15.160 1.00 87.54 C ANISOU 1857 C LEU A 243 11673 13450 8137 -515 -1153 -1567 C ATOM 1858 O LEU A 243 -40.223 19.671 -14.437 1.00 84.60 O ANISOU 1858 O LEU A 243 11185 13038 7923 -468 -1124 -1377 O ATOM 1859 CB LEU A 243 -40.329 19.229 -17.664 1.00 90.47 C ANISOU 1859 CB LEU A 243 11891 14367 8118 -436 -1356 -1619 C ATOM 1860 CG LEU A 243 -41.135 20.537 -17.495 1.00 87.48 C ANISOU 1860 CG LEU A 243 11289 14209 7739 -318 -1427 -1377 C ATOM 1861 CD1 LEU A 243 -40.210 21.767 -17.411 1.00 86.71 C ANISOU 1861 CD1 LEU A 243 11234 14134 7579 -93 -1337 -1168 C ATOM 1862 CD2 LEU A 243 -42.170 20.685 -18.626 1.00 88.16 C ANISOU 1862 CD2 LEU A 243 11232 14629 7638 -360 -1603 -1454 C ATOM 1863 N SER A 244 -40.350 17.431 -14.820 1.00 88.45 N ANISOU 1863 N SER A 244 11926 13406 8276 -707 -1140 -1791 N ATOM 1864 CA SER A 244 -40.847 17.027 -13.508 1.00 87.42 C ANISOU 1864 CA SER A 244 11818 13046 8353 -869 -1084 -1805 C ATOM 1865 C SER A 244 -39.733 16.986 -12.444 1.00 85.79 C ANISOU 1865 C SER A 244 11787 12537 8271 -750 -939 -1708 C ATOM 1866 O SER A 244 -39.946 17.528 -11.363 1.00 86.30 O ANISOU 1866 O SER A 244 11850 12429 8509 -830 -884 -1649 O ATOM 1867 CB SER A 244 -41.567 15.668 -13.616 1.00 0.00 C ATOM 1868 OG SER A 244 -42.846 15.837 -14.189 1.00 0.00 O ATOM 1869 N PHE A 245 -38.579 16.364 -12.759 1.00 84.90 N ANISOU 1869 N PHE A 245 11815 12378 8064 -553 -876 -1694 N ATOM 1870 CA PHE A 245 -37.458 16.147 -11.829 1.00 84.22 C ANISOU 1870 CA PHE A 245 11888 12032 8077 -421 -751 -1619 C ATOM 1871 C PHE A 245 -36.812 17.428 -11.275 1.00 84.06 C ANISOU 1871 C PHE A 245 11703 12066 8170 -279 -728 -1369 C ATOM 1872 O PHE A 245 -36.437 17.442 -10.105 1.00 85.29 O ANISOU 1872 O PHE A 245 11913 12027 8468 -257 -659 -1291 O ATOM 1873 CB PHE A 245 -36.363 15.267 -12.478 1.00 0.00 C ATOM 1874 CG PHE A 245 -36.728 13.842 -12.869 1.00 0.00 C ATOM 1875 CD1 PHE A 245 -37.632 13.066 -12.109 1.00 0.00 C ATOM 1876 CD2 PHE A 245 -36.018 13.220 -13.920 1.00 0.00 C ATOM 1877 CE1 PHE A 245 -37.876 11.744 -12.458 1.00 0.00 C ATOM 1878 CE2 PHE A 245 -36.274 11.897 -14.251 1.00 0.00 C ATOM 1879 CZ PHE A 245 -37.207 11.165 -13.527 1.00 0.00 C ATOM 1880 N VAL A 246 -36.715 18.479 -12.106 1.00 82.22 N ANISOU 1880 N VAL A 246 11286 12088 7865 -185 -783 -1242 N ATOM 1881 CA VAL A 246 -36.150 19.785 -11.743 1.00 79.66 C ANISOU 1881 CA VAL A 246 10825 11801 7642 -65 -749 -1016 C ATOM 1882 C VAL A 246 -37.010 20.615 -10.756 1.00 78.60 C ANISOU 1882 C VAL A 246 10575 11606 7684 -185 -771 -934 C ATOM 1883 O VAL A 246 -36.524 21.634 -10.264 1.00 75.88 O ANISOU 1883 O VAL A 246 10204 11158 7470 -128 -713 -802 O ATOM 1884 CB VAL A 246 -35.864 20.637 -13.009 1.00 78.71 C ANISOU 1884 CB VAL A 246 10568 11944 7396 49 -785 -898 C ATOM 1885 CG1 VAL A 246 -34.724 20.026 -13.844 1.00 79.98 C ANISOU 1885 CG1 VAL A 246 10835 12149 7403 202 -720 -942 C ATOM 1886 CG2 VAL A 246 -37.109 20.915 -13.870 1.00 80.12 C ANISOU 1886 CG2 VAL A 246 10644 12331 7469 -51 -908 -953 C ATOM 1887 N ALA A 247 -38.236 20.151 -10.458 1.00 80.39 N ANISOU 1887 N ALA A 247 10721 11912 7912 -353 -853 -1019 N ATOM 1888 CA ALA A 247 -39.113 20.693 -9.420 1.00 77.52 C ANISOU 1888 CA ALA A 247 10231 11513 7708 -466 -864 -954 C ATOM 1889 C ALA A 247 -39.381 19.673 -8.303 1.00 75.33 C ANISOU 1889 C ALA A 247 10104 10968 7547 -598 -787 -1044 C ATOM 1890 O ALA A 247 -39.461 20.076 -7.143 1.00 75.72 O ANISOU 1890 O ALA A 247 10094 10934 7741 -645 -752 -959 O ATOM 1891 CB ALA A 247 -40.428 21.156 -10.065 1.00 0.00 C ATOM 1892 N ALA A 248 -39.509 18.381 -8.656 1.00 74.36 N ANISOU 1892 N ALA A 248 10195 10699 7358 -651 -750 -1212 N ATOM 1893 CA ALA A 248 -39.830 17.287 -7.740 1.00 74.09 C ANISOU 1893 CA ALA A 248 10354 10381 7418 -771 -662 -1290 C ATOM 1894 C ALA A 248 -38.676 16.910 -6.800 1.00 73.63 C ANISOU 1894 C ALA A 248 10450 10121 7406 -588 -566 -1188 C ATOM 1895 O ALA A 248 -38.931 16.702 -5.617 1.00 77.21 O ANISOU 1895 O ALA A 248 10971 10391 7974 -630 -500 -1134 O ATOM 1896 CB ALA A 248 -40.297 16.062 -8.539 1.00 76.95 C ANISOU 1896 CB ALA A 248 10906 10647 7687 -919 -658 -1525 C ATOM 1897 N ALA A 249 -37.437 16.857 -7.323 1.00 71.63 N ANISOU 1897 N ALA A 249 10245 9916 7055 -381 -556 -1160 N ATOM 1898 CA ALA A 249 -36.226 16.606 -6.532 1.00 71.36 C ANISOU 1898 CA ALA A 249 10322 9736 7055 -188 -478 -1070 C ATOM 1899 C ALA A 249 -35.849 17.799 -5.641 1.00 70.37 C ANISOU 1899 C ALA A 249 10029 9657 7050 -139 -476 -881 C ATOM 1900 O ALA A 249 -35.335 17.585 -4.544 1.00 72.34 O ANISOU 1900 O ALA A 249 10368 9741 7377 -86 -419 -821 O ATOM 1901 CB ALA A 249 -35.060 16.245 -7.464 1.00 0.00 C ATOM 1902 N PHE A 250 -36.149 19.023 -6.110 1.00 67.06 N ANISOU 1902 N PHE A 250 9381 9459 6641 -152 -536 -787 N ATOM 1903 CA PHE A 250 -35.992 20.265 -5.356 1.00 63.48 C ANISOU 1903 CA PHE A 250 8780 9037 6301 -118 -529 -621 C ATOM 1904 C PHE A 250 -36.967 20.347 -4.165 1.00 62.95 C ANISOU 1904 C PHE A 250 8720 8839 6360 -269 -509 -619 C ATOM 1905 O PHE A 250 -36.550 20.728 -3.071 1.00 62.12 O ANISOU 1905 O PHE A 250 8625 8635 6343 -228 -464 -528 O ATOM 1906 CB PHE A 250 -36.098 21.460 -6.327 1.00 62.61 C ANISOU 1906 CB PHE A 250 8460 9164 6165 -97 -588 -523 C ATOM 1907 CG PHE A 250 -35.860 22.822 -5.703 1.00 61.56 C ANISOU 1907 CG PHE A 250 8196 9051 6144 -55 -571 -359 C ATOM 1908 CD1 PHE A 250 -34.548 23.222 -5.379 1.00 60.89 C ANISOU 1908 CD1 PHE A 250 8089 8988 6058 80 -528 -262 C ATOM 1909 CD2 PHE A 250 -36.943 23.630 -5.297 1.00 61.88 C ANISOU 1909 CD2 PHE A 250 8130 9094 6288 -157 -592 -314 C ATOM 1910 CE1 PHE A 250 -34.333 24.428 -4.730 1.00 60.44 C ANISOU 1910 CE1 PHE A 250 7926 8937 6101 95 -508 -130 C ATOM 1911 CE2 PHE A 250 -36.705 24.829 -4.638 1.00 61.78 C ANISOU 1911 CE2 PHE A 250 8019 9081 6373 -117 -567 -177 C ATOM 1912 CZ PHE A 250 -35.406 25.231 -4.364 1.00 60.73 C ANISOU 1912 CZ PHE A 250 7885 8952 6239 0 -527 -89 C ATOM 1913 N PHE A 251 -38.224 19.924 -4.381 1.00 63.36 N ANISOU 1913 N PHE A 251 8760 8902 6412 -451 -539 -727 N ATOM 1914 CA PHE A 251 -39.237 19.777 -3.338 1.00 61.97 C ANISOU 1914 CA PHE A 251 8567 8627 6351 -614 -506 -732 C ATOM 1915 C PHE A 251 -38.881 18.684 -2.313 1.00 64.31 C ANISOU 1915 C PHE A 251 9114 8647 6675 -643 -412 -777 C ATOM 1916 O PHE A 251 -38.911 18.959 -1.118 1.00 65.04 O ANISOU 1916 O PHE A 251 9230 8628 6853 -644 -356 -693 O ATOM 1917 CB PHE A 251 -40.626 19.565 -3.981 1.00 61.61 C ANISOU 1917 CB PHE A 251 8410 8706 6293 -812 -564 -850 C ATOM 1918 CG PHE A 251 -41.778 19.340 -3.011 1.00 62.62 C ANISOU 1918 CG PHE A 251 8511 8749 6532 -1005 -513 -878 C ATOM 1919 CD1 PHE A 251 -42.387 20.439 -2.368 1.00 62.23 C ANISOU 1919 CD1 PHE A 251 8268 8796 6582 -1005 -517 -767 C ATOM 1920 CD2 PHE A 251 -42.134 18.033 -2.615 1.00 63.45 C ANISOU 1920 CD2 PHE A 251 8798 8673 6639 -1192 -450 -1019 C ATOM 1921 CE1 PHE A 251 -43.369 20.227 -1.410 1.00 63.02 C ANISOU 1921 CE1 PHE A 251 8332 8836 6777 -1180 -457 -798 C ATOM 1922 CE2 PHE A 251 -43.112 17.842 -1.647 1.00 65.07 C ANISOU 1922 CE2 PHE A 251 8975 8807 6941 -1388 -384 -1044 C ATOM 1923 CZ PHE A 251 -43.731 18.934 -1.052 1.00 65.87 C ANISOU 1923 CZ PHE A 251 8861 9031 7137 -1380 -387 -934 C ATOM 1924 N LEU A 252 -38.541 17.476 -2.799 1.00 67.15 N ANISOU 1924 N LEU A 252 9682 8883 6951 -658 -390 -908 N ATOM 1925 CA LEU A 252 -38.252 16.290 -1.986 1.00 67.63 C ANISOU 1925 CA LEU A 252 10021 8651 7025 -677 -293 -948 C ATOM 1926 C LEU A 252 -37.037 16.445 -1.052 1.00 64.16 C ANISOU 1926 C LEU A 252 9656 8124 6597 -448 -255 -814 C ATOM 1927 O LEU A 252 -37.052 15.875 0.039 1.00 64.13 O ANISOU 1927 O LEU A 252 9805 7924 6637 -454 -183 -771 O ATOM 1928 CB LEU A 252 -38.117 15.071 -2.930 1.00 0.00 C ATOM 1929 CG LEU A 252 -37.862 13.697 -2.262 1.00 0.00 C ATOM 1930 CD1 LEU A 252 -38.966 13.318 -1.250 1.00 0.00 C ATOM 1931 CD2 LEU A 252 -37.648 12.604 -3.329 1.00 0.00 C ATOM 1932 N CYS A 253 -36.027 17.222 -1.476 1.00 61.91 N ANISOU 1932 N CYS A 253 9257 7999 6266 -249 -301 -746 N ATOM 1933 CA CYS A 253 -34.846 17.525 -0.674 1.00 63.58 C ANISOU 1933 CA CYS A 253 9508 8168 6481 -36 -276 -638 C ATOM 1934 C CYS A 253 -35.152 18.569 0.412 1.00 66.08 C ANISOU 1934 C CYS A 253 9671 8538 6899 -58 -279 -506 C ATOM 1935 O CYS A 253 -34.933 18.288 1.591 1.00 70.36 O ANISOU 1935 O CYS A 253 10307 8966 7461 30 -242 -441 O ATOM 1936 CB CYS A 253 -33.659 17.982 -1.538 1.00 62.41 C ANISOU 1936 CB CYS A 253 9276 8187 6249 161 -309 -623 C ATOM 1937 SG CYS A 253 -32.954 16.570 -2.434 1.00 63.08 S ANISOU 1937 SG CYS A 253 9596 8171 6199 288 -278 -769 S ATOM 1938 N TRP A 254 -35.658 19.739 -0.002 1.00 63.51 N ANISOU 1938 N TRP A 254 9121 8383 6628 -158 -324 -466 N ATOM 1939 CA TRP A 254 -35.781 20.905 0.868 1.00 58.82 C ANISOU 1939 CA TRP A 254 8377 7849 6122 -150 -325 -345 C ATOM 1940 C TRP A 254 -37.021 20.879 1.780 1.00 53.66 C ANISOU 1940 C TRP A 254 7712 7120 5557 -323 -290 -343 C ATOM 1941 O TRP A 254 -36.905 21.242 2.953 1.00 49.73 O ANISOU 1941 O TRP A 254 7194 6585 5118 -303 -261 -262 O ATOM 1942 CB TRP A 254 -35.714 22.188 0.016 1.00 59.38 C ANISOU 1942 CB TRP A 254 8221 8141 6198 -117 -381 -280 C ATOM 1943 CG TRP A 254 -34.368 22.482 -0.587 1.00 63.75 C ANISOU 1943 CG TRP A 254 8745 8786 6689 55 -391 -239 C ATOM 1944 CD1 TRP A 254 -33.892 22.039 -1.775 1.00 66.04 C ANISOU 1944 CD1 TRP A 254 9016 9192 6883 122 -413 -276 C ATOM 1945 CD2 TRP A 254 -33.271 23.229 0.015 1.00 63.42 C ANISOU 1945 CD2 TRP A 254 8681 8747 6669 175 -372 -162 C ATOM 1946 CE2 TRP A 254 -32.162 23.216 -0.886 1.00 62.73 C ANISOU 1946 CE2 TRP A 254 8541 8787 6505 302 -379 -156 C ATOM 1947 CE3 TRP A 254 -33.104 23.926 1.236 1.00 61.75 C ANISOU 1947 CE3 TRP A 254 8479 8460 6524 181 -351 -105 C ATOM 1948 NE1 TRP A 254 -32.601 22.485 -1.965 1.00 65.34 N ANISOU 1948 NE1 TRP A 254 8884 9180 6762 272 -398 -222 N ATOM 1949 CZ2 TRP A 254 -30.954 23.867 -0.597 1.00 61.92 C ANISOU 1949 CZ2 TRP A 254 8377 8749 6401 423 -365 -102 C ATOM 1950 CZ3 TRP A 254 -31.902 24.600 1.532 1.00 60.07 C ANISOU 1950 CZ3 TRP A 254 8215 8307 6300 306 -351 -55 C ATOM 1951 CH2 TRP A 254 -30.837 24.575 0.611 1.00 61.00 C ANISOU 1951 CH2 TRP A 254 8262 8563 6352 420 -359 -56 C ATOM 1952 N SER A 255 -38.181 20.455 1.261 1.00 54.83 N ANISOU 1952 N SER A 255 7863 7260 5710 -499 -288 -439 N ATOM 1953 CA SER A 255 -39.465 20.561 1.970 1.00 55.94 C ANISOU 1953 CA SER A 255 7943 7374 5938 -673 -246 -441 C ATOM 1954 C SER A 255 -39.571 19.792 3.313 1.00 57.17 C ANISOU 1954 C SER A 255 8295 7309 6116 -702 -151 -417 C ATOM 1955 O SER A 255 -40.068 20.400 4.260 1.00 54.87 O ANISOU 1955 O SER A 255 7931 7024 5895 -739 -113 -351 O ATOM 1956 CB SER A 255 -40.650 20.270 1.021 1.00 0.00 C ATOM 1957 OG SER A 255 -41.891 20.597 1.614 1.00 0.00 O ATOM 1958 N PRO A 256 -39.054 18.541 3.431 1.00 55.12 N ANISOU 1958 N PRO A 256 8298 6851 5794 -677 -101 -465 N ATOM 1959 CA PRO A 256 -39.037 17.809 4.719 1.00 53.52 C ANISOU 1959 CA PRO A 256 8299 6438 5596 -685 -8 -417 C ATOM 1960 C PRO A 256 -38.204 18.460 5.838 1.00 53.45 C ANISOU 1960 C PRO A 256 8240 6470 5600 -517 -19 -290 C ATOM 1961 O PRO A 256 -38.574 18.344 7.005 1.00 53.51 O ANISOU 1961 O PRO A 256 8252 6431 5647 -583 39 -239 O ATOM 1962 CB PRO A 256 -38.508 16.411 4.355 1.00 46.88 C ANISOU 1962 CB PRO A 256 7756 5389 4667 -614 29 -476 C ATOM 1963 CG PRO A 256 -38.844 16.259 2.883 1.00 51.33 C ANISOU 1963 CG PRO A 256 8275 6023 5204 -703 -15 -604 C ATOM 1964 CD PRO A 256 -38.611 17.663 2.346 1.00 52.34 C ANISOU 1964 CD PRO A 256 8094 6437 5358 -651 -117 -569 C ATOM 1965 N TYR A 257 -37.114 19.143 5.467 1.00 54.51 N ANISOU 1965 N TYR A 257 8317 6702 5693 -314 -89 -249 N ATOM 1966 CA TYR A 257 -36.329 19.987 6.368 1.00 48.02 C ANISOU 1966 CA TYR A 257 7426 5941 4878 -177 -109 -150 C ATOM 1967 C TYR A 257 -37.114 21.251 6.753 1.00 46.12 C ANISOU 1967 C TYR A 257 6955 5839 4730 -268 -121 -107 C ATOM 1968 O TYR A 257 -37.246 21.572 7.936 1.00 45.45 O ANISOU 1968 O TYR A 257 6866 5732 4672 -268 -90 -52 O ATOM 1969 CB TYR A 257 -34.944 20.264 5.718 1.00 0.00 C ATOM 1970 CG TYR A 257 -34.234 21.553 6.110 1.00 0.00 C ATOM 1971 CD1 TYR A 257 -33.925 21.807 7.462 1.00 0.00 C ATOM 1972 CD2 TYR A 257 -33.920 22.518 5.128 1.00 0.00 C ATOM 1973 CE1 TYR A 257 -33.355 23.039 7.834 1.00 0.00 C ATOM 1974 CE2 TYR A 257 -33.342 23.746 5.500 1.00 0.00 C ATOM 1975 CZ TYR A 257 -33.066 24.007 6.853 1.00 0.00 C ATOM 1976 OH TYR A 257 -32.510 25.196 7.211 1.00 0.00 O ATOM 1977 N GLN A 258 -37.645 21.941 5.742 1.00 49.09 N ANISOU 1977 N GLN A 258 7147 6359 5145 -332 -165 -132 N ATOM 1978 CA GLN A 258 -38.253 23.255 5.899 1.00 48.92 C ANISOU 1978 CA GLN A 258 6921 6456 5209 -392 -174 -88 C ATOM 1979 C GLN A 258 -39.549 23.285 6.724 1.00 51.05 C ANISOU 1979 C GLN A 258 7204 6658 5535 -547 -99 -106 C ATOM 1980 O GLN A 258 -39.786 24.258 7.440 1.00 48.22 O ANISOU 1980 O GLN A 258 6742 6342 5239 -559 -75 -58 O ATOM 1981 CB GLN A 258 -38.374 23.905 4.510 1.00 43.58 C ANISOU 1981 CB GLN A 258 6072 5945 4542 -408 -238 -104 C ATOM 1982 CG GLN A 258 -37.004 24.382 3.978 1.00 45.56 C ANISOU 1982 CG GLN A 258 6273 6294 4742 -262 -293 -65 C ATOM 1983 CD GLN A 258 -36.567 25.710 4.601 1.00 48.07 C ANISOU 1983 CD GLN A 258 6492 6664 5106 -186 -295 27 C ATOM 1984 NE2 GLN A 258 -35.658 26.432 3.960 1.00 45.77 N ANISOU 1984 NE2 GLN A 258 6169 6449 4772 -77 -323 58 N ATOM 1985 OE1 GLN A 258 -37.065 26.113 5.647 1.00 54.72 O ANISOU 1985 OE1 GLN A 258 7288 7482 6019 -233 -264 60 O ATOM 1986 N VAL A 259 -40.331 22.201 6.702 1.00 54.61 N ANISOU 1986 N VAL A 259 7784 6999 5964 -676 -49 -180 N ATOM 1987 CA VAL A 259 -41.498 22.050 7.578 1.00 56.21 C ANISOU 1987 CA VAL A 259 8006 7136 6215 -845 45 -201 C ATOM 1988 C VAL A 259 -41.103 21.767 9.043 1.00 60.25 C ANISOU 1988 C VAL A 259 8687 7505 6700 -794 120 -135 C ATOM 1989 O VAL A 259 -41.782 22.269 9.937 1.00 59.89 O ANISOU 1989 O VAL A 259 8578 7477 6700 -850 179 -104 O ATOM 1990 CB VAL A 259 -42.484 20.948 7.100 1.00 0.00 C ATOM 1991 CG1 VAL A 259 -43.117 21.310 5.745 1.00 0.00 C ATOM 1992 CG2 VAL A 259 -41.917 19.515 7.094 1.00 0.00 C ATOM 1993 N VAL A 260 -39.991 21.051 9.286 1.00 61.12 N ANISOU 1993 N VAL A 260 9015 7483 6725 -672 116 -114 N ATOM 1994 CA VAL A 260 -39.424 20.866 10.627 1.00 57.72 C ANISOU 1994 CA VAL A 260 8754 6935 6241 -592 169 -44 C ATOM 1995 C VAL A 260 -38.896 22.205 11.183 1.00 57.63 C ANISOU 1995 C VAL A 260 8589 7056 6254 -480 119 19 C ATOM 1996 O VAL A 260 -39.171 22.540 12.337 1.00 62.21 O ANISOU 1996 O VAL A 260 9197 7609 6829 -498 175 57 O ATOM 1997 CB VAL A 260 -38.302 19.778 10.638 1.00 53.43 C ANISOU 1997 CB VAL A 260 8464 6246 5591 -440 157 -33 C ATOM 1998 CG1 VAL A 260 -37.413 19.722 11.901 1.00 52.39 C ANISOU 1998 CG1 VAL A 260 8488 6035 5382 -314 185 51 C ATOM 1999 CG2 VAL A 260 -38.903 18.384 10.384 1.00 54.89 C ANISOU 1999 CG2 VAL A 260 8853 6248 5754 -573 233 -100 C ATOM 2000 N ALA A 261 -38.222 22.982 10.325 1.00 54.93 N ANISOU 2000 N ALA A 261 8089 6853 5928 -373 23 24 N ATOM 2001 CA ALA A 261 -37.775 24.340 10.620 1.00 54.03 C ANISOU 2001 CA ALA A 261 7835 6851 5843 -295 -16 71 C ATOM 2002 C ALA A 261 -38.930 25.305 10.941 1.00 57.22 C ANISOU 2002 C ALA A 261 8083 7316 6342 -409 26 73 C ATOM 2003 O ALA A 261 -38.840 26.059 11.912 1.00 61.39 O ANISOU 2003 O ALA A 261 8575 7864 6886 -384 43 101 O ATOM 2004 CB ALA A 261 -36.947 24.872 9.450 1.00 50.18 C ANISOU 2004 CB ALA A 261 7222 6491 5356 -186 -107 77 C ATOM 2005 N LEU A 262 -40.009 25.248 10.149 1.00 56.89 N ANISOU 2005 N LEU A 262 7943 7314 6357 -527 42 32 N ATOM 2006 CA LEU A 262 -41.229 26.027 10.363 1.00 55.15 C ANISOU 2006 CA LEU A 262 7562 7168 6225 -610 83 30 C ATOM 2007 C LEU A 262 -41.889 25.701 11.717 1.00 55.32 C ANISOU 2007 C LEU A 262 7677 7099 6241 -709 198 22 C ATOM 2008 O LEU A 262 -42.198 26.622 12.473 1.00 57.80 O ANISOU 2008 O LEU A 262 7920 7445 6595 -706 243 41 O ATOM 2009 CB LEU A 262 -42.185 25.823 9.168 1.00 55.60 C ANISOU 2009 CB LEU A 262 7468 7329 6328 -693 53 -16 C ATOM 2010 CG LEU A 262 -43.479 26.668 9.191 1.00 57.22 C ANISOU 2010 CG LEU A 262 7486 7637 6620 -757 92 -24 C ATOM 2011 CD1 LEU A 262 -43.183 28.186 9.201 1.00 56.56 C ANISOU 2011 CD1 LEU A 262 7312 7597 6580 -634 75 41 C ATOM 2012 CD2 LEU A 262 -44.415 26.261 8.033 1.00 60.38 C ANISOU 2012 CD2 LEU A 262 7723 8174 7044 -818 37 -73 C ATOM 2013 N ILE A 263 -42.021 24.401 12.028 1.00 55.60 N ANISOU 2013 N ILE A 263 7887 7013 6226 -800 257 -6 N ATOM 2014 CA ILE A 263 -42.508 23.908 13.319 1.00 54.38 C ANISOU 2014 CA ILE A 263 7845 6764 6052 -909 387 -4 C ATOM 2015 C ILE A 263 -41.627 24.385 14.493 1.00 56.80 C ANISOU 2015 C ILE A 263 8268 7019 6295 -792 405 59 C ATOM 2016 O ILE A 263 -42.165 24.858 15.495 1.00 56.97 O ANISOU 2016 O ILE A 263 8284 7042 6321 -843 496 67 O ATOM 2017 CB ILE A 263 -42.642 22.354 13.338 1.00 0.00 C ATOM 2018 CG1 ILE A 263 -43.780 21.895 12.397 1.00 0.00 C ATOM 2019 CG2 ILE A 263 -42.850 21.722 14.735 1.00 0.00 C ATOM 2020 CD1 ILE A 263 -43.677 20.420 11.973 1.00 0.00 C ATOM 2021 N ALA A 264 -40.298 24.312 14.331 1.00 57.60 N ANISOU 2021 N ALA A 264 8464 7097 6325 -632 317 93 N ATOM 2022 CA ALA A 264 -39.333 24.808 15.310 1.00 57.39 C ANISOU 2022 CA ALA A 264 8518 7062 6225 -517 308 138 C ATOM 2023 C ALA A 264 -39.491 26.313 15.589 1.00 59.46 C ANISOU 2023 C ALA A 264 8592 7443 6555 -496 289 132 C ATOM 2024 O ALA A 264 -39.499 26.700 16.752 1.00 64.48 O ANISOU 2024 O ALA A 264 9279 8073 7147 -474 327 143 O ATOM 2025 CB ALA A 264 -37.901 24.485 14.857 1.00 0.00 C ATOM 2026 N THR A 265 -39.681 27.116 14.533 1.00 57.08 N ANISOU 2026 N THR A 265 8092 7244 6354 -500 233 114 N ATOM 2027 CA THR A 265 -39.822 28.576 14.593 1.00 56.95 C ANISOU 2027 CA THR A 265 7921 7309 6408 -475 226 113 C ATOM 2028 C THR A 265 -41.013 29.061 15.459 1.00 57.90 C ANISOU 2028 C THR A 265 7991 7431 6580 -566 340 92 C ATOM 2029 O THR A 265 -40.880 30.037 16.191 1.00 57.99 O ANISOU 2029 O THR A 265 7985 7450 6597 -537 375 86 O ATOM 2030 CB THR A 265 -39.957 29.184 13.167 1.00 55.64 C ANISOU 2030 CB THR A 265 7584 7234 6323 -445 149 117 C ATOM 2031 CG2 THR A 265 -39.977 30.722 13.107 1.00 54.71 C ANISOU 2031 CG2 THR A 265 7344 7165 6279 -410 153 124 C ATOM 2032 OG1 THR A 265 -38.870 28.758 12.360 1.00 54.52 O ANISOU 2032 OG1 THR A 265 7481 7107 6127 -361 59 131 O ATOM 2033 N VAL A 266 -42.137 28.340 15.413 1.00 56.19 N ANISOU 2033 N VAL A 266 7743 7213 6396 -682 403 69 N ATOM 2034 CA VAL A 266 -43.344 28.608 16.206 1.00 56.75 C ANISOU 2034 CA VAL A 266 7739 7312 6512 -773 523 42 C ATOM 2035 C VAL A 266 -43.370 27.842 17.551 1.00 58.63 C ANISOU 2035 C VAL A 266 8169 7454 6655 -820 635 51 C ATOM 2036 O VAL A 266 -44.293 28.057 18.337 1.00 63.37 O ANISOU 2036 O VAL A 266 8725 8081 7273 -871 748 31 O ATOM 2037 CB VAL A 266 -44.637 28.284 15.403 1.00 56.29 C ANISOU 2037 CB VAL A 266 7548 7321 6519 -901 553 0 C ATOM 2038 CG1 VAL A 266 -44.753 29.167 14.149 1.00 54.60 C ANISOU 2038 CG1 VAL A 266 7199 7194 6354 -846 426 0 C ATOM 2039 CG2 VAL A 266 -44.820 26.800 15.038 1.00 56.67 C ANISOU 2039 CG2 VAL A 266 7768 7263 6503 -1042 627 -15 C ATOM 2040 N ARG A 267 -42.356 26.997 17.810 1.00 58.96 N ANISOU 2040 N ARG A 267 8426 7390 6586 -788 611 85 N ATOM 2041 CA ARG A 267 -42.150 26.281 19.073 1.00 60.50 C ANISOU 2041 CA ARG A 267 8840 7486 6661 -808 708 113 C ATOM 2042 C ARG A 267 -40.838 26.697 19.760 1.00 63.23 C ANISOU 2042 C ARG A 267 9293 7828 6906 -652 633 143 C ATOM 2043 O ARG A 267 -40.379 25.967 20.633 1.00 66.27 O ANISOU 2043 O ARG A 267 9898 8131 7153 -611 659 184 O ATOM 2044 CB ARG A 267 -42.224 24.751 18.849 1.00 0.00 C ATOM 2045 CG ARG A 267 -43.587 24.232 18.360 1.00 0.00 C ATOM 2046 CD ARG A 267 -44.683 24.295 19.435 1.00 0.00 C ATOM 2047 NE ARG A 267 -45.997 23.904 18.912 1.00 0.00 N ATOM 2048 CZ ARG A 267 -46.878 24.717 18.306 1.00 0.00 C ATOM 2049 NH1 ARG A 267 -46.628 26.023 18.138 1.00 0.00 N1+ ATOM 2050 NH2 ARG A 267 -48.034 24.207 17.862 1.00 0.00 N1+ ATOM 2051 N ILE A 268 -40.278 27.868 19.437 1.00 61.57 N ANISOU 2051 N ILE A 268 8930 7710 6753 -566 539 120 N ATOM 2052 CA ILE A 268 -39.089 28.404 20.111 1.00 59.36 C ANISOU 2052 CA ILE A 268 8716 7455 6383 -443 457 124 C ATOM 2053 C ILE A 268 -39.299 28.669 21.618 1.00 60.63 C ANISOU 2053 C ILE A 268 8996 7600 6441 -448 546 117 C ATOM 2054 O ILE A 268 -38.370 28.494 22.402 1.00 62.15 O ANISOU 2054 O ILE A 268 9360 7771 6483 -369 514 144 O ATOM 2055 CB ILE A 268 -38.589 29.707 19.436 1.00 0.00 C ATOM 2056 CG1 ILE A 268 -39.682 30.800 19.320 1.00 0.00 C ATOM 2057 CG2 ILE A 268 -37.959 29.378 18.070 1.00 0.00 C ATOM 2058 CD1 ILE A 268 -39.217 32.051 18.572 1.00 0.00 C ATOM 2059 N ARG A 269 -40.537 29.003 22.014 1.00 62.36 N ANISOU 2059 N ARG A 269 9125 7841 6729 -524 655 80 N ATOM 2060 CA ARG A 269 -40.934 29.184 23.412 1.00 65.71 C ANISOU 2060 CA ARG A 269 9660 8260 7049 -530 755 63 C ATOM 2061 C ARG A 269 -40.950 27.857 24.190 1.00 66.55 C ANISOU 2061 C ARG A 269 9984 8280 7021 -580 858 120 C ATOM 2062 O ARG A 269 -40.647 27.856 25.380 1.00 64.91 O ANISOU 2062 O ARG A 269 9947 8061 6658 -539 895 134 O ATOM 2063 CB ARG A 269 -42.325 29.852 23.475 1.00 0.00 C ATOM 2064 CG ARG A 269 -42.443 31.148 22.653 1.00 0.00 C ATOM 2065 CD ARG A 269 -43.806 31.835 22.821 1.00 0.00 C ATOM 2066 NE ARG A 269 -43.974 32.937 21.861 1.00 0.00 N ATOM 2067 CZ ARG A 269 -43.382 34.144 21.910 1.00 0.00 C ATOM 2068 NH1 ARG A 269 -42.585 34.496 22.929 1.00 0.00 N1+ ATOM 2069 NH2 ARG A 269 -43.598 35.017 20.918 1.00 0.00 N1+ ATOM 2070 N GLU A 270 -41.294 26.759 23.498 1.00 69.43 N ANISOU 2070 N GLU A 270 10365 8581 7436 -675 908 152 N ATOM 2071 CA GLU A 270 -41.379 25.407 24.049 1.00 69.93 C ANISOU 2071 CA GLU A 270 10672 8525 7373 -734 1013 215 C ATOM 2072 C GLU A 270 -40.010 24.705 24.056 1.00 70.09 C ANISOU 2072 C GLU A 270 10914 8481 7236 -582 905 280 C ATOM 2073 O GLU A 270 -39.766 23.878 24.930 1.00 70.37 O ANISOU 2073 O GLU A 270 11196 8434 7106 -560 979 343 O ATOM 2074 CB GLU A 270 -42.401 24.585 23.231 1.00 72.51 C ANISOU 2074 CB GLU A 270 10960 8789 7799 -891 1085 215 C ATOM 2075 CG GLU A 270 -43.764 25.260 22.967 1.00 76.64 C ANISOU 2075 CG GLU A 270 11243 9409 8469 -1035 1189 149 C ATOM 2076 CD GLU A 270 -44.503 25.652 24.246 1.00 84.79 C ANISOU 2076 CD GLU A 270 12339 10441 9436 -1137 1385 148 C ATOM 2077 OE1 GLU A 270 -45.212 24.772 24.781 1.00 89.10 O ANISOU 2077 OE1 GLU A 270 13060 10882 9911 -1269 1519 187 O ATOM 2078 OE2 GLU A 270 -44.340 26.818 24.667 1.00 86.80 O1- ANISOU 2078 OE2 GLU A 270 12483 10793 9704 -1087 1417 107 O1- ATOM 2079 N LEU A 271 -39.147 25.064 23.096 1.00 71.56 N ANISOU 2079 N LEU A 271 11013 8714 7462 -466 736 269 N ATOM 2080 CA LEU A 271 -37.764 24.598 22.989 1.00 72.90 C ANISOU 2080 CA LEU A 271 11351 8862 7485 -293 620 320 C ATOM 2081 C LEU A 271 -36.823 25.338 23.962 1.00 72.77 C ANISOU 2081 C LEU A 271 11348 8955 7346 -173 545 301 C ATOM 2082 O LEU A 271 -35.767 24.806 24.294 1.00 75.64 O ANISOU 2082 O LEU A 271 11898 9309 7531 -32 489 354 O ATOM 2083 CB LEU A 271 -37.298 24.757 21.524 1.00 0.00 C ATOM 2084 CG LEU A 271 -37.978 23.769 20.545 1.00 0.00 C ATOM 2085 CD1 LEU A 271 -37.818 24.219 19.076 1.00 0.00 C ATOM 2086 CD2 LEU A 271 -37.498 22.322 20.775 1.00 0.00 C ATOM 2087 N LEU A 272 -37.224 26.533 24.423 1.00 69.95 N ANISOU 2087 N LEU A 272 10802 8702 7073 -219 541 223 N ATOM 2088 CA LEU A 272 -36.642 27.233 25.572 1.00 68.71 C ANISOU 2088 CA LEU A 272 10644 8654 6808 -129 461 176 C ATOM 2089 C LEU A 272 -36.997 26.536 26.905 1.00 69.51 C ANISOU 2089 C LEU A 272 10934 8735 6742 -139 575 192 C ATOM 2090 O LEU A 272 -36.205 26.601 27.845 1.00 70.98 O ANISOU 2090 O LEU A 272 11252 8979 6737 -20 501 202 O ATOM 2091 CB LEU A 272 -37.111 28.708 25.519 1.00 67.46 C ANISOU 2091 CB LEU A 272 10249 8582 6803 -181 427 80 C ATOM 2092 CG LEU A 272 -36.552 29.659 26.602 1.00 69.57 C ANISOU 2092 CG LEU A 272 10500 8950 6983 -138 367 -2 C ATOM 2093 CD1 LEU A 272 -35.012 29.730 26.582 1.00 69.11 C ANISOU 2093 CD1 LEU A 272 10471 8992 6797 -6 194 -2 C ATOM 2094 CD2 LEU A 272 -37.192 31.058 26.477 1.00 68.58 C ANISOU 2094 CD2 LEU A 272 10177 8853 7029 -209 372 -90 C ATOM 2095 N GLN A 273 -38.150 25.842 26.933 1.00 31.02 N ATOM 2096 CA GLN A 273 -38.600 24.951 28.003 1.00 32.28 C ATOM 2097 C GLN A 273 -38.154 23.496 27.716 1.00 31.44 C ATOM 2098 O GLN A 273 -37.197 23.286 26.967 1.00 32.07 O ATOM 2099 CB GLN A 273 -40.132 25.110 28.167 1.00 0.00 C ATOM 2100 CG GLN A 273 -40.561 26.535 28.570 1.00 0.00 C ATOM 2101 CD GLN A 273 -42.082 26.674 28.603 1.00 0.00 C ATOM 2102 NE2 GLN A 273 -42.671 27.176 27.516 1.00 0.00 N ATOM 2103 OE1 GLN A 273 -42.718 26.321 29.592 1.00 0.00 O ATOM 2104 N GLY A 274 -38.822 22.512 28.341 1.00 31.02 N ATOM 2105 CA GLY A 274 -38.453 21.095 28.277 1.00 30.54 C ATOM 2106 C GLY A 274 -39.172 20.310 27.163 1.00 30.29 C ATOM 2107 O GLY A 274 -38.930 19.109 27.050 1.00 30.82 O ATOM 2108 N MET A 275 -40.050 20.948 26.368 1.00 27.98 N ATOM 2109 CA MET A 275 -40.946 20.280 25.415 1.00 27.56 C ATOM 2110 C MET A 275 -40.455 20.371 23.956 1.00 27.51 C ATOM 2111 O MET A 275 -39.566 21.165 23.644 1.00 28.08 O ATOM 2112 CB MET A 275 -42.363 20.882 25.549 1.00 0.00 C ATOM 2113 CG MET A 275 -42.974 20.793 26.960 1.00 0.00 C ATOM 2114 SD MET A 275 -42.611 22.169 28.089 1.00 0.00 S ATOM 2115 CE MET A 275 -43.582 23.482 27.304 1.00 0.00 C ATOM 2116 N TYR A 276 -41.073 19.543 23.091 1.00 68.88 N ANISOU 2116 N TYR A 276 11606 7615 6949 -751 1082 477 N ATOM 2117 CA TYR A 276 -40.891 19.475 21.630 1.00 70.55 C ANISOU 2117 CA TYR A 276 11691 7834 7279 -755 981 415 C ATOM 2118 C TYR A 276 -39.454 19.133 21.175 1.00 70.60 C ANISOU 2118 C TYR A 276 11794 7827 7202 -489 820 452 C ATOM 2119 O TYR A 276 -39.046 19.527 20.084 1.00 70.80 O ANISOU 2119 O TYR A 276 11610 7987 7306 -400 677 401 O ATOM 2120 CB TYR A 276 -41.472 20.739 20.941 1.00 69.78 C ANISOU 2120 CB TYR A 276 11215 7944 7354 -834 918 322 C ATOM 2121 CG TYR A 276 -42.987 20.830 20.949 1.00 69.52 C ANISOU 2121 CG TYR A 276 11042 7960 7413 -1072 1067 275 C ATOM 2122 CD1 TYR A 276 -43.730 20.386 19.834 1.00 69.38 C ANISOU 2122 CD1 TYR A 276 11024 7870 7469 -1296 1169 226 C ATOM 2123 CD2 TYR A 276 -43.662 21.376 22.060 1.00 68.24 C ANISOU 2123 CD2 TYR A 276 10739 7928 7262 -1072 1107 265 C ATOM 2124 CE1 TYR A 276 -45.134 20.497 19.830 1.00 68.80 C ANISOU 2124 CE1 TYR A 276 10785 7878 7478 -1512 1304 172 C ATOM 2125 CE2 TYR A 276 -45.065 21.485 22.059 1.00 67.54 C ANISOU 2125 CE2 TYR A 276 10502 7905 7255 -1265 1250 217 C ATOM 2126 CZ TYR A 276 -45.801 21.052 20.939 1.00 67.74 C ANISOU 2126 CZ TYR A 276 10502 7882 7354 -1484 1346 172 C ATOM 2127 OH TYR A 276 -47.160 21.184 20.919 1.00 68.00 O ANISOU 2127 OH TYR A 276 10353 8016 7467 -1676 1485 116 O ATOM 2128 N LYS A 277 -38.717 18.369 22.000 1.00 69.15 N ANISOU 2128 N LYS A 277 11937 7488 6851 -353 849 545 N ATOM 2129 CA LYS A 277 -37.332 17.951 21.746 1.00 70.28 C ANISOU 2129 CA LYS A 277 12184 7615 6903 -82 707 580 C ATOM 2130 C LYS A 277 -37.177 16.944 20.586 1.00 74.28 C ANISOU 2130 C LYS A 277 12731 8007 7486 -102 691 534 C ATOM 2131 O LYS A 277 -36.067 16.800 20.078 1.00 76.76 O ANISOU 2131 O LYS A 277 13054 8351 7760 120 565 535 O ATOM 2132 CB LYS A 277 -36.715 17.417 23.056 1.00 71.37 C ANISOU 2132 CB LYS A 277 12677 7613 6826 97 744 703 C ATOM 2133 CG LYS A 277 -36.763 18.410 24.238 1.00 73.26 C ANISOU 2133 CG LYS A 277 12892 7992 6949 168 728 744 C ATOM 2134 CD LYS A 277 -35.983 19.718 24.009 1.00 76.36 C ANISOU 2134 CD LYS A 277 13637 8275 7103 395 731 871 C ATOM 2135 CE LYS A 277 -36.162 20.707 25.165 1.00 78.71 C ANISOU 2135 CE LYS A 277 13930 8712 7263 441 726 903 C ATOM 2136 NZ LYS A 277 -35.333 21.908 24.987 1.00 81.72 N1+ ANISOU 2136 NZ LYS A 277 14314 9043 7692 162 923 893 N1+ ATOM 2137 N GLU A 278 -38.293 16.338 20.143 1.00 73.85 N ANISOU 2137 N GLU A 278 12690 7837 7533 -365 817 480 N ATOM 2138 CA GLU A 278 -38.439 15.554 18.911 1.00 68.51 C ANISOU 2138 CA GLU A 278 12036 7067 6929 -415 800 409 C ATOM 2139 C GLU A 278 -38.013 16.322 17.643 1.00 67.54 C ANISOU 2139 C GLU A 278 11576 7173 6912 -349 640 328 C ATOM 2140 O GLU A 278 -37.388 15.733 16.763 1.00 67.43 O ANISOU 2140 O GLU A 278 11583 7125 6913 -276 578 282 O ATOM 2141 CB GLU A 278 -39.911 15.085 18.830 1.00 0.00 C ATOM 2142 CG GLU A 278 -40.313 14.327 17.545 1.00 0.00 C ATOM 2143 CD GLU A 278 -41.786 13.913 17.554 1.00 0.00 C ATOM 2144 OE1 GLU A 278 -42.630 14.795 17.831 1.00 0.00 O ATOM 2145 OE2 GLU A 278 -42.045 12.724 17.269 1.00 0.00 O1- ATOM 2146 N ILE A 279 -38.363 17.616 17.611 1.00 65.60 N ANISOU 2146 N ILE A 279 11037 7154 6735 -370 581 312 N ATOM 2147 CA ILE A 279 -38.118 18.524 16.498 1.00 65.53 C ANISOU 2147 CA ILE A 279 10731 7351 6816 -304 442 254 C ATOM 2148 C ILE A 279 -36.611 18.827 16.369 1.00 71.60 C ANISOU 2148 C ILE A 279 11531 8178 7495 -23 312 287 C ATOM 2149 O ILE A 279 -36.111 18.922 15.252 1.00 77.98 O ANISOU 2149 O ILE A 279 12244 9049 8334 56 227 243 O ATOM 2150 CB ILE A 279 -38.910 19.858 16.688 1.00 63.36 C ANISOU 2150 CB ILE A 279 10174 7268 6632 -389 429 235 C ATOM 2151 CG1 ILE A 279 -40.411 19.626 16.997 1.00 61.66 C ANISOU 2151 CG1 ILE A 279 9891 7031 6508 -652 557 193 C ATOM 2152 CG2 ILE A 279 -38.765 20.851 15.515 1.00 62.44 C ANISOU 2152 CG2 ILE A 279 9785 7342 6598 -318 297 193 C ATOM 2153 CD1 ILE A 279 -41.169 18.785 15.958 1.00 60.01 C ANISOU 2153 CD1 ILE A 279 9610 6806 6384 -794 558 112 C ATOM 2154 N GLY A 280 -35.903 18.888 17.509 1.00 73.07 N ANISOU 2154 N GLY A 280 11847 8360 7557 136 295 360 N ATOM 2155 CA GLY A 280 -34.456 19.100 17.562 1.00 75.70 C ANISOU 2155 CA GLY A 280 12191 8779 7793 414 167 387 C ATOM 2156 C GLY A 280 -33.699 17.855 17.078 1.00 72.31 C ANISOU 2156 C GLY A 280 12000 8179 7295 552 173 399 C ATOM 2157 O GLY A 280 -32.695 17.982 16.382 1.00 72.43 O ANISOU 2157 O GLY A 280 11938 8291 7292 740 71 375 O ATOM 2158 N ILE A 281 -34.216 16.654 17.383 1.00 70.36 N ANISOU 2158 N ILE A 281 12050 7673 7011 458 306 429 N ATOM 2159 CA ILE A 281 -33.719 15.382 16.851 1.00 70.60 C ANISOU 2159 CA ILE A 281 12359 7493 6972 589 332 437 C ATOM 2160 C ILE A 281 -33.942 15.244 15.330 1.00 67.74 C ANISOU 2160 C ILE A 281 11855 7166 6717 525 296 329 C ATOM 2161 O ILE A 281 -33.105 14.648 14.652 1.00 68.54 O ANISOU 2161 O ILE A 281 12036 7237 6769 730 241 311 O ATOM 2162 CB ILE A 281 -34.345 14.181 17.644 1.00 74.40 C ANISOU 2162 CB ILE A 281 13208 7663 7398 454 506 491 C ATOM 2163 CG1 ILE A 281 -33.419 13.745 18.798 1.00 76.90 C ANISOU 2163 CG1 ILE A 281 13822 7873 7525 702 515 624 C ATOM 2164 CG2 ILE A 281 -34.742 12.923 16.835 1.00 78.44 C ANISOU 2164 CG2 ILE A 281 13915 7942 7945 370 581 426 C ATOM 2165 CD1 ILE A 281 -33.017 14.855 19.782 1.00 78.06 C ANISOU 2165 CD1 ILE A 281 13817 8231 7611 758 455 678 C ATOM 2166 N ALA A 282 -35.054 15.795 14.821 1.00 64.41 N ANISOU 2166 N ALA A 282 11213 6826 6433 257 323 254 N ATOM 2167 CA ALA A 282 -35.455 15.710 13.417 1.00 60.69 C ANISOU 2167 CA ALA A 282 10613 6399 6049 174 291 149 C ATOM 2168 C ALA A 282 -34.604 16.558 12.452 1.00 60.79 C ANISOU 2168 C ALA A 282 10313 6684 6100 302 152 121 C ATOM 2169 O ALA A 282 -34.663 16.315 11.243 1.00 63.05 O ANISOU 2169 O ALA A 282 10495 7028 6434 267 117 42 O ATOM 2170 CB ALA A 282 -36.939 16.094 13.298 1.00 0.00 C ATOM 2171 N VAL A 283 -33.847 17.537 12.972 1.00 57.69 N ANISOU 2171 N VAL A 283 9776 6463 5681 435 76 178 N ATOM 2172 CA VAL A 283 -33.046 18.461 12.169 1.00 54.84 C ANISOU 2172 CA VAL A 283 9121 6354 5360 524 -37 152 C ATOM 2173 C VAL A 283 -31.991 17.730 11.316 1.00 56.19 C ANISOU 2173 C VAL A 283 9334 6541 5474 727 -90 119 C ATOM 2174 O VAL A 283 -32.032 17.844 10.095 1.00 56.98 O ANISOU 2174 O VAL A 283 9282 6740 5627 690 -121 57 O ATOM 2175 CB VAL A 283 -32.346 19.557 13.030 1.00 53.22 C ANISOU 2175 CB VAL A 283 8789 6309 5123 623 -102 206 C ATOM 2176 CG1 VAL A 283 -31.398 20.492 12.241 1.00 52.55 C ANISOU 2176 CG1 VAL A 283 8446 6463 5059 736 -208 178 C ATOM 2177 CG2 VAL A 283 -33.377 20.411 13.785 1.00 50.90 C ANISOU 2177 CG2 VAL A 283 8395 6039 4906 418 -51 215 C ATOM 2178 N ASP A 284 -31.076 16.988 11.951 1.00 57.60 N ANISOU 2178 N ASP A 284 9726 6628 5532 962 -99 163 N ATOM 2179 CA ASP A 284 -29.871 16.440 11.310 1.00 56.97 C ANISOU 2179 CA ASP A 284 9680 6579 5387 1200 -146 131 C ATOM 2180 C ASP A 284 -30.171 15.476 10.149 1.00 61.11 C ANISOU 2180 C ASP A 284 10341 6943 5935 1119 -85 49 C ATOM 2181 O ASP A 284 -29.549 15.576 9.092 1.00 59.95 O ANISOU 2181 O ASP A 284 10049 6928 5800 1181 -129 -15 O ATOM 2182 CB ASP A 284 -28.886 15.789 12.310 1.00 0.00 C ATOM 2183 CG ASP A 284 -28.508 16.664 13.508 1.00 0.00 C ATOM 2184 OD1 ASP A 284 -28.582 17.906 13.384 1.00 0.00 O ATOM 2185 OD2 ASP A 284 -28.050 16.080 14.512 1.00 0.00 O1- ATOM 2186 N VAL A 285 -31.150 14.587 10.352 1.00 63.50 N ANISOU 2186 N VAL A 285 10918 6972 6239 972 21 39 N ATOM 2187 CA VAL A 285 -31.571 13.590 9.366 1.00 63.30 C ANISOU 2187 CA VAL A 285 11012 6807 6234 874 71 -66 C ATOM 2188 C VAL A 285 -32.274 14.205 8.136 1.00 64.89 C ANISOU 2188 C VAL A 285 10921 7200 6534 674 32 -150 C ATOM 2189 O VAL A 285 -32.030 13.742 7.022 1.00 70.14 O ANISOU 2189 O VAL A 285 11548 7921 7184 731 5 -232 O ATOM 2190 CB VAL A 285 -32.452 12.488 10.022 1.00 0.00 C ATOM 2191 CG1 VAL A 285 -33.812 12.988 10.550 1.00 0.00 C ATOM 2192 CG2 VAL A 285 -32.653 11.261 9.114 1.00 0.00 C ATOM 2193 N THR A 286 -33.062 15.273 8.338 1.00 62.88 N ANISOU 2193 N THR A 286 10464 7056 6371 460 29 -129 N ATOM 2194 CA THR A 286 -33.704 16.001 7.244 1.00 60.63 C ANISOU 2194 CA THR A 286 9908 6959 6170 298 -13 -192 C ATOM 2195 C THR A 286 -32.733 17.005 6.583 1.00 61.07 C ANISOU 2195 C THR A 286 9711 7272 6219 460 -109 -173 C ATOM 2196 O THR A 286 -32.790 17.173 5.366 1.00 61.98 O ANISOU 2196 O THR A 286 9672 7520 6355 410 -144 -229 O ATOM 2197 CB THR A 286 -34.979 16.745 7.720 1.00 57.95 C ANISOU 2197 CB THR A 286 9423 6670 5927 59 14 -170 C ATOM 2198 CG2 THR A 286 -36.083 15.794 8.202 1.00 57.04 C ANISOU 2198 CG2 THR A 286 9541 6315 5815 -127 129 -188 C ATOM 2199 OG1 THR A 286 -34.720 17.666 8.766 1.00 58.98 O ANISOU 2199 OG1 THR A 286 9431 6910 6067 143 -17 -77 O ATOM 2200 N SER A 287 -31.801 17.589 7.351 1.00 61.51 N ANISOU 2200 N SER A 287 9720 7411 6239 644 -149 -97 N ATOM 2201 CA SER A 287 -30.737 18.462 6.845 1.00 59.79 C ANISOU 2201 CA SER A 287 9265 7438 6014 781 -226 -87 C ATOM 2202 C SER A 287 -29.808 17.721 5.870 1.00 61.59 C ANISOU 2202 C SER A 287 9552 7683 6167 953 -235 -151 C ATOM 2203 O SER A 287 -29.450 18.280 4.837 1.00 60.86 O ANISOU 2203 O SER A 287 9273 7768 6083 953 -265 -184 O ATOM 2204 CB SER A 287 -29.922 19.041 8.013 1.00 59.09 C ANISOU 2204 CB SER A 287 9117 7443 5892 929 -270 -15 C ATOM 2205 OG SER A 287 -30.746 19.852 8.827 1.00 60.99 O ANISOU 2205 OG SER A 287 9260 7711 6203 771 -263 30 O ATOM 2206 N ALA A 288 -29.500 16.447 6.165 1.00 62.59 N ANISOU 2206 N ALA A 288 9951 7621 6210 1111 -200 -165 N ATOM 2207 CA ALA A 288 -28.727 15.576 5.279 1.00 62.27 C ANISOU 2207 CA ALA A 288 9991 7579 6090 1301 -198 -234 C ATOM 2208 C ALA A 288 -29.403 15.354 3.913 1.00 62.18 C ANISOU 2208 C ALA A 288 9981 7543 6100 1132 -172 -336 C ATOM 2209 O ALA A 288 -28.713 15.377 2.894 1.00 61.62 O ANISOU 2209 O ALA A 288 9836 7595 5982 1237 -186 -397 O ATOM 2210 CB ALA A 288 -28.459 14.248 6.004 1.00 0.00 C ATOM 2211 N LEU A 289 -30.739 15.203 3.915 1.00 62.53 N ANISOU 2211 N LEU A 289 10097 7455 6208 868 -134 -363 N ATOM 2212 CA LEU A 289 -31.580 15.107 2.720 1.00 62.90 C ANISOU 2212 CA LEU A 289 10110 7520 6269 688 -129 -468 C ATOM 2213 C LEU A 289 -31.685 16.442 1.949 1.00 64.47 C ANISOU 2213 C LEU A 289 9982 8012 6502 641 -194 -452 C ATOM 2214 O LEU A 289 -31.762 16.418 0.722 1.00 69.51 O ANISOU 2214 O LEU A 289 10567 8754 7092 655 -211 -526 O ATOM 2215 CB LEU A 289 -32.953 14.533 3.145 1.00 60.35 C ANISOU 2215 CB LEU A 289 9894 7028 6010 405 -77 -502 C ATOM 2216 CG LEU A 289 -34.037 14.412 2.048 1.00 61.50 C ANISOU 2216 CG LEU A 289 9971 7224 6170 185 -87 -622 C ATOM 2217 CD1 LEU A 289 -33.576 13.590 0.823 1.00 64.27 C ANISOU 2217 CD1 LEU A 289 10518 7474 6426 269 -67 -749 C ATOM 2218 CD2 LEU A 289 -35.358 13.884 2.642 1.00 61.61 C ANISOU 2218 CD2 LEU A 289 10042 7111 6256 -101 -35 -651 C ATOM 2219 N ALA A 290 -31.660 17.578 2.664 1.00 60.32 N ANISOU 2219 N ALA A 290 9256 7614 6050 586 -225 -355 N ATOM 2220 CA ALA A 290 -31.612 18.916 2.068 1.00 60.47 C ANISOU 2220 CA ALA A 290 8994 7881 6100 552 -274 -322 C ATOM 2221 C ALA A 290 -30.273 19.159 1.356 1.00 63.23 C ANISOU 2221 C ALA A 290 9248 8394 6384 766 -294 -309 C ATOM 2222 O ALA A 290 -30.268 19.500 0.174 1.00 65.34 O ANISOU 2222 O ALA A 290 9364 8835 6628 762 -311 -320 O ATOM 2223 CB ALA A 290 -31.903 19.993 3.124 1.00 61.00 C ANISOU 2223 CB ALA A 290 8905 8008 6265 445 -289 -230 C ATOM 2224 N PHE A 291 -29.164 18.884 2.061 1.00 64.15 N ANISOU 2224 N PHE A 291 9444 8472 6461 960 -289 -283 N ATOM 2225 CA PHE A 291 -27.795 18.945 1.540 1.00 62.83 C ANISOU 2225 CA PHE A 291 9168 8479 6224 1175 -303 -287 C ATOM 2226 C PHE A 291 -27.578 18.094 0.270 1.00 65.43 C ANISOU 2226 C PHE A 291 9604 8794 6463 1269 -274 -386 C ATOM 2227 O PHE A 291 -26.832 18.502 -0.620 1.00 67.16 O ANISOU 2227 O PHE A 291 9673 9211 6632 1359 -273 -403 O ATOM 2228 CB PHE A 291 -26.796 18.494 2.631 1.00 62.98 C ANISOU 2228 CB PHE A 291 9251 8472 6206 1385 -316 -247 C ATOM 2229 CG PHE A 291 -26.640 19.334 3.895 1.00 63.45 C ANISOU 2229 CG PHE A 291 9181 8597 6330 1318 -351 -163 C ATOM 2230 CD1 PHE A 291 -26.776 20.742 3.891 1.00 62.03 C ANISOU 2230 CD1 PHE A 291 8847 8475 6247 1093 -357 -124 C ATOM 2231 CD2 PHE A 291 -26.103 18.720 5.047 1.00 62.76 C ANISOU 2231 CD2 PHE A 291 9130 8519 6196 1497 -382 -126 C ATOM 2232 CE1 PHE A 291 -26.414 21.481 5.010 1.00 59.72 C ANISOU 2232 CE1 PHE A 291 8454 8228 6008 1034 -382 -62 C ATOM 2233 CE2 PHE A 291 -25.756 19.474 6.160 1.00 62.36 C ANISOU 2233 CE2 PHE A 291 8968 8536 6189 1431 -417 -66 C ATOM 2234 CZ PHE A 291 -25.908 20.853 6.139 1.00 60.47 C ANISOU 2234 CZ PHE A 291 8589 8336 6053 1193 -412 -40 C ATOM 2235 N PHE A 292 -28.253 16.937 0.202 1.00 64.81 N ANISOU 2235 N PHE A 292 9789 8477 6358 1233 -241 -460 N ATOM 2236 CA PHE A 292 -28.211 15.973 -0.897 1.00 65.21 C ANISOU 2236 CA PHE A 292 9983 8478 6317 1314 -208 -578 C ATOM 2237 C PHE A 292 -28.717 16.520 -2.251 1.00 66.40 C ANISOU 2237 C PHE A 292 9973 8807 6450 1178 -225 -624 C ATOM 2238 O PHE A 292 -28.380 15.943 -3.281 1.00 70.86 O ANISOU 2238 O PHE A 292 10577 9428 6918 1281 -203 -713 O ATOM 2239 CB PHE A 292 -28.887 14.666 -0.417 1.00 67.12 C ANISOU 2239 CB PHE A 292 10554 8399 6549 1243 -161 -652 C ATOM 2240 CG PHE A 292 -29.044 13.534 -1.416 1.00 69.33 C ANISOU 2240 CG PHE A 292 11025 8585 6734 1305 -121 -796 C ATOM 2241 CD1 PHE A 292 -27.933 12.735 -1.761 1.00 70.29 C ANISOU 2241 CD1 PHE A 292 11251 8695 6760 1605 -90 -834 C ATOM 2242 CD2 PHE A 292 -30.264 13.345 -2.098 1.00 68.71 C ANISOU 2242 CD2 PHE A 292 11019 8433 6655 1067 -114 -905 C ATOM 2243 CE1 PHE A 292 -28.059 11.752 -2.733 1.00 72.30 C ANISOU 2243 CE1 PHE A 292 11699 8849 6922 1670 -44 -978 C ATOM 2244 CE2 PHE A 292 -30.372 12.350 -3.061 1.00 70.76 C ANISOU 2244 CE2 PHE A 292 11467 8601 6819 1109 -78 -1057 C ATOM 2245 CZ PHE A 292 -29.274 11.558 -3.377 1.00 72.69 C ANISOU 2245 CZ PHE A 292 11836 8814 6969 1412 -37 -1093 C ATOM 2246 N ASN A 293 -29.437 17.659 -2.241 1.00 63.79 N ANISOU 2246 N ASN A 293 9469 8570 6199 968 -261 -564 N ATOM 2247 CA ASN A 293 -29.802 18.429 -3.434 1.00 61.88 C ANISOU 2247 CA ASN A 293 9075 8510 5927 860 -285 -585 C ATOM 2248 C ASN A 293 -28.579 18.911 -4.237 1.00 60.26 C ANISOU 2248 C ASN A 293 8689 8548 5661 1007 -276 -545 C ATOM 2249 O ASN A 293 -28.605 18.806 -5.460 1.00 60.03 O ANISOU 2249 O ASN A 293 8600 8658 5552 987 -275 -584 O ATOM 2250 CB ASN A 293 -30.680 19.641 -3.036 1.00 62.44 C ANISOU 2250 CB ASN A 293 9000 8628 6098 645 -325 -510 C ATOM 2251 CG ASN A 293 -31.481 20.234 -4.200 1.00 63.84 C ANISOU 2251 CG ASN A 293 9031 8994 6233 555 -359 -514 C ATOM 2252 ND2 ASN A 293 -32.385 19.451 -4.791 1.00 65.60 N ANISOU 2252 ND2 ASN A 293 9354 9184 6387 467 -375 -633 N ATOM 2253 OD1 ASN A 293 -31.291 21.396 -4.553 1.00 63.23 O ANISOU 2253 OD1 ASN A 293 8763 9088 6173 562 -370 -413 O ATOM 2254 N SER A 294 -27.532 19.397 -3.546 1.00 62.27 N ANISOU 2254 N SER A 294 8850 8869 5940 1148 -266 -473 N ATOM 2255 CA SER A 294 -26.313 19.937 -4.155 1.00 63.55 C ANISOU 2255 CA SER A 294 8815 9278 6053 1260 -242 -439 C ATOM 2256 C SER A 294 -25.535 18.927 -5.019 1.00 62.72 C ANISOU 2256 C SER A 294 8791 9223 5815 1450 -197 -542 C ATOM 2257 O SER A 294 -25.022 19.317 -6.067 1.00 63.14 O ANISOU 2257 O SER A 294 8686 9499 5806 1513 -161 -532 O ATOM 2258 CB SER A 294 -25.411 20.559 -3.069 1.00 63.88 C ANISOU 2258 CB SER A 294 8723 9398 6153 1349 -249 -360 C ATOM 2259 OG SER A 294 -25.889 21.837 -2.702 1.00 65.38 O ANISOU 2259 OG SER A 294 8798 9590 6454 1173 -279 -266 O ATOM 2260 N CYS A 295 -25.498 17.651 -4.598 1.00 64.58 N ANISOU 2260 N CYS A 295 9281 9252 6006 1542 -184 -644 N ATOM 2261 CA CYS A 295 -24.858 16.563 -5.344 1.00 67.60 C ANISOU 2261 CA CYS A 295 9773 9654 6258 1732 -133 -760 C ATOM 2262 C CYS A 295 -25.746 15.969 -6.461 1.00 66.76 C ANISOU 2262 C CYS A 295 9827 9460 6080 1607 -130 -879 C ATOM 2263 O CYS A 295 -25.204 15.258 -7.306 1.00 69.40 O ANISOU 2263 O CYS A 295 10244 9834 6292 1740 -84 -988 O ATOM 2264 CB CYS A 295 -24.268 15.494 -4.401 1.00 71.73 C ANISOU 2264 CB CYS A 295 10495 10001 6759 1975 -110 -800 C ATOM 2265 SG CYS A 295 -25.503 14.374 -3.687 1.00 74.62 S ANISOU 2265 SG CYS A 295 11237 9959 7155 1881 -107 -866 S ATOM 2266 N LEU A 296 -27.058 16.280 -6.477 1.00 65.67 N ANISOU 2266 N LEU A 296 9722 9221 6007 1359 -177 -872 N ATOM 2267 CA LEU A 296 -27.985 15.909 -7.556 1.00 67.31 C ANISOU 2267 CA LEU A 296 10033 9400 6141 1212 -192 -993 C ATOM 2268 C LEU A 296 -27.970 16.911 -8.723 1.00 71.04 C ANISOU 2268 C LEU A 296 10291 10148 6551 1133 -218 -951 C ATOM 2269 O LEU A 296 -28.316 16.517 -9.836 1.00 73.87 O ANISOU 2269 O LEU A 296 10713 10567 6790 1097 -224 -1061 O ATOM 2270 CB LEU A 296 -29.429 15.804 -7.016 1.00 64.88 C ANISOU 2270 CB LEU A 296 9835 8893 5925 975 -231 -1017 C ATOM 2271 CG LEU A 296 -29.702 14.616 -6.073 1.00 65.64 C ANISOU 2271 CG LEU A 296 10223 8665 6051 991 -190 -1090 C ATOM 2272 CD1 LEU A 296 -31.061 14.808 -5.364 1.00 64.68 C ANISOU 2272 CD1 LEU A 296 10160 8403 6012 705 -217 -1120 C ATOM 2273 CD2 LEU A 296 -29.594 13.259 -6.800 1.00 69.06 C ANISOU 2273 CD2 LEU A 296 10899 8981 6358 1131 -135 -1253 C ATOM 2274 N ASN A 297 -27.594 18.177 -8.460 1.00 72.92 N ANISOU 2274 N ASN A 297 10298 10549 6862 1107 -232 -795 N ATOM 2275 CA ASN A 297 -27.654 19.290 -9.417 1.00 75.84 C ANISOU 2275 CA ASN A 297 10489 11154 7172 1033 -247 -729 C ATOM 2276 C ASN A 297 -26.818 19.161 -10.715 1.00 81.08 C ANISOU 2276 C ASN A 297 11142 11999 7667 1173 -189 -789 C ATOM 2277 O ASN A 297 -27.291 19.682 -11.727 1.00 82.64 O ANISOU 2277 O ASN A 297 11299 12341 7761 1097 -210 -796 O ATOM 2278 CB ASN A 297 -27.369 20.631 -8.701 1.00 72.47 C ANISOU 2278 CB ASN A 297 9848 10830 6857 991 -247 -553 C ATOM 2279 CG ASN A 297 -28.427 21.061 -7.675 1.00 71.95 C ANISOU 2279 CG ASN A 297 9772 10629 6936 829 -306 -492 C ATOM 2280 ND2 ASN A 297 -28.073 22.010 -6.812 1.00 71.78 N ANISOU 2280 ND2 ASN A 297 9630 10615 7029 823 -297 -374 N ATOM 2281 OD1 ASN A 297 -29.548 20.558 -7.657 1.00 72.48 O ANISOU 2281 OD1 ASN A 297 9930 10599 7009 703 -354 -559 O ATOM 2282 N PRO A 298 -25.680 18.419 -10.741 1.00 82.80 N ANISOU 2282 N PRO A 298 11381 12238 7840 1382 -116 -829 N ATOM 2283 CA PRO A 298 -25.020 18.041 -12.006 1.00 85.49 C ANISOU 2283 CA PRO A 298 11723 12753 8006 1515 -49 -907 C ATOM 2284 C PRO A 298 -25.892 17.195 -12.947 1.00 86.54 C ANISOU 2284 C PRO A 298 12058 12818 8007 1473 -71 -1075 C ATOM 2285 O PRO A 298 -25.931 17.486 -14.137 1.00 89.24 O ANISOU 2285 O PRO A 298 12363 13346 8197 1467 -54 -1103 O ATOM 2286 CB PRO A 298 -23.756 17.282 -11.564 1.00 88.59 C ANISOU 2286 CB PRO A 298 12130 13133 8395 1765 23 -945 C ATOM 2287 CG PRO A 298 -23.462 17.826 -10.181 1.00 86.85 C ANISOU 2287 CG PRO A 298 11785 12875 8340 1741 -5 -816 C ATOM 2288 CD PRO A 298 -24.849 18.042 -9.598 1.00 83.85 C ANISOU 2288 CD PRO A 298 11484 12306 8068 1521 -90 -784 C ATOM 2289 N MET A 299 -26.585 16.185 -12.396 1.00 86.51 N ANISOU 2289 N MET A 299 12275 12549 8045 1432 -103 -1191 N ATOM 2290 CA MET A 299 -27.431 15.260 -13.151 1.00 89.07 C ANISOU 2290 CA MET A 299 12799 12798 8245 1360 -124 -1376 C ATOM 2291 C MET A 299 -28.802 15.847 -13.526 1.00 88.69 C ANISOU 2291 C MET A 299 12673 12836 8189 1111 -222 -1359 C ATOM 2292 O MET A 299 -29.331 15.470 -14.569 1.00 92.11 O ANISOU 2292 O MET A 299 13148 13387 8465 1061 -248 -1466 O ATOM 2293 CB MET A 299 -27.597 13.935 -12.376 1.00 93.59 C ANISOU 2293 CB MET A 299 13652 13040 8868 1376 -109 -1510 C ATOM 2294 CG MET A 299 -26.269 13.248 -12.003 1.00 99.36 C ANISOU 2294 CG MET A 299 14543 13682 9528 1661 -12 -1601 C ATOM 2295 SD MET A 299 -25.548 13.733 -10.408 1.00102.15 S ANISOU 2295 SD MET A 299 14788 14018 10009 1886 27 -1442 S ATOM 2296 CE MET A 299 -26.564 12.728 -9.293 1.00100.32 C ANISOU 2296 CE MET A 299 14747 13432 9938 1735 -18 -1419 C ATOM 2297 N LEU A 300 -29.350 16.745 -12.687 1.00 86.77 N ANISOU 2297 N LEU A 300 12313 12552 8104 966 -280 -1229 N ATOM 2298 CA LEU A 300 -30.650 17.387 -12.895 1.00 85.50 C ANISOU 2298 CA LEU A 300 12071 12468 7947 750 -379 -1216 C ATOM 2299 C LEU A 300 -30.615 18.472 -13.983 1.00 81.85 C ANISOU 2299 C LEU A 300 11431 12301 7366 763 -401 -1115 C ATOM 2300 O LEU A 300 -31.496 18.477 -14.844 1.00 81.65 O ANISOU 2300 O LEU A 300 11404 12399 7219 668 -473 -1182 O ATOM 2301 CB LEU A 300 -31.151 18.006 -11.569 1.00 84.81 C ANISOU 2301 CB LEU A 300 11901 12265 8058 621 -419 -1100 C ATOM 2302 CG LEU A 300 -31.692 17.004 -10.530 1.00 86.80 C ANISOU 2302 CG LEU A 300 12339 12220 8421 558 -402 -1185 C ATOM 2303 CD1 LEU A 300 -31.903 17.702 -9.175 1.00 85.41 C ANISOU 2303 CD1 LEU A 300 12066 11962 8424 532 -398 -1028 C ATOM 2304 CD2 LEU A 300 -32.983 16.307 -11.003 1.00 89.03 C ANISOU 2304 CD2 LEU A 300 12715 12432 8680 338 -464 -1339 C ATOM 2305 N TYR A 301 -29.641 19.395 -13.889 1.00 80.32 N ANISOU 2305 N TYR A 301 11091 12228 7198 875 -338 -954 N ATOM 2306 CA TYR A 301 -29.652 20.653 -14.640 1.00 81.27 C ANISOU 2306 CA TYR A 301 11052 12595 7232 869 -342 -815 C ATOM 2307 C TYR A 301 -28.619 20.707 -15.774 1.00 83.00 C ANISOU 2307 C TYR A 301 11280 12999 7257 1015 -254 -847 C ATOM 2308 O TYR A 301 -28.866 21.442 -16.729 1.00 83.83 O ANISOU 2308 O TYR A 301 11376 13286 7189 996 -279 -849 O ATOM 2309 CB TYR A 301 -29.462 21.842 -13.666 1.00 79.35 C ANISOU 2309 CB TYR A 301 10639 12362 7149 852 -317 -607 C ATOM 2310 CG TYR A 301 -30.545 21.948 -12.602 1.00 78.27 C ANISOU 2310 CG TYR A 301 10461 12105 7174 703 -403 -549 C ATOM 2311 CD1 TYR A 301 -30.331 21.413 -11.317 1.00 78.10 C ANISOU 2311 CD1 TYR A 301 10507 11863 7306 668 -410 -596 C ATOM 2312 CD2 TYR A 301 -31.790 22.538 -12.904 1.00 78.48 C ANISOU 2312 CD2 TYR A 301 10386 12243 7189 613 -472 -442 C ATOM 2313 CE1 TYR A 301 -31.371 21.398 -10.370 1.00 78.90 C ANISOU 2313 CE1 TYR A 301 10566 11867 7547 532 -472 -547 C ATOM 2314 CE2 TYR A 301 -32.825 22.541 -11.948 1.00 77.76 C ANISOU 2314 CE2 TYR A 301 10244 12058 7244 496 -541 -396 C ATOM 2315 CZ TYR A 301 -32.626 21.943 -10.689 1.00 78.92 C ANISOU 2315 CZ TYR A 301 10448 11995 7543 447 -536 -453 C ATOM 2316 OH TYR A 301 -33.637 21.876 -9.776 1.00 79.76 O ANISOU 2316 OH TYR A 301 10498 12020 7788 329 -591 -412 O ATOM 2317 N VAL A 302 -27.498 19.972 -15.668 1.00 82.01 N ANISOU 2317 N VAL A 302 11166 12849 7144 1172 -151 -871 N ATOM 2318 CA VAL A 302 -26.342 20.169 -16.550 1.00 83.37 C ANISOU 2318 CA VAL A 302 11303 13225 7150 1318 -43 -880 C ATOM 2319 C VAL A 302 -26.146 18.966 -17.491 1.00 86.67 C ANISOU 2319 C VAL A 302 11916 13626 7388 1404 -30 -1101 C ATOM 2320 O VAL A 302 -26.418 19.094 -18.683 1.00 90.32 O ANISOU 2320 O VAL A 302 12408 14256 7654 1390 -36 -1147 O ATOM 2321 CB VAL A 302 -25.035 20.428 -15.745 1.00 83.07 C ANISOU 2321 CB VAL A 302 11149 13212 7201 1455 64 -812 C ATOM 2322 CG1 VAL A 302 -23.857 20.824 -16.658 1.00 82.32 C ANISOU 2322 CG1 VAL A 302 10955 13378 6945 1567 190 -782 C ATOM 2323 CG2 VAL A 302 -25.264 21.487 -14.653 1.00 81.46 C ANISOU 2323 CG2 VAL A 302 10792 12960 7198 1348 36 -634 C ATOM 2324 N PHE A 303 -25.706 17.823 -16.937 1.00 88.57 N ANISOU 2324 N PHE A 303 12308 13659 7686 1498 -8 -1240 N ATOM 2325 CA PHE A 303 -25.436 16.565 -17.640 1.00 91.18 C ANISOU 2325 CA PHE A 303 12848 13942 7857 1614 33 -1460 C ATOM 2326 C PHE A 303 -26.699 15.794 -18.070 1.00 90.22 C ANISOU 2326 C PHE A 303 12906 13701 7671 1446 -70 -1623 C ATOM 2327 O PHE A 303 -26.572 14.753 -18.714 1.00 90.71 O ANISOU 2327 O PHE A 303 13186 13654 7625 1509 -41 -1833 O ATOM 2328 CB PHE A 303 -24.486 15.696 -16.789 1.00 93.33 C ANISOU 2328 CB PHE A 303 13231 14021 8209 1810 106 -1536 C ATOM 2329 CG PHE A 303 -23.124 16.322 -16.526 1.00 95.49 C ANISOU 2329 CG PHE A 303 13317 14468 8496 2006 212 -1429 C ATOM 2330 CD1 PHE A 303 -22.318 16.751 -17.602 1.00 97.05 C ANISOU 2330 CD1 PHE A 303 13385 14957 8534 2078 300 -1401 C ATOM 2331 CD2 PHE A 303 -22.626 16.438 -15.211 1.00 95.45 C ANISOU 2331 CD2 PHE A 303 13256 14357 8655 2108 227 -1360 C ATOM 2332 CE1 PHE A 303 -21.078 17.322 -17.360 1.00 98.85 C ANISOU 2332 CE1 PHE A 303 13415 15368 8776 2232 408 -1313 C ATOM 2333 CE2 PHE A 303 -21.371 16.995 -14.991 1.00 97.65 C ANISOU 2333 CE2 PHE A 303 13331 14831 8942 2275 316 -1278 C ATOM 2334 CZ PHE A 303 -20.607 17.442 -16.061 1.00 99.47 C ANISOU 2334 CZ PHE A 303 13416 15353 9024 2327 410 -1259 C ATOM 2335 N MET A 304 -27.886 16.348 -17.768 1.00 90.97 N ANISOU 2335 N MET A 304 12916 13821 7829 1234 -184 -1543 N ATOM 2336 CA MET A 304 -29.161 16.043 -18.416 1.00 97.80 C ANISOU 2336 CA MET A 304 13890 14671 8596 1062 -290 -1698 C ATOM 2337 C MET A 304 -29.144 16.391 -19.920 1.00106.51 C ANISOU 2337 C MET A 304 14959 16063 9448 1076 -309 -1729 C ATOM 2338 O MET A 304 -29.719 15.646 -20.715 1.00106.67 O ANISOU 2338 O MET A 304 15077 16113 9338 958 -396 -1896 O ATOM 2339 CB MET A 304 -30.282 16.763 -17.625 1.00 0.00 C ATOM 2340 CG MET A 304 -31.628 16.985 -18.338 1.00 0.00 C ATOM 2341 SD MET A 304 -31.768 18.481 -19.367 1.00 0.00 S ATOM 2342 CE MET A 304 -31.860 19.759 -18.087 1.00 0.00 C ATOM 2343 N GLY A 305 -28.458 17.492 -20.277 1.00114.24 N ANISOU 2343 N GLY A 305 15801 17260 10346 1208 -225 -1577 N ATOM 2344 CA GLY A 305 -28.261 17.938 -21.652 1.00122.57 C ANISOU 2344 CA GLY A 305 16834 18595 11142 1240 -222 -1580 C ATOM 2345 C GLY A 305 -27.239 17.032 -22.344 1.00128.90 C ANISOU 2345 C GLY A 305 17756 19460 11762 1429 -90 -1726 C ATOM 2346 O GLY A 305 -26.220 16.662 -21.755 1.00132.41 O ANISOU 2346 O GLY A 305 18246 19773 12293 1575 16 -1767 O ATOM 2347 N GLN A 306 -27.531 16.699 -23.611 1.00127.21 N ANISOU 2347 N GLN A 306 17590 19466 11277 1441 -101 -1803 N ATOM 2348 CA GLN A 306 -26.737 15.841 -24.493 1.00134.65 C ANISOU 2348 CA GLN A 306 18667 20480 12012 1616 22 -1976 C ATOM 2349 C GLN A 306 -25.327 16.400 -24.747 1.00136.57 C ANISOU 2349 C GLN A 306 18764 20899 12227 1795 195 -1817 C ATOM 2350 O GLN A 306 -24.358 15.647 -24.675 1.00137.76 O ANISOU 2350 O GLN A 306 18974 21010 12359 1982 328 -1921 O ATOM 2351 CB GLN A 306 -27.474 15.638 -25.843 1.00140.10 C ANISOU 2351 CB GLN A 306 19460 21370 12403 1563 -49 -2117 C ATOM 2352 CG GLN A 306 -28.768 14.788 -25.804 1.00144.49 C ANISOU 2352 CG GLN A 306 20149 21793 12959 1366 -221 -2317 C ATOM 2353 CD GLN A 306 -29.989 15.460 -25.161 1.00145.35 C ANISOU 2353 CD GLN A 306 20094 21956 13175 1175 -383 -2156 C ATOM 2354 NE2 GLN A 306 -30.939 14.653 -24.685 1.00147.55 N ANISOU 2354 NE2 GLN A 306 20444 22192 13428 990 -538 -2327 N ATOM 2355 OE1 GLN A 306 -30.094 16.684 -25.111 1.00143.08 O ANISOU 2355 OE1 GLN A 306 19619 21752 12992 1191 -367 -1888 O ATOM 2356 N ASP A 307 -25.269 17.717 -25.004 1.00137.21 N ANISOU 2356 N ASP A 307 18655 21173 12306 1740 204 -1567 N ATOM 2357 CA ASP A 307 -24.076 18.519 -25.278 1.00137.59 C ANISOU 2357 CA ASP A 307 18559 21420 12299 1868 382 -1424 C ATOM 2358 C ASP A 307 -23.062 18.533 -24.120 1.00136.38 C ANISOU 2358 C ASP A 307 18303 21135 12380 1969 476 -1384 C ATOM 2359 O ASP A 307 -21.867 18.431 -24.383 1.00137.58 O ANISOU 2359 O ASP A 307 18396 21407 12470 2137 636 -1407 O ATOM 2360 CB ASP A 307 -24.391 19.968 -25.743 1.00137.94 C ANISOU 2360 CB ASP A 307 18451 21647 12311 1759 373 -1155 C ATOM 2361 CG ASP A 307 -25.446 20.769 -24.955 1.00137.94 C ANISOU 2361 CG ASP A 307 18368 21485 12558 1599 237 -1007 C ATOM 2362 OD1 ASP A 307 -26.154 20.187 -24.103 1.00138.07 O ANISOU 2362 OD1 ASP A 307 18477 21324 12661 1514 91 -1131 O ATOM 2363 OD2 ASP A 307 -25.546 21.979 -25.248 1.00137.75 O1- ANISOU 2363 OD2 ASP A 307 18189 21511 12639 1552 288 -773 O1- ATOM 2364 N PHE A 308 -23.547 18.634 -22.871 1.00127.80 N ANISOU 2364 N PHE A 308 17187 19821 11552 1874 379 -1328 N ATOM 2365 CA PHE A 308 -22.715 18.582 -21.666 1.00120.28 C ANISOU 2365 CA PHE A 308 16130 18762 10810 1970 448 -1281 C ATOM 2366 C PHE A 308 -22.178 17.170 -21.383 1.00115.75 C ANISOU 2366 C PHE A 308 15718 18034 10227 2162 495 -1502 C ATOM 2367 O PHE A 308 -21.020 17.036 -20.988 1.00114.88 O ANISOU 2367 O PHE A 308 15519 17969 10160 2345 610 -1501 O ATOM 2368 CB PHE A 308 -23.510 19.089 -20.446 1.00119.95 C ANISOU 2368 CB PHE A 308 16024 18526 11026 1815 332 -1156 C ATOM 2369 CG PHE A 308 -23.902 20.552 -20.497 1.00122.14 C ANISOU 2369 CG PHE A 308 16154 18921 11334 1651 293 -932 C ATOM 2370 CD1 PHE A 308 -23.002 21.548 -20.061 1.00123.81 C ANISOU 2370 CD1 PHE A 308 16165 19261 11616 1648 396 -744 C ATOM 2371 CD2 PHE A 308 -25.103 20.939 -21.123 1.00123.05 C ANISOU 2371 CD2 PHE A 308 16330 19016 11407 1501 156 -915 C ATOM 2372 CE1 PHE A 308 -23.340 22.889 -20.190 1.00124.05 C ANISOU 2372 CE1 PHE A 308 16096 19360 11676 1502 373 -536 C ATOM 2373 CE2 PHE A 308 -25.415 22.283 -21.259 1.00123.23 C ANISOU 2373 CE2 PHE A 308 16234 19132 11453 1384 122 -702 C ATOM 2374 CZ PHE A 308 -24.542 23.253 -20.786 1.00123.47 C ANISOU 2374 CZ PHE A 308 16103 19255 11556 1387 235 -509 C ATOM 2375 N ARG A 309 -23.038 16.154 -21.574 1.00112.57 N ANISOU 2375 N ARG A 309 15556 17450 9765 2126 410 -1696 N ATOM 2376 CA ARG A 309 -22.752 14.753 -21.266 1.00112.70 C ANISOU 2376 CA ARG A 309 15774 17246 9800 2298 449 -1899 C ATOM 2377 C ARG A 309 -21.717 14.120 -22.212 1.00115.78 C ANISOU 2377 C ARG A 309 16209 17799 9982 2541 603 -2031 C ATOM 2378 O ARG A 309 -20.868 13.363 -21.740 1.00116.66 O ANISOU 2378 O ARG A 309 16366 17823 10135 2773 692 -2109 O ATOM 2379 CB ARG A 309 -24.078 13.967 -21.241 1.00113.09 C ANISOU 2379 CB ARG A 309 16082 17041 9845 2153 330 -2079 C ATOM 2380 CG ARG A 309 -23.942 12.527 -20.708 1.00114.23 C ANISOU 2380 CG ARG A 309 16480 16880 10044 2301 370 -2267 C ATOM 2381 CD ARG A 309 -25.280 11.812 -20.468 1.00113.67 C ANISOU 2381 CD ARG A 309 16617 16503 10069 2089 250 -2377 C ATOM 2382 NE ARG A 309 -26.115 11.732 -21.677 1.00115.74 N ANISOU 2382 NE ARG A 309 16995 16826 10154 1910 174 -2537 N ATOM 2383 CZ ARG A 309 -27.129 12.551 -22.001 1.00115.73 C ANISOU 2383 CZ ARG A 309 16883 16928 10162 1657 41 -2467 C ATOM 2384 NH1 ARG A 309 -27.502 13.562 -21.207 1.00114.17 N1+ ANISOU 2384 NH1 ARG A 309 16473 16759 10147 1556 -18 -2238 N1+ ATOM 2385 NH2 ARG A 309 -27.792 12.345 -23.145 1.00117.20 N1+ ANISOU 2385 NH2 ARG A 309 17168 17197 10166 1515 -37 -2634 N1+ ATOM 2386 N GLU A 310 -21.784 14.455 -23.513 1.00115.91 N ANISOU 2386 N GLU A 310 16215 18063 9761 2511 638 -2054 N ATOM 2387 CA GLU A 310 -20.813 14.012 -24.516 1.00116.85 C ANISOU 2387 CA GLU A 310 16377 18359 9664 2739 796 -2186 C ATOM 2388 C GLU A 310 -19.464 14.736 -24.356 1.00115.51 C ANISOU 2388 C GLU A 310 15925 18473 9491 2858 951 -2016 C ATOM 2389 O GLU A 310 -18.430 14.086 -24.490 1.00118.74 O ANISOU 2389 O GLU A 310 16319 18990 9805 3103 1101 -2117 O ATOM 2390 CB GLU A 310 -21.421 14.149 -25.932 1.00117.39 C ANISOU 2390 CB GLU A 310 16582 18574 9445 2662 775 -2309 C ATOM 2391 CG GLU A 310 -21.518 15.585 -26.488 1.00116.25 C ANISOU 2391 CG GLU A 310 16286 18656 9228 2458 707 -2108 C ATOM 2392 CD GLU A 310 -22.268 15.651 -27.818 1.00118.26 C ANISOU 2392 CD GLU A 310 16692 18966 9273 2331 621 -2224 C ATOM 2393 OE1 GLU A 310 -21.633 16.072 -28.809 1.00120.23 O ANISOU 2393 OE1 GLU A 310 16853 19452 9378 2290 664 -2104 O ATOM 2394 OE2 GLU A 310 -23.467 15.295 -27.819 1.00118.78 O1- ANISOU 2394 OE2 GLU A 310 16970 18828 9333 2259 510 -2433 O1- ATOM 2395 N ARG A 311 -19.492 16.042 -24.031 1.00111.76 N ANISOU 2395 N ARG A 311 15225 18122 9116 2688 925 -1771 N ATOM 2396 CA ARG A 311 -18.300 16.876 -23.841 1.00112.99 C ANISOU 2396 CA ARG A 311 15103 18514 9313 2761 1072 -1613 C ATOM 2397 C ARG A 311 -17.474 16.476 -22.604 1.00116.02 C ANISOU 2397 C ARG A 311 15398 18785 9896 2937 1104 -1639 C ATOM 2398 O ARG A 311 -16.255 16.622 -22.637 1.00116.56 O ANISOU 2398 O ARG A 311 15282 19062 9945 3104 1253 -1627 O ATOM 2399 CB ARG A 311 -18.723 18.361 -23.809 1.00112.28 C ANISOU 2399 CB ARG A 311 14830 18518 9314 2521 1031 -1351 C ATOM 2400 CG ARG A 311 -17.587 19.396 -23.927 1.00114.04 C ANISOU 2400 CG ARG A 311 14767 18982 9582 2537 1191 -1186 C ATOM 2401 CD ARG A 311 -17.020 19.477 -25.354 1.00119.15 C ANISOU 2401 CD ARG A 311 15367 19934 9972 2523 1343 -1127 C ATOM 2402 NE ARG A 311 -15.940 20.465 -25.461 1.00122.39 N ANISOU 2402 NE ARG A 311 15507 20588 10405 2563 1534 -1026 N ATOM 2403 CZ ARG A 311 -15.122 20.622 -26.518 1.00125.83 C ANISOU 2403 CZ ARG A 311 15844 21295 10670 2499 1696 -908 C ATOM 2404 NH1 ARG A 311 -14.239 21.628 -26.513 1.00127.28 N1+ ANISOU 2404 NH1 ARG A 311 15768 21677 10916 2503 1869 -829 N1+ ATOM 2405 NH2 ARG A 311 -15.179 19.800 -27.574 1.00127.26 N1+ ANISOU 2405 NH2 ARG A 311 16182 21488 10684 2393 1661 -856 N1+ ATOM 2406 N LEU A 312 -18.144 15.932 -21.573 1.00118.07 N ANISOU 2406 N LEU A 312 15786 18733 10341 2904 967 -1674 N ATOM 2407 CA LEU A 312 -17.543 15.307 -20.392 1.00119.14 C ANISOU 2407 CA LEU A 312 15879 18744 10646 3093 980 -1700 C ATOM 2408 C LEU A 312 -16.723 14.052 -20.750 1.00125.22 C ANISOU 2408 C LEU A 312 16799 19490 11287 3409 1082 -1916 C ATOM 2409 O LEU A 312 -15.575 13.944 -20.320 1.00126.78 O ANISOU 2409 O LEU A 312 16854 19791 11526 3648 1174 -1923 O ATOM 2410 CB LEU A 312 -18.677 15.016 -19.376 1.00115.82 C ANISOU 2410 CB LEU A 312 15595 17984 10427 2969 817 -1679 C ATOM 2411 CG LEU A 312 -18.313 14.202 -18.112 1.00114.97 C ANISOU 2411 CG LEU A 312 15547 17672 10464 3178 806 -1730 C ATOM 2412 CD1 LEU A 312 -17.169 14.834 -17.295 1.00113.97 C ANISOU 2412 CD1 LEU A 312 15117 17686 10499 3194 816 -1557 C ATOM 2413 CD2 LEU A 312 -19.569 13.944 -17.251 1.00113.26 C ANISOU 2413 CD2 LEU A 312 15605 17075 10355 3068 673 -1791 C ATOM 2414 N ILE A 313 -17.329 13.147 -21.539 1.00129.81 N ANISOU 2414 N ILE A 313 17670 19943 11710 3422 1066 -2103 N ATOM 2415 CA ILE A 313 -16.734 11.882 -21.984 1.00135.21 C ANISOU 2415 CA ILE A 313 18554 20545 12276 3725 1163 -2328 C ATOM 2416 C ILE A 313 -15.559 12.095 -22.962 1.00140.19 C ANISOU 2416 C ILE A 313 18983 21504 12780 3902 1337 -2329 C ATOM 2417 O ILE A 313 -14.528 11.446 -22.800 1.00142.07 O ANISOU 2417 O ILE A 313 19176 21740 13064 4176 1423 -2387 O ATOM 2418 CB ILE A 313 -17.806 10.951 -22.634 1.00136.80 C ANISOU 2418 CB ILE A 313 19118 20519 12343 3643 1101 -2538 C ATOM 2419 CG1 ILE A 313 -18.864 10.523 -21.589 1.00134.53 C ANISOU 2419 CG1 ILE A 313 19009 19865 12241 3443 935 -2529 C ATOM 2420 CG2 ILE A 313 -17.247 9.695 -23.349 1.00140.68 C ANISOU 2420 CG2 ILE A 313 19804 20870 12778 3891 1200 -2734 C ATOM 2421 CD1 ILE A 313 -20.156 9.959 -22.201 1.00135.66 C ANISOU 2421 CD1 ILE A 313 19489 19784 12270 3313 868 -2745 C ATOM 2422 N HIS A 314 -15.728 13.008 -23.935 1.00141.94 N ANISOU 2422 N HIS A 314 19068 21985 12875 3728 1383 -2239 N ATOM 2423 CA HIS A 314 -14.723 13.326 -24.954 1.00147.66 C ANISOU 2423 CA HIS A 314 19599 22997 13509 3837 1551 -2218 C ATOM 2424 C HIS A 314 -13.516 14.115 -24.418 1.00149.29 C ANISOU 2424 C HIS A 314 19444 23442 13836 3920 1639 -2068 C ATOM 2425 O HIS A 314 -12.429 13.980 -24.978 1.00153.20 O ANISOU 2425 O HIS A 314 19772 24137 14302 4083 1780 -2087 O ATOM 2426 CB HIS A 314 -15.381 14.078 -26.131 1.00149.34 C ANISOU 2426 CB HIS A 314 19795 23402 13545 3617 1578 -2149 C ATOM 2427 CG HIS A 314 -16.495 13.349 -26.850 1.00152.99 C ANISOU 2427 CG HIS A 314 20571 23708 13853 3566 1519 -2328 C ATOM 2428 CD2 HIS A 314 -17.618 13.820 -27.495 1.00154.24 C ANISOU 2428 CD2 HIS A 314 20806 23976 13823 3406 1512 -2330 C ATOM 2429 ND1 HIS A 314 -16.572 11.968 -26.941 1.00153.92 N ANISOU 2429 ND1 HIS A 314 20973 23514 13997 3677 1459 -2540 N ATOM 2430 CE1 HIS A 314 -17.692 11.676 -27.607 1.00155.77 C ANISOU 2430 CE1 HIS A 314 21433 23683 14071 3568 1418 -2678 C ATOM 2431 NE2 HIS A 314 -18.377 12.752 -27.976 1.00155.66 N ANISOU 2431 NE2 HIS A 314 21293 23933 13919 3413 1442 -2555 N ATOM 2432 N ALA A 315 -13.713 14.910 -23.350 1.00146.45 N ANISOU 2432 N ALA A 315 18957 23077 13612 3804 1561 -1928 N ATOM 2433 CA ALA A 315 -12.648 15.662 -22.686 1.00146.73 C ANISOU 2433 CA ALA A 315 18640 23342 13769 3858 1636 -1802 C ATOM 2434 C ALA A 315 -11.766 14.796 -21.773 1.00148.21 C ANISOU 2434 C ALA A 315 18807 23442 14066 4177 1638 -1905 C ATOM 2435 O ALA A 315 -10.599 15.137 -21.586 1.00148.26 O ANISOU 2435 O ALA A 315 18531 23687 14113 4317 1738 -1878 O ATOM 2436 CB ALA A 315 -13.263 16.820 -21.888 1.00 0.00 C ATOM 2437 N LEU A 316 -12.334 13.710 -21.218 1.00148.94 N ANISOU 2437 N LEU A 316 19196 23191 14204 4292 1526 -2017 N ATOM 2438 CA LEU A 316 -11.643 12.774 -20.333 1.00152.46 C ANISOU 2438 CA LEU A 316 19685 23505 14740 4621 1520 -2106 C ATOM 2439 C LEU A 316 -10.952 11.704 -21.213 1.00158.84 C ANISOU 2439 C LEU A 316 20622 24291 15438 4839 1617 -2261 C ATOM 2440 O LEU A 316 -11.656 11.007 -21.945 1.00163.79 O ANISOU 2440 O LEU A 316 21534 24749 15950 4762 1612 -2376 O ATOM 2441 CB LEU A 316 -12.704 12.175 -19.374 1.00148.70 C ANISOU 2441 CB LEU A 316 19515 22627 14358 4638 1376 -2151 C ATOM 2442 CG LEU A 316 -12.167 11.495 -18.090 1.00145.65 C ANISOU 2442 CG LEU A 316 19130 22102 14111 4918 1329 -2151 C ATOM 2443 CD1 LEU A 316 -11.362 10.198 -18.324 1.00147.58 C ANISOU 2443 CD1 LEU A 316 19551 22209 14313 5260 1387 -2295 C ATOM 2444 CD2 LEU A 316 -11.440 12.485 -17.155 1.00143.64 C ANISOU 2444 CD2 LEU A 316 18437 22171 13968 4927 1340 -1997 C ATOM 2445 N PRO A 317 -9.602 11.606 -21.169 1.00157.97 N ANISOU 2445 N PRO A 317 20307 24358 15357 5106 1702 -2277 N ATOM 2446 CA PRO A 317 -8.847 10.700 -22.055 1.00162.89 C ANISOU 2446 CA PRO A 317 21030 24997 15865 5311 1810 -2418 C ATOM 2447 C PRO A 317 -9.089 9.211 -21.743 1.00168.81 C ANISOU 2447 C PRO A 317 22119 25378 16641 5591 1766 -2564 C ATOM 2448 O PRO A 317 -8.900 8.787 -20.603 1.00168.28 O ANISOU 2448 O PRO A 317 22065 25176 16699 5782 1691 -2533 O ATOM 2449 CB PRO A 317 -7.383 11.116 -21.838 1.00163.42 C ANISOU 2449 CB PRO A 317 20673 25463 15957 5447 1919 -2349 C ATOM 2450 CG PRO A 317 -7.343 11.679 -20.428 1.00159.70 C ANISOU 2450 CG PRO A 317 19950 25079 15650 5423 1831 -2211 C ATOM 2451 CD PRO A 317 -8.700 12.359 -20.291 1.00155.50 C ANISOU 2451 CD PRO A 317 19652 24254 15177 5231 1695 -2171 C ATOM 2452 N ALA A 318 -9.514 8.464 -22.778 1.00172.83 N ANISOU 2452 N ALA A 318 22920 25723 17024 5609 1815 -2722 N ATOM 2453 CA ALA A 318 -9.806 7.025 -22.764 1.00180.13 C ANISOU 2453 CA ALA A 318 24200 26291 17949 5858 1810 -2881 C ATOM 2454 C ALA A 318 -10.989 6.628 -21.855 1.00182.42 C ANISOU 2454 C ALA A 318 24755 26187 18369 5849 1672 -2866 C ATOM 2455 O ALA A 318 -10.975 5.538 -21.280 1.00188.28 O ANISOU 2455 O ALA A 318 25514 26807 19217 6106 1636 -2831 O ATOM 2456 CB ALA A 318 -8.525 6.212 -22.479 1.00 0.00 C ATOM 2457 N SER A 319 -12.000 7.510 -21.756 1.00181.07 N ANISOU 2457 N SER A 319 24794 25826 18177 5539 1593 -2891 N ATOM 2458 CA SER A 319 -13.242 7.273 -21.017 1.00180.64 C ANISOU 2458 CA SER A 319 25004 25395 18235 5461 1470 -2883 C ATOM 2459 C SER A 319 -14.112 6.200 -21.693 1.00181.86 C ANISOU 2459 C SER A 319 25580 25199 18319 5282 1444 -3061 C ATOM 2460 O SER A 319 -14.246 6.210 -22.917 1.00183.72 O ANISOU 2460 O SER A 319 25850 25542 18411 5135 1489 -3160 O ATOM 2461 CB SER A 319 -14.015 8.603 -20.912 1.00174.26 C ANISOU 2461 CB SER A 319 23988 24721 17501 5212 1375 -2718 C ATOM 2462 OG SER A 319 -15.179 8.492 -20.114 1.00171.85 O ANISOU 2462 OG SER A 319 23958 24046 17294 5121 1263 -2721 O ATOM 2463 N LEU A 320 -14.737 5.346 -20.867 1.00174.94 N ANISOU 2463 N LEU A 320 25025 23903 17540 5286 1373 -3100 N ATOM 2464 CA LEU A 320 -15.798 4.433 -21.290 1.00170.49 C ANISOU 2464 CA LEU A 320 24862 22985 16933 5075 1343 -3274 C ATOM 2465 C LEU A 320 -17.098 5.221 -21.543 1.00162.46 C ANISOU 2465 C LEU A 320 23796 22059 15872 4672 1246 -3255 C ATOM 2466 O LEU A 320 -17.400 6.164 -20.810 1.00159.78 O ANISOU 2466 O LEU A 320 23229 21883 15598 4559 1174 -3091 O ATOM 2467 CB LEU A 320 -15.963 3.332 -20.215 1.00170.40 C ANISOU 2467 CB LEU A 320 25203 22492 17050 5162 1306 -3301 C ATOM 2468 CG LEU A 320 -16.997 2.224 -20.530 1.00 0.00 C ATOM 2469 CD1 LEU A 320 -16.692 1.483 -21.851 1.00 0.00 C ATOM 2470 CD2 LEU A 320 -17.142 1.252 -19.339 1.00 0.00 C ATOM 2471 N GLU A 321 -17.834 4.813 -22.590 1.00159.99 N ANISOU 2471 N GLU A 321 23692 21654 15443 4456 1239 -3428 N ATOM 2472 CA GLU A 321 -19.025 5.484 -23.123 1.00155.08 C ANISOU 2472 CA GLU A 321 23019 21151 14751 4084 1135 -3423 C ATOM 2473 C GLU A 321 -20.207 5.025 -22.287 1.00154.86 C ANISOU 2473 C GLU A 321 23310 20732 14799 3838 1030 -3521 C ATOM 2474 O GLU A 321 -21.357 5.405 -22.506 1.00155.30 O ANISOU 2474 O GLU A 321 23504 20743 14759 3564 972 -3664 O ATOM 2475 CB GLU A 321 -19.229 5.141 -24.626 1.00155.62 C ANISOU 2475 CB GLU A 321 23065 21446 14619 3978 1178 -3541 C ATOM 2476 CG GLU A 321 -18.093 5.563 -25.592 1.00153.92 C ANISOU 2476 CG GLU A 321 22592 21570 14320 4224 1315 -3481 C ATOM 2477 CD GLU A 321 -16.805 4.730 -25.530 1.00154.36 C ANISOU 2477 CD GLU A 321 22830 21456 14366 4527 1439 -3628 C ATOM 2478 OE1 GLU A 321 -16.867 3.580 -25.039 1.00154.74 O ANISOU 2478 OE1 GLU A 321 23236 21132 14427 4496 1428 -3808 O ATOM 2479 OE2 GLU A 321 -15.773 5.263 -25.989 1.00154.37 O1- ANISOU 2479 OE2 GLU A 321 22612 21695 14347 4788 1549 -3564 O1- TER HETATM 2480 C1 UNK Z 999 -30.765 31.652 7.364 1.00 0.00 C HETATM 2481 N1 UNK Z 999 -29.775 30.857 6.923 1.00 0.00 N HETATM 2482 O1 UNK Z 999 -31.951 31.336 7.462 1.00 0.00 O HETATM 2483 S1 UNK Z 999 -32.364 27.727 3.530 1.00 0.00 S HETATM 2484 C2 UNK Z 999 -29.839 29.461 6.459 1.00 0.00 C HETATM 2485 N2 UNK Z 999 -29.242 27.330 7.509 1.00 0.00 N HETATM 2486 O2 UNK Z 999 -30.754 28.675 8.545 1.00 0.00 O HETATM 2487 C3 UNK Z 999 -29.977 28.450 7.616 1.00 0.00 C HETATM 2488 N3 UNK Z 999 -28.034 25.246 10.336 1.00 0.00 N HETATM 2489 O3 UNK Z 999 -27.435 22.814 11.369 1.00 0.00 O1- HETATM 2490 C4 UNK Z 999 -30.917 29.284 5.355 1.00 0.00 C HETATM 2491 O4 UNK Z 999 -28.008 27.480 9.955 1.00 0.00 O HETATM 2492 C5 UNK Z 999 -31.037 27.872 4.752 1.00 0.00 C HETATM 2493 O5 UNK Z 999 -25.958 23.628 12.863 1.00 0.00 O HETATM 2494 C6 UNK Z 999 -31.509 28.282 2.033 1.00 0.00 C HETATM 2495 C7 UNK Z 999 -29.290 26.164 8.403 1.00 0.00 C HETATM 2496 C8 UNK Z 999 -28.358 26.342 9.625 1.00 0.00 C HETATM 2497 C9 UNK Z 999 -29.049 24.911 7.506 1.00 0.00 C HETATM 2498 C10 UNK Z 999 -29.164 23.485 8.110 1.00 0.00 C HETATM 2499 C11 UNK Z 999 -30.378 23.280 9.048 1.00 0.00 C HETATM 2500 C12 UNK Z 999 -29.125 22.426 6.985 1.00 0.00 C HETATM 2501 C13 UNK Z 999 -27.155 25.206 11.518 1.00 0.00 C HETATM 2502 C14 UNK Z 999 -26.822 23.732 11.961 1.00 0.00 C HETATM 2503 C15 UNK Z 999 -27.771 25.999 12.714 1.00 0.00 C HETATM 2504 C16 UNK Z 999 -26.741 26.764 13.518 1.00 0.00 C HETATM 2505 C17 UNK Z 999 -26.188 26.203 14.684 1.00 0.00 C HETATM 2506 C18 UNK Z 999 -25.150 26.849 15.332 1.00 0.00 C HETATM 2507 C19 UNK Z 999 -24.632 28.036 14.824 1.00 0.00 C HETATM 2508 C20 UNK Z 999 -25.147 28.587 13.661 1.00 0.00 C HETATM 2509 C21 UNK Z 999 -26.189 27.956 12.997 1.00 0.00 C CONECT 2480 2481 2482 CONECT 2481 2480 2484 CONECT 2482 2480 CONECT 2483 2494 2492 CONECT 2484 2481 2487 2490 CONECT 2485 2495 2487 CONECT 2486 2487 CONECT 2487 2484 2485 2486 CONECT 2488 2501 2496 CONECT 2489 2502 CONECT 2490 2484 2492 CONECT 2491 2496 CONECT 2492 2490 2483 CONECT 2493 2502 CONECT 2494 2483 CONECT 2495 2485 2496 2497 CONECT 2496 2495 2488 2491 CONECT 2497 2495 2498 CONECT 2498 2497 2499 2500 CONECT 2499 2498 CONECT 2500 2498 CONECT 2501 2488 2502 2503 CONECT 2502 2501 2489 2493 CONECT 2503 2501 2504 CONECT 2504 2503 2505 2509 CONECT 2505 2504 2506 CONECT 2506 2505 2507 CONECT 2507 2506 2508 CONECT 2508 2507 2509 CONECT 2509 2504 2508 END