ATOM 1 N ALA A 3 -17.970 -34.630 -21.372 1.00 66.50 A N ANISOU 1 N ALA A 3 11802 4837 8630 1130 -1765 -795 A N ATOM 2 CA ALA A 3 -18.531 -33.329 -21.018 1.00 65.70 A C ANISOU 2 CA ALA A 3 11506 4888 8569 977 -1678 -722 A C ATOM 3 C ALA A 3 -18.848 -33.253 -19.527 1.00 69.16 A C ANISOU 3 C ALA A 3 12013 5277 8987 845 -1718 -543 A C ATOM 4 O ALA A 3 -19.455 -34.169 -18.967 1.00 69.23 A O ANISOU 4 O ALA A 3 12255 5119 8928 673 -1790 -440 A O ATOM 5 CB ALA A 3 -19.779 -33.048 -21.840 1.00 62.60 A C ANISOU 5 CB ALA A 3 11113 4514 8157 701 -1619 -732 A C ATOM 6 N LEU A 4 -18.432 -32.155 -18.895 1.00 70.50 A N ANISOU 6 N LEU A 4 11978 5600 9209 925 -1673 -507 A N ATOM 7 CA LEU A 4 -18.651 -31.938 -17.465 1.00 69.92 A C ANISOU 7 CA LEU A 4 11942 5513 9110 822 -1703 -346 A C ATOM 8 C LEU A 4 -20.138 -32.002 -17.110 1.00 73.33 A C ANISOU 8 C LEU A 4 12455 5931 9476 440 -1668 -207 A C ATOM 9 O LEU A 4 -20.973 -31.410 -17.794 1.00 72.43 A O ANISOU 9 O LEU A 4 12172 5987 9362 258 -1556 -220 A O ATOM 10 CB LEU A 4 -18.061 -30.594 -17.036 1.00 65.86 A C ANISOU 10 CB LEU A 4 11081 5295 8647 921 -1604 -341 A C ATOM 11 N ARG A 5 -20.446 -32.716 -16.028 1.00 77.43 A N ANISOU 11 N ARG A 5 13209 6285 9927 324 -1756 -70 A N ATOM 12 CA ARG A 5 -21.816 -33.092 -15.664 1.00 80.33 A C ANISOU 12 CA ARG A 5 13714 6597 10212 -44 -1748 65 A C ATOM 13 C ARG A 5 -22.852 -31.963 -15.690 1.00 81.67 A C ANISOU 13 C ARG A 5 13604 7056 10372 -287 -1595 119 A C ATOM 14 O ARG A 5 -23.998 -32.195 -16.079 1.00 87.49 A O ANISOU 14 O ARG A 5 14379 7802 11061 -567 -1563 156 A O ATOM 15 CB ARG A 5 -21.817 -33.732 -14.272 1.00 80.89 A C ANISOU 15 CB ARG A 5 13968 6571 10198 -106 -1827 219 A C ATOM 16 N GLN A 6 -22.447 -30.760 -15.280 1.00 76.15 A N ANISOU 16 N GLN A 6 12612 6608 9713 -177 -1502 119 A N ATOM 17 CA GLN A 6 -23.343 -29.600 -15.171 1.00 73.04 A C ANISOU 17 CA GLN A 6 11935 6509 9308 -361 -1354 169 A C ATOM 18 C GLN A 6 -24.501 -29.841 -14.198 1.00 72.67 A C ANISOU 18 C GLN A 6 11981 6475 9157 -668 -1346 332 A C ATOM 19 O GLN A 6 -25.471 -30.515 -14.533 1.00 75.71 A O ANISOU 19 O GLN A 6 12499 6782 9484 -913 -1360 373 A O ATOM 20 CB GLN A 6 -23.899 -29.197 -16.545 1.00 72.01 A C ANISOU 20 CB GLN A 6 11641 6507 9211 -429 -1266 74 A C ATOM 21 CG GLN A 6 -22.844 -28.719 -17.530 1.00 73.64 A C ANISOU 21 CG GLN A 6 11696 6776 9509 -152 -1238 -79 A C ATOM 22 CD GLN A 6 -23.435 -28.000 -18.733 1.00 76.09 A C ANISOU 22 CD GLN A 6 11791 7281 9840 -226 -1127 -147 A C ATOM 23 NE2 GLN A 6 -22.625 -27.822 -19.769 1.00 76.75 A N ANISOU 23 NE2 GLN A 6 11790 7391 9979 -21 -1111 -280 A N ATOM 24 OE1 GLN A 6 -24.604 -27.610 -18.732 1.00 77.16 A O ANISOU 24 OE1 GLN A 6 11831 7553 9933 -458 -1058 -78 A O ATOM 25 N PRO A 7 -24.402 -29.273 -12.987 1.00 69.52 A N ANISOU 25 N PRO A 7 11502 6191 8723 -664 -1319 422 A N ATOM 26 CA PRO A 7 -25.418 -29.426 -11.940 1.00 68.88 A C ANISOU 26 CA PRO A 7 11487 6159 8525 -937 -1299 580 A C ATOM 27 C PRO A 7 -26.695 -28.642 -12.232 1.00 67.08 A C ANISOU 27 C PRO A 7 11019 6203 8267 -1166 -1157 600 A C ATOM 28 O PRO A 7 -26.633 -27.535 -12.770 1.00 64.85 A O ANISOU 28 O PRO A 7 10459 6129 8053 -1064 -1056 516 A O ATOM 29 CB PRO A 7 -24.726 -28.864 -10.690 1.00 68.21 A C ANISOU 29 CB PRO A 7 11344 6152 8422 -796 -1304 630 A C ATOM 30 CG PRO A 7 -23.270 -28.769 -11.044 1.00 67.89 A C ANISOU 30 CG PRO A 7 11283 6027 8483 -457 -1370 510 A C ATOM 31 CD PRO A 7 -23.239 -28.511 -12.508 1.00 67.26 A C ANISOU 31 CD PRO A 7 11071 5990 8496 -394 -1316 374 A C ATOM 32 N GLN A 8 -27.839 -29.210 -11.866 1.00 67.30 A N ANISOU 32 N GLN A 8 11151 6232 8187 -1474 -1152 716 A N ATOM 33 CA GLN A 8 -29.111 -28.514 -12.011 1.00 64.51 A C ANISOU 33 CA GLN A 8 10560 6163 7787 -1694 -1022 746 A C ATOM 34 C GLN A 8 -29.294 -27.501 -10.886 1.00 62.58 A C ANISOU 34 C GLN A 8 10120 6163 7492 -1682 -927 806 A C ATOM 35 O GLN A 8 -28.569 -27.531 -9.892 1.00 65.90 A O ANISOU 35 O GLN A 8 10634 6514 7891 -1567 -974 850 A O ATOM 36 CB GLN A 8 -30.274 -29.508 -12.023 1.00 66.03 A C ANISOU 36 CB GLN A 8 10918 6296 7873 -2047 -1051 846 A C ATOM 37 N VAL A 9 -30.266 -26.610 -11.049 1.00 59.84 A N ANISOU 37 N VAL A 9 9508 6107 7123 -1791 -799 803 A N ATOM 38 CA VAL A 9 -30.553 -25.589 -10.050 1.00 60.48 A C ANISOU 38 CA VAL A 9 9393 6437 7151 -1775 -699 841 A C ATOM 39 C VAL A 9 -30.837 -26.200 -8.677 1.00 62.40 A C ANISOU 39 C VAL A 9 9805 6655 7251 -1942 -728 987 A C ATOM 40 O VAL A 9 -30.303 -25.745 -7.669 1.00 64.20 A O ANISOU 40 O VAL A 9 10019 6926 7450 -1822 -723 1008 A O ATOM 41 CB VAL A 9 -31.752 -24.715 -10.470 1.00 60.47 A C ANISOU 41 CB VAL A 9 9105 6746 7127 -1891 -566 823 A C ATOM 42 N ALA A 10 -31.659 -27.246 -8.650 1.00 61.75 A N ANISOU 42 N ALA A 10 9890 6501 7073 -2229 -763 1088 A N ATOM 43 CA ALA A 10 -32.072 -27.880 -7.400 1.00 62.12 A C ANISOU 43 CA ALA A 10 10102 6537 6963 -2439 -783 1247 A C ATOM 44 C ALA A 10 -30.897 -28.434 -6.590 1.00 63.51 A C ANISOU 44 C ALA A 10 10542 6455 7133 -2279 -908 1293 A C ATOM 45 O ALA A 10 -30.975 -28.538 -5.365 1.00 64.90 A O ANISOU 45 O ALA A 10 10797 6678 7185 -2355 -908 1408 A O ATOM 46 CB ALA A 10 -33.076 -28.990 -7.685 1.00 61.62 A C ANISOU 46 CB ALA A 10 10199 6403 6812 -2791 -816 1344 A C ATOM 47 N GLU A 11 -29.815 -28.795 -7.275 1.00 61.26 A N ANISOU 47 N GLU A 11 10390 5914 6973 -2051 -1014 1202 A N ATOM 48 CA GLU A 11 -28.633 -29.331 -6.606 1.00 59.28 A C ANISOU 48 CA GLU A 11 10377 5422 6726 -1860 -1146 1232 A C ATOM 49 C GLU A 11 -27.751 -28.214 -6.051 1.00 57.85 A C ANISOU 49 C GLU A 11 10002 5386 6592 -1585 -1110 1161 A C ATOM 50 O GLU A 11 -27.214 -28.328 -4.952 1.00 60.07 A O ANISOU 50 O GLU A 11 10394 5627 6802 -1516 -1168 1232 A O ATOM 51 CB GLU A 11 -27.827 -30.206 -7.564 1.00 60.96 A C ANISOU 51 CB GLU A 11 10804 5315 7044 -1712 -1277 1153 A C ATOM 52 CG GLU A 11 -26.486 -30.639 -7.014 1.00 66.12 A C ANISOU 52 CG GLU A 11 11657 5744 7723 -1445 -1415 1153 A C ATOM 53 CD GLU A 11 -25.743 -31.574 -7.946 1.00 71.93 A C ANISOU 53 CD GLU A 11 12614 6166 8549 -1288 -1545 1070 A C ATOM 54 OE1 GLU A 11 -26.288 -31.913 -9.020 1.00 70.72 A O ANISOU 54 OE1 GLU A 11 12477 5959 8434 -1404 -1530 1012 A O ATOM 55 OE2 GLU A 11 -24.612 -31.975 -7.597 1.00 76.52 A O1- ANISOU 55 OE2 GLU A 11 13354 6565 9157 -1040 -1668 1057 A O1- ATOM 56 N LEU A 12 -27.601 -27.139 -6.819 1.00 54.78 A N ANISOU 56 N LEU A 12 9334 5163 6318 -1437 -1020 1023 A N ATOM 57 CA LEU A 12 -26.850 -25.978 -6.368 1.00 51.40 A C ANISOU 57 CA LEU A 12 8707 4884 5938 -1208 -977 948 A C ATOM 58 C LEU A 12 -27.596 -25.297 -5.234 1.00 53.96 A C ANISOU 58 C LEU A 12 8910 5458 6135 -1336 -879 1022 A C ATOM 59 O LEU A 12 -26.995 -24.895 -4.229 1.00 53.90 A O ANISOU 59 O LEU A 12 8899 5496 6084 -1220 -899 1034 A O ATOM 60 CB LEU A 12 -26.614 -24.998 -7.518 1.00 49.64 A C ANISOU 60 CB LEU A 12 8233 4770 5859 -1055 -901 796 A C ATOM 61 CG LEU A 12 -25.585 -25.464 -8.548 1.00 50.14 A C ANISOU 61 CG LEU A 12 8378 4624 6048 -860 -991 697 A C ATOM 62 CD1 LEU A 12 -25.582 -24.559 -9.773 1.00 49.18 A C ANISOU 62 CD1 LEU A 12 8014 4629 6043 -770 -901 570 A C ATOM 63 CD2 LEU A 12 -24.205 -25.530 -7.916 1.00 47.32 A C ANISOU 63 CD2 LEU A 12 8101 4159 5721 -617 -1093 673 A C ATOM 64 N LEU A 13 -28.911 -25.176 -5.405 1.00 52.00 A N ANISOU 64 N LEU A 13 8553 5385 5818 -1571 -774 1065 A N ATOM 65 CA LEU A 13 -29.784 -24.644 -4.364 1.00 51.72 A C ANISOU 65 CA LEU A 13 8401 5610 5640 -1715 -670 1137 A C ATOM 66 C LEU A 13 -29.594 -25.388 -3.040 1.00 54.43 A C ANISOU 66 C LEU A 13 8979 5870 5834 -1801 -745 1278 A C ATOM 67 O LEU A 13 -29.493 -24.770 -1.981 1.00 56.70 A O ANISOU 67 O LEU A 13 9198 6311 6033 -1751 -705 1294 A O ATOM 68 CB LEU A 13 -31.244 -24.725 -4.806 1.00 52.40 A C ANISOU 68 CB LEU A 13 8372 5877 5661 -1982 -570 1179 A C ATOM 69 CG LEU A 13 -32.291 -24.270 -3.791 1.00 53.65 A C ANISOU 69 CG LEU A 13 8394 6338 5653 -2152 -451 1255 A C ATOM 70 CD1 LEU A 13 -32.061 -22.820 -3.415 1.00 52.60 A C ANISOU 70 CD1 LEU A 13 8018 6417 5550 -1935 -360 1149 A C ATOM 71 CD2 LEU A 13 -33.693 -24.468 -4.350 1.00 51.67 A C ANISOU 71 CD2 LEU A 13 8020 6268 5345 -2418 -366 1294 A C ATOM 72 N ALA A 14 -29.532 -26.715 -3.112 1.00 53.56 A N ANISOU 72 N ALA A 14 9158 5504 5688 -1927 -859 1378 A N ATOM 73 CA ALA A 14 -29.406 -27.551 -1.923 1.00 54.48 A C ANISOU 73 CA ALA A 14 9537 5510 5652 -2032 -943 1535 A C ATOM 74 C ALA A 14 -28.027 -27.416 -1.276 1.00 57.12 A C ANISOU 74 C ALA A 14 9964 5723 6017 -1746 -1050 1505 A C ATOM 75 O ALA A 14 -27.897 -27.497 -0.057 1.00 57.85 A O ANISOU 75 O ALA A 14 10152 5858 5971 -1770 -1077 1604 A O ATOM 76 CB ALA A 14 -29.685 -29.002 -2.271 1.00 52.41 A C ANISOU 76 CB ALA A 14 9585 4973 5357 -2236 -1048 1645 A C ATOM 77 N GLU A 15 -27.001 -27.224 -2.099 1.00 57.66 A N ANISOU 77 N GLU A 15 9997 5655 6256 -1482 -1114 1371 A N ATOM 78 CA GLU A 15 -25.652 -26.990 -1.601 1.00 55.98 A C ANISOU 78 CA GLU A 15 9817 5365 6087 -1196 -1212 1320 A C ATOM 79 C GLU A 15 -25.594 -25.644 -0.882 1.00 55.01 A C ANISOU 79 C GLU A 15 9440 5526 5934 -1113 -1112 1257 A C ATOM 80 O GLU A 15 -25.081 -25.541 0.237 1.00 58.38 A O ANISOU 80 O GLU A 15 9929 5985 6268 -1041 -1165 1302 A O ATOM 81 CB GLU A 15 -24.637 -27.028 -2.747 1.00 57.89 A C ANISOU 81 CB GLU A 15 10036 5444 6517 -947 -1281 1178 A C ATOM 82 CG GLU A 15 -23.215 -26.663 -2.338 1.00 63.34 A C ANISOU 82 CG GLU A 15 10699 6103 7263 -646 -1373 1105 A C ATOM 83 CD GLU A 15 -22.337 -26.277 -3.521 1.00 65.89 A C ANISOU 83 CD GLU A 15 10877 6385 7771 -413 -1382 938 A C ATOM 84 OE1 GLU A 15 -22.774 -26.464 -4.678 1.00 65.44 A O ANISOU 84 OE1 GLU A 15 10791 6279 7792 -473 -1338 887 A O ATOM 85 OE2 GLU A 15 -21.211 -25.777 -3.293 1.00 66.54 A O1- ANISOU 85 OE2 GLU A 15 10870 6502 7912 -180 -1433 858 A O1- ATOM 86 N ALA A 16 -26.131 -24.620 -1.541 1.00 49.48 A N ANISOU 86 N ALA A 16 8465 5024 5310 -1120 -975 1151 A N ATOM 87 CA ALA A 16 -26.195 -23.274 -0.989 1.00 48.34 A C ANISOU 87 CA ALA A 16 8082 5139 5148 -1046 -871 1075 A C ATOM 88 C ALA A 16 -27.007 -23.226 0.301 1.00 56.98 A C ANISOU 88 C ALA A 16 9200 6415 6036 -1222 -810 1187 A C ATOM 89 O ALA A 16 -26.646 -22.519 1.242 1.00 60.92 A O ANISOU 89 O ALA A 16 9635 7042 6469 -1127 -799 1158 A O ATOM 90 CB ALA A 16 -26.783 -22.316 -2.011 1.00 44.25 A C ANISOU 90 CB ALA A 16 7301 4773 4737 -1041 -740 962 A C ATOM 91 N ARG A 17 -28.102 -23.981 0.337 1.00 59.90 A N ANISOU 91 N ARG A 17 9658 6805 6295 -1488 -771 1310 A N ATOM 92 CA ARG A 17 -28.994 -24.004 1.491 1.00 61.70 A C ANISOU 92 CA ARG A 17 9897 7236 6311 -1690 -697 1426 A C ATOM 93 C ARG A 17 -28.294 -24.577 2.713 1.00 58.40 A C ANISOU 93 C ARG A 17 9712 6715 5762 -1660 -813 1534 A C ATOM 94 O ARG A 17 -28.367 -24.020 3.808 1.00 57.92 A O ANISOU 94 O ARG A 17 9596 6846 5565 -1652 -767 1547 A O ATOM 95 CB ARG A 17 -30.246 -24.827 1.186 1.00 71.00 A C ANISOU 95 CB ARG A 17 11133 8442 7402 -2007 -644 1546 A C ATOM 96 CG ARG A 17 -31.552 -24.059 1.294 1.00 78.25 A C ANISOU 96 CG ARG A 17 11788 9712 8232 -2159 -464 1530 A C ATOM 97 CD ARG A 17 -32.732 -25.017 1.368 1.00 86.54 A C ANISOU 97 CD ARG A 17 12926 10815 9139 -2514 -428 1687 A C ATOM 98 NE ARG A 17 -34.014 -24.327 1.259 1.00 92.17 A N ANISOU 98 NE ARG A 17 13354 11881 9785 -2651 -258 1658 A N ATOM 99 CZ ARG A 17 -35.195 -24.939 1.279 1.00 96.92 A C ANISOU 99 CZ ARG A 17 13945 12621 10259 -2972 -195 1773 A C ATOM 100 NH1 ARG A 17 -35.258 -26.257 1.407 1.00100.69 A N1+ ANISOU 100 NH1 ARG A 17 14708 12886 10662 -3209 -290 1930 A N1+ ATOM 101 NH2 ARG A 17 -36.313 -24.234 1.171 1.00 97.01 A N ANISOU 101 NH2 ARG A 17 13664 12983 10212 -3059 -41 1730 A N ATOM 102 N ARG A 18 -27.616 -25.700 2.508 1.00 56.28 A N ANISOU 102 N ARG A 18 9713 6141 5529 -1632 -968 1607 A N ATOM 103 CA ARG A 18 -26.950 -26.410 3.586 1.00 57.80 A C ANISOU 103 CA ARG A 18 10166 6199 5597 -1601 -1103 1729 A C ATOM 104 C ARG A 18 -25.780 -25.605 4.138 1.00 56.71 A C ANISOU 104 C ARG A 18 9941 6110 5496 -1313 -1160 1623 A C ATOM 105 O ARG A 18 -25.590 -25.529 5.355 1.00 58.63 A O ANISOU 105 O ARG A 18 10254 6443 5580 -1310 -1190 1692 A O ATOM 106 CB ARG A 18 -26.475 -27.777 3.096 1.00 61.63 A C ANISOU 106 CB ARG A 18 10963 6321 6133 -1602 -1265 1813 A C ATOM 107 CG ARG A 18 -25.675 -28.569 4.112 1.00 66.74 A C ANISOU 107 CG ARG A 18 11904 6788 6666 -1527 -1432 1941 A C ATOM 108 CD ARG A 18 -24.901 -29.678 3.427 1.00 73.09 A C ANISOU 108 CD ARG A 18 12974 7219 7580 -1403 -1606 1956 A C ATOM 109 NE ARG A 18 -24.408 -29.239 2.124 1.00 78.00 A N ANISOU 109 NE ARG A 18 13415 7794 8426 -1207 -1590 1766 A N ATOM 110 CZ ARG A 18 -23.314 -28.505 1.944 1.00 77.98 A C ANISOU 110 CZ ARG A 18 13248 7835 8547 -906 -1624 1616 A C ATOM 111 NH1 ARG A 18 -22.585 -28.127 2.989 1.00 76.60 A N1+ ANISOU 111 NH1 ARG A 18 13064 7745 8296 -761 -1684 1626 A N1+ ATOM 112 NH2 ARG A 18 -22.951 -28.148 0.716 1.00 74.11 A N ANISOU 112 NH2 ARG A 18 12600 7314 8246 -763 -1598 1458 A N ATOM 113 N ALA A 19 -24.999 -25.008 3.243 1.00 53.61 A N ANISOU 113 N ALA A 19 9397 5669 5305 -1084 -1176 1457 A N ATOM 114 CA ALA A 19 -23.872 -24.178 3.650 1.00 51.43 A C ANISOU 114 CA ALA A 19 9010 5451 5081 -828 -1228 1341 A C ATOM 115 C ALA A 19 -24.360 -22.985 4.457 1.00 49.45 A C ANISOU 115 C ALA A 19 8557 5501 4729 -863 -1100 1287 A C ATOM 116 O ALA A 19 -23.766 -22.637 5.478 1.00 51.68 A O ANISOU 116 O ALA A 19 8857 5861 4919 -766 -1153 1280 A O ATOM 117 CB ALA A 19 -23.075 -23.710 2.441 1.00 45.60 A C ANISOU 117 CB ALA A 19 8120 4633 4572 -619 -1243 1176 A C ATOM 118 N PHE A 20 -25.443 -22.366 3.994 1.00 49.33 A N ANISOU 118 N PHE A 20 8355 5661 4726 -991 -936 1243 A N ATOM 119 CA PHE A 20 -26.029 -21.232 4.697 1.00 49.36 A C ANISOU 119 CA PHE A 20 8168 5954 4632 -1015 -804 1181 A C ATOM 120 C PHE A 20 -26.464 -21.614 6.106 1.00 52.88 A C ANISOU 120 C PHE A 20 8746 6521 4824 -1157 -802 1318 A C ATOM 121 O PHE A 20 -26.172 -20.901 7.065 1.00 54.37 A O ANISOU 121 O PHE A 20 8883 6860 4915 -1074 -794 1267 A O ATOM 122 CB PHE A 20 -27.225 -20.670 3.927 1.00 46.76 A C ANISOU 122 CB PHE A 20 7633 5787 4346 -1130 -637 1131 A C ATOM 123 CG PHE A 20 -27.806 -19.424 4.541 1.00 47.17 A C ANISOU 123 CG PHE A 20 7479 6129 4315 -1110 -501 1041 A C ATOM 124 CD1 PHE A 20 -28.728 -19.504 5.573 1.00 46.36 A C ANISOU 124 CD1 PHE A 20 7385 6241 3987 -1276 -417 1129 A C ATOM 125 CD2 PHE A 20 -27.427 -18.173 4.086 1.00 45.42 A C ANISOU 125 CD2 PHE A 20 7061 5962 4233 -925 -458 867 A C ATOM 126 CE1 PHE A 20 -29.254 -18.365 6.141 1.00 46.35 A C ANISOU 126 CE1 PHE A 20 7200 6508 3902 -1234 -293 1031 A C ATOM 127 CE2 PHE A 20 -27.956 -17.029 4.644 1.00 44.24 A C ANISOU 127 CE2 PHE A 20 6748 6053 4009 -890 -342 774 A C ATOM 128 CZ PHE A 20 -28.870 -17.126 5.677 1.00 46.43 A C ANISOU 128 CZ PHE A 20 7033 6548 4061 -1032 -259 849 A C ATOM 129 N ARG A 21 -27.179 -22.731 6.213 1.00 55.44 A N ANISOU 129 N ARG A 21 9247 6782 5036 -1385 -809 1490 A N ATOM 130 CA ARG A 21 -27.716 -23.203 7.484 1.00 59.06 A C ANISOU 130 CA ARG A 21 9844 7361 5236 -1567 -795 1648 A C ATOM 131 C ARG A 21 -26.602 -23.445 8.499 1.00 61.84 A C ANISOU 131 C ARG A 21 10377 7620 5500 -1423 -949 1691 A C ATOM 132 O ARG A 21 -26.729 -23.106 9.675 1.00 64.81 A O ANISOU 132 O ARG A 21 10755 8186 5682 -1451 -920 1722 A O ATOM 133 CB ARG A 21 -28.530 -24.483 7.264 1.00 60.38 A C ANISOU 133 CB ARG A 21 10203 7415 5323 -1848 -802 1835 A C ATOM 134 CG ARG A 21 -28.971 -25.185 8.538 1.00 61.77 A C ANISOU 134 CG ARG A 21 10577 7665 5227 -2058 -813 2034 A C ATOM 135 CD ARG A 21 -29.865 -24.295 9.387 1.00 61.71 A C ANISOU 135 CD ARG A 21 10363 8050 5036 -2153 -639 2008 A C ATOM 136 NE ARG A 21 -30.327 -24.977 10.592 1.00 62.52 A N ANISOU 136 NE ARG A 21 10648 8248 4858 -2374 -637 2206 A N ATOM 137 CZ ARG A 21 -29.603 -25.095 11.700 1.00 62.99 A C ANISOU 137 CZ ARG A 21 10870 8290 4775 -2287 -736 2268 A C ATOM 138 NH1 ARG A 21 -28.385 -24.578 11.746 1.00 61.17 A N1+ ANISOU 138 NH1 ARG A 21 10627 7953 4660 -1986 -848 2138 A N1+ ATOM 139 NH2 ARG A 21 -30.094 -25.731 12.756 1.00 64.80 A N ANISOU 139 NH2 ARG A 21 11269 8616 4735 -2510 -726 2462 A N ATOM 140 N GLU A 22 -25.505 -24.021 8.026 1.00 61.10 A N ANISOU 140 N GLU A 22 10426 7246 5545 -1257 -1114 1685 A N ATOM 141 CA GLU A 22 -24.365 -24.316 8.875 1.00 62.49 A C ANISOU 141 CA GLU A 22 10768 7321 5655 -1093 -1282 1723 A C ATOM 142 C GLU A 22 -23.626 -23.039 9.266 1.00 58.82 A C ANISOU 142 C GLU A 22 10096 7024 5228 -879 -1274 1545 A C ATOM 143 O GLU A 22 -23.076 -22.938 10.361 1.00 59.69 A O ANISOU 143 O GLU A 22 10279 7202 5198 -807 -1355 1570 A O ATOM 144 CB GLU A 22 -23.418 -25.287 8.166 1.00 67.19 A C ANISOU 144 CB GLU A 22 11554 7581 6396 -953 -1459 1751 A C ATOM 145 CG GLU A 22 -22.179 -25.646 8.968 1.00 76.56 A C ANISOU 145 CG GLU A 22 12906 8659 7525 -752 -1652 1789 A C ATOM 146 CD GLU A 22 -21.516 -26.916 8.477 1.00 83.88 A C ANISOU 146 CD GLU A 22 14097 9246 8528 -661 -1829 1875 A C ATOM 147 OE1 GLU A 22 -21.780 -27.316 7.322 1.00 86.02 A O ANISOU 147 OE1 GLU A 22 14375 9361 8948 -697 -1804 1847 A O ATOM 148 OE2 GLU A 22 -20.739 -27.518 9.251 1.00 87.92 A O1- ANISOU 148 OE2 GLU A 22 14816 9647 8942 -545 -1998 1968 A O1- ATOM 149 N GLU A 23 -23.637 -22.061 8.368 1.00 55.75 A N ANISOU 149 N GLU A 23 9457 6701 5023 -789 -1181 1368 A N ATOM 150 CA GLU A 23 -22.887 -20.825 8.556 1.00 53.51 A C ANISOU 150 CA GLU A 23 8983 6539 4810 -594 -1180 1186 A C ATOM 151 C GLU A 23 -23.595 -19.829 9.471 1.00 55.42 A C ANISOU 151 C GLU A 23 9095 7070 4891 -662 -1047 1132 A C ATOM 152 O GLU A 23 -22.963 -19.222 10.340 1.00 53.41 A O ANISOU 152 O GLU A 23 8819 6915 4560 -552 -1099 1062 A O ATOM 153 CB GLU A 23 -22.609 -20.171 7.196 1.00 50.77 A C ANISOU 153 CB GLU A 23 8439 6131 4719 -480 -1134 1028 A C ATOM 154 CG GLU A 23 -21.937 -18.804 7.265 1.00 49.90 A C ANISOU 154 CG GLU A 23 8125 6141 4696 -314 -1116 838 A C ATOM 155 CD GLU A 23 -20.466 -18.881 7.640 1.00 53.14 A C ANISOU 155 CD GLU A 23 8586 6464 5140 -124 -1292 797 A C ATOM 156 OE1 GLU A 23 -19.926 -20.008 7.733 1.00 55.72 A O ANISOU 156 OE1 GLU A 23 9103 6625 5444 -86 -1432 910 A O ATOM 157 OE2 GLU A 23 -19.840 -17.815 7.837 1.00 52.04 A O1- ANISOU 157 OE2 GLU A 23 8299 6423 5049 -10 -1297 650 A O1- ATOM 158 N PHE A 24 -24.902 -19.661 9.285 1.00 49.40 A N ANISOU 158 N PHE A 24 8244 6455 4072 -836 -881 1157 A N ATOM 159 CA PHE A 24 -25.624 -18.601 9.983 1.00 52.70 A C ANISOU 159 CA PHE A 24 8503 7161 4360 -867 -738 1072 A C ATOM 160 C PHE A 24 -26.633 -19.089 11.021 1.00 56.48 A C ANISOU 160 C PHE A 24 9072 7827 4562 -1079 -661 1221 A C ATOM 161 O PHE A 24 -27.272 -18.276 11.692 1.00 60.87 A O ANISOU 161 O PHE A 24 9504 8646 4980 -1101 -538 1152 A O ATOM 162 CB PHE A 24 -26.331 -17.703 8.968 1.00 49.14 A C ANISOU 162 CB PHE A 24 7815 6796 4060 -854 -589 940 A C ATOM 163 CG PHE A 24 -25.394 -17.029 8.010 1.00 47.92 A C ANISOU 163 CG PHE A 24 7552 6499 4157 -658 -642 786 A C ATOM 164 CD1 PHE A 24 -24.604 -15.971 8.425 1.00 46.59 A C ANISOU 164 CD1 PHE A 24 7301 6381 4020 -492 -674 633 A C ATOM 165 CD2 PHE A 24 -25.300 -17.456 6.694 1.00 47.34 A C ANISOU 165 CD2 PHE A 24 7463 6247 4278 -652 -659 793 A C ATOM 166 CE1 PHE A 24 -23.738 -15.350 7.546 1.00 47.91 A C ANISOU 166 CE1 PHE A 24 7366 6427 4410 -338 -719 501 A C ATOM 167 CE2 PHE A 24 -24.436 -16.841 5.813 1.00 44.93 A C ANISOU 167 CE2 PHE A 24 7053 5830 4187 -484 -699 659 A C ATOM 168 CZ PHE A 24 -23.650 -15.787 6.240 1.00 45.89 A C ANISOU 168 CZ PHE A 24 7088 6008 4340 -333 -728 519 A C ATOM 169 N GLY A 25 -26.774 -20.404 11.160 1.00 55.59 A N ANISOU 169 N GLY A 25 9180 7581 4360 -1234 -733 1422 A N ATOM 170 CA GLY A 25 -27.601 -20.970 12.214 1.00 57.93 A C ANISOU 170 CA GLY A 25 9593 8041 4375 -1454 -679 1590 A C ATOM 171 C GLY A 25 -29.087 -21.022 11.916 1.00 61.08 A C ANISOU 171 C GLY A 25 9870 8634 4703 -1689 -495 1642 A C ATOM 172 O GLY A 25 -29.889 -21.406 12.767 1.00 58.74 A O ANISOU 172 O GLY A 25 9632 8524 4162 -1895 -421 1775 A O ATOM 173 N ALA A 26 -29.460 -20.635 10.701 1.00 61.69 A N ANISOU 173 N ALA A 26 9770 8684 4984 -1663 -421 1539 A N ATOM 174 CA ALA A 26 -30.858 -20.656 10.298 1.00 60.74 A C ANISOU 174 CA ALA A 26 9505 8759 4814 -1872 -255 1575 A C ATOM 175 C ALA A 26 -30.967 -20.960 8.816 1.00 62.76 A C ANISOU 175 C ALA A 26 9714 8825 5305 -1885 -268 1551 A C ATOM 176 O ALA A 26 -30.023 -20.733 8.062 1.00 64.11 A O ANISOU 176 O ALA A 26 9885 8783 5692 -1685 -362 1448 A O ATOM 177 CB ALA A 26 -31.528 -19.327 10.621 1.00 55.13 A C ANISOU 177 CB ALA A 26 8523 8383 4041 -1794 -87 1417 A C ATOM 178 N GLU A 27 -32.115 -21.488 8.407 1.00 63.75 A N ANISOU 178 N GLU A 27 9798 9045 5379 -2132 -175 1647 A N ATOM 179 CA GLU A 27 -32.412 -21.661 6.993 1.00 62.22 A C ANISOU 179 CA GLU A 27 9524 8731 5386 -2161 -165 1608 A C ATOM 180 C GLU A 27 -32.500 -20.296 6.320 1.00 56.95 A C ANISOU 180 C GLU A 27 8568 8198 4872 -1952 -70 1398 A C ATOM 181 O GLU A 27 -32.949 -19.331 6.935 1.00 57.94 A O ANISOU 181 O GLU A 27 8519 8596 4898 -1890 45 1313 A O ATOM 182 CB GLU A 27 -33.716 -22.443 6.811 1.00 67.15 A C ANISOU 182 CB GLU A 27 10141 9480 5893 -2493 -79 1751 A C ATOM 183 CG GLU A 27 -33.568 -23.947 6.983 1.00 71.65 A C ANISOU 183 CG GLU A 27 11036 9800 6389 -2713 -203 1958 A C ATOM 184 CD GLU A 27 -32.893 -24.601 5.788 1.00 74.26 A C ANISOU 184 CD GLU A 27 11509 9762 6945 -2644 -339 1940 A C ATOM 185 OE1 GLU A 27 -33.029 -24.073 4.663 1.00 76.49 A O ANISOU 185 OE1 GLU A 27 11604 10050 7410 -2549 -295 1807 A O ATOM 186 OE2 GLU A 27 -32.223 -25.639 5.970 1.00 75.12 A O1- ANISOU 186 OE2 GLU A 27 11922 9578 7043 -2672 -491 2058 A O1- ATOM 187 N PRO A 28 -32.057 -20.204 5.059 1.00 52.52 A N ANISOU 187 N PRO A 28 7968 7440 4547 -1835 -121 1314 A N ATOM 188 CA PRO A 28 -32.170 -18.941 4.322 1.00 48.95 A C ANISOU 188 CA PRO A 28 7261 7093 4243 -1652 -36 1132 A C ATOM 189 C PRO A 28 -33.616 -18.647 3.939 1.00 49.54 A C ANISOU 189 C PRO A 28 7118 7441 4262 -1793 120 1129 A C ATOM 190 O PRO A 28 -34.436 -19.564 3.895 1.00 48.74 A O ANISOU 190 O PRO A 28 7064 7393 4061 -2050 145 1265 A O ATOM 191 CB PRO A 28 -31.301 -19.177 3.084 1.00 45.88 A C ANISOU 191 CB PRO A 28 6927 6410 4094 -1531 -143 1081 A C ATOM 192 CG PRO A 28 -31.346 -20.652 2.877 1.00 48.65 A C ANISOU 192 CG PRO A 28 7506 6566 4415 -1726 -234 1240 A C ATOM 193 CD PRO A 28 -31.441 -21.269 4.249 1.00 52.68 A C ANISOU 193 CD PRO A 28 8188 7130 4698 -1864 -259 1382 A C ATOM 194 N GLU A 29 -33.925 -17.384 3.672 1.00 48.98 A N ANISOU 194 N GLU A 29 6815 7544 4253 -1628 218 977 A N ATOM 195 CA GLU A 29 -35.293 -16.997 3.354 1.00 52.32 A C ANISOU 195 CA GLU A 29 7004 8258 4616 -1720 365 960 A C ATOM 196 C GLU A 29 -35.528 -16.895 1.853 1.00 51.80 A C ANISOU 196 C GLU A 29 6827 8111 4743 -1692 364 910 A C ATOM 197 O GLU A 29 -36.627 -17.172 1.374 1.00 52.97 A O ANISOU 197 O GLU A 29 6849 8429 4848 -1856 438 956 A O ATOM 198 CB GLU A 29 -35.643 -15.667 4.022 1.00 55.96 A C ANISOU 198 CB GLU A 29 7279 8984 5001 -1546 479 824 A C ATOM 199 CG GLU A 29 -35.630 -15.715 5.542 1.00 62.45 A C ANISOU 199 CG GLU A 29 8179 9957 5592 -1590 505 866 A C ATOM 200 CD GLU A 29 -36.133 -14.429 6.168 1.00 67.90 A C ANISOU 200 CD GLU A 29 8677 10932 6188 -1425 629 719 A C ATOM 201 OE1 GLU A 29 -35.686 -14.092 7.282 1.00 72.28 A O ANISOU 201 OE1 GLU A 29 9307 11537 6618 -1348 621 682 A O ATOM 202 OE2 GLU A 29 -36.980 -13.756 5.546 1.00 69.24 A O1- ANISOU 202 OE2 GLU A 29 8627 11279 6404 -1363 731 637 A O1- ATOM 203 N LEU A 30 -34.494 -16.492 1.118 1.00 49.43 A N ANISOU 203 N LEU A 30 6566 7569 4646 -1490 280 816 A N ATOM 204 CA LEU A 30 -34.608 -16.253 -0.319 1.00 48.73 A C ANISOU 204 CA LEU A 30 6371 7405 4739 -1431 279 755 A C ATOM 205 C LEU A 30 -33.563 -17.030 -1.113 1.00 45.74 A C ANISOU 205 C LEU A 30 6175 6689 4513 -1413 142 780 A C ATOM 206 O LEU A 30 -32.504 -17.382 -0.589 1.00 43.27 A O ANISOU 206 O LEU A 30 6042 6189 4211 -1352 42 798 A O ATOM 207 CB LEU A 30 -34.461 -14.762 -0.628 1.00 49.93 A C ANISOU 207 CB LEU A 30 6348 7626 4996 -1175 335 593 A C ATOM 208 CG LEU A 30 -34.998 -13.767 0.400 1.00 57.12 A C ANISOU 208 CG LEU A 30 7130 8800 5771 -1086 441 521 A C ATOM 209 CD1 LEU A 30 -34.636 -12.348 0.006 1.00 59.47 A C ANISOU 209 CD1 LEU A 30 7318 9076 6202 -822 462 360 A C ATOM 210 CD2 LEU A 30 -36.496 -13.906 0.555 1.00 59.75 A C ANISOU 210 CD2 LEU A 30 7295 9457 5950 -1241 564 572 A C ATOM 211 N ALA A 31 -33.866 -17.274 -2.384 1.00 44.31 A N ANISOU 211 N ALA A 31 5941 6450 4446 -1454 136 773 A N ATOM 212 CA ALA A 31 -32.921 -17.885 -3.308 1.00 43.00 A C ANISOU 212 CA ALA A 31 5919 5987 4434 -1406 20 768 A C ATOM 213 C ALA A 31 -33.066 -17.288 -4.707 1.00 44.94 A C ANISOU 213 C ALA A 31 6010 6232 4833 -1309 48 677 A C ATOM 214 O ALA A 31 -34.173 -17.073 -5.192 1.00 43.13 A O ANISOU 214 O ALA A 31 5619 6194 4573 -1394 129 679 A O ATOM 215 CB ALA A 31 -33.118 -19.381 -3.357 1.00 43.92 A C ANISOU 215 CB ALA A 31 6233 5968 4486 -1637 -53 900 A C ATOM 216 N VAL A 32 -31.936 -17.013 -5.346 1.00 44.10 A N ANISOU 216 N VAL A 32 5948 5926 4883 -1129 -20 601 A N ATOM 217 CA VAL A 32 -31.931 -16.495 -6.700 1.00 41.02 A C ANISOU 217 CA VAL A 32 5439 5513 4633 -1036 -3 525 A C ATOM 218 C VAL A 32 -30.882 -17.226 -7.525 1.00 42.66 A C ANISOU 218 C VAL A 32 5794 5455 4960 -988 -111 514 A C ATOM 219 O VAL A 32 -29.985 -17.878 -6.982 1.00 40.76 A O ANISOU 219 O VAL A 32 5729 5045 4714 -965 -201 542 A O ATOM 220 CB VAL A 32 -31.647 -14.979 -6.744 1.00 40.80 A C ANISOU 220 CB VAL A 32 5256 5564 4682 -822 55 412 A C ATOM 221 CG1 VAL A 32 -32.767 -14.201 -6.062 1.00 40.27 A C ANISOU 221 CG1 VAL A 32 5030 5770 4500 -837 166 403 A C ATOM 222 CG2 VAL A 32 -30.298 -14.665 -6.105 1.00 40.85 A C ANISOU 222 CG2 VAL A 32 5359 5424 4737 -674 -12 364 A C ATOM 223 N SER A 33 -31.007 -17.129 -8.843 1.00 41.52 A N ANISOU 223 N SER A 33 5577 5285 4913 -964 -104 471 A N ATOM 224 CA SER A 33 -30.003 -17.690 -9.731 1.00 40.96 A C ANISOU 224 CA SER A 33 5619 4988 4954 -890 -193 438 A C ATOM 225 C SER A 33 -29.834 -16.818 -10.958 1.00 39.66 A C ANISOU 225 C SER A 33 5309 4851 4911 -761 -155 351 A C ATOM 226 O SER A 33 -30.754 -16.108 -11.362 1.00 38.86 A O ANISOU 226 O SER A 33 5045 4923 4799 -778 -74 340 A O ATOM 227 CB SER A 33 -30.369 -19.116 -10.139 1.00 42.58 A C ANISOU 227 CB SER A 33 5984 5078 5117 -1071 -257 507 A C ATOM 228 OG SER A 33 -31.626 -19.152 -10.779 1.00 42.56 A O ANISOU 228 OG SER A 33 5869 5230 5073 -1224 -196 529 A O ATOM 229 N ALA A 34 -28.638 -16.861 -11.528 1.00 38.64 A N ANISOU 229 N ALA A 34 5235 4557 4888 -625 -214 294 A N ATOM 230 CA ALA A 34 -28.334 -16.137 -12.749 1.00 34.69 A C ANISOU 230 CA ALA A 34 4620 4064 4496 -512 -185 222 A C ATOM 231 C ALA A 34 -27.286 -16.930 -13.512 1.00 37.92 A C ANISOU 231 C ALA A 34 5146 4285 4978 -449 -267 187 A C ATOM 232 O ALA A 34 -26.318 -17.417 -12.923 1.00 39.49 A O ANISOU 232 O ALA A 34 5462 4355 5186 -384 -340 182 A O ATOM 233 CB ALA A 34 -27.847 -14.734 -12.445 1.00 31.11 A C ANISOU 233 CB ALA A 34 4047 3674 4100 -362 -137 164 A C ATOM 234 N PRO A 35 -27.489 -17.087 -14.824 1.00 38.39 A N ANISOU 234 N PRO A 35 5171 4339 5078 -459 -258 158 A N ATOM 235 CA PRO A 35 -26.604 -17.933 -15.624 1.00 34.03 A C ANISOU 235 CA PRO A 35 4733 3622 4577 -399 -331 114 A C ATOM 236 C PRO A 35 -25.399 -17.196 -16.194 1.00 32.32 A C ANISOU 236 C PRO A 35 4435 3384 4462 -215 -323 35 A C ATOM 237 O PRO A 35 -25.378 -15.964 -16.266 1.00 26.78 A O ANISOU 237 O PRO A 35 3585 2788 3800 -155 -255 16 A O ATOM 238 CB PRO A 35 -27.521 -18.403 -16.752 1.00 34.08 A C ANISOU 238 CB PRO A 35 4730 3662 4557 -517 -319 117 A C ATOM 239 CG PRO A 35 -28.442 -17.250 -16.955 1.00 34.43 A C ANISOU 239 CG PRO A 35 4579 3911 4593 -537 -224 130 A C ATOM 240 CD PRO A 35 -28.666 -16.640 -15.593 1.00 37.05 A C ANISOU 240 CD PRO A 35 4868 4325 4886 -538 -188 169 A C ATOM 241 N GLY A 36 -24.395 -17.968 -16.589 1.00 32.92 A N ANISOU 241 N GLY A 36 4613 3321 4575 -128 -394 -11 A N ATOM 242 CA GLY A 36 -23.343 -17.464 -17.448 1.00 35.23 A C ANISOU 242 CA GLY A 36 4819 3616 4951 20 -380 -90 A C ATOM 243 C GLY A 36 -23.861 -17.487 -18.878 1.00 35.19 A C ANISOU 243 C GLY A 36 4765 3656 4949 -16 -340 -115 A C ATOM 244 O GLY A 36 -25.046 -17.713 -19.119 1.00 33.56 A O ANISOU 244 O GLY A 36 4566 3498 4686 -152 -321 -73 A O ATOM 245 N ARG A 37 -22.974 -17.268 -19.835 1.00 33.75 A N ANISOU 245 N ARG A 37 4526 3475 4821 99 -328 -184 A N ATOM 246 CA ARG A 37 -23.391 -17.104 -21.219 1.00 33.55 A C ANISOU 246 CA ARG A 37 4437 3519 4791 77 -282 -209 A C ATOM 247 C ARG A 37 -22.389 -17.689 -22.200 1.00 30.25 A C ANISOU 247 C ARG A 37 4056 3044 4395 190 -310 -295 A C ATOM 248 O ARG A 37 -21.209 -17.845 -21.887 1.00 31.11 A O ANISOU 248 O ARG A 37 4177 3100 4543 316 -344 -341 A O ATOM 249 CB ARG A 37 -23.565 -15.627 -21.549 1.00 33.61 A C ANISOU 249 CB ARG A 37 4269 3668 4834 94 -193 -190 A C ATOM 250 CG ARG A 37 -22.203 -15.016 -21.744 1.00 39.37 A C ANISOU 250 CG ARG A 37 4924 4402 5632 226 -177 -240 A C ATOM 251 CD ARG A 37 -22.097 -14.029 -22.864 1.00 41.20 A C ANISOU 251 CD ARG A 37 5030 4737 5888 250 -103 -246 A C ATOM 252 NE ARG A 37 -20.774 -14.157 -23.465 1.00 49.68 A N ANISOU 252 NE ARG A 37 6074 5807 6996 355 -104 -314 A N ATOM 253 CZ ARG A 37 -19.630 -13.784 -22.902 1.00 56.13 A C ANISOU 253 CZ ARG A 37 6841 6619 7865 432 -113 -343 A C ATOM 254 NH1 ARG A 37 -18.493 -13.961 -23.536 1.00 63.27 A N1+ ANISOU 254 NH1 ARG A 37 7699 7553 8789 524 -109 -408 A N1+ ATOM 255 NH2 ARG A 37 -19.607 -13.236 -21.712 1.00 63.37 A N ANISOU 255 NH2 ARG A 37 7749 7521 8809 417 -124 -312 A N ATOM 256 N VAL A 38 -22.870 -17.998 -23.400 1.00 32.94 A N ANISOU 256 N VAL A 38 4403 3413 4701 149 -295 -323 A N ATOM 257 CA VAL A 38 -21.987 -18.166 -24.540 1.00 30.03 A C ANISOU 257 CA VAL A 38 4012 3054 4344 264 -286 -409 A C ATOM 258 C VAL A 38 -22.522 -17.266 -25.641 1.00 33.84 A C ANISOU 258 C VAL A 38 4361 3686 4810 223 -205 -393 A C ATOM 259 O VAL A 38 -23.736 -17.172 -25.848 1.00 34.94 A O ANISOU 259 O VAL A 38 4491 3878 4905 100 -193 -343 A O ATOM 260 CB VAL A 38 -21.887 -19.643 -25.006 1.00 31.55 A C ANISOU 260 CB VAL A 38 4387 3108 4493 281 -367 -481 A C ATOM 261 CG1 VAL A 38 -23.193 -20.134 -25.647 1.00 30.24 A C ANISOU 261 CG1 VAL A 38 4287 2946 4256 120 -378 -463 A C ATOM 262 CG2 VAL A 38 -20.706 -19.821 -25.950 1.00 31.71 A C ANISOU 262 CG2 VAL A 38 4378 3146 4525 448 -358 -588 A C ATOM 263 N ASN A 39 -21.623 -16.563 -26.318 1.00 39.72 A N ANISOU 263 N ASN A 39 4992 4512 5586 322 -150 -428 A N ATOM 264 CA ASN A 39 -22.022 -15.767 -27.474 1.00 38.67 A C ANISOU 264 CA ASN A 39 4754 4513 5427 293 -79 -408 A C ATOM 265 C ASN A 39 -21.912 -16.582 -28.760 1.00 38.26 A C ANISOU 265 C ASN A 39 4755 4471 5310 319 -91 -487 A C ATOM 266 O ASN A 39 -20.815 -16.961 -29.162 1.00 41.76 A O ANISOU 266 O ASN A 39 5204 4905 5759 435 -92 -570 A O ATOM 267 CB ASN A 39 -21.168 -14.501 -27.575 1.00 36.76 A C ANISOU 267 CB ASN A 39 4370 4359 5239 357 -8 -388 A C ATOM 268 CG ASN A 39 -21.808 -13.441 -28.445 1.00 35.31 A C ANISOU 268 CG ASN A 39 4091 4295 5032 308 60 -326 A C ATOM 269 ND2 ASN A 39 -21.033 -12.424 -28.818 1.00 33.08 A N ANISOU 269 ND2 ASN A 39 3707 4083 4781 347 122 -309 A N ATOM 270 OD1 ASN A 39 -22.991 -13.528 -28.770 1.00 34.64 A O ANISOU 270 OD1 ASN A 39 4024 4242 4896 230 52 -288 A O ATOM 271 N LEU A 40 -23.047 -16.860 -29.398 1.00 40.75 A N ANISOU 271 N LEU A 40 5104 4821 5559 215 -102 -471 A N ATOM 272 CA LEU A 40 -23.051 -17.615 -30.659 1.00 40.54 A C ANISOU 272 CA LEU A 40 5138 4810 5457 226 -118 -553 A C ATOM 273 C LEU A 40 -22.316 -16.871 -31.776 1.00 37.81 A C ANISOU 273 C LEU A 40 4672 4602 5092 312 -40 -577 A C ATOM 274 O LEU A 40 -21.523 -17.466 -32.505 1.00 37.01 A O ANISOU 274 O LEU A 40 4604 4502 4955 405 -40 -677 A O ATOM 275 CB LEU A 40 -24.480 -17.930 -31.103 1.00 39.41 A C ANISOU 275 CB LEU A 40 5031 4703 5239 76 -148 -523 A C ATOM 276 CG LEU A 40 -25.353 -18.705 -30.112 1.00 38.61 A C ANISOU 276 CG LEU A 40 5043 4492 5134 -51 -220 -491 A C ATOM 277 CD1 LEU A 40 -26.637 -19.170 -30.788 1.00 37.57 A C ANISOU 277 CD1 LEU A 40 4943 4418 4915 -207 -255 -486 A C ATOM 278 CD2 LEU A 40 -24.591 -19.888 -29.540 1.00 38.01 A C ANISOU 278 CD2 LEU A 40 5142 4222 5079 6 -293 -563 A C ATOM 279 N ILE A 41 -22.581 -15.572 -31.899 1.00 34.49 A N ANISOU 279 N ILE A 41 4120 4296 4689 282 27 -484 A N ATOM 280 CA ILE A 41 -21.898 -14.729 -32.877 1.00 33.72 A C ANISOU 280 CA ILE A 41 3913 4329 4572 338 106 -478 A C ATOM 281 C ILE A 41 -22.145 -13.252 -32.557 1.00 34.42 A C ANISOU 281 C ILE A 41 3892 4478 4708 304 162 -359 A C ATOM 282 O ILE A 41 -23.146 -12.905 -31.919 1.00 33.91 A O ANISOU 282 O ILE A 41 3828 4392 4662 239 142 -288 A O ATOM 283 CB ILE A 41 -22.363 -15.046 -34.336 1.00 38.29 A C ANISOU 283 CB ILE A 41 4506 5007 5036 315 114 -513 A C ATOM 284 CG1 ILE A 41 -21.316 -14.592 -35.352 1.00 37.27 A C ANISOU 284 CG1 ILE A 41 4293 5000 4867 394 191 -543 A C ATOM 285 CG2 ILE A 41 -23.711 -14.413 -34.634 1.00 28.73 A C ANISOU 285 CG2 ILE A 41 3257 3875 3784 213 114 -414 A C ATOM 286 CD1 ILE A 41 -21.598 -15.058 -36.762 1.00 42.66 A C ANISOU 286 CD1 ILE A 41 5005 5782 5421 390 196 -601 A C ATOM 287 N GLY A 42 -21.235 -12.389 -33.005 1.00 33.57 A N ANISOU 287 N GLY A 42 3693 4448 4616 348 232 -339 A N ATOM 288 CA GLY A 42 -21.327 -10.966 -32.737 1.00 31.28 A C ANISOU 288 CA GLY A 42 3326 4187 4374 318 279 -232 A C ATOM 289 C GLY A 42 -20.329 -10.521 -31.683 1.00 35.14 A C ANISOU 289 C GLY A 42 3777 4615 4960 348 289 -237 A C ATOM 290 O GLY A 42 -20.706 -9.961 -30.651 1.00 34.67 A O ANISOU 290 O GLY A 42 3722 4488 4963 323 273 -187 A O ATOM 291 N GLU A 43 -19.049 -10.761 -31.950 1.00 38.10 A N ANISOU 291 N GLU A 43 4106 5030 5339 404 316 -303 A N ATOM 292 CA GLU A 43 -18.000 -10.500 -30.973 1.00 38.09 A C ANISOU 292 CA GLU A 43 4057 4992 5422 435 313 -325 A C ATOM 293 C GLU A 43 -17.397 -9.108 -31.120 1.00 38.82 A C ANISOU 293 C GLU A 43 4053 5148 5549 386 381 -253 A C ATOM 294 O GLU A 43 -17.127 -8.647 -32.236 1.00 39.06 A O ANISOU 294 O GLU A 43 4030 5286 5524 361 445 -223 A O ATOM 295 CB GLU A 43 -16.895 -11.549 -31.091 1.00 39.88 A C ANISOU 295 CB GLU A 43 4272 5243 5636 535 295 -444 A C ATOM 296 CG GLU A 43 -16.431 -12.112 -29.758 1.00 35.85 A C ANISOU 296 CG GLU A 43 3798 4629 5194 592 223 -492 A C ATOM 297 CD GLU A 43 -17.534 -12.846 -29.027 1.00 33.92 A C ANISOU 297 CD GLU A 43 3691 4249 4949 567 148 -481 A C ATOM 298 OE1 GLU A 43 -17.705 -14.049 -29.284 1.00 35.96 A O ANISOU 298 OE1 GLU A 43 4047 4455 5163 612 98 -549 A O ATOM 299 OE2 GLU A 43 -18.237 -12.222 -28.202 1.00 34.03 A O1- ANISOU 299 OE2 GLU A 43 3719 4211 5000 497 138 -406 A O1- ATOM 300 N HIS A 44 -17.175 -8.464 -29.977 1.00 36.08 A N ANISOU 300 N HIS A 44 3695 4729 5285 362 362 -227 A N ATOM 301 CA HIS A 44 -16.616 -7.117 -29.899 1.00 35.65 A C ANISOU 301 CA HIS A 44 3574 4695 5276 296 410 -162 A C ATOM 302 C HIS A 44 -17.447 -6.116 -30.695 1.00 36.35 A C ANISOU 302 C HIS A 44 3687 4795 5330 235 454 -53 A C ATOM 303 O HIS A 44 -16.919 -5.167 -31.286 1.00 32.28 A O ANISOU 303 O HIS A 44 3125 4330 4809 174 511 8 A O ATOM 304 CB HIS A 44 -15.158 -7.113 -30.356 1.00 36.21 A C ANISOU 304 CB HIS A 44 3532 4885 5342 300 456 -209 A C ATOM 305 CG HIS A 44 -14.221 -7.704 -29.346 1.00 41.17 A C ANISOU 305 CG HIS A 44 4118 5500 6024 361 405 -298 A C ATOM 306 CD2 HIS A 44 -13.628 -8.920 -29.285 1.00 42.37 A C ANISOU 306 CD2 HIS A 44 4256 5686 6158 471 369 -403 A C ATOM 307 ND1 HIS A 44 -13.822 -7.024 -28.216 1.00 40.13 A N ANISOU 307 ND1 HIS A 44 3966 5311 5970 319 377 -286 A N ATOM 308 CE1 HIS A 44 -13.014 -7.793 -27.506 1.00 38.91 A C ANISOU 308 CE1 HIS A 44 3774 5170 5840 397 324 -373 A C ATOM 309 NE2 HIS A 44 -12.881 -8.948 -28.132 1.00 39.68 A N ANISOU 309 NE2 HIS A 44 3878 5318 5883 498 318 -443 A N ATOM 310 N THR A 45 -18.759 -6.336 -30.672 1.00 33.76 A N ANISOU 310 N THR A 45 3430 4421 4974 249 421 -24 A N ATOM 311 CA THR A 45 -19.718 -5.417 -31.259 1.00 37.62 A C ANISOU 311 CA THR A 45 3947 4914 5432 219 442 80 A C ATOM 312 C THR A 45 -20.538 -4.669 -30.204 1.00 39.10 A C ANISOU 312 C THR A 45 4182 4996 5679 221 411 125 A C ATOM 313 O THR A 45 -20.970 -3.545 -30.445 1.00 42.09 A O ANISOU 313 O THR A 45 4583 5349 6061 208 429 212 A O ATOM 314 CB THR A 45 -20.693 -6.148 -32.195 1.00 36.51 A C ANISOU 314 CB THR A 45 3832 4843 5197 238 430 80 A C ATOM 315 CG2 THR A 45 -19.968 -6.658 -33.431 1.00 37.45 A C ANISOU 315 CG2 THR A 45 3913 5079 5237 241 471 43 A C ATOM 316 OG1 THR A 45 -21.274 -7.258 -31.502 1.00 36.64 A O ANISOU 316 OG1 THR A 45 3890 4816 5215 263 369 12 A O ATOM 317 N ASP A 46 -20.752 -5.277 -29.039 1.00 37.93 A N ANISOU 317 N ASP A 46 4057 4786 5568 245 363 67 A N ATOM 318 CA ASP A 46 -21.697 -4.703 -28.077 1.00 39.51 A C ANISOU 318 CA ASP A 46 4297 4916 5800 258 337 99 A C ATOM 319 C ASP A 46 -21.297 -3.299 -27.600 1.00 39.99 A C ANISOU 319 C ASP A 46 4371 4899 5925 242 355 141 A C ATOM 320 O ASP A 46 -22.164 -2.432 -27.474 1.00 40.91 A O ANISOU 320 O ASP A 46 4523 4976 6043 268 354 198 A O ATOM 321 CB ASP A 46 -21.920 -5.651 -26.880 1.00 36.24 A C ANISOU 321 CB ASP A 46 3909 4462 5399 273 287 33 A C ATOM 322 CG ASP A 46 -20.689 -5.841 -26.005 1.00 36.57 A C ANISOU 322 CG ASP A 46 3942 4455 5500 273 268 -30 A C ATOM 323 OD1 ASP A 46 -19.552 -5.552 -26.434 1.00 34.33 A O ANISOU 323 OD1 ASP A 46 3611 4194 5239 258 294 -43 A O ATOM 324 OD2 ASP A 46 -20.880 -6.310 -24.863 1.00 38.96 A O1- ANISOU 324 OD2 ASP A 46 4277 4710 5815 284 225 -65 A O1- ATOM 325 N TYR A 47 -20.006 -3.046 -27.385 1.00 37.39 A N ANISOU 325 N TYR A 47 4013 4549 5643 201 368 112 A N ATOM 326 CA TYR A 47 -19.579 -1.693 -27.004 1.00 37.26 A C ANISOU 326 CA TYR A 47 4023 4449 5686 159 379 151 A C ATOM 327 C TYR A 47 -19.420 -0.794 -28.224 1.00 38.98 A C ANISOU 327 C TYR A 47 4247 4684 5879 110 428 244 A C ATOM 328 O TYR A 47 -19.039 0.369 -28.106 1.00 36.68 A O ANISOU 328 O TYR A 47 3997 4311 5630 55 439 290 A O ATOM 329 CB TYR A 47 -18.272 -1.716 -26.196 1.00 38.55 A C ANISOU 329 CB TYR A 47 4145 4594 5908 113 365 84 A C ATOM 330 CG TYR A 47 -17.104 -2.460 -26.819 1.00 36.27 A C ANISOU 330 CG TYR A 47 3762 4416 5601 89 387 41 A C ATOM 331 CD1 TYR A 47 -16.372 -1.909 -27.868 1.00 35.62 A C ANISOU 331 CD1 TYR A 47 3630 4403 5501 17 445 88 A C ATOM 332 CD2 TYR A 47 -16.712 -3.697 -26.330 1.00 33.35 A C ANISOU 332 CD2 TYR A 47 3357 4087 5227 144 349 -48 A C ATOM 333 CE1 TYR A 47 -15.301 -2.584 -28.423 1.00 35.10 A C ANISOU 333 CE1 TYR A 47 3460 4468 5409 8 473 39 A C ATOM 334 CE2 TYR A 47 -15.636 -4.377 -26.877 1.00 33.45 A C ANISOU 334 CE2 TYR A 47 3281 4208 5222 153 366 -100 A C ATOM 335 CZ TYR A 47 -14.938 -3.818 -27.921 1.00 35.17 A C ANISOU 335 CZ TYR A 47 3428 4516 5417 89 432 -62 A C ATOM 336 OH TYR A 47 -13.868 -4.495 -28.463 1.00 37.95 A O ANISOU 336 OH TYR A 47 3674 5004 5741 111 457 -124 A O ATOM 337 N ASN A 48 -19.709 -1.346 -29.397 1.00 42.66 A N ANISOU 337 N ASN A 48 4685 5253 6269 123 453 271 A N ATOM 338 CA ASN A 48 -19.715 -0.575 -30.633 1.00 41.35 A C ANISOU 338 CA ASN A 48 4536 5121 6055 84 497 373 A C ATOM 339 C ASN A 48 -21.145 -0.321 -31.089 1.00 39.42 A C ANISOU 339 C ASN A 48 4346 4874 5759 154 478 443 A C ATOM 340 O ASN A 48 -21.383 0.088 -32.223 1.00 36.81 A O ANISOU 340 O ASN A 48 4031 4592 5363 145 502 530 A O ATOM 341 CB ASN A 48 -18.921 -1.302 -31.719 1.00 40.68 A C ANISOU 341 CB ASN A 48 4373 5182 5903 49 543 353 A C ATOM 342 CG ASN A 48 -17.420 -1.174 -31.526 1.00 38.81 A C ANISOU 342 CG ASN A 48 4063 4978 5705 -30 576 314 A C ATOM 343 ND2 ASN A 48 -16.731 -2.307 -31.427 1.00 36.99 A N ANISOU 343 ND2 ASN A 48 3753 4838 5466 3 575 210 A N ATOM 344 OD1 ASN A 48 -16.887 -0.068 -31.467 1.00 39.19 A O ANISOU 344 OD1 ASN A 48 4129 4971 5790 -120 598 377 A O ATOM 345 N GLN A 49 -22.085 -0.560 -30.177 1.00 41.27 A N ANISOU 345 N GLN A 49 4599 5066 6015 225 434 405 A N ATOM 346 CA GLN A 49 -23.514 -0.416 -30.436 1.00 42.17 A C ANISOU 346 CA GLN A 49 4735 5206 6080 303 409 454 A C ATOM 347 C GLN A 49 -23.948 -1.289 -31.604 1.00 40.59 A C ANISOU 347 C GLN A 49 4492 5148 5783 304 413 464 A C ATOM 348 O GLN A 49 -24.756 -0.878 -32.442 1.00 43.19 A O ANISOU 348 O GLN A 49 4834 5529 6049 341 406 543 A O ATOM 349 CB GLN A 49 -23.876 1.052 -30.693 1.00 46.25 A C ANISOU 349 CB GLN A 49 5330 5634 6609 336 410 558 A C ATOM 350 CG GLN A 49 -23.636 1.947 -29.490 1.00 49.19 A C ANISOU 350 CG GLN A 49 5767 5850 7071 347 395 536 A C ATOM 351 CD GLN A 49 -24.168 3.351 -29.683 1.00 54.53 A C ANISOU 351 CD GLN A 49 6549 6414 7757 407 382 628 A C ATOM 352 NE2 GLN A 49 -23.492 4.325 -29.085 1.00 57.12 A N ANISOU 352 NE2 GLN A 49 6962 6583 8158 364 380 630 A N ATOM 353 OE1 GLN A 49 -25.173 3.560 -30.364 1.00 56.25 A O ANISOU 353 OE1 GLN A 49 6776 6681 7914 493 367 697 A O ATOM 354 N GLY A 50 -23.412 -2.505 -31.639 1.00 37.71 A N ANISOU 354 N GLY A 50 4083 4843 5402 271 415 378 A N ATOM 355 CA GLY A 50 -23.688 -3.435 -32.716 1.00 38.00 A C ANISOU 355 CA GLY A 50 4092 5003 5343 265 414 362 A C ATOM 356 C GLY A 50 -24.758 -4.442 -32.358 1.00 39.26 A C ANISOU 356 C GLY A 50 4243 5202 5470 284 364 310 A C ATOM 357 O GLY A 50 -25.659 -4.154 -31.570 1.00 44.31 A O ANISOU 357 O GLY A 50 4887 5813 6134 316 337 326 A O ATOM 358 N LEU A 51 -24.662 -5.628 -32.944 1.00 38.15 A N ANISOU 358 N LEU A 51 4094 5132 5269 260 353 245 A N ATOM 359 CA LEU A 51 -25.622 -6.692 -32.689 1.00 36.07 A C ANISOU 359 CA LEU A 51 3837 4902 4967 245 302 195 A C ATOM 360 C LEU A 51 -24.910 -7.883 -32.067 1.00 34.77 A C ANISOU 360 C LEU A 51 3703 4675 4832 226 282 90 A C ATOM 361 O LEU A 51 -23.788 -8.205 -32.445 1.00 35.12 A O ANISOU 361 O LEU A 51 3749 4715 4879 236 305 40 A O ATOM 362 CB LEU A 51 -26.326 -7.117 -33.982 1.00 38.13 A C ANISOU 362 CB LEU A 51 4087 5289 5114 228 286 207 A C ATOM 363 CG LEU A 51 -27.167 -6.107 -34.766 1.00 37.08 A C ANISOU 363 CG LEU A 51 3924 5240 4923 259 287 314 A C ATOM 364 CD1 LEU A 51 -27.559 -6.697 -36.117 1.00 37.74 A C ANISOU 364 CD1 LEU A 51 4001 5457 4882 234 270 306 A C ATOM 365 CD2 LEU A 51 -28.413 -5.696 -33.993 1.00 33.69 A C ANISOU 365 CD2 LEU A 51 3466 4822 4514 290 252 355 A C ATOM 366 N VAL A 52 -25.545 -8.532 -31.101 1.00 33.35 A N ANISOU 366 N VAL A 52 3548 4455 4668 204 237 60 A N ATOM 367 CA VAL A 52 -24.973 -9.750 -30.542 1.00 32.70 A C ANISOU 367 CA VAL A 52 3522 4299 4603 189 203 -29 A C ATOM 368 C VAL A 52 -26.041 -10.831 -30.478 1.00 34.54 A C ANISOU 368 C VAL A 52 3798 4549 4775 122 148 -54 A C ATOM 369 O VAL A 52 -27.243 -10.538 -30.466 1.00 32.99 A O ANISOU 369 O VAL A 52 3564 4428 4544 86 137 -1 A O ATOM 370 CB VAL A 52 -24.367 -9.524 -29.134 1.00 35.46 A C ANISOU 370 CB VAL A 52 3884 4547 5041 210 199 -42 A C ATOM 371 CG1 VAL A 52 -23.222 -8.518 -29.193 1.00 38.21 A C ANISOU 371 CG1 VAL A 52 4191 4880 5449 250 247 -27 A C ATOM 372 CG2 VAL A 52 -25.430 -9.086 -28.128 1.00 30.69 A C ANISOU 372 CG2 VAL A 52 3271 3938 4450 190 186 5 A C ATOM 373 N LEU A 53 -25.603 -12.084 -30.460 1.00 34.09 A N ANISOU 373 N LEU A 53 3820 4428 4703 106 108 -136 A N ATOM 374 CA LEU A 53 -26.536 -13.198 -30.378 1.00 34.03 A C ANISOU 374 CA LEU A 53 3880 4411 4639 16 47 -162 A C ATOM 375 C LEU A 53 -26.053 -14.240 -29.363 1.00 36.26 A C ANISOU 375 C LEU A 53 4272 4551 4956 5 -3 -216 A C ATOM 376 O LEU A 53 -25.582 -15.314 -29.736 1.00 35.46 A O ANISOU 376 O LEU A 53 4268 4377 4829 12 -44 -294 A O ATOM 377 CB LEU A 53 -26.724 -13.830 -31.758 1.00 31.19 A C ANISOU 377 CB LEU A 53 3548 4114 4190 -9 29 -210 A C ATOM 378 CG LEU A 53 -27.823 -14.883 -31.916 1.00 32.17 A C ANISOU 378 CG LEU A 53 3735 4249 4239 -132 -38 -234 A C ATOM 379 CD1 LEU A 53 -29.220 -14.290 -31.714 1.00 31.68 A C ANISOU 379 CD1 LEU A 53 3577 4314 4147 -209 -39 -148 A C ATOM 380 CD2 LEU A 53 -27.717 -15.544 -33.269 1.00 30.00 A C ANISOU 380 CD2 LEU A 53 3509 4013 3878 -139 -59 -308 A C ATOM 381 N PRO A 54 -26.149 -13.912 -28.067 1.00 36.51 A N ANISOU 381 N PRO A 54 4296 4538 5039 -2 -3 -176 A N ATOM 382 CA PRO A 54 -25.756 -14.889 -27.054 1.00 38.46 A C ANISOU 382 CA PRO A 54 4656 4652 5306 -16 -58 -210 A C ATOM 383 C PRO A 54 -26.930 -15.751 -26.625 1.00 38.50 A C ANISOU 383 C PRO A 54 4731 4644 5251 -155 -107 -186 A C ATOM 384 O PRO A 54 -28.073 -15.414 -26.927 1.00 37.84 A O ANISOU 384 O PRO A 54 4575 4682 5121 -235 -92 -140 A O ATOM 385 CB PRO A 54 -25.284 -14.007 -25.901 1.00 36.86 A C ANISOU 385 CB PRO A 54 4403 4428 5173 39 -30 -175 A C ATOM 386 CG PRO A 54 -26.197 -12.820 -25.986 1.00 37.27 A C ANISOU 386 CG PRO A 54 4344 4599 5219 19 22 -105 A C ATOM 387 CD PRO A 54 -26.427 -12.592 -27.469 1.00 37.44 A C ANISOU 387 CD PRO A 54 4315 4710 5198 25 45 -105 A C ATOM 388 N MET A 55 -26.646 -16.852 -25.938 1.00 39.31 A N ANISOU 388 N MET A 55 4975 4609 5352 -186 -171 -214 A N ATOM 389 CA MET A 55 -27.684 -17.597 -25.238 1.00 38.67 A C ANISOU 389 CA MET A 55 4969 4506 5218 -341 -214 -172 A C ATOM 390 C MET A 55 -27.217 -17.841 -23.802 1.00 41.30 A C ANISOU 390 C MET A 55 5381 4731 5582 -326 -241 -147 A C ATOM 391 O MET A 55 -26.020 -17.884 -23.532 1.00 43.81 A O ANISOU 391 O MET A 55 5740 4953 5954 -199 -256 -188 A O ATOM 392 CB MET A 55 -28.004 -18.916 -25.953 1.00 36.11 A C ANISOU 392 CB MET A 55 4787 4103 4832 -440 -284 -221 A C ATOM 393 CG MET A 55 -26.929 -19.979 -25.846 1.00 39.76 A C ANISOU 393 CG MET A 55 5431 4363 5315 -362 -353 -294 A C ATOM 394 SD MET A 55 -27.408 -21.503 -26.689 1.00 43.49 A S ANISOU 394 SD MET A 55 6100 4717 5709 -485 -443 -362 A S ATOM 395 CE MET A 55 -26.162 -22.646 -26.122 1.00 34.33 A C ANISOU 395 CE MET A 55 5170 3293 4583 -361 -531 -428 A C ATOM 396 N ALA A 56 -28.158 -17.970 -22.877 1.00 41.94 A N ANISOU 396 N ALA A 56 5468 4848 5620 -454 -244 -79 A N ATOM 397 CA ALA A 56 -27.815 -18.264 -21.491 1.00 41.13 A C ANISOU 397 CA ALA A 56 5453 4653 5523 -457 -273 -47 A C ATOM 398 C ALA A 56 -27.530 -19.753 -21.327 1.00 45.10 A C ANISOU 398 C ALA A 56 6175 4966 5996 -515 -368 -64 A C ATOM 399 O ALA A 56 -28.162 -20.587 -21.979 1.00 44.66 A O ANISOU 399 O ALA A 56 6201 4879 5888 -638 -407 -74 A O ATOM 400 CB ALA A 56 -28.932 -17.827 -20.559 1.00 37.72 A C ANISOU 400 CB ALA A 56 4942 4351 5039 -571 -233 33 A C ATOM 401 N LEU A 57 -26.577 -20.079 -20.457 1.00 47.04 A N ANISOU 401 N LEU A 57 6524 5079 6271 -424 -415 -68 A N ATOM 402 CA LEU A 57 -26.178 -21.466 -20.230 1.00 48.26 A C ANISOU 402 CA LEU A 57 6910 5023 6401 -441 -517 -82 A C ATOM 403 C LEU A 57 -26.870 -22.083 -19.025 1.00 53.52 A C ANISOU 403 C LEU A 57 7699 5637 6998 -605 -556 13 A C ATOM 404 O LEU A 57 -27.406 -21.378 -18.170 1.00 54.53 A O ANISOU 404 O LEU A 57 7721 5897 7102 -663 -500 80 A O ATOM 405 CB LEU A 57 -24.664 -21.566 -20.035 1.00 43.87 A C ANISOU 405 CB LEU A 57 6405 4353 5910 -225 -560 -144 A C ATOM 406 CG LEU A 57 -23.762 -21.069 -21.162 1.00 41.60 A C ANISOU 406 CG LEU A 57 6006 4115 5684 -57 -524 -241 A C ATOM 407 CD1 LEU A 57 -22.297 -21.258 -20.789 1.00 40.37 A C ANISOU 407 CD1 LEU A 57 5889 3869 5581 144 -574 -297 A C ATOM 408 CD2 LEU A 57 -24.087 -21.784 -22.449 1.00 40.06 A C ANISOU 408 CD2 LEU A 57 5883 3881 5457 -96 -544 -304 A C ATOM 409 N GLU A 58 -26.838 -23.410 -18.957 1.00 58.42 A N ANISOU 409 N GLU A 58 8555 6061 7580 -676 -653 19 A N ATOM 410 CA GLU A 58 -27.284 -24.127 -17.767 1.00 60.66 A C ANISOU 410 CA GLU A 58 8999 6257 7792 -826 -704 119 A C ATOM 411 C GLU A 58 -26.301 -23.922 -16.618 1.00 56.60 A C ANISOU 411 C GLU A 58 8521 5684 7302 -674 -732 142 A C ATOM 412 O GLU A 58 -26.642 -24.135 -15.456 1.00 61.28 A O ANISOU 412 O GLU A 58 9188 6267 7830 -776 -749 237 A O ATOM 413 CB GLU A 58 -27.462 -25.615 -18.068 1.00 65.26 A C ANISOU 413 CB GLU A 58 9856 6612 8328 -943 -812 120 A C ATOM 414 CG GLU A 58 -28.795 -25.939 -18.724 1.00 71.00 A C ANISOU 414 CG GLU A 58 10570 7418 8990 -1198 -794 142 A C ATOM 415 CD GLU A 58 -28.832 -27.328 -19.330 1.00 79.83 A C ANISOU 415 CD GLU A 58 11960 8294 10078 -1291 -905 105 A C ATOM 416 OE1 GLU A 58 -27.797 -27.771 -19.873 1.00 82.56 A O ANISOU 416 OE1 GLU A 58 12428 8465 10476 -1091 -968 6 A O ATOM 417 OE2 GLU A 58 -29.899 -27.975 -19.267 1.00 83.90 A O1- ANISOU 417 OE2 GLU A 58 12565 8800 10513 -1565 -931 168 A O1- ATOM 418 N LEU A 59 -25.082 -23.505 -16.946 1.00 50.08 A N ANISOU 418 N LEU A 59 7633 4835 6560 -437 -738 56 A N ATOM 419 CA LEU A 59 -24.120 -23.086 -15.933 1.00 45.68 A C ANISOU 419 CA LEU A 59 7053 4272 6031 -285 -757 65 A C ATOM 420 C LEU A 59 -24.608 -21.789 -15.291 1.00 44.75 A C ANISOU 420 C LEU A 59 6729 4369 5907 -329 -656 106 A C ATOM 421 O LEU A 59 -24.954 -20.833 -15.994 1.00 44.07 A O ANISOU 421 O LEU A 59 6453 4435 5856 -325 -566 72 A O ATOM 422 CB LEU A 59 -22.730 -22.900 -16.544 1.00 43.70 A C ANISOU 422 CB LEU A 59 6751 3985 5868 -38 -780 -45 A C ATOM 423 CG LEU A 59 -22.162 -24.132 -17.254 1.00 45.73 A C ANISOU 423 CG LEU A 59 7203 4041 6131 53 -877 -112 A C ATOM 424 CD1 LEU A 59 -20.836 -23.818 -17.931 1.00 46.40 A C ANISOU 424 CD1 LEU A 59 7183 4152 6294 301 -876 -229 A C ATOM 425 CD2 LEU A 59 -22.004 -25.274 -16.269 1.00 43.49 A C ANISOU 425 CD2 LEU A 59 7182 3547 5794 41 -999 -48 A C ATOM 426 N MET A 60 -24.638 -21.753 -13.960 1.00 40.06 A N ANISOU 426 N MET A 60 6182 3780 5260 -362 -674 179 A N ATOM 427 CA MET A 60 -25.241 -20.625 -13.262 1.00 38.77 A C ANISOU 427 CA MET A 60 5850 3813 5069 -415 -582 214 A C ATOM 428 C MET A 60 -24.620 -20.329 -11.892 1.00 44.12 A C ANISOU 428 C MET A 60 6550 4494 5719 -342 -611 242 A C ATOM 429 O MET A 60 -23.961 -21.171 -11.279 1.00 47.52 A O ANISOU 429 O MET A 60 7154 4777 6123 -296 -712 270 A O ATOM 430 CB MET A 60 -26.736 -20.875 -13.083 1.00 38.04 A C ANISOU 430 CB MET A 60 5760 3815 4879 -649 -535 297 A C ATOM 431 CG MET A 60 -27.026 -22.105 -12.231 1.00 40.48 A C ANISOU 431 CG MET A 60 6298 3995 5088 -795 -614 394 A C ATOM 432 SD MET A 60 -28.713 -22.207 -11.613 1.00 62.87 A S ANISOU 432 SD MET A 60 9098 7006 7785 -1086 -542 507 A S ATOM 433 CE MET A 60 -29.563 -22.913 -13.014 1.00 40.28 A C ANISOU 433 CE MET A 60 6259 4117 4927 -1248 -549 491 A C ATOM 434 N THR A 61 -24.859 -19.114 -11.417 1.00 43.09 A N ANISOU 434 N THR A 61 6251 4532 5588 -327 -529 233 A N ATOM 435 CA THR A 61 -24.496 -18.728 -10.067 1.00 38.43 A C ANISOU 435 CA THR A 61 5671 3981 4950 -288 -545 257 A C ATOM 436 C THR A 61 -25.752 -18.682 -9.204 1.00 37.71 A C ANISOU 436 C THR A 61 5577 4016 4734 -462 -486 341 A C ATOM 437 O THR A 61 -26.726 -18.020 -9.552 1.00 38.10 A O ANISOU 437 O THR A 61 5485 4219 4772 -533 -389 337 A O ATOM 438 CB THR A 61 -23.778 -17.367 -10.048 1.00 37.39 A C ANISOU 438 CB THR A 61 5367 3941 4898 -143 -501 172 A C ATOM 439 CG2 THR A 61 -23.656 -16.842 -8.629 1.00 40.08 A C ANISOU 439 CG2 THR A 61 5705 4355 5171 -131 -504 189 A C ATOM 440 OG1 THR A 61 -22.464 -17.521 -10.600 1.00 38.33 A O ANISOU 440 OG1 THR A 61 5493 3959 5111 12 -566 104 A O ATOM 441 N VAL A 62 -25.731 -19.407 -8.090 1.00 38.53 A N ANISOU 441 N VAL A 62 5838 4067 4736 -527 -547 422 A N ATOM 442 CA VAL A 62 -26.868 -19.456 -7.181 1.00 41.01 A C ANISOU 442 CA VAL A 62 6157 4516 4910 -703 -491 510 A C ATOM 443 C VAL A 62 -26.525 -18.768 -5.861 1.00 44.56 A C ANISOU 443 C VAL A 62 6579 5060 5294 -636 -482 508 A C ATOM 444 O VAL A 62 -25.444 -18.960 -5.296 1.00 46.46 A O ANISOU 444 O VAL A 62 6914 5195 5544 -520 -574 499 A O ATOM 445 CB VAL A 62 -27.324 -20.912 -6.913 1.00 40.49 A C ANISOU 445 CB VAL A 62 6314 4326 4745 -885 -559 628 A C ATOM 446 CG1 VAL A 62 -28.228 -20.992 -5.679 1.00 40.64 A C ANISOU 446 CG1 VAL A 62 6356 4490 4595 -1059 -513 732 A C ATOM 447 CG2 VAL A 62 -28.027 -21.480 -8.134 1.00 41.01 A C ANISOU 447 CG2 VAL A 62 6385 4351 4844 -1007 -546 629 A C ATOM 448 N LEU A 63 -27.461 -17.962 -5.379 1.00 44.90 A N ANISOU 448 N LEU A 63 6485 5312 5261 -701 -375 510 A N ATOM 449 CA LEU A 63 -27.248 -17.159 -4.193 1.00 43.75 A C ANISOU 449 CA LEU A 63 6295 5280 5047 -634 -352 486 A C ATOM 450 C LEU A 63 -28.457 -17.296 -3.266 1.00 45.49 A C ANISOU 450 C LEU A 63 6510 5684 5091 -805 -277 569 A C ATOM 451 O LEU A 63 -29.579 -16.980 -3.662 1.00 46.38 A O ANISOU 451 O LEU A 63 6490 5956 5177 -894 -177 571 A O ATOM 452 CB LEU A 63 -27.015 -15.709 -4.611 1.00 41.52 A C ANISOU 452 CB LEU A 63 5823 5082 4869 -484 -286 362 A C ATOM 453 CG LEU A 63 -26.382 -14.650 -3.723 1.00 40.98 A C ANISOU 453 CG LEU A 63 5704 5073 4794 -356 -284 283 A C ATOM 454 CD1 LEU A 63 -25.789 -13.582 -4.617 1.00 40.82 A C ANISOU 454 CD1 LEU A 63 5556 5021 4930 -216 -264 172 A C ATOM 455 CD2 LEU A 63 -27.415 -14.041 -2.796 1.00 41.78 A C ANISOU 455 CD2 LEU A 63 5734 5384 4757 -414 -187 287 A C ATOM 456 N VAL A 64 -28.238 -17.798 -2.049 1.00 43.28 A N ANISOU 456 N VAL A 64 6370 5395 4680 -852 -328 643 A N ATOM 457 CA VAL A 64 -29.318 -17.890 -1.070 1.00 44.74 A C ANISOU 457 CA VAL A 64 6544 5779 4676 -1016 -250 724 A C ATOM 458 C VAL A 64 -29.028 -16.963 0.108 1.00 50.31 A C ANISOU 458 C VAL A 64 7200 6619 5299 -909 -223 665 A C ATOM 459 O VAL A 64 -27.870 -16.758 0.472 1.00 53.52 A O ANISOU 459 O VAL A 64 7672 6913 5752 -764 -312 617 A O ATOM 460 CB VAL A 64 -29.527 -19.340 -0.556 1.00 46.26 A C ANISOU 460 CB VAL A 64 6962 5873 4741 -1212 -321 884 A C ATOM 461 CG1 VAL A 64 -29.778 -20.291 -1.710 1.00 42.01 A C ANISOU 461 CG1 VAL A 64 6501 5178 4284 -1322 -361 930 A C ATOM 462 CG2 VAL A 64 -28.336 -19.812 0.276 1.00 49.98 A C ANISOU 462 CG2 VAL A 64 7631 6177 5182 -1115 -454 919 A C ATOM 463 N GLY A 65 -30.071 -16.393 0.703 1.00 50.07 A N ANISOU 463 N GLY A 65 7046 6840 5139 -977 -103 662 A N ATOM 464 CA GLY A 65 -29.861 -15.431 1.764 1.00 46.41 A C ANISOU 464 CA GLY A 65 6531 6511 4592 -865 -70 583 A C ATOM 465 C GLY A 65 -31.073 -14.993 2.561 1.00 48.00 A C ANISOU 465 C GLY A 65 6618 7010 4611 -948 64 590 A C ATOM 466 O GLY A 65 -32.153 -15.571 2.458 1.00 50.80 A O ANISOU 466 O GLY A 65 6936 7496 4871 -1132 134 683 A O ATOM 467 N SER A 66 -30.871 -13.960 3.374 1.00 48.28 A N ANISOU 467 N SER A 66 6595 7159 4590 -813 99 483 A N ATOM 468 CA SER A 66 -31.909 -13.399 4.232 1.00 49.96 A C ANISOU 468 CA SER A 66 6694 7669 4619 -843 228 458 A C ATOM 469 C SER A 66 -31.570 -11.952 4.565 1.00 50.88 A C ANISOU 469 C SER A 66 6721 7841 4771 -624 258 279 A C ATOM 470 O SER A 66 -30.394 -11.599 4.649 1.00 50.66 A O ANISOU 470 O SER A 66 6773 7638 4839 -499 159 209 A O ATOM 471 CB SER A 66 -32.046 -14.205 5.528 1.00 51.19 A C ANISOU 471 CB SER A 66 6987 7922 4542 -994 215 579 A C ATOM 472 OG SER A 66 -32.183 -15.587 5.269 1.00 53.24 A O ANISOU 472 OG SER A 66 7383 8072 4775 -1199 159 751 A O ATOM 473 N PRO A 67 -32.594 -11.110 4.767 1.00 49.02 A N ANISOU 473 N PRO A 67 6320 7851 4453 -576 391 200 A N ATOM 474 CA PRO A 67 -32.347 -9.744 5.242 1.00 47.69 A C ANISOU 474 CA PRO A 67 6097 7734 4288 -371 420 25 A C ATOM 475 C PRO A 67 -31.804 -9.719 6.666 1.00 48.27 A C ANISOU 475 C PRO A 67 6291 7857 4192 -360 379 5 A C ATOM 476 O PRO A 67 -32.195 -10.565 7.470 1.00 50.06 A O ANISOU 476 O PRO A 67 6580 8214 4225 -514 397 124 A O ATOM 477 CB PRO A 67 -33.736 -9.099 5.190 1.00 48.89 A C ANISOU 477 CB PRO A 67 6053 8167 4354 -337 575 -31 A C ATOM 478 CG PRO A 67 -34.688 -10.253 5.337 1.00 47.74 A C ANISOU 478 CG PRO A 67 5880 8199 4059 -573 633 133 A C ATOM 479 CD PRO A 67 -34.032 -11.382 4.585 1.00 46.92 A C ANISOU 479 CD PRO A 67 5910 7836 4081 -706 517 263 A C ATOM 480 N ARG A 68 -30.920 -8.770 6.967 1.00 47.63 A N ANISOU 480 N ARG A 68 6248 7674 4174 -193 321 -138 A N ATOM 481 CA ARG A 68 -30.508 -8.509 8.349 1.00 47.64 A C ANISOU 481 CA ARG A 68 6341 7760 4001 -158 293 -194 A C ATOM 482 C ARG A 68 -31.079 -7.177 8.825 1.00 50.65 A C ANISOU 482 C ARG A 68 6623 8314 4308 -2 395 -374 A C ATOM 483 O ARG A 68 -31.523 -6.359 8.020 1.00 52.97 A O ANISOU 483 O ARG A 68 6799 8599 4728 109 457 -466 A O ATOM 484 CB ARG A 68 -28.984 -8.495 8.483 1.00 43.87 A C ANISOU 484 CB ARG A 68 5998 7046 3626 -98 131 -227 A C ATOM 485 CG ARG A 68 -28.303 -9.821 8.193 1.00 45.64 A C ANISOU 485 CG ARG A 68 6343 7099 3898 -214 14 -63 A C ATOM 486 CD ARG A 68 -26.792 -9.644 8.116 1.00 46.46 A C ANISOU 486 CD ARG A 68 6529 6987 4136 -118 -141 -122 A C ATOM 487 NE ARG A 68 -26.230 -9.193 9.388 1.00 49.21 A N ANISOU 487 NE ARG A 68 6951 7408 4341 -63 -197 -202 A N ATOM 488 CZ ARG A 68 -25.503 -9.955 10.201 1.00 54.27 A C ANISOU 488 CZ ARG A 68 7730 8021 4871 -104 -315 -120 A C ATOM 489 NH1 ARG A 68 -25.230 -11.211 9.871 1.00 44.53 A N1+ ANISOU 489 NH1 ARG A 68 6589 6667 3663 -191 -392 45 A N1+ ATOM 490 NH2 ARG A 68 -25.039 -9.456 11.342 1.00 45.90 A N ANISOU 490 NH2 ARG A 68 6724 7045 3670 -50 -365 -206 A N ATOM 491 N LYS A 69 -31.059 -6.953 10.134 1.00 55.99 A N ANISOU 491 N LYS A 69 7357 9142 4775 16 406 -429 A N ATOM 492 CA LYS A 69 -31.598 -5.721 10.699 1.00 54.52 A C ANISOU 492 CA LYS A 69 7097 9125 4494 176 500 -614 A C ATOM 493 C LYS A 69 -30.516 -4.728 11.128 1.00 53.62 A C ANISOU 493 C LYS A 69 7081 8855 4437 323 401 -788 A C ATOM 494 O LYS A 69 -30.832 -3.640 11.600 1.00 56.89 A O ANISOU 494 O LYS A 69 7467 9363 4785 470 459 -964 A O ATOM 495 CB LYS A 69 -32.503 -6.046 11.889 1.00 57.02 A C ANISOU 495 CB LYS A 69 7389 9772 4506 102 607 -579 A C ATOM 496 CG LYS A 69 -33.764 -6.812 11.511 1.00 60.52 A C ANISOU 496 CG LYS A 69 7699 10426 4871 -45 731 -435 A C ATOM 497 CD LYS A 69 -34.602 -7.134 12.736 1.00 64.80 A C ANISOU 497 CD LYS A 69 8212 11315 5093 -138 841 -395 A C ATOM 498 N ASP A 70 -29.248 -5.091 10.946 1.00 50.63 A N ANISOU 498 N ASP A 70 6814 8241 4181 285 249 -747 A N ATOM 499 CA ASP A 70 -28.141 -4.284 11.460 1.00 50.75 A C ANISOU 499 CA ASP A 70 6923 8129 4229 383 139 -897 A C ATOM 500 C ASP A 70 -27.346 -3.503 10.407 1.00 52.77 A C ANISOU 500 C ASP A 70 7166 8125 4760 470 69 -989 A C ATOM 501 O ASP A 70 -26.310 -2.926 10.723 1.00 54.67 A O ANISOU 501 O ASP A 70 7481 8241 5048 517 -38 -1098 A O ATOM 502 CB ASP A 70 -27.176 -5.174 12.253 1.00 52.01 A C ANISOU 502 CB ASP A 70 7217 8255 4291 286 5 -802 A C ATOM 503 CG ASP A 70 -26.664 -6.358 11.445 1.00 55.40 A C ANISOU 503 CG ASP A 70 7675 8520 4855 177 -79 -618 A C ATOM 504 OD1 ASP A 70 -26.799 -6.356 10.201 1.00 55.73 A O ANISOU 504 OD1 ASP A 70 7639 8438 5100 184 -53 -591 A O ATOM 505 OD2 ASP A 70 -26.114 -7.296 12.061 1.00 55.66 A O1- ANISOU 505 OD2 ASP A 70 7818 8545 4784 95 -175 -502 A O1- ATOM 506 N GLY A 71 -27.816 -3.488 9.164 1.00 54.17 A N ANISOU 506 N GLY A 71 7246 8228 5106 479 127 -943 A N ATOM 507 CA GLY A 71 -27.145 -2.743 8.109 1.00 51.53 A C ANISOU 507 CA GLY A 71 6898 7662 5020 551 74 -1016 A C ATOM 508 C GLY A 71 -25.797 -3.330 7.730 1.00 49.27 A C ANISOU 508 C GLY A 71 6671 7180 4867 479 -71 -947 A C ATOM 509 O GLY A 71 -24.929 -2.647 7.186 1.00 48.67 A O ANISOU 509 O GLY A 71 6605 6928 4961 523 -140 -1028 A O ATOM 510 N LEU A 72 -25.634 -4.616 8.012 1.00 47.18 A N ANISOU 510 N LEU A 72 6449 6955 4522 368 -116 -795 A N ATOM 511 CA LEU A 72 -24.385 -5.318 7.771 1.00 45.66 A C ANISOU 511 CA LEU A 72 6316 6605 4428 320 -258 -725 A C ATOM 512 C LEU A 72 -24.540 -6.313 6.622 1.00 49.31 A C ANISOU 512 C LEU A 72 6742 6980 5013 251 -250 -574 A C ATOM 513 O LEU A 72 -25.602 -6.909 6.449 1.00 47.03 A O ANISOU 513 O LEU A 72 6422 6793 4654 184 -159 -476 A O ATOM 514 CB LEU A 72 -23.954 -6.029 9.056 1.00 52.43 A C ANISOU 514 CB LEU A 72 7282 7550 5088 269 -342 -672 A C ATOM 515 CG LEU A 72 -22.529 -6.505 9.304 1.00 54.40 A C ANISOU 515 CG LEU A 72 7606 7685 5377 264 -514 -648 A C ATOM 516 CD1 LEU A 72 -22.297 -6.658 10.822 1.00 49.87 A C ANISOU 516 CD1 LEU A 72 7135 7247 4566 253 -578 -661 A C ATOM 517 CD2 LEU A 72 -22.266 -7.815 8.578 1.00 55.95 A C ANISOU 517 CD2 LEU A 72 7827 7778 5656 202 -568 -476 A C ATOM 518 N VAL A 73 -23.490 -6.497 5.833 1.00 38.24 A N ANISOU 518 N VAL A 73 5340 5401 3788 261 -346 -562 A N ATOM 519 CA VAL A 73 -23.537 -7.514 4.798 1.00 42.13 A C ANISOU 519 CA VAL A 73 5818 5804 4383 203 -353 -430 A C ATOM 520 C VAL A 73 -22.504 -8.582 5.092 1.00 39.81 A C ANISOU 520 C VAL A 73 5620 5429 4076 177 -492 -344 A C ATOM 521 O VAL A 73 -21.335 -8.275 5.285 1.00 40.20 A O ANISOU 521 O VAL A 73 5681 5411 4183 232 -599 -412 A O ATOM 522 CB VAL A 73 -23.295 -6.926 3.390 1.00 39.11 A C ANISOU 522 CB VAL A 73 5343 5292 4225 251 -331 -478 A C ATOM 523 CG1 VAL A 73 -23.367 -8.021 2.348 1.00 34.65 A C ANISOU 523 CG1 VAL A 73 4773 4646 3748 193 -338 -351 A C ATOM 524 CG2 VAL A 73 -24.311 -5.838 3.096 1.00 36.03 A C ANISOU 524 CG2 VAL A 73 4871 4970 3847 301 -205 -560 A C ATOM 525 N SER A 74 -22.946 -9.836 5.121 1.00 39.70 A N ANISOU 525 N SER A 74 5677 5422 3984 90 -496 -193 A N ATOM 526 CA SER A 74 -22.075 -10.956 5.468 1.00 40.86 A C ANISOU 526 CA SER A 74 5944 5485 4097 78 -634 -96 A C ATOM 527 C SER A 74 -22.159 -12.059 4.416 1.00 39.98 A C ANISOU 527 C SER A 74 5864 5243 4083 32 -650 20 A C ATOM 528 O SER A 74 -23.226 -12.630 4.193 1.00 41.19 A O ANISOU 528 O SER A 74 6036 5437 4179 -73 -569 115 A O ATOM 529 CB SER A 74 -22.442 -11.507 6.847 1.00 40.15 A C ANISOU 529 CB SER A 74 5974 5517 3765 12 -652 -16 A C ATOM 530 OG SER A 74 -21.771 -12.727 7.098 1.00 41.79 A O ANISOU 530 OG SER A 74 6320 5625 3933 -3 -784 107 A O ATOM 531 N LEU A 75 -21.025 -12.367 3.791 1.00 37.52 A N ANISOU 531 N LEU A 75 5556 4788 3913 109 -756 7 A N ATOM 532 CA LEU A 75 -21.006 -13.238 2.618 1.00 40.20 A C ANISOU 532 CA LEU A 75 5910 4992 4370 95 -768 79 A C ATOM 533 C LEU A 75 -20.138 -14.475 2.796 1.00 41.88 A C ANISOU 533 C LEU A 75 6265 5082 4567 132 -915 167 A C ATOM 534 O LEU A 75 -19.129 -14.442 3.491 1.00 37.82 A O ANISOU 534 O LEU A 75 5781 4567 4023 217 -1030 137 A O ATOM 535 CB LEU A 75 -20.509 -12.461 1.396 1.00 34.71 A C ANISOU 535 CB LEU A 75 5073 4236 3879 170 -740 -26 A C ATOM 536 CG LEU A 75 -21.178 -11.121 1.109 1.00 35.63 A C ANISOU 536 CG LEU A 75 5060 4439 4039 168 -615 -124 A C ATOM 537 CD1 LEU A 75 -20.434 -10.392 -0.003 1.00 36.79 A C ANISOU 537 CD1 LEU A 75 5094 4508 4377 239 -615 -213 A C ATOM 538 CD2 LEU A 75 -22.636 -11.340 0.738 1.00 36.15 A C ANISOU 538 CD2 LEU A 75 5109 4572 4055 73 -492 -57 A C ATOM 539 N LEU A 76 -20.537 -15.559 2.140 1.00 38.87 A N ANISOU 539 N LEU A 76 5971 4593 4205 74 -919 270 A N ATOM 540 CA LEU A 76 -19.749 -16.783 2.090 1.00 41.38 A C ANISOU 540 CA LEU A 76 6437 4754 4529 131 -1060 348 A C ATOM 541 C LEU A 76 -19.832 -17.395 0.691 1.00 41.92 A C ANISOU 541 C LEU A 76 6506 4685 4737 134 -1046 360 A C ATOM 542 O LEU A 76 -20.908 -17.450 0.092 1.00 41.42 A O ANISOU 542 O LEU A 76 6420 4639 4680 14 -940 392 A O ATOM 543 CB LEU A 76 -20.238 -17.782 3.141 1.00 44.80 A C ANISOU 543 CB LEU A 76 7075 5178 4768 31 -1109 498 A C ATOM 544 CG LEU A 76 -19.678 -19.207 3.087 1.00 50.06 A C ANISOU 544 CG LEU A 76 7948 5650 5422 72 -1254 608 A C ATOM 545 CD1 LEU A 76 -18.157 -19.207 3.136 1.00 50.74 A C ANISOU 545 CD1 LEU A 76 8017 5677 5587 281 -1401 537 A C ATOM 546 CD2 LEU A 76 -20.230 -20.046 4.235 1.00 52.48 A C ANISOU 546 CD2 LEU A 76 8465 5958 5515 -52 -1294 767 A C ATOM 547 N THR A 77 -18.700 -17.844 0.163 1.00 41.24 A N ANISOU 547 N THR A 77 6435 4479 4755 275 -1155 328 A N ATOM 548 CA THR A 77 -18.711 -18.540 -1.114 1.00 44.56 A C ANISOU 548 CA THR A 77 6881 4763 5288 291 -1154 334 A C ATOM 549 C THR A 77 -18.014 -19.880 -0.984 1.00 48.66 A C ANISOU 549 C THR A 77 7596 5109 5782 381 -1307 405 A C ATOM 550 O THR A 77 -17.097 -20.042 -0.182 1.00 47.16 A O ANISOU 550 O THR A 77 7455 4916 5546 497 -1427 408 A O ATOM 551 CB THR A 77 -18.042 -17.717 -2.244 1.00 46.82 A C ANISOU 551 CB THR A 77 6968 5073 5749 396 -1113 202 A C ATOM 552 CG2 THR A 77 -16.565 -17.490 -1.960 1.00 45.59 A C ANISOU 552 CG2 THR A 77 6749 4931 5641 567 -1225 125 A C ATOM 553 OG1 THR A 77 -18.173 -18.423 -3.483 1.00 47.86 A O ANISOU 553 OG1 THR A 77 7132 5086 5967 402 -1103 208 A O ATOM 554 N THR A 78 -18.467 -20.845 -1.775 1.00 52.33 A N ANISOU 554 N THR A 78 8184 5428 6273 330 -1310 461 A N ATOM 555 CA THR A 78 -17.888 -22.179 -1.760 1.00 55.63 A C ANISOU 555 CA THR A 78 8821 5644 6673 421 -1457 525 A C ATOM 556 C THR A 78 -17.241 -22.473 -3.108 1.00 57.16 A C ANISOU 556 C THR A 78 8964 5735 7018 561 -1478 432 A C ATOM 557 O THR A 78 -16.696 -23.553 -3.325 1.00 60.56 A O ANISOU 557 O THR A 78 9564 5987 7457 675 -1598 455 A O ATOM 558 CB THR A 78 -18.950 -23.249 -1.446 1.00 57.38 A C ANISOU 558 CB THR A 78 9285 5744 6771 232 -1465 678 A C ATOM 559 CG2 THR A 78 -19.728 -22.868 -0.199 1.00 56.95 A C ANISOU 559 CG2 THR A 78 9246 5836 6554 71 -1411 766 A C ATOM 560 OG1 THR A 78 -19.863 -23.359 -2.545 1.00 57.52 A O ANISOU 560 OG1 THR A 78 9271 5734 6850 99 -1363 668 A O ATOM 561 N SER A 79 -17.302 -21.494 -4.005 1.00 56.61 A N ANISOU 561 N SER A 79 8669 5780 7060 559 -1363 326 A N ATOM 562 CA SER A 79 -16.811 -21.653 -5.368 1.00 61.50 A C ANISOU 562 CA SER A 79 9218 6339 7811 667 -1354 235 A C ATOM 563 C SER A 79 -15.338 -22.036 -5.439 1.00 68.64 A C ANISOU 563 C SER A 79 10116 7195 8770 912 -1483 168 A C ATOM 564 O SER A 79 -14.485 -21.403 -4.815 1.00 67.18 A O ANISOU 564 O SER A 79 9810 7126 8588 1012 -1524 122 A O ATOM 565 CB SER A 79 -17.037 -20.367 -6.164 1.00 58.91 A C ANISOU 565 CB SER A 79 8638 6167 7578 625 -1211 143 A C ATOM 566 OG SER A 79 -18.411 -20.029 -6.204 1.00 56.78 A O ANISOU 566 OG SER A 79 8358 5953 7261 426 -1095 195 A O ATOM 567 N GLU A 80 -15.053 -23.083 -6.209 1.00 73.88 A N ANISOU 567 N GLU A 80 10907 7693 9470 1012 -1549 156 A N ATOM 568 CA GLU A 80 -13.680 -23.458 -6.513 1.00 74.76 A C ANISOU 568 CA GLU A 80 10986 7777 9643 1271 -1657 71 A C ATOM 569 C GLU A 80 -13.056 -22.387 -7.396 1.00 69.22 A C ANISOU 569 C GLU A 80 9988 7253 9058 1336 -1564 -62 A C ATOM 570 O GLU A 80 -13.592 -22.058 -8.456 1.00 67.87 A O ANISOU 570 O GLU A 80 9735 7104 8947 1252 -1449 -102 A O ATOM 571 CB GLU A 80 -13.625 -24.824 -7.205 1.00 77.26 A C ANISOU 571 CB GLU A 80 11523 7865 9967 1366 -1740 76 A C ATOM 572 N GLY A 81 -11.932 -21.838 -6.950 1.00 63.44 A N ANISOU 572 N GLY A 81 9099 6657 8350 1474 -1617 -125 A N ATOM 573 CA GLY A 81 -11.256 -20.791 -7.691 1.00 57.20 A C ANISOU 573 CA GLY A 81 8029 6045 7661 1515 -1536 -241 A C ATOM 574 C GLY A 81 -11.368 -19.436 -7.021 1.00 54.04 A C ANISOU 574 C GLY A 81 7466 5810 7256 1389 -1469 -249 A C ATOM 575 O GLY A 81 -10.571 -18.540 -7.292 1.00 55.24 A O ANISOU 575 O GLY A 81 7398 6115 7476 1428 -1439 -337 A O ATOM 576 N ALA A 82 -12.359 -19.282 -6.147 1.00 50.45 A N ANISOU 576 N ALA A 82 7123 5330 6715 1232 -1444 -160 A N ATOM 577 CA ALA A 82 -12.529 -18.035 -5.409 1.00 48.97 A C ANISOU 577 CA ALA A 82 6814 5285 6507 1125 -1388 -175 A C ATOM 578 C ALA A 82 -11.303 -17.764 -4.541 1.00 48.29 A C ANISOU 578 C ALA A 82 6644 5300 6403 1245 -1503 -222 A C ATOM 579 O ALA A 82 -10.777 -18.672 -3.897 1.00 49.18 A O ANISOU 579 O ALA A 82 6879 5354 6452 1368 -1642 -182 A O ATOM 580 CB ALA A 82 -13.789 -18.083 -4.557 1.00 48.58 A C ANISOU 580 CB ALA A 82 6911 5201 6346 961 -1349 -73 A C ATOM 581 N ASP A 83 -10.840 -16.518 -4.531 1.00 46.44 A N ANISOU 581 N ASP A 83 6207 5216 6223 1208 -1455 -305 A N ATOM 582 CA ASP A 83 -9.658 -16.174 -3.746 1.00 45.15 A C ANISOU 582 CA ASP A 83 5939 5172 6043 1300 -1566 -362 A C ATOM 583 C ASP A 83 -9.983 -16.025 -2.258 1.00 46.16 A C ANISOU 583 C ASP A 83 6175 5322 6041 1240 -1626 -310 A C ATOM 584 O ASP A 83 -11.127 -15.779 -1.873 1.00 46.32 A O ANISOU 584 O ASP A 83 6293 5308 5997 1099 -1546 -253 A O ATOM 585 CB ASP A 83 -9.013 -14.894 -4.277 1.00 42.83 A C ANISOU 585 CB ASP A 83 5399 5026 5850 1256 -1498 -470 A C ATOM 586 CG ASP A 83 -9.993 -13.751 -4.387 1.00 46.24 A C ANISOU 586 CG ASP A 83 5803 5466 6299 1071 -1358 -474 A C ATOM 587 OD1 ASP A 83 -11.176 -14.008 -4.687 1.00 46.61 A O ANISOU 587 OD1 ASP A 83 5966 5418 6326 994 -1273 -409 A O ATOM 588 OD2 ASP A 83 -9.577 -12.591 -4.179 1.00 49.51 A O1- ANISOU 588 OD2 ASP A 83 6081 5984 6745 1005 -1336 -545 A O1- ATOM 589 N GLU A 84 -8.962 -16.180 -1.427 1.00 48.40 A N ANISOU 589 N GLU A 84 6432 5682 6276 1353 -1769 -332 A N ATOM 590 CA GLU A 84 -9.123 -16.111 0.020 1.00 49.09 A C ANISOU 590 CA GLU A 84 6625 5806 6222 1316 -1847 -286 A C ATOM 591 C GLU A 84 -9.242 -14.668 0.509 1.00 49.24 A C ANISOU 591 C GLU A 84 6520 5954 6236 1180 -1780 -363 A C ATOM 592 O GLU A 84 -8.645 -13.762 -0.071 1.00 47.94 A O ANISOU 592 O GLU A 84 6160 5877 6177 1160 -1739 -466 A O ATOM 593 CB GLU A 84 -7.951 -16.814 0.707 1.00 42.22 A C ANISOU 593 CB GLU A 84 5770 4978 5295 1502 -2039 -283 A C ATOM 594 N PRO A 85 -10.025 -14.446 1.578 1.00 49.13 A N ANISOU 594 N PRO A 85 6627 5949 6090 1082 -1768 -316 A N ATOM 595 CA PRO A 85 -10.806 -15.465 2.287 1.00 48.32 A C ANISOU 595 CA PRO A 85 6758 5755 5847 1070 -1802 -182 A C ATOM 596 C PRO A 85 -12.136 -15.764 1.597 1.00 45.43 A C ANISOU 596 C PRO A 85 6484 5280 5497 957 -1661 -110 A C ATOM 597 O PRO A 85 -12.571 -14.980 0.752 1.00 43.78 A O ANISOU 597 O PRO A 85 6158 5086 5389 882 -1529 -169 A O ATOM 598 CB PRO A 85 -11.032 -14.831 3.661 1.00 46.41 A C ANISOU 598 CB PRO A 85 6555 5621 5457 994 -1825 -190 A C ATOM 599 CG PRO A 85 -11.080 -13.378 3.375 1.00 48.27 A C ANISOU 599 CG PRO A 85 6618 5945 5775 904 -1721 -317 A C ATOM 600 CD PRO A 85 -10.109 -13.134 2.243 1.00 49.12 A C ANISOU 600 CD PRO A 85 6544 6063 6058 975 -1727 -400 A C ATOM 601 N GLN A 86 -12.768 -16.876 1.962 1.00 46.69 A N ANISOU 601 N GLN A 86 6854 5333 5552 938 -1694 21 A N ATOM 602 CA GLN A 86 -14.034 -17.275 1.350 1.00 50.72 A C ANISOU 602 CA GLN A 86 7456 5751 6064 814 -1575 97 A C ATOM 603 C GLN A 86 -15.215 -16.558 1.996 1.00 51.30 A C ANISOU 603 C GLN A 86 7537 5919 6037 648 -1454 117 A C ATOM 604 O GLN A 86 -16.351 -16.664 1.534 1.00 55.54 A O ANISOU 604 O GLN A 86 8105 6427 6569 528 -1338 166 A O ATOM 605 CB GLN A 86 -14.224 -18.790 1.447 1.00 53.18 A C ANISOU 605 CB GLN A 86 8001 5899 6304 841 -1664 231 A C ATOM 606 N ARG A 87 -14.933 -15.823 3.063 1.00 47.47 A N ANISOU 606 N ARG A 87 7015 5559 5463 647 -1485 71 A N ATOM 607 CA ARG A 87 -15.946 -15.038 3.752 1.00 47.00 A C ANISOU 607 CA ARG A 87 6949 5611 5297 519 -1374 63 A C ATOM 608 C ARG A 87 -15.552 -13.578 3.747 1.00 46.38 A C ANISOU 608 C ARG A 87 6695 5638 5291 533 -1331 -91 A C ATOM 609 O ARG A 87 -14.371 -13.243 3.672 1.00 47.51 A O ANISOU 609 O ARG A 87 6744 5797 5509 625 -1421 -174 A O ATOM 610 CB ARG A 87 -16.130 -15.517 5.195 1.00 49.05 A C ANISOU 610 CB ARG A 87 7368 5926 5343 487 -1447 152 A C ATOM 611 CG ARG A 87 -16.603 -16.949 5.312 1.00 48.24 A C ANISOU 611 CG ARG A 87 7474 5707 5149 443 -1491 322 A C ATOM 612 CD ARG A 87 -16.369 -17.527 6.694 1.00 45.77 A C ANISOU 612 CD ARG A 87 7328 5427 4634 451 -1611 418 A C ATOM 613 NE ARG A 87 -15.810 -18.871 6.591 1.00 46.70 A N ANISOU 613 NE ARG A 87 7620 5376 4748 537 -1756 531 A N ATOM 614 CZ ARG A 87 -16.513 -19.986 6.731 1.00 46.36 A C ANISOU 614 CZ ARG A 87 7790 5219 4607 442 -1766 692 A C ATOM 615 NH1 ARG A 87 -15.921 -21.166 6.613 1.00 50.70 A N1+ ANISOU 615 NH1 ARG A 87 8514 5589 5162 543 -1912 783 A N1+ ATOM 616 NH2 ARG A 87 -17.804 -19.923 7.004 1.00 46.20 A N ANISOU 616 NH2 ARG A 87 7810 5266 4476 246 -1633 763 A N ATOM 617 N LEU A 88 -16.548 -12.709 3.830 1.00 47.02 A N ANISOU 617 N LEU A 88 6731 5790 5342 441 -1195 -129 A N ATOM 618 CA LEU A 88 -16.301 -11.286 3.969 1.00 47.49 A C ANISOU 618 CA LEU A 88 6666 5929 5447 444 -1156 -273 A C ATOM 619 C LEU A 88 -17.518 -10.611 4.570 1.00 44.32 A C ANISOU 619 C LEU A 88 6284 5623 4931 364 -1034 -291 A C ATOM 620 O LEU A 88 -18.651 -10.910 4.193 1.00 36.95 A O ANISOU 620 O LEU A 88 5373 4691 3976 298 -926 -221 A O ATOM 621 CB LEU A 88 -15.964 -10.643 2.619 1.00 49.76 A C ANISOU 621 CB LEU A 88 6809 6158 5939 466 -1101 -350 A C ATOM 622 CG LEU A 88 -15.451 -9.209 2.774 1.00 49.08 A C ANISOU 622 CG LEU A 88 6614 6124 5908 466 -1093 -495 A C ATOM 623 CD1 LEU A 88 -14.119 -9.219 3.507 1.00 51.67 A C ANISOU 623 CD1 LEU A 88 6925 6499 6210 521 -1248 -548 A C ATOM 624 CD2 LEU A 88 -15.328 -8.494 1.446 1.00 45.36 A C ANISOU 624 CD2 LEU A 88 6019 5595 5620 459 -1016 -552 A C ATOM 625 N GLN A 89 -17.277 -9.704 5.511 1.00 40.68 A N ANISOU 625 N GLN A 89 5810 5254 4391 373 -1056 -392 A N ATOM 626 CA GLN A 89 -18.339 -8.863 6.045 1.00 39.22 A C ANISOU 626 CA GLN A 89 5626 5169 4106 328 -937 -447 A C ATOM 627 C GLN A 89 -17.977 -7.392 5.879 1.00 41.16 A C ANISOU 627 C GLN A 89 5779 5412 4449 357 -914 -615 A C ATOM 628 O GLN A 89 -16.809 -7.021 5.922 1.00 43.61 A O ANISOU 628 O GLN A 89 6049 5694 4829 388 -1018 -691 A O ATOM 629 CB GLN A 89 -18.606 -9.190 7.518 1.00 41.54 A C ANISOU 629 CB GLN A 89 6034 5585 4163 303 -974 -411 A C ATOM 630 CG GLN A 89 -18.850 -10.664 7.779 1.00 40.79 A C ANISOU 630 CG GLN A 89 6062 5474 3961 261 -1018 -232 A C ATOM 631 CD GLN A 89 -17.581 -11.400 8.167 1.00 48.01 A C ANISOU 631 CD GLN A 89 7044 6333 4863 327 -1200 -190 A C ATOM 632 NE2 GLN A 89 -17.515 -12.682 7.831 1.00 46.32 A N ANISOU 632 NE2 GLN A 89 6924 6020 4655 325 -1256 -47 A N ATOM 633 OE1 GLN A 89 -16.669 -10.821 8.763 1.00 46.83 A O ANISOU 633 OE1 GLN A 89 6865 6231 4696 383 -1296 -290 A O ATOM 634 N PHE A 90 -18.989 -6.563 5.675 1.00 37.73 A N ANISOU 634 N PHE A 90 5311 5008 4016 345 -782 -670 A N ATOM 635 CA PHE A 90 -18.800 -5.126 5.537 1.00 38.03 A C ANISOU 635 CA PHE A 90 5295 5018 4135 373 -754 -826 A C ATOM 636 C PHE A 90 -20.137 -4.456 5.790 1.00 37.96 A C ANISOU 636 C PHE A 90 5294 5087 4041 385 -617 -870 A C ATOM 637 O PHE A 90 -21.182 -5.058 5.561 1.00 37.67 A O ANISOU 637 O PHE A 90 5253 5109 3952 362 -525 -773 A O ATOM 638 CB PHE A 90 -18.258 -4.763 4.145 1.00 39.91 A C ANISOU 638 CB PHE A 90 5440 5126 4598 378 -748 -842 A C ATOM 639 CG PHE A 90 -19.059 -5.342 3.002 1.00 40.03 A C ANISOU 639 CG PHE A 90 5417 5102 4693 367 -653 -737 A C ATOM 640 CD1 PHE A 90 -20.172 -4.682 2.509 1.00 41.30 A C ANISOU 640 CD1 PHE A 90 5545 5271 4875 376 -524 -757 A C ATOM 641 CD2 PHE A 90 -18.686 -6.542 2.412 1.00 40.53 A C ANISOU 641 CD2 PHE A 90 5478 5118 4803 356 -700 -623 A C ATOM 642 CE1 PHE A 90 -20.905 -5.215 1.458 1.00 42.69 A C ANISOU 642 CE1 PHE A 90 5678 5426 5116 359 -447 -663 A C ATOM 643 CE2 PHE A 90 -19.409 -7.077 1.362 1.00 41.21 A C ANISOU 643 CE2 PHE A 90 5537 5166 4955 336 -621 -537 A C ATOM 644 CZ PHE A 90 -20.522 -6.414 0.882 1.00 41.37 A C ANISOU 644 CZ PHE A 90 5515 5211 4993 330 -495 -555 A C ATOM 645 N PRO A 91 -20.118 -3.215 6.289 1.00 40.04 A N ANISOU 645 N PRO A 91 5571 5361 4283 422 -606 -1023 A N ATOM 646 CA PRO A 91 -21.410 -2.543 6.432 1.00 43.87 A C ANISOU 646 CA PRO A 91 6053 5921 4695 466 -471 -1077 A C ATOM 647 C PRO A 91 -21.886 -1.976 5.094 1.00 43.52 A C ANISOU 647 C PRO A 91 5934 5775 4827 497 -385 -1079 A C ATOM 648 O PRO A 91 -21.091 -1.816 4.168 1.00 42.59 A O ANISOU 648 O PRO A 91 5779 5520 4884 480 -432 -1075 A O ATOM 649 CB PRO A 91 -21.118 -1.431 7.447 1.00 42.02 A C ANISOU 649 CB PRO A 91 5882 5710 4374 509 -507 -1252 A C ATOM 650 CG PRO A 91 -19.676 -1.130 7.263 1.00 42.67 A C ANISOU 650 CG PRO A 91 5964 5669 4580 476 -641 -1307 A C ATOM 651 CD PRO A 91 -19.004 -2.410 6.825 1.00 39.58 A C ANISOU 651 CD PRO A 91 5536 5261 4243 426 -715 -1157 A C ATOM 652 N LEU A 92 -23.179 -1.701 4.997 1.00 43.52 A N ANISOU 652 N LEU A 92 5905 5861 4770 544 -259 -1082 A N ATOM 653 CA LEU A 92 -23.732 -1.058 3.819 1.00 42.43 A C ANISOU 653 CA LEU A 92 5702 5642 4775 595 -180 -1092 A C ATOM 654 C LEU A 92 -23.061 0.284 3.582 1.00 44.21 A C ANISOU 654 C LEU A 92 5964 5712 5122 643 -221 -1231 A C ATOM 655 O LEU A 92 -22.647 0.952 4.529 1.00 45.18 A O ANISOU 655 O LEU A 92 6162 5832 5172 665 -271 -1357 A O ATOM 656 CB LEU A 92 -25.241 -0.871 3.971 1.00 43.12 A C ANISOU 656 CB LEU A 92 5747 5885 4753 661 -47 -1097 A C ATOM 657 CG LEU A 92 -26.092 -2.133 3.816 1.00 42.91 A C ANISOU 657 CG LEU A 92 5659 6000 4643 585 16 -941 A C ATOM 658 CD1 LEU A 92 -27.516 -1.854 4.246 1.00 43.53 A C ANISOU 658 CD1 LEU A 92 5680 6283 4575 646 143 -969 A C ATOM 659 CD2 LEU A 92 -26.062 -2.627 2.384 1.00 41.18 A C ANISOU 659 CD2 LEU A 92 5375 5679 4591 543 20 -834 A C ATOM 660 N PRO A 93 -22.934 0.677 2.308 1.00 44.62 A N ANISOU 660 N PRO A 93 5973 5629 5353 649 -205 -1207 A N ATOM 661 CA PRO A 93 -22.459 2.023 1.987 1.00 47.13 A C ANISOU 661 CA PRO A 93 6338 5784 5784 684 -231 -1325 A C ATOM 662 C PRO A 93 -23.421 3.083 2.509 1.00 48.70 A C ANISOU 662 C PRO A 93 6594 6007 5901 809 -161 -1448 A C ATOM 663 O PRO A 93 -24.596 2.789 2.742 1.00 48.50 A O ANISOU 663 O PRO A 93 6528 6136 5766 879 -68 -1422 A O ATOM 664 CB PRO A 93 -22.414 2.026 0.453 1.00 47.36 A C ANISOU 664 CB PRO A 93 6302 5703 5989 665 -202 -1236 A C ATOM 665 CG PRO A 93 -23.370 0.959 0.044 1.00 46.19 A C ANISOU 665 CG PRO A 93 6073 5683 5793 669 -127 -1107 A C ATOM 666 CD PRO A 93 -23.243 -0.102 1.096 1.00 45.03 A C ANISOU 666 CD PRO A 93 5940 5669 5500 615 -163 -1068 A C ATOM 667 N THR A 94 -22.922 4.298 2.701 1.00 49.70 A N ANISOU 667 N THR A 94 6816 5989 6078 837 -208 -1586 A N ATOM 668 CA THR A 94 -23.761 5.414 3.117 1.00 55.49 A C ANISOU 668 CA THR A 94 7628 6707 6751 980 -153 -1722 A C ATOM 669 C THR A 94 -23.415 6.636 2.280 1.00 61.36 A C ANISOU 669 C THR A 94 8448 7206 7659 1003 -179 -1781 A C ATOM 670 O THR A 94 -22.504 6.588 1.455 1.00 60.31 A O ANISOU 670 O THR A 94 8297 6946 7673 889 -234 -1715 A O ATOM 671 CB THR A 94 -23.589 5.735 4.618 1.00 57.25 A C ANISOU 671 CB THR A 94 7945 7003 6806 1004 -195 -1870 A C ATOM 672 CG2 THR A 94 -24.342 4.722 5.471 1.00 57.12 A C ANISOU 672 CG2 THR A 94 7864 7247 6589 1020 -134 -1816 A C ATOM 673 OG1 THR A 94 -22.198 5.688 4.961 1.00 54.86 A O ANISOU 673 OG1 THR A 94 7686 6617 6541 870 -323 -1900 A O ATOM 674 N ALA A 95 -24.141 7.730 2.491 1.00 68.89 A N ANISOU 674 N ALA A 95 9494 8099 8584 1153 -140 -1903 A N ATOM 675 CA ALA A 95 -23.901 8.955 1.735 1.00 73.45 A C ANISOU 675 CA ALA A 95 10180 8421 9307 1184 -168 -1957 A C ATOM 676 C ALA A 95 -22.490 9.486 1.978 1.00 77.41 A C ANISOU 676 C ALA A 95 10784 8745 9881 1029 -290 -2031 A C ATOM 677 O ALA A 95 -21.902 10.127 1.107 1.00 80.09 A O ANISOU 677 O ALA A 95 11176 8880 10373 957 -329 -2008 A O ATOM 678 CB ALA A 95 -24.932 10.012 2.097 1.00 75.21 A C ANISOU 678 CB ALA A 95 10505 8608 9463 1398 -115 -2094 A C ATOM 679 N GLN A 96 -21.950 9.196 3.158 1.00 76.39 A N ANISOU 679 N GLN A 96 10678 8712 9635 969 -351 -2114 A N ATOM 680 CA GLN A 96 -20.646 9.716 3.558 1.00 77.22 A C ANISOU 680 CA GLN A 96 10872 8686 9783 822 -476 -2207 A C ATOM 681 C GLN A 96 -19.510 8.708 3.370 1.00 74.28 A C ANISOU 681 C GLN A 96 10375 8391 9459 643 -546 -2096 A C ATOM 682 O GLN A 96 -18.335 9.073 3.443 1.00 76.09 A O ANISOU 682 O GLN A 96 10635 8525 9752 498 -650 -2144 A O ATOM 683 CB GLN A 96 -20.691 10.173 5.019 1.00 79.37 A C ANISOU 683 CB GLN A 96 11261 9008 9887 875 -518 -2394 A C ATOM 684 N ARG A 97 -19.855 7.445 3.137 1.00 67.87 A N ANISOU 684 N ARG A 97 9424 7752 8611 653 -494 -1951 A N ATOM 685 CA ARG A 97 -18.842 6.410 2.938 1.00 61.64 A C ANISOU 685 CA ARG A 97 8522 7038 7862 519 -560 -1845 A C ATOM 686 C ARG A 97 -19.311 5.326 1.968 1.00 59.00 A C ANISOU 686 C ARG A 97 8058 6782 7577 534 -485 -1666 A C ATOM 687 O ARG A 97 -20.288 4.616 2.222 1.00 57.92 A O ANISOU 687 O ARG A 97 7885 6785 7335 613 -412 -1609 A O ATOM 688 CB ARG A 97 -18.448 5.778 4.276 1.00 61.41 A C ANISOU 688 CB ARG A 97 8497 7167 7670 495 -632 -1891 A C ATOM 689 CG ARG A 97 -17.796 4.420 4.123 1.00 60.54 A C ANISOU 689 CG ARG A 97 8266 7172 7563 422 -678 -1754 A C ATOM 690 CD ARG A 97 -17.178 3.912 5.402 1.00 63.40 A C ANISOU 690 CD ARG A 97 8647 7665 7778 388 -779 -1799 A C ATOM 691 NE ARG A 97 -16.847 2.494 5.286 1.00 64.95 A N ANISOU 691 NE ARG A 97 8749 7974 7955 363 -808 -1652 A N ATOM 692 CZ ARG A 97 -16.016 1.846 6.096 1.00 67.34 A C ANISOU 692 CZ ARG A 97 9042 8376 8170 325 -921 -1648 A C ATOM 693 NH1 ARG A 97 -15.411 2.490 7.085 1.00 69.23 A N1+ ANISOU 693 NH1 ARG A 97 9343 8632 8328 291 -1016 -1785 A N1+ ATOM 694 NH2 ARG A 97 -15.784 0.555 5.908 1.00 67.41 A N ANISOU 694 NH2 ARG A 97 8985 8460 8168 323 -947 -1508 A N ATOM 695 N SER A 98 -18.607 5.198 0.852 1.00 59.22 A N ANISOU 695 N SER A 98 8016 6726 7757 447 -504 -1581 A N ATOM 696 CA SER A 98 -18.993 4.228 -0.158 1.00 60.86 A C ANISOU 696 CA SER A 98 8115 6991 8019 457 -439 -1425 A C ATOM 697 C SER A 98 -18.101 3.002 -0.072 1.00 57.40 A C ANISOU 697 C SER A 98 7587 6651 7573 380 -507 -1347 A C ATOM 698 O SER A 98 -16.993 3.074 0.455 1.00 57.82 A O ANISOU 698 O SER A 98 7639 6706 7625 304 -609 -1404 A O ATOM 699 CB SER A 98 -18.919 4.842 -1.558 1.00 63.42 A C ANISOU 699 CB SER A 98 8423 7171 8504 433 -402 -1375 A C ATOM 700 OG SER A 98 -17.573 5.000 -1.972 1.00 65.70 A O ANISOU 700 OG SER A 98 8676 7392 8897 300 -479 -1374 A O ATOM 701 N LEU A 99 -18.596 1.878 -0.584 1.00 52.07 A N ANISOU 701 N LEU A 99 6839 6058 6887 404 -458 -1221 A N ATOM 702 CA LEU A 99 -17.806 0.656 -0.659 1.00 47.15 A C ANISOU 702 CA LEU A 99 6144 5503 6267 355 -521 -1139 A C ATOM 703 C LEU A 99 -16.614 0.866 -1.578 1.00 48.05 A C ANISOU 703 C LEU A 99 6186 5542 6529 279 -570 -1130 A C ATOM 704 O LEU A 99 -16.564 1.833 -2.338 1.00 48.50 A O ANISOU 704 O LEU A 99 6248 5490 6688 250 -536 -1155 A O ATOM 705 CB LEU A 99 -18.658 -0.514 -1.153 1.00 44.11 A C ANISOU 705 CB LEU A 99 5720 5188 5851 389 -455 -1009 A C ATOM 706 CG LEU A 99 -19.923 -0.806 -0.343 1.00 44.57 A C ANISOU 706 CG LEU A 99 5826 5354 5756 443 -391 -998 A C ATOM 707 CD1 LEU A 99 -20.714 -1.946 -0.958 1.00 42.47 A C ANISOU 707 CD1 LEU A 99 5516 5147 5473 440 -331 -866 A C ATOM 708 CD2 LEU A 99 -19.574 -1.112 1.105 1.00 44.03 A C ANISOU 708 CD2 LEU A 99 5817 5373 5541 435 -465 -1044 A C ATOM 709 N GLU A 100 -15.648 -0.038 -1.505 1.00 50.11 A N ANISOU 709 N GLU A 100 6380 5865 6793 248 -650 -1093 A N ATOM 710 CA GLU A 100 -14.436 0.093 -2.299 1.00 49.79 A C ANISOU 710 CA GLU A 100 6244 5797 6876 178 -697 -1093 A C ATOM 711 C GLU A 100 -13.911 -1.275 -2.686 1.00 47.36 A C ANISOU 711 C GLU A 100 5852 5565 6576 206 -734 -1005 A C ATOM 712 O GLU A 100 -13.945 -2.205 -1.880 1.00 47.35 A O ANISOU 712 O GLU A 100 5881 5636 6473 253 -788 -978 A O ATOM 713 CB GLU A 100 -13.365 0.875 -1.530 1.00 49.53 A C ANISOU 713 CB GLU A 100 6214 5766 6840 100 -799 -1207 A C ATOM 714 N PRO A 101 -13.432 -1.404 -3.930 1.00 46.59 A N ANISOU 714 N PRO A 101 5660 5448 6592 181 -706 -959 A N ATOM 715 CA PRO A 101 -12.839 -2.667 -4.374 1.00 45.65 A C ANISOU 715 CA PRO A 101 5463 5395 6487 225 -745 -894 A C ATOM 716 C PRO A 101 -11.585 -3.006 -3.577 1.00 50.07 A C ANISOU 716 C PRO A 101 5965 6043 7014 227 -876 -943 A C ATOM 717 O PRO A 101 -10.831 -2.113 -3.192 1.00 52.84 A O ANISOU 717 O PRO A 101 6280 6410 7387 151 -929 -1028 A O ATOM 718 CB PRO A 101 -12.511 -2.413 -5.852 1.00 43.68 A C ANISOU 718 CB PRO A 101 5118 5116 6361 188 -682 -863 A C ATOM 719 CG PRO A 101 -12.502 -0.933 -6.013 1.00 44.94 A C ANISOU 719 CG PRO A 101 5296 5201 6578 96 -647 -920 A C ATOM 720 CD PRO A 101 -13.460 -0.389 -4.997 1.00 46.52 A C ANISOU 720 CD PRO A 101 5627 5353 6695 120 -636 -963 A C ATOM 721 N GLY A 102 -11.384 -4.294 -3.320 1.00 50.70 A N ANISOU 721 N GLY A 102 6047 6178 7040 312 -936 -890 A N ATOM 722 CA GLY A 102 -10.219 -4.763 -2.597 1.00 52.40 A C ANISOU 722 CA GLY A 102 6205 6489 7216 346 -1071 -925 A C ATOM 723 C GLY A 102 -10.167 -6.277 -2.601 1.00 52.54 A C ANISOU 723 C GLY A 102 6250 6526 7188 464 -1122 -844 A C ATOM 724 O GLY A 102 -10.613 -6.922 -3.549 1.00 53.07 A O ANISOU 724 O GLY A 102 6323 6542 7297 503 -1056 -777 A O ATOM 725 N THR A 103 -9.623 -6.843 -1.532 1.00 52.61 A N ANISOU 725 N THR A 103 6288 6601 7102 523 -1247 -851 A N ATOM 726 CA THR A 103 -9.554 -8.287 -1.372 1.00 51.18 A C ANISOU 726 CA THR A 103 6169 6415 6861 643 -1317 -770 A C ATOM 727 C THR A 103 -10.629 -8.737 -0.384 1.00 49.37 A C ANISOU 727 C THR A 103 6121 6145 6492 641 -1313 -703 A C ATOM 728 O THR A 103 -10.976 -7.994 0.527 1.00 53.73 A O ANISOU 728 O THR A 103 6722 6727 6967 580 -1310 -747 A O ATOM 729 CB THR A 103 -8.157 -8.734 -0.882 1.00 51.93 A C ANISOU 729 CB THR A 103 6173 6619 6937 731 -1474 -807 A C ATOM 730 N PRO A 104 -11.196 -9.936 -0.583 1.00 48.75 A N ANISOU 730 N PRO A 104 6150 6000 6374 699 -1308 -600 A N ATOM 731 CA PRO A 104 -11.005 -10.838 -1.726 1.00 48.69 A C ANISOU 731 CA PRO A 104 6118 5932 6450 771 -1297 -553 A C ATOM 732 C PRO A 104 -11.628 -10.268 -2.991 1.00 46.17 A C ANISOU 732 C PRO A 104 5736 5567 6239 702 -1152 -561 A C ATOM 733 O PRO A 104 -12.569 -9.474 -2.904 1.00 42.66 A O ANISOU 733 O PRO A 104 5319 5108 5781 611 -1055 -566 A O ATOM 734 CB PRO A 104 -11.734 -12.109 -1.292 1.00 50.74 A C ANISOU 734 CB PRO A 104 6564 6112 6603 806 -1328 -439 A C ATOM 735 CG PRO A 104 -12.811 -11.610 -0.382 1.00 50.05 A C ANISOU 735 CG PRO A 104 6570 6042 6404 703 -1268 -416 A C ATOM 736 CD PRO A 104 -12.169 -10.479 0.381 1.00 49.35 A C ANISOU 736 CD PRO A 104 6396 6052 6300 679 -1309 -520 A C ATOM 737 N ARG A 105 -11.115 -10.673 -4.146 1.00 46.48 A N ANISOU 737 N ARG A 105 5693 5592 6375 758 -1139 -565 A N ATOM 738 CA ARG A 105 -11.552 -10.110 -5.416 1.00 43.92 A C ANISOU 738 CA ARG A 105 5297 5240 6150 698 -1012 -574 A C ATOM 739 C ARG A 105 -12.993 -10.480 -5.764 1.00 42.42 A C ANISOU 739 C ARG A 105 5225 4966 5929 651 -918 -496 A C ATOM 740 O ARG A 105 -13.708 -9.684 -6.377 1.00 43.87 A O ANISOU 740 O ARG A 105 5375 5137 6155 577 -809 -501 A O ATOM 741 CB ARG A 105 -10.612 -10.555 -6.538 1.00 45.29 A C ANISOU 741 CB ARG A 105 5354 5442 6414 778 -1024 -598 A C ATOM 742 N TRP A 106 -13.428 -11.674 -5.372 1.00 39.35 A N ANISOU 742 N TRP A 106 4973 4519 5458 689 -966 -421 A N ATOM 743 CA TRP A 106 -14.764 -12.138 -5.747 1.00 38.11 A C ANISOU 743 CA TRP A 106 4918 4296 5267 626 -884 -345 A C ATOM 744 C TRP A 106 -15.854 -11.277 -5.124 1.00 39.27 A C ANISOU 744 C TRP A 106 5086 4481 5352 526 -803 -337 A C ATOM 745 O TRP A 106 -16.976 -11.224 -5.632 1.00 38.91 A O ANISOU 745 O TRP A 106 5060 4423 5303 462 -707 -298 A O ATOM 746 CB TRP A 106 -14.972 -13.600 -5.346 1.00 40.84 A C ANISOU 746 CB TRP A 106 5427 4562 5528 663 -964 -261 A C ATOM 747 CG TRP A 106 -14.930 -13.838 -3.862 1.00 45.58 A C ANISOU 747 CG TRP A 106 6131 5185 6003 663 -1048 -225 A C ATOM 748 CD1 TRP A 106 -13.839 -14.182 -3.122 1.00 46.22 A C ANISOU 748 CD1 TRP A 106 6226 5284 6052 763 -1181 -242 A C ATOM 749 CD2 TRP A 106 -16.027 -13.750 -2.942 1.00 43.26 A C ANISOU 749 CD2 TRP A 106 5934 4915 5586 561 -1006 -166 A C ATOM 750 CE2 TRP A 106 -15.522 -14.056 -1.662 1.00 47.92 A C ANISOU 750 CE2 TRP A 106 6606 5532 6069 599 -1117 -146 A C ATOM 751 CE3 TRP A 106 -17.386 -13.445 -3.077 1.00 40.24 A C ANISOU 751 CE3 TRP A 106 5566 4556 5168 446 -886 -130 A C ATOM 752 NE1 TRP A 106 -14.184 -14.316 -1.802 1.00 48.45 A N ANISOU 752 NE1 TRP A 106 6621 5591 6196 727 -1228 -193 A N ATOM 753 CZ2 TRP A 106 -16.328 -14.063 -0.519 1.00 45.82 A C ANISOU 753 CZ2 TRP A 106 6443 5315 5654 518 -1103 -90 A C ATOM 754 CZ3 TRP A 106 -18.187 -13.456 -1.947 1.00 40.80 A C ANISOU 754 CZ3 TRP A 106 5723 4685 5094 371 -869 -79 A C ATOM 755 CH2 TRP A 106 -17.655 -13.763 -0.682 1.00 44.00 A C ANISOU 755 CH2 TRP A 106 6215 5114 5387 402 -973 -58 A C ATOM 756 N ALA A 107 -15.520 -10.599 -4.027 1.00 40.91 A N ANISOU 756 N ALA A 107 5287 4749 5507 521 -843 -383 A N ATOM 757 CA ALA A 107 -16.498 -9.787 -3.308 1.00 38.26 A C ANISOU 757 CA ALA A 107 4981 4460 5097 451 -772 -393 A C ATOM 758 C ALA A 107 -16.689 -8.422 -3.953 1.00 37.89 A C ANISOU 758 C ALA A 107 4833 4422 5142 420 -680 -464 A C ATOM 759 O ALA A 107 -17.672 -7.736 -3.680 1.00 40.08 A O ANISOU 759 O ALA A 107 5127 4725 5377 382 -601 -474 A O ATOM 760 CB ALA A 107 -16.088 -9.628 -1.850 1.00 40.24 A C ANISOU 760 CB ALA A 107 5283 4768 5238 461 -856 -422 A C ATOM 761 N ASN A 108 -15.758 -8.024 -4.814 1.00 37.99 A N ANISOU 761 N ASN A 108 4743 4417 5275 439 -691 -511 A N ATOM 762 CA ASN A 108 -15.899 -6.755 -5.525 1.00 41.93 A C ANISOU 762 CA ASN A 108 5166 4902 5863 400 -609 -562 A C ATOM 763 C ASN A 108 -17.132 -6.730 -6.434 1.00 39.11 A C ANISOU 763 C ASN A 108 4817 4520 5524 379 -497 -507 A C ATOM 764 O ASN A 108 -17.766 -5.691 -6.599 1.00 42.38 A O ANISOU 764 O ASN A 108 5219 4926 5956 357 -424 -533 A O ATOM 765 CB ASN A 108 -14.642 -6.459 -6.345 1.00 43.16 A C ANISOU 765 CB ASN A 108 5207 5060 6133 405 -638 -604 A C ATOM 766 CG ASN A 108 -13.414 -6.260 -5.478 1.00 41.51 A C ANISOU 766 CG ASN A 108 4958 4903 5912 413 -748 -672 A C ATOM 767 ND2 ASN A 108 -12.246 -6.573 -6.029 1.00 35.28 A N ANISOU 767 ND2 ASN A 108 4064 4153 5188 442 -799 -691 A N ATOM 768 OD1 ASN A 108 -13.513 -5.835 -4.319 1.00 46.09 A O ANISOU 768 OD1 ASN A 108 5593 5503 6415 395 -787 -712 A O ATOM 769 N TYR A 109 -17.479 -7.875 -7.012 1.00 36.63 A N ANISOU 769 N TYR A 109 4530 4189 5200 390 -492 -435 A N ATOM 770 CA TYR A 109 -18.660 -7.953 -7.867 1.00 36.55 A C ANISOU 770 CA TYR A 109 4521 4173 5195 361 -399 -383 A C ATOM 771 C TYR A 109 -19.933 -7.688 -7.080 1.00 35.19 A C ANISOU 771 C TYR A 109 4398 4051 4922 330 -344 -363 A C ATOM 772 O TYR A 109 -20.807 -6.937 -7.524 1.00 36.78 A O ANISOU 772 O TYR A 109 4562 4273 5137 322 -260 -367 A O ATOM 773 CB TYR A 109 -18.742 -9.316 -8.545 1.00 35.69 A C ANISOU 773 CB TYR A 109 4448 4030 5082 367 -419 -319 A C ATOM 774 CG TYR A 109 -17.533 -9.630 -9.385 1.00 34.87 A C ANISOU 774 CG TYR A 109 4287 3897 5067 420 -463 -347 A C ATOM 775 CD1 TYR A 109 -17.259 -8.895 -10.529 1.00 33.18 A C ANISOU 775 CD1 TYR A 109 3972 3688 4945 417 -405 -375 A C ATOM 776 CD2 TYR A 109 -16.666 -10.662 -9.039 1.00 33.68 A C ANISOU 776 CD2 TYR A 109 4179 3721 4897 481 -563 -345 A C ATOM 777 CE1 TYR A 109 -16.152 -9.170 -11.309 1.00 32.36 A C ANISOU 777 CE1 TYR A 109 3798 3589 4909 463 -434 -404 A C ATOM 778 CE2 TYR A 109 -15.554 -10.948 -9.817 1.00 33.72 A C ANISOU 778 CE2 TYR A 109 4113 3725 4976 550 -599 -383 A C ATOM 779 CZ TYR A 109 -15.310 -10.199 -10.960 1.00 33.91 A C ANISOU 779 CZ TYR A 109 4021 3777 5086 535 -528 -414 A C ATOM 780 OH TYR A 109 -14.217 -10.463 -11.755 1.00 34.76 A O ANISOU 780 OH TYR A 109 4040 3913 5254 599 -550 -454 A O ATOM 781 N VAL A 110 -20.035 -8.321 -5.916 1.00 32.78 A N ANISOU 781 N VAL A 110 4172 3775 4506 319 -394 -341 A N ATOM 782 CA VAL A 110 -21.169 -8.112 -5.026 1.00 34.05 A C ANISOU 782 CA VAL A 110 4371 4016 4548 287 -341 -326 A C ATOM 783 C VAL A 110 -21.195 -6.679 -4.499 1.00 36.92 A C ANISOU 783 C VAL A 110 4704 4410 4915 319 -309 -420 A C ATOM 784 O VAL A 110 -22.231 -6.023 -4.544 1.00 40.85 A O ANISOU 784 O VAL A 110 5177 4959 5384 326 -223 -433 A O ATOM 785 CB VAL A 110 -21.136 -9.096 -3.835 1.00 35.74 A C ANISOU 785 CB VAL A 110 4691 4260 4630 260 -408 -276 A C ATOM 786 CG1 VAL A 110 -22.299 -8.828 -2.882 1.00 30.78 A C ANISOU 786 CG1 VAL A 110 4087 3747 3862 221 -341 -265 A C ATOM 787 CG2 VAL A 110 -21.163 -10.533 -4.343 1.00 33.50 A C ANISOU 787 CG2 VAL A 110 4472 3916 4342 227 -448 -181 A C ATOM 788 N LYS A 111 -20.052 -6.202 -4.007 1.00 38.44 A N ANISOU 788 N LYS A 111 4898 4570 5137 343 -384 -491 A N ATOM 789 CA LYS A 111 -19.923 -4.828 -3.515 1.00 37.67 A C ANISOU 789 CA LYS A 111 4792 4470 5048 363 -371 -594 A C ATOM 790 C LYS A 111 -20.371 -3.808 -4.553 1.00 37.39 A C ANISOU 790 C LYS A 111 4706 4387 5114 378 -289 -617 A C ATOM 791 O LYS A 111 -21.078 -2.847 -4.231 1.00 36.83 A O ANISOU 791 O LYS A 111 4652 4329 5014 411 -235 -671 A O ATOM 792 CB LYS A 111 -18.479 -4.524 -3.120 1.00 39.19 A C ANISOU 792 CB LYS A 111 4975 4630 5285 362 -473 -663 A C ATOM 793 CG LYS A 111 -17.998 -5.145 -1.825 1.00 42.45 A C ANISOU 793 CG LYS A 111 5449 5099 5581 366 -568 -668 A C ATOM 794 CD LYS A 111 -16.596 -4.627 -1.532 1.00 46.06 A C ANISOU 794 CD LYS A 111 5869 5542 6090 362 -667 -752 A C ATOM 795 CE LYS A 111 -15.924 -5.353 -0.387 1.00 48.49 A C ANISOU 795 CE LYS A 111 6222 5910 6291 379 -784 -748 A C ATOM 796 NZ LYS A 111 -14.468 -5.038 -0.375 1.00 48.19 A N1+ ANISOU 796 NZ LYS A 111 6109 5877 6323 375 -888 -817 A N1+ ATOM 797 N GLY A 112 -19.941 -4.022 -5.796 1.00 34.88 A N ANISOU 797 N GLY A 112 4331 4014 4907 366 -284 -578 A N ATOM 798 CA GLY A 112 -20.263 -3.131 -6.898 1.00 31.26 A C ANISOU 798 CA GLY A 112 3830 3503 4542 375 -216 -581 A C ATOM 799 C GLY A 112 -21.750 -2.965 -7.122 1.00 32.14 A C ANISOU 799 C GLY A 112 3942 3665 4606 408 -127 -548 A C ATOM 800 O GLY A 112 -22.242 -1.838 -7.219 1.00 36.34 A O ANISOU 800 O GLY A 112 4480 4171 5157 452 -81 -591 A O ATOM 801 N VAL A 113 -22.468 -4.085 -7.200 1.00 31.80 A N ANISOU 801 N VAL A 113 3892 3694 4497 387 -107 -472 A N ATOM 802 CA VAL A 113 -23.912 -4.060 -7.423 1.00 31.74 A C ANISOU 802 CA VAL A 113 3857 3771 4431 403 -24 -435 A C ATOM 803 C VAL A 113 -24.627 -3.335 -6.287 1.00 35.53 A C ANISOU 803 C VAL A 113 4361 4327 4813 453 11 -496 A C ATOM 804 O VAL A 113 -25.548 -2.544 -6.519 1.00 34.89 A O ANISOU 804 O VAL A 113 4247 4285 4724 518 78 -518 A O ATOM 805 CB VAL A 113 -24.497 -5.487 -7.561 1.00 32.61 A C ANISOU 805 CB VAL A 113 3966 3950 4473 337 -20 -343 A C ATOM 806 CG1 VAL A 113 -26.000 -5.430 -7.753 1.00 27.52 A C ANISOU 806 CG1 VAL A 113 3268 3427 3762 338 64 -308 A C ATOM 807 CG2 VAL A 113 -23.855 -6.222 -8.713 1.00 28.85 A C ANISOU 807 CG2 VAL A 113 3476 3399 4086 306 -53 -297 A C ATOM 808 N ILE A 114 -24.199 -3.614 -5.056 1.00 36.70 A N ANISOU 808 N ILE A 114 4567 4502 4877 434 -38 -528 A N ATOM 809 CA ILE A 114 -24.747 -2.940 -3.884 1.00 34.33 A C ANISOU 809 CA ILE A 114 4297 4280 4466 484 -9 -603 A C ATOM 810 C ILE A 114 -24.509 -1.440 -3.971 1.00 35.12 A C ANISOU 810 C ILE A 114 4416 4290 4639 563 -3 -709 A C ATOM 811 O ILE A 114 -25.428 -0.646 -3.766 1.00 38.44 A O ANISOU 811 O ILE A 114 4832 4760 5014 648 61 -760 A O ATOM 812 CB ILE A 114 -24.131 -3.474 -2.566 1.00 38.20 A C ANISOU 812 CB ILE A 114 4857 4806 4851 446 -79 -620 A C ATOM 813 CG1 ILE A 114 -24.518 -4.937 -2.346 1.00 30.83 A C ANISOU 813 CG1 ILE A 114 3937 3955 3823 365 -85 -507 A C ATOM 814 CG2 ILE A 114 -24.585 -2.619 -1.374 1.00 33.38 A C ANISOU 814 CG2 ILE A 114 4284 4275 4124 506 -51 -721 A C ATOM 815 CD1 ILE A 114 -23.813 -5.579 -1.159 1.00 38.90 A C ANISOU 815 CD1 ILE A 114 5042 4993 4743 330 -170 -500 A C ATOM 816 N GLN A 115 -23.277 -1.058 -4.293 1.00 33.82 A N ANISOU 816 N GLN A 115 4275 3993 4583 536 -71 -741 A N ATOM 817 CA GLN A 115 -22.920 0.356 -4.413 1.00 36.81 A C ANISOU 817 CA GLN A 115 4694 4254 5038 579 -78 -834 A C ATOM 818 C GLN A 115 -23.804 1.115 -5.404 1.00 38.86 A C ANISOU 818 C GLN A 115 4931 4476 5356 653 -4 -818 A C ATOM 819 O GLN A 115 -24.213 2.240 -5.130 1.00 40.55 A O ANISOU 819 O GLN A 115 5200 4644 5564 738 18 -899 A O ATOM 820 CB GLN A 115 -21.453 0.505 -4.828 1.00 35.93 A C ANISOU 820 CB GLN A 115 4583 4027 5040 503 -156 -846 A C ATOM 821 CG GLN A 115 -20.967 1.950 -4.834 1.00 35.68 A C ANISOU 821 CG GLN A 115 4614 3862 5081 508 -178 -942 A C ATOM 822 CD GLN A 115 -20.986 2.565 -3.444 1.00 40.27 A C ANISOU 822 CD GLN A 115 5282 4453 5566 541 -210 -1063 A C ATOM 823 NE2 GLN A 115 -21.506 3.786 -3.337 1.00 33.77 A N ANISOU 823 NE2 GLN A 115 4538 3546 4748 615 -181 -1146 A N ATOM 824 OE1 GLN A 115 -20.548 1.944 -2.477 1.00 38.84 A O ANISOU 824 OE1 GLN A 115 5106 4351 5300 509 -265 -1085 A O ATOM 825 N TYR A 116 -24.101 0.511 -6.554 1.00 38.64 A N ANISOU 825 N TYR A 116 4833 4467 5382 630 28 -717 A N ATOM 826 CA TYR A 116 -24.876 1.224 -7.569 1.00 40.22 A C ANISOU 826 CA TYR A 116 5010 4636 5636 702 86 -691 A C ATOM 827 C TYR A 116 -26.338 0.792 -7.650 1.00 43.17 A C ANISOU 827 C TYR A 116 5313 5169 5921 762 159 -646 A C ATOM 828 O TYR A 116 -27.025 1.132 -8.613 1.00 45.87 A O ANISOU 828 O TYR A 116 5612 5517 6300 819 201 -604 A O ATOM 829 CB TYR A 116 -24.215 1.072 -8.940 1.00 39.90 A C ANISOU 829 CB TYR A 116 4935 4510 5714 640 73 -617 A C ATOM 830 CG TYR A 116 -22.807 1.620 -8.971 1.00 41.19 A C ANISOU 830 CG TYR A 116 5145 4539 5967 572 11 -660 A C ATOM 831 CD1 TYR A 116 -22.571 2.985 -8.866 1.00 40.15 A C ANISOU 831 CD1 TYR A 116 5095 4276 5883 600 -1 -729 A C ATOM 832 CD2 TYR A 116 -21.713 0.771 -9.088 1.00 39.33 A C ANISOU 832 CD2 TYR A 116 4870 4310 5762 480 -40 -634 A C ATOM 833 CE1 TYR A 116 -21.285 3.489 -8.883 1.00 39.31 A C ANISOU 833 CE1 TYR A 116 5024 4060 5853 507 -60 -766 A C ATOM 834 CE2 TYR A 116 -20.428 1.268 -9.103 1.00 39.64 A C ANISOU 834 CE2 TYR A 116 4923 4262 5875 410 -96 -675 A C ATOM 835 CZ TYR A 116 -20.221 2.625 -9.003 1.00 40.23 A C ANISOU 835 CZ TYR A 116 5072 4217 5995 409 -104 -738 A C ATOM 836 OH TYR A 116 -18.942 3.122 -9.024 1.00 44.87 A O ANISOU 836 OH TYR A 116 5666 4729 6652 310 -161 -776 A O ATOM 837 N TYR A 117 -26.819 0.058 -6.648 1.00 41.12 A N ANISOU 837 N TYR A 117 5037 5052 5536 743 174 -650 A N ATOM 838 CA TYR A 117 -28.229 -0.314 -6.613 1.00 39.80 A C ANISOU 838 CA TYR A 117 4787 5067 5269 781 248 -612 A C ATOM 839 C TYR A 117 -29.088 0.934 -6.450 1.00 41.67 A C ANISOU 839 C TYR A 117 5021 5332 5481 942 299 -692 A C ATOM 840 O TYR A 117 -28.896 1.706 -5.517 1.00 42.63 A O ANISOU 840 O TYR A 117 5217 5417 5564 1011 289 -797 A O ATOM 841 CB TYR A 117 -28.524 -1.310 -5.491 1.00 41.84 A C ANISOU 841 CB TYR A 117 5039 5476 5384 709 255 -595 A C ATOM 842 CG TYR A 117 -29.909 -1.915 -5.607 1.00 40.40 A C ANISOU 842 CG TYR A 117 4750 5499 5100 695 330 -531 A C ATOM 843 CD1 TYR A 117 -30.202 -2.829 -6.613 1.00 37.17 A C ANISOU 843 CD1 TYR A 117 4280 5117 4724 605 334 -427 A C ATOM 844 CD2 TYR A 117 -30.926 -1.558 -4.731 1.00 39.33 A C ANISOU 844 CD2 TYR A 117 4569 5543 4830 769 398 -583 A C ATOM 845 CE1 TYR A 117 -31.465 -3.381 -6.741 1.00 37.24 A C ANISOU 845 CE1 TYR A 117 4184 5325 4640 568 396 -370 A C ATOM 846 CE2 TYR A 117 -32.197 -2.108 -4.849 1.00 41.84 A C ANISOU 846 CE2 TYR A 117 4766 6081 5051 741 470 -524 A C ATOM 847 CZ TYR A 117 -32.457 -3.019 -5.860 1.00 42.71 A C ANISOU 847 CZ TYR A 117 4815 6211 5201 630 465 -415 A C ATOM 848 OH TYR A 117 -33.711 -3.575 -5.991 1.00 46.16 A O ANISOU 848 OH TYR A 117 5125 6875 5538 578 530 -356 A O ATOM 849 N PRO A 118 -30.042 1.136 -7.370 1.00 44.98 A N ANISOU 849 N PRO A 118 5358 5816 5917 1013 347 -647 A N ATOM 850 CA PRO A 118 -30.769 2.407 -7.482 1.00 46.01 A C ANISOU 850 CA PRO A 118 5495 5937 6051 1197 381 -715 A C ATOM 851 C PRO A 118 -31.892 2.629 -6.468 1.00 50.33 A C ANISOU 851 C PRO A 118 5987 6687 6451 1313 446 -788 A C ATOM 852 O PRO A 118 -32.376 3.757 -6.372 1.00 55.15 A O ANISOU 852 O PRO A 118 6626 7271 7058 1494 465 -872 A O ATOM 853 CB PRO A 118 -31.348 2.344 -8.901 1.00 43.95 A C ANISOU 853 CB PRO A 118 5150 5698 5851 1220 399 -622 A C ATOM 854 CG PRO A 118 -31.513 0.899 -9.170 1.00 43.73 A C ANISOU 854 CG PRO A 118 5030 5802 5783 1063 408 -524 A C ATOM 855 CD PRO A 118 -30.369 0.210 -8.470 1.00 42.21 A C ANISOU 855 CD PRO A 118 4917 5526 5593 927 358 -530 A C ATOM 856 N ALA A 119 -32.303 1.605 -5.727 1.00 48.31 A N ANISOU 856 N ALA A 119 5659 6628 6069 1219 480 -759 A N ATOM 857 CA ALA A 119 -33.447 1.764 -4.830 1.00 46.44 A C ANISOU 857 CA ALA A 119 5342 6630 5675 1319 557 -820 A C ATOM 858 C ALA A 119 -33.061 1.756 -3.351 1.00 49.99 A C ANISOU 858 C ALA A 119 5870 7113 6011 1300 554 -907 A C ATOM 859 O ALA A 119 -32.013 1.236 -2.968 1.00 50.80 A O ANISOU 859 O ALA A 119 6062 7105 6135 1168 492 -888 A O ATOM 860 CB ALA A 119 -34.482 0.685 -5.106 1.00 44.69 A C ANISOU 860 CB ALA A 119 4955 6662 5363 1224 615 -716 A C ATOM 861 N ALA A 120 -33.939 2.329 -2.531 1.00 51.38 A N ANISOU 861 N ALA A 120 6004 7461 6058 1446 621 -1005 A N ATOM 862 CA ALA A 120 -33.725 2.489 -1.097 1.00 47.82 A C ANISOU 862 CA ALA A 120 5626 7070 5474 1462 628 -1109 A C ATOM 863 C ALA A 120 -35.054 2.324 -0.355 1.00 53.62 A C ANISOU 863 C ALA A 120 6220 8141 6011 1532 738 -1139 A C ATOM 864 O ALA A 120 -36.116 2.564 -0.933 1.00 57.33 A O ANISOU 864 O ALA A 120 6554 8760 6470 1643 800 -1129 A O ATOM 865 CB ALA A 120 -33.110 3.853 -0.807 1.00 43.72 A C ANISOU 865 CB ALA A 120 5260 6332 5019 1616 580 -1260 A C ATOM 866 N PRO A 121 -35.011 1.917 0.926 1.00 52.80 A N ANISOU 866 N PRO A 121 6141 8180 5742 1468 761 -1173 A N ATOM 867 CA PRO A 121 -33.811 1.586 1.700 1.00 51.92 A C ANISOU 867 CA PRO A 121 6180 7927 5619 1344 682 -1183 A C ATOM 868 C PRO A 121 -33.401 0.126 1.546 1.00 52.11 A C ANISOU 868 C PRO A 121 6194 7963 5642 1101 646 -1016 A C ATOM 869 O PRO A 121 -34.224 -0.785 1.673 1.00 52.25 A O ANISOU 869 O PRO A 121 6103 8208 5543 996 711 -918 A O ATOM 870 CB PRO A 121 -34.233 1.892 3.137 1.00 51.30 A C ANISOU 870 CB PRO A 121 6115 8048 5330 1422 739 -1302 A C ATOM 871 CG PRO A 121 -35.691 1.592 3.156 1.00 53.01 A C ANISOU 871 CG PRO A 121 6138 8595 5408 1461 864 -1268 A C ATOM 872 CD PRO A 121 -36.223 1.890 1.767 1.00 54.06 A C ANISOU 872 CD PRO A 121 6171 8679 5692 1542 875 -1222 A C ATOM 873 N LEU A 122 -32.126 -0.081 1.245 1.00 50.00 A N ANISOU 873 N LEU A 122 6043 7450 5506 1013 540 -984 A N ATOM 874 CA LEU A 122 -31.563 -1.417 1.191 1.00 48.27 A C ANISOU 874 CA LEU A 122 5849 7204 5287 812 486 -845 A C ATOM 875 C LEU A 122 -31.121 -1.819 2.596 1.00 49.71 A C ANISOU 875 C LEU A 122 6120 7456 5310 746 457 -866 A C ATOM 876 O LEU A 122 -30.381 -1.083 3.251 1.00 47.89 A O ANISOU 876 O LEU A 122 5990 7128 5078 817 404 -983 A O ATOM 877 CB LEU A 122 -30.386 -1.468 0.216 1.00 45.07 A C ANISOU 877 CB LEU A 122 5510 6530 5085 768 388 -808 A C ATOM 878 CG LEU A 122 -29.937 -2.854 -0.246 1.00 43.21 A C ANISOU 878 CG LEU A 122 5283 6250 4886 596 336 -661 A C ATOM 879 CD1 LEU A 122 -31.072 -3.572 -0.960 1.00 35.89 A C ANISOU 879 CD1 LEU A 122 4238 5469 3931 530 408 -554 A C ATOM 880 CD2 LEU A 122 -28.717 -2.748 -1.145 1.00 43.97 A C ANISOU 880 CD2 LEU A 122 5433 6103 5172 583 246 -653 A C ATOM 881 N PRO A 123 -31.605 -2.971 3.080 1.00 49.90 A N ANISOU 881 N PRO A 123 6115 7654 5190 604 489 -750 A N ATOM 882 CA PRO A 123 -31.140 -3.484 4.372 1.00 49.57 A C ANISOU 882 CA PRO A 123 6174 7673 4990 526 450 -741 A C ATOM 883 C PRO A 123 -29.877 -4.316 4.210 1.00 49.77 A C ANISOU 883 C PRO A 123 6311 7495 5104 414 320 -654 A C ATOM 884 O PRO A 123 -29.510 -4.664 3.087 1.00 46.58 A O ANISOU 884 O PRO A 123 5894 6939 4867 377 279 -587 A O ATOM 885 CB PRO A 123 -32.306 -4.351 4.840 1.00 47.68 A C ANISOU 885 CB PRO A 123 5851 7709 4556 412 547 -637 A C ATOM 886 CG PRO A 123 -32.892 -4.877 3.556 1.00 46.70 A C ANISOU 886 CG PRO A 123 5623 7576 4545 343 577 -531 A C ATOM 887 CD PRO A 123 -32.702 -3.785 2.523 1.00 47.29 A C ANISOU 887 CD PRO A 123 5659 7493 4815 507 566 -628 A C ATOM 888 N GLY A 124 -29.214 -4.625 5.318 1.00 52.73 A N ANISOU 888 N GLY A 124 6794 7880 5362 372 254 -659 A N ATOM 889 CA GLY A 124 -28.111 -5.562 5.290 1.00 48.75 A C ANISOU 889 CA GLY A 124 6391 7223 4909 275 129 -564 A C ATOM 890 C GLY A 124 -28.658 -6.958 5.058 1.00 47.32 A C ANISOU 890 C GLY A 124 6209 7102 4667 119 147 -383 A C ATOM 891 O GLY A 124 -29.871 -7.175 5.133 1.00 47.06 A O ANISOU 891 O GLY A 124 6096 7261 4522 64 257 -336 A O ATOM 892 N PHE A 125 -27.775 -7.909 4.773 1.00 44.76 A N ANISOU 892 N PHE A 125 5976 6619 4414 45 37 -286 A N ATOM 893 CA PHE A 125 -28.209 -9.277 4.530 1.00 44.68 A C ANISOU 893 CA PHE A 125 6003 6620 4354 -109 36 -115 A C ATOM 894 C PHE A 125 -27.071 -10.281 4.704 1.00 38.74 A C ANISOU 894 C PHE A 125 5398 5698 3623 -154 -109 -28 A C ATOM 895 O PHE A 125 -25.896 -9.918 4.697 1.00 43.78 A O ANISOU 895 O PHE A 125 6073 6203 4360 -60 -208 -101 A O ATOM 896 CB PHE A 125 -28.818 -9.401 3.119 1.00 42.38 A C ANISOU 896 CB PHE A 125 5608 6287 4205 -134 92 -80 A C ATOM 897 CG PHE A 125 -27.853 -9.092 2.010 1.00 39.05 A C ANISOU 897 CG PHE A 125 5180 5648 4010 -50 20 -128 A C ATOM 898 CD1 PHE A 125 -27.677 -7.790 1.567 1.00 36.77 A C ANISOU 898 CD1 PHE A 125 4812 5324 3836 85 48 -260 A C ATOM 899 CD2 PHE A 125 -27.123 -10.102 1.410 1.00 40.14 A C ANISOU 899 CD2 PHE A 125 5397 5618 4237 -104 -74 -42 A C ATOM 900 CE1 PHE A 125 -26.788 -7.504 0.554 1.00 38.58 A C ANISOU 900 CE1 PHE A 125 5032 5369 4259 142 -11 -294 A C ATOM 901 CE2 PHE A 125 -26.234 -9.822 0.386 1.00 40.34 A C ANISOU 901 CE2 PHE A 125 5399 5472 4454 -26 -130 -89 A C ATOM 902 CZ PHE A 125 -26.064 -8.524 -0.041 1.00 38.48 A C ANISOU 902 CZ PHE A 125 5075 5219 4325 86 -95 -210 A C ATOM 903 N SER A 126 -27.439 -11.545 4.873 1.00 39.51 A N ANISOU 903 N SER A 126 5583 5807 3622 -299 -125 127 A N ATOM 904 CA SER A 126 -26.479 -12.642 4.879 1.00 44.53 A C ANISOU 904 CA SER A 126 6373 6262 4286 -333 -265 226 A C ATOM 905 C SER A 126 -26.700 -13.493 3.636 1.00 45.68 A C ANISOU 905 C SER A 126 6525 6276 4556 -406 -272 313 A C ATOM 906 O SER A 126 -27.843 -13.708 3.239 1.00 48.95 A O ANISOU 906 O SER A 126 6875 6791 4933 -517 -172 366 A O ATOM 907 CB SER A 126 -26.632 -13.487 6.143 1.00 41.47 A C ANISOU 907 CB SER A 126 6131 5955 3672 -441 -301 346 A C ATOM 908 OG SER A 126 -26.509 -12.677 7.296 1.00 48.09 A O ANISOU 908 OG SER A 126 6959 6938 4376 -375 -287 256 A O ATOM 909 N ALA A 127 -25.625 -13.976 3.018 1.00 41.84 A N ANISOU 909 N ALA A 127 6108 5580 4208 -344 -389 320 A N ATOM 910 CA ALA A 127 -25.777 -14.751 1.792 1.00 40.67 A C ANISOU 910 CA ALA A 127 5973 5300 4179 -398 -399 382 A C ATOM 911 C ALA A 127 -24.644 -15.741 1.529 1.00 37.19 A C ANISOU 911 C ALA A 127 5679 4642 3810 -351 -548 432 A C ATOM 912 O ALA A 127 -23.485 -15.479 1.838 1.00 39.56 A O ANISOU 912 O ALA A 127 5998 4878 4156 -220 -642 371 A O ATOM 913 CB ALA A 127 -25.924 -13.809 0.604 1.00 40.14 A C ANISOU 913 CB ALA A 127 5737 5234 4281 -319 -325 274 A C ATOM 914 N VAL A 128 -25.007 -16.881 0.943 1.00 38.11 A N ANISOU 914 N VAL A 128 5897 4650 3933 -456 -571 537 A N ATOM 915 CA VAL A 128 -24.049 -17.868 0.456 1.00 38.48 A C ANISOU 915 CA VAL A 128 6084 4474 4064 -395 -705 574 A C ATOM 916 C VAL A 128 -24.072 -17.921 -1.077 1.00 43.43 A C ANISOU 916 C VAL A 128 6634 5006 4862 -370 -679 525 A C ATOM 917 O VAL A 128 -25.138 -17.990 -1.697 1.00 41.48 A O ANISOU 917 O VAL A 128 6332 4816 4613 -494 -587 552 A O ATOM 918 CB VAL A 128 -24.340 -19.269 1.030 1.00 41.91 A C ANISOU 918 CB VAL A 128 6750 4813 4361 -530 -778 736 A C ATOM 919 CG1 VAL A 128 -23.574 -20.340 0.266 1.00 39.68 A C ANISOU 919 CG1 VAL A 128 6617 4281 4180 -465 -903 766 A C ATOM 920 CG2 VAL A 128 -23.993 -19.312 2.516 1.00 40.94 A C ANISOU 920 CG2 VAL A 128 6729 4752 4073 -518 -839 788 A C ATOM 921 N VAL A 129 -22.888 -17.871 -1.680 1.00 44.89 A N ANISOU 921 N VAL A 129 6803 5068 5183 -209 -759 450 A N ATOM 922 CA VAL A 129 -22.759 -17.887 -3.130 1.00 41.73 A C ANISOU 922 CA VAL A 129 6330 4588 4937 -167 -738 395 A C ATOM 923 C VAL A 129 -22.171 -19.205 -3.616 1.00 44.08 A C ANISOU 923 C VAL A 129 6800 4678 5269 -131 -854 442 A C ATOM 924 O VAL A 129 -21.152 -19.663 -3.094 1.00 43.19 A O ANISOU 924 O VAL A 129 6790 4474 5147 -16 -975 448 A O ATOM 925 CB VAL A 129 -21.873 -16.735 -3.626 1.00 42.34 A C ANISOU 925 CB VAL A 129 6236 4702 5151 -12 -723 261 A C ATOM 926 CG1 VAL A 129 -21.735 -16.782 -5.143 1.00 42.32 A C ANISOU 926 CG1 VAL A 129 6163 4629 5290 26 -697 212 A C ATOM 927 CG2 VAL A 129 -22.445 -15.402 -3.179 1.00 43.94 A C ANISOU 927 CG2 VAL A 129 6294 5076 5324 -33 -617 204 A C ATOM 928 N VAL A 130 -22.828 -19.822 -4.598 1.00 42.90 A N ANISOU 928 N VAL A 130 6688 4458 5153 -224 -825 470 A N ATOM 929 CA VAL A 130 -22.283 -21.000 -5.264 1.00 42.62 A C ANISOU 929 CA VAL A 130 6815 4213 5167 -173 -929 486 A C ATOM 930 C VAL A 130 -22.396 -20.824 -6.772 1.00 44.61 A C ANISOU 930 C VAL A 130 6958 4448 5543 -151 -873 406 A C ATOM 931 O VAL A 130 -23.250 -20.077 -7.260 1.00 45.57 A O ANISOU 931 O VAL A 130 6928 4705 5682 -237 -757 384 A O ATOM 932 CB VAL A 130 -22.995 -22.307 -4.836 1.00 44.16 A C ANISOU 932 CB VAL A 130 7253 4286 5241 -344 -983 624 A C ATOM 933 CG1 VAL A 130 -22.934 -22.490 -3.328 1.00 46.14 A C ANISOU 933 CG1 VAL A 130 7620 4565 5348 -379 -1035 719 A C ATOM 934 CG2 VAL A 130 -24.429 -22.320 -5.308 1.00 45.43 A C ANISOU 934 CG2 VAL A 130 7365 4536 5361 -567 -873 668 A C ATOM 935 N SER A 131 -21.532 -21.504 -7.516 1.00 44.93 A N ANISOU 935 N SER A 131 7077 4332 5664 -22 -958 361 A N ATOM 936 CA SER A 131 -21.512 -21.334 -8.958 1.00 43.69 A C ANISOU 936 CA SER A 131 6818 4168 5614 17 -909 276 A C ATOM 937 C SER A 131 -20.999 -22.569 -9.685 1.00 43.68 A C ANISOU 937 C SER A 131 6992 3961 5645 93 -1009 259 A C ATOM 938 O SER A 131 -20.073 -23.240 -9.222 1.00 39.64 A O ANISOU 938 O SER A 131 6615 3322 5126 229 -1127 263 A O ATOM 939 CB SER A 131 -20.660 -20.121 -9.335 1.00 43.31 A C ANISOU 939 CB SER A 131 6548 4239 5670 169 -862 167 A C ATOM 940 OG SER A 131 -20.815 -19.796 -10.712 1.00 44.72 A O ANISOU 940 OG SER A 131 6612 4446 5933 177 -791 100 A O ATOM 941 N SER A 132 -21.614 -22.856 -10.829 1.00 43.43 A N ANISOU 941 N SER A 132 6961 3899 5644 13 -966 234 A N ATOM 942 CA SER A 132 -21.145 -23.912 -11.719 1.00 42.92 A C ANISOU 942 CA SER A 132 7045 3646 5616 98 -1048 187 A C ATOM 943 C SER A 132 -20.447 -23.300 -12.931 1.00 44.42 A C ANISOU 943 C SER A 132 7052 3909 5914 253 -998 57 A C ATOM 944 O SER A 132 -19.864 -24.011 -13.749 1.00 47.77 A O ANISOU 944 O SER A 132 7560 4214 6378 371 -1055 -13 A O ATOM 945 CB SER A 132 -22.305 -24.808 -12.162 1.00 39.88 A C ANISOU 945 CB SER A 132 6820 3161 5171 -115 -1050 246 A C ATOM 946 OG SER A 132 -23.385 -24.038 -12.664 1.00 38.80 A O ANISOU 946 OG SER A 132 6505 3205 5031 -274 -925 249 A O ATOM 947 N VAL A 133 -20.511 -21.975 -13.041 1.00 44.13 A N ANISOU 947 N VAL A 133 6776 4069 5920 251 -892 27 A N ATOM 948 CA VAL A 133 -19.799 -21.256 -14.096 1.00 42.84 A C ANISOU 948 CA VAL A 133 6431 3995 5852 381 -838 -80 A C ATOM 949 C VAL A 133 -18.316 -21.187 -13.750 1.00 44.62 A C ANISOU 949 C VAL A 133 6616 4213 6124 594 -907 -141 A C ATOM 950 O VAL A 133 -17.945 -20.667 -12.696 1.00 42.55 A O ANISOU 950 O VAL A 133 6307 4011 5849 620 -925 -117 A O ATOM 951 CB VAL A 133 -20.340 -19.824 -14.287 1.00 39.01 A C ANISOU 951 CB VAL A 133 5723 3703 5394 307 -710 -83 A C ATOM 952 CG1 VAL A 133 -19.832 -19.236 -15.585 1.00 38.31 A C ANISOU 952 CG1 VAL A 133 5482 3688 5387 394 -650 -171 A C ATOM 953 CG2 VAL A 133 -21.854 -19.813 -14.256 1.00 38.74 A C ANISOU 953 CG2 VAL A 133 5709 3716 5295 102 -650 -8 A C ATOM 954 N PRO A 134 -17.459 -21.716 -14.633 1.00 45.39 A N ANISOU 954 N PRO A 134 6725 4253 6268 751 -947 -229 A N ATOM 955 CA PRO A 134 -16.017 -21.723 -14.354 1.00 44.93 A C ANISOU 955 CA PRO A 134 6610 4213 6250 967 -1017 -295 A C ATOM 956 C PRO A 134 -15.471 -20.309 -14.199 1.00 44.69 A C ANISOU 956 C PRO A 134 6327 4380 6273 984 -943 -329 A C ATOM 957 O PRO A 134 -15.630 -19.493 -15.104 1.00 45.79 A O ANISOU 957 O PRO A 134 6310 4629 6457 940 -839 -366 A O ATOM 958 CB PRO A 134 -15.423 -22.416 -15.584 1.00 44.85 A C ANISOU 958 CB PRO A 134 6623 4146 6274 1112 -1038 -395 A C ATOM 959 CG PRO A 134 -16.461 -22.240 -16.659 1.00 43.78 A C ANISOU 959 CG PRO A 134 6466 4033 6137 961 -940 -396 A C ATOM 960 CD PRO A 134 -17.776 -22.294 -15.950 1.00 43.32 A C ANISOU 960 CD PRO A 134 6514 3930 6017 742 -927 -281 A C ATOM 961 N LEU A 135 -14.835 -20.028 -13.066 1.00 44.92 A N ANISOU 961 N LEU A 135 6330 4447 6290 1041 -1003 -313 A N ATOM 962 CA LEU A 135 -14.402 -18.670 -12.755 1.00 42.95 A C ANISOU 962 CA LEU A 135 5869 4367 6082 1024 -944 -341 A C ATOM 963 C LEU A 135 -13.351 -18.162 -13.733 1.00 42.99 A C ANISOU 963 C LEU A 135 5679 4488 6166 1135 -905 -441 A C ATOM 964 O LEU A 135 -12.274 -18.739 -13.862 1.00 44.26 A O ANISOU 964 O LEU A 135 5823 4650 6342 1308 -981 -502 A O ATOM 965 CB LEU A 135 -13.861 -18.591 -11.323 1.00 42.74 A C ANISOU 965 CB LEU A 135 5867 4356 6014 1069 -1035 -314 A C ATOM 966 CG LEU A 135 -14.849 -18.983 -10.223 1.00 40.32 A C ANISOU 966 CG LEU A 135 5740 3968 5611 948 -1066 -207 A C ATOM 967 CD1 LEU A 135 -14.358 -18.524 -8.851 1.00 40.80 A C ANISOU 967 CD1 LEU A 135 5778 4097 5626 970 -1128 -190 A C ATOM 968 CD2 LEU A 135 -16.235 -18.432 -10.518 1.00 33.40 A C ANISOU 968 CD2 LEU A 135 4849 3125 4719 756 -943 -160 A C ATOM 969 N GLY A 136 -13.678 -17.079 -14.427 1.00 41.63 A N ANISOU 969 N GLY A 136 5359 4421 6038 1037 -787 -454 A N ATOM 970 CA GLY A 136 -12.753 -16.468 -15.361 1.00 43.20 A C ANISOU 970 CA GLY A 136 5366 4747 6301 1102 -734 -533 A C ATOM 971 C GLY A 136 -12.438 -17.320 -16.576 1.00 45.37 A C ANISOU 971 C GLY A 136 5659 4998 6582 1210 -731 -592 A C ATOM 972 O GLY A 136 -11.450 -17.071 -17.263 1.00 47.49 A O ANISOU 972 O GLY A 136 5773 5384 6887 1303 -706 -667 A O ATOM 973 N GLY A 137 -13.278 -18.318 -16.843 1.00 42.97 A N ANISOU 973 N GLY A 137 5542 4550 6236 1189 -755 -564 A N ATOM 974 CA GLY A 137 -13.062 -19.230 -17.952 1.00 42.64 A C ANISOU 974 CA GLY A 137 5556 4459 6187 1294 -764 -631 A C ATOM 975 C GLY A 137 -13.627 -18.756 -19.284 1.00 44.40 A C ANISOU 975 C GLY A 137 5699 4751 6418 1205 -648 -648 A C ATOM 976 O GLY A 137 -13.462 -19.428 -20.303 1.00 43.89 A O ANISOU 976 O GLY A 137 5670 4666 6339 1285 -644 -714 A O ATOM 977 N GLY A 138 -14.305 -17.609 -19.281 1.00 42.08 A N ANISOU 977 N GLY A 138 5309 4538 6140 1049 -558 -589 A N ATOM 978 CA GLY A 138 -14.782 -17.004 -20.512 1.00 39.64 A C ANISOU 978 CA GLY A 138 4912 4314 5838 972 -451 -593 A C ATOM 979 C GLY A 138 -16.275 -17.142 -20.755 1.00 40.51 A C ANISOU 979 C GLY A 138 5126 4359 5906 824 -421 -528 A C ATOM 980 O GLY A 138 -16.776 -16.813 -21.835 1.00 41.13 A O ANISOU 980 O GLY A 138 5155 4497 5975 768 -348 -529 A O ATOM 981 N LEU A 139 -16.990 -17.621 -19.744 1.00 39.64 A N ANISOU 981 N LEU A 139 5155 4144 5764 756 -478 -467 A N ATOM 982 CA LEU A 139 -18.429 -17.813 -19.841 1.00 35.02 A C ANISOU 982 CA LEU A 139 4657 3518 5130 603 -456 -401 A C ATOM 983 C LEU A 139 -19.195 -16.875 -18.910 1.00 35.53 A C ANISOU 983 C LEU A 139 4670 3640 5190 489 -415 -322 A C ATOM 984 O LEU A 139 -20.335 -17.159 -18.538 1.00 36.22 A O ANISOU 984 O LEU A 139 4837 3699 5224 367 -415 -260 A O ATOM 985 CB LEU A 139 -18.781 -19.267 -19.539 1.00 33.97 A C ANISOU 985 CB LEU A 139 4744 3219 4944 590 -551 -391 A C ATOM 986 CG LEU A 139 -18.166 -20.276 -20.514 1.00 34.99 A C ANISOU 986 CG LEU A 139 4956 3269 5068 711 -597 -483 A C ATOM 987 CD1 LEU A 139 -18.488 -21.710 -20.084 1.00 33.33 A C ANISOU 987 CD1 LEU A 139 5002 2854 4808 696 -708 -467 A C ATOM 988 CD2 LEU A 139 -18.623 -19.999 -21.966 1.00 30.60 A C ANISOU 988 CD2 LEU A 139 4324 2799 4503 664 -517 -520 A C ATOM 989 N SER A 140 -18.549 -15.769 -18.536 1.00 37.15 A N ANISOU 989 N SER A 140 4741 3931 5444 528 -380 -332 A N ATOM 990 CA SER A 140 -19.177 -14.683 -17.771 1.00 36.01 A C ANISOU 990 CA SER A 140 4535 3848 5299 445 -332 -280 A C ATOM 991 C SER A 140 -19.635 -15.054 -16.368 1.00 34.05 A C ANISOU 991 C SER A 140 4391 3551 4997 397 -384 -230 A C ATOM 992 O SER A 140 -20.756 -14.731 -15.963 1.00 33.66 A O ANISOU 992 O SER A 140 4348 3536 4904 295 -344 -175 A O ATOM 993 CB SER A 140 -20.369 -14.125 -18.541 1.00 37.53 A C ANISOU 993 CB SER A 140 4679 4105 5476 349 -250 -242 A C ATOM 994 OG SER A 140 -19.935 -13.527 -19.737 1.00 33.43 A O ANISOU 994 OG SER A 140 4055 3649 4998 386 -194 -275 A O ATOM 995 N SER A 141 -18.764 -15.722 -15.624 1.00 33.21 A N ANISOU 995 N SER A 141 4359 3376 4884 478 -473 -247 A N ATOM 996 CA SER A 141 -19.035 -16.012 -14.227 1.00 36.96 A C ANISOU 996 CA SER A 141 4933 3813 5299 440 -528 -195 A C ATOM 997 C SER A 141 -19.368 -14.731 -13.461 1.00 34.56 A C ANISOU 997 C SER A 141 4532 3607 4992 390 -470 -182 A C ATOM 998 O SER A 141 -20.331 -14.693 -12.701 1.00 31.25 A O ANISOU 998 O SER A 141 4162 3208 4504 298 -452 -126 A O ATOM 999 CB SER A 141 -17.840 -16.724 -13.590 1.00 34.24 A C ANISOU 999 CB SER A 141 4658 3398 4955 566 -639 -223 A C ATOM 1000 OG SER A 141 -16.648 -15.996 -13.814 1.00 30.74 A O ANISOU 1000 OG SER A 141 4067 3032 4582 671 -635 -295 A O ATOM 1001 N SER A 142 -18.589 -13.678 -13.689 1.00 34.73 A N ANISOU 1001 N SER A 142 4419 3694 5083 445 -439 -236 A N ATOM 1002 CA SER A 142 -18.797 -12.423 -12.974 1.00 40.77 A C ANISOU 1002 CA SER A 142 5112 4527 5851 409 -396 -239 A C ATOM 1003 C SER A 142 -20.166 -11.810 -13.276 1.00 40.17 A C ANISOU 1003 C SER A 142 5011 4501 5752 322 -304 -200 A C ATOM 1004 O SER A 142 -20.852 -11.341 -12.361 1.00 40.89 A O ANISOU 1004 O SER A 142 5115 4632 5791 280 -283 -180 A O ATOM 1005 CB SER A 142 -17.686 -11.419 -13.305 1.00 44.16 A C ANISOU 1005 CB SER A 142 5413 5002 6364 461 -383 -303 A C ATOM 1006 OG SER A 142 -17.766 -10.960 -14.645 1.00 43.39 A O ANISOU 1006 OG SER A 142 5234 4933 6321 450 -310 -311 A O ATOM 1007 N ALA A 143 -20.562 -11.809 -14.548 1.00 35.39 A N ANISOU 1007 N ALA A 143 4363 3907 5175 306 -253 -194 A N ATOM 1008 CA ALA A 143 -21.861 -11.258 -14.925 1.00 34.21 A C ANISOU 1008 CA ALA A 143 4177 3821 5002 241 -175 -157 A C ATOM 1009 C ALA A 143 -22.987 -12.010 -14.224 1.00 33.53 A C ANISOU 1009 C ALA A 143 4171 3751 4820 156 -183 -101 A C ATOM 1010 O ALA A 143 -23.985 -11.411 -13.822 1.00 33.77 A O ANISOU 1010 O ALA A 143 4163 3863 4807 115 -129 -76 A O ATOM 1011 CB ALA A 143 -22.050 -11.303 -16.426 1.00 37.84 A C ANISOU 1011 CB ALA A 143 4589 4295 5494 238 -135 -156 A C ATOM 1012 N SER A 144 -22.820 -13.323 -14.076 1.00 31.97 A N ANISOU 1012 N SER A 144 4086 3476 4584 132 -251 -80 A N ATOM 1013 CA SER A 144 -23.810 -14.139 -13.383 1.00 29.39 A C ANISOU 1013 CA SER A 144 3854 3155 4159 24 -265 -14 A C ATOM 1014 C SER A 144 -23.832 -13.796 -11.895 1.00 34.15 A C ANISOU 1014 C SER A 144 4480 3794 4702 18 -274 2 A C ATOM 1015 O SER A 144 -24.891 -13.801 -11.260 1.00 32.37 A O ANISOU 1015 O SER A 144 4260 3650 4388 -73 -237 50 A O ATOM 1016 CB SER A 144 -23.522 -15.632 -13.579 1.00 32.54 A C ANISOU 1016 CB SER A 144 4403 3426 4533 1 -348 5 A C ATOM 1017 OG SER A 144 -22.308 -16.020 -12.945 1.00 37.79 A O ANISOU 1017 OG SER A 144 5142 4001 5216 100 -433 -19 A O ATOM 1018 N LEU A 145 -22.661 -13.502 -11.338 1.00 34.29 A N ANISOU 1018 N LEU A 145 4502 3769 4757 113 -325 -42 A N ATOM 1019 CA LEU A 145 -22.583 -13.118 -9.931 1.00 36.76 A C ANISOU 1019 CA LEU A 145 4838 4122 5007 115 -341 -39 A C ATOM 1020 C LEU A 145 -23.260 -11.768 -9.729 1.00 37.71 A C ANISOU 1020 C LEU A 145 4849 4355 5125 112 -252 -67 A C ATOM 1021 O LEU A 145 -24.063 -11.598 -8.807 1.00 42.88 A O ANISOU 1021 O LEU A 145 5516 5091 5685 63 -220 -42 A O ATOM 1022 CB LEU A 145 -21.131 -13.079 -9.443 1.00 36.04 A C ANISOU 1022 CB LEU A 145 4762 3974 4957 218 -426 -88 A C ATOM 1023 CG LEU A 145 -20.933 -12.662 -7.976 1.00 37.86 A C ANISOU 1023 CG LEU A 145 5019 4249 5116 226 -457 -96 A C ATOM 1024 CD1 LEU A 145 -21.802 -13.496 -7.052 1.00 42.26 A C ANISOU 1024 CD1 LEU A 145 5697 4822 5538 135 -470 -11 A C ATOM 1025 CD2 LEU A 145 -19.473 -12.773 -7.563 1.00 35.86 A C ANISOU 1025 CD2 LEU A 145 4776 3952 4899 325 -558 -142 A C ATOM 1026 N GLU A 146 -22.949 -10.818 -10.604 1.00 32.96 A N ANISOU 1026 N GLU A 146 4148 3757 4619 168 -211 -117 A N ATOM 1027 CA GLU A 146 -23.542 -9.486 -10.531 1.00 37.21 A C ANISOU 1027 CA GLU A 146 4602 4370 5166 187 -135 -147 A C ATOM 1028 C GLU A 146 -25.065 -9.529 -10.673 1.00 38.02 A C ANISOU 1028 C GLU A 146 4673 4576 5197 127 -63 -100 A C ATOM 1029 O GLU A 146 -25.791 -8.882 -9.913 1.00 38.93 A O ANISOU 1029 O GLU A 146 4761 4782 5250 133 -17 -111 A O ATOM 1030 CB GLU A 146 -22.936 -8.577 -11.609 1.00 38.67 A C ANISOU 1030 CB GLU A 146 4707 4519 5465 243 -110 -190 A C ATOM 1031 CG GLU A 146 -21.470 -8.232 -11.372 1.00 37.08 A C ANISOU 1031 CG GLU A 146 4501 4257 5330 291 -167 -247 A C ATOM 1032 CD GLU A 146 -20.709 -7.888 -12.650 1.00 39.87 A C ANISOU 1032 CD GLU A 146 4786 4579 5785 315 -154 -266 A C ATOM 1033 OE1 GLU A 146 -21.300 -7.950 -13.753 1.00 36.28 A O ANISOU 1033 OE1 GLU A 146 4301 4138 5346 302 -104 -233 A O ATOM 1034 OE2 GLU A 146 -19.507 -7.556 -12.542 1.00 42.09 A O1- ANISOU 1034 OE2 GLU A 146 5037 4836 6120 340 -193 -312 A O1- ATOM 1035 N VAL A 147 -25.551 -10.300 -11.638 1.00 35.39 A N ANISOU 1035 N VAL A 147 4338 4242 4867 71 -56 -55 A N ATOM 1036 CA VAL A 147 -26.983 -10.345 -11.912 1.00 33.65 A C ANISOU 1036 CA VAL A 147 4062 4143 4582 5 7 -12 A C ATOM 1037 C VAL A 147 -27.734 -11.098 -10.810 1.00 34.98 A C ANISOU 1037 C VAL A 147 4283 4385 4622 -97 5 40 A C ATOM 1038 O VAL A 147 -28.820 -10.683 -10.393 1.00 35.76 A O ANISOU 1038 O VAL A 147 4310 4632 4644 -123 70 52 A O ATOM 1039 CB VAL A 147 -27.259 -10.970 -13.293 1.00 33.88 A C ANISOU 1039 CB VAL A 147 4075 4154 4643 -41 5 15 A C ATOM 1040 CG1 VAL A 147 -28.730 -11.335 -13.442 1.00 31.37 A C ANISOU 1040 CG1 VAL A 147 3708 3973 4238 -145 49 68 A C ATOM 1041 CG2 VAL A 147 -26.821 -10.002 -14.400 1.00 29.15 A C ANISOU 1041 CG2 VAL A 147 3399 3531 4144 52 32 -23 A C ATOM 1042 N ALA A 148 -27.146 -12.186 -10.325 1.00 34.83 A N ANISOU 1042 N ALA A 148 4390 4271 4573 -148 -69 72 A N ATOM 1043 CA ALA A 148 -27.683 -12.873 -9.155 1.00 35.46 A C ANISOU 1043 CA ALA A 148 4545 4405 4522 -250 -78 131 A C ATOM 1044 C ALA A 148 -27.760 -11.923 -7.963 1.00 38.86 A C ANISOU 1044 C ALA A 148 4937 4933 4894 -193 -41 94 A C ATOM 1045 O ALA A 148 -28.750 -11.916 -7.227 1.00 38.82 A O ANISOU 1045 O ALA A 148 4904 5074 4771 -264 14 127 A O ATOM 1046 CB ALA A 148 -26.837 -14.085 -8.806 1.00 35.96 A C ANISOU 1046 CB ALA A 148 4774 4317 4572 -280 -181 170 A C ATOM 1047 N THR A 149 -26.715 -11.122 -7.776 1.00 39.40 A N ANISOU 1047 N THR A 149 5001 4932 5039 -72 -69 20 A N ATOM 1048 CA THR A 149 -26.696 -10.159 -6.679 1.00 38.40 A C ANISOU 1048 CA THR A 149 4852 4879 4861 -11 -44 -35 A C ATOM 1049 C THR A 149 -27.803 -9.125 -6.876 1.00 39.99 A C ANISOU 1049 C THR A 149 4932 5219 5045 25 58 -68 A C ATOM 1050 O THR A 149 -28.551 -8.821 -5.935 1.00 42.90 A O ANISOU 1050 O THR A 149 5278 5725 5300 18 109 -76 A O ATOM 1051 CB THR A 149 -25.327 -9.449 -6.556 1.00 34.89 A C ANISOU 1051 CB THR A 149 4420 4326 4511 95 -101 -115 A C ATOM 1052 CG2 THR A 149 -25.378 -8.357 -5.498 1.00 31.99 A C ANISOU 1052 CG2 THR A 149 4037 4028 4091 154 -76 -188 A C ATOM 1053 OG1 THR A 149 -24.323 -10.405 -6.191 1.00 35.28 A O ANISOU 1053 OG1 THR A 149 4571 4278 4556 85 -201 -89 A O ATOM 1054 N TYR A 150 -27.918 -8.602 -8.098 1.00 35.60 A N ANISOU 1054 N TYR A 150 4299 4635 4592 73 86 -86 A N ATOM 1055 CA TYR A 150 -28.963 -7.628 -8.403 1.00 29.91 A C ANISOU 1055 CA TYR A 150 3467 4037 3862 132 171 -112 A C ATOM 1056 C TYR A 150 -30.335 -8.235 -8.148 1.00 31.48 A C ANISOU 1056 C TYR A 150 3608 4420 3933 36 227 -52 A C ATOM 1057 O TYR A 150 -31.214 -7.593 -7.560 1.00 33.17 A O ANISOU 1057 O TYR A 150 3746 4792 4064 80 295 -81 A O ATOM 1058 CB TYR A 150 -28.878 -7.128 -9.857 1.00 31.13 A C ANISOU 1058 CB TYR A 150 3561 4130 4136 186 181 -118 A C ATOM 1059 CG TYR A 150 -29.676 -5.858 -10.047 1.00 30.19 A C ANISOU 1059 CG TYR A 150 3353 4096 4021 296 248 -161 A C ATOM 1060 CD1 TYR A 150 -31.063 -5.887 -10.076 1.00 29.90 A C ANISOU 1060 CD1 TYR A 150 3218 4246 3898 287 311 -134 A C ATOM 1061 CD2 TYR A 150 -29.046 -4.628 -10.139 1.00 29.88 A C ANISOU 1061 CD2 TYR A 150 3333 3954 4067 410 243 -229 A C ATOM 1062 CE1 TYR A 150 -31.798 -4.738 -10.194 1.00 31.37 A C ANISOU 1062 CE1 TYR A 150 3324 4514 4080 418 365 -178 A C ATOM 1063 CE2 TYR A 150 -29.775 -3.469 -10.271 1.00 30.73 A C ANISOU 1063 CE2 TYR A 150 3387 4114 4175 528 294 -268 A C ATOM 1064 CZ TYR A 150 -31.154 -3.531 -10.303 1.00 32.45 A C ANISOU 1064 CZ TYR A 150 3505 4519 4306 547 354 -245 A C ATOM 1065 OH TYR A 150 -31.902 -2.383 -10.437 1.00 34.14 A O ANISOU 1065 OH TYR A 150 3663 4792 4517 695 398 -288 A O ATOM 1066 N THR A 151 -30.517 -9.471 -8.597 1.00 35.05 A N ANISOU 1066 N THR A 151 4094 4858 4365 -98 198 27 A N ATOM 1067 CA THR A 151 -31.799 -10.152 -8.445 1.00 36.78 A C ANISOU 1067 CA THR A 151 4258 5254 4464 -231 245 95 A C ATOM 1068 C THR A 151 -32.134 -10.312 -6.969 1.00 39.81 A C ANISOU 1068 C THR A 151 4671 5755 4701 -283 271 110 A C ATOM 1069 O THR A 151 -33.282 -10.147 -6.560 1.00 41.25 A O ANISOU 1069 O THR A 151 4748 6155 4771 -321 349 122 A O ATOM 1070 CB THR A 151 -31.791 -11.528 -9.127 1.00 36.84 A C ANISOU 1070 CB THR A 151 4339 5182 4475 -386 192 174 A C ATOM 1071 CG2 THR A 151 -33.168 -12.167 -9.062 1.00 34.64 A C ANISOU 1071 CG2 THR A 151 3990 5098 4075 -551 240 244 A C ATOM 1072 OG1 THR A 151 -31.404 -11.372 -10.497 1.00 42.60 A O ANISOU 1072 OG1 THR A 151 5046 5811 5331 -329 168 150 A O ATOM 1073 N PHE A 152 -31.117 -10.618 -6.172 1.00 40.52 A N ANISOU 1073 N PHE A 152 4895 5716 4784 -278 206 107 A N ATOM 1074 CA PHE A 152 -31.291 -10.751 -4.734 1.00 39.78 A C ANISOU 1074 CA PHE A 152 4849 5724 4544 -320 220 121 A C ATOM 1075 C PHE A 152 -31.714 -9.428 -4.104 1.00 38.09 A C ANISOU 1075 C PHE A 152 4534 5653 4284 -185 297 26 A C ATOM 1076 O PHE A 152 -32.633 -9.398 -3.292 1.00 42.49 A O ANISOU 1076 O PHE A 152 5034 6417 4692 -228 368 37 A O ATOM 1077 CB PHE A 152 -30.004 -11.258 -4.079 1.00 40.44 A C ANISOU 1077 CB PHE A 152 5095 5633 4637 -313 118 130 A C ATOM 1078 CG PHE A 152 -30.155 -11.568 -2.618 1.00 44.52 A C ANISOU 1078 CG PHE A 152 5684 6247 4984 -375 120 165 A C ATOM 1079 CD1 PHE A 152 -30.655 -12.794 -2.208 1.00 48.04 A C ANISOU 1079 CD1 PHE A 152 6213 6733 5307 -556 109 286 A C ATOM 1080 CD2 PHE A 152 -29.807 -10.637 -1.657 1.00 41.07 A C ANISOU 1080 CD2 PHE A 152 5243 5861 4503 -264 131 78 A C ATOM 1081 CE1 PHE A 152 -30.801 -13.087 -0.871 1.00 46.84 A C ANISOU 1081 CE1 PHE A 152 6134 6679 4984 -624 113 332 A C ATOM 1082 CE2 PHE A 152 -29.951 -10.926 -0.321 1.00 44.98 A C ANISOU 1082 CE2 PHE A 152 5805 6460 4826 -321 134 110 A C ATOM 1083 CZ PHE A 152 -30.452 -12.153 0.074 1.00 47.09 A C ANISOU 1083 CZ PHE A 152 6150 6777 4964 -501 128 242 A C ATOM 1084 N LEU A 153 -31.051 -8.336 -4.478 1.00 36.05 A N ANISOU 1084 N LEU A 153 4261 5289 4148 -25 283 -70 A N ATOM 1085 CA LEU A 153 -31.359 -7.034 -3.886 1.00 38.50 A C ANISOU 1085 CA LEU A 153 4511 5693 4424 118 342 -175 A C ATOM 1086 C LEU A 153 -32.778 -6.573 -4.220 1.00 41.27 A C ANISOU 1086 C LEU A 153 4705 6256 4720 156 443 -183 A C ATOM 1087 O LEU A 153 -33.384 -5.809 -3.465 1.00 45.63 A O ANISOU 1087 O LEU A 153 5199 6960 5178 250 509 -254 A O ATOM 1088 CB LEU A 153 -30.344 -5.982 -4.337 1.00 31.65 A C ANISOU 1088 CB LEU A 153 3677 4640 3708 257 297 -267 A C ATOM 1089 CG LEU A 153 -28.880 -6.244 -3.959 1.00 41.50 A C ANISOU 1089 CG LEU A 153 5049 5708 5011 243 196 -281 A C ATOM 1090 CD1 LEU A 153 -28.006 -5.076 -4.373 1.00 30.48 A C ANISOU 1090 CD1 LEU A 153 3664 4166 3751 358 166 -375 A C ATOM 1091 CD2 LEU A 153 -28.701 -6.560 -2.453 1.00 32.17 A C ANISOU 1091 CD2 LEU A 153 3946 4596 3682 207 174 -289 A C ATOM 1092 N GLN A 154 -33.303 -7.047 -5.348 1.00 43.18 A N ANISOU 1092 N GLN A 154 4874 6519 5013 91 452 -117 A N ATOM 1093 CA GLN A 154 -34.664 -6.716 -5.770 1.00 42.63 A C ANISOU 1093 CA GLN A 154 4635 6671 4890 120 536 -115 A C ATOM 1094 C GLN A 154 -35.705 -7.242 -4.792 1.00 43.27 A C ANISOU 1094 C GLN A 154 4643 7018 4779 11 608 -76 A C ATOM 1095 O GLN A 154 -36.754 -6.628 -4.600 1.00 41.15 A O ANISOU 1095 O GLN A 154 4226 6980 4428 93 692 -118 A O ATOM 1096 CB GLN A 154 -34.948 -7.279 -7.163 1.00 40.94 A C ANISOU 1096 CB GLN A 154 4369 6429 4758 41 515 -45 A C ATOM 1097 CG GLN A 154 -34.279 -6.530 -8.297 1.00 40.56 A C ANISOU 1097 CG GLN A 154 4338 6196 4877 170 476 -85 A C ATOM 1098 CD GLN A 154 -34.703 -7.056 -9.650 1.00 40.97 A C ANISOU 1098 CD GLN A 154 4326 6262 4980 98 463 -22 A C ATOM 1099 NE2 GLN A 154 -35.843 -6.575 -10.138 1.00 39.14 A N ANISOU 1099 NE2 GLN A 154 3938 6219 4714 158 517 -25 A N ATOM 1100 OE1 GLN A 154 -34.024 -7.897 -10.246 1.00 39.32 A O ANISOU 1100 OE1 GLN A 154 4204 5904 4834 -3 401 24 A O ATOM 1101 N GLN A 155 -35.416 -8.388 -4.186 1.00 45.11 A N ANISOU 1101 N GLN A 155 4980 7226 4935 -172 573 7 A N ATOM 1102 CA GLN A 155 -36.301 -8.955 -3.173 1.00 48.98 A C ANISOU 1102 CA GLN A 155 5422 7961 5226 -308 640 61 A C ATOM 1103 C GLN A 155 -36.221 -8.168 -1.862 1.00 49.31 A C ANISOU 1103 C GLN A 155 5476 8099 5158 -187 684 -28 A C ATOM 1104 O GLN A 155 -37.214 -8.022 -1.150 1.00 51.79 A O ANISOU 1104 O GLN A 155 5676 8693 5311 -200 779 -38 A O ATOM 1105 CB GLN A 155 -35.960 -10.428 -2.938 1.00 48.34 A C ANISOU 1105 CB GLN A 155 5485 7787 5094 -544 576 189 A C ATOM 1106 CG GLN A 155 -36.217 -11.310 -4.146 1.00 44.58 A C ANISOU 1106 CG GLN A 155 5001 7245 4694 -687 539 271 A C ATOM 1107 CD GLN A 155 -37.677 -11.292 -4.562 1.00 47.61 A C ANISOU 1107 CD GLN A 155 5177 7915 4999 -763 628 295 A C ATOM 1108 NE2 GLN A 155 -37.927 -11.034 -5.845 1.00 43.87 A N ANISOU 1108 NE2 GLN A 155 4610 7419 4639 -710 618 275 A N ATOM 1109 OE1 GLN A 155 -38.572 -11.493 -3.736 1.00 48.72 A O ANISOU 1109 OE1 GLN A 155 5232 8313 4968 -869 705 330 A O ATOM 1110 N LEU A 156 -35.035 -7.655 -1.551 1.00 49.49 A N ANISOU 1110 N LEU A 156 5633 7907 5263 -72 615 -98 A N ATOM 1111 CA LEU A 156 -34.838 -6.867 -0.335 1.00 47.89 A C ANISOU 1111 CA LEU A 156 5464 7768 4963 47 641 -199 A C ATOM 1112 C LEU A 156 -35.424 -5.470 -0.496 1.00 47.09 A C ANISOU 1112 C LEU A 156 5243 7764 4884 268 712 -332 A C ATOM 1113 O LEU A 156 -35.854 -4.854 0.476 1.00 46.17 A O ANISOU 1113 O LEU A 156 5092 7814 4635 363 776 -418 A O ATOM 1114 CB LEU A 156 -33.354 -6.767 0.013 1.00 43.37 A C ANISOU 1114 CB LEU A 156 5068 6937 4473 87 532 -236 A C ATOM 1115 CG LEU A 156 -32.580 -8.070 0.228 1.00 46.34 A C ANISOU 1115 CG LEU A 156 5589 7182 4837 -82 441 -119 A C ATOM 1116 CD1 LEU A 156 -31.118 -7.779 0.526 1.00 43.81 A C ANISOU 1116 CD1 LEU A 156 5404 6638 4604 -3 333 -179 A C ATOM 1117 CD2 LEU A 156 -33.197 -8.888 1.351 1.00 49.93 A C ANISOU 1117 CD2 LEU A 156 6068 7831 5072 -234 481 -34 A C ATOM 1118 N CYS A 157 -35.433 -4.978 -1.734 1.00 43.88 A N ANISOU 1118 N CYS A 157 4785 7250 4639 358 696 -349 A N ATOM 1119 CA CYS A 157 -35.845 -3.608 -2.020 1.00 43.12 A C ANISOU 1119 CA CYS A 157 4612 7183 4591 588 739 -468 A C ATOM 1120 C CYS A 157 -36.112 -3.436 -3.521 1.00 43.82 A C ANISOU 1120 C CYS A 157 4622 7204 4824 627 726 -431 A C ATOM 1121 O CYS A 157 -35.228 -3.017 -4.276 1.00 40.24 A O ANISOU 1121 O CYS A 157 4254 6501 4532 683 658 -447 A O ATOM 1122 CB CYS A 157 -34.772 -2.620 -1.540 1.00 40.05 A C ANISOU 1122 CB CYS A 157 4367 6579 4271 728 683 -588 A C ATOM 1123 SG CYS A 157 -35.281 -0.882 -1.501 1.00 52.98 A S ANISOU 1123 SG CYS A 157 5966 8238 5927 1022 732 -756 A S ATOM 1124 N PRO A 158 -37.334 -3.786 -3.956 1.00 46.10 A N ANISOU 1124 N PRO A 158 4739 7733 5044 586 791 -377 A N ATOM 1125 CA PRO A 158 -37.749 -3.719 -5.363 1.00 45.77 A C ANISOU 1125 CA PRO A 158 4604 7678 5109 610 780 -334 A C ATOM 1126 C PRO A 158 -37.375 -2.403 -6.041 1.00 46.47 A C ANISOU 1126 C PRO A 158 4729 7588 5338 839 751 -417 A C ATOM 1127 O PRO A 158 -37.717 -1.335 -5.529 1.00 47.01 A O ANISOU 1127 O PRO A 158 4778 7716 5369 1039 791 -524 A O ATOM 1128 CB PRO A 158 -39.272 -3.872 -5.282 1.00 47.23 A C ANISOU 1128 CB PRO A 158 4570 8224 5152 600 873 -315 A C ATOM 1129 CG PRO A 158 -39.508 -4.653 -4.019 1.00 49.93 A C ANISOU 1129 CG PRO A 158 4915 8740 5318 440 920 -284 A C ATOM 1130 CD PRO A 158 -38.410 -4.275 -3.071 1.00 46.25 A C ANISOU 1130 CD PRO A 158 4634 8078 4860 500 881 -354 A C ATOM 1131 N ASP A 159 -36.673 -2.471 -7.171 1.00 46.32 A N ANISOU 1131 N ASP A 159 4776 7351 5472 812 683 -371 A N ATOM 1132 CA ASP A 159 -36.458 -1.261 -7.950 1.00 47.91 A C ANISOU 1132 CA ASP A 159 5006 7403 5796 1006 660 -425 A C ATOM 1133 C ASP A 159 -37.732 -0.990 -8.741 1.00 48.60 A C ANISOU 1133 C ASP A 159 4917 7695 5854 1103 703 -404 A C ATOM 1134 O ASP A 159 -38.756 -1.632 -8.509 1.00 49.74 A O ANISOU 1134 O ASP A 159 4908 8114 5875 1026 758 -368 A O ATOM 1135 CB ASP A 159 -35.224 -1.365 -8.866 1.00 50.27 A C ANISOU 1135 CB ASP A 159 5430 7416 6255 943 579 -384 A C ATOM 1136 CG ASP A 159 -35.307 -2.505 -9.885 1.00 52.38 A C ANISOU 1136 CG ASP A 159 5648 7705 6550 774 555 -272 A C ATOM 1137 OD1 ASP A 159 -36.409 -3.015 -10.172 1.00 54.75 A O ANISOU 1137 OD1 ASP A 159 5807 8224 6770 723 594 -224 A O ATOM 1138 OD2 ASP A 159 -34.241 -2.885 -10.417 1.00 50.77 A O1- ANISOU 1138 OD2 ASP A 159 5545 7301 6446 692 495 -240 A O1- ATOM 1139 N SER A 160 -37.680 -0.046 -9.670 1.00 52.60 A N ANISOU 1139 N SER A 160 5440 8080 6466 1264 676 -420 A N ATOM 1140 CA SER A 160 -38.858 0.249 -10.484 1.00 56.68 A C ANISOU 1140 CA SER A 160 5791 8789 6956 1377 702 -395 A C ATOM 1141 C SER A 160 -38.493 0.680 -11.900 1.00 55.79 A C ANISOU 1141 C SER A 160 5727 8495 6977 1431 642 -344 A C ATOM 1142 O SER A 160 -39.149 1.543 -12.483 1.00 57.54 A O ANISOU 1142 O SER A 160 5887 8764 7209 1626 643 -358 A O ATOM 1143 CB SER A 160 -39.706 1.332 -9.819 1.00 57.94 A C ANISOU 1143 CB SER A 160 5881 9097 7037 1632 756 -501 A C ATOM 1144 OG SER A 160 -38.981 2.542 -9.692 1.00 57.27 A O ANISOU 1144 OG SER A 160 5969 8748 7043 1810 720 -584 A O ATOM 1145 N GLY A 161 -37.454 0.062 -12.456 1.00 54.05 A N ANISOU 1145 N GLY A 161 5613 8076 6847 1265 590 -284 A N ATOM 1146 CA GLY A 161 -36.959 0.438 -13.770 1.00 51.87 A C ANISOU 1146 CA GLY A 161 5396 7624 6689 1295 538 -233 A C ATOM 1147 C GLY A 161 -36.982 -0.692 -14.784 1.00 52.28 A C ANISOU 1147 C GLY A 161 5391 7724 6750 1113 513 -138 A C ATOM 1148 O GLY A 161 -37.554 -1.747 -14.525 1.00 53.49 A O ANISOU 1148 O GLY A 161 5448 8060 6816 967 534 -107 A O ATOM 1149 N THR A 162 -36.361 -0.464 -15.943 1.00 50.94 A N ANISOU 1149 N THR A 162 5288 7389 6677 1115 469 -92 A N ATOM 1150 CA THR A 162 -36.284 -1.465 -17.008 1.00 48.62 A C ANISOU 1150 CA THR A 162 4960 7118 6394 959 440 -15 A C ATOM 1151 C THR A 162 -35.240 -2.534 -16.695 1.00 48.76 A C ANISOU 1151 C THR A 162 5076 7011 6439 768 417 -8 A C ATOM 1152 O THR A 162 -34.534 -2.453 -15.685 1.00 47.59 A O ANISOU 1152 O THR A 162 5017 6759 6305 758 419 -55 A O ATOM 1153 CB THR A 162 -35.934 -0.823 -18.368 1.00 50.81 A C ANISOU 1153 CB THR A 162 5282 7272 6752 1033 404 31 A C ATOM 1154 CG2 THR A 162 -36.955 0.248 -18.744 1.00 52.99 A C ANISOU 1154 CG2 THR A 162 5477 7654 7001 1245 411 33 A C ATOM 1155 OG1 THR A 162 -34.633 -0.227 -18.292 1.00 51.34 A O ANISOU 1155 OG1 THR A 162 5508 7080 6920 1050 384 9 A O ATOM 1156 N ILE A 163 -35.141 -3.530 -17.568 1.00 46.69 A N ANISOU 1156 N ILE A 163 4802 6760 6180 627 389 46 A N ATOM 1157 CA ILE A 163 -34.147 -4.583 -17.420 1.00 48.75 A C ANISOU 1157 CA ILE A 163 5163 6892 6468 471 358 52 A C ATOM 1158 C ILE A 163 -32.794 -4.071 -17.901 1.00 45.91 A C ANISOU 1158 C ILE A 163 4917 6306 6220 514 329 40 A C ATOM 1159 O ILE A 163 -31.742 -4.532 -17.452 1.00 44.96 A O ANISOU 1159 O ILE A 163 4889 6057 6138 448 305 19 A O ATOM 1160 CB ILE A 163 -34.549 -5.851 -18.200 1.00 51.60 A C ANISOU 1160 CB ILE A 163 5485 7336 6785 311 333 102 A C ATOM 1161 CG1 ILE A 163 -35.875 -6.396 -17.676 1.00 53.02 A C ANISOU 1161 CG1 ILE A 163 5544 7754 6846 230 361 120 A C ATOM 1162 CG2 ILE A 163 -33.487 -6.930 -18.085 1.00 51.33 A C ANISOU 1162 CG2 ILE A 163 5574 7146 6782 181 292 101 A C ATOM 1163 CD1 ILE A 163 -36.177 -7.789 -18.170 1.00 54.66 A C ANISOU 1163 CD1 ILE A 163 5750 8015 7005 28 329 162 A C ATOM 1164 N ALA A 164 -32.829 -3.098 -18.805 1.00 43.98 A N ANISOU 1164 N ALA A 164 4663 6026 6023 625 331 57 A N ATOM 1165 CA ALA A 164 -31.605 -2.498 -19.319 1.00 41.24 A C ANISOU 1165 CA ALA A 164 4412 5483 5773 652 312 55 A C ATOM 1166 C ALA A 164 -30.931 -1.671 -18.231 1.00 38.29 A C ANISOU 1166 C ALA A 164 4121 4986 5444 713 315 -5 A C ATOM 1167 O ALA A 164 -29.713 -1.711 -18.077 1.00 38.94 A O ANISOU 1167 O ALA A 164 4281 4926 5588 662 294 -26 A O ATOM 1168 CB ALA A 164 -31.896 -1.639 -20.550 1.00 38.76 A C ANISOU 1168 CB ALA A 164 4080 5165 5483 744 311 104 A C ATOM 1169 N ALA A 165 -31.728 -0.923 -17.477 1.00 37.48 A N ANISOU 1169 N ALA A 165 3992 4946 5300 827 340 -40 A N ATOM 1170 CA ALA A 165 -31.209 -0.200 -16.322 1.00 38.55 A C ANISOU 1170 CA ALA A 165 4210 4979 5457 882 341 -114 A C ATOM 1171 C ALA A 165 -30.495 -1.151 -15.353 1.00 37.55 A C ANISOU 1171 C ALA A 165 4120 4835 5312 760 325 -144 A C ATOM 1172 O ALA A 165 -29.468 -0.793 -14.782 1.00 39.11 A O ANISOU 1172 O ALA A 165 4404 4896 5559 750 300 -191 A O ATOM 1173 CB ALA A 165 -32.326 0.546 -15.611 1.00 34.31 A C ANISOU 1173 CB ALA A 165 3628 4554 4854 1030 375 -159 A C ATOM 1174 N ARG A 166 -31.022 -2.365 -15.194 1.00 36.88 A N ANISOU 1174 N ARG A 166 3975 4884 5153 660 331 -114 A N ATOM 1175 CA ARG A 166 -30.415 -3.353 -14.297 1.00 39.71 A C ANISOU 1175 CA ARG A 166 4384 5222 5483 547 306 -127 A C ATOM 1176 C ARG A 166 -29.089 -3.871 -14.825 1.00 41.09 A C ANISOU 1176 C ARG A 166 4626 5248 5738 474 258 -116 A C ATOM 1177 O ARG A 166 -28.111 -3.984 -14.075 1.00 41.01 A O ANISOU 1177 O ARG A 166 4685 5148 5750 450 224 -153 A O ATOM 1178 CB ARG A 166 -31.350 -4.537 -14.069 1.00 36.71 A C ANISOU 1178 CB ARG A 166 3941 5008 5000 442 321 -84 A C ATOM 1179 CG ARG A 166 -32.666 -4.170 -13.441 1.00 34.55 A C ANISOU 1179 CG ARG A 166 3572 4929 4626 499 376 -97 A C ATOM 1180 CD ARG A 166 -33.422 -5.411 -13.037 1.00 36.54 A C ANISOU 1180 CD ARG A 166 3774 5339 4768 350 389 -50 A C ATOM 1181 NE ARG A 166 -34.743 -5.070 -12.526 1.00 42.82 A N ANISOU 1181 NE ARG A 166 4444 6367 5458 398 451 -60 A N ATOM 1182 CZ ARG A 166 -35.864 -5.249 -13.210 1.00 43.36 A C ANISOU 1182 CZ ARG A 166 4378 6619 5477 378 476 -21 A C ATOM 1183 NH1 ARG A 166 -35.810 -5.781 -14.423 1.00 46.78 A N1+ ANISOU 1183 NH1 ARG A 166 4803 7015 5958 304 440 29 A N1+ ATOM 1184 NH2 ARG A 166 -37.032 -4.908 -12.682 1.00 38.89 A N ANISOU 1184 NH2 ARG A 166 3677 6290 4808 435 536 -39 A N ATOM 1185 N ALA A 167 -29.074 -4.210 -16.111 1.00 36.50 A N ANISOU 1185 N ALA A 167 4017 4662 5191 444 252 -69 A N ATOM 1186 CA ALA A 167 -27.861 -4.664 -16.766 1.00 34.26 A C ANISOU 1186 CA ALA A 167 3779 4263 4976 393 216 -65 A C ATOM 1187 C ALA A 167 -26.782 -3.600 -16.647 1.00 32.69 A C ANISOU 1187 C ALA A 167 3625 3935 4860 445 207 -103 A C ATOM 1188 O ALA A 167 -25.617 -3.906 -16.411 1.00 36.06 A O ANISOU 1188 O ALA A 167 4090 4282 5328 408 171 -130 A O ATOM 1189 CB ALA A 167 -28.136 -4.995 -18.243 1.00 34.41 A C ANISOU 1189 CB ALA A 167 3755 4316 5003 371 221 -16 A C ATOM 1190 N GLN A 168 -27.183 -2.344 -16.794 1.00 31.75 A N ANISOU 1190 N GLN A 168 3503 3798 4762 532 233 -107 A N ATOM 1191 CA GLN A 168 -26.239 -1.237 -16.766 1.00 34.34 A C ANISOU 1191 CA GLN A 168 3889 3990 5168 561 223 -138 A C ATOM 1192 C GLN A 168 -25.672 -1.002 -15.362 1.00 34.08 A C ANISOU 1192 C GLN A 168 3911 3906 5133 559 197 -212 A C ATOM 1193 O GLN A 168 -24.526 -0.582 -15.217 1.00 35.24 A O ANISOU 1193 O GLN A 168 4100 3949 5342 526 168 -245 A O ATOM 1194 CB GLN A 168 -26.903 0.031 -17.312 1.00 39.47 A C ANISOU 1194 CB GLN A 168 4549 4612 5834 660 249 -116 A C ATOM 1195 CG GLN A 168 -27.024 0.018 -18.835 1.00 47.41 A C ANISOU 1195 CG GLN A 168 5522 5632 6858 652 261 -39 A C ATOM 1196 CD GLN A 168 -28.101 0.952 -19.370 1.00 55.21 A C ANISOU 1196 CD GLN A 168 6503 6647 7828 771 280 -1 A C ATOM 1197 NE2 GLN A 168 -28.165 1.076 -20.690 1.00 54.44 A N ANISOU 1197 NE2 GLN A 168 6389 6556 7739 769 284 72 A N ATOM 1198 OE1 GLN A 168 -28.862 1.554 -18.609 1.00 59.97 A O ANISOU 1198 OE1 GLN A 168 7113 7271 8401 874 289 -38 A O ATOM 1199 N VAL A 169 -26.464 -1.291 -14.335 1.00 34.61 A N ANISOU 1199 N VAL A 169 3971 4062 5119 585 207 -239 A N ATOM 1200 CA VAL A 169 -25.969 -1.245 -12.961 1.00 33.28 A C ANISOU 1200 CA VAL A 169 3854 3867 4923 576 179 -308 A C ATOM 1201 C VAL A 169 -24.901 -2.313 -12.767 1.00 34.56 A C ANISOU 1201 C VAL A 169 4029 4006 5098 484 128 -303 A C ATOM 1202 O VAL A 169 -23.800 -2.035 -12.285 1.00 34.59 A O ANISOU 1202 O VAL A 169 4071 3930 5142 463 84 -350 A O ATOM 1203 CB VAL A 169 -27.100 -1.446 -11.937 1.00 34.83 A C ANISOU 1203 CB VAL A 169 4032 4196 5006 615 210 -328 A C ATOM 1204 CG1 VAL A 169 -26.528 -1.769 -10.550 1.00 39.05 A C ANISOU 1204 CG1 VAL A 169 4620 4727 5489 580 174 -383 A C ATOM 1205 CG2 VAL A 169 -27.990 -0.210 -11.885 1.00 29.83 A C ANISOU 1205 CG2 VAL A 169 3395 3580 4361 745 252 -364 A C ATOM 1206 N CYS A 170 -25.227 -3.532 -13.176 1.00 34.19 A N ANISOU 1206 N CYS A 170 3951 4026 5014 431 128 -248 A N ATOM 1207 CA CYS A 170 -24.288 -4.636 -13.102 1.00 32.31 A C ANISOU 1207 CA CYS A 170 3735 3755 4784 368 73 -241 A C ATOM 1208 C CYS A 170 -23.042 -4.350 -13.927 1.00 35.77 A C ANISOU 1208 C CYS A 170 4161 4108 5321 362 51 -253 A C ATOM 1209 O CYS A 170 -21.928 -4.674 -13.509 1.00 36.64 A O ANISOU 1209 O CYS A 170 4287 4179 5455 345 -2 -285 A O ATOM 1210 CB CYS A 170 -24.957 -5.931 -13.561 1.00 28.47 A C ANISOU 1210 CB CYS A 170 3239 3333 4245 313 76 -181 A C ATOM 1211 SG CYS A 170 -26.244 -6.496 -12.429 1.00 35.46 A S ANISOU 1211 SG CYS A 170 4135 4341 4998 274 97 -157 A S ATOM 1212 N GLN A 171 -23.240 -3.737 -15.093 1.00 34.06 A N ANISOU 1212 N GLN A 171 3909 3879 5152 377 91 -224 A N ATOM 1213 CA GLN A 171 -22.134 -3.317 -15.951 1.00 33.50 A C ANISOU 1213 CA GLN A 171 3817 3748 5162 359 85 -227 A C ATOM 1214 C GLN A 171 -21.243 -2.285 -15.259 1.00 30.36 A C ANISOU 1214 C GLN A 171 3447 3276 4814 352 61 -283 A C ATOM 1215 O GLN A 171 -20.019 -2.342 -15.359 1.00 32.33 A O ANISOU 1215 O GLN A 171 3672 3501 5110 311 29 -307 A O ATOM 1216 CB GLN A 171 -22.667 -2.739 -17.271 1.00 36.16 A C ANISOU 1216 CB GLN A 171 4127 4090 5521 373 135 -173 A C ATOM 1217 CG GLN A 171 -21.585 -2.450 -18.308 1.00 38.53 A C ANISOU 1217 CG GLN A 171 4398 4355 5886 336 141 -159 A C ATOM 1218 CD GLN A 171 -22.093 -1.627 -19.487 1.00 38.95 A C ANISOU 1218 CD GLN A 171 4447 4401 5952 351 187 -98 A C ATOM 1219 NE2 GLN A 171 -21.253 -1.470 -20.509 1.00 37.42 A N ANISOU 1219 NE2 GLN A 171 4224 4201 5793 306 203 -72 A N ATOM 1220 OE1 GLN A 171 -23.219 -1.130 -19.473 1.00 38.37 A O ANISOU 1220 OE1 GLN A 171 4392 4338 5851 407 207 -73 A O ATOM 1221 N GLN A 172 -21.860 -1.336 -14.564 1.00 31.94 A N ANISOU 1221 N GLN A 172 3692 3446 4997 392 74 -311 A N ATOM 1222 CA GLN A 172 -21.114 -0.325 -13.818 1.00 37.15 A C ANISOU 1222 CA GLN A 172 4400 4023 5694 378 43 -376 A C ATOM 1223 C GLN A 172 -20.246 -0.953 -12.718 1.00 40.75 A C ANISOU 1223 C GLN A 172 4857 4500 6127 345 -21 -432 A C ATOM 1224 O GLN A 172 -19.133 -0.497 -12.459 1.00 43.77 A O ANISOU 1224 O GLN A 172 5238 4836 6555 296 -63 -477 A O ATOM 1225 CB GLN A 172 -22.071 0.703 -13.208 1.00 39.72 A C ANISOU 1225 CB GLN A 172 4790 4313 5990 452 66 -410 A C ATOM 1226 CG GLN A 172 -21.372 1.848 -12.490 1.00 45.87 A C ANISOU 1226 CG GLN A 172 5643 4980 6804 435 31 -488 A C ATOM 1227 CD GLN A 172 -20.505 2.678 -13.422 1.00 52.71 A C ANISOU 1227 CD GLN A 172 6522 5740 7764 364 27 -464 A C ATOM 1228 NE2 GLN A 172 -21.122 3.632 -14.113 1.00 55.79 A N ANISOU 1228 NE2 GLN A 172 6967 6050 8180 411 62 -428 A N ATOM 1229 OE1 GLN A 172 -19.298 2.467 -13.519 1.00 53.64 A O ANISOU 1229 OE1 GLN A 172 6600 5857 7924 270 -8 -474 A O ATOM 1230 N ALA A 173 -20.757 -2.001 -12.076 1.00 39.12 A N ANISOU 1230 N ALA A 173 4655 4368 5843 364 -33 -422 A N ATOM 1231 CA ALA A 173 -19.999 -2.715 -11.051 1.00 39.73 A C ANISOU 1231 CA ALA A 173 4745 4467 5883 346 -103 -459 A C ATOM 1232 C ALA A 173 -18.745 -3.348 -11.644 1.00 39.93 A C ANISOU 1232 C ALA A 173 4715 4491 5965 315 -146 -453 A C ATOM 1233 O ALA A 173 -17.658 -3.257 -11.065 1.00 40.27 A O ANISOU 1233 O ALA A 173 4745 4531 6025 295 -209 -503 A O ATOM 1234 CB ALA A 173 -20.868 -3.783 -10.389 1.00 38.17 A C ANISOU 1234 CB ALA A 173 4578 4343 5583 360 -103 -426 A C ATOM 1235 N GLU A 174 -18.915 -3.997 -12.796 1.00 40.11 A N ANISOU 1235 N GLU A 174 4701 4532 6009 316 -115 -398 A N ATOM 1236 CA GLU A 174 -17.809 -4.601 -13.535 1.00 39.80 A C ANISOU 1236 CA GLU A 174 4599 4507 6016 308 -142 -398 A C ATOM 1237 C GLU A 174 -16.750 -3.554 -13.876 1.00 38.40 A C ANISOU 1237 C GLU A 174 4364 4312 5915 262 -142 -432 A C ATOM 1238 O GLU A 174 -15.554 -3.795 -13.726 1.00 40.62 A O ANISOU 1238 O GLU A 174 4586 4627 6221 250 -192 -470 A O ATOM 1239 CB GLU A 174 -18.323 -5.277 -14.815 1.00 38.43 A C ANISOU 1239 CB GLU A 174 4405 4354 5844 317 -96 -342 A C ATOM 1240 CG GLU A 174 -17.255 -6.018 -15.612 1.00 42.59 A C ANISOU 1240 CG GLU A 174 4870 4908 6402 331 -118 -354 A C ATOM 1241 CD GLU A 174 -16.843 -7.340 -14.988 1.00 50.82 A C ANISOU 1241 CD GLU A 174 5948 5956 7406 379 -193 -371 A C ATOM 1242 OE1 GLU A 174 -17.726 -8.075 -14.500 1.00 56.73 A O ANISOU 1242 OE1 GLU A 174 6778 6684 8091 383 -208 -341 A O ATOM 1243 OE2 GLU A 174 -15.633 -7.651 -14.988 1.00 53.48 A O1- ANISOU 1243 OE2 GLU A 174 6230 6321 7770 412 -241 -413 A O1- ATOM 1244 N HIS A 175 -17.200 -2.388 -14.325 1.00 36.98 A N ANISOU 1244 N HIS A 175 4201 4083 5767 234 -88 -417 A N ATOM 1245 CA HIS A 175 -16.302 -1.278 -14.629 1.00 39.39 A C ANISOU 1245 CA HIS A 175 4477 4350 6140 161 -86 -438 A C ATOM 1246 C HIS A 175 -15.559 -0.772 -13.397 1.00 43.61 A C ANISOU 1246 C HIS A 175 5028 4865 6677 124 -154 -516 A C ATOM 1247 O HIS A 175 -14.329 -0.798 -13.345 1.00 48.22 A O ANISOU 1247 O HIS A 175 5536 5492 7292 70 -197 -551 A O ATOM 1248 CB HIS A 175 -17.077 -0.111 -15.245 1.00 37.15 A C ANISOU 1248 CB HIS A 175 4250 3987 5881 150 -26 -398 A C ATOM 1249 CG HIS A 175 -17.392 -0.282 -16.697 1.00 39.20 A C ANISOU 1249 CG HIS A 175 4471 4271 6151 152 35 -321 A C ATOM 1250 CD2 HIS A 175 -18.000 -1.289 -17.368 1.00 39.24 A C ANISOU 1250 CD2 HIS A 175 4449 4342 6118 200 60 -279 A C ATOM 1251 ND1 HIS A 175 -17.090 0.679 -17.637 1.00 38.40 A N ANISOU 1251 ND1 HIS A 175 4370 4125 6095 90 72 -279 A N ATOM 1252 CE1 HIS A 175 -17.495 0.271 -18.826 1.00 40.27 A C ANISOU 1252 CE1 HIS A 175 4574 4410 6316 109 120 -212 A C ATOM 1253 NE2 HIS A 175 -18.051 -0.919 -18.691 1.00 41.76 A N ANISOU 1253 NE2 HIS A 175 4744 4666 6456 176 112 -218 A N ATOM 1254 N SER A 176 -16.319 -0.308 -12.410 1.00 42.54 A N ANISOU 1254 N SER A 176 4984 4679 6500 155 -163 -548 A N ATOM 1255 CA SER A 176 -15.760 0.454 -11.298 1.00 42.36 A C ANISOU 1255 CA SER A 176 5002 4618 6475 114 -222 -631 A C ATOM 1256 C SER A 176 -15.129 -0.410 -10.212 1.00 42.52 A C ANISOU 1256 C SER A 176 4997 4716 6442 130 -305 -678 A C ATOM 1257 O SER A 176 -14.184 0.014 -9.553 1.00 42.14 A O ANISOU 1257 O SER A 176 4932 4675 6404 73 -371 -745 A O ATOM 1258 CB SER A 176 -16.845 1.340 -10.681 1.00 44.11 A C ANISOU 1258 CB SER A 176 5339 4760 6661 160 -197 -661 A C ATOM 1259 OG SER A 176 -17.380 2.237 -11.641 1.00 44.19 A O ANISOU 1259 OG SER A 176 5386 4683 6720 160 -136 -617 A O ATOM 1260 N PHE A 177 -15.642 -1.621 -10.025 1.00 43.48 A N ANISOU 1260 N PHE A 177 5122 4895 6501 202 -308 -640 A N ATOM 1261 CA PHE A 177 -15.166 -2.467 -8.936 1.00 44.05 A C ANISOU 1261 CA PHE A 177 5199 5028 6508 230 -392 -670 A C ATOM 1262 C PHE A 177 -14.335 -3.653 -9.399 1.00 43.81 A C ANISOU 1262 C PHE A 177 5092 5061 6493 261 -435 -643 A C ATOM 1263 O PHE A 177 -13.640 -4.269 -8.595 1.00 41.09 A O ANISOU 1263 O PHE A 177 4739 4765 6109 289 -522 -670 A O ATOM 1264 CB PHE A 177 -16.347 -2.960 -8.104 1.00 43.74 A C ANISOU 1264 CB PHE A 177 5251 5001 6366 284 -379 -649 A C ATOM 1265 CG PHE A 177 -16.785 -1.985 -7.053 1.00 43.48 A C ANISOU 1265 CG PHE A 177 5293 4945 6283 280 -380 -715 A C ATOM 1266 CD1 PHE A 177 -17.475 -0.836 -7.402 1.00 41.46 A C ANISOU 1266 CD1 PHE A 177 5071 4621 6058 281 -313 -733 A C ATOM 1267 CD2 PHE A 177 -16.496 -2.211 -5.715 1.00 42.43 A C ANISOU 1267 CD2 PHE A 177 5202 4856 6062 289 -453 -764 A C ATOM 1268 CE1 PHE A 177 -17.875 0.068 -6.438 1.00 42.91 A C ANISOU 1268 CE1 PHE A 177 5336 4777 6192 298 -317 -811 A C ATOM 1269 CE2 PHE A 177 -16.895 -1.313 -4.746 1.00 41.50 A C ANISOU 1269 CE2 PHE A 177 5159 4725 5886 292 -453 -839 A C ATOM 1270 CZ PHE A 177 -17.584 -0.172 -5.104 1.00 42.46 A C ANISOU 1270 CZ PHE A 177 5317 4773 6043 301 -384 -869 A C ATOM 1271 N ALA A 178 -14.399 -3.982 -10.685 1.00 43.39 A N ANISOU 1271 N ALA A 178 4988 5010 6489 267 -379 -594 A N ATOM 1272 CA ALA A 178 -13.589 -5.087 -11.192 1.00 41.82 A C ANISOU 1272 CA ALA A 178 4718 4869 6302 316 -417 -584 A C ATOM 1273 C ALA A 178 -12.568 -4.599 -12.206 1.00 41.14 A C ANISOU 1273 C ALA A 178 4506 4830 6295 270 -393 -601 A C ATOM 1274 O ALA A 178 -11.694 -5.355 -12.625 1.00 40.46 A O ANISOU 1274 O ALA A 178 4334 4818 6222 318 -424 -614 A O ATOM 1275 CB ALA A 178 -14.469 -6.164 -11.799 1.00 40.57 A C ANISOU 1275 CB ALA A 178 4612 4692 6111 369 -381 -520 A C ATOM 1276 N GLY A 179 -12.681 -3.334 -12.598 1.00 42.99 A N ANISOU 1276 N GLY A 179 4734 5025 6577 181 -337 -601 A N ATOM 1277 CA GLY A 179 -11.748 -2.747 -13.545 1.00 43.46 A C ANISOU 1277 CA GLY A 179 4680 5132 6702 104 -306 -605 A C ATOM 1278 C GLY A 179 -11.816 -3.329 -14.948 1.00 43.54 A C ANISOU 1278 C GLY A 179 4633 5184 6724 135 -239 -555 A C ATOM 1279 O GLY A 179 -10.834 -3.282 -15.687 1.00 44.83 A O ANISOU 1279 O GLY A 179 4675 5439 6920 100 -223 -565 A O ATOM 1280 N MET A 180 -12.971 -3.878 -15.315 1.00 40.97 A N ANISOU 1280 N MET A 180 4390 4810 6366 196 -198 -505 A N ATOM 1281 CA MET A 180 -13.192 -4.396 -16.665 1.00 40.83 A C ANISOU 1281 CA MET A 180 4339 4826 6350 222 -135 -462 A C ATOM 1282 C MET A 180 -14.317 -3.628 -17.359 1.00 39.19 A C ANISOU 1282 C MET A 180 4194 4551 6145 183 -58 -398 A C ATOM 1283 O MET A 180 -15.496 -3.816 -17.044 1.00 35.94 A O ANISOU 1283 O MET A 180 3870 4088 5696 220 -50 -372 A O ATOM 1284 CB MET A 180 -13.522 -5.888 -16.627 1.00 42.15 A C ANISOU 1284 CB MET A 180 4545 5002 6468 326 -169 -461 A C ATOM 1285 CG MET A 180 -12.403 -6.784 -17.132 1.00 49.32 A C ANISOU 1285 CG MET A 180 5358 6001 7380 394 -198 -502 A C ATOM 1286 SD MET A 180 -12.122 -6.626 -18.907 1.00 73.04 A S ANISOU 1286 SD MET A 180 8265 9085 10401 371 -102 -482 A S ATOM 1287 CE MET A 180 -13.697 -7.191 -19.539 1.00 46.50 A C ANISOU 1287 CE MET A 180 5029 5644 6994 394 -60 -422 A C ATOM 1288 N PRO A 181 -13.952 -2.756 -18.310 1.00 37.70 A N ANISOU 1288 N PRO A 181 3956 4375 5993 109 -1 -368 A N ATOM 1289 CA PRO A 181 -14.912 -1.853 -18.946 1.00 38.84 A C ANISOU 1289 CA PRO A 181 4168 4448 6143 78 60 -303 A C ATOM 1290 C PRO A 181 -15.733 -2.542 -20.033 1.00 41.20 A C ANISOU 1290 C PRO A 181 4472 4780 6401 130 108 -249 A C ATOM 1291 O PRO A 181 -15.707 -2.137 -21.196 1.00 38.65 A O ANISOU 1291 O PRO A 181 4123 4481 6080 94 164 -198 A O ATOM 1292 CB PRO A 181 -14.021 -0.758 -19.528 1.00 41.63 A C ANISOU 1292 CB PRO A 181 4472 4804 6543 -37 91 -285 A C ATOM 1293 CG PRO A 181 -12.741 -1.453 -19.827 1.00 43.18 A C ANISOU 1293 CG PRO A 181 4531 5133 6742 -50 79 -324 A C ATOM 1294 CD PRO A 181 -12.573 -2.515 -18.771 1.00 39.26 A C ANISOU 1294 CD PRO A 181 4029 4663 6224 43 3 -392 A C ATOM 1295 N CYS A 182 -16.480 -3.560 -19.618 1.00 41.94 A N ANISOU 1295 N CYS A 182 4608 4876 6451 204 82 -259 A N ATOM 1296 CA CYS A 182 -17.252 -4.411 -20.512 1.00 39.72 A C ANISOU 1296 CA CYS A 182 4337 4630 6124 244 109 -225 A C ATOM 1297 C CYS A 182 -18.413 -3.696 -21.195 1.00 41.60 A C ANISOU 1297 C CYS A 182 4613 4846 6346 236 161 -156 A C ATOM 1298 O CYS A 182 -18.846 -2.621 -20.775 1.00 42.40 A O ANISOU 1298 O CYS A 182 4757 4886 6467 225 170 -138 A O ATOM 1299 CB CYS A 182 -17.800 -5.610 -19.730 1.00 36.40 A C ANISOU 1299 CB CYS A 182 3972 4201 5659 295 59 -248 A C ATOM 1300 SG CYS A 182 -19.031 -5.155 -18.479 1.00 33.86 A S ANISOU 1300 SG CYS A 182 3731 3827 5308 298 48 -234 A S ATOM 1301 N GLY A 183 -18.922 -4.319 -22.249 1.00 41.97 A N ANISOU 1301 N GLY A 183 4649 4945 6352 253 188 -125 A N ATOM 1302 CA GLY A 183 -20.144 -3.870 -22.883 1.00 41.89 A C ANISOU 1302 CA GLY A 183 4667 4940 6310 262 223 -60 A C ATOM 1303 C GLY A 183 -21.322 -4.379 -22.080 1.00 41.16 A C ANISOU 1303 C GLY A 183 4616 4845 6176 294 198 -65 A C ATOM 1304 O GLY A 183 -21.171 -4.789 -20.932 1.00 42.70 A O ANISOU 1304 O GLY A 183 4837 5015 6373 300 159 -107 A O ATOM 1305 N ILE A 184 -22.495 -4.389 -22.692 1.00 40.99 A N ANISOU 1305 N ILE A 184 4596 4869 6109 309 219 -17 A N ATOM 1306 CA ILE A 184 -23.711 -4.693 -21.957 1.00 38.53 A C ANISOU 1306 CA ILE A 184 4302 4584 5751 326 206 -13 A C ATOM 1307 C ILE A 184 -24.144 -6.152 -22.100 1.00 32.61 A C ANISOU 1307 C ILE A 184 3559 3886 4944 293 181 -23 A C ATOM 1308 O ILE A 184 -25.028 -6.608 -21.380 1.00 34.88 A O ANISOU 1308 O ILE A 184 3860 4205 5186 278 167 -20 A O ATOM 1309 CB ILE A 184 -24.864 -3.768 -22.418 1.00 40.08 A C ANISOU 1309 CB ILE A 184 4485 4818 5925 369 237 42 A C ATOM 1310 CG1 ILE A 184 -25.972 -3.715 -21.363 1.00 43.15 A C ANISOU 1310 CG1 ILE A 184 4874 5247 6275 401 233 33 A C ATOM 1311 CG2 ILE A 184 -25.382 -4.194 -23.793 1.00 40.41 A C ANISOU 1311 CG2 ILE A 184 4493 4942 5921 357 249 87 A C ATOM 1312 CD1 ILE A 184 -27.101 -2.765 -21.706 1.00 44.34 A C ANISOU 1312 CD1 ILE A 184 5000 5446 6402 476 258 76 A C ATOM 1313 N MET A 185 -23.506 -6.886 -23.007 1.00 28.89 A N ANISOU 1313 N MET A 185 3084 3423 4470 277 174 -38 A N ATOM 1314 CA MET A 185 -24.033 -8.179 -23.440 1.00 32.63 A C ANISOU 1314 CA MET A 185 3582 3932 4884 243 149 -46 A C ATOM 1315 C MET A 185 -24.169 -9.194 -22.321 1.00 33.61 A C ANISOU 1315 C MET A 185 3769 4016 4985 214 99 -71 A C ATOM 1316 O MET A 185 -25.239 -9.780 -22.136 1.00 32.38 A O ANISOU 1316 O MET A 185 3632 3898 4770 161 87 -49 A O ATOM 1317 CB MET A 185 -23.159 -8.789 -24.539 1.00 35.08 A C ANISOU 1317 CB MET A 185 3890 4246 5192 252 148 -78 A C ATOM 1318 CG MET A 185 -23.500 -10.255 -24.805 1.00 34.49 A C ANISOU 1318 CG MET A 185 3876 4167 5061 220 104 -110 A C ATOM 1319 SD MET A 185 -22.506 -11.059 -26.075 1.00 35.21 A S ANISOU 1319 SD MET A 185 3976 4265 5136 257 101 -173 A S ATOM 1320 CE MET A 185 -20.856 -10.591 -25.581 1.00 43.97 A C ANISOU 1320 CE MET A 185 5041 5344 6322 326 109 -214 A C ATOM 1321 N ASP A 186 -23.074 -9.407 -21.594 1.00 35.58 A N ANISOU 1321 N ASP A 186 4047 4196 5274 242 68 -113 A N ATOM 1322 CA ASP A 186 -22.999 -10.468 -20.593 1.00 32.02 A C ANISOU 1322 CA ASP A 186 3677 3692 4797 224 9 -132 A C ATOM 1323 C ASP A 186 -24.118 -10.347 -19.578 1.00 30.96 A C ANISOU 1323 C ASP A 186 3560 3587 4615 176 13 -94 A C ATOM 1324 O ASP A 186 -24.831 -11.314 -19.311 1.00 29.60 A O ANISOU 1324 O ASP A 186 3446 3419 4383 109 -14 -74 A O ATOM 1325 CB ASP A 186 -21.643 -10.436 -19.895 1.00 36.74 A C ANISOU 1325 CB ASP A 186 4283 4233 5445 280 -27 -178 A C ATOM 1326 CG ASP A 186 -20.495 -10.712 -20.845 1.00 38.32 A C ANISOU 1326 CG ASP A 186 4450 4431 5679 333 -30 -223 A C ATOM 1327 OD1 ASP A 186 -20.745 -10.825 -22.066 1.00 39.41 A O ANISOU 1327 OD1 ASP A 186 4565 4609 5801 326 3 -219 A O ATOM 1328 OD2 ASP A 186 -19.340 -10.836 -20.380 1.00 38.01 A O1- ANISOU 1328 OD2 ASP A 186 4400 4369 5674 386 -66 -267 A O1- ATOM 1329 N GLN A 187 -24.292 -9.139 -19.051 1.00 32.26 A N ANISOU 1329 N GLN A 187 3677 3780 4802 205 50 -87 A N ATOM 1330 CA GLN A 187 -25.282 -8.894 -18.018 1.00 33.72 A C ANISOU 1330 CA GLN A 187 3862 4014 4935 181 63 -65 A C ATOM 1331 C GLN A 187 -26.679 -8.973 -18.591 1.00 34.59 A C ANISOU 1331 C GLN A 187 3926 4229 4987 139 96 -22 A C ATOM 1332 O GLN A 187 -27.607 -9.460 -17.941 1.00 35.15 A O ANISOU 1332 O GLN A 187 4002 4366 4985 77 97 3 A O ATOM 1333 CB GLN A 187 -25.046 -7.530 -17.358 1.00 33.66 A C ANISOU 1333 CB GLN A 187 3827 3998 4966 243 89 -86 A C ATOM 1334 CG GLN A 187 -23.762 -7.441 -16.559 1.00 33.77 A C ANISOU 1334 CG GLN A 187 3877 3931 5021 266 47 -133 A C ATOM 1335 CD GLN A 187 -22.530 -7.253 -17.427 1.00 36.97 A C ANISOU 1335 CD GLN A 187 4256 4289 5503 289 39 -156 A C ATOM 1336 NE2 GLN A 187 -21.361 -7.325 -16.808 1.00 37.10 A N ANISOU 1336 NE2 GLN A 187 4285 4261 5552 305 -6 -200 A N ATOM 1337 OE1 GLN A 187 -22.628 -7.041 -18.637 1.00 39.60 A O ANISOU 1337 OE1 GLN A 187 4550 4643 5856 290 73 -135 A O ATOM 1338 N PHE A 188 -26.828 -8.506 -19.823 1.00 38.53 A N ANISOU 1338 N PHE A 188 4371 4759 5508 164 123 -8 A N ATOM 1339 CA PHE A 188 -28.148 -8.466 -20.433 1.00 37.86 A C ANISOU 1339 CA PHE A 188 4224 4795 5367 137 148 32 A C ATOM 1340 C PHE A 188 -28.666 -9.876 -20.712 1.00 34.07 A C ANISOU 1340 C PHE A 188 3778 4344 4822 25 114 43 A C ATOM 1341 O PHE A 188 -29.832 -10.166 -20.423 1.00 33.58 A O ANISOU 1341 O PHE A 188 3678 4392 4689 -43 121 72 A O ATOM 1342 CB PHE A 188 -28.131 -7.646 -21.723 1.00 43.48 A C ANISOU 1342 CB PHE A 188 4883 5530 6108 194 175 51 A C ATOM 1343 CG PHE A 188 -29.472 -7.078 -22.096 1.00 52.71 A C ANISOU 1343 CG PHE A 188 5968 6831 7227 218 201 93 A C ATOM 1344 CD1 PHE A 188 -29.649 -5.715 -22.225 1.00 57.75 A C ANISOU 1344 CD1 PHE A 188 6572 7475 7896 323 232 111 A C ATOM 1345 CD2 PHE A 188 -30.555 -7.900 -22.293 1.00 60.20 A C ANISOU 1345 CD2 PHE A 188 6876 7900 8098 137 190 112 A C ATOM 1346 CE1 PHE A 188 -30.888 -5.188 -22.560 1.00 61.69 A C ANISOU 1346 CE1 PHE A 188 6990 8104 8345 374 248 147 A C ATOM 1347 CE2 PHE A 188 -31.777 -7.386 -22.612 1.00 65.09 A C ANISOU 1347 CE2 PHE A 188 7395 8669 8666 167 209 146 A C ATOM 1348 CZ PHE A 188 -31.942 -6.024 -22.750 1.00 64.36 A C ANISOU 1348 CZ PHE A 188 7262 8589 8604 300 237 163 A C ATOM 1349 N ILE A 189 -27.825 -10.756 -21.258 1.00 30.80 A N ANISOU 1349 N ILE A 189 3437 3840 4428 5 74 16 A N ATOM 1350 CA ILE A 189 -28.297 -12.110 -21.529 1.00 31.89 A C ANISOU 1350 CA ILE A 189 3639 3974 4505 -105 31 19 A C ATOM 1351 C ILE A 189 -28.559 -12.853 -20.218 1.00 35.49 A C ANISOU 1351 C ILE A 189 4170 4398 4917 -184 1 35 A C ATOM 1352 O ILE A 189 -29.541 -13.596 -20.113 1.00 37.46 A O ANISOU 1352 O ILE A 189 4435 4705 5092 -309 -13 67 A O ATOM 1353 CB ILE A 189 -27.320 -12.915 -22.438 1.00 26.39 A C ANISOU 1353 CB ILE A 189 3019 3176 3833 -86 -8 -30 A C ATOM 1354 CG1 ILE A 189 -27.815 -14.348 -22.610 1.00 28.01 A C ANISOU 1354 CG1 ILE A 189 3325 3343 3974 -202 -64 -35 A C ATOM 1355 CG2 ILE A 189 -25.891 -12.896 -21.917 1.00 27.39 A C ANISOU 1355 CG2 ILE A 189 3194 3188 4025 4 -27 -71 A C ATOM 1356 CD1 ILE A 189 -29.213 -14.430 -23.232 1.00 27.91 A C ANISOU 1356 CD1 ILE A 189 3248 3466 3889 -310 -53 0 A C ATOM 1357 N SER A 190 -27.702 -12.632 -19.219 1.00 35.36 A N ANISOU 1357 N SER A 190 4197 4302 4938 -123 -10 19 A N ATOM 1358 CA SER A 190 -27.896 -13.224 -17.895 1.00 32.91 A C ANISOU 1358 CA SER A 190 3961 3968 4574 -189 -38 44 A C ATOM 1359 C SER A 190 -29.255 -12.851 -17.316 1.00 34.03 A C ANISOU 1359 C SER A 190 4023 4267 4641 -261 11 88 A C ATOM 1360 O SER A 190 -29.923 -13.676 -16.697 1.00 38.41 A O ANISOU 1360 O SER A 190 4627 4852 5115 -386 -5 130 A O ATOM 1361 CB SER A 190 -26.788 -12.788 -16.930 1.00 34.16 A C ANISOU 1361 CB SER A 190 4153 4048 4779 -95 -55 15 A C ATOM 1362 OG SER A 190 -26.624 -13.743 -15.891 1.00 30.95 A O ANISOU 1362 OG SER A 190 3866 3573 4322 -151 -111 36 A O ATOM 1363 N LEU A 191 -29.668 -11.607 -17.525 1.00 34.00 A N ANISOU 1363 N LEU A 191 3896 4366 4657 -180 71 82 A N ATOM 1364 CA LEU A 191 -30.988 -11.159 -17.087 1.00 36.79 A C ANISOU 1364 CA LEU A 191 4146 4897 4936 -213 123 112 A C ATOM 1365 C LEU A 191 -32.132 -11.685 -17.951 1.00 39.94 A C ANISOU 1365 C LEU A 191 4477 5424 5275 -320 127 146 A C ATOM 1366 O LEU A 191 -33.199 -12.012 -17.436 1.00 41.59 A O ANISOU 1366 O LEU A 191 4633 5776 5394 -424 147 182 A O ATOM 1367 CB LEU A 191 -31.048 -9.631 -17.067 1.00 37.06 A C ANISOU 1367 CB LEU A 191 4086 4982 5012 -65 175 87 A C ATOM 1368 CG LEU A 191 -30.307 -8.936 -15.925 1.00 36.05 A C ANISOU 1368 CG LEU A 191 4001 4783 4914 19 180 49 A C ATOM 1369 CD1 LEU A 191 -30.025 -7.500 -16.289 1.00 32.55 A C ANISOU 1369 CD1 LEU A 191 3511 4315 4543 160 210 17 A C ATOM 1370 CD2 LEU A 191 -31.140 -9.006 -14.651 1.00 38.87 A C ANISOU 1370 CD2 LEU A 191 4334 5263 5170 -22 210 60 A C ATOM 1371 N MET A 192 -31.920 -11.769 -19.261 1.00 41.96 A N ANISOU 1371 N MET A 192 4727 5645 5570 -303 108 135 A N ATOM 1372 CA MET A 192 -33.054 -11.920 -20.168 1.00 40.89 A C ANISOU 1372 CA MET A 192 4495 5664 5378 -373 114 160 A C ATOM 1373 C MET A 192 -33.117 -13.199 -21.006 1.00 40.43 A C ANISOU 1373 C MET A 192 4515 5558 5289 -512 57 159 A C ATOM 1374 O MET A 192 -34.009 -13.342 -21.840 1.00 41.51 A O ANISOU 1374 O MET A 192 4572 5825 5376 -579 53 172 A O ATOM 1375 CB MET A 192 -33.107 -10.714 -21.102 1.00 42.06 A C ANISOU 1375 CB MET A 192 4543 5868 5571 -230 146 154 A C ATOM 1376 CG MET A 192 -34.006 -9.601 -20.579 1.00 48.03 A C ANISOU 1376 CG MET A 192 5168 6781 6299 -140 199 168 A C ATOM 1377 SD MET A 192 -34.794 -8.693 -21.926 1.00 91.84 A S ANISOU 1377 SD MET A 192 10584 12472 11840 -40 211 191 A S ATOM 1378 CE MET A 192 -35.239 -10.029 -23.022 1.00 55.34 A C ANISOU 1378 CE MET A 192 5965 7908 7155 -217 158 204 A C ATOM 1379 N GLY A 193 -32.197 -14.130 -20.777 1.00 39.85 A N ANISOU 1379 N GLY A 193 4600 5302 5240 -549 7 138 A N ATOM 1380 CA GLY A 193 -32.230 -15.398 -21.479 1.00 41.20 A C ANISOU 1380 CA GLY A 193 4879 5398 5379 -673 -56 125 A C ATOM 1381 C GLY A 193 -33.549 -16.124 -21.296 1.00 44.89 A C ANISOU 1381 C GLY A 193 5321 5991 5745 -878 -69 171 A C ATOM 1382 O GLY A 193 -34.266 -15.900 -20.325 1.00 44.42 A O ANISOU 1382 O GLY A 193 5192 6052 5634 -937 -32 216 A O ATOM 1383 N GLN A 194 -33.887 -16.976 -22.256 1.00 49.10 A N ANISOU 1383 N GLN A 194 5904 6511 6241 -995 -119 154 A N ATOM 1384 CA GLN A 194 -35.060 -17.834 -22.145 1.00 48.30 A C ANISOU 1384 CA GLN A 194 5801 6510 6041 -1230 -145 193 A C ATOM 1385 C GLN A 194 -34.684 -19.232 -22.603 1.00 47.85 A C ANISOU 1385 C GLN A 194 5957 6254 5970 -1353 -234 161 A C ATOM 1386 O GLN A 194 -33.946 -19.389 -23.578 1.00 50.07 A O ANISOU 1386 O GLN A 194 6309 6422 6296 -1258 -266 95 A O ATOM 1387 CB GLN A 194 -36.227 -17.294 -22.975 1.00 50.52 A C ANISOU 1387 CB GLN A 194 5881 7046 6270 -1267 -119 204 A C ATOM 1388 CG GLN A 194 -36.802 -15.980 -22.477 1.00 56.91 A C ANISOU 1388 CG GLN A 194 6483 8063 7076 -1147 -39 235 A C ATOM 1389 CD GLN A 194 -37.469 -16.108 -21.118 1.00 66.23 A C ANISOU 1389 CD GLN A 194 7622 9351 8192 -1256 -2 288 A C ATOM 1390 NE2 GLN A 194 -37.484 -15.015 -20.359 1.00 66.61 A N ANISOU 1390 NE2 GLN A 194 7564 9486 8258 -1102 66 295 A N ATOM 1391 OE1 GLN A 194 -37.966 -17.174 -20.756 1.00 71.89 A O ANISOU 1391 OE1 GLN A 194 8409 10072 8835 -1480 -35 321 A O ATOM 1392 N LYS A 195 -35.175 -20.243 -21.895 1.00 45.37 A N ANISOU 1392 N LYS A 195 5756 5895 5589 -1563 -274 208 A N ATOM 1393 CA LYS A 195 -34.942 -21.622 -22.298 1.00 48.16 A C ANISOU 1393 CA LYS A 195 6339 6039 5920 -1699 -370 179 A C ATOM 1394 C LYS A 195 -35.402 -21.839 -23.744 1.00 49.66 A C ANISOU 1394 C LYS A 195 6490 6296 6083 -1758 -403 120 A C ATOM 1395 O LYS A 195 -36.496 -21.422 -24.130 1.00 51.12 A O ANISOU 1395 O LYS A 195 6487 6725 6210 -1852 -373 144 A O ATOM 1396 CB LYS A 195 -35.662 -22.591 -21.354 1.00 50.62 A C ANISOU 1396 CB LYS A 195 6761 6327 6144 -1963 -404 259 A C ATOM 1397 CG LYS A 195 -35.495 -24.054 -21.732 1.00 55.31 A C ANISOU 1397 CG LYS A 195 7627 6678 6711 -2123 -514 234 A C ATOM 1398 CD LYS A 195 -36.244 -24.973 -20.779 1.00 58.63 A C ANISOU 1398 CD LYS A 195 8166 7073 7037 -2411 -547 332 A C ATOM 1399 N GLY A 196 -34.550 -22.466 -24.546 1.00 49.88 A N ANISOU 1399 N GLY A 196 6688 6120 6145 -1686 -465 37 A N ATOM 1400 CA GLY A 196 -34.892 -22.777 -25.921 1.00 49.87 A C ANISOU 1400 CA GLY A 196 6682 6162 6106 -1740 -505 -31 A C ATOM 1401 C GLY A 196 -34.706 -21.624 -26.889 1.00 50.52 A C ANISOU 1401 C GLY A 196 6574 6402 6219 -1548 -446 -67 A C ATOM 1402 O GLY A 196 -35.098 -21.720 -28.050 1.00 52.43 A O ANISOU 1402 O GLY A 196 6778 6730 6415 -1588 -471 -115 A O ATOM 1403 N HIS A 197 -34.098 -20.537 -26.426 1.00 46.93 A N ANISOU 1403 N HIS A 197 6012 5982 5837 -1347 -372 -43 A N ATOM 1404 CA HIS A 197 -33.918 -19.367 -27.278 1.00 46.67 A C ANISOU 1404 CA HIS A 197 5813 6086 5833 -1173 -315 -58 A C ATOM 1405 C HIS A 197 -32.521 -18.763 -27.188 1.00 47.36 A C ANISOU 1405 C HIS A 197 5928 6051 6014 -943 -277 -89 A C ATOM 1406 O HIS A 197 -31.865 -18.819 -26.148 1.00 47.73 A O ANISOU 1406 O HIS A 197 6046 5976 6113 -891 -272 -74 A O ATOM 1407 CB HIS A 197 -34.946 -18.286 -26.930 1.00 46.99 A C ANISOU 1407 CB HIS A 197 5625 6377 5850 -1177 -252 18 A C ATOM 1408 CG HIS A 197 -36.364 -18.671 -27.226 1.00 48.76 A C ANISOU 1408 CG HIS A 197 5756 6795 5975 -1383 -281 45 A C ATOM 1409 CD2 HIS A 197 -37.155 -18.410 -28.295 1.00 48.48 A C ANISOU 1409 CD2 HIS A 197 5590 6951 5877 -1416 -294 37 A C ATOM 1410 ND1 HIS A 197 -37.138 -19.401 -26.347 1.00 49.05 A N ANISOU 1410 ND1 HIS A 197 5819 6862 5954 -1598 -301 90 A N ATOM 1411 CE1 HIS A 197 -38.341 -19.578 -26.865 1.00 50.78 A C ANISOU 1411 CE1 HIS A 197 5917 7292 6085 -1762 -324 104 A C ATOM 1412 NE2 HIS A 197 -38.377 -18.988 -28.048 1.00 50.28 A N ANISOU 1412 NE2 HIS A 197 5756 7330 6018 -1649 -325 70 A N ATOM 1413 N ALA A 198 -32.068 -18.193 -28.297 1.00 45.42 A N ANISOU 1413 N ALA A 198 5623 5852 5783 -816 -254 -129 A N ATOM 1414 CA ALA A 198 -30.931 -17.293 -28.265 1.00 41.25 A C ANISOU 1414 CA ALA A 198 5057 5280 5336 -616 -199 -138 A C ATOM 1415 C ALA A 198 -31.524 -15.904 -28.199 1.00 38.55 A C ANISOU 1415 C ALA A 198 4528 5116 5004 -558 -132 -67 A C ATOM 1416 O ALA A 198 -32.725 -15.735 -28.396 1.00 36.64 A O ANISOU 1416 O ALA A 198 4185 5037 4701 -647 -135 -26 A O ATOM 1417 CB ALA A 198 -30.041 -17.462 -29.483 1.00 42.56 A C ANISOU 1417 CB ALA A 198 5271 5400 5502 -517 -204 -216 A C ATOM 1418 N LEU A 199 -30.700 -14.908 -27.915 1.00 38.83 A N ANISOU 1418 N LEU A 199 4517 5123 5115 -408 -79 -53 A N ATOM 1419 CA LEU A 199 -31.220 -13.569 -27.711 1.00 39.53 A C ANISOU 1419 CA LEU A 199 4461 5341 5219 -339 -24 11 A C ATOM 1420 C LEU A 199 -30.503 -12.591 -28.614 1.00 38.79 A C ANISOU 1420 C LEU A 199 4321 5259 5160 -206 17 14 A C ATOM 1421 O LEU A 199 -29.341 -12.276 -28.388 1.00 37.99 A O ANISOU 1421 O LEU A 199 4257 5052 5127 -119 40 -7 A O ATOM 1422 CB LEU A 199 -31.069 -13.150 -26.246 1.00 37.60 A C ANISOU 1422 CB LEU A 199 4212 5049 5026 -309 2 38 A C ATOM 1423 CG LEU A 199 -31.593 -11.774 -25.833 1.00 41.44 A C ANISOU 1423 CG LEU A 199 4571 5644 5531 -222 56 90 A C ATOM 1424 CD1 LEU A 199 -33.109 -11.704 -25.953 1.00 42.28 A C ANISOU 1424 CD1 LEU A 199 4562 5945 5556 -293 55 131 A C ATOM 1425 CD2 LEU A 199 -31.152 -11.442 -24.412 1.00 43.16 A C ANISOU 1425 CD2 LEU A 199 4816 5783 5798 -182 76 92 A C ATOM 1426 N LEU A 200 -31.191 -12.115 -29.645 1.00 35.75 A N ANISOU 1426 N LEU A 200 3853 5012 4720 -198 22 44 A N ATOM 1427 CA LEU A 200 -30.620 -11.076 -30.482 1.00 37.74 A C ANISOU 1427 CA LEU A 200 4065 5284 4992 -83 63 70 A C ATOM 1428 C LEU A 200 -30.725 -9.750 -29.750 1.00 36.61 A C ANISOU 1428 C LEU A 200 3856 5147 4908 10 106 132 A C ATOM 1429 O LEU A 200 -31.819 -9.307 -29.405 1.00 38.97 A O ANISOU 1429 O LEU A 200 4074 5552 5179 13 105 175 A O ATOM 1430 CB LEU A 200 -31.328 -11.003 -31.837 1.00 40.88 A C ANISOU 1430 CB LEU A 200 4409 5826 5298 -100 45 90 A C ATOM 1431 CG LEU A 200 -30.777 -9.944 -32.787 1.00 39.76 A C ANISOU 1431 CG LEU A 200 4239 5710 5158 6 86 134 A C ATOM 1432 CD1 LEU A 200 -29.330 -10.264 -33.141 1.00 35.87 A C ANISOU 1432 CD1 LEU A 200 3824 5107 4696 33 111 77 A C ATOM 1433 CD2 LEU A 200 -31.640 -9.857 -34.038 1.00 42.88 A C ANISOU 1433 CD2 LEU A 200 4578 6268 5446 -9 58 165 A C ATOM 1434 N ILE A 201 -29.587 -9.119 -29.502 1.00 33.72 A N ANISOU 1434 N ILE A 201 3523 4672 4618 86 142 128 A N ATOM 1435 CA ILE A 201 -29.592 -7.848 -28.802 1.00 31.42 A C ANISOU 1435 CA ILE A 201 3197 4356 4385 170 177 175 A C ATOM 1436 C ILE A 201 -29.069 -6.746 -29.702 1.00 34.16 A C ANISOU 1436 C ILE A 201 3536 4695 4749 245 209 224 A C ATOM 1437 O ILE A 201 -27.951 -6.819 -30.212 1.00 34.44 A O ANISOU 1437 O ILE A 201 3607 4672 4805 243 228 203 A O ATOM 1438 CB ILE A 201 -28.742 -7.897 -27.505 1.00 32.85 A C ANISOU 1438 CB ILE A 201 3430 4408 4644 177 184 136 A C ATOM 1439 CG1 ILE A 201 -29.242 -9.002 -26.572 1.00 33.42 A C ANISOU 1439 CG1 ILE A 201 3530 4480 4690 94 150 103 A C ATOM 1440 CG2 ILE A 201 -28.785 -6.564 -26.795 1.00 31.47 A C ANISOU 1440 CG2 ILE A 201 3233 4201 4522 260 214 171 A C ATOM 1441 CD1 ILE A 201 -28.354 -9.237 -25.359 1.00 33.45 A C ANISOU 1441 CD1 ILE A 201 3597 4360 4752 99 144 65 A C ATOM 1442 N ASP A 202 -29.894 -5.730 -29.908 1.00 38.20 A N ANISOU 1442 N ASP A 202 3999 5272 5243 313 216 291 A N ATOM 1443 CA ASP A 202 -29.454 -4.533 -30.598 1.00 37.97 A C ANISOU 1443 CA ASP A 202 3986 5208 5232 384 242 356 A C ATOM 1444 C ASP A 202 -28.866 -3.625 -29.538 1.00 37.19 A C ANISOU 1444 C ASP A 202 3928 4976 5227 432 266 355 A C ATOM 1445 O ASP A 202 -29.591 -3.110 -28.696 1.00 33.58 A O ANISOU 1445 O ASP A 202 3454 4521 4786 491 261 361 A O ATOM 1446 CB ASP A 202 -30.613 -3.855 -31.340 1.00 37.99 A C ANISOU 1446 CB ASP A 202 3937 5329 5168 454 224 433 A C ATOM 1447 CG ASP A 202 -30.146 -2.764 -32.284 1.00 42.44 A C ANISOU 1447 CG ASP A 202 4543 5854 5729 510 243 516 A C ATOM 1448 OD1 ASP A 202 -29.237 -1.995 -31.903 1.00 38.92 A O ANISOU 1448 OD1 ASP A 202 4159 5270 5359 526 274 530 A O ATOM 1449 OD2 ASP A 202 -30.682 -2.680 -33.417 1.00 48.05 A O1- ANISOU 1449 OD2 ASP A 202 5228 6674 6354 528 224 572 A O1- ATOM 1450 N CYS A 203 -27.551 -3.436 -29.563 1.00 38.68 A N ANISOU 1450 N CYS A 203 4163 5061 5471 405 292 340 A N ATOM 1451 CA CYS A 203 -26.893 -2.713 -28.482 1.00 40.03 A C ANISOU 1451 CA CYS A 203 4375 5106 5730 425 304 322 A C ATOM 1452 C CYS A 203 -26.889 -1.214 -28.737 1.00 41.41 A C ANISOU 1452 C CYS A 203 4591 5209 5932 485 319 397 A C ATOM 1453 O CYS A 203 -26.268 -0.451 -27.999 1.00 39.53 A O ANISOU 1453 O CYS A 203 4403 4851 5765 491 327 386 A O ATOM 1454 CB CYS A 203 -25.470 -3.236 -28.280 1.00 35.87 A C ANISOU 1454 CB CYS A 203 3864 4516 5249 361 316 264 A C ATOM 1455 SG CYS A 203 -25.451 -4.963 -27.762 1.00 39.69 A S ANISOU 1455 SG CYS A 203 4339 5034 5709 313 283 174 A S ATOM 1456 N ARG A 204 -27.594 -0.792 -29.781 1.00 43.97 A N ANISOU 1456 N ARG A 204 4908 5603 6197 530 315 475 A N ATOM 1457 CA ARG A 204 -27.808 0.632 -30.004 1.00 44.58 A C ANISOU 1457 CA ARG A 204 5046 5600 6291 609 315 557 A C ATOM 1458 C ARG A 204 -29.182 1.044 -29.499 1.00 45.27 A C ANISOU 1458 C ARG A 204 5109 5733 6358 734 285 566 A C ATOM 1459 O ARG A 204 -29.317 2.002 -28.739 1.00 45.90 A O ANISOU 1459 O ARG A 204 5246 5707 6488 815 281 564 A O ATOM 1460 CB ARG A 204 -27.667 0.993 -31.482 1.00 41.72 A C ANISOU 1460 CB ARG A 204 4704 5278 5869 596 323 653 A C ATOM 1461 CG ARG A 204 -28.022 2.444 -31.770 1.00 41.52 A C ANISOU 1461 CG ARG A 204 4765 5161 5851 688 310 756 A C ATOM 1462 CD ARG A 204 -27.763 2.819 -33.219 1.00 39.88 A C ANISOU 1462 CD ARG A 204 4594 4986 5573 659 320 865 A C ATOM 1463 NE ARG A 204 -28.538 1.996 -34.143 1.00 39.33 A N ANISOU 1463 NE ARG A 204 4441 5106 5396 673 301 876 A N ATOM 1464 CZ ARG A 204 -28.449 2.077 -35.467 1.00 38.63 A C ANISOU 1464 CZ ARG A 204 4365 5094 5217 649 305 960 A C ATOM 1465 NH1 ARG A 204 -27.616 2.946 -36.026 1.00 38.22 A N1+ ANISOU 1465 NH1 ARG A 204 4405 4948 5170 602 335 1051 A N1+ ATOM 1466 NH2 ARG A 204 -29.189 1.286 -36.234 1.00 37.86 A N ANISOU 1466 NH2 ARG A 204 4191 5175 5018 657 279 953 A N ATOM 1467 N SER A 205 -30.202 0.310 -29.925 1.00 44.71 A N ANISOU 1467 N SER A 205 4949 5831 6208 749 264 567 A N ATOM 1468 CA SER A 205 -31.575 0.639 -29.563 1.00 42.06 A C ANISOU 1468 CA SER A 205 4554 5592 5836 870 238 576 A C ATOM 1469 C SER A 205 -32.001 -0.072 -28.288 1.00 38.64 A C ANISOU 1469 C SER A 205 4058 5212 5410 847 243 487 A C ATOM 1470 O SER A 205 -33.013 0.283 -27.690 1.00 44.69 A O ANISOU 1470 O SER A 205 4770 6054 6154 949 235 477 A O ATOM 1471 CB SER A 205 -32.528 0.270 -30.698 1.00 37.19 A C ANISOU 1471 CB SER A 205 3855 5160 5117 888 207 628 A C ATOM 1472 OG SER A 205 -32.661 -1.138 -30.784 1.00 35.97 A O ANISOU 1472 OG SER A 205 3628 5125 4916 764 202 570 A O ATOM 1473 N LEU A 206 -31.225 -1.082 -27.898 1.00 35.25 A N ANISOU 1473 N LEU A 206 3637 4751 5003 718 255 426 A N ATOM 1474 CA LEU A 206 -31.507 -1.940 -26.739 1.00 37.85 A C ANISOU 1474 CA LEU A 206 3927 5125 5328 665 256 354 A C ATOM 1475 C LEU A 206 -32.752 -2.805 -26.957 1.00 41.43 A C ANISOU 1475 C LEU A 206 4271 5778 5691 629 236 355 A C ATOM 1476 O LEU A 206 -33.259 -3.428 -26.022 1.00 43.43 A O ANISOU 1476 O LEU A 206 4480 6099 5921 583 238 313 A O ATOM 1477 CB LEU A 206 -31.635 -1.110 -25.456 1.00 35.04 A C ANISOU 1477 CB LEU A 206 3597 4700 5016 754 270 320 A C ATOM 1478 CG LEU A 206 -30.384 -0.290 -25.123 1.00 35.17 A C ANISOU 1478 CG LEU A 206 3725 4514 5122 762 282 309 A C ATOM 1479 CD1 LEU A 206 -30.501 0.388 -23.757 1.00 36.75 A C ANISOU 1479 CD1 LEU A 206 3961 4647 5355 837 289 254 A C ATOM 1480 CD2 LEU A 206 -29.141 -1.170 -25.188 1.00 33.21 A C ANISOU 1480 CD2 LEU A 206 3506 4204 4907 631 284 276 A C ATOM 1481 N GLU A 207 -33.219 -2.861 -28.202 1.00 40.72 A N ANISOU 1481 N GLU A 207 4140 5789 5542 633 215 405 A N ATOM 1482 CA GLU A 207 -34.263 -3.806 -28.590 1.00 39.19 A C ANISOU 1482 CA GLU A 207 3844 5788 5257 561 186 401 A C ATOM 1483 C GLU A 207 -33.720 -5.230 -28.507 1.00 36.86 A C ANISOU 1483 C GLU A 207 3589 5462 4955 395 177 345 A C ATOM 1484 O GLU A 207 -32.553 -5.479 -28.810 1.00 37.06 A O ANISOU 1484 O GLU A 207 3702 5356 5023 357 185 325 A O ATOM 1485 CB GLU A 207 -34.773 -3.505 -30.003 1.00 41.82 A C ANISOU 1485 CB GLU A 207 4136 6232 5523 605 155 465 A C ATOM 1486 CG GLU A 207 -35.845 -4.463 -30.514 1.00 44.17 A C ANISOU 1486 CG GLU A 207 4323 6742 5718 515 115 457 A C ATOM 1487 CD GLU A 207 -36.529 -3.956 -31.772 1.00 51.10 A C ANISOU 1487 CD GLU A 207 5140 7757 6518 593 76 525 A C ATOM 1488 OE1 GLU A 207 -36.209 -2.829 -32.206 1.00 54.37 A O ANISOU 1488 OE1 GLU A 207 5608 8092 6958 726 83 587 A O ATOM 1489 OE2 GLU A 207 -37.394 -4.676 -32.320 1.00 52.21 A O1- ANISOU 1489 OE2 GLU A 207 5186 8086 6567 516 33 519 A O1- ATOM 1490 N THR A 208 -34.554 -6.163 -28.070 1.00 35.00 A N ANISOU 1490 N THR A 208 3290 5346 4663 296 158 319 A N ATOM 1491 CA THR A 208 -34.125 -7.547 -27.949 1.00 35.74 A C ANISOU 1491 CA THR A 208 3447 5388 4745 140 138 269 A C ATOM 1492 C THR A 208 -35.128 -8.461 -28.600 1.00 37.57 A C ANISOU 1492 C THR A 208 3612 5783 4879 21 95 268 A C ATOM 1493 O THR A 208 -36.319 -8.167 -28.642 1.00 40.67 A O ANISOU 1493 O THR A 208 3878 6362 5211 37 87 298 A O ATOM 1494 CB THR A 208 -33.955 -7.983 -26.485 1.00 37.56 A C ANISOU 1494 CB THR A 208 3713 5551 5006 88 152 234 A C ATOM 1495 CG2 THR A 208 -32.905 -7.139 -25.801 1.00 37.24 A C ANISOU 1495 CG2 THR A 208 3742 5349 5058 189 185 223 A C ATOM 1496 OG1 THR A 208 -35.204 -7.844 -25.799 1.00 40.16 A O ANISOU 1496 OG1 THR A 208 3930 6048 5279 82 162 250 A O ATOM 1497 N SER A 209 -34.646 -9.587 -29.096 1.00 40.93 A N ANISOU 1497 N SER A 209 4121 6143 5286 -97 64 226 A N ATOM 1498 CA SER A 209 -35.523 -10.505 -29.785 1.00 43.90 A C ANISOU 1498 CA SER A 209 4457 6655 5567 -231 13 214 A C ATOM 1499 C SER A 209 -35.182 -11.945 -29.458 1.00 45.22 A C ANISOU 1499 C SER A 209 4742 6714 5726 -393 -22 156 A C ATOM 1500 O SER A 209 -34.037 -12.372 -29.593 1.00 48.43 A O ANISOU 1500 O SER A 209 5277 6946 6178 -379 -24 111 A O ATOM 1501 CB SER A 209 -35.450 -10.275 -31.286 1.00 42.69 A C ANISOU 1501 CB SER A 209 4294 6559 5368 -189 -9 224 A C ATOM 1502 OG SER A 209 -36.376 -11.118 -31.933 1.00 54.26 A O ANISOU 1502 OG SER A 209 5712 8171 6733 -325 -66 207 A O ATOM 1503 N LEU A 210 -36.193 -12.684 -29.018 1.00 44.24 A N ANISOU 1503 N LEU A 210 4575 6698 5538 -547 -51 159 A N ATOM 1504 CA LEU A 210 -36.042 -14.096 -28.716 1.00 42.93 A C ANISOU 1504 CA LEU A 210 4538 6423 5351 -724 -96 116 A C ATOM 1505 C LEU A 210 -36.078 -14.923 -29.991 1.00 47.13 A C ANISOU 1505 C LEU A 210 5131 6955 5820 -814 -157 67 A C ATOM 1506 O LEU A 210 -37.093 -14.961 -30.691 1.00 50.63 A O ANISOU 1506 O LEU A 210 5470 7588 6180 -890 -189 79 A O ATOM 1507 CB LEU A 210 -37.137 -14.552 -27.755 1.00 43.96 A C ANISOU 1507 CB LEU A 210 4602 6676 5425 -882 -101 148 A C ATOM 1508 CG LEU A 210 -37.052 -13.947 -26.354 1.00 46.07 A C ANISOU 1508 CG LEU A 210 4836 6931 5737 -811 -43 182 A C ATOM 1509 CD1 LEU A 210 -38.168 -14.484 -25.467 1.00 50.35 A C ANISOU 1509 CD1 LEU A 210 5305 7624 6202 -988 -41 216 A C ATOM 1510 CD2 LEU A 210 -35.692 -14.229 -25.737 1.00 40.51 A C ANISOU 1510 CD2 LEU A 210 4307 5969 5116 -757 -39 152 A C ATOM 1511 N VAL A 211 -34.960 -15.578 -30.287 1.00 47.14 A N ANISOU 1511 N VAL A 211 5300 6756 5857 -797 -177 4 A N ATOM 1512 CA VAL A 211 -34.830 -16.412 -31.475 1.00 48.64 A C ANISOU 1512 CA VAL A 211 5577 6918 5986 -863 -233 -65 A C ATOM 1513 C VAL A 211 -34.750 -17.887 -31.101 1.00 51.92 A C ANISOU 1513 C VAL A 211 6171 7176 6382 -1028 -299 -121 A C ATOM 1514 O VAL A 211 -33.793 -18.308 -30.453 1.00 54.70 A O ANISOU 1514 O VAL A 211 6660 7326 6798 -981 -298 -149 A O ATOM 1515 CB VAL A 211 -33.579 -16.032 -32.287 1.00 48.21 A C ANISOU 1515 CB VAL A 211 5579 6770 5971 -695 -205 -108 A C ATOM 1516 CG1 VAL A 211 -33.457 -16.904 -33.530 1.00 45.98 A C ANISOU 1516 CG1 VAL A 211 5389 6473 5609 -752 -259 -193 A C ATOM 1517 CG2 VAL A 211 -33.621 -14.561 -32.660 1.00 50.46 A C ANISOU 1517 CG2 VAL A 211 5718 7182 6273 -546 -145 -39 A C ATOM 1518 N PRO A 212 -35.761 -18.675 -31.502 1.00 54.24 A N ANISOU 1518 N PRO A 212 6467 7557 6583 -1226 -363 -136 A N ATOM 1519 CA PRO A 212 -35.806 -20.120 -31.238 1.00 56.91 A C ANISOU 1519 CA PRO A 212 6999 7734 6892 -1414 -439 -186 A C ATOM 1520 C PRO A 212 -34.516 -20.852 -31.615 1.00 59.04 A C ANISOU 1520 C PRO A 212 7486 7748 7197 -1321 -470 -283 A C ATOM 1521 O PRO A 212 -33.920 -20.588 -32.656 1.00 60.61 A O ANISOU 1521 O PRO A 212 7684 7957 7389 -1190 -459 -343 A O ATOM 1522 CB PRO A 212 -36.973 -20.591 -32.106 1.00 55.74 A C ANISOU 1522 CB PRO A 212 6795 7754 6630 -1608 -503 -205 A C ATOM 1523 CG PRO A 212 -37.890 -19.413 -32.133 1.00 53.96 A C ANISOU 1523 CG PRO A 212 6305 7817 6382 -1562 -453 -123 A C ATOM 1524 CD PRO A 212 -36.992 -18.200 -32.159 1.00 52.21 A C ANISOU 1524 CD PRO A 212 6023 7571 6243 -1291 -373 -99 A C ATOM 1525 N LEU A 213 -34.095 -21.757 -30.741 1.00 60.75 A N ANISOU 1525 N LEU A 213 7887 7749 7446 -1381 -508 -296 A N ATOM 1526 CA LEU A 213 -32.873 -22.529 -30.916 1.00 62.47 A C ANISOU 1526 CA LEU A 213 8320 7716 7702 -1274 -546 -390 A C ATOM 1527 C LEU A 213 -33.025 -23.790 -30.076 1.00 67.70 A C ANISOU 1527 C LEU A 213 9199 8171 8352 -1442 -625 -388 A C ATOM 1528 O LEU A 213 -32.426 -23.927 -29.008 1.00 70.02 A O ANISOU 1528 O LEU A 213 9578 8320 8706 -1384 -621 -353 A O ATOM 1529 CB LEU A 213 -31.641 -21.714 -30.503 1.00 61.31 A C ANISOU 1529 CB LEU A 213 8127 7515 7652 -1028 -475 -383 A C ATOM 1530 CG LEU A 213 -30.250 -22.358 -30.422 1.00 63.37 A C ANISOU 1530 CG LEU A 213 8569 7544 7966 -875 -502 -468 A C ATOM 1531 CD1 LEU A 213 -29.737 -22.829 -31.770 1.00 63.42 A C ANISOU 1531 CD1 LEU A 213 8653 7517 7925 -798 -529 -592 A C ATOM 1532 CD2 LEU A 213 -29.263 -21.390 -29.781 1.00 64.55 A C ANISOU 1532 CD2 LEU A 213 8620 7699 8208 -679 -429 -434 A C ATOM 1533 N SER A 214 -33.868 -24.698 -30.555 1.00 71.11 A N ANISOU 1533 N SER A 214 9725 8595 8699 -1663 -703 -419 A N ATOM 1534 CA SER A 214 -34.197 -25.903 -29.810 1.00 73.10 A C ANISOU 1534 CA SER A 214 10194 8656 8925 -1874 -785 -401 A C ATOM 1535 C SER A 214 -34.478 -27.052 -30.773 1.00 73.72 A C ANISOU 1535 C SER A 214 10466 8617 8926 -2024 -890 -506 A C ATOM 1536 O SER A 214 -35.618 -27.280 -31.175 1.00 76.29 A O ANISOU 1536 O SER A 214 10734 9086 9168 -2261 -926 -493 A O ATOM 1537 CB SER A 214 -35.400 -25.653 -28.898 1.00 73.35 A C ANISOU 1537 CB SER A 214 10085 8864 8919 -2093 -759 -273 A C ATOM 1538 OG SER A 214 -35.498 -26.651 -27.901 1.00 73.78 A O ANISOU 1538 OG SER A 214 10349 8724 8961 -2267 -817 -225 A O ATOM 1539 N ASP A 215 -33.419 -27.764 -31.136 1.00 70.39 A N ANISOU 1539 N ASP A 215 10273 7942 8530 -1878 -942 -617 A N ATOM 1540 CA ASP A 215 -33.482 -28.827 -32.127 1.00 66.61 A C ANISOU 1540 CA ASP A 215 10006 7322 7981 -1965 -1042 -747 A C ATOM 1541 C ASP A 215 -32.718 -30.032 -31.603 1.00 67.49 A C ANISOU 1541 C ASP A 215 10459 7065 8122 -1934 -1133 -800 A C ATOM 1542 O ASP A 215 -31.519 -29.946 -31.368 1.00 68.61 A O ANISOU 1542 O ASP A 215 10659 7074 8334 -1667 -1112 -840 A O ATOM 1543 CB ASP A 215 -32.894 -28.345 -33.457 1.00 64.54 A C ANISOU 1543 CB ASP A 215 9658 7166 7701 -1752 -1006 -864 A C ATOM 1544 CG ASP A 215 -33.097 -29.335 -34.598 1.00 65.30 A C ANISOU 1544 CG ASP A 215 9944 7167 7702 -1849 -1105 -1011 A C ATOM 1545 OD1 ASP A 215 -33.229 -30.553 -34.349 1.00 63.49 A O ANISOU 1545 OD1 ASP A 215 9992 6682 7448 -2000 -1212 -1057 A O ATOM 1546 OD2 ASP A 215 -33.106 -28.884 -35.760 1.00 66.46 A O1- ANISOU 1546 OD2 ASP A 215 9971 7487 7791 -1771 -1078 -1083 A O1- ATOM 1547 N PRO A 216 -33.412 -31.163 -31.422 1.00 68.23 A N ANISOU 1547 N PRO A 216 10779 6989 8156 -2208 -1241 -800 A N ATOM 1548 CA PRO A 216 -32.784 -32.384 -30.906 1.00 69.95 A C ANISOU 1548 CA PRO A 216 11361 6824 8393 -2196 -1346 -840 A C ATOM 1549 C PRO A 216 -31.610 -32.859 -31.761 1.00 73.46 A C ANISOU 1549 C PRO A 216 11986 7074 8853 -1914 -1388 -1020 A C ATOM 1550 O PRO A 216 -30.723 -33.546 -31.251 1.00 76.21 A O ANISOU 1550 O PRO A 216 12577 7135 9246 -1764 -1447 -1053 A O ATOM 1551 CB PRO A 216 -33.924 -33.407 -30.940 1.00 72.28 A C ANISOU 1551 CB PRO A 216 11841 7023 8598 -2583 -1453 -823 A C ATOM 1552 CG PRO A 216 -35.167 -32.592 -30.892 1.00 72.97 A C ANISOU 1552 CG PRO A 216 11610 7475 8639 -2806 -1381 -714 A C ATOM 1553 CD PRO A 216 -34.856 -31.338 -31.652 1.00 71.23 A C ANISOU 1553 CD PRO A 216 11084 7537 8445 -2556 -1273 -752 A C ATOM 1554 N LYS A 217 -31.610 -32.499 -33.042 1.00 73.18 A N ANISOU 1554 N LYS A 217 11829 7205 8770 -1836 -1358 -1134 A N ATOM 1555 CA LYS A 217 -30.541 -32.900 -33.949 1.00 74.99 A C ANISOU 1555 CA LYS A 217 12199 7300 8993 -1567 -1384 -1317 A C ATOM 1556 C LYS A 217 -29.401 -31.890 -33.908 1.00 72.64 A C ANISOU 1556 C LYS A 217 11691 7135 8772 -1226 -1268 -1317 A C ATOM 1557 O LYS A 217 -28.361 -32.081 -34.537 1.00 77.68 A O ANISOU 1557 O LYS A 217 12398 7703 9414 -964 -1265 -1457 A O ATOM 1558 CB LYS A 217 -31.072 -33.046 -35.379 1.00 77.69 A C ANISOU 1558 CB LYS A 217 12525 7765 9227 -1656 -1411 -1446 A C ATOM 1559 N LEU A 218 -29.605 -30.817 -33.154 1.00 63.17 A N ANISOU 1559 N LEU A 218 10234 6135 7630 -1236 -1171 -1163 A N ATOM 1560 CA LEU A 218 -28.640 -29.736 -33.079 1.00 58.54 A C ANISOU 1560 CA LEU A 218 9428 5698 7116 -961 -1058 -1146 A C ATOM 1561 C LEU A 218 -28.112 -29.563 -31.651 1.00 57.05 A C ANISOU 1561 C LEU A 218 9248 5408 7022 -882 -1044 -1038 A C ATOM 1562 O LEU A 218 -28.867 -29.663 -30.684 1.00 55.51 A O ANISOU 1562 O LEU A 218 9074 5186 6832 -1085 -1065 -912 A O ATOM 1563 CB LEU A 218 -29.274 -28.434 -33.568 1.00 59.39 A C ANISOU 1563 CB LEU A 218 9211 6150 7205 -1009 -952 -1072 A C ATOM 1564 CG LEU A 218 -28.361 -27.213 -33.476 1.00 64.53 A C ANISOU 1564 CG LEU A 218 9633 6957 7928 -763 -834 -1037 A C ATOM 1565 CD1 LEU A 218 -27.086 -27.469 -34.260 1.00 67.10 A C ANISOU 1565 CD1 LEU A 218 10027 7217 8251 -502 -826 -1187 A C ATOM 1566 CD2 LEU A 218 -29.061 -25.957 -33.969 1.00 66.83 A C ANISOU 1566 CD2 LEU A 218 9641 7557 8195 -817 -744 -956 A C ATOM 1567 N ALA A 219 -26.815 -29.309 -31.515 1.00 55.37 A N ANISOU 1567 N ALA A 219 9009 5155 6873 -594 -1009 -1087 A N ATOM 1568 CA ALA A 219 -26.265 -29.003 -30.199 1.00 54.25 A C ANISOU 1568 CA ALA A 219 8840 4956 6816 -505 -992 -986 A C ATOM 1569 C ALA A 219 -25.178 -27.936 -30.253 1.00 52.38 A C ANISOU 1569 C ALA A 219 8377 4880 6645 -246 -890 -999 A C ATOM 1570 O ALA A 219 -24.604 -27.651 -31.305 1.00 54.05 A O ANISOU 1570 O ALA A 219 8501 5197 6838 -95 -843 -1102 A O ATOM 1571 CB ALA A 219 -25.727 -30.263 -29.542 1.00 54.46 A C ANISOU 1571 CB ALA A 219 9185 4652 6855 -448 -1113 -1023 A C ATOM 1572 N VAL A 220 -24.910 -27.346 -29.097 1.00 50.23 A N ANISOU 1572 N VAL A 220 8011 4634 6442 -211 -856 -890 A N ATOM 1573 CA VAL A 220 -23.878 -26.335 -28.973 1.00 45.29 A C ANISOU 1573 CA VAL A 220 7180 4146 5883 4 -770 -890 A C ATOM 1574 C VAL A 220 -22.766 -26.828 -28.050 1.00 49.38 A C ANISOU 1574 C VAL A 220 7816 4489 6457 189 -829 -908 A C ATOM 1575 O VAL A 220 -22.970 -26.999 -26.844 1.00 48.68 A O ANISOU 1575 O VAL A 220 7803 4303 6391 116 -870 -809 A O ATOM 1576 CB VAL A 220 -24.454 -25.028 -28.439 1.00 39.78 A C ANISOU 1576 CB VAL A 220 6241 3657 5216 -94 -676 -757 A C ATOM 1577 CG1 VAL A 220 -23.382 -23.962 -28.396 1.00 35.05 A C ANISOU 1577 CG1 VAL A 220 5443 3190 4683 105 -591 -762 A C ATOM 1578 CG2 VAL A 220 -25.625 -24.586 -29.303 1.00 38.79 A C ANISOU 1578 CG2 VAL A 220 6004 3706 5029 -267 -633 -732 A C ATOM 1579 N LEU A 221 -21.595 -27.071 -28.629 1.00 50.59 A N ANISOU 1579 N LEU A 221 7980 4619 6622 433 -833 -1035 A N ATOM 1580 CA LEU A 221 -20.456 -27.577 -27.877 1.00 46.36 A C ANISOU 1580 CA LEU A 221 7545 3937 6134 647 -898 -1071 A C ATOM 1581 C LEU A 221 -19.540 -26.435 -27.464 1.00 46.28 A C ANISOU 1581 C LEU A 221 7276 4115 6191 791 -813 -1039 A C ATOM 1582 O LEU A 221 -19.000 -25.719 -28.311 1.00 45.22 A O ANISOU 1582 O LEU A 221 6949 4173 6061 891 -723 -1099 A O ATOM 1583 CB LEU A 221 -19.679 -28.609 -28.699 1.00 46.17 A C ANISOU 1583 CB LEU A 221 7690 3776 6076 851 -965 -1243 A C ATOM 1584 CG LEU A 221 -18.337 -29.066 -28.121 1.00 47.32 A C ANISOU 1584 CG LEU A 221 7900 3815 6266 1136 -1027 -1306 A C ATOM 1585 CD1 LEU A 221 -18.533 -29.812 -26.803 1.00 48.04 A C ANISOU 1585 CD1 LEU A 221 8222 3656 6375 1084 -1147 -1211 A C ATOM 1586 CD2 LEU A 221 -17.574 -29.927 -29.122 1.00 46.34 A C ANISOU 1586 CD2 LEU A 221 7897 3611 6100 1368 -1070 -1498 A C ATOM 1587 N ILE A 222 -19.381 -26.263 -26.155 1.00 45.50 A N ANISOU 1587 N ILE A 222 7183 3967 6139 786 -843 -942 A N ATOM 1588 CA ILE A 222 -18.473 -25.264 -25.616 1.00 42.27 A C ANISOU 1588 CA ILE A 222 6556 3711 5793 912 -783 -916 A C ATOM 1589 C ILE A 222 -17.173 -25.920 -25.183 1.00 47.22 A C ANISOU 1589 C ILE A 222 7261 4235 6447 1167 -865 -992 A C ATOM 1590 O ILE A 222 -17.179 -26.858 -24.382 1.00 51.27 A O ANISOU 1590 O ILE A 222 7998 4532 6951 1189 -980 -968 A O ATOM 1591 CB ILE A 222 -19.089 -24.533 -24.420 1.00 42.94 A C ANISOU 1591 CB ILE A 222 6572 3839 5903 755 -761 -768 A C ATOM 1592 CG1 ILE A 222 -20.470 -23.994 -24.790 1.00 43.82 A C ANISOU 1592 CG1 ILE A 222 6619 4050 5982 516 -694 -693 A C ATOM 1593 CG2 ILE A 222 -18.167 -23.423 -23.938 1.00 41.12 A C ANISOU 1593 CG2 ILE A 222 6117 3771 5737 869 -700 -752 A C ATOM 1594 CD1 ILE A 222 -21.125 -23.229 -23.679 1.00 43.17 A C ANISOU 1594 CD1 ILE A 222 6455 4035 5914 377 -660 -563 A C ATOM 1595 N THR A 223 -16.057 -25.427 -25.706 1.00 46.85 A N ANISOU 1595 N THR A 223 7027 4349 6426 1360 -809 -1080 A N ATOM 1596 CA THR A 223 -14.759 -25.986 -25.359 1.00 48.78 A C ANISOU 1596 CA THR A 223 7301 4541 6691 1627 -882 -1164 A C ATOM 1597 C THR A 223 -13.888 -24.962 -24.644 1.00 47.54 A C ANISOU 1597 C THR A 223 6903 4566 6595 1699 -838 -1124 A C ATOM 1598 O THR A 223 -13.589 -23.902 -25.188 1.00 46.94 A O ANISOU 1598 O THR A 223 6582 4717 6538 1679 -724 -1132 A O ATOM 1599 CB THR A 223 -14.023 -26.500 -26.606 1.00 51.53 A C ANISOU 1599 CB THR A 223 7642 4932 7004 1831 -870 -1334 A C ATOM 1600 CG2 THR A 223 -12.677 -27.096 -26.222 1.00 53.29 A C ANISOU 1600 CG2 THR A 223 7883 5120 7246 2134 -950 -1428 A C ATOM 1601 OG1 THR A 223 -14.820 -27.504 -27.250 1.00 53.96 A O ANISOU 1601 OG1 THR A 223 8200 5051 7252 1762 -925 -1385 A O ATOM 1602 N ASN A 224 -13.486 -25.281 -23.420 1.00 49.76 A N ANISOU 1602 N ASN A 224 7264 4744 6899 1771 -933 -1076 A N ATOM 1603 CA ASN A 224 -12.620 -24.392 -22.654 1.00 49.08 A C ANISOU 1603 CA ASN A 224 6964 4821 6864 1839 -912 -1047 A C ATOM 1604 C ASN A 224 -11.156 -24.693 -22.945 1.00 50.43 A C ANISOU 1604 C ASN A 224 7033 5083 7046 2128 -943 -1176 A C ATOM 1605 O ASN A 224 -10.703 -25.828 -22.795 1.00 51.59 A O ANISOU 1605 O ASN A 224 7359 5071 7173 2323 -1058 -1241 A O ATOM 1606 CB ASN A 224 -12.910 -24.521 -21.156 1.00 48.85 A C ANISOU 1606 CB ASN A 224 7054 4666 6840 1771 -1000 -930 A C ATOM 1607 CG ASN A 224 -12.343 -23.366 -20.340 1.00 49.23 A C ANISOU 1607 CG ASN A 224 6877 4896 6934 1759 -962 -882 A C ATOM 1608 ND2 ASN A 224 -12.953 -23.112 -19.186 1.00 47.06 A N ANISOU 1608 ND2 ASN A 224 6665 4563 6651 1618 -990 -766 A N ATOM 1609 OD1 ASN A 224 -11.373 -22.714 -20.736 1.00 49.87 A O ANISOU 1609 OD1 ASN A 224 6730 5172 7048 1865 -907 -951 A O ATOM 1610 N SER A 225 -10.424 -23.672 -23.375 1.00 50.10 A N ANISOU 1610 N SER A 225 6703 5302 7032 2157 -841 -1211 A N ATOM 1611 CA SER A 225 -8.996 -23.812 -23.631 1.00 51.87 A C ANISOU 1611 CA SER A 225 6771 5676 7262 2415 -854 -1331 A C ATOM 1612 C SER A 225 -8.217 -23.938 -22.328 1.00 51.48 A C ANISOU 1612 C SER A 225 6707 5611 7242 2542 -965 -1305 A C ATOM 1613 O SER A 225 -7.080 -24.412 -22.326 1.00 53.32 A O ANISOU 1613 O SER A 225 6874 5919 7465 2780 -1018 -1395 A O ATOM 1614 CB SER A 225 -8.470 -22.621 -24.429 1.00 51.20 A C ANISOU 1614 CB SER A 225 6374 5890 7191 2365 -707 -1358 A C ATOM 1615 OG SER A 225 -8.631 -21.415 -23.699 1.00 47.32 A O ANISOU 1615 OG SER A 225 5740 5493 6747 2181 -661 -1247 A O ATOM 1616 N ASN A 226 -8.840 -23.506 -21.230 1.00 50.62 A N ANISOU 1616 N ASN A 226 6654 5426 7153 2368 -992 -1174 A N ATOM 1617 CA ASN A 226 -8.202 -23.471 -19.911 1.00 54.17 A C ANISOU 1617 CA ASN A 226 7084 5878 7619 2450 -1093 -1132 A C ATOM 1618 C ASN A 226 -6.891 -22.696 -19.928 1.00 52.78 A C ANISOU 1618 C ASN A 226 6596 5982 7477 2564 -1059 -1199 A C ATOM 1619 O ASN A 226 -5.930 -23.068 -19.265 1.00 48.96 A O ANISOU 1619 O ASN A 226 6076 5535 6994 2762 -1163 -1237 A O ATOM 1620 CB ASN A 226 -7.963 -24.886 -19.377 1.00 56.33 A C ANISOU 1620 CB ASN A 226 7619 5924 7861 2657 -1258 -1154 A C ATOM 1621 CG ASN A 226 -9.238 -25.543 -18.893 1.00 59.23 A C ANISOU 1621 CG ASN A 226 8299 6011 8193 2491 -1315 -1046 A C ATOM 1622 ND2 ASN A 226 -9.836 -24.977 -17.854 1.00 59.50 A N ANISOU 1622 ND2 ASN A 226 8346 6033 8226 2300 -1315 -918 A N ATOM 1623 OD1 ASN A 226 -9.684 -26.545 -19.449 1.00 61.86 A O ANISOU 1623 OD1 ASN A 226 8861 6150 8494 2526 -1357 -1081 A O ATOM 1624 N VAL A 227 -6.863 -21.630 -20.722 1.00 54.02 A N ANISOU 1624 N VAL A 227 6530 6340 7655 2434 -915 -1211 A N ATOM 1625 CA VAL A 227 -5.780 -20.661 -20.691 1.00 52.10 A C ANISOU 1625 CA VAL A 227 5980 6373 7443 2452 -864 -1246 A C ATOM 1626 C VAL A 227 -6.401 -19.270 -20.663 1.00 49.94 A C ANISOU 1626 C VAL A 227 5596 6177 7202 2170 -751 -1153 A C ATOM 1627 O VAL A 227 -7.558 -19.089 -21.048 1.00 46.42 A O ANISOU 1627 O VAL A 227 5267 5621 6748 2004 -688 -1090 A O ATOM 1628 CB VAL A 227 -4.829 -20.789 -21.904 1.00 51.02 A C ANISOU 1628 CB VAL A 227 5654 6442 7287 2616 -796 -1378 A C ATOM 1629 CG1 VAL A 227 -4.226 -22.182 -21.972 1.00 50.69 A C ANISOU 1629 CG1 VAL A 227 5750 6319 7189 2859 -893 -1454 A C ATOM 1630 CG2 VAL A 227 -5.561 -20.457 -23.195 1.00 53.45 A C ANISOU 1630 CG2 VAL A 227 5962 6773 7574 2475 -659 -1378 A C ATOM 1631 N ARG A 228 -5.636 -18.295 -20.191 1.00 52.50 A N ANISOU 1631 N ARG A 228 5701 6687 7561 2120 -733 -1148 A N ATOM 1632 CA ARG A 228 -6.097 -16.916 -20.143 1.00 51.00 A C ANISOU 1632 CA ARG A 228 5411 6563 7404 1868 -634 -1069 A C ATOM 1633 C ARG A 228 -4.906 -15.978 -20.093 1.00 53.85 A C ANISOU 1633 C ARG A 228 5489 7177 7794 1848 -601 -1108 A C ATOM 1634 O ARG A 228 -4.413 -15.658 -19.018 1.00 57.15 A O ANISOU 1634 O ARG A 228 5850 7634 8230 1842 -677 -1097 A O ATOM 1635 CB ARG A 228 -7.001 -16.680 -18.931 1.00 49.07 A C ANISOU 1635 CB ARG A 228 5326 6152 7167 1737 -689 -968 A C ATOM 1636 CG ARG A 228 -7.815 -15.397 -19.027 1.00 49.42 A C ANISOU 1636 CG ARG A 228 5334 6207 7237 1494 -584 -890 A C ATOM 1637 CD ARG A 228 -8.589 -15.102 -17.745 1.00 49.91 A C ANISOU 1637 CD ARG A 228 5524 6144 7296 1385 -635 -808 A C ATOM 1638 NE ARG A 228 -9.509 -13.980 -17.927 1.00 50.51 A N ANISOU 1638 NE ARG A 228 5592 6209 7391 1185 -535 -741 A N ATOM 1639 CZ ARG A 228 -9.143 -12.703 -17.892 1.00 51.06 A C ANISOU 1639 CZ ARG A 228 5512 6388 7499 1072 -479 -735 A C ATOM 1640 NH1 ARG A 228 -7.874 -12.381 -17.677 1.00 47.43 A N1+ ANISOU 1640 NH1 ARG A 228 4883 6076 7063 1115 -508 -792 A N1+ ATOM 1641 NH2 ARG A 228 -10.044 -11.745 -18.075 1.00 53.89 A N ANISOU 1641 NH2 ARG A 228 5895 6711 7872 915 -398 -674 A N ATOM 1642 N HIS A 229 -4.432 -15.552 -21.259 1.00 54.07 A N ANISOU 1642 N HIS A 229 5340 7387 7816 1827 -489 -1152 A N ATOM 1643 CA HIS A 229 -3.306 -14.631 -21.325 1.00 51.15 A C ANISOU 1643 CA HIS A 229 4690 7276 7467 1772 -445 -1183 A C ATOM 1644 C HIS A 229 -3.691 -13.314 -20.666 1.00 49.99 A C ANISOU 1644 C HIS A 229 4524 7104 7365 1521 -418 -1091 A C ATOM 1645 O HIS A 229 -4.870 -12.950 -20.639 1.00 46.38 A O ANISOU 1645 O HIS A 229 4229 6477 6917 1383 -381 -1009 A O ATOM 1646 CB HIS A 229 -2.871 -14.395 -22.772 1.00 50.29 A C ANISOU 1646 CB HIS A 229 4415 7365 7329 1763 -313 -1230 A C ATOM 1647 CG HIS A 229 -2.513 -15.647 -23.511 1.00 51.20 A C ANISOU 1647 CG HIS A 229 4552 7511 7391 2018 -329 -1337 A C ATOM 1648 CD2 HIS A 229 -3.248 -16.445 -24.321 1.00 51.08 A C ANISOU 1648 CD2 HIS A 229 4713 7363 7334 2092 -306 -1359 A C ATOM 1649 ND1 HIS A 229 -1.252 -16.202 -23.469 1.00 52.57 A N ANISOU 1649 ND1 HIS A 229 4554 7878 7544 2239 -379 -1448 A N ATOM 1650 CE1 HIS A 229 -1.228 -17.290 -24.217 1.00 53.90 A C ANISOU 1650 CE1 HIS A 229 4836 7998 7648 2414 -378 -1514 A C ATOM 1651 NE2 HIS A 229 -2.427 -17.460 -24.745 1.00 52.35 A N ANISOU 1651 NE2 HIS A 229 4824 7617 7451 2359 -342 -1487 A N ATOM 1652 N SER A 230 -2.698 -12.604 -20.137 1.00 52.76 A N ANISOU 1652 N SER A 230 4677 7630 7741 1468 -440 -1113 A N ATOM 1653 CA SER A 230 -2.941 -11.341 -19.446 1.00 53.49 A C ANISOU 1653 CA SER A 230 4757 7694 7874 1238 -428 -1045 A C ATOM 1654 C SER A 230 -3.531 -10.302 -20.393 1.00 53.82 A C ANISOU 1654 C SER A 230 4792 7729 7930 1028 -288 -978 A C ATOM 1655 O SER A 230 -4.215 -9.370 -19.964 1.00 53.72 A O ANISOU 1655 O SER A 230 4865 7601 7947 854 -270 -907 A O ATOM 1656 CB SER A 230 -1.649 -10.815 -18.813 1.00 53.84 A C ANISOU 1656 CB SER A 230 4572 7950 7935 1212 -483 -1096 A C ATOM 1657 OG SER A 230 -0.615 -10.684 -19.771 1.00 55.85 A O ANISOU 1657 OG SER A 230 4578 8467 8176 1228 -409 -1154 A O ATOM 1658 N LEU A 231 -3.281 -10.481 -21.687 1.00 54.33 A N ANISOU 1658 N LEU A 231 4763 7915 7964 1060 -192 -1002 A N ATOM 1659 CA LEU A 231 -3.847 -9.604 -22.706 1.00 50.86 A C ANISOU 1659 CA LEU A 231 4331 7473 7521 882 -62 -931 A C ATOM 1660 C LEU A 231 -5.374 -9.592 -22.668 1.00 49.37 A C ANISOU 1660 C LEU A 231 4387 7035 7336 829 -53 -851 A C ATOM 1661 O LEU A 231 -5.996 -8.607 -23.064 1.00 49.66 A O ANISOU 1661 O LEU A 231 4462 7021 7386 660 22 -771 A O ATOM 1662 CB LEU A 231 -3.368 -10.021 -24.095 1.00 50.82 A C ANISOU 1662 CB LEU A 231 4205 7645 7460 958 31 -978 A C ATOM 1663 CG LEU A 231 -1.863 -9.942 -24.335 1.00 53.33 A C ANISOU 1663 CG LEU A 231 4239 8263 7760 996 51 -1056 A C ATOM 1664 CD1 LEU A 231 -1.560 -10.058 -25.823 1.00 54.00 A C ANISOU 1664 CD1 LEU A 231 4210 8533 7777 1015 177 -1082 A C ATOM 1665 CD2 LEU A 231 -1.286 -8.659 -23.749 1.00 51.69 A C ANISOU 1665 CD2 LEU A 231 3897 8144 7599 774 54 -1013 A C ATOM 1666 N ALA A 232 -5.976 -10.679 -22.189 1.00 50.78 A N ANISOU 1666 N ALA A 232 4732 7063 7499 973 -133 -869 A N ATOM 1667 CA ALA A 232 -7.433 -10.754 -22.078 1.00 50.34 A C ANISOU 1667 CA ALA A 232 4892 6797 7439 919 -130 -797 A C ATOM 1668 C ALA A 232 -7.964 -9.581 -21.270 1.00 49.83 A C ANISOU 1668 C ALA A 232 4870 6648 7416 750 -128 -724 A C ATOM 1669 O ALA A 232 -9.036 -9.050 -21.561 1.00 51.18 A O ANISOU 1669 O ALA A 232 5140 6719 7586 650 -75 -653 A O ATOM 1670 CB ALA A 232 -7.863 -12.069 -21.446 1.00 49.73 A C ANISOU 1670 CB ALA A 232 4981 6575 7337 1071 -232 -823 A C ATOM 1671 N SER A 233 -7.193 -9.175 -20.265 1.00 50.04 A N ANISOU 1671 N SER A 233 4817 6723 7471 729 -192 -750 A N ATOM 1672 CA SER A 233 -7.552 -8.044 -19.418 1.00 49.54 A C ANISOU 1672 CA SER A 233 4794 6585 7442 579 -201 -704 A C ATOM 1673 C SER A 233 -7.028 -6.716 -19.954 1.00 48.56 A C ANISOU 1673 C SER A 233 4543 6556 7351 408 -123 -681 A C ATOM 1674 O SER A 233 -7.762 -5.736 -19.992 1.00 48.34 A O ANISOU 1674 O SER A 233 4597 6428 7344 278 -78 -617 A O ATOM 1675 CB SER A 233 -7.032 -8.252 -17.990 1.00 51.85 A C ANISOU 1675 CB SER A 233 5087 6873 7739 628 -320 -746 A C ATOM 1676 OG SER A 233 -7.825 -9.189 -17.281 1.00 54.42 A O ANISOU 1676 OG SER A 233 5586 7059 8031 729 -389 -732 A O ATOM 1677 N SER A 234 -5.763 -6.679 -20.362 1.00 49.00 A N ANISOU 1677 N SER A 234 4401 6809 7408 407 -110 -731 A N ATOM 1678 CA SER A 234 -5.130 -5.402 -20.686 1.00 48.39 A C ANISOU 1678 CA SER A 234 4198 6828 7358 212 -51 -706 A C ATOM 1679 C SER A 234 -5.416 -4.899 -22.108 1.00 49.49 A C ANISOU 1679 C SER A 234 4322 7002 7480 118 76 -641 A C ATOM 1680 O SER A 234 -5.425 -3.691 -22.349 1.00 50.08 A O ANISOU 1680 O SER A 234 4394 7055 7577 -69 128 -580 A O ATOM 1681 CB SER A 234 -3.621 -5.499 -20.472 1.00 47.81 A C ANISOU 1681 CB SER A 234 3894 6986 7286 223 -90 -784 A C ATOM 1682 OG SER A 234 -3.031 -6.400 -21.387 1.00 51.50 A O ANISOU 1682 OG SER A 234 4233 7624 7711 364 -51 -833 A O ATOM 1683 N GLU A 235 -5.648 -5.814 -23.044 1.00 47.31 A N ANISOU 1683 N GLU A 235 4049 6769 7156 246 120 -653 A N ATOM 1684 CA GLU A 235 -5.864 -5.423 -24.435 1.00 46.28 A C ANISOU 1684 CA GLU A 235 3897 6698 6989 169 237 -594 A C ATOM 1685 C GLU A 235 -7.338 -5.135 -24.725 1.00 45.53 A C ANISOU 1685 C GLU A 235 4005 6405 6890 136 266 -508 A C ATOM 1686 O GLU A 235 -7.663 -4.472 -25.712 1.00 46.26 A O ANISOU 1686 O GLU A 235 4110 6508 6959 36 352 -433 A O ATOM 1687 CB GLU A 235 -5.337 -6.504 -25.386 1.00 43.98 A C ANISOU 1687 CB GLU A 235 3500 6575 6634 322 275 -663 A C ATOM 1688 CG GLU A 235 -5.111 -6.037 -26.820 1.00 45.05 A C ANISOU 1688 CG GLU A 235 3544 6860 6714 228 402 -619 A C ATOM 1689 CD GLU A 235 -3.916 -5.092 -26.995 1.00 49.12 A C ANISOU 1689 CD GLU A 235 3853 7577 7234 58 455 -606 A C ATOM 1690 OE1 GLU A 235 -3.215 -4.770 -26.001 1.00 46.30 A O ANISOU 1690 OE1 GLU A 235 3411 7253 6928 8 388 -640 A O ATOM 1691 OE2 GLU A 235 -3.676 -4.676 -28.153 1.00 51.36 A O1- ANISOU 1691 OE2 GLU A 235 4057 7998 7461 -38 564 -560 A O1- ATOM 1692 N TYR A 236 -8.228 -5.625 -23.865 1.00 43.63 A N ANISOU 1692 N TYR A 236 3916 5998 6665 219 193 -514 A N ATOM 1693 CA TYR A 236 -9.651 -5.333 -24.016 1.00 43.75 A C ANISOU 1693 CA TYR A 236 4100 5848 6673 191 213 -438 A C ATOM 1694 C TYR A 236 -9.926 -3.820 -24.045 1.00 45.42 A C ANISOU 1694 C TYR A 236 4347 5990 6919 23 254 -355 A C ATOM 1695 O TYR A 236 -10.540 -3.340 -24.996 1.00 48.80 A O ANISOU 1695 O TYR A 236 4823 6397 7323 -28 322 -280 A O ATOM 1696 CB TYR A 236 -10.483 -6.001 -22.907 1.00 38.49 A C ANISOU 1696 CB TYR A 236 3571 5038 6014 281 128 -457 A C ATOM 1697 CG TYR A 236 -11.976 -5.828 -23.090 1.00 34.55 A C ANISOU 1697 CG TYR A 236 3220 4409 5499 265 151 -387 A C ATOM 1698 CD1 TYR A 236 -12.629 -4.697 -22.619 1.00 32.25 A C ANISOU 1698 CD1 TYR A 236 3000 4017 5238 176 159 -331 A C ATOM 1699 CD2 TYR A 236 -12.734 -6.794 -23.751 1.00 37.20 A C ANISOU 1699 CD2 TYR A 236 3620 4731 5784 343 160 -385 A C ATOM 1700 CE1 TYR A 236 -14.004 -4.525 -22.799 1.00 31.07 A C ANISOU 1700 CE1 TYR A 236 2963 3775 5067 180 179 -272 A C ATOM 1701 CE2 TYR A 236 -14.107 -6.635 -23.930 1.00 34.08 A C ANISOU 1701 CE2 TYR A 236 3335 4247 5367 322 178 -323 A C ATOM 1702 CZ TYR A 236 -14.735 -5.498 -23.451 1.00 30.93 A C ANISOU 1702 CZ TYR A 236 2985 3769 4997 248 188 -265 A C ATOM 1703 OH TYR A 236 -16.099 -5.335 -23.624 1.00 28.70 A O ANISOU 1703 OH TYR A 236 2790 3424 4689 246 204 -209 A O ATOM 1704 N PRO A 237 -9.482 -3.062 -23.018 1.00 40.25 A N ANISOU 1704 N PRO A 237 3684 5293 6316 -59 207 -370 A N ATOM 1705 CA PRO A 237 -9.797 -1.629 -23.087 1.00 39.53 A C ANISOU 1705 CA PRO A 237 3661 5102 6256 -211 240 -295 A C ATOM 1706 C PRO A 237 -9.133 -0.925 -24.268 1.00 40.32 A C ANISOU 1706 C PRO A 237 3670 5308 6341 -345 326 -237 A C ATOM 1707 O PRO A 237 -9.665 0.082 -24.741 1.00 41.83 A O ANISOU 1707 O PRO A 237 3954 5401 6537 -444 368 -147 A O ATOM 1708 CB PRO A 237 -9.256 -1.084 -21.758 1.00 36.37 A C ANISOU 1708 CB PRO A 237 3258 4656 5905 -274 164 -346 A C ATOM 1709 CG PRO A 237 -8.199 -2.038 -21.364 1.00 35.38 A C ANISOU 1709 CG PRO A 237 2987 4685 5771 -198 114 -435 A C ATOM 1710 CD PRO A 237 -8.702 -3.379 -21.807 1.00 37.51 A C ANISOU 1710 CD PRO A 237 3279 4978 5995 -25 118 -451 A C ATOM 1711 N VAL A 238 -8.001 -1.453 -24.733 1.00 38.62 A N ANISOU 1711 N VAL A 238 3278 5296 6101 -342 351 -284 A N ATOM 1712 CA VAL A 238 -7.292 -0.885 -25.876 1.00 41.46 A C ANISOU 1712 CA VAL A 238 3527 5800 6428 -475 442 -231 A C ATOM 1713 C VAL A 238 -8.157 -0.940 -27.144 1.00 43.61 A C ANISOU 1713 C VAL A 238 3877 6053 6639 -449 520 -148 A C ATOM 1714 O VAL A 238 -8.213 0.025 -27.906 1.00 45.83 A O ANISOU 1714 O VAL A 238 4189 6323 6902 -591 584 -48 A O ATOM 1715 CB VAL A 238 -5.951 -1.615 -26.123 1.00 44.49 A C ANISOU 1715 CB VAL A 238 3680 6443 6780 -437 457 -316 A C ATOM 1716 CG1 VAL A 238 -5.292 -1.125 -27.414 1.00 44.54 A C ANISOU 1716 CG1 VAL A 238 3562 6631 6729 -572 569 -257 A C ATOM 1717 CG2 VAL A 238 -5.009 -1.425 -24.934 1.00 36.71 A C ANISOU 1717 CG2 VAL A 238 2594 5504 5849 -485 376 -388 A C ATOM 1718 N ARG A 239 -8.838 -2.066 -27.348 1.00 41.46 A N ANISOU 1718 N ARG A 239 3650 5774 6330 -275 506 -188 A N ATOM 1719 CA ARG A 239 -9.730 -2.244 -28.488 1.00 43.19 A C ANISOU 1719 CA ARG A 239 3945 5982 6483 -237 564 -124 A C ATOM 1720 C ARG A 239 -10.867 -1.230 -28.480 1.00 45.97 A C ANISOU 1720 C ARG A 239 4464 6148 6855 -303 563 -17 A C ATOM 1721 O ARG A 239 -11.298 -0.758 -29.538 1.00 46.88 A O ANISOU 1721 O ARG A 239 4621 6272 6918 -352 623 76 A O ATOM 1722 CB ARG A 239 -10.308 -3.661 -28.502 1.00 41.72 A C ANISOU 1722 CB ARG A 239 3797 5793 6262 -51 527 -199 A C ATOM 1723 CG ARG A 239 -9.295 -4.741 -28.836 1.00 44.20 A C ANISOU 1723 CG ARG A 239 3968 6290 6535 52 536 -304 A C ATOM 1724 CD ARG A 239 -8.734 -4.565 -30.246 1.00 45.04 A C ANISOU 1724 CD ARG A 239 3965 6587 6560 -1 641 -278 A C ATOM 1725 NE ARG A 239 -7.754 -5.602 -30.552 1.00 46.73 A N ANISOU 1725 NE ARG A 239 4034 6992 6729 124 652 -394 A N ATOM 1726 CZ ARG A 239 -6.465 -5.531 -30.238 1.00 47.04 A C ANISOU 1726 CZ ARG A 239 3893 7194 6784 106 657 -452 A C ATOM 1727 NH1 ARG A 239 -5.988 -4.463 -29.614 1.00 49.26 A N1+ ANISOU 1727 NH1 ARG A 239 4124 7465 7127 -57 650 -402 A N1+ ATOM 1728 NH2 ARG A 239 -5.650 -6.529 -30.549 1.00 47.21 A N ANISOU 1728 NH2 ARG A 239 3787 7394 6759 256 664 -567 A N ATOM 1729 N ARG A 240 -11.356 -0.900 -27.288 1.00 42.46 A N ANISOU 1729 N ARG A 240 4114 5542 6476 -291 493 -30 A N ATOM 1730 CA ARG A 240 -12.436 0.069 -27.161 1.00 40.61 A C ANISOU 1730 CA ARG A 240 4036 5131 6262 -323 485 55 A C ATOM 1731 C ARG A 240 -11.963 1.463 -27.559 1.00 44.37 A C ANISOU 1731 C ARG A 240 4535 5568 6756 -496 524 144 A C ATOM 1732 O ARG A 240 -12.701 2.221 -28.185 1.00 48.37 A O ANISOU 1732 O ARG A 240 5151 5984 7242 -525 550 246 A O ATOM 1733 CB ARG A 240 -12.988 0.086 -25.737 1.00 39.02 A C ANISOU 1733 CB ARG A 240 3921 4788 6116 -264 405 3 A C ATOM 1734 CG ARG A 240 -13.597 -1.235 -25.295 1.00 36.28 A C ANISOU 1734 CG ARG A 240 3584 4455 5746 -115 364 -63 A C ATOM 1735 CD ARG A 240 -14.524 -1.023 -24.118 1.00 35.65 A C ANISOU 1735 CD ARG A 240 3616 4234 5695 -66 307 -77 A C ATOM 1736 NE ARG A 240 -15.475 0.049 -24.384 1.00 38.70 A N ANISOU 1736 NE ARG A 240 4110 4510 6085 -88 329 5 A N ATOM 1737 CZ ARG A 240 -16.599 0.245 -23.702 1.00 38.16 A C ANISOU 1737 CZ ARG A 240 4138 4344 6018 -20 300 7 A C ATOM 1738 NH1 ARG A 240 -16.919 -0.562 -22.700 1.00 37.48 A N1+ ANISOU 1738 NH1 ARG A 240 4058 4258 5925 51 254 -59 A N1+ ATOM 1739 NH2 ARG A 240 -17.409 1.248 -24.027 1.00 35.02 A N ANISOU 1739 NH2 ARG A 240 3831 3855 5620 -17 318 79 A N ATOM 1740 N ARG A 241 -10.727 1.795 -27.209 1.00 42.71 A N ANISOU 1740 N ARG A 241 4222 5428 6578 -617 523 109 A N ATOM 1741 CA ARG A 241 -10.174 3.097 -27.565 1.00 44.82 A C ANISOU 1741 CA ARG A 241 4512 5658 6860 -818 557 195 A C ATOM 1742 C ARG A 241 -9.909 3.169 -29.067 1.00 48.18 A C ANISOU 1742 C ARG A 241 4878 6224 7203 -889 653 286 A C ATOM 1743 O ARG A 241 -10.177 4.186 -29.707 1.00 51.12 A O ANISOU 1743 O ARG A 241 5357 6508 7558 -1001 686 409 A O ATOM 1744 CB ARG A 241 -8.887 3.377 -26.781 1.00 42.60 A C ANISOU 1744 CB ARG A 241 4115 5444 6628 -949 527 127 A C ATOM 1745 N GLN A 242 -9.386 2.081 -29.624 1.00 46.66 A N ANISOU 1745 N GLN A 242 4529 6249 6953 -814 693 226 A N ATOM 1746 CA GLN A 242 -9.099 2.019 -31.048 1.00 47.68 A C ANISOU 1746 CA GLN A 242 4586 6545 6983 -865 789 294 A C ATOM 1747 C GLN A 242 -10.384 2.170 -31.868 1.00 48.91 A C ANISOU 1747 C GLN A 242 4897 6602 7086 -798 806 392 A C ATOM 1748 O GLN A 242 -10.399 2.864 -32.882 1.00 51.19 A O ANISOU 1748 O GLN A 242 5223 6917 7311 -906 868 512 A O ATOM 1749 CB GLN A 242 -8.388 0.710 -31.391 1.00 47.23 A C ANISOU 1749 CB GLN A 242 4343 6730 6872 -752 819 181 A C ATOM 1750 CG GLN A 242 -6.964 0.627 -30.861 1.00 47.88 A C ANISOU 1750 CG GLN A 242 4232 6978 6984 -825 817 98 A C ATOM 1751 CD GLN A 242 -6.341 -0.748 -31.041 1.00 49.57 A C ANISOU 1751 CD GLN A 242 4277 7407 7151 -656 827 -32 A C ATOM 1752 NE2 GLN A 242 -5.042 -0.778 -31.312 1.00 53.06 A N ANISOU 1752 NE2 GLN A 242 4505 8095 7561 -729 878 -74 A N ATOM 1753 OE1 GLN A 242 -7.020 -1.770 -30.937 1.00 48.92 A O ANISOU 1753 OE1 GLN A 242 4259 7270 7059 -463 786 -97 A O ATOM 1754 N CYS A 243 -11.462 1.533 -31.416 1.00 46.07 A N ANISOU 1754 N CYS A 243 4625 6137 6744 -628 747 346 A N ATOM 1755 CA CYS A 243 -12.753 1.655 -32.083 1.00 44.95 A C ANISOU 1755 CA CYS A 243 4614 5912 6552 -556 749 429 A C ATOM 1756 C CYS A 243 -13.298 3.076 -31.984 1.00 47.57 A C ANISOU 1756 C CYS A 243 5106 6047 6919 -641 732 552 A C ATOM 1757 O CYS A 243 -13.813 3.621 -32.967 1.00 47.35 A O ANISOU 1757 O CYS A 243 5158 6004 6827 -666 764 671 A O ATOM 1758 CB CYS A 243 -13.765 0.668 -31.496 1.00 42.08 A C ANISOU 1758 CB CYS A 243 4294 5491 6203 -377 685 349 A C ATOM 1759 SG CYS A 243 -13.513 -1.048 -31.993 1.00 43.53 A S ANISOU 1759 SG CYS A 243 4361 5863 6316 -251 699 231 A S ATOM 1760 N GLU A 244 -13.192 3.664 -30.792 1.00 46.70 A N ANISOU 1760 N GLU A 244 5053 5785 6906 -675 675 518 A N ATOM 1761 CA GLU A 244 -13.626 5.041 -30.559 1.00 47.39 A C ANISOU 1761 CA GLU A 244 5312 5659 7037 -747 648 613 A C ATOM 1762 C GLU A 244 -12.861 6.017 -31.444 1.00 49.49 A C ANISOU 1762 C GLU A 244 5595 5941 7269 -948 706 735 A C ATOM 1763 O GLU A 244 -13.437 6.956 -31.995 1.00 53.33 A O ANISOU 1763 O GLU A 244 6235 6295 7732 -980 707 864 A O ATOM 1764 CB GLU A 244 -13.444 5.425 -29.088 1.00 51.50 A C ANISOU 1764 CB GLU A 244 5876 6033 7657 -760 578 528 A C ATOM 1765 CG GLU A 244 -14.458 4.791 -28.148 1.00 55.58 A C ANISOU 1765 CG GLU A 244 6433 6485 8201 -573 517 442 A C ATOM 1766 CD GLU A 244 -13.966 4.717 -26.709 1.00 61.82 A C ANISOU 1766 CD GLU A 244 7201 7224 9064 -583 458 326 A C ATOM 1767 OE1 GLU A 244 -12.924 5.334 -26.394 1.00 66.89 A O ANISOU 1767 OE1 GLU A 244 7816 7852 9745 -738 452 314 A O ATOM 1768 OE2 GLU A 244 -14.624 4.036 -25.892 1.00 61.51 A O1- ANISOU 1768 OE2 GLU A 244 7170 7169 9034 -446 415 249 A O1- ATOM 1769 N GLU A 245 -11.561 5.782 -31.582 1.00 47.43 A N ANISOU 1769 N GLU A 245 5172 5852 6996 -1083 752 699 A N ATOM 1770 CA GLU A 245 -10.700 6.669 -32.348 1.00 51.04 A C ANISOU 1770 CA GLU A 245 5620 6357 7414 -1311 815 812 A C ATOM 1771 C GLU A 245 -11.020 6.607 -33.843 1.00 54.45 A C ANISOU 1771 C GLU A 245 6062 6902 7723 -1310 890 931 A C ATOM 1772 O GLU A 245 -10.856 7.596 -34.557 1.00 58.64 A O ANISOU 1772 O GLU A 245 6686 7383 8212 -1471 926 1078 A O ATOM 1773 CB GLU A 245 -9.227 6.324 -32.100 1.00 50.83 A C ANISOU 1773 CB GLU A 245 5377 6539 7396 -1444 849 728 A C ATOM 1774 N VAL A 246 -11.478 5.449 -34.313 1.00 55.08 A N ANISOU 1774 N VAL A 246 6061 7129 7740 -1137 908 871 A N ATOM 1775 CA VAL A 246 -11.878 5.299 -35.714 1.00 56.98 A C ANISOU 1775 CA VAL A 246 6314 7486 7851 -1115 970 968 A C ATOM 1776 C VAL A 246 -13.225 5.970 -35.974 1.00 56.42 A C ANISOU 1776 C VAL A 246 6454 7213 7770 -1034 921 1084 A C ATOM 1777 O VAL A 246 -13.404 6.652 -36.985 1.00 58.46 A O ANISOU 1777 O VAL A 246 6801 7467 7943 -1109 956 1235 A O ATOM 1778 CB VAL A 246 -11.963 3.819 -36.133 1.00 55.13 A C ANISOU 1778 CB VAL A 246 5939 7461 7546 -954 995 851 A C ATOM 1779 CG1 VAL A 246 -12.522 3.699 -37.544 1.00 57.81 A C ANISOU 1779 CG1 VAL A 246 6314 7905 7744 -923 1045 946 A C ATOM 1780 CG2 VAL A 246 -10.598 3.167 -36.049 1.00 54.03 A C ANISOU 1780 CG2 VAL A 246 5585 7545 7398 -1009 1048 742 A C ATOM 1781 N ALA A 247 -14.169 5.778 -35.057 1.00 54.35 A N ANISOU 1781 N ALA A 247 6267 6797 7585 -875 839 1016 A N ATOM 1782 CA ALA A 247 -15.470 6.435 -35.152 1.00 53.69 A C ANISOU 1782 CA ALA A 247 6367 6532 7502 -772 784 1109 A C ATOM 1783 C ALA A 247 -15.322 7.957 -35.101 1.00 60.54 A C ANISOU 1783 C ALA A 247 7410 7188 8407 -907 768 1241 A C ATOM 1784 O ALA A 247 -16.037 8.681 -35.792 1.00 63.65 A O ANISOU 1784 O ALA A 247 7952 7484 8749 -880 754 1379 A O ATOM 1785 CB ALA A 247 -16.394 5.954 -34.042 1.00 43.35 A C ANISOU 1785 CB ALA A 247 5079 5123 6268 -593 708 997 A C ATOM 1786 N ARG A 248 -14.388 8.430 -34.281 1.00 61.32 A N ANISOU 1786 N ARG A 248 7497 7211 8590 -1052 762 1197 A N ATOM 1787 CA ARG A 248 -14.130 9.858 -34.146 1.00 62.12 A C ANISOU 1787 CA ARG A 248 7778 7091 8735 -1209 739 1308 A C ATOM 1788 C ARG A 248 -13.625 10.463 -35.451 1.00 62.93 A C ANISOU 1788 C ARG A 248 7916 7258 8734 -1392 809 1481 A C ATOM 1789 O ARG A 248 -14.051 11.548 -35.845 1.00 65.46 A O ANISOU 1789 O ARG A 248 8448 7384 9039 -1434 782 1631 A O ATOM 1790 CB ARG A 248 -13.117 10.113 -33.026 1.00 62.64 A C ANISOU 1790 CB ARG A 248 7795 7103 8902 -1354 718 1208 A C ATOM 1791 CG ARG A 248 -12.726 11.575 -32.856 1.00 64.72 A C ANISOU 1791 CG ARG A 248 8249 7130 9210 -1554 691 1310 A C ATOM 1792 N ALA A 249 -12.719 9.751 -36.117 1.00 60.11 A N ANISOU 1792 N ALA A 249 7360 7180 8300 -1491 897 1462 A N ATOM 1793 CA ALA A 249 -12.113 10.238 -37.352 1.00 60.30 A C ANISOU 1793 CA ALA A 249 7386 7317 8207 -1686 980 1620 A C ATOM 1794 C ALA A 249 -13.110 10.270 -38.513 1.00 62.95 A C ANISOU 1794 C ALA A 249 7827 7666 8423 -1569 987 1751 A C ATOM 1795 O ALA A 249 -12.963 11.065 -39.441 1.00 69.09 A O ANISOU 1795 O ALA A 249 8715 8424 9111 -1712 1024 1930 A O ATOM 1796 CB ALA A 249 -10.907 9.382 -37.717 1.00 57.01 A C ANISOU 1796 CB ALA A 249 6702 7231 7730 -1791 1077 1540 A C ATOM 1797 N LEU A 250 -14.122 9.410 -38.457 1.00 60.00 A N ANISOU 1797 N LEU A 250 7424 7332 8040 -1321 949 1667 A N ATOM 1798 CA LEU A 250 -15.102 9.310 -39.536 1.00 59.76 A C ANISOU 1798 CA LEU A 250 7466 7350 7889 -1197 945 1770 A C ATOM 1799 C LEU A 250 -16.334 10.168 -39.276 1.00 60.67 A C ANISOU 1799 C LEU A 250 7809 7194 8048 -1060 847 1857 A C ATOM 1800 O LEU A 250 -17.271 10.175 -40.071 1.00 61.50 A O ANISOU 1800 O LEU A 250 7986 7322 8061 -935 823 1946 A O ATOM 1801 CB LEU A 250 -15.524 7.853 -39.747 1.00 57.45 A C ANISOU 1801 CB LEU A 250 7007 7276 7544 -1019 957 1631 A C ATOM 1802 CG LEU A 250 -14.723 7.017 -40.751 1.00 60.99 A C ANISOU 1802 CG LEU A 250 7278 8034 7861 -1089 1059 1604 A C ATOM 1803 CD1 LEU A 250 -13.229 7.025 -40.454 1.00 61.71 A C ANISOU 1803 CD1 LEU A 250 7226 8238 7984 -1281 1132 1552 A C ATOM 1804 CD2 LEU A 250 -15.252 5.594 -40.769 1.00 61.52 A C ANISOU 1804 CD2 LEU A 250 7225 8252 7899 -895 1045 1447 A C ATOM 1805 N GLY A 251 -16.330 10.891 -38.160 1.00 62.04 A N ANISOU 1805 N GLY A 251 8094 7122 8355 -1074 786 1825 A N ATOM 1806 CA GLY A 251 -17.449 11.746 -37.804 1.00 61.38 A C ANISOU 1806 CA GLY A 251 8227 6773 8320 -924 691 1887 A C ATOM 1807 C GLY A 251 -18.674 10.957 -37.385 1.00 60.06 A C ANISOU 1807 C GLY A 251 8003 6648 8169 -652 636 1776 A C ATOM 1808 O GLY A 251 -19.790 11.480 -37.387 1.00 62.43 A O ANISOU 1808 O GLY A 251 8443 6810 8468 -483 565 1835 A O ATOM 1809 N ALA A 252 -18.466 9.697 -37.015 1.00 57.77 A N ANISOU 1809 N ALA A 252 7507 6551 7890 -611 665 1617 A N ATOM 1810 CA ALA A 252 -19.570 8.806 -36.666 1.00 56.05 A C ANISOU 1810 CA ALA A 252 7217 6403 7675 -391 621 1513 A C ATOM 1811 C ALA A 252 -19.728 8.658 -35.160 1.00 56.46 A C ANISOU 1811 C ALA A 252 7256 6341 7855 -316 574 1366 A C ATOM 1812 O ALA A 252 -18.741 8.615 -34.425 1.00 58.07 A O ANISOU 1812 O ALA A 252 7410 6522 8133 -436 593 1286 A O ATOM 1813 CB ALA A 252 -19.369 7.443 -37.311 1.00 20.00 A C ATOM 1814 N ALA A 253 -20.977 8.575 -34.710 1.00 55.63 A N ANISOU 1814 N ALA A 253 7186 6184 7765 -117 512 1330 A N ATOM 1815 CA ALA A 253 -21.284 8.385 -33.296 1.00 53.32 A C ANISOU 1815 CA ALA A 253 6879 5809 7572 -28 470 1193 A C ATOM 1816 C ALA A 253 -20.745 7.049 -32.790 1.00 54.12 A C ANISOU 1816 C ALA A 253 6797 6075 7690 -61 500 1046 A C ATOM 1817 O ALA A 253 -20.301 6.937 -31.643 1.00 54.96 A O ANISOU 1817 O ALA A 253 6880 6121 7880 -85 485 940 A O ATOM 1818 CB ALA A 253 -22.784 8.477 -33.062 1.00 20.00 A C ATOM 1819 N SER A 254 -20.798 6.037 -33.650 1.00 52.01 A N ANISOU 1819 N SER A 254 6412 6011 7336 -53 534 1041 A N ATOM 1820 CA SER A 254 -20.237 4.725 -33.345 1.00 49.62 A C ANISOU 1820 CA SER A 254 5956 5860 7037 -77 559 911 A C ATOM 1821 C SER A 254 -20.003 3.964 -34.637 1.00 48.42 A C ANISOU 1821 C SER A 254 5717 5906 6773 -109 609 936 A C ATOM 1822 O SER A 254 -20.461 4.379 -35.695 1.00 48.41 A O ANISOU 1822 O SER A 254 5769 5937 6686 -99 617 1051 A O ATOM 1823 CB SER A 254 -21.161 3.928 -32.429 1.00 48.74 A C ANISOU 1823 CB SER A 254 5806 5760 6954 59 511 803 A C ATOM 1824 OG SER A 254 -22.321 3.514 -33.128 1.00 51.02 A O ANISOU 1824 OG SER A 254 6082 6143 7160 164 493 838 A O ATOM 1825 N LEU A 255 -19.302 2.839 -34.550 1.00 48.45 A N ANISOU 1825 N LEU A 255 5595 6043 6770 -135 638 825 A N ATOM 1826 CA LEU A 255 -19.025 2.032 -35.733 1.00 49.36 A C ANISOU 1826 CA LEU A 255 5628 6352 6774 -151 686 822 A C ATOM 1827 C LEU A 255 -20.287 1.376 -36.291 1.00 48.83 A C ANISOU 1827 C LEU A 255 5569 6358 6625 -35 650 821 A C ATOM 1828 O LEU A 255 -20.255 0.780 -37.363 1.00 49.90 A O ANISOU 1828 O LEU A 255 5661 6646 6652 -39 680 824 A O ATOM 1829 CB LEU A 255 -17.976 0.965 -35.417 1.00 47.34 A C ANISOU 1829 CB LEU A 255 5245 6207 6535 -177 715 686 A C ATOM 1830 CG LEU A 255 -16.573 1.500 -35.133 1.00 44.63 A C ANISOU 1830 CG LEU A 255 4850 5866 6243 -309 760 685 A C ATOM 1831 CD1 LEU A 255 -15.577 0.357 -34.999 1.00 41.23 A C ANISOU 1831 CD1 LEU A 255 4274 5584 5807 -300 786 550 A C ATOM 1832 CD2 LEU A 255 -16.147 2.482 -36.225 1.00 43.88 A C ANISOU 1832 CD2 LEU A 255 4786 5811 6075 -437 823 829 A C ATOM 1833 N ARG A 256 -21.395 1.484 -35.564 1.00 47.04 A N ANISOU 1833 N ARG A 256 5391 6038 6445 63 587 812 A N ATOM 1834 CA ARG A 256 -22.672 0.980 -36.053 1.00 45.53 A C ANISOU 1834 CA ARG A 256 5196 5926 6176 159 546 821 A C ATOM 1835 C ARG A 256 -23.153 1.790 -37.261 1.00 46.12 A C ANISOU 1835 C ARG A 256 5333 6036 6154 169 548 967 A C ATOM 1836 O ARG A 256 -23.866 1.274 -38.113 1.00 47.18 A O ANISOU 1836 O ARG A 256 5442 6299 6183 212 531 981 A O ATOM 1837 CB ARG A 256 -23.722 1.009 -34.939 1.00 41.51 A C ANISOU 1837 CB ARG A 256 4707 5332 5734 256 484 782 A C ATOM 1838 CG ARG A 256 -25.109 0.532 -35.357 1.00 38.34 A C ANISOU 1838 CG ARG A 256 4281 5033 5254 345 438 791 A C ATOM 1839 CD ARG A 256 -25.112 -0.945 -35.726 1.00 39.01 A C ANISOU 1839 CD ARG A 256 4289 5256 5276 317 437 692 A C ATOM 1840 NE ARG A 256 -26.447 -1.418 -36.091 1.00 42.29 A N ANISOU 1840 NE ARG A 256 4675 5778 5615 375 385 696 A N ATOM 1841 CZ ARG A 256 -27.376 -1.797 -35.216 1.00 42.76 A C ANISOU 1841 CZ ARG A 256 4705 5838 5705 418 341 647 A C ATOM 1842 NH1 ARG A 256 -28.561 -2.214 -35.641 1.00 39.78 A N1+ ANISOU 1842 NH1 ARG A 256 4283 5586 5248 451 296 654 A N1+ ATOM 1843 NH2 ARG A 256 -27.122 -1.758 -33.913 1.00 42.94 A N ANISOU 1843 NH2 ARG A 256 4736 5752 5829 422 343 591 A N ATOM 1844 N GLU A 257 -22.745 3.055 -37.328 1.00 49.32 A N ANISOU 1844 N GLU A 257 5831 6321 6589 121 564 1079 A N ATOM 1845 CA GLU A 257 -23.185 3.968 -38.383 1.00 52.49 A C ANISOU 1845 CA GLU A 257 6323 6719 6902 134 556 1239 A C ATOM 1846 C GLU A 257 -22.299 3.886 -39.619 1.00 57.13 A C ANISOU 1846 C GLU A 257 6887 7439 7379 15 627 1302 A C ATOM 1847 O GLU A 257 -22.535 4.572 -40.616 1.00 61.59 A O ANISOU 1847 O GLU A 257 7530 8023 7849 5 628 1446 A O ATOM 1848 CB GLU A 257 -23.202 5.407 -37.866 1.00 54.45 A C ANISOU 1848 CB GLU A 257 6713 6745 7230 138 531 1338 A C ATOM 1849 CG GLU A 257 -23.878 5.577 -36.517 1.00 56.53 A C ANISOU 1849 CG GLU A 257 7000 6875 7605 249 475 1259 A C ATOM 1850 CD GLU A 257 -25.359 5.263 -36.565 1.00 60.97 A C ANISOU 1850 CD GLU A 257 7533 7512 8122 419 413 1251 A C ATOM 1851 OE1 GLU A 257 -25.991 5.534 -37.611 1.00 64.61 A O ANISOU 1851 OE1 GLU A 257 8024 8044 8480 474 391 1358 A O ATOM 1852 OE2 GLU A 257 -25.890 4.748 -35.558 1.00 58.81 A O1- ANISOU 1852 OE2 GLU A 257 7200 7239 7905 491 387 1141 A O1- ATOM 1853 N VAL A 258 -21.272 3.048 -39.548 1.00 56.23 A N ANISOU 1853 N VAL A 258 6667 7426 7271 -67 686 1195 A N ATOM 1854 CA VAL A 258 -20.293 2.953 -40.619 1.00 54.93 A C ANISOU 1854 CA VAL A 258 6459 7411 7002 -182 767 1234 A C ATOM 1855 C VAL A 258 -20.399 1.624 -41.355 1.00 56.25 A C ANISOU 1855 C VAL A 258 6526 7787 7058 -137 784 1132 A C ATOM 1856 O VAL A 258 -20.497 0.567 -40.734 1.00 57.69 A O ANISOU 1856 O VAL A 258 6641 7992 7289 -77 760 982 A O ATOM 1857 CB VAL A 258 -18.860 3.127 -40.073 1.00 51.53 A C ANISOU 1857 CB VAL A 258 5971 6958 6648 -315 830 1191 A C ATOM 1858 CG1 VAL A 258 -17.835 2.935 -41.177 1.00 51.59 A C ANISOU 1858 CG1 VAL A 258 5901 7166 6536 -429 926 1217 A C ATOM 1859 CG2 VAL A 258 -18.706 4.496 -39.441 1.00 52.25 A C ANISOU 1859 CG2 VAL A 258 6181 6834 6837 -385 810 1294 A C ATOM 1860 N GLN A 259 -20.386 1.684 -42.681 1.00 57.00 A N ANISOU 1860 N GLN A 259 6629 8030 6999 -169 821 1214 A N ATOM 1861 CA GLN A 259 -20.365 0.479 -43.496 1.00 57.18 A C ANISOU 1861 CA GLN A 259 6570 8258 6898 -137 843 1111 A C ATOM 1862 C GLN A 259 -19.005 0.323 -44.157 1.00 57.70 A C ANISOU 1862 C GLN A 259 6557 8480 6886 -242 951 1092 A C ATOM 1863 O GLN A 259 -18.248 1.289 -44.264 1.00 58.81 A O ANISOU 1863 O GLN A 259 6717 8595 7035 -361 1008 1205 A O ATOM 1864 CB GLN A 259 -21.468 0.514 -44.552 1.00 57.48 A C ANISOU 1864 CB GLN A 259 6662 8386 6792 -78 798 1194 A C ATOM 1865 N LEU A 260 -18.709 -0.896 -44.597 1.00 57.24 A N ANISOU 1865 N LEU A 260 6412 8587 6749 -201 978 947 A N ATOM 1866 CA LEU A 260 -17.417 -1.233 -45.187 1.00 59.48 A C ANISOU 1866 CA LEU A 260 6592 9056 6951 -267 1084 892 A C ATOM 1867 C LEU A 260 -16.980 -0.244 -46.271 1.00 60.94 A C ANISOU 1867 C LEU A 260 6801 9352 7002 -391 1164 1066 A C ATOM 1868 O LEU A 260 -15.837 0.211 -46.275 1.00 60.17 A O ANISOU 1868 O LEU A 260 6637 9315 6909 -509 1250 1099 A O ATOM 1869 CB LEU A 260 -17.465 -2.651 -45.760 1.00 60.67 A C ANISOU 1869 CB LEU A 260 6687 9367 6997 -172 1086 722 A C ATOM 1870 CG LEU A 260 -16.236 -3.162 -46.518 1.00 62.52 A C ANISOU 1870 CG LEU A 260 6808 9832 7115 -197 1195 637 A C ATOM 1871 CD1 LEU A 260 -14.997 -3.140 -45.628 1.00 62.74 A C ANISOU 1871 CD1 LEU A 260 6727 9847 7266 -233 1245 569 A C ATOM 1872 CD2 LEU A 260 -16.497 -4.564 -47.056 1.00 60.72 A C ANISOU 1872 CD2 LEU A 260 6566 9720 6785 -78 1173 459 A C ATOM 1873 N GLU A 261 -17.898 0.101 -47.169 1.00 61.86 A N ANISOU 1873 N GLU A 261 7010 9499 6995 -371 1131 1183 A N ATOM 1874 CA GLU A 261 -17.589 1.001 -48.279 1.00 67.08 A C ANISOU 1874 CA GLU A 261 7716 10267 7505 -486 1198 1364 A C ATOM 1875 C GLU A 261 -17.223 2.400 -47.788 1.00 64.74 A C ANISOU 1875 C GLU A 261 7499 9792 7306 -613 1210 1537 A C ATOM 1876 O GLU A 261 -16.258 2.999 -48.267 1.00 61.97 A O ANISOU 1876 O GLU A 261 7127 9531 6888 -769 1304 1633 A O ATOM 1877 CB GLU A 261 -18.764 1.070 -49.264 1.00 72.87 A C ANISOU 1877 CB GLU A 261 8545 11056 8087 -417 1136 1457 A C ATOM 1878 CG GLU A 261 -20.141 0.991 -48.618 1.00 76.73 A C ANISOU 1878 CG GLU A 261 9103 11377 8673 -286 1003 1443 A C ATOM 1879 CD GLU A 261 -20.574 -0.440 -48.325 1.00 78.16 A C ANISOU 1879 CD GLU A 261 9211 11615 8872 -177 956 1228 A C ATOM 1880 OE1 GLU A 261 -19.806 -1.374 -48.643 1.00 79.58 A O ANISOU 1880 OE1 GLU A 261 9301 11944 8990 -184 1020 1085 A O ATOM 1881 OE2 GLU A 261 -21.676 -0.631 -47.768 1.00 77.09 A O1- ANISOU 1881 OE2 GLU A 261 9108 11373 8809 -85 855 1201 A O1- ATOM 1882 N GLU A 262 -17.989 2.912 -46.828 1.00 63.94 A N ANISOU 1882 N GLU A 262 7493 9445 7358 -553 1114 1570 A N ATOM 1883 CA GLU A 262 -17.679 4.199 -46.217 1.00 64.70 A C ANISOU 1883 CA GLU A 262 7687 9333 7565 -660 1109 1706 A C ATOM 1884 C GLU A 262 -16.321 4.121 -45.529 1.00 66.87 A C ANISOU 1884 C GLU A 262 7846 9629 7935 -784 1184 1619 A C ATOM 1885 O GLU A 262 -15.544 5.078 -45.534 1.00 69.94 A O ANISOU 1885 O GLU A 262 8268 9969 8337 -956 1234 1736 A O ATOM 1886 CB GLU A 262 -18.766 4.605 -45.222 1.00 62.61 A C ANISOU 1886 CB GLU A 262 7528 8814 7445 -537 992 1713 A C ATOM 1887 N LEU A 263 -16.038 2.959 -44.952 1.00 66.23 A N ANISOU 1887 N LEU A 263 7628 9623 7913 -700 1186 1415 A N ATOM 1888 CA LEU A 263 -14.760 2.712 -44.299 1.00 66.85 A C ANISOU 1888 CA LEU A 263 7569 9757 8072 -783 1247 1310 A C ATOM 1889 C LEU A 263 -13.632 2.652 -45.329 1.00 69.26 A C ANISOU 1889 C LEU A 263 7758 10331 8227 -912 1374 1334 A C ATOM 1890 O LEU A 263 -12.547 3.188 -45.100 1.00 71.76 A O ANISOU 1890 O LEU A 263 8003 10685 8576 -1072 1439 1367 A O ATOM 1891 CB LEU A 263 -14.821 1.417 -43.487 1.00 62.83 A C ANISOU 1891 CB LEU A 263 6964 9261 7649 -634 1204 1091 A C ATOM 1892 CG LEU A 263 -13.577 1.046 -42.687 1.00 63.14 A C ANISOU 1892 CG LEU A 263 6856 9355 7781 -678 1244 965 A C ATOM 1893 CD1 LEU A 263 -13.336 2.073 -41.597 1.00 66.12 A C ANISOU 1893 CD1 LEU A 263 7289 9522 8312 -779 1208 1028 A C ATOM 1894 CD2 LEU A 263 -13.719 -0.349 -42.100 1.00 59.78 A C ANISOU 1894 CD2 LEU A 263 6360 8950 7404 -509 1197 761 A C ATOM 1895 N GLU A 264 -13.898 1.998 -46.460 1.00 69.20 A N ANISOU 1895 N GLU A 264 7725 10522 8047 -847 1409 1314 A N ATOM 1896 CA GLU A 264 -12.946 1.943 -47.570 1.00 70.47 A C ANISOU 1896 CA GLU A 264 7779 10966 8029 -955 1537 1342 A C ATOM 1897 C GLU A 264 -12.520 3.339 -47.999 1.00 69.53 A C ANISOU 1897 C GLU A 264 7736 10822 7862 -1177 1593 1572 A C ATOM 1898 O GLU A 264 -11.331 3.622 -48.141 1.00 70.26 A O ANISOU 1898 O GLU A 264 7710 11066 7919 -1342 1696 1593 A O ATOM 1899 CB GLU A 264 -13.547 1.214 -48.778 1.00 74.31 A C ANISOU 1899 CB GLU A 264 8279 11636 8320 -850 1547 1313 A C ATOM 1900 CG GLU A 264 -13.941 -0.235 -48.551 1.00 76.63 A C ANISOU 1900 CG GLU A 264 8516 11970 8631 -651 1496 1085 A C ATOM 1901 CD GLU A 264 -12.785 -1.198 -48.701 1.00 80.43 A C ANISOU 1901 CD GLU A 264 8814 12685 9060 -618 1587 901 A C ATOM 1902 OE1 GLU A 264 -11.622 -0.742 -48.725 1.00 82.07 A O ANISOU 1902 OE1 GLU A 264 8906 13021 9257 -749 1686 936 A O ATOM 1903 OE2 GLU A 264 -13.046 -2.415 -48.802 1.00 81.80 A O1- ANISOU 1903 OE2 GLU A 264 8961 12918 9201 -459 1555 720 A O1- ATOM 1904 N ALA A 265 -13.506 4.207 -48.206 1.00 69.59 A N ANISOU 1904 N ALA A 265 7941 10638 7861 -1181 1520 1747 A N ATOM 1905 CA ALA A 265 -13.264 5.555 -48.715 1.00 71.22 A C ANISOU 1905 CA ALA A 265 8272 10783 8005 -1381 1556 1990 A C ATOM 1906 C ALA A 265 -12.451 6.410 -47.743 1.00 74.46 A C ANISOU 1906 C ALA A 265 8687 11029 8574 -1556 1565 2031 A C ATOM 1907 O ALA A 265 -11.776 7.353 -48.153 1.00 78.02 A O ANISOU 1907 O ALA A 265 9181 11498 8966 -1782 1631 2197 A O ATOM 1908 CB ALA A 265 -14.586 6.238 -49.035 1.00 67.12 A C ANISOU 1908 CB ALA A 265 7977 10066 7459 -1298 1452 2151 A C ATOM 1909 N ALA A 266 -12.515 6.077 -46.458 1.00 73.21 A N ANISOU 1909 N ALA A 266 8492 10716 8610 -1464 1496 1882 A N ATOM 1910 CA ALA A 266 -11.804 6.847 -45.444 1.00 74.36 A C ANISOU 1910 CA ALA A 266 8645 10698 8910 -1619 1488 1900 A C ATOM 1911 C ALA A 266 -10.589 6.089 -44.916 1.00 77.58 A C ANISOU 1911 C ALA A 266 8808 11303 9367 -1661 1555 1720 A C ATOM 1912 O ALA A 266 -10.211 6.242 -43.754 1.00 78.77 A O ANISOU 1912 O ALA A 266 8928 11321 9679 -1691 1511 1643 A O ATOM 1913 CB ALA A 266 -12.743 7.207 -44.303 1.00 70.60 A C ANISOU 1913 CB ALA A 266 8322 9890 8613 -1495 1355 1879 A C ATOM 1914 N ARG A 267 -9.977 5.280 -45.777 1.00 79.76 A N ANISOU 1914 N ARG A 267 8908 11903 9494 -1652 1656 1649 A N ATOM 1915 CA ARG A 267 -8.832 4.466 -45.380 1.00 81.59 A C ANISOU 1915 CA ARG A 267 8891 12358 9753 -1650 1719 1467 A C ATOM 1916 C ARG A 267 -7.616 5.322 -45.042 1.00 84.09 A C ANISOU 1916 C ARG A 267 9118 12722 10110 -1917 1782 1536 A C ATOM 1917 O ARG A 267 -6.835 4.982 -44.155 1.00 84.62 A O ANISOU 1917 O ARG A 267 9028 12838 10285 -1923 1777 1398 A O ATOM 1918 CB ARG A 267 -8.475 3.465 -46.481 1.00 84.03 A C ANISOU 1918 CB ARG A 267 9044 13011 9872 -1567 1819 1377 A C ATOM 1919 CG ARG A 267 -7.424 2.447 -46.065 1.00 86.51 A C ANISOU 1919 CG ARG A 267 9106 13552 10213 -1490 1867 1159 A C ATOM 1920 CD ARG A 267 -7.520 1.172 -46.890 1.00 88.73 A C ANISOU 1920 CD ARG A 267 9297 14069 10349 -1291 1910 1008 A C ATOM 1921 NE ARG A 267 -6.718 0.094 -46.313 1.00 88.58 A N ANISOU 1921 NE ARG A 267 9076 14194 10384 -1150 1919 780 A N ATOM 1922 CZ ARG A 267 -6.824 -1.184 -46.661 1.00 86.16 A C ANISOU 1922 CZ ARG A 267 8712 14018 10006 -928 1920 598 A C ATOM 1923 NH1 ARG A 267 -7.703 -1.551 -47.585 1.00 85.10 A N1+ ANISOU 1923 NH1 ARG A 267 8695 13899 9741 -837 1913 612 A N1+ ATOM 1924 NH2 ARG A 267 -6.053 -2.096 -46.084 1.00 84.29 A N ANISOU 1924 NH2 ARG A 267 8308 13892 9827 -793 1919 399 A N ATOM 1925 N ASP A 268 -7.466 6.438 -45.746 1.00 85.78 A N ANISOU 1925 N ASP A 268 9438 12921 10233 -2147 1833 1753 A N ATOM 1926 CA ASP A 268 -6.339 7.336 -45.518 1.00 88.35 A C ANISOU 1926 CA ASP A 268 9696 13290 10583 -2447 1893 1842 A C ATOM 1927 C ASP A 268 -6.604 8.274 -44.344 1.00 88.71 A C ANISOU 1927 C ASP A 268 9917 12964 10825 -2529 1779 1892 A C ATOM 1928 O ASP A 268 -5.824 9.189 -44.084 1.00 91.96 A O ANISOU 1928 O ASP A 268 10332 13337 11272 -2800 1803 1984 A O ATOM 1929 CB ASP A 268 -6.036 8.146 -46.780 1.00 90.78 A C ANISOU 1929 CB ASP A 268 10060 13733 10699 -2686 1998 2066 A C ATOM 1930 N LEU A 269 -7.704 8.037 -43.633 1.00 85.59 A N ANISOU 1930 N LEU A 269 9665 12304 10550 -2300 1656 1824 A N ATOM 1931 CA LEU A 269 -8.094 8.892 -42.516 1.00 84.18 A C ANISOU 1931 CA LEU A 269 9671 11768 10548 -2336 1544 1856 A C ATOM 1932 C LEU A 269 -7.851 8.222 -41.164 1.00 80.67 A C ANISOU 1932 C LEU A 269 9101 11284 10265 -2216 1479 1642 A C ATOM 1933 O LEU A 269 -7.959 8.863 -40.119 1.00 83.26 A O ANISOU 1933 O LEU A 269 9542 11356 10737 -2260 1394 1635 A O ATOM 1934 CB LEU A 269 -9.565 9.293 -42.644 1.00 83.94 A C ANISOU 1934 CB LEU A 269 9908 11456 10529 -2173 1448 1954 A C ATOM 1935 N VAL A 270 -7.536 6.930 -41.184 1.00 74.93 A N ANISOU 1935 N VAL A 270 8159 10805 9508 -2055 1514 1466 A N ATOM 1936 CA VAL A 270 -7.207 6.199 -39.961 1.00 67.75 A C ANISOU 1936 CA VAL A 270 7120 9890 8733 -1937 1455 1267 A C ATOM 1937 C VAL A 270 -5.947 5.364 -40.167 1.00 67.93 A C ANISOU 1937 C VAL A 270 6845 10271 8693 -1958 1545 1139 A C ATOM 1938 O VAL A 270 -5.442 5.255 -41.284 1.00 68.38 A O ANISOU 1938 O VAL A 270 6794 10590 8598 -2036 1657 1189 A O ATOM 1939 CB VAL A 270 -8.353 5.268 -39.511 1.00 60.29 A C ANISOU 1939 CB VAL A 270 6245 8821 7841 -1638 1367 1149 A C ATOM 1940 CG1 VAL A 270 -9.646 6.046 -39.335 1.00 57.75 A C ANISOU 1940 CG1 VAL A 270 6190 8183 7569 -1588 1281 1265 A C ATOM 1941 CG2 VAL A 270 -8.538 4.137 -40.507 1.00 58.91 A C ANISOU 1941 CG2 VAL A 270 5972 8883 7529 -1479 1425 1083 A C ATOM 1942 N SER A 271 -5.448 4.765 -39.091 1.00 66.89 A N ANISOU 1942 N SER A 271 6581 10163 8673 -1874 1494 971 A N ATOM 1943 CA SER A 271 -4.249 3.938 -39.169 1.00 67.36 A C ANISOU 1943 CA SER A 271 6348 10560 8684 -1855 1562 833 A C ATOM 1944 C SER A 271 -4.538 2.587 -39.813 1.00 70.28 A C ANISOU 1944 C SER A 271 6641 11105 8959 -1593 1593 710 A C ATOM 1945 O SER A 271 -5.696 2.188 -39.955 1.00 70.29 A O ANISOU 1945 O SER A 271 6806 10943 8957 -1421 1539 708 A O ATOM 1946 CB SER A 271 -3.650 3.732 -37.779 1.00 63.69 A C ANISOU 1946 CB SER A 271 5778 10055 8364 -1832 1481 696 A C ATOM 1947 OG SER A 271 -4.535 3.006 -36.950 1.00 60.52 A O ANISOU 1947 OG SER A 271 5486 9452 8058 -1584 1372 589 A O ATOM 1948 N LYS A 272 -3.477 1.888 -40.202 1.00 73.28 A N ANISOU 1948 N LYS A 272 6766 11822 9255 -1564 1676 601 A N ATOM 1949 CA LYS A 272 -3.602 0.554 -40.775 1.00 73.78 A C ANISOU 1949 CA LYS A 272 6749 12057 9225 -1308 1703 457 A C ATOM 1950 C LYS A 272 -4.250 -0.383 -39.769 1.00 72.89 A C ANISOU 1950 C LYS A 272 6716 11743 9235 -1055 1575 311 A C ATOM 1951 O LYS A 272 -5.138 -1.167 -40.108 1.00 74.13 A O ANISOU 1951 O LYS A 272 6984 11827 9355 -865 1542 260 A O ATOM 1952 CB LYS A 272 -2.233 0.016 -41.195 1.00 75.76 A C ANISOU 1952 CB LYS A 272 6698 12709 9379 -1306 1808 346 A C ATOM 1953 N GLU A 273 -3.799 -0.279 -38.525 1.00 70.65 A N ANISOU 1953 N GLU A 273 6380 11373 9092 -1071 1499 250 A N ATOM 1954 CA GLU A 273 -4.291 -1.116 -37.443 1.00 67.85 A C ANISOU 1954 CA GLU A 273 6092 10836 8852 -856 1377 121 A C ATOM 1955 C GLU A 273 -5.724 -0.743 -37.080 1.00 65.13 A C ANISOU 1955 C GLU A 273 6016 10152 8576 -833 1292 207 A C ATOM 1956 O GLU A 273 -6.558 -1.614 -36.850 1.00 64.19 A O ANISOU 1956 O GLU A 273 5997 9916 8477 -636 1226 131 A O ATOM 1957 CB GLU A 273 -3.370 -0.990 -36.228 1.00 69.94 A C ANISOU 1957 CB GLU A 273 6223 11121 9231 -901 1320 46 A C ATOM 1958 CG GLU A 273 -3.725 -1.892 -35.066 1.00 72.75 A C ANISOU 1958 CG GLU A 273 6633 11318 9691 -684 1194 -85 A C ATOM 1959 CD GLU A 273 -2.732 -1.775 -33.924 1.00 79.52 A C ANISOU 1959 CD GLU A 273 7342 12231 10641 -726 1136 -159 A C ATOM 1960 OE1 GLU A 273 -2.569 -0.660 -33.381 1.00 82.29 A O ANISOU 1960 OE1 GLU A 273 7723 12482 11060 -940 1116 -73 A O ATOM 1961 OE2 GLU A 273 -2.105 -2.799 -33.578 1.00 81.53 A O1- ANISOU 1961 OE2 GLU A 273 7454 12627 10895 -542 1104 -306 A O1- ATOM 1962 N GLY A 274 -6.008 0.554 -37.039 1.00 63.24 A N ANISOU 1962 N GLY A 274 5895 9761 8370 -1034 1294 365 A N ATOM 1963 CA GLY A 274 -7.356 1.029 -36.788 1.00 58.87 A C ANISOU 1963 CA GLY A 274 5587 8911 7870 -1006 1222 454 A C ATOM 1964 C GLY A 274 -8.326 0.558 -37.854 1.00 56.04 A C ANISOU 1964 C GLY A 274 5324 8568 7401 -891 1246 489 A C ATOM 1965 O GLY A 274 -9.456 0.172 -37.552 1.00 52.58 A O ANISOU 1965 O GLY A 274 5023 7958 6998 -750 1171 469 A O ATOM 1966 N PHE A 275 -7.879 0.583 -39.106 1.00 58.31 A N ANISOU 1966 N PHE A 275 5530 9080 7545 -958 1352 539 A N ATOM 1967 CA PHE A 275 -8.706 0.131 -40.218 1.00 56.77 A C ANISOU 1967 CA PHE A 275 5413 8935 7222 -860 1378 567 A C ATOM 1968 C PHE A 275 -9.063 -1.341 -40.070 1.00 55.47 A C ANISOU 1968 C PHE A 275 5223 8801 7051 -619 1331 390 A C ATOM 1969 O PHE A 275 -10.189 -1.742 -40.357 1.00 56.25 A O ANISOU 1969 O PHE A 275 5453 8800 7121 -510 1283 393 A O ATOM 1970 CB PHE A 275 -8.003 0.362 -41.556 1.00 60.22 A C ANISOU 1970 CB PHE A 275 5746 9645 7488 -978 1508 636 A C ATOM 1971 CG PHE A 275 -8.849 0.015 -42.749 1.00 63.33 A C ANISOU 1971 CG PHE A 275 6231 10098 7734 -895 1532 677 A C ATOM 1972 CD1 PHE A 275 -8.832 -1.266 -43.284 1.00 64.05 A C ANISOU 1972 CD1 PHE A 275 6246 10360 7731 -716 1552 523 A C ATOM 1973 CD2 PHE A 275 -9.669 0.967 -43.332 1.00 65.91 A C ANISOU 1973 CD2 PHE A 275 6729 10303 8010 -990 1526 866 A C ATOM 1974 CE1 PHE A 275 -9.615 -1.590 -44.377 1.00 64.63 A C ANISOU 1974 CE1 PHE A 275 6405 10491 7659 -650 1566 551 A C ATOM 1975 CE2 PHE A 275 -10.452 0.650 -44.430 1.00 67.41 A C ANISOU 1975 CE2 PHE A 275 6996 10563 8054 -913 1539 904 A C ATOM 1976 CZ PHE A 275 -10.425 -0.631 -44.951 1.00 66.12 A C ANISOU 1976 CZ PHE A 275 6748 10579 7794 -751 1559 743 A C ATOM 1977 N ARG A 276 -8.105 -2.149 -39.629 1.00 56.00 A N ANISOU 1977 N ARG A 276 5126 9006 7144 -538 1338 236 A N ATOM 1978 CA ARG A 276 -8.364 -3.568 -39.423 1.00 55.76 A C ANISOU 1978 CA ARG A 276 5094 8978 7115 -309 1283 65 A C ATOM 1979 C ARG A 276 -9.361 -3.782 -38.289 1.00 54.24 A C ANISOU 1979 C ARG A 276 5054 8502 7053 -225 1158 46 A C ATOM 1980 O ARG A 276 -10.202 -4.676 -38.356 1.00 54.57 A O ANISOU 1980 O ARG A 276 5190 8467 7076 -84 1103 -21 A O ATOM 1981 CB ARG A 276 -7.069 -4.323 -39.135 1.00 58.18 A C ANISOU 1981 CB ARG A 276 5196 9486 7423 -223 1309 -90 A C ATOM 1982 CG ARG A 276 -6.163 -4.466 -40.345 1.00 66.10 A C ANISOU 1982 CG ARG A 276 6032 10816 8269 -245 1437 -116 A C ATOM 1983 CD ARG A 276 -4.994 -5.388 -40.042 1.00 73.18 A C ANISOU 1983 CD ARG A 276 6725 11914 9164 -100 1449 -297 A C ATOM 1984 NE ARG A 276 -4.222 -4.932 -38.890 1.00 76.47 A N ANISOU 1984 NE ARG A 276 7034 12311 9710 -176 1409 -301 A N ATOM 1985 CZ ARG A 276 -3.213 -5.610 -38.358 1.00 79.01 A C ANISOU 1985 CZ ARG A 276 7178 12782 10060 -52 1391 -447 A C ATOM 1986 NH1 ARG A 276 -2.861 -6.780 -38.875 1.00 82.62 A N1+ ANISOU 1986 NH1 ARG A 276 7558 13403 10429 169 1412 -603 A N1+ ATOM 1987 NH2 ARG A 276 -2.559 -5.124 -37.308 1.00 76.39 A N ANISOU 1987 NH2 ARG A 276 6750 12434 9839 -139 1346 -442 A N ATOM 1988 N ARG A 277 -9.267 -2.956 -37.251 1.00 53.36 A N ANISOU 1988 N ARG A 277 4967 8242 7065 -323 1113 103 A N ATOM 1989 CA ARG A 277 -10.196 -3.048 -36.132 1.00 51.75 A C ANISOU 1989 CA ARG A 277 4900 7787 6975 -256 1004 91 A C ATOM 1990 C ARG A 277 -11.617 -2.736 -36.604 1.00 47.30 A C ANISOU 1990 C ARG A 277 4508 7087 6377 -249 981 192 A C ATOM 1991 O ARG A 277 -12.554 -3.485 -36.328 1.00 44.58 A O ANISOU 1991 O ARG A 277 4252 6643 6045 -128 914 140 A O ATOM 1992 CB ARG A 277 -9.789 -2.097 -34.999 1.00 52.55 A C ANISOU 1992 CB ARG A 277 4999 7769 7198 -374 968 133 A C ATOM 1993 CG ARG A 277 -8.362 -2.285 -34.475 1.00 54.10 A C ANISOU 1993 CG ARG A 277 5009 8117 7430 -400 980 41 A C ATOM 1994 CD ARG A 277 -8.168 -3.649 -33.844 1.00 49.62 A C ANISOU 1994 CD ARG A 277 4392 7572 6888 -200 916 -121 A C ATOM 1995 NE ARG A 277 -6.829 -3.836 -33.290 1.00 49.54 A N ANISOU 1995 NE ARG A 277 4197 7715 6911 -200 914 -210 A N ATOM 1996 CZ ARG A 277 -5.873 -4.562 -33.862 1.00 51.79 A C ANISOU 1996 CZ ARG A 277 4309 8245 7123 -116 966 -307 A C ATOM 1997 NH1 ARG A 277 -6.098 -5.177 -35.015 1.00 50.50 A N1+ ANISOU 1997 NH1 ARG A 277 4148 8192 6847 -31 1027 -332 A N1+ ATOM 1998 NH2 ARG A 277 -4.692 -4.679 -33.274 1.00 55.74 A N ANISOU 1998 NH2 ARG A 277 4629 8892 7659 -109 953 -387 A N ATOM 1999 N ALA A 278 -11.768 -1.634 -37.331 1.00 46.45 A N ANISOU 1999 N ALA A 278 4445 6983 6220 -382 1033 341 A N ATOM 2000 CA ALA A 278 -13.081 -1.199 -37.790 1.00 44.66 A C ANISOU 2000 CA ALA A 278 4373 6638 5958 -370 1005 450 A C ATOM 2001 C ALA A 278 -13.694 -2.168 -38.807 1.00 46.52 A C ANISOU 2001 C ALA A 278 4620 6987 6068 -261 1014 405 A C ATOM 2002 O ALA A 278 -14.917 -2.297 -38.885 1.00 45.91 A O ANISOU 2002 O ALA A 278 4652 6814 5979 -195 957 434 A O ATOM 2003 CB ALA A 278 -12.992 0.195 -38.379 1.00 43.75 A C ANISOU 2003 CB ALA A 278 4315 6501 5810 -532 1054 626 A C ATOM 2004 N ARG A 279 -12.854 -2.847 -39.583 1.00 47.67 A N ANISOU 2004 N ARG A 279 4649 7347 6115 -241 1084 327 A N ATOM 2005 CA ARG A 279 -13.367 -3.766 -40.591 1.00 47.69 A C ANISOU 2005 CA ARG A 279 4671 7460 5987 -143 1092 270 A C ATOM 2006 C ARG A 279 -14.000 -4.994 -39.945 1.00 45.36 A C ANISOU 2006 C ARG A 279 4427 7066 5743 7 1001 130 A C ATOM 2007 O ARG A 279 -15.031 -5.477 -40.410 1.00 43.76 A O ANISOU 2007 O ARG A 279 4311 6837 5478 63 959 123 A O ATOM 2008 CB ARG A 279 -12.269 -4.194 -41.566 1.00 49.58 A C ANISOU 2008 CB ARG A 279 4774 7965 6100 -145 1194 205 A C ATOM 2009 CG ARG A 279 -12.806 -4.994 -42.757 1.00 48.72 A C ANISOU 2009 CG ARG A 279 4702 7979 5831 -59 1208 153 A C ATOM 2010 CD ARG A 279 -11.777 -5.124 -43.865 1.00 48.56 A C ANISOU 2010 CD ARG A 279 4552 8242 5657 -83 1328 122 A C ATOM 2011 NE ARG A 279 -10.546 -5.726 -43.370 1.00 51.65 A N ANISOU 2011 NE ARG A 279 4788 8743 6091 -18 1360 -23 A N ATOM 2012 CZ ARG A 279 -9.411 -5.784 -44.053 1.00 54.01 A C ANISOU 2012 CZ ARG A 279 4926 9310 6284 -37 1471 -66 A C ATOM 2013 NH1 ARG A 279 -9.340 -5.278 -45.278 1.00 57.02 A N1+ ANISOU 2013 NH1 ARG A 279 5290 9874 6502 -134 1567 30 A N1+ ATOM 2014 NH2 ARG A 279 -8.346 -6.350 -43.507 1.00 54.45 A N ANISOU 2014 NH2 ARG A 279 4833 9465 6389 45 1485 -205 A N ATOM 2015 N HIS A 280 -13.396 -5.495 -38.870 1.00 46.99 A N ANISOU 2015 N HIS A 280 4582 7216 6055 61 965 25 A N ATOM 2016 CA HIS A 280 -14.001 -6.613 -38.150 1.00 43.39 A C ANISOU 2016 CA HIS A 280 4196 6638 5651 185 872 -88 A C ATOM 2017 C HIS A 280 -15.379 -6.252 -37.630 1.00 40.38 A C ANISOU 2017 C HIS A 280 3943 6076 5323 166 799 -6 A C ATOM 2018 O HIS A 280 -16.329 -7.020 -37.771 1.00 40.17 A O ANISOU 2018 O HIS A 280 3996 6005 5261 225 744 -47 A O ATOM 2019 CB HIS A 280 -13.166 -7.068 -36.957 1.00 41.61 A C ANISOU 2019 CB HIS A 280 3911 6365 5535 242 834 -188 A C ATOM 2020 CG HIS A 280 -13.987 -7.788 -35.930 1.00 37.66 A C ANISOU 2020 CG HIS A 280 3520 5679 5112 316 729 -240 A C ATOM 2021 CD2 HIS A 280 -14.604 -7.341 -34.811 1.00 35.02 A C ANISOU 2021 CD2 HIS A 280 3251 5175 4878 283 668 -186 A C ATOM 2022 ND1 HIS A 280 -14.331 -9.115 -36.056 1.00 38.16 A N ANISOU 2022 ND1 HIS A 280 3646 5719 5134 429 678 -353 A N ATOM 2023 CE1 HIS A 280 -15.099 -9.468 -35.040 1.00 37.65 A C ANISOU 2023 CE1 HIS A 280 3679 5484 5144 447 591 -358 A C ATOM 2024 NE2 HIS A 280 -15.277 -8.410 -34.271 1.00 39.32 A N ANISOU 2024 NE2 HIS A 280 3885 5616 5438 366 588 -261 A N ATOM 2025 N VAL A 281 -15.469 -5.093 -36.990 1.00 40.08 A N ANISOU 2025 N VAL A 281 3922 5936 5369 82 795 101 A N ATOM 2026 CA VAL A 281 -16.706 -4.668 -36.346 1.00 39.52 A C ANISOU 2026 CA VAL A 281 3958 5702 5358 83 729 169 A C ATOM 2027 C VAL A 281 -17.829 -4.557 -37.362 1.00 42.41 A C ANISOU 2027 C VAL A 281 4388 6104 5621 88 724 244 A C ATOM 2028 O VAL A 281 -18.886 -5.175 -37.213 1.00 43.60 A O ANISOU 2028 O VAL A 281 4596 6210 5761 142 662 214 A O ATOM 2029 CB VAL A 281 -16.529 -3.320 -35.630 1.00 34.80 A C ANISOU 2029 CB VAL A 281 3377 4993 4852 -2 733 268 A C ATOM 2030 CG1 VAL A 281 -17.863 -2.812 -35.111 1.00 34.18 A C ANISOU 2030 CG1 VAL A 281 3405 4769 4814 22 673 337 A C ATOM 2031 CG2 VAL A 281 -15.522 -3.458 -34.500 1.00 33.78 A C ANISOU 2031 CG2 VAL A 281 3185 4828 4824 -9 718 187 A C ATOM 2032 N VAL A 282 -17.577 -3.763 -38.396 1.00 43.26 A N ANISOU 2032 N VAL A 282 4483 6304 5648 21 788 346 A N ATOM 2033 CA VAL A 282 -18.524 -3.553 -39.479 1.00 43.64 A C ANISOU 2033 CA VAL A 282 4588 6412 5582 24 785 431 A C ATOM 2034 C VAL A 282 -18.969 -4.881 -40.088 1.00 42.98 A C ANISOU 2034 C VAL A 282 4504 6425 5403 97 759 318 A C ATOM 2035 O VAL A 282 -20.160 -5.122 -40.257 1.00 44.80 A O ANISOU 2035 O VAL A 282 4791 6634 5596 129 699 334 A O ATOM 2036 CB VAL A 282 -17.907 -2.649 -40.569 1.00 46.99 A C ANISOU 2036 CB VAL A 282 4993 6948 5912 -67 869 549 A C ATOM 2037 CG1 VAL A 282 -18.690 -2.743 -41.844 1.00 50.41 A C ANISOU 2037 CG1 VAL A 282 5468 7493 6192 -48 868 607 A C ATOM 2038 CG2 VAL A 282 -17.845 -1.207 -40.083 1.00 45.94 A C ANISOU 2038 CG2 VAL A 282 4915 6679 5862 -150 872 690 A C ATOM 2039 N GLY A 283 -18.008 -5.749 -40.390 1.00 41.23 A N ANISOU 2039 N GLY A 283 4218 6309 5140 125 799 197 A N ATOM 2040 CA GLY A 283 -18.310 -7.060 -40.930 1.00 40.18 A C ANISOU 2040 CA GLY A 283 4104 6244 4919 199 770 69 A C ATOM 2041 C GLY A 283 -19.052 -7.954 -39.956 1.00 44.51 A C ANISOU 2041 C GLY A 283 4716 6650 5548 251 675 -16 A C ATOM 2042 O GLY A 283 -19.929 -8.721 -40.356 1.00 49.04 A O ANISOU 2042 O GLY A 283 5348 7232 6053 273 621 -64 A O ATOM 2043 N GLU A 284 -18.710 -7.850 -38.673 1.00 42.95 A N ANISOU 2043 N GLU A 284 4508 6326 5486 258 651 -32 A N ATOM 2044 CA GLU A 284 -19.296 -8.708 -37.648 1.00 40.35 A C ANISOU 2044 CA GLU A 284 4240 5863 5229 297 566 -106 A C ATOM 2045 C GLU A 284 -20.743 -8.341 -37.371 1.00 38.79 A C ANISOU 2045 C GLU A 284 4099 5598 5041 263 510 -22 A C ATOM 2046 O GLU A 284 -21.587 -9.214 -37.164 1.00 40.99 A O ANISOU 2046 O GLU A 284 4434 5837 5305 271 445 -75 A O ATOM 2047 CB GLU A 284 -18.481 -8.633 -36.354 1.00 38.59 A C ANISOU 2047 CB GLU A 284 3986 5542 5133 314 557 -139 A C ATOM 2048 CG GLU A 284 -18.936 -9.581 -35.268 1.00 33.71 A C ANISOU 2048 CG GLU A 284 3437 4791 4578 353 472 -213 A C ATOM 2049 CD GLU A 284 -18.507 -11.015 -35.504 1.00 36.33 A C ANISOU 2049 CD GLU A 284 3807 5130 4866 432 441 -355 A C ATOM 2050 OE1 GLU A 284 -17.944 -11.323 -36.584 1.00 41.24 A O ANISOU 2050 OE1 GLU A 284 4396 5875 5399 469 487 -412 A O ATOM 2051 OE2 GLU A 284 -18.748 -11.845 -34.602 1.00 34.61 A O1- ANISOU 2051 OE2 GLU A 284 3663 4792 4697 460 369 -412 A O1- ATOM 2052 N ILE A 285 -21.026 -7.045 -37.364 1.00 39.22 A N ANISOU 2052 N ILE A 285 4140 5641 5119 225 535 109 A N ATOM 2053 CA ILE A 285 -22.395 -6.565 -37.218 1.00 39.63 A C ANISOU 2053 CA ILE A 285 4229 5660 5170 218 488 194 A C ATOM 2054 C ILE A 285 -23.276 -7.131 -38.335 1.00 41.65 A C ANISOU 2054 C ILE A 285 4501 6029 5294 217 460 187 A C ATOM 2055 O ILE A 285 -24.378 -7.623 -38.082 1.00 37.89 A O ANISOU 2055 O ILE A 285 4048 5544 4806 215 395 171 A O ATOM 2056 CB ILE A 285 -22.437 -5.023 -37.219 1.00 39.92 A C ANISOU 2056 CB ILE A 285 4266 5664 5239 198 519 335 A C ATOM 2057 CG1 ILE A 285 -21.795 -4.493 -35.931 1.00 39.42 A C ANISOU 2057 CG1 ILE A 285 4198 5469 5309 189 525 330 A C ATOM 2058 CG2 ILE A 285 -23.865 -4.513 -37.356 1.00 39.15 A C ANISOU 2058 CG2 ILE A 285 4197 5569 5110 223 471 423 A C ATOM 2059 CD1 ILE A 285 -21.555 -2.996 -35.913 1.00 39.76 A C ANISOU 2059 CD1 ILE A 285 4263 5452 5392 155 557 451 A C ATOM 2060 N ARG A 286 -22.764 -7.083 -39.564 1.00 44.57 A N ANISOU 2060 N ARG A 286 4855 6521 5557 210 509 195 A N ATOM 2061 CA ARG A 286 -23.457 -7.644 -40.723 1.00 47.00 A C ANISOU 2061 CA ARG A 286 5182 6955 5723 208 483 175 A C ATOM 2062 C ARG A 286 -23.695 -9.141 -40.552 1.00 43.33 A C ANISOU 2062 C ARG A 286 4756 6470 5240 216 426 24 A C ATOM 2063 O ARG A 286 -24.820 -9.623 -40.704 1.00 41.85 A O ANISOU 2063 O ARG A 286 4596 6304 5003 192 357 12 A O ATOM 2064 CB ARG A 286 -22.656 -7.375 -42.003 1.00 51.18 A C ANISOU 2064 CB ARG A 286 5688 7627 6133 199 558 197 A C ATOM 2065 CG ARG A 286 -23.102 -8.168 -43.232 1.00 54.76 A C ANISOU 2065 CG ARG A 286 6163 8221 6421 203 537 135 A C ATOM 2066 CD ARG A 286 -24.370 -7.603 -43.859 1.00 58.08 A C ANISOU 2066 CD ARG A 286 6599 8713 6757 186 487 249 A C ATOM 2067 NE ARG A 286 -24.240 -6.188 -44.200 1.00 60.78 A N ANISOU 2067 NE ARG A 286 6931 9075 7087 176 532 421 A N ATOM 2068 CZ ARG A 286 -23.771 -5.731 -45.357 1.00 63.64 A C ANISOU 2068 CZ ARG A 286 7291 9568 7320 156 591 489 A C ATOM 2069 NH1 ARG A 286 -23.378 -6.574 -46.302 1.00 64.66 A N1+ ANISOU 2069 NH1 ARG A 286 7415 9839 7314 155 618 387 A N1+ ATOM 2070 NH2 ARG A 286 -23.695 -4.425 -45.570 1.00 66.15 A N ANISOU 2070 NH2 ARG A 286 7626 9873 7637 135 623 659 A N ATOM 2071 N ARG A 287 -22.632 -9.870 -40.222 1.00 41.16 A N ANISOU 2071 N ARG A 287 4485 6151 5003 249 448 -90 A N ATOM 2072 CA ARG A 287 -22.719 -11.318 -40.055 1.00 38.99 A C ANISOU 2072 CA ARG A 287 4276 5824 4713 268 390 -238 A C ATOM 2073 C ARG A 287 -23.699 -11.734 -38.960 1.00 40.06 A C ANISOU 2073 C ARG A 287 4460 5834 4926 229 308 -237 A C ATOM 2074 O ARG A 287 -24.312 -12.795 -39.047 1.00 41.63 A O ANISOU 2074 O ARG A 287 4731 6008 5080 200 241 -317 A O ATOM 2075 CB ARG A 287 -21.341 -11.905 -39.760 1.00 37.60 A C ANISOU 2075 CB ARG A 287 4093 5614 4579 340 424 -350 A C ATOM 2076 CG ARG A 287 -20.418 -11.928 -40.961 1.00 40.10 A C ANISOU 2076 CG ARG A 287 4364 6087 4784 383 500 -399 A C ATOM 2077 CD ARG A 287 -19.133 -12.665 -40.647 1.00 42.01 A C ANISOU 2077 CD ARG A 287 4590 6312 5061 478 523 -532 A C ATOM 2078 NE ARG A 287 -18.380 -11.997 -39.595 1.00 45.35 A N ANISOU 2078 NE ARG A 287 4941 6675 5616 482 550 -481 A N ATOM 2079 CZ ARG A 287 -17.389 -11.139 -39.806 1.00 47.23 A C ANISOU 2079 CZ ARG A 287 5067 7021 5859 473 639 -431 A C ATOM 2080 NH1 ARG A 287 -17.010 -10.848 -41.044 1.00 46.18 A N1+ ANISOU 2080 NH1 ARG A 287 4879 7067 5600 463 717 -419 A N1+ ATOM 2081 NH2 ARG A 287 -16.767 -10.580 -38.772 1.00 47.53 A N ANISOU 2081 NH2 ARG A 287 5047 6994 6019 462 647 -394 A N ATOM 2082 N THR A 288 -23.862 -10.903 -37.937 1.00 41.32 A N ANISOU 2082 N THR A 288 4586 5921 5193 220 313 -148 A N ATOM 2083 CA THR A 288 -24.773 -11.244 -36.849 1.00 38.12 A C ANISOU 2083 CA THR A 288 4213 5421 4850 181 248 -143 A C ATOM 2084 C THR A 288 -26.225 -11.090 -37.278 1.00 39.97 A C ANISOU 2084 C THR A 288 4433 5742 5013 126 204 -82 A C ATOM 2085 O THR A 288 -27.080 -11.877 -36.872 1.00 41.59 A O ANISOU 2085 O THR A 288 4672 5922 5206 66 140 -118 A O ATOM 2086 CB THR A 288 -24.498 -10.389 -35.602 1.00 36.32 A C ANISOU 2086 CB THR A 288 3953 5101 4747 199 269 -79 A C ATOM 2087 CG2 THR A 288 -25.390 -10.818 -34.441 1.00 33.36 A C ANISOU 2087 CG2 THR A 288 3608 4647 4420 159 210 -82 A C ATOM 2088 OG1 THR A 288 -23.129 -10.556 -35.224 1.00 36.54 A O ANISOU 2088 OG1 THR A 288 3978 5072 4834 246 301 -140 A O ATOM 2089 N ALA A 289 -26.504 -10.084 -38.104 1.00 39.44 A N ANISOU 2089 N ALA A 289 4313 5783 4890 141 235 14 A N ATOM 2090 CA ALA A 289 -27.830 -9.942 -38.701 1.00 38.23 A C ANISOU 2090 CA ALA A 289 4132 5746 4649 107 187 69 A C ATOM 2091 C ALA A 289 -28.119 -11.107 -39.649 1.00 39.66 A C ANISOU 2091 C ALA A 289 4357 6004 4709 57 141 -29 A C ATOM 2092 O ALA A 289 -29.227 -11.650 -39.656 1.00 41.90 A O ANISOU 2092 O ALA A 289 4639 6337 4945 -12 71 -45 A O ATOM 2093 CB ALA A 289 -27.954 -8.617 -39.434 1.00 34.47 A C ANISOU 2093 CB ALA A 289 3609 5358 4132 153 223 197 A C ATOM 2094 N GLN A 290 -27.122 -11.485 -40.446 1.00 39.98 A N ANISOU 2094 N GLN A 290 4433 6064 4694 86 179 -101 A N ATOM 2095 CA GLN A 290 -27.251 -12.635 -41.346 1.00 39.94 A C ANISOU 2095 CA GLN A 290 4492 6114 4570 52 137 -219 A C ATOM 2096 C GLN A 290 -27.424 -13.927 -40.545 1.00 40.31 A C ANISOU 2096 C GLN A 290 4628 6025 4665 2 70 -333 A C ATOM 2097 O GLN A 290 -28.247 -14.778 -40.893 1.00 41.01 A O ANISOU 2097 O GLN A 290 4768 6138 4676 -81 -4 -393 A O ATOM 2098 CB GLN A 290 -26.030 -12.755 -42.268 1.00 41.20 A C ANISOU 2098 CB GLN A 290 4666 6326 4661 117 204 -285 A C ATOM 2099 CG GLN A 290 -25.858 -11.621 -43.271 1.00 43.90 A C ANISOU 2099 CG GLN A 290 4942 6818 4918 142 268 -173 A C ATOM 2100 CD GLN A 290 -24.492 -11.637 -43.945 1.00 51.41 A C ANISOU 2100 CD GLN A 290 5885 7828 5819 199 356 -227 A C ATOM 2101 NE2 GLN A 290 -24.406 -11.032 -45.122 1.00 51.30 A N ANISOU 2101 NE2 GLN A 290 5842 7976 5675 199 401 -162 A N ATOM 2102 OE1 GLN A 290 -23.525 -12.179 -43.407 1.00 56.17 A O ANISOU 2102 OE1 GLN A 290 6503 8348 6493 245 382 -324 A O ATOM 2103 N ALA A 291 -26.654 -14.065 -39.465 1.00 33.94 A N ANISOU 2103 N ALA A 291 3845 5072 3979 42 91 -357 A N ATOM 2104 CA ALA A 291 -26.703 -15.275 -38.652 1.00 33.19 A C ANISOU 2104 CA ALA A 291 3856 4827 3930 3 26 -451 A C ATOM 2105 C ALA A 291 -28.082 -15.444 -38.027 1.00 36.52 A C ANISOU 2105 C ALA A 291 4273 5245 4357 -118 -40 -399 A C ATOM 2106 O ALA A 291 -28.660 -16.532 -38.073 1.00 38.97 A O ANISOU 2106 O ALA A 291 4674 5513 4620 -213 -115 -471 A O ATOM 2107 CB ALA A 291 -25.624 -15.247 -37.577 1.00 31.90 A C ANISOU 2107 CB ALA A 291 3706 4527 3890 80 58 -467 A C ATOM 2108 N ALA A 292 -28.607 -14.360 -37.458 1.00 39.42 A N ANISOU 2108 N ALA A 292 4536 5663 4778 -117 -13 -277 A N ATOM 2109 CA ALA A 292 -29.959 -14.347 -36.900 1.00 42.62 A C ANISOU 2109 CA ALA A 292 4896 6118 5179 -217 -62 -219 A C ATOM 2110 C ALA A 292 -30.989 -14.792 -37.942 1.00 43.27 A C ANISOU 2110 C ALA A 292 4967 6343 5131 -310 -123 -239 A C ATOM 2111 O ALA A 292 -31.841 -15.627 -37.656 1.00 47.61 A O ANISOU 2111 O ALA A 292 5549 6892 5650 -440 -191 -271 A O ATOM 2112 CB ALA A 292 -30.309 -12.955 -36.368 1.00 29.96 A C ANISOU 2112 CB ALA A 292 3175 4575 3635 -158 -17 -93 A C ATOM 2113 N ALA A 293 -30.909 -14.236 -39.147 1.00 37.78 A N ANISOU 2113 N ALA A 293 4226 5777 4351 -256 -101 -217 A N ATOM 2114 CA ALA A 293 -31.824 -14.636 -40.211 1.00 45.37 A C ANISOU 2114 CA ALA A 293 5175 6889 5174 -338 -165 -242 A C ATOM 2115 C ALA A 293 -31.634 -16.112 -40.544 1.00 46.88 A C ANISOU 2115 C ALA A 293 5509 6994 5309 -424 -224 -391 A C ATOM 2116 O ALA A 293 -32.607 -16.857 -40.678 1.00 52.57 A O ANISOU 2116 O ALA A 293 6251 7760 5963 -564 -306 -429 A O ATOM 2117 CB ALA A 293 -31.624 -13.778 -41.454 1.00 34.20 A C ANISOU 2117 CB ALA A 293 3706 5621 3669 -253 -129 -189 A C ATOM 2118 N ALA A 294 -30.378 -16.534 -40.665 1.00 45.09 A N ANISOU 2118 N ALA A 294 5381 6644 5107 -339 -187 -480 A N ATOM 2119 CA ALA A 294 -30.073 -17.923 -40.984 1.00 44.58 A C ANISOU 2119 CA ALA A 294 5477 6470 4992 -383 -244 -635 A C ATOM 2120 C ALA A 294 -30.616 -18.856 -39.908 1.00 50.48 A C ANISOU 2120 C ALA A 294 6317 7065 5799 -511 -317 -661 A C ATOM 2121 O ALA A 294 -31.090 -19.954 -40.205 1.00 52.98 A O ANISOU 2121 O ALA A 294 6752 7331 6046 -630 -401 -755 A O ATOM 2122 CB ALA A 294 -28.573 -18.115 -41.149 1.00 39.14 A C ANISOU 2122 CB ALA A 294 4855 5685 4332 -235 -184 -720 A C ATOM 2123 N LEU A 295 -30.552 -18.406 -38.657 1.00 52.19 A N ANISOU 2123 N LEU A 295 6487 7208 6136 -495 -286 -576 A N ATOM 2124 CA LEU A 295 -31.010 -19.206 -37.529 1.00 54.49 A C ANISOU 2124 CA LEU A 295 6862 7361 6480 -616 -343 -580 A C ATOM 2125 C LEU A 295 -32.528 -19.385 -37.535 1.00 56.66 A C ANISOU 2125 C LEU A 295 7078 7764 6688 -808 -406 -534 A C ATOM 2126 O LEU A 295 -33.031 -20.465 -37.227 1.00 63.69 A O ANISOU 2126 O LEU A 295 8084 8562 7552 -968 -483 -583 A O ATOM 2127 CB LEU A 295 -30.559 -18.570 -36.212 1.00 55.03 A C ANISOU 2127 CB LEU A 295 6882 7350 6678 -544 -288 -498 A C ATOM 2128 CG LEU A 295 -30.694 -19.420 -34.948 1.00 57.51 A C ANISOU 2128 CG LEU A 295 7309 7493 7049 -638 -336 -502 A C ATOM 2129 CD1 LEU A 295 -29.919 -20.722 -35.084 1.00 56.88 A C ANISOU 2129 CD1 LEU A 295 7443 7208 6961 -622 -394 -630 A C ATOM 2130 CD2 LEU A 295 -30.215 -18.640 -33.734 1.00 58.86 A C ANISOU 2130 CD2 LEU A 295 7414 7617 7332 -549 -277 -422 A C ATOM 2131 N ARG A 296 -33.250 -18.327 -37.892 1.00 51.92 A N ANISOU 2131 N ARG A 296 6298 7377 6054 -793 -378 -439 A N ATOM 2132 CA ARG A 296 -34.707 -18.363 -37.911 1.00 51.55 A C ANISOU 2132 CA ARG A 296 6148 7500 5938 -954 -433 -391 A C ATOM 2133 C ARG A 296 -35.237 -19.426 -38.874 1.00 60.03 A C ANISOU 2133 C ARG A 296 7312 8610 6889 -1108 -527 -491 A C ATOM 2134 O ARG A 296 -36.063 -20.258 -38.496 1.00 63.17 A O ANISOU 2134 O ARG A 296 7749 8997 7255 -1309 -598 -510 A O ATOM 2135 CB ARG A 296 -35.271 -16.992 -38.293 1.00 50.78 A C ANISOU 2135 CB ARG A 296 5848 7628 5818 -861 -392 -280 A C ATOM 2136 CG ARG A 296 -34.969 -15.881 -37.305 1.00 54.85 A C ANISOU 2136 CG ARG A 296 6275 8117 6448 -730 -312 -180 A C ATOM 2137 CD ARG A 296 -35.570 -14.556 -37.765 1.00 59.02 A C ANISOU 2137 CD ARG A 296 6632 8847 6946 -627 -286 -75 A C ATOM 2138 NE ARG A 296 -35.353 -13.482 -36.794 1.00 59.92 A N ANISOU 2138 NE ARG A 296 6679 8923 7167 -505 -218 11 A N ATOM 2139 CZ ARG A 296 -34.510 -12.468 -36.974 1.00 57.37 A C ANISOU 2139 CZ ARG A 296 6353 8548 6894 -346 -154 58 A C ATOM 2140 NH1 ARG A 296 -33.804 -12.379 -38.095 1.00 56.36 A N1+ ANISOU 2140 NH1 ARG A 296 6275 8422 6716 -291 -140 36 A N1+ ATOM 2141 NH2 ARG A 296 -34.379 -11.538 -36.039 1.00 54.42 A N ANISOU 2141 NH2 ARG A 296 5933 8129 6616 -252 -103 125 A N ATOM 2142 N ARG A 297 -34.755 -19.394 -40.116 1.00 61.36 A N ANISOU 2142 N ARG A 297 7514 8824 6978 -1025 -526 -557 A N ATOM 2143 CA ARG A 297 -35.204 -20.329 -41.146 1.00 58.73 A C ANISOU 2143 CA ARG A 297 7270 8534 6512 -1155 -616 -668 A C ATOM 2144 C ARG A 297 -34.474 -21.671 -41.055 1.00 59.63 A C ANISOU 2144 C ARG A 297 7633 8389 6635 -1193 -662 -813 A C ATOM 2145 O ARG A 297 -34.482 -22.458 -42.002 1.00 62.88 A O ANISOU 2145 O ARG A 297 8164 8788 6941 -1249 -726 -937 A O ATOM 2146 CB ARG A 297 -35.016 -19.720 -42.539 1.00 55.71 A C ANISOU 2146 CB ARG A 297 6823 8324 6018 -1044 -597 -679 A C ATOM 2147 CG ARG A 297 -33.566 -19.532 -42.928 1.00 54.48 A C ANISOU 2147 CG ARG A 297 6747 8064 5888 -849 -517 -732 A C ATOM 2148 CD ARG A 297 -33.388 -18.946 -44.320 1.00 52.74 A C ANISOU 2148 CD ARG A 297 6469 8029 5540 -757 -492 -734 A C ATOM 2149 NE ARG A 297 -31.993 -19.063 -44.733 1.00 53.09 A N ANISOU 2149 NE ARG A 297 6607 7979 5587 -604 -423 -818 A N ATOM 2150 CZ ARG A 297 -31.067 -18.127 -44.538 1.00 51.88 A C ANISOU 2150 CZ ARG A 297 6385 7821 5507 -449 -317 -742 A C ATOM 2151 NH1 ARG A 297 -31.385 -16.978 -43.953 1.00 49.64 A N1+ ANISOU 2151 NH1 ARG A 297 5961 7597 5302 -419 -274 -583 A N1+ ATOM 2152 NH2 ARG A 297 -29.818 -18.336 -44.937 1.00 49.93 A N ANISOU 2152 NH2 ARG A 297 6208 7515 5249 -325 -256 -830 A N ATOM 2153 N GLY A 298 -33.842 -21.922 -39.911 1.00 59.29 A N ANISOU 2153 N GLY A 298 7674 8138 6714 -1153 -634 -801 A N ATOM 2154 CA GLY A 298 -33.234 -23.210 -39.620 1.00 59.45 A C ANISOU 2154 CA GLY A 298 7942 7891 6756 -1184 -690 -922 A C ATOM 2155 C GLY A 298 -32.019 -23.567 -40.456 1.00 60.56 A C ANISOU 2155 C GLY A 298 8209 7934 6865 -1005 -672 -1059 A C ATOM 2156 O GLY A 298 -31.657 -24.738 -40.566 1.00 64.59 A O ANISOU 2156 O GLY A 298 8942 8246 7354 -1027 -741 -1191 A O ATOM 2157 N ASP A 299 -31.378 -22.559 -41.038 1.00 56.21 A N ANISOU 2157 N ASP A 299 7524 7523 6309 -825 -580 -1028 A N ATOM 2158 CA ASP A 299 -30.244 -22.785 -41.925 1.00 50.99 A C ANISOU 2158 CA ASP A 299 6942 6831 5599 -652 -546 -1153 A C ATOM 2159 C ASP A 299 -28.932 -22.872 -41.143 1.00 47.00 A C ANISOU 2159 C ASP A 299 6498 6148 5212 -477 -493 -1179 A C ATOM 2160 O ASP A 299 -28.172 -21.905 -41.070 1.00 44.97 A O ANISOU 2160 O ASP A 299 6108 5971 5007 -330 -394 -1114 A O ATOM 2161 CB ASP A 299 -30.166 -21.674 -42.974 1.00 48.28 A C ANISOU 2161 CB ASP A 299 6428 6741 5176 -562 -471 -1099 A C ATOM 2162 CG ASP A 299 -29.249 -22.021 -44.122 1.00 49.99 A C ANISOU 2162 CG ASP A 299 6721 6982 5289 -429 -444 -1241 A C ATOM 2163 OD1 ASP A 299 -28.587 -23.078 -44.056 1.00 51.71 A O ANISOU 2163 OD1 ASP A 299 7119 7016 5512 -375 -480 -1389 A O ATOM 2164 OD2 ASP A 299 -29.178 -21.231 -45.086 1.00 51.09 A O1- ANISOU 2164 OD2 ASP A 299 6745 7330 5337 -371 -388 -1203 A O1- ATOM 2165 N TYR A 300 -28.666 -24.050 -40.590 1.00 48.32 A N ANISOU 2165 N TYR A 300 6872 6073 5414 -497 -566 -1274 A N ATOM 2166 CA TYR A 300 -27.521 -24.275 -39.710 1.00 51.84 A C ANISOU 2166 CA TYR A 300 7390 6336 5972 -338 -541 -1297 A C ATOM 2167 C TYR A 300 -26.174 -24.246 -40.430 1.00 50.55 A C ANISOU 2167 C TYR A 300 7226 6197 5782 -102 -477 -1412 A C ATOM 2168 O TYR A 300 -25.156 -23.866 -39.844 1.00 50.23 A O ANISOU 2168 O TYR A 300 7127 6125 5832 56 -416 -1390 A O ATOM 2169 CB TYR A 300 -27.681 -25.614 -38.987 1.00 58.28 A C ANISOU 2169 CB TYR A 300 8454 6874 6815 -426 -653 -1364 A C ATOM 2170 CG TYR A 300 -28.946 -25.713 -38.164 1.00 65.66 A C ANISOU 2170 CG TYR A 300 9387 7788 7771 -675 -709 -1247 A C ATOM 2171 CD1 TYR A 300 -29.530 -24.577 -37.614 1.00 66.33 A C ANISOU 2171 CD1 TYR A 300 9250 8048 7904 -732 -644 -1084 A C ATOM 2172 CD2 TYR A 300 -29.556 -26.942 -37.936 1.00 70.75 A C ANISOU 2172 CD2 TYR A 300 10256 8243 8383 -856 -827 -1301 A C ATOM 2173 CE1 TYR A 300 -30.688 -24.660 -36.860 1.00 69.24 A C ANISOU 2173 CE1 TYR A 300 9595 8431 8281 -950 -686 -984 A C ATOM 2174 CE2 TYR A 300 -30.714 -27.036 -37.180 1.00 73.17 A C ANISOU 2174 CE2 TYR A 300 10544 8558 8698 -1103 -870 -1189 A C ATOM 2175 CZ TYR A 300 -31.275 -25.891 -36.645 1.00 72.32 A C ANISOU 2175 CZ TYR A 300 10189 8656 8631 -1143 -794 -1033 A C ATOM 2176 OH TYR A 300 -32.424 -25.975 -35.891 1.00 72.11 A O ANISOU 2176 OH TYR A 300 10124 8672 8603 -1379 -827 -928 A O ATOM 2177 N ARG A 301 -26.164 -24.661 -41.691 1.00 50.49 A N ANISOU 2177 N ARG A 301 7278 6263 5643 -81 -493 -1538 A N ATOM 2178 CA ARG A 301 -24.928 -24.681 -42.460 1.00 50.59 A C ANISOU 2178 CA ARG A 301 7282 6333 5606 141 -426 -1660 A C ATOM 2179 C ARG A 301 -24.446 -23.258 -42.717 1.00 48.18 A C ANISOU 2179 C ARG A 301 6728 6265 5314 223 -293 -1542 A C ATOM 2180 O ARG A 301 -23.256 -22.964 -42.593 1.00 48.58 A O ANISOU 2180 O ARG A 301 6711 6339 5409 399 -216 -1566 A O ATOM 2181 CB ARG A 301 -25.116 -25.441 -43.779 1.00 50.73 A C ANISOU 2181 CB ARG A 301 7424 6390 5459 134 -473 -1828 A C ATOM 2182 CG ARG A 301 -25.205 -26.951 -43.604 1.00 54.94 A C ANISOU 2182 CG ARG A 301 8248 6648 5979 109 -601 -1986 A C ATOM 2183 CD ARG A 301 -25.332 -27.677 -44.942 1.00 59.22 A C ANISOU 2183 CD ARG A 301 8923 7229 6351 115 -647 -2173 A C ATOM 2184 N ALA A 302 -25.376 -22.373 -43.061 1.00 45.72 A N ANISOU 2184 N ALA A 302 6281 6128 4963 93 -272 -1413 A N ATOM 2185 CA ALA A 302 -25.035 -20.977 -43.289 1.00 44.92 A C ANISOU 2185 CA ALA A 302 5970 6226 4872 150 -158 -1282 A C ATOM 2186 C ALA A 302 -24.599 -20.323 -41.975 1.00 46.35 A C ANISOU 2186 C ALA A 302 6066 6324 5219 188 -116 -1167 A C ATOM 2187 O ALA A 302 -23.617 -19.578 -41.939 1.00 48.39 A O ANISOU 2187 O ALA A 302 6212 6655 5518 304 -22 -1131 A O ATOM 2188 CB ALA A 302 -26.213 -20.229 -43.910 1.00 41.11 A C ANISOU 2188 CB ALA A 302 5385 5927 4308 15 -166 -1168 A C ATOM 2189 N PHE A 303 -25.321 -20.619 -40.898 1.00 45.80 A N ANISOU 2189 N PHE A 303 6052 6112 5236 80 -185 -1112 A N ATOM 2190 CA PHE A 303 -24.973 -20.089 -39.583 1.00 44.80 A C ANISOU 2190 CA PHE A 303 5864 5900 5256 109 -156 -1013 A C ATOM 2191 C PHE A 303 -23.540 -20.483 -39.216 1.00 46.33 A C ANISOU 2191 C PHE A 303 6101 5992 5510 284 -129 -1106 A C ATOM 2192 O PHE A 303 -22.757 -19.657 -38.738 1.00 42.33 A O ANISOU 2192 O PHE A 303 5473 5527 5083 367 -57 -1042 A O ATOM 2193 CB PHE A 303 -25.958 -20.587 -38.518 1.00 45.48 A C ANISOU 2193 CB PHE A 303 6032 5849 5400 -38 -240 -964 A C ATOM 2194 CG PHE A 303 -25.898 -19.812 -37.230 1.00 46.25 A C ANISOU 2194 CG PHE A 303 6038 5912 5623 -36 -205 -839 A C ATOM 2195 CD1 PHE A 303 -24.935 -20.094 -36.276 1.00 46.77 A C ANISOU 2195 CD1 PHE A 303 6157 5830 5785 65 -205 -865 A C ATOM 2196 CD2 PHE A 303 -26.799 -18.793 -36.981 1.00 45.67 A C ANISOU 2196 CD2 PHE A 303 5828 5961 5565 -121 -177 -702 A C ATOM 2197 CE1 PHE A 303 -24.872 -19.373 -35.101 1.00 44.52 A C ANISOU 2197 CE1 PHE A 303 5792 5521 5604 65 -177 -759 A C ATOM 2198 CE2 PHE A 303 -26.746 -18.071 -35.808 1.00 43.51 A C ANISOU 2198 CE2 PHE A 303 5480 5655 5398 -109 -146 -602 A C ATOM 2199 CZ PHE A 303 -25.780 -18.362 -34.866 1.00 44.43 A C ANISOU 2199 CZ PHE A 303 5653 5624 5603 -25 -145 -631 A C ATOM 2200 N GLY A 304 -23.198 -21.745 -39.470 1.00 47.72 A N ANISOU 2200 N GLY A 304 6450 6039 5644 342 -194 -1261 A N ATOM 2201 CA GLY A 304 -21.877 -22.257 -39.157 1.00 47.63 A C ANISOU 2201 CA GLY A 304 6488 5932 5678 533 -185 -1366 A C ATOM 2202 C GLY A 304 -20.788 -21.544 -39.930 1.00 49.87 A C ANISOU 2202 C GLY A 304 6612 6414 5923 680 -71 -1394 A C ATOM 2203 O GLY A 304 -19.763 -21.159 -39.361 1.00 52.05 A O ANISOU 2203 O GLY A 304 6795 6704 6279 797 -21 -1380 A O ATOM 2204 N ARG A 305 -21.017 -21.368 -41.230 1.00 46.75 A N ANISOU 2204 N ARG A 305 6181 6186 5396 661 -32 -1431 A N ATOM 2205 CA ARG A 305 -20.070 -20.682 -42.100 1.00 44.13 A C ANISOU 2205 CA ARG A 305 5698 6072 4998 771 84 -1448 A C ATOM 2206 C ARG A 305 -19.837 -19.255 -41.623 1.00 40.54 A C ANISOU 2206 C ARG A 305 5050 5726 4627 732 173 -1273 A C ATOM 2207 O ARG A 305 -18.708 -18.764 -41.635 1.00 39.80 A O ANISOU 2207 O ARG A 305 4833 5734 4555 835 258 -1276 A O ATOM 2208 CB ARG A 305 -20.570 -20.682 -43.553 1.00 41.79 A C ANISOU 2208 CB ARG A 305 5408 5942 4530 724 103 -1492 A C ATOM 2209 N LEU A 306 -20.916 -18.598 -41.209 1.00 41.77 A N ANISOU 2209 N LEU A 306 5180 5865 4826 582 149 -1126 A N ATOM 2210 CA LEU A 306 -20.843 -17.247 -40.664 1.00 43.55 A C ANISOU 2210 CA LEU A 306 5256 6154 5137 540 216 -961 A C ATOM 2211 C LEU A 306 -20.054 -17.226 -39.348 1.00 46.75 A C ANISOU 2211 C LEU A 306 5642 6435 5688 606 213 -954 A C ATOM 2212 O LEU A 306 -19.415 -16.223 -39.020 1.00 47.16 A O ANISOU 2212 O LEU A 306 5563 6554 5801 621 284 -870 A O ATOM 2213 CB LEU A 306 -22.255 -16.673 -40.470 1.00 42.80 A C ANISOU 2213 CB LEU A 306 5152 6060 5050 391 177 -826 A C ATOM 2214 CG LEU A 306 -23.031 -16.445 -41.782 1.00 43.97 A C ANISOU 2214 CG LEU A 306 5286 6369 5052 327 182 -804 A C ATOM 2215 CD1 LEU A 306 -24.528 -16.251 -41.551 1.00 43.57 A C ANISOU 2215 CD1 LEU A 306 5243 6312 4999 193 113 -711 A C ATOM 2216 CD2 LEU A 306 -22.469 -15.265 -42.557 1.00 41.74 A C ANISOU 2216 CD2 LEU A 306 4874 6267 4718 358 287 -715 A C ATOM 2217 N MET A 307 -20.083 -18.332 -38.605 1.00 44.28 A N ANISOU 2217 N MET A 307 5466 5938 5422 638 124 -1039 A N ATOM 2218 CA MET A 307 -19.285 -18.432 -37.382 1.00 43.93 A C ANISOU 2218 CA MET A 307 5415 5779 5498 718 108 -1043 A C ATOM 2219 C MET A 307 -17.801 -18.502 -37.711 1.00 43.45 A C ANISOU 2219 C MET A 307 5272 5811 5427 887 168 -1140 A C ATOM 2220 O MET A 307 -16.975 -17.938 -36.985 1.00 37.72 A O ANISOU 2220 O MET A 307 4438 5107 4788 936 203 -1101 A O ATOM 2221 CB MET A 307 -19.680 -19.657 -36.550 1.00 43.02 A C ANISOU 2221 CB MET A 307 5489 5438 5420 713 -9 -1103 A C ATOM 2222 CG MET A 307 -21.044 -19.566 -35.897 1.00 41.53 A C ANISOU 2222 CG MET A 307 5357 5165 5259 537 -64 -996 A C ATOM 2223 SD MET A 307 -21.555 -21.174 -35.281 1.00 40.88 A S ANISOU 2223 SD MET A 307 5528 4831 5175 497 -200 -1076 A S ATOM 2224 CE MET A 307 -20.450 -21.368 -33.883 1.00 53.90 A C ANISOU 2224 CE MET A 307 7197 6340 6941 633 -226 -1078 A C ATOM 2225 N VAL A 308 -17.475 -19.200 -38.803 1.00 42.60 A N ANISOU 2225 N VAL A 308 5208 5771 5206 976 179 -1274 A N ATOM 2226 CA VAL A 308 -16.091 -19.376 -39.228 1.00 41.70 A C ANISOU 2226 CA VAL A 308 5006 5778 5060 1153 240 -1388 A C ATOM 2227 C VAL A 308 -15.522 -18.052 -39.728 1.00 46.27 A C ANISOU 2227 C VAL A 308 5368 6594 5618 1115 369 -1293 A C ATOM 2228 O VAL A 308 -14.356 -17.740 -39.477 1.00 52.06 A O ANISOU 2228 O VAL A 308 5966 7426 6389 1207 426 -1313 A O ATOM 2229 CB VAL A 308 -15.958 -20.453 -40.332 1.00 47.10 A C ANISOU 2229 CB VAL A 308 5801 6486 5609 1263 222 -1567 A C ATOM 2230 CG1 VAL A 308 -14.510 -20.611 -40.754 1.00 41.27 A C ANISOU 2230 CG1 VAL A 308 4948 5904 4829 1466 294 -1692 A C ATOM 2231 CG2 VAL A 308 -16.505 -21.789 -39.848 1.00 46.22 A C ANISOU 2231 CG2 VAL A 308 5935 6110 5517 1286 85 -1661 A C ATOM 2232 N GLU A 309 -16.345 -17.269 -40.424 1.00 43.60 A N ANISOU 2232 N GLU A 309 4999 6350 5218 974 411 -1183 A N ATOM 2233 CA GLU A 309 -15.921 -15.946 -40.877 1.00 45.17 A C ANISOU 2233 CA GLU A 309 5023 6743 5396 911 525 -1066 A C ATOM 2234 C GLU A 309 -15.687 -15.017 -39.686 1.00 43.15 A C ANISOU 2234 C GLU A 309 4683 6424 5287 852 532 -941 A C ATOM 2235 O GLU A 309 -14.762 -14.200 -39.691 1.00 40.92 A O ANISOU 2235 O GLU A 309 4253 6270 5025 849 615 -895 A O ATOM 2236 CB GLU A 309 -16.951 -15.327 -41.829 1.00 50.28 A C ANISOU 2236 CB GLU A 309 5683 7479 5944 784 547 -964 A C ATOM 2237 CG GLU A 309 -17.217 -16.123 -43.102 1.00 57.14 A C ANISOU 2237 CG GLU A 309 6627 8437 6646 823 542 -1082 A C ATOM 2238 CD GLU A 309 -18.272 -15.471 -43.991 1.00 65.27 A C ANISOU 2238 CD GLU A 309 7662 9565 7573 696 551 -969 A C ATOM 2239 OE1 GLU A 309 -18.414 -14.226 -43.949 1.00 66.82 A O ANISOU 2239 OE1 GLU A 309 7766 9824 7797 609 603 -802 A O ATOM 2240 OE2 GLU A 309 -18.960 -16.204 -44.737 1.00 68.36 A O1- ANISOU 2240 OE2 GLU A 309 8157 9965 7851 687 499 -1051 A O1- ATOM 2241 N SER A 310 -16.532 -15.150 -38.668 1.00 42.64 A N ANISOU 2241 N SER A 310 4714 6170 5317 796 446 -890 A N ATOM 2242 CA SER A 310 -16.397 -14.362 -37.450 1.00 41.83 A C ANISOU 2242 CA SER A 310 4556 5991 5349 747 440 -789 A C ATOM 2243 C SER A 310 -15.036 -14.610 -36.800 1.00 41.45 A C ANISOU 2243 C SER A 310 4430 5954 5364 863 448 -867 A C ATOM 2244 O SER A 310 -14.340 -13.671 -36.411 1.00 39.98 A O ANISOU 2244 O SER A 310 4115 5838 5237 831 501 -801 A O ATOM 2245 CB SER A 310 -17.529 -14.692 -36.473 1.00 44.09 A C ANISOU 2245 CB SER A 310 4965 6085 5702 684 344 -747 A C ATOM 2246 OG SER A 310 -17.358 -14.023 -35.237 1.00 46.40 A O ANISOU 2246 OG SER A 310 5214 6302 6113 654 335 -669 A O ATOM 2247 N HIS A 311 -14.644 -15.875 -36.713 1.00 42.02 A N ANISOU 2247 N HIS A 311 4583 5961 5420 1001 390 -1012 A N ATOM 2248 CA HIS A 311 -13.382 -16.217 -36.077 1.00 42.64 A C ANISOU 2248 CA HIS A 311 4591 6056 5555 1140 380 -1095 A C ATOM 2249 C HIS A 311 -12.179 -15.725 -36.879 1.00 44.75 A C ANISOU 2249 C HIS A 311 4665 6574 5763 1195 491 -1133 A C ATOM 2250 O HIS A 311 -11.236 -15.171 -36.316 1.00 47.21 A O ANISOU 2250 O HIS A 311 4832 6968 6139 1209 522 -1113 A O ATOM 2251 CB HIS A 311 -13.266 -17.721 -35.863 1.00 43.36 A C ANISOU 2251 CB HIS A 311 4837 6006 5634 1298 283 -1242 A C ATOM 2252 CG HIS A 311 -12.027 -18.114 -35.122 1.00 44.30 A C ANISOU 2252 CG HIS A 311 4890 6132 5811 1465 253 -1324 A C ATOM 2253 CD2 HIS A 311 -10.844 -18.606 -35.558 1.00 43.55 A C ANISOU 2253 CD2 HIS A 311 4705 6171 5670 1654 280 -1460 A C ATOM 2254 ND1 HIS A 311 -11.902 -17.967 -33.756 1.00 44.97 A N ANISOU 2254 ND1 HIS A 311 4981 6097 6007 1455 189 -1267 A N ATOM 2255 CE1 HIS A 311 -10.700 -18.368 -33.381 1.00 46.97 A C ANISOU 2255 CE1 HIS A 311 5157 6407 6284 1629 168 -1359 A C ATOM 2256 NE2 HIS A 311 -10.038 -18.761 -34.456 1.00 45.99 A N ANISOU 2256 NE2 HIS A 311 4966 6439 6068 1758 224 -1479 A N ATOM 2257 N ARG A 312 -12.211 -15.944 -38.190 1.00 46.43 A N ANISOU 2257 N ARG A 312 4873 6923 5846 1219 551 -1190 A N ATOM 2258 CA ARG A 312 -11.144 -15.479 -39.068 1.00 45.67 A C ANISOU 2258 CA ARG A 312 4590 7096 5668 1254 670 -1220 A C ATOM 2259 C ARG A 312 -10.962 -13.971 -38.916 1.00 41.41 A C ANISOU 2259 C ARG A 312 3905 6655 5172 1081 750 -1052 A C ATOM 2260 O ARG A 312 -9.844 -13.483 -38.786 1.00 39.09 A O ANISOU 2260 O ARG A 312 3437 6520 4897 1090 814 -1053 A O ATOM 2261 CB ARG A 312 -11.447 -15.843 -40.529 1.00 47.75 A C ANISOU 2261 CB ARG A 312 4892 7485 5765 1274 722 -1285 A C ATOM 2262 N SER A 313 -12.077 -13.248 -38.918 1.00 36.84 A N ANISOU 2262 N SER A 313 3405 5981 4611 925 739 -910 A N ATOM 2263 CA SER A 313 -12.085 -11.811 -38.684 1.00 40.00 A C ANISOU 2263 CA SER A 313 3721 6413 5064 762 793 -744 A C ATOM 2264 C SER A 313 -11.478 -11.456 -37.313 1.00 42.06 A C ANISOU 2264 C SER A 313 3920 6592 5469 755 756 -725 A C ATOM 2265 O SER A 313 -10.622 -10.573 -37.216 1.00 45.08 A O ANISOU 2265 O SER A 313 4159 7094 5877 682 821 -671 A O ATOM 2266 CB SER A 313 -13.518 -11.282 -38.798 1.00 38.23 A C ANISOU 2266 CB SER A 313 3620 6067 4838 643 761 -616 A C ATOM 2267 OG SER A 313 -13.586 -9.883 -38.583 1.00 41.69 A O ANISOU 2267 OG SER A 313 4006 6506 5326 502 803 -457 A O ATOM 2268 N LEU A 314 -11.909 -12.157 -36.266 1.00 40.10 A N ANISOU 2268 N LEU A 314 3783 6148 5304 819 649 -768 A N ATOM 2269 CA LEU A 314 -11.374 -11.946 -34.914 1.00 43.29 A C ANISOU 2269 CA LEU A 314 4145 6471 5832 827 599 -761 A C ATOM 2270 C LEU A 314 -9.884 -12.261 -34.826 1.00 47.58 A C ANISOU 2270 C LEU A 314 4529 7174 6375 941 624 -867 A C ATOM 2271 O LEU A 314 -9.171 -11.707 -33.986 1.00 45.76 A O ANISOU 2271 O LEU A 314 4194 6968 6224 908 617 -842 A O ATOM 2272 CB LEU A 314 -12.131 -12.802 -33.891 1.00 38.56 A C ANISOU 2272 CB LEU A 314 3709 5645 5295 884 479 -792 A C ATOM 2273 CG LEU A 314 -13.541 -12.345 -33.520 1.00 35.79 A C ANISOU 2273 CG LEU A 314 3481 5142 4977 761 444 -678 A C ATOM 2274 CD1 LEU A 314 -14.306 -13.478 -32.871 1.00 36.02 A C ANISOU 2274 CD1 LEU A 314 3675 4990 5021 816 339 -729 A C ATOM 2275 CD2 LEU A 314 -13.491 -11.141 -32.598 1.00 36.02 A C ANISOU 2275 CD2 LEU A 314 3455 5132 5099 656 452 -572 A C ATOM 2276 N ARG A 315 -9.422 -13.155 -35.696 1.00 49.87 A N ANISOU 2276 N ARG A 315 4796 7583 6569 1081 650 -992 A N ATOM 2277 CA ARG A 315 -8.042 -13.625 -35.655 1.00 48.20 A C ANISOU 2277 CA ARG A 315 4430 7541 6345 1234 667 -1116 A C ATOM 2278 C ARG A 315 -7.106 -12.737 -36.471 1.00 49.85 A C ANISOU 2278 C ARG A 315 4414 8038 6487 1151 801 -1085 A C ATOM 2279 O ARG A 315 -5.953 -12.522 -36.097 1.00 49.86 A O ANISOU 2279 O ARG A 315 4231 8198 6517 1182 824 -1121 A O ATOM 2280 CB ARG A 315 -7.965 -15.066 -36.166 1.00 45.89 A C ANISOU 2280 CB ARG A 315 4229 7232 5976 1452 626 -1283 A C ATOM 2281 CG ARG A 315 -6.589 -15.712 -36.052 1.00 48.09 A C ANISOU 2281 CG ARG A 315 4361 7670 6240 1664 624 -1432 A C ATOM 2282 CD ARG A 315 -6.542 -16.972 -36.892 1.00 52.65 A C ANISOU 2282 CD ARG A 315 5032 8260 6711 1873 611 -1600 A C ATOM 2283 NE ARG A 315 -6.884 -16.665 -38.278 1.00 57.39 A N ANISOU 2283 NE ARG A 315 5615 9010 7182 1791 719 -1588 A N ATOM 2284 CZ ARG A 315 -7.293 -17.556 -39.175 1.00 58.70 A C ANISOU 2284 CZ ARG A 315 5914 9150 7238 1896 712 -1700 A C ATOM 2285 NH1 ARG A 315 -7.421 -18.834 -38.846 1.00 62.55 A N1+ ANISOU 2285 NH1 ARG A 315 6579 9449 7739 2084 599 -1834 A N1+ ATOM 2286 NH2 ARG A 315 -7.579 -17.163 -40.405 1.00 55.53 A N ANISOU 2286 NH2 ARG A 315 5483 8907 6710 1806 812 -1676 A N ATOM 2287 N ASP A 316 -7.608 -12.217 -37.584 1.00 50.51 A N ANISOU 2287 N ASP A 316 4513 8203 6475 1037 887 -1012 A N ATOM 2288 CA ASP A 316 -6.757 -11.513 -38.533 1.00 51.40 A C ANISOU 2288 CA ASP A 316 4432 8605 6493 958 1022 -984 A C ATOM 2289 C ASP A 316 -6.901 -9.989 -38.489 1.00 51.42 A C ANISOU 2289 C ASP A 316 4389 8618 6530 705 1081 -794 A C ATOM 2290 O ASP A 316 -5.922 -9.273 -38.688 1.00 51.99 A O ANISOU 2290 O ASP A 316 4274 8898 6581 608 1167 -758 A O ATOM 2291 CB ASP A 316 -7.036 -12.028 -39.946 1.00 53.02 A C ANISOU 2291 CB ASP A 316 4676 8935 6533 1019 1088 -1045 A C ATOM 2292 CG ASP A 316 -6.665 -13.493 -40.111 1.00 56.52 A C ANISOU 2292 CG ASP A 316 5150 9399 6925 1280 1044 -1254 A C ATOM 2293 OD1 ASP A 316 -5.857 -13.998 -39.303 1.00 55.87 A O ANISOU 2293 OD1 ASP A 316 4992 9321 6915 1422 993 -1351 A O ATOM 2294 OD2 ASP A 316 -7.179 -14.141 -41.045 1.00 58.80 A O1- ANISOU 2294 OD2 ASP A 316 5546 9696 7099 1350 1052 -1325 A O1- ATOM 2295 N ASP A 317 -8.109 -9.496 -38.220 1.00 52.77 A N ANISOU 2295 N ASP A 317 4731 8567 6753 599 1031 -674 A N ATOM 2296 CA ASP A 317 -8.374 -8.055 -38.243 1.00 51.89 A C ANISOU 2296 CA ASP A 317 4618 8428 6669 379 1075 -493 A C ATOM 2297 C ASP A 317 -8.442 -7.420 -36.841 1.00 50.16 A C ANISOU 2297 C ASP A 317 4426 8024 6606 302 1001 -433 A C ATOM 2298 O ASP A 317 -7.860 -6.360 -36.608 1.00 51.73 A O ANISOU 2298 O ASP A 317 4536 8273 6845 149 1042 -347 A O ATOM 2299 CB ASP A 317 -9.674 -7.767 -39.013 1.00 47.32 A C ANISOU 2299 CB ASP A 317 4199 7756 6024 317 1077 -391 A C ATOM 2300 CG ASP A 317 -9.470 -7.703 -40.528 1.00 49.86 A C ANISOU 2300 CG ASP A 317 4467 8305 6174 290 1185 -376 A C ATOM 2301 OD1 ASP A 317 -8.323 -7.508 -40.979 1.00 50.77 A O ANISOU 2301 OD1 ASP A 317 4409 8654 6226 261 1280 -399 A O ATOM 2302 OD2 ASP A 317 -10.468 -7.830 -41.271 1.00 51.73 A O1- ANISOU 2302 OD2 ASP A 317 4826 8500 6328 292 1175 -338 A O1- ATOM 2303 N TYR A 318 -9.145 -8.055 -35.908 1.00 46.58 A N ANISOU 2303 N TYR A 318 4102 7360 6235 397 891 -478 A N ATOM 2304 CA TYR A 318 -9.235 -7.505 -34.555 1.00 43.37 A C ANISOU 2304 CA TYR A 318 3727 6789 5961 337 820 -433 A C ATOM 2305 C TYR A 318 -8.109 -8.055 -33.675 1.00 46.53 A C ANISOU 2305 C TYR A 318 4007 7254 6420 435 776 -548 A C ATOM 2306 O TYR A 318 -7.768 -7.471 -32.644 1.00 48.88 A O ANISOU 2306 O TYR A 318 4270 7491 6810 366 736 -520 A O ATOM 2307 CB TYR A 318 -10.584 -7.828 -33.923 1.00 40.74 A C ANISOU 2307 CB TYR A 318 3585 6215 5677 373 729 -410 A C ATOM 2308 CG TYR A 318 -11.196 -6.666 -33.168 1.00 42.96 A C ANISOU 2308 CG TYR A 318 3938 6342 6044 242 705 -289 A C ATOM 2309 CD1 TYR A 318 -11.455 -5.466 -33.815 1.00 42.80 A C ANISOU 2309 CD1 TYR A 318 3927 6337 5997 100 768 -159 A C ATOM 2310 CD2 TYR A 318 -11.507 -6.763 -31.811 1.00 42.62 A C ANISOU 2310 CD2 TYR A 318 3961 6135 6097 268 616 -306 A C ATOM 2311 CE1 TYR A 318 -12.015 -4.399 -33.148 1.00 45.62 A C ANISOU 2311 CE1 TYR A 318 4366 6539 6429 3 741 -58 A C ATOM 2312 CE2 TYR A 318 -12.066 -5.687 -31.129 1.00 44.74 A C ANISOU 2312 CE2 TYR A 318 4297 6268 6433 164 597 -210 A C ATOM 2313 CZ TYR A 318 -12.313 -4.512 -31.803 1.00 47.35 A C ANISOU 2313 CZ TYR A 318 4642 6605 6743 39 657 -93 A C ATOM 2314 OH TYR A 318 -12.870 -3.451 -31.130 1.00 50.82 A O ANISOU 2314 OH TYR A 318 5167 6894 7249 -41 632 -9 A O ATOM 2315 N GLU A 319 -7.547 -9.189 -34.092 1.00 46.87 A N ANISOU 2315 N GLU A 319 3990 7417 6401 607 778 -682 A N ATOM 2316 CA GLU A 319 -6.397 -9.812 -33.438 1.00 47.34 A C ANISOU 2316 CA GLU A 319 3917 7576 6493 740 738 -802 A C ATOM 2317 C GLU A 319 -6.588 -10.028 -31.939 1.00 47.41 A C ANISOU 2317 C GLU A 319 4009 7388 6616 782 614 -812 A C ATOM 2318 O GLU A 319 -5.786 -9.563 -31.132 1.00 45.06 A O ANISOU 2318 O GLU A 319 3593 7147 6382 740 591 -814 A O ATOM 2319 CB GLU A 319 -5.145 -8.973 -33.682 1.00 48.95 A C ANISOU 2319 CB GLU A 319 3882 8034 6682 631 825 -784 A C ATOM 2320 CG GLU A 319 -4.709 -8.929 -35.137 1.00 51.34 A C ANISOU 2320 CG GLU A 319 4068 8588 6850 615 954 -795 A C ATOM 2321 CD GLU A 319 -3.556 -7.978 -35.363 1.00 54.08 A C ANISOU 2321 CD GLU A 319 4182 9189 7177 455 1048 -751 A C ATOM 2322 OE1 GLU A 319 -3.796 -6.754 -35.369 1.00 56.94 A O ANISOU 2322 OE1 GLU A 319 4568 9500 7567 223 1085 -604 A O ATOM 2323 OE2 GLU A 319 -2.413 -8.449 -35.532 1.00 56.25 A O1- ANISOU 2323 OE2 GLU A 319 4250 9717 7407 560 1083 -863 A O1- ATOM 2324 N VAL A 320 -7.650 -10.742 -31.578 1.00 46.66 A N ANISOU 2324 N VAL A 320 4115 7076 6537 854 535 -820 A N ATOM 2325 CA VAL A 320 -7.935 -11.041 -30.182 1.00 45.54 A C ANISOU 2325 CA VAL A 320 4072 6747 6483 894 420 -824 A C ATOM 2326 C VAL A 320 -8.049 -12.543 -29.967 1.00 47.59 A C ANISOU 2326 C VAL A 320 4447 6912 6724 1098 331 -934 A C ATOM 2327 O VAL A 320 -8.646 -12.998 -28.998 1.00 47.04 A O ANISOU 2327 O VAL A 320 4523 6650 6700 1127 235 -923 A O ATOM 2328 CB VAL A 320 -9.224 -10.360 -29.709 1.00 44.69 A C ANISOU 2328 CB VAL A 320 4118 6443 6421 754 399 -705 A C ATOM 2329 CG1 VAL A 320 -9.074 -8.851 -29.786 1.00 45.19 A C ANISOU 2329 CG1 VAL A 320 4097 6560 6513 565 467 -599 A C ATOM 2330 CG2 VAL A 320 -10.415 -10.831 -30.545 1.00 43.92 A C ANISOU 2330 CG2 VAL A 320 4165 6264 6258 761 412 -685 A C ATOM 2331 N SER A 321 -7.468 -13.313 -30.877 1.00 49.46 A N ANISOU 2331 N SER A 321 4627 7282 6884 1240 364 -1040 A N ATOM 2332 CA SER A 321 -7.409 -14.755 -30.706 1.00 47.43 A C ANISOU 2332 CA SER A 321 4485 6929 6606 1455 274 -1159 A C ATOM 2333 C SER A 321 -6.049 -15.137 -30.126 1.00 49.46 A C ANISOU 2333 C SER A 321 4594 7312 6888 1623 229 -1256 A C ATOM 2334 O SER A 321 -5.281 -14.271 -29.696 1.00 51.34 A O ANISOU 2334 O SER A 321 4649 7691 7167 1543 256 -1222 A O ATOM 2335 CB SER A 321 -7.660 -15.468 -32.035 1.00 46.49 A C ANISOU 2335 CB SER A 321 4423 6858 6381 1538 322 -1237 A C ATOM 2336 OG SER A 321 -7.854 -16.856 -31.836 1.00 46.90 A O ANISOU 2336 OG SER A 321 4651 6751 6419 1721 221 -1341 A O ATOM 2337 N CYS A 322 -5.757 -16.431 -30.106 1.00 47.84 A N ANISOU 2337 N CYS A 322 4471 7051 6653 1855 153 -1379 A N ATOM 2338 CA CYS A 322 -4.465 -16.916 -29.647 1.00 51.38 A C ANISOU 2338 CA CYS A 322 4779 7632 7111 2060 101 -1485 A C ATOM 2339 C CYS A 322 -4.258 -18.322 -30.204 1.00 55.94 A C ANISOU 2339 C CYS A 322 5463 8170 7622 2327 54 -1636 A C ATOM 2340 O CYS A 322 -5.230 -18.969 -30.591 1.00 58.11 A O ANISOU 2340 O CYS A 322 5967 8249 7865 2327 27 -1642 A O ATOM 2341 CB CYS A 322 -4.388 -16.893 -28.111 1.00 49.43 A C ANISOU 2341 CB CYS A 322 4580 7249 6953 2062 -21 -1438 A C ATOM 2342 SG CYS A 322 -5.529 -17.997 -27.251 1.00 57.98 A S ANISOU 2342 SG CYS A 322 6013 7958 8059 2121 -168 -1413 A S ATOM 2343 N PRO A 323 -2.996 -18.794 -30.263 1.00 57.67 A N ANISOU 2343 N PRO A 323 5544 8561 7806 2517 39 -1736 A N ATOM 2344 CA PRO A 323 -2.711 -20.121 -30.826 1.00 57.15 A C ANISOU 2344 CA PRO A 323 5620 8436 7659 2730 -8 -1850 A C ATOM 2345 C PRO A 323 -3.548 -21.238 -30.208 1.00 58.07 A C ANISOU 2345 C PRO A 323 6058 8205 7802 2831 -151 -1865 A C ATOM 2346 O PRO A 323 -3.838 -22.219 -30.890 1.00 61.82 A O ANISOU 2346 O PRO A 323 6710 8569 8211 2942 -175 -1948 A O ATOM 2347 CB PRO A 323 -1.226 -20.324 -30.509 1.00 57.88 A C ANISOU 2347 CB PRO A 323 5543 8718 7730 2855 -35 -1893 A C ATOM 2348 CG PRO A 323 -0.671 -18.950 -30.436 1.00 58.56 A C ANISOU 2348 CG PRO A 323 5346 9058 7845 2668 63 -1819 A C ATOM 2349 CD PRO A 323 -1.760 -18.108 -29.837 1.00 58.95 A C ANISOU 2349 CD PRO A 323 5451 8962 7985 2477 62 -1712 A C ATOM 2350 N GLU A 324 -3.935 -21.091 -28.945 1.00 56.87 A N ANISOU 2350 N GLU A 324 5986 7883 7737 2781 -247 -1784 A N ATOM 2351 CA GLU A 324 -4.783 -22.086 -28.298 1.00 57.07 A C ANISOU 2351 CA GLU A 324 6327 7573 7783 2837 -381 -1774 A C ATOM 2352 C GLU A 324 -6.169 -22.136 -28.940 1.00 57.51 A C ANISOU 2352 C GLU A 324 6566 7465 7821 2700 -347 -1750 A C ATOM 2353 O GLU A 324 -6.615 -23.196 -29.383 1.00 60.23 A O ANISOU 2353 O GLU A 324 7135 7632 8118 2798 -402 -1826 A O ATOM 2354 CB GLU A 324 -4.909 -21.805 -26.799 1.00 53.65 A C ANISOU 2354 CB GLU A 324 5929 7020 7434 2784 -480 -1676 A C ATOM 2355 CG GLU A 324 -3.658 -22.139 -25.996 1.00 55.94 A C ANISOU 2355 CG GLU A 324 6134 7399 7722 2924 -561 -1690 A C ATOM 2356 CD GLU A 324 -2.609 -21.043 -26.056 1.00 58.52 A C ANISOU 2356 CD GLU A 324 6122 8052 8062 2867 -472 -1687 A C ATOM 2357 OE1 GLU A 324 -2.948 -19.908 -26.456 1.00 57.20 A O ANISOU 2357 OE1 GLU A 324 5802 8008 7923 2689 -360 -1645 A O ATOM 2358 OE2 GLU A 324 -1.442 -21.316 -25.701 1.00 62.49 A O1- ANISOU 2358 OE2 GLU A 324 6513 8688 8543 2991 -517 -1725 A O1- ATOM 2359 N LEU A 325 -6.840 -20.987 -28.990 1.00 52.25 A N ANISOU 2359 N LEU A 325 5821 6852 7179 2429 -258 -1620 A N ATOM 2360 CA LEU A 325 -8.172 -20.899 -29.578 1.00 48.23 A C ANISOU 2360 CA LEU A 325 5465 6220 6640 2238 -219 -1555 A C ATOM 2361 C LEU A 325 -8.160 -21.320 -31.040 1.00 48.41 A C ANISOU 2361 C LEU A 325 5493 6335 6565 2311 -149 -1666 A C ATOM 2362 O LEU A 325 -9.028 -22.070 -31.482 1.00 47.80 A O ANISOU 2362 O LEU A 325 5634 6086 6443 2293 -188 -1695 A O ATOM 2363 CB LEU A 325 -8.722 -19.480 -29.448 1.00 47.53 A C ANISOU 2363 CB LEU A 325 5255 6214 6589 1975 -129 -1407 A C ATOM 2364 CG LEU A 325 -9.026 -19.001 -28.029 1.00 45.80 A C ANISOU 2364 CG LEU A 325 5066 5881 6453 1866 -193 -1292 A C ATOM 2365 CD1 LEU A 325 -9.386 -17.514 -28.028 1.00 40.83 A C ANISOU 2365 CD1 LEU A 325 4297 5358 5857 1639 -96 -1171 A C ATOM 2366 CD2 LEU A 325 -10.145 -19.840 -27.419 1.00 45.29 A C ANISOU 2366 CD2 LEU A 325 5278 5540 6392 1824 -295 -1250 A C ATOM 2367 N ASP A 326 -7.168 -20.841 -31.783 1.00 49.14 A N ANISOU 2367 N ASP A 326 5344 6710 6617 2385 -46 -1731 A N ATOM 2368 CA ASP A 326 -7.043 -21.170 -33.197 1.00 51.62 A C ANISOU 2368 CA ASP A 326 5635 7156 6821 2464 34 -1843 A C ATOM 2369 C ASP A 326 -6.952 -22.675 -33.418 1.00 55.79 A C ANISOU 2369 C ASP A 326 6375 7522 7300 2710 -66 -2005 A C ATOM 2370 O ASP A 326 -7.610 -23.223 -34.304 1.00 58.51 A O ANISOU 2370 O ASP A 326 6876 7789 7566 2701 -60 -2066 A O ATOM 2371 CB ASP A 326 -5.817 -20.481 -33.803 1.00 52.40 A C ANISOU 2371 CB ASP A 326 5421 7611 6879 2523 157 -1891 A C ATOM 2372 CG ASP A 326 -5.930 -18.971 -33.791 1.00 52.02 A C ANISOU 2372 CG ASP A 326 5189 7713 6864 2259 262 -1733 A C ATOM 2373 OD1 ASP A 326 -7.064 -18.452 -33.862 1.00 47.21 A O ANISOU 2373 OD1 ASP A 326 4689 6981 6268 2047 277 -1611 A O ATOM 2374 OD2 ASP A 326 -4.879 -18.303 -33.713 1.00 56.69 A O1- ANISOU 2374 OD2 ASP A 326 5527 8547 7466 2265 327 -1733 A O1- ATOM 2375 N GLN A 327 -6.138 -23.340 -32.606 1.00 57.59 A N ANISOU 2375 N GLN A 327 6627 7689 7567 2899 -165 -2052 A N ATOM 2376 CA GLN A 327 -5.935 -24.777 -32.745 1.00 60.17 A C ANISOU 2376 CA GLN A 327 7178 7841 7841 3077 -270 -2149 A C ATOM 2377 C GLN A 327 -7.219 -25.519 -32.374 1.00 59.11 A C ANISOU 2377 C GLN A 327 7381 7349 7729 3014 -382 -2130 A C ATOM 2378 O GLN A 327 -7.575 -26.513 -33.011 1.00 59.56 A O ANISOU 2378 O GLN A 327 7652 7260 7719 3074 -428 -2218 A O ATOM 2379 CB GLN A 327 -4.742 -25.230 -31.893 1.00 63.71 A C ANISOU 2379 CB GLN A 327 7570 8320 8317 3236 -352 -2152 A C ATOM 2380 CG GLN A 327 -4.754 -26.681 -31.444 1.00 68.96 A C ANISOU 2380 CG GLN A 327 8524 8708 8971 3390 -507 -2197 A C ATOM 2381 CD GLN A 327 -3.513 -27.055 -30.637 1.00 74.09 A C ANISOU 2381 CD GLN A 327 9092 9425 9635 3562 -583 -2203 A C ATOM 2382 NE2 GLN A 327 -2.382 -27.191 -31.320 1.00 77.31 A N ANISOU 2382 NE2 GLN A 327 9322 10076 9977 3715 -531 -2301 A N ATOM 2383 OE1 GLN A 327 -3.574 -27.231 -29.422 1.00 74.87 A O ANISOU 2383 OE1 GLN A 327 9285 9368 9795 3559 -690 -2122 A O ATOM 2384 N LEU A 328 -7.936 -25.010 -31.375 1.00 56.64 A N ANISOU 2384 N LEU A 328 7114 6903 7505 2870 -424 -2011 A N ATOM 2385 CA LEU A 328 -9.237 -25.565 -31.015 1.00 54.58 A C ANISOU 2385 CA LEU A 328 7150 6336 7253 2708 -512 -1937 A C ATOM 2386 C LEU A 328 -10.248 -25.412 -32.150 1.00 51.75 A C ANISOU 2386 C LEU A 328 6846 5994 6822 2526 -438 -1936 A C ATOM 2387 O LEU A 328 -11.048 -26.312 -32.403 1.00 49.36 A O ANISOU 2387 O LEU A 328 6804 5470 6479 2490 -513 -1974 A O ATOM 2388 CB LEU A 328 -9.776 -24.900 -29.748 1.00 51.44 A C ANISOU 2388 CB LEU A 328 6745 5858 6940 2509 -542 -1756 A C ATOM 2389 CG LEU A 328 -9.132 -25.340 -28.435 1.00 55.28 A C ANISOU 2389 CG LEU A 328 7288 6229 7487 2656 -663 -1740 A C ATOM 2390 CD1 LEU A 328 -9.814 -24.672 -27.249 1.00 54.73 A C ANISOU 2390 CD1 LEU A 328 7228 6085 7481 2435 -684 -1564 A C ATOM 2391 CD2 LEU A 328 -9.183 -26.858 -28.315 1.00 56.06 A C ANISOU 2391 CD2 LEU A 328 7694 6055 7549 2809 -802 -1814 A C ATOM 2392 N VAL A 329 -10.210 -24.270 -32.828 1.00 49.98 A N ANISOU 2392 N VAL A 329 6382 6031 6577 2404 -297 -1887 A N ATOM 2393 CA VAL A 329 -11.129 -24.031 -33.933 1.00 52.01 A C ANISOU 2393 CA VAL A 329 6670 6336 6757 2238 -226 -1876 A C ATOM 2394 C VAL A 329 -10.813 -24.923 -35.133 1.00 52.34 A C ANISOU 2394 C VAL A 329 6793 6407 6686 2414 -221 -2064 A C ATOM 2395 O VAL A 329 -11.716 -25.541 -35.692 1.00 54.45 A O ANISOU 2395 O VAL A 329 7263 6534 6893 2337 -263 -2102 A O ATOM 2396 CB VAL A 329 -11.117 -22.554 -34.372 1.00 49.15 A C ANISOU 2396 CB VAL A 329 6043 6239 6393 2075 -82 -1767 A C ATOM 2397 CG1 VAL A 329 -11.896 -22.377 -35.679 1.00 48.72 A C ANISOU 2397 CG1 VAL A 329 6009 6268 6234 1954 -11 -1775 A C ATOM 2398 CG2 VAL A 329 -11.706 -21.686 -33.281 1.00 43.41 A C ANISOU 2398 CG2 VAL A 329 5282 5448 5764 1878 -92 -1588 A C ATOM 2399 N GLU A 330 -9.540 -25.000 -35.517 1.00 52.48 A N ANISOU 2399 N GLU A 330 6651 6619 6671 2650 -172 -2189 A N ATOM 2400 CA GLU A 330 -9.140 -25.821 -36.663 1.00 56.23 A C ANISOU 2400 CA GLU A 330 7186 7151 7027 2849 -156 -2387 A C ATOM 2401 C GLU A 330 -9.493 -27.292 -36.457 1.00 56.21 A C ANISOU 2401 C GLU A 330 7527 6818 7014 2960 -312 -2486 A C ATOM 2402 O GLU A 330 -9.966 -27.957 -37.376 1.00 56.59 A O ANISOU 2402 O GLU A 330 7740 6794 6966 2962 -327 -2588 A O ATOM 2403 CB GLU A 330 -7.638 -25.689 -36.942 1.00 59.29 A C ANISOU 2403 CB GLU A 330 7327 7816 7384 3042 -84 -2455 A C ATOM 2404 CG GLU A 330 -7.182 -24.281 -37.300 1.00 58.57 A C ANISOU 2404 CG GLU A 330 6900 8072 7284 2945 78 -2387 A C ATOM 2405 CD GLU A 330 -8.074 -23.623 -38.334 1.00 56.60 A C ANISOU 2405 CD GLU A 330 6633 7921 6951 2732 179 -2333 A C ATOM 2406 N ALA A 331 -9.263 -27.793 -35.248 1.00 57.86 A N ANISOU 2406 N ALA A 331 7843 6828 7314 3007 -428 -2419 A N ATOM 2407 CA ALA A 331 -9.597 -29.174 -34.919 1.00 60.07 A C ANISOU 2407 CA ALA A 331 8453 6781 7589 3051 -579 -2450 A C ATOM 2408 C ALA A 331 -11.098 -29.417 -35.034 1.00 59.36 A C ANISOU 2408 C ALA A 331 8619 6448 7485 2843 -636 -2432 A C ATOM 2409 O ALA A 331 -11.533 -30.456 -35.539 1.00 62.12 A O ANISOU 2409 O ALA A 331 9218 6613 7773 2839 -709 -2510 A O ATOM 2410 CB ALA A 331 -9.115 -29.517 -33.527 1.00 60.76 A C ANISOU 2410 CB ALA A 331 8591 6728 7767 3115 -685 -2357 A C ATOM 2411 N ALA A 332 -11.882 -28.449 -34.570 1.00 53.73 A N ANISOU 2411 N ALA A 332 7818 5769 6827 2606 -595 -2282 A N ATOM 2412 CA ALA A 332 -13.337 -28.552 -34.602 1.00 52.51 A C ANISOU 2412 CA ALA A 332 7839 5454 6659 2317 -633 -2188 A C ATOM 2413 C ALA A 332 -13.875 -28.644 -36.030 1.00 56.06 A C ANISOU 2413 C ALA A 332 8314 5995 6990 2246 -579 -2282 A C ATOM 2414 O ALA A 332 -14.775 -29.436 -36.310 1.00 60.03 A O ANISOU 2414 O ALA A 332 9067 6296 7446 2132 -662 -2319 A O ATOM 2415 CB ALA A 332 -13.957 -27.372 -33.886 1.00 45.65 A C ANISOU 2415 CB ALA A 332 6802 4680 5863 2068 -574 -1977 A C ATOM 2416 N LEU A 333 -13.317 -27.840 -36.930 1.00 55.56 A N ANISOU 2416 N LEU A 333 7995 6243 6872 2301 -441 -2318 A N ATOM 2417 CA LEU A 333 -13.791 -27.784 -38.310 1.00 55.70 A C ANISOU 2417 CA LEU A 333 8008 6393 6763 2229 -378 -2394 A C ATOM 2418 C LEU A 333 -13.378 -29.014 -39.109 1.00 59.08 A C ANISOU 2418 C LEU A 333 8634 6723 7090 2452 -436 -2629 A C ATOM 2419 O LEU A 333 -13.783 -29.178 -40.262 1.00 63.33 A O ANISOU 2419 O LEU A 333 9217 7338 7507 2409 -406 -2722 A O ATOM 2420 CB LEU A 333 -13.276 -26.516 -38.995 1.00 53.52 A C ANISOU 2420 CB LEU A 333 7404 6483 6449 2215 -210 -2345 A C ATOM 2421 CG LEU A 333 -13.855 -25.205 -38.453 1.00 49.80 A C ANISOU 2421 CG LEU A 333 6757 6109 6054 1971 -147 -2120 A C ATOM 2422 CD1 LEU A 333 -13.138 -23.996 -39.036 1.00 44.94 A C ANISOU 2422 CD1 LEU A 333 5839 5826 5409 1979 9 -2073 A C ATOM 2423 CD2 LEU A 333 -15.348 -25.131 -38.739 1.00 49.43 A C ANISOU 2423 CD2 LEU A 333 6828 5980 5973 1711 -179 -2033 A C ATOM 2424 N ALA A 334 -12.576 -29.879 -38.497 1.00 56.74 A N ANISOU 2424 N ALA A 334 8464 6256 6838 2701 -527 -2730 A N ATOM 2425 CA ALA A 334 -12.121 -31.093 -39.164 1.00 58.83 A C ANISOU 2425 CA ALA A 334 8890 6436 7028 2854 -578 -2866 A C ATOM 2426 C ALA A 334 -13.020 -32.280 -38.832 1.00 57.68 A C ANISOU 2426 C ALA A 334 9112 5911 6892 2740 -736 -2867 A C ATOM 2427 O ALA A 334 -12.826 -33.378 -39.346 1.00 59.56 A O ANISOU 2427 O ALA A 334 9530 6027 7073 2836 -796 -2974 A O ATOM 2428 CB ALA A 334 -10.678 -31.399 -38.783 1.00 57.50 A C ANISOU 2428 CB ALA A 334 8594 6355 6899 3106 -573 -2881 A C ATOM 2429 N VAL A 335 -14.009 -32.052 -37.976 1.00 56.31 A N ANISOU 2429 N VAL A 335 9049 5558 6788 2524 -801 -2743 A N ATOM 2430 CA VAL A 335 -14.879 -33.127 -37.516 1.00 58.50 A C ANISOU 2430 CA VAL A 335 9661 5486 7081 2370 -948 -2708 A C ATOM 2431 C VAL A 335 -16.194 -33.159 -38.280 1.00 58.32 A C ANISOU 2431 C VAL A 335 9776 5410 6972 2118 -970 -2746 A C ATOM 2432 O VAL A 335 -16.907 -32.156 -38.334 1.00 56.82 A O ANISOU 2432 O VAL A 335 9420 5386 6784 1907 -900 -2634 A O ATOM 2433 CB VAL A 335 -15.186 -32.996 -36.015 1.00 58.52 A C ANISOU 2433 CB VAL A 335 9720 5314 7202 2259 -1020 -2532 A C ATOM 2434 CG1 VAL A 335 -16.013 -34.182 -35.538 1.00 56.14 A C ANISOU 2434 CG1 VAL A 335 9759 4669 6904 2090 -1164 -2481 A C ATOM 2435 CG2 VAL A 335 -13.896 -32.884 -35.225 1.00 59.29 A C ANISOU 2435 CG2 VAL A 335 9662 5490 7374 2495 -1005 -2490 A C ATOM 2436 N PRO A 336 -16.519 -34.316 -38.874 1.00 60.14 A N ANISOU 2436 N PRO A 336 10253 5465 7134 2085 -1050 -2839 A N ATOM 2437 CA PRO A 336 -17.779 -34.500 -39.603 1.00 61.61 A C ANISOU 2437 CA PRO A 336 10586 5593 7229 1825 -1090 -2879 A C ATOM 2438 C PRO A 336 -18.982 -34.154 -38.730 1.00 61.70 A C ANISOU 2438 C PRO A 336 10671 5477 7296 1513 -1154 -2721 A C ATOM 2439 O PRO A 336 -19.021 -34.543 -37.562 1.00 61.06 A O ANISOU 2439 O PRO A 336 10696 5193 7311 1465 -1225 -2595 A O ATOM 2440 CB PRO A 336 -17.766 -35.988 -39.959 1.00 61.79 A C ANISOU 2440 CB PRO A 336 10888 5375 7213 1857 -1190 -2973 A C ATOM 2441 CG PRO A 336 -16.325 -36.361 -39.965 1.00 63.42 A C ANISOU 2441 CG PRO A 336 11022 5633 7440 2203 -1158 -3046 A C ATOM 2442 CD PRO A 336 -15.683 -35.528 -38.897 1.00 64.00 A C ANISOU 2442 CD PRO A 336 10889 5807 7623 2298 -1112 -2917 A C ATOM 2443 N GLY A 337 -19.936 -33.415 -39.287 1.00 60.26 A N ANISOU 2443 N GLY A 337 10337 5499 7062 1260 -1091 -2643 A N ATOM 2444 CA GLY A 337 -21.125 -33.027 -38.552 1.00 58.76 A C ANISOU 2444 CA GLY A 337 10115 5289 6922 927 -1111 -2438 A C ATOM 2445 C GLY A 337 -21.008 -31.665 -37.893 1.00 56.91 A C ANISOU 2445 C GLY A 337 9549 5298 6777 898 -989 -2245 A C ATOM 2446 O GLY A 337 -21.972 -31.157 -37.312 1.00 56.82 A O ANISOU 2446 O GLY A 337 9459 5326 6802 645 -983 -2074 A O ATOM 2447 N VAL A 338 -19.826 -31.067 -37.972 1.00 54.48 A N ANISOU 2447 N VAL A 338 9043 5159 6499 1155 -893 -2277 A N ATOM 2448 CA VAL A 338 -19.628 -29.746 -37.399 1.00 53.41 A C ANISOU 2448 CA VAL A 338 8603 5247 6444 1131 -779 -2108 A C ATOM 2449 C VAL A 338 -19.982 -28.677 -38.425 1.00 54.12 A C ANISOU 2449 C VAL A 338 8447 5653 6462 1041 -657 -2072 A C ATOM 2450 O VAL A 338 -19.436 -28.660 -39.527 1.00 57.27 A O ANISOU 2450 O VAL A 338 8790 6200 6770 1180 -600 -2202 A O ATOM 2451 CB VAL A 338 -18.176 -29.550 -36.902 1.00 53.03 A C ANISOU 2451 CB VAL A 338 8444 5240 6466 1423 -737 -2144 A C ATOM 2452 CG1 VAL A 338 -17.901 -28.082 -36.603 1.00 48.06 A C ANISOU 2452 CG1 VAL A 338 7483 4881 5897 1394 -606 -1997 A C ATOM 2453 CG2 VAL A 338 -17.915 -30.414 -35.673 1.00 53.76 A C ANISOU 2453 CG2 VAL A 338 8754 5032 6639 1494 -861 -2127 A C ATOM 2454 N TYR A 339 -20.913 -27.800 -38.061 1.00 53.54 A N ANISOU 2454 N TYR A 339 8234 5685 6422 814 -620 -1894 A N ATOM 2455 CA TYR A 339 -21.332 -26.708 -38.933 1.00 50.66 A C ANISOU 2455 CA TYR A 339 7645 5607 5997 724 -515 -1830 A C ATOM 2456 C TYR A 339 -20.357 -25.543 -38.862 1.00 48.24 A C ANISOU 2456 C TYR A 339 7076 5513 5740 864 -387 -1767 A C ATOM 2457 O TYR A 339 -20.027 -24.942 -39.878 1.00 44.02 A O ANISOU 2457 O TYR A 339 6396 5201 5127 919 -294 -1796 A O ATOM 2458 CB TYR A 339 -22.731 -26.214 -38.562 1.00 50.79 A C ANISOU 2458 CB TYR A 339 7613 5657 6026 447 -533 -1668 A C ATOM 2459 CG TYR A 339 -23.831 -27.236 -38.713 1.00 53.15 A C ANISOU 2459 CG TYR A 339 8133 5798 6263 252 -652 -1713 A C ATOM 2460 CD1 TYR A 339 -24.311 -27.590 -39.966 1.00 54.78 A C ANISOU 2460 CD1 TYR A 339 8397 6079 6338 190 -676 -1819 A C ATOM 2461 CD2 TYR A 339 -24.405 -27.831 -37.599 1.00 53.87 A C ANISOU 2461 CD2 TYR A 339 8375 5675 6420 110 -743 -1643 A C ATOM 2462 CE1 TYR A 339 -25.324 -28.520 -40.104 1.00 56.96 A C ANISOU 2462 CE1 TYR A 339 8874 6213 6554 -14 -793 -1863 A C ATOM 2463 CE2 TYR A 339 -25.416 -28.761 -37.728 1.00 56.20 A C ANISOU 2463 CE2 TYR A 339 8871 5828 6654 -101 -853 -1676 A C ATOM 2464 CZ TYR A 339 -25.871 -29.103 -38.979 1.00 58.21 A C ANISOU 2464 CZ TYR A 339 9178 6155 6784 -166 -880 -1789 A C ATOM 2465 OH TYR A 339 -26.879 -30.030 -39.102 1.00 62.03 A O ANISOU 2465 OH TYR A 339 9862 6499 7205 -399 -996 -1825 A O ATOM 2466 N GLY A 340 -19.907 -25.216 -37.653 1.00 49.71 A N ANISOU 2466 N GLY A 340 7207 5633 6048 907 -383 -1676 A N ATOM 2467 CA GLY A 340 -19.013 -24.088 -37.472 1.00 47.34 A C ANISOU 2467 CA GLY A 340 6663 5520 5803 1007 -271 -1609 A C ATOM 2468 C GLY A 340 -18.415 -23.978 -36.084 1.00 46.27 A C ANISOU 2468 C GLY A 340 6507 5279 5795 1075 -294 -1544 A C ATOM 2469 O GLY A 340 -18.897 -24.580 -35.129 1.00 46.31 A O ANISOU 2469 O GLY A 340 6669 5077 5851 1006 -389 -1505 A O ATOM 2470 N SER A 341 -17.352 -23.192 -35.978 1.00 45.35 A N ANISOU 2470 N SER A 341 6194 5318 5720 1200 -208 -1530 A N ATOM 2471 CA SER A 341 -16.637 -23.037 -34.727 1.00 43.89 A C ANISOU 2471 CA SER A 341 5965 5066 5644 1282 -230 -1483 A C ATOM 2472 C SER A 341 -15.947 -21.685 -34.708 1.00 44.53 A C ANISOU 2472 C SER A 341 5781 5373 5766 1293 -113 -1404 A C ATOM 2473 O SER A 341 -15.514 -21.189 -35.748 1.00 45.58 A O ANISOU 2473 O SER A 341 5779 5708 5834 1329 -19 -1440 A O ATOM 2474 CB SER A 341 -15.621 -24.163 -34.539 1.00 44.97 A C ANISOU 2474 CB SER A 341 6224 5080 5783 1519 -302 -1633 A C ATOM 2475 OG SER A 341 -15.049 -24.128 -33.243 1.00 45.75 A O ANISOU 2475 OG SER A 341 6309 5094 5982 1590 -348 -1581 A O ATOM 2476 N ARG A 342 -15.862 -21.091 -33.522 1.00 41.11 A N ANISOU 2476 N ARG A 342 5284 4904 5433 1248 -122 -1295 A N ATOM 2477 CA ARG A 342 -15.248 -19.785 -33.358 1.00 39.33 A C ANISOU 2477 CA ARG A 342 4829 4859 5256 1231 -26 -1215 A C ATOM 2478 C ARG A 342 -14.916 -19.534 -31.893 1.00 42.35 A C ANISOU 2478 C ARG A 342 5191 5155 5744 1238 -71 -1148 A C ATOM 2479 O ARG A 342 -15.560 -20.094 -30.998 1.00 40.99 A O ANISOU 2479 O ARG A 342 5174 4798 5604 1188 -161 -1112 A O ATOM 2480 CB ARG A 342 -16.185 -18.687 -33.876 1.00 34.71 A C ANISOU 2480 CB ARG A 342 4159 4381 4647 1046 48 -1093 A C ATOM 2481 CG ARG A 342 -17.556 -18.715 -33.234 1.00 34.28 A C ANISOU 2481 CG ARG A 342 4217 4191 4616 885 -10 -995 A C ATOM 2482 CD ARG A 342 -18.434 -17.558 -33.683 1.00 36.76 A C ANISOU 2482 CD ARG A 342 4432 4622 4911 736 57 -875 A C ATOM 2483 NE ARG A 342 -17.913 -16.270 -33.243 1.00 40.09 A N ANISOU 2483 NE ARG A 342 4695 5136 5402 722 127 -785 A N ATOM 2484 CZ ARG A 342 -18.174 -15.713 -32.064 1.00 42.61 A C ANISOU 2484 CZ ARG A 342 4999 5385 5805 665 108 -698 A C ATOM 2485 NH1 ARG A 342 -18.955 -16.321 -31.179 1.00 41.69 A N1+ ANISOU 2485 NH1 ARG A 342 5005 5124 5710 614 30 -679 A N1+ ATOM 2486 NH2 ARG A 342 -17.648 -14.541 -31.770 1.00 47.53 A N ANISOU 2486 NH2 ARG A 342 5491 6085 6482 650 169 -631 A N ATOM 2487 N MET A 343 -13.919 -18.692 -31.640 1.00 45.97 A N ANISOU 2487 N MET A 343 5462 5757 6250 1286 -12 -1129 A N ATOM 2488 CA MET A 343 -13.683 -18.227 -30.277 1.00 45.59 A C ANISOU 2488 CA MET A 343 5375 5653 6294 1262 -48 -1055 A C ATOM 2489 C MET A 343 -14.911 -17.454 -29.833 1.00 46.66 A C ANISOU 2489 C MET A 343 5537 5735 6456 1065 -36 -918 A C ATOM 2490 O MET A 343 -15.593 -16.830 -30.653 1.00 46.78 A O ANISOU 2490 O MET A 343 5511 5831 6432 958 31 -866 A O ATOM 2491 CB MET A 343 -12.437 -17.347 -30.182 1.00 44.19 A C ANISOU 2491 CB MET A 343 4976 5660 6155 1314 18 -1058 A C ATOM 2492 CG MET A 343 -12.468 -16.145 -31.109 1.00 45.41 A C ANISOU 2492 CG MET A 343 4975 5997 6282 1198 140 -996 A C ATOM 2493 SD MET A 343 -11.501 -14.743 -30.522 1.00 47.07 A S ANISOU 2493 SD MET A 343 4965 6353 6566 1134 201 -927 A S ATOM 2494 CE MET A 343 -12.621 -14.079 -29.292 1.00 30.78 A C ANISOU 2494 CE MET A 343 2999 4117 4579 982 154 -796 A C ATOM 2495 N THR A 344 -15.213 -17.509 -28.544 1.00 44.97 A N ANISOU 2495 N THR A 344 5393 5396 6299 1027 -102 -861 A N ATOM 2496 CA THR A 344 -16.339 -16.751 -28.027 1.00 42.12 A C ANISOU 2496 CA THR A 344 5042 5004 5959 861 -87 -741 A C ATOM 2497 C THR A 344 -15.880 -15.906 -26.849 1.00 40.85 A C ANISOU 2497 C THR A 344 4795 4854 5873 847 -87 -685 A C ATOM 2498 O THR A 344 -14.886 -16.218 -26.197 1.00 41.21 A O ANISOU 2498 O THR A 344 4821 4885 5951 955 -134 -733 A O ATOM 2499 CB THR A 344 -17.504 -17.668 -27.612 1.00 40.37 A C ANISOU 2499 CB THR A 344 5009 4622 5708 784 -164 -718 A C ATOM 2500 CG2 THR A 344 -17.199 -18.387 -26.295 1.00 39.29 A C ANISOU 2500 CG2 THR A 344 4985 4339 5604 838 -260 -721 A C ATOM 2501 OG1 THR A 344 -18.699 -16.888 -27.480 1.00 38.23 A O ANISOU 2501 OG1 THR A 344 4712 4379 5433 628 -127 -614 A O ATOM 2502 N GLY A 345 -16.591 -14.819 -26.592 1.00 39.83 A N ANISOU 2502 N GLY A 345 4613 4754 5765 723 -41 -589 A N ATOM 2503 CA GLY A 345 -16.209 -13.924 -25.520 1.00 32.36 A C ANISOU 2503 CA GLY A 345 3596 3816 4884 700 -40 -544 A C ATOM 2504 C GLY A 345 -15.069 -12.997 -25.882 1.00 36.33 A C ANISOU 2504 C GLY A 345 3933 4452 5421 723 22 -560 A C ATOM 2505 O GLY A 345 -14.814 -12.738 -27.061 1.00 37.72 A O ANISOU 2505 O GLY A 345 4034 4733 5565 723 90 -573 A O ATOM 2506 N GLY A 346 -14.370 -12.517 -24.856 1.00 37.01 A N ANISOU 2506 N GLY A 346 3961 4539 5561 732 -4 -557 A N ATOM 2507 CA GLY A 346 -13.396 -11.452 -25.000 1.00 31.59 A C ANISOU 2507 CA GLY A 346 3117 3973 4913 704 50 -555 A C ATOM 2508 C GLY A 346 -12.191 -11.771 -25.854 1.00 35.60 A C ANISOU 2508 C GLY A 346 3505 4622 5401 792 81 -633 A C ATOM 2509 O GLY A 346 -11.711 -10.907 -26.580 1.00 42.44 A O ANISOU 2509 O GLY A 346 4247 5614 6265 730 162 -613 A O ATOM 2510 N GLY A 347 -11.693 -13.001 -25.772 1.00 36.34 A N ANISOU 2510 N GLY A 347 3637 4698 5473 939 18 -721 A N ATOM 2511 CA GLY A 347 -10.501 -13.376 -26.517 1.00 39.41 A C ANISOU 2511 CA GLY A 347 3900 5240 5836 1056 45 -813 A C ATOM 2512 C GLY A 347 -9.273 -13.674 -25.669 1.00 43.27 A C ANISOU 2512 C GLY A 347 4298 5786 6359 1175 -22 -881 A C ATOM 2513 O GLY A 347 -9.329 -13.607 -24.441 1.00 46.66 A O ANISOU 2513 O GLY A 347 4775 6125 6830 1163 -98 -853 A O ATOM 2514 N PHE A 348 -8.170 -14.009 -26.341 1.00 44.21 A N ANISOU 2514 N PHE A 348 4276 6073 6447 1297 5 -972 A N ATOM 2515 CA PHE A 348 -6.874 -14.290 -25.714 1.00 45.65 A C ANISOU 2515 CA PHE A 348 4328 6366 6652 1433 -54 -1049 A C ATOM 2516 C PHE A 348 -6.935 -15.451 -24.726 1.00 50.21 A C ANISOU 2516 C PHE A 348 5064 6777 7238 1593 -193 -1089 A C ATOM 2517 O PHE A 348 -6.303 -15.416 -23.662 1.00 53.40 A O ANISOU 2517 O PHE A 348 5419 7195 7677 1642 -273 -1097 A O ATOM 2518 CB PHE A 348 -6.334 -13.043 -25.010 1.00 41.84 A C ANISOU 2518 CB PHE A 348 3693 5980 6226 1290 -38 -995 A C ATOM 2519 CG PHE A 348 -6.176 -11.862 -25.914 1.00 39.61 A C ANISOU 2519 CG PHE A 348 3267 5848 5936 1120 90 -944 A C ATOM 2520 CD1 PHE A 348 -5.116 -11.789 -26.799 1.00 41.15 A C ANISOU 2520 CD1 PHE A 348 3258 6287 6090 1160 164 -1005 A C ATOM 2521 CD2 PHE A 348 -7.082 -10.819 -25.873 1.00 37.76 A C ANISOU 2521 CD2 PHE A 348 3104 5516 5727 924 135 -833 A C ATOM 2522 CE1 PHE A 348 -4.967 -10.700 -27.637 1.00 42.59 A C ANISOU 2522 CE1 PHE A 348 3322 6607 6254 984 283 -943 A C ATOM 2523 CE2 PHE A 348 -6.938 -9.728 -26.704 1.00 41.12 A C ANISOU 2523 CE2 PHE A 348 3424 6057 6142 768 243 -774 A C ATOM 2524 CZ PHE A 348 -5.876 -9.669 -27.587 1.00 42.92 A C ANISOU 2524 CZ PHE A 348 3459 6522 6326 786 318 -823 A C ATOM 2525 N GLY A 349 -7.685 -16.482 -25.097 1.00 47.53 A N ANISOU 2525 N GLY A 349 4922 6280 6859 1667 -227 -1112 A N ATOM 2526 CA GLY A 349 -7.940 -17.610 -24.219 1.00 45.45 A C ANISOU 2526 CA GLY A 349 4860 5815 6595 1787 -359 -1127 A C ATOM 2527 C GLY A 349 -9.439 -17.786 -24.079 1.00 42.77 A C ANISOU 2527 C GLY A 349 4738 5267 6243 1644 -369 -1041 A C ATOM 2528 O GLY A 349 -10.198 -17.310 -24.916 1.00 40.10 A O ANISOU 2528 O GLY A 349 4399 4950 5887 1513 -281 -1003 A O ATOM 2529 N GLY A 350 -9.871 -18.456 -23.018 1.00 42.27 A N ANISOU 2529 N GLY A 350 4857 5019 6185 1663 -478 -1005 A N ATOM 2530 CA GLY A 350 -11.288 -18.670 -22.793 1.00 37.34 A C ANISOU 2530 CA GLY A 350 4426 4218 5542 1516 -490 -921 A C ATOM 2531 C GLY A 350 -11.831 -19.834 -23.599 1.00 35.28 A C ANISOU 2531 C GLY A 350 4348 3829 5229 1567 -517 -971 A C ATOM 2532 O GLY A 350 -11.120 -20.803 -23.877 1.00 35.35 A O ANISOU 2532 O GLY A 350 4414 3802 5217 1760 -578 -1070 A O ATOM 2533 N CYS A 351 -13.096 -19.730 -23.990 1.00 34.23 A N ANISOU 2533 N CYS A 351 4305 3632 5071 1399 -476 -910 A N ATOM 2534 CA CYS A 351 -13.779 -20.823 -24.671 1.00 39.42 A C ANISOU 2534 CA CYS A 351 5155 4151 5673 1402 -512 -950 A C ATOM 2535 C CYS A 351 -13.992 -20.601 -26.168 1.00 40.24 A C ANISOU 2535 C CYS A 351 5187 4367 5735 1375 -419 -1001 A C ATOM 2536 O CYS A 351 -14.028 -19.465 -26.640 1.00 41.93 A O ANISOU 2536 O CYS A 351 5224 4746 5961 1288 -316 -962 A O ATOM 2537 CB CYS A 351 -15.131 -21.073 -24.002 1.00 38.46 A C ANISOU 2537 CB CYS A 351 5205 3875 5533 1221 -552 -847 A C ATOM 2538 SG CYS A 351 -14.994 -21.678 -22.305 1.00 46.59 A S ANISOU 2538 SG CYS A 351 6387 4738 6575 1253 -678 -786 A S ATOM 2539 N THR A 352 -14.122 -21.700 -26.908 1.00 38.09 A N ANISOU 2539 N THR A 352 5066 3997 5409 1451 -462 -1090 A N ATOM 2540 CA THR A 352 -14.687 -21.657 -28.254 1.00 40.40 A C ANISOU 2540 CA THR A 352 5351 4359 5641 1384 -393 -1127 A C ATOM 2541 C THR A 352 -16.119 -22.179 -28.212 1.00 42.88 A C ANISOU 2541 C THR A 352 5857 4516 5919 1207 -439 -1070 A C ATOM 2542 O THR A 352 -16.475 -22.964 -27.330 1.00 43.93 A O ANISOU 2542 O THR A 352 6175 4458 6059 1183 -538 -1040 A O ATOM 2543 CB THR A 352 -13.887 -22.501 -29.274 1.00 39.61 A C ANISOU 2543 CB THR A 352 5283 4281 5486 1583 -402 -1286 A C ATOM 2544 CG2 THR A 352 -12.416 -22.124 -29.266 1.00 39.22 A C ANISOU 2544 CG2 THR A 352 5033 4407 5464 1771 -363 -1353 A C ATOM 2545 OG1 THR A 352 -14.034 -23.893 -28.969 1.00 40.50 A O ANISOU 2545 OG1 THR A 352 5657 4153 5578 1668 -528 -1348 A O ATOM 2546 N VAL A 353 -16.939 -21.742 -29.162 1.00 43.73 A N ANISOU 2546 N VAL A 353 5918 4717 5981 1076 -371 -1049 A N ATOM 2547 CA VAL A 353 -18.289 -22.272 -29.301 1.00 44.94 A C ANISOU 2547 CA VAL A 353 6229 4759 6087 903 -413 -1011 A C ATOM 2548 C VAL A 353 -18.404 -23.001 -30.641 1.00 46.32 A C ANISOU 2548 C VAL A 353 6491 4932 6178 938 -419 -1128 A C ATOM 2549 O VAL A 353 -17.936 -22.518 -31.673 1.00 47.33 A O ANISOU 2549 O VAL A 353 6483 5229 6271 1006 -338 -1183 A O ATOM 2550 CB VAL A 353 -19.363 -21.160 -29.188 1.00 42.05 A C ANISOU 2550 CB VAL A 353 5742 4507 5728 706 -345 -880 A C ATOM 2551 CG1 VAL A 353 -19.137 -20.067 -30.230 1.00 40.36 A C ANISOU 2551 CG1 VAL A 353 5328 4507 5497 717 -233 -877 A C ATOM 2552 CG2 VAL A 353 -20.757 -21.751 -29.318 1.00 42.56 A C ANISOU 2552 CG2 VAL A 353 5946 4490 5737 524 -392 -845 A C ATOM 2553 N THR A 354 -18.992 -24.190 -30.615 1.00 46.95 A N ANISOU 2553 N THR A 354 6807 4814 6217 888 -518 -1169 A N ATOM 2554 CA THR A 354 -19.119 -24.989 -31.825 1.00 46.19 A C ANISOU 2554 CA THR A 354 6828 4687 6035 919 -541 -1297 A C ATOM 2555 C THR A 354 -20.559 -25.434 -32.011 1.00 50.35 A C ANISOU 2555 C THR A 354 7493 5129 6507 682 -591 -1254 A C ATOM 2556 O THR A 354 -21.209 -25.907 -31.076 1.00 49.24 A O ANISOU 2556 O THR A 354 7491 4831 6387 552 -665 -1179 A O ATOM 2557 CB THR A 354 -18.194 -26.225 -31.796 1.00 46.17 A C ANISOU 2557 CB THR A 354 7017 4501 6024 1136 -633 -1440 A C ATOM 2558 CG2 THR A 354 -18.374 -27.074 -33.065 1.00 41.65 A C ANISOU 2558 CG2 THR A 354 6587 3884 5353 1169 -661 -1589 A C ATOM 2559 OG1 THR A 354 -16.830 -25.797 -31.701 1.00 43.85 A O ANISOU 2559 OG1 THR A 354 6559 4331 5772 1364 -583 -1489 A O ATOM 2560 N LEU A 355 -21.057 -25.268 -33.228 1.00 52.96 A N ANISOU 2560 N LEU A 355 7777 5586 6759 616 -550 -1299 A N ATOM 2561 CA LEU A 355 -22.412 -25.666 -33.552 1.00 51.08 A C ANISOU 2561 CA LEU A 355 7644 5309 6457 387 -598 -1272 A C ATOM 2562 C LEU A 355 -22.336 -26.922 -34.400 1.00 51.74 A C ANISOU 2562 C LEU A 355 7952 5246 6458 432 -680 -1435 A C ATOM 2563 O LEU A 355 -21.676 -26.932 -35.440 1.00 49.89 A O ANISOU 2563 O LEU A 355 7679 5108 6170 583 -640 -1557 A O ATOM 2564 CB LEU A 355 -23.133 -24.521 -34.257 1.00 49.49 A C ANISOU 2564 CB LEU A 355 7225 5360 6218 271 -506 -1194 A C ATOM 2565 CG LEU A 355 -24.657 -24.514 -34.241 1.00 53.49 A C ANISOU 2565 CG LEU A 355 7745 5897 6681 13 -539 -1109 A C ATOM 2566 CD1 LEU A 355 -25.122 -23.148 -33.773 1.00 54.80 A C ANISOU 2566 CD1 LEU A 355 7683 6246 6894 -52 -454 -956 A C ATOM 2567 CD2 LEU A 355 -25.200 -24.790 -35.639 1.00 53.92 A C ANISOU 2567 CD2 LEU A 355 7824 6044 6620 -52 -550 -1194 A C ATOM 2568 N LEU A 356 -22.976 -27.991 -33.932 1.00 54.97 A N ANISOU 2568 N LEU A 356 8609 5422 6855 300 -796 -1439 A N ATOM 2569 CA LEU A 356 -22.816 -29.304 -34.548 1.00 57.35 A C ANISOU 2569 CA LEU A 356 9181 5518 7090 356 -897 -1602 A C ATOM 2570 C LEU A 356 -24.082 -30.130 -34.496 1.00 58.72 A C ANISOU 2570 C LEU A 356 9564 5536 7212 78 -999 -1580 A C ATOM 2571 O LEU A 356 -24.983 -29.834 -33.717 1.00 56.22 A O ANISOU 2571 O LEU A 356 9202 5240 6921 -142 -1002 -1430 A O ATOM 2572 CB LEU A 356 -21.696 -30.086 -33.858 1.00 60.47 A C ANISOU 2572 CB LEU A 356 9749 5686 7542 589 -966 -1671 A C ATOM 2573 CG LEU A 356 -21.616 -30.042 -32.323 1.00 63.95 A C ANISOU 2573 CG LEU A 356 10220 6004 8075 561 -1002 -1530 A C ATOM 2574 CD1 LEU A 356 -22.775 -30.741 -31.626 1.00 67.67 A C ANISOU 2574 CD1 LEU A 356 10904 6277 8531 284 -1100 -1435 A C ATOM 2575 CD2 LEU A 356 -20.310 -30.664 -31.868 1.00 67.10 A C ANISOU 2575 CD2 LEU A 356 10739 6240 8518 855 -1060 -1617 A C ATOM 2576 N GLU A 357 -24.133 -31.184 -35.306 1.00 62.46 A N ANISOU 2576 N GLU A 357 10271 5857 7606 84 -1085 -1736 A N ATOM 2577 CA GLU A 357 -25.182 -32.183 -35.171 1.00 64.11 A C ANISOU 2577 CA GLU A 357 10735 5856 7767 -180 -1206 -1732 A C ATOM 2578 C GLU A 357 -24.969 -32.918 -33.855 1.00 66.27 A C ANISOU 2578 C GLU A 357 11230 5838 8111 -184 -1298 -1662 A C ATOM 2579 O GLU A 357 -23.841 -33.271 -33.518 1.00 69.79 A O ANISOU 2579 O GLU A 357 11772 6139 8603 83 -1323 -1727 A O ATOM 2580 CB GLU A 357 -25.170 -33.156 -36.348 1.00 66.96 A C ANISOU 2580 CB GLU A 357 11318 6096 8025 -152 -1285 -1933 A C ATOM 2581 N ALA A 358 -26.049 -33.135 -33.110 1.00 64.70 A N ANISOU 2581 N ALA A 358 11103 5569 7910 -486 -1347 -1526 A N ATOM 2582 CA ALA A 358 -25.964 -33.715 -31.771 1.00 63.04 A C ANISOU 2582 CA ALA A 358 11085 5112 7754 -529 -1424 -1423 A C ATOM 2583 C ALA A 358 -25.205 -35.042 -31.757 1.00 66.18 A C ANISOU 2583 C ALA A 358 11856 5142 8148 -363 -1558 -1553 A C ATOM 2584 O ALA A 358 -24.503 -35.357 -30.797 1.00 68.56 A O ANISOU 2584 O ALA A 358 12244 5297 8509 -213 -1589 -1493 A O ATOM 2585 CB ALA A 358 -27.359 -33.902 -31.189 1.00 60.59 A C ANISOU 2585 CB ALA A 358 10819 4792 7410 -919 -1460 -1277 A C ATOM 2586 N SER A 359 -25.334 -35.803 -32.838 1.00 67.00 A N ANISOU 2586 N SER A 359 12102 5177 8180 -368 -1605 -1699 A N ATOM 2587 CA SER A 359 -24.706 -37.115 -32.937 1.00 69.59 A C ANISOU 2587 CA SER A 359 12659 5279 8502 -203 -1676 -1770 A C ATOM 2588 C SER A 359 -23.187 -37.030 -33.048 1.00 67.10 A C ANISOU 2588 C SER A 359 12287 4977 8232 218 -1642 -1875 A C ATOM 2589 O SER A 359 -22.485 -38.018 -32.827 1.00 67.36 A O ANISOU 2589 O SER A 359 12487 4830 8277 397 -1703 -1905 A O ATOM 2590 CB SER A 359 -25.264 -37.870 -34.142 1.00 74.48 A C ANISOU 2590 CB SER A 359 13406 5862 9031 -319 -1720 -1902 A C ATOM 2591 OG SER A 359 -26.679 -37.900 -34.102 1.00 77.58 A O ANISOU 2591 OG SER A 359 13809 6291 9376 -715 -1747 -1807 A O ATOM 2592 N ALA A 360 -22.686 -35.846 -33.385 1.00 63.91 A N ANISOU 2592 N ALA A 360 11637 4800 7847 373 -1546 -1928 A N ATOM 2593 CA ALA A 360 -21.267 -35.669 -33.670 1.00 63.18 A C ANISOU 2593 CA ALA A 360 11433 4791 7782 760 -1494 -2041 A C ATOM 2594 C ALA A 360 -20.485 -35.188 -32.453 1.00 63.63 A C ANISOU 2594 C ALA A 360 11380 4862 7936 917 -1474 -1928 A C ATOM 2595 O ALA A 360 -19.255 -35.176 -32.466 1.00 64.79 A O ANISOU 2595 O ALA A 360 11435 5071 8111 1228 -1445 -1995 A O ATOM 2596 CB ALA A 360 -21.085 -34.697 -34.825 1.00 58.58 A C ANISOU 2596 CB ALA A 360 10636 4475 7148 853 -1394 -2174 A C ATOM 2597 N ALA A 361 -21.200 -34.792 -31.406 1.00 63.17 A N ANISOU 2597 N ALA A 361 11318 4765 7919 694 -1489 -1757 A N ATOM 2598 CA ALA A 361 -20.564 -34.252 -30.206 1.00 62.37 A C ANISOU 2598 CA ALA A 361 11108 4689 7902 814 -1472 -1643 A C ATOM 2599 C ALA A 361 -19.551 -35.215 -29.556 1.00 64.73 A C ANISOU 2599 C ALA A 361 11534 4837 8225 1045 -1542 -1633 A C ATOM 2600 O ALA A 361 -18.457 -34.785 -29.192 1.00 64.95 A O ANISOU 2600 O ALA A 361 11407 4969 8302 1301 -1509 -1646 A O ATOM 2601 CB ALA A 361 -21.627 -33.831 -29.194 1.00 60.24 A C ANISOU 2601 CB ALA A 361 10814 4424 7652 499 -1469 -1442 A C ATOM 2602 N PRO A 362 -19.898 -36.510 -29.405 1.00 67.69 A N ANISOU 2602 N PRO A 362 12184 4976 8558 955 -1645 -1610 A N ATOM 2603 CA PRO A 362 -18.867 -37.413 -28.872 1.00 71.68 A C ANISOU 2603 CA PRO A 362 12814 5347 9076 1205 -1721 -1617 A C ATOM 2604 C PRO A 362 -17.615 -37.491 -29.750 1.00 73.77 A C ANISOU 2604 C PRO A 362 12971 5723 9334 1557 -1686 -1795 A C ATOM 2605 O PRO A 362 -16.499 -37.474 -29.228 1.00 73.64 A O ANISOU 2605 O PRO A 362 12873 5755 9353 1814 -1694 -1796 A O ATOM 2606 CB PRO A 362 -19.574 -38.771 -28.835 1.00 73.84 A C ANISOU 2606 CB PRO A 362 13413 5351 9292 1028 -1834 -1587 A C ATOM 2607 CG PRO A 362 -21.014 -38.444 -28.743 1.00 72.71 A C ANISOU 2607 CG PRO A 362 13285 5214 9126 639 -1817 -1485 A C ATOM 2608 CD PRO A 362 -21.195 -37.199 -29.553 1.00 69.01 A C ANISOU 2608 CD PRO A 362 12556 4996 8667 621 -1704 -1560 A C ATOM 2609 N HIS A 363 -17.805 -37.572 -31.064 1.00 73.51 A N ANISOU 2609 N HIS A 363 12932 5751 9248 1559 -1648 -1944 A N ATOM 2610 CA HIS A 363 -16.687 -37.655 -32.000 1.00 73.87 A C ANISOU 2610 CA HIS A 363 12870 5929 9270 1873 -1602 -2119 A C ATOM 2611 C HIS A 363 -15.880 -36.359 -32.026 1.00 69.46 A C ANISOU 2611 C HIS A 363 11968 5670 8754 2043 -1482 -2136 A C ATOM 2612 O HIS A 363 -14.666 -36.374 -32.233 1.00 73.16 A O ANISOU 2612 O HIS A 363 12307 6267 9226 2333 -1453 -2221 A O ATOM 2613 CB HIS A 363 -17.185 -37.977 -33.409 1.00 76.95 A C ANISOU 2613 CB HIS A 363 13329 6331 9577 1807 -1583 -2271 A C ATOM 2614 CG HIS A 363 -18.050 -39.196 -33.483 1.00 83.62 A C ANISOU 2614 CG HIS A 363 14497 6897 10377 1609 -1696 -2261 A C ATOM 2615 CD2 HIS A 363 -17.803 -40.436 -33.969 1.00 90.56 A C ANISOU 2615 CD2 HIS A 363 15605 7594 11208 1711 -1777 -2366 A C ATOM 2616 ND1 HIS A 363 -19.349 -39.216 -33.024 1.00 84.26 A N ANISOU 2616 ND1 HIS A 363 14691 6868 10457 1251 -1736 -2132 A N ATOM 2617 CE1 HIS A 363 -19.865 -40.416 -33.221 1.00 89.60 A C ANISOU 2617 CE1 HIS A 363 15646 7311 11086 1132 -1835 -2152 A C ATOM 2618 NE2 HIS A 363 -18.948 -41.175 -33.794 1.00 92.81 A N ANISOU 2618 NE2 HIS A 363 16140 7657 11467 1410 -1865 -2296 A N ATOM 2619 N ALA A 364 -16.560 -35.237 -31.821 1.00 60.62 A N ANISOU 2619 N ALA A 364 10699 4672 7664 1856 -1415 -2056 A N ATOM 2620 CA ALA A 364 -15.904 -33.940 -31.865 1.00 57.60 A C ANISOU 2620 CA ALA A 364 9993 4569 7322 1986 -1298 -2067 A C ATOM 2621 C ALA A 364 -15.075 -33.709 -30.604 1.00 58.98 A C ANISOU 2621 C ALA A 364 10073 4762 7576 2120 -1318 -1961 A C ATOM 2622 O ALA A 364 -14.024 -33.076 -30.649 1.00 57.81 A O ANISOU 2622 O ALA A 364 9678 4833 7454 2328 -1247 -2001 A O ATOM 2623 CB ALA A 364 -16.929 -32.832 -32.042 1.00 51.73 A C ANISOU 2623 CB ALA A 364 9139 3933 6583 1748 -1233 -2020 A C ATOM 2624 N MET A 365 -15.550 -34.229 -29.479 1.00 59.76 A N ANISOU 2624 N MET A 365 10362 4645 7701 1986 -1416 -1823 A N ATOM 2625 CA MET A 365 -14.834 -34.061 -28.223 1.00 60.22 A C ANISOU 2625 CA MET A 365 10353 4711 7817 2097 -1448 -1718 A C ATOM 2626 C MET A 365 -13.528 -34.852 -28.215 1.00 60.20 A C ANISOU 2626 C MET A 365 10365 4708 7799 2402 -1499 -1798 A C ATOM 2627 O MET A 365 -12.495 -34.341 -27.785 1.00 56.70 A O ANISOU 2627 O MET A 365 9713 4436 7393 2590 -1470 -1797 A O ATOM 2628 CB MET A 365 -15.718 -34.465 -27.041 1.00 59.90 A C ANISOU 2628 CB MET A 365 10525 4449 7786 1866 -1538 -1547 A C ATOM 2629 CG MET A 365 -16.671 -33.357 -26.619 1.00 58.24 A C ANISOU 2629 CG MET A 365 10207 4311 7611 1617 -1479 -1437 A C ATOM 2630 SD MET A 365 -17.687 -33.777 -25.197 1.00 57.81 A S ANISOU 2630 SD MET A 365 10371 4043 7550 1333 -1568 -1228 A S ATOM 2631 CE MET A 365 -18.793 -34.984 -25.919 1.00 55.02 A C ANISOU 2631 CE MET A 365 10312 3477 7116 1097 -1633 -1252 A C ATOM 2632 N ARG A 366 -13.567 -36.084 -28.708 1.00 62.53 A N ANISOU 2632 N ARG A 366 10900 4820 8038 2449 -1578 -1873 A N ATOM 2633 CA ARG A 366 -12.364 -36.906 -28.740 1.00 66.83 A C ANISOU 2633 CA ARG A 366 11481 5351 8562 2748 -1637 -1958 A C ATOM 2634 C ARG A 366 -11.304 -36.296 -29.656 1.00 69.29 A C ANISOU 2634 C ARG A 366 11500 5963 8864 2984 -1529 -2101 A C ATOM 2635 O ARG A 366 -10.131 -36.221 -29.290 1.00 73.69 A O ANISOU 2635 O ARG A 366 11908 6655 9436 3215 -1533 -2122 A O ATOM 2636 CB ARG A 366 -12.692 -38.331 -29.184 1.00 70.53 A C ANISOU 2636 CB ARG A 366 12277 5553 8968 2745 -1742 -2021 A C ATOM 2637 CG ARG A 366 -11.469 -39.215 -29.349 1.00 76.06 A C ANISOU 2637 CG ARG A 366 13026 6234 9638 3073 -1807 -2130 A C ATOM 2638 CD ARG A 366 -11.843 -40.610 -29.824 1.00 81.08 A C ANISOU 2638 CD ARG A 366 14003 6590 10215 3066 -1913 -2198 A C ATOM 2639 NE ARG A 366 -12.561 -41.368 -28.802 1.00 84.24 A N ANISOU 2639 NE ARG A 366 14697 6694 10615 2885 -2037 -2052 A N ATOM 2640 CZ ARG A 366 -11.974 -42.128 -27.881 1.00 84.62 A C ANISOU 2640 CZ ARG A 366 14898 6593 10660 3029 -2154 -1995 A C ATOM 2641 NH1 ARG A 366 -10.653 -42.233 -27.848 1.00 85.67 A N1+ ANISOU 2641 NH1 ARG A 366 14911 6848 10793 3363 -2168 -2078 A N1+ ATOM 2642 NH2 ARG A 366 -12.708 -42.785 -26.993 1.00 83.34 A N ANISOU 2642 NH2 ARG A 366 15006 6172 10486 2836 -2258 -1854 A N ATOM 2643 N HIS A 367 -11.725 -35.841 -30.833 1.00 65.92 A N ANISOU 2643 N HIS A 367 10984 5659 8403 2913 -1431 -2196 A N ATOM 2644 CA HIS A 367 -10.795 -35.318 -31.832 1.00 67.05 A C ANISOU 2644 CA HIS A 367 10863 6098 8516 3112 -1319 -2333 A C ATOM 2645 C HIS A 367 -10.198 -33.974 -31.431 1.00 68.11 A C ANISOU 2645 C HIS A 367 10653 6519 8706 3147 -1216 -2277 A C ATOM 2646 O HIS A 367 -8.998 -33.747 -31.598 1.00 70.01 A O ANISOU 2646 O HIS A 367 10677 6984 8941 3362 -1169 -2341 A O ATOM 2647 CB HIS A 367 -11.488 -35.181 -33.190 1.00 67.65 A C ANISOU 2647 CB HIS A 367 10951 6229 8523 3008 -1245 -2443 A C ATOM 2648 CG HIS A 367 -10.570 -34.752 -34.294 1.00 68.86 A C ANISOU 2648 CG HIS A 367 10856 6687 8622 3202 -1128 -2585 A C ATOM 2649 CD2 HIS A 367 -9.675 -35.453 -35.030 1.00 71.60 A C ANISOU 2649 CD2 HIS A 367 11203 7098 8904 3439 -1130 -2727 A C ATOM 2650 ND1 HIS A 367 -10.504 -33.452 -34.746 1.00 66.72 A N ANISOU 2650 ND1 HIS A 367 10291 6709 8350 3156 -986 -2585 A N ATOM 2651 CE1 HIS A 367 -9.610 -33.370 -35.716 1.00 67.34 A C ANISOU 2651 CE1 HIS A 367 10194 7030 8362 3340 -900 -2712 A C ATOM 2652 NE2 HIS A 367 -9.093 -34.569 -35.907 1.00 71.65 A N ANISOU 2652 NE2 HIS A 367 10910 7446 8868 3518 -985 -2804 A N ATOM 2653 N ILE A 368 -11.041 -33.083 -30.917 1.00 66.30 A N ANISOU 2653 N ILE A 368 10372 6290 8529 2925 -1182 -2161 A N ATOM 2654 CA ILE A 368 -10.588 -31.775 -30.455 1.00 63.28 A C ANISOU 2654 CA ILE A 368 9682 6154 8207 2930 -1091 -2097 A C ATOM 2655 C ILE A 368 -9.563 -31.921 -29.333 1.00 62.01 A C ANISOU 2655 C ILE A 368 9456 6015 8091 3086 -1155 -2037 A C ATOM 2656 O ILE A 368 -8.523 -31.267 -29.345 1.00 60.46 A O ANISOU 2656 O ILE A 368 8983 6080 7910 3222 -1086 -2065 A O ATOM 2657 CB ILE A 368 -11.778 -30.910 -29.980 1.00 59.63 A C ANISOU 2657 CB ILE A 368 9223 5638 7794 2664 -1067 -1978 A C ATOM 2658 CG1 ILE A 368 -12.557 -30.386 -31.192 1.00 55.39 A C ANISOU 2658 CG1 ILE A 368 8642 5195 7210 2542 -975 -2054 A C ATOM 2659 CG2 ILE A 368 -11.300 -29.754 -29.110 1.00 56.67 A C ANISOU 2659 CG2 ILE A 368 8592 5443 7499 2671 -1015 -1885 A C ATOM 2660 CD1 ILE A 368 -13.918 -29.819 -30.855 1.00 52.93 A C ANISOU 2660 CD1 ILE A 368 8368 4824 6919 2219 -961 -1912 A C ATOM 2661 N GLN A 369 -9.850 -32.805 -28.384 1.00 63.95 A N ANISOU 2661 N GLN A 369 9959 5993 8346 3057 -1288 -1956 A N ATOM 2662 CA GLN A 369 -8.962 -33.038 -27.249 1.00 66.39 A C ANISOU 2662 CA GLN A 369 10244 6298 8682 3200 -1368 -1895 A C ATOM 2663 C GLN A 369 -7.609 -33.584 -27.695 1.00 69.78 A C ANISOU 2663 C GLN A 369 10581 6860 9071 3493 -1380 -2021 A C ATOM 2664 O GLN A 369 -6.566 -33.135 -27.223 1.00 69.53 A O ANISOU 2664 O GLN A 369 10330 7028 9061 3632 -1367 -2018 A O ATOM 2665 CB GLN A 369 -9.620 -34.001 -26.255 1.00 68.10 A C ANISOU 2665 CB GLN A 369 10791 6189 8894 3102 -1510 -1785 A C ATOM 2666 CG GLN A 369 -8.815 -34.313 -25.001 1.00 70.19 A C ANISOU 2666 CG GLN A 369 11072 6424 9174 3238 -1610 -1713 A C ATOM 2667 CD GLN A 369 -8.781 -33.158 -24.010 1.00 70.67 A C ANISOU 2667 CD GLN A 369 10933 6623 9296 3148 -1572 -1598 A C ATOM 2668 NE2 GLN A 369 -9.093 -33.454 -22.757 1.00 73.97 A N ANISOU 2668 NE2 GLN A 369 11514 6874 9719 3071 -1671 -1466 A N ATOM 2669 OE1 GLN A 369 -8.512 -32.013 -24.369 1.00 69.19 A O ANISOU 2669 OE1 GLN A 369 10457 6687 9145 3139 -1457 -1626 A O ATOM 2670 N GLU A 370 -7.631 -34.546 -28.614 1.00 74.21 A N ANISOU 2670 N GLU A 370 11309 7319 9568 3582 -1407 -2137 A N ATOM 2671 CA GLU A 370 -6.406 -35.163 -29.116 1.00 76.42 A C ANISOU 2671 CA GLU A 370 11525 7712 9799 3870 -1424 -2270 A C ATOM 2672 C GLU A 370 -5.583 -34.191 -29.959 1.00 77.61 A C ANISOU 2672 C GLU A 370 11311 8241 9935 3961 -1276 -2360 A C ATOM 2673 O GLU A 370 -4.354 -34.264 -29.979 1.00 79.70 A O ANISOU 2673 O GLU A 370 11407 8696 10181 4181 -1273 -2427 A O ATOM 2674 CB GLU A 370 -6.734 -36.416 -29.935 1.00 75.92 A C ANISOU 2674 CB GLU A 370 11746 7432 9668 3930 -1489 -2376 A C ATOM 2675 N HIS A 371 -6.266 -33.285 -30.653 1.00 75.82 A N ANISOU 2675 N HIS A 371 10964 8131 9713 3784 -1154 -2358 A N ATOM 2676 CA HIS A 371 -5.600 -32.298 -31.498 1.00 76.14 A C ANISOU 2676 CA HIS A 371 10666 8533 9732 3828 -1002 -2426 A C ATOM 2677 C HIS A 371 -5.253 -31.023 -30.733 1.00 75.81 A C ANISOU 2677 C HIS A 371 10344 8700 9762 3748 -937 -2321 A C ATOM 2678 O HIS A 371 -4.769 -30.054 -31.321 1.00 77.12 A O ANISOU 2678 O HIS A 371 10217 9168 9916 3736 -806 -2348 A O ATOM 2679 CB HIS A 371 -6.477 -31.954 -32.706 1.00 75.97 A C ANISOU 2679 CB HIS A 371 10655 8548 9663 3687 -902 -2484 A C ATOM 2680 CG HIS A 371 -6.225 -32.818 -33.903 1.00 80.30 A C ANISOU 2680 CG HIS A 371 11297 9102 10113 3831 -897 -2643 A C ATOM 2681 CD2 HIS A 371 -6.285 -34.162 -34.065 1.00 82.84 A C ANISOU 2681 CD2 HIS A 371 11902 9182 10393 3942 -1010 -2719 A C ATOM 2682 ND1 HIS A 371 -5.857 -32.302 -35.127 1.00 81.53 A N ANISOU 2682 ND1 HIS A 371 11242 9540 10194 3870 -761 -2744 A N ATOM 2683 CE1 HIS A 371 -5.702 -33.288 -35.991 1.00 84.41 A C ANISOU 2683 CE1 HIS A 371 11755 9843 10475 4006 -791 -2881 A C ATOM 2684 NE2 HIS A 371 -5.954 -34.428 -35.372 1.00 85.11 A N ANISOU 2684 NE2 HIS A 371 12145 9608 10586 4055 -943 -2872 A N ATOM 2685 N TYR A 372 -5.501 -31.027 -29.425 1.00 73.72 A N ANISOU 2685 N TYR A 372 10174 8275 9563 3682 -1030 -2197 A N ATOM 2686 CA TYR A 372 -5.225 -29.862 -28.588 1.00 71.96 A C ANISOU 2686 CA TYR A 372 9712 8219 9409 3599 -986 -2096 A C ATOM 2687 C TYR A 372 -4.010 -30.087 -27.690 1.00 73.77 A C ANISOU 2687 C TYR A 372 9845 8535 9650 3776 -1061 -2087 A C ATOM 2688 O TYR A 372 -3.926 -31.095 -26.987 1.00 74.65 A O ANISOU 2688 O TYR A 372 10179 8432 9753 3875 -1197 -2069 A O ATOM 2689 CB TYR A 372 -6.443 -29.511 -27.731 1.00 68.25 A C ANISOU 2689 CB TYR A 372 9390 7539 9002 3375 -1025 -1959 A C ATOM 2690 CG TYR A 372 -6.265 -28.264 -26.895 1.00 63.90 A C ANISOU 2690 CG TYR A 372 8607 7150 8524 3278 -979 -1860 A C ATOM 2691 CD1 TYR A 372 -5.865 -27.066 -27.477 1.00 61.80 A C ANISOU 2691 CD1 TYR A 372 8026 7185 8271 3235 -839 -1882 A C ATOM 2692 CD2 TYR A 372 -6.510 -28.277 -25.528 1.00 62.36 A C ANISOU 2692 CD2 TYR A 372 8513 6805 8377 3219 -1077 -1741 A C ATOM 2693 CE1 TYR A 372 -5.706 -25.924 -26.719 1.00 59.97 A C ANISOU 2693 CE1 TYR A 372 7588 7089 8106 3136 -803 -1794 A C ATOM 2694 CE2 TYR A 372 -6.355 -27.134 -24.765 1.00 58.96 A C ANISOU 2694 CE2 TYR A 372 7875 6518 8008 3131 -1041 -1659 A C ATOM 2695 CZ TYR A 372 -5.950 -25.965 -25.365 1.00 57.27 A C ANISOU 2695 CZ TYR A 372 7353 6592 7815 3090 -906 -1689 A C ATOM 2696 OH TYR A 372 -5.792 -24.830 -24.608 1.00 55.24 A O ANISOU 2696 OH TYR A 372 6898 6469 7621 2993 -876 -1612 A O ATOM 2697 N GLY A 373 -3.082 -29.133 -27.710 1.00 74.00 A N ANISOU 2697 N GLY A 373 9543 8881 9694 3805 -974 -2097 A N ATOM 2698 CA GLY A 373 -1.836 -29.246 -26.973 1.00 77.60 A C ANISOU 2698 CA GLY A 373 9861 9472 10150 3971 -1035 -2105 A C ATOM 2699 C GLY A 373 -1.982 -29.108 -25.469 1.00 79.82 A C ANISOU 2699 C GLY A 373 10211 9626 10491 3914 -1138 -1981 A C ATOM 2700 O GLY A 373 -1.152 -29.606 -24.709 1.00 83.50 A O ANISOU 2700 O GLY A 373 10682 10098 10946 4073 -1239 -1984 A O ATOM 2701 N GLY A 374 -3.033 -28.422 -25.035 1.00 77.50 A N ANISOU 2701 N GLY A 374 9967 9227 10254 3693 -1116 -1873 A N ATOM 2702 CA GLY A 374 -3.303 -28.275 -23.616 1.00 76.00 A C ANISOU 2702 CA GLY A 374 9859 8906 10110 3621 -1211 -1751 A C ATOM 2703 C GLY A 374 -4.356 -29.267 -23.165 1.00 74.58 A C ANISOU 2703 C GLY A 374 10055 8364 9919 3565 -1321 -1687 A C ATOM 2704 O GLY A 374 -4.505 -30.336 -23.759 1.00 76.63 A O ANISOU 2704 O GLY A 374 10519 8468 10128 3652 -1364 -1752 A O ATOM 2705 N THR A 375 -5.099 -28.913 -22.122 1.00 70.37 A N ANISOU 2705 N THR A 375 9614 7697 9425 3409 -1367 -1560 A N ATOM 2706 CA THR A 375 -6.165 -29.779 -21.632 1.00 68.29 A C ANISOU 2706 CA THR A 375 9701 7100 9144 3311 -1464 -1478 A C ATOM 2707 C THR A 375 -7.526 -29.102 -21.747 1.00 61.72 A C ANISOU 2707 C THR A 375 8922 6181 8348 3054 -1398 -1403 A C ATOM 2708 O THR A 375 -7.874 -28.240 -20.939 1.00 57.22 A O ANISOU 2708 O THR A 375 8273 5644 7822 2927 -1387 -1309 A O ATOM 2709 CB THR A 375 -5.926 -30.192 -20.176 1.00 69.97 A C ANISOU 2709 CB THR A 375 10040 7196 9349 3351 -1599 -1379 A C ATOM 2710 CG2 THR A 375 -7.044 -31.104 -19.697 1.00 71.85 A C ANISOU 2710 CG2 THR A 375 10645 7098 9557 3222 -1691 -1283 A C ATOM 2711 OG1 THR A 375 -4.674 -30.885 -20.080 1.00 73.52 A O ANISOU 2711 OG1 THR A 375 10454 7719 9760 3604 -1670 -1454 A O ATOM 2712 N ALA A 376 -8.296 -29.498 -22.755 1.00 58.57 A N ANISOU 2712 N ALA A 376 8656 5673 7925 2981 -1360 -1452 A N ATOM 2713 CA ALA A 376 -9.595 -28.887 -22.997 1.00 57.55 A C ANISOU 2713 CA ALA A 376 8572 5473 7821 2743 -1298 -1397 A C ATOM 2714 C ALA A 376 -10.658 -29.429 -22.050 1.00 57.70 A C ANISOU 2714 C ALA A 376 8881 5213 7829 2570 -1395 -1266 A C ATOM 2715 O ALA A 376 -10.616 -30.590 -21.643 1.00 60.14 A O ANISOU 2715 O ALA A 376 9431 5326 8092 2617 -1505 -1243 A O ATOM 2716 CB ALA A 376 -10.026 -29.095 -24.453 1.00 56.99 A C ANISOU 2716 CB ALA A 376 8531 5407 7716 2721 -1225 -1505 A C ATOM 2717 N THR A 377 -11.605 -28.562 -21.706 1.00 54.71 A N ANISOU 2717 N THR A 377 8473 4825 7489 2364 -1351 -1179 A N ATOM 2718 CA THR A 377 -12.778 -28.926 -20.925 1.00 56.23 A C ANISOU 2718 CA THR A 377 8914 4789 7661 2144 -1416 -1046 A C ATOM 2719 C THR A 377 -14.013 -28.707 -21.802 1.00 56.50 A C ANISOU 2719 C THR A 377 8961 4835 7671 1882 -1320 -1030 A C ATOM 2720 O THR A 377 -14.058 -27.759 -22.584 1.00 54.29 A O ANISOU 2720 O THR A 377 8436 4783 7408 1826 -1190 -1063 A O ATOM 2721 CB THR A 377 -12.862 -28.095 -19.624 1.00 58.76 A C ANISOU 2721 CB THR A 377 9118 5206 8002 2028 -1406 -907 A C ATOM 2722 CG2 THR A 377 -14.115 -28.432 -18.827 1.00 59.89 A C ANISOU 2722 CG2 THR A 377 9482 5172 8101 1765 -1444 -757 A C ATOM 2723 OG1 THR A 377 -11.708 -28.366 -18.817 1.00 61.94 A O ANISOU 2723 OG1 THR A 377 9510 5610 8413 2265 -1505 -922 A O ATOM 2724 N PHE A 378 -15.003 -29.587 -21.690 1.00 58.46 A N ANISOU 2724 N PHE A 378 9496 4843 7873 1719 -1391 -976 A N ATOM 2725 CA PHE A 378 -16.135 -29.564 -22.613 1.00 56.56 A C ANISOU 2725 CA PHE A 378 9285 4608 7600 1490 -1323 -980 A C ATOM 2726 C PHE A 378 -17.486 -29.335 -21.938 1.00 55.29 A C ANISOU 2726 C PHE A 378 9178 4419 7412 1161 -1303 -820 A C ATOM 2727 O PHE A 378 -17.788 -29.946 -20.912 1.00 59.69 A O ANISOU 2727 O PHE A 378 9942 4794 7943 1085 -1397 -719 A O ATOM 2728 CB PHE A 378 -16.183 -30.870 -23.404 1.00 57.80 A C ANISOU 2728 CB PHE A 378 9725 4524 7712 1569 -1416 -1094 A C ATOM 2729 CG PHE A 378 -15.002 -31.076 -24.309 1.00 59.39 A C ANISOU 2729 CG PHE A 378 9832 4816 7916 1869 -1401 -1264 A C ATOM 2730 CD1 PHE A 378 -14.841 -30.299 -25.448 1.00 56.63 A C ANISOU 2730 CD1 PHE A 378 9251 4694 7572 1905 -1281 -1365 A C ATOM 2731 CD2 PHE A 378 -14.064 -32.060 -24.036 1.00 62.37 A C ANISOU 2731 CD2 PHE A 378 10306 5122 8268 2073 -1483 -1295 A C ATOM 2732 CE1 PHE A 378 -13.758 -30.490 -26.291 1.00 57.15 A C ANISOU 2732 CE1 PHE A 378 9218 4872 7626 2170 -1256 -1520 A C ATOM 2733 CE2 PHE A 378 -12.979 -32.259 -24.875 1.00 63.39 A C ANISOU 2733 CE2 PHE A 378 10316 5384 8386 2326 -1455 -1440 A C ATOM 2734 CZ PHE A 378 -12.826 -31.472 -26.004 1.00 61.80 A C ANISOU 2734 CZ PHE A 378 9896 5395 8191 2368 -1336 -1550 A C ATOM 2735 N TYR A 379 -18.295 -28.455 -22.524 1.00 48.85 A N ANISOU 2735 N TYR A 379 8173 3796 6593 972 -1181 -794 A N ATOM 2736 CA TYR A 379 -19.673 -28.260 -22.081 1.00 52.13 A C ANISOU 2736 CA TYR A 379 8618 4219 6972 664 -1153 -662 A C ATOM 2737 C TYR A 379 -20.662 -28.438 -23.235 1.00 53.62 A C ANISOU 2737 C TYR A 379 8829 4428 7116 489 -1115 -702 A C ATOM 2738 O TYR A 379 -20.576 -27.740 -24.246 1.00 54.12 A O ANISOU 2738 O TYR A 379 8696 4677 7191 528 -1023 -772 A O ATOM 2739 CB TYR A 379 -19.873 -26.871 -21.471 1.00 53.04 A C ANISOU 2739 CB TYR A 379 8460 4573 7119 585 -1045 -570 A C ATOM 2740 CG TYR A 379 -18.960 -26.515 -20.319 1.00 55.35 A C ANISOU 2740 CG TYR A 379 8695 4886 7448 729 -1073 -531 A C ATOM 2741 CD1 TYR A 379 -17.823 -25.742 -20.525 1.00 54.64 A C ANISOU 2741 CD1 TYR A 379 8390 4953 7418 932 -1026 -603 A C ATOM 2742 CD2 TYR A 379 -19.248 -26.924 -19.023 1.00 57.56 A C ANISOU 2742 CD2 TYR A 379 9128 5046 7695 646 -1147 -417 A C ATOM 2743 CE1 TYR A 379 -16.992 -25.397 -19.479 1.00 53.70 A C ANISOU 2743 CE1 TYR A 379 8206 4870 7327 1050 -1059 -573 A C ATOM 2744 CE2 TYR A 379 -18.418 -26.585 -17.966 1.00 55.92 A C ANISOU 2744 CE2 TYR A 379 8866 4870 7510 777 -1180 -384 A C ATOM 2745 CZ TYR A 379 -17.292 -25.821 -18.203 1.00 56.21 A C ANISOU 2745 CZ TYR A 379 8683 5064 7610 979 -1139 -466 A C ATOM 2746 OH TYR A 379 -16.458 -25.477 -17.163 1.00 59.08 A O ANISOU 2746 OH TYR A 379 8982 5473 7991 1099 -1180 -440 A O ATOM 2747 N LEU A 380 -21.596 -29.371 -23.078 1.00 55.13 A N ANISOU 2747 N LEU A 380 9262 4436 7251 286 -1191 -654 A N ATOM 2748 CA LEU A 380 -22.703 -29.531 -24.020 1.00 54.88 A C ANISOU 2748 CA LEU A 380 9247 4439 7167 69 -1165 -673 A C ATOM 2749 C LEU A 380 -23.940 -28.827 -23.475 1.00 57.50 A C ANISOU 2749 C LEU A 380 9439 4934 7472 -207 -1094 -531 A C ATOM 2750 O LEU A 380 -24.643 -29.368 -22.623 1.00 58.27 A O ANISOU 2750 O LEU A 380 9690 4921 7528 -401 -1147 -424 A O ATOM 2751 CB LEU A 380 -23.004 -31.009 -24.267 1.00 55.90 A C ANISOU 2751 CB LEU A 380 9728 4271 7241 -7 -1297 -719 A C ATOM 2752 CG LEU A 380 -22.181 -31.733 -25.332 1.00 59.20 A C ANISOU 2752 CG LEU A 380 10279 4558 7656 220 -1353 -902 A C ATOM 2753 CD1 LEU A 380 -22.366 -33.242 -25.213 1.00 63.74 A C ANISOU 2753 CD1 LEU A 380 11259 4774 8186 165 -1508 -929 A C ATOM 2754 CD2 LEU A 380 -22.563 -31.247 -26.731 1.00 56.24 A C ANISOU 2754 CD2 LEU A 380 9736 4379 7254 176 -1266 -998 A C ATOM 2755 N SER A 381 -24.215 -27.625 -23.968 1.00 58.76 A N ANISOU 2755 N SER A 381 9313 5363 7651 -223 -973 -527 A N ATOM 2756 CA SER A 381 -25.232 -26.795 -23.341 1.00 59.12 A C ANISOU 2756 CA SER A 381 9194 5589 7681 -420 -899 -400 A C ATOM 2757 C SER A 381 -26.433 -26.497 -24.235 1.00 57.89 A C ANISOU 2757 C SER A 381 8925 5595 7474 -617 -846 -396 A C ATOM 2758 O SER A 381 -26.297 -26.258 -25.432 1.00 58.81 A O ANISOU 2758 O SER A 381 8960 5795 7591 -547 -814 -487 A O ATOM 2759 CB SER A 381 -24.605 -25.481 -22.869 1.00 60.75 A C ANISOU 2759 CB SER A 381 9154 5976 7952 -272 -807 -373 A C ATOM 2760 OG SER A 381 -25.450 -24.821 -21.940 1.00 63.60 A O ANISOU 2760 OG SER A 381 9407 6464 8295 -427 -755 -252 A O ATOM 2761 N GLN A 382 -27.614 -26.525 -23.629 1.00 56.77 A N ANISOU 2761 N GLN A 382 8776 5512 7280 -864 -839 -287 A N ATOM 2762 CA GLN A 382 -28.828 -26.044 -24.265 1.00 54.11 A C ANISOU 2762 CA GLN A 382 8277 5388 6896 -1048 -782 -262 A C ATOM 2763 C GLN A 382 -29.088 -24.605 -23.832 1.00 47.96 A C ANISOU 2763 C GLN A 382 7216 4861 6146 -1009 -668 -192 A C ATOM 2764 O GLN A 382 -28.515 -24.133 -22.848 1.00 47.88 A O ANISOU 2764 O GLN A 382 7170 4844 6180 -903 -644 -148 A O ATOM 2765 CB GLN A 382 -30.021 -26.934 -23.907 1.00 60.41 A C ANISOU 2765 CB GLN A 382 9212 6133 7609 -1354 -840 -190 A C ATOM 2766 CG GLN A 382 -30.076 -28.254 -24.664 1.00 69.82 A C ANISOU 2766 CG GLN A 382 10666 7104 8757 -1445 -950 -272 A C ATOM 2767 CD GLN A 382 -30.029 -28.070 -26.175 1.00 75.93 A C ANISOU 2767 CD GLN A 382 11362 7966 9524 -1372 -935 -396 A C ATOM 2768 NE2 GLN A 382 -30.777 -27.091 -26.679 1.00 77.33 A N ANISOU 2768 NE2 GLN A 382 11275 8426 9683 -1431 -850 -371 A N ATOM 2769 OE1 GLN A 382 -29.326 -28.797 -26.879 1.00 78.54 A O ANISOU 2769 OE1 GLN A 382 11868 8114 9857 -1254 -1001 -515 A O ATOM 2770 N ALA A 383 -29.941 -23.908 -24.573 1.00 44.95 A N ANISOU 2770 N ALA A 383 6644 4698 5737 -1084 -606 -186 A N ATOM 2771 CA ALA A 383 -30.296 -22.534 -24.242 1.00 43.02 A C ANISOU 2771 CA ALA A 383 6148 4684 5515 -1041 -505 -125 A C ATOM 2772 C ALA A 383 -31.123 -22.510 -22.966 1.00 46.37 A C ANISOU 2772 C ALA A 383 6550 5171 5898 -1199 -491 -17 A C ATOM 2773 O ALA A 383 -32.138 -23.199 -22.870 1.00 50.71 A O ANISOU 2773 O ALA A 383 7153 5744 6370 -1429 -523 26 A O ATOM 2774 CB ALA A 383 -31.060 -21.879 -25.395 1.00 40.06 A C ANISOU 2774 CB ALA A 383 5593 4519 5110 -1074 -459 -142 A C ATOM 2775 N ALA A 384 -30.692 -21.713 -21.994 1.00 43.20 A N ANISOU 2775 N ALA A 384 6067 4809 5539 -1086 -440 25 A N ATOM 2776 CA ALA A 384 -31.309 -21.720 -20.671 1.00 42.78 A C ANISOU 2776 CA ALA A 384 6010 4808 5437 -1211 -424 120 A C ATOM 2777 C ALA A 384 -31.995 -20.403 -20.314 1.00 42.31 A C ANISOU 2777 C ALA A 384 5704 5002 5371 -1187 -323 162 A C ATOM 2778 O ALA A 384 -31.856 -19.400 -21.012 1.00 41.55 A O ANISOU 2778 O ALA A 384 5453 5013 5323 -1051 -270 124 A O ATOM 2779 CB ALA A 384 -30.264 -22.060 -19.615 1.00 41.99 A C ANISOU 2779 CB ALA A 384 6062 4523 5368 -1110 -467 133 A C ATOM 2780 N ASP A 385 -32.733 -20.417 -19.209 1.00 44.39 A N ANISOU 2780 N ASP A 385 5941 5359 5567 -1316 -298 242 A N ATOM 2781 CA ASP A 385 -33.443 -19.231 -18.747 1.00 46.95 A C ANISOU 2781 CA ASP A 385 6041 5925 5871 -1284 -204 274 A C ATOM 2782 C ASP A 385 -32.491 -18.200 -18.149 1.00 42.16 A C ANISOU 2782 C ASP A 385 5389 5290 5341 -1061 -164 249 A C ATOM 2783 O ASP A 385 -31.331 -18.497 -17.868 1.00 40.36 A O ANISOU 2783 O ASP A 385 5296 4874 5167 -961 -211 223 A O ATOM 2784 CB ASP A 385 -34.503 -19.612 -17.711 1.00 54.41 A C ANISOU 2784 CB ASP A 385 6969 6997 6705 -1492 -183 360 A C ATOM 2785 CG ASP A 385 -35.703 -20.297 -18.325 1.00 58.47 A C ANISOU 2785 CG ASP A 385 7448 7630 7136 -1731 -201 388 A C ATOM 2786 OD1 ASP A 385 -36.133 -19.883 -19.418 1.00 60.16 A O ANISOU 2786 OD1 ASP A 385 7529 7966 7365 -1703 -187 347 A O ATOM 2787 OD2 ASP A 385 -36.225 -21.246 -17.709 1.00 61.73 A O1- ANISOU 2787 OD2 ASP A 385 7969 8023 7464 -1959 -232 455 A O1- ATOM 2788 N GLY A 386 -32.991 -16.985 -17.965 1.00 39.37 A N ANISOU 2788 N GLY A 386 4844 5127 4988 -983 -84 253 A N ATOM 2789 CA GLY A 386 -32.217 -15.932 -17.341 1.00 38.51 A C ANISOU 2789 CA GLY A 386 4692 5000 4942 -797 -46 228 A C ATOM 2790 C GLY A 386 -32.440 -15.946 -15.839 1.00 43.76 A C ANISOU 2790 C GLY A 386 5380 5708 5540 -847 -27 273 A C ATOM 2791 O GLY A 386 -32.837 -16.964 -15.275 1.00 46.60 A O ANISOU 2791 O GLY A 386 5841 6046 5818 -1016 -59 329 A O ATOM 2792 N ALA A 387 -32.196 -14.810 -15.195 1.00 40.60 A N ANISOU 2792 N ALA A 387 4894 5367 5164 -706 24 250 A N ATOM 2793 CA ALA A 387 -32.261 -14.717 -13.745 1.00 38.62 A C ANISOU 2793 CA ALA A 387 4669 5159 4847 -725 43 277 A C ATOM 2794 C ALA A 387 -33.627 -15.125 -13.184 1.00 41.61 A C ANISOU 2794 C ALA A 387 4985 5733 5091 -906 85 343 A C ATOM 2795 O ALA A 387 -34.660 -14.706 -13.687 1.00 45.32 A O ANISOU 2795 O ALA A 387 5295 6395 5530 -932 139 345 A O ATOM 2796 CB ALA A 387 -31.912 -13.305 -13.307 1.00 35.91 A C ANISOU 2796 CB ALA A 387 4231 4863 4549 -543 95 224 A C ATOM 2797 N LYS A 388 -33.624 -15.947 -12.140 1.00 43.20 A N ANISOU 2797 N LYS A 388 5309 5899 5207 -1032 60 402 A N ATOM 2798 CA LYS A 388 -34.870 -16.377 -11.510 1.00 46.35 A C ANISOU 2798 CA LYS A 388 5650 6496 5463 -1230 105 474 A C ATOM 2799 C LYS A 388 -34.852 -16.221 -9.990 1.00 47.60 A C ANISOU 2799 C LYS A 388 5839 6722 5524 -1238 138 506 A C ATOM 2800 O LYS A 388 -33.788 -16.122 -9.374 1.00 44.91 A O ANISOU 2800 O LYS A 388 5617 6227 5220 -1127 96 486 A O ATOM 2801 CB LYS A 388 -35.174 -17.832 -11.873 1.00 47.88 A C ANISOU 2801 CB LYS A 388 5986 6597 5610 -1466 38 543 A C ATOM 2802 CG LYS A 388 -35.739 -18.013 -13.283 1.00 47.52 A C ANISOU 2802 CG LYS A 388 5861 6594 5601 -1527 28 521 A C ATOM 2803 CD LYS A 388 -36.075 -19.467 -13.557 1.00 49.35 A C ANISOU 2803 CD LYS A 388 6253 6723 5776 -1781 -45 582 A C ATOM 2804 N VAL A 389 -36.040 -16.210 -9.394 1.00 50.68 A N ANISOU 2804 N VAL A 389 6111 7366 5780 -1371 213 553 A N ATOM 2805 CA VAL A 389 -36.176 -16.102 -7.944 1.00 50.40 A C ANISOU 2805 CA VAL A 389 6092 7437 5621 -1399 256 587 A C ATOM 2806 C VAL A 389 -37.044 -17.223 -7.374 1.00 51.87 A C ANISOU 2806 C VAL A 389 6329 7731 5648 -1693 264 705 A C ATOM 2807 O VAL A 389 -38.078 -17.576 -7.947 1.00 50.58 A O ANISOU 2807 O VAL A 389 6056 7725 5437 -1860 294 740 A O ATOM 2808 CB VAL A 389 -36.779 -14.746 -7.534 1.00 50.44 A C ANISOU 2808 CB VAL A 389 5881 7695 5590 -1243 363 517 A C ATOM 2809 N LEU A 390 -36.615 -17.785 -6.246 1.00 52.55 A N ANISOU 2809 N LEU A 390 6584 7737 5647 -1766 234 771 A N ATOM 2810 CA LEU A 390 -37.416 -18.774 -5.531 1.00 54.62 A C ANISOU 2810 CA LEU A 390 6907 8108 5736 -2055 250 898 A C ATOM 2811 C LEU A 390 -37.498 -18.423 -4.055 1.00 58.30 A C ANISOU 2811 C LEU A 390 7365 8731 6057 -2043 312 925 A C ATOM 2812 O LEU A 390 -36.478 -18.208 -3.404 1.00 60.60 A O ANISOU 2812 O LEU A 390 7786 8869 6373 -1894 264 901 A O ATOM 2813 CB LEU A 390 -36.843 -20.183 -5.698 1.00 53.71 A C ANISOU 2813 CB LEU A 390 7079 7692 5636 -2217 125 988 A C ATOM 2814 CG LEU A 390 -37.586 -21.244 -4.880 1.00 57.96 A C ANISOU 2814 CG LEU A 390 7726 8307 5991 -2538 130 1138 A C ATOM 2815 CD1 LEU A 390 -39.051 -21.312 -5.294 1.00 61.98 A C ANISOU 2815 CD1 LEU A 390 8023 9116 6412 -2763 217 1169 A C ATOM 2816 CD2 LEU A 390 -36.926 -22.614 -4.994 1.00 56.98 A C ANISOU 2816 CD2 LEU A 390 7929 7836 5885 -2670 -9 1225 A C ATOM 2817 N CYS A 391 -38.716 -18.360 -3.531 1.00 59.18 A N ANISOU 2817 N CYS A 391 7314 9167 6006 -2200 418 972 A N ATOM 2818 CA CYS A 391 -38.915 -18.083 -2.116 1.00 59.68 A C ANISOU 2818 CA CYS A 391 7359 9417 5899 -2211 490 1000 A C ATOM 2819 C CYS A 391 -38.771 -19.369 -1.312 1.00 60.05 A C ANISOU 2819 C CYS A 391 7651 9351 5813 -2467 430 1157 A C ATOM 2820 O CYS A 391 -39.355 -20.394 -1.655 1.00 61.68 A O ANISOU 2820 O CYS A 391 7921 9545 5969 -2743 407 1265 A O ATOM 2821 CB CYS A 391 -40.286 -17.445 -1.879 1.00 61.59 A C ANISOU 2821 CB CYS A 391 7306 10087 6009 -2255 638 977 A C ATOM 2822 SG CYS A 391 -40.572 -15.941 -2.853 1.00 59.49 A S ANISOU 2822 SG CYS A 391 6763 9952 5887 -1945 699 804 A S ATOM 2823 N LEU A 392 -37.977 -19.314 -0.250 1.00 61.43 A N ANISOU 2823 N LEU A 392 7978 9434 5929 -2379 397 1172 A N ATOM 2824 CA LEU A 392 -37.756 -20.481 0.597 1.00 63.36 A C ANISOU 2824 CA LEU A 392 8479 9555 6039 -2595 330 1330 A C ATOM 2825 C LEU A 392 -38.551 -20.354 1.889 1.00 65.49 A C ANISOU 2825 C LEU A 392 8667 10153 6063 -2729 445 1397 A C ATOM 2826 O LEU A 392 -38.960 -19.255 2.262 1.00 66.47 A O ANISOU 2826 O LEU A 392 8566 10552 6139 -2579 558 1293 A O ATOM 2827 CB LEU A 392 -36.267 -20.655 0.903 1.00 60.87 A C ANISOU 2827 CB LEU A 392 8411 8906 5811 -2412 195 1317 A C ATOM 2828 CG LEU A 392 -35.316 -20.624 -0.297 1.00 59.59 A C ANISOU 2828 CG LEU A 392 8310 8444 5889 -2227 90 1226 A C ATOM 2829 CD1 LEU A 392 -33.882 -20.883 0.152 1.00 61.51 A C ANISOU 2829 CD1 LEU A 392 8783 8400 6187 -2065 -43 1225 A C ATOM 2830 CD2 LEU A 392 -35.741 -21.617 -1.380 1.00 55.98 A C ANISOU 2830 CD2 LEU A 392 7924 7855 5492 -2424 42 1287 A C ATOM 2831 OXT LEU A 392 -38.804 -21.339 2.582 1.00 65.57 A O1- ANISOU 2831 OXT LEU A 392 8840 10162 5913 -2988 426 1556 A O1- TER HETATM 2832 C1 GAL A 401 -16.659 -9.964 -23.198 1.00 43.80 E C ANISOU 2832 C1 GAL A 401 4875 5287 6478 471 41 -352 E C HETATM 2833 O1 GAL A 401 -15.548 -10.388 -22.511 1.00 53.63 E O ANISOU 2833 O1 GAL A 401 6095 6534 7749 537 -13 -411 E O HETATM 2834 C2 GAL A 401 -17.268 -8.688 -22.610 1.00 37.57 E C ANISOU 2834 C2 GAL A 401 4083 4475 5718 398 69 -292 E C HETATM 2835 O2 GAL A 401 -17.650 -8.855 -21.268 1.00 36.31 E O ANISOU 2835 O2 GAL A 401 3988 4248 5558 397 16 -291 E O HETATM 2836 C3 GAL A 401 -18.540 -8.328 -23.403 1.00 36.13 E C ANISOU 2836 C3 GAL A 401 3926 4303 5500 354 118 -228 E C HETATM 2837 O3 GAL A 401 -19.108 -7.090 -22.964 1.00 32.77 E O ANISOU 2837 O3 GAL A 401 3499 3853 5098 315 144 -177 E O HETATM 2838 C4 GAL A 401 -18.227 -8.228 -24.918 1.00 33.85 E C ANISOU 2838 C4 GAL A 401 3579 4093 5188 353 173 -221 E C HETATM 2839 O4 GAL A 401 -17.523 -7.046 -25.218 1.00 37.00 E O ANISOU 2839 O4 GAL A 401 3905 4527 5625 316 221 -195 E O HETATM 2840 C5 GAL A 401 -17.383 -9.428 -25.366 1.00 38.62 E C ANISOU 2840 C5 GAL A 401 4174 4731 5770 419 149 -298 E C HETATM 2841 O5 GAL A 401 -16.261 -9.675 -24.499 1.00 43.98 E O ANISOU 2841 O5 GAL A 401 4822 5399 6490 468 105 -355 E O HETATM 2842 C6 GAL A 401 -16.783 -9.275 -26.746 1.00 34.99 E C ANISOU 2842 C6 GAL A 401 3637 4376 5281 426 211 -309 E C HETATM 2843 O6 GAL A 401 -17.671 -9.772 -27.704 1.00 34.73 E O ANISOU 2843 O6 GAL A 401 3653 4363 5181 420 224 -296 E O HETATM 2844 O01 HFK A 402 -9.720 -12.546 -11.460 1.00 43.93 F O HETATM 2845 C02 HFK A 402 -10.463 -12.965 -12.504 1.00 42.61 F C HETATM 2846 C03 HFK A 402 -10.179 -11.992 -13.684 1.00 38.06 F C HETATM 2847 C04 HFK A 402 -10.915 -12.398 -14.929 1.00 38.74 F C HETATM 2848 C05 HFK A 402 -12.461 -12.621 -14.667 1.00 36.16 F C HETATM 2849 C06 HFK A 402 -12.778 -13.440 -13.406 1.00 42.32 F C HETATM 2850 C07 HFK A 402 -12.002 -13.010 -12.166 1.00 45.41 F C HETATM 2851 C08 HFK A 402 -12.395 -13.761 -10.884 1.00 47.49 F C HETATM 2852 C09 HFK A 402 -11.682 -15.102 -11.227 1.00 53.91 F C HETATM 2853 C10 HFK A 402 -11.041 -15.751 -10.030 1.00 56.99 F C HETATM 2854 C11 HFK A 402 -11.835 -15.578 -8.762 1.00 57.15 F C HETATM 2855 C12 HFK A 402 -11.982 -14.083 -8.378 1.00 51.23 F C HETATM 2856 C13 HFK A 402 -11.965 -13.158 -9.567 1.00 50.37 F C HETATM 2857 N14 HFK A 402 -13.691 -14.479 -11.049 1.00 47.44 F N HETATM 2858 C15 HFK A 402 -14.680 -13.647 -11.797 1.00 45.72 F C HETATM 2859 N16 HFK A 402 -14.228 -13.426 -13.241 1.00 43.97 F N HETATM 2860 N17 HFK A 402 -15.870 -14.208 -11.876 1.00 42.45 F N HETATM 2861 C18 HFK A 402 -16.567 -14.829 -10.749 1.00 40.76 F C HETATM 2862 N19 HFK A 402 -17.785 -15.298 -10.851 1.00 40.59 F N HETATM 2863 C20 HFK A 402 -18.169 -15.835 -9.602 1.00 40.26 F C HETATM 2864 C21 HFK A 402 -17.073 -15.638 -8.729 1.00 41.15 F C HETATM 2865 O22 HFK A 402 -16.099 -15.015 -9.464 1.00 44.23 F O HETATM 2866 C23 HFK A 402 -17.172 -16.102 -7.351 1.00 36.96 F C HETATM 2867 C24 HFK A 402 -18.315 -16.709 -6.913 1.00 36.54 F C HETATM 2868 C25 HFK A 402 -19.446 -16.910 -7.819 1.00 40.06 F C HETATM 2869 C26 HFK A 402 -19.359 -16.468 -9.156 1.00 40.20 F C HETATM 2870 C1 J4Q A 403 -10.936 -9.927 -10.152 1.00153.58 G C HETATM 2871 N1 J4Q A 403 -9.124 -8.213 -8.218 1.00 94.73 G N HETATM 2872 O1 J4Q A 403 -12.600 -7.927 -9.450 1.00 92.91 G O HETATM 2873 S1 J4Q A 403 -11.220 -8.176 -10.020 1.00 93.86 G S HETATM 2874 C2 J4Q A 403 -9.982 -7.487 -8.922 1.00 91.92 G C HETATM 2875 N2 J4Q A 403 -9.777 -6.188 -8.689 1.00 89.00 G N HETATM 2876 O2 J4Q A 403 -11.096 -7.568 -11.405 1.00 94.71 G O HETATM 2877 S2 J4Q A 403 -8.567 -3.031 -11.491 1.00121.95 G S HETATM 2878 C3 J4Q A 403 -8.341 -7.388 -7.505 1.00 95.27 G C HETATM 2879 N3 J4Q A 403 -10.415 -2.618 -10.042 1.00 98.80 G N HETATM 2880 C4 J4Q A 403 -8.766 -6.082 -7.815 1.00 93.20 G C HETATM 2881 C5 J4Q A 403 -10.495 -5.103 -9.266 1.00 85.37 G C HETATM 2882 C6 J4Q A 403 -9.578 -4.076 -9.619 1.00 85.41 G C HETATM 2883 C7 J4Q A 403 -8.880 -4.426 -10.718 1.00 87.19 G C HETATM 2884 C8 J4Q A 403 -9.555 -1.919 -10.784 1.00 99.81 G C HETATM 2885 O HOH A 501 -22.796 0.958 -47.300 1.00 47.59 O O HETATM 2886 O HOH A 502 -10.680 -17.436 -19.198 1.00 58.72 O O HETATM 2887 O HOH A 503 -20.471 -15.811 8.536 1.00 51.13 O O HETATM 2888 O HOH A 504 -5.932 3.270 -43.042 1.00 63.96 O O HETATM 2889 O HOH A 505 -14.314 -25.403 -17.873 1.00 69.81 O O HETATM 2890 O HOH A 506 -34.239 -1.896 -32.945 1.00 47.28 O O HETATM 2891 O HOH A 507 -16.118 8.776 3.997 1.00 67.69 O O HETATM 2892 O HOH A 508 -5.656 -32.407 -25.182 1.00 63.58 O O HETATM 2893 O HOH A 509 -16.679 -25.692 -28.909 1.00 44.48 O O HETATM 2894 O HOH A 510 -15.061 -5.898 4.664 1.00 50.34 O O HETATM 2895 O HOH A 511 -30.432 -4.188 7.884 1.00 40.54 O O HETATM 2896 O HOH A 512 -18.026 2.043 -31.917 1.00 45.29 O O HETATM 2897 O HOH A 513 -27.458 3.671 -5.290 1.00 63.55 O O HETATM 2898 O HOH A 514 -22.166 5.672 -0.815 1.00 46.44 O O HETATM 2899 O HOH A 515 -19.783 -14.032 6.265 1.00 36.12 O O HETATM 2900 O HOH A 516 -18.663 -11.524 -16.937 1.00 47.45 O O HETATM 2901 O HOH A 517 -3.129 -6.746 -30.369 1.00 56.26 O O HETATM 2902 O HOH A 518 -14.755 -10.017 7.286 1.00 48.53 O O HETATM 2903 O HOH A 519 -14.008 -9.459 -14.090 1.00 40.10 O O HETATM 2904 O HOH A 520 -36.940 -12.761 -21.423 1.00 56.90 O O HETATM 2905 O HOH A 521 -2.134 -4.669 -23.642 1.00 43.34 O O HETATM 2906 O HOH A 522 -33.765 -9.838 -11.976 1.00 56.44 O O HETATM 2907 O HOH A 523 -28.782 1.728 -14.488 1.00 47.30 O O HETATM 2908 O HOH A 524 -24.424 -23.534 12.549 1.00 50.56 O O HETATM 2909 O HOH A 525 -13.885 -7.074 -1.984 1.00 44.97 O O HETATM 2910 O HOH A 526 -20.704 -7.550 -20.834 1.00 44.15 O O HETATM 2911 O HOH A 527 -29.501 1.864 -2.155 1.00 57.49 O O HETATM 2912 O HOH A 528 -27.413 3.139 -10.419 1.00 46.15 O O HETATM 2913 O HOH A 529 -20.896 -20.245 11.799 1.00 41.29 O O HETATM 2914 O HOH A 530 -24.895 4.936 -33.009 1.00 50.39 O O HETATM 2915 O HOH A 531 -22.372 -2.151 -24.752 1.00 36.62 O O HETATM 2916 O HOH A 532 -35.320 -5.303 -24.765 1.00 51.33 O O HETATM 2917 O HOH A 533 -31.835 -0.362 -12.315 1.00 56.88 O O HETATM 2918 O HOH A 534 -14.799 -17.566 -23.750 1.00 41.10 O O HETATM 2919 O HOH A 535 -23.876 -12.707 11.766 1.00 46.52 O O HETATM 2920 O HOH A 536 -13.374 -25.291 -31.302 1.00 45.11 O O HETATM 2921 O HOH A 537 -20.104 -8.117 -28.664 1.00 35.22 O O HETATM 2922 O HOH A 538 -38.622 -0.715 -2.947 1.00 63.21 O O HETATM 2923 O HOH A 539 -3.433 -32.792 -24.784 1.00 71.02 O O HETATM 2924 O HOH A 540 -20.160 2.144 5.169 1.00 45.61 O O HETATM 2925 O HOH A 541 -16.747 -17.397 -16.697 1.00 55.80 O O HETATM 2926 O HOH A 542 -8.777 9.241 -33.526 1.00 58.44 O O HETATM 2927 O HOH A 543 -16.019 -13.164 -15.447 1.00 42.85 O O HETATM 2928 O HOH A 544 -18.895 -9.222 -18.067 1.00 42.40 O O HETATM 2929 O HOH A 545 -31.045 -18.145 -23.484 1.00 43.14 O O HETATM 2930 O HOH A 546 -29.218 0.698 -39.041 1.00 54.11 O O HETATM 2931 O HOH A 547 -26.608 -7.408 14.891 1.00 42.12 O O HETATM 2932 O HOH A 548 -27.668 3.719 -39.139 1.00 57.73 O O HETATM 2933 O HOH A 549 -37.766 -5.060 -8.552 1.00 42.87 O O HETATM 2934 O HOH A 550 -17.422 -22.723 -10.343 1.00 62.14 O O HETATM 2935 O HOH A 551 -9.964 -20.376 -19.654 1.00 62.92 O O HETATM 2936 O HOH A 552 -12.775 -10.730 -17.613 1.00 53.18 O O HETATM 2937 O HOH A 553 -32.001 -16.541 8.058 1.00 54.76 O O HETATM 2938 O HOH A 554 -17.250 -1.233 4.062 1.00 61.37 O O HETATM 2939 O HOH A 555 -0.880 -1.228 -31.012 1.00 53.61 O O HETATM 2940 O HOH A 556 -11.084 -18.937 3.270 1.00 59.70 O O HETATM 2941 O HOH A 557 -15.538 -1.425 1.147 1.00 41.68 O O HETATM 2942 O HOH A 558 -30.859 -18.889 -13.662 1.00 45.40 O O HETATM 2943 O HOH A 559 -11.754 -14.475 -19.870 1.00 62.79 O O HETATM 2944 O HOH A 560 -14.145 -22.590 -11.482 1.00 51.37 O O HETATM 2945 O HOH A 561 -10.403 12.724 -39.978 1.00 57.92 O O HETATM 2946 O HOH A 562 -22.498 -3.444 -41.470 1.00 58.97 O O HETATM 2947 O HOH A 563 -16.696 -12.082 -19.265 1.00 61.08 O O HETATM 2948 O HOH A 564 -24.336 0.452 7.395 1.00 66.28 O O HETATM 2949 O HOH A 565 -19.500 1.049 -21.629 1.00 59.74 O O HETATM 2950 O HOH A 566 -21.226 0.031 -23.361 1.00 34.75 O O HETATM 2951 O HOH A 567 -15.252 -15.111 -17.441 1.00 28.06 O O HETATM 2952 O HOH A 568 -25.670 4.928 -6.263 1.00 48.49 O O HETATM 2953 O HOH A 569 -2.466 -32.749 -22.863 1.00 57.12 O O HETATM 2954 O HOH A 570 -29.745 2.221 1.097 1.00 45.10 O O HETATM 2955 O HOH A 571 -23.270 5.340 -6.039 1.00 56.45 O O HETATM 2956 O HOH A 572 -16.865 -8.706 -17.986 1.00 64.32 O O HETATM 2957 O HOH A 573 -30.290 -3.825 15.023 1.00 61.82 O O HETATM 2958 O HOH A 574 -34.533 -9.003 -14.658 1.00 49.28 O O HETATM 2959 O HOH A 575 -19.839 -26.197 -6.713 1.00 65.38 O O HETATM 2960 O HOH A 576 -32.161 -24.808 -44.235 1.00 61.36 O O HETATM 2961 O HOH A 577 -14.659 -11.074 -16.691 1.00 35.03 O O HETATM 2962 O HOH A 578 -19.960 -26.954 -9.689 1.00 69.42 O O HETATM 2963 O HOH A 579 -32.405 -23.119 -45.672 1.00 54.36 O O HETATM 2964 O HOH A 580 -25.178 4.822 -0.795 1.00 56.39 O O HETATM 2965 O HOH A 581 -28.641 -2.279 15.427 1.00 72.74 O O CONECT 2832 2833 2834 2841 CONECT 2833 2832 CONECT 2834 2832 2835 2836 CONECT 2835 2834 CONECT 2836 2834 2837 2838 CONECT 2837 2836 CONECT 2838 2836 2839 2840 CONECT 2839 2838 CONECT 2840 2838 2841 2842 CONECT 2841 2832 2840 CONECT 2842 2840 2843 CONECT 2843 2842 CONECT 2844 2845 CONECT 2845 2844 2846 2850 CONECT 2846 2845 2847 CONECT 2847 2846 2848 CONECT 2848 2847 2849 CONECT 2849 2848 2850 2859 CONECT 2850 2845 2849 2851 CONECT 2851 2850 2852 2857 2856 CONECT 2852 2851 2853 CONECT 2853 2852 2854 CONECT 2854 2853 2855 CONECT 2855 2854 2856 CONECT 2856 2851 2855 CONECT 2857 2851 2858 CONECT 2858 2857 2859 2860 CONECT 2859 2849 2858 CONECT 2860 2858 2861 CONECT 2861 2860 2862 2865 CONECT 2862 2861 2863 CONECT 2863 2862 2864 2869 CONECT 2864 2863 2865 2866 CONECT 2865 2861 2864 CONECT 2866 2864 2867 CONECT 2867 2866 2868 CONECT 2868 2867 2869 CONECT 2869 2863 2868 CONECT 2870 2873 CONECT 2871 2874 2878 CONECT 2872 2873 CONECT 2873 2870 2872 2874 2876 CONECT 2874 2871 2873 2875 CONECT 2875 2874 2880 2881 CONECT 2876 2873 CONECT 2877 2883 2884 CONECT 2878 2871 2880 CONECT 2879 2882 2884 CONECT 2880 2875 2878 CONECT 2881 2875 2882 CONECT 2882 2879 2881 2883 CONECT 2883 2882 2877 CONECT 2884 2879 2877 END