ATOM 1 N LYS A 3 25.309 36.758 47.985 1.00 31.66 N ANISOU 1 N LYS A 3 4004 4034 3988 -55 2 -21 N ATOM 2 CA LYS A 3 24.176 36.396 48.882 1.00 31.28 C ANISOU 2 CA LYS A 3 3957 3972 3956 -17 -4 -17 C ATOM 3 C LYS A 3 24.642 36.233 50.324 1.00 30.62 C ANISOU 3 C LYS A 3 3837 3890 3905 8 0 -40 C ATOM 4 O LYS A 3 25.688 35.635 50.598 1.00 31.62 O ANISOU 4 O LYS A 3 3897 4025 4093 41 -20 -42 O ATOM 5 CB LYS A 3 23.506 35.105 48.403 1.00 31.59 C ANISOU 5 CB LYS A 3 4015 4010 3976 -31 -32 -33 C ATOM 6 N GLN A 4 23.857 36.758 51.250 1.00 28.31 N ANISOU 6 N GLN A 4 3574 3576 3607 2 16 -26 N ATOM 7 CA GLN A 4 24.122 36.568 52.666 1.00 25.84 C ANISOU 7 CA GLN A 4 3283 3237 3299 -24 21 -48 C ATOM 8 C GLN A 4 22.832 36.175 53.376 1.00 23.11 C ANISOU 8 C GLN A 4 2994 2852 2933 -6 19 -55 C ATOM 9 O GLN A 4 21.736 36.338 52.843 1.00 22.85 O ANISOU 9 O GLN A 4 2939 2853 2888 -41 31 -49 O ATOM 10 CB GLN A 4 24.717 37.839 53.289 1.00 26.47 C ANISOU 10 CB GLN A 4 3373 3320 3362 -2 21 -43 C ATOM 11 CG GLN A 4 23.888 39.094 53.078 1.00 26.97 C ANISOU 11 CG GLN A 4 3417 3346 3481 -5 -10 -50 C ATOM 12 CD GLN A 4 24.528 40.311 53.694 1.00 27.10 C ANISOU 12 CD GLN A 4 3388 3398 3511 -47 60 -61 C ATOM 13 OE1 GLN A 4 25.726 40.553 53.503 1.00 27.86 O ANISOU 13 OE1 GLN A 4 3320 3582 3680 31 141 -73 O ATOM 14 NE2 GLN A 4 23.739 41.087 54.448 1.00 24.88 N ANISOU 14 NE2 GLN A 4 3153 3090 3208 -80 133 -66 N ATOM 15 N LEU A 5 22.980 35.660 54.583 1.00 19.63 N ANISOU 15 N LEU A 5 2605 2342 2511 0 40 -130 N ATOM 16 CA LEU A 5 21.844 35.338 55.420 1.00 17.18 C ANISOU 16 CA LEU A 5 2264 2018 2245 -2 13 -123 C ATOM 17 C LEU A 5 21.159 36.618 55.915 1.00 14.71 C ANISOU 17 C LEU A 5 1973 1756 1859 -9 35 -65 C ATOM 18 O LEU A 5 21.793 37.679 56.003 1.00 14.66 O ANISOU 18 O LEU A 5 2075 1652 1843 -120 134 -141 O ATOM 19 CB LEU A 5 22.321 34.573 56.635 1.00 17.90 C ANISOU 19 CB LEU A 5 2346 2135 2318 -1 3 -109 C ATOM 20 CG LEU A 5 22.805 33.132 56.481 1.00 19.69 C ANISOU 20 CG LEU A 5 2601 2313 2566 45 -35 -120 C ATOM 21 CD1 LEU A 5 23.242 32.614 57.834 1.00 20.60 C ANISOU 21 CD1 LEU A 5 2763 2372 2692 56 -18 -27 C ATOM 22 CD2 LEU A 5 21.698 32.274 55.919 1.00 20.55 C ANISOU 22 CD2 LEU A 5 2602 2492 2714 15 -12 -51 C ATOM 23 N PRO A 6 19.875 36.532 56.271 1.00 12.13 N ANISOU 23 N PRO A 6 1733 1392 1484 26 10 -28 N ATOM 24 CA PRO A 6 19.286 37.685 56.973 1.00 10.84 C ANISOU 24 CA PRO A 6 1571 1207 1341 42 11 -77 C ATOM 25 C PRO A 6 20.105 38.050 58.206 1.00 10.19 C ANISOU 25 C PRO A 6 1463 1083 1325 49 -20 -75 C ATOM 26 O PRO A 6 20.569 37.158 58.921 1.00 10.55 O ANISOU 26 O PRO A 6 1650 973 1383 65 -43 -229 O ATOM 27 CB PRO A 6 17.900 37.192 57.390 1.00 10.44 C ANISOU 27 CB PRO A 6 1545 1079 1341 66 0 -42 C ATOM 28 CG PRO A 6 17.569 36.099 56.341 1.00 11.01 C ANISOU 28 CG PRO A 6 1580 1339 1264 -5 33 -80 C ATOM 29 CD PRO A 6 18.910 35.436 56.071 1.00 11.71 C ANISOU 29 CD PRO A 6 1652 1391 1405 91 -32 -42 C ATOM 30 N ASN A 7 20.227 39.358 58.464 1.00 10.33 N ANISOU 30 N ASN A 7 1481 1125 1319 14 19 -172 N ATOM 31 CA ASN A 7 20.895 39.860 59.643 1.00 10.57 C ANISOU 31 CA ASN A 7 1416 1238 1360 36 -26 -61 C ATOM 32 C ASN A 7 19.998 39.685 60.859 1.00 10.26 C ANISOU 32 C ASN A 7 1375 1210 1310 37 -70 -91 C ATOM 33 O ASN A 7 18.777 39.704 60.747 1.00 10.22 O ANISOU 33 O ASN A 7 1436 1137 1310 66 -155 -116 O ATOM 34 CB ASN A 7 21.179 41.358 59.497 1.00 10.95 C ANISOU 34 CB ASN A 7 1483 1275 1402 11 -41 -56 C ATOM 35 CG ASN A 7 22.249 41.688 58.473 1.00 11.30 C ANISOU 35 CG ASN A 7 1583 1274 1434 0 -18 -74 C ATOM 36 OD1 ASN A 7 22.068 42.629 57.675 1.00 14.44 O ANISOU 36 OD1 ASN A 7 1996 1709 1781 12 -162 134 O ATOM 37 ND2 ASN A 7 23.380 40.979 58.505 1.00 10.24 N ANISOU 37 ND2 ASN A 7 1422 1084 1381 -174 -99 -6 N ATOM 38 N LEU A 8 20.624 39.511 62.022 1.00 9.86 N ANISOU 38 N LEU A 8 1328 1126 1291 73 -88 3 N ATOM 39 CA LEU A 8 19.987 39.703 63.293 1.00 9.79 C ANISOU 39 CA LEU A 8 1297 1170 1252 6 -89 -110 C ATOM 40 C LEU A 8 20.424 41.068 63.822 1.00 9.57 C ANISOU 40 C LEU A 8 1257 1087 1290 -66 -50 -63 C ATOM 41 O LEU A 8 21.616 41.317 64.007 1.00 10.03 O ANISOU 41 O LEU A 8 1313 1205 1290 40 -172 -198 O ATOM 42 CB LEU A 8 20.407 38.624 64.290 1.00 9.89 C ANISOU 42 CB LEU A 8 1408 1037 1310 6 -80 -74 C ATOM 43 CG LEU A 8 19.909 38.866 65.724 1.00 10.11 C ANISOU 43 CG LEU A 8 1381 1167 1292 -8 -40 116 C ATOM 44 CD1 LEU A 8 18.399 39.111 65.812 1.00 11.56 C ANISOU 44 CD1 LEU A 8 1580 1300 1510 -35 -32 148 C ATOM 45 CD2 LEU A 8 20.311 37.750 66.643 1.00 10.67 C ANISOU 45 CD2 LEU A 8 1631 1135 1286 -23 -136 132 C ATOM 46 N GLN A 9 19.441 41.919 64.077 1.00 9.12 N ANISOU 46 N GLN A 9 1283 971 1210 -111 -110 -218 N ATOM 47 CA GLN A 9 19.652 43.259 64.623 1.00 8.65 C ANISOU 47 CA GLN A 9 1266 863 1156 -37 -31 -110 C ATOM 48 C GLN A 9 19.003 43.346 65.987 1.00 9.18 C ANISOU 48 C GLN A 9 1301 920 1264 -22 -53 -60 C ATOM 49 O GLN A 9 17.904 42.839 66.175 1.00 9.28 O ANISOU 49 O GLN A 9 1422 766 1338 -81 -129 -54 O ATOM 50 CB GLN A 9 19.080 44.285 63.664 1.00 8.44 C ANISOU 50 CB GLN A 9 1117 950 1138 -14 -32 -144 C ATOM 51 CG GLN A 9 19.033 45.688 64.173 1.00 8.00 C ANISOU 51 CG GLN A 9 1264 680 1095 45 -19 -26 C ATOM 52 CD GLN A 9 18.707 46.687 63.054 1.00 9.30 C ANISOU 52 CD GLN A 9 1409 1154 968 -99 106 31 C ATOM 53 OE1 GLN A 9 19.081 46.466 61.918 1.00 9.34 O ANISOU 53 OE1 GLN A 9 1570 963 1013 -141 133 -162 O ATOM 54 NE2 GLN A 9 18.025 47.766 63.385 1.00 8.14 N ANISOU 54 NE2 GLN A 9 1343 534 1213 -203 -2 55 N ATOM 55 N VAL A 10 19.676 44.019 66.924 1.00 9.44 N ANISOU 55 N VAL A 10 1379 886 1319 -81 -23 -57 N ATOM 56 CA VAL A 10 19.072 44.318 68.224 1.00 9.66 C ANISOU 56 CA VAL A 10 1438 961 1270 -59 -3 -55 C ATOM 57 C VAL A 10 18.823 45.820 68.353 1.00 9.32 C ANISOU 57 C VAL A 10 1397 861 1283 -29 32 -76 C ATOM 58 O VAL A 10 19.724 46.627 68.118 1.00 9.39 O ANISOU 58 O VAL A 10 1367 942 1256 -110 11 -99 O ATOM 59 CB VAL A 10 19.931 43.824 69.436 1.00 9.67 C ANISOU 59 CB VAL A 10 1445 916 1312 29 -6 29 C ATOM 60 CG1 VAL A 10 21.307 44.505 69.479 1.00 11.86 C ANISOU 60 CG1 VAL A 10 1599 1426 1479 21 -38 -134 C ATOM 61 CG2 VAL A 10 19.211 44.067 70.734 1.00 10.84 C ANISOU 61 CG2 VAL A 10 1569 1068 1480 129 19 68 C ATOM 62 N ALA A 11 17.578 46.157 68.656 1.00 8.74 N ANISOU 62 N ALA A 11 1363 717 1241 -103 -1 -111 N ATOM 63 CA ALA A 11 17.175 47.524 68.932 1.00 9.36 C ANISOU 63 CA ALA A 11 1340 939 1275 25 -12 -93 C ATOM 64 C ALA A 11 17.338 47.782 70.418 1.00 9.21 C ANISOU 64 C ALA A 11 1371 938 1188 -9 -14 -4 C ATOM 65 O ALA A 11 16.898 46.980 71.249 1.00 9.99 O ANISOU 65 O ALA A 11 1537 917 1341 -57 42 -84 O ATOM 66 CB ALA A 11 15.700 47.718 68.534 1.00 10.36 C ANISOU 66 CB ALA A 11 1373 1144 1417 83 -2 -44 C ATOM 67 N LEU A 12 17.931 48.928 70.740 1.00 8.49 N ANISOU 67 N LEU A 12 1232 909 1085 45 -11 -33 N ATOM 68 CA LEU A 12 18.051 49.435 72.114 1.00 8.80 C ANISOU 68 CA LEU A 12 1174 1017 1152 -1 38 -32 C ATOM 69 C LEU A 12 17.146 50.647 72.289 1.00 8.65 C ANISOU 69 C LEU A 12 1149 944 1191 25 12 18 C ATOM 70 O LEU A 12 17.464 51.758 71.852 1.00 8.05 O ANISOU 70 O LEU A 12 1076 728 1252 87 24 -100 O ATOM 71 CB LEU A 12 19.495 49.788 72.447 1.00 9.46 C ANISOU 71 CB LEU A 12 1237 1110 1245 66 15 -76 C ATOM 72 CG LEU A 12 20.569 48.809 71.976 1.00 9.25 C ANISOU 72 CG LEU A 12 1271 1081 1163 70 78 -147 C ATOM 73 CD1 LEU A 12 21.911 49.501 71.959 1.00 10.04 C ANISOU 73 CD1 LEU A 12 1261 1401 1150 104 -55 -129 C ATOM 74 CD2 LEU A 12 20.552 47.557 72.862 1.00 10.87 C ANISOU 74 CD2 LEU A 12 1385 1474 1268 102 66 0 C ATOM 75 N ASP A 13 15.986 50.432 72.896 1.00 8.88 N ANISOU 75 N ASP A 13 1174 1021 1179 -8 59 69 N ATOM 76 CA ASP A 13 14.960 51.468 73.010 1.00 9.73 C ANISOU 76 CA ASP A 13 1345 1088 1261 7 40 -9 C ATOM 77 C ASP A 13 14.787 51.978 74.438 1.00 9.68 C ANISOU 77 C ASP A 13 1215 1176 1285 60 38 -9 C ATOM 78 O ASP A 13 13.750 52.556 74.776 1.00 10.16 O ANISOU 78 O ASP A 13 1219 1282 1359 79 145 -191 O ATOM 79 CB ASP A 13 13.617 50.986 72.447 1.00 10.33 C ANISOU 79 CB ASP A 13 1372 1329 1223 7 56 41 C ATOM 80 CG ASP A 13 13.702 50.538 70.978 1.00 11.17 C ANISOU 80 CG ASP A 13 1683 1157 1402 -60 45 -122 C ATOM 81 OD1 ASP A 13 14.220 51.327 70.160 1.00 12.21 O ANISOU 81 OD1 ASP A 13 1897 1641 1100 83 -94 139 O ATOM 82 OD2 ASP A 13 13.248 49.411 70.604 1.00 14.99 O ANISOU 82 OD2 ASP A 13 2158 1539 1998 -189 -105 -93 O ATOM 83 N HIS A 14 15.829 51.795 75.245 1.00 9.26 N ANISOU 83 N HIS A 14 1180 1086 1252 8 -5 -57 N ATOM 84 CA HIS A 14 15.852 52.157 76.657 1.00 8.85 C ANISOU 84 CA HIS A 14 1111 1042 1209 -5 -6 -79 C ATOM 85 C HIS A 14 15.750 53.665 76.847 1.00 9.20 C ANISOU 85 C HIS A 14 1161 1125 1206 -17 34 -58 C ATOM 86 O HIS A 14 16.133 54.453 75.974 1.00 9.59 O ANISOU 86 O HIS A 14 1148 1323 1171 -65 139 -39 O ATOM 87 CB HIS A 14 17.136 51.622 77.310 1.00 8.83 C ANISOU 87 CB HIS A 14 1192 981 1181 25 -13 -166 C ATOM 88 CG HIS A 14 17.353 50.162 77.054 1.00 7.86 C ANISOU 88 CG HIS A 14 1006 837 1143 -48 -1 -81 C ATOM 89 ND1 HIS A 14 17.862 49.689 75.865 1.00 8.44 N ANISOU 89 ND1 HIS A 14 1203 644 1359 52 37 -138 N ATOM 90 CD2 HIS A 14 17.061 49.078 77.799 1.00 8.93 C ANISOU 90 CD2 HIS A 14 1374 759 1258 -57 -15 -144 C ATOM 91 CE1 HIS A 14 17.904 48.367 75.904 1.00 8.64 C ANISOU 91 CE1 HIS A 14 1482 670 1129 -1 21 -9 C ATOM 92 NE2 HIS A 14 17.416 47.973 77.065 1.00 8.14 N ANISOU 92 NE2 HIS A 14 1127 836 1130 -66 103 -152 N ATOM 93 N SER A 15 15.206 54.056 77.993 1.00 9.28 N ANISOU 93 N SER A 15 1162 1227 1136 -79 70 -51 N ATOM 94 CA SER A 15 15.068 55.461 78.340 1.00 10.03 C ANISOU 94 CA SER A 15 1216 1332 1263 56 2 -109 C ATOM 95 C SER A 15 16.269 56.072 79.074 1.00 10.34 C ANISOU 95 C SER A 15 1276 1320 1334 68 -7 -118 C ATOM 96 O SER A 15 16.223 57.222 79.499 1.00 10.28 O ANISOU 96 O SER A 15 1245 1282 1379 192 -77 -220 O ATOM 97 CB SER A 15 13.776 55.658 79.141 1.00 10.39 C ANISOU 97 CB SER A 15 1219 1450 1277 31 42 -109 C ATOM 98 OG SER A 15 12.629 55.471 78.336 1.00 10.49 O ANISOU 98 OG SER A 15 1344 1425 1215 -31 -141 -131 O ATOM 99 N ASN A 16 17.337 55.287 79.224 1.00 9.90 N ANISOU 99 N ASN A 16 1233 1242 1285 71 -55 -171 N ATOM 100 CA ASN A 16 18.557 55.752 79.849 1.00 10.22 C ANISOU 100 CA ASN A 16 1263 1366 1251 55 -42 -38 C ATOM 101 C ASN A 16 19.783 55.066 79.250 1.00 10.42 C ANISOU 101 C ASN A 16 1359 1310 1288 3 -73 -126 C ATOM 102 O ASN A 16 19.695 54.055 78.542 1.00 10.18 O ANISOU 102 O ASN A 16 1457 1102 1307 -31 -95 -141 O ATOM 103 CB ASN A 16 18.460 55.615 81.378 1.00 10.10 C ANISOU 103 CB ASN A 16 1276 1345 1216 39 -30 -101 C ATOM 104 CG ASN A 16 18.180 54.204 81.820 1.00 12.34 C ANISOU 104 CG ASN A 16 1492 1674 1522 18 -31 9 C ATOM 105 OD1 ASN A 16 18.662 53.247 81.228 1.00 12.03 O ANISOU 105 OD1 ASN A 16 1436 1626 1506 -3 -10 30 O ATOM 106 ND2 ASN A 16 17.365 54.065 82.862 1.00 16.21 N ANISOU 106 ND2 ASN A 16 2198 2086 1875 -10 220 186 N ATOM 107 N LEU A 17 20.925 55.688 79.481 1.00 10.43 N ANISOU 107 N LEU A 17 1381 1326 1253 -69 -86 -118 N ATOM 108 CA LEU A 17 22.188 55.288 78.898 1.00 10.56 C ANISOU 108 CA LEU A 17 1396 1265 1349 -49 -103 -63 C ATOM 109 C LEU A 17 22.594 53.904 79.399 1.00 10.37 C ANISOU 109 C LEU A 17 1323 1274 1342 -25 -56 -70 C ATOM 110 O LEU A 17 22.974 53.030 78.596 1.00 9.63 O ANISOU 110 O LEU A 17 1254 994 1409 -67 10 -136 O ATOM 111 CB LEU A 17 23.254 56.321 79.238 1.00 11.03 C ANISOU 111 CB LEU A 17 1490 1251 1450 -42 -84 -64 C ATOM 112 CG LEU A 17 24.597 56.033 78.601 1.00 13.00 C ANISOU 112 CG LEU A 17 1727 1576 1636 -98 -71 -54 C ATOM 113 CD1 LEU A 17 24.496 56.123 77.065 1.00 13.35 C ANISOU 113 CD1 LEU A 17 2031 1487 1553 -285 92 -19 C ATOM 114 CD2 LEU A 17 25.675 56.930 79.165 1.00 13.56 C ANISOU 114 CD2 LEU A 17 1666 1627 1857 -117 -12 -55 C ATOM 115 N LYS A 18 22.464 53.681 80.707 1.00 10.27 N ANISOU 115 N LYS A 18 1294 1275 1332 -15 -36 -18 N ATOM 116 CA LYS A 18 22.880 52.407 81.284 1.00 10.37 C ANISOU 116 CA LYS A 18 1369 1247 1322 -12 -21 -36 C ATOM 117 C LYS A 18 22.100 51.229 80.695 1.00 10.14 C ANISOU 117 C LYS A 18 1329 1173 1348 -6 -10 -24 C ATOM 118 O LYS A 18 22.678 50.185 80.421 1.00 11.25 O ANISOU 118 O LYS A 18 1526 1228 1517 14 -22 -25 O ATOM 119 CB LYS A 18 22.777 52.438 82.816 1.00 10.53 C ANISOU 119 CB LYS A 18 1465 1254 1280 19 -21 -39 C ATOM 120 CG LYS A 18 21.355 52.417 83.363 1.00 11.53 C ANISOU 120 CG LYS A 18 1608 1427 1344 -103 -75 -64 C ATOM 121 CD LYS A 18 21.343 52.599 84.875 1.00 14.34 C ANISOU 121 CD LYS A 18 1801 2067 1578 107 -47 -4 C ATOM 122 CE LYS A 18 19.961 52.382 85.461 1.00 16.05 C ANISOU 122 CE LYS A 18 2139 2174 1783 -84 38 16 C ATOM 123 NZ LYS A 18 19.987 52.614 86.943 1.00 18.03 N ANISOU 123 NZ LYS A 18 2459 2565 1823 -244 175 -91 N ATOM 124 N GLY A 19 20.810 51.405 80.436 1.00 9.45 N ANISOU 124 N GLY A 19 1242 1025 1321 21 -55 -74 N ATOM 125 CA GLY A 19 20.029 50.272 79.911 1.00 10.13 C ANISOU 125 CA GLY A 19 1330 1161 1356 -82 -38 37 C ATOM 126 C GLY A 19 20.465 49.868 78.510 1.00 9.34 C ANISOU 126 C GLY A 19 1328 1035 1183 -40 -72 21 C ATOM 127 O GLY A 19 20.559 48.671 78.164 1.00 10.12 O ANISOU 127 O GLY A 19 1458 1251 1134 -66 -144 144 O ATOM 128 N ALA A 20 20.736 50.882 77.673 1.00 9.20 N ANISOU 128 N ALA A 20 1186 1109 1201 2 -65 101 N ATOM 129 CA ALA A 20 21.218 50.637 76.298 1.00 9.15 C ANISOU 129 CA ALA A 20 1187 1128 1162 -9 -46 31 C ATOM 130 C ALA A 20 22.581 49.961 76.297 1.00 9.29 C ANISOU 130 C ALA A 20 1236 1138 1156 29 -84 37 C ATOM 131 O ALA A 20 22.809 48.987 75.579 1.00 9.23 O ANISOU 131 O ALA A 20 1216 1120 1169 11 -117 43 O ATOM 132 CB ALA A 20 21.316 51.946 75.510 1.00 9.43 C ANISOU 132 CB ALA A 20 1212 1156 1213 135 -98 119 C ATOM 133 N ILE A 21 23.503 50.475 77.103 1.00 9.14 N ANISOU 133 N ILE A 21 1162 1089 1220 -30 -82 17 N ATOM 134 CA ILE A 21 24.869 49.943 77.097 1.00 9.74 C ANISOU 134 CA ILE A 21 1290 1088 1320 3 -54 52 C ATOM 135 C ILE A 21 24.867 48.530 77.674 1.00 9.61 C ANISOU 135 C ILE A 21 1298 1041 1309 45 -81 44 C ATOM 136 O ILE A 21 25.485 47.623 77.118 1.00 9.88 O ANISOU 136 O ILE A 21 1367 940 1446 24 -32 42 O ATOM 137 CB ILE A 21 25.832 50.875 77.859 1.00 9.27 C ANISOU 137 CB ILE A 21 1198 987 1335 4 -57 58 C ATOM 138 CG1 ILE A 21 25.936 52.241 77.130 1.00 10.54 C ANISOU 138 CG1 ILE A 21 1462 1040 1502 -69 -155 143 C ATOM 139 CG2 ILE A 21 27.218 50.228 78.015 1.00 8.99 C ANISOU 139 CG2 ILE A 21 1007 1228 1180 8 -220 2 C ATOM 140 CD1 ILE A 21 26.743 53.288 77.858 1.00 13.51 C ANISOU 140 CD1 ILE A 21 1684 1607 1842 37 -68 -61 C ATOM 141 N THR A 22 24.119 48.327 78.746 1.00 9.53 N ANISOU 141 N THR A 22 1425 904 1289 16 -8 59 N ATOM 142 CA THR A 22 24.114 46.992 79.367 1.00 9.64 C ANISOU 142 CA THR A 22 1463 955 1243 32 -111 16 C ATOM 143 C THR A 22 23.512 45.964 78.419 1.00 9.90 C ANISOU 143 C THR A 22 1392 1090 1279 20 -110 17 C ATOM 144 O THR A 22 24.034 44.875 78.270 1.00 10.22 O ANISOU 144 O THR A 22 1553 984 1344 21 -135 44 O ATOM 145 CB THR A 22 23.409 47.010 80.718 1.00 9.70 C ANISOU 145 CB THR A 22 1526 909 1250 34 -130 -8 C ATOM 146 OG1 THR A 22 24.139 47.855 81.607 1.00 11.07 O ANISOU 146 OG1 THR A 22 1930 1103 1173 -14 -206 -252 O ATOM 147 CG2 THR A 22 23.378 45.637 81.361 1.00 11.25 C ANISOU 147 CG2 THR A 22 1746 1275 1253 -49 -170 -97 C ATOM 148 N ALA A 23 22.419 46.328 77.759 1.00 9.72 N ANISOU 148 N ALA A 23 1373 1101 1220 -84 -126 -34 N ATOM 149 CA ALA A 23 21.777 45.397 76.813 1.00 8.83 C ANISOU 149 CA ALA A 23 1278 899 1176 -123 -101 -66 C ATOM 150 C ALA A 23 22.704 45.106 75.621 1.00 9.17 C ANISOU 150 C ALA A 23 1368 954 1160 -75 -50 -35 C ATOM 151 O ALA A 23 22.836 43.944 75.171 1.00 10.14 O ANISOU 151 O ALA A 23 1616 967 1270 -108 -125 -56 O ATOM 152 CB ALA A 23 20.446 45.936 76.334 1.00 8.91 C ANISOU 152 CB ALA A 23 1279 896 1209 -228 -74 -55 C ATOM 153 N ALA A 24 23.342 46.147 75.088 1.00 9.58 N ANISOU 153 N ALA A 24 1353 1030 1254 -54 -37 -55 N ATOM 154 CA ALA A 24 24.261 45.995 73.950 1.00 9.94 C ANISOU 154 CA ALA A 24 1317 1111 1348 -7 -54 7 C ATOM 155 C ALA A 24 25.407 45.057 74.246 1.00 10.89 C ANISOU 155 C ALA A 24 1427 1258 1452 17 -51 12 C ATOM 156 O ALA A 24 25.727 44.174 73.439 1.00 11.57 O ANISOU 156 O ALA A 24 1490 1221 1686 119 -119 36 O ATOM 157 CB ALA A 24 24.820 47.338 73.526 1.00 10.11 C ANISOU 157 CB ALA A 24 1439 1032 1367 -5 -61 -9 C ATOM 158 N VAL A 25 26.006 45.226 75.411 1.00 11.30 N ANISOU 158 N VAL A 25 1496 1305 1489 -6 -66 22 N ATOM 159 CA VAL A 25 27.117 44.360 75.813 1.00 12.09 C ANISOU 159 CA VAL A 25 1551 1417 1626 -14 -9 18 C ATOM 160 C VAL A 25 26.656 42.908 75.981 1.00 11.98 C ANISOU 160 C VAL A 25 1583 1347 1622 43 11 36 C ATOM 161 O VAL A 25 27.401 41.988 75.667 1.00 13.37 O ANISOU 161 O VAL A 25 1660 1569 1848 95 88 5 O ATOM 162 CB VAL A 25 27.820 44.910 77.080 1.00 11.88 C ANISOU 162 CB VAL A 25 1577 1425 1511 2 -50 70 C ATOM 163 CG1 VAL A 25 28.849 43.896 77.637 1.00 11.99 C ANISOU 163 CG1 VAL A 25 1575 1303 1675 -29 -115 -43 C ATOM 164 CG2 VAL A 25 28.521 46.215 76.753 1.00 13.02 C ANISOU 164 CG2 VAL A 25 1660 1496 1791 -85 47 2 C ATOM 165 N SER A 26 25.419 42.708 76.442 1.00 11.96 N ANISOU 165 N SER A 26 1602 1256 1685 40 12 28 N ATOM 166 CA SER A 26 24.891 41.350 76.666 1.00 12.36 C ANISOU 166 CA SER A 26 1693 1354 1648 -5 -72 57 C ATOM 167 C SER A 26 24.728 40.522 75.405 1.00 12.28 C ANISOU 167 C SER A 26 1698 1365 1601 34 -128 74 C ATOM 168 O SER A 26 24.808 39.296 75.475 1.00 12.92 O ANISOU 168 O SER A 26 1935 1358 1613 -18 -233 112 O ATOM 169 CB SER A 26 23.566 41.388 77.444 1.00 12.00 C ANISOU 169 CB SER A 26 1615 1424 1517 -32 -83 63 C ATOM 170 OG SER A 26 22.471 41.832 76.649 1.00 14.12 O ANISOU 170 OG SER A 26 1952 1435 1974 15 -159 -4 O ATOM 171 N VAL A 27 24.428 41.172 74.273 1.00 12.54 N ANISOU 171 N VAL A 27 1744 1426 1594 -11 -95 71 N ATOM 172 CA VAL A 27 24.131 40.470 73.018 1.00 13.13 C ANISOU 172 CA VAL A 27 1751 1557 1677 2 -55 -20 C ATOM 173 C VAL A 27 25.044 40.795 71.839 1.00 14.06 C ANISOU 173 C VAL A 27 1869 1713 1759 33 -77 11 C ATOM 174 O VAL A 27 25.000 40.115 70.813 1.00 14.23 O ANISOU 174 O VAL A 27 1879 1639 1889 49 -105 -90 O ATOM 175 CB VAL A 27 22.660 40.666 72.537 1.00 13.23 C ANISOU 175 CB VAL A 27 1772 1585 1667 6 -62 -28 C ATOM 176 CG1 VAL A 27 21.666 40.189 73.551 1.00 13.73 C ANISOU 176 CG1 VAL A 27 1879 1695 1642 -66 -75 -97 C ATOM 177 CG2 VAL A 27 22.364 42.092 72.128 1.00 13.67 C ANISOU 177 CG2 VAL A 27 1731 1650 1810 -36 -19 -29 C ATOM 178 N GLY A 28 25.868 41.822 71.983 1.00 14.84 N ANISOU 178 N GLY A 28 1979 1821 1836 -28 -50 -48 N ATOM 179 CA GLY A 28 26.638 42.371 70.874 1.00 15.23 C ANISOU 179 CA GLY A 28 1981 1900 1903 8 -31 -28 C ATOM 180 C GLY A 28 27.396 41.369 70.028 1.00 15.52 C ANISOU 180 C GLY A 28 2061 1891 1944 28 -41 -47 C ATOM 181 O GLY A 28 27.343 41.406 68.807 1.00 15.00 O ANISOU 181 O GLY A 28 1969 1772 1957 61 -45 -79 O ATOM 182 N ASN A 29 28.088 40.449 70.674 1.00 16.26 N ANISOU 182 N ASN A 29 2102 2062 2013 26 -84 -32 N ATOM 183 CA ASN A 29 28.904 39.494 69.949 1.00 17.56 C ANISOU 183 CA ASN A 29 2246 2210 2216 20 -23 -36 C ATOM 184 C ASN A 29 28.085 38.527 69.103 1.00 16.62 C ANISOU 184 C ASN A 29 2165 2073 2073 39 -7 -31 C ATOM 185 O ASN A 29 28.599 37.914 68.163 1.00 17.90 O ANISOU 185 O ASN A 29 2348 2249 2202 37 41 -98 O ATOM 186 CB ASN A 29 29.783 38.720 70.928 1.00 18.71 C ANISOU 186 CB ASN A 29 2420 2347 2341 18 -35 -3 C ATOM 187 CG ASN A 29 30.927 39.555 71.474 1.00 24.73 C ANISOU 187 CG ASN A 29 3133 3124 3136 -49 -15 -5 C ATOM 188 OD1 ASN A 29 31.227 40.662 70.973 1.00 28.91 O ANISOU 188 OD1 ASN A 29 3803 3315 3867 35 1 11 O ATOM 189 ND2 ASN A 29 31.595 39.025 72.498 1.00 29.64 N ANISOU 189 ND2 ASN A 29 3854 3779 3626 72 -49 56 N ATOM 190 N GLU A 30 26.814 38.381 69.449 1.00 15.35 N ANISOU 190 N GLU A 30 2021 1834 1976 -2 -56 -54 N ATOM 191 CA GLU A 30 25.953 37.402 68.806 1.00 14.47 C ANISOU 191 CA GLU A 30 1977 1628 1891 4 -74 -38 C ATOM 192 C GLU A 30 25.088 37.958 67.688 1.00 14.02 C ANISOU 192 C GLU A 30 1960 1454 1912 -13 -113 -9 C ATOM 193 O GLU A 30 24.450 37.192 66.968 1.00 14.37 O ANISOU 193 O GLU A 30 2192 1250 2017 18 -206 -49 O ATOM 194 CB GLU A 30 25.062 36.732 69.842 1.00 14.30 C ANISOU 194 CB GLU A 30 1961 1597 1873 22 -57 -2 C ATOM 195 CG GLU A 30 25.821 36.072 70.989 1.00 15.58 C ANISOU 195 CG GLU A 30 2037 1858 2023 103 -101 19 C ATOM 196 CD GLU A 30 26.733 34.930 70.546 1.00 16.67 C ANISOU 196 CD GLU A 30 2238 1857 2237 90 -89 -29 C ATOM 197 OE1 GLU A 30 26.409 34.229 69.560 1.00 16.60 O ANISOU 197 OE1 GLU A 30 2217 1674 2413 25 -188 -18 O ATOM 198 OE2 GLU A 30 27.789 34.738 71.201 1.00 17.71 O ANISOU 198 OE2 GLU A 30 2459 1737 2530 283 -305 25 O ATOM 199 N VAL A 31 25.055 39.285 67.541 1.00 11.68 N ANISOU 199 N VAL A 31 1646 1119 1671 -51 -21 32 N ATOM 200 CA VAL A 31 24.204 39.929 66.543 1.00 11.46 C ANISOU 200 CA VAL A 31 1533 1256 1562 -21 9 -30 C ATOM 201 C VAL A 31 25.047 40.519 65.437 1.00 10.79 C ANISOU 201 C VAL A 31 1490 1047 1560 2 -14 -2 C ATOM 202 O VAL A 31 26.264 40.660 65.583 1.00 11.99 O ANISOU 202 O VAL A 31 1671 1137 1748 67 -83 8 O ATOM 203 CB VAL A 31 23.267 41.023 67.175 1.00 11.15 C ANISOU 203 CB VAL A 31 1409 1294 1531 -21 16 -20 C ATOM 204 CG1 VAL A 31 22.487 40.412 68.343 1.00 11.47 C ANISOU 204 CG1 VAL A 31 1425 1470 1461 -33 40 -50 C ATOM 205 CG2 VAL A 31 24.042 42.250 67.627 1.00 12.87 C ANISOU 205 CG2 VAL A 31 1676 1568 1643 63 -42 -57 C ATOM 206 N ASP A 32 24.392 40.853 64.329 1.00 10.65 N ANISOU 206 N ASP A 32 1474 1111 1462 -21 5 -51 N ATOM 207 CA ASP A 32 25.051 41.453 63.168 1.00 10.44 C ANISOU 207 CA ASP A 32 1402 1116 1447 -38 34 -20 C ATOM 208 C ASP A 32 24.958 42.977 63.173 1.00 10.83 C ANISOU 208 C ASP A 32 1441 1163 1511 9 69 -73 C ATOM 209 O ASP A 32 25.798 43.658 62.577 1.00 11.18 O ANISOU 209 O ASP A 32 1547 1054 1644 -58 132 -139 O ATOM 210 CB ASP A 32 24.394 40.918 61.895 1.00 11.20 C ANISOU 210 CB ASP A 32 1452 1274 1527 35 52 -51 C ATOM 211 CG ASP A 32 24.412 39.427 61.843 1.00 12.29 C ANISOU 211 CG ASP A 32 1600 1368 1702 10 59 -8 C ATOM 212 OD1 ASP A 32 25.544 38.895 61.901 1.00 13.18 O ANISOU 212 OD1 ASP A 32 1823 1038 2145 426 -36 -148 O ATOM 213 OD2 ASP A 32 23.345 38.779 61.771 1.00 13.05 O ANISOU 213 OD2 ASP A 32 1942 1383 1633 243 -261 -132 O ATOM 214 N VAL A 33 23.888 43.489 63.767 1.00 9.98 N ANISOU 214 N VAL A 33 1355 1083 1353 -13 89 -53 N ATOM 215 CA VAL A 33 23.621 44.937 63.742 1.00 8.79 C ANISOU 215 CA VAL A 33 1182 962 1195 68 36 -65 C ATOM 216 C VAL A 33 23.125 45.404 65.128 1.00 9.63 C ANISOU 216 C VAL A 33 1307 1137 1215 3 7 -30 C ATOM 217 O VAL A 33 22.279 44.739 65.739 1.00 8.63 O ANISOU 217 O VAL A 33 1182 882 1214 -21 36 -121 O ATOM 218 CB VAL A 33 22.512 45.292 62.705 1.00 9.24 C ANISOU 218 CB VAL A 33 1254 1084 1170 -20 24 -55 C ATOM 219 CG1 VAL A 33 22.345 46.772 62.534 1.00 8.03 C ANISOU 219 CG1 VAL A 33 926 923 1199 76 53 -55 C ATOM 220 CG2 VAL A 33 22.731 44.598 61.351 1.00 7.52 C ANISOU 220 CG2 VAL A 33 1017 783 1055 27 17 0 C ATOM 221 N ILE A 34 23.663 46.521 65.615 1.00 9.11 N ANISOU 221 N ILE A 34 1324 1010 1124 52 31 -39 N ATOM 222 CA ILE A 34 23.229 47.119 66.891 1.00 9.71 C ANISOU 222 CA ILE A 34 1243 1188 1255 52 33 -68 C ATOM 223 C ILE A 34 22.641 48.494 66.613 1.00 8.34 C ANISOU 223 C ILE A 34 1110 901 1156 -52 59 -20 C ATOM 224 O ILE A 34 23.254 49.318 65.940 1.00 8.59 O ANISOU 224 O ILE A 34 1163 881 1218 -13 56 -58 O ATOM 225 CB ILE A 34 24.399 47.243 67.903 1.00 10.18 C ANISOU 225 CB ILE A 34 1319 1237 1313 59 28 -70 C ATOM 226 CG1 ILE A 34 25.003 45.871 68.165 1.00 11.84 C ANISOU 226 CG1 ILE A 34 1596 1375 1526 3 14 26 C ATOM 227 CG2 ILE A 34 23.907 47.830 69.216 1.00 10.93 C ANISOU 227 CG2 ILE A 34 1502 1374 1277 -29 -38 -91 C ATOM 228 CD1 ILE A 34 26.311 45.901 68.809 1.00 13.11 C ANISOU 228 CD1 ILE A 34 1757 1429 1796 37 -149 60 C ATOM 229 N GLU A 35 21.455 48.741 67.156 1.00 7.65 N ANISOU 229 N GLU A 35 1027 720 1158 -17 51 -44 N ATOM 230 CA GLU A 35 20.680 49.950 66.843 1.00 7.67 C ANISOU 230 CA GLU A 35 1006 823 1082 13 18 -14 C ATOM 231 C GLU A 35 20.416 50.772 68.108 1.00 7.49 C ANISOU 231 C GLU A 35 967 836 1041 16 -3 -58 C ATOM 232 O GLU A 35 19.853 50.279 69.082 1.00 7.62 O ANISOU 232 O GLU A 35 992 719 1180 38 5 -145 O ATOM 233 CB GLU A 35 19.337 49.591 66.192 1.00 7.18 C ANISOU 233 CB GLU A 35 991 806 931 34 -16 -1 C ATOM 234 CG GLU A 35 18.381 50.770 66.047 1.00 8.23 C ANISOU 234 CG GLU A 35 1176 901 1047 4 21 151 C ATOM 235 CD GLU A 35 17.112 50.405 65.301 1.00 9.58 C ANISOU 235 CD GLU A 35 1443 976 1221 -32 -89 77 C ATOM 236 OE1 GLU A 35 16.666 49.231 65.383 1.00 9.99 O ANISOU 236 OE1 GLU A 35 1672 955 1168 -118 24 133 O ATOM 237 OE2 GLU A 35 16.566 51.282 64.586 1.00 11.76 O ANISOU 237 OE2 GLU A 35 1880 1019 1567 -1 -146 33 O ATOM 238 N ALA A 36 20.844 52.029 68.074 1.00 6.88 N ANISOU 238 N ALA A 36 933 696 983 28 -15 -46 N ATOM 239 CA ALA A 36 20.461 53.006 69.078 1.00 7.86 C ANISOU 239 CA ALA A 36 1074 924 988 50 2 -56 C ATOM 240 C ALA A 36 19.076 53.522 68.723 1.00 7.61 C ANISOU 240 C ALA A 36 1094 820 975 111 92 -133 C ATOM 241 O ALA A 36 18.921 54.296 67.752 1.00 7.24 O ANISOU 241 O ALA A 36 1139 710 901 187 94 -151 O ATOM 242 CB ALA A 36 21.463 54.167 69.084 1.00 7.86 C ANISOU 242 CB ALA A 36 991 841 1155 16 -21 0 C ATOM 243 N GLY A 37 18.066 53.098 69.477 1.00 7.67 N ANISOU 243 N GLY A 37 1106 808 999 111 56 -130 N ATOM 244 CA GLY A 37 16.695 53.418 69.136 1.00 8.28 C ANISOU 244 CA GLY A 37 1071 1038 1036 72 -1 -84 C ATOM 245 C GLY A 37 16.311 54.862 69.415 1.00 7.31 C ANISOU 245 C GLY A 37 961 887 927 32 -47 -5 C ATOM 246 O GLY A 37 16.942 55.533 70.229 1.00 7.96 O ANISOU 246 O GLY A 37 1032 981 1009 123 -143 -45 O ATOM 247 N THR A 38 15.244 55.342 68.765 1.00 7.87 N ANISOU 247 N THR A 38 952 948 1091 -9 -30 -46 N ATOM 248 CA THR A 38 14.852 56.755 68.858 1.00 7.55 C ANISOU 248 CA THR A 38 934 895 1040 8 -19 10 C ATOM 249 C THR A 38 14.553 57.162 70.297 1.00 7.78 C ANISOU 249 C THR A 38 1005 899 1049 -26 -13 -16 C ATOM 250 O THR A 38 14.944 58.246 70.731 1.00 8.13 O ANISOU 250 O THR A 38 977 965 1143 -1 -95 -38 O ATOM 251 CB THR A 38 13.592 57.039 68.029 1.00 7.95 C ANISOU 251 CB THR A 38 1000 958 1060 -7 -56 -26 C ATOM 252 OG1 THR A 38 13.672 56.367 66.764 1.00 8.69 O ANISOU 252 OG1 THR A 38 993 955 1353 115 -129 -252 O ATOM 253 CG2 THR A 38 13.456 58.522 67.773 1.00 7.78 C ANISOU 253 CG2 THR A 38 1199 893 861 -117 -28 33 C ATOM 254 N VAL A 39 13.846 56.306 71.041 1.00 7.56 N ANISOU 254 N VAL A 39 935 844 1091 -6 24 -37 N ATOM 255 CA VAL A 39 13.528 56.631 72.435 1.00 8.29 C ANISOU 255 CA VAL A 39 1024 1059 1064 -55 8 9 C ATOM 256 C VAL A 39 14.814 56.918 73.230 1.00 7.08 C ANISOU 256 C VAL A 39 936 804 948 -51 43 -82 C ATOM 257 O VAL A 39 14.864 57.801 74.086 1.00 6.98 O ANISOU 257 O VAL A 39 947 618 1085 -89 31 -193 O ATOM 258 CB VAL A 39 12.749 55.468 73.109 1.00 8.24 C ANISOU 258 CB VAL A 39 968 1047 1113 -39 25 5 C ATOM 259 CG1 VAL A 39 12.664 55.708 74.613 1.00 7.98 C ANISOU 259 CG1 VAL A 39 851 1062 1116 -102 24 -121 C ATOM 260 CG2 VAL A 39 11.362 55.315 72.472 1.00 9.56 C ANISOU 260 CG2 VAL A 39 1045 1368 1219 -113 -31 26 C ATOM 261 N CYS A 40 15.842 56.128 72.964 1.00 8.30 N ANISOU 261 N CYS A 40 1071 986 1093 -35 38 -88 N ATOM 262 CA CYS A 40 17.109 56.244 73.658 1.00 6.99 C ANISOU 262 CA CYS A 40 883 783 988 20 2 -89 C ATOM 263 C CYS A 40 17.879 57.483 73.207 1.00 7.41 C ANISOU 263 C CYS A 40 1043 840 931 62 11 -78 C ATOM 264 O CYS A 40 18.363 58.248 74.038 1.00 6.92 O ANISOU 264 O CYS A 40 1063 556 1007 19 -25 -113 O ATOM 265 CB CYS A 40 17.961 54.991 73.451 1.00 7.63 C ANISOU 265 CB CYS A 40 990 821 1087 -59 8 -118 C ATOM 266 SG CYS A 40 19.258 54.883 74.692 1.00 10.12 S ANISOU 266 SG CYS A 40 1181 1107 1556 -6 -64 -108 S ATOM 267 N LEU A 41 17.991 57.682 71.894 1.00 6.80 N ANISOU 267 N LEU A 41 938 811 833 106 -13 -28 N ATOM 268 CA LEU A 41 18.678 58.859 71.394 1.00 7.07 C ANISOU 268 CA LEU A 41 938 874 873 65 1 -44 C ATOM 269 C LEU A 41 18.047 60.166 71.877 1.00 7.29 C ANISOU 269 C LEU A 41 886 864 1019 51 24 -35 C ATOM 270 O LEU A 41 18.756 61.112 72.237 1.00 8.01 O ANISOU 270 O LEU A 41 1044 817 1182 160 -34 -175 O ATOM 271 CB LEU A 41 18.777 58.834 69.873 1.00 7.70 C ANISOU 271 CB LEU A 41 978 999 945 102 19 -68 C ATOM 272 CG LEU A 41 19.686 57.739 69.291 1.00 7.93 C ANISOU 272 CG LEU A 41 994 890 1127 101 -18 -184 C ATOM 273 CD1 LEU A 41 19.528 57.754 67.807 1.00 7.34 C ANISOU 273 CD1 LEU A 41 952 762 1075 13 -74 -71 C ATOM 274 CD2 LEU A 41 21.151 58.002 69.685 1.00 7.49 C ANISOU 274 CD2 LEU A 41 934 754 1155 219 68 -298 C ATOM 275 N LEU A 42 16.720 60.247 71.890 1.00 7.29 N ANISOU 275 N LEU A 42 950 736 1081 68 -37 -82 N ATOM 276 CA LEU A 42 16.078 61.466 72.407 1.00 6.74 C ANISOU 276 CA LEU A 42 944 594 1020 30 27 11 C ATOM 277 C LEU A 42 16.349 61.685 73.872 1.00 6.51 C ANISOU 277 C LEU A 42 970 465 1038 26 31 -105 C ATOM 278 O LEU A 42 16.268 62.828 74.333 1.00 7.62 O ANISOU 278 O LEU A 42 1118 572 1204 144 14 -210 O ATOM 279 CB LEU A 42 14.559 61.456 72.145 1.00 7.42 C ANISOU 279 CB LEU A 42 1027 596 1194 68 -37 -45 C ATOM 280 CG LEU A 42 14.141 61.522 70.676 1.00 8.65 C ANISOU 280 CG LEU A 42 1133 971 1180 18 37 -37 C ATOM 281 CD1 LEU A 42 12.686 61.128 70.528 1.00 8.16 C ANISOU 281 CD1 LEU A 42 1034 1102 964 -28 -13 59 C ATOM 282 CD2 LEU A 42 14.424 62.893 70.105 1.00 8.50 C ANISOU 282 CD2 LEU A 42 1258 986 986 11 13 -56 C ATOM 283 N GLN A 43 16.618 60.607 74.619 1.00 7.60 N ANISOU 283 N GLN A 43 1029 804 1055 33 60 -45 N ATOM 284 CA GLN A 43 17.003 60.727 76.028 1.00 7.34 C ANISOU 284 CA GLN A 43 985 771 1032 98 41 -20 C ATOM 285 C GLN A 43 18.469 61.068 76.266 1.00 7.20 C ANISOU 285 C GLN A 43 987 752 994 67 -50 -19 C ATOM 286 O GLN A 43 18.770 61.866 77.134 1.00 7.67 O ANISOU 286 O GLN A 43 1035 781 1098 100 45 -117 O ATOM 287 CB GLN A 43 16.680 59.445 76.800 1.00 7.49 C ANISOU 287 CB GLN A 43 963 822 1059 -14 58 53 C ATOM 288 CG GLN A 43 15.251 59.276 77.180 1.00 8.21 C ANISOU 288 CG GLN A 43 1064 910 1143 145 109 -77 C ATOM 289 CD GLN A 43 14.789 60.291 78.199 1.00 8.22 C ANISOU 289 CD GLN A 43 992 1040 1089 25 40 -111 C ATOM 290 OE1 GLN A 43 14.456 61.418 77.853 1.00 7.38 O ANISOU 290 OE1 GLN A 43 793 951 1060 -38 149 -137 O ATOM 291 NE2 GLN A 43 14.736 59.878 79.461 1.00 8.47 N ANISOU 291 NE2 GLN A 43 1268 1004 943 66 138 -101 N ATOM 292 N VAL A 44 19.381 60.445 75.514 1.00 7.56 N ANISOU 292 N VAL A 44 980 853 1036 44 -37 -57 N ATOM 293 CA VAL A 44 20.799 60.492 75.866 1.00 7.90 C ANISOU 293 CA VAL A 44 1009 891 1099 22 -56 -56 C ATOM 294 C VAL A 44 21.682 61.193 74.858 1.00 7.22 C ANISOU 294 C VAL A 44 916 801 1024 18 -45 -7 C ATOM 295 O VAL A 44 22.814 61.512 75.189 1.00 8.25 O ANISOU 295 O VAL A 44 1029 885 1220 -59 -42 25 O ATOM 296 CB VAL A 44 21.364 59.119 76.191 1.00 8.82 C ANISOU 296 CB VAL A 44 1075 1121 1153 84 -68 20 C ATOM 297 CG1 VAL A 44 20.441 58.392 77.168 1.00 9.94 C ANISOU 297 CG1 VAL A 44 1193 1257 1325 34 -81 12 C ATOM 298 CG2 VAL A 44 21.560 58.314 74.936 1.00 8.92 C ANISOU 298 CG2 VAL A 44 1147 1123 1115 -2 -154 -53 C ATOM 299 N GLY A 45 21.180 61.436 73.654 1.00 7.27 N ANISOU 299 N GLY A 45 931 771 1057 -9 -5 -84 N ATOM 300 CA GLY A 45 21.943 62.106 72.604 1.00 7.10 C ANISOU 300 CA GLY A 45 1032 766 897 -65 3 -66 C ATOM 301 C GLY A 45 22.846 61.117 71.887 1.00 7.06 C ANISOU 301 C GLY A 45 952 813 916 -10 43 12 C ATOM 302 O GLY A 45 22.776 59.908 72.133 1.00 8.85 O ANISOU 302 O GLY A 45 1353 1063 946 -110 151 37 O ATOM 303 N SER A 46 23.730 61.648 71.055 1.00 7.40 N ANISOU 303 N SER A 46 898 914 998 9 45 -32 N ATOM 304 CA SER A 46 24.433 60.852 70.060 1.00 7.29 C ANISOU 304 CA SER A 46 964 724 1080 29 38 -77 C ATOM 305 C SER A 46 25.721 60.241 70.575 1.00 7.76 C ANISOU 305 C SER A 46 1044 786 1118 61 86 -81 C ATOM 306 O SER A 46 26.324 59.423 69.889 1.00 7.74 O ANISOU 306 O SER A 46 1227 521 1192 205 107 -143 O ATOM 307 CB SER A 46 24.683 61.692 68.813 1.00 7.84 C ANISOU 307 CB SER A 46 1007 796 1176 56 109 -102 C ATOM 308 OG SER A 46 25.557 62.781 69.088 1.00 9.47 O ANISOU 308 OG SER A 46 1260 858 1479 67 -38 -19 O ATOM 309 N GLU A 47 26.164 60.608 71.767 1.00 8.31 N ANISOU 309 N GLU A 47 1113 841 1200 59 73 -127 N ATOM 310 CA GLU A 47 27.401 60.035 72.279 1.00 8.99 C ANISOU 310 CA GLU A 47 1164 967 1284 15 9 -109 C ATOM 311 C GLU A 47 27.267 58.493 72.386 1.00 9.14 C ANISOU 311 C GLU A 47 1222 931 1318 -19 16 -97 C ATOM 312 O GLU A 47 28.220 57.766 72.186 1.00 9.15 O ANISOU 312 O GLU A 47 1248 783 1443 -131 -74 -161 O ATOM 313 CB GLU A 47 27.880 60.683 73.576 1.00 9.14 C ANISOU 313 CB GLU A 47 1145 1056 1272 40 -17 -140 C ATOM 314 CG GLU A 47 29.236 60.149 74.032 1.00 10.39 C ANISOU 314 CG GLU A 47 1364 1285 1296 48 -100 -137 C ATOM 315 CD GLU A 47 29.847 60.872 75.219 1.00 11.59 C ANISOU 315 CD GLU A 47 1355 1491 1558 -9 -124 -178 C ATOM 316 OE1 GLU A 47 29.114 61.421 76.068 1.00 14.20 O ANISOU 316 OE1 GLU A 47 1764 1931 1697 117 -238 -497 O ATOM 317 OE2 GLU A 47 31.092 60.829 75.319 1.00 14.28 O ANISOU 317 OE2 GLU A 47 1710 1821 1893 92 -102 -235 O ATOM 318 N LEU A 48 26.057 58.023 72.641 1.00 9.30 N ANISOU 318 N LEU A 48 1210 961 1363 -31 46 -71 N ATOM 319 CA LEU A 48 25.784 56.589 72.667 1.00 8.85 C ANISOU 319 CA LEU A 48 1192 956 1213 -3 62 -13 C ATOM 320 C LEU A 48 26.283 55.903 71.397 1.00 8.50 C ANISOU 320 C LEU A 48 1141 936 1151 3 5 2 C ATOM 321 O LEU A 48 26.845 54.786 71.462 1.00 7.84 O ANISOU 321 O LEU A 48 1021 822 1135 16 46 104 O ATOM 322 CB LEU A 48 24.284 56.327 72.858 1.00 9.44 C ANISOU 322 CB LEU A 48 1250 1053 1284 -58 23 -48 C ATOM 323 CG LEU A 48 23.813 54.863 72.760 1.00 10.31 C ANISOU 323 CG LEU A 48 1415 1145 1354 -21 26 -167 C ATOM 324 CD1 LEU A 48 24.431 53.999 73.827 1.00 12.51 C ANISOU 324 CD1 LEU A 48 1883 1296 1571 -15 -52 -64 C ATOM 325 CD2 LEU A 48 22.302 54.777 72.838 1.00 11.72 C ANISOU 325 CD2 LEU A 48 1533 1397 1523 -135 63 -188 C ATOM 326 N VAL A 49 26.083 56.549 70.249 1.00 8.97 N ANISOU 326 N VAL A 49 1241 1038 1129 -24 21 -79 N ATOM 327 CA VAL A 49 26.510 55.942 68.978 1.00 8.43 C ANISOU 327 CA VAL A 49 1062 1062 1078 -55 -20 -113 C ATOM 328 C VAL A 49 28.019 55.677 68.999 1.00 8.51 C ANISOU 328 C VAL A 49 1071 1005 1154 -10 -29 -74 C ATOM 329 O VAL A 49 28.488 54.626 68.593 1.00 8.13 O ANISOU 329 O VAL A 49 1017 905 1167 -122 -65 -144 O ATOM 330 CB VAL A 49 26.135 56.825 67.758 1.00 8.31 C ANISOU 330 CB VAL A 49 1080 984 1094 -33 -8 -71 C ATOM 331 CG1 VAL A 49 26.691 56.256 66.468 1.00 9.13 C ANISOU 331 CG1 VAL A 49 1347 953 1167 -95 94 -173 C ATOM 332 CG2 VAL A 49 24.620 56.961 67.655 1.00 9.42 C ANISOU 332 CG2 VAL A 49 1142 1297 1139 -68 -62 -147 C ATOM 333 N GLU A 50 28.758 56.666 69.474 1.00 8.42 N ANISOU 333 N GLU A 50 1031 951 1215 -87 -67 -120 N ATOM 334 CA GLU A 50 30.213 56.566 69.588 1.00 9.14 C ANISOU 334 CA GLU A 50 1193 968 1310 -15 -54 -56 C ATOM 335 C GLU A 50 30.673 55.490 70.603 1.00 9.33 C ANISOU 335 C GLU A 50 1222 1023 1299 -40 -82 -53 C ATOM 336 O GLU A 50 31.634 54.762 70.359 1.00 10.16 O ANISOU 336 O GLU A 50 1473 941 1445 5 -91 27 O ATOM 337 CB GLU A 50 30.790 57.940 69.929 1.00 9.95 C ANISOU 337 CB GLU A 50 1274 1022 1482 -26 -15 -9 C ATOM 338 CG GLU A 50 32.295 58.032 69.813 1.00 10.96 C ANISOU 338 CG GLU A 50 1437 1100 1628 -96 -133 -33 C ATOM 339 CD GLU A 50 32.839 59.460 69.839 1.00 14.50 C ANISOU 339 CD GLU A 50 1745 1525 2238 -159 -75 51 C ATOM 340 OE1 GLU A 50 32.092 60.399 69.546 1.00 16.25 O ANISOU 340 OE1 GLU A 50 1782 1556 2833 -243 -10 -232 O ATOM 341 OE2 GLU A 50 34.050 59.618 70.116 1.00 15.70 O ANISOU 341 OE2 GLU A 50 1829 1788 2348 -101 -168 -21 O ATOM 342 N VAL A 51 29.969 55.382 71.717 1.00 9.09 N ANISOU 342 N VAL A 51 1306 898 1247 -45 -115 -66 N ATOM 343 CA VAL A 51 30.267 54.352 72.715 1.00 8.13 C ANISOU 343 CA VAL A 51 1225 764 1100 -83 -113 -141 C ATOM 344 C VAL A 51 30.054 52.971 72.085 1.00 8.96 C ANISOU 344 C VAL A 51 1329 840 1233 -25 -117 -158 C ATOM 345 O VAL A 51 30.881 52.093 72.274 1.00 9.21 O ANISOU 345 O VAL A 51 1228 1047 1222 13 -257 -171 O ATOM 346 CB VAL A 51 29.406 54.525 73.981 1.00 8.33 C ANISOU 346 CB VAL A 51 1193 766 1205 -29 -64 -103 C ATOM 347 CG1 VAL A 51 29.523 53.328 74.916 1.00 9.71 C ANISOU 347 CG1 VAL A 51 1587 950 1150 -272 23 12 C ATOM 348 CG2 VAL A 51 29.773 55.842 74.704 1.00 8.04 C ANISOU 348 CG2 VAL A 51 1124 882 1049 -48 -49 -294 C ATOM 349 N LEU A 52 28.971 52.820 71.339 1.00 8.50 N ANISOU 349 N LEU A 52 1268 746 1216 96 -127 -89 N ATOM 350 CA LEU A 52 28.685 51.538 70.704 1.00 9.52 C ANISOU 350 CA LEU A 52 1341 924 1352 -5 -37 -115 C ATOM 351 C LEU A 52 29.755 51.199 69.678 1.00 9.66 C ANISOU 351 C LEU A 52 1345 955 1369 58 -24 -104 C ATOM 352 O LEU A 52 30.160 50.053 69.582 1.00 10.15 O ANISOU 352 O LEU A 52 1415 942 1497 140 -33 -188 O ATOM 353 CB LEU A 52 27.307 51.511 70.073 1.00 9.64 C ANISOU 353 CB LEU A 52 1396 921 1343 68 -75 -64 C ATOM 354 CG LEU A 52 26.144 51.596 71.046 1.00 10.04 C ANISOU 354 CG LEU A 52 1448 907 1458 12 -44 -70 C ATOM 355 CD1 LEU A 52 24.842 51.797 70.315 1.00 11.40 C ANISOU 355 CD1 LEU A 52 1604 1175 1550 91 -129 35 C ATOM 356 CD2 LEU A 52 26.076 50.334 71.924 1.00 10.44 C ANISOU 356 CD2 LEU A 52 1564 1160 1242 13 3 -34 C ATOM 357 N ARG A 53 30.211 52.199 68.921 1.00 9.40 N ANISOU 357 N ARG A 53 1297 956 1316 56 103 -82 N ATOM 358 CA ARG A 53 31.264 51.996 67.930 1.00 9.35 C ANISOU 358 CA ARG A 53 1244 1084 1223 73 27 -64 C ATOM 359 C ARG A 53 32.567 51.553 68.571 1.00 10.03 C ANISOU 359 C ARG A 53 1325 1192 1292 100 -7 -81 C ATOM 360 O ARG A 53 33.245 50.684 68.053 1.00 10.18 O ANISOU 360 O ARG A 53 1319 1183 1363 242 -70 -135 O ATOM 361 CB ARG A 53 31.446 53.237 67.076 1.00 9.06 C ANISOU 361 CB ARG A 53 1266 997 1177 14 44 -118 C ATOM 362 CG ARG A 53 32.613 53.194 66.085 1.00 8.14 C ANISOU 362 CG ARG A 53 1100 813 1180 -1 -34 -97 C ATOM 363 CD ARG A 53 32.628 51.995 65.179 1.00 10.13 C ANISOU 363 CD ARG A 53 1361 1298 1189 108 65 -98 C ATOM 364 NE ARG A 53 31.586 52.151 64.179 1.00 11.35 N ANISOU 364 NE ARG A 53 1522 1395 1392 -21 -109 -127 N ATOM 365 CZ ARG A 53 30.881 51.171 63.631 1.00 10.68 C ANISOU 365 CZ ARG A 53 1385 1299 1372 -25 -17 -69 C ATOM 366 NH1 ARG A 53 31.064 49.923 64.019 1.00 11.17 N ANISOU 366 NH1 ARG A 53 1180 1516 1549 -32 -55 -256 N ATOM 367 NH2 ARG A 53 29.949 51.466 62.730 1.00 10.45 N ANISOU 367 NH2 ARG A 53 1517 1186 1264 49 -235 -407 N ATOM 368 N SER A 54 32.882 52.125 69.721 1.00 9.82 N ANISOU 368 N SER A 54 1325 1074 1330 89 -14 -79 N ATOM 369 CA SER A 54 34.070 51.761 70.481 1.00 10.46 C ANISOU 369 CA SER A 54 1357 1202 1414 23 -83 -87 C ATOM 370 C SER A 54 33.983 50.299 70.994 1.00 10.52 C ANISOU 370 C SER A 54 1322 1237 1438 40 -57 -67 C ATOM 371 O SER A 54 34.953 49.530 70.928 1.00 11.38 O ANISOU 371 O SER A 54 1343 1329 1649 70 -66 -118 O ATOM 372 CB SER A 54 34.215 52.748 71.642 1.00 10.67 C ANISOU 372 CB SER A 54 1382 1235 1437 75 -56 -151 C ATOM 373 OG SER A 54 35.386 52.500 72.376 1.00 13.16 O ANISOU 373 OG SER A 54 1599 1590 1808 23 -159 -152 O ATOM 374 N LEU A 55 32.829 49.925 71.530 1.00 10.53 N ANISOU 374 N LEU A 55 1312 1333 1353 53 -88 -60 N ATOM 375 CA LEU A 55 32.639 48.573 72.007 1.00 10.95 C ANISOU 375 CA LEU A 55 1437 1329 1391 71 -56 -53 C ATOM 376 C LEU A 55 32.645 47.545 70.875 1.00 11.60 C ANISOU 376 C LEU A 55 1518 1361 1526 117 -90 -103 C ATOM 377 O LEU A 55 33.066 46.397 71.098 1.00 12.16 O ANISOU 377 O LEU A 55 1625 1300 1692 198 -109 -180 O ATOM 378 CB LEU A 55 31.306 48.470 72.762 1.00 10.84 C ANISOU 378 CB LEU A 55 1361 1419 1335 68 -65 -53 C ATOM 379 CG LEU A 55 31.264 49.171 74.128 1.00 10.59 C ANISOU 379 CG LEU A 55 1378 1265 1381 26 -15 -28 C ATOM 380 CD1 LEU A 55 29.821 49.341 74.612 1.00 11.55 C ANISOU 380 CD1 LEU A 55 1611 1249 1525 6 1 -114 C ATOM 381 CD2 LEU A 55 32.067 48.349 75.111 1.00 11.01 C ANISOU 381 CD2 LEU A 55 1550 1246 1386 -20 -225 -199 C ATOM 382 N PHE A 56 32.156 47.957 69.696 1.00 11.98 N ANISOU 382 N PHE A 56 1680 1398 1474 126 -28 -214 N ATOM 383 CA PHE A 56 31.915 47.054 68.554 1.00 12.32 C ANISOU 383 CA PHE A 56 1704 1357 1620 86 -75 -180 C ATOM 384 C PHE A 56 32.457 47.637 67.233 1.00 13.65 C ANISOU 384 C PHE A 56 1898 1553 1735 149 -88 -195 C ATOM 385 O PHE A 56 31.699 48.153 66.396 1.00 14.02 O ANISOU 385 O PHE A 56 1996 1556 1774 286 -67 -207 O ATOM 386 CB PHE A 56 30.424 46.740 68.488 1.00 12.92 C ANISOU 386 CB PHE A 56 1786 1480 1640 100 -89 -259 C ATOM 387 CG PHE A 56 29.900 46.082 69.727 1.00 13.16 C ANISOU 387 CG PHE A 56 1573 1650 1775 32 -36 -205 C ATOM 388 CD1 PHE A 56 30.197 44.753 70.020 1.00 14.55 C ANISOU 388 CD1 PHE A 56 1858 1868 1800 -87 -8 -68 C ATOM 389 CD2 PHE A 56 29.119 46.791 70.632 1.00 15.60 C ANISOU 389 CD2 PHE A 56 1949 2020 1958 -5 56 -383 C ATOM 390 CE1 PHE A 56 29.732 44.159 71.188 1.00 15.74 C ANISOU 390 CE1 PHE A 56 1977 2021 1982 -54 -34 -102 C ATOM 391 CE2 PHE A 56 28.664 46.189 71.780 1.00 15.03 C ANISOU 391 CE2 PHE A 56 1851 1914 1944 2 -39 -313 C ATOM 392 CZ PHE A 56 28.954 44.885 72.055 1.00 15.30 C ANISOU 392 CZ PHE A 56 1943 2074 1795 -114 -32 -81 C ATOM 393 N PRO A 57 33.780 47.632 67.066 1.00 15.52 N ANISOU 393 N PRO A 57 2076 1806 2015 188 -27 -118 N ATOM 394 CA PRO A 57 34.427 48.306 65.929 1.00 17.45 C ANISOU 394 CA PRO A 57 2208 2171 2250 136 0 -63 C ATOM 395 C PRO A 57 33.957 47.808 64.561 1.00 18.88 C ANISOU 395 C PRO A 57 2322 2473 2378 147 10 -41 C ATOM 396 O PRO A 57 33.960 48.582 63.598 1.00 20.41 O ANISOU 396 O PRO A 57 2462 2920 2371 192 82 -50 O ATOM 397 CB PRO A 57 35.925 48.000 66.124 1.00 17.45 C ANISOU 397 CB PRO A 57 2182 2210 2238 82 -3 -51 C ATOM 398 CG PRO A 57 36.013 47.030 67.287 1.00 17.27 C ANISOU 398 CG PRO A 57 2175 2123 2261 183 0 -28 C ATOM 399 CD PRO A 57 34.755 47.079 68.031 1.00 15.66 C ANISOU 399 CD PRO A 57 2097 1849 2001 163 -73 -81 C ATOM 400 N ASP A 58 33.518 46.557 64.497 1.00 20.15 N ANISOU 400 N ASP A 58 2445 2656 2553 145 -25 -107 N ATOM 401 CA ASP A 58 33.236 45.923 63.212 1.00 21.02 C ANISOU 401 CA ASP A 58 2590 2742 2651 98 -29 -125 C ATOM 402 C ASP A 58 31.775 45.477 63.067 1.00 20.21 C ANISOU 402 C ASP A 58 2486 2642 2549 94 -40 -195 C ATOM 403 O ASP A 58 31.452 44.645 62.220 1.00 21.43 O ANISOU 403 O ASP A 58 2615 2846 2679 124 -68 -318 O ATOM 404 CB ASP A 58 34.216 44.765 62.997 1.00 21.93 C ANISOU 404 CB ASP A 58 2681 2862 2787 129 -38 -98 C ATOM 405 CG ASP A 58 35.694 45.226 63.004 1.00 23.63 C ANISOU 405 CG ASP A 58 2914 3026 3036 28 -33 -54 C ATOM 406 OD1 ASP A 58 36.049 46.246 62.368 1.00 24.82 O ANISOU 406 OD1 ASP A 58 2944 3258 3226 157 20 -110 O ATOM 407 OD2 ASP A 58 36.547 44.578 63.639 1.00 28.29 O ANISOU 407 OD2 ASP A 58 3255 3857 3633 128 -105 -9 O ATOM 408 N LYS A 59 30.885 46.029 63.886 1.00 17.48 N ANISOU 408 N LYS A 59 2184 2237 2219 137 -69 -171 N ATOM 409 CA LYS A 59 29.475 45.703 63.792 1.00 16.15 C ANISOU 409 CA LYS A 59 2053 2028 2054 78 -50 -103 C ATOM 410 C LYS A 59 28.810 46.804 63.023 1.00 13.56 C ANISOU 410 C LYS A 59 1662 1721 1769 89 -91 -110 C ATOM 411 O LYS A 59 29.288 47.933 63.006 1.00 13.77 O ANISOU 411 O LYS A 59 1548 1812 1870 4 -146 -49 O ATOM 412 CB LYS A 59 28.826 45.634 65.167 1.00 16.95 C ANISOU 412 CB LYS A 59 2197 2121 2120 133 -38 -43 C ATOM 413 CG LYS A 59 27.896 44.484 65.331 1.00 20.84 C ANISOU 413 CG LYS A 59 2641 2670 2606 -15 19 -87 C ATOM 414 CD LYS A 59 28.644 43.139 65.095 1.00 23.70 C ANISOU 414 CD LYS A 59 2903 3011 3090 124 15 -4 C ATOM 415 CE LYS A 59 28.868 42.373 66.368 1.00 24.72 C ANISOU 415 CE LYS A 59 3000 3164 3229 -39 68 29 C ATOM 416 NZ LYS A 59 28.989 40.926 66.072 1.00 25.90 N ANISOU 416 NZ LYS A 59 3039 3539 3262 98 44 26 N ATOM 417 N ILE A 60 27.696 46.488 62.377 1.00 11.57 N ANISOU 417 N ILE A 60 1438 1394 1563 73 -68 -157 N ATOM 418 CA ILE A 60 26.894 47.552 61.759 1.00 10.00 C ANISOU 418 CA ILE A 60 1343 1139 1316 63 -70 -97 C ATOM 419 C ILE A 60 26.157 48.300 62.885 1.00 9.33 C ANISOU 419 C ILE A 60 1275 1030 1240 33 -8 -92 C ATOM 420 O ILE A 60 25.575 47.676 63.753 1.00 8.41 O ANISOU 420 O ILE A 60 1227 803 1162 68 36 -142 O ATOM 421 CB ILE A 60 25.888 46.978 60.737 1.00 10.60 C ANISOU 421 CB ILE A 60 1360 1295 1370 0 -64 -112 C ATOM 422 CG1 ILE A 60 26.638 46.355 59.549 1.00 11.35 C ANISOU 422 CG1 ILE A 60 1426 1365 1518 46 -45 -146 C ATOM 423 CG2 ILE A 60 24.957 48.079 60.256 1.00 11.10 C ANISOU 423 CG2 ILE A 60 1468 1360 1387 21 -89 -61 C ATOM 424 CD1 ILE A 60 25.792 45.428 58.654 1.00 14.32 C ANISOU 424 CD1 ILE A 60 1832 1838 1770 -56 5 -146 C ATOM 425 N ILE A 61 26.211 49.637 62.881 1.00 9.01 N ANISOU 425 N ILE A 61 1204 962 1258 139 -19 -87 N ATOM 426 CA ILE A 61 25.541 50.449 63.907 1.00 9.38 C ANISOU 426 CA ILE A 61 1227 1109 1226 94 0 -77 C ATOM 427 C ILE A 61 24.512 51.364 63.247 1.00 8.75 C ANISOU 427 C ILE A 61 1169 1029 1126 78 24 -85 C ATOM 428 O ILE A 61 24.815 52.047 62.275 1.00 8.06 O ANISOU 428 O ILE A 61 1007 835 1218 46 132 -150 O ATOM 429 CB ILE A 61 26.565 51.297 64.688 1.00 9.51 C ANISOU 429 CB ILE A 61 1293 1063 1254 123 -47 -78 C ATOM 430 CG1 ILE A 61 27.516 50.399 65.472 1.00 11.18 C ANISOU 430 CG1 ILE A 61 1408 1378 1460 188 -38 -218 C ATOM 431 CG2 ILE A 61 25.870 52.299 65.638 1.00 9.78 C ANISOU 431 CG2 ILE A 61 1368 1098 1249 92 86 -81 C ATOM 432 CD1 ILE A 61 28.574 51.092 66.180 1.00 14.67 C ANISOU 432 CD1 ILE A 61 1832 1823 1915 78 -71 -80 C ATOM 433 N VAL A 62 23.305 51.359 63.794 1.00 8.35 N ANISOU 433 N VAL A 62 1011 982 1179 55 -6 -105 N ATOM 434 CA VAL A 62 22.177 52.131 63.300 1.00 8.24 C ANISOU 434 CA VAL A 62 1071 912 1147 113 40 -121 C ATOM 435 C VAL A 62 21.887 53.245 64.305 1.00 8.35 C ANISOU 435 C VAL A 62 1068 1023 1080 48 73 -126 C ATOM 436 O VAL A 62 21.799 52.983 65.507 1.00 8.62 O ANISOU 436 O VAL A 62 993 1109 1171 55 101 -141 O ATOM 437 CB VAL A 62 20.918 51.259 63.177 1.00 8.56 C ANISOU 437 CB VAL A 62 1155 950 1145 110 -45 -166 C ATOM 438 CG1 VAL A 62 19.753 52.062 62.599 1.00 9.42 C ANISOU 438 CG1 VAL A 62 1263 1014 1299 263 73 -190 C ATOM 439 CG2 VAL A 62 21.195 50.034 62.313 1.00 9.39 C ANISOU 439 CG2 VAL A 62 1378 893 1297 149 153 -264 C ATOM 440 N ALA A 63 21.835 54.476 63.793 1.00 7.31 N ANISOU 440 N ALA A 63 927 850 1000 55 158 -129 N ATOM 441 CA ALA A 63 21.318 55.623 64.567 1.00 7.56 C ANISOU 441 CA ALA A 63 1057 831 983 29 72 -86 C ATOM 442 C ALA A 63 19.856 55.795 64.129 1.00 7.56 C ANISOU 442 C ALA A 63 1055 911 905 18 23 -77 C ATOM 443 O ALA A 63 19.567 56.296 63.038 1.00 7.82 O ANISOU 443 O ALA A 63 1039 1063 867 97 15 -154 O ATOM 444 CB ALA A 63 22.123 56.870 64.284 1.00 8.26 C ANISOU 444 CB ALA A 63 1141 1004 991 -13 53 -31 C ATOM 445 N ASP A 64 18.931 55.417 65.007 1.00 7.24 N ANISOU 445 N ASP A 64 1032 701 1017 -7 0 -103 N ATOM 446 CA ASP A 64 17.507 55.419 64.673 1.00 7.72 C ANISOU 446 CA ASP A 64 1134 836 964 -36 -1 -87 C ATOM 447 C ASP A 64 16.924 56.785 65.017 1.00 7.38 C ANISOU 447 C ASP A 64 1136 747 920 -8 19 -101 C ATOM 448 O ASP A 64 16.198 56.921 65.979 1.00 7.96 O ANISOU 448 O ASP A 64 1386 741 895 -85 0 -49 O ATOM 449 CB ASP A 64 16.829 54.278 65.424 1.00 8.33 C ANISOU 449 CB ASP A 64 1151 1013 1001 -6 45 -38 C ATOM 450 CG ASP A 64 15.342 54.174 65.182 1.00 9.52 C ANISOU 450 CG ASP A 64 1254 1228 1132 -66 28 61 C ATOM 451 OD1 ASP A 64 14.809 54.649 64.168 1.00 9.41 O ANISOU 451 OD1 ASP A 64 1238 1236 1099 46 115 147 O ATOM 452 OD2 ASP A 64 14.645 53.581 66.038 1.00 11.76 O ANISOU 452 OD2 ASP A 64 1281 1503 1681 -144 54 246 O ATOM 453 N THR A 65 17.239 57.788 64.200 1.00 7.19 N ANISOU 453 N THR A 65 1088 810 831 -25 63 -114 N ATOM 454 CA THR A 65 16.766 59.146 64.476 1.00 7.66 C ANISOU 454 CA THR A 65 1086 877 947 -13 51 -44 C ATOM 455 C THR A 65 15.368 59.438 63.925 1.00 8.05 C ANISOU 455 C THR A 65 1088 987 980 18 51 -33 C ATOM 456 O THR A 65 14.756 60.433 64.292 1.00 8.79 O ANISOU 456 O THR A 65 1128 1205 1005 176 101 -131 O ATOM 457 CB THR A 65 17.696 60.204 63.873 1.00 7.66 C ANISOU 457 CB THR A 65 1024 948 937 -125 47 2 C ATOM 458 OG1 THR A 65 17.786 60.001 62.462 1.00 10.27 O ANISOU 458 OG1 THR A 65 1419 1541 940 3 80 51 O ATOM 459 CG2 THR A 65 19.092 60.063 64.408 1.00 8.60 C ANISOU 459 CG2 THR A 65 1128 915 1225 -23 26 54 C ATOM 460 N LYS A 66 14.871 58.601 63.013 1.00 8.60 N ANISOU 460 N LYS A 66 1138 1026 1102 30 -10 -18 N ATOM 461 CA LYS A 66 13.575 58.829 62.365 1.00 8.95 C ANISOU 461 CA LYS A 66 1132 1138 1129 -25 -35 7 C ATOM 462 C LYS A 66 13.512 60.269 61.865 1.00 9.54 C ANISOU 462 C LYS A 66 1185 1239 1199 55 -44 69 C ATOM 463 O LYS A 66 12.507 60.981 62.019 1.00 9.06 O ANISOU 463 O LYS A 66 1109 1249 1083 96 -49 22 O ATOM 464 CB LYS A 66 12.425 58.478 63.305 1.00 9.26 C ANISOU 464 CB LYS A 66 1056 1213 1248 43 -35 24 C ATOM 465 CG LYS A 66 12.357 56.970 63.563 1.00 9.48 C ANISOU 465 CG LYS A 66 1243 1181 1177 -125 -42 -67 C ATOM 466 CD LYS A 66 11.132 56.553 64.366 1.00 11.43 C ANISOU 466 CD LYS A 66 1327 1528 1488 25 50 -7 C ATOM 467 CE LYS A 66 10.974 55.030 64.471 1.00 12.14 C ANISOU 467 CE LYS A 66 1489 1620 1504 48 63 156 C ATOM 468 NZ LYS A 66 12.151 54.327 65.101 1.00 12.37 N ANISOU 468 NZ LYS A 66 1290 1845 1562 -69 18 170 N ATOM 469 N CYS A 67 14.634 60.681 61.279 1.00 9.77 N ANISOU 469 N CYS A 67 1266 1193 1250 -10 13 57 N ATOM 470 CA CYS A 67 14.829 62.048 60.795 1.00 10.52 C ANISOU 470 CA CYS A 67 1381 1257 1356 13 -9 53 C ATOM 471 C CYS A 67 13.750 62.503 59.818 1.00 10.70 C ANISOU 471 C CYS A 67 1411 1304 1348 -6 -19 -19 C ATOM 472 O CYS A 67 13.448 61.813 58.838 1.00 10.59 O ANISOU 472 O CYS A 67 1497 1188 1339 -59 -21 -13 O ATOM 473 CB CYS A 67 16.207 62.155 60.165 1.00 10.95 C ANISOU 473 CB CYS A 67 1495 1286 1376 15 22 55 C ATOM 474 SG CYS A 67 16.529 63.682 59.360 1.00 13.58 S ANISOU 474 SG CYS A 67 1695 1635 1830 -69 35 330 S ATOM 475 N ALA A 68 13.152 63.655 60.128 1.00 10.20 N ANISOU 475 N ALA A 68 1362 1212 1302 10 -27 0 N ATOM 476 CA ALA A 68 12.093 64.249 59.298 1.00 10.60 C ANISOU 476 CA ALA A 68 1461 1227 1337 -5 -61 -22 C ATOM 477 C ALA A 68 12.543 65.478 58.520 1.00 10.55 C ANISOU 477 C ALA A 68 1476 1278 1252 64 -7 -16 C ATOM 478 O ALA A 68 11.881 65.836 57.548 1.00 10.11 O ANISOU 478 O ALA A 68 1448 1067 1326 173 -27 -71 O ATOM 479 CB ALA A 68 10.885 64.626 60.149 1.00 10.49 C ANISOU 479 CB ALA A 68 1448 1162 1374 21 -17 45 C ATOM 480 N ASP A 69 13.621 66.122 58.972 1.00 10.64 N ANISOU 480 N ASP A 69 1459 1295 1288 22 11 0 N ATOM 481 CA ASP A 69 14.047 67.388 58.422 1.00 11.15 C ANISOU 481 CA ASP A 69 1457 1411 1367 14 21 -34 C ATOM 482 C ASP A 69 15.509 67.635 58.840 1.00 11.29 C ANISOU 482 C ASP A 69 1443 1422 1425 37 23 -32 C ATOM 483 O ASP A 69 16.042 66.931 59.725 1.00 10.70 O ANISOU 483 O ASP A 69 1530 1094 1440 49 -15 29 O ATOM 484 CB ASP A 69 13.127 68.494 58.963 1.00 11.56 C ANISOU 484 CB ASP A 69 1635 1304 1454 26 -23 -33 C ATOM 485 CG ASP A 69 13.109 69.757 58.124 1.00 14.08 C ANISOU 485 CG ASP A 69 1936 1643 1770 36 2 32 C ATOM 486 OD1 ASP A 69 13.865 69.896 57.136 1.00 15.63 O ANISOU 486 OD1 ASP A 69 2335 1569 2035 167 146 150 O ATOM 487 OD2 ASP A 69 12.357 70.678 58.496 1.00 15.11 O ANISOU 487 OD2 ASP A 69 2042 1552 2148 65 -45 -30 O ATOM 488 N ALA A 70 16.151 68.615 58.200 1.00 11.02 N ANISOU 488 N ALA A 70 1421 1345 1419 78 28 -67 N ATOM 489 CA ALA A 70 17.584 68.862 58.402 1.00 11.51 C ANISOU 489 CA ALA A 70 1478 1444 1449 39 -17 -39 C ATOM 490 C ALA A 70 18.389 67.575 58.193 1.00 12.00 C ANISOU 490 C ALA A 70 1635 1475 1449 9 -20 -59 C ATOM 491 O ALA A 70 19.255 67.200 59.013 1.00 11.02 O ANISOU 491 O ALA A 70 1576 1299 1311 -71 -3 -49 O ATOM 492 CB ALA A 70 17.839 69.478 59.790 1.00 11.54 C ANISOU 492 CB ALA A 70 1418 1489 1478 85 -16 -77 C ATOM 493 N GLY A 71 18.111 66.908 57.068 1.00 11.88 N ANISOU 493 N GLY A 71 1688 1397 1427 -11 -58 -118 N ATOM 494 CA GLY A 71 18.678 65.600 56.808 1.00 11.54 C ANISOU 494 CA GLY A 71 1590 1415 1379 5 -18 -64 C ATOM 495 C GLY A 71 20.187 65.585 56.783 1.00 10.81 C ANISOU 495 C GLY A 71 1484 1287 1334 -23 -31 -77 C ATOM 496 O GLY A 71 20.805 64.690 57.337 1.00 11.31 O ANISOU 496 O GLY A 71 1524 1430 1342 -136 -54 -89 O ATOM 497 N GLY A 72 20.787 66.598 56.173 1.00 10.37 N ANISOU 497 N GLY A 72 1371 1254 1315 21 25 -47 N ATOM 498 CA GLY A 72 22.237 66.683 56.096 1.00 10.17 C ANISOU 498 CA GLY A 72 1362 1159 1342 -16 28 18 C ATOM 499 C GLY A 72 22.884 66.819 57.463 1.00 10.28 C ANISOU 499 C GLY A 72 1363 1159 1382 -10 39 17 C ATOM 500 O GLY A 72 23.912 66.198 57.739 1.00 11.65 O ANISOU 500 O GLY A 72 1548 1357 1519 -1 -5 -7 O ATOM 501 N THR A 73 22.290 67.642 58.316 1.00 9.44 N ANISOU 501 N THR A 73 1287 992 1306 -8 60 34 N ATOM 502 CA THR A 73 22.821 67.903 59.642 1.00 10.33 C ANISOU 502 CA THR A 73 1418 1135 1372 22 68 52 C ATOM 503 C THR A 73 22.690 66.701 60.553 1.00 9.63 C ANISOU 503 C THR A 73 1281 1167 1210 2 65 22 C ATOM 504 O THR A 73 23.654 66.308 61.194 1.00 10.55 O ANISOU 504 O THR A 73 1369 1290 1348 82 126 129 O ATOM 505 CB THR A 73 22.113 69.150 60.273 1.00 9.95 C ANISOU 505 CB THR A 73 1378 1085 1317 8 107 32 C ATOM 506 OG1 THR A 73 22.363 70.298 59.457 1.00 13.12 O ANISOU 506 OG1 THR A 73 2156 1141 1686 112 -10 219 O ATOM 507 CG2 THR A 73 22.628 69.455 61.690 1.00 12.36 C ANISOU 507 CG2 THR A 73 1607 1497 1593 108 98 40 C ATOM 508 N VAL A 74 21.515 66.090 60.594 1.00 9.57 N ANISOU 508 N VAL A 74 1283 1141 1212 0 23 40 N ATOM 509 CA VAL A 74 21.285 64.957 61.509 1.00 9.05 C ANISOU 509 CA VAL A 74 1265 971 1201 2 0 8 C ATOM 510 C VAL A 74 22.155 63.743 61.062 1.00 10.10 C ANISOU 510 C VAL A 74 1439 1098 1298 40 21 -25 C ATOM 511 O VAL A 74 22.766 63.050 61.897 1.00 11.12 O ANISOU 511 O VAL A 74 1638 1195 1390 0 -68 -109 O ATOM 512 CB VAL A 74 19.761 64.627 61.619 1.00 8.66 C ANISOU 512 CB VAL A 74 1234 915 1142 44 15 -8 C ATOM 513 CG1 VAL A 74 19.507 63.340 62.468 1.00 8.26 C ANISOU 513 CG1 VAL A 74 1094 956 1085 -65 -62 139 C ATOM 514 CG2 VAL A 74 18.941 65.846 62.121 1.00 9.62 C ANISOU 514 CG2 VAL A 74 1363 938 1354 36 176 -20 C ATOM 515 N ALA A 75 22.231 63.517 59.751 1.00 10.09 N ANISOU 515 N ALA A 75 1486 1020 1328 80 40 -99 N ATOM 516 CA ALA A 75 23.081 62.444 59.202 1.00 10.22 C ANISOU 516 CA ALA A 75 1408 1103 1370 58 44 -20 C ATOM 517 C ALA A 75 24.540 62.675 59.509 1.00 9.49 C ANISOU 517 C ALA A 75 1320 999 1283 5 30 -40 C ATOM 518 O ALA A 75 25.222 61.789 60.005 1.00 9.60 O ANISOU 518 O ALA A 75 1309 1049 1288 -63 74 17 O ATOM 519 CB ALA A 75 22.871 62.287 57.707 1.00 10.57 C ANISOU 519 CB ALA A 75 1427 1156 1432 98 50 -126 C ATOM 520 N LYS A 76 25.036 63.881 59.229 1.00 9.80 N ANISOU 520 N LYS A 76 1305 1069 1348 9 64 33 N ATOM 521 CA LYS A 76 26.419 64.227 59.603 1.00 9.99 C ANISOU 521 CA LYS A 76 1262 1125 1408 5 6 -44 C ATOM 522 C LYS A 76 26.673 64.060 61.090 1.00 9.46 C ANISOU 522 C LYS A 76 1191 1015 1387 -61 63 -74 C ATOM 523 O LYS A 76 27.690 63.487 61.486 1.00 9.77 O ANISOU 523 O LYS A 76 1166 1085 1459 74 73 -188 O ATOM 524 CB LYS A 76 26.823 65.630 59.152 1.00 11.33 C ANISOU 524 CB LYS A 76 1494 1340 1469 -33 -2 -17 C ATOM 525 CG LYS A 76 28.297 65.945 59.415 1.00 13.83 C ANISOU 525 CG LYS A 76 1692 1729 1833 14 -17 -22 C ATOM 526 CD LYS A 76 28.641 67.401 59.161 1.00 19.40 C ANISOU 526 CD LYS A 76 2552 2369 2449 -92 -6 141 C ATOM 527 CE LYS A 76 30.153 67.584 58.987 1.00 23.12 C ANISOU 527 CE LYS A 76 2974 2804 3005 -91 -12 70 C ATOM 528 NZ LYS A 76 30.465 69.032 58.735 1.00 25.61 N ANISOU 528 NZ LYS A 76 3404 2901 3426 -329 24 87 N ATOM 529 N ASN A 77 25.761 64.548 61.927 1.00 8.84 N ANISOU 529 N ASN A 77 1096 966 1294 -110 46 -92 N ATOM 530 CA ASN A 77 25.939 64.424 63.367 1.00 9.04 C ANISOU 530 CA ASN A 77 1140 1060 1233 -89 -5 -25 C ATOM 531 C ASN A 77 26.099 63.008 63.864 1.00 9.01 C ANISOU 531 C ASN A 77 1190 1073 1160 -31 -19 -62 C ATOM 532 O ASN A 77 26.889 62.767 64.770 1.00 9.72 O ANISOU 532 O ASN A 77 1293 1233 1166 0 -34 -18 O ATOM 533 CB ASN A 77 24.804 65.085 64.143 1.00 8.37 C ANISOU 533 CB ASN A 77 1122 811 1246 -26 9 -30 C ATOM 534 CG ASN A 77 24.854 66.627 64.099 1.00 8.72 C ANISOU 534 CG ASN A 77 1229 757 1327 -65 31 12 C ATOM 535 OD1 ASN A 77 25.872 67.224 63.716 1.00 10.76 O ANISOU 535 OD1 ASN A 77 1563 946 1577 -81 145 105 O ATOM 536 ND2 ASN A 77 23.753 67.263 64.518 1.00 9.71 N ANISOU 536 ND2 ASN A 77 1399 900 1389 52 175 -60 N ATOM 537 N ASN A 78 25.342 62.069 63.284 1.00 8.96 N ANISOU 537 N ASN A 78 1241 1047 1116 -53 -11 13 N ATOM 538 CA ASN A 78 25.439 60.674 63.695 1.00 9.05 C ANISOU 538 CA ASN A 78 1199 1047 1191 39 -22 -23 C ATOM 539 C ASN A 78 26.527 59.907 62.970 1.00 9.08 C ANISOU 539 C ASN A 78 1262 1057 1129 82 2 -29 C ATOM 540 O ASN A 78 27.082 59.000 63.560 1.00 9.26 O ANISOU 540 O ASN A 78 1434 1118 966 217 1 38 O ATOM 541 CB ASN A 78 24.089 59.981 63.563 1.00 8.12 C ANISOU 541 CB ASN A 78 1078 881 1124 10 -29 -13 C ATOM 542 CG ASN A 78 23.122 60.445 64.614 1.00 9.83 C ANISOU 542 CG ASN A 78 1289 1168 1277 -113 -36 -112 C ATOM 543 OD1 ASN A 78 23.147 59.960 65.739 1.00 10.77 O ANISOU 543 OD1 ASN A 78 1586 1220 1284 -208 30 -241 O ATOM 544 ND2 ASN A 78 22.305 61.432 64.268 1.00 9.07 N ANISOU 544 ND2 ASN A 78 1180 1064 1202 81 -31 -32 N ATOM 545 N ALA A 79 26.859 60.290 61.738 1.00 9.49 N ANISOU 545 N ALA A 79 1307 1112 1183 68 80 -28 N ATOM 546 CA ALA A 79 27.960 59.657 60.991 1.00 9.88 C ANISOU 546 CA ALA A 79 1255 1211 1287 100 94 -8 C ATOM 547 C ALA A 79 29.305 59.970 61.640 1.00 9.74 C ANISOU 547 C ALA A 79 1260 1220 1219 123 104 5 C ATOM 548 O ALA A 79 30.185 59.109 61.707 1.00 10.73 O ANISOU 548 O ALA A 79 1210 1573 1292 290 233 6 O ATOM 549 CB ALA A 79 27.964 60.123 59.544 1.00 10.14 C ANISOU 549 CB ALA A 79 1240 1344 1269 32 54 -76 C ATOM 550 N VAL A 80 29.486 61.193 62.140 1.00 9.62 N ANISOU 550 N VAL A 80 1192 1213 1248 72 77 -43 N ATOM 551 CA VAL A 80 30.755 61.507 62.797 1.00 10.35 C ANISOU 551 CA VAL A 80 1315 1194 1422 -33 49 -8 C ATOM 552 C VAL A 80 30.931 60.731 64.103 1.00 9.46 C ANISOU 552 C VAL A 80 1206 1100 1286 -69 27 -35 C ATOM 553 O VAL A 80 32.049 60.533 64.543 1.00 11.03 O ANISOU 553 O VAL A 80 1433 1212 1545 3 57 114 O ATOM 554 CB VAL A 80 30.957 63.022 63.021 1.00 10.91 C ANISOU 554 CB VAL A 80 1411 1257 1478 -61 71 -2 C ATOM 555 CG1 VAL A 80 30.944 63.772 61.699 1.00 11.83 C ANISOU 555 CG1 VAL A 80 1479 1424 1589 37 0 115 C ATOM 556 CG2 VAL A 80 29.942 63.582 63.988 1.00 13.51 C ANISOU 556 CG2 VAL A 80 1815 1556 1759 -33 104 23 C ATOM 557 N ARG A 81 29.823 60.277 64.708 1.00 8.96 N ANISOU 557 N ARG A 81 1225 912 1267 -154 -44 -5 N ATOM 558 CA ARG A 81 29.852 59.444 65.930 1.00 8.85 C ANISOU 558 CA ARG A 81 1197 965 1200 -48 4 -25 C ATOM 559 C ARG A 81 30.179 57.990 65.587 1.00 9.17 C ANISOU 559 C ARG A 81 1164 1056 1264 -102 -23 -34 C ATOM 560 O ARG A 81 30.487 57.200 66.470 1.00 11.02 O ANISOU 560 O ARG A 81 1538 1309 1338 -38 -11 -6 O ATOM 561 CB ARG A 81 28.491 59.499 66.641 1.00 8.63 C ANISOU 561 CB ARG A 81 1212 927 1139 -82 29 -11 C ATOM 562 CG ARG A 81 28.142 60.815 67.320 1.00 8.59 C ANISOU 562 CG ARG A 81 1191 911 1159 68 38 24 C ATOM 563 CD ARG A 81 28.968 61.037 68.549 1.00 8.99 C ANISOU 563 CD ARG A 81 1343 870 1201 21 88 -61 C ATOM 564 NE ARG A 81 28.457 62.142 69.351 1.00 10.85 N ANISOU 564 NE ARG A 81 1517 1240 1365 0 -10 -113 N ATOM 565 CZ ARG A 81 29.078 62.626 70.422 1.00 12.76 C ANISOU 565 CZ ARG A 81 1652 1492 1703 -105 0 -94 C ATOM 566 NH1 ARG A 81 30.252 62.148 70.780 1.00 11.19 N ANISOU 566 NH1 ARG A 81 1465 1047 1740 190 -126 -140 N ATOM 567 NH2 ARG A 81 28.528 63.604 71.132 1.00 11.50 N ANISOU 567 NH2 ARG A 81 1418 1501 1450 74 130 -303 N ATOM 568 N GLY A 82 30.090 57.654 64.310 1.00 9.92 N ANISOU 568 N GLY A 82 1227 1222 1318 -20 -21 -106 N ATOM 569 CA GLY A 82 30.375 56.293 63.831 1.00 10.03 C ANISOU 569 CA GLY A 82 1291 1183 1336 26 -24 -95 C ATOM 570 C GLY A 82 29.203 55.463 63.287 1.00 10.32 C ANISOU 570 C GLY A 82 1278 1266 1375 15 -7 -122 C ATOM 571 O GLY A 82 29.384 54.278 63.010 1.00 11.10 O ANISOU 571 O GLY A 82 1447 1417 1351 17 22 -235 O ATOM 572 N ALA A 83 28.011 56.049 63.119 1.00 10.19 N ANISOU 572 N ALA A 83 1331 1250 1289 4 15 -125 N ATOM 573 CA ALA A 83 26.899 55.294 62.537 1.00 10.34 C ANISOU 573 CA ALA A 83 1339 1242 1345 -12 34 -31 C ATOM 574 C ALA A 83 27.159 54.822 61.117 1.00 10.26 C ANISOU 574 C ALA A 83 1374 1168 1355 -2 68 -77 C ATOM 575 O ALA A 83 27.779 55.538 60.300 1.00 10.22 O ANISOU 575 O ALA A 83 1447 1159 1276 18 143 -138 O ATOM 576 CB ALA A 83 25.598 56.104 62.561 1.00 10.64 C ANISOU 576 CB ALA A 83 1352 1278 1410 29 48 -34 C ATOM 577 N ASP A 84 26.629 53.636 60.808 1.00 9.75 N ANISOU 577 N ASP A 84 1319 1101 1282 23 62 -42 N ATOM 578 CA ASP A 84 26.575 53.153 59.425 1.00 8.55 C ANISOU 578 CA ASP A 84 1161 945 1143 27 51 -63 C ATOM 579 C ASP A 84 25.258 53.487 58.731 1.00 8.56 C ANISOU 579 C ASP A 84 1199 1001 1051 34 79 -38 C ATOM 580 O ASP A 84 25.245 54.007 57.606 1.00 8.65 O ANISOU 580 O ASP A 84 1221 972 1091 92 158 124 O ATOM 581 CB ASP A 84 26.789 51.639 59.413 1.00 9.17 C ANISOU 581 CB ASP A 84 1122 1109 1253 132 33 -54 C ATOM 582 CG ASP A 84 28.180 51.248 59.890 1.00 8.39 C ANISOU 582 CG ASP A 84 1064 1007 1116 186 8 -57 C ATOM 583 OD1 ASP A 84 29.198 51.810 59.385 1.00 10.43 O ANISOU 583 OD1 ASP A 84 1308 1027 1625 4 -26 -3 O ATOM 584 OD2 ASP A 84 28.278 50.361 60.757 1.00 11.26 O ANISOU 584 OD2 ASP A 84 1729 1116 1432 263 50 -110 O ATOM 585 N TRP A 85 24.152 53.189 59.411 1.00 8.70 N ANISOU 585 N TRP A 85 1219 996 1090 28 30 -27 N ATOM 586 CA TRP A 85 22.816 53.389 58.885 1.00 8.77 C ANISOU 586 CA TRP A 85 1147 1027 1158 84 69 -82 C ATOM 587 C TRP A 85 22.101 54.388 59.755 1.00 9.31 C ANISOU 587 C TRP A 85 1231 1143 1160 134 -5 -92 C ATOM 588 O TRP A 85 22.294 54.391 60.953 1.00 9.60 O ANISOU 588 O TRP A 85 1200 1255 1191 298 36 -74 O ATOM 589 CB TRP A 85 22.009 52.100 58.881 1.00 8.94 C ANISOU 589 CB TRP A 85 1179 1028 1188 86 68 -110 C ATOM 590 CG TRP A 85 22.620 51.007 58.051 1.00 9.55 C ANISOU 590 CG TRP A 85 1253 1153 1221 6 -25 -210 C ATOM 591 CD1 TRP A 85 23.583 51.149 57.100 1.00 9.95 C ANISOU 591 CD1 TRP A 85 1434 1177 1170 -38 -48 -115 C ATOM 592 CD2 TRP A 85 22.317 49.607 58.115 1.00 11.49 C ANISOU 592 CD2 TRP A 85 1551 1437 1379 -55 89 -192 C ATOM 593 NE1 TRP A 85 23.894 49.925 56.559 1.00 11.09 N ANISOU 593 NE1 TRP A 85 1574 1387 1252 -26 54 -220 N ATOM 594 CE2 TRP A 85 23.132 48.960 57.161 1.00 10.83 C ANISOU 594 CE2 TRP A 85 1396 1424 1292 -75 27 -136 C ATOM 595 CE3 TRP A 85 21.441 48.834 58.889 1.00 11.52 C ANISOU 595 CE3 TRP A 85 1555 1290 1531 -116 5 -149 C ATOM 596 CZ2 TRP A 85 23.095 47.582 56.958 1.00 11.51 C ANISOU 596 CZ2 TRP A 85 1505 1412 1454 -91 96 -121 C ATOM 597 CZ3 TRP A 85 21.407 47.448 58.695 1.00 10.13 C ANISOU 597 CZ3 TRP A 85 1286 1129 1431 -25 -30 -99 C ATOM 598 CH2 TRP A 85 22.235 46.842 57.742 1.00 9.41 C ANISOU 598 CH2 TRP A 85 1210 1309 1054 -40 27 -131 C ATOM 599 N MET A 86 21.300 55.242 59.127 1.00 9.75 N ANISOU 599 N MET A 86 1266 1217 1220 143 12 -27 N ATOM 600 CA MET A 86 20.403 56.131 59.860 1.00 9.16 C ANISOU 600 CA MET A 86 1163 1157 1161 135 26 21 C ATOM 601 C MET A 86 18.987 55.999 59.308 1.00 8.78 C ANISOU 601 C MET A 86 1182 1108 1045 42 17 -33 C ATOM 602 O MET A 86 18.789 55.890 58.082 1.00 8.81 O ANISOU 602 O MET A 86 1225 1094 1028 72 102 -26 O ATOM 603 CB MET A 86 20.847 57.586 59.750 1.00 9.42 C ANISOU 603 CB MET A 86 1109 1275 1195 67 45 -43 C ATOM 604 CG MET A 86 20.100 58.492 60.703 1.00 8.28 C ANISOU 604 CG MET A 86 845 961 1339 213 -27 95 C ATOM 605 SD MET A 86 20.442 60.242 60.560 1.00 11.61 S ANISOU 605 SD MET A 86 1696 1089 1624 13 84 -115 S ATOM 606 CE MET A 86 19.490 60.729 59.106 1.00 10.86 C ANISOU 606 CE MET A 86 1425 1300 1400 151 -31 38 C ATOM 607 N THR A 87 17.995 56.047 60.195 1.00 8.01 N ANISOU 607 N THR A 87 1105 971 966 4 -9 4 N ATOM 608 CA THR A 87 16.612 56.079 59.748 1.00 8.07 C ANISOU 608 CA THR A 87 1144 975 945 -33 -42 -20 C ATOM 609 C THR A 87 16.095 57.486 59.449 1.00 8.82 C ANISOU 609 C THR A 87 1219 1016 1114 -16 -105 -80 C ATOM 610 O THR A 87 16.383 58.463 60.166 1.00 8.15 O ANISOU 610 O THR A 87 1246 853 997 -34 -201 -175 O ATOM 611 CB THR A 87 15.654 55.380 60.746 1.00 7.90 C ANISOU 611 CB THR A 87 1242 861 898 -97 -76 10 C ATOM 612 OG1 THR A 87 15.713 56.020 62.022 1.00 8.77 O ANISOU 612 OG1 THR A 87 1261 1077 994 -58 -56 -83 O ATOM 613 CG2 THR A 87 16.036 53.892 60.956 1.00 7.70 C ANISOU 613 CG2 THR A 87 1197 777 952 -35 39 24 C ATOM 614 N CYS A 88 15.277 57.574 58.396 1.00 8.95 N ANISOU 614 N CYS A 88 1204 1090 1104 50 -115 -100 N ATOM 615 CA CYS A 88 14.427 58.741 58.155 1.00 8.90 C ANISOU 615 CA CYS A 88 1167 1006 1208 36 -41 -66 C ATOM 616 C CYS A 88 13.001 58.256 58.210 1.00 9.06 C ANISOU 616 C CYS A 88 1180 1070 1191 56 -9 -86 C ATOM 617 O CYS A 88 12.687 57.163 57.683 1.00 10.28 O ANISOU 617 O CYS A 88 1399 1182 1325 0 -37 -122 O ATOM 618 CB CYS A 88 14.651 59.318 56.766 1.00 9.81 C ANISOU 618 CB CYS A 88 1168 1220 1339 43 -52 -58 C ATOM 619 SG CYS A 88 16.106 60.341 56.560 1.00 10.57 S ANISOU 619 SG CYS A 88 1650 1034 1331 -21 23 109 S ATOM 620 N ILE A 89 12.139 59.046 58.851 1.00 8.96 N ANISOU 620 N ILE A 89 1177 1025 1201 47 38 -1 N ATOM 621 CA ILE A 89 10.710 58.769 58.830 1.00 9.68 C ANISOU 621 CA ILE A 89 1232 1139 1308 44 -22 0 C ATOM 622 C ILE A 89 10.220 58.928 57.381 1.00 9.80 C ANISOU 622 C ILE A 89 1211 1189 1323 33 -68 -15 C ATOM 623 O ILE A 89 10.737 59.743 56.618 1.00 9.59 O ANISOU 623 O ILE A 89 1207 1262 1172 -17 -164 -32 O ATOM 624 CB ILE A 89 9.962 59.698 59.860 1.00 10.31 C ANISOU 624 CB ILE A 89 1261 1275 1378 69 17 28 C ATOM 625 CG1 ILE A 89 8.513 59.226 60.108 1.00 9.89 C ANISOU 625 CG1 ILE A 89 1171 1101 1483 42 7 97 C ATOM 626 CG2 ILE A 89 10.041 61.162 59.481 1.00 11.13 C ANISOU 626 CG2 ILE A 89 1435 1318 1475 30 -36 72 C ATOM 627 CD1 ILE A 89 8.452 57.844 60.773 1.00 10.09 C ANISOU 627 CD1 ILE A 89 1186 1299 1347 82 -36 61 C ATOM 628 N CYS A 90 9.226 58.146 56.992 1.00 10.25 N ANISOU 628 N CYS A 90 1373 1157 1362 65 -110 -6 N ATOM 629 CA CYS A 90 8.762 58.161 55.606 1.00 11.47 C ANISOU 629 CA CYS A 90 1533 1429 1396 11 -60 40 C ATOM 630 C CYS A 90 8.123 59.492 55.207 1.00 12.42 C ANISOU 630 C CYS A 90 1672 1553 1494 24 -41 25 C ATOM 631 O CYS A 90 7.958 59.762 54.018 1.00 13.85 O ANISOU 631 O CYS A 90 1967 1705 1590 60 -71 -12 O ATOM 632 CB CYS A 90 7.798 56.995 55.364 1.00 11.11 C ANISOU 632 CB CYS A 90 1528 1360 1332 1 -111 127 C ATOM 633 SG CYS A 90 6.405 56.918 56.523 1.00 12.85 S ANISOU 633 SG CYS A 90 1396 1749 1736 12 -125 274 S ATOM 634 N SER A 91 7.749 60.293 56.204 1.00 13.24 N ANISOU 634 N SER A 91 1743 1662 1625 34 21 -39 N ATOM 635 CA SER A 91 7.225 61.661 56.049 1.00 14.19 C ANISOU 635 CA SER A 91 1906 1724 1759 25 -8 9 C ATOM 636 C SER A 91 8.251 62.643 55.507 1.00 13.95 C ANISOU 636 C SER A 91 1847 1685 1766 79 -45 33 C ATOM 637 O SER A 91 7.891 63.699 54.986 1.00 14.50 O ANISOU 637 O SER A 91 2047 1612 1850 122 -52 139 O ATOM 638 CB SER A 91 6.780 62.216 57.421 1.00 13.99 C ANISOU 638 CB SER A 91 1842 1588 1883 49 34 -69 C ATOM 639 OG SER A 91 5.827 61.411 58.056 1.00 17.45 O ANISOU 639 OG SER A 91 2401 2044 2186 120 40 -158 O ATOM 640 N ALA A 92 9.528 62.377 55.751 1.00 12.97 N ANISOU 640 N ALA A 92 1682 1575 1671 93 42 18 N ATOM 641 CA ALA A 92 10.585 63.231 55.255 1.00 12.19 C ANISOU 641 CA ALA A 92 1600 1495 1534 47 12 0 C ATOM 642 C ALA A 92 10.500 63.379 53.734 1.00 12.05 C ANISOU 642 C ALA A 92 1545 1507 1525 75 35 -24 C ATOM 643 O ALA A 92 10.212 62.426 53.016 1.00 12.83 O ANISOU 643 O ALA A 92 1666 1688 1518 117 7 -58 O ATOM 644 CB ALA A 92 11.945 62.666 55.644 1.00 12.17 C ANISOU 644 CB ALA A 92 1627 1442 1552 45 50 58 C ATOM 645 N THR A 93 10.735 64.579 53.246 1.00 12.14 N ANISOU 645 N THR A 93 1524 1597 1490 63 64 -12 N ATOM 646 CA THR A 93 10.699 64.811 51.810 1.00 12.51 C ANISOU 646 CA THR A 93 1671 1524 1556 55 -20 67 C ATOM 647 C THR A 93 11.896 64.185 51.114 1.00 12.62 C ANISOU 647 C THR A 93 1658 1634 1500 17 -2 25 C ATOM 648 O THR A 93 12.889 63.826 51.757 1.00 12.76 O ANISOU 648 O THR A 93 1670 1741 1437 35 -101 35 O ATOM 649 CB THR A 93 10.709 66.299 51.514 1.00 12.81 C ANISOU 649 CB THR A 93 1746 1548 1574 10 -4 59 C ATOM 650 OG1 THR A 93 11.966 66.836 51.935 1.00 12.78 O ANISOU 650 OG1 THR A 93 1915 1323 1616 5 5 96 O ATOM 651 CG2 THR A 93 9.563 66.998 52.262 1.00 13.02 C ANISOU 651 CG2 THR A 93 1932 1381 1632 148 -23 173 C ATOM 652 N ILE A 94 11.801 64.072 49.793 1.00 13.57 N ANISOU 652 N ILE A 94 1761 1732 1663 42 -19 53 N ATOM 653 CA ILE A 94 12.890 63.554 48.977 1.00 13.43 C ANISOU 653 CA ILE A 94 1830 1735 1535 43 -14 52 C ATOM 654 C ILE A 94 14.157 64.422 49.126 1.00 13.21 C ANISOU 654 C ILE A 94 1757 1747 1515 36 9 16 C ATOM 655 O ILE A 94 15.225 63.877 49.340 1.00 13.29 O ANISOU 655 O ILE A 94 1809 1789 1450 49 87 55 O ATOM 656 CB ILE A 94 12.439 63.375 47.479 1.00 13.30 C ANISOU 656 CB ILE A 94 1820 1640 1593 39 -58 69 C ATOM 657 CG1 ILE A 94 11.438 62.216 47.363 1.00 14.89 C ANISOU 657 CG1 ILE A 94 1990 2017 1649 40 -118 -23 C ATOM 658 CG2 ILE A 94 13.648 63.159 46.574 1.00 14.24 C ANISOU 658 CG2 ILE A 94 2005 1789 1614 78 -37 125 C ATOM 659 CD1 ILE A 94 11.995 60.877 47.753 1.00 15.42 C ANISOU 659 CD1 ILE A 94 1987 2021 1852 -12 -253 -19 C ATOM 660 N PRO A 95 14.061 65.765 49.057 1.00 13.68 N ANISOU 660 N PRO A 95 1787 1793 1614 31 -25 31 N ATOM 661 CA PRO A 95 15.279 66.556 49.339 1.00 13.38 C ANISOU 661 CA PRO A 95 1764 1740 1580 2 -60 24 C ATOM 662 C PRO A 95 15.927 66.283 50.711 1.00 12.74 C ANISOU 662 C PRO A 95 1715 1624 1499 -6 -31 10 C ATOM 663 O PRO A 95 17.150 66.160 50.803 1.00 11.74 O ANISOU 663 O PRO A 95 1721 1472 1266 8 -94 83 O ATOM 664 CB PRO A 95 14.800 68.003 49.195 1.00 14.05 C ANISOU 664 CB PRO A 95 1881 1837 1617 -12 -30 -3 C ATOM 665 CG PRO A 95 13.630 67.907 48.254 1.00 14.16 C ANISOU 665 CG PRO A 95 1807 1807 1766 80 -87 29 C ATOM 666 CD PRO A 95 12.945 66.638 48.630 1.00 13.82 C ANISOU 666 CD PRO A 95 1781 1837 1632 42 -52 -57 C ATOM 667 N THR A 96 15.110 66.145 51.745 1.00 12.23 N ANISOU 667 N THR A 96 1663 1502 1483 23 -60 8 N ATOM 668 CA THR A 96 15.634 65.812 53.077 1.00 11.74 C ANISOU 668 CA THR A 96 1590 1406 1464 -18 -22 -48 C ATOM 669 C THR A 96 16.341 64.436 53.066 1.00 11.34 C ANISOU 669 C THR A 96 1490 1363 1454 1 -29 -47 C ATOM 670 O THR A 96 17.453 64.271 53.601 1.00 10.65 O ANISOU 670 O THR A 96 1495 1108 1443 -17 -44 -21 O ATOM 671 CB THR A 96 14.497 65.804 54.090 1.00 11.38 C ANISOU 671 CB THR A 96 1514 1366 1444 46 -10 -70 C ATOM 672 OG1 THR A 96 14.025 67.139 54.295 1.00 11.64 O ANISOU 672 OG1 THR A 96 1717 1158 1545 -103 38 65 O ATOM 673 CG2 THR A 96 14.954 65.245 55.433 1.00 10.85 C ANISOU 673 CG2 THR A 96 1394 1358 1370 74 -57 -168 C ATOM 674 N MET A 97 15.688 63.432 52.469 1.00 11.55 N ANISOU 674 N MET A 97 1466 1457 1464 -70 -88 -60 N ATOM 675 CA MET A 97 16.296 62.087 52.394 1.00 12.13 C ANISOU 675 CA MET A 97 1608 1531 1470 -57 -57 -45 C ATOM 676 C MET A 97 17.584 62.076 51.563 1.00 12.22 C ANISOU 676 C MET A 97 1623 1522 1496 -57 -64 -76 C ATOM 677 O MET A 97 18.565 61.452 51.954 1.00 11.92 O ANISOU 677 O MET A 97 1696 1383 1448 -28 -59 -208 O ATOM 678 CB MET A 97 15.325 61.047 51.846 1.00 12.47 C ANISOU 678 CB MET A 97 1621 1574 1542 -85 -76 -65 C ATOM 679 CG MET A 97 14.131 60.752 52.747 1.00 12.08 C ANISOU 679 CG MET A 97 1662 1480 1445 -131 -120 -44 C ATOM 680 SD MET A 97 13.208 59.409 52.031 1.00 13.81 S ANISOU 680 SD MET A 97 1936 1410 1898 -8 34 -112 S ATOM 681 CE MET A 97 11.875 59.172 53.233 1.00 11.94 C ANISOU 681 CE MET A 97 1681 1108 1744 -76 9 -145 C ATOM 682 N LYS A 98 17.591 62.788 50.437 1.00 12.53 N ANISOU 682 N LYS A 98 1668 1638 1452 -105 -21 -22 N ATOM 683 CA LYS A 98 18.821 62.891 49.633 1.00 13.65 C ANISOU 683 CA LYS A 98 1767 1790 1627 -12 13 30 C ATOM 684 C LYS A 98 19.934 63.593 50.400 1.00 12.59 C ANISOU 684 C LYS A 98 1636 1635 1512 -29 46 86 C ATOM 685 O LYS A 98 21.094 63.169 50.340 1.00 12.41 O ANISOU 685 O LYS A 98 1523 1702 1487 -20 38 85 O ATOM 686 CB LYS A 98 18.577 63.645 48.323 1.00 13.80 C ANISOU 686 CB LYS A 98 1827 1803 1613 14 -6 86 C ATOM 687 CG LYS A 98 17.987 62.832 47.216 1.00 19.04 C ANISOU 687 CG LYS A 98 2477 2454 2302 18 -20 -10 C ATOM 688 CD LYS A 98 18.038 63.647 45.899 1.00 23.23 C ANISOU 688 CD LYS A 98 3176 2938 2709 -32 -62 127 C ATOM 689 CE LYS A 98 17.354 62.886 44.737 1.00 26.52 C ANISOU 689 CE LYS A 98 3516 3317 3244 -25 -86 3 C ATOM 690 NZ LYS A 98 16.587 63.796 43.787 1.00 27.91 N ANISOU 690 NZ LYS A 98 3699 3610 3292 -121 -103 36 N ATOM 691 N ALA A 99 19.606 64.664 51.119 1.00 11.64 N ANISOU 691 N ALA A 99 1529 1521 1372 12 86 54 N ATOM 692 CA ALA A 99 20.645 65.388 51.862 1.00 11.05 C ANISOU 692 CA ALA A 99 1472 1339 1386 -6 62 22 C ATOM 693 C ALA A 99 21.259 64.499 52.945 1.00 11.36 C ANISOU 693 C ALA A 99 1501 1413 1402 -54 47 17 C ATOM 694 O ALA A 99 22.466 64.536 53.179 1.00 11.53 O ANISOU 694 O ALA A 99 1517 1476 1385 -18 -38 5 O ATOM 695 CB ALA A 99 20.088 66.672 52.483 1.00 10.95 C ANISOU 695 CB ALA A 99 1525 1215 1418 -6 64 106 C ATOM 696 N ALA A 100 20.421 63.669 53.573 1.00 10.19 N ANISOU 696 N ALA A 100 1467 1143 1259 -45 47 12 N ATOM 697 CA ALA A 100 20.864 62.761 54.619 1.00 10.40 C ANISOU 697 CA ALA A 100 1435 1182 1335 14 35 26 C ATOM 698 C ALA A 100 21.750 61.688 54.006 1.00 9.74 C ANISOU 698 C ALA A 100 1440 1028 1231 21 35 97 C ATOM 699 O ALA A 100 22.835 61.405 54.523 1.00 10.27 O ANISOU 699 O ALA A 100 1511 1123 1265 -17 9 9 O ATOM 700 CB ALA A 100 19.670 62.134 55.318 1.00 9.80 C ANISOU 700 CB ALA A 100 1400 1040 1281 44 87 83 C ATOM 701 N ARG A 101 21.323 61.123 52.881 1.00 9.99 N ANISOU 701 N ARG A 101 1426 1131 1238 20 29 113 N ATOM 702 CA ARG A 101 22.150 60.122 52.192 1.00 10.82 C ANISOU 702 CA ARG A 101 1480 1344 1287 21 70 74 C ATOM 703 C ARG A 101 23.507 60.680 51.778 1.00 11.55 C ANISOU 703 C ARG A 101 1534 1500 1352 17 87 -15 C ATOM 704 O ARG A 101 24.536 60.026 51.980 1.00 12.70 O ANISOU 704 O ARG A 101 1670 1776 1380 -8 78 15 O ATOM 705 CB ARG A 101 21.453 59.526 50.979 1.00 10.91 C ANISOU 705 CB ARG A 101 1448 1379 1317 -17 93 60 C ATOM 706 CG ARG A 101 22.317 58.505 50.280 1.00 11.12 C ANISOU 706 CG ARG A 101 1595 1366 1261 -54 41 66 C ATOM 707 CD ARG A 101 21.613 57.750 49.179 1.00 13.12 C ANISOU 707 CD ARG A 101 1811 1497 1676 -97 10 -36 C ATOM 708 NE ARG A 101 21.209 58.600 48.076 1.00 15.61 N ANISOU 708 NE ARG A 101 2039 2131 1760 -74 31 34 N ATOM 709 CZ ARG A 101 21.988 58.945 47.054 1.00 19.95 C ANISOU 709 CZ ARG A 101 2474 2790 2315 43 69 170 C ATOM 710 NH1 ARG A 101 23.252 58.521 46.993 1.00 18.40 N ANISOU 710 NH1 ARG A 101 2289 2778 1921 118 61 204 N ATOM 711 NH2 ARG A 101 21.492 59.719 46.078 1.00 19.38 N ANISOU 711 NH2 ARG A 101 2472 2611 2280 61 -11 348 N ATOM 712 N LYS A 102 23.501 61.868 51.187 1.00 13.00 N ANISOU 712 N LYS A 102 1680 1711 1546 -51 100 -7 N ATOM 713 CA LYS A 102 24.751 62.493 50.760 1.00 14.46 C ANISOU 713 CA LYS A 102 1774 1862 1856 -25 65 -43 C ATOM 714 C LYS A 102 25.690 62.723 51.940 1.00 13.70 C ANISOU 714 C LYS A 102 1708 1740 1758 -6 87 -22 C ATOM 715 O LYS A 102 26.890 62.485 51.828 1.00 13.13 O ANISOU 715 O LYS A 102 1625 1521 1841 46 84 -24 O ATOM 716 CB LYS A 102 24.496 63.788 49.976 1.00 15.80 C ANISOU 716 CB LYS A 102 2009 1973 2018 -4 47 7 C ATOM 717 CG LYS A 102 23.853 63.571 48.596 1.00 19.62 C ANISOU 717 CG LYS A 102 2485 2489 2478 -70 -3 -7 C ATOM 718 CD LYS A 102 23.694 64.912 47.798 1.00 25.32 C ANISOU 718 CD LYS A 102 3311 3186 3120 72 -34 62 C ATOM 719 CE LYS A 102 22.692 64.773 46.594 1.00 27.69 C ANISOU 719 CE LYS A 102 3605 3515 3401 -27 -118 14 C ATOM 720 NZ LYS A 102 22.214 66.080 46.000 1.00 29.36 N ANISOU 720 NZ LYS A 102 3815 3765 3574 100 -40 50 N ATOM 721 N ALA A 103 25.145 63.153 53.076 1.00 12.89 N ANISOU 721 N ALA A 103 1635 1556 1706 -4 60 -57 N ATOM 722 CA ALA A 103 25.979 63.425 54.246 1.00 13.03 C ANISOU 722 CA ALA A 103 1684 1626 1640 12 55 8 C ATOM 723 C ALA A 103 26.565 62.166 54.867 1.00 12.79 C ANISOU 723 C ALA A 103 1668 1504 1686 -45 39 10 C ATOM 724 O ALA A 103 27.735 62.156 55.268 1.00 13.24 O ANISOU 724 O ALA A 103 1806 1502 1723 -62 21 214 O ATOM 725 CB ALA A 103 25.219 64.216 55.292 1.00 13.02 C ANISOU 725 CB ALA A 103 1702 1522 1721 93 73 -8 C ATOM 726 N ILE A 104 25.769 61.090 54.942 1.00 12.97 N ANISOU 726 N ILE A 104 1583 1686 1657 -66 67 24 N ATOM 727 CA ILE A 104 26.258 59.884 55.582 1.00 11.70 C ANISOU 727 CA ILE A 104 1452 1477 1517 -87 90 -59 C ATOM 728 C ILE A 104 27.284 59.189 54.674 1.00 12.23 C ANISOU 728 C ILE A 104 1538 1552 1557 -49 92 -39 C ATOM 729 O ILE A 104 28.262 58.649 55.161 1.00 12.47 O ANISOU 729 O ILE A 104 1580 1571 1585 -80 169 -19 O ATOM 730 CB ILE A 104 25.119 58.933 56.088 1.00 11.78 C ANISOU 730 CB ILE A 104 1462 1574 1438 -42 141 -71 C ATOM 731 CG1 ILE A 104 25.678 57.938 57.112 1.00 11.45 C ANISOU 731 CG1 ILE A 104 1420 1412 1515 -52 166 -95 C ATOM 732 CG2 ILE A 104 24.435 58.261 54.940 1.00 10.69 C ANISOU 732 CG2 ILE A 104 1225 1334 1500 -77 78 -47 C ATOM 733 CD1 ILE A 104 24.610 57.338 58.035 1.00 13.05 C ANISOU 733 CD1 ILE A 104 1578 1761 1617 89 203 62 C ATOM 734 N GLU A 105 27.066 59.256 53.360 1.00 12.57 N ANISOU 734 N GLU A 105 1581 1675 1518 0 116 -50 N ATOM 735 CA GLU A 105 28.023 58.730 52.373 1.00 13.96 C ANISOU 735 CA GLU A 105 1773 1842 1688 13 75 -53 C ATOM 736 C GLU A 105 29.327 59.512 52.370 1.00 14.31 C ANISOU 736 C GLU A 105 1786 1928 1721 13 104 -48 C ATOM 737 O GLU A 105 30.395 58.939 52.154 1.00 14.58 O ANISOU 737 O GLU A 105 1900 1894 1743 141 114 -60 O ATOM 738 CB GLU A 105 27.435 58.748 50.969 1.00 14.05 C ANISOU 738 CB GLU A 105 1762 1894 1681 -35 73 -56 C ATOM 739 CG GLU A 105 26.442 57.640 50.715 1.00 15.23 C ANISOU 739 CG GLU A 105 1930 2062 1792 -103 89 -24 C ATOM 740 CD GLU A 105 25.823 57.713 49.338 1.00 18.29 C ANISOU 740 CD GLU A 105 2414 2459 2075 -166 23 8 C ATOM 741 OE1 GLU A 105 26.198 58.603 48.541 1.00 21.16 O ANISOU 741 OE1 GLU A 105 3050 2805 2184 -433 93 211 O ATOM 742 OE2 GLU A 105 24.929 56.909 49.067 1.00 16.64 O ANISOU 742 OE2 GLU A 105 2423 2176 1720 -338 67 17 O ATOM 743 N ASP A 106 29.255 60.818 52.610 1.00 14.52 N ANISOU 743 N ASP A 106 1821 1919 1777 44 122 -51 N ATOM 744 CA ASP A 106 30.468 61.638 52.617 1.00 15.78 C ANISOU 744 CA ASP A 106 1964 2034 1996 -25 68 -38 C ATOM 745 C ASP A 106 31.426 61.210 53.732 1.00 15.41 C ANISOU 745 C ASP A 106 1876 1980 1999 5 91 -1 C ATOM 746 O ASP A 106 32.641 61.146 53.532 1.00 15.71 O ANISOU 746 O ASP A 106 1773 2210 1984 -52 87 93 O ATOM 747 CB ASP A 106 30.121 63.112 52.800 1.00 16.49 C ANISOU 747 CB ASP A 106 2075 2057 2131 25 92 18 C ATOM 748 CG ASP A 106 31.334 64.000 52.678 1.00 21.42 C ANISOU 748 CG ASP A 106 2658 2725 2753 -120 96 -19 C ATOM 749 OD1 ASP A 106 31.981 63.960 51.611 1.00 25.35 O ANISOU 749 OD1 ASP A 106 3120 3325 3185 -109 153 106 O ATOM 750 OD2 ASP A 106 31.699 64.729 53.621 1.00 26.32 O ANISOU 750 OD2 ASP A 106 3324 3324 3350 -224 207 -66 O ATOM 751 N ILE A 107 30.882 60.894 54.908 1.00 15.18 N ANISOU 751 N ILE A 107 1867 1982 1919 -29 91 -30 N ATOM 752 CA ILE A 107 31.700 60.492 56.047 1.00 15.96 C ANISOU 752 CA ILE A 107 2006 2053 2003 -19 79 4 C ATOM 753 C ILE A 107 32.019 58.987 56.055 1.00 15.55 C ANISOU 753 C ILE A 107 1897 2057 1951 14 30 -3 C ATOM 754 O ILE A 107 33.117 58.568 56.451 1.00 15.57 O ANISOU 754 O ILE A 107 1843 2160 1912 10 -41 42 O ATOM 755 CB ILE A 107 31.021 60.949 57.380 1.00 16.67 C ANISOU 755 CB ILE A 107 2124 2164 2044 -20 84 -10 C ATOM 756 CG1 ILE A 107 31.232 62.457 57.603 1.00 19.31 C ANISOU 756 CG1 ILE A 107 2543 2418 2375 -37 4 25 C ATOM 757 CG2 ILE A 107 31.531 60.122 58.577 1.00 17.64 C ANISOU 757 CG2 ILE A 107 2279 2267 2153 42 89 48 C ATOM 758 CD1 ILE A 107 32.681 62.888 57.699 1.00 22.10 C ANISOU 758 CD1 ILE A 107 2829 2717 2848 -15 59 0 C ATOM 759 N ASN A 108 31.067 58.197 55.566 1.00 14.46 N ANISOU 759 N ASN A 108 1756 1940 1795 -34 63 0 N ATOM 760 CA ASN A 108 31.141 56.749 55.572 1.00 14.53 C ANISOU 760 CA ASN A 108 1834 1921 1764 -21 58 -11 C ATOM 761 C ASN A 108 30.821 56.175 54.173 1.00 14.70 C ANISOU 761 C ASN A 108 1855 1970 1760 -56 50 -5 C ATOM 762 O ASN A 108 29.742 55.627 53.941 1.00 14.04 O ANISOU 762 O ASN A 108 1873 1868 1591 -68 -14 28 O ATOM 763 CB ASN A 108 30.137 56.223 56.632 1.00 13.95 C ANISOU 763 CB ASN A 108 1786 1814 1699 -42 95 -21 C ATOM 764 CG ASN A 108 30.259 54.705 56.917 1.00 14.84 C ANISOU 764 CG ASN A 108 1948 1886 1805 59 148 -39 C ATOM 765 OD1 ASN A 108 30.883 53.911 56.165 1.00 12.82 O ANISOU 765 OD1 ASN A 108 1846 1278 1744 223 214 -176 O ATOM 766 ND2 ASN A 108 29.617 54.292 58.001 1.00 13.72 N ANISOU 766 ND2 ASN A 108 1664 1802 1747 66 148 38 N ATOM 767 N PRO A 109 31.731 56.344 53.209 1.00 15.26 N ANISOU 767 N PRO A 109 1880 2007 1910 -42 75 -21 N ATOM 768 CA PRO A 109 31.445 55.863 51.850 1.00 15.74 C ANISOU 768 CA PRO A 109 1943 2049 1986 -40 102 -14 C ATOM 769 C PRO A 109 31.227 54.368 51.735 1.00 16.69 C ANISOU 769 C PRO A 109 2025 2196 2119 -37 126 -61 C ATOM 770 O PRO A 109 30.423 53.951 50.899 1.00 16.88 O ANISOU 770 O PRO A 109 2102 2150 2160 -106 102 -146 O ATOM 771 CB PRO A 109 32.674 56.294 51.039 1.00 15.55 C ANISOU 771 CB PRO A 109 1904 2084 1918 -7 116 -2 C ATOM 772 CG PRO A 109 33.687 56.713 51.991 1.00 16.05 C ANISOU 772 CG PRO A 109 1970 2137 1991 0 118 -58 C ATOM 773 CD PRO A 109 33.037 57.028 53.299 1.00 15.99 C ANISOU 773 CD PRO A 109 1929 2162 1982 -47 94 -18 C ATOM 774 N ASP A 110 31.904 53.588 52.570 1.00 18.03 N ANISOU 774 N ASP A 110 2206 2312 2330 -24 139 -38 N ATOM 775 CA ASP A 110 31.868 52.126 52.456 1.00 19.53 C ANISOU 775 CA ASP A 110 2425 2479 2516 -40 108 -56 C ATOM 776 C ASP A 110 30.529 51.534 52.883 1.00 18.78 C ANISOU 776 C ASP A 110 2330 2385 2419 -8 120 -87 C ATOM 777 O ASP A 110 30.053 50.596 52.255 1.00 18.90 O ANISOU 777 O ASP A 110 2346 2338 2498 38 179 -180 O ATOM 778 CB ASP A 110 32.955 51.476 53.298 1.00 20.94 C ANISOU 778 CB ASP A 110 2610 2664 2681 -38 89 -45 C ATOM 779 CG ASP A 110 34.349 51.880 52.880 1.00 25.16 C ANISOU 779 CG ASP A 110 3049 3260 3250 -70 80 0 C ATOM 780 OD1 ASP A 110 34.506 52.449 51.773 1.00 27.78 O ANISOU 780 OD1 ASP A 110 3453 3654 3448 -79 141 92 O ATOM 781 OD2 ASP A 110 35.307 51.658 53.659 1.00 28.79 O ANISOU 781 OD2 ASP A 110 3355 3844 3737 -58 15 -43 O ATOM 782 N LYS A 111 29.950 52.067 53.963 1.00 17.25 N ANISOU 782 N LYS A 111 2151 2201 2199 38 121 -62 N ATOM 783 CA LYS A 111 28.756 51.463 54.564 1.00 16.27 C ANISOU 783 CA LYS A 111 2094 2014 2074 31 74 -28 C ATOM 784 C LYS A 111 27.561 52.423 54.751 1.00 14.83 C ANISOU 784 C LYS A 111 1929 1810 1893 3 79 -32 C ATOM 785 O LYS A 111 26.451 51.964 55.016 1.00 14.54 O ANISOU 785 O LYS A 111 1956 1685 1882 23 107 -44 O ATOM 786 CB LYS A 111 29.111 50.828 55.925 1.00 16.65 C ANISOU 786 CB LYS A 111 2176 2041 2109 39 57 20 C ATOM 787 CG LYS A 111 30.152 49.679 55.940 1.00 18.42 C ANISOU 787 CG LYS A 111 2305 2341 2350 99 53 -55 C ATOM 788 CD LYS A 111 29.974 48.747 57.195 1.00 19.84 C ANISOU 788 CD LYS A 111 2616 2399 2521 110 2 44 C ATOM 789 CE LYS A 111 30.758 49.205 58.500 1.00 21.11 C ANISOU 789 CE LYS A 111 2760 2658 2603 120 22 73 C ATOM 790 NZ LYS A 111 30.399 48.579 59.898 1.00 18.27 N ANISOU 790 NZ LYS A 111 2411 2198 2332 295 0 38 N ATOM 791 N GLY A 112 27.777 53.738 54.607 1.00 12.92 N ANISOU 791 N GLY A 112 1662 1637 1608 51 59 -28 N ATOM 792 CA GLY A 112 26.753 54.746 54.886 1.00 12.40 C ANISOU 792 CA GLY A 112 1617 1578 1516 -38 35 -42 C ATOM 793 C GLY A 112 25.476 54.617 54.081 1.00 11.52 C ANISOU 793 C GLY A 112 1517 1441 1418 18 56 -12 C ATOM 794 O GLY A 112 25.514 54.608 52.852 1.00 11.96 O ANISOU 794 O GLY A 112 1608 1583 1352 -11 100 33 O ATOM 795 N GLU A 113 24.342 54.526 54.774 1.00 10.47 N ANISOU 795 N GLU A 113 1462 1231 1284 -16 112 -50 N ATOM 796 CA GLU A 113 23.045 54.371 54.136 1.00 10.06 C ANISOU 796 CA GLU A 113 1402 1240 1178 31 75 -48 C ATOM 797 C GLU A 113 21.919 54.956 54.970 1.00 9.84 C ANISOU 797 C GLU A 113 1366 1245 1126 29 28 -13 C ATOM 798 O GLU A 113 22.020 55.022 56.216 1.00 10.82 O ANISOU 798 O GLU A 113 1536 1405 1169 34 9 -39 O ATOM 799 CB GLU A 113 22.716 52.879 53.966 1.00 10.18 C ANISOU 799 CB GLU A 113 1368 1241 1259 -8 82 -112 C ATOM 800 CG GLU A 113 23.539 52.117 52.941 1.00 11.98 C ANISOU 800 CG GLU A 113 1701 1506 1344 -59 187 -142 C ATOM 801 CD GLU A 113 22.840 50.846 52.503 1.00 13.70 C ANISOU 801 CD GLU A 113 1779 1724 1701 -38 58 -123 C ATOM 802 OE1 GLU A 113 21.659 50.918 52.087 1.00 14.86 O ANISOU 802 OE1 GLU A 113 1772 1987 1885 -145 66 -247 O ATOM 803 OE2 GLU A 113 23.475 49.781 52.595 1.00 16.72 O ANISOU 803 OE2 GLU A 113 2189 1795 2369 19 2 -217 O ATOM 804 N ILE A 114 20.842 55.311 54.269 1.00 8.60 N ANISOU 804 N ILE A 114 1194 1072 998 0 71 -14 N ATOM 805 CA ILE A 114 19.575 55.710 54.857 1.00 8.75 C ANISOU 805 CA ILE A 114 1210 1084 1031 -6 24 -3 C ATOM 806 C ILE A 114 18.581 54.541 54.770 1.00 9.15 C ANISOU 806 C ILE A 114 1297 1112 1064 5 27 -31 C ATOM 807 O ILE A 114 18.578 53.744 53.804 1.00 10.01 O ANISOU 807 O ILE A 114 1413 1221 1169 145 27 -91 O ATOM 808 CB ILE A 114 19.033 56.985 54.161 1.00 8.17 C ANISOU 808 CB ILE A 114 1226 1020 858 -15 37 7 C ATOM 809 CG1 ILE A 114 20.071 58.106 54.244 1.00 8.41 C ANISOU 809 CG1 ILE A 114 1295 1060 841 -145 140 159 C ATOM 810 CG2 ILE A 114 17.691 57.433 54.743 1.00 8.66 C ANISOU 810 CG2 ILE A 114 1193 947 1151 -79 -26 -31 C ATOM 811 CD1 ILE A 114 20.512 58.499 55.621 1.00 9.53 C ANISOU 811 CD1 ILE A 114 1413 1063 1143 -95 45 74 C ATOM 812 N GLN A 115 17.763 54.431 55.816 1.00 8.89 N ANISOU 812 N GLN A 115 1294 1027 1054 -32 95 -8 N ATOM 813 CA GLN A 115 16.664 53.462 55.883 1.00 8.38 C ANISOU 813 CA GLN A 115 1203 1051 930 -29 31 -33 C ATOM 814 C GLN A 115 15.376 54.237 56.114 1.00 8.70 C ANISOU 814 C GLN A 115 1237 1094 973 1 -19 23 C ATOM 815 O GLN A 115 15.333 55.103 56.976 1.00 8.85 O ANISOU 815 O GLN A 115 1303 1123 936 92 -25 0 O ATOM 816 CB GLN A 115 16.861 52.510 57.069 1.00 7.58 C ANISOU 816 CB GLN A 115 1128 802 947 -29 -9 -9 C ATOM 817 CG GLN A 115 18.222 51.822 57.176 1.00 7.87 C ANISOU 817 CG GLN A 115 1085 1050 852 -70 63 38 C ATOM 818 CD GLN A 115 18.283 50.910 58.383 1.00 7.13 C ANISOU 818 CD GLN A 115 970 856 882 80 -103 -15 C ATOM 819 OE1 GLN A 115 18.137 51.396 59.514 1.00 8.36 O ANISOU 819 OE1 GLN A 115 1709 509 956 113 2 -106 O ATOM 820 NE2 GLN A 115 18.415 49.586 58.154 1.00 8.15 N ANISOU 820 NE2 GLN A 115 1095 891 1110 -72 -166 16 N ATOM 821 N VAL A 116 14.317 53.881 55.391 1.00 8.48 N ANISOU 821 N VAL A 116 1187 1157 878 -41 -18 65 N ATOM 822 CA VAL A 116 13.025 54.526 55.551 1.00 9.11 C ANISOU 822 CA VAL A 116 1259 1196 1006 -52 26 14 C ATOM 823 C VAL A 116 12.159 53.737 56.552 1.00 8.88 C ANISOU 823 C VAL A 116 1184 1117 1071 -129 95 -38 C ATOM 824 O VAL A 116 11.792 52.570 56.347 1.00 9.11 O ANISOU 824 O VAL A 116 1414 1019 1025 -105 129 -170 O ATOM 825 CB VAL A 116 12.254 54.655 54.244 1.00 8.72 C ANISOU 825 CB VAL A 116 1174 1216 923 -47 -1 -17 C ATOM 826 CG1 VAL A 116 10.952 55.441 54.475 1.00 10.50 C ANISOU 826 CG1 VAL A 116 1387 1389 1213 21 -78 47 C ATOM 827 CG2 VAL A 116 13.085 55.387 53.188 1.00 9.25 C ANISOU 827 CG2 VAL A 116 1513 1134 865 -78 34 48 C ATOM 828 N GLU A 117 11.802 54.420 57.634 1.00 9.10 N ANISOU 828 N GLU A 117 1252 1088 1114 -112 101 -140 N ATOM 829 CA GLU A 117 10.885 53.921 58.658 1.00 8.86 C ANISOU 829 CA GLU A 117 1174 1055 1135 -64 21 -59 C ATOM 830 C GLU A 117 9.439 54.111 58.221 1.00 9.17 C ANISOU 830 C GLU A 117 1204 1068 1212 15 18 -34 C ATOM 831 O GLU A 117 9.009 55.227 57.965 1.00 9.37 O ANISOU 831 O GLU A 117 1176 1023 1360 29 -55 31 O ATOM 832 CB GLU A 117 11.157 54.631 59.999 1.00 8.89 C ANISOU 832 CB GLU A 117 1160 1119 1098 -14 0 -100 C ATOM 833 CG GLU A 117 12.284 53.979 60.819 1.00 8.98 C ANISOU 833 CG GLU A 117 1270 997 1142 -100 -111 -75 C ATOM 834 CD GLU A 117 11.875 52.711 61.566 1.00 11.08 C ANISOU 834 CD GLU A 117 1539 1307 1361 13 -6 -39 C ATOM 835 OE1 GLU A 117 10.732 52.252 61.389 1.00 11.99 O ANISOU 835 OE1 GLU A 117 1646 1374 1534 -146 18 164 O ATOM 836 OE2 GLU A 117 12.696 52.170 62.335 1.00 12.51 O ANISOU 836 OE2 GLU A 117 1820 1516 1415 8 -48 -75 O ATOM 837 N LEU A 118 8.716 53.002 58.099 1.00 8.34 N ANISOU 837 N LEU A 118 1073 987 1108 -20 -34 -36 N ATOM 838 CA LEU A 118 7.371 52.987 57.520 1.00 8.13 C ANISOU 838 CA LEU A 118 1064 920 1105 -8 22 -46 C ATOM 839 C LEU A 118 6.314 53.117 58.594 1.00 8.59 C ANISOU 839 C LEU A 118 1156 981 1124 18 7 -27 C ATOM 840 O LEU A 118 6.131 52.196 59.398 1.00 8.67 O ANISOU 840 O LEU A 118 1172 956 1163 -31 56 72 O ATOM 841 CB LEU A 118 7.175 51.712 56.694 1.00 8.07 C ANISOU 841 CB LEU A 118 1095 889 1082 -37 -77 -82 C ATOM 842 CG LEU A 118 8.137 51.519 55.523 1.00 9.19 C ANISOU 842 CG LEU A 118 1189 933 1370 -65 -52 -43 C ATOM 843 CD1 LEU A 118 7.907 50.175 54.872 1.00 9.89 C ANISOU 843 CD1 LEU A 118 1464 838 1453 -7 -216 -65 C ATOM 844 CD2 LEU A 118 7.996 52.596 54.465 1.00 11.27 C ANISOU 844 CD2 LEU A 118 1553 1482 1244 3 -151 121 C ATOM 845 N TYR A 119 5.678 54.298 58.629 1.00 8.64 N ANISOU 845 N TYR A 119 1118 995 1169 41 5 15 N ATOM 846 CA TYR A 119 4.562 54.608 59.517 1.00 10.12 C ANISOU 846 CA TYR A 119 1264 1229 1351 61 -32 -53 C ATOM 847 C TYR A 119 3.445 55.282 58.738 1.00 10.92 C ANISOU 847 C TYR A 119 1412 1203 1533 51 -42 -22 C ATOM 848 O TYR A 119 3.696 56.108 57.859 1.00 12.72 O ANISOU 848 O TYR A 119 1541 1571 1719 100 -3 -37 O ATOM 849 CB TYR A 119 5.003 55.545 60.648 1.00 9.80 C ANISOU 849 CB TYR A 119 1312 1039 1370 45 -26 -36 C ATOM 850 CG TYR A 119 5.811 54.833 61.722 1.00 9.35 C ANISOU 850 CG TYR A 119 1198 1199 1153 25 26 -175 C ATOM 851 CD1 TYR A 119 5.203 54.347 62.870 1.00 11.47 C ANISOU 851 CD1 TYR A 119 1431 1499 1427 30 18 -65 C ATOM 852 CD2 TYR A 119 7.174 54.571 61.552 1.00 10.21 C ANISOU 852 CD2 TYR A 119 1259 1231 1390 -70 -19 -94 C ATOM 853 CE1 TYR A 119 5.924 53.692 63.839 1.00 9.35 C ANISOU 853 CE1 TYR A 119 1107 1273 1172 -151 72 -114 C ATOM 854 CE2 TYR A 119 7.904 53.888 62.511 1.00 8.68 C ANISOU 854 CE2 TYR A 119 1433 875 991 -4 23 -135 C ATOM 855 CZ TYR A 119 7.273 53.455 63.659 1.00 9.15 C ANISOU 855 CZ TYR A 119 1270 953 1251 13 -28 -233 C ATOM 856 OH TYR A 119 7.982 52.796 64.641 1.00 11.20 O ANISOU 856 OH TYR A 119 1537 1193 1526 200 -122 -156 O ATOM 857 N GLY A 120 2.212 54.964 59.119 1.00 12.58 N ANISOU 857 N GLY A 120 1515 1511 1751 68 2 7 N ATOM 858 CA GLY A 120 1.031 55.609 58.553 1.00 14.48 C ANISOU 858 CA GLY A 120 1802 1737 1960 74 -23 -42 C ATOM 859 C GLY A 120 0.778 55.219 57.111 1.00 16.08 C ANISOU 859 C GLY A 120 2035 1988 2085 34 -15 -29 C ATOM 860 O GLY A 120 1.197 54.129 56.683 1.00 15.68 O ANISOU 860 O GLY A 120 2003 1866 2085 -34 -15 -120 O ATOM 861 N ASP A 121 0.132 56.113 56.369 1.00 18.37 N ANISOU 861 N ASP A 121 2319 2324 2336 57 -22 -11 N ATOM 862 CA ASP A 121 -0.376 55.829 55.019 1.00 20.14 C ANISOU 862 CA ASP A 121 2558 2585 2506 43 -33 9 C ATOM 863 C ASP A 121 0.602 56.092 53.876 1.00 19.64 C ANISOU 863 C ASP A 121 2487 2493 2480 61 -37 38 C ATOM 864 O ASP A 121 0.313 56.861 52.930 1.00 20.99 O ANISOU 864 O ASP A 121 2707 2627 2639 131 -76 87 O ATOM 865 CB ASP A 121 -1.634 56.673 54.774 1.00 21.42 C ANISOU 865 CB ASP A 121 2683 2786 2668 70 -52 -3 C ATOM 866 CG ASP A 121 -2.742 56.337 55.719 1.00 25.33 C ANISOU 866 CG ASP A 121 3114 3314 3193 -5 37 5 C ATOM 867 OD1 ASP A 121 -2.948 55.127 55.992 1.00 28.61 O ANISOU 867 OD1 ASP A 121 3550 3531 3786 -117 -24 -66 O ATOM 868 OD2 ASP A 121 -3.435 57.251 56.214 1.00 29.65 O ANISOU 868 OD2 ASP A 121 3617 3788 3859 65 42 -134 O ATOM 869 N TRP A 122 1.749 55.446 53.924 1.00 17.85 N ANISOU 869 N TRP A 122 2253 2249 2279 52 -59 91 N ATOM 870 CA TRP A 122 2.711 55.563 52.837 1.00 16.69 C ANISOU 870 CA TRP A 122 2067 2115 2160 40 -65 49 C ATOM 871 C TRP A 122 2.241 54.750 51.639 1.00 16.18 C ANISOU 871 C TRP A 122 1988 2055 2102 28 -81 72 C ATOM 872 O TRP A 122 1.475 53.795 51.802 1.00 17.04 O ANISOU 872 O TRP A 122 2135 2081 2256 -8 -124 78 O ATOM 873 CB TRP A 122 4.107 55.110 53.286 1.00 16.47 C ANISOU 873 CB TRP A 122 1974 2151 2130 36 -74 58 C ATOM 874 CG TRP A 122 4.132 53.701 53.685 1.00 15.26 C ANISOU 874 CG TRP A 122 1864 1915 2019 5 -73 12 C ATOM 875 CD1 TRP A 122 3.862 53.207 54.914 1.00 14.64 C ANISOU 875 CD1 TRP A 122 1771 1852 1939 63 -129 29 C ATOM 876 CD2 TRP A 122 4.386 52.568 52.836 1.00 12.91 C ANISOU 876 CD2 TRP A 122 1465 1779 1658 8 -97 51 C ATOM 877 NE1 TRP A 122 3.949 51.831 54.894 1.00 13.82 N ANISOU 877 NE1 TRP A 122 1890 1631 1729 138 -41 131 N ATOM 878 CE2 TRP A 122 4.274 51.417 53.632 1.00 12.56 C ANISOU 878 CE2 TRP A 122 1537 1652 1581 36 -218 -22 C ATOM 879 CE3 TRP A 122 4.732 52.420 51.491 1.00 12.60 C ANISOU 879 CE3 TRP A 122 1500 1655 1632 15 -159 -20 C ATOM 880 CZ2 TRP A 122 4.474 50.142 53.129 1.00 11.59 C ANISOU 880 CZ2 TRP A 122 1444 1366 1593 52 -76 196 C ATOM 881 CZ3 TRP A 122 4.907 51.160 50.983 1.00 11.68 C ANISOU 881 CZ3 TRP A 122 1415 1491 1529 70 -98 127 C ATOM 882 CH2 TRP A 122 4.791 50.028 51.806 1.00 11.50 C ANISOU 882 CH2 TRP A 122 1515 1368 1486 -32 -82 153 C ATOM 883 N THR A 123 2.688 55.138 50.453 1.00 15.57 N ANISOU 883 N THR A 123 1937 1976 2001 42 -62 44 N ATOM 884 CA THR A 123 2.290 54.487 49.206 1.00 14.93 C ANISOU 884 CA THR A 123 1880 1927 1865 29 -77 97 C ATOM 885 C THR A 123 3.487 53.878 48.449 1.00 14.33 C ANISOU 885 C THR A 123 1830 1810 1805 50 -108 74 C ATOM 886 O THR A 123 4.650 54.228 48.691 1.00 13.39 O ANISOU 886 O THR A 123 1773 1736 1579 18 -211 172 O ATOM 887 CB THR A 123 1.611 55.503 48.254 1.00 15.27 C ANISOU 887 CB THR A 123 1946 1915 1938 71 -72 56 C ATOM 888 OG1 THR A 123 2.579 56.466 47.826 1.00 16.45 O ANISOU 888 OG1 THR A 123 2043 2170 2034 191 -106 232 O ATOM 889 CG2 THR A 123 0.472 56.253 48.931 1.00 15.88 C ANISOU 889 CG2 THR A 123 2011 2055 1965 104 -139 124 C ATOM 890 N TYR A 124 3.195 52.981 47.507 1.00 13.38 N ANISOU 890 N TYR A 124 1735 1689 1658 -21 -99 100 N ATOM 891 CA TYR A 124 4.225 52.439 46.631 1.00 13.71 C ANISOU 891 CA TYR A 124 1812 1654 1740 -18 -43 74 C ATOM 892 C TYR A 124 4.786 53.496 45.640 1.00 14.40 C ANISOU 892 C TYR A 124 1877 1736 1857 -36 -19 59 C ATOM 893 O TYR A 124 5.927 53.386 45.189 1.00 14.53 O ANISOU 893 O TYR A 124 1920 1641 1960 -22 -39 72 O ATOM 894 CB TYR A 124 3.694 51.226 45.887 1.00 12.91 C ANISOU 894 CB TYR A 124 1717 1546 1641 -38 -14 89 C ATOM 895 CG TYR A 124 3.374 50.058 46.807 1.00 13.90 C ANISOU 895 CG TYR A 124 1877 1604 1800 -72 -17 120 C ATOM 896 CD1 TYR A 124 4.398 49.397 47.480 1.00 12.05 C ANISOU 896 CD1 TYR A 124 1728 1407 1442 -61 -4 136 C ATOM 897 CD2 TYR A 124 2.061 49.611 46.994 1.00 15.49 C ANISOU 897 CD2 TYR A 124 1899 1975 2009 15 -49 152 C ATOM 898 CE1 TYR A 124 4.130 48.311 48.324 1.00 12.60 C ANISOU 898 CE1 TYR A 124 1728 1558 1500 -21 17 133 C ATOM 899 CE2 TYR A 124 1.781 48.513 47.840 1.00 14.64 C ANISOU 899 CE2 TYR A 124 1760 1913 1888 -50 -56 192 C ATOM 900 CZ TYR A 124 2.824 47.886 48.508 1.00 13.71 C ANISOU 900 CZ TYR A 124 1753 1734 1719 -101 45 262 C ATOM 901 OH TYR A 124 2.589 46.795 49.334 1.00 13.86 O ANISOU 901 OH TYR A 124 1827 1704 1732 42 -197 475 O ATOM 902 N ASP A 125 3.995 54.516 45.315 1.00 15.21 N ANISOU 902 N ASP A 125 1985 1852 1940 -38 -62 1 N ATOM 903 CA ASP A 125 4.500 55.609 44.490 1.00 16.25 C ANISOU 903 CA ASP A 125 2113 1981 2080 -24 -71 38 C ATOM 904 C ASP A 125 5.574 56.384 45.258 1.00 15.32 C ANISOU 904 C ASP A 125 2020 1825 1974 -14 -49 37 C ATOM 905 O ASP A 125 6.626 56.708 44.702 1.00 15.28 O ANISOU 905 O ASP A 125 2054 1794 1956 -12 -71 99 O ATOM 906 CB ASP A 125 3.359 56.518 44.013 1.00 17.23 C ANISOU 906 CB ASP A 125 2205 2139 2201 11 -106 39 C ATOM 907 CG ASP A 125 2.386 55.779 43.102 1.00 21.04 C ANISOU 907 CG ASP A 125 2699 2643 2651 -12 -85 27 C ATOM 908 OD1 ASP A 125 2.840 54.984 42.249 1.00 25.52 O ANISOU 908 OD1 ASP A 125 3409 3290 2997 -57 -174 -85 O ATOM 909 OD2 ASP A 125 1.164 55.915 43.228 1.00 26.44 O ANISOU 909 OD2 ASP A 125 3130 3457 3456 1 -140 -14 O ATOM 910 N GLN A 126 5.338 56.615 46.545 1.00 14.89 N ANISOU 910 N GLN A 126 1968 1782 1904 -28 -65 36 N ATOM 911 CA GLN A 126 6.365 57.214 47.406 1.00 14.79 C ANISOU 911 CA GLN A 126 1943 1803 1870 -37 -27 39 C ATOM 912 C GLN A 126 7.587 56.299 47.485 1.00 14.31 C ANISOU 912 C GLN A 126 1916 1761 1759 -31 -43 67 C ATOM 913 O GLN A 126 8.728 56.756 47.345 1.00 13.69 O ANISOU 913 O GLN A 126 1921 1604 1673 -59 15 228 O ATOM 914 CB GLN A 126 5.803 57.487 48.805 1.00 14.96 C ANISOU 914 CB GLN A 126 1965 1777 1941 -57 10 32 C ATOM 915 CG GLN A 126 4.716 58.554 48.873 1.00 16.61 C ANISOU 915 CG GLN A 126 2121 1950 2238 -34 8 11 C ATOM 916 CD GLN A 126 4.076 58.664 50.262 1.00 18.99 C ANISOU 916 CD GLN A 126 2587 2254 2371 16 20 50 C ATOM 917 OE1 GLN A 126 4.040 57.699 51.016 1.00 19.45 O ANISOU 917 OE1 GLN A 126 2673 2172 2545 359 19 166 O ATOM 918 NE2 GLN A 126 3.572 59.847 50.593 1.00 21.41 N ANISOU 918 NE2 GLN A 126 2805 2617 2710 208 -57 -89 N ATOM 919 N ALA A 127 7.357 55.002 47.702 1.00 13.87 N ANISOU 919 N ALA A 127 1850 1764 1653 -43 -30 68 N ATOM 920 CA ALA A 127 8.468 54.061 47.805 1.00 13.80 C ANISOU 920 CA ALA A 127 1830 1772 1639 -49 -57 94 C ATOM 921 C ALA A 127 9.355 54.103 46.567 1.00 13.72 C ANISOU 921 C ALA A 127 1828 1771 1611 -19 -93 134 C ATOM 922 O ALA A 127 10.574 54.059 46.675 1.00 13.27 O ANISOU 922 O ALA A 127 1764 1743 1533 11 -113 273 O ATOM 923 CB ALA A 127 7.962 52.643 48.075 1.00 14.26 C ANISOU 923 CB ALA A 127 1876 1811 1732 -41 -38 99 C ATOM 924 N GLN A 128 8.761 54.250 45.380 1.00 12.95 N ANISOU 924 N GLN A 128 1801 1625 1494 -70 -121 105 N ATOM 925 CA GLN A 128 9.586 54.316 44.168 1.00 13.35 C ANISOU 925 CA GLN A 128 1775 1742 1551 -16 -104 61 C ATOM 926 C GLN A 128 10.411 55.616 44.156 1.00 12.89 C ANISOU 926 C GLN A 128 1733 1673 1491 -14 -69 73 C ATOM 927 O GLN A 128 11.533 55.645 43.672 1.00 13.42 O ANISOU 927 O GLN A 128 1883 1727 1489 0 -98 97 O ATOM 928 CB GLN A 128 8.719 54.173 42.898 1.00 13.38 C ANISOU 928 CB GLN A 128 1766 1787 1528 -23 -92 62 C ATOM 929 CG GLN A 128 9.511 54.110 41.602 1.00 14.32 C ANISOU 929 CG GLN A 128 2016 2060 1363 -92 -211 11 C ATOM 930 CD GLN A 128 10.379 52.867 41.512 1.00 15.09 C ANISOU 930 CD GLN A 128 2204 1957 1570 -91 -75 -30 C ATOM 931 OE1 GLN A 128 9.886 51.744 41.674 1.00 16.56 O ANISOU 931 OE1 GLN A 128 2489 1867 1933 -132 -180 -40 O ATOM 932 NE2 GLN A 128 11.676 53.055 41.310 1.00 16.32 N ANISOU 932 NE2 GLN A 128 2401 2130 1670 -207 8 -96 N ATOM 933 N GLN A 129 9.859 56.692 44.710 1.00 13.17 N ANISOU 933 N GLN A 129 1805 1701 1494 -41 -89 81 N ATOM 934 CA GLN A 129 10.610 57.938 44.827 1.00 13.53 C ANISOU 934 CA GLN A 129 1843 1740 1554 -35 -40 64 C ATOM 935 C GLN A 129 11.842 57.766 45.731 1.00 12.98 C ANISOU 935 C GLN A 129 1800 1668 1462 -61 -16 12 C ATOM 936 O GLN A 129 12.907 58.286 45.426 1.00 12.85 O ANISOU 936 O GLN A 129 1906 1648 1329 -115 22 5 O ATOM 937 CB GLN A 129 9.723 59.064 45.332 1.00 14.19 C ANISOU 937 CB GLN A 129 1856 1802 1734 -59 -55 94 C ATOM 938 CG GLN A 129 8.640 59.485 44.374 1.00 18.22 C ANISOU 938 CG GLN A 129 2393 2190 2336 -28 -102 117 C ATOM 939 CD GLN A 129 7.946 60.679 44.935 1.00 24.89 C ANISOU 939 CD GLN A 129 3182 2939 3334 98 18 -10 C ATOM 940 OE1 GLN A 129 8.527 61.767 44.979 1.00 27.52 O ANISOU 940 OE1 GLN A 129 3587 3212 3657 49 -16 -50 O ATOM 941 NE2 GLN A 129 6.737 60.480 45.439 1.00 28.08 N ANISOU 941 NE2 GLN A 129 3519 3380 3767 151 87 -8 N ATOM 942 N TRP A 130 11.710 56.982 46.808 1.00 11.56 N ANISOU 942 N TRP A 130 1716 1394 1282 -73 35 45 N ATOM 943 CA TRP A 130 12.856 56.731 47.667 1.00 11.59 C ANISOU 943 CA TRP A 130 1617 1438 1346 -38 26 27 C ATOM 944 C TRP A 130 13.942 55.999 46.874 1.00 11.87 C ANISOU 944 C TRP A 130 1659 1484 1364 -54 -5 23 C ATOM 945 O TRP A 130 15.099 56.398 46.896 1.00 11.45 O ANISOU 945 O TRP A 130 1586 1446 1319 -51 -48 3 O ATOM 946 CB TRP A 130 12.485 55.932 48.954 1.00 11.43 C ANISOU 946 CB TRP A 130 1569 1476 1295 -54 0 41 C ATOM 947 CG TRP A 130 11.312 56.503 49.712 1.00 11.76 C ANISOU 947 CG TRP A 130 1609 1565 1294 6 -49 52 C ATOM 948 CD1 TRP A 130 10.970 57.815 49.830 1.00 14.00 C ANISOU 948 CD1 TRP A 130 1835 1783 1701 -7 29 120 C ATOM 949 CD2 TRP A 130 10.328 55.766 50.439 1.00 12.93 C ANISOU 949 CD2 TRP A 130 1712 1636 1564 -81 -65 1 C ATOM 950 NE1 TRP A 130 9.823 57.943 50.573 1.00 14.52 N ANISOU 950 NE1 TRP A 130 1749 1854 1912 167 -1 55 N ATOM 951 CE2 TRP A 130 9.396 56.695 50.944 1.00 14.02 C ANISOU 951 CE2 TRP A 130 1838 1862 1624 -50 -114 57 C ATOM 952 CE3 TRP A 130 10.115 54.395 50.680 1.00 13.04 C ANISOU 952 CE3 TRP A 130 1723 1753 1475 -55 -210 79 C ATOM 953 CZ2 TRP A 130 8.295 56.312 51.715 1.00 15.00 C ANISOU 953 CZ2 TRP A 130 1874 1928 1895 68 -90 -54 C ATOM 954 CZ3 TRP A 130 9.005 54.019 51.421 1.00 13.62 C ANISOU 954 CZ3 TRP A 130 1858 1594 1723 -166 -74 22 C ATOM 955 CH2 TRP A 130 8.113 54.970 51.930 1.00 15.43 C ANISOU 955 CH2 TRP A 130 1926 1988 1946 -100 -4 126 C ATOM 956 N LEU A 131 13.555 54.958 46.133 1.00 12.16 N ANISOU 956 N LEU A 131 1732 1521 1365 -94 -43 36 N ATOM 957 CA LEU A 131 14.518 54.189 45.334 1.00 13.56 C ANISOU 957 CA LEU A 131 1847 1723 1581 -94 -23 59 C ATOM 958 C LEU A 131 15.236 55.095 44.332 1.00 14.61 C ANISOU 958 C LEU A 131 1970 1923 1658 -118 15 49 C ATOM 959 O LEU A 131 16.457 55.030 44.177 1.00 14.90 O ANISOU 959 O LEU A 131 2054 2010 1597 -170 12 130 O ATOM 960 CB LEU A 131 13.814 53.051 44.579 1.00 13.40 C ANISOU 960 CB LEU A 131 1843 1739 1509 -68 -18 -51 C ATOM 961 CG LEU A 131 13.280 51.895 45.437 1.00 13.45 C ANISOU 961 CG LEU A 131 1863 1689 1558 -105 -59 -10 C ATOM 962 CD1 LEU A 131 12.362 51.008 44.620 1.00 14.53 C ANISOU 962 CD1 LEU A 131 2024 1913 1582 -119 27 -18 C ATOM 963 CD2 LEU A 131 14.370 51.030 46.070 1.00 12.09 C ANISOU 963 CD2 LEU A 131 1782 1365 1446 -156 32 -86 C ATOM 964 N ASP A 132 14.455 55.946 43.677 1.00 15.46 N ANISOU 964 N ASP A 132 2083 1976 1812 -98 15 79 N ATOM 965 CA ASP A 132 15.000 56.856 42.648 1.00 15.83 C ANISOU 965 CA ASP A 132 2136 2034 1842 -117 33 9 C ATOM 966 C ASP A 132 15.981 57.830 43.254 1.00 15.85 C ANISOU 966 C ASP A 132 2099 2009 1914 -167 53 36 C ATOM 967 O ASP A 132 16.898 58.288 42.566 1.00 16.75 O ANISOU 967 O ASP A 132 2174 2192 1997 -186 64 0 O ATOM 968 CB ASP A 132 13.888 57.639 41.958 1.00 16.47 C ANISOU 968 CB ASP A 132 2211 2096 1951 -100 6 27 C ATOM 969 CG ASP A 132 13.005 56.774 41.087 1.00 17.41 C ANISOU 969 CG ASP A 132 2301 2261 2053 -73 -11 18 C ATOM 970 OD1 ASP A 132 13.372 55.616 40.786 1.00 17.96 O ANISOU 970 OD1 ASP A 132 2806 2168 1848 -107 -36 70 O ATOM 971 OD2 ASP A 132 11.915 57.248 40.695 1.00 19.95 O ANISOU 971 OD2 ASP A 132 2384 2795 2400 -174 -162 64 O ATOM 972 N ALA A 133 15.765 58.139 44.544 1.00 14.64 N ANISOU 972 N ALA A 133 1946 1811 1804 -180 38 18 N ATOM 973 CA ALA A 133 16.644 59.033 45.313 1.00 14.41 C ANISOU 973 CA ALA A 133 1911 1768 1793 -111 -2 19 C ATOM 974 C ALA A 133 17.862 58.308 45.895 1.00 14.50 C ANISOU 974 C ALA A 133 1914 1773 1820 -111 -6 22 C ATOM 975 O ALA A 133 18.661 58.927 46.614 1.00 14.79 O ANISOU 975 O ALA A 133 2058 1761 1800 -105 -59 -5 O ATOM 976 CB ALA A 133 15.852 59.753 46.427 1.00 14.25 C ANISOU 976 CB ALA A 133 1873 1746 1794 -90 -4 46 C ATOM 977 N GLY A 134 18.009 57.018 45.569 1.00 14.27 N ANISOU 977 N GLY A 134 1878 1803 1739 -85 20 -13 N ATOM 978 CA GLY A 134 19.145 56.176 45.964 1.00 13.80 C ANISOU 978 CA GLY A 134 1814 1716 1714 -89 61 -14 C ATOM 979 C GLY A 134 19.020 55.526 47.332 1.00 12.85 C ANISOU 979 C GLY A 134 1740 1474 1665 -60 -26 -35 C ATOM 980 O GLY A 134 19.985 55.067 47.892 1.00 13.42 O ANISOU 980 O GLY A 134 1820 1600 1679 -177 -62 -21 O ATOM 981 N ILE A 135 17.806 55.490 47.853 1.00 12.80 N ANISOU 981 N ILE A 135 1819 1505 1539 -87 46 -3 N ATOM 982 CA ILE A 135 17.522 54.890 49.149 1.00 13.20 C ANISOU 982 CA ILE A 135 1837 1648 1530 -32 -22 10 C ATOM 983 C ILE A 135 16.740 53.582 48.971 1.00 12.56 C ANISOU 983 C ILE A 135 1749 1581 1439 -7 -16 -13 C ATOM 984 O ILE A 135 15.603 53.550 48.463 1.00 13.10 O ANISOU 984 O ILE A 135 1831 1651 1495 -53 -68 -23 O ATOM 985 CB ILE A 135 16.796 55.915 50.045 1.00 13.65 C ANISOU 985 CB ILE A 135 1868 1734 1583 -50 5 34 C ATOM 986 CG1 ILE A 135 17.759 57.092 50.322 1.00 16.01 C ANISOU 986 CG1 ILE A 135 2094 2056 1934 -90 -84 -14 C ATOM 987 CG2 ILE A 135 16.290 55.265 51.364 1.00 13.38 C ANISOU 987 CG2 ILE A 135 1825 1714 1543 -86 -59 36 C ATOM 988 CD1 ILE A 135 17.139 58.338 50.836 1.00 18.24 C ANISOU 988 CD1 ILE A 135 2485 2174 2271 -15 -14 -51 C ATOM 989 N SER A 136 17.344 52.497 49.434 1.00 11.21 N ANISOU 989 N SER A 136 1667 1299 1291 -2 16 -81 N ATOM 990 CA SER A 136 16.827 51.165 49.106 1.00 11.09 C ANISOU 990 CA SER A 136 1598 1320 1294 -62 74 -76 C ATOM 991 C SER A 136 16.722 50.238 50.287 1.00 10.23 C ANISOU 991 C SER A 136 1528 1139 1218 -31 82 -68 C ATOM 992 O SER A 136 16.762 49.035 50.118 1.00 11.09 O ANISOU 992 O SER A 136 1737 1229 1247 -44 132 -113 O ATOM 993 CB SER A 136 17.653 50.534 47.979 1.00 11.33 C ANISOU 993 CB SER A 136 1582 1385 1337 -29 124 -14 C ATOM 994 OG SER A 136 18.983 50.308 48.366 1.00 11.32 O ANISOU 994 OG SER A 136 1542 1418 1339 -216 31 14 O ATOM 995 N GLN A 137 16.596 50.813 51.489 1.00 9.43 N ANISOU 995 N GLN A 137 1407 1088 1087 -21 90 0 N ATOM 996 CA GLN A 137 16.233 50.063 52.693 1.00 9.02 C ANISOU 996 CA GLN A 137 1258 1106 1061 -20 38 17 C ATOM 997 C GLN A 137 14.969 50.647 53.289 1.00 8.97 C ANISOU 997 C GLN A 137 1270 1119 1018 8 71 22 C ATOM 998 O GLN A 137 14.803 51.884 53.350 1.00 9.85 O ANISOU 998 O GLN A 137 1409 1278 1053 -34 95 19 O ATOM 999 CB GLN A 137 17.339 50.118 53.744 1.00 8.80 C ANISOU 999 CB GLN A 137 1131 1221 989 -58 23 2 C ATOM 1000 CG GLN A 137 18.565 49.308 53.423 1.00 8.64 C ANISOU 1000 CG GLN A 137 1272 845 1166 47 -54 23 C ATOM 1001 CD GLN A 137 19.385 49.034 54.675 1.00 10.19 C ANISOU 1001 CD GLN A 137 1461 1223 1187 11 -44 -48 C ATOM 1002 OE1 GLN A 137 18.884 48.414 55.611 1.00 10.98 O ANISOU 1002 OE1 GLN A 137 1775 1023 1371 -105 12 -182 O ATOM 1003 NE2 GLN A 137 20.649 49.474 54.689 1.00 10.33 N ANISOU 1003 NE2 GLN A 137 1324 1122 1479 10 126 -258 N ATOM 1004 N ALA A 138 14.101 49.764 53.757 1.00 9.47 N ANISOU 1004 N ALA A 138 1238 1239 1120 84 77 -41 N ATOM 1005 CA ALA A 138 12.851 50.143 54.414 1.00 9.14 C ANISOU 1005 CA ALA A 138 1190 1253 1028 8 128 21 C ATOM 1006 C ALA A 138 12.607 49.256 55.610 1.00 8.57 C ANISOU 1006 C ALA A 138 1188 1054 1011 -27 80 11 C ATOM 1007 O ALA A 138 12.919 48.063 55.576 1.00 9.44 O ANISOU 1007 O ALA A 138 1238 1217 1128 -144 72 -1 O ATOM 1008 CB ALA A 138 11.694 50.048 53.454 1.00 9.80 C ANISOU 1008 CB ALA A 138 1203 1399 1118 -34 129 42 C ATOM 1009 N ILE A 139 12.028 49.844 56.664 1.00 7.66 N ANISOU 1009 N ILE A 139 1130 921 858 -92 107 -5 N ATOM 1010 CA ILE A 139 11.748 49.106 57.895 1.00 7.68 C ANISOU 1010 CA ILE A 139 1092 940 883 -50 35 -15 C ATOM 1011 C ILE A 139 10.240 48.952 58.026 1.00 8.23 C ANISOU 1011 C ILE A 139 1127 1005 994 7 2 -13 C ATOM 1012 O ILE A 139 9.512 49.941 58.169 1.00 7.73 O ANISOU 1012 O ILE A 139 1098 922 914 91 -14 -38 O ATOM 1013 CB ILE A 139 12.240 49.887 59.158 1.00 8.16 C ANISOU 1013 CB ILE A 139 1182 1008 907 -47 11 -101 C ATOM 1014 CG1 ILE A 139 13.658 50.474 59.000 1.00 9.42 C ANISOU 1014 CG1 ILE A 139 1272 1259 1045 43 25 30 C ATOM 1015 CG2 ILE A 139 12.095 49.029 60.386 1.00 8.06 C ANISOU 1015 CG2 ILE A 139 1243 1044 773 -68 -1 -168 C ATOM 1016 CD1 ILE A 139 14.701 49.515 58.629 1.00 10.08 C ANISOU 1016 CD1 ILE A 139 1439 952 1437 -242 -59 -52 C ATOM 1017 N TYR A 140 9.790 47.707 57.996 1.00 8.01 N ANISOU 1017 N TYR A 140 1060 912 1068 66 33 59 N ATOM 1018 CA TYR A 140 8.369 47.371 58.062 1.00 8.06 C ANISOU 1018 CA TYR A 140 1045 936 1081 -37 -17 -4 C ATOM 1019 C TYR A 140 8.025 46.784 59.437 1.00 8.67 C ANISOU 1019 C TYR A 140 1168 1018 1106 -42 3 -6 C ATOM 1020 O TYR A 140 8.677 45.836 59.876 1.00 9.36 O ANISOU 1020 O TYR A 140 1272 1209 1076 -69 0 40 O ATOM 1021 CB TYR A 140 7.991 46.375 56.931 1.00 8.96 C ANISOU 1021 CB TYR A 140 1203 1063 1136 12 25 -70 C ATOM 1022 CG TYR A 140 6.505 46.221 56.751 1.00 8.44 C ANISOU 1022 CG TYR A 140 1126 866 1213 -6 34 75 C ATOM 1023 CD1 TYR A 140 5.833 46.911 55.740 1.00 11.61 C ANISOU 1023 CD1 TYR A 140 1264 1586 1558 -14 -101 83 C ATOM 1024 CD2 TYR A 140 5.755 45.419 57.621 1.00 9.21 C ANISOU 1024 CD2 TYR A 140 1149 1030 1320 -143 0 28 C ATOM 1025 CE1 TYR A 140 4.452 46.821 55.598 1.00 11.07 C ANISOU 1025 CE1 TYR A 140 1203 1500 1502 -177 -227 101 C ATOM 1026 CE2 TYR A 140 4.367 45.326 57.488 1.00 10.13 C ANISOU 1026 CE2 TYR A 140 1230 1431 1186 -286 -212 5 C ATOM 1027 CZ TYR A 140 3.730 46.029 56.464 1.00 10.30 C ANISOU 1027 CZ TYR A 140 1317 1266 1330 -62 -106 45 C ATOM 1028 OH TYR A 140 2.379 45.928 56.304 1.00 12.51 O ANISOU 1028 OH TYR A 140 1455 1673 1625 -115 -232 198 O ATOM 1029 N HIS A 141 7.012 47.361 60.097 1.00 8.33 N ANISOU 1029 N HIS A 141 1121 952 1089 -77 -33 84 N ATOM 1030 CA HIS A 141 6.540 46.947 61.415 1.00 9.67 C ANISOU 1030 CA HIS A 141 1302 1158 1213 -24 14 -41 C ATOM 1031 C HIS A 141 5.300 46.090 61.311 1.00 9.32 C ANISOU 1031 C HIS A 141 1270 1069 1202 -49 -3 18 C ATOM 1032 O HIS A 141 4.375 46.415 60.554 1.00 9.54 O ANISOU 1032 O HIS A 141 1319 1062 1241 -73 -13 -80 O ATOM 1033 CB HIS A 141 6.165 48.185 62.245 1.00 10.31 C ANISOU 1033 CB HIS A 141 1449 1181 1287 -3 -1 -10 C ATOM 1034 CG HIS A 141 7.338 49.037 62.613 1.00 12.39 C ANISOU 1034 CG HIS A 141 1611 1547 1548 -158 -14 -7 C ATOM 1035 ND1 HIS A 141 7.999 49.852 61.714 1.00 15.03 N ANISOU 1035 ND1 HIS A 141 2101 1686 1923 -89 -129 -54 N ATOM 1036 CD2 HIS A 141 7.968 49.192 63.795 1.00 13.46 C ANISOU 1036 CD2 HIS A 141 1842 1575 1696 -29 -31 166 C ATOM 1037 CE1 HIS A 141 8.987 50.468 62.338 1.00 13.10 C ANISOU 1037 CE1 HIS A 141 1581 1677 1717 -6 49 151 C ATOM 1038 NE2 HIS A 141 8.994 50.074 63.600 1.00 15.57 N ANISOU 1038 NE2 HIS A 141 1930 1944 2041 19 -104 28 N ATOM 1039 N GLN A 142 5.246 45.012 62.097 1.00 9.33 N ANISOU 1039 N GLN A 142 1229 1064 1250 -32 16 -10 N ATOM 1040 CA GLN A 142 3.993 44.271 62.195 1.00 9.86 C ANISOU 1040 CA GLN A 142 1278 1164 1303 -78 8 -11 C ATOM 1041 C GLN A 142 2.841 45.228 62.527 1.00 10.05 C ANISOU 1041 C GLN A 142 1342 1157 1319 -90 25 -48 C ATOM 1042 O GLN A 142 2.973 46.172 63.331 1.00 10.28 O ANISOU 1042 O GLN A 142 1526 884 1495 -106 1 -135 O ATOM 1043 CB GLN A 142 4.056 43.157 63.235 1.00 9.69 C ANISOU 1043 CB GLN A 142 1266 1102 1312 11 2 -26 C ATOM 1044 CG GLN A 142 2.933 42.159 62.987 1.00 10.39 C ANISOU 1044 CG GLN A 142 1331 1202 1415 -156 47 -16 C ATOM 1045 CD GLN A 142 2.765 41.091 64.053 1.00 12.33 C ANISOU 1045 CD GLN A 142 1703 1462 1519 -10 -43 35 C ATOM 1046 OE1 GLN A 142 3.497 41.053 65.049 1.00 13.62 O ANISOU 1046 OE1 GLN A 142 1482 1812 1879 -98 -49 -128 O ATOM 1047 NE2 GLN A 142 1.777 40.211 63.848 1.00 14.47 N ANISOU 1047 NE2 GLN A 142 1995 1795 1708 -272 3 88 N ATOM 1048 N SER A 143 1.696 45.016 61.888 1.00 11.15 N ANISOU 1048 N SER A 143 1456 1347 1432 -132 -45 -61 N ATOM 1049 CA SER A 143 0.509 45.791 62.213 1.00 13.47 C ANISOU 1049 CA SER A 143 1743 1694 1677 -86 -33 -39 C ATOM 1050 C SER A 143 0.311 45.771 63.727 1.00 14.01 C ANISOU 1050 C SER A 143 1848 1715 1757 -72 -24 -8 C ATOM 1051 O SER A 143 0.355 44.692 64.337 1.00 12.98 O ANISOU 1051 O SER A 143 1714 1538 1677 -79 28 101 O ATOM 1052 CB SER A 143 -0.699 45.214 61.470 1.00 13.85 C ANISOU 1052 CB SER A 143 1801 1722 1738 -166 -83 -77 C ATOM 1053 OG SER A 143 -0.580 45.588 60.091 1.00 18.20 O ANISOU 1053 OG SER A 143 2377 2434 2105 -74 -87 -43 O ATOM 1054 N ARG A 144 0.168 46.963 64.323 1.00 14.81 N ANISOU 1054 N ARG A 144 1996 1732 1898 -35 19 3 N ATOM 1055 CA ARG A 144 0.265 47.124 65.771 1.00 16.41 C ANISOU 1055 CA ARG A 144 2188 1915 2131 -14 -10 -86 C ATOM 1056 C ARG A 144 -0.830 46.382 66.510 1.00 16.93 C ANISOU 1056 C ARG A 144 2260 1963 2210 -13 -13 -100 C ATOM 1057 O ARG A 144 -0.593 45.842 67.592 1.00 16.62 O ANISOU 1057 O ARG A 144 2235 1815 2263 -19 -137 -214 O ATOM 1058 CB ARG A 144 0.240 48.614 66.123 1.00 16.94 C ANISOU 1058 CB ARG A 144 2281 1949 2204 -10 1 -90 C ATOM 1059 CG ARG A 144 0.500 48.986 67.587 1.00 18.22 C ANISOU 1059 CG ARG A 144 2395 2256 2270 -3 -29 -43 C ATOM 1060 CD ARG A 144 1.800 48.451 68.189 1.00 19.83 C ANISOU 1060 CD ARG A 144 2431 2519 2584 -36 29 33 C ATOM 1061 NE ARG A 144 3.042 48.777 67.462 1.00 19.16 N ANISOU 1061 NE ARG A 144 2262 2503 2512 -131 143 -38 N ATOM 1062 CZ ARG A 144 3.756 49.902 67.595 1.00 21.48 C ANISOU 1062 CZ ARG A 144 2598 2746 2816 -5 85 -86 C ATOM 1063 NH1 ARG A 144 3.365 50.894 68.400 1.00 21.29 N ANISOU 1063 NH1 ARG A 144 2664 2702 2722 -63 46 -225 N ATOM 1064 NH2 ARG A 144 4.892 50.042 66.900 1.00 20.78 N ANISOU 1064 NH2 ARG A 144 2681 2605 2609 -118 150 -33 N ATOM 1065 N ASP A 145 -2.031 46.349 65.922 1.00 18.56 N ANISOU 1065 N ASP A 145 2386 2252 2413 1 -5 -81 N ATOM 1066 CA ASP A 145 -3.149 45.604 66.505 1.00 20.47 C ANISOU 1066 CA ASP A 145 2622 2522 2631 8 56 -2 C ATOM 1067 C ASP A 145 -2.823 44.129 66.665 1.00 20.35 C ANISOU 1067 C ASP A 145 2596 2538 2596 17 67 45 C ATOM 1068 O ASP A 145 -3.077 43.539 67.715 1.00 20.40 O ANISOU 1068 O ASP A 145 2663 2451 2635 69 116 124 O ATOM 1069 CB ASP A 145 -4.411 45.739 65.640 1.00 21.30 C ANISOU 1069 CB ASP A 145 2700 2654 2737 -19 9 20 C ATOM 1070 CG ASP A 145 -5.034 47.113 65.720 1.00 26.34 C ANISOU 1070 CG ASP A 145 3351 3301 3355 88 -1 -8 C ATOM 1071 OD1 ASP A 145 -5.706 47.509 64.730 1.00 31.61 O ANISOU 1071 OD1 ASP A 145 3953 4107 3948 111 -175 196 O ATOM 1072 OD2 ASP A 145 -4.881 47.833 66.732 1.00 29.70 O ANISOU 1072 OD2 ASP A 145 4020 3593 3670 59 -88 -162 O ATOM 1073 N ALA A 146 -2.291 43.540 65.597 1.00 19.82 N ANISOU 1073 N ALA A 146 2552 2417 2560 13 54 4 N ATOM 1074 CA ALA A 146 -1.871 42.138 65.596 1.00 19.94 C ANISOU 1074 CA ALA A 146 2559 2457 2559 16 14 -8 C ATOM 1075 C ALA A 146 -0.703 41.889 66.556 1.00 19.73 C ANISOU 1075 C ALA A 146 2541 2421 2532 -12 12 1 C ATOM 1076 O ALA A 146 -0.637 40.856 67.235 1.00 19.84 O ANISOU 1076 O ALA A 146 2605 2301 2631 -124 24 -23 O ATOM 1077 CB ALA A 146 -1.495 41.719 64.175 1.00 19.58 C ANISOU 1077 CB ALA A 146 2514 2421 2503 27 -12 -18 C ATOM 1078 N LEU A 147 0.225 42.839 66.605 1.00 19.53 N ANISOU 1078 N LEU A 147 2538 2370 2509 -18 32 -20 N ATOM 1079 CA LEU A 147 1.370 42.754 67.492 1.00 20.15 C ANISOU 1079 CA LEU A 147 2618 2505 2531 12 52 0 C ATOM 1080 C LEU A 147 0.898 42.740 68.939 1.00 21.17 C ANISOU 1080 C LEU A 147 2777 2670 2597 44 41 8 C ATOM 1081 O LEU A 147 1.269 41.850 69.708 1.00 21.88 O ANISOU 1081 O LEU A 147 2905 2796 2611 120 43 23 O ATOM 1082 CB LEU A 147 2.315 43.944 67.255 1.00 19.69 C ANISOU 1082 CB LEU A 147 2558 2407 2513 -6 68 -37 C ATOM 1083 CG LEU A 147 3.621 43.970 68.054 1.00 20.43 C ANISOU 1083 CG LEU A 147 2655 2536 2569 43 61 21 C ATOM 1084 CD1 LEU A 147 4.295 42.593 68.064 1.00 21.51 C ANISOU 1084 CD1 LEU A 147 2800 2582 2788 61 93 -31 C ATOM 1085 CD2 LEU A 147 4.548 45.001 67.482 1.00 19.67 C ANISOU 1085 CD2 LEU A 147 2472 2498 2503 -86 -59 -146 C ATOM 1086 N LEU A 148 0.067 43.717 69.296 1.00 21.63 N ANISOU 1086 N LEU A 148 2805 2772 2640 36 27 12 N ATOM 1087 CA LEU A 148 -0.428 43.826 70.670 1.00 22.25 C ANISOU 1087 CA LEU A 148 2900 2821 2732 16 34 -5 C ATOM 1088 C LEU A 148 -1.234 42.584 71.088 1.00 22.28 C ANISOU 1088 C LEU A 148 2938 2797 2728 -21 42 -10 C ATOM 1089 O LEU A 148 -1.173 42.163 72.253 1.00 22.93 O ANISOU 1089 O LEU A 148 3115 2780 2815 -28 49 -6 O ATOM 1090 CB LEU A 148 -1.223 45.128 70.875 1.00 22.42 C ANISOU 1090 CB LEU A 148 2891 2847 2781 2 6 29 C ATOM 1091 CG LEU A 148 -0.469 46.469 71.013 1.00 24.58 C ANISOU 1091 CG LEU A 148 3140 3098 3098 5 -19 -7 C ATOM 1092 CD1 LEU A 148 -1.384 47.491 71.653 1.00 26.69 C ANISOU 1092 CD1 LEU A 148 3326 3368 3447 -19 25 -44 C ATOM 1093 CD2 LEU A 148 0.869 46.396 71.793 1.00 25.61 C ANISOU 1093 CD2 LEU A 148 3274 3185 3268 -10 -19 -11 C ATOM 1094 N ALA A 149 -1.930 41.976 70.136 1.00 22.59 N ANISOU 1094 N ALA A 149 2936 2851 2794 -21 82 3 N ATOM 1095 CA ALA A 149 -2.722 40.776 70.391 1.00 22.62 C ANISOU 1095 CA ALA A 149 2953 2819 2820 -16 56 20 C ATOM 1096 C ALA A 149 -1.944 39.453 70.340 1.00 23.05 C ANISOU 1096 C ALA A 149 3015 2864 2876 -22 47 37 C ATOM 1097 O ALA A 149 -2.480 38.408 70.643 1.00 23.40 O ANISOU 1097 O ALA A 149 3148 2874 2867 -85 67 84 O ATOM 1098 CB ALA A 149 -3.880 40.717 69.461 1.00 22.68 C ANISOU 1098 CB ALA A 149 2901 2840 2875 -35 83 32 C ATOM 1099 N GLY A 150 -0.679 39.503 69.970 1.00 23.07 N ANISOU 1099 N GLY A 150 3026 2870 2867 -5 31 48 N ATOM 1100 CA GLY A 150 0.119 38.293 70.020 1.00 22.53 C ANISOU 1100 CA GLY A 150 2962 2790 2808 6 1 50 C ATOM 1101 C GLY A 150 -0.067 37.446 68.788 1.00 22.29 C ANISOU 1101 C GLY A 150 2933 2705 2831 -24 -23 38 C ATOM 1102 O GLY A 150 0.227 36.260 68.778 1.00 22.98 O ANISOU 1102 O GLY A 150 3059 2744 2926 -7 -47 120 O ATOM 1103 N GLU A 151 -0.555 38.073 67.735 1.00 21.75 N ANISOU 1103 N GLU A 151 2897 2603 2764 -50 -13 61 N ATOM 1104 CA GLU A 151 -0.926 37.366 66.529 1.00 21.44 C ANISOU 1104 CA GLU A 151 2828 2594 2721 -57 14 33 C ATOM 1105 C GLU A 151 0.273 37.033 65.672 1.00 20.56 C ANISOU 1105 C GLU A 151 2738 2455 2616 -73 5 63 C ATOM 1106 O GLU A 151 1.292 37.684 65.748 1.00 20.61 O ANISOU 1106 O GLU A 151 2769 2445 2614 -136 4 53 O ATOM 1107 CB GLU A 151 -1.913 38.181 65.732 1.00 22.29 C ANISOU 1107 CB GLU A 151 2933 2726 2811 -43 -3 6 C ATOM 1108 CG GLU A 151 -3.295 38.118 66.267 1.00 24.28 C ANISOU 1108 CG GLU A 151 3107 3007 3112 -1 12 51 C ATOM 1109 CD GLU A 151 -4.318 38.734 65.345 1.00 27.96 C ANISOU 1109 CD GLU A 151 3490 3572 3561 82 -58 -6 C ATOM 1110 OE1 GLU A 151 -4.218 38.592 64.102 1.00 27.98 O ANISOU 1110 OE1 GLU A 151 3567 3551 3513 171 41 198 O ATOM 1111 OE2 GLU A 151 -5.237 39.342 65.890 1.00 29.74 O ANISOU 1111 OE2 GLU A 151 3688 3756 3856 229 25 -142 O ATOM 1112 N THR A 152 0.131 36.006 64.855 1.00 19.52 N ANISOU 1112 N THR A 152 2631 2321 2463 -121 28 77 N ATOM 1113 CA THR A 152 1.070 35.756 63.783 1.00 17.95 C ANISOU 1113 CA THR A 152 2346 2164 2307 -98 -22 77 C ATOM 1114 C THR A 152 1.079 36.963 62.844 1.00 15.84 C ANISOU 1114 C THR A 152 2104 1897 2016 -127 8 86 C ATOM 1115 O THR A 152 0.153 37.750 62.831 1.00 14.74 O ANISOU 1115 O THR A 152 1989 1701 1908 -201 77 46 O ATOM 1116 CB THR A 152 0.695 34.490 62.995 1.00 18.47 C ANISOU 1116 CB THR A 152 2439 2211 2365 -57 -1 57 C ATOM 1117 OG1 THR A 152 1.832 33.975 62.313 1.00 18.29 O ANISOU 1117 OG1 THR A 152 2310 2162 2476 -196 -96 86 O ATOM 1118 CG2 THR A 152 -0.408 34.778 61.996 1.00 19.57 C ANISOU 1118 CG2 THR A 152 2474 2382 2577 -133 -33 25 C ATOM 1119 N TRP A 153 2.133 37.070 62.057 1.00 14.87 N ANISOU 1119 N TRP A 153 1909 1774 1966 -50 -36 86 N ATOM 1120 CA TRP A 153 2.143 37.987 60.933 1.00 14.25 C ANISOU 1120 CA TRP A 153 1784 1814 1813 -58 -22 71 C ATOM 1121 C TRP A 153 1.072 37.615 59.926 1.00 14.36 C ANISOU 1121 C TRP A 153 1802 1790 1862 -43 -87 8 C ATOM 1122 O TRP A 153 1.101 36.542 59.370 1.00 14.93 O ANISOU 1122 O TRP A 153 1887 1848 1936 -70 -176 -15 O ATOM 1123 CB TRP A 153 3.503 37.994 60.251 1.00 14.56 C ANISOU 1123 CB TRP A 153 1825 1824 1882 -73 3 43 C ATOM 1124 CG TRP A 153 4.482 38.881 60.918 1.00 13.32 C ANISOU 1124 CG TRP A 153 1730 1634 1694 -141 16 108 C ATOM 1125 CD1 TRP A 153 5.009 38.739 62.147 1.00 13.41 C ANISOU 1125 CD1 TRP A 153 1762 1645 1685 -44 -9 78 C ATOM 1126 CD2 TRP A 153 5.064 40.064 60.366 1.00 11.32 C ANISOU 1126 CD2 TRP A 153 1517 1208 1575 -128 14 4 C ATOM 1127 NE1 TRP A 153 5.878 39.756 62.416 1.00 12.29 N ANISOU 1127 NE1 TRP A 153 1555 1637 1475 -180 -88 138 N ATOM 1128 CE2 TRP A 153 5.934 40.585 61.334 1.00 11.67 C ANISOU 1128 CE2 TRP A 153 1494 1464 1476 55 -19 122 C ATOM 1129 CE3 TRP A 153 4.937 40.723 59.151 1.00 11.72 C ANISOU 1129 CE3 TRP A 153 1623 1396 1434 -79 -8 -11 C ATOM 1130 CZ2 TRP A 153 6.664 41.737 61.120 1.00 11.23 C ANISOU 1130 CZ2 TRP A 153 1514 1374 1377 -92 -126 31 C ATOM 1131 CZ3 TRP A 153 5.659 41.865 58.947 1.00 12.43 C ANISOU 1131 CZ3 TRP A 153 1785 1501 1437 -18 -70 77 C ATOM 1132 CH2 TRP A 153 6.511 42.363 59.921 1.00 12.69 C ANISOU 1132 CH2 TRP A 153 1617 1530 1672 -14 -74 87 C ATOM 1133 N GLY A 154 0.143 38.525 59.672 1.00 14.04 N ANISOU 1133 N GLY A 154 1785 1749 1798 -89 -110 31 N ATOM 1134 CA GLY A 154 -0.931 38.234 58.751 1.00 13.74 C ANISOU 1134 CA GLY A 154 1663 1763 1793 -97 -78 53 C ATOM 1135 C GLY A 154 -0.517 38.309 57.295 1.00 13.47 C ANISOU 1135 C GLY A 154 1651 1737 1728 -134 -45 77 C ATOM 1136 O GLY A 154 0.527 38.846 56.972 1.00 13.52 O ANISOU 1136 O GLY A 154 1555 1846 1737 -161 -56 143 O ATOM 1137 N GLU A 155 -1.349 37.777 56.411 1.00 12.92 N ANISOU 1137 N GLU A 155 1577 1679 1651 -182 -67 99 N ATOM 1138 CA GLU A 155 -1.000 37.754 55.007 1.00 13.66 C ANISOU 1138 CA GLU A 155 1727 1749 1713 -104 -48 -18 C ATOM 1139 C GLU A 155 -0.839 39.131 54.386 1.00 13.33 C ANISOU 1139 C GLU A 155 1662 1743 1659 -128 -39 -50 C ATOM 1140 O GLU A 155 -0.002 39.325 53.531 1.00 13.28 O ANISOU 1140 O GLU A 155 1703 1767 1576 -120 9 -146 O ATOM 1141 CB GLU A 155 -1.969 36.908 54.186 1.00 13.80 C ANISOU 1141 CB GLU A 155 1727 1717 1797 -126 -62 -3 C ATOM 1142 CG GLU A 155 -1.906 35.447 54.514 1.00 14.40 C ANISOU 1142 CG GLU A 155 1911 1657 1901 -65 -18 18 C ATOM 1143 CD GLU A 155 -0.561 34.818 54.180 1.00 14.13 C ANISOU 1143 CD GLU A 155 1990 1350 2029 -174 -20 67 C ATOM 1144 OE1 GLU A 155 -0.123 34.901 53.021 1.00 17.91 O ANISOU 1144 OE1 GLU A 155 2394 2233 2175 -55 67 -138 O ATOM 1145 OE2 GLU A 155 0.057 34.264 55.081 1.00 16.57 O ANISOU 1145 OE2 GLU A 155 2275 1785 2236 49 -162 -43 O ATOM 1146 N LYS A 156 -1.679 40.064 54.815 1.00 13.63 N ANISOU 1146 N LYS A 156 1691 1769 1717 -115 -11 -7 N ATOM 1147 CA LYS A 156 -1.599 41.438 54.327 1.00 13.35 C ANISOU 1147 CA LYS A 156 1689 1728 1653 -88 -56 44 C ATOM 1148 C LYS A 156 -0.222 42.039 54.622 1.00 12.65 C ANISOU 1148 C LYS A 156 1620 1634 1552 -118 -74 31 C ATOM 1149 O LYS A 156 0.387 42.623 53.736 1.00 12.43 O ANISOU 1149 O LYS A 156 1602 1687 1432 -52 -160 12 O ATOM 1150 CB LYS A 156 -2.688 42.303 54.897 1.00 13.72 C ANISOU 1150 CB LYS A 156 1750 1827 1632 -62 17 58 C ATOM 1151 N ASP A 157 0.282 41.883 55.845 1.00 11.55 N ANISOU 1151 N ASP A 157 1582 1355 1450 -67 -50 110 N ATOM 1152 CA ASP A 157 1.615 42.391 56.170 1.00 12.06 C ANISOU 1152 CA ASP A 157 1615 1559 1408 -51 -86 54 C ATOM 1153 C ASP A 157 2.653 41.700 55.315 1.00 11.14 C ANISOU 1153 C ASP A 157 1566 1388 1277 -80 -128 57 C ATOM 1154 O ASP A 157 3.521 42.364 54.759 1.00 10.87 O ANISOU 1154 O ASP A 157 1436 1439 1255 -217 -143 43 O ATOM 1155 CB ASP A 157 1.975 42.200 57.657 1.00 12.00 C ANISOU 1155 CB ASP A 157 1666 1498 1392 -63 -53 16 C ATOM 1156 CG ASP A 157 1.419 43.319 58.584 1.00 12.23 C ANISOU 1156 CG ASP A 157 1688 1565 1391 -53 -44 -82 C ATOM 1157 OD1 ASP A 157 1.058 44.411 58.120 1.00 12.40 O ANISOU 1157 OD1 ASP A 157 1817 1358 1536 -76 -124 -125 O ATOM 1158 OD2 ASP A 157 1.315 43.103 59.810 1.00 11.59 O ANISOU 1158 OD2 ASP A 157 1686 1369 1348 -314 104 -142 O ATOM 1159 N LEU A 158 2.575 40.363 55.212 1.00 11.07 N ANISOU 1159 N LEU A 158 1587 1343 1273 -58 -123 -33 N ATOM 1160 CA LEU A 158 3.517 39.632 54.394 1.00 11.32 C ANISOU 1160 CA LEU A 158 1520 1343 1436 -53 -93 -9 C ATOM 1161 C LEU A 158 3.493 40.091 52.919 1.00 11.28 C ANISOU 1161 C LEU A 158 1545 1322 1418 -22 -120 -107 C ATOM 1162 O LEU A 158 4.536 40.222 52.288 1.00 11.59 O ANISOU 1162 O LEU A 158 1657 1389 1355 -116 -203 -117 O ATOM 1163 CB LEU A 158 3.324 38.125 54.554 1.00 11.58 C ANISOU 1163 CB LEU A 158 1589 1338 1469 7 -81 -35 C ATOM 1164 CG LEU A 158 3.635 37.677 55.988 1.00 11.78 C ANISOU 1164 CG LEU A 158 1602 1391 1480 -59 -14 31 C ATOM 1165 CD1 LEU A 158 3.192 36.251 56.160 1.00 11.77 C ANISOU 1165 CD1 LEU A 158 1782 1102 1587 27 -70 141 C ATOM 1166 CD2 LEU A 158 5.100 37.808 56.367 1.00 12.25 C ANISOU 1166 CD2 LEU A 158 1764 1341 1549 -22 13 89 C ATOM 1167 N ASN A 159 2.303 40.356 52.387 1.00 11.85 N ANISOU 1167 N ASN A 159 1593 1356 1552 -1 -99 -88 N ATOM 1168 CA ASN A 159 2.174 40.823 51.006 1.00 12.29 C ANISOU 1168 CA ASN A 159 1668 1478 1522 -37 0 -57 C ATOM 1169 C ASN A 159 2.914 42.133 50.753 1.00 12.26 C ANISOU 1169 C ASN A 159 1608 1541 1508 -65 -27 -19 C ATOM 1170 O ASN A 159 3.520 42.322 49.692 1.00 13.15 O ANISOU 1170 O ASN A 159 1777 1670 1549 -85 59 -50 O ATOM 1171 CB ASN A 159 0.714 41.023 50.620 1.00 12.53 C ANISOU 1171 CB ASN A 159 1684 1483 1591 -72 -28 -78 C ATOM 1172 CG ASN A 159 -0.018 39.728 50.341 1.00 14.13 C ANISOU 1172 CG ASN A 159 1848 1696 1823 -68 7 -110 C ATOM 1173 OD1 ASN A 159 -1.268 39.695 50.355 1.00 16.22 O ANISOU 1173 OD1 ASN A 159 2028 2008 2127 -174 -105 -273 O ATOM 1174 ND2 ASN A 159 0.727 38.663 50.087 1.00 14.51 N ANISOU 1174 ND2 ASN A 159 1796 1842 1875 -14 -157 -171 N ATOM 1175 N LYS A 160 2.828 43.042 51.708 1.00 11.30 N ANISOU 1175 N LYS A 160 1480 1466 1347 3 -8 -15 N ATOM 1176 CA LYS A 160 3.492 44.337 51.569 1.00 10.88 C ANISOU 1176 CA LYS A 160 1506 1314 1313 -3 -49 -11 C ATOM 1177 C LYS A 160 5.013 44.192 51.651 1.00 10.21 C ANISOU 1177 C LYS A 160 1493 1142 1244 -6 -23 -97 C ATOM 1178 O LYS A 160 5.757 44.786 50.878 1.00 10.46 O ANISOU 1178 O LYS A 160 1568 1182 1224 -6 -39 -129 O ATOM 1179 CB LYS A 160 2.948 45.344 52.589 1.00 11.31 C ANISOU 1179 CB LYS A 160 1482 1375 1438 45 -17 21 C ATOM 1180 CG LYS A 160 1.431 45.579 52.446 1.00 11.22 C ANISOU 1180 CG LYS A 160 1421 1346 1494 -12 -66 88 C ATOM 1181 CD LYS A 160 0.962 46.834 53.154 1.00 14.25 C ANISOU 1181 CD LYS A 160 1846 1753 1813 97 4 -97 C ATOM 1182 CE LYS A 160 1.391 48.077 52.414 1.00 15.54 C ANISOU 1182 CE LYS A 160 1784 1958 2160 88 -24 -26 C ATOM 1183 NZ LYS A 160 0.759 49.293 53.039 1.00 18.21 N ANISOU 1183 NZ LYS A 160 2188 2178 2550 37 -54 -78 N ATOM 1184 N VAL A 161 5.477 43.384 52.596 1.00 10.17 N ANISOU 1184 N VAL A 161 1436 1223 1205 -22 -38 -54 N ATOM 1185 CA VAL A 161 6.897 43.038 52.659 1.00 10.74 C ANISOU 1185 CA VAL A 161 1444 1312 1323 -29 -41 -42 C ATOM 1186 C VAL A 161 7.356 42.461 51.335 1.00 10.64 C ANISOU 1186 C VAL A 161 1465 1271 1305 -31 -68 -5 C ATOM 1187 O VAL A 161 8.365 42.903 50.784 1.00 10.78 O ANISOU 1187 O VAL A 161 1544 1351 1198 -100 -118 41 O ATOM 1188 CB VAL A 161 7.220 42.122 53.848 1.00 10.33 C ANISOU 1188 CB VAL A 161 1354 1310 1261 -52 -47 -68 C ATOM 1189 CG1 VAL A 161 8.670 41.644 53.784 1.00 11.30 C ANISOU 1189 CG1 VAL A 161 1565 1385 1344 6 -66 -258 C ATOM 1190 CG2 VAL A 161 6.905 42.867 55.182 1.00 9.92 C ANISOU 1190 CG2 VAL A 161 1298 1044 1424 -21 -112 -100 C ATOM 1191 N LYS A 162 6.620 41.483 50.812 1.00 11.90 N ANISOU 1191 N LYS A 162 1542 1591 1386 -71 -88 -18 N ATOM 1192 CA LYS A 162 6.982 40.863 49.547 1.00 12.16 C ANISOU 1192 CA LYS A 162 1647 1454 1519 -106 -16 -53 C ATOM 1193 C LYS A 162 7.056 41.868 48.405 1.00 11.71 C ANISOU 1193 C LYS A 162 1581 1459 1410 -153 -71 -80 C ATOM 1194 O LYS A 162 7.984 41.815 47.595 1.00 12.75 O ANISOU 1194 O LYS A 162 1688 1529 1624 -229 -54 -66 O ATOM 1195 CB LYS A 162 5.995 39.749 49.202 1.00 12.11 C ANISOU 1195 CB LYS A 162 1669 1523 1409 -116 -52 -141 C ATOM 1196 CG LYS A 162 6.187 38.524 50.039 1.00 12.52 C ANISOU 1196 CG LYS A 162 1687 1479 1589 6 -3 -80 C ATOM 1197 CD LYS A 162 4.945 37.655 50.035 1.00 13.65 C ANISOU 1197 CD LYS A 162 1988 1566 1632 -60 -39 15 C ATOM 1198 CE LYS A 162 5.101 36.443 50.931 1.00 14.46 C ANISOU 1198 CE LYS A 162 2035 1678 1778 -92 -35 -9 C ATOM 1199 NZ LYS A 162 3.935 35.457 50.822 1.00 14.63 N ANISOU 1199 NZ LYS A 162 1982 1748 1826 -230 -68 -62 N ATOM 1200 N LYS A 163 6.095 42.782 48.364 1.00 10.80 N ANISOU 1200 N LYS A 163 1600 1153 1349 -188 -88 0 N ATOM 1201 CA LYS A 163 6.039 43.769 47.284 1.00 11.62 C ANISOU 1201 CA LYS A 163 1655 1387 1372 -101 -49 34 C ATOM 1202 C LYS A 163 7.198 44.751 47.345 1.00 11.78 C ANISOU 1202 C LYS A 163 1678 1411 1383 -74 0 -3 C ATOM 1203 O LYS A 163 7.760 45.115 46.316 1.00 11.86 O ANISOU 1203 O LYS A 163 1772 1395 1338 -25 98 -49 O ATOM 1204 CB LYS A 163 4.702 44.502 47.288 1.00 12.36 C ANISOU 1204 CB LYS A 163 1742 1461 1492 -79 -46 33 C ATOM 1205 CG LYS A 163 4.549 45.572 46.173 1.00 14.82 C ANISOU 1205 CG LYS A 163 2002 1802 1827 -91 -24 109 C ATOM 1206 CD LYS A 163 4.693 44.996 44.759 1.00 21.14 C ANISOU 1206 CD LYS A 163 2679 2761 2593 -22 16 -4 C ATOM 1207 CE LYS A 163 3.653 45.578 43.781 1.00 24.28 C ANISOU 1207 CE LYS A 163 3079 3157 2989 -7 -81 58 C ATOM 1208 NZ LYS A 163 3.798 47.034 43.505 1.00 26.16 N ANISOU 1208 NZ LYS A 163 3226 3383 3330 -29 -156 66 N ATOM 1209 N LEU A 164 7.553 45.198 48.547 1.00 11.09 N ANISOU 1209 N LEU A 164 1548 1393 1269 -89 -3 1 N ATOM 1210 CA LEU A 164 8.707 46.081 48.690 1.00 10.61 C ANISOU 1210 CA LEU A 164 1479 1230 1320 -55 -63 -41 C ATOM 1211 C LEU A 164 10.010 45.414 48.258 1.00 10.65 C ANISOU 1211 C LEU A 164 1498 1244 1304 -93 -46 -41 C ATOM 1212 O LEU A 164 10.853 46.031 47.614 1.00 10.54 O ANISOU 1212 O LEU A 164 1588 1058 1356 -117 -38 -70 O ATOM 1213 CB LEU A 164 8.819 46.589 50.122 1.00 10.97 C ANISOU 1213 CB LEU A 164 1518 1392 1257 -23 -5 6 C ATOM 1214 CG LEU A 164 7.755 47.524 50.636 1.00 11.13 C ANISOU 1214 CG LEU A 164 1473 1305 1448 2 -57 -7 C ATOM 1215 CD1 LEU A 164 7.908 47.631 52.140 1.00 11.34 C ANISOU 1215 CD1 LEU A 164 1546 1502 1258 92 76 61 C ATOM 1216 CD2 LEU A 164 7.844 48.922 49.977 1.00 10.74 C ANISOU 1216 CD2 LEU A 164 1664 1264 1150 50 76 45 C ATOM 1217 N ILE A 165 10.153 44.131 48.585 1.00 11.16 N ANISOU 1217 N ILE A 165 1578 1270 1389 -45 -54 6 N ATOM 1218 CA ILE A 165 11.333 43.363 48.201 1.00 12.12 C ANISOU 1218 CA ILE A 165 1653 1490 1461 -72 10 -9 C ATOM 1219 C ILE A 165 11.383 43.289 46.665 1.00 12.97 C ANISOU 1219 C ILE A 165 1748 1647 1531 -52 20 -17 C ATOM 1220 O ILE A 165 12.433 43.511 46.057 1.00 13.01 O ANISOU 1220 O ILE A 165 1770 1679 1491 -63 3 -60 O ATOM 1221 CB ILE A 165 11.313 41.938 48.833 1.00 12.25 C ANISOU 1221 CB ILE A 165 1652 1493 1509 -22 3 14 C ATOM 1222 CG1 ILE A 165 11.578 42.025 50.344 1.00 12.01 C ANISOU 1222 CG1 ILE A 165 1690 1451 1421 -37 -7 76 C ATOM 1223 CG2 ILE A 165 12.325 41.018 48.141 1.00 12.32 C ANISOU 1223 CG2 ILE A 165 1719 1557 1402 -24 44 132 C ATOM 1224 CD1 ILE A 165 11.296 40.753 51.155 1.00 11.55 C ANISOU 1224 CD1 ILE A 165 1697 1373 1317 70 -85 -28 C ATOM 1225 N GLU A 166 10.226 43.030 46.053 1.00 13.99 N ANISOU 1225 N GLU A 166 1908 1791 1616 -72 35 -52 N ATOM 1226 CA GLU A 166 10.174 42.893 44.600 1.00 15.84 C ANISOU 1226 CA GLU A 166 2152 2014 1851 -93 17 -41 C ATOM 1227 C GLU A 166 10.496 44.208 43.901 1.00 15.52 C ANISOU 1227 C GLU A 166 2149 1965 1782 -38 54 -53 C ATOM 1228 O GLU A 166 11.109 44.213 42.842 1.00 15.88 O ANISOU 1228 O GLU A 166 2293 2037 1703 -210 103 -154 O ATOM 1229 CB GLU A 166 8.843 42.311 44.149 1.00 17.31 C ANISOU 1229 CB GLU A 166 2267 2238 2071 -56 36 -9 C ATOM 1230 CG GLU A 166 8.788 40.781 44.290 1.00 21.07 C ANISOU 1230 CG GLU A 166 2804 2502 2698 25 15 -6 C ATOM 1231 CD GLU A 166 10.135 40.056 44.046 1.00 26.79 C ANISOU 1231 CD GLU A 166 3420 3383 3374 27 64 -10 C ATOM 1232 OE1 GLU A 166 10.723 39.487 45.010 1.00 28.15 O ANISOU 1232 OE1 GLU A 166 3684 3565 3447 113 8 -22 O ATOM 1233 OE2 GLU A 166 10.602 40.025 42.886 1.00 29.95 O ANISOU 1233 OE2 GLU A 166 4057 3765 3554 88 137 17 O ATOM 1234 N MET A 167 10.132 45.328 44.523 1.00 14.67 N ANISOU 1234 N MET A 167 2105 1787 1680 -81 35 -57 N ATOM 1235 CA MET A 167 10.477 46.662 44.002 1.00 14.55 C ANISOU 1235 CA MET A 167 2040 1843 1646 -31 32 10 C ATOM 1236 C MET A 167 11.977 46.946 44.052 1.00 13.89 C ANISOU 1236 C MET A 167 1994 1722 1561 -79 36 -53 C ATOM 1237 O MET A 167 12.449 47.856 43.387 1.00 14.54 O ANISOU 1237 O MET A 167 2115 1862 1544 -117 58 -78 O ATOM 1238 CB MET A 167 9.744 47.747 44.799 1.00 14.67 C ANISOU 1238 CB MET A 167 2080 1834 1657 -37 47 91 C ATOM 1239 CG MET A 167 8.269 47.817 44.502 1.00 15.87 C ANISOU 1239 CG MET A 167 2129 2108 1790 -17 31 182 C ATOM 1240 SD MET A 167 7.451 49.130 45.417 1.00 19.12 S ANISOU 1240 SD MET A 167 2739 2625 1899 43 -16 270 S ATOM 1241 CE MET A 167 7.949 50.537 44.515 1.00 16.56 C ANISOU 1241 CE MET A 167 2396 1933 1960 26 164 307 C ATOM 1242 N GLY A 168 12.728 46.193 44.850 1.00 12.69 N ANISOU 1242 N GLY A 168 1799 1587 1436 -89 18 -122 N ATOM 1243 CA GLY A 168 14.162 46.421 44.983 1.00 12.88 C ANISOU 1243 CA GLY A 168 1768 1660 1466 -76 24 -94 C ATOM 1244 C GLY A 168 14.636 46.867 46.368 1.00 12.50 C ANISOU 1244 C GLY A 168 1674 1586 1486 -120 -34 -89 C ATOM 1245 O GLY A 168 15.816 47.161 46.539 1.00 13.69 O ANISOU 1245 O GLY A 168 1778 1859 1562 -91 -1 -139 O ATOM 1246 N PHE A 169 13.739 46.886 47.354 1.00 11.49 N ANISOU 1246 N PHE A 169 1543 1441 1382 -145 -48 -101 N ATOM 1247 CA PHE A 169 14.147 47.166 48.746 1.00 11.31 C ANISOU 1247 CA PHE A 169 1544 1405 1348 -62 -12 -67 C ATOM 1248 C PHE A 169 14.809 46.003 49.456 1.00 11.23 C ANISOU 1248 C PHE A 169 1500 1392 1372 -42 -3 -73 C ATOM 1249 O PHE A 169 14.390 44.823 49.317 1.00 11.20 O ANISOU 1249 O PHE A 169 1636 1190 1427 -35 -66 -178 O ATOM 1250 CB PHE A 169 12.967 47.657 49.596 1.00 11.07 C ANISOU 1250 CB PHE A 169 1511 1444 1249 -93 -4 -30 C ATOM 1251 CG PHE A 169 12.528 49.063 49.274 1.00 12.40 C ANISOU 1251 CG PHE A 169 1686 1633 1392 11 -31 -25 C ATOM 1252 CD1 PHE A 169 13.126 50.159 49.889 1.00 12.65 C ANISOU 1252 CD1 PHE A 169 1883 1407 1512 22 -52 -2 C ATOM 1253 CD2 PHE A 169 11.533 49.290 48.336 1.00 12.55 C ANISOU 1253 CD2 PHE A 169 1619 1633 1513 -16 -64 -1 C ATOM 1254 CE1 PHE A 169 12.730 51.465 49.596 1.00 11.97 C ANISOU 1254 CE1 PHE A 169 1747 1510 1290 69 -41 110 C ATOM 1255 CE2 PHE A 169 11.119 50.580 48.033 1.00 12.18 C ANISOU 1255 CE2 PHE A 169 1676 1449 1500 -102 -130 28 C ATOM 1256 CZ PHE A 169 11.707 51.677 48.669 1.00 11.51 C ANISOU 1256 CZ PHE A 169 1615 1297 1459 -40 -87 81 C ATOM 1257 N ARG A 170 15.824 46.337 50.254 1.00 10.23 N ANISOU 1257 N ARG A 170 1401 1193 1291 37 27 -95 N ATOM 1258 CA ARG A 170 16.253 45.471 51.347 1.00 10.56 C ANISOU 1258 CA ARG A 170 1456 1295 1261 64 28 -66 C ATOM 1259 C ARG A 170 15.363 45.815 52.531 1.00 10.50 C ANISOU 1259 C ARG A 170 1451 1285 1253 95 -15 -26 C ATOM 1260 O ARG A 170 15.455 46.914 53.077 1.00 10.54 O ANISOU 1260 O ARG A 170 1615 1353 1035 -15 -43 -135 O ATOM 1261 CB ARG A 170 17.737 45.660 51.664 1.00 10.03 C ANISOU 1261 CB ARG A 170 1353 1245 1211 151 64 -18 C ATOM 1262 CG ARG A 170 18.666 44.849 50.723 1.00 11.19 C ANISOU 1262 CG ARG A 170 1561 1344 1346 103 90 -64 C ATOM 1263 CD ARG A 170 20.113 45.370 50.735 1.00 10.67 C ANISOU 1263 CD ARG A 170 1520 1103 1430 -47 76 -18 C ATOM 1264 NE ARG A 170 20.139 46.751 50.255 1.00 11.31 N ANISOU 1264 NE ARG A 170 1582 1229 1485 -29 120 -86 N ATOM 1265 CZ ARG A 170 20.882 47.736 50.749 1.00 12.63 C ANISOU 1265 CZ ARG A 170 1838 1471 1487 -69 141 -181 C ATOM 1266 NH1 ARG A 170 21.773 47.527 51.701 1.00 10.77 N ANISOU 1266 NH1 ARG A 170 1467 1184 1439 -47 43 -117 N ATOM 1267 NH2 ARG A 170 20.727 48.944 50.241 1.00 13.05 N ANISOU 1267 NH2 ARG A 170 2078 1658 1220 27 95 -138 N ATOM 1268 N VAL A 171 14.480 44.890 52.881 1.00 10.14 N ANISOU 1268 N VAL A 171 1364 1207 1282 41 -9 -44 N ATOM 1269 CA VAL A 171 13.450 45.119 53.873 1.00 10.52 C ANISOU 1269 CA VAL A 171 1409 1311 1278 -1 0 -58 C ATOM 1270 C VAL A 171 13.837 44.513 55.232 1.00 9.82 C ANISOU 1270 C VAL A 171 1366 1162 1202 25 -26 -77 C ATOM 1271 O VAL A 171 14.196 43.349 55.351 1.00 9.92 O ANISOU 1271 O VAL A 171 1517 1118 1132 60 15 -15 O ATOM 1272 CB VAL A 171 12.080 44.577 53.399 1.00 11.15 C ANISOU 1272 CB VAL A 171 1473 1369 1391 -36 -2 -45 C ATOM 1273 CG1 VAL A 171 11.010 44.705 54.476 1.00 11.69 C ANISOU 1273 CG1 VAL A 171 1441 1427 1570 81 -8 58 C ATOM 1274 CG2 VAL A 171 11.659 45.295 52.127 1.00 10.73 C ANISOU 1274 CG2 VAL A 171 1309 1359 1408 16 -56 -78 C ATOM 1275 N SER A 172 13.803 45.348 56.264 1.00 9.00 N ANISOU 1275 N SER A 172 1397 852 1169 -46 -38 -123 N ATOM 1276 CA SER A 172 13.934 44.887 57.623 1.00 7.95 C ANISOU 1276 CA SER A 172 1188 799 1030 -42 -127 -86 C ATOM 1277 C SER A 172 12.544 44.759 58.217 1.00 8.46 C ANISOU 1277 C SER A 172 1234 889 1089 -58 -69 -35 C ATOM 1278 O SER A 172 11.670 45.586 57.936 1.00 9.29 O ANISOU 1278 O SER A 172 1364 1024 1139 -30 -69 -23 O ATOM 1279 CB SER A 172 14.718 45.897 58.462 1.00 7.37 C ANISOU 1279 CB SER A 172 1126 617 1055 -102 -136 -21 C ATOM 1280 OG SER A 172 16.030 46.006 58.027 1.00 8.89 O ANISOU 1280 OG SER A 172 1461 829 1087 -128 -140 -82 O ATOM 1281 N VAL A 173 12.317 43.714 59.022 1.00 8.31 N ANISOU 1281 N VAL A 173 1280 875 1003 -60 -83 -67 N ATOM 1282 CA VAL A 173 11.040 43.588 59.710 1.00 9.04 C ANISOU 1282 CA VAL A 173 1286 1048 1100 -87 -85 -73 C ATOM 1283 C VAL A 173 11.251 43.650 61.226 1.00 9.46 C ANISOU 1283 C VAL A 173 1272 1156 1165 -78 -30 -36 C ATOM 1284 O VAL A 173 12.311 43.269 61.747 1.00 8.67 O ANISOU 1284 O VAL A 173 1193 1000 1101 -12 -76 -91 O ATOM 1285 CB VAL A 173 10.269 42.285 59.315 1.00 9.89 C ANISOU 1285 CB VAL A 173 1425 1162 1168 -89 -70 -48 C ATOM 1286 CG1 VAL A 173 9.891 42.257 57.865 1.00 9.66 C ANISOU 1286 CG1 VAL A 173 1576 1020 1073 29 -113 -152 C ATOM 1287 CG2 VAL A 173 11.092 41.060 59.659 1.00 9.48 C ANISOU 1287 CG2 VAL A 173 1549 985 1064 -175 -119 -57 C ATOM 1288 N THR A 174 10.228 44.127 61.927 1.00 9.70 N ANISOU 1288 N THR A 174 1324 1162 1200 -62 -44 -35 N ATOM 1289 CA THR A 174 10.258 44.200 63.385 1.00 11.37 C ANISOU 1289 CA THR A 174 1541 1435 1344 -40 -22 -19 C ATOM 1290 C THR A 174 8.882 43.981 63.944 1.00 11.14 C ANISOU 1290 C THR A 174 1481 1381 1367 -42 -60 -2 C ATOM 1291 O THR A 174 7.883 44.303 63.281 1.00 11.56 O ANISOU 1291 O THR A 174 1716 1410 1263 43 -49 22 O ATOM 1292 CB THR A 174 10.835 45.544 63.855 1.00 11.09 C ANISOU 1292 CB THR A 174 1467 1368 1376 -29 -50 -25 C ATOM 1293 OG1 THR A 174 11.062 45.495 65.272 1.00 14.14 O ANISOU 1293 OG1 THR A 174 2051 1839 1479 -94 -46 -76 O ATOM 1294 CG2 THR A 174 9.894 46.702 63.599 1.00 11.62 C ANISOU 1294 CG2 THR A 174 1592 1363 1458 -34 -1 -61 C ATOM 1295 N GLY A 175 8.824 43.401 65.150 1.00 11.27 N ANISOU 1295 N GLY A 175 1505 1420 1357 -35 -22 11 N ATOM 1296 CA GLY A 175 7.559 43.070 65.810 1.00 11.96 C ANISOU 1296 CA GLY A 175 1548 1498 1495 -88 -19 44 C ATOM 1297 C GLY A 175 7.185 41.615 65.612 1.00 12.56 C ANISOU 1297 C GLY A 175 1626 1574 1573 -39 13 84 C ATOM 1298 O GLY A 175 7.255 41.123 64.503 1.00 13.42 O ANISOU 1298 O GLY A 175 1741 1748 1607 -127 29 175 O ATOM 1299 N GLY A 176 6.822 40.917 66.697 1.00 13.51 N ANISOU 1299 N GLY A 176 1764 1656 1713 -45 11 76 N ATOM 1300 CA GLY A 176 6.302 39.563 66.574 1.00 14.36 C ANISOU 1300 CA GLY A 176 1871 1749 1835 -51 -25 22 C ATOM 1301 C GLY A 176 7.370 38.556 66.203 1.00 15.28 C ANISOU 1301 C GLY A 176 2031 1813 1960 -67 -26 -65 C ATOM 1302 O GLY A 176 7.074 37.510 65.600 1.00 15.57 O ANISOU 1302 O GLY A 176 2120 1706 2089 -106 -13 -102 O ATOM 1303 N LEU A 177 8.623 38.856 66.528 1.00 15.04 N ANISOU 1303 N LEU A 177 2008 1822 1883 -16 -91 -15 N ATOM 1304 CA LEU A 177 9.713 37.988 66.132 1.00 15.81 C ANISOU 1304 CA LEU A 177 2130 1972 1906 -7 -59 4 C ATOM 1305 C LEU A 177 10.224 37.182 67.306 1.00 17.22 C ANISOU 1305 C LEU A 177 2349 2133 2059 35 -113 36 C ATOM 1306 O LEU A 177 10.546 37.734 68.350 1.00 18.06 O ANISOU 1306 O LEU A 177 2580 2282 1999 75 -203 115 O ATOM 1307 CB LEU A 177 10.859 38.784 65.538 1.00 14.85 C ANISOU 1307 CB LEU A 177 2029 1763 1847 -52 -66 -36 C ATOM 1308 CG LEU A 177 10.486 39.713 64.389 1.00 14.52 C ANISOU 1308 CG LEU A 177 1896 1790 1830 -37 44 33 C ATOM 1309 CD1 LEU A 177 11.751 40.381 63.931 1.00 14.38 C ANISOU 1309 CD1 LEU A 177 1943 1635 1884 -184 9 -90 C ATOM 1310 CD2 LEU A 177 9.804 38.974 63.263 1.00 13.75 C ANISOU 1310 CD2 LEU A 177 1765 1720 1739 -70 62 80 C ATOM 1311 N SER A 178 10.295 35.877 67.112 1.00 18.43 N ANISOU 1311 N SER A 178 2507 2268 2226 15 -87 28 N ATOM 1312 CA SER A 178 10.928 34.996 68.078 1.00 19.43 C ANISOU 1312 CA SER A 178 2619 2387 2375 15 -20 58 C ATOM 1313 C SER A 178 11.500 33.817 67.325 1.00 19.35 C ANISOU 1313 C SER A 178 2634 2327 2388 24 -20 61 C ATOM 1314 O SER A 178 11.201 33.605 66.144 1.00 18.11 O ANISOU 1314 O SER A 178 2637 2038 2203 33 -43 121 O ATOM 1315 CB SER A 178 9.925 34.539 69.148 1.00 20.29 C ANISOU 1315 CB SER A 178 2686 2526 2497 -10 -12 69 C ATOM 1316 OG SER A 178 8.924 33.693 68.598 1.00 22.30 O ANISOU 1316 OG SER A 178 2932 2707 2832 -149 83 90 O ATOM 1317 N VAL A 179 12.321 33.031 67.992 1.00 19.80 N ANISOU 1317 N VAL A 179 2606 2467 2448 50 -34 53 N ATOM 1318 CA VAL A 179 12.948 31.911 67.300 1.00 20.64 C ANISOU 1318 CA VAL A 179 2699 2571 2571 15 -6 4 C ATOM 1319 C VAL A 179 11.877 30.974 66.704 1.00 21.88 C ANISOU 1319 C VAL A 179 2840 2750 2722 47 -5 4 C ATOM 1320 O VAL A 179 12.022 30.485 65.582 1.00 22.12 O ANISOU 1320 O VAL A 179 2911 2736 2757 38 -71 -26 O ATOM 1321 CB VAL A 179 14.036 31.219 68.214 1.00 20.54 C ANISOU 1321 CB VAL A 179 2696 2528 2579 45 4 19 C ATOM 1322 CG1 VAL A 179 13.424 30.596 69.462 1.00 20.82 C ANISOU 1322 CG1 VAL A 179 2769 2472 2668 -7 25 19 C ATOM 1323 CG2 VAL A 179 14.897 30.242 67.421 1.00 20.27 C ANISOU 1323 CG2 VAL A 179 2642 2521 2537 -18 48 14 C ATOM 1324 N ASP A 180 10.783 30.775 67.424 1.00 23.30 N ANISOU 1324 N ASP A 180 2980 2939 2931 1 13 -1 N ATOM 1325 CA ASP A 180 9.687 29.952 66.929 1.00 24.81 C ANISOU 1325 CA ASP A 180 3176 3092 3157 -4 14 -28 C ATOM 1326 C ASP A 180 8.891 30.573 65.774 1.00 24.38 C ANISOU 1326 C ASP A 180 3127 3029 3107 -26 19 -11 C ATOM 1327 O ASP A 180 8.281 29.848 64.997 1.00 25.18 O ANISOU 1327 O ASP A 180 3210 3113 3241 -32 -3 -39 O ATOM 1328 CB ASP A 180 8.752 29.558 68.088 1.00 26.14 C ANISOU 1328 CB ASP A 180 3340 3282 3309 -35 24 -13 C ATOM 1329 CG ASP A 180 9.482 28.811 69.197 1.00 29.67 C ANISOU 1329 CG ASP A 180 3831 3710 3730 23 10 24 C ATOM 1330 OD1 ASP A 180 10.379 28.000 68.882 1.00 33.53 O ANISOU 1330 OD1 ASP A 180 4305 4211 4222 83 32 60 O ATOM 1331 OD2 ASP A 180 9.211 29.013 70.409 1.00 34.50 O ANISOU 1331 OD2 ASP A 180 4447 4428 4230 -86 54 12 O ATOM 1332 N THR A 181 8.903 31.898 65.625 1.00 24.18 N ANISOU 1332 N THR A 181 3082 3032 3070 78 1 -54 N ATOM 1333 CA THR A 181 8.131 32.535 64.523 1.00 23.52 C ANISOU 1333 CA THR A 181 3009 2988 2939 58 -8 -18 C ATOM 1334 C THR A 181 8.909 32.871 63.263 1.00 22.53 C ANISOU 1334 C THR A 181 2914 2827 2818 84 -32 -79 C ATOM 1335 O THR A 181 8.334 33.378 62.297 1.00 22.91 O ANISOU 1335 O THR A 181 2968 2898 2838 141 -64 -84 O ATOM 1336 CB THR A 181 7.381 33.814 64.970 1.00 23.56 C ANISOU 1336 CB THR A 181 2986 2997 2965 55 -10 -43 C ATOM 1337 OG1 THR A 181 8.294 34.917 65.111 1.00 24.52 O ANISOU 1337 OG1 THR A 181 3061 3220 3032 105 -18 -90 O ATOM 1338 CG2 THR A 181 6.665 33.600 66.284 1.00 24.05 C ANISOU 1338 CG2 THR A 181 3046 3074 3017 1 -32 69 C ATOM 1339 N LEU A 182 10.210 32.639 63.256 1.00 20.44 N ANISOU 1339 N LEU A 182 2673 2504 2590 42 -27 -106 N ATOM 1340 CA LEU A 182 10.958 32.885 62.049 1.00 19.41 C ANISOU 1340 CA LEU A 182 2527 2357 2490 -8 -59 -70 C ATOM 1341 C LEU A 182 10.398 32.052 60.890 1.00 17.94 C ANISOU 1341 C LEU A 182 2332 2155 2327 -14 -36 -69 C ATOM 1342 O LEU A 182 10.281 32.565 59.800 1.00 17.96 O ANISOU 1342 O LEU A 182 2340 2142 2340 -60 -37 -94 O ATOM 1343 CB LEU A 182 12.442 32.629 62.239 1.00 19.43 C ANISOU 1343 CB LEU A 182 2515 2340 2527 19 -61 -70 C ATOM 1344 CG LEU A 182 13.189 33.696 63.025 1.00 20.70 C ANISOU 1344 CG LEU A 182 2747 2578 2540 -44 -60 -40 C ATOM 1345 CD1 LEU A 182 14.513 33.140 63.489 1.00 22.18 C ANISOU 1345 CD1 LEU A 182 2930 2716 2778 -91 27 -96 C ATOM 1346 CD2 LEU A 182 13.392 34.972 62.187 1.00 22.36 C ANISOU 1346 CD2 LEU A 182 3036 2658 2801 -18 -62 0 C ATOM 1347 N LYS A 183 10.011 30.802 61.147 1.00 17.54 N ANISOU 1347 N LYS A 183 2215 2157 2290 -44 -47 -9 N ATOM 1348 CA LYS A 183 9.482 29.930 60.090 1.00 17.12 C ANISOU 1348 CA LYS A 183 2253 2035 2216 -12 12 14 C ATOM 1349 C LYS A 183 8.296 30.540 59.302 1.00 16.44 C ANISOU 1349 C LYS A 183 2111 1981 2152 -72 29 24 C ATOM 1350 O LYS A 183 8.083 30.195 58.150 1.00 15.68 O ANISOU 1350 O LYS A 183 2053 1824 2078 -161 68 -24 O ATOM 1351 CB LYS A 183 9.151 28.518 60.635 1.00 17.67 C ANISOU 1351 CB LYS A 183 2289 2094 2328 0 -16 -7 C ATOM 1352 CG LYS A 183 7.990 28.423 61.600 1.00 20.22 C ANISOU 1352 CG LYS A 183 2644 2476 2561 21 35 72 C ATOM 1353 CD LYS A 183 7.705 26.975 61.998 1.00 23.32 C ANISOU 1353 CD LYS A 183 2997 2858 3004 -155 -21 28 C ATOM 1354 CE LYS A 183 8.828 26.364 62.841 1.00 25.10 C ANISOU 1354 CE LYS A 183 3299 3043 3194 -21 12 23 C ATOM 1355 NZ LYS A 183 9.115 27.099 64.101 1.00 25.76 N ANISOU 1355 NZ LYS A 183 3354 3133 3301 -185 -117 1 N ATOM 1356 N LEU A 184 7.562 31.479 59.903 1.00 16.80 N ANISOU 1356 N LEU A 184 2227 2032 2123 -9 49 44 N ATOM 1357 CA LEU A 184 6.502 32.227 59.186 1.00 18.23 C ANISOU 1357 CA LEU A 184 2345 2305 2277 31 10 2 C ATOM 1358 C LEU A 184 7.011 32.891 57.920 1.00 17.04 C ANISOU 1358 C LEU A 184 2170 2155 2148 51 -14 -18 C ATOM 1359 O LEU A 184 6.258 33.096 56.962 1.00 17.20 O ANISOU 1359 O LEU A 184 2090 2257 2187 34 -43 -1 O ATOM 1360 CB LEU A 184 5.945 33.367 60.053 1.00 18.96 C ANISOU 1360 CB LEU A 184 2434 2384 2383 113 50 43 C ATOM 1361 CG LEU A 184 5.385 33.035 61.418 1.00 22.42 C ANISOU 1361 CG LEU A 184 2846 2916 2756 39 3 -6 C ATOM 1362 CD1 LEU A 184 4.995 34.332 62.153 1.00 23.02 C ANISOU 1362 CD1 LEU A 184 2963 2914 2867 121 58 -25 C ATOM 1363 CD2 LEU A 184 4.230 32.093 61.254 1.00 24.70 C ANISOU 1363 CD2 LEU A 184 3166 3136 3081 -50 1 46 C ATOM 1364 N PHE A 185 8.275 33.284 57.958 1.00 15.15 N ANISOU 1364 N PHE A 185 1919 1853 1983 59 -7 -54 N ATOM 1365 CA PHE A 185 8.903 34.040 56.895 1.00 14.45 C ANISOU 1365 CA PHE A 185 1840 1746 1903 46 -38 -80 C ATOM 1366 C PHE A 185 9.603 33.178 55.855 1.00 14.18 C ANISOU 1366 C PHE A 185 1832 1685 1867 -6 -9 -42 C ATOM 1367 O PHE A 185 10.286 33.702 54.985 1.00 14.12 O ANISOU 1367 O PHE A 185 1810 1705 1848 -52 -14 -39 O ATOM 1368 CB PHE A 185 9.913 35.009 57.493 1.00 14.13 C ANISOU 1368 CB PHE A 185 1845 1597 1926 14 -1 -119 C ATOM 1369 CG PHE A 185 9.276 36.140 58.285 1.00 14.19 C ANISOU 1369 CG PHE A 185 1786 1647 1957 90 -60 -139 C ATOM 1370 CD1 PHE A 185 8.843 37.291 57.648 1.00 14.87 C ANISOU 1370 CD1 PHE A 185 1883 1784 1984 125 -8 -162 C ATOM 1371 CD2 PHE A 185 9.116 36.033 59.662 1.00 14.85 C ANISOU 1371 CD2 PHE A 185 1704 1891 2044 -18 27 -176 C ATOM 1372 CE1 PHE A 185 8.277 38.349 58.405 1.00 15.03 C ANISOU 1372 CE1 PHE A 185 1998 1584 2127 118 -84 -115 C ATOM 1373 CE2 PHE A 185 8.545 37.058 60.404 1.00 15.59 C ANISOU 1373 CE2 PHE A 185 1867 1921 2133 -82 15 -12 C ATOM 1374 CZ PHE A 185 8.112 38.210 59.773 1.00 14.95 C ANISOU 1374 CZ PHE A 185 1854 1611 2216 -8 -39 -159 C ATOM 1375 N GLU A 186 9.421 31.865 55.933 1.00 13.99 N ANISOU 1375 N GLU A 186 1837 1640 1838 -36 -56 -28 N ATOM 1376 CA GLU A 186 10.047 30.954 54.987 1.00 14.88 C ANISOU 1376 CA GLU A 186 1962 1770 1920 -29 -63 -6 C ATOM 1377 C GLU A 186 9.741 31.397 53.555 1.00 15.06 C ANISOU 1377 C GLU A 186 2017 1699 2007 -59 -94 -88 C ATOM 1378 O GLU A 186 8.603 31.728 53.225 1.00 15.92 O ANISOU 1378 O GLU A 186 2094 1786 2167 -90 -169 -198 O ATOM 1379 CB GLU A 186 9.583 29.511 55.243 1.00 14.51 C ANISOU 1379 CB GLU A 186 1825 1733 1953 -75 -97 -72 C ATOM 1380 CG GLU A 186 10.545 28.407 54.743 1.00 15.51 C ANISOU 1380 CG GLU A 186 2044 1824 2025 -63 9 72 C ATOM 1381 CD GLU A 186 10.635 28.284 53.215 1.00 15.54 C ANISOU 1381 CD GLU A 186 2090 1719 2096 -91 -69 -210 C ATOM 1382 OE1 GLU A 186 9.588 28.403 52.559 1.00 16.73 O ANISOU 1382 OE1 GLU A 186 1999 1936 2421 -168 -106 -169 O ATOM 1383 OE2 GLU A 186 11.752 28.105 52.663 1.00 15.32 O ANISOU 1383 OE2 GLU A 186 2059 1683 2079 -56 -11 -91 O ATOM 1384 N GLY A 187 10.772 31.429 52.725 1.00 14.71 N ANISOU 1384 N GLY A 187 1998 1620 1970 -66 -40 -86 N ATOM 1385 CA GLY A 187 10.624 31.881 51.351 1.00 15.25 C ANISOU 1385 CA GLY A 187 2102 1713 1977 -64 -51 -70 C ATOM 1386 C GLY A 187 10.532 33.386 51.137 1.00 15.07 C ANISOU 1386 C GLY A 187 2148 1658 1920 -51 -57 -43 C ATOM 1387 O GLY A 187 10.366 33.834 49.996 1.00 16.02 O ANISOU 1387 O GLY A 187 2345 1703 2036 -63 -80 -105 O ATOM 1388 N VAL A 188 10.629 34.168 52.212 1.00 14.23 N ANISOU 1388 N VAL A 188 1991 1594 1821 -32 -107 -30 N ATOM 1389 CA VAL A 188 10.631 35.639 52.104 1.00 13.13 C ANISOU 1389 CA VAL A 188 1796 1425 1766 -50 -80 -35 C ATOM 1390 C VAL A 188 12.067 36.124 52.319 1.00 12.39 C ANISOU 1390 C VAL A 188 1783 1274 1649 -2 -47 -127 C ATOM 1391 O VAL A 188 12.676 35.800 53.323 1.00 11.83 O ANISOU 1391 O VAL A 188 1844 1001 1649 -126 -112 -274 O ATOM 1392 CB VAL A 188 9.654 36.301 53.137 1.00 13.21 C ANISOU 1392 CB VAL A 188 1752 1451 1816 -9 -84 -40 C ATOM 1393 CG1 VAL A 188 9.549 37.819 52.948 1.00 13.96 C ANISOU 1393 CG1 VAL A 188 1925 1449 1928 -125 -89 -18 C ATOM 1394 CG2 VAL A 188 8.264 35.673 53.029 1.00 13.50 C ANISOU 1394 CG2 VAL A 188 1662 1541 1926 -38 -56 16 C ATOM 1395 N ASP A 189 12.593 36.861 51.350 1.00 12.99 N ANISOU 1395 N ASP A 189 1837 1395 1701 -1 27 -149 N ATOM 1396 CA ASP A 189 13.979 37.334 51.316 1.00 13.47 C ANISOU 1396 CA ASP A 189 1913 1532 1670 -19 -11 -173 C ATOM 1397 C ASP A 189 14.196 38.556 52.240 1.00 13.23 C ANISOU 1397 C ASP A 189 1926 1510 1590 -64 -37 -157 C ATOM 1398 O ASP A 189 14.603 39.628 51.805 1.00 13.72 O ANISOU 1398 O ASP A 189 2105 1506 1601 -104 -88 -226 O ATOM 1399 CB ASP A 189 14.320 37.676 49.858 1.00 14.47 C ANISOU 1399 CB ASP A 189 1991 1736 1770 -3 16 -137 C ATOM 1400 CG ASP A 189 15.778 38.008 49.643 1.00 17.43 C ANISOU 1400 CG ASP A 189 2294 2181 2145 -42 12 -114 C ATOM 1401 OD1 ASP A 189 16.641 37.380 50.284 1.00 20.65 O ANISOU 1401 OD1 ASP A 189 2637 2659 2550 154 4 -130 O ATOM 1402 OD2 ASP A 189 16.116 38.886 48.809 1.00 20.43 O ANISOU 1402 OD2 ASP A 189 2778 2435 2548 57 131 55 O ATOM 1403 N VAL A 190 13.911 38.352 53.514 1.00 12.32 N ANISOU 1403 N VAL A 190 1775 1445 1460 -33 -5 -223 N ATOM 1404 CA VAL A 190 14.056 39.394 54.545 1.00 11.07 C ANISOU 1404 CA VAL A 190 1603 1174 1428 -30 -25 -171 C ATOM 1405 C VAL A 190 15.534 39.755 54.660 1.00 11.01 C ANISOU 1405 C VAL A 190 1581 1164 1439 -19 12 -131 C ATOM 1406 O VAL A 190 16.388 38.873 54.763 1.00 10.73 O ANISOU 1406 O VAL A 190 1636 814 1625 -21 -64 -274 O ATOM 1407 CB VAL A 190 13.532 38.900 55.924 1.00 11.24 C ANISOU 1407 CB VAL A 190 1562 1264 1444 17 -33 -206 C ATOM 1408 CG1 VAL A 190 13.878 39.882 57.047 1.00 10.87 C ANISOU 1408 CG1 VAL A 190 1567 1138 1422 -95 43 -179 C ATOM 1409 CG2 VAL A 190 12.033 38.638 55.878 1.00 11.54 C ANISOU 1409 CG2 VAL A 190 1582 1210 1590 -144 -33 -131 C ATOM 1410 N PHE A 191 15.835 41.053 54.691 1.00 9.78 N ANISOU 1410 N PHE A 191 1433 896 1384 9 6 -93 N ATOM 1411 CA PHE A 191 17.226 41.526 54.780 1.00 9.44 C ANISOU 1411 CA PHE A 191 1394 945 1245 30 -1 19 C ATOM 1412 C PHE A 191 17.760 41.474 56.207 1.00 9.86 C ANISOU 1412 C PHE A 191 1389 1027 1328 20 -11 -33 C ATOM 1413 O PHE A 191 18.877 41.033 56.435 1.00 9.26 O ANISOU 1413 O PHE A 191 1579 685 1253 41 -30 6 O ATOM 1414 CB PHE A 191 17.339 42.950 54.205 1.00 9.31 C ANISOU 1414 CB PHE A 191 1376 886 1274 21 43 80 C ATOM 1415 CG PHE A 191 18.676 43.615 54.452 1.00 9.37 C ANISOU 1415 CG PHE A 191 1448 966 1144 97 -54 -20 C ATOM 1416 CD1 PHE A 191 19.839 43.127 53.859 1.00 10.59 C ANISOU 1416 CD1 PHE A 191 1349 1460 1214 0 -10 -29 C ATOM 1417 CD2 PHE A 191 18.761 44.752 55.241 1.00 8.65 C ANISOU 1417 CD2 PHE A 191 1400 626 1259 -32 -115 63 C ATOM 1418 CE1 PHE A 191 21.053 43.728 54.069 1.00 10.60 C ANISOU 1418 CE1 PHE A 191 1582 1437 1007 -58 56 -158 C ATOM 1419 CE2 PHE A 191 20.002 45.374 55.441 1.00 10.66 C ANISOU 1419 CE2 PHE A 191 1403 1235 1412 -90 13 -139 C ATOM 1420 CZ PHE A 191 21.140 44.853 54.854 1.00 11.62 C ANISOU 1420 CZ PHE A 191 1589 1280 1545 -191 -123 -17 C ATOM 1421 N THR A 192 16.936 41.936 57.148 1.00 9.66 N ANISOU 1421 N THR A 192 1340 1023 1307 0 13 -42 N ATOM 1422 CA THR A 192 17.264 41.984 58.557 1.00 9.88 C ANISOU 1422 CA THR A 192 1327 1129 1297 -27 -20 -81 C ATOM 1423 C THR A 192 16.044 41.741 59.411 1.00 9.33 C ANISOU 1423 C THR A 192 1298 1028 1218 -13 -37 -91 C ATOM 1424 O THR A 192 14.968 42.286 59.117 1.00 9.64 O ANISOU 1424 O THR A 192 1346 1058 1259 93 -26 -71 O ATOM 1425 CB THR A 192 17.839 43.372 58.930 1.00 9.87 C ANISOU 1425 CB THR A 192 1303 1095 1352 -68 30 -86 C ATOM 1426 OG1 THR A 192 19.058 43.614 58.217 1.00 10.02 O ANISOU 1426 OG1 THR A 192 1496 1074 1238 -108 120 -179 O ATOM 1427 CG2 THR A 192 18.171 43.439 60.429 1.00 11.09 C ANISOU 1427 CG2 THR A 192 1493 1272 1448 -124 0 -54 C ATOM 1428 N PHE A 193 16.216 40.942 60.468 1.00 8.92 N ANISOU 1428 N PHE A 193 1297 962 1128 -34 12 -104 N ATOM 1429 CA PHE A 193 15.193 40.771 61.512 1.00 9.28 C ANISOU 1429 CA PHE A 193 1328 934 1263 -20 16 -33 C ATOM 1430 C PHE A 193 15.620 41.628 62.722 1.00 9.19 C ANISOU 1430 C PHE A 193 1278 967 1243 -21 -12 -66 C ATOM 1431 O PHE A 193 16.721 41.448 63.239 1.00 9.10 O ANISOU 1431 O PHE A 193 1220 820 1415 40 -23 -29 O ATOM 1432 CB PHE A 193 15.074 39.310 61.933 1.00 9.22 C ANISOU 1432 CB PHE A 193 1369 889 1242 -48 -18 -26 C ATOM 1433 CG PHE A 193 14.420 38.445 60.882 1.00 10.36 C ANISOU 1433 CG PHE A 193 1450 1134 1350 -90 -21 -106 C ATOM 1434 CD1 PHE A 193 13.032 38.415 60.753 1.00 11.82 C ANISOU 1434 CD1 PHE A 193 1597 1363 1529 -192 -140 -21 C ATOM 1435 CD2 PHE A 193 15.188 37.703 60.001 1.00 11.26 C ANISOU 1435 CD2 PHE A 193 1475 1151 1650 0 24 -94 C ATOM 1436 CE1 PHE A 193 12.428 37.620 59.753 1.00 12.20 C ANISOU 1436 CE1 PHE A 193 1665 1330 1639 -99 -45 -75 C ATOM 1437 CE2 PHE A 193 14.586 36.911 59.019 1.00 12.45 C ANISOU 1437 CE2 PHE A 193 1578 1464 1688 -35 -5 -104 C ATOM 1438 CZ PHE A 193 13.216 36.877 58.901 1.00 12.44 C ANISOU 1438 CZ PHE A 193 1637 1332 1755 -66 -44 -5 C ATOM 1439 N ILE A 194 14.762 42.551 63.169 1.00 9.22 N ANISOU 1439 N ILE A 194 1214 1068 1219 -66 -21 -80 N ATOM 1440 CA ILE A 194 15.103 43.456 64.282 1.00 9.53 C ANISOU 1440 CA ILE A 194 1272 1149 1197 -27 -19 -139 C ATOM 1441 C ILE A 194 14.390 42.965 65.538 1.00 9.73 C ANISOU 1441 C ILE A 194 1335 1103 1259 -56 -55 -148 C ATOM 1442 O ILE A 194 13.170 43.044 65.622 1.00 10.09 O ANISOU 1442 O ILE A 194 1390 1224 1217 -49 -54 -126 O ATOM 1443 CB ILE A 194 14.659 44.897 64.002 1.00 9.32 C ANISOU 1443 CB ILE A 194 1255 1111 1172 -72 -43 -111 C ATOM 1444 CG1 ILE A 194 15.250 45.428 62.693 1.00 9.61 C ANISOU 1444 CG1 ILE A 194 1206 1126 1319 4 32 -110 C ATOM 1445 CG2 ILE A 194 15.039 45.782 65.189 1.00 10.84 C ANISOU 1445 CG2 ILE A 194 1565 1312 1240 -6 20 -150 C ATOM 1446 CD1 ILE A 194 14.646 46.778 62.274 1.00 10.98 C ANISOU 1446 CD1 ILE A 194 1413 1221 1538 28 -49 81 C ATOM 1447 N ALA A 195 15.161 42.445 66.488 1.00 10.02 N ANISOU 1447 N ALA A 195 1405 1105 1296 -68 -54 -109 N ATOM 1448 CA ALA A 195 14.654 42.008 67.768 1.00 10.95 C ANISOU 1448 CA ALA A 195 1541 1198 1418 -69 -23 -33 C ATOM 1449 C ALA A 195 15.006 43.067 68.795 1.00 11.24 C ANISOU 1449 C ALA A 195 1596 1287 1385 -119 20 -39 C ATOM 1450 O ALA A 195 15.833 43.943 68.540 1.00 13.02 O ANISOU 1450 O ALA A 195 1880 1451 1616 -265 133 -128 O ATOM 1451 CB ALA A 195 15.256 40.660 68.158 1.00 11.40 C ANISOU 1451 CB ALA A 195 1528 1263 1541 -37 -141 -25 C ATOM 1452 N GLY A 196 14.360 43.000 69.943 1.00 10.86 N ANISOU 1452 N GLY A 196 1491 1267 1367 -143 72 -8 N ATOM 1453 CA GLY A 196 14.598 43.933 71.034 1.00 10.60 C ANISOU 1453 CA GLY A 196 1540 1198 1289 -126 58 78 C ATOM 1454 C GLY A 196 14.557 43.230 72.387 1.00 11.73 C ANISOU 1454 C GLY A 196 1669 1349 1438 -14 31 137 C ATOM 1455 O GLY A 196 15.420 42.403 72.684 1.00 11.63 O ANISOU 1455 O GLY A 196 1716 1265 1438 51 40 135 O ATOM 1456 N ARG A 197 13.586 43.604 73.209 1.00 12.92 N ANISOU 1456 N ARG A 197 1740 1551 1617 -40 46 186 N ATOM 1457 CA ARG A 197 13.475 43.114 74.587 1.00 14.94 C ANISOU 1457 CA ARG A 197 1954 1868 1855 14 32 90 C ATOM 1458 C ARG A 197 13.293 41.602 74.713 1.00 14.59 C ANISOU 1458 C ARG A 197 1889 1827 1826 -6 -10 77 C ATOM 1459 O ARG A 197 13.741 41.003 75.682 1.00 14.44 O ANISOU 1459 O ARG A 197 1854 1867 1765 32 -138 119 O ATOM 1460 CB ARG A 197 12.358 43.873 75.308 1.00 15.68 C ANISOU 1460 CB ARG A 197 2093 1858 2006 18 96 50 C ATOM 1461 CG ARG A 197 12.685 45.372 75.531 1.00 19.17 C ANISOU 1461 CG ARG A 197 2547 2351 2382 -50 29 20 C ATOM 1462 CD ARG A 197 11.525 46.102 76.179 1.00 24.44 C ANISOU 1462 CD ARG A 197 3217 3093 2976 50 81 -2 C ATOM 1463 NE ARG A 197 11.575 46.040 77.642 1.00 29.30 N ANISOU 1463 NE ARG A 197 3778 3795 3558 45 70 -78 N ATOM 1464 CZ ARG A 197 10.510 46.169 78.441 1.00 32.02 C ANISOU 1464 CZ ARG A 197 3948 4207 4010 -9 84 -17 C ATOM 1465 NH1 ARG A 197 9.302 46.371 77.923 1.00 33.26 N ANISOU 1465 NH1 ARG A 197 4045 4343 4246 72 66 18 N ATOM 1466 NH2 ARG A 197 10.658 46.104 79.766 1.00 32.19 N ANISOU 1466 NH2 ARG A 197 4042 4199 3989 30 93 0 N ATOM 1467 N GLY A 198 12.670 40.979 73.720 1.00 15.13 N ANISOU 1467 N GLY A 198 1977 1897 1873 24 -39 67 N ATOM 1468 CA GLY A 198 12.539 39.521 73.668 1.00 15.15 C ANISOU 1468 CA GLY A 198 2047 1764 1942 37 -20 15 C ATOM 1469 C GLY A 198 13.884 38.837 73.821 1.00 15.18 C ANISOU 1469 C GLY A 198 2061 1806 1901 17 -28 11 C ATOM 1470 O GLY A 198 13.992 37.802 74.490 1.00 16.04 O ANISOU 1470 O GLY A 198 2263 1813 2018 59 -37 51 O ATOM 1471 N ILE A 199 14.919 39.413 73.217 1.00 14.16 N ANISOU 1471 N ILE A 199 1937 1686 1757 57 -23 -37 N ATOM 1472 CA ILE A 199 16.263 38.888 73.393 1.00 14.66 C ANISOU 1472 CA ILE A 199 1938 1795 1838 -26 -45 0 C ATOM 1473 C ILE A 199 17.021 39.507 74.573 1.00 14.45 C ANISOU 1473 C ILE A 199 1947 1700 1843 0 -77 28 C ATOM 1474 O ILE A 199 17.685 38.795 75.321 1.00 14.38 O ANISOU 1474 O ILE A 199 2113 1431 1918 -19 -128 199 O ATOM 1475 CB ILE A 199 17.053 39.005 72.082 1.00 15.00 C ANISOU 1475 CB ILE A 199 1981 1858 1859 31 -39 -90 C ATOM 1476 CG1 ILE A 199 16.507 38.011 71.054 1.00 15.12 C ANISOU 1476 CG1 ILE A 199 1931 2013 1800 -133 -46 -39 C ATOM 1477 CG2 ILE A 199 18.497 38.736 72.307 1.00 15.11 C ANISOU 1477 CG2 ILE A 199 1903 1886 1953 7 14 -69 C ATOM 1478 CD1 ILE A 199 17.089 38.205 69.718 1.00 18.45 C ANISOU 1478 CD1 ILE A 199 2400 2379 2230 -136 34 -87 C ATOM 1479 N THR A 200 16.953 40.815 74.753 1.00 13.60 N ANISOU 1479 N THR A 200 1820 1652 1692 -2 -46 13 N ATOM 1480 CA THR A 200 17.828 41.450 75.755 1.00 14.06 C ANISOU 1480 CA THR A 200 1943 1683 1714 -67 -18 3 C ATOM 1481 C THR A 200 17.332 41.257 77.181 1.00 14.73 C ANISOU 1481 C THR A 200 2002 1829 1762 -57 -17 0 C ATOM 1482 O THR A 200 18.113 41.371 78.102 1.00 14.98 O ANISOU 1482 O THR A 200 2125 1783 1782 -93 -51 21 O ATOM 1483 CB THR A 200 18.035 42.958 75.491 1.00 13.04 C ANISOU 1483 CB THR A 200 1825 1555 1573 -59 -34 21 C ATOM 1484 OG1 THR A 200 16.770 43.613 75.516 1.00 13.43 O ANISOU 1484 OG1 THR A 200 2217 1230 1654 -130 -30 77 O ATOM 1485 CG2 THR A 200 18.670 43.185 74.142 1.00 15.22 C ANISOU 1485 CG2 THR A 200 2106 1850 1825 -73 19 32 C ATOM 1486 N GLU A 201 16.051 40.936 77.345 1.00 15.47 N ANISOU 1486 N GLU A 201 2052 2006 1818 -87 47 -35 N ATOM 1487 CA GLU A 201 15.483 40.616 78.674 1.00 17.00 C ANISOU 1487 CA GLU A 201 2252 2163 2044 -73 48 47 C ATOM 1488 C GLU A 201 15.394 39.123 78.943 1.00 16.92 C ANISOU 1488 C GLU A 201 2238 2154 2035 -70 49 99 C ATOM 1489 O GLU A 201 14.813 38.714 79.956 1.00 17.34 O ANISOU 1489 O GLU A 201 2324 2179 2085 -131 76 177 O ATOM 1490 CB GLU A 201 14.084 41.229 78.821 1.00 18.12 C ANISOU 1490 CB GLU A 201 2370 2389 2122 -31 99 57 C ATOM 1491 CG GLU A 201 14.079 42.736 78.837 1.00 21.36 C ANISOU 1491 CG GLU A 201 2841 2645 2628 -95 76 37 C ATOM 1492 CD GLU A 201 12.697 43.328 79.025 1.00 25.17 C ANISOU 1492 CD GLU A 201 3153 3138 3269 -86 100 -7 C ATOM 1493 OE1 GLU A 201 11.658 42.619 78.952 1.00 27.00 O ANISOU 1493 OE1 GLU A 201 3333 3559 3364 -165 -12 -86 O ATOM 1494 OE2 GLU A 201 12.642 44.539 79.252 1.00 27.80 O ANISOU 1494 OE2 GLU A 201 3350 3457 3753 -227 131 -131 O ATOM 1495 N ALA A 202 15.933 38.312 78.041 1.00 16.78 N ANISOU 1495 N ALA A 202 2253 1993 2127 -82 49 133 N ATOM 1496 CA ALA A 202 15.900 36.856 78.221 1.00 16.84 C ANISOU 1496 CA ALA A 202 2224 1995 2177 -52 8 101 C ATOM 1497 C ALA A 202 16.846 36.473 79.341 1.00 17.20 C ANISOU 1497 C ALA A 202 2264 2027 2244 -24 -8 114 C ATOM 1498 O ALA A 202 17.697 37.270 79.735 1.00 17.16 O ANISOU 1498 O ALA A 202 2272 2006 2241 4 -32 239 O ATOM 1499 CB ALA A 202 16.252 36.107 76.917 1.00 17.03 C ANISOU 1499 CB ALA A 202 2289 1996 2183 -64 25 83 C ATOM 1500 N LYS A 203 16.683 35.261 79.872 1.00 17.80 N ANISOU 1500 N LYS A 203 2321 2138 2303 -36 17 137 N ATOM 1501 CA LYS A 203 17.513 34.809 80.980 1.00 18.16 C ANISOU 1501 CA LYS A 203 2390 2169 2341 1 -8 50 C ATOM 1502 C LYS A 203 18.976 34.814 80.575 1.00 18.06 C ANISOU 1502 C LYS A 203 2414 2166 2280 -4 -9 40 C ATOM 1503 O LYS A 203 19.836 35.268 81.322 1.00 19.19 O ANISOU 1503 O LYS A 203 2636 2271 2384 79 -56 50 O ATOM 1504 CB LYS A 203 17.072 33.404 81.457 1.00 18.52 C ANISOU 1504 CB LYS A 203 2415 2249 2370 -38 17 132 C ATOM 1505 N ASN A 204 19.250 34.318 79.374 1.00 17.33 N ANISOU 1505 N ASN A 204 2361 2071 2151 47 -13 4 N ATOM 1506 CA ASN A 204 20.572 34.399 78.788 1.00 16.44 C ANISOU 1506 CA ASN A 204 2222 1982 2040 38 -24 2 C ATOM 1507 C ASN A 204 20.504 35.089 77.421 1.00 15.44 C ANISOU 1507 C ASN A 204 2093 1847 1925 5 14 -14 C ATOM 1508 O ASN A 204 20.311 34.438 76.379 1.00 14.61 O ANISOU 1508 O ASN A 204 2059 1617 1873 34 -2 -97 O ATOM 1509 CB ASN A 204 21.165 33.008 78.643 1.00 17.19 C ANISOU 1509 CB ASN A 204 2355 2098 2079 115 -39 25 C ATOM 1510 CG ASN A 204 22.543 33.015 78.001 1.00 18.28 C ANISOU 1510 CG ASN A 204 2422 2309 2215 19 -106 50 C ATOM 1511 OD1 ASN A 204 23.124 34.058 77.693 1.00 20.92 O ANISOU 1511 OD1 ASN A 204 2832 2743 2372 120 -234 218 O ATOM 1512 ND2 ASN A 204 23.072 31.827 77.788 1.00 22.02 N ANISOU 1512 ND2 ASN A 204 3120 2622 2623 171 -94 94 N ATOM 1513 N PRO A 205 20.618 36.414 77.419 1.00 14.74 N ANISOU 1513 N PRO A 205 1986 1769 1842 -26 5 -52 N ATOM 1514 CA PRO A 205 20.470 37.148 76.168 1.00 13.70 C ANISOU 1514 CA PRO A 205 1851 1576 1777 -50 -26 17 C ATOM 1515 C PRO A 205 21.401 36.664 75.061 1.00 13.27 C ANISOU 1515 C PRO A 205 1835 1454 1751 -113 -44 96 C ATOM 1516 O PRO A 205 20.944 36.491 73.931 1.00 13.11 O ANISOU 1516 O PRO A 205 1914 1422 1644 -152 -95 159 O ATOM 1517 CB PRO A 205 20.762 38.597 76.587 1.00 14.25 C ANISOU 1517 CB PRO A 205 1896 1656 1860 -28 -43 -17 C ATOM 1518 CG PRO A 205 20.425 38.619 78.013 1.00 14.95 C ANISOU 1518 CG PRO A 205 1923 1889 1868 5 -12 -40 C ATOM 1519 CD PRO A 205 20.871 37.324 78.555 1.00 14.61 C ANISOU 1519 CD PRO A 205 1978 1775 1798 -56 13 -41 C ATOM 1520 N ALA A 206 22.663 36.385 75.371 1.00 12.93 N ANISOU 1520 N ALA A 206 1804 1388 1718 -66 25 93 N ATOM 1521 CA ALA A 206 23.574 35.916 74.347 1.00 13.09 C ANISOU 1521 CA ALA A 206 1860 1396 1715 -44 -9 49 C ATOM 1522 C ALA A 206 23.120 34.568 73.735 1.00 13.45 C ANISOU 1522 C ALA A 206 1871 1545 1692 -88 -25 5 C ATOM 1523 O ALA A 206 23.209 34.370 72.524 1.00 12.94 O ANISOU 1523 O ALA A 206 1919 1321 1675 -149 -90 0 O ATOM 1524 CB ALA A 206 24.998 35.857 74.899 1.00 13.16 C ANISOU 1524 CB ALA A 206 1810 1469 1721 -10 50 -32 C ATOM 1525 N GLY A 207 22.629 33.669 74.588 1.00 13.16 N ANISOU 1525 N GLY A 207 1885 1409 1705 -82 -84 15 N ATOM 1526 CA GLY A 207 22.139 32.360 74.157 1.00 13.52 C ANISOU 1526 CA GLY A 207 1920 1474 1740 -68 -66 45 C ATOM 1527 C GLY A 207 20.893 32.531 73.298 1.00 13.26 C ANISOU 1527 C GLY A 207 1879 1425 1733 -32 -74 57 C ATOM 1528 O GLY A 207 20.772 31.893 72.260 1.00 12.89 O ANISOU 1528 O GLY A 207 2030 1174 1694 13 -74 74 O ATOM 1529 N ALA A 208 19.999 33.444 73.695 1.00 12.63 N ANISOU 1529 N ALA A 208 1784 1316 1697 -81 -83 1 N ATOM 1530 CA ALA A 208 18.768 33.689 72.938 1.00 12.87 C ANISOU 1530 CA ALA A 208 1773 1427 1690 -38 -35 57 C ATOM 1531 C ALA A 208 19.079 34.302 71.580 1.00 12.67 C ANISOU 1531 C ALA A 208 1740 1448 1625 -32 -114 22 C ATOM 1532 O ALA A 208 18.510 33.891 70.571 1.00 13.95 O ANISOU 1532 O ALA A 208 1980 1567 1751 -87 -164 -11 O ATOM 1533 CB ALA A 208 17.803 34.525 73.734 1.00 12.72 C ANISOU 1533 CB ALA A 208 1831 1291 1710 3 -9 86 C ATOM 1534 N ALA A 209 20.044 35.214 71.551 1.00 12.03 N ANISOU 1534 N ALA A 209 1639 1354 1578 40 -49 60 N ATOM 1535 CA ALA A 209 20.504 35.818 70.306 1.00 11.93 C ANISOU 1535 CA ALA A 209 1610 1411 1510 36 -77 10 C ATOM 1536 C ALA A 209 21.096 34.763 69.378 1.00 12.37 C ANISOU 1536 C ALA A 209 1772 1388 1537 101 -91 -8 C ATOM 1537 O ALA A 209 20.748 34.707 68.195 1.00 12.37 O ANISOU 1537 O ALA A 209 1975 1251 1472 151 -87 51 O ATOM 1538 CB ALA A 209 21.526 36.947 70.572 1.00 10.73 C ANISOU 1538 CB ALA A 209 1520 1157 1398 12 -34 52 C ATOM 1539 N ARG A 210 21.966 33.903 69.918 1.00 11.98 N ANISOU 1539 N ARG A 210 1727 1373 1451 113 -71 -50 N ATOM 1540 CA ARG A 210 22.553 32.855 69.087 1.00 12.47 C ANISOU 1540 CA ARG A 210 1708 1450 1579 127 -84 25 C ATOM 1541 C ARG A 210 21.504 31.873 68.562 1.00 12.71 C ANISOU 1541 C ARG A 210 1774 1494 1560 102 -103 28 C ATOM 1542 O ARG A 210 21.631 31.412 67.430 1.00 13.42 O ANISOU 1542 O ARG A 210 1927 1562 1607 191 -224 54 O ATOM 1543 CB ARG A 210 23.646 32.111 69.844 1.00 12.42 C ANISOU 1543 CB ARG A 210 1761 1470 1486 139 -90 17 C ATOM 1544 CG ARG A 210 24.437 31.200 68.958 1.00 13.59 C ANISOU 1544 CG ARG A 210 1824 1633 1705 188 -85 18 C ATOM 1545 CD ARG A 210 25.435 30.398 69.757 1.00 14.65 C ANISOU 1545 CD ARG A 210 2056 1706 1803 301 -166 22 C ATOM 1546 NE ARG A 210 26.475 31.296 70.244 1.00 15.08 N ANISOU 1546 NE ARG A 210 2161 1659 1907 121 -191 73 N ATOM 1547 CZ ARG A 210 27.414 30.951 71.121 1.00 17.11 C ANISOU 1547 CZ ARG A 210 2323 1950 2229 33 -98 98 C ATOM 1548 NH1 ARG A 210 27.475 29.709 71.579 1.00 15.08 N ANISOU 1548 NH1 ARG A 210 2257 1491 1979 122 -204 126 N ATOM 1549 NH2 ARG A 210 28.305 31.825 71.517 1.00 17.65 N ANISOU 1549 NH2 ARG A 210 2304 2268 2133 49 -218 -6 N ATOM 1550 N ALA A 211 20.500 31.532 69.374 1.00 13.11 N ANISOU 1550 N ALA A 211 1746 1550 1686 21 -102 24 N ATOM 1551 CA ALA A 211 19.451 30.587 68.936 1.00 13.63 C ANISOU 1551 CA ALA A 211 1844 1549 1782 -40 -74 -23 C ATOM 1552 C ALA A 211 18.647 31.186 67.786 1.00 14.17 C ANISOU 1552 C ALA A 211 1920 1619 1842 -71 -72 -41 C ATOM 1553 O ALA A 211 18.277 30.490 66.850 1.00 14.37 O ANISOU 1553 O ALA A 211 2003 1528 1926 -148 -88 -123 O ATOM 1554 CB ALA A 211 18.550 30.233 70.069 1.00 13.79 C ANISOU 1554 CB ALA A 211 1878 1545 1815 -71 -126 -15 C ATOM 1555 N PHE A 212 18.422 32.502 67.850 1.00 14.04 N ANISOU 1555 N PHE A 212 1854 1592 1888 -70 -52 21 N ATOM 1556 CA PHE A 212 17.677 33.209 66.826 1.00 14.21 C ANISOU 1556 CA PHE A 212 1893 1631 1875 -24 -38 6 C ATOM 1557 C PHE A 212 18.480 33.157 65.516 1.00 14.57 C ANISOU 1557 C PHE A 212 1897 1727 1912 -37 -39 26 C ATOM 1558 O PHE A 212 17.937 32.810 64.460 1.00 14.78 O ANISOU 1558 O PHE A 212 2008 1714 1894 -113 -82 11 O ATOM 1559 CB PHE A 212 17.456 34.655 67.301 1.00 14.12 C ANISOU 1559 CB PHE A 212 1859 1589 1914 -19 -33 12 C ATOM 1560 CG PHE A 212 16.400 35.422 66.545 1.00 14.36 C ANISOU 1560 CG PHE A 212 1868 1651 1934 -23 -11 29 C ATOM 1561 CD1 PHE A 212 15.200 35.748 67.158 1.00 16.10 C ANISOU 1561 CD1 PHE A 212 2057 1772 2287 127 -88 125 C ATOM 1562 CD2 PHE A 212 16.655 35.918 65.280 1.00 15.36 C ANISOU 1562 CD2 PHE A 212 2009 1759 2067 3 -174 26 C ATOM 1563 CE1 PHE A 212 14.238 36.499 66.476 1.00 17.24 C ANISOU 1563 CE1 PHE A 212 1994 2294 2261 61 -75 69 C ATOM 1564 CE2 PHE A 212 15.692 36.668 64.595 1.00 16.45 C ANISOU 1564 CE2 PHE A 212 2037 2103 2108 90 -107 75 C ATOM 1565 CZ PHE A 212 14.485 36.959 65.212 1.00 16.20 C ANISOU 1565 CZ PHE A 212 1957 2052 2145 -13 7 55 C ATOM 1566 N LYS A 213 19.786 33.433 65.597 1.00 14.62 N ANISOU 1566 N LYS A 213 1882 1768 1904 -30 -38 11 N ATOM 1567 CA LYS A 213 20.639 33.406 64.418 1.00 15.27 C ANISOU 1567 CA LYS A 213 1960 1885 1957 -52 -62 -24 C ATOM 1568 C LYS A 213 20.791 31.960 63.875 1.00 14.60 C ANISOU 1568 C LYS A 213 1894 1784 1867 -20 -43 -14 C ATOM 1569 O LYS A 213 20.865 31.761 62.641 1.00 14.83 O ANISOU 1569 O LYS A 213 1974 1743 1917 -57 -89 -79 O ATOM 1570 CB LYS A 213 21.989 34.086 64.724 1.00 15.16 C ANISOU 1570 CB LYS A 213 1962 1844 1952 -28 -72 38 C ATOM 1571 CG LYS A 213 22.915 34.224 63.551 1.00 18.38 C ANISOU 1571 CG LYS A 213 2332 2343 2309 -36 -100 27 C ATOM 1572 CD LYS A 213 22.577 35.447 62.704 1.00 20.55 C ANISOU 1572 CD LYS A 213 2628 2536 2644 42 -70 96 C ATOM 1573 CE LYS A 213 23.187 35.329 61.322 1.00 20.92 C ANISOU 1573 CE LYS A 213 2680 2665 2604 88 -47 163 C ATOM 1574 NZ LYS A 213 22.735 36.427 60.420 1.00 19.79 N ANISOU 1574 NZ LYS A 213 2459 2547 2513 309 -247 38 N ATOM 1575 N ASP A 214 20.807 30.960 64.774 1.00 14.15 N ANISOU 1575 N ASP A 214 1867 1676 1830 -26 -53 -126 N ATOM 1576 CA ASP A 214 20.868 29.550 64.371 1.00 14.34 C ANISOU 1576 CA ASP A 214 1900 1673 1875 -4 -31 -68 C ATOM 1577 C ASP A 214 19.650 29.200 63.483 1.00 13.86 C ANISOU 1577 C ASP A 214 1854 1614 1797 -15 -25 -57 C ATOM 1578 O ASP A 214 19.762 28.474 62.490 1.00 13.95 O ANISOU 1578 O ASP A 214 1894 1537 1868 -8 -93 -69 O ATOM 1579 CB ASP A 214 20.866 28.609 65.594 1.00 14.41 C ANISOU 1579 CB ASP A 214 1966 1606 1903 -17 -89 -99 C ATOM 1580 CG ASP A 214 22.185 28.552 66.341 1.00 16.98 C ANISOU 1580 CG ASP A 214 2226 1946 2277 7 -52 -44 C ATOM 1581 OD1 ASP A 214 23.232 28.971 65.821 1.00 19.85 O ANISOU 1581 OD1 ASP A 214 2206 2591 2745 36 -23 -70 O ATOM 1582 OD2 ASP A 214 22.197 28.053 67.495 1.00 19.73 O ANISOU 1582 OD2 ASP A 214 2852 2091 2553 187 -424 41 O ATOM 1583 N GLU A 215 18.482 29.704 63.855 1.00 13.60 N ANISOU 1583 N GLU A 215 1833 1505 1829 5 -54 -49 N ATOM 1584 CA GLU A 215 17.253 29.423 63.129 1.00 13.77 C ANISOU 1584 CA GLU A 215 1858 1538 1833 -40 -61 -43 C ATOM 1585 C GLU A 215 17.208 30.163 61.787 1.00 13.88 C ANISOU 1585 C GLU A 215 1877 1563 1833 -70 -118 -33 C ATOM 1586 O GLU A 215 16.724 29.623 60.790 1.00 13.92 O ANISOU 1586 O GLU A 215 1969 1406 1912 -163 -216 -71 O ATOM 1587 CB GLU A 215 16.036 29.746 63.996 1.00 13.99 C ANISOU 1587 CB GLU A 215 1872 1611 1832 -30 -34 -41 C ATOM 1588 CG GLU A 215 14.701 29.523 63.321 1.00 14.58 C ANISOU 1588 CG GLU A 215 1868 1630 2041 -44 42 -24 C ATOM 1589 CD GLU A 215 14.355 28.037 63.129 1.00 17.06 C ANISOU 1589 CD GLU A 215 2201 1900 2380 -38 -24 -32 C ATOM 1590 OE1 GLU A 215 15.229 27.162 63.367 1.00 18.50 O ANISOU 1590 OE1 GLU A 215 2308 2046 2672 29 -236 116 O ATOM 1591 OE2 GLU A 215 13.197 27.754 62.726 1.00 16.98 O ANISOU 1591 OE2 GLU A 215 2197 1822 2434 -23 -118 81 O ATOM 1592 N ILE A 216 17.693 31.407 61.765 1.00 13.38 N ANISOU 1592 N ILE A 216 1835 1474 1774 -77 -153 -9 N ATOM 1593 CA ILE A 216 17.907 32.103 60.498 1.00 13.25 C ANISOU 1593 CA ILE A 216 1788 1538 1708 -31 -94 -31 C ATOM 1594 C ILE A 216 18.787 31.233 59.580 1.00 13.87 C ANISOU 1594 C ILE A 216 1915 1589 1763 -16 -56 -44 C ATOM 1595 O ILE A 216 18.456 31.030 58.436 1.00 13.76 O ANISOU 1595 O ILE A 216 2034 1443 1752 -55 -101 -24 O ATOM 1596 CB ILE A 216 18.572 33.487 60.707 1.00 12.77 C ANISOU 1596 CB ILE A 216 1702 1478 1668 -41 -106 24 C ATOM 1597 CG1 ILE A 216 17.596 34.455 61.378 1.00 12.73 C ANISOU 1597 CG1 ILE A 216 1703 1515 1618 -145 -50 -34 C ATOM 1598 CG2 ILE A 216 19.073 34.032 59.381 1.00 12.95 C ANISOU 1598 CG2 ILE A 216 1716 1569 1633 -58 -77 -41 C ATOM 1599 CD1 ILE A 216 18.269 35.803 61.795 1.00 12.31 C ANISOU 1599 CD1 ILE A 216 1279 1587 1808 -220 -60 -3 C ATOM 1600 N LYS A 217 19.889 30.707 60.114 1.00 14.39 N ANISOU 1600 N LYS A 217 1944 1670 1851 34 -37 -99 N ATOM 1601 CA LYS A 217 20.783 29.821 59.346 1.00 15.44 C ANISOU 1601 CA LYS A 217 2076 1791 1998 38 18 -88 C ATOM 1602 C LYS A 217 20.069 28.554 58.871 1.00 15.47 C ANISOU 1602 C LYS A 217 2114 1820 1944 10 21 -94 C ATOM 1603 O LYS A 217 20.300 28.087 57.744 1.00 15.94 O ANISOU 1603 O LYS A 217 2357 1798 1900 59 80 -94 O ATOM 1604 CB LYS A 217 22.008 29.438 60.179 1.00 16.64 C ANISOU 1604 CB LYS A 217 2151 1969 2203 8 5 -71 C ATOM 1605 CG LYS A 217 23.126 28.751 59.399 1.00 19.71 C ANISOU 1605 CG LYS A 217 2593 2327 2566 29 73 -163 C ATOM 1606 CD LYS A 217 24.434 28.871 60.166 1.00 25.85 C ANISOU 1606 CD LYS A 217 3184 3293 3344 91 3 -51 C ATOM 1607 CE LYS A 217 25.477 27.857 59.713 1.00 29.24 C ANISOU 1607 CE LYS A 217 3577 3726 3803 84 -14 -49 C ATOM 1608 NZ LYS A 217 26.759 28.075 60.471 1.00 31.01 N ANISOU 1608 NZ LYS A 217 3801 3984 3995 37 -177 -49 N ATOM 1609 N ARG A 218 19.229 27.959 59.715 1.00 14.84 N ANISOU 1609 N ARG A 218 2024 1704 1910 13 27 -117 N ATOM 1610 CA ARG A 218 18.497 26.747 59.274 1.00 15.12 C ANISOU 1610 CA ARG A 218 2017 1744 1984 2 -50 -143 C ATOM 1611 C ARG A 218 17.570 27.025 58.083 1.00 15.10 C ANISOU 1611 C ARG A 218 2024 1753 1960 25 -43 -126 C ATOM 1612 O ARG A 218 17.507 26.241 57.115 1.00 14.88 O ANISOU 1612 O ARG A 218 2044 1704 1904 -25 -88 -192 O ATOM 1613 CB ARG A 218 17.686 26.161 60.423 1.00 14.69 C ANISOU 1613 CB ARG A 218 1929 1618 2032 42 -34 -127 C ATOM 1614 CG ARG A 218 17.066 24.777 60.141 1.00 16.84 C ANISOU 1614 CG ARG A 218 2161 1930 2305 -135 6 -123 C ATOM 1615 CD ARG A 218 16.069 24.343 61.192 1.00 17.24 C ANISOU 1615 CD ARG A 218 2219 1989 2341 -160 -11 -74 C ATOM 1616 NE ARG A 218 14.839 25.143 61.237 1.00 17.93 N ANISOU 1616 NE ARG A 218 2396 2013 2404 -202 -23 -73 N ATOM 1617 CZ ARG A 218 13.836 25.055 60.360 1.00 18.48 C ANISOU 1617 CZ ARG A 218 2386 2079 2556 -93 0 21 C ATOM 1618 NH1 ARG A 218 13.891 24.208 59.320 1.00 17.93 N ANISOU 1618 NH1 ARG A 218 2411 2060 2340 -173 51 -54 N ATOM 1619 NH2 ARG A 218 12.753 25.810 60.523 1.00 18.82 N ANISOU 1619 NH2 ARG A 218 2466 1884 2801 -234 68 -45 N ATOM 1620 N ILE A 219 16.828 28.122 58.161 1.00 14.97 N ANISOU 1620 N ILE A 219 2030 1757 1898 66 -49 -181 N ATOM 1621 CA ILE A 219 15.794 28.436 57.172 1.00 14.52 C ANISOU 1621 CA ILE A 219 1943 1684 1889 27 -59 -176 C ATOM 1622 C ILE A 219 16.379 29.000 55.885 1.00 14.49 C ANISOU 1622 C ILE A 219 1933 1653 1916 57 -79 -134 C ATOM 1623 O ILE A 219 16.000 28.575 54.802 1.00 14.97 O ANISOU 1623 O ILE A 219 1998 1674 2014 2 -218 -187 O ATOM 1624 CB ILE A 219 14.746 29.406 57.744 1.00 14.55 C ANISOU 1624 CB ILE A 219 1873 1785 1868 43 1 -141 C ATOM 1625 CG1 ILE A 219 14.023 28.760 58.933 1.00 14.07 C ANISOU 1625 CG1 ILE A 219 1908 1565 1871 -181 -28 -164 C ATOM 1626 CG2 ILE A 219 13.781 29.872 56.659 1.00 14.83 C ANISOU 1626 CG2 ILE A 219 2153 1554 1924 5 -79 -208 C ATOM 1627 CD1 ILE A 219 13.214 29.760 59.768 1.00 14.92 C ANISOU 1627 CD1 ILE A 219 1843 1842 1983 -78 47 -124 C ATOM 1628 N TRP A 220 17.315 29.933 55.990 1.00 14.23 N ANISOU 1628 N TRP A 220 1925 1601 1880 9 -84 -148 N ATOM 1629 CA TRP A 220 17.864 30.615 54.828 1.00 14.42 C ANISOU 1629 CA TRP A 220 1935 1641 1901 -5 -41 -122 C ATOM 1630 C TRP A 220 19.238 30.129 54.379 1.00 14.76 C ANISOU 1630 C TRP A 220 1999 1659 1951 -45 -16 -140 C ATOM 1631 O TRP A 220 19.691 30.535 53.317 1.00 15.49 O ANISOU 1631 O TRP A 220 2200 1641 2043 -48 -4 -203 O ATOM 1632 CB TRP A 220 17.911 32.153 55.078 1.00 13.79 C ANISOU 1632 CB TRP A 220 1841 1511 1886 -79 -66 -74 C ATOM 1633 CG TRP A 220 16.562 32.832 55.034 1.00 13.71 C ANISOU 1633 CG TRP A 220 1867 1525 1815 -119 -54 -126 C ATOM 1634 CD1 TRP A 220 15.967 33.410 53.942 1.00 12.35 C ANISOU 1634 CD1 TRP A 220 1761 1070 1860 -157 -36 -134 C ATOM 1635 CD2 TRP A 220 15.656 33.015 56.121 1.00 12.39 C ANISOU 1635 CD2 TRP A 220 1859 1179 1669 -107 -28 -74 C ATOM 1636 NE1 TRP A 220 14.734 33.917 54.287 1.00 12.81 N ANISOU 1636 NE1 TRP A 220 1917 1282 1666 -186 -114 -118 N ATOM 1637 CE2 TRP A 220 14.513 33.670 55.617 1.00 11.85 C ANISOU 1637 CE2 TRP A 220 1762 1092 1647 -226 -50 -84 C ATOM 1638 CE3 TRP A 220 15.684 32.680 57.479 1.00 12.65 C ANISOU 1638 CE3 TRP A 220 1841 1239 1725 -109 23 -72 C ATOM 1639 CZ2 TRP A 220 13.436 34.019 56.426 1.00 11.81 C ANISOU 1639 CZ2 TRP A 220 1646 1238 1603 -122 -95 -92 C ATOM 1640 CZ3 TRP A 220 14.603 33.033 58.274 1.00 12.71 C ANISOU 1640 CZ3 TRP A 220 1874 1217 1736 -62 -120 -191 C ATOM 1641 CH2 TRP A 220 13.488 33.659 57.739 1.00 13.63 C ANISOU 1641 CH2 TRP A 220 1874 1426 1878 42 -93 -62 C ATOM 1642 N GLY A 221 19.887 29.265 55.163 1.00 15.59 N ANISOU 1642 N GLY A 221 2053 1811 2056 -60 5 -92 N ATOM 1643 CA GLY A 221 21.234 28.754 54.832 1.00 16.22 C ANISOU 1643 CA GLY A 221 2114 1900 2147 -18 -21 -73 C ATOM 1644 C GLY A 221 21.291 27.821 53.637 1.00 17.21 C ANISOU 1644 C GLY A 221 2267 1979 2291 -12 -74 -46 C ATOM 1645 O GLY A 221 20.251 27.261 53.258 1.00 18.16 O ANISOU 1645 O GLY A 221 2330 2101 2469 63 -27 -56 O TER 1646 GLY A 221 ATOM 3688 N GLN A 4 -5.495 86.711 73.677 1.00 29.58 N ANISOU 3688 N GLN B 4 3666 3784 3787 3 3 23 N ATOM 3689 CA GLN A 4 -4.016 86.608 73.525 1.00 29.26 C ANISOU 3689 CA GLN B 4 3645 3721 3750 15 11 -7 C ATOM 3690 C GLN A 4 -3.578 86.910 72.106 1.00 28.99 C ANISOU 3690 C GLN B 4 3627 3664 3723 4 -9 -11 C ATOM 3691 O GLN A 4 -4.266 86.573 71.140 1.00 29.73 O ANISOU 3691 O GLN B 4 3695 3796 3802 6 -35 -11 O ATOM 3692 N LEU A 5 -2.423 87.551 71.978 1.00 28.03 N ANISOU 3692 N LEU B 5 3536 3481 3630 33 -2 -44 N ATOM 3693 CA LEU A 5 -1.817 87.809 70.679 1.00 26.86 C ANISOU 3693 CA LEU B 5 3420 3288 3497 68 11 -70 C ATOM 3694 C LEU A 5 -1.124 86.517 70.219 1.00 24.95 C ANISOU 3694 C LEU B 5 3187 3046 3248 104 17 -60 C ATOM 3695 O LEU A 5 -0.893 85.630 71.033 1.00 25.15 O ANISOU 3695 O LEU B 5 3262 2989 3303 168 39 -112 O ATOM 3696 CB LEU A 5 -0.788 88.937 70.797 1.00 27.56 C ANISOU 3696 CB LEU B 5 3458 3408 3604 54 11 -53 C ATOM 3697 CG LEU A 5 -1.276 90.284 71.344 1.00 29.54 C ANISOU 3697 CG LEU B 5 3744 3670 3806 25 13 -68 C ATOM 3698 CD1 LEU A 5 -0.114 91.248 71.438 1.00 31.55 C ANISOU 3698 CD1 LEU B 5 4020 3897 4071 -44 22 -21 C ATOM 3699 CD2 LEU A 5 -2.392 90.847 70.488 1.00 31.20 C ANISOU 3699 CD2 LEU B 5 4000 3918 3935 61 -19 11 C ATOM 3700 N PRO A 6 -0.783 86.414 68.935 1.00 22.86 N ANISOU 3700 N PRO B 6 2930 2726 3028 127 -18 -63 N ATOM 3701 CA PRO A 6 0.081 85.307 68.497 1.00 21.35 C ANISOU 3701 CA PRO B 6 2738 2504 2867 139 -34 -22 C ATOM 3702 C PRO A 6 1.367 85.250 69.310 1.00 20.12 C ANISOU 3702 C PRO B 6 2616 2297 2732 93 -84 -1 C ATOM 3703 O PRO A 6 2.008 86.271 69.537 1.00 19.92 O ANISOU 3703 O PRO B 6 2602 2090 2875 148 -134 42 O ATOM 3704 CB PRO A 6 0.421 85.677 67.052 1.00 21.22 C ANISOU 3704 CB PRO B 6 2707 2525 2828 119 -54 9 C ATOM 3705 CG PRO A 6 -0.766 86.508 66.585 1.00 21.56 C ANISOU 3705 CG PRO B 6 2767 2521 2904 153 16 8 C ATOM 3706 CD PRO A 6 -1.156 87.286 67.808 1.00 22.65 C ANISOU 3706 CD PRO B 6 2889 2777 2937 96 -28 -57 C ATOM 3707 N ASN A 7 1.752 84.045 69.735 1.00 18.75 N ANISOU 3707 N ASN B 7 2412 2139 2573 97 -87 -29 N ATOM 3708 CA ASN A 7 3.012 83.833 70.434 1.00 17.57 C ANISOU 3708 CA ASN B 7 2201 2105 2369 52 -27 -36 C ATOM 3709 C ASN A 7 4.215 84.027 69.504 1.00 17.18 C ANISOU 3709 C ASN B 7 2185 2039 2303 73 -46 -22 C ATOM 3710 O ASN A 7 4.146 83.690 68.322 1.00 16.73 O ANISOU 3710 O ASN B 7 2155 1932 2270 144 -59 0 O ATOM 3711 CB ASN A 7 3.082 82.402 70.958 1.00 17.76 C ANISOU 3711 CB ASN B 7 2192 2130 2425 78 -33 -29 C ATOM 3712 CG ASN A 7 2.063 82.087 72.046 1.00 17.79 C ANISOU 3712 CG ASN B 7 2163 2136 2459 57 10 -97 C ATOM 3713 OD1 ASN A 7 1.464 81.007 72.053 1.00 19.19 O ANISOU 3713 OD1 ASN B 7 2267 2228 2793 96 -185 -166 O ATOM 3714 ND2 ASN A 7 1.924 82.977 73.008 1.00 17.64 N ANISOU 3714 ND2 ASN B 7 2145 2036 2519 299 78 -237 N ATOM 3715 N LEU A 8 5.311 84.541 70.064 1.00 15.74 N ANISOU 3715 N LEU B 8 1990 1752 2237 62 -7 -74 N ATOM 3716 CA LEU A 8 6.626 84.445 69.449 1.00 15.86 C ANISOU 3716 CA LEU B 8 2023 1824 2179 59 -62 -22 C ATOM 3717 C LEU A 8 7.360 83.263 70.077 1.00 15.36 C ANISOU 3717 C LEU B 8 1975 1736 2123 156 -70 -47 C ATOM 3718 O LEU A 8 7.517 83.216 71.281 1.00 15.38 O ANISOU 3718 O LEU B 8 1970 1622 2250 331 -136 -37 O ATOM 3719 CB LEU A 8 7.443 85.714 69.687 1.00 15.21 C ANISOU 3719 CB LEU B 8 1958 1641 2177 71 -57 3 C ATOM 3720 CG LEU A 8 8.910 85.635 69.230 1.00 15.94 C ANISOU 3720 CG LEU B 8 2084 1748 2225 -63 -17 33 C ATOM 3721 CD1 LEU A 8 9.102 85.182 67.759 1.00 15.03 C ANISOU 3721 CD1 LEU B 8 2006 1589 2115 -99 84 170 C ATOM 3722 CD2 LEU A 8 9.657 86.959 69.516 1.00 17.47 C ANISOU 3722 CD2 LEU B 8 2250 1976 2411 -197 -26 63 C ATOM 3723 N GLN A 9 7.809 82.329 69.246 1.00 15.22 N ANISOU 3723 N GLN B 9 1970 1736 2075 94 -97 -14 N ATOM 3724 CA GLN A 9 8.532 81.148 69.688 1.00 15.15 C ANISOU 3724 CA GLN B 9 1925 1748 2082 104 -34 -22 C ATOM 3725 C GLN A 9 9.922 81.171 69.076 1.00 15.24 C ANISOU 3725 C GLN B 9 1962 1779 2047 59 -13 -9 C ATOM 3726 O GLN A 9 10.090 81.546 67.917 1.00 16.08 O ANISOU 3726 O GLN B 9 2148 1773 2188 175 35 36 O ATOM 3727 CB GLN A 9 7.778 79.900 69.210 1.00 14.24 C ANISOU 3727 CB GLN B 9 1845 1600 1962 71 -91 19 C ATOM 3728 CG GLN A 9 8.423 78.547 69.564 1.00 13.60 C ANISOU 3728 CG GLN B 9 1752 1461 1954 271 -49 -78 C ATOM 3729 CD GLN A 9 7.463 77.356 69.362 1.00 13.22 C ANISOU 3729 CD GLN B 9 1755 1552 1714 223 -100 47 C ATOM 3730 OE1 GLN A 9 6.260 77.436 69.644 1.00 13.67 O ANISOU 3730 OE1 GLN B 9 1981 1380 1832 226 -98 156 O ATOM 3731 NE2 GLN A 9 8.012 76.233 68.877 1.00 11.84 N ANISOU 3731 NE2 GLN B 9 1516 1422 1560 439 -99 -26 N ATOM 3732 N VAL A 10 10.912 80.752 69.845 1.00 15.39 N ANISOU 3732 N VAL B 10 2027 1733 2086 74 -2 -5 N ATOM 3733 CA VAL A 10 12.250 80.561 69.296 1.00 15.72 C ANISOU 3733 CA VAL B 10 1999 1845 2127 30 -5 6 C ATOM 3734 C VAL A 10 12.587 79.076 69.233 1.00 15.14 C ANISOU 3734 C VAL B 10 1869 1845 2038 34 12 -37 C ATOM 3735 O VAL A 10 12.449 78.368 70.220 1.00 14.72 O ANISOU 3735 O VAL B 10 1711 1724 2155 104 9 -43 O ATOM 3736 CB VAL A 10 13.341 81.332 70.100 1.00 16.27 C ANISOU 3736 CB VAL B 10 2114 1928 2139 33 -15 -41 C ATOM 3737 CG1 VAL A 10 13.390 80.865 71.572 1.00 17.87 C ANISOU 3737 CG1 VAL B 10 2412 2001 2374 7 -9 10 C ATOM 3738 CG2 VAL A 10 14.695 81.173 69.443 1.00 16.63 C ANISOU 3738 CG2 VAL B 10 2218 1802 2297 -87 -61 -68 C ATOM 3739 N ALA A 11 13.034 78.629 68.066 1.00 15.10 N ANISOU 3739 N ALA B 11 1900 1841 1994 28 -13 -22 N ATOM 3740 CA ALA A 11 13.468 77.249 67.848 1.00 14.57 C ANISOU 3740 CA ALA B 11 1839 1762 1932 -4 17 17 C ATOM 3741 C ALA A 11 14.987 77.165 68.021 1.00 14.05 C ANISOU 3741 C ALA B 11 1768 1670 1899 17 5 50 C ATOM 3742 O ALA A 11 15.749 77.954 67.425 1.00 14.84 O ANISOU 3742 O ALA B 11 1941 1556 2139 9 -3 176 O ATOM 3743 CB ALA A 11 13.058 76.782 66.479 1.00 14.99 C ANISOU 3743 CB ALA B 11 1865 1813 2017 -11 -5 -47 C ATOM 3744 N LEU A 12 15.417 76.219 68.850 1.00 11.82 N ANISOU 3744 N LEU B 12 1503 1328 1659 -45 -21 57 N ATOM 3745 CA LEU A 12 16.826 75.965 69.122 1.00 11.45 C ANISOU 3745 CA LEU B 12 1448 1381 1521 -23 -3 -15 C ATOM 3746 C LEU A 12 17.221 74.679 68.420 1.00 11.14 C ANISOU 3746 C LEU B 12 1398 1323 1509 -17 -47 -11 C ATOM 3747 O LEU A 12 16.968 73.580 68.934 1.00 10.74 O ANISOU 3747 O LEU B 12 1539 1134 1408 6 -103 -79 O ATOM 3748 CB LEU A 12 17.044 75.816 70.629 1.00 10.80 C ANISOU 3748 CB LEU B 12 1397 1198 1506 -22 -64 22 C ATOM 3749 CG LEU A 12 16.545 76.973 71.515 1.00 12.70 C ANISOU 3749 CG LEU B 12 1604 1643 1577 61 91 -99 C ATOM 3750 CD1 LEU A 12 16.562 76.590 72.979 1.00 13.16 C ANISOU 3750 CD1 LEU B 12 1797 1586 1617 38 -122 0 C ATOM 3751 CD2 LEU A 12 17.395 78.191 71.279 1.00 12.46 C ANISOU 3751 CD2 LEU B 12 1681 1488 1564 34 127 -97 C ATOM 3752 N ASP A 13 17.809 74.808 67.235 1.00 11.32 N ANISOU 3752 N ASP B 13 1490 1317 1493 32 -49 -21 N ATOM 3753 CA ASP A 13 18.129 73.649 66.383 1.00 12.03 C ANISOU 3753 CA ASP B 13 1522 1472 1576 2 -20 -39 C ATOM 3754 C ASP A 13 19.639 73.382 66.304 1.00 11.16 C ANISOU 3754 C ASP B 13 1488 1268 1483 93 -44 8 C ATOM 3755 O ASP A 13 20.129 72.748 65.373 1.00 12.66 O ANISOU 3755 O ASP B 13 1726 1472 1612 65 -50 -7 O ATOM 3756 CB ASP A 13 17.534 73.854 64.983 1.00 12.54 C ANISOU 3756 CB ASP B 13 1570 1553 1642 47 -2 -4 C ATOM 3757 CG ASP A 13 16.001 73.976 65.001 1.00 15.33 C ANISOU 3757 CG ASP B 13 1770 2077 1977 -84 31 33 C ATOM 3758 OD1 ASP A 13 15.331 73.148 65.652 1.00 16.42 O ANISOU 3758 OD1 ASP B 13 1896 2198 2143 -316 58 111 O ATOM 3759 OD2 ASP A 13 15.424 74.878 64.363 1.00 18.25 O ANISOU 3759 OD2 ASP B 13 2071 2412 2448 -91 221 235 O ATOM 3760 N HIS A 14 20.372 73.859 67.299 1.00 10.24 N ANISOU 3760 N HIS B 14 1405 1034 1451 63 -24 46 N ATOM 3761 CA HIS A 14 21.824 73.695 67.341 1.00 9.88 C ANISOU 3761 CA HIS B 14 1322 1077 1352 22 37 18 C ATOM 3762 C HIS A 14 22.285 72.235 67.506 1.00 10.11 C ANISOU 3762 C HIS B 14 1315 1110 1414 32 20 -15 C ATOM 3763 O HIS A 14 21.558 71.419 68.062 1.00 10.62 O ANISOU 3763 O HIS B 14 1361 1211 1460 51 43 15 O ATOM 3764 CB HIS A 14 22.364 74.504 68.492 1.00 10.52 C ANISOU 3764 CB HIS B 14 1385 1166 1446 47 69 61 C ATOM 3765 CG HIS A 14 21.860 75.907 68.510 1.00 10.19 C ANISOU 3765 CG HIS B 14 1492 1094 1285 -1 186 14 C ATOM 3766 ND1 HIS A 14 20.720 76.272 69.178 1.00 12.02 N ANISOU 3766 ND1 HIS B 14 1787 1041 1739 39 245 -158 N ATOM 3767 CD2 HIS A 14 22.296 77.016 67.867 1.00 12.59 C ANISOU 3767 CD2 HIS B 14 1997 1066 1718 -14 170 8 C ATOM 3768 CE1 HIS A 14 20.515 77.571 69.014 1.00 12.69 C ANISOU 3768 CE1 HIS B 14 1860 1266 1693 51 304 -75 C ATOM 3769 NE2 HIS A 14 21.449 78.040 68.215 1.00 11.03 N ANISOU 3769 NE2 HIS B 14 1871 1063 1257 65 199 -13 N ATOM 3770 N SER A 15 23.513 71.954 67.088 1.00 10.32 N ANISOU 3770 N SER B 15 1363 1088 1470 0 17 -62 N ATOM 3771 CA SER A 15 24.075 70.609 67.138 1.00 10.96 C ANISOU 3771 CA SER B 15 1426 1224 1512 64 14 -69 C ATOM 3772 C SER A 15 24.866 70.349 68.426 1.00 10.93 C ANISOU 3772 C SER B 15 1472 1161 1520 40 -62 -107 C ATOM 3773 O SER A 15 25.485 69.304 68.581 1.00 11.76 O ANISOU 3773 O SER B 15 1511 1227 1729 -28 -76 -74 O ATOM 3774 CB SER A 15 24.915 70.326 65.881 1.00 11.00 C ANISOU 3774 CB SER B 15 1400 1282 1496 128 -8 -92 C ATOM 3775 OG SER A 15 24.068 70.242 64.762 1.00 11.64 O ANISOU 3775 OG SER B 15 1723 1300 1400 268 102 -263 O ATOM 3776 N ASN A 16 24.870 71.325 69.337 1.00 10.65 N ANISOU 3776 N ASN B 16 1428 1149 1468 61 -9 -102 N ATOM 3777 CA ASN A 16 25.457 71.123 70.639 1.00 10.69 C ANISOU 3777 CA ASN B 16 1409 1196 1456 53 -38 -79 C ATOM 3778 C ASN A 16 24.714 71.880 71.745 1.00 10.46 C ANISOU 3778 C ASN B 16 1451 1114 1410 63 -75 -79 C ATOM 3779 O ASN A 16 23.879 72.757 71.492 1.00 11.20 O ANISOU 3779 O ASN B 16 1716 1069 1471 32 -133 -72 O ATOM 3780 CB ASN A 16 26.955 71.460 70.615 1.00 10.63 C ANISOU 3780 CB ASN B 16 1330 1151 1558 41 -22 -113 C ATOM 3781 CG ASN A 16 27.233 72.873 70.085 1.00 12.15 C ANISOU 3781 CG ASN B 16 1492 1429 1693 -66 65 40 C ATOM 3782 OD1 ASN A 16 26.556 73.825 70.436 1.00 12.58 O ANISOU 3782 OD1 ASN B 16 1640 1556 1581 -254 -123 -160 O ATOM 3783 ND2 ASN A 16 28.237 72.993 69.240 1.00 15.07 N ANISOU 3783 ND2 ASN B 16 1889 1739 2096 -84 290 2 N ATOM 3784 N LEU A 17 25.023 71.507 72.974 1.00 10.45 N ANISOU 3784 N LEU B 17 1490 1130 1349 87 -91 -35 N ATOM 3785 CA LEU A 17 24.363 72.044 74.133 1.00 11.36 C ANISOU 3785 CA LEU B 17 1475 1335 1503 39 9 23 C ATOM 3786 C LEU A 17 24.661 73.519 74.291 1.00 11.49 C ANISOU 3786 C LEU B 17 1500 1347 1518 38 -17 -89 C ATOM 3787 O LEU A 17 23.766 74.303 74.599 1.00 12.77 O ANISOU 3787 O LEU B 17 1524 1551 1775 56 -43 -116 O ATOM 3788 CB LEU A 17 24.811 71.292 75.379 1.00 12.09 C ANISOU 3788 CB LEU B 17 1542 1508 1545 22 -7 32 C ATOM 3789 CG LEU A 17 24.125 71.575 76.698 1.00 13.76 C ANISOU 3789 CG LEU B 17 1780 1742 1706 22 -11 87 C ATOM 3790 CD1 LEU A 17 22.635 71.285 76.606 1.00 14.17 C ANISOU 3790 CD1 LEU B 17 1709 1958 1717 -100 46 29 C ATOM 3791 CD2 LEU A 17 24.805 70.698 77.771 1.00 14.66 C ANISOU 3791 CD2 LEU B 17 2046 1902 1622 -32 35 137 C ATOM 3792 N LYS A 18 25.920 73.904 74.142 1.00 11.08 N ANISOU 3792 N LYS B 18 1453 1207 1548 21 -55 -126 N ATOM 3793 CA LYS A 18 26.274 75.301 74.383 1.00 11.49 C ANISOU 3793 CA LYS B 18 1556 1265 1544 19 -79 -98 C ATOM 3794 C LYS A 18 25.523 76.252 73.448 1.00 11.70 C ANISOU 3794 C LYS B 18 1539 1319 1587 -8 -87 -112 C ATOM 3795 O LYS A 18 25.085 77.316 73.875 1.00 12.09 O ANISOU 3795 O LYS B 18 1623 1199 1770 -13 -50 -98 O ATOM 3796 CB LYS A 18 27.784 75.515 74.315 1.00 11.49 C ANISOU 3796 CB LYS B 18 1573 1283 1506 -2 -116 -76 C ATOM 3797 CG LYS A 18 28.433 75.415 72.943 1.00 12.97 C ANISOU 3797 CG LYS B 18 1685 1506 1736 61 -20 -57 C ATOM 3798 CD LYS A 18 29.931 75.470 73.038 1.00 15.45 C ANISOU 3798 CD LYS B 18 1895 1963 2012 -53 -51 -11 C ATOM 3799 CE LYS A 18 30.567 75.542 71.668 1.00 16.98 C ANISOU 3799 CE LYS B 18 2186 2135 2130 -18 -22 135 C ATOM 3800 NZ LYS A 18 32.043 75.720 71.725 1.00 16.95 N ANISOU 3800 NZ LYS B 18 2291 1928 2220 -114 -112 133 N ATOM 3801 N GLY A 19 25.344 75.854 72.189 1.00 12.07 N ANISOU 3801 N GLY B 19 1545 1393 1647 -11 -14 -108 N ATOM 3802 CA GLY A 19 24.650 76.662 71.213 1.00 11.58 C ANISOU 3802 CA GLY B 19 1457 1339 1603 -14 -52 -73 C ATOM 3803 C GLY A 19 23.210 76.897 71.619 1.00 11.55 C ANISOU 3803 C GLY B 19 1455 1361 1571 16 -53 -67 C ATOM 3804 O GLY A 19 22.712 78.019 71.512 1.00 12.76 O ANISOU 3804 O GLY B 19 1652 1374 1822 14 -127 6 O ATOM 3805 N ALA A 20 22.523 75.843 72.043 1.00 11.27 N ANISOU 3805 N ALA B 20 1491 1273 1516 53 -57 2 N ATOM 3806 CA ALA A 20 21.120 75.950 72.451 1.00 10.74 C ANISOU 3806 CA ALA B 20 1447 1204 1428 67 32 -65 C ATOM 3807 C ALA A 20 20.957 76.831 73.716 1.00 11.18 C ANISOU 3807 C ALA B 20 1559 1252 1436 66 -20 -83 C ATOM 3808 O ALA A 20 20.087 77.711 73.785 1.00 10.72 O ANISOU 3808 O ALA B 20 1501 1142 1429 58 -29 -183 O ATOM 3809 CB ALA A 20 20.515 74.550 72.684 1.00 11.32 C ANISOU 3809 CB ALA B 20 1491 1197 1613 47 74 -24 C ATOM 3810 N ILE A 21 21.795 76.572 74.705 1.00 10.54 N ANISOU 3810 N ILE B 21 1432 1134 1437 84 2 -109 N ATOM 3811 CA ILE A 21 21.698 77.270 75.980 1.00 10.97 C ANISOU 3811 CA ILE B 21 1487 1203 1478 7 -51 -66 C ATOM 3812 C ILE A 21 22.009 78.760 75.759 1.00 11.55 C ANISOU 3812 C ILE B 21 1517 1254 1617 -24 -28 -48 C ATOM 3813 O ILE A 21 21.276 79.629 76.218 1.00 11.42 O ANISOU 3813 O ILE B 21 1535 1038 1767 -49 -20 -114 O ATOM 3814 CB ILE A 21 22.600 76.635 77.037 1.00 10.80 C ANISOU 3814 CB ILE B 21 1351 1299 1454 -1 0 -83 C ATOM 3815 CG1 ILE A 21 22.033 75.259 77.437 1.00 11.59 C ANISOU 3815 CG1 ILE B 21 1563 1320 1521 -88 -147 -111 C ATOM 3816 CG2 ILE A 21 22.702 77.562 78.285 1.00 12.40 C ANISOU 3816 CG2 ILE B 21 1621 1502 1587 41 -117 -170 C ATOM 3817 CD1 ILE A 21 22.908 74.465 78.370 1.00 13.18 C ANISOU 3817 CD1 ILE B 21 1648 1335 2023 -319 -29 -112 C ATOM 3818 N THR A 22 23.067 79.031 75.013 1.00 11.93 N ANISOU 3818 N THR B 22 1595 1219 1717 -70 -2 -51 N ATOM 3819 CA THR A 22 23.465 80.424 74.755 1.00 12.62 C ANISOU 3819 CA THR B 22 1700 1293 1801 -61 -58 -91 C ATOM 3820 C THR A 22 22.386 81.196 74.001 1.00 12.78 C ANISOU 3820 C THR B 22 1647 1374 1835 -30 -86 -129 C ATOM 3821 O THR A 22 22.037 82.320 74.375 1.00 13.61 O ANISOU 3821 O THR B 22 1728 1390 2050 24 -163 -193 O ATOM 3822 CB THR A 22 24.804 80.457 74.051 1.00 12.81 C ANISOU 3822 CB THR B 22 1692 1312 1861 -25 -54 -46 C ATOM 3823 OG1 THR A 22 25.773 79.876 74.933 1.00 14.54 O ANISOU 3823 OG1 THR B 22 1910 1558 2054 -105 -169 -14 O ATOM 3824 CG2 THR A 22 25.260 81.902 73.704 1.00 13.46 C ANISOU 3824 CG2 THR B 22 1778 1422 1911 -92 -6 -155 C ATOM 3825 N ALA A 23 21.845 80.594 72.937 1.00 12.20 N ANISOU 3825 N ALA B 23 1587 1318 1730 48 -122 -114 N ATOM 3826 CA ALA A 23 20.742 81.184 72.187 1.00 12.03 C ANISOU 3826 CA ALA B 23 1586 1305 1679 -1 -35 0 C ATOM 3827 C ALA A 23 19.500 81.419 73.055 1.00 12.12 C ANISOU 3827 C ALA B 23 1587 1242 1776 42 -39 -17 C ATOM 3828 O ALA A 23 18.890 82.488 72.997 1.00 13.35 O ANISOU 3828 O ALA B 23 1726 1196 2147 18 -48 -12 O ATOM 3829 CB ALA A 23 20.416 80.301 70.998 1.00 12.34 C ANISOU 3829 CB ALA B 23 1597 1390 1702 64 -54 5 C ATOM 3830 N ALA A 24 19.153 80.444 73.903 1.00 11.88 N ANISOU 3830 N ALA B 24 1588 1274 1653 50 30 -12 N ATOM 3831 CA ALA A 24 17.951 80.585 74.740 1.00 11.78 C ANISOU 3831 CA ALA B 24 1574 1255 1646 20 35 -82 C ATOM 3832 C ALA A 24 18.110 81.747 75.733 1.00 12.98 C ANISOU 3832 C ALA B 24 1706 1373 1853 113 37 -139 C ATOM 3833 O ALA A 24 17.171 82.532 75.972 1.00 12.94 O ANISOU 3833 O ALA B 24 1723 1046 2145 262 -15 -140 O ATOM 3834 CB ALA A 24 17.676 79.318 75.468 1.00 11.71 C ANISOU 3834 CB ALA B 24 1637 1235 1574 102 29 -76 C ATOM 3835 N VAL A 25 19.281 81.847 76.317 1.00 13.20 N ANISOU 3835 N VAL B 25 1707 1437 1870 60 24 -181 N ATOM 3836 CA VAL A 25 19.545 82.901 77.291 1.00 14.16 C ANISOU 3836 CA VAL B 25 1802 1667 1911 12 -31 -176 C ATOM 3837 C VAL A 25 19.497 84.272 76.610 1.00 15.01 C ANISOU 3837 C VAL B 25 1943 1705 2056 24 -19 -172 C ATOM 3838 O VAL A 25 19.001 85.259 77.190 1.00 15.84 O ANISOU 3838 O VAL B 25 1971 1733 2315 116 -6 -218 O ATOM 3839 CB VAL A 25 20.886 82.644 78.016 1.00 14.20 C ANISOU 3839 CB VAL B 25 1850 1667 1876 34 -68 -127 C ATOM 3840 CG1 VAL A 25 21.344 83.900 78.809 1.00 13.93 C ANISOU 3840 CG1 VAL B 25 1814 1572 1906 -77 -174 -172 C ATOM 3841 CG2 VAL A 25 20.770 81.423 78.941 1.00 13.31 C ANISOU 3841 CG2 VAL B 25 1812 1529 1717 36 -95 -214 C ATOM 3842 N SER A 26 19.958 84.330 75.370 1.00 16.40 N ANISOU 3842 N SER B 26 2130 1814 2285 -11 -15 -115 N ATOM 3843 CA SER A 26 20.031 85.586 74.627 1.00 17.70 C ANISOU 3843 CA SER B 26 2281 2033 2412 -6 -30 -44 C ATOM 3844 C SER A 26 18.654 86.155 74.303 1.00 18.52 C ANISOU 3844 C SER B 26 2393 2057 2586 21 -17 -59 C ATOM 3845 O SER A 26 18.502 87.365 74.243 1.00 18.92 O ANISOU 3845 O SER B 26 2451 1924 2810 52 -54 -135 O ATOM 3846 CB SER A 26 20.857 85.425 73.347 1.00 17.79 C ANISOU 3846 CB SER B 26 2286 2058 2414 1 -15 -56 C ATOM 3847 OG SER A 26 20.120 84.797 72.313 1.00 18.35 O ANISOU 3847 OG SER B 26 2280 2089 2600 6 23 -43 O ATOM 3848 N VAL A 27 17.652 85.293 74.113 1.00 18.43 N ANISOU 3848 N VAL B 27 2343 2114 2545 -33 -52 -74 N ATOM 3849 CA VAL A 27 16.321 85.754 73.678 1.00 18.18 C ANISOU 3849 CA VAL B 27 2343 2133 2429 37 -24 -13 C ATOM 3850 C VAL A 27 15.168 85.384 74.602 1.00 18.06 C ANISOU 3850 C VAL B 27 2295 2137 2427 25 -49 -33 C ATOM 3851 O VAL A 27 14.037 85.850 74.400 1.00 17.30 O ANISOU 3851 O VAL B 27 2227 1944 2401 139 -71 5 O ATOM 3852 CB VAL A 27 15.956 85.263 72.248 1.00 18.76 C ANISOU 3852 CB VAL B 27 2395 2206 2526 -4 -45 -9 C ATOM 3853 CG1 VAL A 27 17.051 85.602 71.265 1.00 19.57 C ANISOU 3853 CG1 VAL B 27 2543 2358 2532 117 22 -19 C ATOM 3854 CG2 VAL A 27 15.636 83.760 72.229 1.00 18.00 C ANISOU 3854 CG2 VAL B 27 2245 2145 2449 20 29 17 C ATOM 3855 N GLY A 28 15.429 84.550 75.599 1.00 17.97 N ANISOU 3855 N GLY B 28 2313 2102 2413 71 -55 -46 N ATOM 3856 CA GLY A 28 14.366 83.989 76.413 1.00 19.48 C ANISOU 3856 CA GLY B 28 2427 2380 2594 51 -25 -37 C ATOM 3857 C GLY A 28 13.372 84.983 76.995 1.00 20.82 C ANISOU 3857 C GLY B 28 2539 2603 2768 45 -31 -77 C ATOM 3858 O GLY A 28 12.156 84.758 76.949 1.00 20.66 O ANISOU 3858 O GLY B 28 2445 2576 2830 42 -16 -77 O ATOM 3859 N ASN A 29 13.881 86.083 77.548 1.00 21.97 N ANISOU 3859 N ASN B 29 2693 2724 2930 51 -47 -103 N ATOM 3860 CA ASN A 29 13.021 87.110 78.145 1.00 23.84 C ANISOU 3860 CA ASN B 29 2959 3001 3098 53 -4 -93 C ATOM 3861 C ASN A 29 12.069 87.755 77.148 1.00 23.43 C ANISOU 3861 C ASN B 29 2918 2940 3043 56 -3 -79 C ATOM 3862 O ASN A 29 10.996 88.232 77.531 1.00 24.06 O ANISOU 3862 O ASN B 29 3007 2983 3152 77 62 -95 O ATOM 3863 CB ASN A 29 13.875 88.208 78.805 1.00 24.80 C ANISOU 3863 CB ASN B 29 3091 3109 3223 41 -34 -121 C ATOM 3864 CG ASN A 29 14.498 87.752 80.109 1.00 27.63 C ANISOU 3864 CG ASN B 29 3507 3518 3470 28 12 -38 C ATOM 3865 OD1 ASN A 29 13.985 86.838 80.770 1.00 30.25 O ANISOU 3865 OD1 ASN B 29 3963 3608 3921 0 54 -98 O ATOM 3866 ND2 ASN A 29 15.599 88.394 80.501 1.00 30.43 N ANISOU 3866 ND2 ASN B 29 3854 3904 3803 -79 -23 -10 N ATOM 3867 N GLU A 30 12.465 87.770 75.879 1.00 22.67 N ANISOU 3867 N GLU B 30 2859 2805 2950 72 2 -33 N ATOM 3868 CA GLU A 30 11.734 88.484 74.833 1.00 22.18 C ANISOU 3868 CA GLU B 30 2814 2718 2893 32 -68 -62 C ATOM 3869 C GLU A 30 10.762 87.624 74.038 1.00 21.04 C ANISOU 3869 C GLU B 30 2685 2516 2791 28 -104 -26 C ATOM 3870 O GLU A 30 10.093 88.146 73.144 1.00 21.95 O ANISOU 3870 O GLU B 30 2897 2476 2965 68 -159 -45 O ATOM 3871 CB GLU A 30 12.702 89.142 73.859 1.00 22.33 C ANISOU 3871 CB GLU B 30 2844 2749 2889 56 -55 -33 C ATOM 3872 CG GLU A 30 13.674 90.124 74.489 1.00 24.85 C ANISOU 3872 CG GLU B 30 3155 3043 3244 25 -76 -100 C ATOM 3873 CD GLU A 30 12.987 91.309 75.156 1.00 27.54 C ANISOU 3873 CD GLU B 30 3485 3286 3690 64 -104 -168 C ATOM 3874 OE1 GLU A 30 11.838 91.647 74.788 1.00 27.91 O ANISOU 3874 OE1 GLU B 30 3669 3116 3817 80 -202 -208 O ATOM 3875 OE2 GLU A 30 13.609 91.905 76.063 1.00 28.42 O ANISOU 3875 OE2 GLU B 30 3611 3333 3853 66 -91 -173 O ATOM 3876 N VAL A 31 10.691 86.323 74.354 1.00 18.80 N ANISOU 3876 N VAL B 31 2403 2167 2573 96 -83 -86 N ATOM 3877 CA VAL A 31 9.796 85.403 73.644 1.00 17.30 C ANISOU 3877 CA VAL B 31 2177 2057 2336 82 -58 -46 C ATOM 3878 C VAL A 31 8.790 84.748 74.597 1.00 16.09 C ANISOU 3878 C VAL B 31 2115 1845 2152 155 -70 -42 C ATOM 3879 O VAL A 31 8.918 84.833 75.805 1.00 16.23 O ANISOU 3879 O VAL B 31 2128 1828 2211 214 -109 -84 O ATOM 3880 CB VAL A 31 10.562 84.265 72.846 1.00 17.08 C ANISOU 3880 CB VAL B 31 2213 1987 2290 72 -35 -51 C ATOM 3881 CG1 VAL A 31 11.576 84.838 71.851 1.00 16.94 C ANISOU 3881 CG1 VAL B 31 2104 1970 2362 106 -37 -108 C ATOM 3882 CG2 VAL A 31 11.221 83.251 73.787 1.00 17.47 C ANISOU 3882 CG2 VAL B 31 2147 2148 2341 58 -37 -12 C ATOM 3883 N ASP A 32 7.783 84.100 74.026 1.00 15.03 N ANISOU 3883 N ASP B 32 1953 1730 2026 152 -58 -1 N ATOM 3884 CA ASP A 32 6.716 83.460 74.772 1.00 14.84 C ANISOU 3884 CA ASP B 32 1941 1717 1979 66 -52 -45 C ATOM 3885 C ASP A 32 6.944 81.962 74.933 1.00 13.91 C ANISOU 3885 C ASP B 32 1817 1621 1846 22 -6 -30 C ATOM 3886 O ASP A 32 6.491 81.341 75.908 1.00 15.37 O ANISOU 3886 O ASP B 32 2094 1775 1969 -10 -18 -169 O ATOM 3887 CB ASP A 32 5.392 83.671 74.043 1.00 15.33 C ANISOU 3887 CB ASP B 32 2012 1806 2007 84 -61 -49 C ATOM 3888 CG ASP A 32 5.072 85.144 73.814 1.00 17.65 C ANISOU 3888 CG ASP B 32 2380 1976 2349 151 -34 -89 C ATOM 3889 OD1 ASP A 32 5.015 85.880 74.821 1.00 20.77 O ANISOU 3889 OD1 ASP B 32 2605 2230 3056 182 51 -420 O ATOM 3890 OD2 ASP A 32 4.894 85.603 72.666 1.00 19.27 O ANISOU 3890 OD2 ASP B 32 2651 1894 2775 279 -26 -263 O ATOM 3891 N VAL A 33 7.658 81.391 73.969 1.00 12.91 N ANISOU 3891 N VAL B 33 1705 1429 1772 0 -1 -62 N ATOM 3892 CA VAL A 33 7.835 79.950 73.893 1.00 12.21 C ANISOU 3892 CA VAL B 33 1480 1450 1709 33 1 -63 C ATOM 3893 C VAL A 33 9.280 79.668 73.501 1.00 12.06 C ANISOU 3893 C VAL B 33 1458 1472 1652 33 59 -92 C ATOM 3894 O VAL A 33 9.803 80.279 72.569 1.00 12.72 O ANISOU 3894 O VAL B 33 1453 1547 1833 46 112 -60 O ATOM 3895 CB VAL A 33 6.921 79.324 72.828 1.00 11.60 C ANISOU 3895 CB VAL B 33 1464 1383 1558 33 -6 -77 C ATOM 3896 CG1 VAL A 33 7.009 77.815 72.891 1.00 11.39 C ANISOU 3896 CG1 VAL B 33 1468 1286 1571 4 -94 8 C ATOM 3897 CG2 VAL A 33 5.447 79.784 72.980 1.00 11.46 C ANISOU 3897 CG2 VAL B 33 1446 1231 1675 46 -86 -135 C ATOM 3898 N ILE A 34 9.899 78.734 74.198 1.00 12.00 N ANISOU 3898 N ILE B 34 1468 1443 1646 9 50 -116 N ATOM 3899 CA ILE A 34 11.253 78.299 73.851 1.00 12.28 C ANISOU 3899 CA ILE B 34 1544 1402 1717 62 20 -118 C ATOM 3900 C ILE A 34 11.214 76.809 73.491 1.00 10.62 C ANISOU 3900 C ILE B 34 1397 1142 1494 81 68 -103 C ATOM 3901 O ILE A 34 10.693 75.994 74.251 1.00 11.09 O ANISOU 3901 O ILE B 34 1546 1065 1601 54 101 -263 O ATOM 3902 CB ILE A 34 12.216 78.567 74.991 1.00 12.78 C ANISOU 3902 CB ILE B 34 1612 1541 1703 69 54 -126 C ATOM 3903 CG1 ILE A 34 12.245 80.066 75.293 1.00 15.21 C ANISOU 3903 CG1 ILE B 34 1822 1832 2121 38 -59 -123 C ATOM 3904 CG2 ILE A 34 13.616 78.038 74.652 1.00 13.39 C ANISOU 3904 CG2 ILE B 34 1613 1478 1994 -16 -108 -89 C ATOM 3905 CD1 ILE A 34 12.786 80.401 76.669 1.00 16.93 C ANISOU 3905 CD1 ILE B 34 2120 2176 2137 110 74 -210 C ATOM 3906 N GLU A 35 11.740 76.478 72.314 1.00 10.52 N ANISOU 3906 N GLU B 35 1391 1136 1470 64 28 -93 N ATOM 3907 CA GLU A 35 11.666 75.098 71.780 1.00 9.83 C ANISOU 3907 CA GLU B 35 1269 1057 1407 30 24 -88 C ATOM 3908 C GLU A 35 13.037 74.431 71.658 1.00 10.06 C ANISOU 3908 C GLU B 35 1339 1109 1375 -9 42 -81 C ATOM 3909 O GLU A 35 13.916 74.964 70.972 1.00 10.35 O ANISOU 3909 O GLU B 35 1375 1178 1379 -17 27 -78 O ATOM 3910 CB GLU A 35 10.994 75.126 70.397 1.00 9.73 C ANISOU 3910 CB GLU B 35 1288 1063 1344 53 2 -125 C ATOM 3911 CG GLU A 35 10.950 73.755 69.688 1.00 10.61 C ANISOU 3911 CG GLU B 35 1503 1169 1359 75 -61 -173 C ATOM 3912 CD GLU A 35 10.215 73.750 68.354 1.00 12.21 C ANISOU 3912 CD GLU B 35 1731 1316 1592 8 -126 -107 C ATOM 3913 OE1 GLU A 35 10.256 74.771 67.634 1.00 12.96 O ANISOU 3913 OE1 GLU B 35 1928 1523 1472 73 -130 -90 O ATOM 3914 OE2 GLU A 35 9.639 72.679 67.996 1.00 14.45 O ANISOU 3914 OE2 GLU B 35 1933 1669 1888 -60 -236 -271 O ATOM 3915 N ALA A 36 13.195 73.256 72.275 1.00 10.02 N ANISOU 3915 N ALA B 36 1256 1200 1351 60 11 -34 N ATOM 3916 CA ALA A 36 14.389 72.420 72.094 1.00 9.44 C ANISOU 3916 CA ALA B 36 1262 1098 1225 38 48 -96 C ATOM 3917 C ALA A 36 14.125 71.628 70.829 1.00 9.80 C ANISOU 3917 C ALA B 36 1255 1192 1275 21 45 -108 C ATOM 3918 O ALA A 36 13.279 70.741 70.840 1.00 10.43 O ANISOU 3918 O ALA B 36 1341 1185 1436 51 101 -94 O ATOM 3919 CB ALA A 36 14.576 71.460 73.266 1.00 9.12 C ANISOU 3919 CB ALA B 36 1154 1085 1225 28 -9 -89 C ATOM 3920 N GLY A 37 14.788 72.019 69.740 1.00 9.69 N ANISOU 3920 N GLY B 37 1265 1220 1197 84 15 -99 N ATOM 3921 CA GLY A 37 14.548 71.412 68.438 1.00 9.53 C ANISOU 3921 CA GLY B 37 1200 1213 1206 46 -12 -95 C ATOM 3922 C GLY A 37 15.056 69.994 68.318 1.00 9.27 C ANISOU 3922 C GLY B 37 1108 1208 1206 38 -55 -109 C ATOM 3923 O GLY A 37 15.936 69.535 69.083 1.00 9.74 O ANISOU 3923 O GLY B 37 1162 1210 1327 162 -16 -111 O ATOM 3924 N THR A 38 14.476 69.276 67.354 1.00 9.27 N ANISOU 3924 N THR B 38 1116 1197 1208 29 -77 -108 N ATOM 3925 CA THR A 38 14.825 67.882 67.145 1.00 8.96 C ANISOU 3925 CA THR B 38 1126 1085 1193 12 -77 -91 C ATOM 3926 C THR A 38 16.328 67.650 66.931 1.00 9.43 C ANISOU 3926 C THR B 38 1211 1109 1264 -35 -9 -59 C ATOM 3927 O THR A 38 16.902 66.720 67.493 1.00 9.30 O ANISOU 3927 O THR B 38 1157 982 1393 0 -90 -107 O ATOM 3928 CB THR A 38 14.042 67.255 65.960 1.00 9.58 C ANISOU 3928 CB THR B 38 1199 1298 1143 -11 -14 -72 C ATOM 3929 OG1 THR A 38 12.707 67.757 65.918 1.00 9.83 O ANISOU 3929 OG1 THR B 38 1435 1193 1108 192 -28 -138 O ATOM 3930 CG2 THR A 38 13.965 65.754 66.139 1.00 9.94 C ANISOU 3930 CG2 THR B 38 1284 1217 1273 30 -158 -139 C ATOM 3931 N VAL A 39 16.951 68.489 66.118 1.00 8.76 N ANISOU 3931 N VAL B 39 1211 934 1182 -68 9 -34 N ATOM 3932 CA VAL A 39 18.373 68.346 65.820 1.00 8.74 C ANISOU 3932 CA VAL B 39 1268 953 1099 -15 -16 3 C ATOM 3933 C VAL A 39 19.170 68.391 67.114 1.00 8.22 C ANISOU 3933 C VAL B 39 1176 840 1105 -45 -57 28 C ATOM 3934 O VAL A 39 20.111 67.635 67.296 1.00 9.07 O ANISOU 3934 O VAL B 39 1343 894 1209 26 -168 -35 O ATOM 3935 CB VAL A 39 18.883 69.461 64.835 1.00 8.91 C ANISOU 3935 CB VAL B 39 1296 948 1141 -119 1 -33 C ATOM 3936 CG1 VAL A 39 20.395 69.487 64.773 1.00 9.08 C ANISOU 3936 CG1 VAL B 39 1331 945 1174 38 4 -3 C ATOM 3937 CG2 VAL A 39 18.285 69.288 63.433 1.00 10.98 C ANISOU 3937 CG2 VAL B 39 1480 1362 1329 8 -22 -53 C ATOM 3938 N CYS A 40 18.774 69.288 68.011 1.00 7.93 N ANISOU 3938 N CYS B 40 1173 706 1133 35 -82 111 N ATOM 3939 CA CYS A 40 19.466 69.429 69.271 1.00 8.51 C ANISOU 3939 CA CYS B 40 1216 819 1197 13 5 -16 C ATOM 3940 C CYS A 40 19.184 68.268 70.224 1.00 7.48 C ANISOU 3940 C CYS B 40 1012 660 1170 -2 -23 34 C ATOM 3941 O CYS A 40 20.113 67.703 70.801 1.00 7.80 O ANISOU 3941 O CYS B 40 1143 514 1307 5 41 -7 O ATOM 3942 CB CYS A 40 19.099 70.767 69.914 1.00 8.18 C ANISOU 3942 CB CYS B 40 1133 742 1231 20 22 -97 C ATOM 3943 SG CYS A 40 20.240 71.207 71.194 1.00 12.49 S ANISOU 3943 SG CYS B 40 2044 1278 1421 49 -82 -159 S ATOM 3944 N LEU A 41 17.916 67.913 70.407 1.00 8.00 N ANISOU 3944 N LEU B 41 1125 716 1197 61 40 3 N ATOM 3945 CA LEU A 41 17.599 66.796 71.302 1.00 7.32 C ANISOU 3945 CA LEU B 41 1075 703 1003 6 31 -34 C ATOM 3946 C LEU A 41 18.285 65.506 70.844 1.00 7.19 C ANISOU 3946 C LEU B 41 1073 747 910 61 45 -3 C ATOM 3947 O LEU A 41 18.769 64.757 71.680 1.00 7.56 O ANISOU 3947 O LEU B 41 1189 576 1105 133 -8 -92 O ATOM 3948 CB LEU A 41 16.081 66.580 71.380 1.00 7.94 C ANISOU 3948 CB LEU B 41 1146 705 1163 31 85 -48 C ATOM 3949 CG LEU A 41 15.260 67.659 72.094 1.00 7.43 C ANISOU 3949 CG LEU B 41 1089 731 1000 144 19 -59 C ATOM 3950 CD1 LEU A 41 13.793 67.432 71.842 1.00 9.21 C ANISOU 3950 CD1 LEU B 41 1371 929 1196 11 43 46 C ATOM 3951 CD2 LEU A 41 15.608 67.662 73.566 1.00 10.58 C ANISOU 3951 CD2 LEU B 41 1736 1004 1277 243 108 -155 C ATOM 3952 N LEU A 42 18.357 65.242 69.538 1.00 7.30 N ANISOU 3952 N LEU B 42 1091 744 939 28 -14 -17 N ATOM 3953 CA LEU A 42 19.066 64.026 69.061 1.00 7.41 C ANISOU 3953 CA LEU B 42 1016 829 968 45 -9 -42 C ATOM 3954 C LEU A 42 20.570 64.027 69.350 1.00 7.69 C ANISOU 3954 C LEU B 42 1064 782 1073 80 -46 -57 C ATOM 3955 O LEU A 42 21.209 62.971 69.440 1.00 8.98 O ANISOU 3955 O LEU B 42 1262 855 1294 83 -89 -81 O ATOM 3956 CB LEU A 42 18.811 63.787 67.564 1.00 7.73 C ANISOU 3956 CB LEU B 42 1104 849 982 10 -9 -45 C ATOM 3957 CG LEU A 42 17.380 63.392 67.186 1.00 8.26 C ANISOU 3957 CG LEU B 42 1070 975 1092 165 -18 -19 C ATOM 3958 CD1 LEU A 42 17.166 63.565 65.719 1.00 9.36 C ANISOU 3958 CD1 LEU B 42 1275 1013 1269 167 -19 13 C ATOM 3959 CD2 LEU A 42 17.084 61.951 67.593 1.00 8.61 C ANISOU 3959 CD2 LEU B 42 1188 908 1175 27 -163 -111 C ATOM 3960 N GLN A 43 21.136 65.217 69.510 1.00 8.39 N ANISOU 3960 N GLN B 43 1132 933 1122 40 -6 -32 N ATOM 3961 CA GLN A 43 22.529 65.368 69.906 1.00 8.24 C ANISOU 3961 CA GLN B 43 1138 918 1071 107 -61 6 C ATOM 3962 C GLN A 43 22.785 65.272 71.396 1.00 8.36 C ANISOU 3962 C GLN B 43 1157 963 1054 104 -29 -71 C ATOM 3963 O GLN A 43 23.792 64.688 71.819 1.00 8.49 O ANISOU 3963 O GLN B 43 1214 872 1139 110 -93 -69 O ATOM 3964 CB GLN A 43 23.057 66.716 69.426 1.00 8.29 C ANISOU 3964 CB GLN B 43 1209 828 1112 170 0 -34 C ATOM 3965 CG GLN A 43 23.426 66.723 67.926 1.00 8.39 C ANISOU 3965 CG GLN B 43 1104 868 1213 188 -22 103 C ATOM 3966 CD GLN A 43 24.630 65.827 67.614 1.00 9.82 C ANISOU 3966 CD GLN B 43 1223 924 1583 142 74 52 C ATOM 3967 OE1 GLN A 43 24.480 64.617 67.464 1.00 9.50 O ANISOU 3967 OE1 GLN B 43 1404 879 1327 -6 40 -141 O ATOM 3968 NE2 GLN A 43 25.813 66.423 67.524 1.00 10.73 N ANISOU 3968 NE2 GLN B 43 1249 1260 1567 72 74 2 N ATOM 3969 N VAL A 44 21.939 65.938 72.185 1.00 7.70 N ANISOU 3969 N VAL B 44 1077 846 1001 118 0 -6 N ATOM 3970 CA VAL A 44 22.268 66.188 73.585 1.00 8.62 C ANISOU 3970 CA VAL B 44 1114 1014 1146 29 -33 -68 C ATOM 3971 C VAL A 44 21.340 65.484 74.579 1.00 8.41 C ANISOU 3971 C VAL B 44 1074 1000 1121 19 -37 -16 C ATOM 3972 O VAL A 44 21.613 65.462 75.772 1.00 7.77 O ANISOU 3972 O VAL B 44 940 998 1013 29 20 -43 O ATOM 3973 CB VAL A 44 22.293 67.724 73.902 1.00 8.72 C ANISOU 3973 CB VAL B 44 1135 1047 1128 0 -47 -83 C ATOM 3974 CG1 VAL A 44 23.194 68.489 72.920 1.00 11.01 C ANISOU 3974 CG1 VAL B 44 1437 1328 1415 -45 4 -99 C ATOM 3975 CG2 VAL A 44 20.891 68.300 73.950 1.00 9.02 C ANISOU 3975 CG2 VAL B 44 1243 938 1243 146 -34 -111 C ATOM 3976 N GLY A 45 20.228 64.938 74.090 1.00 8.37 N ANISOU 3976 N GLY B 45 1035 1006 1138 -9 15 -8 N ATOM 3977 CA GLY A 45 19.274 64.291 74.961 1.00 8.26 C ANISOU 3977 CA GLY B 45 1045 943 1149 -43 33 -26 C ATOM 3978 C GLY A 45 18.371 65.276 75.692 1.00 7.74 C ANISOU 3978 C GLY B 45 1040 714 1183 -38 3 -10 C ATOM 3979 O GLY A 45 18.385 66.504 75.443 1.00 8.29 O ANISOU 3979 O GLY B 45 1107 645 1396 131 0 3 O ATOM 3980 N SER A 46 17.567 64.748 76.604 1.00 7.92 N ANISOU 3980 N SER B 46 1076 809 1123 35 30 -91 N ATOM 3981 CA SER A 46 16.446 65.516 77.155 1.00 8.01 C ANISOU 3981 CA SER B 46 1081 859 1103 19 -16 -146 C ATOM 3982 C SER A 46 16.815 66.405 78.342 1.00 7.75 C ANISOU 3982 C SER B 46 1042 794 1107 -13 12 -199 C ATOM 3983 O SER A 46 15.978 67.207 78.809 1.00 8.01 O ANISOU 3983 O SER B 46 1124 832 1087 -53 26 -247 O ATOM 3984 CB SER A 46 15.329 64.582 77.549 1.00 7.24 C ANISOU 3984 CB SER B 46 1089 706 953 57 55 -147 C ATOM 3985 OG SER A 46 15.719 63.798 78.655 1.00 7.48 O ANISOU 3985 OG SER B 46 1203 670 968 36 -188 -290 O ATOM 3986 N GLU A 47 18.023 66.269 78.884 1.00 8.50 N ANISOU 3986 N GLU B 47 1041 968 1221 -39 33 -174 N ATOM 3987 CA GLU A 47 18.393 67.201 79.988 1.00 9.54 C ANISOU 3987 CA GLU B 47 1148 1133 1340 22 -6 -174 C ATOM 3988 C GLU A 47 18.228 68.666 79.590 1.00 9.82 C ANISOU 3988 C GLU B 47 1130 1266 1334 77 -18 -145 C ATOM 3989 O GLU A 47 17.886 69.491 80.430 1.00 9.95 O ANISOU 3989 O GLU B 47 1383 1020 1378 74 -116 -352 O ATOM 3990 CB GLU A 47 19.785 66.951 80.549 1.00 9.86 C ANISOU 3990 CB GLU B 47 1150 1185 1411 -12 15 -136 C ATOM 3991 CG GLU A 47 20.021 67.675 81.860 1.00 11.60 C ANISOU 3991 CG GLU B 47 1187 1608 1609 28 -100 -172 C ATOM 3992 CD GLU A 47 21.297 67.278 82.539 1.00 13.37 C ANISOU 3992 CD GLU B 47 1488 1703 1886 66 -127 -73 C ATOM 3993 OE1 GLU A 47 22.223 66.778 81.855 1.00 15.14 O ANISOU 3993 OE1 GLU B 47 1615 2052 2085 75 -47 -209 O ATOM 3994 OE2 GLU A 47 21.355 67.480 83.762 1.00 15.77 O ANISOU 3994 OE2 GLU B 47 1799 2188 2003 228 -146 -180 O ATOM 3995 N LEU A 48 18.464 68.983 78.322 1.00 9.78 N ANISOU 3995 N LEU B 48 1112 1235 1369 111 29 -67 N ATOM 3996 CA LEU A 48 18.300 70.334 77.830 1.00 9.96 C ANISOU 3996 CA LEU B 48 1093 1229 1461 88 27 -31 C ATOM 3997 C LEU A 48 16.916 70.893 78.192 1.00 9.91 C ANISOU 3997 C LEU B 48 1168 1133 1463 77 83 -92 C ATOM 3998 O LEU A 48 16.800 72.074 78.516 1.00 9.57 O ANISOU 3998 O LEU B 48 1134 877 1625 49 143 -62 O ATOM 3999 CB LEU A 48 18.469 70.361 76.321 1.00 10.03 C ANISOU 3999 CB LEU B 48 1095 1211 1504 168 92 -2 C ATOM 4000 CG LEU A 48 18.107 71.674 75.620 1.00 11.34 C ANISOU 4000 CG LEU B 48 1267 1480 1559 174 18 77 C ATOM 4001 CD1 LEU A 48 18.936 72.845 76.151 1.00 11.56 C ANISOU 4001 CD1 LEU B 48 1249 1534 1610 189 -38 137 C ATOM 4002 CD2 LEU A 48 18.280 71.464 74.141 1.00 12.13 C ANISOU 4002 CD2 LEU B 48 1252 1678 1676 46 -92 183 C ATOM 4003 N VAL A 49 15.870 70.055 78.142 1.00 9.74 N ANISOU 4003 N VAL B 49 1162 1100 1439 43 7 -168 N ATOM 4004 CA VAL A 49 14.503 70.515 78.455 1.00 10.69 C ANISOU 4004 CA VAL B 49 1314 1257 1488 8 -4 -79 C ATOM 4005 C VAL A 49 14.440 71.035 79.902 1.00 10.49 C ANISOU 4005 C VAL B 49 1314 1253 1418 75 0 -25 C ATOM 4006 O VAL A 49 13.850 72.100 80.182 1.00 11.13 O ANISOU 4006 O VAL B 49 1319 1328 1580 144 -35 -46 O ATOM 4007 CB VAL A 49 13.472 69.387 78.194 1.00 10.90 C ANISOU 4007 CB VAL B 49 1290 1348 1504 2 1 -16 C ATOM 4008 CG1 VAL A 49 12.074 69.810 78.674 1.00 11.24 C ANISOU 4008 CG1 VAL B 49 1271 1308 1691 79 91 13 C ATOM 4009 CG2 VAL A 49 13.462 69.029 76.713 1.00 11.86 C ANISOU 4009 CG2 VAL B 49 1402 1483 1619 31 4 -93 C ATOM 4010 N GLU A 50 15.070 70.297 80.815 1.00 10.38 N ANISOU 4010 N GLU B 50 1279 1264 1398 120 -12 -41 N ATOM 4011 CA GLU A 50 15.038 70.628 82.227 1.00 10.49 C ANISOU 4011 CA GLU B 50 1284 1296 1405 21 20 -32 C ATOM 4012 C GLU A 50 15.900 71.846 82.534 1.00 10.10 C ANISOU 4012 C GLU B 50 1275 1247 1314 16 13 -113 C ATOM 4013 O GLU A 50 15.525 72.703 83.368 1.00 10.53 O ANISOU 4013 O GLU B 50 1293 1308 1398 76 84 -151 O ATOM 4014 CB GLU A 50 15.489 69.402 83.029 1.00 11.34 C ANISOU 4014 CB GLU B 50 1404 1421 1482 41 -55 31 C ATOM 4015 CG GLU A 50 15.389 69.566 84.522 1.00 13.28 C ANISOU 4015 CG GLU B 50 1763 1704 1578 -35 87 -49 C ATOM 4016 CD GLU A 50 15.618 68.263 85.278 1.00 17.28 C ANISOU 4016 CD GLU B 50 2429 2154 1983 -51 -70 56 C ATOM 4017 OE1 GLU A 50 15.729 67.183 84.644 1.00 17.43 O ANISOU 4017 OE1 GLU B 50 2636 2482 1503 14 -58 12 O ATOM 4018 OE2 GLU A 50 15.693 68.314 86.526 1.00 19.10 O ANISOU 4018 OE2 GLU B 50 2705 2661 1892 -214 155 3 O ATOM 4019 N VAL A 51 17.015 71.989 81.820 1.00 10.50 N ANISOU 4019 N VAL B 51 1338 1281 1369 -25 -41 -170 N ATOM 4020 CA VAL A 51 17.800 73.230 81.911 1.00 10.00 C ANISOU 4020 CA VAL B 51 1332 1077 1388 8 -60 -120 C ATOM 4021 C VAL A 51 16.988 74.462 81.489 1.00 11.01 C ANISOU 4021 C VAL B 51 1426 1297 1458 21 -87 -85 C ATOM 4022 O VAL A 51 17.024 75.481 82.177 1.00 11.10 O ANISOU 4022 O VAL B 51 1291 1242 1684 59 -127 -211 O ATOM 4023 CB VAL A 51 19.115 73.164 81.098 1.00 10.68 C ANISOU 4023 CB VAL B 51 1449 1215 1393 -15 -70 -73 C ATOM 4024 CG1 VAL A 51 19.846 74.508 81.106 1.00 11.08 C ANISOU 4024 CG1 VAL B 51 1641 1171 1396 -66 91 -179 C ATOM 4025 CG2 VAL A 51 20.043 72.076 81.627 1.00 8.92 C ANISOU 4025 CG2 VAL B 51 1179 985 1225 -22 55 -87 C ATOM 4026 N LEU A 52 16.246 74.348 80.394 1.00 10.72 N ANISOU 4026 N LEU B 52 1383 1228 1459 44 -106 -38 N ATOM 4027 CA LEU A 52 15.411 75.446 79.901 1.00 11.03 C ANISOU 4027 CA LEU B 52 1409 1253 1526 51 -66 -64 C ATOM 4028 C LEU A 52 14.307 75.759 80.911 1.00 11.67 C ANISOU 4028 C LEU B 52 1481 1356 1596 11 -36 -40 C ATOM 4029 O LEU A 52 13.996 76.942 81.150 1.00 12.30 O ANISOU 4029 O LEU B 52 1476 1462 1733 56 -96 -124 O ATOM 4030 CB LEU A 52 14.829 75.126 78.508 1.00 11.07 C ANISOU 4030 CB LEU B 52 1394 1240 1571 31 -31 -2 C ATOM 4031 CG LEU A 52 15.827 75.038 77.357 1.00 12.21 C ANISOU 4031 CG LEU B 52 1768 1373 1495 31 -21 -111 C ATOM 4032 CD1 LEU A 52 15.135 74.495 76.091 1.00 13.05 C ANISOU 4032 CD1 LEU B 52 1646 1693 1617 -80 -103 -125 C ATOM 4033 CD2 LEU A 52 16.534 76.380 77.078 1.00 12.18 C ANISOU 4033 CD2 LEU B 52 1646 1500 1478 -33 -12 -159 C ATOM 4034 N ARG A 53 13.735 74.718 81.519 1.00 12.51 N ANISOU 4034 N ARG B 53 1501 1535 1717 -5 -43 -65 N ATOM 4035 CA ARG A 53 12.672 74.915 82.501 1.00 12.22 C ANISOU 4035 CA ARG B 53 1476 1527 1639 -46 11 -78 C ATOM 4036 C ARG A 53 13.193 75.697 83.726 1.00 13.45 C ANISOU 4036 C ARG B 53 1613 1663 1834 -10 -29 -126 C ATOM 4037 O ARG A 53 12.490 76.570 84.280 1.00 14.33 O ANISOU 4037 O ARG B 53 1802 1622 2019 -82 -18 -163 O ATOM 4038 CB ARG A 53 12.030 73.570 82.895 1.00 12.33 C ANISOU 4038 CB ARG B 53 1438 1563 1681 -30 -17 -43 C ATOM 4039 CG ARG A 53 11.059 73.652 84.071 1.00 12.22 C ANISOU 4039 CG ARG B 53 1418 1634 1589 -27 -6 -78 C ATOM 4040 CD ARG A 53 9.944 74.688 83.904 1.00 14.29 C ANISOU 4040 CD ARG B 53 1690 1839 1899 -18 39 -82 C ATOM 4041 NE ARG A 53 8.999 74.251 82.894 1.00 15.32 N ANISOU 4041 NE ARG B 53 2036 1927 1855 126 -70 -105 N ATOM 4042 CZ ARG A 53 8.374 75.037 82.039 1.00 14.75 C ANISOU 4042 CZ ARG B 53 2062 1744 1796 104 -20 -107 C ATOM 4043 NH1 ARG A 53 8.595 76.359 82.008 1.00 12.39 N ANISOU 4043 NH1 ARG B 53 1767 1481 1457 36 -132 -226 N ATOM 4044 NH2 ARG A 53 7.522 74.489 81.188 1.00 13.29 N ANISOU 4044 NH2 ARG B 53 1771 1324 1952 126 -24 -154 N ATOM 4045 N SER A 54 14.397 75.344 84.175 1.00 14.00 N ANISOU 4045 N SER B 54 1672 1784 1862 -26 -51 -187 N ATOM 4046 CA SER A 54 15.045 76.038 85.280 1.00 13.93 C ANISOU 4046 CA SER B 54 1742 1756 1792 13 -1 -136 C ATOM 4047 C SER A 54 15.336 77.492 84.937 1.00 13.79 C ANISOU 4047 C SER B 54 1746 1722 1771 64 -5 -132 C ATOM 4048 O SER A 54 15.128 78.373 85.797 1.00 14.05 O ANISOU 4048 O SER B 54 1894 1551 1892 -13 -45 -265 O ATOM 4049 CB SER A 54 16.336 75.304 85.670 1.00 14.06 C ANISOU 4049 CB SER B 54 1764 1852 1726 80 -43 -48 C ATOM 4050 OG SER A 54 16.940 75.918 86.791 1.00 15.21 O ANISOU 4050 OG SER B 54 1723 1951 2104 -78 -10 -78 O ATOM 4051 N LEU A 55 15.789 77.757 83.710 1.00 13.77 N ANISOU 4051 N LEU B 55 1719 1674 1837 67 -13 -162 N ATOM 4052 CA LEU A 55 16.137 79.111 83.282 1.00 14.47 C ANISOU 4052 CA LEU B 55 1773 1804 1919 68 -30 -87 C ATOM 4053 C LEU A 55 14.893 79.971 83.105 1.00 15.56 C ANISOU 4053 C LEU B 55 1853 1909 2148 71 -35 -137 C ATOM 4054 O LEU A 55 14.942 81.179 83.332 1.00 16.08 O ANISOU 4054 O LEU B 55 1827 1915 2367 65 -45 -259 O ATOM 4055 CB LEU A 55 16.937 79.101 81.984 1.00 13.93 C ANISOU 4055 CB LEU B 55 1760 1659 1874 53 -89 -65 C ATOM 4056 CG LEU A 55 18.418 78.730 82.040 1.00 13.25 C ANISOU 4056 CG LEU B 55 1680 1653 1699 -59 -37 -60 C ATOM 4057 CD1 LEU A 55 18.965 78.378 80.673 1.00 12.31 C ANISOU 4057 CD1 LEU B 55 1616 1389 1671 65 -38 -62 C ATOM 4058 CD2 LEU A 55 19.175 79.889 82.656 1.00 13.78 C ANISOU 4058 CD2 LEU B 55 1801 1706 1727 -56 -152 -67 C ATOM 4059 N PHE A 56 13.784 79.334 82.730 1.00 15.85 N ANISOU 4059 N PHE B 56 1911 1971 2137 48 -46 -159 N ATOM 4060 CA PHE A 56 12.563 80.037 82.310 1.00 16.64 C ANISOU 4060 CA PHE B 56 2081 2027 2214 78 -26 -111 C ATOM 4061 C PHE A 56 11.339 79.370 82.930 1.00 16.60 C ANISOU 4061 C PHE B 56 2011 2037 2257 47 -70 -159 C ATOM 4062 O PHE A 56 10.577 78.670 82.241 1.00 16.45 O ANISOU 4062 O PHE B 56 1938 1996 2314 61 -74 -319 O ATOM 4063 CB PHE A 56 12.490 80.077 80.782 1.00 16.84 C ANISOU 4063 CB PHE B 56 2128 2019 2249 105 -59 -83 C ATOM 4064 CG PHE A 56 13.651 80.798 80.148 1.00 19.76 C ANISOU 4064 CG PHE B 56 2433 2512 2562 76 -56 13 C ATOM 4065 CD1 PHE A 56 13.732 82.189 80.200 1.00 22.09 C ANISOU 4065 CD1 PHE B 56 2732 2826 2833 5 -71 38 C ATOM 4066 CD2 PHE A 56 14.661 80.092 79.502 1.00 21.81 C ANISOU 4066 CD2 PHE B 56 2627 2915 2744 96 17 60 C ATOM 4067 CE1 PHE A 56 14.803 82.858 79.632 1.00 23.22 C ANISOU 4067 CE1 PHE B 56 2888 2977 2955 73 -9 133 C ATOM 4068 CE2 PHE A 56 15.736 80.757 78.946 1.00 22.42 C ANISOU 4068 CE2 PHE B 56 2773 2893 2852 74 -3 116 C ATOM 4069 CZ PHE A 56 15.804 82.140 78.999 1.00 23.03 C ANISOU 4069 CZ PHE B 56 2886 3031 2833 51 3 31 C ATOM 4070 N PRO A 57 11.147 79.535 84.250 1.00 16.58 N ANISOU 4070 N PRO B 57 2059 2036 2205 34 -57 -171 N ATOM 4071 CA PRO A 57 10.062 78.817 84.923 1.00 17.74 C ANISOU 4071 CA PRO B 57 2230 2227 2282 46 -4 -126 C ATOM 4072 C PRO A 57 8.682 79.171 84.393 1.00 19.14 C ANISOU 4072 C PRO B 57 2382 2495 2393 41 17 -158 C ATOM 4073 O PRO A 57 7.784 78.337 84.506 1.00 20.31 O ANISOU 4073 O PRO B 57 2479 2729 2507 38 83 -213 O ATOM 4074 CB PRO A 57 10.184 79.243 86.396 1.00 17.30 C ANISOU 4074 CB PRO B 57 2143 2180 2250 75 -7 -139 C ATOM 4075 CG PRO A 57 11.525 79.792 86.533 1.00 17.87 C ANISOU 4075 CG PRO B 57 2229 2198 2360 -50 -17 -137 C ATOM 4076 CD PRO A 57 11.946 80.320 85.207 1.00 16.70 C ANISOU 4076 CD PRO B 57 2167 1986 2191 8 -95 -146 C ATOM 4077 N ASP A 58 8.522 80.362 83.822 1.00 20.36 N ANISOU 4077 N ASP B 58 2550 2667 2519 108 2 -124 N ATOM 4078 CA ASP A 58 7.182 80.835 83.448 1.00 21.87 C ANISOU 4078 CA ASP B 58 2718 2859 2731 103 -13 -107 C ATOM 4079 C ASP A 58 6.956 80.951 81.943 1.00 21.57 C ANISOU 4079 C ASP B 58 2673 2820 2703 139 -3 -83 C ATOM 4080 O ASP A 58 5.959 81.526 81.494 1.00 22.17 O ANISOU 4080 O ASP B 58 2761 2911 2750 230 37 -98 O ATOM 4081 CB ASP A 58 6.839 82.137 84.184 1.00 22.50 C ANISOU 4081 CB ASP B 58 2815 2903 2828 129 -4 -104 C ATOM 4082 CG ASP A 58 6.922 81.982 85.692 1.00 24.85 C ANISOU 4082 CG ASP B 58 3154 3223 3063 74 56 -43 C ATOM 4083 OD1 ASP A 58 6.184 81.141 86.258 1.00 27.15 O ANISOU 4083 OD1 ASP B 58 3418 3498 3399 158 80 7 O ATOM 4084 OD2 ASP A 58 7.746 82.649 86.344 1.00 27.99 O ANISOU 4084 OD2 ASP B 58 3703 3603 3326 36 146 -228 O ATOM 4085 N LYS A 59 7.858 80.341 81.173 1.00 20.16 N ANISOU 4085 N LYS B 59 2480 2621 2557 125 -26 -134 N ATOM 4086 CA LYS A 59 7.763 80.313 79.726 1.00 19.46 C ANISOU 4086 CA LYS B 59 2413 2452 2526 80 2 -87 C ATOM 4087 C LYS A 59 7.194 78.967 79.286 1.00 17.28 C ANISOU 4087 C LYS B 59 2154 2174 2236 79 -23 -113 C ATOM 4088 O LYS A 59 7.332 77.966 79.983 1.00 18.01 O ANISOU 4088 O LYS B 59 2240 2235 2369 140 -116 -135 O ATOM 4089 CB LYS A 59 9.156 80.501 79.123 1.00 20.08 C ANISOU 4089 CB LYS B 59 2440 2571 2617 37 5 -92 C ATOM 4090 CG LYS A 59 9.230 81.485 77.994 1.00 23.20 C ANISOU 4090 CG LYS B 59 2885 2957 2970 54 38 -12 C ATOM 4091 CD LYS A 59 8.745 82.878 78.401 1.00 26.36 C ANISOU 4091 CD LYS B 59 3364 3354 3298 -4 29 -55 C ATOM 4092 CE LYS A 59 9.855 83.783 78.851 1.00 27.96 C ANISOU 4092 CE LYS B 59 3518 3584 3522 -79 2 39 C ATOM 4093 NZ LYS A 59 9.430 85.190 78.714 1.00 30.07 N ANISOU 4093 NZ LYS B 59 3814 3865 3746 42 -22 -36 N ATOM 4094 N ILE A 60 6.539 78.937 78.134 1.00 15.17 N ANISOU 4094 N ILE B 60 1876 1773 2115 126 -11 -124 N ATOM 4095 CA ILE A 60 6.139 77.653 77.556 1.00 13.17 C ANISOU 4095 CA ILE B 60 1665 1508 1830 99 14 -161 C ATOM 4096 C ILE A 60 7.385 76.977 76.968 1.00 11.86 C ANISOU 4096 C ILE B 60 1493 1343 1670 67 5 -134 C ATOM 4097 O ILE A 60 8.140 77.602 76.242 1.00 11.48 O ANISOU 4097 O ILE B 60 1556 1203 1600 138 46 -278 O ATOM 4098 CB ILE A 60 5.048 77.823 76.483 1.00 13.18 C ANISOU 4098 CB ILE B 60 1611 1466 1931 97 1 -148 C ATOM 4099 CG1 ILE A 60 3.762 78.332 77.135 1.00 14.18 C ANISOU 4099 CG1 ILE B 60 1730 1706 1949 162 77 -164 C ATOM 4100 CG2 ILE A 60 4.766 76.475 75.794 1.00 13.51 C ANISOU 4100 CG2 ILE B 60 1645 1499 1989 -34 71 -184 C ATOM 4101 CD1 ILE A 60 2.854 79.072 76.188 1.00 16.62 C ANISOU 4101 CD1 ILE B 60 2062 1989 2261 67 -39 -152 C ATOM 4102 N ILE A 61 7.591 75.699 77.316 1.00 10.85 N ANISOU 4102 N ILE B 61 1322 1227 1572 83 32 -181 N ATOM 4103 CA ILE A 61 8.711 74.897 76.789 1.00 11.22 C ANISOU 4103 CA ILE B 61 1434 1261 1566 45 29 -229 C ATOM 4104 C ILE A 61 8.200 73.781 75.866 1.00 11.17 C ANISOU 4104 C ILE B 61 1399 1304 1541 16 13 -201 C ATOM 4105 O ILE A 61 7.329 72.993 76.236 1.00 11.06 O ANISOU 4105 O ILE B 61 1317 1260 1626 19 139 -400 O ATOM 4106 CB ILE A 61 9.567 74.315 77.919 1.00 11.23 C ANISOU 4106 CB ILE B 61 1459 1214 1591 91 60 -242 C ATOM 4107 CG1 ILE A 61 10.094 75.415 78.889 1.00 13.68 C ANISOU 4107 CG1 ILE B 61 1827 1587 1782 -50 79 -257 C ATOM 4108 CG2 ILE A 61 10.740 73.448 77.351 1.00 12.19 C ANISOU 4108 CG2 ILE B 61 1429 1380 1822 88 57 -144 C ATOM 4109 CD1 ILE A 61 10.989 76.471 78.297 1.00 16.15 C ANISOU 4109 CD1 ILE B 61 2214 1916 2004 -101 12 -163 C ATOM 4110 N VAL A 62 8.800 73.699 74.687 1.00 10.84 N ANISOU 4110 N VAL B 62 1296 1338 1482 43 -55 -205 N ATOM 4111 CA VAL A 62 8.459 72.658 73.715 1.00 10.12 C ANISOU 4111 CA VAL B 62 1212 1204 1428 -13 -9 -168 C ATOM 4112 C VAL A 62 9.615 71.669 73.603 1.00 9.71 C ANISOU 4112 C VAL B 62 1181 1098 1410 -2 5 -150 C ATOM 4113 O VAL A 62 10.781 72.082 73.449 1.00 9.88 O ANISOU 4113 O VAL B 62 1158 1139 1454 158 107 -164 O ATOM 4114 CB VAL A 62 8.218 73.258 72.322 1.00 10.60 C ANISOU 4114 CB VAL B 62 1272 1234 1518 0 -69 -169 C ATOM 4115 CG1 VAL A 62 7.835 72.159 71.294 1.00 11.02 C ANISOU 4115 CG1 VAL B 62 1354 1458 1374 33 -92 -201 C ATOM 4116 CG2 VAL A 62 7.146 74.345 72.359 1.00 12.00 C ANISOU 4116 CG2 VAL B 62 1330 1428 1801 33 -4 -85 C ATOM 4117 N ALA A 63 9.286 70.369 73.650 1.00 9.07 N ANISOU 4117 N ALA B 63 1121 995 1328 28 112 -111 N ATOM 4118 CA ALA A 63 10.233 69.295 73.367 1.00 8.16 C ANISOU 4118 CA ALA B 63 1105 909 1085 65 5 -102 C ATOM 4119 C ALA A 63 9.886 68.830 71.944 1.00 8.71 C ANISOU 4119 C ALA B 63 1175 1011 1119 103 -23 -62 C ATOM 4120 O ALA A 63 8.869 68.184 71.717 1.00 8.96 O ANISOU 4120 O ALA B 63 1231 1093 1080 201 -70 -89 O ATOM 4121 CB ALA A 63 10.115 68.140 74.383 1.00 8.37 C ANISOU 4121 CB ALA B 63 1101 1042 1036 82 16 -108 C ATOM 4122 N ASP A 64 10.713 69.215 70.988 1.00 9.74 N ANISOU 4122 N ASP B 64 1276 1198 1226 91 -38 -50 N ATOM 4123 CA ASP A 64 10.427 68.924 69.572 1.00 10.00 C ANISOU 4123 CA ASP B 64 1220 1327 1252 55 3 -56 C ATOM 4124 C ASP A 64 10.972 67.541 69.206 1.00 9.33 C ANISOU 4124 C ASP B 64 1155 1156 1234 9 -3 -58 C ATOM 4125 O ASP A 64 11.985 67.422 68.527 1.00 9.49 O ANISOU 4125 O ASP B 64 1101 1220 1283 92 30 -31 O ATOM 4126 CB ASP A 64 11.001 70.056 68.717 1.00 10.74 C ANISOU 4126 CB ASP B 64 1337 1403 1341 72 -63 -32 C ATOM 4127 CG ASP A 64 10.776 69.889 67.242 1.00 11.95 C ANISOU 4127 CG ASP B 64 1593 1506 1442 -31 18 -78 C ATOM 4128 OD1 ASP A 64 9.815 69.174 66.817 1.00 12.29 O ANISOU 4128 OD1 ASP B 64 1584 1808 1276 113 4 -115 O ATOM 4129 OD2 ASP A 64 11.567 70.491 66.466 1.00 14.07 O ANISOU 4129 OD2 ASP B 64 2042 1712 1590 -24 -22 -61 O ATOM 4130 N THR A 65 10.310 66.487 69.673 1.00 8.96 N ANISOU 4130 N THR B 65 1053 1172 1177 53 34 -43 N ATOM 4131 CA THR A 65 10.810 65.139 69.428 1.00 8.74 C ANISOU 4131 CA THR B 65 1051 1130 1138 61 -30 -96 C ATOM 4132 C THR A 65 10.335 64.551 68.108 1.00 9.30 C ANISOU 4132 C THR B 65 1166 1223 1145 168 -49 -78 C ATOM 4133 O THR A 65 10.846 63.509 67.689 1.00 8.70 O ANISOU 4133 O THR B 65 1262 993 1049 151 -10 -10 O ATOM 4134 CB THR A 65 10.367 64.209 70.550 1.00 9.55 C ANISOU 4134 CB THR B 65 1083 1349 1195 21 -4 -114 C ATOM 4135 OG1 THR A 65 8.930 64.221 70.601 1.00 9.77 O ANISOU 4135 OG1 THR B 65 1043 1253 1413 93 8 -112 O ATOM 4136 CG2 THR A 65 10.901 64.689 71.910 1.00 8.97 C ANISOU 4136 CG2 THR B 65 1126 1233 1048 -82 -30 -7 C ATOM 4137 N LYS A 66 9.326 65.177 67.483 1.00 9.64 N ANISOU 4137 N LYS B 66 1236 1204 1223 166 -50 -128 N ATOM 4138 CA LYS A 66 8.716 64.625 66.258 1.00 9.93 C ANISOU 4138 CA LYS B 66 1326 1232 1212 112 -47 -77 C ATOM 4139 C LYS A 66 8.433 63.115 66.436 1.00 10.49 C ANISOU 4139 C LYS B 66 1426 1272 1286 118 -9 -74 C ATOM 4140 O LYS A 66 8.690 62.267 65.551 1.00 9.94 O ANISOU 4140 O LYS B 66 1484 1066 1224 92 -43 -95 O ATOM 4141 CB LYS A 66 9.594 64.940 65.052 1.00 10.76 C ANISOU 4141 CB LYS B 66 1346 1340 1401 77 -12 -83 C ATOM 4142 CG LYS A 66 9.601 66.435 64.706 1.00 10.23 C ANISOU 4142 CG LYS B 66 1483 1186 1218 110 -47 -96 C ATOM 4143 CD LYS A 66 10.366 66.745 63.450 1.00 11.33 C ANISOU 4143 CD LYS B 66 1411 1339 1554 -15 50 -76 C ATOM 4144 CE LYS A 66 10.340 68.217 63.098 1.00 11.90 C ANISOU 4144 CE LYS B 66 1617 1449 1452 -119 -115 -97 C ATOM 4145 NZ LYS A 66 10.885 69.052 64.220 1.00 13.15 N ANISOU 4145 NZ LYS B 66 2095 1677 1222 -114 74 -256 N ATOM 4146 N CYS A 67 7.887 62.799 67.606 1.00 10.34 N ANISOU 4146 N CYS B 67 1356 1224 1346 41 26 -57 N ATOM 4147 CA CYS A 67 7.624 61.443 68.006 1.00 11.34 C ANISOU 4147 CA CYS B 67 1414 1458 1435 13 -10 -109 C ATOM 4148 C CYS A 67 6.791 60.714 66.954 1.00 10.43 C ANISOU 4148 C CYS B 67 1249 1378 1334 40 -41 -145 C ATOM 4149 O CYS A 67 5.736 61.206 66.549 1.00 10.01 O ANISOU 4149 O CYS B 67 1173 1395 1236 59 -65 -380 O ATOM 4150 CB CYS A 67 6.895 61.475 69.338 1.00 12.01 C ANISOU 4150 CB CYS B 67 1403 1663 1495 -30 27 -51 C ATOM 4151 SG CYS A 67 6.384 59.888 69.967 1.00 13.72 S ANISOU 4151 SG CYS B 67 1767 1786 1659 -49 -64 -139 S ATOM 4152 N ALA A 68 7.267 59.537 66.546 1.00 10.18 N ANISOU 4152 N ALA B 68 1165 1322 1380 -10 -29 -100 N ATOM 4153 CA ALA A 68 6.552 58.652 65.617 1.00 9.77 C ANISOU 4153 CA ALA B 68 1170 1255 1283 16 1 -76 C ATOM 4154 C ALA A 68 5.980 57.395 66.265 1.00 9.41 C ANISOU 4154 C ALA B 68 1058 1237 1281 0 35 -97 C ATOM 4155 O ALA A 68 5.117 56.752 65.668 1.00 10.41 O ANISOU 4155 O ALA B 68 1246 1342 1365 -31 17 -222 O ATOM 4156 CB ALA A 68 7.474 58.231 64.526 1.00 10.22 C ANISOU 4156 CB ALA B 68 1203 1331 1347 -34 75 -16 C ATOM 4157 N ASP A 69 6.517 57.002 67.415 1.00 8.95 N ANISOU 4157 N ASP B 69 1117 1133 1149 -66 -3 -184 N ATOM 4158 CA ASP A 69 6.145 55.753 68.074 1.00 9.74 C ANISOU 4158 CA ASP B 69 1272 1259 1170 19 5 -97 C ATOM 4159 C ASP A 69 6.559 55.863 69.533 1.00 9.60 C ANISOU 4159 C ASP B 69 1209 1273 1164 7 -1 -122 C ATOM 4160 O ASP A 69 7.236 56.825 69.914 1.00 9.89 O ANISOU 4160 O ASP B 69 1286 1253 1216 -58 104 -137 O ATOM 4161 CB ASP A 69 6.893 54.585 67.389 1.00 9.83 C ANISOU 4161 CB ASP B 69 1271 1187 1276 18 37 -138 C ATOM 4162 CG ASP A 69 6.186 53.243 67.515 1.00 11.81 C ANISOU 4162 CG ASP B 69 1585 1343 1559 15 75 -136 C ATOM 4163 OD1 ASP A 69 5.162 53.124 68.222 1.00 11.63 O ANISOU 4163 OD1 ASP B 69 1931 992 1495 -567 136 -316 O ATOM 4164 OD2 ASP A 69 6.654 52.261 66.885 1.00 13.63 O ANISOU 4164 OD2 ASP B 69 2261 1073 1844 11 197 -219 O ATOM 4165 N ALA A 70 6.145 54.884 70.333 1.00 9.71 N ANISOU 4165 N ALA B 70 1287 1195 1205 -3 -55 -105 N ATOM 4166 CA ALA A 70 6.340 54.860 71.779 1.00 9.82 C ANISOU 4166 CA ALA B 70 1284 1199 1248 24 -49 -90 C ATOM 4167 C ALA A 70 5.901 56.198 72.372 1.00 9.66 C ANISOU 4167 C ALA B 70 1269 1156 1243 26 -28 -79 C ATOM 4168 O ALA A 70 6.612 56.800 73.167 1.00 9.63 O ANISOU 4168 O ALA B 70 1366 1154 1136 105 -72 -37 O ATOM 4169 CB ALA A 70 7.796 54.543 72.090 1.00 10.01 C ANISOU 4169 CB ALA B 70 1224 1243 1337 29 -20 -127 C ATOM 4170 N GLY A 71 4.699 56.632 71.975 1.00 9.15 N ANISOU 4170 N GLY B 71 1201 1038 1236 -24 -31 -125 N ATOM 4171 CA GLY A 71 4.129 57.903 72.386 1.00 9.04 C ANISOU 4171 CA GLY B 71 1137 1009 1288 31 -10 -63 C ATOM 4172 C GLY A 71 4.137 58.163 73.865 1.00 9.57 C ANISOU 4172 C GLY B 71 1183 1112 1339 -24 -60 -34 C ATOM 4173 O GLY A 71 4.525 59.241 74.288 1.00 10.10 O ANISOU 4173 O GLY B 71 1279 1052 1504 46 -51 -183 O ATOM 4174 N GLY A 72 3.642 57.210 74.656 1.00 10.03 N ANISOU 4174 N GLY B 72 1290 1215 1305 -122 -9 -46 N ATOM 4175 CA GLY A 72 3.542 57.401 76.100 1.00 10.32 C ANISOU 4175 CA GLY B 72 1236 1331 1351 -78 -13 -53 C ATOM 4176 C GLY A 72 4.917 57.498 76.733 1.00 9.98 C ANISOU 4176 C GLY B 72 1221 1288 1283 -55 -3 -80 C ATOM 4177 O GLY A 72 5.148 58.269 77.655 1.00 10.15 O ANISOU 4177 O GLY B 72 1182 1383 1288 -120 -10 -157 O ATOM 4178 N THR A 73 5.852 56.698 76.228 1.00 9.21 N ANISOU 4178 N THR B 73 1155 1072 1270 -91 21 -94 N ATOM 4179 CA THR A 73 7.210 56.728 76.777 1.00 9.63 C ANISOU 4179 CA THR B 73 1265 1103 1289 -43 60 29 C ATOM 4180 C THR A 73 7.922 58.050 76.437 1.00 8.86 C ANISOU 4180 C THR B 73 1207 1000 1158 -58 6 -16 C ATOM 4181 O THR A 73 8.524 58.689 77.313 1.00 8.84 O ANISOU 4181 O THR B 73 1085 1080 1193 -15 42 -25 O ATOM 4182 CB THR A 73 8.018 55.537 76.273 1.00 9.24 C ANISOU 4182 CB THR B 73 1243 1014 1251 23 47 55 C ATOM 4183 OG1 THR A 73 7.437 54.324 76.764 1.00 11.51 O ANISOU 4183 OG1 THR B 73 1744 1095 1534 -41 141 165 O ATOM 4184 CG2 THR A 73 9.446 55.587 76.822 1.00 10.23 C ANISOU 4184 CG2 THR B 73 1239 1163 1485 28 17 -62 C ATOM 4185 N VAL A 74 7.896 58.438 75.173 1.00 8.88 N ANISOU 4185 N VAL B 74 1184 1060 1128 -21 8 -42 N ATOM 4186 CA VAL A 74 8.553 59.678 74.772 1.00 8.62 C ANISOU 4186 CA VAL B 74 1075 1062 1138 55 21 -25 C ATOM 4187 C VAL A 74 7.955 60.897 75.476 1.00 9.18 C ANISOU 4187 C VAL B 74 1083 1211 1194 66 24 -4 C ATOM 4188 O VAL A 74 8.688 61.757 75.983 1.00 8.89 O ANISOU 4188 O VAL B 74 1004 1230 1142 173 19 -18 O ATOM 4189 CB VAL A 74 8.632 59.831 73.236 1.00 9.21 C ANISOU 4189 CB VAL B 74 1170 1138 1190 69 19 -67 C ATOM 4190 CG1 VAL A 74 9.331 61.108 72.859 1.00 10.06 C ANISOU 4190 CG1 VAL B 74 1167 1327 1327 -14 56 4 C ATOM 4191 CG2 VAL A 74 9.388 58.675 72.624 1.00 9.42 C ANISOU 4191 CG2 VAL B 74 1177 1131 1271 90 89 -132 C ATOM 4192 N ALA A 75 6.623 60.944 75.541 1.00 8.66 N ANISOU 4192 N ALA B 75 886 1235 1169 75 -3 -71 N ATOM 4193 CA ALA A 75 5.966 62.070 76.198 1.00 9.42 C ANISOU 4193 CA ALA B 75 1063 1271 1242 48 -1 -91 C ATOM 4194 C ALA A 75 6.308 62.104 77.683 1.00 9.05 C ANISOU 4194 C ALA B 75 1022 1207 1207 5 25 -123 C ATOM 4195 O ALA A 75 6.579 63.168 78.226 1.00 9.05 O ANISOU 4195 O ALA B 75 1010 1084 1342 77 0 -257 O ATOM 4196 CB ALA A 75 4.459 62.042 75.982 1.00 9.50 C ANISOU 4196 CB ALA B 75 1036 1338 1234 22 40 -47 C ATOM 4197 N LYS A 76 6.266 60.960 78.352 1.00 8.81 N ANISOU 4197 N LYS B 76 1076 1169 1102 1 -19 -143 N ATOM 4198 CA LYS A 76 6.637 60.896 79.787 1.00 9.81 C ANISOU 4198 CA LYS B 76 1147 1328 1249 1 13 -74 C ATOM 4199 C LYS A 76 8.074 61.407 79.984 1.00 9.43 C ANISOU 4199 C LYS B 76 1065 1272 1245 12 36 -133 C ATOM 4200 O LYS A 76 8.346 62.216 80.882 1.00 10.05 O ANISOU 4200 O LYS B 76 1071 1391 1355 6 117 -204 O ATOM 4201 CB LYS A 76 6.456 59.487 80.361 1.00 10.78 C ANISOU 4201 CB LYS B 76 1325 1434 1335 -32 60 -70 C ATOM 4202 CG LYS A 76 6.993 59.307 81.792 1.00 14.53 C ANISOU 4202 CG LYS B 76 1872 1886 1760 -116 -61 49 C ATOM 4203 CD LYS A 76 7.048 57.809 82.103 1.00 20.46 C ANISOU 4203 CD LYS B 76 2705 2475 2592 -60 -89 39 C ATOM 4204 CE LYS A 76 7.368 57.500 83.553 1.00 24.38 C ANISOU 4204 CE LYS B 76 3161 3092 3007 -64 -152 37 C ATOM 4205 NZ LYS A 76 7.852 56.083 83.675 1.00 27.09 N ANISOU 4205 NZ LYS B 76 3587 3335 3368 44 -185 -43 N ATOM 4206 N ASN A 77 8.987 60.926 79.152 1.00 9.12 N ANISOU 4206 N ASN B 77 1034 1311 1118 -5 38 -129 N ATOM 4207 CA ASN A 77 10.393 61.269 79.302 1.00 9.15 C ANISOU 4207 CA ASN B 77 1108 1194 1173 -15 34 -152 C ATOM 4208 C ASN A 77 10.640 62.785 79.238 1.00 9.04 C ANISOU 4208 C ASN B 77 1116 1196 1120 -12 10 -131 C ATOM 4209 O ASN A 77 11.504 63.305 79.944 1.00 10.96 O ANISOU 4209 O ASN B 77 1355 1452 1356 -85 -43 -272 O ATOM 4210 CB ASN A 77 11.224 60.546 78.244 1.00 8.80 C ANISOU 4210 CB ASN B 77 1186 1100 1057 33 69 -40 C ATOM 4211 CG ASN A 77 11.429 59.071 78.559 1.00 8.96 C ANISOU 4211 CG ASN B 77 1268 1029 1107 130 35 -152 C ATOM 4212 OD1 ASN A 77 11.157 58.634 79.661 1.00 9.62 O ANISOU 4212 OD1 ASN B 77 1512 1135 1008 404 47 -146 O ATOM 4213 ND2 ASN A 77 11.938 58.306 77.578 1.00 7.74 N ANISOU 4213 ND2 ASN B 77 1272 584 1084 299 -14 -287 N ATOM 4214 N ASN A 78 9.945 63.467 78.338 1.00 8.13 N ANISOU 4214 N ASN B 78 925 1024 1138 59 15 -195 N ATOM 4215 CA ASN A 78 10.068 64.912 78.173 1.00 8.17 C ANISOU 4215 CA ASN B 78 986 1072 1046 29 9 -126 C ATOM 4216 C ASN A 78 9.223 65.706 79.140 1.00 8.46 C ANISOU 4216 C ASN B 78 1067 1043 1103 50 34 -190 C ATOM 4217 O ASN A 78 9.630 66.808 79.568 1.00 8.94 O ANISOU 4217 O ASN B 78 986 1146 1262 -9 70 -332 O ATOM 4218 CB ASN A 78 9.827 65.275 76.721 1.00 8.45 C ANISOU 4218 CB ASN B 78 1026 1053 1132 183 24 -120 C ATOM 4219 CG ASN A 78 10.973 64.818 75.858 1.00 10.46 C ANISOU 4219 CG ASN B 78 1272 1422 1279 35 40 -71 C ATOM 4220 OD1 ASN A 78 11.997 65.481 75.795 1.00 8.94 O ANISOU 4220 OD1 ASN B 78 1129 1218 1048 8 92 -151 O ATOM 4221 ND2 ASN A 78 10.841 63.631 75.265 1.00 10.79 N ANISOU 4221 ND2 ASN B 78 1414 1397 1289 175 17 -127 N ATOM 4222 N ALA A 79 8.065 65.164 79.498 1.00 8.78 N ANISOU 4222 N ALA B 79 1084 1165 1087 22 -5 -256 N ATOM 4223 CA ALA A 79 7.228 65.837 80.511 1.00 8.95 C ANISOU 4223 CA ALA B 79 1162 1055 1183 91 26 -252 C ATOM 4224 C ALA A 79 7.891 65.851 81.884 1.00 9.08 C ANISOU 4224 C ALA B 79 1154 1100 1196 100 8 -276 C ATOM 4225 O ALA A 79 7.811 66.866 82.592 1.00 9.56 O ANISOU 4225 O ALA B 79 1345 950 1337 75 -74 -449 O ATOM 4226 CB ALA A 79 5.819 65.248 80.584 1.00 9.34 C ANISOU 4226 CB ALA B 79 1147 1167 1231 80 -16 -225 C ATOM 4227 N VAL A 80 8.541 64.760 82.281 1.00 10.16 N ANISOU 4227 N VAL B 80 1398 1207 1253 46 -1 -209 N ATOM 4228 CA VAL A 80 9.264 64.750 83.558 1.00 11.66 C ANISOU 4228 CA VAL B 80 1560 1498 1371 67 -3 -135 C ATOM 4229 C VAL A 80 10.410 65.768 83.594 1.00 11.65 C ANISOU 4229 C VAL B 80 1617 1483 1327 30 -6 -135 C ATOM 4230 O VAL A 80 10.765 66.237 84.689 1.00 12.07 O ANISOU 4230 O VAL B 80 1904 1447 1232 35 40 -243 O ATOM 4231 CB VAL A 80 9.759 63.354 83.992 1.00 12.81 C ANISOU 4231 CB VAL B 80 1652 1658 1558 -4 -47 -24 C ATOM 4232 CG1 VAL A 80 8.618 62.335 84.082 1.00 13.48 C ANISOU 4232 CG1 VAL B 80 1764 1668 1689 -24 27 46 C ATOM 4233 CG2 VAL A 80 10.806 62.844 83.076 1.00 14.17 C ANISOU 4233 CG2 VAL B 80 1892 1829 1661 127 19 -132 C ATOM 4234 N ARG A 81 10.957 66.147 82.423 1.00 11.56 N ANISOU 4234 N ARG B 81 1531 1448 1411 8 -19 -106 N ATOM 4235 CA ARG A 81 11.995 67.195 82.290 1.00 11.51 C ANISOU 4235 CA ARG B 81 1409 1521 1441 -15 -28 -25 C ATOM 4236 C ARG A 81 11.397 68.606 82.371 1.00 11.37 C ANISOU 4236 C ARG B 81 1355 1491 1473 -17 -65 -74 C ATOM 4237 O ARG A 81 12.116 69.594 82.518 1.00 12.38 O ANISOU 4237 O ARG B 81 1435 1505 1762 4 -77 -118 O ATOM 4238 CB ARG A 81 12.743 67.022 80.964 1.00 11.48 C ANISOU 4238 CB ARG B 81 1403 1536 1424 -54 -4 -29 C ATOM 4239 CG ARG A 81 13.608 65.778 80.858 1.00 11.58 C ANISOU 4239 CG ARG B 81 1294 1590 1514 -70 -36 -14 C ATOM 4240 CD ARG A 81 14.816 65.839 81.750 1.00 11.88 C ANISOU 4240 CD ARG B 81 1492 1359 1663 74 -59 -87 C ATOM 4241 NE ARG A 81 15.806 64.838 81.385 1.00 11.27 N ANISOU 4241 NE ARG B 81 1210 1501 1568 -66 -137 -208 N ATOM 4242 CZ ARG A 81 16.914 64.614 82.062 1.00 11.91 C ANISOU 4242 CZ ARG B 81 1508 1319 1699 132 -104 -150 C ATOM 4243 NH1 ARG A 81 17.196 65.315 83.169 1.00 12.24 N ANISOU 4243 NH1 ARG B 81 1724 1424 1502 175 -262 -307 N ATOM 4244 NH2 ARG A 81 17.747 63.676 81.629 1.00 11.77 N ANISOU 4244 NH2 ARG B 81 1395 1492 1585 203 -61 -184 N ATOM 4245 N GLY A 82 10.069 68.696 82.283 1.00 10.98 N ANISOU 4245 N GLY B 82 1212 1483 1475 24 -53 -53 N ATOM 4246 CA GLY A 82 9.359 69.970 82.360 1.00 10.67 C ANISOU 4246 CA GLY B 82 1285 1402 1366 79 -45 -119 C ATOM 4247 C GLY A 82 8.741 70.540 81.081 1.00 10.59 C ANISOU 4247 C GLY B 82 1249 1389 1385 89 -33 -175 C ATOM 4248 O GLY A 82 8.293 71.670 81.071 1.00 11.24 O ANISOU 4248 O GLY B 82 1307 1395 1566 70 -76 -129 O ATOM 4249 N ALA A 83 8.682 69.753 80.004 1.00 9.73 N ANISOU 4249 N ALA B 83 1184 1208 1304 123 -39 -209 N ATOM 4250 CA ALA A 83 8.055 70.203 78.778 1.00 9.29 C ANISOU 4250 CA ALA B 83 1111 1141 1277 37 -9 -164 C ATOM 4251 C ALA A 83 6.568 70.496 78.990 1.00 8.91 C ANISOU 4251 C ALA B 83 1076 1115 1193 55 1 -138 C ATOM 4252 O ALA A 83 5.866 69.774 79.696 1.00 10.04 O ANISOU 4252 O ALA B 83 1238 1221 1354 94 -22 -67 O ATOM 4253 CB ALA A 83 8.206 69.127 77.687 1.00 9.25 C ANISOU 4253 CB ALA B 83 1150 1104 1261 138 78 -110 C ATOM 4254 N ASP A 84 6.098 71.526 78.308 1.00 9.26 N ANISOU 4254 N ASP B 84 1153 1119 1247 -14 -50 -196 N ATOM 4255 CA ASP A 84 4.661 71.792 78.166 1.00 10.08 C ANISOU 4255 CA ASP B 84 1171 1346 1313 14 -46 -138 C ATOM 4256 C ASP A 84 4.065 71.165 76.904 1.00 10.58 C ANISOU 4256 C ASP B 84 1185 1475 1358 -46 -20 -141 C ATOM 4257 O ASP A 84 2.986 70.551 76.952 1.00 11.67 O ANISOU 4257 O ASP B 84 1089 1802 1539 -9 -19 -223 O ATOM 4258 CB ASP A 84 4.397 73.278 78.105 1.00 9.96 C ANISOU 4258 CB ASP B 84 1234 1322 1226 5 -44 -112 C ATOM 4259 CG ASP A 84 4.812 73.980 79.378 1.00 11.29 C ANISOU 4259 CG ASP B 84 1454 1405 1428 13 -28 -197 C ATOM 4260 OD1 ASP A 84 4.394 73.520 80.487 1.00 12.29 O ANISOU 4260 OD1 ASP B 84 1619 1529 1520 73 -40 -457 O ATOM 4261 OD2 ASP A 84 5.554 74.977 79.294 1.00 13.97 O ANISOU 4261 OD2 ASP B 84 1726 1869 1710 -31 83 -407 O ATOM 4262 N TRP A 85 4.717 71.404 75.771 1.00 10.26 N ANISOU 4262 N TRP B 85 1095 1458 1345 45 -5 -102 N ATOM 4263 CA TRP A 85 4.249 70.873 74.498 1.00 9.73 C ANISOU 4263 CA TRP B 85 1094 1288 1313 70 51 -132 C ATOM 4264 C TRP A 85 5.288 69.946 73.910 1.00 9.68 C ANISOU 4264 C TRP B 85 1093 1199 1384 73 71 -94 C ATOM 4265 O TRP A 85 6.478 70.178 74.075 1.00 10.32 O ANISOU 4265 O TRP B 85 1143 1275 1503 176 18 -161 O ATOM 4266 CB TRP A 85 4.030 72.005 73.501 1.00 9.71 C ANISOU 4266 CB TRP B 85 1097 1222 1368 105 86 -121 C ATOM 4267 CG TRP A 85 3.039 73.083 73.930 1.00 10.26 C ANISOU 4267 CG TRP B 85 1064 1408 1424 104 -108 -40 C ATOM 4268 CD1 TRP A 85 2.051 72.975 74.849 1.00 12.11 C ANISOU 4268 CD1 TRP B 85 1380 1660 1559 162 -94 -153 C ATOM 4269 CD2 TRP A 85 2.952 74.406 73.393 1.00 12.70 C ANISOU 4269 CD2 TRP B 85 1455 1544 1825 120 -121 -104 C ATOM 4270 NE1 TRP A 85 1.342 74.154 74.928 1.00 12.89 N ANISOU 4270 NE1 TRP B 85 1487 1677 1733 144 -188 -161 N ATOM 4271 CE2 TRP A 85 1.886 75.062 74.059 1.00 12.86 C ANISOU 4271 CE2 TRP B 85 1413 1714 1758 12 -44 -146 C ATOM 4272 CE3 TRP A 85 3.658 75.105 72.415 1.00 12.10 C ANISOU 4272 CE3 TRP B 85 1323 1657 1617 152 -113 -141 C ATOM 4273 CZ2 TRP A 85 1.521 76.387 73.778 1.00 13.46 C ANISOU 4273 CZ2 TRP B 85 1416 1913 1783 116 -29 -151 C ATOM 4274 CZ3 TRP A 85 3.302 76.435 72.137 1.00 12.85 C ANISOU 4274 CZ3 TRP B 85 1585 1604 1693 117 -40 -263 C ATOM 4275 CH2 TRP A 85 2.240 77.062 72.832 1.00 14.16 C ANISOU 4275 CH2 TRP B 85 1659 1739 1982 20 -42 -200 C ATOM 4276 N MET A 86 4.816 68.904 73.228 1.00 9.42 N ANISOU 4276 N MET B 86 1094 1190 1295 62 111 -173 N ATOM 4277 CA MET A 86 5.691 67.981 72.505 1.00 9.52 C ANISOU 4277 CA MET B 86 1104 1237 1277 76 82 -108 C ATOM 4278 C MET A 86 5.128 67.737 71.111 1.00 9.54 C ANISOU 4278 C MET B 86 1121 1260 1240 38 49 -91 C ATOM 4279 O MET A 86 3.919 67.626 70.919 1.00 9.35 O ANISOU 4279 O MET B 86 1020 1272 1261 97 17 -169 O ATOM 4280 CB MET A 86 5.859 66.651 73.256 1.00 10.25 C ANISOU 4280 CB MET B 86 1317 1327 1249 87 78 -128 C ATOM 4281 CG MET A 86 6.885 65.708 72.571 1.00 10.68 C ANISOU 4281 CG MET B 86 1130 1376 1552 94 150 -67 C ATOM 4282 SD MET A 86 7.025 64.099 73.277 1.00 11.59 S ANISOU 4282 SD MET B 86 1276 1458 1667 82 123 -163 S ATOM 4283 CE MET A 86 5.636 63.218 72.541 1.00 12.24 C ANISOU 4283 CE MET B 86 1372 1528 1750 47 -39 -60 C ATOM 4284 N THR A 87 6.014 67.691 70.126 1.00 9.70 N ANISOU 4284 N THR B 87 1087 1428 1168 95 13 -88 N ATOM 4285 CA THR A 87 5.623 67.411 68.741 1.00 9.40 C ANISOU 4285 CA THR B 87 1097 1307 1167 63 -45 -84 C ATOM 4286 C THR A 87 5.562 65.908 68.478 1.00 10.03 C ANISOU 4286 C THR B 87 1214 1363 1231 97 -43 -80 C ATOM 4287 O THR A 87 6.405 65.109 68.977 1.00 9.57 O ANISOU 4287 O THR B 87 1135 1219 1279 175 -107 -120 O ATOM 4288 CB THR A 87 6.559 68.115 67.701 1.00 9.87 C ANISOU 4288 CB THR B 87 1175 1372 1201 37 -73 -110 C ATOM 4289 OG1 THR A 87 7.922 67.751 67.926 1.00 9.67 O ANISOU 4289 OG1 THR B 87 1044 1328 1301 94 12 -358 O ATOM 4290 CG2 THR A 87 6.512 69.605 67.797 1.00 11.17 C ANISOU 4290 CG2 THR B 87 1412 1467 1366 151 -78 -100 C ATOM 4291 N CYS A 88 4.533 65.517 67.722 1.00 10.02 N ANISOU 4291 N CYS B 88 1240 1283 1283 80 -16 1 N ATOM 4292 CA CYS A 88 4.500 64.223 67.086 1.00 10.48 C ANISOU 4292 CA CYS B 88 1334 1407 1242 9 0 -30 C ATOM 4293 C CYS A 88 4.532 64.460 65.596 1.00 10.44 C ANISOU 4293 C CYS B 88 1367 1324 1273 26 -15 -5 C ATOM 4294 O CYS A 88 3.875 65.396 65.099 1.00 10.80 O ANISOU 4294 O CYS B 88 1461 1410 1233 66 -101 -51 O ATOM 4295 CB CYS A 88 3.203 63.511 67.439 1.00 11.15 C ANISOU 4295 CB CYS B 88 1364 1487 1386 -14 75 -66 C ATOM 4296 SG CYS A 88 3.160 62.685 69.056 1.00 12.46 S ANISOU 4296 SG CYS B 88 1449 1895 1389 172 92 -9 S ATOM 4297 N ILE A 89 5.292 63.647 64.881 1.00 10.47 N ANISOU 4297 N ILE B 89 1319 1337 1322 6 9 50 N ATOM 4298 CA ILE A 89 5.252 63.684 63.418 1.00 10.94 C ANISOU 4298 CA ILE B 89 1463 1344 1347 62 -1 -24 C ATOM 4299 C ILE A 89 3.861 63.247 62.941 1.00 10.57 C ANISOU 4299 C ILE B 89 1386 1303 1324 37 49 -61 C ATOM 4300 O ILE A 89 3.253 62.365 63.529 1.00 10.42 O ANISOU 4300 O ILE B 89 1497 1177 1284 103 33 -224 O ATOM 4301 CB ILE A 89 6.407 62.854 62.793 1.00 10.98 C ANISOU 4301 CB ILE B 89 1377 1397 1395 -18 89 28 C ATOM 4302 CG1 ILE A 89 6.597 63.184 61.315 1.00 11.49 C ANISOU 4302 CG1 ILE B 89 1769 1226 1367 48 -48 -91 C ATOM 4303 CG2 ILE A 89 6.186 61.343 63.008 1.00 12.10 C ANISOU 4303 CG2 ILE B 89 1684 1426 1487 201 -38 -54 C ATOM 4304 CD1 ILE A 89 7.187 64.562 61.049 1.00 13.30 C ANISOU 4304 CD1 ILE B 89 1794 1593 1665 -205 43 -116 C ATOM 4305 N CYS A 90 3.380 63.843 61.852 1.00 11.53 N ANISOU 4305 N CYS B 90 1528 1390 1461 97 -2 -84 N ATOM 4306 CA CYS A 90 2.036 63.549 61.352 1.00 12.37 C ANISOU 4306 CA CYS B 90 1600 1543 1555 27 -47 -100 C ATOM 4307 C CYS A 90 1.819 62.086 60.921 1.00 13.01 C ANISOU 4307 C CYS B 90 1614 1649 1680 18 -28 -89 C ATOM 4308 O CYS A 90 0.683 61.614 60.850 1.00 14.08 O ANISOU 4308 O CYS B 90 1685 1889 1774 -17 -99 -201 O ATOM 4309 CB CYS A 90 1.659 64.494 60.203 1.00 12.80 C ANISOU 4309 CB CYS B 90 1697 1612 1552 11 -66 -86 C ATOM 4310 SG CYS A 90 2.835 64.540 58.830 1.00 14.51 S ANISOU 4310 SG CYS B 90 2404 1736 1372 -7 -197 -281 S ATOM 4311 N SER A 91 2.895 61.356 60.645 1.00 13.47 N ANISOU 4311 N SER B 91 1682 1697 1737 24 -32 -125 N ATOM 4312 CA SER A 91 2.733 59.933 60.337 1.00 13.78 C ANISOU 4312 CA SER B 91 1780 1689 1767 35 13 -62 C ATOM 4313 C SER A 91 2.554 58.996 61.559 1.00 12.84 C ANISOU 4313 C SER B 91 1714 1546 1619 -11 24 -62 C ATOM 4314 O SER A 91 2.238 57.814 61.402 1.00 14.21 O ANISOU 4314 O SER B 91 1973 1651 1773 82 58 -138 O ATOM 4315 CB SER A 91 3.836 59.449 59.427 1.00 14.14 C ANISOU 4315 CB SER B 91 1875 1689 1809 17 21 -93 C ATOM 4316 OG SER A 91 5.063 59.761 59.954 1.00 16.26 O ANISOU 4316 OG SER B 91 1842 2015 2320 135 12 -210 O ATOM 4317 N ALA A 92 2.713 59.530 62.764 1.00 12.28 N ANISOU 4317 N ALA B 92 1604 1577 1484 4 42 -17 N ATOM 4318 CA ALA A 92 2.432 58.789 64.008 1.00 11.23 C ANISOU 4318 CA ALA B 92 1486 1418 1363 -41 -9 -64 C ATOM 4319 C ALA A 92 0.974 58.369 63.971 1.00 11.54 C ANISOU 4319 C ALA B 92 1468 1505 1409 -20 -34 -84 C ATOM 4320 O ALA A 92 0.126 59.145 63.569 1.00 12.35 O ANISOU 4320 O ALA B 92 1631 1558 1500 17 -50 -136 O ATOM 4321 CB ALA A 92 2.676 59.678 65.226 1.00 10.88 C ANISOU 4321 CB ALA B 92 1415 1429 1288 6 -77 -39 C ATOM 4322 N THR A 93 0.687 57.142 64.380 1.00 11.14 N ANISOU 4322 N THR B 93 1339 1492 1399 -58 -43 -146 N ATOM 4323 CA THR A 93 -0.693 56.675 64.425 1.00 11.77 C ANISOU 4323 CA THR B 93 1379 1535 1556 -41 -12 -118 C ATOM 4324 C THR A 93 -1.471 57.419 65.514 1.00 12.12 C ANISOU 4324 C THR B 93 1418 1571 1616 -20 -30 -152 C ATOM 4325 O THR A 93 -0.891 58.038 66.421 1.00 11.56 O ANISOU 4325 O THR B 93 1346 1427 1618 68 -39 -317 O ATOM 4326 CB THR A 93 -0.744 55.166 64.733 1.00 11.78 C ANISOU 4326 CB THR B 93 1387 1517 1572 -42 -17 -80 C ATOM 4327 OG1 THR A 93 -0.288 54.954 66.067 1.00 12.46 O ANISOU 4327 OG1 THR B 93 1523 1547 1663 -143 54 -163 O ATOM 4328 CG2 THR A 93 0.164 54.334 63.776 1.00 12.76 C ANISOU 4328 CG2 THR B 93 1419 1696 1731 2 7 -137 C ATOM 4329 N ILE A 94 -2.792 57.345 65.421 1.00 12.95 N ANISOU 4329 N ILE B 94 1504 1727 1689 -8 -45 -120 N ATOM 4330 CA ILE A 94 -3.675 57.900 66.440 1.00 14.13 C ANISOU 4330 CA ILE B 94 1649 1928 1792 22 -22 -138 C ATOM 4331 C ILE A 94 -3.410 57.282 67.819 1.00 13.71 C ANISOU 4331 C ILE B 94 1579 1872 1755 -32 5 -157 C ATOM 4332 O ILE A 94 -3.276 58.028 68.781 1.00 14.24 O ANISOU 4332 O ILE B 94 1570 2054 1786 -23 52 -316 O ATOM 4333 CB ILE A 94 -5.188 57.839 66.014 1.00 14.81 C ANISOU 4333 CB ILE B 94 1736 2014 1875 5 -30 -110 C ATOM 4334 CG1 ILE A 94 -5.411 58.739 64.787 1.00 17.62 C ANISOU 4334 CG1 ILE B 94 2126 2345 2221 56 -37 -68 C ATOM 4335 CG2 ILE A 94 -6.154 58.199 67.184 1.00 14.80 C ANISOU 4335 CG2 ILE B 94 1680 1981 1962 68 -98 -107 C ATOM 4336 CD1 ILE A 94 -5.156 60.199 64.976 1.00 19.30 C ANISOU 4336 CD1 ILE B 94 2307 2524 2501 -92 0 59 C ATOM 4337 N PRO A 95 -3.328 55.951 67.940 1.00 13.33 N ANISOU 4337 N PRO B 95 1571 1818 1672 -75 0 -115 N ATOM 4338 CA PRO A 95 -2.955 55.380 69.237 1.00 13.07 C ANISOU 4338 CA PRO B 95 1524 1747 1694 -64 -29 -107 C ATOM 4339 C PRO A 95 -1.646 55.951 69.812 1.00 12.30 C ANISOU 4339 C PRO B 95 1422 1699 1549 -81 -8 -103 C ATOM 4340 O PRO A 95 -1.601 56.241 71.005 1.00 11.98 O ANISOU 4340 O PRO B 95 1301 1728 1520 -182 5 -196 O ATOM 4341 CB PRO A 95 -2.867 53.888 68.961 1.00 13.42 C ANISOU 4341 CB PRO B 95 1634 1746 1717 -75 -9 -48 C ATOM 4342 CG PRO A 95 -3.788 53.658 67.785 1.00 14.32 C ANISOU 4342 CG PRO B 95 1724 1894 1821 -89 -60 -41 C ATOM 4343 CD PRO A 95 -3.717 54.913 66.954 1.00 13.92 C ANISOU 4343 CD PRO B 95 1669 1811 1806 -17 -22 -115 C ATOM 4344 N THR A 96 -0.636 56.177 68.979 1.00 11.53 N ANISOU 4344 N THR B 96 1399 1627 1354 -30 22 -167 N ATOM 4345 CA THR A 96 0.603 56.753 69.460 1.00 11.48 C ANISOU 4345 CA THR B 96 1390 1550 1420 14 34 -64 C ATOM 4346 C THR A 96 0.380 58.179 69.954 1.00 12.01 C ANISOU 4346 C THR B 96 1447 1611 1505 -21 -30 -107 C ATOM 4347 O THR A 96 0.860 58.542 71.028 1.00 12.12 O ANISOU 4347 O THR B 96 1390 1762 1453 -106 -61 -143 O ATOM 4348 CB THR A 96 1.649 56.739 68.352 1.00 11.47 C ANISOU 4348 CB THR B 96 1357 1575 1424 46 43 -53 C ATOM 4349 OG1 THR A 96 2.040 55.383 68.122 1.00 10.71 O ANISOU 4349 OG1 THR B 96 1412 1497 1157 32 50 -104 O ATOM 4350 CG2 THR A 96 2.893 57.523 68.760 1.00 12.28 C ANISOU 4350 CG2 THR B 96 1484 1681 1499 29 -5 -80 C ATOM 4351 N MET A 97 -0.358 58.969 69.171 1.00 11.25 N ANISOU 4351 N MET B 97 1325 1434 1514 -41 -42 -117 N ATOM 4352 CA MET A 97 -0.603 60.367 69.521 1.00 11.15 C ANISOU 4352 CA MET B 97 1306 1393 1535 -11 -39 -144 C ATOM 4353 C MET A 97 -1.435 60.466 70.800 1.00 11.22 C ANISOU 4353 C MET B 97 1380 1400 1480 6 -16 -142 C ATOM 4354 O MET A 97 -1.160 61.288 71.689 1.00 11.05 O ANISOU 4354 O MET B 97 1116 1509 1572 61 -11 -298 O ATOM 4355 CB MET A 97 -1.298 61.101 68.389 1.00 11.37 C ANISOU 4355 CB MET B 97 1402 1399 1518 -55 -12 -102 C ATOM 4356 CG MET A 97 -0.459 61.307 67.147 1.00 11.99 C ANISOU 4356 CG MET B 97 1565 1537 1451 -38 -40 -205 C ATOM 4357 SD MET A 97 -1.311 62.445 66.062 1.00 15.70 S ANISOU 4357 SD MET B 97 1975 2185 1803 171 -25 -51 S ATOM 4358 CE MET A 97 -0.103 62.610 64.730 1.00 13.89 C ANISOU 4358 CE MET B 97 1654 2004 1616 -46 8 -33 C ATOM 4359 N LYS A 98 -2.458 59.626 70.895 1.00 11.82 N ANISOU 4359 N LYS B 98 1325 1642 1522 15 32 -81 N ATOM 4360 CA LYS A 98 -3.280 59.552 72.108 1.00 12.86 C ANISOU 4360 CA LYS B 98 1565 1699 1621 36 112 -79 C ATOM 4361 C LYS A 98 -2.511 59.139 73.371 1.00 12.16 C ANISOU 4361 C LYS B 98 1476 1608 1536 -43 143 -91 C ATOM 4362 O LYS A 98 -2.691 59.729 74.441 1.00 12.63 O ANISOU 4362 O LYS B 98 1471 1771 1555 96 250 -164 O ATOM 4363 CB LYS A 98 -4.469 58.630 71.892 1.00 14.19 C ANISOU 4363 CB LYS B 98 1734 1861 1794 -44 22 -149 C ATOM 4364 CG LYS A 98 -5.654 59.274 71.187 1.00 18.06 C ANISOU 4364 CG LYS B 98 2318 2235 2305 67 54 -47 C ATOM 4365 CD LYS A 98 -6.890 58.358 71.343 1.00 22.40 C ANISOU 4365 CD LYS B 98 2787 2687 3034 -95 -22 -73 C ATOM 4366 CE LYS A 98 -8.123 58.897 70.670 1.00 25.47 C ANISOU 4366 CE LYS B 98 3250 3150 3276 -72 -55 -25 C ATOM 4367 NZ LYS A 98 -8.991 57.813 70.103 1.00 27.50 N ANISOU 4367 NZ LYS B 98 3511 3419 3517 -95 -41 -35 N ATOM 4368 N ALA A 99 -1.635 58.152 73.254 1.00 11.46 N ANISOU 4368 N ALA B 99 1444 1423 1485 -87 109 12 N ATOM 4369 CA ALA A 99 -0.781 57.756 74.372 1.00 11.03 C ANISOU 4369 CA ALA B 99 1340 1381 1468 -104 64 -25 C ATOM 4370 C ALA A 99 0.133 58.904 74.794 1.00 10.40 C ANISOU 4370 C ALA B 99 1289 1335 1324 -76 40 -23 C ATOM 4371 O ALA A 99 0.384 59.122 75.974 1.00 10.96 O ANISOU 4371 O ALA B 99 1389 1395 1379 -120 196 -100 O ATOM 4372 CB ALA A 99 0.048 56.536 73.995 1.00 11.20 C ANISOU 4372 CB ALA B 99 1397 1352 1506 -92 12 2 C ATOM 4373 N ALA A 100 0.652 59.621 73.810 1.00 10.71 N ANISOU 4373 N ALA B 100 1334 1353 1383 -98 36 -61 N ATOM 4374 CA ALA A 100 1.535 60.747 74.084 1.00 10.31 C ANISOU 4374 CA ALA B 100 1215 1311 1390 -21 5 -64 C ATOM 4375 C ALA A 100 0.747 61.823 74.813 1.00 10.85 C ANISOU 4375 C ALA B 100 1238 1412 1470 45 -15 -95 C ATOM 4376 O ALA A 100 1.212 62.368 75.821 1.00 10.85 O ANISOU 4376 O ALA B 100 1108 1492 1520 87 6 -119 O ATOM 4377 CB ALA A 100 2.131 61.270 72.802 1.00 10.48 C ANISOU 4377 CB ALA B 100 1220 1333 1427 -11 19 -48 C ATOM 4378 N ARG A 101 -0.472 62.089 74.337 1.00 11.05 N ANISOU 4378 N ARG B 101 1211 1426 1560 134 29 -157 N ATOM 4379 CA ARG A 101 -1.292 63.152 74.954 1.00 11.65 C ANISOU 4379 CA ARG B 101 1431 1397 1598 154 -13 -117 C ATOM 4380 C ARG A 101 -1.635 62.835 76.389 1.00 12.00 C ANISOU 4380 C ARG B 101 1394 1500 1662 142 4 -129 C ATOM 4381 O ARG A 101 -1.537 63.696 77.273 1.00 12.44 O ANISOU 4381 O ARG B 101 1443 1550 1733 253 -7 -137 O ATOM 4382 CB ARG A 101 -2.574 63.432 74.156 1.00 11.97 C ANISOU 4382 CB ARG B 101 1457 1517 1573 156 -17 -154 C ATOM 4383 CG ARG A 101 -3.440 64.506 74.832 1.00 14.59 C ANISOU 4383 CG ARG B 101 1868 1723 1952 182 51 -15 C ATOM 4384 CD ARG A 101 -4.622 64.954 73.993 1.00 17.12 C ANISOU 4384 CD ARG B 101 1988 2312 2202 -22 -11 -133 C ATOM 4385 NE ARG A 101 -5.527 63.842 73.715 1.00 21.53 N ANISOU 4385 NE ARG B 101 2559 2874 2744 -81 98 -95 N ATOM 4386 CZ ARG A 101 -6.402 63.316 74.579 1.00 24.41 C ANISOU 4386 CZ ARG B 101 3032 3265 2977 -212 130 -58 C ATOM 4387 NH1 ARG A 101 -6.524 63.782 75.818 1.00 23.92 N ANISOU 4387 NH1 ARG B 101 2808 3387 2891 -225 -6 -100 N ATOM 4388 NH2 ARG A 101 -7.171 62.316 74.189 1.00 25.21 N ANISOU 4388 NH2 ARG B 101 3148 3435 2993 -289 68 -37 N ATOM 4389 N LYS A 102 -2.019 61.590 76.630 1.00 12.96 N ANISOU 4389 N LYS B 102 1589 1685 1647 91 57 -20 N ATOM 4390 CA LYS A 102 -2.432 61.175 77.957 1.00 14.68 C ANISOU 4390 CA LYS B 102 1808 1989 1777 30 12 -72 C ATOM 4391 C LYS A 102 -1.260 61.222 78.937 1.00 13.97 C ANISOU 4391 C LYS B 102 1664 1958 1687 -17 50 -111 C ATOM 4392 O LYS A 102 -1.421 61.664 80.069 1.00 13.77 O ANISOU 4392 O LYS B 102 1564 2007 1658 -81 58 -272 O ATOM 4393 CB LYS A 102 -3.064 59.808 77.895 1.00 15.57 C ANISOU 4393 CB LYS B 102 1921 2109 1885 -3 89 -49 C ATOM 4394 CG LYS A 102 -4.486 59.839 77.299 1.00 20.33 C ANISOU 4394 CG LYS B 102 2526 2714 2483 20 -25 -18 C ATOM 4395 CD LYS A 102 -5.444 58.895 78.028 1.00 26.33 C ANISOU 4395 CD LYS B 102 3419 3300 3284 -44 -12 21 C ATOM 4396 CE LYS A 102 -4.955 57.446 77.983 1.00 28.80 C ANISOU 4396 CE LYS B 102 3692 3635 3615 41 -80 38 C ATOM 4397 NZ LYS A 102 -3.845 57.144 78.980 1.00 29.88 N ANISOU 4397 NZ LYS B 102 3848 3880 3624 38 -97 75 N ATOM 4398 N ALA A 103 -0.074 60.838 78.485 1.00 12.89 N ANISOU 4398 N ALA B 103 1567 1769 1560 30 -5 -117 N ATOM 4399 CA ALA A 103 1.100 60.868 79.347 1.00 11.60 C ANISOU 4399 CA ALA B 103 1459 1568 1380 86 4 -90 C ATOM 4400 C ALA A 103 1.511 62.310 79.696 1.00 11.08 C ANISOU 4400 C ALA B 103 1412 1477 1321 137 28 -90 C ATOM 4401 O ALA A 103 1.815 62.593 80.853 1.00 11.76 O ANISOU 4401 O ALA B 103 1551 1538 1379 108 -79 -140 O ATOM 4402 CB ALA A 103 2.280 60.085 78.690 1.00 10.71 C ANISOU 4402 CB ALA B 103 1409 1359 1300 114 35 -60 C ATOM 4403 N ILE A 104 1.510 63.215 78.712 1.00 10.16 N ANISOU 4403 N ILE B 104 1298 1299 1260 133 80 -134 N ATOM 4404 CA ILE A 104 1.885 64.606 78.973 1.00 10.77 C ANISOU 4404 CA ILE B 104 1344 1423 1323 5 63 -149 C ATOM 4405 C ILE A 104 0.821 65.294 79.829 1.00 11.57 C ANISOU 4405 C ILE B 104 1452 1544 1398 33 60 -250 C ATOM 4406 O ILE A 104 1.175 66.125 80.643 1.00 12.03 O ANISOU 4406 O ILE B 104 1462 1640 1467 21 155 -501 O ATOM 4407 CB ILE A 104 2.256 65.395 77.696 1.00 10.35 C ANISOU 4407 CB ILE B 104 1276 1344 1312 27 37 -172 C ATOM 4408 CG1 ILE A 104 3.096 66.633 78.060 1.00 11.03 C ANISOU 4408 CG1 ILE B 104 1447 1276 1465 -15 18 -91 C ATOM 4409 CG2 ILE A 104 1.039 65.842 76.917 1.00 10.52 C ANISOU 4409 CG2 ILE B 104 1335 1402 1257 -119 123 -122 C ATOM 4410 CD1 ILE A 104 3.796 67.236 76.877 1.00 12.74 C ANISOU 4410 CD1 ILE B 104 1593 1546 1702 -166 -21 37 C ATOM 4411 N GLU A 105 -0.460 64.967 79.654 1.00 12.54 N ANISOU 4411 N GLU B 105 1593 1692 1479 -6 161 -242 N ATOM 4412 CA GLU A 105 -1.519 65.549 80.498 1.00 13.70 C ANISOU 4412 CA GLU B 105 1636 1801 1769 42 110 -209 C ATOM 4413 C GLU A 105 -1.391 65.079 81.924 1.00 13.95 C ANISOU 4413 C GLU B 105 1664 1841 1793 -2 102 -223 C ATOM 4414 O GLU A 105 -1.742 65.799 82.860 1.00 14.25 O ANISOU 4414 O GLU B 105 1830 1805 1778 -64 114 -442 O ATOM 4415 CB GLU A 105 -2.916 65.181 79.987 1.00 14.39 C ANISOU 4415 CB GLU B 105 1736 1911 1821 37 99 -189 C ATOM 4416 CG GLU A 105 -3.302 65.920 78.735 1.00 14.73 C ANISOU 4416 CG GLU B 105 1686 1935 1975 194 78 -174 C ATOM 4417 CD GLU A 105 -4.611 65.443 78.123 1.00 16.33 C ANISOU 4417 CD GLU B 105 1975 2035 2192 41 -18 -55 C ATOM 4418 OE1 GLU A 105 -5.189 64.434 78.603 1.00 20.16 O ANISOU 4418 OE1 GLU B 105 2215 2919 2525 32 -25 -22 O ATOM 4419 OE2 GLU A 105 -5.053 66.072 77.127 1.00 16.78 O ANISOU 4419 OE2 GLU B 105 1768 2233 2373 201 42 -178 O ATOM 4420 N ASP A 106 -0.966 63.841 82.117 1.00 14.43 N ANISOU 4420 N ASP B 106 1767 1846 1868 -47 43 -139 N ATOM 4421 CA ASP A 106 -0.870 63.306 83.468 1.00 15.78 C ANISOU 4421 CA ASP B 106 2000 2053 1941 -10 34 -87 C ATOM 4422 C ASP A 106 0.195 64.008 84.308 1.00 15.16 C ANISOU 4422 C ASP B 106 1869 2057 1834 27 30 -81 C ATOM 4423 O ASP A 106 -0.018 64.267 85.496 1.00 15.71 O ANISOU 4423 O ASP B 106 1915 2231 1822 50 41 -134 O ATOM 4424 CB ASP A 106 -0.626 61.802 83.471 1.00 17.17 C ANISOU 4424 CB ASP B 106 2199 2196 2127 17 32 -56 C ATOM 4425 CG ASP A 106 -1.229 61.141 84.682 1.00 23.11 C ANISOU 4425 CG ASP B 106 2932 2960 2888 -14 45 53 C ATOM 4426 OD1 ASP A 106 -2.453 61.298 84.879 1.00 29.51 O ANISOU 4426 OD1 ASP B 106 3437 3902 3871 155 67 -31 O ATOM 4427 OD2 ASP A 106 -0.535 60.487 85.485 1.00 27.02 O ANISOU 4427 OD2 ASP B 106 3467 3418 3379 93 -208 87 O ATOM 4428 N ILE A 107 1.336 64.312 83.690 1.00 14.18 N ANISOU 4428 N ILE B 107 1775 1871 1739 19 34 -70 N ATOM 4429 CA ILE A 107 2.435 64.952 84.380 1.00 14.25 C ANISOU 4429 CA ILE B 107 1709 1933 1771 44 58 -42 C ATOM 4430 C ILE A 107 2.233 66.458 84.416 1.00 13.24 C ANISOU 4430 C ILE B 107 1543 1828 1659 -12 52 -53 C ATOM 4431 O ILE A 107 2.638 67.120 85.364 1.00 14.40 O ANISOU 4431 O ILE B 107 1641 2076 1751 93 50 -102 O ATOM 4432 CB ILE A 107 3.770 64.574 83.720 1.00 14.53 C ANISOU 4432 CB ILE B 107 1730 1968 1821 18 63 -53 C ATOM 4433 CG1 ILE A 107 4.093 63.099 84.031 1.00 16.66 C ANISOU 4433 CG1 ILE B 107 2085 2175 2069 61 114 -19 C ATOM 4434 CG2 ILE A 107 4.888 65.537 84.176 1.00 14.29 C ANISOU 4434 CG2 ILE B 107 1825 1815 1789 -18 122 -59 C ATOM 4435 CD1 ILE A 107 5.159 62.504 83.148 1.00 18.48 C ANISOU 4435 CD1 ILE B 107 2361 2261 2398 126 132 121 C ATOM 4436 N ASN A 108 1.595 66.988 83.379 1.00 12.50 N ANISOU 4436 N ASN B 108 1460 1756 1533 17 42 -107 N ATOM 4437 CA ASN A 108 1.420 68.418 83.200 1.00 11.92 C ANISOU 4437 CA ASN B 108 1480 1598 1450 22 7 -116 C ATOM 4438 C ASN A 108 -0.052 68.771 82.900 1.00 12.72 C ANISOU 4438 C ASN B 108 1562 1685 1586 38 44 -140 C ATOM 4439 O ASN A 108 -0.405 69.119 81.774 1.00 12.76 O ANISOU 4439 O ASN B 108 1587 1729 1530 241 90 -212 O ATOM 4440 CB ASN A 108 2.373 68.929 82.099 1.00 11.32 C ANISOU 4440 CB ASN B 108 1320 1536 1442 31 39 -147 C ATOM 4441 CG ASN A 108 2.455 70.468 82.008 1.00 12.46 C ANISOU 4441 CG ASN B 108 1417 1682 1634 65 39 -16 C ATOM 4442 OD1 ASN A 108 1.636 71.197 82.554 1.00 13.09 O ANISOU 4442 OD1 ASN B 108 1386 1760 1826 184 225 -338 O ATOM 4443 ND2 ASN A 108 3.473 70.954 81.304 1.00 12.64 N ANISOU 4443 ND2 ASN B 108 1353 2007 1441 73 33 -64 N ATOM 4444 N PRO A 109 -0.924 68.666 83.911 1.00 13.91 N ANISOU 4444 N PRO B 109 1664 1883 1737 74 91 -125 N ATOM 4445 CA PRO A 109 -2.349 68.923 83.678 1.00 15.49 C ANISOU 4445 CA PRO B 109 1842 2144 1897 47 82 -83 C ATOM 4446 C PRO A 109 -2.667 70.386 83.352 1.00 16.71 C ANISOU 4446 C PRO B 109 2016 2315 2018 67 85 -29 C ATOM 4447 O PRO A 109 -3.698 70.647 82.749 1.00 18.55 O ANISOU 4447 O PRO B 109 2150 2638 2259 118 96 -80 O ATOM 4448 CB PRO A 109 -3.003 68.487 85.005 1.00 15.65 C ANISOU 4448 CB PRO B 109 1823 2218 1904 57 105 -54 C ATOM 4449 CG PRO A 109 -1.933 68.564 86.013 1.00 15.07 C ANISOU 4449 CG PRO B 109 1733 2146 1845 30 167 -76 C ATOM 4450 CD PRO A 109 -0.665 68.245 85.296 1.00 14.22 C ANISOU 4450 CD PRO B 109 1656 1936 1810 22 126 -116 C ATOM 4451 N ASP A 110 -1.795 71.309 83.758 1.00 17.09 N ANISOU 4451 N ASP B 110 2153 2245 2092 53 108 -26 N ATOM 4452 CA ASP A 110 -1.884 72.742 83.431 1.00 18.88 C ANISOU 4452 CA ASP B 110 2321 2487 2364 42 89 -16 C ATOM 4453 C ASP A 110 -1.829 73.015 81.928 1.00 17.53 C ANISOU 4453 C ASP B 110 2096 2333 2229 59 70 -48 C ATOM 4454 O ASP A 110 -2.692 73.697 81.379 1.00 17.84 O ANISOU 4454 O ASP B 110 1968 2491 2317 139 146 -101 O ATOM 4455 CB ASP A 110 -0.683 73.476 84.030 1.00 19.62 C ANISOU 4455 CB ASP B 110 2410 2588 2455 -15 66 -41 C ATOM 4456 CG ASP A 110 -0.889 73.938 85.447 1.00 24.10 C ANISOU 4456 CG ASP B 110 2955 3205 2994 66 4 -61 C ATOM 4457 OD1 ASP A 110 -2.024 74.317 85.823 1.00 25.43 O ANISOU 4457 OD1 ASP B 110 3047 3384 3232 56 159 -173 O ATOM 4458 OD2 ASP A 110 0.099 73.979 86.228 1.00 27.61 O ANISOU 4458 OD2 ASP B 110 3458 3738 3293 -34 -91 -169 O ATOM 4459 N LYS A 111 -0.766 72.513 81.278 1.00 15.77 N ANISOU 4459 N LYS B 111 1912 2068 2010 52 59 -145 N ATOM 4460 CA LYS A 111 -0.406 72.978 79.945 1.00 14.70 C ANISOU 4460 CA LYS B 111 1826 1868 1889 65 38 -177 C ATOM 4461 C LYS A 111 -0.099 71.839 78.977 1.00 12.76 C ANISOU 4461 C LYS B 111 1557 1627 1664 122 52 -161 C ATOM 4462 O LYS A 111 0.122 72.099 77.812 1.00 13.61 O ANISOU 4462 O LYS B 111 1685 1746 1739 229 120 -204 O ATOM 4463 CB LYS A 111 0.831 73.904 79.991 1.00 14.88 C ANISOU 4463 CB LYS B 111 1814 1874 1965 23 63 -146 C ATOM 4464 CG LYS A 111 0.679 75.224 80.836 1.00 18.55 C ANISOU 4464 CG LYS B 111 2410 2308 2328 42 20 -227 C ATOM 4465 CD LYS A 111 1.796 76.256 80.498 1.00 21.76 C ANISOU 4465 CD LYS B 111 2749 2767 2753 -49 143 -101 C ATOM 4466 CE LYS A 111 2.963 76.265 81.542 1.00 24.14 C ANISOU 4466 CE LYS B 111 3140 3120 2910 -37 37 -56 C ATOM 4467 NZ LYS A 111 4.268 77.031 81.217 1.00 23.32 N ANISOU 4467 NZ LYS B 111 3100 3197 2561 -113 146 -118 N ATOM 4468 N GLY A 112 -0.070 70.608 79.464 1.00 11.14 N ANISOU 4468 N GLY B 112 1356 1450 1424 81 81 -231 N ATOM 4469 CA GLY A 112 0.449 69.503 78.648 1.00 10.29 C ANISOU 4469 CA GLY B 112 1250 1301 1356 44 72 -207 C ATOM 4470 C GLY A 112 -0.335 69.256 77.368 1.00 10.45 C ANISOU 4470 C GLY B 112 1222 1408 1338 45 103 -237 C ATOM 4471 O GLY A 112 -1.553 69.035 77.429 1.00 10.33 O ANISOU 4471 O GLY B 112 1116 1401 1405 15 244 -329 O ATOM 4472 N GLU A 113 0.355 69.298 76.223 1.00 10.13 N ANISOU 4472 N GLU B 113 1219 1330 1298 71 75 -248 N ATOM 4473 CA GLU A 113 -0.285 69.163 74.920 1.00 10.50 C ANISOU 4473 CA GLU B 113 1209 1460 1320 40 86 -209 C ATOM 4474 C GLU A 113 0.645 68.576 73.893 1.00 9.80 C ANISOU 4474 C GLU B 113 1143 1293 1285 13 50 -207 C ATOM 4475 O GLU A 113 1.868 68.750 73.974 1.00 9.52 O ANISOU 4475 O GLU B 113 1105 1232 1278 6 82 -215 O ATOM 4476 CB GLU A 113 -0.736 70.505 74.376 1.00 11.17 C ANISOU 4476 CB GLU B 113 1268 1590 1384 70 80 -151 C ATOM 4477 CG GLU A 113 -1.912 71.135 75.109 1.00 12.24 C ANISOU 4477 CG GLU B 113 1431 1772 1445 156 79 -186 C ATOM 4478 CD GLU A 113 -2.570 72.227 74.310 1.00 15.19 C ANISOU 4478 CD GLU B 113 1703 2233 1835 314 -31 -188 C ATOM 4479 OE1 GLU A 113 -2.773 72.037 73.092 1.00 16.23 O ANISOU 4479 OE1 GLU B 113 1712 2512 1940 521 74 -216 O ATOM 4480 OE2 GLU A 113 -2.898 73.285 74.905 1.00 18.39 O ANISOU 4480 OE2 GLU B 113 2470 2236 2280 292 -131 -252 O ATOM 4481 N ILE A 114 0.037 67.913 72.906 1.00 9.31 N ANISOU 4481 N ILE B 114 1232 1147 1158 -57 18 -123 N ATOM 4482 CA ILE A 114 0.752 67.451 71.736 1.00 9.45 C ANISOU 4482 CA ILE B 114 1172 1170 1246 55 -13 -144 C ATOM 4483 C ILE A 114 0.494 68.424 70.596 1.00 9.65 C ANISOU 4483 C ILE B 114 1236 1209 1219 89 -9 -136 C ATOM 4484 O ILE A 114 -0.610 68.988 70.488 1.00 10.88 O ANISOU 4484 O ILE B 114 1356 1480 1298 247 -98 -144 O ATOM 4485 CB ILE A 114 0.288 66.018 71.364 1.00 9.70 C ANISOU 4485 CB ILE B 114 1149 1252 1284 -1 12 -148 C ATOM 4486 CG1 ILE A 114 0.501 65.058 72.535 1.00 9.44 C ANISOU 4486 CG1 ILE B 114 1113 1131 1340 -20 -34 -310 C ATOM 4487 CG2 ILE A 114 0.945 65.531 70.071 1.00 10.67 C ANISOU 4487 CG2 ILE B 114 1290 1468 1296 107 25 -127 C ATOM 4488 CD1 ILE A 114 1.935 64.920 73.006 1.00 11.47 C ANISOU 4488 CD1 ILE B 114 1397 1367 1591 -68 -174 -183 C ATOM 4489 N GLN A 115 1.493 68.598 69.737 1.00 9.67 N ANISOU 4489 N GLN B 115 1184 1265 1223 40 -29 -87 N ATOM 4490 CA GLN A 115 1.386 69.387 68.493 1.00 9.57 C ANISOU 4490 CA GLN B 115 1215 1184 1238 113 -17 -69 C ATOM 4491 C GLN A 115 1.772 68.491 67.318 1.00 10.53 C ANISOU 4491 C GLN B 115 1288 1400 1312 152 -57 -105 C ATOM 4492 O GLN A 115 2.771 67.781 67.385 1.00 9.90 O ANISOU 4492 O GLN B 115 1128 1358 1273 246 -85 -119 O ATOM 4493 CB GLN A 115 2.319 70.596 68.474 1.00 10.58 C ANISOU 4493 CB GLN B 115 1323 1376 1321 100 -76 -52 C ATOM 4494 CG GLN A 115 2.399 71.414 69.719 1.00 10.46 C ANISOU 4494 CG GLN B 115 1509 974 1491 102 22 -92 C ATOM 4495 CD GLN A 115 3.460 72.472 69.596 1.00 12.32 C ANISOU 4495 CD GLN B 115 1507 1430 1743 24 18 -91 C ATOM 4496 OE1 GLN A 115 4.658 72.170 69.506 1.00 12.44 O ANISOU 4496 OE1 GLN B 115 1445 1441 1840 88 -41 -256 O ATOM 4497 NE2 GLN A 115 3.037 73.729 69.606 1.00 12.32 N ANISOU 4497 NE2 GLN B 115 1681 1187 1810 284 -86 -64 N ATOM 4498 N VAL A 116 1.030 68.564 66.227 1.00 10.69 N ANISOU 4498 N VAL B 116 1317 1401 1343 156 -64 -97 N ATOM 4499 CA VAL A 116 1.329 67.707 65.090 1.00 10.93 C ANISOU 4499 CA VAL B 116 1357 1438 1357 76 -117 -92 C ATOM 4500 C VAL A 116 2.263 68.438 64.111 1.00 10.86 C ANISOU 4500 C VAL B 116 1428 1352 1345 73 -79 -76 C ATOM 4501 O VAL A 116 1.919 69.489 63.545 1.00 10.74 O ANISOU 4501 O VAL B 116 1443 1344 1293 155 -80 4 O ATOM 4502 CB VAL A 116 0.042 67.229 64.358 1.00 11.27 C ANISOU 4502 CB VAL B 116 1398 1447 1435 43 -124 -105 C ATOM 4503 CG1 VAL A 116 0.416 66.356 63.146 1.00 10.45 C ANISOU 4503 CG1 VAL B 116 1308 1281 1380 30 -57 -25 C ATOM 4504 CG2 VAL A 116 -0.857 66.475 65.285 1.00 12.13 C ANISOU 4504 CG2 VAL B 116 1442 1689 1478 -74 -165 -98 C ATOM 4505 N GLU A 117 3.441 67.867 63.879 1.00 11.11 N ANISOU 4505 N GLU B 117 1419 1417 1384 55 -54 -65 N ATOM 4506 CA GLU A 117 4.370 68.396 62.874 1.00 10.90 C ANISOU 4506 CA GLU B 117 1392 1360 1387 63 -29 -95 C ATOM 4507 C GLU A 117 4.006 67.970 61.446 1.00 11.51 C ANISOU 4507 C GLU B 117 1414 1444 1513 55 -47 -112 C ATOM 4508 O GLU A 117 4.010 66.788 61.151 1.00 11.17 O ANISOU 4508 O GLU B 117 1396 1272 1575 60 -2 -119 O ATOM 4509 CB GLU A 117 5.793 67.991 63.211 1.00 11.17 C ANISOU 4509 CB GLU B 117 1480 1374 1389 111 -70 -112 C ATOM 4510 CG GLU A 117 6.446 68.949 64.187 1.00 11.18 C ANISOU 4510 CG GLU B 117 1452 1430 1363 102 -67 -107 C ATOM 4511 CD GLU A 117 6.958 70.204 63.558 1.00 12.36 C ANISOU 4511 CD GLU B 117 1518 1643 1532 134 -96 -55 C ATOM 4512 OE1 GLU A 117 6.685 70.436 62.350 1.00 14.20 O ANISOU 4512 OE1 GLU B 117 1969 1757 1668 198 64 -113 O ATOM 4513 OE2 GLU A 117 7.650 70.970 64.267 1.00 13.84 O ANISOU 4513 OE2 GLU B 117 1785 1524 1949 18 -138 -135 O ATOM 4514 N LEU A 118 3.736 68.934 60.562 1.00 11.85 N ANISOU 4514 N LEU B 118 1489 1549 1463 47 -41 -119 N ATOM 4515 CA LEU A 118 3.239 68.623 59.204 1.00 12.77 C ANISOU 4515 CA LEU B 118 1646 1627 1576 89 -50 -69 C ATOM 4516 C LEU A 118 4.352 68.500 58.162 1.00 12.68 C ANISOU 4516 C LEU B 118 1664 1603 1547 56 -34 -52 C ATOM 4517 O LEU A 118 4.998 69.487 57.787 1.00 12.75 O ANISOU 4517 O LEU B 118 1760 1508 1576 108 -66 -100 O ATOM 4518 CB LEU A 118 2.191 69.641 58.744 1.00 12.91 C ANISOU 4518 CB LEU B 118 1667 1673 1563 77 -38 -66 C ATOM 4519 CG LEU A 118 0.946 69.824 59.619 1.00 14.09 C ANISOU 4519 CG LEU B 118 1723 1781 1847 83 -61 -58 C ATOM 4520 CD1 LEU A 118 0.166 71.031 59.063 1.00 12.89 C ANISOU 4520 CD1 LEU B 118 1640 1594 1661 40 -21 87 C ATOM 4521 CD2 LEU A 118 0.095 68.581 59.662 1.00 14.52 C ANISOU 4521 CD2 LEU B 118 1678 1983 1853 61 -44 100 C ATOM 4522 N TYR A 119 4.560 67.273 57.689 1.00 12.63 N ANISOU 4522 N TYR B 119 1673 1505 1618 59 -55 -49 N ATOM 4523 CA TYR A 119 5.570 66.963 56.686 1.00 13.59 C ANISOU 4523 CA TYR B 119 1744 1719 1699 20 -24 -9 C ATOM 4524 C TYR A 119 4.962 66.012 55.679 1.00 14.47 C ANISOU 4524 C TYR B 119 1896 1769 1832 2 0 -47 C ATOM 4525 O TYR A 119 4.120 65.186 56.024 1.00 15.03 O ANISOU 4525 O TYR B 119 2020 1870 1819 68 105 -45 O ATOM 4526 CB TYR A 119 6.785 66.255 57.333 1.00 13.18 C ANISOU 4526 CB TYR B 119 1713 1609 1683 75 -33 -25 C ATOM 4527 CG TYR A 119 7.716 67.233 58.014 1.00 12.59 C ANISOU 4527 CG TYR B 119 1543 1736 1502 63 -102 78 C ATOM 4528 CD1 TYR A 119 8.848 67.713 57.373 1.00 12.23 C ANISOU 4528 CD1 TYR B 119 1565 1757 1325 102 -99 125 C ATOM 4529 CD2 TYR A 119 7.447 67.692 59.301 1.00 12.18 C ANISOU 4529 CD2 TYR B 119 1516 1542 1566 224 -180 -43 C ATOM 4530 CE1 TYR A 119 9.689 68.647 57.982 1.00 12.17 C ANISOU 4530 CE1 TYR B 119 1521 1717 1386 99 -84 89 C ATOM 4531 CE2 TYR A 119 8.281 68.618 59.923 1.00 11.85 C ANISOU 4531 CE2 TYR B 119 1411 1528 1563 62 -75 33 C ATOM 4532 CZ TYR A 119 9.394 69.104 59.255 1.00 11.92 C ANISOU 4532 CZ TYR B 119 1542 1566 1421 113 -181 116 C ATOM 4533 OH TYR A 119 10.215 70.004 59.891 1.00 12.37 O ANISOU 4533 OH TYR B 119 1966 1110 1623 200 -129 12 O ATOM 4534 N GLY A 120 5.397 66.140 54.434 1.00 16.31 N ANISOU 4534 N GLY B 120 2071 2034 2089 4 1 14 N ATOM 4535 CA GLY A 120 4.937 65.295 53.352 1.00 18.57 C ANISOU 4535 CA GLY B 120 2393 2374 2287 29 -28 -9 C ATOM 4536 C GLY A 120 3.451 65.425 53.043 1.00 20.07 C ANISOU 4536 C GLY B 120 2517 2598 2508 58 -47 -7 C ATOM 4537 O GLY A 120 2.854 66.485 53.279 1.00 20.68 O ANISOU 4537 O GLY B 120 2652 2637 2565 97 -143 -22 O ATOM 4538 N ASP A 121 2.863 64.336 52.542 1.00 22.03 N ANISOU 4538 N ASP B 121 2814 2807 2747 38 -17 -25 N ATOM 4539 CA ASP A 121 1.487 64.316 52.006 1.00 23.93 C ANISOU 4539 CA ASP B 121 3011 3075 3005 1 -25 -24 C ATOM 4540 C ASP A 121 0.347 64.085 52.997 1.00 24.14 C ANISOU 4540 C ASP B 121 3074 3051 3046 -22 -9 -18 C ATOM 4541 O ASP A 121 -0.398 63.092 52.887 1.00 25.12 O ANISOU 4541 O ASP B 121 3215 3145 3183 -33 -61 -64 O ATOM 4542 CB ASP A 121 1.358 63.237 50.926 1.00 24.58 C ANISOU 4542 CB ASP B 121 3111 3119 3107 28 -23 -48 C ATOM 4543 CG ASP A 121 2.234 63.496 49.731 1.00 27.55 C ANISOU 4543 CG ASP B 121 3561 3541 3365 3 -17 -20 C ATOM 4544 OD1 ASP A 121 2.618 64.658 49.516 1.00 29.35 O ANISOU 4544 OD1 ASP B 121 3899 3602 3650 -116 -121 -153 O ATOM 4545 OD2 ASP A 121 2.557 62.552 48.963 1.00 30.63 O ANISOU 4545 OD2 ASP B 121 4108 3721 3809 100 -34 -142 O ATOM 4546 N TRP A 122 0.145 65.025 53.902 1.00 23.38 N ANISOU 4546 N TRP B 122 3008 2966 2908 -47 -20 -9 N ATOM 4547 CA TRP A 122 -0.934 64.934 54.881 1.00 22.55 C ANISOU 4547 CA TRP B 122 2863 2898 2804 39 -40 -11 C ATOM 4548 C TRP A 122 -2.279 65.423 54.307 1.00 22.61 C ANISOU 4548 C TRP B 122 2904 2915 2771 41 -53 4 C ATOM 4549 O TRP A 122 -2.300 66.224 53.376 1.00 22.92 O ANISOU 4549 O TRP B 122 2969 2993 2745 104 -69 34 O ATOM 4550 CB TRP A 122 -0.541 65.702 56.150 1.00 21.84 C ANISOU 4550 CB TRP B 122 2764 2832 2703 -4 -37 -15 C ATOM 4551 CG TRP A 122 -0.399 67.150 55.928 1.00 19.94 C ANISOU 4551 CG TRP B 122 2548 2614 2412 90 -68 -50 C ATOM 4552 CD1 TRP A 122 0.724 67.821 55.552 1.00 19.30 C ANISOU 4552 CD1 TRP B 122 2550 2498 2283 90 -80 -30 C ATOM 4553 CD2 TRP A 122 -1.437 68.128 56.033 1.00 18.83 C ANISOU 4553 CD2 TRP B 122 2509 2486 2157 81 -89 -50 C ATOM 4554 NE1 TRP A 122 0.449 69.169 55.424 1.00 18.93 N ANISOU 4554 NE1 TRP B 122 2575 2318 2298 98 -140 -98 N ATOM 4555 CE2 TRP A 122 -0.873 69.381 55.713 1.00 17.68 C ANISOU 4555 CE2 TRP B 122 2368 2335 2012 99 -124 -125 C ATOM 4556 CE3 TRP A 122 -2.788 68.063 56.377 1.00 18.89 C ANISOU 4556 CE3 TRP B 122 2435 2481 2259 112 -126 -115 C ATOM 4557 CZ2 TRP A 122 -1.625 70.579 55.728 1.00 17.99 C ANISOU 4557 CZ2 TRP B 122 2429 2181 2224 65 -126 -22 C ATOM 4558 CZ3 TRP A 122 -3.535 69.241 56.394 1.00 19.29 C ANISOU 4558 CZ3 TRP B 122 2631 2286 2411 111 -159 42 C ATOM 4559 CH2 TRP A 122 -2.945 70.486 56.071 1.00 18.46 C ANISOU 4559 CH2 TRP B 122 2430 2159 2425 1 -168 -22 C ATOM 4560 N THR A 123 -3.385 64.946 54.877 1.00 22.24 N ANISOU 4560 N THR B 123 2857 2885 2709 65 -72 -8 N ATOM 4561 CA THR A 123 -4.727 65.292 54.409 1.00 21.94 C ANISOU 4561 CA THR B 123 2786 2830 2719 60 -50 7 C ATOM 4562 C THR A 123 -5.579 65.934 55.499 1.00 21.78 C ANISOU 4562 C THR B 123 2776 2801 2699 86 -79 -14 C ATOM 4563 O THR A 123 -5.283 65.807 56.691 1.00 21.12 O ANISOU 4563 O THR B 123 2701 2727 2597 126 -123 -68 O ATOM 4564 CB THR A 123 -5.498 64.058 53.860 1.00 21.86 C ANISOU 4564 CB THR B 123 2809 2772 2724 78 -33 19 C ATOM 4565 OG1 THR A 123 -5.887 63.200 54.937 1.00 21.92 O ANISOU 4565 OG1 THR B 123 2772 2887 2669 -28 -105 24 O ATOM 4566 CG2 THR A 123 -4.654 63.220 52.903 1.00 22.35 C ANISOU 4566 CG2 THR B 123 2809 2902 2781 52 18 -39 C ATOM 4567 N TYR A 124 -6.667 66.594 55.086 1.00 21.69 N ANISOU 4567 N TYR B 124 2713 2802 2725 101 -121 -22 N ATOM 4568 CA TYR A 124 -7.603 67.173 56.052 1.00 21.55 C ANISOU 4568 CA TYR B 124 2693 2813 2680 93 -129 -10 C ATOM 4569 C TYR A 124 -8.395 66.104 56.805 1.00 21.61 C ANISOU 4569 C TYR B 124 2667 2816 2728 118 -157 -13 C ATOM 4570 O TYR A 124 -8.811 66.315 57.943 1.00 21.09 O ANISOU 4570 O TYR B 124 2580 2804 2629 138 -240 5 O ATOM 4571 CB TYR A 124 -8.530 68.204 55.383 1.00 21.58 C ANISOU 4571 CB TYR B 124 2721 2790 2687 109 -123 -19 C ATOM 4572 CG TYR A 124 -7.774 69.403 54.854 1.00 22.51 C ANISOU 4572 CG TYR B 124 2900 2935 2716 29 -60 -52 C ATOM 4573 CD1 TYR A 124 -7.163 70.308 55.721 1.00 22.72 C ANISOU 4573 CD1 TYR B 124 2962 2868 2801 -43 -83 -46 C ATOM 4574 CD2 TYR A 124 -7.649 69.630 53.479 1.00 23.05 C ANISOU 4574 CD2 TYR B 124 2989 2981 2786 2 -68 39 C ATOM 4575 CE1 TYR A 124 -6.462 71.392 55.248 1.00 22.09 C ANISOU 4575 CE1 TYR B 124 2881 2787 2725 29 -51 -91 C ATOM 4576 CE2 TYR A 124 -6.947 70.718 52.998 1.00 22.96 C ANISOU 4576 CE2 TYR B 124 2964 2919 2839 -6 -68 2 C ATOM 4577 CZ TYR A 124 -6.351 71.601 53.889 1.00 22.23 C ANISOU 4577 CZ TYR B 124 2854 2816 2775 27 -81 -53 C ATOM 4578 OH TYR A 124 -5.664 72.689 53.399 1.00 23.22 O ANISOU 4578 OH TYR B 124 3163 2755 2904 32 -142 -83 O ATOM 4579 N ASP A 125 -8.590 64.951 56.173 1.00 22.09 N ANISOU 4579 N ASP B 125 2753 2881 2757 96 -151 -37 N ATOM 4580 CA ASP A 125 -9.214 63.807 56.819 1.00 22.94 C ANISOU 4580 CA ASP B 125 2860 2969 2885 64 -124 -62 C ATOM 4581 C ASP A 125 -8.390 63.293 58.003 1.00 22.24 C ANISOU 4581 C ASP B 125 2775 2886 2788 47 -98 -63 C ATOM 4582 O ASP A 125 -8.941 62.984 59.045 1.00 22.89 O ANISOU 4582 O ASP B 125 2755 3067 2874 75 -135 -113 O ATOM 4583 CB ASP A 125 -9.433 62.688 55.799 1.00 23.19 C ANISOU 4583 CB ASP B 125 2946 2954 2909 81 -113 -92 C ATOM 4584 CG ASP A 125 -10.576 62.991 54.827 1.00 26.09 C ANISOU 4584 CG ASP B 125 3366 3293 3254 81 -152 -110 C ATOM 4585 OD1 ASP A 125 -11.426 63.859 55.115 1.00 28.08 O ANISOU 4585 OD1 ASP B 125 3404 3628 3634 155 -91 -158 O ATOM 4586 OD2 ASP A 125 -10.680 62.360 53.758 1.00 28.09 O ANISOU 4586 OD2 ASP B 125 3735 3627 3310 34 -221 -151 O ATOM 4587 N GLN A 126 -7.075 63.196 57.815 1.00 21.78 N ANISOU 4587 N GLN B 126 2723 2822 2730 50 -99 -77 N ATOM 4588 CA GLN A 126 -6.147 62.822 58.884 1.00 20.85 C ANISOU 4588 CA GLN B 126 2598 2684 2639 22 -89 -31 C ATOM 4589 C GLN A 126 -6.216 63.878 59.974 1.00 19.27 C ANISOU 4589 C GLN B 126 2323 2533 2462 0 -120 -6 C ATOM 4590 O GLN A 126 -6.282 63.575 61.155 1.00 18.39 O ANISOU 4590 O GLN B 126 2150 2461 2375 -25 -200 2 O ATOM 4591 CB GLN A 126 -4.709 62.714 58.348 1.00 21.60 C ANISOU 4591 CB GLN B 126 2721 2758 2727 1 -62 -9 C ATOM 4592 CG GLN A 126 -4.402 61.501 57.467 1.00 23.31 C ANISOU 4592 CG GLN B 126 2943 2949 2964 45 -10 -34 C ATOM 4593 CD GLN A 126 -3.075 61.624 56.701 1.00 24.36 C ANISOU 4593 CD GLN B 126 3066 3055 3133 27 19 -35 C ATOM 4594 OE1 GLN A 126 -2.443 62.679 56.688 1.00 23.68 O ANISOU 4594 OE1 GLN B 126 2937 3109 2952 27 -101 -85 O ATOM 4595 NE2 GLN A 126 -2.668 60.535 56.041 1.00 25.64 N ANISOU 4595 NE2 GLN B 126 3143 3390 3207 64 10 -85 N ATOM 4596 N ALA A 127 -6.228 65.136 59.569 1.00 17.75 N ANISOU 4596 N ALA B 127 2170 2347 2223 43 -173 -38 N ATOM 4597 CA ALA A 127 -6.252 66.224 60.539 1.00 17.18 C ANISOU 4597 CA ALA B 127 2097 2254 2176 33 -144 -42 C ATOM 4598 C ALA A 127 -7.483 66.166 61.433 1.00 17.14 C ANISOU 4598 C ALA B 127 2072 2255 2185 17 -151 -47 C ATOM 4599 O ALA A 127 -7.415 66.470 62.618 1.00 16.78 O ANISOU 4599 O ALA B 127 1962 2263 2149 13 -201 -75 O ATOM 4600 CB ALA A 127 -6.136 67.571 59.839 1.00 16.55 C ANISOU 4600 CB ALA B 127 2087 2199 2001 62 -187 -29 C ATOM 4601 N GLN A 128 -8.618 65.758 60.870 1.00 17.51 N ANISOU 4601 N GLN B 128 2139 2228 2284 -27 -159 -88 N ATOM 4602 CA GLN A 128 -9.826 65.666 61.659 1.00 17.73 C ANISOU 4602 CA GLN B 128 2140 2254 2342 -30 -133 -87 C ATOM 4603 C GLN A 128 -9.691 64.550 62.688 1.00 17.85 C ANISOU 4603 C GLN B 128 2107 2305 2370 -20 -133 -105 C ATOM 4604 O GLN A 128 -10.187 64.658 63.792 1.00 17.77 O ANISOU 4604 O GLN B 128 1966 2383 2401 10 -169 -154 O ATOM 4605 CB GLN A 128 -11.049 65.437 60.758 1.00 18.10 C ANISOU 4605 CB GLN B 128 2181 2280 2415 3 -151 -97 C ATOM 4606 CG GLN A 128 -12.391 65.485 61.491 1.00 19.52 C ANISOU 4606 CG GLN B 128 2240 2603 2572 -82 -100 -43 C ATOM 4607 CD GLN A 128 -12.612 66.792 62.227 1.00 21.08 C ANISOU 4607 CD GLN B 128 2306 2844 2860 -21 -109 -47 C ATOM 4608 OE1 GLN A 128 -12.505 67.887 61.639 1.00 21.98 O ANISOU 4608 OE1 GLN B 128 2331 2940 3080 41 -262 13 O ATOM 4609 NE2 GLN A 128 -12.920 66.692 63.515 1.00 22.70 N ANISOU 4609 NE2 GLN B 128 2360 3268 2996 8 -196 -87 N ATOM 4610 N GLN A 129 -8.985 63.480 62.339 1.00 17.69 N ANISOU 4610 N GLN B 129 2085 2288 2348 -20 -95 -130 N ATOM 4611 CA GLN A 129 -8.738 62.413 63.317 1.00 17.82 C ANISOU 4611 CA GLN B 129 2137 2343 2288 -9 -78 -86 C ATOM 4612 C GLN A 129 -7.863 62.932 64.466 1.00 16.91 C ANISOU 4612 C GLN B 129 1999 2254 2172 -36 -79 -31 C ATOM 4613 O GLN A 129 -8.061 62.533 65.606 1.00 16.52 O ANISOU 4613 O GLN B 129 1845 2294 2137 -139 -14 -2 O ATOM 4614 CB GLN A 129 -8.082 61.174 62.702 1.00 18.84 C ANISOU 4614 CB GLN B 129 2304 2446 2408 -18 -86 -152 C ATOM 4615 CG GLN A 129 -8.818 60.514 61.555 1.00 21.35 C ANISOU 4615 CG GLN B 129 2659 2815 2635 -31 -139 -132 C ATOM 4616 CD GLN A 129 -7.929 59.482 60.892 1.00 24.42 C ANISOU 4616 CD GLN B 129 3221 3019 3036 13 -88 -82 C ATOM 4617 OE1 GLN A 129 -7.454 58.552 61.544 1.00 27.01 O ANISOU 4617 OE1 GLN B 129 3653 3202 3406 40 -164 -56 O ATOM 4618 NE2 GLN A 129 -7.659 59.663 59.607 1.00 27.52 N ANISOU 4618 NE2 GLN B 129 3664 3457 3334 -6 20 -19 N ATOM 4619 N TRP A 130 -6.905 63.817 64.176 1.00 16.12 N ANISOU 4619 N TRP B 130 1968 2103 2054 -9 -84 -7 N ATOM 4620 CA TRP A 130 -6.103 64.412 65.258 1.00 15.60 C ANISOU 4620 CA TRP B 130 1879 2080 1968 29 -94 -28 C ATOM 4621 C TRP A 130 -7.009 65.170 66.221 1.00 15.87 C ANISOU 4621 C TRP B 130 1932 2065 2029 47 -87 -20 C ATOM 4622 O TRP A 130 -6.938 64.933 67.420 1.00 15.77 O ANISOU 4622 O TRP B 130 1889 2050 2049 -31 -124 -121 O ATOM 4623 CB TRP A 130 -4.964 65.308 64.747 1.00 14.74 C ANISOU 4623 CB TRP B 130 1829 1879 1891 43 -122 -18 C ATOM 4624 CG TRP A 130 -4.093 64.652 63.740 1.00 14.33 C ANISOU 4624 CG TRP B 130 1661 1950 1830 7 -178 -18 C ATOM 4625 CD1 TRP A 130 -3.772 63.330 63.661 1.00 14.42 C ANISOU 4625 CD1 TRP B 130 1741 1774 1963 8 -57 19 C ATOM 4626 CD2 TRP A 130 -3.455 65.285 62.631 1.00 12.38 C ANISOU 4626 CD2 TRP B 130 1288 1545 1868 -23 -195 35 C ATOM 4627 NE1 TRP A 130 -2.973 63.099 62.569 1.00 13.39 N ANISOU 4627 NE1 TRP B 130 1448 1628 2012 -113 -53 30 N ATOM 4628 CE2 TRP A 130 -2.780 64.284 61.904 1.00 13.03 C ANISOU 4628 CE2 TRP B 130 1564 1681 1706 9 -127 3 C ATOM 4629 CE3 TRP A 130 -3.388 66.601 62.176 1.00 12.76 C ANISOU 4629 CE3 TRP B 130 1233 1691 1924 6 -309 -9 C ATOM 4630 CZ2 TRP A 130 -2.051 64.559 60.765 1.00 15.18 C ANISOU 4630 CZ2 TRP B 130 1933 1785 2049 -61 -40 33 C ATOM 4631 CZ3 TRP A 130 -2.691 66.873 61.027 1.00 14.60 C ANISOU 4631 CZ3 TRP B 130 1700 1901 1943 5 -52 11 C ATOM 4632 CH2 TRP A 130 -2.023 65.865 60.329 1.00 15.65 C ANISOU 4632 CH2 TRP B 130 2073 1776 2097 88 -13 57 C ATOM 4633 N LEU A 131 -7.922 65.994 65.686 1.00 16.18 N ANISOU 4633 N LEU B 131 1938 2088 2121 63 -52 -49 N ATOM 4634 CA LEU A 131 -8.898 66.704 66.527 1.00 16.83 C ANISOU 4634 CA LEU B 131 2024 2181 2189 39 -23 -54 C ATOM 4635 C LEU A 131 -9.771 65.742 67.311 1.00 17.49 C ANISOU 4635 C LEU B 131 2029 2320 2296 40 -30 -66 C ATOM 4636 O LEU A 131 -9.964 65.908 68.511 1.00 17.80 O ANISOU 4636 O LEU B 131 1856 2524 2383 58 -38 -90 O ATOM 4637 CB LEU A 131 -9.772 67.622 65.694 1.00 16.33 C ANISOU 4637 CB LEU B 131 1988 2126 2089 77 -38 -62 C ATOM 4638 CG LEU A 131 -9.100 68.765 64.931 1.00 16.54 C ANISOU 4638 CG LEU B 131 2020 2156 2107 89 -14 -69 C ATOM 4639 CD1 LEU A 131 -10.070 69.267 63.866 1.00 17.99 C ANISOU 4639 CD1 LEU B 131 2278 2223 2333 173 -58 -71 C ATOM 4640 CD2 LEU A 131 -8.599 69.925 65.812 1.00 17.42 C ANISOU 4640 CD2 LEU B 131 2056 2242 2317 20 -120 -26 C ATOM 4641 N ASP A 132 -10.262 64.699 66.643 1.00 17.78 N ANISOU 4641 N ASP B 132 2096 2303 2356 -31 -34 -87 N ATOM 4642 CA ASP A 132 -11.096 63.717 67.345 1.00 18.14 C ANISOU 4642 CA ASP B 132 2187 2331 2374 -13 -34 -59 C ATOM 4643 C ASP A 132 -10.322 63.054 68.477 1.00 18.13 C ANISOU 4643 C ASP B 132 2163 2383 2343 -44 -30 -78 C ATOM 4644 O ASP A 132 -10.910 62.681 69.472 1.00 18.22 O ANISOU 4644 O ASP B 132 2125 2466 2331 -106 -59 -93 O ATOM 4645 CB ASP A 132 -11.644 62.656 66.371 1.00 18.57 C ANISOU 4645 CB ASP B 132 2216 2453 2387 -7 -43 -112 C ATOM 4646 CG ASP A 132 -12.523 63.253 65.297 1.00 20.05 C ANISOU 4646 CG ASP B 132 2400 2627 2590 9 -30 -83 C ATOM 4647 OD1 ASP A 132 -12.987 64.397 65.462 1.00 21.59 O ANISOU 4647 OD1 ASP B 132 2429 2696 3079 66 -61 -153 O ATOM 4648 OD2 ASP A 132 -12.767 62.606 64.260 1.00 22.38 O ANISOU 4648 OD2 ASP B 132 2750 2898 2855 69 -107 -190 O ATOM 4649 N ALA A 133 -8.995 62.948 68.313 1.00 18.09 N ANISOU 4649 N ALA B 133 2114 2416 2341 15 -30 -70 N ATOM 4650 CA ALA A 133 -8.099 62.362 69.318 1.00 17.92 C ANISOU 4650 CA ALA B 133 2143 2382 2283 -5 21 -66 C ATOM 4651 C ALA A 133 -7.717 63.301 70.459 1.00 17.72 C ANISOU 4651 C ALA B 133 2113 2388 2230 5 54 -63 C ATOM 4652 O ALA A 133 -6.979 62.890 71.366 1.00 17.10 O ANISOU 4652 O ALA B 133 1871 2395 2229 -61 50 -63 O ATOM 4653 CB ALA A 133 -6.804 61.844 68.628 1.00 18.07 C ANISOU 4653 CB ALA B 133 2129 2401 2336 47 -8 -109 C ATOM 4654 N GLY A 134 -8.199 64.537 70.406 1.00 17.15 N ANISOU 4654 N GLY B 134 2032 2324 2159 -40 49 -102 N ATOM 4655 CA GLY A 134 -7.987 65.508 71.477 1.00 17.00 C ANISOU 4655 CA GLY B 134 2045 2220 2193 51 27 -148 C ATOM 4656 C GLY A 134 -6.787 66.403 71.245 1.00 16.80 C ANISOU 4656 C GLY B 134 2079 2170 2130 69 18 -129 C ATOM 4657 O GLY A 134 -6.387 67.163 72.133 1.00 17.24 O ANISOU 4657 O GLY B 134 2065 2261 2223 133 -107 -167 O ATOM 4658 N ILE A 135 -6.225 66.344 70.040 1.00 16.74 N ANISOU 4658 N ILE B 135 2104 2114 2140 77 -8 -106 N ATOM 4659 CA ILE A 135 -5.030 67.102 69.691 1.00 16.04 C ANISOU 4659 CA ILE B 135 2027 1987 2077 62 -40 -80 C ATOM 4660 C ILE A 135 -5.423 68.199 68.709 1.00 15.85 C ANISOU 4660 C ILE B 135 1925 2006 2089 94 -37 -77 C ATOM 4661 O ILE A 135 -5.969 67.923 67.636 1.00 15.82 O ANISOU 4661 O ILE B 135 1758 1976 2274 88 -124 -161 O ATOM 4662 CB ILE A 135 -3.961 66.171 69.100 1.00 16.19 C ANISOU 4662 CB ILE B 135 2008 2034 2108 53 -10 -47 C ATOM 4663 CG1 ILE A 135 -3.595 65.135 70.170 1.00 17.10 C ANISOU 4663 CG1 ILE B 135 2176 2231 2087 79 -109 -44 C ATOM 4664 CG2 ILE A 135 -2.741 66.944 68.636 1.00 14.44 C ANISOU 4664 CG2 ILE B 135 2014 1599 1870 111 -104 -28 C ATOM 4665 CD1 ILE A 135 -2.835 63.940 69.677 1.00 17.98 C ANISOU 4665 CD1 ILE B 135 2338 2204 2289 214 -47 -112 C ATOM 4666 N SER A 136 -5.137 69.443 69.076 1.00 14.74 N ANISOU 4666 N SER B 136 1763 1865 1970 14 -76 -82 N ATOM 4667 CA SER A 136 -5.653 70.607 68.330 1.00 14.33 C ANISOU 4667 CA SER B 136 1649 1870 1926 140 -39 -72 C ATOM 4668 C SER A 136 -4.618 71.684 68.050 1.00 13.63 C ANISOU 4668 C SER B 136 1647 1681 1848 150 -98 -99 C ATOM 4669 O SER A 136 -4.956 72.858 67.839 1.00 14.15 O ANISOU 4669 O SER B 136 1707 1686 1983 249 -157 -60 O ATOM 4670 CB SER A 136 -6.876 71.208 69.045 1.00 14.78 C ANISOU 4670 CB SER B 136 1656 1987 1971 95 -18 -83 C ATOM 4671 OG SER A 136 -6.559 71.563 70.370 1.00 14.88 O ANISOU 4671 OG SER B 136 1323 2291 2038 137 18 -187 O ATOM 4672 N GLN A 137 -3.349 71.293 67.994 1.00 12.80 N ANISOU 4672 N GLN B 137 1561 1600 1699 144 -121 -151 N ATOM 4673 CA GLN A 137 -2.297 72.157 67.510 1.00 12.06 C ANISOU 4673 CA GLN B 137 1495 1505 1581 125 -101 -131 C ATOM 4674 C GLN A 137 -1.580 71.475 66.354 1.00 11.81 C ANISOU 4674 C GLN B 137 1489 1399 1597 81 -73 -157 C ATOM 4675 O GLN A 137 -1.381 70.245 66.359 1.00 12.07 O ANISOU 4675 O GLN B 137 1467 1413 1704 129 -80 -255 O ATOM 4676 CB GLN A 137 -1.258 72.477 68.607 1.00 12.05 C ANISOU 4676 CB GLN B 137 1486 1507 1584 67 -89 -201 C ATOM 4677 CG GLN A 137 -1.750 73.324 69.771 1.00 11.59 C ANISOU 4677 CG GLN B 137 1363 1457 1581 132 -48 -111 C ATOM 4678 CD GLN A 137 -0.592 73.930 70.518 1.00 11.06 C ANISOU 4678 CD GLN B 137 1431 1200 1569 247 -27 -198 C ATOM 4679 OE1 GLN A 137 0.292 74.561 69.907 1.00 10.80 O ANISOU 4679 OE1 GLN B 137 1134 1379 1588 280 -139 -186 O ATOM 4680 NE2 GLN A 137 -0.541 73.693 71.818 1.00 13.41 N ANISOU 4680 NE2 GLN B 137 1483 1763 1847 317 49 -200 N ATOM 4681 N ALA A 138 -1.170 72.266 65.380 1.00 11.58 N ANISOU 4681 N ALA B 138 1483 1336 1580 117 -101 -125 N ATOM 4682 CA ALA A 138 -0.441 71.752 64.235 1.00 12.46 C ANISOU 4682 CA ALA B 138 1587 1561 1586 75 -101 -30 C ATOM 4683 C ALA A 138 0.593 72.760 63.793 1.00 12.72 C ANISOU 4683 C ALA B 138 1641 1552 1639 92 -105 -14 C ATOM 4684 O ALA A 138 0.358 73.969 63.857 1.00 13.50 O ANISOU 4684 O ALA B 138 1681 1586 1859 197 -160 -21 O ATOM 4685 CB ALA A 138 -1.417 71.415 63.082 1.00 12.58 C ANISOU 4685 CB ALA B 138 1585 1580 1614 31 -99 -57 C ATOM 4686 N ILE A 139 1.749 72.264 63.355 1.00 12.32 N ANISOU 4686 N ILE B 139 1622 1523 1535 139 -78 -41 N ATOM 4687 CA ILE A 139 2.850 73.108 62.903 1.00 12.75 C ANISOU 4687 CA ILE B 139 1683 1546 1612 88 -84 -69 C ATOM 4688 C ILE A 139 2.950 73.057 61.387 1.00 13.69 C ANISOU 4688 C ILE B 139 1804 1620 1774 69 -89 -71 C ATOM 4689 O ILE A 139 3.196 71.991 60.831 1.00 12.84 O ANISOU 4689 O ILE B 139 1780 1369 1730 214 -220 -110 O ATOM 4690 CB ILE A 139 4.221 72.638 63.518 1.00 13.04 C ANISOU 4690 CB ILE B 139 1672 1609 1671 135 -34 -61 C ATOM 4691 CG1 ILE A 139 4.101 72.245 65.006 1.00 13.02 C ANISOU 4691 CG1 ILE B 139 1611 1690 1643 43 9 -136 C ATOM 4692 CG2 ILE A 139 5.327 73.666 63.258 1.00 13.15 C ANISOU 4692 CG2 ILE B 139 1607 1597 1789 96 -121 -66 C ATOM 4693 CD1 ILE A 139 3.624 73.355 65.917 1.00 14.49 C ANISOU 4693 CD1 ILE B 139 1764 1858 1881 113 -24 -78 C ATOM 4694 N TYR A 140 2.758 74.211 60.741 1.00 14.88 N ANISOU 4694 N TYR B 140 1916 1817 1918 92 -75 -28 N ATOM 4695 CA TYR A 140 2.799 74.345 59.282 1.00 16.01 C ANISOU 4695 CA TYR B 140 2079 1957 2045 100 -68 26 C ATOM 4696 C TYR A 140 4.062 75.073 58.835 1.00 15.86 C ANISOU 4696 C TYR B 140 2101 1940 1986 106 -80 13 C ATOM 4697 O TYR A 140 4.395 76.161 59.329 1.00 16.33 O ANISOU 4697 O TYR B 140 2296 1822 2087 256 -97 39 O ATOM 4698 CB TYR A 140 1.561 75.084 58.755 1.00 16.33 C ANISOU 4698 CB TYR B 140 2065 2025 2112 19 -69 30 C ATOM 4699 CG TYR A 140 1.433 75.010 57.247 1.00 18.34 C ANISOU 4699 CG TYR B 140 2421 2265 2281 17 -48 56 C ATOM 4700 CD1 TYR A 140 0.692 73.993 56.647 1.00 20.58 C ANISOU 4700 CD1 TYR B 140 2635 2729 2452 -37 -59 13 C ATOM 4701 CD2 TYR A 140 2.090 75.919 56.432 1.00 19.54 C ANISOU 4701 CD2 TYR B 140 2482 2615 2327 13 -101 -3 C ATOM 4702 CE1 TYR A 140 0.586 73.900 55.280 1.00 22.78 C ANISOU 4702 CE1 TYR B 140 2952 3016 2686 -59 -59 67 C ATOM 4703 CE2 TYR A 140 2.000 75.838 55.040 1.00 21.09 C ANISOU 4703 CE2 TYR B 140 2784 2724 2504 158 -118 38 C ATOM 4704 CZ TYR A 140 1.238 74.828 54.479 1.00 22.11 C ANISOU 4704 CZ TYR B 140 2975 2735 2687 -3 -141 47 C ATOM 4705 OH TYR A 140 1.126 74.705 53.116 1.00 23.60 O ANISOU 4705 OH TYR B 140 3270 2935 2761 109 -111 -46 O ATOM 4706 N HIS A 141 4.750 74.474 57.873 1.00 16.51 N ANISOU 4706 N HIS B 141 2202 2018 2053 136 -99 30 N ATOM 4707 CA HIS A 141 6.041 74.932 57.382 1.00 16.28 C ANISOU 4707 CA HIS B 141 2225 1970 1990 40 -72 44 C ATOM 4708 C HIS A 141 5.890 75.551 55.996 1.00 17.55 C ANISOU 4708 C HIS B 141 2359 2131 2175 67 -69 65 C ATOM 4709 O HIS A 141 5.223 74.972 55.127 1.00 17.34 O ANISOU 4709 O HIS B 141 2411 1949 2228 83 -83 59 O ATOM 4710 CB HIS A 141 6.970 73.727 57.242 1.00 15.84 C ANISOU 4710 CB HIS B 141 2144 1992 1883 61 -96 -11 C ATOM 4711 CG HIS A 141 7.474 73.192 58.539 1.00 14.62 C ANISOU 4711 CG HIS B 141 2126 1576 1851 -20 -7 14 C ATOM 4712 ND1 HIS A 141 6.726 72.371 59.362 1.00 15.94 N ANISOU 4712 ND1 HIS B 141 2227 1934 1893 35 -75 27 N ATOM 4713 CD2 HIS A 141 8.664 73.367 59.155 1.00 12.89 C ANISOU 4713 CD2 HIS B 141 1833 1494 1567 102 18 -153 C ATOM 4714 CE1 HIS A 141 7.439 72.072 60.433 1.00 13.12 C ANISOU 4714 CE1 HIS B 141 1911 1441 1631 -24 50 7 C ATOM 4715 NE2 HIS A 141 8.618 72.661 60.331 1.00 14.21 N ANISOU 4715 NE2 HIS B 141 2104 1315 1980 -3 -29 -73 N ATOM 4716 N GLN A 142 6.551 76.682 55.759 1.00 18.69 N ANISOU 4716 N GLN B 142 2495 2255 2351 27 -38 41 N ATOM 4717 CA GLN A 142 6.509 77.275 54.414 1.00 20.47 C ANISOU 4717 CA GLN B 142 2683 2579 2516 44 -3 43 C ATOM 4718 C GLN A 142 6.996 76.250 53.384 1.00 21.08 C ANISOU 4718 C GLN B 142 2780 2640 2588 60 -3 21 C ATOM 4719 O GLN A 142 7.976 75.540 53.627 1.00 21.20 O ANISOU 4719 O GLN B 142 2839 2653 2561 114 -31 56 O ATOM 4720 CB GLN A 142 7.381 78.529 54.314 1.00 20.94 C ANISOU 4720 CB GLN B 142 2752 2593 2608 59 20 54 C ATOM 4721 CG GLN A 142 7.268 79.186 52.940 1.00 23.41 C ANISOU 4721 CG GLN B 142 3024 2949 2921 54 3 96 C ATOM 4722 CD GLN A 142 8.046 80.473 52.804 1.00 27.39 C ANISOU 4722 CD GLN B 142 3524 3406 3477 -10 -14 69 C ATOM 4723 OE1 GLN A 142 9.141 80.629 53.361 1.00 28.54 O ANISOU 4723 OE1 GLN B 142 3655 3554 3633 -77 -147 32 O ATOM 4724 NE2 GLN A 142 7.492 81.401 52.026 1.00 28.61 N ANISOU 4724 NE2 GLN B 142 3738 3444 3689 58 -40 144 N ATOM 4725 N SER A 143 6.326 76.180 52.235 1.00 22.47 N ANISOU 4725 N SER B 143 2950 2847 2739 53 -19 26 N ATOM 4726 CA SER A 143 6.796 75.337 51.115 1.00 24.21 C ANISOU 4726 CA SER B 143 3145 3060 2994 19 -28 0 C ATOM 4727 C SER A 143 8.214 75.714 50.677 1.00 25.24 C ANISOU 4727 C SER B 143 3263 3194 3132 5 12 0 C ATOM 4728 O SER A 143 8.572 76.890 50.639 1.00 25.81 O ANISOU 4728 O SER B 143 3362 3269 3173 -69 57 60 O ATOM 4729 CB SER A 143 5.833 75.442 49.921 1.00 24.27 C ANISOU 4729 CB SER B 143 3141 3108 2972 18 -48 -4 C ATOM 4730 OG SER A 143 4.624 74.768 50.205 1.00 24.57 O ANISOU 4730 OG SER B 143 3137 3126 3070 31 -129 -6 O ATOM 4731 N ARG A 144 9.029 74.716 50.366 1.00 26.95 N ANISOU 4731 N ARG B 144 3448 3432 3357 6 -14 6 N ATOM 4732 CA ARG A 144 10.394 74.971 49.926 1.00 28.13 C ANISOU 4732 CA ARG B 144 3578 3575 3535 29 16 5 C ATOM 4733 C ARG A 144 10.511 74.707 48.438 1.00 29.04 C ANISOU 4733 C ARG B 144 3685 3718 3627 29 12 35 C ATOM 4734 O ARG A 144 11.153 75.481 47.731 1.00 30.21 O ANISOU 4734 O ARG B 144 3812 3885 3781 41 43 24 O ATOM 4735 CB ARG A 144 11.390 74.113 50.714 1.00 28.64 C ANISOU 4735 CB ARG B 144 3634 3671 3577 35 2 4 C ATOM 4736 CG ARG A 144 11.578 74.532 52.167 1.00 28.88 C ANISOU 4736 CG ARG B 144 3692 3652 3627 50 -14 13 C ATOM 4737 CD ARG A 144 12.430 73.537 52.965 1.00 29.26 C ANISOU 4737 CD ARG B 144 3794 3681 3640 95 -19 47 C ATOM 4738 NE ARG A 144 12.099 73.568 54.394 1.00 28.67 N ANISOU 4738 NE ARG B 144 3688 3633 3572 26 -14 104 N ATOM 4739 CZ ARG A 144 12.472 72.641 55.267 1.00 28.61 C ANISOU 4739 CZ ARG B 144 3683 3634 3554 67 -12 44 C ATOM 4740 NH1 ARG A 144 13.207 71.606 54.871 1.00 28.32 N ANISOU 4740 NH1 ARG B 144 3712 3542 3503 20 -8 83 N ATOM 4741 NH2 ARG A 144 12.115 72.750 56.545 1.00 27.95 N ANISOU 4741 NH2 ARG B 144 3531 3480 3609 92 -80 51 N ATOM 4742 N THR A 152 8.898 83.984 50.569 1.00 36.33 N ANISOU 4742 N THR B 152 4596 4583 4624 0 -19 11 N ATOM 4743 CA THR A 152 7.678 84.775 50.427 1.00 36.26 C ANISOU 4743 CA THR B 152 4597 4588 4591 -7 -8 20 C ATOM 4744 C THR A 152 6.448 83.864 50.456 1.00 35.82 C ANISOU 4744 C THR B 152 4570 4531 4509 -3 -7 7 C ATOM 4745 O THR A 152 6.276 83.027 49.566 1.00 36.24 O ANISOU 4745 O THR B 152 4645 4581 4543 -31 -21 2 O ATOM 4746 CB THR A 152 7.721 85.565 49.135 1.00 36.46 C ANISOU 4746 CB THR B 152 4632 4628 4590 3 -3 25 C ATOM 4747 N TRP A 153 5.614 84.012 51.489 1.00 34.90 N ANISOU 4747 N TRP B 153 4412 4412 4436 3 -17 9 N ATOM 4748 CA TRP A 153 4.473 83.121 51.703 1.00 33.49 C ANISOU 4748 CA TRP B 153 4260 4202 4262 18 -27 26 C ATOM 4749 C TRP A 153 3.409 83.374 50.646 1.00 33.65 C ANISOU 4749 C TRP B 153 4269 4213 4301 29 -31 15 C ATOM 4750 O TRP A 153 2.924 84.493 50.509 1.00 34.10 O ANISOU 4750 O TRP B 153 4333 4216 4407 75 -36 16 O ATOM 4751 CB TRP A 153 3.881 83.315 53.103 1.00 32.94 C ANISOU 4751 CB TRP B 153 4189 4132 4194 21 -41 30 C ATOM 4752 CG TRP A 153 4.649 82.599 54.175 1.00 29.82 C ANISOU 4752 CG TRP B 153 3828 3716 3783 -13 -47 21 C ATOM 4753 CD1 TRP A 153 5.885 82.920 54.636 1.00 28.80 C ANISOU 4753 CD1 TRP B 153 3751 3579 3612 41 -73 57 C ATOM 4754 CD2 TRP A 153 4.240 81.428 54.894 1.00 26.81 C ANISOU 4754 CD2 TRP B 153 3376 3440 3369 21 -45 31 C ATOM 4755 NE1 TRP A 153 6.273 82.028 55.609 1.00 26.89 N ANISOU 4755 NE1 TRP B 153 3548 3330 3338 11 -113 33 N ATOM 4756 CE2 TRP A 153 5.276 81.107 55.791 1.00 26.17 C ANISOU 4756 CE2 TRP B 153 3392 3257 3292 -18 -84 43 C ATOM 4757 CE3 TRP A 153 3.088 80.625 54.880 1.00 24.87 C ANISOU 4757 CE3 TRP B 153 3248 3089 3111 32 -177 53 C ATOM 4758 CZ2 TRP A 153 5.205 80.009 56.658 1.00 25.06 C ANISOU 4758 CZ2 TRP B 153 3251 3148 3119 -29 -91 118 C ATOM 4759 CZ3 TRP A 153 3.012 79.534 55.743 1.00 24.29 C ANISOU 4759 CZ3 TRP B 153 3067 3104 3057 5 -110 -5 C ATOM 4760 CH2 TRP A 153 4.066 79.240 56.623 1.00 24.29 C ANISOU 4760 CH2 TRP B 153 3174 2994 3061 97 -152 99 C ATOM 4761 N GLY A 154 3.069 82.343 49.886 1.00 33.14 N ANISOU 4761 N GLY B 154 4206 4156 4227 22 -28 19 N ATOM 4762 CA GLY A 154 2.117 82.479 48.794 1.00 32.88 C ANISOU 4762 CA GLY B 154 4166 4150 4175 10 -27 18 C ATOM 4763 C GLY A 154 0.761 81.914 49.154 1.00 32.68 C ANISOU 4763 C GLY B 154 4128 4169 4116 19 -28 13 C ATOM 4764 O GLY A 154 0.569 81.369 50.250 1.00 32.46 O ANISOU 4764 O GLY B 154 4125 4155 4052 45 -65 50 O ATOM 4765 N GLU A 155 -0.172 82.010 48.208 1.00 32.27 N ANISOU 4765 N GLU B 155 4103 4122 4035 39 -52 16 N ATOM 4766 CA GLU A 155 -1.568 81.646 48.440 1.00 32.17 C ANISOU 4766 CA GLU B 155 4095 4111 4016 19 -54 7 C ATOM 4767 C GLU A 155 -1.822 80.176 48.768 1.00 31.26 C ANISOU 4767 C GLU B 155 3982 4031 3864 41 -66 1 C ATOM 4768 O GLU A 155 -2.704 79.872 49.562 1.00 31.06 O ANISOU 4768 O GLU B 155 3961 4033 3806 21 -111 5 O ATOM 4769 CB GLU A 155 -2.429 82.051 47.234 1.00 32.60 C ANISOU 4769 CB GLU B 155 4149 4157 4080 38 -54 12 C ATOM 4770 CG GLU A 155 -2.535 83.557 47.041 1.00 34.73 C ANISOU 4770 CG GLU B 155 4450 4364 4381 32 -48 12 C ATOM 4771 CD GLU A 155 -3.144 84.264 48.244 1.00 37.35 C ANISOU 4771 CD GLU B 155 4780 4740 4671 29 -6 -21 C ATOM 4772 OE1 GLU A 155 -4.252 83.861 48.677 1.00 38.91 O ANISOU 4772 OE1 GLU B 155 4983 4928 4870 -37 12 -3 O ATOM 4773 OE2 GLU A 155 -2.510 85.220 48.755 1.00 38.51 O ANISOU 4773 OE2 GLU B 155 4948 4787 4894 3 -110 -20 O ATOM 4774 N LYS A 156 -1.083 79.261 48.142 1.00 30.71 N ANISOU 4774 N LYS B 156 3895 3974 3796 24 -75 15 N ATOM 4775 CA LYS A 156 -1.253 77.852 48.438 1.00 30.00 C ANISOU 4775 CA LYS B 156 3812 3866 3720 18 -42 13 C ATOM 4776 C LYS A 156 -1.012 77.600 49.935 1.00 29.57 C ANISOU 4776 C LYS B 156 3742 3810 3680 12 -36 33 C ATOM 4777 O LYS A 156 -1.825 76.949 50.585 1.00 30.19 O ANISOU 4777 O LYS B 156 3798 3949 3722 9 -59 42 O ATOM 4778 CB LYS A 156 -0.320 76.994 47.579 1.00 30.29 C ANISOU 4778 CB LYS B 156 3837 3910 3762 7 -23 6 C ATOM 4779 N ASP A 157 0.084 78.136 50.472 1.00 28.19 N ANISOU 4779 N ASP B 157 3610 3588 3512 6 -27 34 N ATOM 4780 CA ASP A 157 0.430 77.942 51.886 1.00 27.15 C ANISOU 4780 CA ASP B 157 3454 3460 3400 16 -30 19 C ATOM 4781 C ASP A 157 -0.558 78.653 52.813 1.00 27.04 C ANISOU 4781 C ASP B 157 3446 3425 3401 22 -65 6 C ATOM 4782 O ASP A 157 -1.084 78.049 53.744 1.00 27.06 O ANISOU 4782 O ASP B 157 3394 3465 3423 18 -86 23 O ATOM 4783 CB ASP A 157 1.855 78.418 52.178 1.00 26.77 C ANISOU 4783 CB ASP B 157 3435 3395 3337 54 -30 46 C ATOM 4784 CG ASP A 157 2.923 77.439 51.697 1.00 26.36 C ANISOU 4784 CG ASP B 157 3414 3377 3224 27 -36 -5 C ATOM 4785 OD1 ASP A 157 2.645 76.228 51.546 1.00 22.59 O ANISOU 4785 OD1 ASP B 157 3038 2809 2736 221 -203 64 O ATOM 4786 OD2 ASP A 157 4.076 77.854 51.475 1.00 26.91 O ANISOU 4786 OD2 ASP B 157 3441 3453 3330 41 46 -33 O ATOM 4787 N LEU A 158 -0.824 79.928 52.547 1.00 26.95 N ANISOU 4787 N LEU B 158 3426 3427 3384 43 -78 7 N ATOM 4788 CA LEU A 158 -1.767 80.695 53.372 1.00 26.42 C ANISOU 4788 CA LEU B 158 3387 3330 3318 49 -45 11 C ATOM 4789 C LEU A 158 -3.151 80.071 53.423 1.00 26.23 C ANISOU 4789 C LEU B 158 3385 3284 3295 75 -41 25 C ATOM 4790 O LEU A 158 -3.781 80.041 54.469 1.00 25.52 O ANISOU 4790 O LEU B 158 3330 3134 3233 146 -58 67 O ATOM 4791 CB LEU A 158 -1.879 82.135 52.874 1.00 26.62 C ANISOU 4791 CB LEU B 158 3435 3342 3337 34 -42 21 C ATOM 4792 CG LEU A 158 -0.620 82.973 53.070 1.00 27.05 C ANISOU 4792 CG LEU B 158 3436 3417 3421 39 -45 33 C ATOM 4793 CD1 LEU A 158 -0.773 84.344 52.415 1.00 27.86 C ANISOU 4793 CD1 LEU B 158 3597 3409 3578 -3 -65 57 C ATOM 4794 CD2 LEU A 158 -0.303 83.116 54.562 1.00 27.34 C ANISOU 4794 CD2 LEU B 158 3507 3417 3463 37 -77 2 C ATOM 4795 N ASN A 159 -3.611 79.554 52.289 1.00 26.38 N ANISOU 4795 N ASN B 159 3378 3329 3316 58 -68 27 N ATOM 4796 CA ASN A 159 -4.919 78.918 52.214 1.00 27.05 C ANISOU 4796 CA ASN B 159 3462 3428 3387 16 -47 33 C ATOM 4797 C ASN A 159 -5.016 77.667 53.077 1.00 26.52 C ANISOU 4797 C ASN B 159 3396 3344 3334 21 -41 9 C ATOM 4798 O ASN A 159 -6.049 77.434 53.707 1.00 27.23 O ANISOU 4798 O ASN B 159 3520 3444 3381 3 -84 29 O ATOM 4799 CB ASN A 159 -5.301 78.607 50.759 1.00 27.43 C ANISOU 4799 CB ASN B 159 3527 3473 3422 38 -59 19 C ATOM 4800 CG ASN A 159 -5.842 79.830 50.017 1.00 28.73 C ANISOU 4800 CG ASN B 159 3679 3666 3572 50 -69 78 C ATOM 4801 OD1 ASN A 159 -5.830 79.872 48.777 1.00 32.06 O ANISOU 4801 OD1 ASN B 159 4064 4305 3812 141 -55 64 O ATOM 4802 ND2 ASN A 159 -6.317 80.822 50.765 1.00 28.75 N ANISOU 4802 ND2 ASN B 159 3504 3820 3600 151 -92 130 N ATOM 4803 N LYS A 160 -3.945 76.878 53.116 1.00 26.06 N ANISOU 4803 N LYS B 160 3334 3320 3247 15 -46 12 N ATOM 4804 CA LYS A 160 -3.925 75.682 53.948 1.00 25.20 C ANISOU 4804 CA LYS B 160 3205 3218 3150 54 -44 0 C ATOM 4805 C LYS A 160 -3.928 76.063 55.436 1.00 24.11 C ANISOU 4805 C LYS B 160 3047 3086 3028 87 -59 26 C ATOM 4806 O LYS A 160 -4.640 75.458 56.230 1.00 23.61 O ANISOU 4806 O LYS B 160 3004 3092 2871 136 -126 46 O ATOM 4807 CB LYS A 160 -2.719 74.787 53.597 1.00 25.78 C ANISOU 4807 CB LYS B 160 3271 3266 3257 44 -28 -17 C ATOM 4808 CG LYS A 160 -2.854 74.040 52.249 1.00 27.37 C ANISOU 4808 CG LYS B 160 3476 3500 3422 47 -3 -43 C ATOM 4809 CD LYS A 160 -1.490 73.548 51.763 1.00 29.93 C ANISOU 4809 CD LYS B 160 3772 3818 3780 12 -37 -10 C ATOM 4810 CE LYS A 160 -1.573 72.487 50.678 1.00 30.57 C ANISOU 4810 CE LYS B 160 3867 3871 3876 24 -55 5 C ATOM 4811 NZ LYS A 160 -1.339 71.108 51.205 1.00 30.96 N ANISOU 4811 NZ LYS B 160 3799 3956 4007 -36 -69 -82 N ATOM 4812 N VAL A 161 -3.153 77.081 55.795 1.00 23.36 N ANISOU 4812 N VAL B 161 2950 3019 2905 119 -69 22 N ATOM 4813 CA VAL A 161 -3.124 77.600 57.163 1.00 22.96 C ANISOU 4813 CA VAL B 161 2874 2907 2941 124 -57 5 C ATOM 4814 C VAL A 161 -4.544 78.017 57.574 1.00 22.50 C ANISOU 4814 C VAL B 161 2822 2825 2902 158 -76 8 C ATOM 4815 O VAL A 161 -5.038 77.637 58.649 1.00 20.89 O ANISOU 4815 O VAL B 161 2604 2554 2779 300 -208 37 O ATOM 4816 CB VAL A 161 -2.081 78.744 57.287 1.00 23.21 C ANISOU 4816 CB VAL B 161 2922 2925 2971 120 -22 -15 C ATOM 4817 CG1 VAL A 161 -2.222 79.538 58.601 1.00 22.75 C ANISOU 4817 CG1 VAL B 161 2861 2897 2885 102 -80 32 C ATOM 4818 CG2 VAL A 161 -0.669 78.172 57.153 1.00 23.59 C ANISOU 4818 CG2 VAL B 161 2934 3041 2985 91 -35 39 C ATOM 4819 N LYS A 162 -5.225 78.740 56.678 1.00 23.12 N ANISOU 4819 N LYS B 162 2911 2959 2914 140 -90 18 N ATOM 4820 CA LYS A 162 -6.568 79.243 56.973 1.00 23.60 C ANISOU 4820 CA LYS B 162 2938 3033 2994 102 -74 32 C ATOM 4821 C LYS A 162 -7.591 78.133 57.214 1.00 23.51 C ANISOU 4821 C LYS B 162 2878 3105 2947 114 -130 39 C ATOM 4822 O LYS A 162 -8.402 78.230 58.136 1.00 24.01 O ANISOU 4822 O LYS B 162 2848 3268 3005 170 -151 25 O ATOM 4823 CB LYS A 162 -7.047 80.195 55.875 1.00 23.98 C ANISOU 4823 CB LYS B 162 3008 3097 3004 85 -60 49 C ATOM 4824 CG LYS A 162 -6.314 81.535 55.858 1.00 24.76 C ANISOU 4824 CG LYS B 162 3132 3144 3130 87 -60 6 C ATOM 4825 CD LYS A 162 -6.695 82.374 54.615 1.00 26.28 C ANISOU 4825 CD LYS B 162 3414 3313 3258 59 -3 54 C ATOM 4826 CE LYS A 162 -5.733 83.534 54.381 1.00 26.97 C ANISOU 4826 CE LYS B 162 3440 3414 3390 104 4 -7 C ATOM 4827 NZ LYS A 162 -6.157 84.375 53.199 1.00 27.85 N ANISOU 4827 NZ LYS B 162 3643 3512 3424 129 -53 -31 N ATOM 4828 N LYS A 163 -7.529 77.065 56.426 1.00 22.80 N ANISOU 4828 N LYS B 163 2826 2987 2849 101 -134 29 N ATOM 4829 CA LYS A 163 -8.457 75.949 56.603 1.00 22.45 C ANISOU 4829 CA LYS B 163 2795 2935 2796 37 -81 21 C ATOM 4830 C LYS A 163 -8.218 75.202 57.902 1.00 21.01 C ANISOU 4830 C LYS B 163 2580 2744 2658 26 -50 -7 C ATOM 4831 O LYS A 163 -9.164 74.804 58.575 1.00 20.79 O ANISOU 4831 O LYS B 163 2560 2753 2586 -11 -59 -12 O ATOM 4832 CB LYS A 163 -8.415 74.955 55.431 1.00 23.09 C ANISOU 4832 CB LYS B 163 2928 2950 2894 97 -89 24 C ATOM 4833 CG LYS A 163 -9.674 74.074 55.364 1.00 26.04 C ANISOU 4833 CG LYS B 163 3336 3342 3214 -18 -70 6 C ATOM 4834 CD LYS A 163 -9.630 73.097 54.190 1.00 29.58 C ANISOU 4834 CD LYS B 163 3818 3697 3722 14 -54 -30 C ATOM 4835 CE LYS A 163 -10.547 71.883 54.411 1.00 31.69 C ANISOU 4835 CE LYS B 163 4011 3964 4064 20 0 16 C ATOM 4836 NZ LYS A 163 -12.008 72.149 54.231 1.00 33.00 N ANISOU 4836 NZ LYS B 163 4087 4197 4253 56 20 27 N ATOM 4837 N LEU A 164 -6.951 75.028 58.267 1.00 19.46 N ANISOU 4837 N LEU B 164 2373 2540 2478 41 -4 -7 N ATOM 4838 CA LEU A 164 -6.619 74.342 59.504 1.00 18.76 C ANISOU 4838 CA LEU B 164 2268 2439 2421 71 -54 -9 C ATOM 4839 C LEU A 164 -7.196 75.091 60.700 1.00 18.68 C ANISOU 4839 C LEU B 164 2243 2420 2435 81 -84 -26 C ATOM 4840 O LEU A 164 -7.752 74.480 61.615 1.00 18.67 O ANISOU 4840 O LEU B 164 2188 2380 2523 212 -176 -38 O ATOM 4841 CB LEU A 164 -5.105 74.134 59.627 1.00 18.18 C ANISOU 4841 CB LEU B 164 2196 2383 2329 32 -72 -6 C ATOM 4842 CG LEU A 164 -4.518 73.055 58.696 1.00 18.34 C ANISOU 4842 CG LEU B 164 2231 2431 2306 48 -77 -8 C ATOM 4843 CD1 LEU A 164 -3.009 73.183 58.646 1.00 17.88 C ANISOU 4843 CD1 LEU B 164 2118 2447 2229 204 -106 118 C ATOM 4844 CD2 LEU A 164 -4.941 71.667 59.140 1.00 18.59 C ANISOU 4844 CD2 LEU B 164 2292 2459 2310 162 -141 15 C ATOM 4845 N ILE A 165 -7.106 76.414 60.662 1.00 19.66 N ANISOU 4845 N ILE B 165 2376 2538 2554 128 -104 -20 N ATOM 4846 CA ILE A 165 -7.702 77.252 61.704 1.00 20.71 C ANISOU 4846 CA ILE B 165 2514 2659 2694 86 -84 -63 C ATOM 4847 C ILE A 165 -9.235 77.106 61.766 1.00 21.43 C ANISOU 4847 C ILE B 165 2620 2729 2791 98 -71 -55 C ATOM 4848 O ILE A 165 -9.813 76.952 62.850 1.00 20.68 O ANISOU 4848 O ILE B 165 2442 2690 2725 109 -193 -67 O ATOM 4849 CB ILE A 165 -7.280 78.722 61.522 1.00 21.07 C ANISOU 4849 CB ILE B 165 2577 2676 2750 88 -90 -65 C ATOM 4850 CG1 ILE A 165 -5.762 78.873 61.746 1.00 20.27 C ANISOU 4850 CG1 ILE B 165 2410 2584 2705 147 -1 -91 C ATOM 4851 CG2 ILE A 165 -8.019 79.601 62.527 1.00 21.66 C ANISOU 4851 CG2 ILE B 165 2549 2846 2834 137 -26 -152 C ATOM 4852 CD1 ILE A 165 -5.129 80.172 61.280 1.00 20.15 C ANISOU 4852 CD1 ILE B 165 2402 2698 2555 219 71 -132 C ATOM 4853 N GLU A 166 -9.859 77.120 60.591 1.00 22.66 N ANISOU 4853 N GLU B 166 2807 2912 2890 97 -57 -46 N ATOM 4854 CA GLU A 166 -11.307 76.917 60.435 1.00 23.61 C ANISOU 4854 CA GLU B 166 2927 3008 3035 61 -33 -49 C ATOM 4855 C GLU A 166 -11.739 75.612 61.070 1.00 22.83 C ANISOU 4855 C GLU B 166 2776 2923 2973 66 -27 -54 C ATOM 4856 O GLU A 166 -12.741 75.568 61.779 1.00 23.05 O ANISOU 4856 O GLU B 166 2677 2974 3106 169 -74 -109 O ATOM 4857 CB GLU A 166 -11.705 76.891 58.952 1.00 25.01 C ANISOU 4857 CB GLU B 166 3144 3199 3158 62 -14 -31 C ATOM 4858 CG GLU A 166 -12.244 78.187 58.368 1.00 29.44 C ANISOU 4858 CG GLU B 166 3783 3701 3703 66 -24 0 C ATOM 4859 CD GLU A 166 -13.147 77.930 57.170 1.00 33.99 C ANISOU 4859 CD GLU B 166 4317 4406 4188 53 -113 -4 C ATOM 4860 OE1 GLU A 166 -12.702 77.234 56.218 1.00 34.94 O ANISOU 4860 OE1 GLU B 166 4559 4550 4167 68 -94 -10 O ATOM 4861 OE2 GLU A 166 -14.303 78.408 57.192 1.00 36.66 O ANISOU 4861 OE2 GLU B 166 4528 4799 4599 123 -45 -28 O ATOM 4862 N MET A 167 -10.967 74.548 60.826 1.00 21.60 N ANISOU 4862 N MET B 167 2598 2775 2832 57 -55 -36 N ATOM 4863 CA MET A 167 -11.245 73.220 61.385 1.00 21.47 C ANISOU 4863 CA MET B 167 2592 2783 2781 72 -56 -26 C ATOM 4864 C MET A 167 -11.190 73.142 62.915 1.00 20.63 C ANISOU 4864 C MET B 167 2448 2693 2697 112 -28 -29 C ATOM 4865 O MET A 167 -11.757 72.221 63.527 1.00 20.68 O ANISOU 4865 O MET B 167 2371 2821 2663 135 -62 -28 O ATOM 4866 CB MET A 167 -10.260 72.197 60.796 1.00 21.53 C ANISOU 4866 CB MET B 167 2659 2754 2767 96 -58 -28 C ATOM 4867 CG MET A 167 -10.497 71.885 59.328 1.00 22.15 C ANISOU 4867 CG MET B 167 2720 2805 2891 57 -104 -99 C ATOM 4868 SD MET A 167 -9.349 70.656 58.708 1.00 25.42 S ANISOU 4868 SD MET B 167 2872 3361 3423 131 -102 -333 S ATOM 4869 CE MET A 167 -9.909 69.239 59.600 1.00 24.20 C ANISOU 4869 CE MET B 167 2918 3004 3269 254 -74 -196 C ATOM 4870 N GLY A 168 -10.475 74.079 63.522 1.00 20.15 N ANISOU 4870 N GLY B 168 2355 2674 2625 118 -65 -4 N ATOM 4871 CA GLY A 168 -10.360 74.162 64.975 1.00 19.12 C ANISOU 4871 CA GLY B 168 2205 2527 2532 132 -65 -10 C ATOM 4872 C GLY A 168 -8.942 73.973 65.519 1.00 18.08 C ANISOU 4872 C GLY B 168 2093 2362 2414 184 -78 6 C ATOM 4873 O GLY A 168 -8.779 73.722 66.713 1.00 18.03 O ANISOU 4873 O GLY B 168 1888 2402 2561 337 -184 -10 O ATOM 4874 N PHE A 169 -7.943 74.136 64.655 1.00 16.90 N ANISOU 4874 N PHE B 169 1962 2140 2317 198 -86 -20 N ATOM 4875 CA PHE A 169 -6.525 74.098 65.064 1.00 16.48 C ANISOU 4875 CA PHE B 169 1943 2132 2184 142 -68 -27 C ATOM 4876 C PHE A 169 -5.966 75.445 65.476 1.00 16.59 C ANISOU 4876 C PHE B 169 2036 2090 2175 154 -59 -14 C ATOM 4877 O PHE A 169 -6.191 76.467 64.807 1.00 17.43 O ANISOU 4877 O PHE B 169 2180 2057 2383 234 -134 -6 O ATOM 4878 CB PHE A 169 -5.619 73.534 63.938 1.00 16.16 C ANISOU 4878 CB PHE B 169 1813 2150 2176 158 -44 -25 C ATOM 4879 CG PHE A 169 -5.698 72.029 63.767 1.00 15.96 C ANISOU 4879 CG PHE B 169 1768 2157 2136 125 -104 -68 C ATOM 4880 CD1 PHE A 169 -4.933 71.186 64.565 1.00 16.59 C ANISOU 4880 CD1 PHE B 169 1849 2282 2170 162 -79 -25 C ATOM 4881 CD2 PHE A 169 -6.534 71.451 62.795 1.00 15.81 C ANISOU 4881 CD2 PHE B 169 1811 2044 2151 229 -117 -147 C ATOM 4882 CE1 PHE A 169 -4.989 69.814 64.401 1.00 16.70 C ANISOU 4882 CE1 PHE B 169 1865 2133 2345 88 -157 -61 C ATOM 4883 CE2 PHE A 169 -6.606 70.058 62.621 1.00 15.65 C ANISOU 4883 CE2 PHE B 169 1834 1996 2114 120 -123 -86 C ATOM 4884 CZ PHE A 169 -5.848 69.241 63.438 1.00 16.85 C ANISOU 4884 CZ PHE B 169 2123 2006 2270 210 -107 -44 C ATOM 4885 N ARG A 170 -5.199 75.420 66.563 1.00 16.54 N ANISOU 4885 N ARG B 170 1985 2094 2202 144 -42 -45 N ATOM 4886 CA ARG A 170 -4.239 76.450 66.887 1.00 15.99 C ANISOU 4886 CA ARG B 170 1956 1953 2165 149 -22 -63 C ATOM 4887 C ARG A 170 -2.981 76.153 66.064 1.00 15.97 C ANISOU 4887 C ARG B 170 1952 1940 2174 107 -86 -55 C ATOM 4888 O ARG A 170 -2.262 75.180 66.350 1.00 15.58 O ANISOU 4888 O ARG B 170 1929 1709 2280 287 -126 -66 O ATOM 4889 CB ARG A 170 -3.959 76.454 68.395 1.00 15.82 C ANISOU 4889 CB ARG B 170 1867 1999 2143 96 -25 -53 C ATOM 4890 CG ARG A 170 -5.014 77.248 69.232 1.00 17.09 C ANISOU 4890 CG ARG B 170 2046 2217 2229 144 43 -100 C ATOM 4891 CD ARG A 170 -5.049 76.896 70.717 1.00 15.46 C ANISOU 4891 CD ARG B 170 1806 1989 2079 83 77 -20 C ATOM 4892 NE ARG A 170 -5.295 75.473 70.929 1.00 16.07 N ANISOU 4892 NE ARG B 170 1897 2069 2140 204 -12 -92 N ATOM 4893 CZ ARG A 170 -4.640 74.698 71.798 1.00 17.98 C ANISOU 4893 CZ ARG B 170 2082 2317 2432 52 -41 -50 C ATOM 4894 NH1 ARG A 170 -3.719 75.187 72.614 1.00 18.10 N ANISOU 4894 NH1 ARG B 170 2086 2219 2572 174 -106 -342 N ATOM 4895 NH2 ARG A 170 -4.927 73.410 71.859 1.00 17.27 N ANISOU 4895 NH2 ARG B 170 1944 2157 2460 157 -126 -205 N ATOM 4896 N VAL A 171 -2.780 76.941 65.018 1.00 15.48 N ANISOU 4896 N VAL B 171 1911 1831 2140 63 -86 -43 N ATOM 4897 CA VAL A 171 -1.734 76.721 64.024 1.00 16.12 C ANISOU 4897 CA VAL B 171 2034 1956 2134 56 -82 -20 C ATOM 4898 C VAL A 171 -0.499 77.568 64.293 1.00 16.23 C ANISOU 4898 C VAL B 171 2063 1939 2164 97 -96 -24 C ATOM 4899 O VAL A 171 -0.591 78.795 64.415 1.00 16.84 O ANISOU 4899 O VAL B 171 2169 2000 2226 176 -184 5 O ATOM 4900 CB VAL A 171 -2.270 77.023 62.596 1.00 15.91 C ANISOU 4900 CB VAL B 171 2042 1870 2129 86 -57 -21 C ATOM 4901 CG1 VAL A 171 -1.157 76.988 61.576 1.00 17.69 C ANISOU 4901 CG1 VAL B 171 2173 2230 2317 12 -102 56 C ATOM 4902 CG2 VAL A 171 -3.401 76.036 62.235 1.00 15.88 C ANISOU 4902 CG2 VAL B 171 1964 1885 2181 158 -133 9 C ATOM 4903 N SER A 172 0.659 76.906 64.410 1.00 16.13 N ANISOU 4903 N SER B 172 2025 1977 2127 123 -76 -68 N ATOM 4904 CA SER A 172 1.941 77.599 64.412 1.00 15.55 C ANISOU 4904 CA SER B 172 2039 1821 2045 134 -33 -3 C ATOM 4905 C SER A 172 2.496 77.531 63.009 1.00 15.13 C ANISOU 4905 C SER B 172 1988 1746 2015 128 -47 2 C ATOM 4906 O SER A 172 2.327 76.524 62.316 1.00 15.24 O ANISOU 4906 O SER B 172 2148 1571 2072 116 -34 -39 O ATOM 4907 CB SER A 172 2.949 76.944 65.379 1.00 15.96 C ANISOU 4907 CB SER B 172 1980 2045 2038 180 -39 0 C ATOM 4908 OG SER A 172 2.409 76.761 66.680 1.00 15.89 O ANISOU 4908 OG SER B 172 1948 2098 1988 336 -41 -8 O ATOM 4909 N VAL A 173 3.156 78.602 62.600 1.00 14.58 N ANISOU 4909 N VAL B 173 1912 1691 1936 101 -45 28 N ATOM 4910 CA VAL A 173 3.786 78.700 61.300 1.00 14.52 C ANISOU 4910 CA VAL B 173 1934 1665 1916 48 -65 50 C ATOM 4911 C VAL A 173 5.278 78.919 61.477 1.00 15.01 C ANISOU 4911 C VAL B 173 2027 1691 1986 -45 -45 63 C ATOM 4912 O VAL A 173 5.715 79.530 62.457 1.00 15.06 O ANISOU 4912 O VAL B 173 2053 1570 2096 -113 -113 71 O ATOM 4913 CB VAL A 173 3.168 79.826 60.428 1.00 14.62 C ANISOU 4913 CB VAL B 173 1994 1645 1915 18 -72 42 C ATOM 4914 CG1 VAL A 173 1.703 79.564 60.183 1.00 13.91 C ANISOU 4914 CG1 VAL B 173 1870 1557 1858 147 -58 103 C ATOM 4915 CG2 VAL A 173 3.366 81.181 61.071 1.00 14.43 C ANISOU 4915 CG2 VAL B 173 1974 1589 1917 -13 -87 17 C ATOM 4916 N THR A 174 6.044 78.403 60.529 1.00 16.14 N ANISOU 4916 N THR B 174 2161 1857 2113 -63 -29 38 N ATOM 4917 CA THR A 174 7.499 78.512 60.543 1.00 17.47 C ANISOU 4917 CA THR B 174 2272 2127 2236 1 -18 52 C ATOM 4918 C THR A 174 8.053 78.433 59.137 1.00 18.74 C ANISOU 4918 C THR B 174 2463 2273 2382 20 -16 77 C ATOM 4919 O THR A 174 7.432 77.824 58.258 1.00 18.07 O ANISOU 4919 O THR B 174 2346 2206 2311 -7 -41 139 O ATOM 4920 CB THR A 174 8.142 77.413 61.426 1.00 17.06 C ANISOU 4920 CB THR B 174 2216 2088 2179 9 -11 26 C ATOM 4921 OG1 THR A 174 9.524 77.713 61.642 1.00 17.82 O ANISOU 4921 OG1 THR B 174 2226 2261 2280 -23 -26 166 O ATOM 4922 CG2 THR A 174 8.096 76.066 60.753 1.00 17.81 C ANISOU 4922 CG2 THR B 174 2343 2249 2172 38 -83 19 C ATOM 4923 N GLY A 175 9.226 79.045 58.952 1.00 20.68 N ANISOU 4923 N GLY B 175 2640 2563 2652 25 -24 59 N ATOM 4924 CA GLY A 175 9.891 79.133 57.653 1.00 23.13 C ANISOU 4924 CA GLY B 175 2961 2887 2938 33 1 61 C ATOM 4925 C GLY A 175 9.587 80.492 57.036 1.00 25.09 C ANISOU 4925 C GLY B 175 3219 3113 3198 2 -5 56 C ATOM 4926 O GLY A 175 8.434 80.905 57.036 1.00 25.42 O ANISOU 4926 O GLY B 175 3275 3146 3236 17 -1 101 O ATOM 4927 N GLY A 176 10.626 81.183 56.558 1.00 26.93 N ANISOU 4927 N GLY B 176 3449 3377 3404 5 16 58 N ATOM 4928 CA GLY A 176 10.517 82.505 55.924 1.00 28.19 C ANISOU 4928 CA GLY B 176 3631 3512 3566 0 11 30 C ATOM 4929 C GLY A 176 9.826 83.594 56.731 1.00 29.12 C ANISOU 4929 C GLY B 176 3733 3619 3709 -2 0 35 C ATOM 4930 O GLY A 176 9.035 84.378 56.186 1.00 29.30 O ANISOU 4930 O GLY B 176 3771 3597 3763 -18 15 39 O ATOM 4931 N LEU A 177 10.124 83.646 58.028 1.00 29.76 N ANISOU 4931 N LEU B 177 3815 3714 3776 -15 -5 15 N ATOM 4932 CA LEU A 177 9.486 84.600 58.914 1.00 30.48 C ANISOU 4932 CA LEU B 177 3888 3820 3873 -12 -12 19 C ATOM 4933 C LEU A 177 10.465 85.682 59.336 1.00 31.63 C ANISOU 4933 C LEU B 177 4005 3971 4042 -40 -24 4 C ATOM 4934 O LEU A 177 11.551 85.387 59.817 1.00 31.23 O ANISOU 4934 O LEU B 177 3953 3885 4028 -54 -26 2 O ATOM 4935 CB LEU A 177 8.915 83.909 60.148 1.00 30.22 C ANISOU 4935 CB LEU B 177 3837 3814 3832 -11 -25 24 C ATOM 4936 CG LEU A 177 7.764 82.921 59.967 1.00 29.93 C ANISOU 4936 CG LEU B 177 3829 3742 3799 -17 -22 68 C ATOM 4937 CD1 LEU A 177 7.298 82.463 61.351 1.00 29.92 C ANISOU 4937 CD1 LEU B 177 3847 3754 3766 -27 4 3 C ATOM 4938 CD2 LEU A 177 6.592 83.512 59.194 1.00 29.10 C ANISOU 4938 CD2 LEU B 177 3718 3632 3705 -84 -17 105 C ATOM 4939 N SER A 178 10.054 86.932 59.163 1.00 33.36 N ANISOU 4939 N SER B 178 4243 4187 4245 -31 -11 20 N ATOM 4940 CA SER A 178 10.844 88.083 59.592 1.00 34.99 C ANISOU 4940 CA SER B 178 4459 4377 4456 -42 -20 15 C ATOM 4941 C SER A 178 9.906 89.182 60.048 1.00 36.11 C ANISOU 4941 C SER B 178 4592 4522 4604 -20 -16 32 C ATOM 4942 O SER A 178 8.681 89.060 59.910 1.00 36.19 O ANISOU 4942 O SER B 178 4622 4479 4649 -62 -63 66 O ATOM 4943 CB SER A 178 11.751 88.580 58.459 1.00 34.97 C ANISOU 4943 CB SER B 178 4452 4378 4458 -46 -12 13 C ATOM 4944 OG SER A 178 11.000 89.220 57.438 1.00 35.43 O ANISOU 4944 OG SER B 178 4545 4381 4534 -56 -38 59 O ATOM 4945 N VAL A 179 10.461 90.258 60.600 1.00 37.36 N ANISOU 4945 N VAL B 179 4752 4692 4751 -33 -27 16 N ATOM 4946 CA VAL A 179 9.626 91.405 60.972 1.00 38.84 C ANISOU 4946 CA VAL B 179 4926 4888 4942 -7 -6 2 C ATOM 4947 C VAL A 179 8.765 91.870 59.789 1.00 39.40 C ANISOU 4947 C VAL B 179 4988 4969 5011 -12 -14 8 C ATOM 4948 O VAL A 179 7.611 92.249 59.972 1.00 39.85 O ANISOU 4948 O VAL B 179 5012 5024 5104 -15 -4 12 O ATOM 4949 CB VAL A 179 10.443 92.599 61.549 1.00 38.96 C ANISOU 4949 CB VAL B 179 4953 4896 4952 -4 -7 -6 C ATOM 4950 CG1 VAL A 179 10.761 92.366 63.021 1.00 39.36 C ANISOU 4950 CG1 VAL B 179 5020 4944 4988 11 -5 0 C ATOM 4951 CG2 VAL A 179 11.724 92.850 60.751 1.00 39.13 C ANISOU 4951 CG2 VAL B 179 4971 4885 5008 -2 33 -8 C ATOM 4952 N ASP A 180 9.325 91.796 58.582 1.00 40.10 N ANISOU 4952 N ASP B 180 5084 5066 5085 -11 -14 8 N ATOM 4953 CA ASP A 180 8.676 92.319 57.373 1.00 40.55 C ANISOU 4953 CA ASP B 180 5145 5124 5138 -8 -12 9 C ATOM 4954 C ASP A 180 7.647 91.390 56.737 1.00 40.09 C ANISOU 4954 C ASP B 180 5086 5069 5074 9 -10 17 C ATOM 4955 O ASP A 180 6.671 91.857 56.165 1.00 40.28 O ANISOU 4955 O ASP B 180 5113 5103 5088 14 -24 38 O ATOM 4956 CB ASP A 180 9.733 92.719 56.338 1.00 41.06 C ANISOU 4956 CB ASP B 180 5223 5194 5181 -7 6 6 C ATOM 4957 CG ASP A 180 10.380 94.045 56.665 1.00 42.68 C ANISOU 4957 CG ASP B 180 5433 5384 5398 -40 2 13 C ATOM 4958 OD1 ASP A 180 10.701 94.278 57.851 1.00 44.37 O ANISOU 4958 OD1 ASP B 180 5703 5590 5565 -61 -7 12 O ATOM 4959 OD2 ASP A 180 10.580 94.895 55.775 1.00 45.22 O ANISOU 4959 OD2 ASP B 180 5736 5735 5711 -23 41 59 O ATOM 4960 N THR A 181 7.854 90.081 56.837 1.00 39.39 N ANISOU 4960 N THR B 181 4997 4983 4984 11 -12 7 N ATOM 4961 CA THR A 181 6.905 89.134 56.252 1.00 38.32 C ANISOU 4961 CA THR B 181 4860 4851 4847 20 -3 6 C ATOM 4962 C THR A 181 5.699 88.849 57.154 1.00 37.73 C ANISOU 4962 C THR B 181 4806 4769 4760 7 -16 5 C ATOM 4963 O THR A 181 4.785 88.134 56.744 1.00 37.72 O ANISOU 4963 O THR B 181 4814 4753 4764 10 -22 13 O ATOM 4964 CB THR A 181 7.592 87.821 55.808 1.00 38.42 C ANISOU 4964 CB THR B 181 4874 4874 4850 25 -2 3 C ATOM 4965 OG1 THR A 181 8.440 87.329 56.850 1.00 38.30 O ANISOU 4965 OG1 THR B 181 4808 4882 4861 83 2 -3 O ATOM 4966 CG2 THR A 181 8.478 88.066 54.595 1.00 38.14 C ANISOU 4966 CG2 THR B 181 4850 4797 4843 26 14 22 C ATOM 4967 N LEU A 182 5.676 89.417 58.364 1.00 36.81 N ANISOU 4967 N LEU B 182 4671 4648 4666 8 -9 3 N ATOM 4968 CA LEU A 182 4.519 89.255 59.249 1.00 36.07 C ANISOU 4968 CA LEU B 182 4592 4546 4564 13 -22 1 C ATOM 4969 C LEU A 182 3.261 89.893 58.649 1.00 35.57 C ANISOU 4969 C LEU B 182 4521 4490 4502 11 -31 8 C ATOM 4970 O LEU A 182 2.149 89.426 58.916 1.00 34.99 O ANISOU 4970 O LEU B 182 4488 4386 4421 12 -40 24 O ATOM 4971 CB LEU A 182 4.796 89.807 60.657 1.00 36.09 C ANISOU 4971 CB LEU B 182 4572 4558 4581 17 -28 -4 C ATOM 4972 CG LEU A 182 5.706 88.979 61.577 1.00 35.81 C ANISOU 4972 CG LEU B 182 4576 4509 4520 -4 -16 24 C ATOM 4973 CD1 LEU A 182 5.876 89.668 62.924 1.00 35.49 C ANISOU 4973 CD1 LEU B 182 4480 4438 4564 23 -24 28 C ATOM 4974 CD2 LEU A 182 5.187 87.548 61.771 1.00 35.83 C ANISOU 4974 CD2 LEU B 182 4555 4498 4561 -17 -10 2 C ATOM 4975 N LYS A 183 3.463 90.948 57.848 1.00 35.57 N ANISOU 4975 N LYS B 183 4515 4482 4515 -5 -30 13 N ATOM 4976 CA LYS A 183 2.422 91.611 57.035 1.00 35.54 C ANISOU 4976 CA LYS B 183 4500 4490 4513 0 -32 17 C ATOM 4977 C LYS A 183 1.536 90.641 56.277 1.00 35.14 C ANISOU 4977 C LYS B 183 4447 4445 4459 13 -23 33 C ATOM 4978 O LYS A 183 0.325 90.810 56.230 1.00 34.95 O ANISOU 4978 O LYS B 183 4403 4417 4460 22 -45 64 O ATOM 4979 CB LYS A 183 3.071 92.525 55.984 1.00 35.88 C ANISOU 4979 CB LYS B 183 4542 4537 4551 2 -31 10 C ATOM 4980 CG LYS A 183 3.288 93.956 56.439 1.00 36.70 C ANISOU 4980 CG LYS B 183 4655 4605 4682 3 -27 -7 C ATOM 4981 CD LYS A 183 4.284 94.670 55.539 1.00 38.43 C ANISOU 4981 CD LYS B 183 4867 4875 4857 11 0 -4 C ATOM 4982 CE LYS A 183 5.237 95.539 56.353 1.00 39.25 C ANISOU 4982 CE LYS B 183 4974 4965 4974 22 -14 -20 C ATOM 4983 NZ LYS A 183 6.015 94.724 57.339 1.00 39.93 N ANISOU 4983 NZ LYS B 183 5051 5033 5086 16 -9 0 N ATOM 4984 N LEU A 184 2.168 89.635 55.675 1.00 34.50 N ANISOU 4984 N LEU B 184 4368 4382 4355 27 -20 36 N ATOM 4985 CA LEU A 184 1.499 88.659 54.825 1.00 33.90 C ANISOU 4985 CA LEU B 184 4308 4293 4277 24 -15 39 C ATOM 4986 C LEU A 184 0.431 87.855 55.561 1.00 33.37 C ANISOU 4986 C LEU B 184 4255 4234 4190 25 -33 43 C ATOM 4987 O LEU A 184 -0.412 87.215 54.928 1.00 33.17 O ANISOU 4987 O LEU B 184 4245 4214 4142 28 -74 72 O ATOM 4988 CB LEU A 184 2.535 87.704 54.204 1.00 34.15 C ANISOU 4988 CB LEU B 184 4350 4335 4290 13 -16 29 C ATOM 4989 CG LEU A 184 3.713 88.366 53.475 1.00 35.11 C ANISOU 4989 CG LEU B 184 4430 4465 4444 12 -9 32 C ATOM 4990 CD1 LEU A 184 4.571 87.337 52.758 1.00 35.70 C ANISOU 4990 CD1 LEU B 184 4598 4407 4558 53 -22 33 C ATOM 4991 CD2 LEU A 184 3.237 89.440 52.484 1.00 35.69 C ANISOU 4991 CD2 LEU B 184 4504 4550 4505 -22 -26 52 C ATOM 4992 N PHE A 185 0.482 87.884 56.894 1.00 32.59 N ANISOU 4992 N PHE B 185 4147 4127 4107 26 -22 25 N ATOM 4993 CA PHE A 185 -0.431 87.122 57.733 1.00 31.72 C ANISOU 4993 CA PHE B 185 4028 3999 4025 43 -34 35 C ATOM 4994 C PHE A 185 -1.494 88.018 58.370 1.00 31.30 C ANISOU 4994 C PHE B 185 3968 3919 4003 57 -43 49 C ATOM 4995 O PHE A 185 -2.197 87.596 59.297 1.00 30.39 O ANISOU 4995 O PHE B 185 3853 3719 3975 98 -70 130 O ATOM 4996 CB PHE A 185 0.343 86.390 58.839 1.00 31.71 C ANISOU 4996 CB PHE B 185 4031 3994 4022 62 -26 27 C ATOM 4997 CG PHE A 185 1.249 85.293 58.337 1.00 31.20 C ANISOU 4997 CG PHE B 185 3950 3952 3950 26 -43 24 C ATOM 4998 CD1 PHE A 185 0.781 83.992 58.234 1.00 31.20 C ANISOU 4998 CD1 PHE B 185 3962 3982 3909 58 -75 -10 C ATOM 4999 CD2 PHE A 185 2.567 85.557 57.993 1.00 30.63 C ANISOU 4999 CD2 PHE B 185 3883 3923 3829 44 -7 18 C ATOM 5000 CE1 PHE A 185 1.606 82.973 57.790 1.00 30.90 C ANISOU 5000 CE1 PHE B 185 3901 3911 3928 13 -29 -5 C ATOM 5001 CE2 PHE A 185 3.399 84.540 57.545 1.00 30.54 C ANISOU 5001 CE2 PHE B 185 3893 3827 3882 -2 -24 34 C ATOM 5002 CZ PHE A 185 2.917 83.251 57.445 1.00 31.00 C ANISOU 5002 CZ PHE B 185 3908 3942 3926 61 -37 -5 C ATOM 5003 N GLU A 186 -1.601 89.261 57.894 1.00 31.36 N ANISOU 5003 N GLU B 186 3987 3920 4006 39 -57 57 N ATOM 5004 CA GLU A 186 -2.665 90.160 58.349 1.00 31.61 C ANISOU 5004 CA GLU B 186 4027 3942 4041 32 -49 23 C ATOM 5005 C GLU A 186 -4.016 89.472 58.163 1.00 30.71 C ANISOU 5005 C GLU B 186 3932 3804 3932 70 -59 45 C ATOM 5006 O GLU A 186 -4.305 88.957 57.082 1.00 30.67 O ANISOU 5006 O GLU B 186 3927 3764 3961 77 -127 51 O ATOM 5007 CB GLU A 186 -2.638 91.479 57.561 1.00 32.48 C ANISOU 5007 CB GLU B 186 4157 4062 4122 16 -38 46 C ATOM 5008 CG GLU A 186 -1.994 92.643 58.310 1.00 35.66 C ANISOU 5008 CG GLU B 186 4541 4467 4542 -11 -40 -6 C ATOM 5009 CD GLU A 186 -1.722 93.862 57.422 1.00 39.58 C ANISOU 5009 CD GLU B 186 5124 4944 4969 26 -1 54 C ATOM 5010 OE1 GLU A 186 -1.167 93.702 56.305 1.00 41.24 O ANISOU 5010 OE1 GLU B 186 5315 5213 5140 123 32 33 O ATOM 5011 OE2 GLU A 186 -2.047 94.997 57.853 1.00 41.62 O ANISOU 5011 OE2 GLU B 186 5405 5174 5234 53 0 15 O ATOM 5012 N GLY A 187 -4.824 89.433 59.216 1.00 29.86 N ANISOU 5012 N GLY B 187 3789 3666 3887 67 -37 54 N ATOM 5013 CA GLY A 187 -6.154 88.853 59.123 1.00 29.75 C ANISOU 5013 CA GLY B 187 3756 3678 3869 75 -34 55 C ATOM 5014 C GLY A 187 -6.257 87.365 59.410 1.00 29.58 C ANISOU 5014 C GLY B 187 3700 3655 3881 59 -23 58 C ATOM 5015 O GLY A 187 -7.367 86.841 59.562 1.00 29.90 O ANISOU 5015 O GLY B 187 3701 3695 3964 134 -50 91 O ATOM 5016 N VAL A 188 -5.121 86.668 59.471 1.00 28.88 N ANISOU 5016 N VAL B 188 3621 3583 3766 36 -32 66 N ATOM 5017 CA VAL A 188 -5.128 85.249 59.860 1.00 27.59 C ANISOU 5017 CA VAL B 188 3499 3392 3590 60 -29 11 C ATOM 5018 C VAL A 188 -4.813 85.082 61.359 1.00 26.11 C ANISOU 5018 C VAL B 188 3289 3184 3446 95 -27 13 C ATOM 5019 O VAL A 188 -3.931 85.751 61.910 1.00 25.54 O ANISOU 5019 O VAL B 188 3252 3000 3452 192 -86 -10 O ATOM 5020 CB VAL A 188 -4.264 84.318 58.921 1.00 27.91 C ANISOU 5020 CB VAL B 188 3538 3463 3604 24 2 21 C ATOM 5021 CG1 VAL A 188 -3.019 84.984 58.457 1.00 28.74 C ANISOU 5021 CG1 VAL B 188 3654 3589 3676 -10 7 -10 C ATOM 5022 CG2 VAL A 188 -3.921 82.986 59.605 1.00 28.14 C ANISOU 5022 CG2 VAL B 188 3525 3515 3652 49 -30 16 C ATOM 5023 N ASP A 189 -5.576 84.196 61.997 1.00 24.58 N ANISOU 5023 N ASP B 189 3128 2962 3248 121 -60 9 N ATOM 5024 CA ASP A 189 -5.543 83.980 63.435 1.00 23.67 C ANISOU 5024 CA ASP B 189 2982 2909 3101 110 -48 17 C ATOM 5025 C ASP A 189 -4.423 82.975 63.804 1.00 22.50 C ANISOU 5025 C ASP B 189 2790 2814 2942 108 -72 18 C ATOM 5026 O ASP A 189 -4.670 81.924 64.395 1.00 22.93 O ANISOU 5026 O ASP B 189 2735 2947 3028 184 -85 51 O ATOM 5027 CB ASP A 189 -6.924 83.500 63.886 1.00 24.37 C ANISOU 5027 CB ASP B 189 3068 2998 3195 115 -35 12 C ATOM 5028 CG ASP A 189 -7.045 83.317 65.395 1.00 25.28 C ANISOU 5028 CG ASP B 189 3169 3138 3297 120 -72 38 C ATOM 5029 OD1 ASP A 189 -6.411 84.066 66.161 1.00 27.03 O ANISOU 5029 OD1 ASP B 189 3582 3109 3579 68 -82 -29 O ATOM 5030 OD2 ASP A 189 -7.794 82.420 65.858 1.00 27.26 O ANISOU 5030 OD2 ASP B 189 3388 3264 3706 217 36 107 O ATOM 5031 N VAL A 190 -3.197 83.329 63.447 1.00 21.27 N ANISOU 5031 N VAL B 190 2696 2666 2721 158 -80 25 N ATOM 5032 CA VAL A 190 -2.005 82.530 63.771 1.00 20.35 C ANISOU 5032 CA VAL B 190 2601 2492 2637 138 -56 18 C ATOM 5033 C VAL A 190 -1.850 82.414 65.292 1.00 19.51 C ANISOU 5033 C VAL B 190 2501 2387 2523 128 -84 41 C ATOM 5034 O VAL A 190 -1.896 83.410 66.009 1.00 19.80 O ANISOU 5034 O VAL B 190 2555 2319 2646 251 -158 60 O ATOM 5035 CB VAL A 190 -0.723 83.155 63.160 1.00 19.88 C ANISOU 5035 CB VAL B 190 2521 2453 2579 95 -43 29 C ATOM 5036 CG1 VAL A 190 0.537 82.482 63.700 1.00 20.30 C ANISOU 5036 CG1 VAL B 190 2633 2403 2674 131 -47 0 C ATOM 5037 CG2 VAL A 190 -0.757 83.096 61.642 1.00 19.64 C ANISOU 5037 CG2 VAL B 190 2510 2391 2561 131 -53 -42 C ATOM 5038 N PHE A 191 -1.700 81.183 65.780 1.00 18.32 N ANISOU 5038 N PHE B 191 2334 2230 2394 141 -44 -1 N ATOM 5039 CA PHE A 191 -1.517 80.929 67.213 1.00 17.49 C ANISOU 5039 CA PHE B 191 2210 2161 2273 95 0 -15 C ATOM 5040 C PHE A 191 -0.097 81.234 67.688 1.00 17.04 C ANISOU 5040 C PHE B 191 2174 2092 2207 101 -8 -15 C ATOM 5041 O PHE A 191 0.092 81.766 68.772 1.00 17.48 O ANISOU 5041 O PHE B 191 2228 2046 2367 105 2 -62 O ATOM 5042 CB PHE A 191 -1.876 79.478 67.523 1.00 17.51 C ANISOU 5042 CB PHE B 191 2185 2208 2260 44 -16 14 C ATOM 5043 CG PHE A 191 -1.553 79.043 68.931 1.00 16.67 C ANISOU 5043 CG PHE B 191 2110 2133 2089 39 2 -46 C ATOM 5044 CD1 PHE A 191 -2.229 79.594 70.034 1.00 14.72 C ANISOU 5044 CD1 PHE B 191 1710 1835 2045 100 32 -97 C ATOM 5045 CD2 PHE A 191 -0.583 78.058 69.153 1.00 16.92 C ANISOU 5045 CD2 PHE B 191 2045 2172 2212 17 -4 25 C ATOM 5046 CE1 PHE A 191 -1.939 79.163 71.331 1.00 14.80 C ANISOU 5046 CE1 PHE B 191 1701 1854 2068 57 21 -105 C ATOM 5047 CE2 PHE A 191 -0.277 77.630 70.454 1.00 16.71 C ANISOU 5047 CE2 PHE B 191 2078 2093 2176 54 -65 -4 C ATOM 5048 CZ PHE A 191 -0.955 78.172 71.544 1.00 15.47 C ANISOU 5048 CZ PHE B 191 1917 1933 2026 22 -101 79 C ATOM 5049 N THR A 192 0.898 80.875 66.876 1.00 16.58 N ANISOU 5049 N THR B 192 2067 2073 2159 120 -34 -21 N ATOM 5050 CA THR A 192 2.315 81.059 67.218 1.00 15.52 C ANISOU 5050 CA THR B 192 1974 1818 2103 92 -41 7 C ATOM 5051 C THR A 192 3.148 81.209 65.946 1.00 15.14 C ANISOU 5051 C THR B 192 1928 1766 2055 148 -84 0 C ATOM 5052 O THR A 192 2.964 80.466 64.987 1.00 14.60 O ANISOU 5052 O THR B 192 1835 1666 2044 229 -149 8 O ATOM 5053 CB THR A 192 2.843 79.844 68.047 1.00 15.50 C ANISOU 5053 CB THR B 192 1967 1852 2068 101 -43 18 C ATOM 5054 OG1 THR A 192 2.146 79.747 69.295 1.00 14.57 O ANISOU 5054 OG1 THR B 192 2009 1418 2109 186 -125 52 O ATOM 5055 CG2 THR A 192 4.355 79.983 68.361 1.00 16.37 C ANISOU 5055 CG2 THR B 192 1992 2020 2206 62 -86 19 C ATOM 5056 N PHE A 193 4.048 82.190 65.936 1.00 14.49 N ANISOU 5056 N PHE B 193 1827 1642 2034 149 -81 13 N ATOM 5057 CA PHE A 193 5.081 82.304 64.918 1.00 14.99 C ANISOU 5057 CA PHE B 193 1908 1780 2006 73 -115 30 C ATOM 5058 C PHE A 193 6.392 81.737 65.469 1.00 15.03 C ANISOU 5058 C PHE B 193 1897 1813 1998 98 -77 0 C ATOM 5059 O PHE A 193 6.863 82.170 66.521 1.00 15.17 O ANISOU 5059 O PHE B 193 1970 1795 1999 118 -181 64 O ATOM 5060 CB PHE A 193 5.306 83.767 64.509 1.00 15.24 C ANISOU 5060 CB PHE B 193 1944 1732 2114 145 -126 39 C ATOM 5061 CG PHE A 193 4.161 84.379 63.748 1.00 16.01 C ANISOU 5061 CG PHE B 193 1979 1946 2158 50 -126 29 C ATOM 5062 CD1 PHE A 193 4.040 84.193 62.385 1.00 15.91 C ANISOU 5062 CD1 PHE B 193 2010 1825 2209 185 -145 46 C ATOM 5063 CD2 PHE A 193 3.226 85.155 64.403 1.00 17.19 C ANISOU 5063 CD2 PHE B 193 2218 1988 2324 41 -86 42 C ATOM 5064 CE1 PHE A 193 2.975 84.753 61.679 1.00 18.57 C ANISOU 5064 CE1 PHE B 193 2283 2361 2411 118 -180 50 C ATOM 5065 CE2 PHE A 193 2.158 85.722 63.716 1.00 16.81 C ANISOU 5065 CE2 PHE B 193 2179 1861 2344 86 -126 7 C ATOM 5066 CZ PHE A 193 2.037 85.531 62.358 1.00 18.21 C ANISOU 5066 CZ PHE B 193 2372 2169 2375 178 -90 -3 C ATOM 5067 N ILE A 194 6.996 80.811 64.725 1.00 15.28 N ANISOU 5067 N ILE B 194 1960 1830 2015 70 -109 -12 N ATOM 5068 CA ILE A 194 8.234 80.171 65.152 1.00 15.28 C ANISOU 5068 CA ILE B 194 1911 1873 2021 126 -50 -51 C ATOM 5069 C ILE A 194 9.404 80.720 64.360 1.00 16.19 C ANISOU 5069 C ILE B 194 2011 1990 2148 116 -47 1 C ATOM 5070 O ILE A 194 9.526 80.463 63.162 1.00 16.90 O ANISOU 5070 O ILE B 194 2053 2141 2224 189 -28 19 O ATOM 5071 CB ILE A 194 8.192 78.622 64.998 1.00 15.06 C ANISOU 5071 CB ILE B 194 1881 1875 1964 71 -87 -40 C ATOM 5072 CG1 ILE A 194 6.927 78.045 65.620 1.00 15.49 C ANISOU 5072 CG1 ILE B 194 2013 1881 1988 40 -26 -98 C ATOM 5073 CG2 ILE A 194 9.470 78.000 65.610 1.00 13.71 C ANISOU 5073 CG2 ILE B 194 1739 1530 1938 158 -116 -281 C ATOM 5074 CD1 ILE A 194 6.792 76.565 65.456 1.00 17.11 C ANISOU 5074 CD1 ILE B 194 2268 2145 2087 6 -38 -87 C ATOM 5075 N ALA A 195 10.266 81.459 65.046 1.00 16.96 N ANISOU 5075 N ALA B 195 2161 2022 2259 92 -22 0 N ATOM 5076 CA ALA A 195 11.506 81.949 64.472 1.00 17.58 C ANISOU 5076 CA ALA B 195 2244 2080 2355 68 5 24 C ATOM 5077 C ALA A 195 12.678 81.132 65.010 1.00 18.91 C ANISOU 5077 C ALA B 195 2430 2251 2501 98 33 24 C ATOM 5078 O ALA A 195 12.542 80.414 65.995 1.00 19.23 O ANISOU 5078 O ALA B 195 2470 2187 2650 208 104 40 O ATOM 5079 CB ALA A 195 11.681 83.452 64.812 1.00 17.69 C ANISOU 5079 CB ALA B 195 2295 2019 2404 42 -19 12 C ATOM 5080 N GLY A 196 13.827 81.266 64.366 1.00 20.33 N ANISOU 5080 N GLY B 196 2592 2460 2672 47 41 81 N ATOM 5081 CA GLY A 196 15.028 80.539 64.740 1.00 21.59 C ANISOU 5081 CA GLY B 196 2750 2635 2819 17 12 66 C ATOM 5082 C GLY A 196 16.255 81.413 64.568 1.00 22.76 C ANISOU 5082 C GLY B 196 2938 2782 2926 -2 13 48 C ATOM 5083 O GLY A 196 16.434 82.405 65.276 1.00 22.16 O ANISOU 5083 O GLY B 196 2936 2604 2877 81 37 99 O ATOM 5084 N ARG A 197 17.099 81.047 63.619 1.00 24.72 N ANISOU 5084 N ARG B 197 3186 3026 3179 11 29 16 N ATOM 5085 CA ARG A 197 18.385 81.706 63.449 1.00 26.88 C ANISOU 5085 CA ARG B 197 3439 3331 3441 0 18 10 C ATOM 5086 C ARG A 197 18.259 83.179 63.037 1.00 26.95 C ANISOU 5086 C ARG B 197 3453 3318 3468 -10 20 16 C ATOM 5087 O ARG A 197 19.118 83.969 63.386 1.00 27.18 O ANISOU 5087 O ARG B 197 3500 3314 3511 -39 16 32 O ATOM 5088 CB ARG A 197 19.237 80.962 62.431 1.00 27.66 C ANISOU 5088 CB ARG B 197 3525 3441 3540 15 53 -19 C ATOM 5089 CG ARG A 197 19.652 79.549 62.858 1.00 30.04 C ANISOU 5089 CG ARG B 197 3835 3736 3841 49 15 71 C ATOM 5090 CD ARG A 197 20.381 78.806 61.725 1.00 34.82 C ANISOU 5090 CD ARG B 197 4428 4407 4395 46 106 10 C ATOM 5091 NE ARG A 197 21.169 79.740 60.917 1.00 38.65 N ANISOU 5091 NE ARG B 197 4957 4835 4893 -20 101 39 N ATOM 5092 CZ ARG A 197 21.819 79.444 59.793 1.00 41.28 C ANISOU 5092 CZ ARG B 197 5258 5205 5221 -9 118 3 C ATOM 5093 NH1 ARG A 197 21.804 78.210 59.290 1.00 42.32 N ANISOU 5093 NH1 ARG B 197 5379 5307 5393 30 102 -29 N ATOM 5094 NH2 ARG A 197 22.491 80.409 59.164 1.00 41.73 N ANISOU 5094 NH2 ARG B 197 5253 5282 5321 23 94 72 N ATOM 5095 N GLY A 198 17.195 83.530 62.308 1.00 27.25 N ANISOU 5095 N GLY B 198 3514 3366 3473 -26 6 24 N ATOM 5096 CA GLY A 198 16.884 84.929 61.990 1.00 27.50 C ANISOU 5096 CA GLY B 198 3513 3431 3503 0 -16 40 C ATOM 5097 C GLY A 198 16.935 85.839 63.208 1.00 27.62 C ANISOU 5097 C GLY B 198 3526 3439 3529 -11 -18 32 C ATOM 5098 O GLY A 198 17.369 86.987 63.108 1.00 28.64 O ANISOU 5098 O GLY B 198 3665 3591 3623 -44 -23 77 O ATOM 5099 N ILE A 199 16.517 85.322 64.366 1.00 27.43 N ANISOU 5099 N ILE B 199 3451 3428 3542 1 -23 18 N ATOM 5100 CA ILE A 199 16.571 86.057 65.641 1.00 27.05 C ANISOU 5100 CA ILE B 199 3440 3365 3472 0 -10 10 C ATOM 5101 C ILE A 199 17.881 85.807 66.405 1.00 26.30 C ANISOU 5101 C ILE B 199 3348 3215 3428 -12 -5 1 C ATOM 5102 O ILE A 199 18.569 86.748 66.816 1.00 26.12 O ANISOU 5102 O ILE B 199 3361 3094 3470 -7 23 14 O ATOM 5103 CB ILE A 199 15.375 85.664 66.557 1.00 27.65 C ANISOU 5103 CB ILE B 199 3490 3479 3536 18 -15 -42 C ATOM 5104 CG1 ILE A 199 14.044 85.966 65.874 1.00 28.66 C ANISOU 5104 CG1 ILE B 199 3630 3610 3649 21 1 -2 C ATOM 5105 CG2 ILE A 199 15.464 86.355 67.917 1.00 28.33 C ANISOU 5105 CG2 ILE B 199 3558 3593 3610 7 -21 16 C ATOM 5106 CD1 ILE A 199 13.714 87.436 65.775 1.00 29.59 C ANISOU 5106 CD1 ILE B 199 3854 3615 3771 27 4 -62 C ATOM 5107 N THR A 200 18.205 84.536 66.645 1.00 25.34 N ANISOU 5107 N THR B 200 3197 3098 3333 -4 -24 -4 N ATOM 5108 CA THR A 200 19.288 84.192 67.567 1.00 24.81 C ANISOU 5108 CA THR B 200 3135 3041 3249 0 0 45 C ATOM 5109 C THR A 200 20.680 84.518 67.015 1.00 25.90 C ANISOU 5109 C THR B 200 3276 3183 3379 -11 13 29 C ATOM 5110 O THR A 200 21.630 84.672 67.798 1.00 26.34 O ANISOU 5110 O THR B 200 3358 3185 3462 -9 25 66 O ATOM 5111 CB THR A 200 19.238 82.692 67.979 1.00 24.13 C ANISOU 5111 CB THR B 200 3021 2981 3165 -15 -9 34 C ATOM 5112 OG1 THR A 200 19.362 81.869 66.815 1.00 22.00 O ANISOU 5112 OG1 THR B 200 2554 2824 2980 33 -17 122 O ATOM 5113 CG2 THR A 200 17.900 82.350 68.677 1.00 23.14 C ANISOU 5113 CG2 THR B 200 2982 2789 3020 -16 9 28 C ATOM 5114 N GLU A 201 20.795 84.609 65.685 1.00 27.12 N ANISOU 5114 N GLU B 201 3452 3349 3501 -6 11 35 N ATOM 5115 CA GLU A 201 22.062 84.972 65.010 1.00 28.10 C ANISOU 5115 CA GLU B 201 3555 3475 3645 -26 32 34 C ATOM 5116 C GLU A 201 22.163 86.460 64.630 1.00 29.28 C ANISOU 5116 C GLU B 201 3719 3624 3782 -18 33 36 C ATOM 5117 O GLU A 201 23.133 86.864 63.985 1.00 29.56 O ANISOU 5117 O GLU B 201 3753 3580 3898 -73 41 49 O ATOM 5118 CB GLU A 201 22.272 84.140 63.748 1.00 28.04 C ANISOU 5118 CB GLU B 201 3545 3485 3621 -6 19 41 C ATOM 5119 CG GLU A 201 22.564 82.655 63.976 1.00 28.49 C ANISOU 5119 CG GLU B 201 3661 3448 3714 -6 10 12 C ATOM 5120 CD GLU A 201 22.844 81.920 62.671 1.00 29.93 C ANISOU 5120 CD GLU B 201 3828 3729 3812 -19 -18 21 C ATOM 5121 OE1 GLU A 201 22.672 82.535 61.591 1.00 30.89 O ANISOU 5121 OE1 GLU B 201 4029 3763 3942 -122 10 103 O ATOM 5122 OE2 GLU A 201 23.206 80.719 62.712 1.00 29.18 O ANISOU 5122 OE2 GLU B 201 3770 3593 3725 33 -53 20 O ATOM 5123 N ALA A 202 21.158 87.251 65.000 1.00 30.51 N ANISOU 5123 N ALA B 202 3882 3780 3929 -13 34 20 N ATOM 5124 CA ALA A 202 21.199 88.708 64.834 1.00 31.44 C ANISOU 5124 CA ALA B 202 4001 3923 4020 -12 21 35 C ATOM 5125 C ALA A 202 22.233 89.352 65.778 1.00 32.20 C ANISOU 5125 C ALA B 202 4084 4040 4109 -24 3 31 C ATOM 5126 O ALA A 202 22.564 88.789 66.821 1.00 32.58 O ANISOU 5126 O ALA B 202 4081 4134 4162 -17 1 39 O ATOM 5127 CB ALA A 202 19.811 89.305 65.075 1.00 31.36 C ANISOU 5127 CB ALA B 202 3989 3908 4016 -38 11 38 C ATOM 5128 N LYS A 203 22.730 90.534 65.407 1.00 32.88 N ANISOU 5128 N LYS B 203 4191 4120 4182 -45 10 33 N ATOM 5129 CA LYS A 203 23.715 91.267 66.214 1.00 33.18 C ANISOU 5129 CA LYS B 203 4222 4146 4239 -32 -1 16 C ATOM 5130 C LYS A 203 23.207 91.470 67.636 1.00 33.28 C ANISOU 5130 C LYS B 203 4226 4146 4273 -38 -12 -7 C ATOM 5131 O LYS A 203 23.929 91.244 68.608 1.00 33.34 O ANISOU 5131 O LYS B 203 4199 4130 4338 -64 -35 -16 O ATOM 5132 CB LYS A 203 24.039 92.607 65.567 1.00 33.45 C ANISOU 5132 CB LYS B 203 4281 4171 4257 -41 9 8 C ATOM 5133 N ASN A 204 21.943 91.864 67.748 1.00 33.16 N ANISOU 5133 N ASN B 204 4203 4117 4277 -7 -9 -14 N ATOM 5134 CA ASN A 204 21.274 91.975 69.033 1.00 33.22 C ANISOU 5134 CA ASN B 204 4216 4162 4242 -7 -5 4 C ATOM 5135 C ASN A 204 20.061 91.028 69.051 1.00 32.55 C ANISOU 5135 C ASN B 204 4137 4058 4172 0 -3 17 C ATOM 5136 O ASN A 204 18.956 91.428 68.682 1.00 32.61 O ANISOU 5136 O ASN B 204 4133 4057 4197 11 0 37 O ATOM 5137 CB ASN A 204 20.871 93.437 69.258 1.00 33.50 C ANISOU 5137 CB ASN B 204 4258 4168 4302 9 -11 -2 C ATOM 5138 CG ASN A 204 20.120 93.659 70.563 1.00 35.49 C ANISOU 5138 CG ASN B 204 4542 4437 4504 11 -11 9 C ATOM 5139 OD1 ASN A 204 20.020 92.771 71.416 1.00 37.58 O ANISOU 5139 OD1 ASN B 204 4906 4537 4835 29 -8 10 O ATOM 5140 ND2 ASN A 204 19.576 94.864 70.721 1.00 37.39 N ANISOU 5140 ND2 ASN B 204 4800 4631 4774 37 25 -21 N ATOM 5141 N PRO A 205 20.258 89.758 69.446 1.00 31.99 N ANISOU 5141 N PRO B 205 4045 4004 4106 -10 -9 14 N ATOM 5142 CA PRO A 205 19.146 88.797 69.442 1.00 31.36 C ANISOU 5142 CA PRO B 205 3973 3922 4017 -1 4 16 C ATOM 5143 C PRO A 205 17.934 89.254 70.272 1.00 31.05 C ANISOU 5143 C PRO B 205 3948 3862 3987 0 0 16 C ATOM 5144 O PRO A 205 16.806 89.110 69.812 1.00 30.10 O ANISOU 5144 O PRO B 205 3871 3702 3864 46 -28 14 O ATOM 5145 CB PRO A 205 19.780 87.517 70.012 1.00 31.39 C ANISOU 5145 CB PRO B 205 3957 3922 4046 -14 -3 5 C ATOM 5146 CG PRO A 205 21.251 87.658 69.680 1.00 31.61 C ANISOU 5146 CG PRO B 205 3994 3951 4064 0 5 -8 C ATOM 5147 CD PRO A 205 21.519 89.127 69.884 1.00 31.87 C ANISOU 5147 CD PRO B 205 4017 3977 4113 -14 6 16 C ATOM 5148 N ALA A 206 18.168 89.818 71.456 1.00 31.25 N ANISOU 5148 N ALA B 206 3965 3903 4005 -13 -1 20 N ATOM 5149 CA ALA A 206 17.070 90.269 72.312 1.00 31.94 C ANISOU 5149 CA ALA B 206 4046 3992 4096 0 -1 15 C ATOM 5150 C ALA A 206 16.258 91.401 71.662 1.00 32.59 C ANISOU 5150 C ALA B 206 4106 4076 4198 2 3 33 C ATOM 5151 O ALA A 206 15.046 91.503 71.875 1.00 32.62 O ANISOU 5151 O ALA B 206 4098 4047 4248 -9 20 34 O ATOM 5152 CB ALA A 206 17.595 90.695 73.675 1.00 32.00 C ANISOU 5152 CB ALA B 206 4050 4007 4101 3 -27 19 C ATOM 5153 N GLY A 207 16.939 92.240 70.877 1.00 33.16 N ANISOU 5153 N GLY B 207 4171 4162 4265 8 16 47 N ATOM 5154 CA GLY A 207 16.316 93.337 70.142 1.00 33.44 C ANISOU 5154 CA GLY B 207 4234 4192 4280 7 -3 36 C ATOM 5155 C GLY A 207 15.569 92.876 68.902 1.00 33.59 C ANISOU 5155 C GLY B 207 4258 4204 4301 3 -4 36 C ATOM 5156 O GLY A 207 14.510 93.409 68.589 1.00 33.83 O ANISOU 5156 O GLY B 207 4293 4196 4362 12 -25 64 O ATOM 5157 N ALA A 208 16.109 91.878 68.205 1.00 33.40 N ANISOU 5157 N ALA B 208 4248 4181 4261 -3 8 32 N ATOM 5158 CA ALA A 208 15.444 91.294 67.046 1.00 33.24 C ANISOU 5158 CA ALA B 208 4222 4177 4230 2 -4 22 C ATOM 5159 C ALA A 208 14.134 90.634 67.457 1.00 33.15 C ANISOU 5159 C ALA B 208 4222 4147 4224 9 -10 16 C ATOM 5160 O ALA A 208 13.107 90.834 66.808 1.00 33.23 O ANISOU 5160 O ALA B 208 4269 4107 4249 0 -28 -14 O ATOM 5161 CB ALA A 208 16.350 90.285 66.364 1.00 33.23 C ANISOU 5161 CB ALA B 208 4229 4158 4238 0 -6 24 C ATOM 5162 N ALA A 209 14.189 89.850 68.536 1.00 32.95 N ANISOU 5162 N ALA B 209 4179 4141 4196 -1 -3 14 N ATOM 5163 CA ALA A 209 13.022 89.200 69.123 1.00 32.63 C ANISOU 5163 CA ALA B 209 4152 4090 4154 -15 -7 2 C ATOM 5164 C ALA A 209 11.999 90.221 69.595 1.00 32.84 C ANISOU 5164 C ALA B 209 4187 4095 4195 -15 -19 5 C ATOM 5165 O ALA A 209 10.801 90.029 69.408 1.00 32.69 O ANISOU 5165 O ALA B 209 4219 4013 4187 -25 -15 7 O ATOM 5166 CB ALA A 209 13.442 88.306 70.288 1.00 32.48 C ANISOU 5166 CB ALA B 209 4129 4078 4132 -22 6 -2 C ATOM 5167 N ARG A 210 12.471 91.303 70.214 1.00 33.34 N ANISOU 5167 N ARG B 210 4242 4162 4261 -10 -31 -16 N ATOM 5168 CA ARG A 210 11.575 92.347 70.712 1.00 33.91 C ANISOU 5168 CA ARG B 210 4322 4231 4327 -8 -21 -35 C ATOM 5169 C ARG A 210 10.882 93.043 69.550 1.00 33.10 C ANISOU 5169 C ARG B 210 4243 4096 4238 -9 -15 -36 C ATOM 5170 O ARG A 210 9.681 93.272 69.605 1.00 33.33 O ANISOU 5170 O ARG B 210 4320 4052 4290 -27 -33 -47 O ATOM 5171 CB ARG A 210 12.328 93.366 71.575 1.00 34.58 C ANISOU 5171 CB ARG B 210 4400 4318 4421 -21 -26 -48 C ATOM 5172 CG ARG A 210 11.439 94.427 72.245 1.00 36.90 C ANISOU 5172 CG ARG B 210 4660 4653 4706 0 10 -43 C ATOM 5173 CD ARG A 210 12.036 94.923 73.575 1.00 40.40 C ANISOU 5173 CD ARG B 210 5114 5108 5125 -15 8 -58 C ATOM 5174 NE ARG A 210 13.494 94.778 73.583 1.00 43.30 N ANISOU 5174 NE ARG B 210 5455 5509 5485 10 -47 -38 N ATOM 5175 CZ ARG A 210 14.257 94.737 74.671 1.00 45.18 C ANISOU 5175 CZ ARG B 210 5732 5717 5714 7 -29 4 C ATOM 5176 NH1 ARG A 210 13.723 94.853 75.888 1.00 45.86 N ANISOU 5176 NH1 ARG B 210 5860 5781 5784 25 26 14 N ATOM 5177 NH2 ARG A 210 15.572 94.587 74.537 1.00 45.53 N ANISOU 5177 NH2 ARG B 210 5685 5762 5849 23 25 12 N ATOM 5178 N ALA A 211 11.641 93.353 68.501 1.00 32.23 N ANISOU 5178 N ALA B 211 4148 3957 4139 -25 -22 -20 N ATOM 5179 CA ALA A 211 11.092 93.927 67.271 1.00 31.60 C ANISOU 5179 CA ALA B 211 4020 3910 4074 -15 -41 -13 C ATOM 5180 C ALA A 211 10.001 93.019 66.703 1.00 31.06 C ANISOU 5180 C ALA B 211 3952 3806 4042 -3 -41 5 C ATOM 5181 O ALA A 211 8.917 93.473 66.349 1.00 31.34 O ANISOU 5181 O ALA B 211 3946 3820 4139 -10 -88 -8 O ATOM 5182 CB ALA A 211 12.191 94.119 66.249 1.00 31.55 C ANISOU 5182 CB ALA B 211 4028 3902 4057 -34 -34 12 C ATOM 5183 N PHE A 212 10.307 91.730 66.620 1.00 30.18 N ANISOU 5183 N PHE B 212 3846 3680 3939 10 -51 12 N ATOM 5184 CA PHE A 212 9.358 90.719 66.168 1.00 28.92 C ANISOU 5184 CA PHE B 212 3724 3470 3794 22 -42 12 C ATOM 5185 C PHE A 212 8.059 90.757 66.962 1.00 28.43 C ANISOU 5185 C PHE B 212 3701 3340 3759 -11 -40 16 C ATOM 5186 O PHE A 212 6.980 90.855 66.388 1.00 27.68 O ANISOU 5186 O PHE B 212 3643 3101 3771 -88 -41 5 O ATOM 5187 CB PHE A 212 9.989 89.327 66.292 1.00 28.87 C ANISOU 5187 CB PHE B 212 3718 3476 3775 36 -42 21 C ATOM 5188 CG PHE A 212 9.426 88.315 65.333 1.00 27.73 C ANISOU 5188 CG PHE B 212 3592 3315 3628 49 -50 41 C ATOM 5189 CD1 PHE A 212 10.157 87.922 64.221 1.00 27.26 C ANISOU 5189 CD1 PHE B 212 3562 3267 3527 44 -57 70 C ATOM 5190 CD2 PHE A 212 8.169 87.759 65.545 1.00 27.75 C ANISOU 5190 CD2 PHE B 212 3565 3364 3612 90 -24 -8 C ATOM 5191 CE1 PHE A 212 9.652 86.986 63.329 1.00 27.19 C ANISOU 5191 CE1 PHE B 212 3547 3334 3448 52 -51 84 C ATOM 5192 CE2 PHE A 212 7.642 86.813 64.651 1.00 27.35 C ANISOU 5192 CE2 PHE B 212 3514 3375 3501 10 -63 2 C ATOM 5193 CZ PHE A 212 8.395 86.423 63.545 1.00 27.28 C ANISOU 5193 CZ PHE B 212 3494 3402 3468 0 -51 0 C ATOM 5194 N LYS A 213 8.170 90.692 68.284 1.00 28.58 N ANISOU 5194 N LYS B 213 3701 3401 3754 -14 -15 -1 N ATOM 5195 CA LYS A 213 7.005 90.698 69.159 1.00 29.27 C ANISOU 5195 CA LYS B 213 3734 3568 3818 21 -10 0 C ATOM 5196 C LYS A 213 6.276 92.043 69.062 1.00 29.90 C ANISOU 5196 C LYS B 213 3788 3653 3919 31 -2 12 C ATOM 5197 O LYS A 213 5.053 92.094 69.180 1.00 29.64 O ANISOU 5197 O LYS B 213 3712 3589 3960 66 -31 43 O ATOM 5198 CB LYS A 213 7.416 90.362 70.602 1.00 29.30 C ANISOU 5198 CB LYS B 213 3755 3596 3781 16 1 -33 C ATOM 5199 CG LYS A 213 6.265 90.093 71.590 1.00 29.83 C ANISOU 5199 CG LYS B 213 3782 3670 3880 -15 22 -13 C ATOM 5200 CD LYS A 213 5.233 89.059 71.086 1.00 30.30 C ANISOU 5200 CD LYS B 213 3841 3828 3843 2 5 -19 C ATOM 5201 CE LYS A 213 4.220 88.734 72.209 1.00 30.67 C ANISOU 5201 CE LYS B 213 3832 3817 4002 -44 64 -4 C ATOM 5202 NZ LYS A 213 3.313 87.590 71.878 1.00 30.01 N ANISOU 5202 NZ LYS B 213 3713 3860 3828 8 53 -108 N ATOM 5203 N ASP A 214 7.030 93.118 68.826 1.00 30.66 N ANISOU 5203 N ASP B 214 3870 3779 4001 35 6 23 N ATOM 5204 CA ASP A 214 6.440 94.452 68.671 1.00 31.57 C ANISOU 5204 CA ASP B 214 4004 3900 4089 26 -9 19 C ATOM 5205 C ASP A 214 5.596 94.562 67.391 1.00 31.57 C ANISOU 5205 C ASP B 214 3998 3900 4095 13 -9 6 C ATOM 5206 O ASP A 214 4.538 95.188 67.398 1.00 31.74 O ANISOU 5206 O ASP B 214 4014 3843 4202 29 -32 1 O ATOM 5207 CB ASP A 214 7.517 95.551 68.739 1.00 31.93 C ANISOU 5207 CB ASP B 214 4029 3962 4141 25 -12 10 C ATOM 5208 CG ASP A 214 7.962 95.861 70.178 1.00 33.54 C ANISOU 5208 CG ASP B 214 4256 4154 4333 38 -19 16 C ATOM 5209 OD1 ASP A 214 7.294 95.427 71.147 1.00 35.07 O ANISOU 5209 OD1 ASP B 214 4424 4283 4616 94 55 36 O ATOM 5210 OD2 ASP A 214 8.988 96.545 70.392 1.00 34.96 O ANISOU 5210 OD2 ASP B 214 4364 4307 4610 -23 -91 -25 O ATOM 5211 N GLU A 215 6.058 93.950 66.307 1.00 31.32 N ANISOU 5211 N GLU B 215 3992 3858 4048 17 -4 23 N ATOM 5212 CA GLU A 215 5.285 93.883 65.070 1.00 31.10 C ANISOU 5212 CA GLU B 215 3952 3848 4014 17 -27 44 C ATOM 5213 C GLU A 215 4.045 92.978 65.189 1.00 30.85 C ANISOU 5213 C GLU B 215 3915 3806 3998 23 -42 54 C ATOM 5214 O GLU A 215 3.017 93.261 64.582 1.00 30.49 O ANISOU 5214 O GLU B 215 3878 3666 4041 41 -62 46 O ATOM 5215 CB GLU A 215 6.182 93.460 63.897 1.00 31.26 C ANISOU 5215 CB GLU B 215 3992 3883 4002 30 -23 50 C ATOM 5216 CG GLU A 215 5.469 93.256 62.548 1.00 33.04 C ANISOU 5216 CG GLU B 215 4256 4109 4188 12 -34 56 C ATOM 5217 CD GLU A 215 4.976 94.549 61.885 1.00 35.42 C ANISOU 5217 CD GLU B 215 4665 4353 4437 51 -21 55 C ATOM 5218 OE1 GLU A 215 4.910 95.609 62.556 1.00 35.03 O ANISOU 5218 OE1 GLU B 215 4785 4108 4417 88 -9 70 O ATOM 5219 OE2 GLU A 215 4.644 94.491 60.675 1.00 36.28 O ANISOU 5219 OE2 GLU B 215 4779 4500 4502 64 -96 184 O ATOM 5220 N ILE A 216 4.138 91.889 65.956 1.00 30.47 N ANISOU 5220 N ILE B 216 3831 3785 3961 17 -35 41 N ATOM 5221 CA ILE A 216 2.958 91.075 66.265 1.00 30.01 C ANISOU 5221 CA ILE B 216 3792 3726 3882 43 -24 9 C ATOM 5222 C ILE A 216 1.926 91.956 66.981 1.00 30.78 C ANISOU 5222 C ILE B 216 3904 3796 3993 57 -20 -12 C ATOM 5223 O ILE A 216 0.743 91.944 66.633 1.00 30.20 O ANISOU 5223 O ILE B 216 3872 3595 4007 118 -43 -5 O ATOM 5224 CB ILE A 216 3.317 89.826 67.124 1.00 29.47 C ANISOU 5224 CB ILE B 216 3721 3686 3789 27 -8 -3 C ATOM 5225 CG1 ILE A 216 4.091 88.805 66.291 1.00 28.79 C ANISOU 5225 CG1 ILE B 216 3606 3585 3748 57 -82 -1 C ATOM 5226 CG2 ILE A 216 2.067 89.147 67.674 1.00 28.68 C ANISOU 5226 CG2 ILE B 216 3669 3501 3725 39 -49 -14 C ATOM 5227 CD1 ILE A 216 4.645 87.624 67.122 1.00 28.00 C ANISOU 5227 CD1 ILE B 216 3620 3321 3697 -60 -64 30 C ATOM 5228 N LYS A 217 2.390 92.716 67.972 1.00 31.70 N ANISOU 5228 N LYS B 217 4030 3927 4084 58 -38 -15 N ATOM 5229 CA LYS A 217 1.530 93.598 68.763 1.00 32.85 C ANISOU 5229 CA LYS B 217 4172 4100 4208 39 -16 -7 C ATOM 5230 C LYS A 217 0.884 94.678 67.891 1.00 33.33 C ANISOU 5230 C LYS B 217 4254 4124 4284 28 -14 0 C ATOM 5231 O LYS A 217 -0.275 95.034 68.103 1.00 33.65 O ANISOU 5231 O LYS B 217 4278 4132 4375 32 -32 0 O ATOM 5232 CB LYS A 217 2.320 94.241 69.911 1.00 32.97 C ANISOU 5232 CB LYS B 217 4187 4126 4213 25 -20 -15 C ATOM 5233 N ARG A 218 1.628 95.180 66.910 1.00 33.87 N ANISOU 5233 N ARG B 218 4336 4195 4336 10 -7 0 N ATOM 5234 CA ARG A 218 1.120 96.244 66.044 1.00 34.23 C ANISOU 5234 CA ARG B 218 4370 4258 4375 36 -22 0 C ATOM 5235 C ARG A 218 -0.039 95.711 65.212 1.00 34.50 C ANISOU 5235 C ARG B 218 4373 4291 4444 28 -23 -7 C ATOM 5236 O ARG A 218 -1.128 96.308 65.192 1.00 34.68 O ANISOU 5236 O ARG B 218 4435 4216 4522 55 -34 19 O ATOM 5237 CB ARG A 218 2.230 96.821 65.144 1.00 34.19 C ANISOU 5237 CB ARG B 218 4365 4259 4365 32 0 7 C ATOM 5238 CG ARG A 218 1.797 98.042 64.307 1.00 34.27 C ANISOU 5238 CG ARG B 218 4397 4285 4339 40 -11 35 C ATOM 5239 CD ARG A 218 2.889 98.593 63.358 1.00 33.64 C ANISOU 5239 CD ARG B 218 4318 4190 4270 12 -27 23 C ATOM 5240 NE ARG A 218 3.185 97.691 62.239 1.00 34.59 N ANISOU 5240 NE ARG B 218 4489 4248 4402 40 -43 83 N ATOM 5241 CZ ARG A 218 2.368 97.450 61.202 1.00 34.88 C ANISOU 5241 CZ ARG B 218 4478 4370 4402 62 -19 29 C ATOM 5242 NH1 ARG A 218 1.188 98.055 61.092 1.00 34.83 N ANISOU 5242 NH1 ARG B 218 4414 4376 4441 102 -49 24 N ATOM 5243 NH2 ARG A 218 2.736 96.589 60.259 1.00 35.24 N ANISOU 5243 NH2 ARG B 218 4542 4426 4421 111 -20 98 N ATOM 5244 N ILE A 219 0.187 94.564 64.568 1.00 34.28 N ANISOU 5244 N ILE B 219 4361 4257 4404 52 -30 -19 N ATOM 5245 CA ILE A 219 -0.774 93.981 63.635 1.00 34.03 C ANISOU 5245 CA ILE B 219 4324 4250 4354 41 -17 -15 C ATOM 5246 C ILE A 219 -2.004 93.359 64.317 1.00 33.84 C ANISOU 5246 C ILE B 219 4307 4221 4329 40 -27 0 C ATOM 5247 O ILE A 219 -3.130 93.608 63.886 1.00 33.81 O ANISOU 5247 O ILE B 219 4326 4181 4336 61 -55 13 O ATOM 5248 CB ILE A 219 -0.078 92.954 62.718 1.00 34.06 C ANISOU 5248 CB ILE B 219 4335 4265 4341 47 -31 0 C ATOM 5249 CG1 ILE A 219 0.933 93.665 61.808 1.00 34.06 C ANISOU 5249 CG1 ILE B 219 4292 4276 4369 22 -19 -22 C ATOM 5250 CG2 ILE A 219 -1.113 92.165 61.904 1.00 34.11 C ANISOU 5250 CG2 ILE B 219 4318 4260 4379 49 -53 -9 C ATOM 5251 CD1 ILE A 219 1.923 92.719 61.103 1.00 34.27 C ANISOU 5251 CD1 ILE B 219 4305 4341 4375 77 -56 -36 C ATOM 5252 N TRP A 220 -1.792 92.555 65.362 1.00 33.60 N ANISOU 5252 N TRP B 220 4260 4204 4300 43 -28 11 N ATOM 5253 CA TRP A 220 -2.885 91.837 66.045 1.00 33.57 C ANISOU 5253 CA TRP B 220 4227 4234 4292 48 -20 17 C ATOM 5254 C TRP A 220 -3.364 92.539 67.317 1.00 34.46 C ANISOU 5254 C TRP B 220 4328 4350 4411 61 -11 10 C ATOM 5255 O TRP A 220 -4.333 92.100 67.946 1.00 34.93 O ANISOU 5255 O TRP B 220 4367 4398 4506 86 -17 46 O ATOM 5256 CB TRP A 220 -2.473 90.376 66.369 1.00 32.65 C ANISOU 5256 CB TRP B 220 4124 4117 4164 63 -19 -5 C ATOM 5257 CG TRP A 220 -2.419 89.501 65.140 1.00 30.07 C ANISOU 5257 CG TRP B 220 3774 3733 3917 50 -31 22 C ATOM 5258 CD1 TRP A 220 -3.425 88.737 64.639 1.00 27.82 C ANISOU 5258 CD1 TRP B 220 3543 3427 3599 79 -37 2 C ATOM 5259 CD2 TRP A 220 -1.301 89.327 64.247 1.00 26.86 C ANISOU 5259 CD2 TRP B 220 3502 3195 3509 47 -40 -12 C ATOM 5260 NE1 TRP A 220 -3.013 88.110 63.490 1.00 26.27 N ANISOU 5260 NE1 TRP B 220 3377 3151 3452 121 -59 36 N ATOM 5261 CE2 TRP A 220 -1.712 88.449 63.231 1.00 25.28 C ANISOU 5261 CE2 TRP B 220 3320 3020 3265 111 -58 52 C ATOM 5262 CE3 TRP A 220 0.010 89.826 64.214 1.00 25.32 C ANISOU 5262 CE3 TRP B 220 3278 3062 3279 93 -8 34 C ATOM 5263 CZ2 TRP A 220 -0.874 88.068 62.187 1.00 23.81 C ANISOU 5263 CZ2 TRP B 220 3072 2788 3185 134 -67 118 C ATOM 5264 CZ3 TRP A 220 0.842 89.449 63.178 1.00 23.31 C ANISOU 5264 CZ3 TRP B 220 3062 2658 3135 135 -86 89 C ATOM 5265 CH2 TRP A 220 0.397 88.573 62.181 1.00 22.76 C ANISOU 5265 CH2 TRP B 220 3024 2658 2966 155 -41 130 C ATOM 5266 N GLY A 221 -2.687 93.619 67.695 1.00 35.35 N ANISOU 5266 N GLY B 221 4446 4470 4513 53 -3 14 N ATOM 5267 CA GLY A 221 -2.971 94.317 68.947 1.00 35.98 C ANISOU 5267 CA GLY B 221 4531 4582 4556 37 5 -12 C ATOM 5268 C GLY A 221 -4.178 95.228 68.868 1.00 36.31 C ANISOU 5268 C GLY B 221 4598 4594 4603 48 27 -19 C ATOM 5269 O GLY A 221 -4.968 95.265 69.807 1.00 36.66 O ANISOU 5269 O GLY B 221 4655 4646 4628 30 43 -49 O TER 5270 GLY B 221 ATOM 1919 N GLN A 4 39.340 36.672 102.385 1.00 27.76 N ANISOU 1919 N GLN C 4 3543 3528 3475 50 -68 -11 N ATOM 1920 CA GLN A 4 39.964 36.066 101.178 1.00 27.23 C ANISOU 1920 CA GLN C 4 3506 3426 3411 51 -34 14 C ATOM 1921 C GLN A 4 41.195 36.810 100.667 1.00 26.99 C ANISOU 1921 C GLN C 4 3490 3401 3362 40 0 18 C ATOM 1922 O GLN A 4 41.785 37.633 101.363 1.00 27.17 O ANISOU 1922 O GLN C 4 3598 3382 3343 42 34 44 O ATOM 1923 N LEU A 5 41.557 36.521 99.420 1.00 26.05 N ANISOU 1923 N LEU C 5 3366 3253 3275 16 -18 46 N ATOM 1924 CA LEU A 5 42.764 37.042 98.796 1.00 24.64 C ANISOU 1924 CA LEU C 5 3193 3055 3114 -26 -7 67 C ATOM 1925 C LEU A 5 42.700 38.558 98.587 1.00 22.65 C ANISOU 1925 C LEU C 5 2949 2828 2826 -18 -5 92 C ATOM 1926 O LEU A 5 41.622 39.146 98.600 1.00 22.29 O ANISOU 1926 O LEU C 5 3039 2686 2743 -55 -78 186 O ATOM 1927 CB LEU A 5 42.979 36.353 97.440 1.00 24.94 C ANISOU 1927 CB LEU C 5 3234 3051 3187 -38 2 46 C ATOM 1928 CG LEU A 5 43.265 34.843 97.411 1.00 25.52 C ANISOU 1928 CG LEU C 5 3266 3117 3312 -35 26 44 C ATOM 1929 CD1 LEU A 5 42.877 34.238 96.070 1.00 25.53 C ANISOU 1929 CD1 LEU C 5 3321 3011 3369 -33 41 54 C ATOM 1930 CD2 LEU A 5 44.725 34.580 97.702 1.00 25.04 C ANISOU 1930 CD2 LEU C 5 3200 3042 3271 -24 70 48 C ATOM 1931 N PRO A 6 43.860 39.187 98.377 1.00 20.98 N ANISOU 1931 N PRO C 6 2740 2645 2585 -53 31 104 N ATOM 1932 CA PRO A 6 43.896 40.585 97.924 1.00 19.58 C ANISOU 1932 CA PRO C 6 2576 2438 2423 -72 96 70 C ATOM 1933 C PRO A 6 43.104 40.749 96.629 1.00 18.74 C ANISOU 1933 C PRO C 6 2455 2306 2359 -101 115 31 C ATOM 1934 O PRO A 6 43.178 39.883 95.755 1.00 18.42 O ANISOU 1934 O PRO C 6 2495 2200 2303 -170 199 137 O ATOM 1935 CB PRO A 6 45.367 40.828 97.638 1.00 19.67 C ANISOU 1935 CB PRO C 6 2561 2473 2437 -99 101 56 C ATOM 1936 CG PRO A 6 46.109 39.768 98.424 1.00 19.83 C ANISOU 1936 CG PRO C 6 2617 2530 2386 -52 77 143 C ATOM 1937 CD PRO A 6 45.206 38.611 98.552 1.00 20.83 C ANISOU 1937 CD PRO C 6 2715 2650 2547 -60 58 85 C ATOM 1938 N ASN A 7 42.347 41.841 96.533 1.00 17.84 N ANISOU 1938 N ASN C 7 2347 2184 2246 -84 136 34 N ATOM 1939 CA ASN A 7 41.570 42.146 95.350 1.00 16.82 C ANISOU 1939 CA ASN C 7 2160 2100 2129 -75 53 35 C ATOM 1940 C ASN A 7 42.464 42.611 94.244 1.00 15.95 C ANISOU 1940 C ASN C 7 2048 1977 2034 -112 83 40 C ATOM 1941 O ASN A 7 43.501 43.225 94.493 1.00 15.25 O ANISOU 1941 O ASN C 7 1876 1865 2051 -277 119 96 O ATOM 1942 CB ASN A 7 40.579 43.284 95.624 1.00 17.06 C ANISOU 1942 CB ASN C 7 2242 2080 2158 -73 66 57 C ATOM 1943 CG ASN A 7 39.534 42.933 96.654 1.00 16.82 C ANISOU 1943 CG ASN C 7 2171 2157 2063 -62 -31 -32 C ATOM 1944 OD1 ASN A 7 39.282 43.710 97.568 1.00 19.21 O ANISOU 1944 OD1 ASN C 7 2550 2493 2256 -8 1 46 O ATOM 1945 ND2 ASN A 7 38.883 41.795 96.490 1.00 15.81 N ANISOU 1945 ND2 ASN C 7 2349 2083 1574 -29 -121 -32 N ATOM 1946 N LEU A 8 42.022 42.329 93.022 1.00 14.99 N ANISOU 1946 N LEU C 8 1954 1881 1861 -130 0 69 N ATOM 1947 CA LEU A 8 42.507 43.034 91.836 1.00 14.12 C ANISOU 1947 CA LEU C 8 1852 1758 1754 -108 32 35 C ATOM 1948 C LEU A 8 41.456 44.079 91.465 1.00 13.66 C ANISOU 1948 C LEU C 8 1804 1700 1684 -83 79 47 C ATOM 1949 O LEU A 8 40.282 43.751 91.279 1.00 13.68 O ANISOU 1949 O LEU C 8 1864 1679 1654 -81 62 49 O ATOM 1950 CB LEU A 8 42.687 42.057 90.667 1.00 13.52 C ANISOU 1950 CB LEU C 8 1758 1665 1713 -126 -5 21 C ATOM 1951 CG LEU A 8 42.983 42.766 89.321 1.00 14.50 C ANISOU 1951 CG LEU C 8 1903 1832 1771 -74 24 2 C ATOM 1952 CD1 LEU A 8 44.207 43.652 89.404 1.00 15.44 C ANISOU 1952 CD1 LEU C 8 1968 2011 1887 -117 26 54 C ATOM 1953 CD2 LEU A 8 43.170 41.707 88.239 1.00 15.62 C ANISOU 1953 CD2 LEU C 8 2000 2043 1889 -172 -46 -165 C ATOM 1954 N GLN A 9 41.905 45.321 91.396 1.00 13.50 N ANISOU 1954 N GLN C 9 1792 1693 1642 -141 84 14 N ATOM 1955 CA GLN A 9 41.086 46.465 91.028 1.00 12.75 C ANISOU 1955 CA GLN C 9 1745 1532 1565 -81 83 34 C ATOM 1956 C GLN A 9 41.598 47.009 89.698 1.00 12.27 C ANISOU 1956 C GLN C 9 1636 1530 1493 -74 34 -32 C ATOM 1957 O GLN A 9 42.806 47.094 89.506 1.00 12.27 O ANISOU 1957 O GLN C 9 1706 1512 1442 -96 -10 13 O ATOM 1958 CB GLN A 9 41.242 47.549 92.102 1.00 12.76 C ANISOU 1958 CB GLN C 9 1749 1640 1459 -129 52 0 C ATOM 1959 CG GLN A 9 40.451 48.850 91.877 1.00 12.23 C ANISOU 1959 CG GLN C 9 1606 1483 1556 -93 129 30 C ATOM 1960 CD GLN A 9 40.369 49.724 93.129 1.00 12.67 C ANISOU 1960 CD GLN C 9 1456 1779 1576 -189 0 88 C ATOM 1961 OE1 GLN A 9 40.167 49.221 94.242 1.00 14.31 O ANISOU 1961 OE1 GLN C 9 1773 2032 1628 -70 39 96 O ATOM 1962 NE2 GLN A 9 40.480 51.034 92.945 1.00 12.56 N ANISOU 1962 NE2 GLN C 9 1522 1340 1911 -297 59 -62 N ATOM 1963 N VAL A 10 40.694 47.403 88.800 1.00 11.56 N ANISOU 1963 N VAL C 10 1536 1380 1473 -71 68 -7 N ATOM 1964 CA VAL A 10 41.090 48.160 87.600 1.00 11.43 C ANISOU 1964 CA VAL C 10 1471 1416 1456 -67 24 5 C ATOM 1965 C VAL A 10 40.650 49.621 87.732 1.00 11.11 C ANISOU 1965 C VAL C 10 1406 1373 1440 -112 26 77 C ATOM 1966 O VAL A 10 39.478 49.878 88.007 1.00 11.26 O ANISOU 1966 O VAL C 10 1402 1485 1389 -233 14 144 O ATOM 1967 CB VAL A 10 40.474 47.611 86.282 1.00 12.07 C ANISOU 1967 CB VAL C 10 1565 1492 1527 -38 30 1 C ATOM 1968 CG1 VAL A 10 38.934 47.652 86.307 1.00 13.61 C ANISOU 1968 CG1 VAL C 10 1694 1772 1704 9 83 -78 C ATOM 1969 CG2 VAL A 10 41.004 48.393 85.075 1.00 11.92 C ANISOU 1969 CG2 VAL C 10 1486 1505 1536 50 -61 -36 C ATOM 1970 N ALA A 11 41.581 50.542 87.497 1.00 10.65 N ANISOU 1970 N ALA C 11 1325 1309 1410 -175 74 61 N ATOM 1971 CA ALA A 11 41.315 51.988 87.446 1.00 10.28 C ANISOU 1971 CA ALA C 11 1355 1245 1305 -65 47 39 C ATOM 1972 C ALA A 11 41.069 52.410 85.991 1.00 10.14 C ANISOU 1972 C ALA C 11 1300 1283 1266 -88 1 10 C ATOM 1973 O ALA A 11 41.832 52.025 85.071 1.00 10.31 O ANISOU 1973 O ALA C 11 1263 1368 1283 -153 -86 33 O ATOM 1974 CB ALA A 11 42.460 52.729 88.003 1.00 10.89 C ANISOU 1974 CB ALA C 11 1462 1378 1296 -78 58 33 C ATOM 1975 N LEU A 12 39.991 53.175 85.796 1.00 9.59 N ANISOU 1975 N LEU C 12 1271 1146 1224 -71 -23 -40 N ATOM 1976 CA LEU A 12 39.611 53.731 84.512 1.00 9.35 C ANISOU 1976 CA LEU C 12 1147 1160 1243 -94 -10 -46 C ATOM 1977 C LEU A 12 39.849 55.238 84.556 1.00 9.01 C ANISOU 1977 C LEU C 12 1120 1125 1177 -75 1 -83 C ATOM 1978 O LEU A 12 39.032 55.975 85.089 1.00 9.90 O ANISOU 1978 O LEU C 12 1213 1188 1360 -255 12 -63 O ATOM 1979 CB LEU A 12 38.130 53.426 84.214 1.00 9.53 C ANISOU 1979 CB LEU C 12 1200 1187 1232 -35 53 -33 C ATOM 1980 CG LEU A 12 37.689 51.972 84.401 1.00 10.23 C ANISOU 1980 CG LEU C 12 1191 1249 1447 -28 7 100 C ATOM 1981 CD1 LEU A 12 36.206 51.854 84.425 1.00 10.71 C ANISOU 1981 CD1 LEU C 12 1340 1261 1466 170 154 46 C ATOM 1982 CD2 LEU A 12 38.281 51.078 83.327 1.00 11.20 C ANISOU 1982 CD2 LEU C 12 1491 1275 1489 -30 118 -22 C ATOM 1983 N ASP A 13 40.984 55.686 84.027 1.00 9.29 N ANISOU 1983 N ASP C 13 1170 1257 1102 -95 -19 -62 N ATOM 1984 CA ASP A 13 41.401 57.088 84.107 1.00 9.51 C ANISOU 1984 CA ASP C 13 1224 1254 1133 -67 36 -71 C ATOM 1985 C ASP A 13 41.311 57.779 82.744 1.00 9.80 C ANISOU 1985 C ASP C 13 1263 1333 1124 -8 -52 -75 C ATOM 1986 O ASP A 13 41.995 58.752 82.481 1.00 10.05 O ANISOU 1986 O ASP C 13 1503 1275 1041 -10 -55 -56 O ATOM 1987 CB ASP A 13 42.824 57.218 84.671 1.00 10.15 C ANISOU 1987 CB ASP C 13 1306 1328 1220 -96 -29 -111 C ATOM 1988 CG ASP A 13 42.979 56.574 86.045 1.00 13.06 C ANISOU 1988 CG ASP C 13 1661 1737 1563 -114 34 33 C ATOM 1989 OD1 ASP A 13 42.168 56.867 86.938 1.00 14.56 O ANISOU 1989 OD1 ASP C 13 1504 2276 1753 -91 -26 51 O ATOM 1990 OD2 ASP A 13 43.922 55.784 86.280 1.00 16.95 O ANISOU 1990 OD2 ASP C 13 2233 2151 2055 -282 38 154 O ATOM 1991 N HIS A 14 40.438 57.261 81.883 1.00 9.47 N ANISOU 1991 N HIS C 14 1160 1281 1158 -31 15 -29 N ATOM 1992 CA HIS A 14 40.273 57.824 80.541 1.00 9.50 C ANISOU 1992 CA HIS C 14 1164 1266 1177 -84 13 -38 C ATOM 1993 C HIS A 14 39.703 59.225 80.505 1.00 9.55 C ANISOU 1993 C HIS C 14 1205 1264 1159 -122 13 -32 C ATOM 1994 O HIS A 14 39.027 59.673 81.452 1.00 9.72 O ANISOU 1994 O HIS C 14 1099 1202 1390 -302 -18 -35 O ATOM 1995 CB HIS A 14 39.418 56.881 79.710 1.00 9.86 C ANISOU 1995 CB HIS C 14 1107 1323 1316 -101 56 -16 C ATOM 1996 CG HIS A 14 39.881 55.464 79.781 1.00 9.03 C ANISOU 1996 CG HIS C 14 1001 1129 1299 7 -106 5 C ATOM 1997 ND1 HIS A 14 39.603 54.636 80.851 1.00 8.46 N ANISOU 1997 ND1 HIS C 14 982 811 1420 -56 -30 -106 N ATOM 1998 CD2 HIS A 14 40.696 54.758 78.960 1.00 10.78 C ANISOU 1998 CD2 HIS C 14 1494 1200 1400 -139 -141 -64 C ATOM 1999 CE1 HIS A 14 40.153 53.453 80.639 1.00 10.27 C ANISOU 1999 CE1 HIS C 14 1056 1188 1658 -56 -46 6 C ATOM 2000 NE2 HIS A 14 40.836 53.510 79.512 1.00 9.97 N ANISOU 2000 NE2 HIS C 14 1219 1061 1508 -9 -102 -194 N ATOM 2001 N SER A 15 39.941 59.918 79.391 1.00 9.77 N ANISOU 2001 N SER C 15 1198 1231 1282 -119 -59 -2 N ATOM 2002 CA SER A 15 39.470 61.296 79.264 1.00 10.35 C ANISOU 2002 CA SER C 15 1315 1260 1356 -40 20 -29 C ATOM 2003 C SER A 15 38.109 61.369 78.557 1.00 10.62 C ANISOU 2003 C SER C 15 1395 1252 1386 -55 89 -27 C ATOM 2004 O SER A 15 37.617 62.451 78.304 1.00 11.12 O ANISOU 2004 O SER C 15 1451 1271 1501 -157 130 1 O ATOM 2005 CB SER A 15 40.525 62.177 78.590 1.00 11.02 C ANISOU 2005 CB SER C 15 1419 1513 1255 29 -22 -11 C ATOM 2006 OG SER A 15 41.648 62.374 79.453 1.00 11.21 O ANISOU 2006 OG SER C 15 1455 1438 1366 11 -8 -200 O ATOM 2007 N ASN A 16 37.502 60.219 78.266 1.00 10.48 N ANISOU 2007 N ASN C 16 1338 1225 1417 -90 96 -30 N ATOM 2008 CA ASN A 16 36.171 60.192 77.685 1.00 10.36 C ANISOU 2008 CA ASN C 16 1311 1263 1363 -20 100 -54 C ATOM 2009 C ASN A 16 35.392 58.965 78.154 1.00 9.90 C ANISOU 2009 C ASN C 16 1313 1200 1247 -86 109 -90 C ATOM 2010 O ASN A 16 35.947 58.016 78.717 1.00 9.74 O ANISOU 2010 O ASN C 16 1271 1134 1293 -165 130 -171 O ATOM 2011 CB ASN A 16 36.213 60.290 76.157 1.00 10.54 C ANISOU 2011 CB ASN C 16 1387 1234 1381 -13 68 -54 C ATOM 2012 CG ASN A 16 37.099 59.242 75.520 1.00 11.32 C ANISOU 2012 CG ASN C 16 1282 1475 1541 -6 66 26 C ATOM 2013 OD1 ASN A 16 37.137 58.112 75.953 1.00 11.11 O ANISOU 2013 OD1 ASN C 16 1393 1067 1759 -97 -20 -235 O ATOM 2014 ND2 ASN A 16 37.792 59.615 74.471 1.00 14.83 N ANISOU 2014 ND2 ASN C 16 1808 1896 1931 -13 -135 175 N ATOM 2015 N LEU A 17 34.085 59.022 77.943 1.00 9.67 N ANISOU 2015 N LEU C 17 1245 1251 1177 -115 21 -93 N ATOM 2016 CA LEU A 17 33.192 57.989 78.395 1.00 9.65 C ANISOU 2016 CA LEU C 17 1262 1172 1230 -118 92 -77 C ATOM 2017 C LEU A 17 33.468 56.655 77.676 1.00 8.76 C ANISOU 2017 C LEU C 17 1221 992 1115 -137 85 -9 C ATOM 2018 O LEU A 17 33.523 55.599 78.323 1.00 9.14 O ANISOU 2018 O LEU C 17 1381 949 1139 -199 188 -24 O ATOM 2019 CB LEU A 17 31.744 58.448 78.181 1.00 10.25 C ANISOU 2019 CB LEU C 17 1375 1277 1239 -125 113 -45 C ATOM 2020 CG LEU A 17 30.657 57.509 78.652 1.00 12.72 C ANISOU 2020 CG LEU C 17 1547 1730 1554 -95 52 -20 C ATOM 2021 CD1 LEU A 17 30.707 57.374 80.170 1.00 14.60 C ANISOU 2021 CD1 LEU C 17 1876 2098 1572 -47 -27 130 C ATOM 2022 CD2 LEU A 17 29.314 58.038 78.183 1.00 12.89 C ANISOU 2022 CD2 LEU C 17 1513 1816 1566 6 -38 -221 C ATOM 2023 N LYS A 18 33.601 56.697 76.349 1.00 8.87 N ANISOU 2023 N LYS C 18 1209 986 1173 -123 98 -104 N ATOM 2024 CA LYS A 18 33.805 55.456 75.584 1.00 9.30 C ANISOU 2024 CA LYS C 18 1284 1029 1221 -107 55 -51 C ATOM 2025 C LYS A 18 35.075 54.722 76.025 1.00 10.29 C ANISOU 2025 C LYS C 18 1295 1227 1384 -73 17 -41 C ATOM 2026 O LYS A 18 35.081 53.497 76.099 1.00 10.92 O ANISOU 2026 O LYS C 18 1499 1122 1527 -108 -88 -19 O ATOM 2027 CB LYS A 18 33.857 55.713 74.090 1.00 9.36 C ANISOU 2027 CB LYS C 18 1178 1195 1182 -64 85 -143 C ATOM 2028 CG LYS A 18 35.047 56.503 73.584 1.00 9.94 C ANISOU 2028 CG LYS C 18 1190 1259 1325 -182 29 115 C ATOM 2029 CD LYS A 18 34.906 56.755 72.106 1.00 13.31 C ANISOU 2029 CD LYS C 18 1738 1685 1632 -177 -46 0 C ATOM 2030 CE LYS A 18 36.136 57.437 71.510 1.00 13.97 C ANISOU 2030 CE LYS C 18 1801 1666 1840 -37 5 141 C ATOM 2031 NZ LYS A 18 35.989 57.715 70.050 1.00 14.78 N ANISOU 2031 NZ LYS C 18 1942 1983 1691 -214 -49 203 N ATOM 2032 N GLY A 19 36.130 55.458 76.351 1.00 9.66 N ANISOU 2032 N GLY C 19 1277 1087 1304 -63 -19 -65 N ATOM 2033 CA GLY A 19 37.378 54.817 76.775 1.00 10.35 C ANISOU 2033 CA GLY C 19 1246 1293 1393 -19 23 -42 C ATOM 2034 C GLY A 19 37.199 54.041 78.062 1.00 10.65 C ANISOU 2034 C GLY C 19 1312 1280 1452 -33 1 -66 C ATOM 2035 O GLY A 19 37.630 52.894 78.165 1.00 12.01 O ANISOU 2035 O GLY C 19 1520 1429 1612 -101 35 -26 O ATOM 2036 N ALA A 20 36.519 54.648 79.035 1.00 9.74 N ANISOU 2036 N ALA C 20 1249 1082 1369 -31 8 -137 N ATOM 2037 CA ALA A 20 36.225 53.958 80.303 1.00 10.15 C ANISOU 2037 CA ALA C 20 1279 1200 1377 5 30 -91 C ATOM 2038 C ALA A 20 35.335 52.739 80.126 1.00 10.73 C ANISOU 2038 C ALA C 20 1401 1207 1468 -21 63 -73 C ATOM 2039 O ALA A 20 35.584 51.714 80.713 1.00 10.75 O ANISOU 2039 O ALA C 20 1323 1187 1575 4 124 -154 O ATOM 2040 CB ALA A 20 35.596 54.910 81.301 1.00 10.96 C ANISOU 2040 CB ALA C 20 1452 1227 1482 -87 -33 -46 C ATOM 2041 N ILE A 21 34.246 52.890 79.380 1.00 10.76 N ANISOU 2041 N ILE C 21 1331 1226 1531 0 86 -42 N ATOM 2042 CA ILE A 21 33.313 51.793 79.214 1.00 10.71 C ANISOU 2042 CA ILE C 21 1404 1228 1437 -41 90 -45 C ATOM 2043 C ILE A 21 33.948 50.616 78.468 1.00 9.18 C ANISOU 2043 C ILE C 21 1272 939 1275 -74 98 -20 C ATOM 2044 O ILE A 21 33.833 49.475 78.919 1.00 9.86 O ANISOU 2044 O ILE C 21 1503 843 1399 -151 77 -78 O ATOM 2045 CB ILE A 21 32.016 52.259 78.521 1.00 10.77 C ANISOU 2045 CB ILE C 21 1319 1273 1498 -29 64 -33 C ATOM 2046 CG1 ILE A 21 31.348 53.345 79.387 1.00 11.85 C ANISOU 2046 CG1 ILE C 21 1441 1455 1603 -139 105 -74 C ATOM 2047 CG2 ILE A 21 31.100 51.049 78.303 1.00 11.96 C ANISOU 2047 CG2 ILE C 21 1604 1327 1611 2 51 -149 C ATOM 2048 CD1 ILE A 21 30.063 53.920 78.843 1.00 13.22 C ANISOU 2048 CD1 ILE C 21 1517 1820 1685 10 -38 -64 C ATOM 2049 N THR A 22 34.615 50.895 77.364 1.00 9.05 N ANISOU 2049 N THR C 22 1248 887 1304 -121 71 -60 N ATOM 2050 CA THR A 22 35.291 49.855 76.577 1.00 9.24 C ANISOU 2050 CA THR C 22 1287 1006 1216 -91 45 -125 C ATOM 2051 C THR A 22 36.354 49.140 77.417 1.00 9.78 C ANISOU 2051 C THR C 22 1310 1099 1304 -92 107 -159 C ATOM 2052 O THR A 22 36.430 47.909 77.404 1.00 10.37 O ANISOU 2052 O THR C 22 1492 1087 1361 -128 181 -112 O ATOM 2053 CB THR A 22 35.849 50.423 75.270 1.00 9.42 C ANISOU 2053 CB THR C 22 1348 994 1236 -69 119 -164 C ATOM 2054 OG1 THR A 22 34.751 50.947 74.510 1.00 11.21 O ANISOU 2054 OG1 THR C 22 1695 1311 1251 -169 112 -148 O ATOM 2055 CG2 THR A 22 36.537 49.317 74.407 1.00 10.44 C ANISOU 2055 CG2 THR C 22 1362 1330 1271 -187 44 -47 C ATOM 2056 N ALA A 23 37.150 49.898 78.171 1.00 9.78 N ANISOU 2056 N ALA C 23 1364 968 1382 -79 116 -151 N ATOM 2057 CA ALA A 23 38.163 49.314 79.067 1.00 10.75 C ANISOU 2057 CA ALA C 23 1403 1208 1473 -85 74 -86 C ATOM 2058 C ALA A 23 37.542 48.421 80.155 1.00 10.93 C ANISOU 2058 C ALA C 23 1387 1259 1507 -50 86 -1 C ATOM 2059 O ALA A 23 38.036 47.312 80.448 1.00 12.11 O ANISOU 2059 O ALA C 23 1576 1337 1687 -49 94 25 O ATOM 2060 CB ALA A 23 39.038 50.376 79.676 1.00 11.27 C ANISOU 2060 CB ALA C 23 1472 1276 1533 -105 114 -108 C ATOM 2061 N ALA A 24 36.453 48.889 80.754 1.00 10.41 N ANISOU 2061 N ALA C 24 1424 1162 1370 -19 91 -6 N ATOM 2062 CA ALA A 24 35.767 48.121 81.785 1.00 10.32 C ANISOU 2062 CA ALA C 24 1425 1174 1322 24 82 -17 C ATOM 2063 C ALA A 24 35.213 46.804 81.254 1.00 11.29 C ANISOU 2063 C ALA C 24 1621 1234 1434 -7 96 21 C ATOM 2064 O ALA A 24 35.345 45.752 81.906 1.00 12.60 O ANISOU 2064 O ALA C 24 1976 1220 1591 38 133 -33 O ATOM 2065 CB ALA A 24 34.658 48.951 82.402 1.00 10.81 C ANISOU 2065 CB ALA C 24 1438 1284 1386 7 92 10 C ATOM 2066 N VAL A 25 34.596 46.849 80.079 1.00 11.17 N ANISOU 2066 N VAL C 25 1636 1147 1460 -8 96 24 N ATOM 2067 CA VAL A 25 34.008 45.665 79.505 1.00 12.68 C ANISOU 2067 CA VAL C 25 1704 1460 1652 29 134 -13 C ATOM 2068 C VAL A 25 35.101 44.647 79.176 1.00 12.07 C ANISOU 2068 C VAL C 25 1725 1222 1637 0 114 18 C ATOM 2069 O VAL A 25 34.910 43.442 79.345 1.00 13.18 O ANISOU 2069 O VAL C 25 1925 1227 1856 100 169 -8 O ATOM 2070 CB VAL A 25 33.124 46.029 78.283 1.00 12.17 C ANISOU 2070 CB VAL C 25 1686 1352 1586 9 154 -7 C ATOM 2071 CG1 VAL A 25 32.784 44.784 77.450 1.00 14.56 C ANISOU 2071 CG1 VAL C 25 1945 1657 1931 20 134 -124 C ATOM 2072 CG2 VAL A 25 31.864 46.730 78.768 1.00 13.84 C ANISOU 2072 CG2 VAL C 25 1767 1746 1745 -51 169 3 C ATOM 2073 N SER A 26 36.282 45.131 78.785 1.00 12.55 N ANISOU 2073 N SER C 26 1749 1351 1667 -15 105 12 N ATOM 2074 CA SER A 26 37.396 44.251 78.417 1.00 13.22 C ANISOU 2074 CA SER C 26 1852 1466 1703 -71 31 12 C ATOM 2075 C SER A 26 37.946 43.406 79.589 1.00 14.34 C ANISOU 2075 C SER C 26 1986 1652 1808 -128 75 17 C ATOM 2076 O SER A 26 38.460 42.319 79.360 1.00 15.15 O ANISOU 2076 O SER C 26 2181 1618 1957 -95 -4 32 O ATOM 2077 CB SER A 26 38.533 45.009 77.739 1.00 12.71 C ANISOU 2077 CB SER C 26 1776 1381 1670 -88 67 8 C ATOM 2078 OG SER A 26 39.285 45.789 78.671 1.00 13.65 O ANISOU 2078 OG SER C 26 1977 1464 1744 -37 -16 -21 O ATOM 2079 N VAL A 27 37.839 43.899 80.827 1.00 13.91 N ANISOU 2079 N VAL C 27 1949 1540 1796 -131 55 -16 N ATOM 2080 CA VAL A 27 38.400 43.175 81.971 1.00 14.51 C ANISOU 2080 CA VAL C 27 1927 1744 1839 -16 79 3 C ATOM 2081 C VAL A 27 37.444 42.937 83.126 1.00 14.86 C ANISOU 2081 C VAL C 27 1936 1788 1919 -8 73 -28 C ATOM 2082 O VAL A 27 37.802 42.251 84.078 1.00 14.80 O ANISOU 2082 O VAL C 27 1962 1770 1888 -17 100 8 O ATOM 2083 CB VAL A 27 39.653 43.885 82.539 1.00 14.60 C ANISOU 2083 CB VAL C 27 1914 1762 1871 -16 49 -10 C ATOM 2084 CG1 VAL A 27 40.741 44.030 81.483 1.00 14.56 C ANISOU 2084 CG1 VAL C 27 1880 1781 1870 11 13 33 C ATOM 2085 CG2 VAL A 27 39.271 45.234 83.133 1.00 15.03 C ANISOU 2085 CG2 VAL C 27 1859 1867 1983 23 0 29 C ATOM 2086 N GLY A 28 36.230 43.469 83.056 1.00 15.93 N ANISOU 2086 N GLY C 28 2019 1959 2075 -22 73 16 N ATOM 2087 CA GLY A 28 35.361 43.515 84.230 1.00 17.55 C ANISOU 2087 CA GLY C 28 2204 2230 2231 -2 41 47 C ATOM 2088 C GLY A 28 35.131 42.191 84.919 1.00 18.71 C ANISOU 2088 C GLY C 28 2349 2411 2345 -4 45 72 C ATOM 2089 O GLY A 28 35.167 42.123 86.153 1.00 19.28 O ANISOU 2089 O GLY C 28 2470 2493 2360 2 37 92 O ATOM 2090 N ASN A 29 34.926 41.148 84.126 1.00 19.60 N ANISOU 2090 N ASN C 29 2498 2509 2439 -7 49 71 N ATOM 2091 CA ASN A 29 34.605 39.835 84.643 1.00 20.81 C ANISOU 2091 CA ASN C 29 2636 2611 2657 46 75 19 C ATOM 2092 C ASN A 29 35.807 39.133 85.277 1.00 20.49 C ANISOU 2092 C ASN C 29 2572 2583 2630 63 42 46 C ATOM 2093 O ASN A 29 35.633 38.184 86.054 1.00 20.74 O ANISOU 2093 O ASN C 29 2599 2558 2723 128 88 106 O ATOM 2094 CB ASN A 29 33.918 38.994 83.560 1.00 21.69 C ANISOU 2094 CB ASN C 29 2786 2716 2737 40 74 -3 C ATOM 2095 CG ASN A 29 32.499 39.498 83.273 1.00 24.71 C ANISOU 2095 CG ASN C 29 3056 3155 3177 84 68 -38 C ATOM 2096 OD1 ASN A 29 31.708 39.708 84.202 1.00 28.81 O ANISOU 2096 OD1 ASN C 29 3555 3662 3727 110 -12 -71 O ATOM 2097 ND2 ASN A 29 32.188 39.744 81.998 1.00 27.17 N ANISOU 2097 ND2 ASN C 29 3474 3452 3395 112 105 0 N ATOM 2098 N GLU A 30 37.010 39.640 84.996 1.00 19.43 N ANISOU 2098 N GLU C 30 2439 2436 2507 75 21 44 N ATOM 2099 CA GLU A 30 38.241 39.064 85.520 1.00 18.46 C ANISOU 2099 CA GLU C 30 2329 2300 2385 -1 3 46 C ATOM 2100 C GLU A 30 38.841 39.847 86.692 1.00 17.50 C ANISOU 2100 C GLU C 30 2219 2131 2296 -24 16 50 C ATOM 2101 O GLU A 30 39.930 39.511 87.182 1.00 18.06 O ANISOU 2101 O GLU C 30 2237 2149 2473 -31 82 47 O ATOM 2102 CB GLU A 30 39.295 38.927 84.408 1.00 18.16 C ANISOU 2102 CB GLU C 30 2313 2223 2364 12 -27 55 C ATOM 2103 CG GLU A 30 38.951 37.955 83.302 1.00 19.97 C ANISOU 2103 CG GLU C 30 2577 2465 2545 -73 -77 30 C ATOM 2104 CD GLU A 30 38.560 36.576 83.822 1.00 22.19 C ANISOU 2104 CD GLU C 30 2838 2640 2951 0 -86 -83 C ATOM 2105 OE1 GLU A 30 39.133 36.095 84.837 1.00 21.75 O ANISOU 2105 OE1 GLU C 30 3034 2270 2959 -114 -162 -54 O ATOM 2106 OE2 GLU A 30 37.658 35.990 83.210 1.00 25.48 O ANISOU 2106 OE2 GLU C 30 3213 3088 3378 39 -150 -222 O ATOM 2107 N VAL A 31 38.167 40.906 87.121 1.00 16.00 N ANISOU 2107 N VAL C 31 2091 1943 2044 -54 54 87 N ATOM 2108 CA VAL A 31 38.630 41.694 88.264 1.00 15.45 C ANISOU 2108 CA VAL C 31 1972 1879 2016 -24 82 58 C ATOM 2109 C VAL A 31 37.608 41.658 89.382 1.00 15.09 C ANISOU 2109 C VAL C 31 1936 1813 1981 -15 76 85 C ATOM 2110 O VAL A 31 36.474 41.224 89.176 1.00 15.25 O ANISOU 2110 O VAL C 31 1887 1948 1956 47 201 64 O ATOM 2111 CB VAL A 31 38.945 43.176 87.882 1.00 14.78 C ANISOU 2111 CB VAL C 31 1900 1749 1967 -5 79 56 C ATOM 2112 CG1 VAL A 31 39.943 43.251 86.734 1.00 15.33 C ANISOU 2112 CG1 VAL C 31 2095 1859 1870 2 160 -22 C ATOM 2113 CG2 VAL A 31 37.678 43.954 87.557 1.00 15.65 C ANISOU 2113 CG2 VAL C 31 1846 2037 2061 49 25 43 C ATOM 2114 N ASP A 32 38.010 42.131 90.559 1.00 15.54 N ANISOU 2114 N ASP C 32 1967 1959 1978 -29 78 27 N ATOM 2115 CA ASP A 32 37.136 42.214 91.740 1.00 15.80 C ANISOU 2115 CA ASP C 32 1981 1959 2063 -70 -9 40 C ATOM 2116 C ASP A 32 36.519 43.593 91.956 1.00 15.69 C ANISOU 2116 C ASP C 32 1987 1926 2048 -78 -46 17 C ATOM 2117 O ASP A 32 35.421 43.712 92.507 1.00 15.53 O ANISOU 2117 O ASP C 32 1968 1857 2074 -132 -103 105 O ATOM 2118 CB ASP A 32 37.923 41.852 92.995 1.00 16.29 C ANISOU 2118 CB ASP C 32 2032 2077 2080 -83 -24 29 C ATOM 2119 CG ASP A 32 38.642 40.535 92.858 1.00 16.90 C ANISOU 2119 CG ASP C 32 2147 2063 2210 -42 -16 31 C ATOM 2120 OD1 ASP A 32 37.961 39.520 92.579 1.00 19.46 O ANISOU 2120 OD1 ASP C 32 2455 2410 2529 115 -80 230 O ATOM 2121 OD2 ASP A 32 39.893 40.484 92.965 1.00 18.50 O ANISOU 2121 OD2 ASP C 32 2279 2391 2358 -114 58 103 O ATOM 2122 N VAL A 33 37.251 44.625 91.556 1.00 15.00 N ANISOU 2122 N VAL C 33 1977 1807 1915 -121 -53 11 N ATOM 2123 CA VAL A 33 36.850 46.001 91.808 1.00 14.39 C ANISOU 2123 CA VAL C 33 1934 1709 1825 -91 -45 25 C ATOM 2124 C VAL A 33 37.048 46.831 90.540 1.00 14.00 C ANISOU 2124 C VAL C 33 1869 1633 1816 -33 -30 35 C ATOM 2125 O VAL A 33 38.063 46.698 89.850 1.00 13.72 O ANISOU 2125 O VAL C 33 1803 1615 1792 -104 -66 39 O ATOM 2126 CB VAL A 33 37.674 46.629 92.937 1.00 14.30 C ANISOU 2126 CB VAL C 33 1906 1719 1806 -130 -41 68 C ATOM 2127 CG1 VAL A 33 37.062 47.947 93.345 1.00 13.81 C ANISOU 2127 CG1 VAL C 33 1851 1664 1729 -156 -12 36 C ATOM 2128 CG2 VAL A 33 37.785 45.683 94.158 1.00 15.42 C ANISOU 2128 CG2 VAL C 33 2126 1861 1872 -68 -14 128 C ATOM 2129 N ILE A 34 36.074 47.671 90.217 1.00 13.12 N ANISOU 2129 N ILE C 34 1730 1558 1696 -40 -58 40 N ATOM 2130 CA ILE A 34 36.176 48.553 89.050 1.00 13.02 C ANISOU 2130 CA ILE C 34 1772 1582 1590 -35 -52 41 C ATOM 2131 C ILE A 34 36.059 49.986 89.546 1.00 12.12 C ANISOU 2131 C ILE C 34 1670 1471 1463 -104 -96 79 C ATOM 2132 O ILE A 34 35.111 50.326 90.255 1.00 12.93 O ANISOU 2132 O ILE C 34 1713 1656 1544 -125 -140 177 O ATOM 2133 CB ILE A 34 35.082 48.246 88.057 1.00 13.10 C ANISOU 2133 CB ILE C 34 1797 1616 1562 -46 -57 17 C ATOM 2134 CG1 ILE A 34 35.192 46.773 87.645 1.00 14.50 C ANISOU 2134 CG1 ILE C 34 1922 1783 1804 21 7 -46 C ATOM 2135 CG2 ILE A 34 35.134 49.235 86.868 1.00 12.87 C ANISOU 2135 CG2 ILE C 34 1914 1423 1553 45 0 30 C ATOM 2136 CD1 ILE A 34 34.073 46.309 86.786 1.00 15.96 C ANISOU 2136 CD1 ILE C 34 2036 1956 2072 194 142 -95 C ATOM 2137 N GLU A 35 37.000 50.835 89.134 1.00 11.23 N ANISOU 2137 N GLU C 35 1564 1377 1324 -133 -122 0 N ATOM 2138 CA GLU A 35 37.095 52.194 89.658 1.00 11.05 C ANISOU 2138 CA GLU C 35 1508 1362 1328 -51 -51 83 C ATOM 2139 C GLU A 35 36.955 53.239 88.555 1.00 11.00 C ANISOU 2139 C GLU C 35 1497 1373 1309 -137 -66 87 C ATOM 2140 O GLU A 35 37.714 53.219 87.587 1.00 11.45 O ANISOU 2140 O GLU C 35 1511 1536 1301 -99 -30 155 O ATOM 2141 CB GLU A 35 38.440 52.376 90.368 1.00 11.40 C ANISOU 2141 CB GLU C 35 1583 1427 1321 -145 -23 12 C ATOM 2142 CG GLU A 35 38.730 53.803 90.829 1.00 12.26 C ANISOU 2142 CG GLU C 35 1614 1529 1514 5 -25 31 C ATOM 2143 CD GLU A 35 40.069 53.968 91.522 1.00 14.84 C ANISOU 2143 CD GLU C 35 1937 1920 1780 -164 1 -91 C ATOM 2144 OE1 GLU A 35 41.025 53.206 91.223 1.00 14.02 O ANISOU 2144 OE1 GLU C 35 1778 1902 1646 -266 -104 -88 O ATOM 2145 OE2 GLU A 35 40.192 54.900 92.349 1.00 15.66 O ANISOU 2145 OE2 GLU C 35 2327 1863 1760 -200 40 -340 O ATOM 2146 N ALA A 36 35.974 54.126 88.713 1.00 10.85 N ANISOU 2146 N ALA C 36 1374 1432 1316 -107 -63 123 N ATOM 2147 CA ALA A 36 35.850 55.301 87.872 1.00 10.55 C ANISOU 2147 CA ALA C 36 1346 1259 1402 -83 -18 49 C ATOM 2148 C ALA A 36 36.850 56.360 88.383 1.00 10.15 C ANISOU 2148 C ALA C 36 1293 1225 1336 -51 27 64 C ATOM 2149 O ALA A 36 36.630 56.978 89.435 1.00 10.56 O ANISOU 2149 O ALA C 36 1414 1216 1380 -5 2 29 O ATOM 2150 CB ALA A 36 34.401 55.818 87.896 1.00 10.35 C ANISOU 2150 CB ALA C 36 1262 1329 1338 5 -56 111 C ATOM 2151 N GLY A 37 37.962 56.525 87.673 1.00 10.40 N ANISOU 2151 N GLY C 37 1378 1226 1345 -67 5 -48 N ATOM 2152 CA GLY A 37 39.046 57.418 88.120 1.00 10.19 C ANISOU 2152 CA GLY C 37 1355 1246 1270 -73 2 -39 C ATOM 2153 C GLY A 37 38.718 58.921 88.066 1.00 10.66 C ANISOU 2153 C GLY C 37 1397 1359 1294 -72 -16 -73 C ATOM 2154 O GLY A 37 37.834 59.345 87.345 1.00 10.56 O ANISOU 2154 O GLY C 37 1414 1348 1248 -130 4 -83 O ATOM 2155 N THR A 38 39.459 59.729 88.821 1.00 10.83 N ANISOU 2155 N THR C 38 1381 1392 1339 -59 -32 -122 N ATOM 2156 CA THR A 38 39.206 61.164 88.888 1.00 10.76 C ANISOU 2156 CA THR C 38 1330 1425 1330 -59 9 -107 C ATOM 2157 C THR A 38 39.248 61.858 87.558 1.00 10.09 C ANISOU 2157 C THR C 38 1204 1321 1307 -51 -32 -161 C ATOM 2158 O THR A 38 38.399 62.672 87.273 1.00 10.05 O ANISOU 2158 O THR C 38 1175 1202 1441 -114 -61 -266 O ATOM 2159 CB THR A 38 40.166 61.897 89.858 1.00 11.15 C ANISOU 2159 CB THR C 38 1357 1496 1382 -20 26 -85 C ATOM 2160 OG1 THR A 38 40.420 61.060 90.987 1.00 10.90 O ANISOU 2160 OG1 THR C 38 1365 1603 1171 -98 92 -109 O ATOM 2161 CG2 THR A 38 39.501 63.133 90.388 1.00 12.35 C ANISOU 2161 CG2 THR C 38 1769 1521 1402 -69 2 -66 C ATOM 2162 N VAL A 39 40.213 61.496 86.713 1.00 9.16 N ANISOU 2162 N VAL C 39 1018 1258 1203 -89 -75 -178 N ATOM 2163 CA VAL A 39 40.337 62.148 85.422 1.00 9.10 C ANISOU 2163 CA VAL C 39 1134 1133 1189 -111 -60 -141 C ATOM 2164 C VAL A 39 39.057 61.947 84.617 1.00 9.12 C ANISOU 2164 C VAL C 39 1127 1192 1144 -104 -45 -142 C ATOM 2165 O VAL A 39 38.582 62.865 83.963 1.00 9.08 O ANISOU 2165 O VAL C 39 1222 1167 1061 -140 30 -252 O ATOM 2166 CB VAL A 39 41.547 61.584 84.630 1.00 9.26 C ANISOU 2166 CB VAL C 39 1154 1107 1255 -136 -115 -68 C ATOM 2167 CG1 VAL A 39 41.441 61.935 83.172 1.00 9.79 C ANISOU 2167 CG1 VAL C 39 1170 1235 1313 -117 -80 -136 C ATOM 2168 CG2 VAL A 39 42.855 62.073 85.250 1.00 9.59 C ANISOU 2168 CG2 VAL C 39 1274 1123 1244 -216 -71 -97 C ATOM 2169 N CYS A 40 38.530 60.731 84.670 1.00 9.48 N ANISOU 2169 N CYS C 40 1200 1214 1186 -149 -30 -139 N ATOM 2170 CA CYS A 40 37.331 60.379 83.924 1.00 9.42 C ANISOU 2170 CA CYS C 40 1128 1209 1240 -26 -35 -99 C ATOM 2171 C CYS A 40 36.086 61.054 84.500 1.00 9.48 C ANISOU 2171 C CYS C 40 1229 1203 1168 -84 -7 -138 C ATOM 2172 O CYS A 40 35.312 61.640 83.744 1.00 8.14 O ANISOU 2172 O CYS C 40 972 1028 1091 -93 -10 -208 O ATOM 2173 CB CYS A 40 37.143 58.877 83.870 1.00 10.78 C ANISOU 2173 CB CYS C 40 1404 1343 1347 -55 -13 -82 C ATOM 2174 SG CYS A 40 36.013 58.341 82.571 1.00 11.90 S ANISOU 2174 SG CYS C 40 1306 1320 1893 -73 -41 -277 S ATOM 2175 N LEU A 41 35.909 60.975 85.822 1.00 9.24 N ANISOU 2175 N LEU C 41 1134 1205 1169 -92 -66 -89 N ATOM 2176 CA LEU A 41 34.760 61.597 86.471 1.00 9.85 C ANISOU 2176 CA LEU C 41 1237 1357 1146 -83 -10 -54 C ATOM 2177 C LEU A 41 34.730 63.097 86.202 1.00 9.13 C ANISOU 2177 C LEU C 41 1169 1216 1083 -46 3 -81 C ATOM 2178 O LEU A 41 33.676 63.668 85.927 1.00 8.89 O ANISOU 2178 O LEU C 41 1214 1234 930 -32 116 -205 O ATOM 2179 CB LEU A 41 34.751 61.323 87.989 1.00 10.01 C ANISOU 2179 CB LEU C 41 1187 1476 1138 -112 -50 1 C ATOM 2180 CG LEU A 41 34.452 59.884 88.423 1.00 10.81 C ANISOU 2180 CG LEU C 41 1208 1624 1275 -57 12 75 C ATOM 2181 CD1 LEU A 41 34.634 59.764 89.921 1.00 12.66 C ANISOU 2181 CD1 LEU C 41 1564 1845 1400 16 -89 -2 C ATOM 2182 CD2 LEU A 41 33.057 59.365 87.986 1.00 10.83 C ANISOU 2182 CD2 LEU C 41 1473 1315 1324 52 115 19 C ATOM 2183 N LEU A 42 35.885 63.747 86.268 1.00 8.82 N ANISOU 2183 N LEU C 42 1103 1194 1052 -58 48 -101 N ATOM 2184 CA LEU A 42 35.924 65.173 85.979 1.00 9.23 C ANISOU 2184 CA LEU C 42 1172 1154 1180 -12 7 -116 C ATOM 2185 C LEU A 42 35.576 65.514 84.518 1.00 9.36 C ANISOU 2185 C LEU C 42 1239 1100 1217 -20 27 -148 C ATOM 2186 O LEU A 42 35.136 66.634 84.217 1.00 9.40 O ANISOU 2186 O LEU C 42 1278 1028 1264 -174 10 -241 O ATOM 2187 CB LEU A 42 37.258 65.785 86.378 1.00 9.31 C ANISOU 2187 CB LEU C 42 1126 1320 1090 -8 29 -134 C ATOM 2188 CG LEU A 42 37.549 65.900 87.875 1.00 9.66 C ANISOU 2188 CG LEU C 42 1244 1223 1203 43 119 -113 C ATOM 2189 CD1 LEU A 42 39.048 66.163 88.044 1.00 9.99 C ANISOU 2189 CD1 LEU C 42 1103 1473 1218 -89 -36 -235 C ATOM 2190 CD2 LEU A 42 36.695 66.974 88.542 1.00 10.30 C ANISOU 2190 CD2 LEU C 42 1241 1517 1153 -96 9 -351 C ATOM 2191 N GLN A 43 35.765 64.553 83.606 1.00 8.89 N ANISOU 2191 N GLN C 43 1214 1043 1120 -122 -78 -220 N ATOM 2192 CA GLN A 43 35.354 64.722 82.219 1.00 8.64 C ANISOU 2192 CA GLN C 43 1171 942 1170 -140 -93 -124 C ATOM 2193 C GLN A 43 33.879 64.405 81.952 1.00 8.47 C ANISOU 2193 C GLN C 43 1257 919 1041 -117 -59 -186 C ATOM 2194 O GLN A 43 33.243 65.080 81.173 1.00 8.37 O ANISOU 2194 O GLN C 43 1228 855 1098 -189 -97 -141 O ATOM 2195 CB GLN A 43 36.208 63.831 81.323 1.00 8.79 C ANISOU 2195 CB GLN C 43 1274 928 1137 -120 -113 -113 C ATOM 2196 CG GLN A 43 37.569 64.360 81.059 1.00 8.30 C ANISOU 2196 CG GLN C 43 1209 742 1203 -235 -164 -31 C ATOM 2197 CD GLN A 43 37.524 65.610 80.184 1.00 9.00 C ANISOU 2197 CD GLN C 43 1303 812 1303 66 -189 33 C ATOM 2198 OE1 GLN A 43 37.279 66.713 80.660 1.00 9.68 O ANISOU 2198 OE1 GLN C 43 1044 1165 1466 -28 -141 -156 O ATOM 2199 NE2 GLN A 43 37.759 65.435 78.908 1.00 10.70 N ANISOU 2199 NE2 GLN C 43 1810 980 1275 -12 -273 94 N ATOM 2200 N VAL A 44 33.335 63.391 82.613 1.00 8.61 N ANISOU 2200 N VAL C 44 1128 1033 1108 -52 -21 -57 N ATOM 2201 CA VAL A 44 32.051 62.798 82.181 1.00 9.05 C ANISOU 2201 CA VAL C 44 1190 1102 1144 5 55 -109 C ATOM 2202 C VAL A 44 30.963 62.870 83.230 1.00 9.84 C ANISOU 2202 C VAL C 44 1218 1218 1302 -25 94 -128 C ATOM 2203 O VAL A 44 29.790 62.678 82.915 1.00 8.76 O ANISOU 2203 O VAL C 44 1009 1064 1255 34 67 -136 O ATOM 2204 CB VAL A 44 32.201 61.324 81.672 1.00 10.02 C ANISOU 2204 CB VAL C 44 1253 1221 1331 -3 48 -99 C ATOM 2205 CG1 VAL A 44 33.285 61.250 80.611 1.00 11.20 C ANISOU 2205 CG1 VAL C 44 1378 1426 1452 -38 55 -156 C ATOM 2206 CG2 VAL A 44 32.473 60.380 82.805 1.00 9.49 C ANISOU 2206 CG2 VAL C 44 1220 1072 1313 -46 -36 -222 C ATOM 2207 N GLY A 45 31.334 63.216 84.474 1.00 9.79 N ANISOU 2207 N GLY C 45 1202 1267 1249 -37 121 -173 N ATOM 2208 CA GLY A 45 30.367 63.213 85.564 1.00 9.99 C ANISOU 2208 CA GLY C 45 1242 1223 1330 -3 57 -143 C ATOM 2209 C GLY A 45 30.022 61.833 86.075 1.00 10.96 C ANISOU 2209 C GLY C 45 1365 1363 1433 -14 -29 -100 C ATOM 2210 O GLY A 45 30.623 60.836 85.681 1.00 10.45 O ANISOU 2210 O GLY C 45 1403 1094 1471 -97 -86 -129 O ATOM 2211 N SER A 46 29.065 61.798 86.997 1.00 10.47 N ANISOU 2211 N SER C 46 1302 1265 1410 -15 -68 -128 N ATOM 2212 CA SER A 46 28.795 60.645 87.810 1.00 10.49 C ANISOU 2212 CA SER C 46 1313 1298 1372 -14 -18 -92 C ATOM 2213 C SER A 46 27.935 59.571 87.134 1.00 9.44 C ANISOU 2213 C SER C 46 1222 1146 1219 60 25 -50 C ATOM 2214 O SER A 46 27.829 58.469 87.664 1.00 9.63 O ANISOU 2214 O SER C 46 1300 1317 1039 -14 23 -105 O ATOM 2215 CB SER A 46 28.178 61.070 89.140 1.00 10.77 C ANISOU 2215 CB SER C 46 1391 1248 1451 -4 -23 -78 C ATOM 2216 OG SER A 46 26.924 61.680 88.931 1.00 10.74 O ANISOU 2216 OG SER C 46 1152 1387 1539 -51 -91 -134 O ATOM 2217 N GLU A 47 27.363 59.848 85.964 1.00 9.84 N ANISOU 2217 N GLU C 47 1293 1129 1314 61 48 -62 N ATOM 2218 CA GLU A 47 26.532 58.832 85.305 1.00 10.31 C ANISOU 2218 CA GLU C 47 1327 1251 1339 27 29 -2 C ATOM 2219 C GLU A 47 27.382 57.600 84.992 1.00 10.15 C ANISOU 2219 C GLU C 47 1351 1179 1325 33 -7 -17 C ATOM 2220 O GLU A 47 26.878 56.479 84.991 1.00 11.33 O ANISOU 2220 O GLU C 47 1405 1403 1494 52 -14 -58 O ATOM 2221 CB GLU A 47 25.823 59.355 84.067 1.00 10.92 C ANISOU 2221 CB GLU C 47 1441 1325 1382 -28 42 -30 C ATOM 2222 CG GLU A 47 24.720 58.384 83.617 1.00 11.55 C ANISOU 2222 CG GLU C 47 1598 1411 1379 -69 141 1 C ATOM 2223 CD GLU A 47 23.862 58.892 82.488 1.00 14.63 C ANISOU 2223 CD GLU C 47 1940 1888 1728 -69 169 -65 C ATOM 2224 OE1 GLU A 47 24.331 59.746 81.708 1.00 17.40 O ANISOU 2224 OE1 GLU C 47 2466 2237 1907 -82 109 -44 O ATOM 2225 OE2 GLU A 47 22.722 58.398 82.376 1.00 16.00 O ANISOU 2225 OE2 GLU C 47 1876 2185 2017 14 110 -9 O ATOM 2226 N LEU A 48 28.680 57.806 84.768 1.00 10.23 N ANISOU 2226 N LEU C 48 1317 1185 1383 -35 -39 38 N ATOM 2227 CA LEU A 48 29.602 56.696 84.586 1.00 10.58 C ANISOU 2227 CA LEU C 48 1383 1286 1349 -11 -52 18 C ATOM 2228 C LEU A 48 29.513 55.638 85.708 1.00 10.32 C ANISOU 2228 C LEU C 48 1364 1256 1298 -4 -56 14 C ATOM 2229 O LEU A 48 29.565 54.437 85.421 1.00 9.90 O ANISOU 2229 O LEU C 48 1347 1134 1278 1 -31 60 O ATOM 2230 CB LEU A 48 31.029 57.187 84.433 1.00 11.23 C ANISOU 2230 CB LEU C 48 1459 1402 1406 -58 -95 -36 C ATOM 2231 CG LEU A 48 32.122 56.128 84.345 1.00 13.12 C ANISOU 2231 CG LEU C 48 1602 1633 1750 -83 21 119 C ATOM 2232 CD1 LEU A 48 31.967 55.197 83.130 1.00 14.59 C ANISOU 2232 CD1 LEU C 48 1657 1835 2051 -137 -25 85 C ATOM 2233 CD2 LEU A 48 33.476 56.839 84.366 1.00 14.55 C ANISOU 2233 CD2 LEU C 48 1702 1616 2210 -85 56 172 C ATOM 2234 N VAL A 49 29.354 56.082 86.959 1.00 10.20 N ANISOU 2234 N VAL C 49 1349 1281 1244 36 -110 31 N ATOM 2235 CA VAL A 49 29.266 55.148 88.095 1.00 10.29 C ANISOU 2235 CA VAL C 49 1370 1276 1263 -34 -13 10 C ATOM 2236 C VAL A 49 28.037 54.250 87.952 1.00 11.00 C ANISOU 2236 C VAL C 49 1417 1377 1385 -23 -10 14 C ATOM 2237 O VAL A 49 28.110 53.033 88.167 1.00 11.27 O ANISOU 2237 O VAL C 49 1340 1399 1543 9 114 107 O ATOM 2238 CB VAL A 49 29.249 55.907 89.439 1.00 10.35 C ANISOU 2238 CB VAL C 49 1330 1279 1321 -72 -41 9 C ATOM 2239 CG1 VAL A 49 29.064 54.952 90.621 1.00 11.20 C ANISOU 2239 CG1 VAL C 49 1568 1501 1186 -27 -42 60 C ATOM 2240 CG2 VAL A 49 30.560 56.726 89.599 1.00 10.55 C ANISOU 2240 CG2 VAL C 49 1458 1284 1263 53 -7 -34 C ATOM 2241 N GLU A 50 26.928 54.854 87.532 1.00 10.88 N ANISOU 2241 N GLU C 50 1407 1345 1382 14 39 18 N ATOM 2242 CA GLU A 50 25.677 54.144 87.386 1.00 11.17 C ANISOU 2242 CA GLU C 50 1428 1346 1469 0 18 -3 C ATOM 2243 C GLU A 50 25.752 53.156 86.206 1.00 10.34 C ANISOU 2243 C GLU C 50 1336 1274 1319 19 14 -8 C ATOM 2244 O GLU A 50 25.246 52.010 86.267 1.00 10.62 O ANISOU 2244 O GLU C 50 1458 1278 1299 -40 -46 115 O ATOM 2245 CB GLU A 50 24.518 55.141 87.259 1.00 11.78 C ANISOU 2245 CB GLU C 50 1448 1411 1615 -30 51 -8 C ATOM 2246 CG GLU A 50 23.164 54.505 87.461 1.00 14.75 C ANISOU 2246 CG GLU C 50 1755 1754 2095 51 31 -68 C ATOM 2247 CD GLU A 50 22.004 55.484 87.402 1.00 16.67 C ANISOU 2247 CD GLU C 50 1875 2034 2425 -51 117 -11 C ATOM 2248 OE1 GLU A 50 22.200 56.672 87.681 1.00 16.31 O ANISOU 2248 OE1 GLU C 50 1706 1937 2553 84 12 8 O ATOM 2249 OE2 GLU A 50 20.868 55.045 87.125 1.00 19.76 O ANISOU 2249 OE2 GLU C 50 2190 2428 2888 48 226 -96 O ATOM 2250 N VAL A 51 26.426 53.565 85.146 1.00 9.57 N ANISOU 2250 N VAL C 51 1333 1104 1196 -2 0 -96 N ATOM 2251 CA VAL A 51 26.625 52.665 83.993 1.00 9.65 C ANISOU 2251 CA VAL C 51 1328 1157 1182 33 22 -108 C ATOM 2252 C VAL A 51 27.444 51.449 84.426 1.00 9.87 C ANISOU 2252 C VAL C 51 1297 1197 1254 15 28 -71 C ATOM 2253 O VAL A 51 27.113 50.296 84.098 1.00 10.11 O ANISOU 2253 O VAL C 51 1383 1105 1351 85 82 29 O ATOM 2254 CB VAL A 51 27.300 53.386 82.796 1.00 9.78 C ANISOU 2254 CB VAL C 51 1340 1167 1209 9 28 -123 C ATOM 2255 CG1 VAL A 51 27.713 52.363 81.705 1.00 10.13 C ANISOU 2255 CG1 VAL C 51 1662 1011 1174 -93 34 -108 C ATOM 2256 CG2 VAL A 51 26.385 54.427 82.218 1.00 9.60 C ANISOU 2256 CG2 VAL C 51 1278 1188 1179 80 155 -56 C ATOM 2257 N LEU A 52 28.534 51.698 85.146 1.00 10.07 N ANISOU 2257 N LEU C 52 1335 1185 1305 41 61 12 N ATOM 2258 CA LEU A 52 29.396 50.609 85.627 1.00 10.20 C ANISOU 2258 CA LEU C 52 1334 1215 1324 -10 51 46 C ATOM 2259 C LEU A 52 28.634 49.666 86.561 1.00 10.61 C ANISOU 2259 C LEU C 52 1400 1316 1314 0 25 42 C ATOM 2260 O LEU A 52 28.766 48.449 86.483 1.00 10.97 O ANISOU 2260 O LEU C 52 1550 1411 1205 -9 13 -47 O ATOM 2261 CB LEU A 52 30.643 51.157 86.333 1.00 10.04 C ANISOU 2261 CB LEU C 52 1356 1170 1286 -42 123 121 C ATOM 2262 CG LEU A 52 31.632 51.915 85.451 1.00 9.14 C ANISOU 2262 CG LEU C 52 1198 1085 1187 -101 66 86 C ATOM 2263 CD1 LEU A 52 32.703 52.546 86.308 1.00 11.17 C ANISOU 2263 CD1 LEU C 52 1224 1438 1580 -96 97 177 C ATOM 2264 CD2 LEU A 52 32.234 50.961 84.406 1.00 9.75 C ANISOU 2264 CD2 LEU C 52 1395 906 1400 48 67 61 C ATOM 2265 N ARG A 53 27.798 50.239 87.417 1.00 11.72 N ANISOU 2265 N ARG C 53 1548 1464 1439 5 -4 -6 N ATOM 2266 CA ARG A 53 26.966 49.445 88.330 1.00 12.57 C ANISOU 2266 CA ARG C 53 1732 1542 1499 74 -8 -2 C ATOM 2267 C ARG A 53 26.035 48.489 87.598 1.00 12.89 C ANISOU 2267 C ARG C 53 1812 1538 1546 105 0 -4 C ATOM 2268 O ARG A 53 25.847 47.366 88.028 1.00 13.23 O ANISOU 2268 O ARG C 53 2068 1509 1449 208 112 -93 O ATOM 2269 CB ARG A 53 26.173 50.367 89.283 1.00 12.74 C ANISOU 2269 CB ARG C 53 1692 1564 1585 50 5 -22 C ATOM 2270 CG ARG A 53 25.154 49.662 90.232 1.00 14.77 C ANISOU 2270 CG ARG C 53 1912 1828 1871 82 -25 56 C ATOM 2271 CD ARG A 53 25.736 48.486 91.005 1.00 17.93 C ANISOU 2271 CD ARG C 53 2328 2293 2191 82 18 67 C ATOM 2272 NE ARG A 53 26.617 48.923 92.068 1.00 20.59 N ANISOU 2272 NE ARG C 53 2545 2712 2564 -88 57 109 N ATOM 2273 CZ ARG A 53 27.661 48.220 92.516 1.00 20.69 C ANISOU 2273 CZ ARG C 53 2679 2652 2528 -68 72 103 C ATOM 2274 NH1 ARG A 53 28.007 47.067 91.948 1.00 19.84 N ANISOU 2274 NH1 ARG C 53 2601 2525 2411 -31 155 127 N ATOM 2275 NH2 ARG A 53 28.397 48.716 93.497 1.00 20.20 N ANISOU 2275 NH2 ARG C 53 2540 2733 2399 -66 67 135 N ATOM 2276 N SER A 54 25.475 48.959 86.494 1.00 13.55 N ANISOU 2276 N SER C 54 1854 1631 1664 116 3 -13 N ATOM 2277 CA SER A 54 24.545 48.211 85.688 1.00 13.30 C ANISOU 2277 CA SER C 54 1784 1632 1635 72 15 -22 C ATOM 2278 C SER A 54 25.264 47.076 84.959 1.00 12.97 C ANISOU 2278 C SER C 54 1726 1497 1702 46 32 61 C ATOM 2279 O SER A 54 24.741 45.959 84.859 1.00 13.35 O ANISOU 2279 O SER C 54 1769 1563 1738 123 79 106 O ATOM 2280 CB SER A 54 23.850 49.175 84.723 1.00 13.40 C ANISOU 2280 CB SER C 54 1813 1563 1716 73 57 0 C ATOM 2281 OG SER A 54 22.850 48.553 83.962 1.00 14.09 O ANISOU 2281 OG SER C 54 1882 1747 1724 -109 -21 -327 O ATOM 2282 N LEU A 55 26.470 47.347 84.485 1.00 12.59 N ANISOU 2282 N LEU C 55 1689 1451 1642 12 67 31 N ATOM 2283 CA LEU A 55 27.214 46.384 83.710 1.00 12.59 C ANISOU 2283 CA LEU C 55 1711 1411 1662 -17 58 63 C ATOM 2284 C LEU A 55 27.748 45.269 84.607 1.00 14.44 C ANISOU 2284 C LEU C 55 1970 1596 1918 -26 101 33 C ATOM 2285 O LEU A 55 27.893 44.124 84.191 1.00 14.82 O ANISOU 2285 O LEU C 55 2088 1516 2027 13 198 39 O ATOM 2286 CB LEU A 55 28.382 47.091 83.040 1.00 12.34 C ANISOU 2286 CB LEU C 55 1661 1310 1717 0 111 19 C ATOM 2287 CG LEU A 55 28.128 47.844 81.754 1.00 11.10 C ANISOU 2287 CG LEU C 55 1540 1180 1495 -44 115 23 C ATOM 2288 CD1 LEU A 55 29.327 48.710 81.338 1.00 11.15 C ANISOU 2288 CD1 LEU C 55 1236 1433 1567 -124 161 -116 C ATOM 2289 CD2 LEU A 55 27.746 46.903 80.668 1.00 12.22 C ANISOU 2289 CD2 LEU C 55 1645 1305 1691 -147 316 -56 C ATOM 2290 N PHE A 56 28.049 45.660 85.838 1.00 16.43 N ANISOU 2290 N PHE C 56 2208 1927 2107 29 114 72 N ATOM 2291 CA PHE A 56 28.804 44.857 86.778 1.00 18.31 C ANISOU 2291 CA PHE C 56 2339 2255 2362 43 125 80 C ATOM 2292 C PHE A 56 28.142 44.879 88.157 1.00 19.50 C ANISOU 2292 C PHE C 56 2527 2417 2466 83 105 112 C ATOM 2293 O PHE A 56 28.621 45.511 89.067 1.00 19.76 O ANISOU 2293 O PHE C 56 2537 2455 2515 209 165 207 O ATOM 2294 CB PHE A 56 30.244 45.353 86.857 1.00 18.27 C ANISOU 2294 CB PHE C 56 2302 2274 2365 63 110 102 C ATOM 2295 CG PHE A 56 30.941 45.354 85.543 1.00 21.32 C ANISOU 2295 CG PHE C 56 2568 2765 2767 28 109 81 C ATOM 2296 CD1 PHE A 56 31.175 44.176 84.881 1.00 23.51 C ANISOU 2296 CD1 PHE C 56 2825 3086 3019 11 36 -8 C ATOM 2297 CD2 PHE A 56 31.335 46.537 84.951 1.00 22.16 C ANISOU 2297 CD2 PHE C 56 2660 2908 2850 6 26 107 C ATOM 2298 CE1 PHE A 56 31.793 44.182 83.660 1.00 25.22 C ANISOU 2298 CE1 PHE C 56 2980 3368 3231 -17 -1 50 C ATOM 2299 CE2 PHE A 56 31.945 46.533 83.744 1.00 24.22 C ANISOU 2299 CE2 PHE C 56 2888 3237 3077 -25 24 126 C ATOM 2300 CZ PHE A 56 32.171 45.364 83.094 1.00 23.70 C ANISOU 2300 CZ PHE C 56 2785 3153 3066 0 36 59 C ATOM 2301 N PRO A 57 27.025 44.174 88.282 1.00 20.97 N ANISOU 2301 N PRO C 57 2648 2647 2671 54 150 60 N ATOM 2302 CA PRO A 57 26.166 44.279 89.451 1.00 22.62 C ANISOU 2302 CA PRO C 57 2844 2852 2898 59 79 50 C ATOM 2303 C PRO A 57 26.676 43.867 90.844 1.00 24.29 C ANISOU 2303 C PRO C 57 3068 3103 3058 51 41 18 C ATOM 2304 O PRO A 57 26.454 44.641 91.754 1.00 25.92 O ANISOU 2304 O PRO C 57 3347 3269 3229 85 72 41 O ATOM 2305 CB PRO A 57 24.925 43.471 89.055 1.00 22.41 C ANISOU 2305 CB PRO C 57 2775 2809 2928 38 72 21 C ATOM 2306 CG PRO A 57 25.013 43.221 87.678 1.00 21.90 C ANISOU 2306 CG PRO C 57 2710 2818 2789 34 123 60 C ATOM 2307 CD PRO A 57 26.233 43.834 87.093 1.00 21.20 C ANISOU 2307 CD PRO C 57 2700 2648 2704 88 115 57 C ATOM 2308 N ASP A 58 27.234 42.673 91.031 1.00 25.39 N ANISOU 2308 N ASP C 58 3212 3209 3226 47 0 30 N ATOM 2309 CA ASP A 58 28.393 42.142 90.293 1.00 24.86 C ANISOU 2309 CA ASP C 58 3105 3164 3174 52 -12 0 C ATOM 2310 C ASP A 58 29.708 42.240 91.109 1.00 23.71 C ANISOU 2310 C ASP C 58 2989 3024 2995 4 -5 65 C ATOM 2311 O ASP A 58 30.226 41.265 91.680 1.00 23.69 O ANISOU 2311 O ASP C 58 2913 3045 3041 68 -16 102 O ATOM 2312 N LYS A 59 30.192 43.462 91.182 1.00 21.55 N ANISOU 2312 N LYS C 59 2688 2799 2699 10 6 100 N ATOM 2313 CA LYS A 59 31.564 43.771 91.487 1.00 19.94 C ANISOU 2313 CA LYS C 59 2471 2627 2477 -16 21 94 C ATOM 2314 C LYS A 59 31.524 44.952 92.436 1.00 19.06 C ANISOU 2314 C LYS C 59 2363 2541 2335 -48 4 135 C ATOM 2315 O LYS A 59 30.514 45.602 92.566 1.00 20.32 O ANISOU 2315 O LYS C 59 2416 2833 2469 -62 1 187 O ATOM 2316 CB LYS A 59 32.302 44.145 90.201 1.00 19.53 C ANISOU 2316 CB LYS C 59 2472 2530 2419 -47 18 62 C ATOM 2317 CG LYS A 59 32.414 43.000 89.174 1.00 20.41 C ANISOU 2317 CG LYS C 59 2591 2688 2474 26 19 17 C ATOM 2318 CD LYS A 59 33.308 41.890 89.657 1.00 20.62 C ANISOU 2318 CD LYS C 59 2724 2493 2616 43 8 4 C ATOM 2319 CE LYS A 59 33.659 40.925 88.551 1.00 21.99 C ANISOU 2319 CE LYS C 59 2913 2706 2733 -64 -90 108 C ATOM 2320 NZ LYS A 59 34.365 39.719 88.980 1.00 22.76 N ANISOU 2320 NZ LYS C 59 2859 2916 2872 -63 -51 12 N ATOM 2321 N ILE A 60 32.632 45.213 93.103 1.00 17.76 N ANISOU 2321 N ILE C 60 2237 2291 2218 -26 13 161 N ATOM 2322 CA ILE A 60 32.775 46.426 93.892 1.00 16.58 C ANISOU 2322 CA ILE C 60 2100 2155 2044 -46 -23 136 C ATOM 2323 C ILE A 60 33.030 47.624 92.958 1.00 15.35 C ANISOU 2323 C ILE C 60 1939 1930 1963 -80 -27 142 C ATOM 2324 O ILE A 60 33.845 47.541 92.081 1.00 15.64 O ANISOU 2324 O ILE C 60 2172 1941 1829 -73 -48 286 O ATOM 2325 CB ILE A 60 33.911 46.265 94.905 1.00 16.54 C ANISOU 2325 CB ILE C 60 2103 2107 2072 -55 0 130 C ATOM 2326 CG1 ILE A 60 33.547 45.187 95.920 1.00 18.86 C ANISOU 2326 CG1 ILE C 60 2403 2475 2285 -62 -66 124 C ATOM 2327 CG2 ILE A 60 34.234 47.560 95.605 1.00 15.82 C ANISOU 2327 CG2 ILE C 60 1962 2121 1925 -58 -51 174 C ATOM 2328 CD1 ILE A 60 34.686 44.711 96.778 1.00 21.20 C ANISOU 2328 CD1 ILE C 60 2534 2859 2660 -63 -19 39 C ATOM 2329 N ILE A 61 32.306 48.716 93.168 1.00 14.56 N ANISOU 2329 N ILE C 61 1918 1816 1798 -93 -85 105 N ATOM 2330 CA ILE A 61 32.457 49.900 92.337 1.00 14.37 C ANISOU 2330 CA ILE C 61 1784 1864 1812 -106 -69 112 C ATOM 2331 C ILE A 61 33.015 51.056 93.137 1.00 14.05 C ANISOU 2331 C ILE C 61 1777 1894 1667 -114 -41 105 C ATOM 2332 O ILE A 61 32.511 51.400 94.188 1.00 14.76 O ANISOU 2332 O ILE C 61 1810 2047 1749 -169 -59 96 O ATOM 2333 CB ILE A 61 31.120 50.385 91.727 1.00 14.73 C ANISOU 2333 CB ILE C 61 1897 1913 1787 -86 -29 119 C ATOM 2334 CG1 ILE A 61 30.491 49.328 90.846 1.00 15.52 C ANISOU 2334 CG1 ILE C 61 1969 1855 2072 -65 2 195 C ATOM 2335 CG2 ILE A 61 31.316 51.684 90.938 1.00 15.17 C ANISOU 2335 CG2 ILE C 61 1897 1890 1975 -108 -70 184 C ATOM 2336 CD1 ILE A 61 29.421 49.870 90.009 1.00 19.11 C ANISOU 2336 CD1 ILE C 61 2353 2447 2459 33 80 95 C ATOM 2337 N VAL A 62 34.068 51.654 92.606 1.00 13.00 N ANISOU 2337 N VAL C 62 1659 1728 1551 -102 3 127 N ATOM 2338 CA VAL A 62 34.731 52.748 93.267 1.00 12.29 C ANISOU 2338 CA VAL C 62 1609 1608 1453 -71 -13 152 C ATOM 2339 C VAL A 62 34.497 54.048 92.495 1.00 11.78 C ANISOU 2339 C VAL C 62 1631 1449 1393 -89 -8 118 C ATOM 2340 O VAL A 62 34.687 54.075 91.280 1.00 12.14 O ANISOU 2340 O VAL C 62 1614 1476 1521 -130 -21 167 O ATOM 2341 CB VAL A 62 36.248 52.503 93.378 1.00 12.72 C ANISOU 2341 CB VAL C 62 1698 1629 1504 -58 -39 159 C ATOM 2342 CG1 VAL A 62 36.901 53.681 94.097 1.00 12.73 C ANISOU 2342 CG1 VAL C 62 1650 1600 1585 -2 -75 88 C ATOM 2343 CG2 VAL A 62 36.533 51.191 94.116 1.00 13.24 C ANISOU 2343 CG2 VAL C 62 1695 1765 1567 -111 42 283 C ATOM 2344 N ALA A 63 34.076 55.102 93.203 1.00 11.19 N ANISOU 2344 N ALA C 63 1534 1410 1306 -77 1 105 N ATOM 2345 CA ALA A 63 33.998 56.457 92.635 1.00 10.99 C ANISOU 2345 CA ALA C 63 1432 1485 1255 -117 -24 39 C ATOM 2346 C ALA A 63 35.195 57.264 93.156 1.00 10.77 C ANISOU 2346 C ALA C 63 1438 1515 1139 -76 -22 -54 C ATOM 2347 O ALA A 63 35.223 57.718 94.312 1.00 11.44 O ANISOU 2347 O ALA C 63 1425 1751 1169 -69 70 -130 O ATOM 2348 CB ALA A 63 32.651 57.153 93.007 1.00 11.31 C ANISOU 2348 CB ALA C 63 1486 1528 1283 -186 -8 45 C ATOM 2349 N ASP A 64 36.210 57.438 92.306 1.00 10.45 N ANISOU 2349 N ASP C 64 1353 1483 1134 -121 -2 -117 N ATOM 2350 CA ASP A 64 37.471 58.064 92.707 1.00 10.79 C ANISOU 2350 CA ASP C 64 1385 1494 1217 -105 -73 -97 C ATOM 2351 C ASP A 64 37.394 59.587 92.628 1.00 10.91 C ANISOU 2351 C ASP C 64 1454 1479 1209 -71 -66 -123 C ATOM 2352 O ASP A 64 37.950 60.206 91.730 1.00 11.01 O ANISOU 2352 O ASP C 64 1389 1660 1133 -38 -85 -281 O ATOM 2353 CB ASP A 64 38.585 57.516 91.817 1.00 10.58 C ANISOU 2353 CB ASP C 64 1383 1377 1258 -205 -43 -88 C ATOM 2354 CG ASP A 64 39.918 58.095 92.104 1.00 11.03 C ANISOU 2354 CG ASP C 64 1428 1499 1263 -170 -18 -116 C ATOM 2355 OD1 ASP A 64 40.184 58.536 93.257 1.00 12.72 O ANISOU 2355 OD1 ASP C 64 1517 1867 1447 -376 -8 -57 O ATOM 2356 OD2 ASP A 64 40.759 58.109 91.181 1.00 13.40 O ANISOU 2356 OD2 ASP C 64 1401 1973 1717 -110 39 -244 O ATOM 2357 N THR A 65 36.685 60.209 93.581 1.00 11.80 N ANISOU 2357 N THR C 65 1558 1574 1349 -8 -80 -168 N ATOM 2358 CA THR A 65 36.467 61.664 93.516 1.00 12.16 C ANISOU 2358 CA THR C 65 1564 1629 1425 -51 -89 -109 C ATOM 2359 C THR A 65 37.575 62.499 94.187 1.00 11.86 C ANISOU 2359 C THR C 65 1556 1551 1397 -87 -66 -163 C ATOM 2360 O THR A 65 37.659 63.694 93.950 1.00 12.37 O ANISOU 2360 O THR C 65 1607 1633 1460 -114 -38 -164 O ATOM 2361 CB THR A 65 35.131 62.086 94.172 1.00 12.47 C ANISOU 2361 CB THR C 65 1547 1732 1457 31 -83 -89 C ATOM 2362 OG1 THR A 65 35.158 61.690 95.544 1.00 15.42 O ANISOU 2362 OG1 THR C 65 1791 2443 1623 77 -113 -71 O ATOM 2363 CG2 THR A 65 33.942 61.403 93.521 1.00 12.25 C ANISOU 2363 CG2 THR C 65 1529 1860 1262 -121 -150 -185 C ATOM 2364 N LYS A 66 38.381 61.888 95.038 1.00 11.61 N ANISOU 2364 N LYS C 66 1620 1428 1364 -97 -83 -176 N ATOM 2365 CA LYS A 66 39.438 62.560 95.765 1.00 11.78 C ANISOU 2365 CA LYS C 66 1551 1508 1416 -103 -23 -164 C ATOM 2366 C LYS A 66 38.835 63.779 96.468 1.00 11.99 C ANISOU 2366 C LYS C 66 1581 1485 1489 -119 6 -144 C ATOM 2367 O LYS A 66 39.401 64.868 96.468 1.00 12.60 O ANISOU 2367 O LYS C 66 1650 1661 1476 -130 -13 -281 O ATOM 2368 CB LYS A 66 40.622 62.914 94.854 1.00 11.66 C ANISOU 2368 CB LYS C 66 1531 1474 1422 -61 46 -84 C ATOM 2369 CG LYS A 66 41.409 61.669 94.424 1.00 11.94 C ANISOU 2369 CG LYS C 66 1483 1611 1442 -44 102 -114 C ATOM 2370 CD LYS A 66 42.625 62.019 93.594 1.00 13.89 C ANISOU 2370 CD LYS C 66 1713 1909 1655 -73 22 -11 C ATOM 2371 CE LYS A 66 43.423 60.780 93.227 1.00 13.40 C ANISOU 2371 CE LYS C 66 1694 1847 1550 -56 -78 -203 C ATOM 2372 NZ LYS A 66 42.652 59.877 92.355 1.00 13.82 N ANISOU 2372 NZ LYS C 66 1588 2136 1527 78 -44 -200 N ATOM 2373 N CYS A 67 37.659 63.540 97.037 1.00 11.91 N ANISOU 2373 N CYS C 67 1618 1450 1455 -112 -5 -171 N ATOM 2374 CA CYS A 67 36.857 64.585 97.649 1.00 13.06 C ANISOU 2374 CA CYS C 67 1683 1719 1558 -90 -26 -220 C ATOM 2375 C CYS A 67 37.646 65.296 98.764 1.00 12.84 C ANISOU 2375 C CYS C 67 1693 1681 1502 -74 -18 -194 C ATOM 2376 O CYS A 67 38.245 64.645 99.640 1.00 12.91 O ANISOU 2376 O CYS C 67 1899 1571 1435 -132 -107 -208 O ATOM 2377 CB CYS A 67 35.569 63.992 98.175 1.00 12.68 C ANISOU 2377 CB CYS C 67 1677 1649 1492 -96 -21 -204 C ATOM 2378 SG CYS A 67 34.610 65.104 99.203 1.00 16.09 S ANISOU 2378 SG CYS C 67 1735 2608 1769 -194 -177 -579 S ATOM 2379 N ALA A 68 37.653 66.628 98.673 1.00 13.06 N ANISOU 2379 N ALA C 68 1676 1742 1544 -44 -24 -126 N ATOM 2380 CA ALA A 68 38.342 67.539 99.599 1.00 13.30 C ANISOU 2380 CA ALA C 68 1666 1788 1597 -65 -8 -159 C ATOM 2381 C ALA A 68 37.377 68.347 100.454 1.00 13.82 C ANISOU 2381 C ALA C 68 1757 1882 1609 -47 -4 -227 C ATOM 2382 O ALA A 68 37.803 68.967 101.433 1.00 14.13 O ANISOU 2382 O ALA C 68 1873 1893 1602 -137 -69 -382 O ATOM 2383 CB ALA A 68 39.182 68.495 98.833 1.00 13.92 C ANISOU 2383 CB ALA C 68 1750 1844 1692 -12 8 -142 C ATOM 2384 N ASP A 69 36.108 68.405 100.058 1.00 13.66 N ANISOU 2384 N ASP C 69 1722 1838 1629 -76 -39 -251 N ATOM 2385 CA ASP A 69 35.140 69.322 100.703 1.00 14.53 C ANISOU 2385 CA ASP C 69 1797 1980 1740 -54 -47 -171 C ATOM 2386 C ASP A 69 33.738 68.942 100.266 1.00 14.33 C ANISOU 2386 C ASP C 69 1775 1925 1742 -31 -63 -193 C ATOM 2387 O ASP A 69 33.557 68.192 99.296 1.00 14.04 O ANISOU 2387 O ASP C 69 1812 1948 1571 -95 -130 -310 O ATOM 2388 CB ASP A 69 35.438 70.775 100.318 1.00 14.74 C ANISOU 2388 CB ASP C 69 1827 1964 1806 -69 -75 -222 C ATOM 2389 CG ASP A 69 34.984 71.789 101.379 1.00 16.33 C ANISOU 2389 CG ASP C 69 2096 2114 1994 -60 -114 -145 C ATOM 2390 OD1 ASP A 69 34.291 71.415 102.343 1.00 19.10 O ANISOU 2390 OD1 ASP C 69 2412 2555 2287 -75 -464 -335 O ATOM 2391 OD2 ASP A 69 35.340 72.966 101.295 1.00 18.31 O ANISOU 2391 OD2 ASP C 69 2488 2269 2201 -244 -228 -275 O ATOM 2392 N ALA A 70 32.736 69.469 100.960 1.00 14.22 N ANISOU 2392 N ALA C 70 1771 1905 1728 -26 -114 -207 N ATOM 2393 CA ALA A 70 31.347 69.087 100.717 1.00 14.27 C ANISOU 2393 CA ALA C 70 1757 1942 1723 -20 -55 -137 C ATOM 2394 C ALA A 70 31.229 67.569 100.698 1.00 14.23 C ANISOU 2394 C ALA C 70 1725 1954 1724 -49 -45 -100 C ATOM 2395 O ALA A 70 30.588 66.982 99.820 1.00 14.51 O ANISOU 2395 O ALA C 70 1717 2183 1613 -103 57 -137 O ATOM 2396 CB ALA A 70 30.822 69.701 99.440 1.00 14.60 C ANISOU 2396 CB ALA C 70 1764 1931 1849 -37 -43 -174 C ATOM 2397 N GLY A 71 31.834 66.935 101.696 1.00 14.48 N ANISOU 2397 N GLY C 71 1758 2012 1731 -71 -19 -58 N ATOM 2398 CA GLY A 71 31.858 65.485 101.817 1.00 14.04 C ANISOU 2398 CA GLY C 71 1774 1861 1697 -35 -32 -42 C ATOM 2399 C GLY A 71 30.517 64.782 101.743 1.00 14.27 C ANISOU 2399 C GLY C 71 1800 1894 1726 -47 -7 -45 C ATOM 2400 O GLY A 71 30.343 63.826 100.992 1.00 13.68 O ANISOU 2400 O GLY C 71 1801 1777 1619 -70 15 -13 O ATOM 2401 N GLY A 72 29.552 65.276 102.519 1.00 13.87 N ANISOU 2401 N GLY C 72 1737 1845 1687 -52 -57 -53 N ATOM 2402 CA GLY A 72 28.217 64.706 102.524 1.00 14.04 C ANISOU 2402 CA GLY C 72 1729 1881 1724 -41 -60 -104 C ATOM 2403 C GLY A 72 27.564 64.744 101.155 1.00 13.79 C ANISOU 2403 C GLY C 72 1690 1845 1704 -60 -88 -76 C ATOM 2404 O GLY A 72 26.953 63.773 100.731 1.00 13.82 O ANISOU 2404 O GLY C 72 1769 1777 1705 1 -58 -136 O ATOM 2405 N THR A 73 27.695 65.865 100.468 1.00 12.62 N ANISOU 2405 N THR C 73 1540 1662 1590 -89 -93 -107 N ATOM 2406 CA THR A 73 27.097 66.026 99.160 1.00 12.38 C ANISOU 2406 CA THR C 73 1574 1643 1485 -115 -116 -127 C ATOM 2407 C THR A 73 27.781 65.150 98.097 1.00 12.58 C ANISOU 2407 C THR C 73 1566 1688 1524 -105 -99 -132 C ATOM 2408 O THR A 73 27.116 64.460 97.318 1.00 12.41 O ANISOU 2408 O THR C 73 1640 1653 1422 -163 -158 -207 O ATOM 2409 CB THR A 73 27.184 67.501 98.732 1.00 11.72 C ANISOU 2409 CB THR C 73 1499 1471 1481 -159 -128 -110 C ATOM 2410 OG1 THR A 73 26.492 68.345 99.703 1.00 13.80 O ANISOU 2410 OG1 THR C 73 1863 1915 1465 -267 -236 -229 O ATOM 2411 CG2 THR A 73 26.526 67.695 97.382 1.00 11.12 C ANISOU 2411 CG2 THR C 73 1621 1268 1333 -91 -195 -281 C ATOM 2412 N VAL A 74 29.106 65.238 98.016 1.00 12.65 N ANISOU 2412 N VAL C 74 1586 1781 1438 -163 -68 -122 N ATOM 2413 CA VAL A 74 29.807 64.424 97.017 1.00 12.58 C ANISOU 2413 CA VAL C 74 1505 1791 1483 -142 -70 -111 C ATOM 2414 C VAL A 74 29.563 62.924 97.274 1.00 12.93 C ANISOU 2414 C VAL C 74 1543 1868 1500 -123 -59 -86 C ATOM 2415 O VAL A 74 29.308 62.168 96.345 1.00 13.80 O ANISOU 2415 O VAL C 74 1672 2028 1543 -104 -31 -100 O ATOM 2416 CB VAL A 74 31.308 64.755 96.969 1.00 11.83 C ANISOU 2416 CB VAL C 74 1401 1670 1425 -138 -123 -107 C ATOM 2417 CG1 VAL A 74 32.029 63.848 95.933 1.00 10.98 C ANISOU 2417 CG1 VAL C 74 1460 1326 1384 -153 -90 -256 C ATOM 2418 CG2 VAL A 74 31.543 66.239 96.665 1.00 13.31 C ANISOU 2418 CG2 VAL C 74 1493 1948 1613 -2 -175 -80 C ATOM 2419 N ALA A 75 29.635 62.472 98.526 1.00 13.00 N ANISOU 2419 N ALA C 75 1641 1804 1493 -111 -110 -44 N ATOM 2420 CA ALA A 75 29.377 61.069 98.837 1.00 13.12 C ANISOU 2420 CA ALA C 75 1607 1823 1555 -89 -55 16 C ATOM 2421 C ALA A 75 27.943 60.661 98.450 1.00 12.85 C ANISOU 2421 C ALA C 75 1548 1755 1579 -82 -72 35 C ATOM 2422 O ALA A 75 27.747 59.638 97.816 1.00 11.99 O ANISOU 2422 O ALA C 75 1395 1793 1367 -145 -182 133 O ATOM 2423 CB ALA A 75 29.669 60.771 100.296 1.00 13.19 C ANISOU 2423 CB ALA C 75 1612 1833 1567 -107 -32 21 C ATOM 2424 N LYS A 76 26.947 61.500 98.764 1.00 13.51 N ANISOU 2424 N LYS C 76 1638 1883 1609 -70 -94 13 N ATOM 2425 CA LYS A 76 25.572 61.148 98.412 1.00 13.40 C ANISOU 2425 CA LYS C 76 1629 1810 1652 -14 -91 -48 C ATOM 2426 C LYS A 76 25.416 61.030 96.902 1.00 12.83 C ANISOU 2426 C LYS C 76 1576 1697 1602 -3 -58 -58 C ATOM 2427 O LYS A 76 24.823 60.056 96.386 1.00 12.57 O ANISOU 2427 O LYS C 76 1529 1713 1533 3 -156 -100 O ATOM 2428 CB LYS A 76 24.578 62.178 98.974 1.00 13.85 C ANISOU 2428 CB LYS C 76 1738 1812 1710 -39 -69 -99 C ATOM 2429 CG LYS A 76 23.149 61.885 98.573 1.00 16.53 C ANISOU 2429 CG LYS C 76 1936 2268 2073 -17 -70 -115 C ATOM 2430 CD LYS A 76 22.150 62.843 99.200 1.00 21.38 C ANISOU 2430 CD LYS C 76 2622 2722 2778 -95 -50 -149 C ATOM 2431 CE LYS A 76 20.715 62.503 98.747 1.00 22.90 C ANISOU 2431 CE LYS C 76 2754 2968 2977 -52 51 -116 C ATOM 2432 NZ LYS A 76 19.697 63.355 99.416 1.00 26.47 N ANISOU 2432 NZ LYS C 76 3160 3527 3371 -72 3 -213 N ATOM 2433 N ASN A 77 25.957 62.020 96.202 1.00 12.63 N ANISOU 2433 N ASN C 77 1538 1723 1536 -83 -78 -57 N ATOM 2434 CA ASN A 77 25.879 62.088 94.754 1.00 12.76 C ANISOU 2434 CA ASN C 77 1588 1676 1583 -85 3 -39 C ATOM 2435 C ASN A 77 26.405 60.828 94.087 1.00 12.06 C ANISOU 2435 C ASN C 77 1514 1587 1478 -110 -37 11 C ATOM 2436 O ASN A 77 25.827 60.349 93.126 1.00 12.44 O ANISOU 2436 O ASN C 77 1467 1681 1579 -181 -19 54 O ATOM 2437 CB ASN A 77 26.613 63.322 94.232 1.00 12.58 C ANISOU 2437 CB ASN C 77 1554 1648 1575 -119 -45 -35 C ATOM 2438 CG ASN A 77 25.837 64.604 94.476 1.00 13.15 C ANISOU 2438 CG ASN C 77 1688 1574 1733 -64 1 -126 C ATOM 2439 OD1 ASN A 77 24.654 64.559 94.843 1.00 13.35 O ANISOU 2439 OD1 ASN C 77 1287 1653 2132 -155 -211 -224 O ATOM 2440 ND2 ASN A 77 26.485 65.743 94.272 1.00 9.60 N ANISOU 2440 ND2 ASN C 77 1150 1061 1434 42 -23 -77 N ATOM 2441 N ASN A 78 27.493 60.289 94.609 1.00 11.75 N ANISOU 2441 N ASN C 78 1468 1551 1446 -107 -19 3 N ATOM 2442 CA ASN A 78 28.051 59.070 94.040 1.00 11.50 C ANISOU 2442 CA ASN C 78 1430 1548 1391 -100 -31 3 C ATOM 2443 C ASN A 78 27.426 57.793 94.593 1.00 12.06 C ANISOU 2443 C ASN C 78 1497 1602 1482 -37 11 -2 C ATOM 2444 O ASN A 78 27.322 56.785 93.879 1.00 11.57 O ANISOU 2444 O ASN C 78 1518 1508 1367 -51 -117 51 O ATOM 2445 CB ASN A 78 29.565 59.096 94.183 1.00 11.67 C ANISOU 2445 CB ASN C 78 1413 1551 1468 -28 -15 -27 C ATOM 2446 CG ASN A 78 30.195 60.097 93.221 1.00 11.51 C ANISOU 2446 CG ASN C 78 1330 1637 1402 -128 -20 47 C ATOM 2447 OD1 ASN A 78 30.426 59.775 92.047 1.00 11.34 O ANISOU 2447 OD1 ASN C 78 1333 1685 1289 -127 -273 -53 O ATOM 2448 ND2 ASN A 78 30.386 61.331 93.680 1.00 11.11 N ANISOU 2448 ND2 ASN C 78 959 1826 1434 61 -20 -177 N ATOM 2449 N ALA A 79 26.970 57.826 95.843 1.00 12.42 N ANISOU 2449 N ALA C 79 1522 1692 1502 8 -52 14 N ATOM 2450 CA ALA A 79 26.287 56.657 96.399 1.00 13.54 C ANISOU 2450 CA ALA C 79 1689 1767 1686 37 -27 25 C ATOM 2451 C ALA A 79 24.952 56.395 95.692 1.00 13.93 C ANISOU 2451 C ALA C 79 1731 1825 1737 35 -63 35 C ATOM 2452 O ALA A 79 24.587 55.226 95.448 1.00 14.86 O ANISOU 2452 O ALA C 79 1898 1936 1810 110 -108 -57 O ATOM 2453 CB ALA A 79 26.084 56.793 97.916 1.00 14.16 C ANISOU 2453 CB ALA C 79 1750 1909 1719 50 -11 40 C ATOM 2454 N VAL A 80 24.219 57.458 95.359 1.00 14.27 N ANISOU 2454 N VAL C 80 1751 1831 1837 33 -76 20 N ATOM 2455 CA VAL A 80 22.949 57.290 94.644 1.00 14.88 C ANISOU 2455 CA VAL C 80 1853 1906 1894 15 -41 -2 C ATOM 2456 C VAL A 80 23.166 56.696 93.253 1.00 14.55 C ANISOU 2456 C VAL C 80 1774 1860 1892 40 -24 -30 C ATOM 2457 O VAL A 80 22.275 56.053 92.716 1.00 15.41 O ANISOU 2457 O VAL C 80 1865 1967 2020 74 -54 -58 O ATOM 2458 CB VAL A 80 22.107 58.604 94.586 1.00 15.98 C ANISOU 2458 CB VAL C 80 1984 2051 2036 -1 -28 -26 C ATOM 2459 CG1 VAL A 80 21.664 59.003 95.973 1.00 17.14 C ANISOU 2459 CG1 VAL C 80 2127 2259 2126 -25 -44 -76 C ATOM 2460 CG2 VAL A 80 22.837 59.729 93.933 1.00 17.43 C ANISOU 2460 CG2 VAL C 80 2181 2240 2199 7 -81 -32 C ATOM 2461 N ARG A 81 24.358 56.909 92.685 1.00 13.32 N ANISOU 2461 N ARG C 81 1587 1759 1714 7 -11 -26 N ATOM 2462 CA ARG A 81 24.735 56.271 91.408 1.00 13.34 C ANISOU 2462 CA ARG C 81 1602 1761 1703 7 -3 -24 C ATOM 2463 C ARG A 81 25.099 54.788 91.549 1.00 13.30 C ANISOU 2463 C ARG C 81 1596 1779 1678 34 -12 -10 C ATOM 2464 O ARG A 81 25.182 54.045 90.555 1.00 13.30 O ANISOU 2464 O ARG C 81 1646 1802 1602 -11 -15 -4 O ATOM 2465 CB ARG A 81 25.894 57.015 90.765 1.00 13.44 C ANISOU 2465 CB ARG C 81 1597 1795 1714 -16 -20 2 C ATOM 2466 CG ARG A 81 25.607 58.442 90.305 1.00 13.11 C ANISOU 2466 CG ARG C 81 1694 1673 1615 72 -6 -79 C ATOM 2467 CD ARG A 81 24.616 58.505 89.155 1.00 13.51 C ANISOU 2467 CD ARG C 81 1771 1621 1740 5 35 -24 C ATOM 2468 NE ARG A 81 24.645 59.782 88.459 1.00 12.46 N ANISOU 2468 NE ARG C 81 1705 1527 1501 240 66 -184 N ATOM 2469 CZ ARG A 81 23.884 60.096 87.414 1.00 12.48 C ANISOU 2469 CZ ARG C 81 1765 1410 1566 80 -25 -12 C ATOM 2470 NH1 ARG A 81 23.012 59.243 86.897 1.00 13.30 N ANISOU 2470 NH1 ARG C 81 1769 1712 1571 248 104 -144 N ATOM 2471 NH2 ARG A 81 23.988 61.275 86.869 1.00 13.05 N ANISOU 2471 NH2 ARG C 81 1804 1557 1594 163 -86 120 N ATOM 2472 N GLY A 82 25.335 54.353 92.774 1.00 12.99 N ANISOU 2472 N GLY C 82 1623 1719 1593 -28 -15 -11 N ATOM 2473 CA GLY A 82 25.658 52.962 93.031 1.00 13.33 C ANISOU 2473 CA GLY C 82 1668 1734 1661 -30 -16 42 C ATOM 2474 C GLY A 82 27.091 52.673 93.455 1.00 13.23 C ANISOU 2474 C GLY C 82 1686 1713 1625 -74 2 57 C ATOM 2475 O GLY A 82 27.476 51.527 93.472 1.00 13.86 O ANISOU 2475 O GLY C 82 1774 1714 1778 -72 69 95 O ATOM 2476 N ALA A 83 27.865 53.677 93.819 1.00 12.58 N ANISOU 2476 N ALA C 83 1657 1601 1519 -71 -86 143 N ATOM 2477 CA ALA A 83 29.211 53.461 94.337 1.00 13.02 C ANISOU 2477 CA ALA C 83 1682 1764 1499 -57 -55 141 C ATOM 2478 C ALA A 83 29.230 52.688 95.662 1.00 13.74 C ANISOU 2478 C ALA C 83 1751 1882 1585 -106 -66 172 C ATOM 2479 O ALA A 83 28.411 52.946 96.556 1.00 14.92 O ANISOU 2479 O ALA C 83 1814 2203 1650 -121 15 257 O ATOM 2480 CB ALA A 83 29.923 54.786 94.549 1.00 12.55 C ANISOU 2480 CB ALA C 83 1711 1613 1444 -63 -139 113 C ATOM 2481 N ASP A 84 30.188 51.765 95.776 1.00 14.13 N ANISOU 2481 N ASP C 84 1733 1952 1682 -27 -45 140 N ATOM 2482 CA ASP A 84 30.507 51.134 97.058 1.00 14.74 C ANISOU 2482 CA ASP C 84 1811 2032 1755 -8 -75 72 C ATOM 2483 C ASP A 84 31.523 51.939 97.852 1.00 14.84 C ANISOU 2483 C ASP C 84 1782 2102 1753 -6 -93 30 C ATOM 2484 O ASP A 84 31.316 52.251 99.042 1.00 15.41 O ANISOU 2484 O ASP C 84 1864 2247 1743 -84 -153 28 O ATOM 2485 CB ASP A 84 30.994 49.715 96.832 1.00 15.11 C ANISOU 2485 CB ASP C 84 1842 2014 1883 38 -62 80 C ATOM 2486 CG ASP A 84 29.917 48.838 96.249 1.00 15.93 C ANISOU 2486 CG ASP C 84 2009 2061 1983 21 -31 116 C ATOM 2487 OD1 ASP A 84 28.744 48.904 96.730 1.00 15.93 O ANISOU 2487 OD1 ASP C 84 1974 1955 2122 105 -129 406 O ATOM 2488 OD2 ASP A 84 30.179 48.092 95.298 1.00 17.13 O ANISOU 2488 OD2 ASP C 84 2164 2061 2283 -60 -256 353 O ATOM 2489 N TRP A 85 32.623 52.310 97.200 1.00 14.34 N ANISOU 2489 N TRP C 85 1748 2068 1631 -20 -106 20 N ATOM 2490 CA TRP A 85 33.686 53.056 97.868 1.00 14.19 C ANISOU 2490 CA TRP C 85 1784 1937 1668 -67 -75 -2 C ATOM 2491 C TRP A 85 33.868 54.374 97.167 1.00 13.61 C ANISOU 2491 C TRP C 85 1737 1864 1569 -78 -63 5 C ATOM 2492 O TRP A 85 33.719 54.460 95.942 1.00 14.05 O ANISOU 2492 O TRP C 85 1854 1931 1552 -143 30 -2 O ATOM 2493 CB TRP A 85 35.024 52.284 97.859 1.00 14.41 C ANISOU 2493 CB TRP C 85 1793 1989 1693 -67 -81 17 C ATOM 2494 CG TRP A 85 34.965 50.885 98.441 1.00 15.74 C ANISOU 2494 CG TRP C 85 1993 2116 1868 -160 -71 69 C ATOM 2495 CD1 TRP A 85 34.051 50.396 99.323 1.00 15.17 C ANISOU 2495 CD1 TRP C 85 1936 1964 1861 -111 103 180 C ATOM 2496 CD2 TRP A 85 35.861 49.808 98.160 1.00 17.06 C ANISOU 2496 CD2 TRP C 85 2228 2244 2008 -160 35 171 C ATOM 2497 NE1 TRP A 85 34.319 49.078 99.611 1.00 16.47 N ANISOU 2497 NE1 TRP C 85 2236 2135 1883 -168 17 168 N ATOM 2498 CE2 TRP A 85 35.425 48.692 98.906 1.00 16.26 C ANISOU 2498 CE2 TRP C 85 2114 2248 1813 -140 42 123 C ATOM 2499 CE3 TRP A 85 36.998 49.676 97.354 1.00 19.01 C ANISOU 2499 CE3 TRP C 85 2411 2578 2234 -181 10 109 C ATOM 2500 CZ2 TRP A 85 36.078 47.469 98.862 1.00 16.75 C ANISOU 2500 CZ2 TRP C 85 2319 2190 1856 15 10 137 C ATOM 2501 CZ3 TRP A 85 37.643 48.450 97.308 1.00 19.10 C ANISOU 2501 CZ3 TRP C 85 2481 2444 2333 -22 19 108 C ATOM 2502 CH2 TRP A 85 37.187 47.365 98.066 1.00 17.91 C ANISOU 2502 CH2 TRP C 85 2351 2308 2142 -48 71 98 C ATOM 2503 N MET A 86 34.197 55.399 97.940 1.00 13.51 N ANISOU 2503 N MET C 86 1686 1886 1559 -64 -28 -36 N ATOM 2504 CA MET A 86 34.601 56.693 97.406 1.00 13.78 C ANISOU 2504 CA MET C 86 1710 1909 1614 -44 -4 28 C ATOM 2505 C MET A 86 35.914 57.136 98.021 1.00 13.96 C ANISOU 2505 C MET C 86 1724 1978 1601 -64 -11 20 C ATOM 2506 O MET A 86 36.139 56.912 99.209 1.00 14.71 O ANISOU 2506 O MET C 86 1789 2246 1552 -113 12 2 O ATOM 2507 CB MET A 86 33.531 57.756 97.678 1.00 14.08 C ANISOU 2507 CB MET C 86 1733 1924 1689 -83 -27 6 C ATOM 2508 CG MET A 86 33.784 59.080 96.960 1.00 14.55 C ANISOU 2508 CG MET C 86 1834 2027 1667 -64 -32 15 C ATOM 2509 SD MET A 86 32.656 60.437 97.274 1.00 16.06 S ANISOU 2509 SD MET C 86 1893 2691 1516 -436 -183 -65 S ATOM 2510 CE MET A 86 33.268 60.989 98.819 1.00 15.25 C ANISOU 2510 CE MET C 86 1982 2189 1622 -264 -130 -137 C ATOM 2511 N THR A 87 36.787 57.758 97.228 1.00 13.05 N ANISOU 2511 N THR C 87 1605 1876 1477 -55 -24 24 N ATOM 2512 CA THR A 87 38.021 58.315 97.772 1.00 12.91 C ANISOU 2512 CA THR C 87 1643 1792 1468 -42 -53 -1 C ATOM 2513 C THR A 87 37.812 59.743 98.257 1.00 13.20 C ANISOU 2513 C THR C 87 1685 1802 1528 -21 -42 -40 C ATOM 2514 O THR A 87 37.110 60.557 97.621 1.00 13.87 O ANISOU 2514 O THR C 87 1840 1998 1428 -58 -49 -90 O ATOM 2515 CB THR A 87 39.168 58.343 96.742 1.00 12.93 C ANISOU 2515 CB THR C 87 1599 1797 1514 -68 -30 8 C ATOM 2516 OG1 THR A 87 38.752 59.091 95.595 1.00 12.63 O ANISOU 2516 OG1 THR C 87 1505 1943 1350 -82 -102 142 O ATOM 2517 CG2 THR A 87 39.545 56.942 96.255 1.00 13.39 C ANISOU 2517 CG2 THR C 87 1706 1766 1614 7 8 1 C ATOM 2518 N CYS A 88 38.452 60.027 99.383 1.00 13.63 N ANISOU 2518 N CYS C 88 1702 1930 1545 -50 -27 -19 N ATOM 2519 CA CYS A 88 38.687 61.382 99.852 1.00 13.37 C ANISOU 2519 CA CYS C 88 1658 1848 1571 -114 8 -73 C ATOM 2520 C CYS A 88 40.173 61.663 99.815 1.00 13.43 C ANISOU 2520 C CYS C 88 1699 1853 1550 -115 1 -84 C ATOM 2521 O CYS A 88 40.974 60.790 100.192 1.00 13.58 O ANISOU 2521 O CYS C 88 1716 1824 1618 -197 57 -45 O ATOM 2522 CB CYS A 88 38.213 61.558 101.304 1.00 13.76 C ANISOU 2522 CB CYS C 88 1707 1896 1622 -58 -36 -3 C ATOM 2523 SG CYS A 88 36.433 61.827 101.550 1.00 16.56 S ANISOU 2523 SG CYS C 88 1760 2801 1729 -331 -108 -123 S ATOM 2524 N ILE A 89 40.555 62.867 99.395 1.00 13.09 N ANISOU 2524 N ILE C 89 1547 1842 1584 -100 20 -138 N ATOM 2525 CA ILE A 89 41.974 63.257 99.426 1.00 14.28 C ANISOU 2525 CA ILE C 89 1683 1997 1742 -100 9 -173 C ATOM 2526 C ILE A 89 42.357 63.433 100.894 1.00 15.00 C ANISOU 2526 C ILE C 89 1743 2159 1795 -191 0 -139 C ATOM 2527 O ILE A 89 41.536 63.872 101.701 1.00 15.19 O ANISOU 2527 O ILE C 89 1685 2299 1785 -256 -86 -163 O ATOM 2528 CB ILE A 89 42.236 64.529 98.572 1.00 14.61 C ANISOU 2528 CB ILE C 89 1735 2081 1733 -80 7 -107 C ATOM 2529 CG1 ILE A 89 43.729 64.795 98.378 1.00 14.55 C ANISOU 2529 CG1 ILE C 89 1726 1991 1810 -15 103 -185 C ATOM 2530 CG2 ILE A 89 41.580 65.742 99.161 1.00 15.04 C ANISOU 2530 CG2 ILE C 89 1947 1924 1842 -74 37 -182 C ATOM 2531 CD1 ILE A 89 44.416 63.782 97.499 1.00 15.66 C ANISOU 2531 CD1 ILE C 89 1906 2122 1922 -73 143 -98 C ATOM 2532 N CYS A 90 43.594 63.085 101.241 1.00 15.35 N ANISOU 2532 N CYS C 90 1777 2217 1836 -195 0 -160 N ATOM 2533 CA CYS A 90 44.032 63.082 102.627 1.00 16.20 C ANISOU 2533 CA CYS C 90 1994 2255 1905 -149 -12 -99 C ATOM 2534 C CYS A 90 44.054 64.464 103.262 1.00 16.72 C ANISOU 2534 C CYS C 90 2107 2263 1982 -61 -7 -121 C ATOM 2535 O CYS A 90 44.048 64.572 104.487 1.00 17.16 O ANISOU 2535 O CYS C 90 2250 2349 1921 -6 -84 -196 O ATOM 2536 CB CYS A 90 45.407 62.423 102.765 1.00 16.06 C ANISOU 2536 CB CYS C 90 1894 2302 1904 -179 33 -96 C ATOM 2537 SG CYS A 90 46.676 63.151 101.739 1.00 17.81 S ANISOU 2537 SG CYS C 90 2083 3012 1669 -462 33 -251 S ATOM 2538 N SER A 91 44.041 65.516 102.457 1.00 17.29 N ANISOU 2538 N SER C 91 2198 2328 2041 -6 -49 -75 N ATOM 2539 CA SER A 91 43.969 66.880 103.012 1.00 19.04 C ANISOU 2539 CA SER C 91 2406 2486 2340 -37 -45 -90 C ATOM 2540 C SER A 91 42.542 67.330 103.378 1.00 18.29 C ANISOU 2540 C SER C 91 2323 2402 2222 -94 -48 -56 C ATOM 2541 O SER A 91 42.373 68.426 103.940 1.00 18.99 O ANISOU 2541 O SER C 91 2361 2582 2269 -122 -92 -144 O ATOM 2542 CB SER A 91 44.577 67.901 102.073 1.00 19.84 C ANISOU 2542 CB SER C 91 2489 2584 2465 -22 -14 -42 C ATOM 2543 OG SER A 91 43.902 67.898 100.849 1.00 22.63 O ANISOU 2543 OG SER C 91 2893 2965 2741 91 41 -158 O ATOM 2544 N ALA A 92 41.538 66.522 103.050 1.00 17.40 N ANISOU 2544 N ALA C 92 2224 2348 2037 -143 -78 -81 N ATOM 2545 CA ALA A 92 40.182 66.776 103.533 1.00 16.86 C ANISOU 2545 CA ALA C 92 2155 2268 1982 -134 -42 -79 C ATOM 2546 C ALA A 92 40.150 66.629 105.058 1.00 16.78 C ANISOU 2546 C ALA C 92 2180 2274 1919 -184 -80 -83 C ATOM 2547 O ALA A 92 40.768 65.725 105.622 1.00 16.01 O ANISOU 2547 O ALA C 92 2102 2398 1583 -212 -117 -226 O ATOM 2548 CB ALA A 92 39.185 65.848 102.885 1.00 17.45 C ANISOU 2548 CB ALA C 92 2171 2328 2131 -164 -25 -74 C ATOM 2549 N THR A 93 39.392 67.505 105.717 1.00 16.54 N ANISOU 2549 N THR C 93 2174 2186 1922 -163 -25 -99 N ATOM 2550 CA THR A 93 39.353 67.534 107.170 1.00 17.20 C ANISOU 2550 CA THR C 93 2254 2231 2050 -109 -71 -102 C ATOM 2551 C THR A 93 38.521 66.388 107.699 1.00 16.97 C ANISOU 2551 C THR C 93 2156 2285 2005 -95 -71 -82 C ATOM 2552 O THR A 93 37.788 65.735 106.956 1.00 16.07 O ANISOU 2552 O THR C 93 2005 2266 1834 -124 -161 -122 O ATOM 2553 CB THR A 93 38.745 68.852 107.679 1.00 17.60 C ANISOU 2553 CB THR C 93 2310 2283 2091 -124 -73 -129 C ATOM 2554 OG1 THR A 93 37.369 68.894 107.297 1.00 18.28 O ANISOU 2554 OG1 THR C 93 2461 2407 2076 -183 -199 -189 O ATOM 2555 CG2 THR A 93 39.443 70.061 107.061 1.00 18.80 C ANISOU 2555 CG2 THR C 93 2515 2467 2160 -64 -134 -104 C ATOM 2556 N ILE A 94 38.631 66.156 109.000 1.00 17.35 N ANISOU 2556 N ILE C 94 2231 2357 2001 -70 -65 -60 N ATOM 2557 CA ILE A 94 37.937 65.047 109.624 1.00 17.58 C ANISOU 2557 CA ILE C 94 2228 2389 2060 -23 -15 -50 C ATOM 2558 C ILE A 94 36.431 65.248 109.514 1.00 17.10 C ANISOU 2558 C ILE C 94 2147 2345 2005 -47 -58 -58 C ATOM 2559 O ILE A 94 35.744 64.296 109.201 1.00 17.41 O ANISOU 2559 O ILE C 94 2194 2428 1992 -122 -70 -133 O ATOM 2560 CB ILE A 94 38.417 64.809 111.088 1.00 18.00 C ANISOU 2560 CB ILE C 94 2275 2450 2114 6 9 -2 C ATOM 2561 CG1 ILE A 94 39.845 64.256 111.088 1.00 18.63 C ANISOU 2561 CG1 ILE C 94 2359 2520 2200 31 4 -24 C ATOM 2562 CG2 ILE A 94 37.468 63.889 111.852 1.00 18.33 C ANISOU 2562 CG2 ILE C 94 2404 2465 2094 -4 2 -1 C ATOM 2563 CD1 ILE A 94 40.009 62.848 110.574 1.00 19.92 C ANISOU 2563 CD1 ILE C 94 2449 2631 2489 -113 19 -12 C ATOM 2564 N PRO A 95 35.914 66.464 109.772 1.00 17.28 N ANISOU 2564 N PRO C 95 2138 2392 2033 -38 -40 -54 N ATOM 2565 CA PRO A 95 34.472 66.706 109.559 1.00 17.37 C ANISOU 2565 CA PRO C 95 2151 2386 2063 -39 -25 -52 C ATOM 2566 C PRO A 95 34.000 66.424 108.124 1.00 17.55 C ANISOU 2566 C PRO C 95 2157 2482 2026 14 -29 -34 C ATOM 2567 O PRO A 95 32.930 65.853 107.940 1.00 17.89 O ANISOU 2567 O PRO C 95 2195 2594 2005 31 -17 -62 O ATOM 2568 CB PRO A 95 34.305 68.177 109.934 1.00 17.56 C ANISOU 2568 CB PRO C 95 2169 2373 2127 -60 -55 -83 C ATOM 2569 CG PRO A 95 35.416 68.419 110.943 1.00 17.30 C ANISOU 2569 CG PRO C 95 2166 2335 2069 -95 -40 -63 C ATOM 2570 CD PRO A 95 36.582 67.650 110.340 1.00 16.93 C ANISOU 2570 CD PRO C 95 2099 2270 2061 -44 -37 -58 C ATOM 2571 N THR A 96 34.801 66.793 107.125 1.00 17.50 N ANISOU 2571 N THR C 96 2167 2543 1937 2 -47 -69 N ATOM 2572 CA THR A 96 34.502 66.410 105.732 1.00 16.61 C ANISOU 2572 CA THR C 96 2073 2389 1850 -45 -71 -52 C ATOM 2573 C THR A 96 34.453 64.899 105.528 1.00 16.81 C ANISOU 2573 C THR C 96 2065 2430 1891 -48 -131 -55 C ATOM 2574 O THR A 96 33.514 64.375 104.932 1.00 17.05 O ANISOU 2574 O THR C 96 1967 2586 1924 -101 -198 -55 O ATOM 2575 CB THR A 96 35.524 67.061 104.797 1.00 16.53 C ANISOU 2575 CB THR C 96 2107 2382 1789 -17 -36 -80 C ATOM 2576 OG1 THR A 96 35.313 68.478 104.804 1.00 15.39 O ANISOU 2576 OG1 THR C 96 2077 2420 1349 -235 -195 -192 O ATOM 2577 CG2 THR A 96 35.364 66.545 103.333 1.00 15.87 C ANISOU 2577 CG2 THR C 96 1953 2347 1728 -53 -33 -122 C ATOM 2578 N MET A 97 35.468 64.195 106.025 1.00 16.03 N ANISOU 2578 N MET C 97 2023 2226 1840 -93 -117 -6 N ATOM 2579 CA MET A 97 35.520 62.740 105.898 1.00 16.72 C ANISOU 2579 CA MET C 97 2108 2284 1961 -29 -33 -35 C ATOM 2580 C MET A 97 34.369 62.038 106.616 1.00 16.58 C ANISOU 2580 C MET C 97 2110 2272 1916 -23 -66 -44 C ATOM 2581 O MET A 97 33.796 61.101 106.097 1.00 16.45 O ANISOU 2581 O MET C 97 2131 2392 1726 -69 -38 -39 O ATOM 2582 CB MET A 97 36.855 62.221 106.416 1.00 16.45 C ANISOU 2582 CB MET C 97 2077 2208 1964 -100 -37 -34 C ATOM 2583 CG MET A 97 38.003 62.584 105.516 1.00 17.14 C ANISOU 2583 CG MET C 97 2074 2387 2050 -64 41 -10 C ATOM 2584 SD MET A 97 39.463 61.674 105.991 1.00 18.99 S ANISOU 2584 SD MET C 97 2104 2808 2304 -440 -249 48 S ATOM 2585 CE MET A 97 40.690 62.422 104.813 1.00 19.98 C ANISOU 2585 CE MET C 97 2308 2945 2336 -177 -98 -63 C ATOM 2586 N LYS A 98 34.055 62.491 107.831 1.00 17.35 N ANISOU 2586 N LYS C 98 2208 2394 1988 3 -10 -61 N ATOM 2587 CA LYS A 98 32.924 61.973 108.594 1.00 17.47 C ANISOU 2587 CA LYS C 98 2199 2420 2015 -47 -39 -53 C ATOM 2588 C LYS A 98 31.588 62.205 107.866 1.00 16.58 C ANISOU 2588 C LYS C 98 2135 2327 1836 -55 -60 -64 C ATOM 2589 O LYS A 98 30.738 61.320 107.806 1.00 16.12 O ANISOU 2589 O LYS C 98 2018 2395 1710 -86 -79 -81 O ATOM 2590 CB LYS A 98 32.875 62.657 109.966 1.00 18.78 C ANISOU 2590 CB LYS C 98 2405 2584 2145 7 -19 -88 C ATOM 2591 CG LYS A 98 34.012 62.280 110.913 1.00 20.95 C ANISOU 2591 CG LYS C 98 2640 2688 2628 -100 16 -25 C ATOM 2592 CD LYS A 98 33.920 63.070 112.241 1.00 25.45 C ANISOU 2592 CD LYS C 98 3309 3349 3009 -11 -6 -90 C ATOM 2593 CE LYS A 98 34.636 62.347 113.356 1.00 27.46 C ANISOU 2593 CE LYS C 98 3560 3518 3355 -38 22 -42 C ATOM 2594 NZ LYS A 98 34.445 63.021 114.679 1.00 29.00 N ANISOU 2594 NZ LYS C 98 3801 3827 3389 -44 -125 -93 N ATOM 2595 N ALA A 99 31.408 63.400 107.314 1.00 15.61 N ANISOU 2595 N ALA C 99 1994 2154 1781 -85 -77 -59 N ATOM 2596 CA ALA A 99 30.190 63.687 106.554 1.00 15.60 C ANISOU 2596 CA ALA C 99 1951 2175 1800 -53 -48 -70 C ATOM 2597 C ALA A 99 30.101 62.820 105.300 1.00 15.76 C ANISOU 2597 C ALA C 99 1929 2245 1811 -64 -77 -65 C ATOM 2598 O ALA A 99 29.027 62.329 104.941 1.00 15.43 O ANISOU 2598 O ALA C 99 1836 2395 1630 -108 -98 -94 O ATOM 2599 CB ALA A 99 30.141 65.128 106.185 1.00 15.57 C ANISOU 2599 CB ALA C 99 1976 2152 1787 -68 -51 -65 C ATOM 2600 N ALA A 100 31.238 62.599 104.643 1.00 15.50 N ANISOU 2600 N ALA C 100 1788 2285 1815 -63 -79 -53 N ATOM 2601 CA ALA A 100 31.270 61.642 103.535 1.00 14.96 C ANISOU 2601 CA ALA C 100 1778 2137 1767 -70 -57 -49 C ATOM 2602 C ALA A 100 30.904 60.204 103.938 1.00 14.88 C ANISOU 2602 C ALA C 100 1734 2205 1715 -70 -87 -8 C ATOM 2603 O ALA A 100 30.094 59.562 103.270 1.00 14.47 O ANISOU 2603 O ALA C 100 1677 2309 1509 -63 -147 -26 O ATOM 2604 CB ALA A 100 32.640 61.684 102.859 1.00 14.99 C ANISOU 2604 CB ALA C 100 1749 2164 1779 -135 -51 -4 C ATOM 2605 N ARG A 101 31.492 59.688 105.027 1.00 14.84 N ANISOU 2605 N ARG C 101 1808 2100 1730 -97 -52 37 N ATOM 2606 CA ARG A 101 31.234 58.302 105.442 1.00 16.02 C ANISOU 2606 CA ARG C 101 1949 2227 1908 -69 -35 24 C ATOM 2607 C ARG A 101 29.784 58.073 105.811 1.00 16.67 C ANISOU 2607 C ARG C 101 2035 2278 2018 -32 -51 34 C ATOM 2608 O ARG A 101 29.211 57.070 105.439 1.00 17.56 O ANISOU 2608 O ARG C 101 2050 2472 2146 -11 -189 29 O ATOM 2609 CB ARG A 101 32.115 57.895 106.630 1.00 15.52 C ANISOU 2609 CB ARG C 101 1899 2130 1865 -98 16 13 C ATOM 2610 CG ARG A 101 31.786 56.485 107.120 1.00 18.06 C ANISOU 2610 CG ARG C 101 2217 2492 2152 -101 -28 84 C ATOM 2611 CD ARG A 101 32.761 55.955 108.167 1.00 19.42 C ANISOU 2611 CD ARG C 101 2336 2696 2343 -77 65 78 C ATOM 2612 NE ARG A 101 32.826 56.811 109.339 1.00 22.92 N ANISOU 2612 NE ARG C 101 2814 3033 2860 -128 -25 29 N ATOM 2613 CZ ARG A 101 31.895 56.871 110.289 1.00 24.76 C ANISOU 2613 CZ ARG C 101 3093 3287 3026 -9 -40 2 C ATOM 2614 NH1 ARG A 101 30.789 56.149 110.216 1.00 26.30 N ANISOU 2614 NH1 ARG C 101 3259 3630 3102 -8 -12 -21 N ATOM 2615 NH2 ARG A 101 32.072 57.677 111.320 1.00 25.70 N ANISOU 2615 NH2 ARG C 101 3174 3383 3205 -106 -110 -168 N ATOM 2616 N LYS A 102 29.218 59.011 106.555 1.00 17.96 N ANISOU 2616 N LYS C 102 2213 2373 2236 -7 -44 6 N ATOM 2617 CA LYS A 102 27.827 58.934 106.973 1.00 18.69 C ANISOU 2617 CA LYS C 102 2338 2421 2341 -27 -48 3 C ATOM 2618 C LYS A 102 26.884 58.955 105.780 1.00 18.42 C ANISOU 2618 C LYS C 102 2294 2423 2278 -36 -70 -13 C ATOM 2619 O LYS A 102 25.942 58.170 105.726 1.00 18.03 O ANISOU 2619 O LYS C 102 2313 2374 2162 -9 -116 -43 O ATOM 2620 CB LYS A 102 27.509 60.065 107.936 1.00 19.87 C ANISOU 2620 CB LYS C 102 2464 2598 2487 8 -11 -35 C ATOM 2621 CG LYS A 102 28.120 59.811 109.299 1.00 23.11 C ANISOU 2621 CG LYS C 102 2950 2955 2872 33 -27 38 C ATOM 2622 CD LYS A 102 27.740 60.883 110.320 1.00 28.24 C ANISOU 2622 CD LYS C 102 3672 3552 3506 -42 -59 -65 C ATOM 2623 CE LYS A 102 27.726 60.304 111.730 1.00 31.10 C ANISOU 2623 CE LYS C 102 4040 3927 3847 -93 2 16 C ATOM 2624 NZ LYS A 102 28.870 59.346 111.963 1.00 32.39 N ANISOU 2624 NZ LYS C 102 4179 3987 4140 -128 21 25 N ATOM 2625 N ALA A 103 27.152 59.834 104.811 1.00 17.86 N ANISOU 2625 N ALA C 103 2165 2436 2182 -40 -103 0 N ATOM 2626 CA ALA A 103 26.333 59.880 103.593 1.00 17.50 C ANISOU 2626 CA ALA C 103 2085 2434 2127 -57 -76 -8 C ATOM 2627 C ALA A 103 26.396 58.588 102.797 1.00 17.26 C ANISOU 2627 C ALA C 103 2053 2439 2066 -30 -96 7 C ATOM 2628 O ALA A 103 25.375 58.088 102.350 1.00 17.58 O ANISOU 2628 O ALA C 103 1985 2662 2033 -28 -172 -1 O ATOM 2629 CB ALA A 103 26.714 61.052 102.735 1.00 17.07 C ANISOU 2629 CB ALA C 103 2092 2376 2018 -60 -76 -45 C ATOM 2630 N ILE A 104 27.591 58.031 102.592 1.00 16.90 N ANISOU 2630 N ILE C 104 1981 2376 2065 -36 -64 6 N ATOM 2631 CA ILE A 104 27.683 56.798 101.807 1.00 17.27 C ANISOU 2631 CA ILE C 104 2086 2342 2131 -42 -76 12 C ATOM 2632 C ILE A 104 27.098 55.613 102.565 1.00 17.69 C ANISOU 2632 C ILE C 104 2200 2366 2153 -12 -79 -14 C ATOM 2633 O ILE A 104 26.459 54.759 101.958 1.00 17.45 O ANISOU 2633 O ILE C 104 2213 2413 2004 -3 -194 9 O ATOM 2634 CB ILE A 104 29.132 56.539 101.270 1.00 17.21 C ANISOU 2634 CB ILE C 104 2071 2316 2151 -82 -37 -1 C ATOM 2635 CG1 ILE A 104 29.098 55.561 100.093 1.00 16.20 C ANISOU 2635 CG1 ILE C 104 2052 2059 2042 -141 13 78 C ATOM 2636 CG2 ILE A 104 30.081 56.069 102.381 1.00 18.28 C ANISOU 2636 CG2 ILE C 104 2270 2448 2225 -15 -7 72 C ATOM 2637 CD1 ILE A 104 30.324 55.693 99.169 1.00 14.67 C ANISOU 2637 CD1 ILE C 104 1996 1782 1795 -127 -21 154 C ATOM 2638 N GLU A 105 27.245 55.602 103.894 1.00 18.83 N ANISOU 2638 N GLU C 105 2367 2488 2297 12 -52 77 N ATOM 2639 CA GLU A 105 26.625 54.567 104.728 1.00 19.86 C ANISOU 2639 CA GLU C 105 2502 2589 2452 21 -59 44 C ATOM 2640 C GLU A 105 25.101 54.665 104.729 1.00 20.50 C ANISOU 2640 C GLU C 105 2553 2694 2542 28 -44 41 C ATOM 2641 O GLU A 105 24.431 53.651 104.762 1.00 21.11 O ANISOU 2641 O GLU C 105 2581 2759 2680 24 -87 -22 O ATOM 2642 CB GLU A 105 27.166 54.620 106.172 1.00 19.79 C ANISOU 2642 CB GLU C 105 2508 2577 2432 31 -22 87 C ATOM 2643 CG GLU A 105 28.603 54.123 106.334 1.00 20.11 C ANISOU 2643 CG GLU C 105 2572 2638 2429 16 -127 81 C ATOM 2644 CD GLU A 105 29.136 54.260 107.766 1.00 22.76 C ANISOU 2644 CD GLU C 105 2903 3099 2644 -26 -23 37 C ATOM 2645 OE1 GLU A 105 28.375 54.673 108.680 1.00 24.28 O ANISOU 2645 OE1 GLU C 105 3064 3522 2639 -118 -178 53 O ATOM 2646 OE2 GLU A 105 30.324 53.973 107.984 1.00 22.34 O ANISOU 2646 OE2 GLU C 105 2832 3329 2325 -110 -237 -6 O ATOM 2647 N ASP A 106 24.565 55.881 104.674 1.00 21.52 N ANISOU 2647 N ASP C 106 2660 2835 2680 29 -50 44 N ATOM 2648 CA ASP A 106 23.105 56.099 104.634 1.00 22.25 C ANISOU 2648 CA ASP C 106 2743 2937 2772 14 -59 25 C ATOM 2649 C ASP A 106 22.473 55.354 103.438 1.00 21.96 C ANISOU 2649 C ASP C 106 2714 2946 2680 37 -51 39 C ATOM 2650 O ASP A 106 21.475 54.627 103.579 1.00 21.58 O ANISOU 2650 O ASP C 106 2648 3041 2510 33 -59 -12 O ATOM 2651 CB ASP A 106 22.808 57.611 104.605 1.00 22.86 C ANISOU 2651 CB ASP C 106 2834 2979 2872 13 -56 40 C ATOM 2652 CG ASP A 106 21.314 57.933 104.600 1.00 26.27 C ANISOU 2652 CG ASP C 106 3166 3493 3322 -43 -38 40 C ATOM 2653 OD1 ASP A 106 20.645 57.672 105.614 1.00 28.90 O ANISOU 2653 OD1 ASP C 106 3275 4022 3682 -51 -155 -6 O ATOM 2654 OD2 ASP A 106 20.773 58.473 103.608 1.00 29.93 O ANISOU 2654 OD2 ASP C 106 3535 3960 3873 -153 -32 65 O ATOM 2655 N ILE A 107 23.099 55.501 102.268 1.00 21.73 N ANISOU 2655 N ILE C 107 2660 2913 2680 50 -82 29 N ATOM 2656 CA ILE A 107 22.621 54.908 101.026 1.00 21.84 C ANISOU 2656 CA ILE C 107 2737 2882 2679 38 -57 24 C ATOM 2657 C ILE A 107 23.038 53.451 100.871 1.00 21.46 C ANISOU 2657 C ILE C 107 2673 2859 2619 58 -79 19 C ATOM 2658 O ILE A 107 22.272 52.633 100.340 1.00 21.87 O ANISOU 2658 O ILE C 107 2673 3074 2562 80 -74 -11 O ATOM 2659 CB ILE A 107 23.137 55.730 99.813 1.00 21.84 C ANISOU 2659 CB ILE C 107 2759 2846 2692 36 -83 7 C ATOM 2660 CG1 ILE A 107 22.714 57.201 99.946 1.00 22.69 C ANISOU 2660 CG1 ILE C 107 2983 2893 2743 28 -38 28 C ATOM 2661 CG2 ILE A 107 22.654 55.132 98.482 1.00 22.71 C ANISOU 2661 CG2 ILE C 107 2834 3020 2774 3 30 64 C ATOM 2662 CD1 ILE A 107 21.233 57.418 99.805 1.00 24.00 C ANISOU 2662 CD1 ILE C 107 3177 2963 2980 -17 6 41 C ATOM 2663 N ASN A 108 24.248 53.129 101.324 1.00 21.07 N ANISOU 2663 N ASN C 108 2619 2848 2539 88 -96 33 N ATOM 2664 CA ASN A 108 24.849 51.824 101.095 1.00 21.24 C ANISOU 2664 CA ASN C 108 2632 2850 2589 31 -82 76 C ATOM 2665 C ASN A 108 25.367 51.261 102.410 1.00 21.95 C ANISOU 2665 C ASN C 108 2741 2953 2645 44 -91 80 C ATOM 2666 O ASN A 108 26.568 51.119 102.584 1.00 21.72 O ANISOU 2666 O ASN C 108 2703 2986 2561 32 -191 114 O ATOM 2667 CB ASN A 108 26.012 51.933 100.075 1.00 20.99 C ANISOU 2667 CB ASN C 108 2588 2852 2535 51 -69 77 C ATOM 2668 CG ASN A 108 26.505 50.566 99.566 1.00 20.42 C ANISOU 2668 CG ASN C 108 2526 2729 2503 -8 -29 128 C ATOM 2669 OD1 ASN A 108 26.219 49.537 100.159 1.00 21.42 O ANISOU 2669 OD1 ASN C 108 2749 2797 2591 109 -89 31 O ATOM 2670 ND2 ASN A 108 27.276 50.567 98.455 1.00 18.69 N ANISOU 2670 ND2 ASN C 108 2459 2471 2171 -108 50 183 N ATOM 2671 N PRO A 109 24.463 50.966 103.361 1.00 22.74 N ANISOU 2671 N PRO C 109 2841 3031 2766 45 -89 90 N ATOM 2672 CA PRO A 109 24.909 50.442 104.665 1.00 23.43 C ANISOU 2672 CA PRO C 109 2931 3095 2874 66 -76 77 C ATOM 2673 C PRO A 109 25.777 49.195 104.574 1.00 23.71 C ANISOU 2673 C PRO C 109 2953 3129 2926 92 -94 94 C ATOM 2674 O PRO A 109 26.677 49.042 105.394 1.00 23.87 O ANISOU 2674 O PRO C 109 2986 3196 2886 135 -99 161 O ATOM 2675 CB PRO A 109 23.594 50.130 105.410 1.00 23.42 C ANISOU 2675 CB PRO C 109 2933 3101 2861 43 -96 66 C ATOM 2676 CG PRO A 109 22.516 50.204 104.394 1.00 23.32 C ANISOU 2676 CG PRO C 109 2908 3083 2868 38 -118 54 C ATOM 2677 CD PRO A 109 22.998 51.122 103.288 1.00 22.82 C ANISOU 2677 CD PRO C 109 2880 2987 2802 36 -88 57 C ATOM 2678 N ASP A 110 25.527 48.321 103.600 1.00 24.14 N ANISOU 2678 N ASP C 110 3039 3143 2990 77 -89 60 N ATOM 2679 CA ASP A 110 26.240 47.042 103.538 1.00 24.64 C ANISOU 2679 CA ASP C 110 3105 3168 3088 28 -58 56 C ATOM 2680 C ASP A 110 27.708 47.195 103.172 1.00 24.07 C ANISOU 2680 C ASP C 110 3043 3075 3026 0 -34 89 C ATOM 2681 O ASP A 110 28.552 46.481 103.717 1.00 24.01 O ANISOU 2681 O ASP C 110 3115 3062 2944 30 -53 167 O ATOM 2682 CB ASP A 110 25.600 46.083 102.525 1.00 25.67 C ANISOU 2682 CB ASP C 110 3241 3299 3212 45 -38 37 C ATOM 2683 CG ASP A 110 24.228 45.577 102.952 1.00 28.58 C ANISOU 2683 CG ASP C 110 3512 3735 3612 58 -31 1 C ATOM 2684 OD1 ASP A 110 23.832 45.740 104.136 1.00 29.76 O ANISOU 2684 OD1 ASP C 110 3719 3962 3624 51 -112 -47 O ATOM 2685 OD2 ASP A 110 23.514 44.977 102.111 1.00 31.42 O ANISOU 2685 OD2 ASP C 110 3827 4187 3921 155 54 -36 O ATOM 2686 N LYS A 111 28.010 48.104 102.236 1.00 23.30 N ANISOU 2686 N LYS C 111 2967 2979 2907 -53 -17 92 N ATOM 2687 CA LYS A 111 29.354 48.183 101.648 1.00 22.73 C ANISOU 2687 CA LYS C 111 2882 2866 2887 -26 12 100 C ATOM 2688 C LYS A 111 29.964 49.569 101.612 1.00 21.07 C ANISOU 2688 C LYS C 111 2673 2685 2646 -43 12 126 C ATOM 2689 O LYS A 111 31.143 49.704 101.297 1.00 20.72 O ANISOU 2689 O LYS C 111 2674 2602 2596 -67 -1 249 O ATOM 2690 CB LYS A 111 29.363 47.628 100.209 1.00 23.48 C ANISOU 2690 CB LYS C 111 2963 3035 2923 -62 42 73 C ATOM 2691 CG LYS A 111 28.778 46.224 100.032 1.00 26.12 C ANISOU 2691 CG LYS C 111 3321 3287 3316 16 9 74 C ATOM 2692 CD LYS A 111 29.292 45.532 98.751 1.00 30.17 C ANISOU 2692 CD LYS C 111 3870 3825 3768 25 -12 -18 C ATOM 2693 CE LYS A 111 28.411 45.835 97.517 1.00 32.67 C ANISOU 2693 CE LYS C 111 4101 4168 4144 45 -1 -37 C ATOM 2694 NZ LYS A 111 29.096 45.720 96.138 1.00 32.75 N ANISOU 2694 NZ LYS C 111 4120 4087 4235 149 -168 -26 N ATOM 2695 N GLY A 112 29.165 50.582 101.930 1.00 19.30 N ANISOU 2695 N GLY C 112 2496 2406 2430 -3 -12 114 N ATOM 2696 CA GLY A 112 29.564 51.982 101.750 1.00 18.15 C ANISOU 2696 CA GLY C 112 2308 2347 2239 2 -45 74 C ATOM 2697 C GLY A 112 30.763 52.360 102.590 1.00 18.22 C ANISOU 2697 C GLY C 112 2297 2397 2227 -10 -81 55 C ATOM 2698 O GLY A 112 30.734 52.218 103.809 1.00 18.16 O ANISOU 2698 O GLY C 112 2249 2553 2096 -13 -110 80 O ATOM 2699 N GLU A 113 31.835 52.805 101.942 1.00 17.34 N ANISOU 2699 N GLU C 113 2214 2281 2094 -46 -106 26 N ATOM 2700 CA GLU A 113 33.046 53.207 102.658 1.00 17.59 C ANISOU 2700 CA GLU C 113 2263 2344 2076 -69 -59 17 C ATOM 2701 C GLU A 113 33.785 54.351 102.010 1.00 16.73 C ANISOU 2701 C GLU C 113 2121 2262 1973 -78 -37 7 C ATOM 2702 O GLU A 113 33.705 54.547 100.802 1.00 15.89 O ANISOU 2702 O GLU C 113 1995 2262 1778 -126 -64 68 O ATOM 2703 CB GLU A 113 34.038 52.047 102.745 1.00 17.95 C ANISOU 2703 CB GLU C 113 2341 2324 2152 -89 -46 -8 C ATOM 2704 CG GLU A 113 33.737 50.978 103.751 1.00 20.75 C ANISOU 2704 CG GLU C 113 2683 2730 2470 -42 -17 52 C ATOM 2705 CD GLU A 113 34.935 50.081 103.955 1.00 21.12 C ANISOU 2705 CD GLU C 113 2759 2779 2485 -104 -49 59 C ATOM 2706 OE1 GLU A 113 35.965 50.576 104.428 1.00 22.09 O ANISOU 2706 OE1 GLU C 113 2856 2994 2543 -83 44 86 O ATOM 2707 OE2 GLU A 113 34.867 48.901 103.602 1.00 21.97 O ANISOU 2707 OE2 GLU C 113 2973 2793 2582 -61 -2 165 O ATOM 2708 N ILE A 114 34.543 55.069 102.828 1.00 16.42 N ANISOU 2708 N ILE C 114 2146 2270 1820 -119 -35 18 N ATOM 2709 CA ILE A 114 35.496 56.056 102.368 1.00 16.10 C ANISOU 2709 CA ILE C 114 2038 2207 1869 -88 1 59 C ATOM 2710 C ILE A 114 36.891 55.424 102.365 1.00 16.11 C ANISOU 2710 C ILE C 114 2053 2224 1844 -104 3 111 C ATOM 2711 O ILE A 114 37.218 54.562 103.214 1.00 16.57 O ANISOU 2711 O ILE C 114 2071 2371 1851 -168 4 196 O ATOM 2712 CB ILE A 114 35.425 57.318 103.243 1.00 16.21 C ANISOU 2712 CB ILE C 114 2061 2268 1828 -103 42 68 C ATOM 2713 CG1 ILE A 114 33.997 57.876 103.232 1.00 17.08 C ANISOU 2713 CG1 ILE C 114 2002 2420 2067 -110 -88 -25 C ATOM 2714 CG2 ILE A 114 36.432 58.409 102.827 1.00 17.02 C ANISOU 2714 CG2 ILE C 114 2206 2242 2018 -67 40 16 C ATOM 2715 CD1 ILE A 114 33.440 58.205 101.862 1.00 17.75 C ANISOU 2715 CD1 ILE C 114 2101 2482 2162 -198 -67 -47 C ATOM 2716 N GLN A 115 37.696 55.829 101.389 1.00 15.40 N ANISOU 2716 N GLN C 115 1948 2176 1725 -104 -6 76 N ATOM 2717 CA GLN A 115 39.095 55.418 101.274 1.00 15.07 C ANISOU 2717 CA GLN C 115 1922 2128 1674 -142 12 -3 C ATOM 2718 C GLN A 115 39.903 56.685 101.189 1.00 14.63 C ANISOU 2718 C GLN C 115 1864 2136 1557 -132 -17 -20 C ATOM 2719 O GLN A 115 39.533 57.610 100.495 1.00 15.10 O ANISOU 2719 O GLN C 115 1899 2320 1516 -233 -42 -85 O ATOM 2720 CB GLN A 115 39.371 54.647 99.977 1.00 14.27 C ANISOU 2720 CB GLN C 115 1865 1930 1627 -74 0 40 C ATOM 2721 CG GLN A 115 38.460 53.517 99.644 1.00 15.16 C ANISOU 2721 CG GLN C 115 2050 2007 1702 -212 52 26 C ATOM 2722 CD GLN A 115 38.841 52.901 98.331 1.00 14.85 C ANISOU 2722 CD GLN C 115 2118 1859 1665 -145 -67 13 C ATOM 2723 OE1 GLN A 115 38.724 53.541 97.281 1.00 15.76 O ANISOU 2723 OE1 GLN C 115 2034 2207 1744 -381 13 125 O ATOM 2724 NE2 GLN A 115 39.311 51.676 98.372 1.00 14.44 N ANISOU 2724 NE2 GLN C 115 2215 1770 1502 -171 -40 74 N ATOM 2725 N VAL A 116 41.038 56.735 101.886 1.00 15.06 N ANISOU 2725 N VAL C 116 1885 2236 1599 -208 7 -12 N ATOM 2726 CA VAL A 116 41.862 57.923 101.910 1.00 14.60 C ANISOU 2726 CA VAL C 116 1817 2134 1596 -147 2 0 C ATOM 2727 C VAL A 116 42.994 57.850 100.871 1.00 14.78 C ANISOU 2727 C VAL C 116 1878 2109 1628 -169 -3 -11 C ATOM 2728 O VAL A 116 43.836 56.940 100.912 1.00 14.54 O ANISOU 2728 O VAL C 116 1842 2157 1525 -219 56 73 O ATOM 2729 CB VAL A 116 42.433 58.217 103.342 1.00 15.23 C ANISOU 2729 CB VAL C 116 1893 2185 1708 -125 -6 -59 C ATOM 2730 CG1 VAL A 116 43.225 59.479 103.327 1.00 14.49 C ANISOU 2730 CG1 VAL C 116 1905 2087 1512 -138 -30 87 C ATOM 2731 CG2 VAL A 116 41.323 58.336 104.356 1.00 15.94 C ANISOU 2731 CG2 VAL C 116 1986 2245 1823 -83 -5 -58 C ATOM 2732 N GLU A 117 42.982 58.807 99.934 1.00 13.85 N ANISOU 2732 N GLU C 117 1689 2054 1519 -114 -30 -24 N ATOM 2733 CA GLU A 117 44.032 58.921 98.902 1.00 13.58 C ANISOU 2733 CA GLU C 117 1663 1897 1597 -116 -2 -46 C ATOM 2734 C GLU A 117 45.235 59.680 99.471 1.00 13.23 C ANISOU 2734 C GLU C 117 1617 1800 1608 -80 15 -42 C ATOM 2735 O GLU A 117 45.119 60.856 99.852 1.00 13.29 O ANISOU 2735 O GLU C 117 1588 1953 1507 -230 75 -167 O ATOM 2736 CB GLU A 117 43.492 59.600 97.628 1.00 13.58 C ANISOU 2736 CB GLU C 117 1659 1887 1611 -147 -24 -55 C ATOM 2737 CG GLU A 117 42.741 58.636 96.702 1.00 13.11 C ANISOU 2737 CG GLU C 117 1676 1708 1595 -152 12 -48 C ATOM 2738 CD GLU A 117 43.659 57.809 95.823 1.00 13.47 C ANISOU 2738 CD GLU C 117 1705 1824 1587 -92 35 -81 C ATOM 2739 OE1 GLU A 117 44.881 57.817 96.066 1.00 14.27 O ANISOU 2739 OE1 GLU C 117 1632 2117 1672 50 -244 -175 O ATOM 2740 OE2 GLU A 117 43.154 57.119 94.917 1.00 13.81 O ANISOU 2740 OE2 GLU C 117 1780 1713 1752 -115 2 -364 O ATOM 2741 N LEU A 118 46.393 59.017 99.480 1.00 13.03 N ANISOU 2741 N LEU C 118 1640 1800 1511 -87 -24 -48 N ATOM 2742 CA LEU A 118 47.586 59.539 100.115 1.00 13.53 C ANISOU 2742 CA LEU C 118 1741 1849 1548 -66 14 -63 C ATOM 2743 C LEU A 118 48.476 60.269 99.124 1.00 14.34 C ANISOU 2743 C LEU C 118 1797 1957 1693 -92 6 -93 C ATOM 2744 O LEU A 118 49.091 59.632 98.257 1.00 14.69 O ANISOU 2744 O LEU C 118 1852 2130 1598 -228 -53 -191 O ATOM 2745 CB LEU A 118 48.389 58.406 100.793 1.00 13.47 C ANISOU 2745 CB LEU C 118 1666 1810 1640 -75 61 -84 C ATOM 2746 CG LEU A 118 47.629 57.575 101.836 1.00 14.18 C ANISOU 2746 CG LEU C 118 1867 1906 1615 -97 22 -52 C ATOM 2747 CD1 LEU A 118 48.374 56.336 102.222 1.00 15.32 C ANISOU 2747 CD1 LEU C 118 2026 2037 1757 26 33 -50 C ATOM 2748 CD2 LEU A 118 47.297 58.404 103.103 1.00 14.91 C ANISOU 2748 CD2 LEU C 118 1744 2162 1757 -157 88 -32 C ATOM 2749 N TYR A 119 48.530 61.584 99.269 1.00 13.59 N ANISOU 2749 N TYR C 119 1756 1772 1635 -137 -17 -173 N ATOM 2750 CA TYR A 119 49.305 62.508 98.440 1.00 14.70 C ANISOU 2750 CA TYR C 119 1885 1894 1804 -85 -16 -123 C ATOM 2751 C TYR A 119 49.960 63.526 99.363 1.00 16.19 C ANISOU 2751 C TYR C 119 2048 2150 1952 -65 0 -124 C ATOM 2752 O TYR A 119 49.382 63.927 100.366 1.00 17.05 O ANISOU 2752 O TYR C 119 2090 2350 2038 -135 -62 -167 O ATOM 2753 CB TYR A 119 48.431 63.263 97.418 1.00 14.21 C ANISOU 2753 CB TYR C 119 1821 1809 1769 -111 -4 -132 C ATOM 2754 CG TYR A 119 48.018 62.426 96.240 1.00 12.64 C ANISOU 2754 CG TYR C 119 1620 1624 1556 -118 50 -56 C ATOM 2755 CD1 TYR A 119 48.773 62.420 95.061 1.00 14.25 C ANISOU 2755 CD1 TYR C 119 1660 2079 1674 -13 119 -80 C ATOM 2756 CD2 TYR A 119 46.924 61.585 96.316 1.00 12.77 C ANISOU 2756 CD2 TYR C 119 1742 1669 1437 -37 147 -78 C ATOM 2757 CE1 TYR A 119 48.423 61.599 93.980 1.00 12.84 C ANISOU 2757 CE1 TYR C 119 1662 1702 1514 -82 16 -54 C ATOM 2758 CE2 TYR A 119 46.569 60.751 95.224 1.00 11.17 C ANISOU 2758 CE2 TYR C 119 1561 1433 1248 67 73 -191 C ATOM 2759 CZ TYR A 119 47.317 60.793 94.070 1.00 12.72 C ANISOU 2759 CZ TYR C 119 1583 1750 1498 -15 152 -212 C ATOM 2760 OH TYR A 119 46.969 59.990 93.010 1.00 13.03 O ANISOU 2760 OH TYR C 119 1804 1917 1227 -17 227 -221 O ATOM 2761 N GLY A 120 51.160 63.951 99.005 1.00 17.78 N ANISOU 2761 N GLY C 120 2215 2383 2155 -69 -17 -65 N ATOM 2762 CA GLY A 120 51.929 64.901 99.794 1.00 19.42 C ANISOU 2762 CA GLY C 120 2412 2528 2439 -9 -8 -59 C ATOM 2763 C GLY A 120 52.365 64.427 101.174 1.00 20.71 C ANISOU 2763 C GLY C 120 2561 2702 2604 -8 -17 -22 C ATOM 2764 O GLY A 120 52.501 63.221 101.419 1.00 20.48 O ANISOU 2764 O GLY C 120 2455 2768 2558 -19 -43 -90 O ATOM 2765 N ASP A 121 52.510 65.397 102.081 1.00 22.74 N ANISOU 2765 N ASP C 121 2805 2968 2865 -17 -4 -59 N ATOM 2766 CA ASP A 121 53.121 65.210 103.405 1.00 24.48 C ANISOU 2766 CA ASP C 121 3100 3185 3016 -27 -1 -25 C ATOM 2767 C ASP A 121 52.133 64.847 104.531 1.00 24.89 C ANISOU 2767 C ASP C 121 3162 3216 3079 -3 -20 -41 C ATOM 2768 O ASP A 121 51.978 65.601 105.515 1.00 25.62 O ANISOU 2768 O ASP C 121 3287 3325 3120 -49 -44 -54 O ATOM 2769 CB ASP A 121 53.879 66.484 103.818 1.00 24.89 C ANISOU 2769 CB ASP C 121 3150 3180 3126 -14 12 -39 C ATOM 2770 CG ASP A 121 55.125 66.747 102.979 1.00 27.58 C ANISOU 2770 CG ASP C 121 3491 3551 3435 0 5 -38 C ATOM 2771 OD1 ASP A 121 55.880 65.787 102.693 1.00 29.31 O ANISOU 2771 OD1 ASP C 121 3716 3725 3693 -99 -16 -189 O ATOM 2772 OD2 ASP A 121 55.395 67.911 102.593 1.00 29.52 O ANISOU 2772 OD2 ASP C 121 3834 3710 3673 101 7 12 O ATOM 2773 N TRP A 122 51.497 63.692 104.406 1.00 25.11 N ANISOU 2773 N TRP C 122 3213 3259 3067 -3 -12 -45 N ATOM 2774 CA TRP A 122 50.552 63.206 105.418 1.00 25.25 C ANISOU 2774 CA TRP C 122 3177 3260 3153 5 -7 -23 C ATOM 2775 C TRP A 122 51.319 62.598 106.592 1.00 25.65 C ANISOU 2775 C TRP C 122 3190 3361 3193 -10 0 -42 C ATOM 2776 O TRP A 122 52.489 62.213 106.432 1.00 26.09 O ANISOU 2776 O TRP C 122 3157 3504 3251 16 -7 -90 O ATOM 2777 CB TRP A 122 49.609 62.168 104.816 1.00 25.09 C ANISOU 2777 CB TRP C 122 3148 3246 3137 4 16 0 C ATOM 2778 CG TRP A 122 50.297 60.972 104.241 1.00 24.69 C ANISOU 2778 CG TRP C 122 3084 3257 3039 -25 -15 12 C ATOM 2779 CD1 TRP A 122 50.774 60.836 102.967 1.00 24.87 C ANISOU 2779 CD1 TRP C 122 3053 3315 3081 14 24 22 C ATOM 2780 CD2 TRP A 122 50.563 59.721 104.904 1.00 24.63 C ANISOU 2780 CD2 TRP C 122 3012 3270 3076 -51 -22 -35 C ATOM 2781 NE1 TRP A 122 51.329 59.592 102.801 1.00 23.92 N ANISOU 2781 NE1 TRP C 122 2888 3243 2954 -30 7 -52 N ATOM 2782 CE2 TRP A 122 51.222 58.888 103.974 1.00 24.16 C ANISOU 2782 CE2 TRP C 122 2982 3225 2971 4 14 -41 C ATOM 2783 CE3 TRP A 122 50.334 59.236 106.199 1.00 23.92 C ANISOU 2783 CE3 TRP C 122 2967 3144 2975 -16 7 -4 C ATOM 2784 CZ2 TRP A 122 51.638 57.599 104.289 1.00 24.27 C ANISOU 2784 CZ2 TRP C 122 2955 3302 2965 -102 17 -21 C ATOM 2785 CZ3 TRP A 122 50.743 57.956 106.516 1.00 23.95 C ANISOU 2785 CZ3 TRP C 122 3014 3194 2892 -35 26 -24 C ATOM 2786 CH2 TRP A 122 51.390 57.141 105.560 1.00 23.40 C ANISOU 2786 CH2 TRP C 122 2834 3190 2866 -80 21 1 C ATOM 2787 N THR A 123 50.668 62.476 107.754 1.00 25.40 N ANISOU 2787 N THR C 123 3191 3277 3181 -36 -5 -77 N ATOM 2788 CA THR A 123 51.335 61.939 108.944 1.00 25.25 C ANISOU 2788 CA THR C 123 3173 3288 3132 -39 -17 -83 C ATOM 2789 C THR A 123 50.576 60.758 109.552 1.00 24.86 C ANISOU 2789 C THR C 123 3133 3243 3068 -43 -9 -87 C ATOM 2790 O THR A 123 49.377 60.575 109.298 1.00 24.79 O ANISOU 2790 O THR C 123 3069 3312 3035 -127 -29 -141 O ATOM 2791 CB THR A 123 51.532 63.029 110.018 1.00 25.28 C ANISOU 2791 CB THR C 123 3194 3237 3175 -46 -4 -81 C ATOM 2792 OG1 THR A 123 50.253 63.401 110.560 1.00 26.78 O ANISOU 2792 OG1 THR C 123 3328 3537 3309 -44 -35 -93 O ATOM 2793 CG2 THR A 123 52.155 64.288 109.418 1.00 24.98 C ANISOU 2793 CG2 THR C 123 3133 3238 3117 13 -31 -74 C ATOM 2794 N TYR A 124 51.274 59.958 110.354 1.00 24.68 N ANISOU 2794 N TYR C 124 3101 3262 3013 -47 6 -66 N ATOM 2795 CA TYR A 124 50.653 58.831 111.049 1.00 24.87 C ANISOU 2795 CA TYR C 124 3136 3262 3051 -62 38 -18 C ATOM 2796 C TYR A 124 49.675 59.286 112.136 1.00 24.93 C ANISOU 2796 C TYR C 124 3128 3302 3040 -52 52 15 C ATOM 2797 O TYR A 124 48.746 58.555 112.473 1.00 24.78 O ANISOU 2797 O TYR C 124 3104 3358 2952 -82 95 19 O ATOM 2798 CB TYR A 124 51.718 57.904 111.635 1.00 24.98 C ANISOU 2798 CB TYR C 124 3160 3299 3030 -77 31 24 C ATOM 2799 CG TYR A 124 52.512 57.165 110.589 1.00 25.29 C ANISOU 2799 CG TYR C 124 3245 3212 3149 -77 51 21 C ATOM 2800 CD1 TYR A 124 51.901 56.226 109.762 1.00 25.76 C ANISOU 2800 CD1 TYR C 124 3286 3348 3155 -82 87 17 C ATOM 2801 CD2 TYR A 124 53.868 57.411 110.414 1.00 25.78 C ANISOU 2801 CD2 TYR C 124 3252 3329 3210 -118 61 64 C ATOM 2802 CE1 TYR A 124 52.630 55.539 108.796 1.00 26.48 C ANISOU 2802 CE1 TYR C 124 3329 3569 3161 -67 63 47 C ATOM 2803 CE2 TYR A 124 54.605 56.728 109.446 1.00 26.76 C ANISOU 2803 CE2 TYR C 124 3372 3522 3273 -32 47 8 C ATOM 2804 CZ TYR A 124 53.982 55.796 108.649 1.00 26.61 C ANISOU 2804 CZ TYR C 124 3406 3506 3195 7 8 26 C ATOM 2805 OH TYR A 124 54.701 55.108 107.701 1.00 26.67 O ANISOU 2805 OH TYR C 124 3334 3526 3271 -55 -8 80 O ATOM 2806 N ASP A 125 49.885 60.490 112.661 1.00 25.55 N ANISOU 2806 N ASP C 125 3190 3406 3112 -66 31 -20 N ATOM 2807 CA ASP A 125 48.943 61.105 113.595 1.00 25.97 C ANISOU 2807 CA ASP C 125 3265 3436 3165 -44 11 -8 C ATOM 2808 C ASP A 125 47.637 61.387 112.863 1.00 24.98 C ANISOU 2808 C ASP C 125 3136 3340 3013 0 17 -5 C ATOM 2809 O ASP A 125 46.557 61.092 113.374 1.00 25.11 O ANISOU 2809 O ASP C 125 3219 3462 2856 -36 13 0 O ATOM 2810 CB ASP A 125 49.511 62.406 114.190 1.00 26.65 C ANISOU 2810 CB ASP C 125 3357 3483 3284 1 19 0 C ATOM 2811 CG ASP A 125 50.449 62.172 115.390 1.00 29.18 C ANISOU 2811 CG ASP C 125 3751 3737 3598 2 50 -17 C ATOM 2812 OD1 ASP A 125 50.622 61.018 115.847 1.00 31.26 O ANISOU 2812 OD1 ASP C 125 4174 3992 3711 -42 106 -36 O ATOM 2813 OD2 ASP A 125 51.037 63.143 115.921 1.00 32.18 O ANISOU 2813 OD2 ASP C 125 4163 4042 4019 59 82 -149 O ATOM 2814 N GLN A 126 47.738 61.957 111.661 1.00 24.48 N ANISOU 2814 N GLN C 126 3069 3283 2947 -25 16 -20 N ATOM 2815 CA GLN A 126 46.563 62.170 110.804 1.00 23.67 C ANISOU 2815 CA GLN C 126 2988 3169 2834 -40 15 -15 C ATOM 2816 C GLN A 126 45.872 60.839 110.502 1.00 22.96 C ANISOU 2816 C GLN C 126 2920 3127 2674 -62 51 -36 C ATOM 2817 O GLN A 126 44.651 60.726 110.598 1.00 22.57 O ANISOU 2817 O GLN C 126 2888 3204 2483 -97 87 -70 O ATOM 2818 CB GLN A 126 46.955 62.877 109.497 1.00 23.79 C ANISOU 2818 CB GLN C 126 3023 3141 2876 -54 -30 -15 C ATOM 2819 CG GLN A 126 47.291 64.349 109.635 1.00 24.47 C ANISOU 2819 CG GLN C 126 3055 3227 3014 14 -17 -77 C ATOM 2820 CD GLN A 126 47.836 64.963 108.357 1.00 25.78 C ANISOU 2820 CD GLN C 126 3277 3339 3178 -27 -51 -53 C ATOM 2821 OE1 GLN A 126 48.168 64.246 107.411 1.00 24.19 O ANISOU 2821 OE1 GLN C 126 3040 3248 2901 0 -27 -176 O ATOM 2822 NE2 GLN A 126 47.959 66.298 108.335 1.00 26.75 N ANISOU 2822 NE2 GLN C 126 3447 3267 3449 -5 3 -59 N ATOM 2823 N ALA A 127 46.659 59.819 110.172 1.00 22.75 N ANISOU 2823 N ALA C 127 2874 3113 2655 -64 63 -31 N ATOM 2824 CA ALA A 127 46.111 58.497 109.866 1.00 22.55 C ANISOU 2824 CA ALA C 127 2840 3060 2666 -40 55 -2 C ATOM 2825 C ALA A 127 45.294 57.914 111.020 1.00 22.78 C ANISOU 2825 C ALA C 127 2858 3090 2706 -2 69 0 C ATOM 2826 O ALA A 127 44.252 57.295 110.808 1.00 22.11 O ANISOU 2826 O ALA C 127 2777 3106 2518 -4 146 -28 O ATOM 2827 CB ALA A 127 47.213 57.535 109.439 1.00 22.57 C ANISOU 2827 CB ALA C 127 2862 3020 2690 -68 65 19 C ATOM 2828 N GLN A 128 45.769 58.126 112.248 1.00 23.03 N ANISOU 2828 N GLN C 128 2900 3139 2709 -5 64 -29 N ATOM 2829 CA GLN A 128 45.049 57.664 113.432 1.00 23.23 C ANISOU 2829 CA GLN C 128 2937 3104 2784 -28 23 -17 C ATOM 2830 C GLN A 128 43.701 58.386 113.577 1.00 22.87 C ANISOU 2830 C GLN C 128 2910 3064 2716 -35 7 -22 C ATOM 2831 O GLN A 128 42.708 57.764 113.956 1.00 22.58 O ANISOU 2831 O GLN C 128 2905 3085 2587 -76 -42 -28 O ATOM 2832 CB GLN A 128 45.911 57.828 114.700 1.00 23.67 C ANISOU 2832 CB GLN C 128 2976 3172 2844 -49 24 -12 C ATOM 2833 CG GLN A 128 45.308 57.202 115.954 1.00 23.06 C ANISOU 2833 CG GLN C 128 2959 3059 2744 -70 65 14 C ATOM 2834 CD GLN A 128 44.978 55.720 115.806 1.00 22.55 C ANISOU 2834 CD GLN C 128 2906 3124 2537 -85 89 39 C ATOM 2835 OE1 GLN A 128 45.853 54.903 115.523 1.00 22.89 O ANISOU 2835 OE1 GLN C 128 3009 3412 2273 -205 204 33 O ATOM 2836 NE2 GLN A 128 43.711 55.367 116.018 1.00 22.82 N ANISOU 2836 NE2 GLN C 128 2852 3187 2630 -86 170 17 N ATOM 2837 N GLN A 129 43.675 59.680 113.257 1.00 22.19 N ANISOU 2837 N GLN C 129 2862 2964 2605 -52 -10 -40 N ATOM 2838 CA GLN A 129 42.429 60.460 113.240 1.00 22.25 C ANISOU 2838 CA GLN C 129 2835 2971 2645 -44 -17 -35 C ATOM 2839 C GLN A 129 41.430 59.876 112.226 1.00 21.23 C ANISOU 2839 C GLN C 129 2718 2895 2453 -85 -29 -10 C ATOM 2840 O GLN A 129 40.237 59.806 112.491 1.00 21.06 O ANISOU 2840 O GLN C 129 2728 2988 2283 -158 -137 -48 O ATOM 2841 CB GLN A 129 42.693 61.943 112.944 1.00 22.63 C ANISOU 2841 CB GLN C 129 2910 2978 2708 -65 5 -33 C ATOM 2842 CG GLN A 129 43.612 62.687 113.931 1.00 26.34 C ANISOU 2842 CG GLN C 129 3267 3442 3299 -14 47 -72 C ATOM 2843 CD GLN A 129 44.013 64.078 113.426 1.00 30.66 C ANISOU 2843 CD GLN C 129 3835 3869 3943 -9 52 -16 C ATOM 2844 OE1 GLN A 129 43.161 64.868 113.018 1.00 33.47 O ANISOU 2844 OE1 GLN C 129 4239 4173 4305 -33 156 10 O ATOM 2845 NE2 GLN A 129 45.313 64.378 113.450 1.00 32.94 N ANISOU 2845 NE2 GLN C 129 4194 4149 4172 -23 28 3 N ATOM 2846 N TRP A 130 41.919 59.426 111.067 1.00 20.46 N ANISOU 2846 N TRP C 130 2624 2758 2390 -123 -61 -24 N ATOM 2847 CA TRP A 130 41.035 58.785 110.105 1.00 19.61 C ANISOU 2847 CA TRP C 130 2487 2669 2293 -83 -33 -49 C ATOM 2848 C TRP A 130 40.369 57.541 110.688 1.00 20.04 C ANISOU 2848 C TRP C 130 2533 2816 2263 -76 -29 -49 C ATOM 2849 O TRP A 130 39.151 57.371 110.564 1.00 19.35 O ANISOU 2849 O TRP C 130 2343 2968 2039 -144 -70 -92 O ATOM 2850 CB TRP A 130 41.762 58.438 108.773 1.00 19.61 C ANISOU 2850 CB TRP C 130 2500 2661 2288 -87 -39 -32 C ATOM 2851 CG TRP A 130 42.480 59.599 108.180 1.00 17.89 C ANISOU 2851 CG TRP C 130 2214 2432 2150 -89 5 -50 C ATOM 2852 CD1 TRP A 130 42.151 60.912 108.314 1.00 17.03 C ANISOU 2852 CD1 TRP C 130 2154 2332 1984 -98 20 -74 C ATOM 2853 CD2 TRP A 130 43.688 59.570 107.402 1.00 17.59 C ANISOU 2853 CD2 TRP C 130 2192 2444 2045 -121 63 -54 C ATOM 2854 NE1 TRP A 130 43.068 61.706 107.678 1.00 16.73 N ANISOU 2854 NE1 TRP C 130 2198 2385 1771 -167 -4 -96 N ATOM 2855 CE2 TRP A 130 44.033 60.909 107.116 1.00 16.32 C ANISOU 2855 CE2 TRP C 130 1964 2337 1900 -141 45 -67 C ATOM 2856 CE3 TRP A 130 44.505 58.545 106.914 1.00 17.52 C ANISOU 2856 CE3 TRP C 130 2163 2446 2047 0 109 -87 C ATOM 2857 CZ2 TRP A 130 45.146 61.252 106.345 1.00 17.27 C ANISOU 2857 CZ2 TRP C 130 2171 2401 1987 -91 171 -43 C ATOM 2858 CZ3 TRP A 130 45.625 58.884 106.168 1.00 16.01 C ANISOU 2858 CZ3 TRP C 130 1966 2354 1763 -46 53 7 C ATOM 2859 CH2 TRP A 130 45.940 60.224 105.899 1.00 15.45 C ANISOU 2859 CH2 TRP C 130 1834 2263 1770 -91 49 -88 C ATOM 2860 N LEU A 131 41.152 56.677 111.337 1.00 20.49 N ANISOU 2860 N LEU C 131 2540 2806 2436 -95 -18 -64 N ATOM 2861 CA LEU A 131 40.612 55.454 111.937 1.00 21.73 C ANISOU 2861 CA LEU C 131 2732 2911 2614 -75 -12 -23 C ATOM 2862 C LEU A 131 39.597 55.768 113.036 1.00 22.11 C ANISOU 2862 C LEU C 131 2779 2974 2647 -43 -48 -32 C ATOM 2863 O LEU A 131 38.584 55.073 113.173 1.00 22.92 O ANISOU 2863 O LEU C 131 2956 3161 2591 -55 -81 -24 O ATOM 2864 CB LEU A 131 41.735 54.574 112.515 1.00 21.84 C ANISOU 2864 CB LEU C 131 2758 2896 2642 -75 4 -29 C ATOM 2865 CG LEU A 131 42.725 53.961 111.525 1.00 22.10 C ANISOU 2865 CG LEU C 131 2763 2840 2791 -127 47 3 C ATOM 2866 CD1 LEU A 131 44.003 53.496 112.275 1.00 22.80 C ANISOU 2866 CD1 LEU C 131 2885 2943 2835 -83 88 -56 C ATOM 2867 CD2 LEU A 131 42.057 52.814 110.760 1.00 23.99 C ANISOU 2867 CD2 LEU C 131 3039 3195 2879 -84 70 0 C ATOM 2868 N ASP A 132 39.897 56.799 113.820 1.00 22.72 N ANISOU 2868 N ASP C 132 2868 3018 2743 -78 -47 -11 N ATOM 2869 CA ASP A 132 39.039 57.245 114.923 1.00 23.10 C ANISOU 2869 CA ASP C 132 2889 3123 2764 -58 -51 -3 C ATOM 2870 C ASP A 132 37.742 57.852 114.403 1.00 23.26 C ANISOU 2870 C ASP C 132 2876 3177 2783 -70 -32 34 C ATOM 2871 O ASP A 132 36.761 57.957 115.150 1.00 23.48 O ANISOU 2871 O ASP C 132 2879 3348 2692 -85 -32 103 O ATOM 2872 CB ASP A 132 39.749 58.322 115.758 1.00 23.22 C ANISOU 2872 CB ASP C 132 2889 3141 2789 -58 -46 -66 C ATOM 2873 CG ASP A 132 40.917 57.783 116.578 1.00 23.26 C ANISOU 2873 CG ASP C 132 3022 3192 2620 -48 -68 1 C ATOM 2874 OD1 ASP A 132 41.093 56.549 116.686 1.00 24.46 O ANISOU 2874 OD1 ASP C 132 3288 3296 2707 -213 -52 -17 O ATOM 2875 OD2 ASP A 132 41.685 58.598 117.140 1.00 21.11 O ANISOU 2875 OD2 ASP C 132 2753 3344 1923 -25 -207 29 O ATOM 2876 N ALA A 133 37.765 58.286 113.135 1.00 22.93 N ANISOU 2876 N ALA C 133 2829 3123 2758 -79 -29 39 N ATOM 2877 CA ALA A 133 36.584 58.788 112.437 1.00 22.08 C ANISOU 2877 CA ALA C 133 2696 2959 2731 -47 -35 37 C ATOM 2878 C ALA A 133 35.821 57.717 111.653 1.00 21.19 C ANISOU 2878 C ALA C 133 2597 2864 2588 -56 -80 56 C ATOM 2879 O ALA A 133 34.852 58.033 110.962 1.00 20.94 O ANISOU 2879 O ALA C 133 2550 2849 2557 -54 -88 122 O ATOM 2880 CB ALA A 133 36.974 59.949 111.526 1.00 22.46 C ANISOU 2880 CB ALA C 133 2763 2988 2780 -29 -17 7 C ATOM 2881 N GLY A 134 36.228 56.454 111.768 1.00 20.40 N ANISOU 2881 N GLY C 134 2484 2765 2499 -7 -73 67 N ATOM 2882 CA GLY A 134 35.542 55.336 111.137 1.00 20.36 C ANISOU 2882 CA GLY C 134 2546 2748 2441 -35 -32 33 C ATOM 2883 C GLY A 134 36.023 54.985 109.740 1.00 20.64 C ANISOU 2883 C GLY C 134 2604 2767 2470 -7 -13 22 C ATOM 2884 O GLY A 134 35.390 54.165 109.073 1.00 21.00 O ANISOU 2884 O GLY C 134 2678 2954 2345 -74 45 69 O ATOM 2885 N ILE A 135 37.146 55.581 109.319 1.00 21.12 N ANISOU 2885 N ILE C 135 2664 2868 2490 -33 -37 43 N ATOM 2886 CA ILE A 135 37.701 55.385 107.971 1.00 21.39 C ANISOU 2886 CA ILE C 135 2729 2864 2534 -20 -21 6 C ATOM 2887 C ILE A 135 38.936 54.487 108.051 1.00 21.22 C ANISOU 2887 C ILE C 135 2708 2847 2505 -24 -22 57 C ATOM 2888 O ILE A 135 39.960 54.915 108.571 1.00 21.34 O ANISOU 2888 O ILE C 135 2705 2942 2460 -65 -2 90 O ATOM 2889 CB ILE A 135 38.193 56.712 107.358 1.00 21.46 C ANISOU 2889 CB ILE C 135 2721 2897 2535 -22 -12 55 C ATOM 2890 CG1 ILE A 135 37.251 57.895 107.643 1.00 21.91 C ANISOU 2890 CG1 ILE C 135 2844 2915 2565 30 -47 -8 C ATOM 2891 CG2 ILE A 135 38.530 56.501 105.866 1.00 21.72 C ANISOU 2891 CG2 ILE C 135 2728 2986 2537 -121 -28 -89 C ATOM 2892 CD1 ILE A 135 36.227 58.149 106.657 1.00 21.80 C ANISOU 2892 CD1 ILE C 135 2681 2833 2769 -86 29 -61 C ATOM 2893 N SER A 136 38.859 53.274 107.513 1.00 21.15 N ANISOU 2893 N SER C 136 2707 2843 2484 -95 -9 47 N ATOM 2894 CA SER A 136 39.954 52.307 107.669 1.00 20.90 C ANISOU 2894 CA SER C 136 2675 2804 2459 -88 -38 37 C ATOM 2895 C SER A 136 40.479 51.721 106.356 1.00 20.18 C ANISOU 2895 C SER C 136 2623 2690 2352 -119 -23 43 C ATOM 2896 O SER A 136 40.965 50.591 106.336 1.00 19.85 O ANISOU 2896 O SER C 136 2669 2682 2190 -106 12 55 O ATOM 2897 CB SER A 136 39.532 51.182 108.623 1.00 21.14 C ANISOU 2897 CB SER C 136 2700 2801 2529 -85 0 78 C ATOM 2898 OG SER A 136 38.387 50.492 108.159 1.00 21.14 O ANISOU 2898 OG SER C 136 2732 2989 2308 -82 -189 144 O ATOM 2899 N GLN A 137 40.345 52.476 105.265 1.00 18.72 N ANISOU 2899 N GLN C 137 2405 2533 2174 -95 -73 55 N ATOM 2900 CA GLN A 137 41.002 52.139 103.997 1.00 17.41 C ANISOU 2900 CA GLN C 137 2217 2383 2012 -77 -41 16 C ATOM 2901 C GLN A 137 41.885 53.296 103.555 1.00 16.87 C ANISOU 2901 C GLN C 137 2163 2372 1873 -88 -49 37 C ATOM 2902 O GLN A 137 41.523 54.468 103.718 1.00 16.00 O ANISOU 2902 O GLN C 137 2052 2495 1531 -156 -78 -10 O ATOM 2903 CB GLN A 137 39.971 51.873 102.899 1.00 16.51 C ANISOU 2903 CB GLN C 137 2067 2285 1920 -52 -43 31 C ATOM 2904 CG GLN A 137 39.173 50.597 103.054 1.00 17.60 C ANISOU 2904 CG GLN C 137 2269 2380 2036 -38 25 -21 C ATOM 2905 CD GLN A 137 38.630 50.116 101.729 1.00 17.88 C ANISOU 2905 CD GLN C 137 2260 2515 2017 -22 126 114 C ATOM 2906 OE1 GLN A 137 39.377 49.964 100.773 1.00 18.69 O ANISOU 2906 OE1 GLN C 137 2318 2625 2158 -213 168 158 O ATOM 2907 NE2 GLN A 137 37.333 49.891 101.665 1.00 19.64 N ANISOU 2907 NE2 GLN C 137 2482 2856 2124 -51 61 159 N ATOM 2908 N ALA A 138 43.052 52.981 102.984 1.00 16.90 N ANISOU 2908 N ALA C 138 2177 2335 1909 -87 -50 54 N ATOM 2909 CA ALA A 138 43.920 54.035 102.448 1.00 16.72 C ANISOU 2909 CA ALA C 138 2169 2265 1917 -54 -40 28 C ATOM 2910 C ALA A 138 44.581 53.539 101.174 1.00 16.27 C ANISOU 2910 C ALA C 138 2114 2203 1862 -89 -48 2 C ATOM 2911 O ALA A 138 44.772 52.329 101.009 1.00 16.35 O ANISOU 2911 O ALA C 138 2185 2242 1782 -91 -17 93 O ATOM 2912 CB ALA A 138 44.965 54.439 103.426 1.00 17.12 C ANISOU 2912 CB ALA C 138 2218 2328 1957 -62 -73 -23 C ATOM 2913 N ILE A 139 44.907 54.482 100.285 1.00 15.51 N ANISOU 2913 N ILE C 139 2001 2070 1820 -120 -79 11 N ATOM 2914 CA ILE A 139 45.471 54.162 98.967 1.00 15.69 C ANISOU 2914 CA ILE C 139 1984 2146 1829 -84 -23 -5 C ATOM 2915 C ILE A 139 46.897 54.724 98.885 1.00 15.10 C ANISOU 2915 C ILE C 139 1931 2053 1751 -78 -2 3 C ATOM 2916 O ILE A 139 47.104 55.931 98.963 1.00 13.73 O ANISOU 2916 O ILE C 139 1806 1887 1521 -180 46 -7 O ATOM 2917 CB ILE A 139 44.636 54.766 97.793 1.00 15.49 C ANISOU 2917 CB ILE C 139 1970 2177 1737 -105 -43 -27 C ATOM 2918 CG1 ILE A 139 43.111 54.580 97.963 1.00 16.42 C ANISOU 2918 CG1 ILE C 139 2067 2303 1865 12 -54 -55 C ATOM 2919 CG2 ILE A 139 45.138 54.216 96.455 1.00 14.92 C ANISOU 2919 CG2 ILE C 139 1877 2186 1605 -201 -21 -42 C ATOM 2920 CD1 ILE A 139 42.622 53.153 98.090 1.00 17.66 C ANISOU 2920 CD1 ILE C 139 2301 2404 2002 54 -3 -153 C ATOM 2921 N TYR A 140 47.868 53.829 98.728 1.00 15.45 N ANISOU 2921 N TYR C 140 1974 2032 1864 -101 24 -39 N ATOM 2922 CA TYR A 140 49.281 54.179 98.762 1.00 15.33 C ANISOU 2922 CA TYR C 140 1939 2058 1825 -103 16 3 C ATOM 2923 C TYR A 140 49.905 54.009 97.393 1.00 15.20 C ANISOU 2923 C TYR C 140 1836 2081 1858 -118 55 14 C ATOM 2924 O TYR A 140 49.800 52.937 96.781 1.00 15.41 O ANISOU 2924 O TYR C 140 1895 2115 1845 -150 31 72 O ATOM 2925 CB TYR A 140 50.033 53.296 99.771 1.00 15.74 C ANISOU 2925 CB TYR C 140 2005 2040 1935 -108 30 -12 C ATOM 2926 CG TYR A 140 51.442 53.785 99.989 1.00 17.08 C ANISOU 2926 CG TYR C 140 2074 2269 2146 -91 56 -38 C ATOM 2927 CD1 TYR A 140 51.734 54.682 101.005 1.00 18.67 C ANISOU 2927 CD1 TYR C 140 2246 2416 2430 -120 61 -133 C ATOM 2928 CD2 TYR A 140 52.477 53.404 99.136 1.00 17.34 C ANISOU 2928 CD2 TYR C 140 2070 2262 2253 -75 31 -64 C ATOM 2929 CE1 TYR A 140 53.008 55.154 101.194 1.00 18.82 C ANISOU 2929 CE1 TYR C 140 2126 2554 2470 -130 22 -75 C ATOM 2930 CE2 TYR A 140 53.769 53.873 99.321 1.00 17.51 C ANISOU 2930 CE2 TYR C 140 2132 2289 2229 -73 113 -98 C ATOM 2931 CZ TYR A 140 54.024 54.740 100.348 1.00 19.08 C ANISOU 2931 CZ TYR C 140 2274 2574 2400 -44 57 -120 C ATOM 2932 OH TYR A 140 55.299 55.204 100.528 1.00 20.40 O ANISOU 2932 OH TYR C 140 2182 2883 2684 -165 170 -250 O ATOM 2933 N HIS A 141 50.546 55.071 96.937 1.00 14.86 N ANISOU 2933 N HIS C 141 1790 2065 1789 -129 52 15 N ATOM 2934 CA HIS A 141 51.132 55.146 95.604 1.00 15.47 C ANISOU 2934 CA HIS C 141 1818 2127 1931 -83 1 -34 C ATOM 2935 C HIS A 141 52.627 54.956 95.655 1.00 15.54 C ANISOU 2935 C HIS C 141 1842 2093 1967 -145 3 -71 C ATOM 2936 O HIS A 141 53.307 55.537 96.506 1.00 15.60 O ANISOU 2936 O HIS C 141 1763 2112 2050 -182 -40 -98 O ATOM 2937 CB HIS A 141 50.856 56.515 94.999 1.00 15.41 C ANISOU 2937 CB HIS C 141 1797 2097 1961 -88 57 -25 C ATOM 2938 CG HIS A 141 49.413 56.754 94.685 1.00 15.80 C ANISOU 2938 CG HIS C 141 1846 2186 1969 -99 -15 -17 C ATOM 2939 ND1 HIS A 141 48.473 57.056 95.646 1.00 17.29 N ANISOU 2939 ND1 HIS C 141 1982 2357 2227 -297 78 -72 N ATOM 2940 CD2 HIS A 141 48.749 56.718 93.508 1.00 14.55 C ANISOU 2940 CD2 HIS C 141 1700 2102 1726 -205 73 -170 C ATOM 2941 CE1 HIS A 141 47.292 57.207 95.065 1.00 14.09 C ANISOU 2941 CE1 HIS C 141 1595 2181 1575 -78 36 -167 C ATOM 2942 NE2 HIS A 141 47.434 56.999 93.773 1.00 16.76 N ANISOU 2942 NE2 HIS C 141 1955 2319 2093 -44 69 -103 N ATOM 2943 N GLN A 142 53.151 54.151 94.726 1.00 16.02 N ANISOU 2943 N GLN C 142 1934 2194 1956 -126 -34 -81 N ATOM 2944 CA GLN A 142 54.609 54.039 94.611 1.00 16.72 C ANISOU 2944 CA GLN C 142 2017 2264 2070 -101 8 -68 C ATOM 2945 C GLN A 142 55.251 55.430 94.507 1.00 17.42 C ANISOU 2945 C GLN C 142 2160 2301 2157 -96 13 -89 C ATOM 2946 O GLN A 142 54.753 56.294 93.781 1.00 16.99 O ANISOU 2946 O GLN C 142 2045 2239 2170 -127 36 -121 O ATOM 2947 CB GLN A 142 54.984 53.210 93.377 1.00 16.38 C ANISOU 2947 CB GLN C 142 1997 2214 2013 -90 13 -90 C ATOM 2948 CG GLN A 142 56.459 52.828 93.334 1.00 17.81 C ANISOU 2948 CG GLN C 142 2195 2394 2177 -143 -13 -120 C ATOM 2949 CD GLN A 142 56.861 52.108 92.058 1.00 20.86 C ANISOU 2949 CD GLN C 142 2658 2838 2427 -132 -61 -127 C ATOM 2950 OE1 GLN A 142 56.354 52.390 90.972 1.00 22.22 O ANISOU 2950 OE1 GLN C 142 2887 3047 2507 -196 -37 -102 O ATOM 2951 NE2 GLN A 142 57.794 51.202 92.184 1.00 22.41 N ANISOU 2951 NE2 GLN C 142 2884 2922 2709 -256 80 -108 N ATOM 2952 N SER A 143 56.365 55.646 95.216 1.00 19.14 N ANISOU 2952 N SER C 143 2370 2568 2331 -105 50 -109 N ATOM 2953 CA SER A 143 57.154 56.871 95.066 1.00 21.80 C ANISOU 2953 CA SER C 143 2713 2895 2673 -37 37 -70 C ATOM 2954 C SER A 143 57.699 57.034 93.657 1.00 23.39 C ANISOU 2954 C SER C 143 2926 3061 2899 -7 6 -66 C ATOM 2955 O SER A 143 58.166 56.069 93.071 1.00 23.90 O ANISOU 2955 O SER C 143 2986 3205 2890 -6 -56 -131 O ATOM 2956 CB SER A 143 58.332 56.879 96.047 1.00 21.92 C ANISOU 2956 CB SER C 143 2666 2922 2740 -60 75 -55 C ATOM 2957 OG SER A 143 57.854 56.929 97.375 1.00 23.03 O ANISOU 2957 OG SER C 143 2811 3232 2705 -140 160 -24 O ATOM 2958 N ARG A 144 57.668 58.262 93.150 1.00 25.21 N ANISOU 2958 N ARG C 144 3209 3222 3147 21 1 -19 N ATOM 2959 CA ARG A 144 58.008 58.568 91.752 1.00 26.88 C ANISOU 2959 CA ARG C 144 3422 3406 3384 20 24 -8 C ATOM 2960 C ARG A 144 59.396 59.185 91.605 1.00 27.37 C ANISOU 2960 C ARG C 144 3514 3420 3465 40 21 10 C ATOM 2961 O ARG A 144 59.652 60.274 92.113 1.00 27.62 O ANISOU 2961 O ARG C 144 3578 3407 3507 85 39 0 O ATOM 2962 CB ARG A 144 56.941 59.508 91.153 1.00 27.27 C ANISOU 2962 CB ARG C 144 3499 3421 3440 6 32 16 C ATOM 2963 CG ARG A 144 55.581 58.835 90.961 1.00 28.40 C ANISOU 2963 CG ARG C 144 3562 3642 3586 -29 0 26 C ATOM 2964 CD ARG A 144 54.495 59.745 90.399 1.00 28.92 C ANISOU 2964 CD ARG C 144 3560 3679 3747 -39 -57 48 C ATOM 2965 NE ARG A 144 53.173 59.157 90.635 1.00 29.22 N ANISOU 2965 NE ARG C 144 3567 3736 3799 -69 23 -68 N ATOM 2966 CZ ARG A 144 52.013 59.745 90.358 1.00 27.47 C ANISOU 2966 CZ ARG C 144 3431 3494 3511 24 87 -58 C ATOM 2967 NH1 ARG A 144 51.992 60.956 89.801 1.00 27.68 N ANISOU 2967 NH1 ARG C 144 3489 3500 3527 5 37 -31 N ATOM 2968 NH2 ARG A 144 50.865 59.118 90.654 1.00 25.13 N ANISOU 2968 NH2 ARG C 144 3211 3199 3138 -97 55 -179 N ATOM 2969 N GLU A 151 63.795 51.812 94.429 1.00 38.70 N ANISOU 2969 N GLU C 151 4938 4879 4886 -13 16 -47 N ATOM 2970 CA GLU A 151 63.120 50.634 93.920 1.00 38.45 C ANISOU 2970 CA GLU C 151 4884 4863 4859 -33 13 -12 C ATOM 2971 C GLU A 151 62.338 50.922 92.644 1.00 37.81 C ANISOU 2971 C GLU C 151 4828 4775 4760 -14 12 3 C ATOM 2972 O GLU A 151 62.105 52.067 92.286 1.00 38.34 O ANISOU 2972 O GLU C 151 4908 4814 4844 -32 22 30 O ATOM 2973 N THR A 152 61.918 49.868 91.970 1.00 36.57 N ANISOU 2973 N THR C 152 4627 4638 4630 -15 -7 12 N ATOM 2974 CA THR A 152 60.550 49.403 92.055 1.00 35.11 C ANISOU 2974 CA THR C 152 4433 4466 4442 -28 -5 12 C ATOM 2975 C THR A 152 60.213 48.916 93.457 1.00 33.11 C ANISOU 2975 C THR C 152 4147 4224 4208 -44 -16 -9 C ATOM 2976 O THR A 152 60.773 47.946 93.931 1.00 33.18 O ANISOU 2976 O THR C 152 4171 4229 4204 -37 -24 23 O ATOM 2977 CB THR A 152 60.318 48.300 91.038 1.00 35.45 C ANISOU 2977 CB THR C 152 4474 4516 4477 -38 -11 -7 C ATOM 2978 OG1 THR A 152 60.812 48.734 89.768 1.00 36.75 O ANISOU 2978 OG1 THR C 152 4630 4713 4620 -63 -21 25 O ATOM 2979 CG2 THR A 152 58.846 47.961 90.930 1.00 35.81 C ANISOU 2979 CG2 THR C 152 4559 4557 4488 -15 -20 -24 C ATOM 2980 N TRP A 153 59.296 49.610 94.114 1.00 30.85 N ANISOU 2980 N TRP C 153 3859 3954 3909 -50 10 14 N ATOM 2981 CA TRP A 153 58.787 49.200 95.410 1.00 28.57 C ANISOU 2981 CA TRP C 153 3572 3686 3595 -63 27 -5 C ATOM 2982 C TRP A 153 59.872 48.840 96.404 1.00 28.52 C ANISOU 2982 C TRP C 153 3546 3690 3599 -61 40 -7 C ATOM 2983 O TRP A 153 59.910 47.734 96.921 1.00 28.33 O ANISOU 2983 O TRP C 153 3493 3704 3565 -64 104 -18 O ATOM 2984 CB TRP A 153 57.723 48.101 95.302 1.00 27.86 C ANISOU 2984 CB TRP C 153 3484 3618 3481 -91 11 3 C ATOM 2985 CG TRP A 153 56.425 48.640 94.786 1.00 25.39 C ANISOU 2985 CG TRP C 153 3163 3395 3088 -89 -26 -45 C ATOM 2986 CD1 TRP A 153 55.947 48.544 93.521 1.00 24.71 C ANISOU 2986 CD1 TRP C 153 2914 3375 3098 -142 -21 -74 C ATOM 2987 CD2 TRP A 153 55.460 49.401 95.517 1.00 23.90 C ANISOU 2987 CD2 TRP C 153 2973 3254 2851 -145 11 -50 C ATOM 2988 NE1 TRP A 153 54.755 49.193 93.412 1.00 23.91 N ANISOU 2988 NE1 TRP C 153 2911 3190 2980 -182 -3 -87 N ATOM 2989 CE2 TRP A 153 54.420 49.710 94.633 1.00 22.92 C ANISOU 2989 CE2 TRP C 153 2834 3072 2801 -165 -32 -37 C ATOM 2990 CE3 TRP A 153 55.366 49.834 96.843 1.00 22.65 C ANISOU 2990 CE3 TRP C 153 2761 3055 2789 -148 47 -55 C ATOM 2991 CZ2 TRP A 153 53.310 50.448 95.023 1.00 21.11 C ANISOU 2991 CZ2 TRP C 153 2578 2875 2567 -132 -21 -22 C ATOM 2992 CZ3 TRP A 153 54.265 50.556 97.222 1.00 20.51 C ANISOU 2992 CZ3 TRP C 153 2694 2613 2484 -31 9 -143 C ATOM 2993 CH2 TRP A 153 53.254 50.854 96.321 1.00 19.97 C ANISOU 2993 CH2 TRP C 153 2508 2504 2574 -167 29 -51 C ATOM 2994 N GLY A 154 60.744 49.795 96.677 1.00 28.53 N ANISOU 2994 N GLY C 154 3552 3688 3600 -66 45 -16 N ATOM 2995 CA GLY A 154 61.752 49.618 97.698 1.00 28.93 C ANISOU 2995 CA GLY C 154 3622 3739 3628 -34 62 -2 C ATOM 2996 C GLY A 154 61.248 49.689 99.121 1.00 28.74 C ANISOU 2996 C GLY C 154 3595 3718 3607 -22 53 12 C ATOM 2997 O GLY A 154 60.058 49.748 99.370 1.00 28.45 O ANISOU 2997 O GLY C 154 3562 3706 3540 -65 102 32 O ATOM 2998 N GLU A 155 62.178 49.667 100.069 1.00 28.56 N ANISOU 2998 N GLU C 155 3558 3692 3599 -8 71 12 N ATOM 2999 CA GLU A 155 61.834 49.451 101.465 1.00 28.58 C ANISOU 2999 CA GLU C 155 3535 3704 3619 -37 89 -19 C ATOM 3000 C GLU A 155 61.176 50.682 102.098 1.00 27.24 C ANISOU 3000 C GLU C 155 3334 3581 3434 -33 121 -26 C ATOM 3001 O GLU A 155 60.355 50.565 102.985 1.00 26.66 O ANISOU 3001 O GLU C 155 3156 3583 3389 -66 167 -54 O ATOM 3002 CB GLU A 155 63.073 48.993 102.257 1.00 28.98 C ANISOU 3002 CB GLU C 155 3586 3746 3678 -40 98 2 C ATOM 3003 CG GLU A 155 63.614 47.654 101.783 1.00 31.77 C ANISOU 3003 CG GLU C 155 3966 4057 4046 -34 46 -18 C ATOM 3004 CD GLU A 155 62.784 46.497 102.250 1.00 33.98 C ANISOU 3004 CD GLU C 155 4364 4225 4320 -8 16 -4 C ATOM 3005 OE1 GLU A 155 62.381 46.511 103.413 1.00 35.28 O ANISOU 3005 OE1 GLU C 155 4527 4357 4520 -51 6 -14 O ATOM 3006 OE2 GLU A 155 62.530 45.573 101.453 1.00 35.26 O ANISOU 3006 OE2 GLU C 155 4533 4405 4458 7 39 -25 O ATOM 3007 N LYS A 156 61.549 51.853 101.613 1.00 26.55 N ANISOU 3007 N LYS C 156 3211 3510 3363 -32 97 -49 N ATOM 3008 CA LYS A 156 60.893 53.087 102.000 1.00 26.23 C ANISOU 3008 CA LYS C 156 3184 3463 3318 -40 67 -31 C ATOM 3009 C LYS A 156 59.367 52.969 101.889 1.00 26.11 C ANISOU 3009 C LYS C 156 3167 3483 3267 -46 40 -37 C ATOM 3010 O LYS A 156 58.654 53.326 102.809 1.00 26.75 O ANISOU 3010 O LYS C 156 3228 3644 3290 -129 59 -51 O ATOM 3011 CB LYS A 156 61.389 54.216 101.167 1.00 26.12 C ANISOU 3011 CB LYS C 156 3161 3422 3341 -39 59 -50 C ATOM 3012 N ASP A 157 58.892 52.483 100.751 1.00 24.82 N ANISOU 3012 N ASP C 157 2996 3304 3128 -19 45 -37 N ATOM 3013 CA ASP A 157 57.463 52.434 100.466 1.00 23.79 C ANISOU 3013 CA ASP C 157 2887 3177 2972 -24 47 -11 C ATOM 3014 C ASP A 157 56.812 51.269 101.206 1.00 23.57 C ANISOU 3014 C ASP C 157 2898 3175 2880 -38 67 -6 C ATOM 3015 O ASP A 157 55.750 51.400 101.774 1.00 23.48 O ANISOU 3015 O ASP C 157 2876 3239 2806 -89 42 18 O ATOM 3016 CB ASP A 157 57.234 52.263 98.960 1.00 23.37 C ANISOU 3016 CB ASP C 157 2762 3171 2945 -20 54 -6 C ATOM 3017 CG ASP A 157 57.319 53.581 98.184 1.00 22.37 C ANISOU 3017 CG ASP C 157 2460 3151 2885 -55 68 -11 C ATOM 3018 OD1 ASP A 157 57.142 54.650 98.772 1.00 21.48 O ANISOU 3018 OD1 ASP C 157 1957 3305 2897 -175 129 -66 O ATOM 3019 OD2 ASP A 157 57.574 53.539 96.980 1.00 22.61 O ANISOU 3019 OD2 ASP C 157 2352 3395 2841 -265 138 16 O ATOM 3020 N LEU A 158 57.468 50.121 101.169 1.00 23.51 N ANISOU 3020 N LEU C 158 2937 3123 2870 -8 66 -35 N ATOM 3021 CA LEU A 158 56.909 48.915 101.744 1.00 23.68 C ANISOU 3021 CA LEU C 158 2955 3114 2927 -11 63 -40 C ATOM 3022 C LEU A 158 56.750 49.063 103.247 1.00 23.46 C ANISOU 3022 C LEU C 158 2946 3068 2898 -14 52 -3 C ATOM 3023 O LEU A 158 55.782 48.604 103.835 1.00 22.80 O ANISOU 3023 O LEU C 158 2893 2975 2792 -37 84 -43 O ATOM 3024 CB LEU A 158 57.767 47.714 101.391 1.00 23.99 C ANISOU 3024 CB LEU C 158 2978 3138 2996 -36 77 -36 C ATOM 3025 CG LEU A 158 57.726 47.292 99.925 1.00 24.80 C ANISOU 3025 CG LEU C 158 3032 3238 3151 -23 26 -51 C ATOM 3026 CD1 LEU A 158 58.848 46.307 99.615 1.00 24.81 C ANISOU 3026 CD1 LEU C 158 3073 3245 3107 -145 49 -80 C ATOM 3027 CD2 LEU A 158 56.362 46.698 99.572 1.00 23.95 C ANISOU 3027 CD2 LEU C 158 2979 3035 3082 -46 71 -85 C ATOM 3028 N ASN A 159 57.701 49.751 103.856 1.00 23.62 N ANISOU 3028 N ASN C 159 2969 3065 2939 -28 46 7 N ATOM 3029 CA ASN A 159 57.645 49.946 105.286 1.00 24.09 C ANISOU 3029 CA ASN C 159 3050 3096 3006 -65 23 -4 C ATOM 3030 C ASN A 159 56.434 50.784 105.671 1.00 23.86 C ANISOU 3030 C ASN C 159 3026 3038 3000 -95 31 0 C ATOM 3031 O ASN A 159 55.751 50.484 106.623 1.00 23.43 O ANISOU 3031 O ASN C 159 2938 3022 2941 -177 70 -7 O ATOM 3032 CB ASN A 159 58.936 50.560 105.819 1.00 24.47 C ANISOU 3032 CB ASN C 159 3084 3168 3045 -50 14 -4 C ATOM 3033 CG ASN A 159 60.068 49.548 105.939 1.00 25.74 C ANISOU 3033 CG ASN C 159 3269 3346 3163 -56 71 12 C ATOM 3034 OD1 ASN A 159 61.227 49.903 105.851 1.00 28.05 O ANISOU 3034 OD1 ASN C 159 3429 3766 3461 -80 148 17 O ATOM 3035 ND2 ASN A 159 59.726 48.293 106.142 1.00 26.03 N ANISOU 3035 ND2 ASN C 159 3201 3473 3214 -88 154 91 N ATOM 3036 N LYS A 160 56.162 51.810 104.879 1.00 24.04 N ANISOU 3036 N LYS C 160 3054 3071 3009 -111 37 -23 N ATOM 3037 CA LYS A 160 54.961 52.622 105.066 1.00 23.88 C ANISOU 3037 CA LYS C 160 2998 3054 3019 -73 27 -19 C ATOM 3038 C LYS A 160 53.671 51.807 104.897 1.00 23.24 C ANISOU 3038 C LYS C 160 2901 3042 2886 -86 34 4 C ATOM 3039 O LYS A 160 52.767 51.909 105.705 1.00 22.98 O ANISOU 3039 O LYS C 160 2811 3053 2866 -114 56 38 O ATOM 3040 CB LYS A 160 55.014 53.840 104.142 1.00 24.34 C ANISOU 3040 CB LYS C 160 3045 3158 3043 -83 25 -18 C ATOM 3041 CG LYS A 160 55.882 54.955 104.712 1.00 25.28 C ANISOU 3041 CG LYS C 160 3155 3174 3277 -25 5 -51 C ATOM 3042 CD LYS A 160 56.462 55.861 103.630 1.00 26.94 C ANISOU 3042 CD LYS C 160 3514 3394 3327 -67 -11 -38 C ATOM 3043 CE LYS A 160 56.427 57.338 104.066 1.00 27.56 C ANISOU 3043 CE LYS C 160 3606 3499 3366 -43 -14 -65 C ATOM 3044 NZ LYS A 160 57.223 58.238 103.189 1.00 26.97 N ANISOU 3044 NZ LYS C 160 3420 3463 3363 62 -60 -180 N ATOM 3045 N VAL A 161 53.617 50.965 103.868 1.00 22.48 N ANISOU 3045 N VAL C 161 2814 2875 2851 -88 47 12 N ATOM 3046 CA VAL A 161 52.473 50.090 103.652 1.00 22.06 C ANISOU 3046 CA VAL C 161 2769 2831 2782 -82 34 1 C ATOM 3047 C VAL A 161 52.281 49.149 104.850 1.00 22.62 C ANISOU 3047 C VAL C 161 2831 2927 2836 -89 54 15 C ATOM 3048 O VAL A 161 51.162 48.976 105.345 1.00 22.51 O ANISOU 3048 O VAL C 161 2841 2942 2770 -142 61 40 O ATOM 3049 CB VAL A 161 52.585 49.321 102.296 1.00 21.60 C ANISOU 3049 CB VAL C 161 2694 2780 2731 -79 -7 0 C ATOM 3050 CG1 VAL A 161 51.526 48.258 102.164 1.00 21.29 C ANISOU 3050 CG1 VAL C 161 2787 2664 2635 -73 -5 -41 C ATOM 3051 CG2 VAL A 161 52.457 50.278 101.125 1.00 21.25 C ANISOU 3051 CG2 VAL C 161 2709 2669 2693 -50 32 -33 C ATOM 3052 N LYS A 162 53.379 48.562 105.335 1.00 23.47 N ANISOU 3052 N LYS C 162 2901 3086 2931 -109 60 36 N ATOM 3053 CA LYS A 162 53.323 47.630 106.471 1.00 23.63 C ANISOU 3053 CA LYS C 162 2941 3098 2939 -88 65 67 C ATOM 3054 C LYS A 162 52.832 48.315 107.757 1.00 23.71 C ANISOU 3054 C LYS C 162 2944 3167 2895 -84 126 96 C ATOM 3055 O LYS A 162 52.013 47.763 108.487 1.00 23.85 O ANISOU 3055 O LYS C 162 2983 3251 2827 -66 193 174 O ATOM 3056 CB LYS A 162 54.688 46.946 106.695 1.00 23.81 C ANISOU 3056 CB LYS C 162 2919 3158 2967 -106 77 74 C ATOM 3057 CG LYS A 162 54.931 45.750 105.754 1.00 24.11 C ANISOU 3057 CG LYS C 162 2991 3153 3014 -66 70 90 C ATOM 3058 CD LYS A 162 56.279 45.039 105.983 1.00 26.10 C ANISOU 3058 CD LYS C 162 3144 3340 3432 -43 -51 60 C ATOM 3059 CE LYS A 162 57.411 45.706 105.208 1.00 27.47 C ANISOU 3059 CE LYS C 162 3412 3503 3521 -93 -53 113 C ATOM 3060 NZ LYS A 162 58.555 44.751 104.943 1.00 27.96 N ANISOU 3060 NZ LYS C 162 3367 3755 3502 -101 -83 43 N ATOM 3061 N LYS A 163 53.317 49.526 107.999 1.00 23.77 N ANISOU 3061 N LYS C 163 2972 3131 2925 -75 122 77 N ATOM 3062 CA LYS A 163 52.892 50.326 109.141 1.00 24.69 C ANISOU 3062 CA LYS C 163 3093 3227 3060 -45 72 36 C ATOM 3063 C LYS A 163 51.399 50.657 109.093 1.00 24.03 C ANISOU 3063 C LYS C 163 3014 3162 2952 -51 58 44 C ATOM 3064 O LYS A 163 50.709 50.597 110.113 1.00 24.05 O ANISOU 3064 O LYS C 163 2988 3205 2943 -103 108 54 O ATOM 3065 CB LYS A 163 53.714 51.607 109.206 1.00 25.33 C ANISOU 3065 CB LYS C 163 3200 3276 3146 0 45 46 C ATOM 3066 CG LYS A 163 53.578 52.378 110.500 1.00 28.51 C ANISOU 3066 CG LYS C 163 3645 3608 3577 22 9 -15 C ATOM 3067 CD LYS A 163 54.950 52.859 110.981 1.00 32.03 C ANISOU 3067 CD LYS C 163 4040 4071 4056 58 99 -40 C ATOM 3068 CE LYS A 163 54.827 53.856 112.132 1.00 34.85 C ANISOU 3068 CE LYS C 163 4401 4409 4429 -13 62 -64 C ATOM 3069 NZ LYS A 163 56.179 54.217 112.698 1.00 36.03 N ANISOU 3069 NZ LYS C 163 4475 4571 4641 49 169 -48 N ATOM 3070 N LEU A 164 50.896 51.010 107.913 1.00 23.30 N ANISOU 3070 N LEU C 164 2923 3105 2823 -45 55 11 N ATOM 3071 CA LEU A 164 49.469 51.326 107.786 1.00 22.90 C ANISOU 3071 CA LEU C 164 2910 3035 2755 -46 63 24 C ATOM 3072 C LEU A 164 48.636 50.080 108.048 1.00 22.87 C ANISOU 3072 C LEU C 164 2906 3081 2702 -54 95 19 C ATOM 3073 O LEU A 164 47.591 50.166 108.679 1.00 22.97 O ANISOU 3073 O LEU C 164 2988 3176 2564 -30 86 51 O ATOM 3074 CB LEU A 164 49.145 51.937 106.419 1.00 22.60 C ANISOU 3074 CB LEU C 164 2851 2982 2751 -74 58 -5 C ATOM 3075 CG LEU A 164 49.664 53.364 106.178 1.00 22.53 C ANISOU 3075 CG LEU C 164 2797 2992 2772 -26 24 27 C ATOM 3076 CD1 LEU A 164 49.630 53.717 104.694 1.00 23.50 C ANISOU 3076 CD1 LEU C 164 2903 3187 2837 -7 55 -17 C ATOM 3077 CD2 LEU A 164 48.903 54.415 107.003 1.00 22.69 C ANISOU 3077 CD2 LEU C 164 2966 3021 2634 -36 121 2 C ATOM 3078 N ILE A 165 49.112 48.923 107.587 1.00 22.72 N ANISOU 3078 N ILE C 165 2943 2981 2707 -60 111 50 N ATOM 3079 CA ILE A 165 48.427 47.667 107.861 1.00 23.38 C ANISOU 3079 CA ILE C 165 2987 3035 2861 -37 64 0 C ATOM 3080 C ILE A 165 48.392 47.402 109.383 1.00 23.32 C ANISOU 3080 C ILE C 165 3003 2989 2867 -36 67 32 C ATOM 3081 O ILE A 165 47.341 47.088 109.948 1.00 23.84 O ANISOU 3081 O ILE C 165 3056 3107 2893 -85 99 -1 O ATOM 3082 CB ILE A 165 49.074 46.492 107.069 1.00 23.60 C ANISOU 3082 CB ILE C 165 3035 3060 2868 -45 66 16 C ATOM 3083 CG1 ILE A 165 48.849 46.687 105.554 1.00 24.10 C ANISOU 3083 CG1 ILE C 165 3067 3156 2933 -22 30 23 C ATOM 3084 CG2 ILE A 165 48.506 45.143 107.514 1.00 23.98 C ANISOU 3084 CG2 ILE C 165 3029 3076 3007 40 48 6 C ATOM 3085 CD1 ILE A 165 49.805 45.902 104.669 1.00 23.65 C ANISOU 3085 CD1 ILE C 165 2993 3164 2827 -85 17 88 C ATOM 3086 N GLU A 166 49.531 47.553 110.047 1.00 23.86 N ANISOU 3086 N GLU C 166 3047 3058 2960 -15 23 21 N ATOM 3087 CA GLU A 166 49.603 47.333 111.497 1.00 23.75 C ANISOU 3087 CA GLU C 166 3028 3055 2938 -26 20 29 C ATOM 3088 C GLU A 166 48.661 48.262 112.285 1.00 23.78 C ANISOU 3088 C GLU C 166 3037 3067 2931 -38 11 18 C ATOM 3089 O GLU A 166 48.097 47.841 113.295 1.00 23.75 O ANISOU 3089 O GLU C 166 3054 3081 2889 -111 -2 57 O ATOM 3090 CB GLU A 166 51.056 47.471 111.994 1.00 23.79 C ANISOU 3090 CB GLU C 166 3028 3029 2978 -32 45 47 C ATOM 3091 N MET A 167 48.479 49.501 111.812 1.00 23.57 N ANISOU 3091 N MET C 167 3030 3058 2867 -61 20 -9 N ATOM 3092 CA MET A 167 47.583 50.484 112.452 1.00 23.74 C ANISOU 3092 CA MET C 167 3040 3090 2889 -51 15 -19 C ATOM 3093 C MET A 167 46.103 50.113 112.358 1.00 23.60 C ANISOU 3093 C MET C 167 3048 3074 2844 -64 0 -3 C ATOM 3094 O MET A 167 45.285 50.596 113.156 1.00 24.24 O ANISOU 3094 O MET C 167 3149 3218 2842 -119 10 7 O ATOM 3095 CB MET A 167 47.788 51.874 111.849 1.00 23.64 C ANISOU 3095 CB MET C 167 3033 3035 2914 -49 20 -60 C ATOM 3096 CG MET A 167 49.041 52.563 112.306 1.00 24.91 C ANISOU 3096 CG MET C 167 3219 3298 2946 -115 36 -101 C ATOM 3097 SD MET A 167 49.298 54.202 111.584 1.00 25.50 S ANISOU 3097 SD MET C 167 3547 3440 2702 -338 78 -46 S ATOM 3098 CE MET A 167 48.137 55.235 112.500 1.00 24.86 C ANISOU 3098 CE MET C 167 3399 3352 2693 -282 119 -15 C ATOM 3099 N GLY A 168 45.757 49.279 111.382 1.00 22.71 N ANISOU 3099 N GLY C 168 2930 2980 2716 -21 3 23 N ATOM 3100 CA GLY A 168 44.394 48.800 111.202 1.00 21.53 C ANISOU 3100 CA GLY C 168 2818 2819 2544 -47 45 58 C ATOM 3101 C GLY A 168 43.779 49.151 109.854 1.00 20.82 C ANISOU 3101 C GLY C 168 2715 2721 2473 -44 48 54 C ATOM 3102 O GLY A 168 42.582 48.972 109.660 1.00 20.68 O ANISOU 3102 O GLY C 168 2777 2731 2349 -77 40 97 O ATOM 3103 N PHE A 169 44.597 49.660 108.938 1.00 20.29 N ANISOU 3103 N PHE C 169 2616 2704 2389 -89 68 59 N ATOM 3104 CA PHE A 169 44.130 49.993 107.592 1.00 20.06 C ANISOU 3104 CA PHE C 169 2593 2605 2420 -103 75 34 C ATOM 3105 C PHE A 169 44.106 48.780 106.677 1.00 19.90 C ANISOU 3105 C PHE C 169 2572 2574 2414 -61 81 33 C ATOM 3106 O PHE A 169 45.011 47.932 106.713 1.00 20.03 O ANISOU 3106 O PHE C 169 2566 2696 2346 -126 63 65 O ATOM 3107 CB PHE A 169 45.025 51.055 106.948 1.00 19.70 C ANISOU 3107 CB PHE C 169 2517 2596 2370 -92 74 35 C ATOM 3108 CG PHE A 169 44.788 52.452 107.453 1.00 19.68 C ANISOU 3108 CG PHE C 169 2554 2561 2360 -125 86 34 C ATOM 3109 CD1 PHE A 169 43.760 53.227 106.928 1.00 17.59 C ANISOU 3109 CD1 PHE C 169 2167 2517 1997 -122 140 63 C ATOM 3110 CD2 PHE A 169 45.593 52.997 108.445 1.00 18.85 C ANISOU 3110 CD2 PHE C 169 2400 2377 2385 -51 25 -7 C ATOM 3111 CE1 PHE A 169 43.545 54.525 107.386 1.00 18.92 C ANISOU 3111 CE1 PHE C 169 2428 2687 2075 -62 110 57 C ATOM 3112 CE2 PHE A 169 45.379 54.295 108.909 1.00 19.46 C ANISOU 3112 CE2 PHE C 169 2503 2552 2339 -131 18 -18 C ATOM 3113 CZ PHE A 169 44.358 55.059 108.379 1.00 19.88 C ANISOU 3113 CZ PHE C 169 2426 2844 2282 -29 6 7 C ATOM 3114 N ARG A 170 43.071 48.711 105.844 1.00 19.33 N ANISOU 3114 N ARG C 170 2502 2497 2343 -97 91 60 N ATOM 3115 CA ARG A 170 43.070 47.832 104.682 1.00 18.89 C ANISOU 3115 CA ARG C 170 2447 2483 2246 -48 44 32 C ATOM 3116 C ARG A 170 43.698 48.676 103.571 1.00 18.86 C ANISOU 3116 C ARG C 170 2417 2552 2196 -82 21 47 C ATOM 3117 O ARG A 170 43.112 49.672 103.150 1.00 19.08 O ANISOU 3117 O ARG C 170 2469 2681 2099 -158 44 10 O ATOM 3118 CB ARG A 170 41.654 47.403 104.326 1.00 18.66 C ANISOU 3118 CB ARG C 170 2421 2458 2210 -69 21 15 C ATOM 3119 CG ARG A 170 41.164 46.160 105.048 1.00 19.32 C ANISOU 3119 CG ARG C 170 2375 2586 2379 43 42 13 C ATOM 3120 CD ARG A 170 39.644 46.017 105.007 1.00 19.98 C ANISOU 3120 CD ARG C 170 2501 2690 2401 13 -44 79 C ATOM 3121 NE ARG A 170 39.020 47.171 105.631 1.00 20.97 N ANISOU 3121 NE ARG C 170 2709 2857 2401 -44 -118 94 N ATOM 3122 CZ ARG A 170 37.905 47.747 105.215 1.00 20.70 C ANISOU 3122 CZ ARG C 170 2685 2818 2362 -85 -58 63 C ATOM 3123 NH1 ARG A 170 37.229 47.269 104.184 1.00 21.27 N ANISOU 3123 NH1 ARG C 170 2739 2879 2463 -12 -67 39 N ATOM 3124 NH2 ARG A 170 37.465 48.818 105.840 1.00 21.30 N ANISOU 3124 NH2 ARG C 170 2869 2992 2229 -92 -107 84 N ATOM 3125 N VAL A 171 44.909 48.313 103.149 1.00 18.46 N ANISOU 3125 N VAL C 171 2388 2519 2105 -98 26 55 N ATOM 3126 CA VAL A 171 45.726 49.202 102.315 1.00 17.82 C ANISOU 3126 CA VAL C 171 2237 2381 2149 -87 45 20 C ATOM 3127 C VAL A 171 45.672 48.723 100.862 1.00 17.02 C ANISOU 3127 C VAL C 171 2202 2257 2005 -119 48 36 C ATOM 3128 O VAL A 171 45.916 47.550 100.569 1.00 16.56 O ANISOU 3128 O VAL C 171 2143 2224 1925 -258 74 89 O ATOM 3129 CB VAL A 171 47.216 49.292 102.825 1.00 18.14 C ANISOU 3129 CB VAL C 171 2315 2395 2182 -86 36 8 C ATOM 3130 CG1 VAL A 171 48.107 49.946 101.804 1.00 18.66 C ANISOU 3130 CG1 VAL C 171 2305 2380 2403 11 52 14 C ATOM 3131 CG2 VAL A 171 47.276 50.052 104.140 1.00 17.98 C ANISOU 3131 CG2 VAL C 171 2188 2421 2222 -48 121 -2 C ATOM 3132 N SER A 172 45.280 49.631 99.975 1.00 16.27 N ANISOU 3132 N SER C 172 2086 2123 1971 -196 41 19 N ATOM 3133 CA SER A 172 45.412 49.427 98.545 1.00 15.53 C ANISOU 3133 CA SER C 172 2028 2026 1847 -150 100 -19 C ATOM 3134 C SER A 172 46.710 50.045 98.081 1.00 15.80 C ANISOU 3134 C SER C 172 2050 2031 1922 -160 95 -14 C ATOM 3135 O SER A 172 47.108 51.102 98.560 1.00 16.38 O ANISOU 3135 O SER C 172 2090 2176 1955 -213 114 -139 O ATOM 3136 CB SER A 172 44.247 50.093 97.802 1.00 14.76 C ANISOU 3136 CB SER C 172 1972 1902 1732 -158 124 24 C ATOM 3137 OG SER A 172 43.023 49.515 98.192 1.00 15.50 O ANISOU 3137 OG SER C 172 2124 2071 1694 -200 211 -64 O ATOM 3138 N VAL A 173 47.366 49.408 97.122 1.00 15.82 N ANISOU 3138 N VAL C 173 2019 2154 1838 -131 57 3 N ATOM 3139 CA VAL A 173 48.552 49.987 96.519 1.00 15.78 C ANISOU 3139 CA VAL C 173 2007 2089 1898 -89 79 14 C ATOM 3140 C VAL A 173 48.368 50.135 95.008 1.00 15.54 C ANISOU 3140 C VAL C 173 1954 2051 1897 -91 26 24 C ATOM 3141 O VAL A 173 47.622 49.378 94.377 1.00 15.90 O ANISOU 3141 O VAL C 173 2008 2218 1815 -94 30 13 O ATOM 3142 CB VAL A 173 49.852 49.154 96.824 1.00 16.26 C ANISOU 3142 CB VAL C 173 2039 2161 1975 -109 89 42 C ATOM 3143 CG1 VAL A 173 50.141 49.140 98.328 1.00 16.32 C ANISOU 3143 CG1 VAL C 173 2261 2054 1885 -112 90 -3 C ATOM 3144 CG2 VAL A 173 49.775 47.747 96.266 1.00 14.84 C ANISOU 3144 CG2 VAL C 173 1780 2109 1748 -182 157 19 C ATOM 3145 N THR A 174 49.091 51.091 94.458 1.00 15.16 N ANISOU 3145 N THR C 174 1870 2014 1875 -154 9 12 N ATOM 3146 CA THR A 174 49.065 51.390 93.033 1.00 15.70 C ANISOU 3146 CA THR C 174 1965 2095 1902 -147 8 -22 C ATOM 3147 C THR A 174 50.387 51.981 92.574 1.00 15.84 C ANISOU 3147 C THR C 174 1993 2041 1982 -124 15 -27 C ATOM 3148 O THR A 174 51.122 52.580 93.361 1.00 15.35 O ANISOU 3148 O THR C 174 1879 2104 1848 -241 -3 -64 O ATOM 3149 CB THR A 174 47.882 52.320 92.670 1.00 15.57 C ANISOU 3149 CB THR C 174 1969 2074 1872 -110 19 8 C ATOM 3150 OG1 THR A 174 47.676 52.280 91.248 1.00 16.51 O ANISOU 3150 OG1 THR C 174 1929 2517 1825 -166 2 -4 O ATOM 3151 CG2 THR A 174 48.153 53.761 93.083 1.00 15.38 C ANISOU 3151 CG2 THR C 174 1786 2138 1916 -173 38 -39 C ATOM 3152 N GLY A 175 50.671 51.832 91.284 1.00 16.75 N ANISOU 3152 N GLY C 175 2121 2169 2072 -115 40 -43 N ATOM 3153 CA GLY A 175 51.928 52.282 90.679 1.00 18.65 C ANISOU 3153 CA GLY C 175 2321 2404 2361 -73 15 -24 C ATOM 3154 C GLY A 175 52.947 51.142 90.564 1.00 20.03 C ANISOU 3154 C GLY C 175 2551 2522 2536 -107 0 -11 C ATOM 3155 O GLY A 175 53.165 50.416 91.526 1.00 20.63 O ANISOU 3155 O GLY C 175 2548 2672 2615 -147 79 -67 O ATOM 3156 N GLY A 176 53.548 50.977 89.387 1.00 21.57 N ANISOU 3156 N GLY C 176 2724 2735 2733 -72 -2 4 N ATOM 3157 CA GLY A 176 54.530 49.925 89.148 1.00 22.75 C ANISOU 3157 CA GLY C 176 2862 2907 2873 -50 -36 -1 C ATOM 3158 C GLY A 176 54.113 48.515 89.544 1.00 23.30 C ANISOU 3158 C GLY C 176 2928 2979 2945 -57 8 3 C ATOM 3159 O GLY A 176 54.928 47.750 90.104 1.00 24.30 O ANISOU 3159 O GLY C 176 3014 3146 3072 -116 -36 -23 O ATOM 3160 N LEU A 177 52.849 48.177 89.286 1.00 22.50 N ANISOU 3160 N LEU C 177 2805 2912 2829 -48 -1 -9 N ATOM 3161 CA LEU A 177 52.353 46.836 89.534 1.00 22.49 C ANISOU 3161 CA LEU C 177 2838 2911 2795 -37 24 -36 C ATOM 3162 C LEU A 177 52.234 46.045 88.243 1.00 23.06 C ANISOU 3162 C LEU C 177 2945 2967 2848 -33 48 -62 C ATOM 3163 O LEU A 177 51.668 46.528 87.257 1.00 23.16 O ANISOU 3163 O LEU C 177 2995 2988 2815 -43 104 -114 O ATOM 3164 CB LEU A 177 50.984 46.874 90.213 1.00 22.24 C ANISOU 3164 CB LEU C 177 2800 2886 2761 -42 38 -25 C ATOM 3165 CG LEU A 177 50.887 47.518 91.596 1.00 21.98 C ANISOU 3165 CG LEU C 177 2802 2806 2741 -50 2 -44 C ATOM 3166 CD1 LEU A 177 49.451 47.449 92.055 1.00 22.54 C ANISOU 3166 CD1 LEU C 177 2803 2890 2869 -76 -76 -34 C ATOM 3167 CD2 LEU A 177 51.789 46.822 92.600 1.00 22.37 C ANISOU 3167 CD2 LEU C 177 2808 3024 2664 -13 -35 -60 C ATOM 3168 N SER A 178 52.769 44.830 88.269 1.00 23.79 N ANISOU 3168 N SER C 178 2988 3098 2950 -15 36 -79 N ATOM 3169 CA SER A 178 52.597 43.850 87.195 1.00 24.37 C ANISOU 3169 CA SER C 178 3039 3156 3063 7 12 -73 C ATOM 3170 C SER A 178 52.643 42.462 87.802 1.00 24.58 C ANISOU 3170 C SER C 178 3068 3163 3108 -6 12 -52 C ATOM 3171 O SER A 178 52.897 42.320 89.000 1.00 24.22 O ANISOU 3171 O SER C 178 2970 3117 3116 16 37 -38 O ATOM 3172 CB SER A 178 53.708 43.989 86.165 1.00 24.64 C ANISOU 3172 CB SER C 178 3069 3235 3056 -4 -8 -63 C ATOM 3173 OG SER A 178 54.972 43.741 86.767 1.00 25.34 O ANISOU 3173 OG SER C 178 3085 3420 3123 -62 48 -119 O ATOM 3174 N VAL A 179 52.392 41.437 86.985 1.00 24.92 N ANISOU 3174 N VAL C 179 3162 3135 3169 -25 9 -60 N ATOM 3175 CA VAL A 179 52.563 40.061 87.435 1.00 26.03 C ANISOU 3175 CA VAL C 179 3336 3236 3317 -13 13 -56 C ATOM 3176 C VAL A 179 53.919 39.894 88.103 1.00 26.38 C ANISOU 3176 C VAL C 179 3395 3268 3359 -43 10 -70 C ATOM 3177 O VAL A 179 54.015 39.317 89.186 1.00 26.63 O ANISOU 3177 O VAL C 179 3415 3277 3425 -70 7 -80 O ATOM 3178 CB VAL A 179 52.408 39.034 86.263 1.00 26.23 C ANISOU 3178 CB VAL C 179 3359 3250 3353 -29 25 -54 C ATOM 3179 CG1 VAL A 179 53.058 37.681 86.620 1.00 26.67 C ANISOU 3179 CG1 VAL C 179 3428 3247 3456 15 31 -61 C ATOM 3180 CG2 VAL A 179 50.946 38.846 85.939 1.00 26.33 C ANISOU 3180 CG2 VAL C 179 3385 3219 3400 28 42 -64 C ATOM 3181 N ASP A 180 54.948 40.435 87.463 1.00 27.19 N ANISOU 3181 N ASP C 180 3473 3394 3461 -36 -15 -75 N ATOM 3182 CA ASP A 180 56.332 40.244 87.887 1.00 28.13 C ANISOU 3182 CA ASP C 180 3587 3562 3539 -43 23 -50 C ATOM 3183 C ASP A 180 56.671 40.943 89.203 1.00 27.36 C ANISOU 3183 C ASP C 180 3463 3485 3447 -67 24 -36 C ATOM 3184 O ASP A 180 57.510 40.450 89.959 1.00 27.64 O ANISOU 3184 O ASP C 180 3540 3565 3395 -119 24 -34 O ATOM 3185 CB ASP A 180 57.300 40.684 86.777 1.00 29.17 C ANISOU 3185 CB ASP C 180 3707 3688 3688 -9 -5 -38 C ATOM 3186 CG ASP A 180 57.076 39.938 85.459 1.00 32.29 C ANISOU 3186 CG ASP C 180 4135 4099 4034 0 -7 -39 C ATOM 3187 OD1 ASP A 180 56.522 38.811 85.475 1.00 35.49 O ANISOU 3187 OD1 ASP C 180 4557 4425 4500 56 -42 -42 O ATOM 3188 OD2 ASP A 180 57.444 40.442 84.371 1.00 35.55 O ANISOU 3188 OD2 ASP C 180 4634 4528 4343 -15 26 24 O ATOM 3189 N THR A 181 56.027 42.072 89.496 1.00 26.11 N ANISOU 3189 N THR C 181 3288 3347 3284 -75 30 -23 N ATOM 3190 CA THR A 181 56.342 42.791 90.737 1.00 24.87 C ANISOU 3190 CA THR C 181 3098 3204 3146 -71 33 -18 C ATOM 3191 C THR A 181 55.520 42.349 91.959 1.00 24.26 C ANISOU 3191 C THR C 181 3003 3116 3097 -80 40 -30 C ATOM 3192 O THR A 181 55.872 42.720 93.073 1.00 24.31 O ANISOU 3192 O THR C 181 2944 3187 3103 -80 39 -48 O ATOM 3193 CB THR A 181 56.321 44.334 90.577 1.00 25.21 C ANISOU 3193 CB THR C 181 3119 3271 3186 -64 30 -8 C ATOM 3194 OG1 THR A 181 55.019 44.791 90.173 1.00 24.23 O ANISOU 3194 OG1 THR C 181 3013 3117 3076 -177 47 -80 O ATOM 3195 CG2 THR A 181 57.322 44.796 89.513 1.00 25.59 C ANISOU 3195 CG2 THR C 181 3126 3331 3264 -47 -23 -7 C ATOM 3196 N LEU A 182 54.454 41.564 91.770 1.00 23.32 N ANISOU 3196 N LEU C 182 2950 2944 2964 -129 54 1 N ATOM 3197 CA LEU A 182 53.620 41.137 92.891 1.00 23.57 C ANISOU 3197 CA LEU C 182 2990 2968 2995 -126 66 8 C ATOM 3198 C LEU A 182 54.419 40.398 93.966 1.00 24.42 C ANISOU 3198 C LEU C 182 3138 3084 3054 -134 66 40 C ATOM 3199 O LEU A 182 54.122 40.538 95.144 1.00 24.85 O ANISOU 3199 O LEU C 182 3199 3101 3140 -168 92 28 O ATOM 3200 CB LEU A 182 52.435 40.276 92.437 1.00 22.96 C ANISOU 3200 CB LEU C 182 2925 2898 2901 -140 68 -7 C ATOM 3201 CG LEU A 182 51.293 41.048 91.769 1.00 22.01 C ANISOU 3201 CG LEU C 182 2787 2840 2734 -75 67 -34 C ATOM 3202 CD1 LEU A 182 50.324 40.053 91.160 1.00 22.16 C ANISOU 3202 CD1 LEU C 182 2774 2904 2742 -105 87 13 C ATOM 3203 CD2 LEU A 182 50.573 41.988 92.758 1.00 19.95 C ANISOU 3203 CD2 LEU C 182 2357 2540 2680 -150 107 -28 C ATOM 3204 N LYS A 183 55.421 39.622 93.539 1.00 25.45 N ANISOU 3204 N LYS C 183 3242 3226 3198 -133 68 35 N ATOM 3205 CA LYS A 183 56.285 38.853 94.462 1.00 26.10 C ANISOU 3205 CA LYS C 183 3304 3325 3285 -93 60 29 C ATOM 3206 C LYS A 183 57.024 39.739 95.468 1.00 25.73 C ANISOU 3206 C LYS C 183 3242 3285 3248 -52 56 37 C ATOM 3207 O LYS A 183 57.408 39.276 96.532 1.00 25.85 O ANISOU 3207 O LYS C 183 3271 3306 3243 -45 95 77 O ATOM 3208 CB LYS A 183 57.285 37.965 93.693 1.00 26.64 C ANISOU 3208 CB LYS C 183 3370 3385 3368 -86 51 9 C ATOM 3209 CG LYS A 183 58.251 38.714 92.778 1.00 28.20 C ANISOU 3209 CG LYS C 183 3511 3582 3621 -72 28 22 C ATOM 3210 CD LYS A 183 59.166 37.759 91.984 1.00 31.85 C ANISOU 3210 CD LYS C 183 3987 4052 4059 -70 -15 -57 C ATOM 3211 CE LYS A 183 58.411 36.910 90.960 1.00 33.36 C ANISOU 3211 CE LYS C 183 4190 4257 4227 -114 19 -8 C ATOM 3212 NZ LYS A 183 57.739 37.720 89.907 1.00 34.65 N ANISOU 3212 NZ LYS C 183 4373 4472 4317 -93 -32 13 N ATOM 3213 N LEU A 184 57.207 41.013 95.145 1.00 25.31 N ANISOU 3213 N LEU C 184 3172 3225 3217 -48 66 6 N ATOM 3214 CA LEU A 184 57.803 41.958 96.087 1.00 25.42 C ANISOU 3214 CA LEU C 184 3177 3276 3204 -50 50 -2 C ATOM 3215 C LEU A 184 56.967 42.200 97.343 1.00 25.19 C ANISOU 3215 C LEU C 184 3139 3250 3180 -53 49 0 C ATOM 3216 O LEU A 184 57.470 42.791 98.299 1.00 25.42 O ANISOU 3216 O LEU C 184 3134 3338 3185 -127 63 25 O ATOM 3217 CB LEU A 184 58.060 43.301 95.407 1.00 25.25 C ANISOU 3217 CB LEU C 184 3171 3203 3220 -33 72 -18 C ATOM 3218 CG LEU A 184 58.979 43.332 94.189 1.00 26.82 C ANISOU 3218 CG LEU C 184 3350 3446 3394 -23 30 0 C ATOM 3219 CD1 LEU A 184 59.254 44.770 93.755 1.00 27.29 C ANISOU 3219 CD1 LEU C 184 3408 3473 3486 -77 38 -23 C ATOM 3220 CD2 LEU A 184 60.282 42.586 94.453 1.00 28.18 C ANISOU 3220 CD2 LEU C 184 3424 3687 3595 -51 18 27 C ATOM 3221 N PHE A 185 55.707 41.762 97.329 1.00 25.00 N ANISOU 3221 N PHE C 185 3119 3228 3150 -68 60 1 N ATOM 3222 CA PHE A 185 54.776 41.984 98.435 1.00 24.63 C ANISOU 3222 CA PHE C 185 3034 3178 3144 -57 70 -8 C ATOM 3223 C PHE A 185 54.490 40.714 99.227 1.00 25.60 C ANISOU 3223 C PHE C 185 3182 3295 3247 -63 61 -9 C ATOM 3224 O PHE A 185 53.612 40.700 100.095 1.00 24.93 O ANISOU 3224 O PHE C 185 3025 3289 3155 -136 115 -7 O ATOM 3225 CB PHE A 185 53.443 42.532 97.897 1.00 24.36 C ANISOU 3225 CB PHE C 185 3029 3172 3055 -58 48 -11 C ATOM 3226 CG PHE A 185 53.525 43.927 97.353 1.00 22.35 C ANISOU 3226 CG PHE C 185 2582 2972 2935 -21 73 -15 C ATOM 3227 CD1 PHE A 185 53.249 45.014 98.172 1.00 21.84 C ANISOU 3227 CD1 PHE C 185 2515 2961 2821 56 160 -25 C ATOM 3228 CD2 PHE A 185 53.817 44.153 96.011 1.00 22.61 C ANISOU 3228 CD2 PHE C 185 2561 3018 3010 -51 79 1 C ATOM 3229 CE1 PHE A 185 53.288 46.306 97.680 1.00 22.31 C ANISOU 3229 CE1 PHE C 185 2627 2892 2954 -11 187 1 C ATOM 3230 CE2 PHE A 185 53.868 45.448 95.499 1.00 22.51 C ANISOU 3230 CE2 PHE C 185 2607 2971 2975 13 118 -52 C ATOM 3231 CZ PHE A 185 53.612 46.533 96.336 1.00 22.95 C ANISOU 3231 CZ PHE C 185 2700 3043 2976 -73 89 -83 C ATOM 3232 N GLU A 186 55.200 39.627 98.929 1.00 26.83 N ANISOU 3232 N GLU C 186 3347 3393 3455 -94 31 -2 N ATOM 3233 CA GLU A 186 54.898 38.370 99.621 1.00 27.99 C ANISOU 3233 CA GLU C 186 3532 3531 3572 -40 25 21 C ATOM 3234 C GLU A 186 54.962 38.608 101.117 1.00 27.50 C ANISOU 3234 C GLU C 186 3470 3459 3516 -53 55 39 C ATOM 3235 O GLU A 186 55.839 39.307 101.579 1.00 27.00 O ANISOU 3235 O GLU C 186 3380 3383 3496 -67 170 104 O ATOM 3236 CB GLU A 186 55.871 37.246 99.234 1.00 28.86 C ANISOU 3236 CB GLU C 186 3637 3635 3692 -62 -1 1 C ATOM 3237 CG GLU A 186 55.407 35.877 99.721 1.00 32.37 C ANISOU 3237 CG GLU C 186 4064 4078 4155 -19 -13 7 C ATOM 3238 CD GLU A 186 56.272 34.749 99.205 1.00 36.84 C ANISOU 3238 CD GLU C 186 4639 4584 4773 -85 -13 -34 C ATOM 3239 OE1 GLU A 186 57.492 34.802 99.473 1.00 38.72 O ANISOU 3239 OE1 GLU C 186 4788 4965 4959 -126 41 -28 O ATOM 3240 OE2 GLU A 186 55.736 33.820 98.540 1.00 39.11 O ANISOU 3240 OE2 GLU C 186 4924 4937 4997 -1 68 -48 O ATOM 3241 N GLY A 187 54.007 38.052 101.859 1.00 27.23 N ANISOU 3241 N GLY C 187 3436 3460 3447 -59 54 34 N ATOM 3242 CA GLY A 187 53.971 38.213 103.306 1.00 27.03 C ANISOU 3242 CA GLY C 187 3429 3435 3406 -78 27 20 C ATOM 3243 C GLY A 187 53.440 39.553 103.790 1.00 26.89 C ANISOU 3243 C GLY C 187 3465 3393 3358 -58 31 19 C ATOM 3244 O GLY A 187 53.411 39.799 104.993 1.00 26.79 O ANISOU 3244 O GLY C 187 3458 3393 3324 -91 70 29 O ATOM 3245 N VAL A 188 53.019 40.420 102.863 1.00 26.29 N ANISOU 3245 N VAL C 188 3370 3317 3300 -81 45 -7 N ATOM 3246 CA VAL A 188 52.397 41.699 103.229 1.00 25.48 C ANISOU 3246 CA VAL C 188 3256 3232 3193 -37 60 -20 C ATOM 3247 C VAL A 188 50.902 41.586 102.948 1.00 24.84 C ANISOU 3247 C VAL C 188 3186 3134 3118 -59 53 -7 C ATOM 3248 O VAL A 188 50.496 41.168 101.857 1.00 24.23 O ANISOU 3248 O VAL C 188 3120 3078 3006 -92 102 -23 O ATOM 3249 CB VAL A 188 53.005 42.900 102.458 1.00 25.66 C ANISOU 3249 CB VAL C 188 3284 3252 3210 -41 51 -33 C ATOM 3250 CG1 VAL A 188 52.419 44.218 102.959 1.00 26.12 C ANISOU 3250 CG1 VAL C 188 3307 3364 3252 -73 74 -84 C ATOM 3251 CG2 VAL A 188 54.515 42.919 102.593 1.00 25.78 C ANISOU 3251 CG2 VAL C 188 3289 3267 3237 -18 36 -42 C ATOM 3252 N ASP A 189 50.099 41.982 103.929 1.00 24.03 N ANISOU 3252 N ASP C 189 3089 3052 2986 -41 40 23 N ATOM 3253 CA ASP A 189 48.657 41.776 103.913 1.00 23.87 C ANISOU 3253 CA ASP C 189 3064 3026 2977 -76 52 50 C ATOM 3254 C ASP A 189 47.923 42.842 103.079 1.00 22.55 C ANISOU 3254 C ASP C 189 2911 2887 2770 -104 34 77 C ATOM 3255 O ASP A 189 46.965 43.459 103.552 1.00 22.58 O ANISOU 3255 O ASP C 189 2954 2959 2665 -148 53 96 O ATOM 3256 CB ASP A 189 48.145 41.760 105.359 1.00 24.46 C ANISOU 3256 CB ASP C 189 3171 3056 3066 -51 47 20 C ATOM 3257 CG ASP A 189 46.699 41.350 105.474 1.00 26.86 C ANISOU 3257 CG ASP C 189 3415 3385 3403 -62 38 28 C ATOM 3258 OD1 ASP A 189 46.254 40.482 104.690 1.00 28.85 O ANISOU 3258 OD1 ASP C 189 3766 3649 3545 43 167 -13 O ATOM 3259 OD2 ASP A 189 45.969 41.861 106.355 1.00 29.96 O ANISOU 3259 OD2 ASP C 189 3844 3900 3638 -102 42 -21 O ATOM 3260 N VAL A 190 48.370 43.033 101.838 1.00 21.14 N ANISOU 3260 N VAL C 190 2752 2690 2590 -155 71 87 N ATOM 3261 CA VAL A 190 47.762 44.019 100.921 1.00 20.23 C ANISOU 3261 CA VAL C 190 2638 2565 2482 -99 43 119 C ATOM 3262 C VAL A 190 46.295 43.659 100.677 1.00 19.31 C ANISOU 3262 C VAL C 190 2527 2463 2345 -80 59 101 C ATOM 3263 O VAL A 190 45.980 42.502 100.392 1.00 19.50 O ANISOU 3263 O VAL C 190 2550 2434 2425 -111 67 247 O ATOM 3264 CB VAL A 190 48.545 44.102 99.578 1.00 19.92 C ANISOU 3264 CB VAL C 190 2603 2542 2421 -128 68 86 C ATOM 3265 CG1 VAL A 190 47.847 45.061 98.587 1.00 19.62 C ANISOU 3265 CG1 VAL C 190 2612 2380 2460 -94 71 134 C ATOM 3266 CG2 VAL A 190 49.973 44.551 99.802 1.00 20.52 C ANISOU 3266 CG2 VAL C 190 2620 2662 2515 -109 16 102 C ATOM 3267 N PHE A 191 45.400 44.643 100.822 1.00 18.60 N ANISOU 3267 N PHE C 191 2415 2387 2263 -55 28 122 N ATOM 3268 CA PHE A 191 43.952 44.432 100.655 1.00 18.60 C ANISOU 3268 CA PHE C 191 2392 2410 2263 -92 30 50 C ATOM 3269 C PHE A 191 43.535 44.460 99.183 1.00 17.97 C ANISOU 3269 C PHE C 191 2270 2343 2213 -79 39 44 C ATOM 3270 O PHE A 191 42.725 43.647 98.747 1.00 18.48 O ANISOU 3270 O PHE C 191 2274 2475 2273 -131 82 77 O ATOM 3271 CB PHE A 191 43.174 45.485 101.463 1.00 18.87 C ANISOU 3271 CB PHE C 191 2450 2480 2240 -74 14 32 C ATOM 3272 CG PHE A 191 41.690 45.521 101.189 1.00 19.44 C ANISOU 3272 CG PHE C 191 2490 2499 2395 -140 4 28 C ATOM 3273 CD1 PHE A 191 40.861 44.453 101.533 1.00 20.01 C ANISOU 3273 CD1 PHE C 191 2454 2696 2450 -103 -16 42 C ATOM 3274 CD2 PHE A 191 41.121 46.651 100.598 1.00 20.36 C ANISOU 3274 CD2 PHE C 191 2601 2693 2441 -162 46 27 C ATOM 3275 CE1 PHE A 191 39.469 44.500 101.286 1.00 20.18 C ANISOU 3275 CE1 PHE C 191 2601 2559 2506 -117 -40 111 C ATOM 3276 CE2 PHE A 191 39.751 46.705 100.349 1.00 20.60 C ANISOU 3276 CE2 PHE C 191 2615 2674 2538 -103 49 47 C ATOM 3277 CZ PHE A 191 38.923 45.637 100.689 1.00 19.94 C ANISOU 3277 CZ PHE C 191 2469 2622 2483 -108 -17 52 C ATOM 3278 N THR A 192 44.083 45.414 98.435 1.00 16.69 N ANISOU 3278 N THR C 192 2117 2202 2021 -87 46 27 N ATOM 3279 CA THR A 192 43.793 45.546 96.998 1.00 15.58 C ANISOU 3279 CA THR C 192 1982 2000 1937 -97 99 41 C ATOM 3280 C THR A 192 45.018 45.992 96.209 1.00 14.70 C ANISOU 3280 C THR C 192 1884 1871 1827 -121 128 33 C ATOM 3281 O THR A 192 45.735 46.880 96.636 1.00 14.69 O ANISOU 3281 O THR C 192 1770 1938 1874 -111 169 -13 O ATOM 3282 CB THR A 192 42.637 46.551 96.796 1.00 15.63 C ANISOU 3282 CB THR C 192 2011 1961 1965 -54 95 46 C ATOM 3283 OG1 THR A 192 41.430 46.002 97.334 1.00 15.31 O ANISOU 3283 OG1 THR C 192 2014 1857 1946 -214 31 225 O ATOM 3284 CG2 THR A 192 42.373 46.825 95.310 1.00 15.21 C ANISOU 3284 CG2 THR C 192 1953 1855 1970 -161 149 128 C ATOM 3285 N PHE A 193 45.244 45.367 95.053 1.00 14.80 N ANISOU 3285 N PHE C 193 1932 1904 1785 -125 76 93 N ATOM 3286 CA PHE A 193 46.204 45.849 94.063 1.00 14.72 C ANISOU 3286 CA PHE C 193 1896 1892 1803 -164 38 86 C ATOM 3287 C PHE A 193 45.428 46.568 92.956 1.00 14.35 C ANISOU 3287 C PHE C 193 1862 1847 1741 -134 46 91 C ATOM 3288 O PHE A 193 44.516 45.988 92.387 1.00 14.90 O ANISOU 3288 O PHE C 193 1961 1859 1838 -224 90 164 O ATOM 3289 CB PHE A 193 46.998 44.682 93.456 1.00 15.00 C ANISOU 3289 CB PHE C 193 1978 1910 1810 -190 3 104 C ATOM 3290 CG PHE A 193 47.927 44.028 94.430 1.00 15.86 C ANISOU 3290 CG PHE C 193 2018 2092 1915 -183 86 22 C ATOM 3291 CD1 PHE A 193 49.135 44.614 94.740 1.00 16.39 C ANISOU 3291 CD1 PHE C 193 2140 1996 2089 -195 26 103 C ATOM 3292 CD2 PHE A 193 47.579 42.827 95.052 1.00 17.22 C ANISOU 3292 CD2 PHE C 193 1993 2331 2216 -44 13 124 C ATOM 3293 CE1 PHE A 193 50.017 44.016 95.672 1.00 18.10 C ANISOU 3293 CE1 PHE C 193 2229 2457 2188 -160 208 17 C ATOM 3294 CE2 PHE A 193 48.458 42.211 95.974 1.00 19.74 C ANISOU 3294 CE2 PHE C 193 2325 2622 2552 -46 77 109 C ATOM 3295 CZ PHE A 193 49.674 42.826 96.280 1.00 19.56 C ANISOU 3295 CZ PHE C 193 2417 2551 2461 -59 127 12 C ATOM 3296 N ILE A 194 45.815 47.806 92.654 1.00 14.12 N ANISOU 3296 N ILE C 194 1836 1797 1732 -113 35 101 N ATOM 3297 CA ILE A 194 45.138 48.615 91.618 1.00 13.75 C ANISOU 3297 CA ILE C 194 1757 1785 1680 -84 66 48 C ATOM 3298 C ILE A 194 46.002 48.686 90.358 1.00 14.29 C ANISOU 3298 C ILE C 194 1854 1820 1756 -84 62 27 C ATOM 3299 O ILE A 194 47.100 49.209 90.410 1.00 14.65 O ANISOU 3299 O ILE C 194 1848 1961 1755 -91 -7 71 O ATOM 3300 CB ILE A 194 44.835 50.076 92.120 1.00 14.08 C ANISOU 3300 CB ILE C 194 1832 1802 1715 -134 89 59 C ATOM 3301 CG1 ILE A 194 44.101 50.068 93.464 1.00 13.61 C ANISOU 3301 CG1 ILE C 194 1692 1706 1772 -68 53 0 C ATOM 3302 CG2 ILE A 194 44.069 50.885 91.026 1.00 12.61 C ANISOU 3302 CG2 ILE C 194 1604 1716 1470 -132 166 -17 C ATOM 3303 CD1 ILE A 194 43.820 51.486 94.042 1.00 13.44 C ANISOU 3303 CD1 ILE C 194 1666 1679 1759 -223 -25 75 C ATOM 3304 N ALA A 195 45.505 48.131 89.248 1.00 14.20 N ANISOU 3304 N ALA C 195 1805 1856 1733 -127 63 -3 N ATOM 3305 CA ALA A 195 46.154 48.250 87.938 1.00 14.18 C ANISOU 3305 CA ALA C 195 1823 1794 1769 -97 62 -24 C ATOM 3306 C ALA A 195 45.292 49.083 87.007 1.00 13.54 C ANISOU 3306 C ALA C 195 1701 1723 1719 -44 74 -54 C ATOM 3307 O ALA A 195 44.148 49.351 87.313 1.00 15.33 O ANISOU 3307 O ALA C 195 1822 2095 1905 -40 49 0 O ATOM 3308 CB ALA A 195 46.368 46.882 87.327 1.00 14.45 C ANISOU 3308 CB ALA C 195 1898 1738 1852 -189 59 19 C ATOM 3309 N GLY A 196 45.865 49.528 85.904 1.00 13.38 N ANISOU 3309 N GLY C 196 1712 1715 1656 -86 86 -114 N ATOM 3310 CA GLY A 196 45.145 50.348 84.943 1.00 12.82 C ANISOU 3310 CA GLY C 196 1714 1511 1645 -23 44 -65 C ATOM 3311 C GLY A 196 45.464 49.951 83.527 1.00 13.54 C ANISOU 3311 C GLY C 196 1771 1621 1751 18 69 -64 C ATOM 3312 O GLY A 196 45.107 48.840 83.109 1.00 12.31 O ANISOU 3312 O GLY C 196 1682 1263 1729 -15 33 -114 O ATOM 3313 N ARG A 197 46.129 50.837 82.785 1.00 13.75 N ANISOU 3313 N ARG C 197 1825 1628 1772 38 49 0 N ATOM 3314 CA ARG A 197 46.397 50.598 81.369 1.00 15.83 C ANISOU 3314 CA ARG C 197 2024 2014 1974 9 14 -9 C ATOM 3315 C ARG A 197 47.293 49.381 81.121 1.00 15.80 C ANISOU 3315 C ARG C 197 2019 2038 1944 5 -26 -33 C ATOM 3316 O ARG A 197 47.227 48.764 80.061 1.00 16.01 O ANISOU 3316 O ARG C 197 2090 2105 1885 -53 -13 -39 O ATOM 3317 CB ARG A 197 46.989 51.857 80.699 1.00 16.58 C ANISOU 3317 CB ARG C 197 2152 2106 2039 32 -17 6 C ATOM 3318 CG ARG A 197 46.066 53.062 80.720 1.00 18.82 C ANISOU 3318 CG ARG C 197 2367 2395 2387 -14 34 -26 C ATOM 3319 CD ARG A 197 46.719 54.316 80.172 1.00 22.87 C ANISOU 3319 CD ARG C 197 2959 2877 2850 14 -94 74 C ATOM 3320 NE ARG A 197 46.790 54.294 78.711 1.00 25.81 N ANISOU 3320 NE ARG C 197 3306 3273 3225 16 -1 40 N ATOM 3321 CZ ARG A 197 47.459 55.180 77.961 1.00 26.84 C ANISOU 3321 CZ ARG C 197 3339 3460 3397 5 -41 48 C ATOM 3322 NH1 ARG A 197 48.143 56.177 78.537 1.00 28.42 N ANISOU 3322 NH1 ARG C 197 3606 3595 3595 103 -11 94 N ATOM 3323 NH2 ARG A 197 47.450 55.063 76.634 1.00 26.18 N ANISOU 3323 NH2 ARG C 197 3192 3433 3320 35 -33 20 N ATOM 3324 N GLY A 198 48.091 48.999 82.110 1.00 15.77 N ANISOU 3324 N GLY C 198 2000 2031 1959 -90 13 -54 N ATOM 3325 CA GLY A 198 48.919 47.797 81.990 1.00 16.72 C ANISOU 3325 CA GLY C 198 2047 2177 2127 -100 -13 -88 C ATOM 3326 C GLY A 198 48.071 46.596 81.640 1.00 16.38 C ANISOU 3326 C GLY C 198 2036 2110 2077 -155 11 -102 C ATOM 3327 O GLY A 198 48.478 45.742 80.839 1.00 17.65 O ANISOU 3327 O GLY C 198 2050 2364 2292 -241 34 -235 O ATOM 3328 N ILE A 199 46.872 46.521 82.225 1.00 15.25 N ANISOU 3328 N ILE C 199 1881 1932 1978 -170 31 -47 N ATOM 3329 CA ILE A 199 45.959 45.454 81.876 1.00 15.01 C ANISOU 3329 CA ILE C 199 1896 1895 1911 -130 15 -20 C ATOM 3330 C ILE A 199 44.964 45.815 80.784 1.00 14.32 C ANISOU 3330 C ILE C 199 1849 1765 1825 -133 0 -38 C ATOM 3331 O ILE A 199 44.725 44.986 79.892 1.00 14.26 O ANISOU 3331 O ILE C 199 1950 1648 1820 -197 22 -54 O ATOM 3332 CB ILE A 199 45.273 44.787 83.098 1.00 15.87 C ANISOU 3332 CB ILE C 199 1995 2046 1985 -142 21 11 C ATOM 3333 CG1 ILE A 199 44.406 45.745 83.896 1.00 15.63 C ANISOU 3333 CG1 ILE C 199 2092 1849 1996 -53 27 -3 C ATOM 3334 CG2 ILE A 199 46.327 44.104 84.040 1.00 16.54 C ANISOU 3334 CG2 ILE C 199 2092 2117 2074 -146 103 69 C ATOM 3335 CD1 ILE A 199 43.510 44.996 84.911 1.00 17.33 C ANISOU 3335 CD1 ILE C 199 2256 2144 2184 -40 25 -3 C ATOM 3336 N THR A 200 44.398 47.025 80.801 1.00 13.36 N ANISOU 3336 N THR C 200 1732 1660 1684 -112 -14 -56 N ATOM 3337 CA THR A 200 43.355 47.341 79.813 1.00 13.03 C ANISOU 3337 CA THR C 200 1656 1608 1686 -127 0 -4 C ATOM 3338 C THR A 200 43.892 47.551 78.397 1.00 13.06 C ANISOU 3338 C THR C 200 1633 1641 1687 -164 -11 6 C ATOM 3339 O THR A 200 43.142 47.418 77.428 1.00 12.87 O ANISOU 3339 O THR C 200 1640 1585 1663 -206 6 -42 O ATOM 3340 CB THR A 200 42.456 48.521 80.238 1.00 12.90 C ANISOU 3340 CB THR C 200 1586 1603 1711 -88 26 -12 C ATOM 3341 OG1 THR A 200 43.241 49.709 80.415 1.00 12.50 O ANISOU 3341 OG1 THR C 200 1508 1586 1653 -215 41 -103 O ATOM 3342 CG2 THR A 200 41.752 48.200 81.550 1.00 11.91 C ANISOU 3342 CG2 THR C 200 1596 1249 1679 -93 30 -77 C ATOM 3343 N GLU A 201 45.189 47.837 78.272 1.00 13.55 N ANISOU 3343 N GLU C 201 1712 1704 1731 -76 10 51 N ATOM 3344 CA GLU A 201 45.820 48.013 76.961 1.00 14.58 C ANISOU 3344 CA GLU C 201 1880 1845 1812 -96 -41 -64 C ATOM 3345 C GLU A 201 46.720 46.823 76.605 1.00 14.67 C ANISOU 3345 C GLU C 201 1883 1846 1844 -79 -63 -55 C ATOM 3346 O GLU A 201 47.470 46.890 75.650 1.00 15.09 O ANISOU 3346 O GLU C 201 2016 1932 1783 -87 -123 -177 O ATOM 3347 CB GLU A 201 46.657 49.305 76.891 1.00 15.32 C ANISOU 3347 CB GLU C 201 2018 1932 1868 -42 -43 -41 C ATOM 3348 CG GLU A 201 45.916 50.620 77.106 1.00 19.78 C ANISOU 3348 CG GLU C 201 2611 2532 2371 -134 -73 -125 C ATOM 3349 CD GLU A 201 46.762 51.826 76.715 1.00 25.97 C ANISOU 3349 CD GLU C 201 3393 3173 3301 11 31 10 C ATOM 3350 OE1 GLU A 201 47.925 51.984 77.197 1.00 28.00 O ANISOU 3350 OE1 GLU C 201 3679 3246 3712 191 158 13 O ATOM 3351 OE2 GLU A 201 46.282 52.620 75.892 1.00 29.72 O ANISOU 3351 OE2 GLU C 201 3823 3633 3836 -124 140 -10 O ATOM 3352 N ALA A 202 46.666 45.759 77.393 1.00 14.72 N ANISOU 3352 N ALA C 202 1948 1774 1870 -138 -54 -112 N ATOM 3353 CA ALA A 202 47.387 44.530 77.045 1.00 14.89 C ANISOU 3353 CA ALA C 202 1928 1819 1910 -138 8 -117 C ATOM 3354 C ALA A 202 46.826 43.927 75.749 1.00 15.48 C ANISOU 3354 C ALA C 202 2039 1872 1968 -93 9 -122 C ATOM 3355 O ALA A 202 45.695 44.178 75.365 1.00 15.02 O ANISOU 3355 O ALA C 202 2052 1762 1891 -141 16 -135 O ATOM 3356 CB ALA A 202 47.302 43.543 78.170 1.00 14.64 C ANISOU 3356 CB ALA C 202 1874 1797 1891 -93 26 -144 C ATOM 3357 N LYS A 203 47.625 43.095 75.101 1.00 16.20 N ANISOU 3357 N LYS C 203 2097 1963 2094 -51 -1 -107 N ATOM 3358 CA LYS A 203 47.209 42.460 73.857 1.00 17.14 C ANISOU 3358 CA LYS C 203 2199 2155 2157 25 0 -78 C ATOM 3359 C LYS A 203 45.982 41.539 74.045 1.00 16.83 C ANISOU 3359 C LYS C 203 2186 2026 2180 39 30 -63 C ATOM 3360 O LYS A 203 45.196 41.353 73.104 1.00 17.89 O ANISOU 3360 O LYS C 203 2368 2141 2286 100 129 46 O ATOM 3361 CB LYS A 203 48.391 41.709 73.228 1.00 17.41 C ANISOU 3361 CB LYS C 203 2233 2177 2205 -55 6 -139 C ATOM 3362 CG LYS A 203 48.969 40.584 74.075 1.00 19.43 C ANISOU 3362 CG LYS C 203 2546 2386 2449 2 -78 -25 C ATOM 3363 CD LYS A 203 50.214 40.006 73.424 1.00 21.90 C ANISOU 3363 CD LYS C 203 2783 2642 2895 16 -48 -24 C ATOM 3364 CE LYS A 203 50.697 38.757 74.144 1.00 24.06 C ANISOU 3364 CE LYS C 203 2996 3058 3086 -14 -25 -3 C ATOM 3365 NZ LYS A 203 52.045 38.372 73.639 1.00 25.04 N ANISOU 3365 NZ LYS C 203 3077 3123 3314 -203 -116 31 N ATOM 3366 N ASN A 204 45.850 40.954 75.236 1.00 15.50 N ANISOU 3366 N ASN C 204 2009 1875 2002 55 16 -79 N ATOM 3367 CA ASN A 204 44.610 40.277 75.678 1.00 15.09 C ANISOU 3367 CA ASN C 204 1990 1781 1962 -4 -10 -74 C ATOM 3368 C ASN A 204 44.254 40.764 77.073 1.00 14.21 C ANISOU 3368 C ASN C 204 1937 1661 1800 -27 56 -26 C ATOM 3369 O ASN A 204 44.780 40.255 78.050 1.00 14.73 O ANISOU 3369 O ASN C 204 1968 1732 1894 -25 136 -58 O ATOM 3370 CB ASN A 204 44.763 38.752 75.657 1.00 14.85 C ANISOU 3370 CB ASN C 204 1977 1730 1933 -6 -31 -8 C ATOM 3371 CG ASN A 204 43.590 38.030 76.301 1.00 15.14 C ANISOU 3371 CG ASN C 204 1916 1720 2116 -41 -81 -65 C ATOM 3372 OD1 ASN A 204 42.530 38.612 76.568 1.00 16.47 O ANISOU 3372 OD1 ASN C 204 2142 1791 2323 -209 -40 -4 O ATOM 3373 ND2 ASN A 204 43.782 36.748 76.578 1.00 16.39 N ANISOU 3373 ND2 ASN C 204 2131 1770 2324 -79 -82 -17 N ATOM 3374 N PRO A 205 43.437 41.826 77.166 1.00 13.41 N ANISOU 3374 N PRO C 205 1796 1615 1682 -66 70 -89 N ATOM 3375 CA PRO A 205 43.147 42.453 78.466 1.00 12.67 C ANISOU 3375 CA PRO C 205 1685 1452 1675 -54 50 -77 C ATOM 3376 C PRO A 205 42.564 41.494 79.503 1.00 13.26 C ANISOU 3376 C PRO C 205 1758 1549 1730 -103 41 -51 C ATOM 3377 O PRO A 205 43.044 41.454 80.634 1.00 12.97 O ANISOU 3377 O PRO C 205 1826 1269 1831 -219 118 -56 O ATOM 3378 CB PRO A 205 42.190 43.592 78.090 1.00 12.82 C ANISOU 3378 CB PRO C 205 1694 1539 1636 -37 74 -88 C ATOM 3379 CG PRO A 205 42.577 43.937 76.726 1.00 13.01 C ANISOU 3379 CG PRO C 205 1714 1495 1732 -44 58 -107 C ATOM 3380 CD PRO A 205 42.775 42.569 76.073 1.00 13.07 C ANISOU 3380 CD PRO C 205 1861 1443 1660 -131 65 -98 C ATOM 3381 N ALA A 206 41.550 40.722 79.122 1.00 13.18 N ANISOU 3381 N ALA C 206 1712 1557 1737 -89 25 -35 N ATOM 3382 CA ALA A 206 40.978 39.716 80.045 1.00 13.77 C ANISOU 3382 CA ALA C 206 1764 1671 1797 -68 26 -2 C ATOM 3383 C ALA A 206 42.051 38.757 80.575 1.00 14.17 C ANISOU 3383 C ALA C 206 1798 1764 1821 -102 22 17 C ATOM 3384 O ALA A 206 42.063 38.413 81.765 1.00 14.58 O ANISOU 3384 O ALA C 206 1887 1866 1787 -201 -71 -31 O ATOM 3385 CB ALA A 206 39.864 38.916 79.364 1.00 14.04 C ANISOU 3385 CB ALA C 206 1715 1718 1901 -30 -5 0 C ATOM 3386 N GLY A 207 42.912 38.290 79.674 1.00 13.89 N ANISOU 3386 N GLY C 207 1757 1739 1781 -126 87 51 N ATOM 3387 CA GLY A 207 43.951 37.329 80.041 1.00 14.21 C ANISOU 3387 CA GLY C 207 1879 1624 1893 -106 78 18 C ATOM 3388 C GLY A 207 45.013 37.957 80.925 1.00 13.65 C ANISOU 3388 C GLY C 207 1835 1528 1820 -114 98 20 C ATOM 3389 O GLY A 207 45.542 37.303 81.848 1.00 13.95 O ANISOU 3389 O GLY C 207 2036 1339 1925 -236 114 -12 O ATOM 3390 N ALA A 208 45.310 39.239 80.692 1.00 13.51 N ANISOU 3390 N ALA C 208 1776 1510 1844 -96 62 -40 N ATOM 3391 CA ALA A 208 46.278 39.948 81.534 1.00 13.64 C ANISOU 3391 CA ALA C 208 1793 1585 1804 -112 54 -81 C ATOM 3392 C ALA A 208 45.712 40.150 82.945 1.00 13.76 C ANISOU 3392 C ALA C 208 1806 1589 1831 -84 60 -60 C ATOM 3393 O ALA A 208 46.417 39.978 83.948 1.00 13.41 O ANISOU 3393 O ALA C 208 1902 1376 1816 -216 181 -121 O ATOM 3394 CB ALA A 208 46.657 41.277 80.910 1.00 13.69 C ANISOU 3394 CB ALA C 208 1756 1643 1801 -82 32 -112 C ATOM 3395 N ALA A 209 44.435 40.509 83.029 1.00 14.02 N ANISOU 3395 N ALA C 209 1800 1654 1873 -61 60 -66 N ATOM 3396 CA ALA A 209 43.756 40.591 84.326 1.00 14.07 C ANISOU 3396 CA ALA C 209 1807 1697 1839 -51 21 -26 C ATOM 3397 C ALA A 209 43.726 39.225 85.037 1.00 14.95 C ANISOU 3397 C ALA C 209 1984 1772 1921 -67 21 -40 C ATOM 3398 O ALA A 209 44.059 39.146 86.219 1.00 14.47 O ANISOU 3398 O ALA C 209 2093 1581 1823 -122 63 -68 O ATOM 3399 CB ALA A 209 42.346 41.144 84.159 1.00 13.61 C ANISOU 3399 CB ALA C 209 1695 1665 1809 -51 84 -56 C ATOM 3400 N ARG A 210 43.371 38.156 84.315 1.00 15.22 N ANISOU 3400 N ARG C 210 2069 1802 1909 14 65 0 N ATOM 3401 CA ARG A 210 43.335 36.827 84.911 1.00 16.40 C ANISOU 3401 CA ARG C 210 2180 1957 2091 -24 43 0 C ATOM 3402 C ARG A 210 44.721 36.418 85.404 1.00 16.83 C ANISOU 3402 C ARG C 210 2226 2016 2153 -43 74 8 C ATOM 3403 O ARG A 210 44.833 35.841 86.471 1.00 17.61 O ANISOU 3403 O ARG C 210 2299 2136 2253 -71 120 41 O ATOM 3404 CB ARG A 210 42.799 35.788 83.919 1.00 15.93 C ANISOU 3404 CB ARG C 210 2167 1901 1983 2 57 52 C ATOM 3405 CG ARG A 210 42.488 34.430 84.535 1.00 17.18 C ANISOU 3405 CG ARG C 210 2333 1949 2243 -20 -107 -25 C ATOM 3406 CD ARG A 210 42.017 33.407 83.502 1.00 18.51 C ANISOU 3406 CD ARG C 210 2386 2304 2341 150 19 39 C ATOM 3407 NE ARG A 210 40.823 33.874 82.807 1.00 20.21 N ANISOU 3407 NE ARG C 210 2683 2410 2584 140 -33 66 N ATOM 3408 CZ ARG A 210 40.812 34.414 81.592 1.00 19.89 C ANISOU 3408 CZ ARG C 210 2654 2435 2466 53 52 -144 C ATOM 3409 NH1 ARG A 210 41.932 34.534 80.894 1.00 19.27 N ANISOU 3409 NH1 ARG C 210 2444 2343 2534 133 60 -262 N ATOM 3410 NH2 ARG A 210 39.661 34.814 81.065 1.00 21.98 N ANISOU 3410 NH2 ARG C 210 3011 2584 2755 -1 116 -54 N ATOM 3411 N ALA A 211 45.769 36.718 84.643 1.00 17.33 N ANISOU 3411 N ALA C 211 2240 2084 2258 -77 71 15 N ATOM 3412 CA ALA A 211 47.140 36.331 85.030 1.00 18.36 C ANISOU 3412 CA ALA C 211 2366 2264 2344 -83 43 -3 C ATOM 3413 C ALA A 211 47.577 37.061 86.306 1.00 19.00 C ANISOU 3413 C ALA C 211 2453 2374 2390 -130 45 -17 C ATOM 3414 O ALA A 211 48.326 36.538 87.143 1.00 19.64 O ANISOU 3414 O ALA C 211 2634 2445 2382 -249 13 68 O ATOM 3415 CB ALA A 211 48.115 36.613 83.897 1.00 18.17 C ANISOU 3415 CB ALA C 211 2360 2257 2286 -102 52 3 C ATOM 3416 N PHE A 212 47.103 38.292 86.444 1.00 18.87 N ANISOU 3416 N PHE C 212 2475 2281 2414 -128 49 -4 N ATOM 3417 CA PHE A 212 47.446 39.111 87.599 1.00 18.66 C ANISOU 3417 CA PHE C 212 2427 2288 2376 -108 53 1 C ATOM 3418 C PHE A 212 46.758 38.522 88.839 1.00 19.26 C ANISOU 3418 C PHE C 212 2541 2382 2395 -113 39 -38 C ATOM 3419 O PHE A 212 47.393 38.342 89.879 1.00 19.55 O ANISOU 3419 O PHE C 212 2626 2447 2352 -197 96 0 O ATOM 3420 CB PHE A 212 47.031 40.555 87.288 1.00 18.44 C ANISOU 3420 CB PHE C 212 2447 2215 2342 -56 23 -3 C ATOM 3421 CG PHE A 212 47.589 41.576 88.207 1.00 18.95 C ANISOU 3421 CG PHE C 212 2402 2390 2407 -100 49 -30 C ATOM 3422 CD1 PHE A 212 48.425 42.565 87.714 1.00 17.86 C ANISOU 3422 CD1 PHE C 212 2331 2145 2309 -46 0 -51 C ATOM 3423 CD2 PHE A 212 47.250 41.588 89.559 1.00 18.83 C ANISOU 3423 CD2 PHE C 212 2442 2377 2332 -133 -31 -42 C ATOM 3424 CE1 PHE A 212 48.934 43.557 88.560 1.00 19.79 C ANISOU 3424 CE1 PHE C 212 2530 2490 2499 -90 108 -87 C ATOM 3425 CE2 PHE A 212 47.764 42.576 90.417 1.00 18.66 C ANISOU 3425 CE2 PHE C 212 2380 2173 2535 -125 101 22 C ATOM 3426 CZ PHE A 212 48.611 43.548 89.907 1.00 20.63 C ANISOU 3426 CZ PHE C 212 2597 2574 2664 -45 -21 -29 C ATOM 3427 N LYS A 213 45.491 38.144 88.706 1.00 19.71 N ANISOU 3427 N LYS C 213 2591 2440 2458 -108 31 -21 N ATOM 3428 CA LYS A 213 44.765 37.489 89.796 1.00 20.86 C ANISOU 3428 CA LYS C 213 2722 2575 2629 -46 5 -23 C ATOM 3429 C LYS A 213 45.309 36.096 90.144 1.00 21.42 C ANISOU 3429 C LYS C 213 2836 2625 2677 -38 4 11 C ATOM 3430 O LYS A 213 45.318 35.721 91.316 1.00 21.56 O ANISOU 3430 O LYS C 213 2908 2576 2705 -59 3 28 O ATOM 3431 CB LYS A 213 43.265 37.419 89.469 1.00 21.42 C ANISOU 3431 CB LYS C 213 2774 2652 2710 0 25 -9 C ATOM 3432 CG LYS A 213 42.372 37.013 90.615 1.00 23.02 C ANISOU 3432 CG LYS C 213 2974 2879 2891 2 -24 -47 C ATOM 3433 CD LYS A 213 42.365 38.016 91.769 1.00 23.69 C ANISOU 3433 CD LYS C 213 3025 2913 3063 -1 5 -35 C ATOM 3434 CE LYS A 213 41.628 37.434 92.961 1.00 23.49 C ANISOU 3434 CE LYS C 213 3051 2884 2986 -136 -17 51 C ATOM 3435 NZ LYS A 213 41.534 38.365 94.099 1.00 22.04 N ANISOU 3435 NZ LYS C 213 3034 2499 2837 -170 251 93 N ATOM 3436 N ASP A 214 45.749 35.340 89.134 1.00 21.78 N ANISOU 3436 N ASP C 214 2887 2625 2763 -73 24 4 N ATOM 3437 CA ASP A 214 46.306 33.997 89.349 1.00 22.71 C ANISOU 3437 CA ASP C 214 2955 2815 2857 -64 41 23 C ATOM 3438 C ASP A 214 47.590 34.076 90.173 1.00 22.73 C ANISOU 3438 C ASP C 214 2964 2830 2840 -45 82 7 C ATOM 3439 O ASP A 214 47.824 33.211 91.010 1.00 23.25 O ANISOU 3439 O ASP C 214 3109 2864 2860 -79 156 12 O ATOM 3440 CB ASP A 214 46.611 33.287 88.016 1.00 22.85 C ANISOU 3440 CB ASP C 214 2997 2778 2906 -69 39 19 C ATOM 3441 CG ASP A 214 45.367 32.829 87.273 1.00 23.80 C ANISOU 3441 CG ASP C 214 3141 2882 3020 -102 40 90 C ATOM 3442 OD1 ASP A 214 44.252 32.839 87.832 1.00 25.63 O ANISOU 3442 OD1 ASP C 214 3234 3040 3463 -16 108 198 O ATOM 3443 OD2 ASP A 214 45.473 32.451 86.092 1.00 25.70 O ANISOU 3443 OD2 ASP C 214 3507 3037 3219 -285 227 104 O ATOM 3444 N GLU A 215 48.415 35.090 89.898 1.00 22.48 N ANISOU 3444 N GLU C 215 2904 2819 2815 -49 54 8 N ATOM 3445 CA GLU A 215 49.643 35.354 90.657 1.00 22.42 C ANISOU 3445 CA GLU C 215 2863 2819 2835 -65 46 18 C ATOM 3446 C GLU A 215 49.332 35.782 92.098 1.00 22.91 C ANISOU 3446 C GLU C 215 2938 2873 2890 -98 58 5 C ATOM 3447 O GLU A 215 49.995 35.333 93.041 1.00 23.24 O ANISOU 3447 O GLU C 215 3001 2852 2975 -148 120 9 O ATOM 3448 CB GLU A 215 50.517 36.386 89.927 1.00 22.35 C ANISOU 3448 CB GLU C 215 2862 2816 2812 -45 55 24 C ATOM 3449 CG GLU A 215 51.893 36.698 90.547 1.00 21.83 C ANISOU 3449 CG GLU C 215 2709 2750 2834 -113 6 33 C ATOM 3450 CD GLU A 215 52.864 35.517 90.613 1.00 22.99 C ANISOU 3450 CD GLU C 215 2807 2829 3098 -31 103 48 C ATOM 3451 OE1 GLU A 215 52.523 34.369 90.202 1.00 22.18 O ANISOU 3451 OE1 GLU C 215 2758 2528 3139 -378 281 -48 O ATOM 3452 OE2 GLU A 215 53.992 35.764 91.091 1.00 21.58 O ANISOU 3452 OE2 GLU C 215 2369 2716 3113 -264 92 15 O ATOM 3453 N ILE A 216 48.328 36.640 92.291 1.00 22.90 N ANISOU 3453 N ILE C 216 2899 2896 2906 -132 56 38 N ATOM 3454 CA ILE A 216 47.786 36.856 93.640 1.00 23.06 C ANISOU 3454 CA ILE C 216 2928 2913 2919 -103 47 10 C ATOM 3455 C ILE A 216 47.439 35.501 94.323 1.00 23.91 C ANISOU 3455 C ILE C 216 3041 3022 3020 -81 39 29 C ATOM 3456 O ILE A 216 47.864 35.250 95.453 1.00 24.14 O ANISOU 3456 O ILE C 216 3072 3020 3078 -130 70 19 O ATOM 3457 CB ILE A 216 46.551 37.817 93.629 1.00 22.88 C ANISOU 3457 CB ILE C 216 2884 2919 2887 -97 53 32 C ATOM 3458 CG1 ILE A 216 46.984 39.234 93.242 1.00 22.24 C ANISOU 3458 CG1 ILE C 216 2817 2806 2827 -63 82 -26 C ATOM 3459 CG2 ILE A 216 45.863 37.840 94.972 1.00 22.93 C ANISOU 3459 CG2 ILE C 216 2818 2944 2948 -113 101 43 C ATOM 3460 CD1 ILE A 216 45.832 40.197 92.929 1.00 21.52 C ANISOU 3460 CD1 ILE C 216 2833 2697 2645 -120 90 -55 C ATOM 3461 N LYS A 217 46.690 34.632 93.643 1.00 24.75 N ANISOU 3461 N LYS C 217 3194 3083 3126 -60 28 21 N ATOM 3462 CA LYS A 217 46.296 33.340 94.218 1.00 26.52 C ANISOU 3462 CA LYS C 217 3404 3321 3347 -37 23 33 C ATOM 3463 C LYS A 217 47.501 32.494 94.604 1.00 26.39 C ANISOU 3463 C LYS C 217 3422 3263 3340 -66 9 18 C ATOM 3464 O LYS A 217 47.486 31.838 95.642 1.00 26.52 O ANISOU 3464 O LYS C 217 3509 3259 3307 -110 6 43 O ATOM 3465 CB LYS A 217 45.400 32.541 93.266 1.00 26.96 C ANISOU 3465 CB LYS C 217 3480 3360 3403 -1 9 21 C ATOM 3466 CG LYS A 217 44.953 31.182 93.844 1.00 30.17 C ANISOU 3466 CG LYS C 217 3866 3726 3870 24 17 40 C ATOM 3467 CD LYS A 217 43.536 30.789 93.421 1.00 34.14 C ANISOU 3467 CD LYS C 217 4250 4355 4366 20 50 13 C ATOM 3468 CE LYS A 217 43.466 30.364 91.954 1.00 36.54 C ANISOU 3468 CE LYS C 217 4616 4661 4605 32 20 27 C ATOM 3469 NZ LYS A 217 43.409 31.547 91.030 1.00 37.59 N ANISOU 3469 NZ LYS C 217 4792 4715 4772 -16 28 96 N ATOM 3470 N ARG A 218 48.541 32.523 93.778 1.00 26.73 N ANISOU 3470 N ARG C 218 3436 3347 3370 -68 28 29 N ATOM 3471 CA ARG A 218 49.726 31.697 94.017 1.00 26.90 C ANISOU 3471 CA ARG C 218 3440 3365 3413 -59 24 31 C ATOM 3472 C ARG A 218 50.461 32.146 95.278 1.00 27.03 C ANISOU 3472 C ARG C 218 3492 3361 3417 -47 30 27 C ATOM 3473 O ARG A 218 50.821 31.320 96.122 1.00 27.16 O ANISOU 3473 O ARG C 218 3555 3329 3433 -64 31 62 O ATOM 3474 CB ARG A 218 50.664 31.740 92.807 1.00 27.09 C ANISOU 3474 CB ARG C 218 3434 3412 3445 -68 18 8 C ATOM 3475 CG ARG A 218 51.867 30.795 92.888 1.00 27.67 C ANISOU 3475 CG ARG C 218 3522 3484 3506 -97 29 29 C ATOM 3476 CD ARG A 218 52.831 30.954 91.715 1.00 28.44 C ANISOU 3476 CD ARG C 218 3573 3588 3646 -108 32 75 C ATOM 3477 NE ARG A 218 53.611 32.199 91.734 1.00 29.77 N ANISOU 3477 NE ARG C 218 3790 3691 3829 -129 61 42 N ATOM 3478 CZ ARG A 218 54.614 32.474 92.570 1.00 31.83 C ANISOU 3478 CZ ARG C 218 4026 3991 4075 -17 46 30 C ATOM 3479 NH1 ARG A 218 54.999 31.603 93.508 1.00 32.65 N ANISOU 3479 NH1 ARG C 218 4116 4117 4172 -56 102 71 N ATOM 3480 NH2 ARG A 218 55.240 33.640 92.473 1.00 32.04 N ANISOU 3480 NH2 ARG C 218 4007 4009 4156 -19 58 52 N ATOM 3481 N ILE A 219 50.677 33.454 95.399 1.00 26.77 N ANISOU 3481 N ILE C 219 3448 3320 3401 -49 27 23 N ATOM 3482 CA ILE A 219 51.448 34.037 96.502 1.00 26.40 C ANISOU 3482 CA ILE C 219 3376 3319 3335 -45 54 28 C ATOM 3483 C ILE A 219 50.673 34.074 97.830 1.00 26.50 C ANISOU 3483 C ILE C 219 3393 3348 3326 -47 50 17 C ATOM 3484 O ILE A 219 51.270 33.912 98.899 1.00 26.69 O ANISOU 3484 O ILE C 219 3459 3402 3278 -39 106 29 O ATOM 3485 CB ILE A 219 51.945 35.460 96.124 1.00 26.13 C ANISOU 3485 CB ILE C 219 3323 3290 3314 -48 42 28 C ATOM 3486 CG1 ILE A 219 52.900 35.403 94.931 1.00 26.33 C ANISOU 3486 CG1 ILE C 219 3359 3350 3294 -74 90 46 C ATOM 3487 CG2 ILE A 219 52.650 36.150 97.308 1.00 25.52 C ANISOU 3487 CG2 ILE C 219 3291 3197 3208 -72 52 53 C ATOM 3488 CD1 ILE A 219 53.224 36.760 94.338 1.00 26.59 C ANISOU 3488 CD1 ILE C 219 3376 3320 3404 -57 46 41 C ATOM 3489 N TRP A 220 49.358 34.281 97.767 1.00 26.52 N ANISOU 3489 N TRP C 220 3398 3347 3328 -42 45 17 N ATOM 3490 CA TRP A 220 48.547 34.465 98.976 1.00 26.66 C ANISOU 3490 CA TRP C 220 3387 3370 3371 -64 30 37 C ATOM 3491 C TRP A 220 47.609 33.305 99.311 1.00 27.74 C ANISOU 3491 C TRP C 220 3539 3508 3490 -44 30 40 C ATOM 3492 O TRP A 220 47.094 33.237 100.429 1.00 28.43 O ANISOU 3492 O TRP C 220 3656 3614 3531 -54 14 44 O ATOM 3493 CB TRP A 220 47.744 35.784 98.893 1.00 26.12 C ANISOU 3493 CB TRP C 220 3334 3289 3301 -40 17 45 C ATOM 3494 CG TRP A 220 48.575 36.967 99.211 1.00 23.74 C ANISOU 3494 CG TRP C 220 3063 2958 2999 -95 5 56 C ATOM 3495 CD1 TRP A 220 48.808 37.494 100.440 1.00 23.45 C ANISOU 3495 CD1 TRP C 220 2941 3001 2969 -67 -17 99 C ATOM 3496 CD2 TRP A 220 49.320 37.769 98.287 1.00 22.10 C ANISOU 3496 CD2 TRP C 220 2827 2724 2843 -127 -31 -3 C ATOM 3497 NE1 TRP A 220 49.645 38.582 100.347 1.00 22.29 N ANISOU 3497 NE1 TRP C 220 2827 2772 2870 -158 4 58 N ATOM 3498 CE2 TRP A 220 49.976 38.771 99.034 1.00 21.05 C ANISOU 3498 CE2 TRP C 220 2652 2611 2734 -110 30 52 C ATOM 3499 CE3 TRP A 220 49.478 37.758 96.897 1.00 21.19 C ANISOU 3499 CE3 TRP C 220 2778 2554 2718 -158 60 -3 C ATOM 3500 CZ2 TRP A 220 50.791 39.731 98.442 1.00 20.62 C ANISOU 3500 CZ2 TRP C 220 2515 2696 2622 -276 146 101 C ATOM 3501 CZ3 TRP A 220 50.296 38.698 96.316 1.00 20.23 C ANISOU 3501 CZ3 TRP C 220 2559 2529 2596 -163 44 80 C ATOM 3502 CH2 TRP A 220 50.945 39.676 97.081 1.00 20.23 C ANISOU 3502 CH2 TRP C 220 2551 2586 2547 -288 38 -15 C ATOM 3503 N GLY A 221 47.377 32.406 98.357 1.00 28.52 N ANISOU 3503 N GLY C 221 3641 3608 3586 -45 39 37 N ATOM 3504 CA GLY A 221 46.377 31.348 98.508 1.00 29.52 C ANISOU 3504 CA GLY C 221 3754 3718 3745 -29 53 41 C ATOM 3505 C GLY A 221 46.975 30.021 98.919 1.00 30.26 C ANISOU 3505 C GLY C 221 3853 3790 3852 -30 84 51 C ATOM 3506 O GLY A 221 47.843 29.990 99.788 1.00 30.90 O ANISOU 3506 O GLY C 221 3933 3834 3970 -45 124 65 O TER 3507 GLY C 221 ATOM 5452 N GLN A 4 44.005 97.162 89.991 1.00 28.29 N ANISOU 5452 N GLN D 4 3549 3528 3671 -7 -50 -40 N ATOM 5453 CA GLN A 4 42.529 96.965 89.843 1.00 27.62 C ANISOU 5453 CA GLN D 4 3520 3460 3513 11 -18 -30 C ATOM 5454 C GLN A 4 41.891 96.640 91.176 1.00 26.75 C ANISOU 5454 C GLN D 4 3431 3320 3410 14 -7 -42 C ATOM 5455 O GLN A 4 42.588 96.362 92.138 1.00 27.56 O ANISOU 5455 O GLN D 4 3559 3451 3462 -3 -13 -60 O ATOM 5456 N LEU A 5 40.565 96.673 91.230 1.00 25.50 N ANISOU 5456 N LEU D 5 3327 3134 3227 22 -46 -58 N ATOM 5457 CA LEU A 5 39.815 96.289 92.428 1.00 23.89 C ANISOU 5457 CA LEU D 5 3148 2905 3021 45 -37 -70 C ATOM 5458 C LEU A 5 39.878 94.779 92.674 1.00 22.49 C ANISOU 5458 C LEU D 5 2980 2760 2801 7 -77 -134 C ATOM 5459 O LEU A 5 40.095 94.003 91.737 1.00 22.74 O ANISOU 5459 O LEU D 5 3076 2674 2888 50 -97 -272 O ATOM 5460 CB LEU A 5 38.345 96.698 92.285 1.00 23.78 C ANISOU 5460 CB LEU D 5 3129 2866 3038 14 -43 -39 C ATOM 5461 CG LEU A 5 37.999 98.184 92.154 1.00 24.87 C ANISOU 5461 CG LEU D 5 3220 3048 3180 7 12 -1 C ATOM 5462 CD1 LEU A 5 36.490 98.372 91.862 1.00 24.76 C ANISOU 5462 CD1 LEU D 5 3128 3002 3274 -56 -54 1 C ATOM 5463 CD2 LEU A 5 38.420 98.914 93.416 1.00 24.71 C ANISOU 5463 CD2 LEU D 5 3282 2848 3259 59 20 -58 C ATOM 5464 N PRO A 6 39.661 94.345 93.919 1.00 20.54 N ANISOU 5464 N PRO D 6 2750 2483 2569 31 -42 -131 N ATOM 5465 CA PRO A 6 39.406 92.921 94.159 1.00 19.26 C ANISOU 5465 CA PRO D 6 2518 2351 2447 35 -41 -148 C ATOM 5466 C PRO A 6 38.252 92.435 93.266 1.00 18.33 C ANISOU 5466 C PRO D 6 2406 2171 2386 49 -19 -189 C ATOM 5467 O PRO A 6 37.273 93.150 93.079 1.00 17.90 O ANISOU 5467 O PRO D 6 2452 1974 2374 90 -18 -309 O ATOM 5468 CB PRO A 6 39.006 92.882 95.630 1.00 19.31 C ANISOU 5468 CB PRO D 6 2543 2388 2405 58 12 -144 C ATOM 5469 CG PRO A 6 39.690 94.097 96.240 1.00 18.90 C ANISOU 5469 CG PRO D 6 2502 2271 2405 26 -31 -142 C ATOM 5470 CD PRO A 6 39.629 95.140 95.166 1.00 19.97 C ANISOU 5470 CD PRO D 6 2677 2429 2478 28 -54 -133 C ATOM 5471 N ASN A 7 38.394 91.243 92.680 1.00 17.69 N ANISOU 5471 N ASN D 7 2247 2104 2370 28 -63 -223 N ATOM 5472 CA ASN A 7 37.330 90.647 91.871 1.00 16.61 C ANISOU 5472 CA ASN D 7 2140 1948 2222 -5 -41 -187 C ATOM 5473 C ASN A 7 36.195 90.100 92.746 1.00 15.66 C ANISOU 5473 C ASN D 7 2061 1770 2117 -33 -57 -199 C ATOM 5474 O ASN A 7 36.407 89.688 93.884 1.00 15.34 O ANISOU 5474 O ASN D 7 2174 1425 2228 -25 -131 -339 O ATOM 5475 CB ASN A 7 37.867 89.436 91.093 1.00 16.60 C ANISOU 5475 CB ASN D 7 2129 1962 2215 -40 -52 -210 C ATOM 5476 CG ASN A 7 38.857 89.789 90.030 1.00 15.69 C ANISOU 5476 CG ASN D 7 1998 1697 2265 86 4 -170 C ATOM 5477 OD1 ASN A 7 39.903 89.103 89.891 1.00 20.05 O ANISOU 5477 OD1 ASN D 7 2209 2559 2848 157 -117 -208 O ATOM 5478 ND2 ASN A 7 38.539 90.791 89.218 1.00 15.24 N ANISOU 5478 ND2 ASN D 7 1804 1826 2159 -72 -138 -329 N ATOM 5479 N LEU A 8 34.995 90.072 92.179 1.00 15.48 N ANISOU 5479 N LEU D 8 2064 1719 2097 13 -99 -242 N ATOM 5480 CA LEU A 8 33.906 89.289 92.714 1.00 14.96 C ANISOU 5480 CA LEU D 8 1961 1712 2010 17 -59 -222 C ATOM 5481 C LEU A 8 33.810 88.035 91.843 1.00 15.04 C ANISOU 5481 C LEU D 8 1974 1763 1974 51 -62 -235 C ATOM 5482 O LEU A 8 33.665 88.140 90.629 1.00 15.54 O ANISOU 5482 O LEU D 8 2155 1789 1961 40 -57 -313 O ATOM 5483 CB LEU A 8 32.584 90.072 92.636 1.00 14.99 C ANISOU 5483 CB LEU D 8 2000 1654 2042 21 -80 -260 C ATOM 5484 CG LEU A 8 31.317 89.316 93.060 1.00 14.51 C ANISOU 5484 CG LEU D 8 1836 1675 2001 12 -32 -222 C ATOM 5485 CD1 LEU A 8 31.490 88.523 94.354 1.00 14.50 C ANISOU 5485 CD1 LEU D 8 1950 1680 1877 -134 -57 -245 C ATOM 5486 CD2 LEU A 8 30.115 90.260 93.128 1.00 16.05 C ANISOU 5486 CD2 LEU D 8 2083 1835 2178 -68 -19 -234 C ATOM 5487 N GLN A 9 33.858 86.886 92.501 1.00 14.88 N ANISOU 5487 N GLN D 9 1974 1679 1999 13 -34 -303 N ATOM 5488 CA GLN A 9 33.729 85.564 91.878 1.00 14.82 C ANISOU 5488 CA GLN D 9 1959 1681 1989 36 -34 -262 C ATOM 5489 C GLN A 9 32.510 84.827 92.449 1.00 14.91 C ANISOU 5489 C GLN D 9 1962 1707 1995 41 -16 -241 C ATOM 5490 O GLN A 9 32.295 84.790 93.667 1.00 14.37 O ANISOU 5490 O GLN D 9 1923 1528 2006 66 -95 -394 O ATOM 5491 CB GLN A 9 35.001 84.770 92.155 1.00 14.48 C ANISOU 5491 CB GLN D 9 1931 1626 1944 10 -30 -334 C ATOM 5492 CG GLN A 9 35.019 83.341 91.623 1.00 12.65 C ANISOU 5492 CG GLN D 9 1766 1368 1671 30 -68 -328 C ATOM 5493 CD GLN A 9 36.394 82.730 91.687 1.00 12.26 C ANISOU 5493 CD GLN D 9 1661 1416 1580 73 -188 -408 C ATOM 5494 OE1 GLN A 9 37.399 83.393 91.407 1.00 13.98 O ANISOU 5494 OE1 GLN D 9 1981 1312 2017 108 -211 -473 O ATOM 5495 NE2 GLN A 9 36.452 81.448 92.042 1.00 12.14 N ANISOU 5495 NE2 GLN D 9 1392 1411 1808 -146 -225 -175 N ATOM 5496 N VAL A 10 31.734 84.205 91.561 1.00 14.96 N ANISOU 5496 N VAL D 10 1983 1689 2011 -23 -57 -245 N ATOM 5497 CA VAL A 10 30.649 83.338 91.983 1.00 15.51 C ANISOU 5497 CA VAL D 10 2010 1884 1999 -5 -51 -148 C ATOM 5498 C VAL A 10 31.102 81.885 91.790 1.00 14.75 C ANISOU 5498 C VAL D 10 1883 1818 1901 -17 -72 -153 C ATOM 5499 O VAL A 10 31.538 81.494 90.688 1.00 15.25 O ANISOU 5499 O VAL D 10 1866 1980 1947 -5 -123 -243 O ATOM 5500 CB VAL A 10 29.335 83.643 91.217 1.00 15.91 C ANISOU 5500 CB VAL D 10 2042 1878 2122 23 -49 -142 C ATOM 5501 CG1 VAL A 10 29.513 83.475 89.709 1.00 16.41 C ANISOU 5501 CG1 VAL D 10 2038 2111 2084 41 -107 -60 C ATOM 5502 CG2 VAL A 10 28.178 82.767 91.702 1.00 15.87 C ANISOU 5502 CG2 VAL D 10 1892 2088 2049 -1 -170 -125 C ATOM 5503 N ALA A 11 30.991 81.110 92.867 1.00 13.48 N ANISOU 5503 N ALA D 11 1691 1625 1803 -79 -14 -131 N ATOM 5504 CA ALA A 11 31.171 79.658 92.855 1.00 13.60 C ANISOU 5504 CA ALA D 11 1686 1667 1813 0 -62 -194 C ATOM 5505 C ALA A 11 29.851 78.968 92.549 1.00 12.93 C ANISOU 5505 C ALA D 11 1571 1590 1749 13 -70 -256 C ATOM 5506 O ALA A 11 28.833 79.250 93.163 1.00 13.20 O ANISOU 5506 O ALA D 11 1668 1538 1809 -8 -171 -482 O ATOM 5507 CB ALA A 11 31.668 79.196 94.190 1.00 13.32 C ANISOU 5507 CB ALA D 11 1604 1620 1835 13 -13 -155 C ATOM 5508 N LEU A 12 29.880 78.028 91.618 1.00 12.52 N ANISOU 5508 N LEU D 12 1545 1603 1608 -30 -101 -235 N ATOM 5509 CA LEU A 12 28.725 77.215 91.287 1.00 12.32 C ANISOU 5509 CA LEU D 12 1477 1632 1570 -45 -59 -145 C ATOM 5510 C LEU A 12 28.975 75.791 91.785 1.00 12.14 C ANISOU 5510 C LEU D 12 1483 1562 1566 -36 -52 -157 C ATOM 5511 O LEU A 12 29.627 74.975 91.106 1.00 11.84 O ANISOU 5511 O LEU D 12 1506 1396 1594 -79 -56 -255 O ATOM 5512 CB LEU A 12 28.495 77.238 89.780 1.00 12.47 C ANISOU 5512 CB LEU D 12 1469 1700 1568 -109 -80 -112 C ATOM 5513 CG LEU A 12 28.468 78.602 89.080 1.00 12.17 C ANISOU 5513 CG LEU D 12 1447 1733 1443 -52 -54 -108 C ATOM 5514 CD1 LEU A 12 28.530 78.425 87.558 1.00 12.05 C ANISOU 5514 CD1 LEU D 12 1467 1730 1382 -103 48 -83 C ATOM 5515 CD2 LEU A 12 27.214 79.410 89.465 1.00 12.41 C ANISOU 5515 CD2 LEU D 12 1392 1722 1597 -53 54 -153 C ATOM 5516 N ASP A 13 28.481 75.490 92.984 1.00 11.46 N ANISOU 5516 N ASP D 13 1473 1443 1439 -35 -86 -176 N ATOM 5517 CA ASP A 13 28.712 74.189 93.607 1.00 12.06 C ANISOU 5517 CA ASP D 13 1528 1529 1526 -73 -97 -143 C ATOM 5518 C ASP A 13 27.466 73.290 93.557 1.00 11.38 C ANISOU 5518 C ASP D 13 1410 1428 1483 -157 -126 -169 C ATOM 5519 O ASP A 13 27.335 72.374 94.363 1.00 11.22 O ANISOU 5519 O ASP D 13 1469 1421 1370 -68 -228 -177 O ATOM 5520 CB ASP A 13 29.209 74.359 95.062 1.00 13.33 C ANISOU 5520 CB ASP D 13 1630 1712 1722 -64 -51 -176 C ATOM 5521 CG ASP A 13 30.454 75.219 95.157 1.00 16.02 C ANISOU 5521 CG ASP D 13 1937 2023 2124 -6 -94 -140 C ATOM 5522 OD1 ASP A 13 31.446 74.910 94.472 1.00 17.52 O ANISOU 5522 OD1 ASP D 13 1926 2516 2211 -22 -232 -344 O ATOM 5523 OD2 ASP A 13 30.497 76.213 95.913 1.00 19.21 O ANISOU 5523 OD2 ASP D 13 2405 2649 2244 154 -101 -553 O ATOM 5524 N HIS A 14 26.594 73.506 92.568 1.00 11.05 N ANISOU 5524 N HIS D 14 1456 1395 1347 -131 -109 -172 N ATOM 5525 CA HIS A 14 25.365 72.706 92.404 1.00 10.78 C ANISOU 5525 CA HIS D 14 1382 1295 1418 -103 -58 -179 C ATOM 5526 C HIS A 14 25.619 71.234 92.059 1.00 10.57 C ANISOU 5526 C HIS D 14 1290 1291 1433 -38 -47 -176 C ATOM 5527 O HIS A 14 26.676 70.895 91.506 1.00 10.93 O ANISOU 5527 O HIS D 14 1293 1409 1451 -31 -148 -361 O ATOM 5528 CB HIS A 14 24.488 73.363 91.350 1.00 11.34 C ANISOU 5528 CB HIS D 14 1415 1450 1442 -35 -12 -168 C ATOM 5529 CG HIS A 14 24.264 74.825 91.612 1.00 12.83 C ANISOU 5529 CG HIS D 14 1583 1566 1726 -73 -30 -135 C ATOM 5530 ND1 HIS A 14 25.170 75.796 91.247 1.00 13.47 N ANISOU 5530 ND1 HIS D 14 1710 1820 1586 -219 -162 39 N ATOM 5531 CD2 HIS A 14 23.277 75.467 92.289 1.00 13.30 C ANISOU 5531 CD2 HIS D 14 1545 1854 1651 -48 -108 -141 C ATOM 5532 CE1 HIS A 14 24.727 76.978 91.644 1.00 14.44 C ANISOU 5532 CE1 HIS D 14 1819 1782 1884 -112 -99 -95 C ATOM 5533 NE2 HIS A 14 23.586 76.802 92.292 1.00 12.83 N ANISOU 5533 NE2 HIS D 14 1553 1696 1623 -170 -145 -122 N ATOM 5534 N SER A 15 24.656 70.381 92.383 1.00 10.67 N ANISOU 5534 N SER D 15 1340 1326 1386 -44 -22 -156 N ATOM 5535 CA SER A 15 24.753 68.945 92.085 1.00 10.79 C ANISOU 5535 CA SER D 15 1394 1307 1398 -73 54 -120 C ATOM 5536 C SER A 15 24.169 68.578 90.744 1.00 11.21 C ANISOU 5536 C SER D 15 1439 1373 1447 -65 49 -154 C ATOM 5537 O SER A 15 24.100 67.396 90.405 1.00 11.75 O ANISOU 5537 O SER D 15 1587 1336 1539 -128 133 -288 O ATOM 5538 CB SER A 15 24.121 68.086 93.186 1.00 11.45 C ANISOU 5538 CB SER D 15 1445 1494 1409 -69 39 -119 C ATOM 5539 OG SER A 15 24.852 68.244 94.388 1.00 11.83 O ANISOU 5539 OG SER D 15 1496 1443 1554 -204 187 -311 O ATOM 5540 N ASN A 16 23.774 69.576 89.963 1.00 11.62 N ANISOU 5540 N ASN D 16 1509 1471 1433 -67 61 -179 N ATOM 5541 CA ASN A 16 23.279 69.307 88.613 1.00 11.66 C ANISOU 5541 CA ASN D 16 1483 1468 1480 -52 31 -117 C ATOM 5542 C ASN A 16 23.561 70.468 87.651 1.00 10.97 C ANISOU 5542 C ASN D 16 1374 1342 1450 -60 51 -123 C ATOM 5543 O ASN A 16 23.883 71.584 88.062 1.00 11.63 O ANISOU 5543 O ASN D 16 1509 1407 1502 -100 -54 -249 O ATOM 5544 CB ASN A 16 21.789 68.945 88.621 1.00 11.50 C ANISOU 5544 CB ASN D 16 1534 1306 1527 51 52 -142 C ATOM 5545 CG ASN A 16 20.940 69.946 89.368 1.00 12.87 C ANISOU 5545 CG ASN D 16 1513 1622 1752 -84 -48 -9 C ATOM 5546 OD1 ASN A 16 21.135 71.154 89.253 1.00 11.49 O ANISOU 5546 OD1 ASN D 16 1442 1356 1566 -159 -78 10 O ATOM 5547 ND2 ASN A 16 19.974 69.447 90.122 1.00 16.38 N ANISOU 5547 ND2 ASN D 16 1976 1945 2299 -43 -96 200 N ATOM 5548 N LEU A 17 23.439 70.195 86.360 1.00 10.52 N ANISOU 5548 N LEU D 17 1295 1280 1422 -89 -11 -200 N ATOM 5549 CA LEU A 17 23.722 71.168 85.332 1.00 10.65 C ANISOU 5549 CA LEU D 17 1353 1277 1416 -62 52 -186 C ATOM 5550 C LEU A 17 22.770 72.369 85.436 1.00 11.16 C ANISOU 5550 C LEU D 17 1511 1246 1482 -38 0 -156 C ATOM 5551 O LEU A 17 23.209 73.522 85.367 1.00 10.73 O ANISOU 5551 O LEU D 17 1583 1116 1379 56 -84 -298 O ATOM 5552 CB LEU A 17 23.659 70.522 83.938 1.00 11.27 C ANISOU 5552 CB LEU D 17 1417 1325 1539 -106 12 -181 C ATOM 5553 CG LEU A 17 23.943 71.459 82.761 1.00 12.80 C ANISOU 5553 CG LEU D 17 1533 1767 1562 -2 -32 -247 C ATOM 5554 CD1 LEU A 17 25.343 72.055 82.824 1.00 14.22 C ANISOU 5554 CD1 LEU D 17 1750 1864 1785 94 -132 -166 C ATOM 5555 CD2 LEU A 17 23.731 70.702 81.421 1.00 14.45 C ANISOU 5555 CD2 LEU D 17 1773 1865 1851 78 -91 -386 C ATOM 5556 N LYS A 18 21.482 72.106 85.592 1.00 11.24 N ANISOU 5556 N LYS D 18 1511 1251 1507 -25 22 -125 N ATOM 5557 CA LYS A 18 20.500 73.190 85.541 1.00 11.69 C ANISOU 5557 CA LYS D 18 1564 1354 1524 -45 35 -95 C ATOM 5558 C LYS A 18 20.760 74.187 86.660 1.00 11.50 C ANISOU 5558 C LYS D 18 1573 1300 1497 -66 29 -102 C ATOM 5559 O LYS A 18 20.572 75.374 86.468 1.00 12.13 O ANISOU 5559 O LYS D 18 1753 1218 1635 -60 -7 -137 O ATOM 5560 CB LYS A 18 19.071 72.689 85.612 1.00 12.33 C ANISOU 5560 CB LYS D 18 1582 1585 1517 -61 7 -64 C ATOM 5561 CG LYS A 18 18.667 71.949 86.888 1.00 13.00 C ANISOU 5561 CG LYS D 18 1573 1575 1790 160 -13 -112 C ATOM 5562 CD LYS A 18 17.203 71.510 86.850 1.00 14.30 C ANISOU 5562 CD LYS D 18 1534 1993 1906 62 -20 -56 C ATOM 5563 CE LYS A 18 16.728 71.004 88.178 1.00 16.17 C ANISOU 5563 CE LYS D 18 1901 2200 2041 209 95 -113 C ATOM 5564 NZ LYS A 18 15.336 70.476 88.092 1.00 17.43 N ANISOU 5564 NZ LYS D 18 2077 2324 2220 138 -28 -24 N ATOM 5565 N GLY A 19 21.208 73.705 87.809 1.00 11.09 N ANISOU 5565 N GLY D 19 1527 1196 1487 -45 56 -138 N ATOM 5566 CA GLY A 19 21.415 74.578 88.955 1.00 11.32 C ANISOU 5566 CA GLY D 19 1542 1330 1427 -60 53 -134 C ATOM 5567 C GLY A 19 22.583 75.511 88.694 1.00 11.40 C ANISOU 5567 C GLY D 19 1543 1318 1471 -59 21 -153 C ATOM 5568 O GLY A 19 22.490 76.711 88.920 1.00 11.79 O ANISOU 5568 O GLY D 19 1687 1257 1536 -83 3 -190 O ATOM 5569 N ALA A 20 23.680 74.968 88.177 1.00 11.12 N ANISOU 5569 N ALA D 20 1429 1367 1428 -75 22 -120 N ATOM 5570 CA ALA A 20 24.846 75.781 87.856 1.00 11.05 C ANISOU 5570 CA ALA D 20 1415 1332 1450 -41 19 -135 C ATOM 5571 C ALA A 20 24.551 76.804 86.771 1.00 11.09 C ANISOU 5571 C ALA D 20 1401 1279 1532 -65 45 -154 C ATOM 5572 O ALA A 20 24.943 77.955 86.893 1.00 11.18 O ANISOU 5572 O ALA D 20 1428 1213 1603 -50 95 -245 O ATOM 5573 CB ALA A 20 26.050 74.905 87.446 1.00 10.76 C ANISOU 5573 CB ALA D 20 1361 1276 1451 -47 -18 -145 C ATOM 5574 N ILE A 21 23.858 76.391 85.710 1.00 10.88 N ANISOU 5574 N ILE D 21 1370 1261 1504 -100 84 -149 N ATOM 5575 CA ILE A 21 23.612 77.286 84.584 1.00 11.05 C ANISOU 5575 CA ILE D 21 1382 1291 1522 -49 34 -127 C ATOM 5576 C ILE A 21 22.669 78.411 84.983 1.00 10.87 C ANISOU 5576 C ILE D 21 1288 1260 1582 -24 51 -180 C ATOM 5577 O ILE A 21 22.898 79.569 84.628 1.00 11.57 O ANISOU 5577 O ILE D 21 1284 1343 1767 -66 105 -174 O ATOM 5578 CB ILE A 21 23.057 76.525 83.342 1.00 10.82 C ANISOU 5578 CB ILE D 21 1301 1284 1524 -33 58 -82 C ATOM 5579 CG1 ILE A 21 24.113 75.543 82.820 1.00 12.73 C ANISOU 5579 CG1 ILE D 21 1524 1594 1716 -85 59 -72 C ATOM 5580 CG2 ILE A 21 22.622 77.490 82.244 1.00 12.36 C ANISOU 5580 CG2 ILE D 21 1659 1518 1517 -10 -47 -3 C ATOM 5581 CD1 ILE A 21 25.408 76.192 82.481 1.00 15.82 C ANISOU 5581 CD1 ILE D 21 2105 1877 2026 24 -116 -64 C ATOM 5582 N THR A 22 21.636 78.062 85.742 1.00 10.68 N ANISOU 5582 N THR D 22 1361 1164 1530 -77 -15 -289 N ATOM 5583 CA THR A 22 20.635 79.051 86.146 1.00 11.37 C ANISOU 5583 CA THR D 22 1431 1291 1596 -55 -41 -289 C ATOM 5584 C THR A 22 21.263 80.075 87.088 1.00 11.34 C ANISOU 5584 C THR D 22 1444 1252 1610 -33 -42 -234 C ATOM 5585 O THR A 22 21.015 81.275 86.953 1.00 11.49 O ANISOU 5585 O THR D 22 1617 972 1775 -33 11 -319 O ATOM 5586 CB THR A 22 19.443 78.360 86.793 1.00 11.28 C ANISOU 5586 CB THR D 22 1416 1261 1609 -8 -52 -315 C ATOM 5587 OG1 THR A 22 18.819 77.486 85.833 1.00 12.96 O ANISOU 5587 OG1 THR D 22 1542 1587 1792 64 -102 -547 O ATOM 5588 CG2 THR A 22 18.396 79.365 87.239 1.00 12.67 C ANISOU 5588 CG2 THR D 22 1536 1416 1859 -76 -69 -313 C ATOM 5589 N ALA A 23 22.069 79.609 88.028 1.00 12.15 N ANISOU 5589 N ALA D 23 1598 1383 1633 -9 -35 -250 N ATOM 5590 CA ALA A 23 22.751 80.531 88.924 1.00 11.91 C ANISOU 5590 CA ALA D 23 1575 1355 1594 -28 -29 -250 C ATOM 5591 C ALA A 23 23.726 81.424 88.173 1.00 12.25 C ANISOU 5591 C ALA D 23 1609 1414 1628 -42 -79 -210 C ATOM 5592 O ALA A 23 23.779 82.622 88.419 1.00 13.12 O ANISOU 5592 O ALA D 23 1726 1495 1762 -42 -44 -351 O ATOM 5593 CB ALA A 23 23.459 79.795 90.033 1.00 12.17 C ANISOU 5593 CB ALA D 23 1650 1376 1596 -75 -40 -249 C ATOM 5594 N ALA A 24 24.530 80.836 87.286 1.00 12.38 N ANISOU 5594 N ALA D 24 1604 1489 1611 -1 -39 -187 N ATOM 5595 CA ALA A 24 25.487 81.604 86.506 1.00 12.42 C ANISOU 5595 CA ALA D 24 1546 1460 1710 -5 -26 -137 C ATOM 5596 C ALA A 24 24.803 82.716 85.733 1.00 12.63 C ANISOU 5596 C ALA D 24 1580 1452 1764 18 7 -117 C ATOM 5597 O ALA A 24 25.273 83.848 85.732 1.00 13.06 O ANISOU 5597 O ALA D 24 1675 1329 1957 -96 -22 -240 O ATOM 5598 CB ALA A 24 26.242 80.687 85.543 1.00 12.33 C ANISOU 5598 CB ALA D 24 1533 1491 1660 49 -51 -115 C ATOM 5599 N VAL A 25 23.680 82.404 85.082 1.00 13.48 N ANISOU 5599 N VAL D 25 1684 1593 1845 -67 19 -125 N ATOM 5600 CA VAL A 25 22.974 83.405 84.291 1.00 14.17 C ANISOU 5600 CA VAL D 25 1817 1702 1862 -77 32 -109 C ATOM 5601 C VAL A 25 22.382 84.500 85.204 1.00 14.43 C ANISOU 5601 C VAL D 25 1819 1739 1924 -91 5 -94 C ATOM 5602 O VAL A 25 22.353 85.675 84.838 1.00 14.38 O ANISOU 5602 O VAL D 25 1780 1696 1985 -46 42 -91 O ATOM 5603 CB VAL A 25 21.925 82.740 83.406 1.00 14.24 C ANISOU 5603 CB VAL D 25 1801 1721 1886 -114 34 -120 C ATOM 5604 CG1 VAL A 25 20.978 83.760 82.750 1.00 14.08 C ANISOU 5604 CG1 VAL D 25 1900 1722 1725 -179 106 -64 C ATOM 5605 CG2 VAL A 25 22.640 81.891 82.341 1.00 13.62 C ANISOU 5605 CG2 VAL D 25 1790 1609 1773 -37 -90 -167 C ATOM 5606 N SER A 26 21.940 84.118 86.398 1.00 14.69 N ANISOU 5606 N SER D 26 1870 1757 1952 -66 -3 -137 N ATOM 5607 CA SER A 26 21.310 85.089 87.304 1.00 15.06 C ANISOU 5607 CA SER D 26 2004 1674 2042 -65 -14 -196 C ATOM 5608 C SER A 26 22.265 86.214 87.755 1.00 16.06 C ANISOU 5608 C SER D 26 2041 1828 2230 -51 -18 -155 C ATOM 5609 O SER A 26 21.806 87.333 88.058 1.00 17.42 O ANISOU 5609 O SER D 26 2314 1861 2441 -96 -31 -153 O ATOM 5610 CB SER A 26 20.691 84.395 88.517 1.00 14.40 C ANISOU 5610 CB SER D 26 1931 1544 1994 -81 21 -196 C ATOM 5611 OG SER A 26 21.670 83.961 89.450 1.00 15.51 O ANISOU 5611 OG SER D 26 2344 1591 1958 -104 -45 -332 O ATOM 5612 N VAL A 27 23.565 85.925 87.831 1.00 16.91 N ANISOU 5612 N VAL D 27 2105 1992 2325 6 -29 -181 N ATOM 5613 CA VAL A 27 24.536 86.913 88.357 1.00 17.43 C ANISOU 5613 CA VAL D 27 2203 2023 2394 17 -40 -135 C ATOM 5614 C VAL A 27 25.700 87.220 87.420 1.00 18.43 C ANISOU 5614 C VAL D 27 2315 2160 2525 60 -50 -147 C ATOM 5615 O VAL A 27 26.497 88.101 87.713 1.00 17.93 O ANISOU 5615 O VAL D 27 2369 1833 2609 89 -100 -245 O ATOM 5616 CB VAL A 27 25.122 86.483 89.729 1.00 16.88 C ANISOU 5616 CB VAL D 27 2148 1983 2282 32 -23 -151 C ATOM 5617 CG1 VAL A 27 24.038 86.291 90.759 1.00 17.08 C ANISOU 5617 CG1 VAL D 27 2228 1900 2358 -53 -4 -163 C ATOM 5618 CG2 VAL A 27 25.955 85.205 89.604 1.00 17.88 C ANISOU 5618 CG2 VAL D 27 2171 2262 2358 -28 -19 -94 C ATOM 5619 N GLY A 28 25.784 86.528 86.282 1.00 19.65 N ANISOU 5619 N GLY D 28 2478 2338 2648 58 -56 -148 N ATOM 5620 CA GLY A 28 26.974 86.585 85.422 1.00 21.31 C ANISOU 5620 CA GLY D 28 2702 2593 2801 52 -51 -86 C ATOM 5621 C GLY A 28 27.437 87.966 84.997 1.00 22.34 C ANISOU 5621 C GLY D 28 2834 2711 2942 40 -35 -74 C ATOM 5622 O GLY A 28 28.633 88.243 85.015 1.00 22.57 O ANISOU 5622 O GLY D 28 2862 2661 3050 33 -46 -129 O ATOM 5623 N ASN A 29 26.488 88.818 84.616 1.00 23.59 N ANISOU 5623 N ASN D 29 3026 2901 3034 39 26 -58 N ATOM 5624 CA ASN A 29 26.770 90.199 84.225 1.00 24.55 C ANISOU 5624 CA ASN D 29 3169 3048 3110 32 3 -9 C ATOM 5625 C ASN A 29 27.344 91.047 85.360 1.00 23.72 C ANISOU 5625 C ASN D 29 3023 2948 3039 32 -5 -3 C ATOM 5626 O ASN A 29 27.997 92.054 85.104 1.00 23.92 O ANISOU 5626 O ASN D 29 3062 2921 3106 22 -46 32 O ATOM 5627 CB ASN A 29 25.490 90.879 83.704 1.00 25.59 C ANISOU 5627 CB ASN D 29 3299 3165 3256 21 20 -22 C ATOM 5628 CG ASN A 29 25.097 90.419 82.299 1.00 29.99 C ANISOU 5628 CG ASN D 29 3851 3862 3681 -41 36 -18 C ATOM 5629 OD1 ASN A 29 25.853 89.709 81.612 1.00 33.30 O ANISOU 5629 OD1 ASN D 29 4408 4217 4027 -103 -23 -100 O ATOM 5630 ND2 ASN A 29 23.906 90.830 81.861 1.00 33.00 N ANISOU 5630 ND2 ASN D 29 4138 4294 4105 -137 72 10 N ATOM 5631 N GLU A 30 27.067 90.656 86.604 1.00 22.37 N ANISOU 5631 N GLU D 30 2851 2775 2872 -12 28 -23 N ATOM 5632 CA GLU A 30 27.478 91.433 87.778 1.00 21.70 C ANISOU 5632 CA GLU D 30 2761 2655 2827 -18 33 -50 C ATOM 5633 C GLU A 30 28.812 91.021 88.385 1.00 21.01 C ANISOU 5633 C GLU D 30 2713 2534 2735 -2 69 -111 C ATOM 5634 O GLU A 30 29.374 91.769 89.189 1.00 22.41 O ANISOU 5634 O GLU D 30 2888 2643 2981 -51 96 -237 O ATOM 5635 CB GLU A 30 26.391 91.384 88.862 1.00 21.74 C ANISOU 5635 CB GLU D 30 2812 2662 2784 -13 49 -24 C ATOM 5636 CG GLU A 30 25.024 91.863 88.393 1.00 24.27 C ANISOU 5636 CG GLU D 30 3042 2935 3242 -55 23 -10 C ATOM 5637 CD GLU A 30 25.060 93.278 87.832 1.00 26.92 C ANISOU 5637 CD GLU D 30 3460 3176 3592 -24 33 42 C ATOM 5638 OE1 GLU A 30 25.841 94.100 88.354 1.00 28.70 O ANISOU 5638 OE1 GLU D 30 3612 3370 3921 -53 22 -18 O ATOM 5639 OE2 GLU A 30 24.312 93.562 86.876 1.00 28.30 O ANISOU 5639 OE2 GLU D 30 3788 3237 3725 -112 33 157 O ATOM 5640 N VAL A 31 29.323 89.846 88.013 1.00 19.84 N ANISOU 5640 N VAL D 31 2577 2368 2590 26 50 -134 N ATOM 5641 CA VAL A 31 30.567 89.320 88.578 1.00 18.39 C ANISOU 5641 CA VAL D 31 2441 2167 2377 52 9 -128 C ATOM 5642 C VAL A 31 31.726 89.395 87.573 1.00 17.84 C ANISOU 5642 C VAL D 31 2401 2068 2310 60 10 -161 C ATOM 5643 O VAL A 31 31.509 89.582 86.372 1.00 17.99 O ANISOU 5643 O VAL D 31 2404 2130 2299 53 2 -167 O ATOM 5644 CB VAL A 31 30.397 87.872 89.101 1.00 18.33 C ANISOU 5644 CB VAL D 31 2387 2207 2369 16 34 -111 C ATOM 5645 CG1 VAL A 31 29.216 87.770 90.066 1.00 18.27 C ANISOU 5645 CG1 VAL D 31 2366 2179 2397 0 -13 -174 C ATOM 5646 CG2 VAL A 31 30.240 86.895 87.937 1.00 18.16 C ANISOU 5646 CG2 VAL D 31 2411 2126 2360 -26 -18 -167 C ATOM 5647 N ASP A 32 32.946 89.279 88.087 1.00 17.19 N ANISOU 5647 N ASP D 32 2339 1997 2195 15 -19 -186 N ATOM 5648 CA ASP A 32 34.167 89.278 87.291 1.00 17.57 C ANISOU 5648 CA ASP D 32 2328 2081 2265 61 1 -149 C ATOM 5649 C ASP A 32 34.650 87.862 86.954 1.00 17.16 C ANISOU 5649 C ASP D 32 2234 2052 2233 37 -42 -156 C ATOM 5650 O ASP A 32 35.313 87.660 85.926 1.00 17.68 O ANISOU 5650 O ASP D 32 2248 2112 2356 109 -57 -264 O ATOM 5651 CB ASP A 32 35.281 89.999 88.038 1.00 18.13 C ANISOU 5651 CB ASP D 32 2403 2156 2327 0 9 -151 C ATOM 5652 CG ASP A 32 34.841 91.341 88.551 1.00 18.50 C ANISOU 5652 CG ASP D 32 2608 2071 2347 13 22 -109 C ATOM 5653 OD1 ASP A 32 34.527 92.194 87.703 1.00 19.83 O ANISOU 5653 OD1 ASP D 32 3005 1956 2571 -66 113 -43 O ATOM 5654 OD2 ASP A 32 34.774 91.558 89.784 1.00 19.53 O ANISOU 5654 OD2 ASP D 32 2848 2040 2532 -152 -104 -296 O ATOM 5655 N VAL A 33 34.337 86.901 87.819 1.00 15.89 N ANISOU 5655 N VAL D 33 2076 1808 2153 5 -12 -123 N ATOM 5656 CA VAL A 33 34.826 85.527 87.651 1.00 15.35 C ANISOU 5656 CA VAL D 33 1998 1831 2001 8 -83 -137 C ATOM 5657 C VAL A 33 33.701 84.524 87.911 1.00 14.72 C ANISOU 5657 C VAL D 33 1964 1691 1938 25 -130 -180 C ATOM 5658 O VAL A 33 32.961 84.657 88.882 1.00 13.21 O ANISOU 5658 O VAL D 33 1812 1388 1818 83 -265 -262 O ATOM 5659 CB VAL A 33 35.985 85.229 88.622 1.00 15.89 C ANISOU 5659 CB VAL D 33 2037 1858 2142 7 -41 -83 C ATOM 5660 CG1 VAL A 33 36.558 83.830 88.358 1.00 15.46 C ANISOU 5660 CG1 VAL D 33 2033 1896 1943 -74 -15 -130 C ATOM 5661 CG2 VAL A 33 37.098 86.278 88.531 1.00 15.00 C ANISOU 5661 CG2 VAL D 33 2018 1819 1860 49 -198 -196 C ATOM 5662 N ILE A 34 33.574 83.513 87.047 1.00 13.20 N ANISOU 5662 N ILE D 34 1728 1529 1757 -37 -144 -224 N ATOM 5663 CA ILE A 34 32.569 82.456 87.226 1.00 14.06 C ANISOU 5663 CA ILE D 34 1809 1678 1854 -46 -119 -146 C ATOM 5664 C ILE A 34 33.275 81.121 87.356 1.00 13.13 C ANISOU 5664 C ILE D 34 1696 1544 1749 18 -95 -153 C ATOM 5665 O ILE A 34 34.120 80.789 86.539 1.00 14.05 O ANISOU 5665 O ILE D 34 1812 1648 1877 -9 -149 -283 O ATOM 5666 CB ILE A 34 31.565 82.426 86.065 1.00 14.11 C ANISOU 5666 CB ILE D 34 1851 1642 1867 -20 -88 -102 C ATOM 5667 CG1 ILE A 34 30.918 83.804 85.911 1.00 16.63 C ANISOU 5667 CG1 ILE D 34 2136 1985 2197 -92 -90 -92 C ATOM 5668 CG2 ILE A 34 30.479 81.367 86.298 1.00 15.35 C ANISOU 5668 CG2 ILE D 34 1865 2007 1959 -28 -62 -102 C ATOM 5669 CD1 ILE A 34 30.276 84.011 84.608 1.00 19.48 C ANISOU 5669 CD1 ILE D 34 2491 2367 2542 -57 -2 -39 C ATOM 5670 N GLU A 35 32.931 80.395 88.406 1.00 12.75 N ANISOU 5670 N GLU D 35 1685 1546 1612 -4 -73 -125 N ATOM 5671 CA GLU A 35 33.623 79.168 88.790 1.00 12.25 C ANISOU 5671 CA GLU D 35 1568 1495 1589 6 -135 -154 C ATOM 5672 C GLU A 35 32.697 77.958 88.767 1.00 12.04 C ANISOU 5672 C GLU D 35 1520 1535 1520 59 -129 -209 C ATOM 5673 O GLU A 35 31.693 77.913 89.475 1.00 11.93 O ANISOU 5673 O GLU D 35 1504 1450 1577 65 -218 -321 O ATOM 5674 CB GLU A 35 34.228 79.327 90.182 1.00 12.57 C ANISOU 5674 CB GLU D 35 1616 1604 1554 37 -101 -72 C ATOM 5675 CG GLU A 35 34.777 78.043 90.775 1.00 13.11 C ANISOU 5675 CG GLU D 35 1699 1589 1690 -127 -84 -207 C ATOM 5676 CD GLU A 35 35.483 78.203 92.101 1.00 16.14 C ANISOU 5676 CD GLU D 35 2214 1892 2026 -180 0 -308 C ATOM 5677 OE1 GLU A 35 34.998 79.007 92.941 1.00 14.45 O ANISOU 5677 OE1 GLU D 35 1795 1819 1875 -234 -170 -425 O ATOM 5678 OE2 GLU A 35 36.534 77.522 92.298 1.00 16.49 O ANISOU 5678 OE2 GLU D 35 2180 1865 2221 -255 -83 -400 O ATOM 5679 N ALA A 36 33.060 76.991 87.934 1.00 10.71 N ANISOU 5679 N ALA D 36 1306 1347 1416 -20 -93 -217 N ATOM 5680 CA ALA A 36 32.481 75.655 87.956 1.00 10.97 C ANISOU 5680 CA ALA D 36 1388 1387 1393 -1 -59 -169 C ATOM 5681 C ALA A 36 33.084 74.897 89.116 1.00 10.57 C ANISOU 5681 C ALA D 36 1276 1370 1368 -40 -21 -200 C ATOM 5682 O ALA A 36 34.250 74.479 89.056 1.00 11.18 O ANISOU 5682 O ALA D 36 1338 1536 1373 -112 -93 -246 O ATOM 5683 CB ALA A 36 32.768 74.918 86.638 1.00 10.90 C ANISOU 5683 CB ALA D 36 1337 1451 1353 -6 -50 -188 C ATOM 5684 N GLY A 37 32.303 74.748 90.185 1.00 10.30 N ANISOU 5684 N GLY D 37 1354 1278 1279 -53 -36 -230 N ATOM 5685 CA GLY A 37 32.779 74.154 91.416 1.00 10.01 C ANISOU 5685 CA GLY D 37 1239 1264 1299 -67 -43 -235 C ATOM 5686 C GLY A 37 33.012 72.660 91.329 1.00 9.84 C ANISOU 5686 C GLY D 37 1213 1242 1283 -55 -72 -200 C ATOM 5687 O GLY A 37 32.408 71.988 90.476 1.00 9.80 O ANISOU 5687 O GLY D 37 1059 1302 1361 -51 -67 -402 O ATOM 5688 N THR A 38 33.838 72.126 92.227 1.00 10.32 N ANISOU 5688 N THR D 38 1250 1426 1244 28 -18 -286 N ATOM 5689 CA THR A 38 34.173 70.695 92.191 1.00 10.41 C ANISOU 5689 CA THR D 38 1318 1379 1256 -51 -27 -153 C ATOM 5690 C THR A 38 32.954 69.769 92.288 1.00 10.80 C ANISOU 5690 C THR D 38 1339 1448 1315 -46 -100 -188 C ATOM 5691 O THR A 38 32.842 68.777 91.564 1.00 10.64 O ANISOU 5691 O THR D 38 1306 1491 1247 -12 -22 -222 O ATOM 5692 CB THR A 38 35.180 70.304 93.290 1.00 11.56 C ANISOU 5692 CB THR D 38 1426 1595 1371 -54 -52 -166 C ATOM 5693 OG1 THR A 38 36.190 71.298 93.384 1.00 12.06 O ANISOU 5693 OG1 THR D 38 1594 1625 1361 45 35 -269 O ATOM 5694 CG2 THR A 38 35.887 69.001 92.952 1.00 11.16 C ANISOU 5694 CG2 THR D 38 1436 1357 1444 -54 30 -157 C ATOM 5695 N VAL A 39 32.028 70.096 93.184 1.00 10.72 N ANISOU 5695 N VAL D 39 1379 1391 1301 -96 -110 -208 N ATOM 5696 CA VAL A 39 30.832 69.276 93.363 1.00 10.75 C ANISOU 5696 CA VAL D 39 1352 1409 1323 -100 -114 -165 C ATOM 5697 C VAL A 39 30.092 69.164 92.024 1.00 10.44 C ANISOU 5697 C VAL D 39 1288 1399 1278 -66 -113 -180 C ATOM 5698 O VAL A 39 29.634 68.061 91.651 1.00 10.06 O ANISOU 5698 O VAL D 39 1209 1350 1263 -64 -50 -180 O ATOM 5699 CB VAL A 39 29.901 69.896 94.436 1.00 11.78 C ANISOU 5699 CB VAL D 39 1503 1599 1371 -71 -119 -143 C ATOM 5700 CG1 VAL A 39 28.507 69.245 94.410 1.00 11.91 C ANISOU 5700 CG1 VAL D 39 1539 1649 1334 -69 -106 -180 C ATOM 5701 CG2 VAL A 39 30.547 69.788 95.792 1.00 12.50 C ANISOU 5701 CG2 VAL D 39 1482 1688 1577 -246 -82 -86 C ATOM 5702 N CYS A 40 30.006 70.280 91.298 1.00 10.05 N ANISOU 5702 N CYS D 40 1167 1372 1279 -101 -84 -197 N ATOM 5703 CA CYS A 40 29.322 70.312 90.006 1.00 10.78 C ANISOU 5703 CA CYS D 40 1308 1421 1367 -65 -99 -175 C ATOM 5704 C CYS A 40 30.081 69.569 88.918 1.00 9.99 C ANISOU 5704 C CYS D 40 1180 1341 1275 -44 -86 -203 C ATOM 5705 O CYS A 40 29.495 68.741 88.228 1.00 9.23 O ANISOU 5705 O CYS D 40 1177 1055 1273 -25 -108 -223 O ATOM 5706 CB CYS A 40 29.007 71.738 89.557 1.00 11.65 C ANISOU 5706 CB CYS D 40 1400 1526 1499 -71 -69 -171 C ATOM 5707 SG CYS A 40 27.673 71.811 88.340 1.00 13.06 S ANISOU 5707 SG CYS D 40 1684 1734 1543 -261 -117 -405 S ATOM 5708 N LEU A 41 31.379 69.826 88.799 1.00 9.38 N ANISOU 5708 N LEU D 41 1168 1269 1127 -106 -76 -237 N ATOM 5709 CA LEU A 41 32.184 69.086 87.791 1.00 8.98 C ANISOU 5709 CA LEU D 41 1063 1340 1008 -110 -81 -158 C ATOM 5710 C LEU A 41 32.125 67.573 87.988 1.00 9.59 C ANISOU 5710 C LEU D 41 1147 1399 1097 -85 -50 -116 C ATOM 5711 O LEU A 41 32.061 66.814 87.025 1.00 9.39 O ANISOU 5711 O LEU D 41 1234 1237 1094 -201 -71 -182 O ATOM 5712 CB LEU A 41 33.634 69.598 87.759 1.00 9.03 C ANISOU 5712 CB LEU D 41 1068 1395 968 -46 -8 -147 C ATOM 5713 CG LEU A 41 33.804 71.022 87.238 1.00 9.44 C ANISOU 5713 CG LEU D 41 1020 1439 1127 -125 -17 -201 C ATOM 5714 CD1 LEU A 41 35.236 71.464 87.505 1.00 10.53 C ANISOU 5714 CD1 LEU D 41 1167 1483 1350 -36 -56 -236 C ATOM 5715 CD2 LEU A 41 33.462 71.148 85.766 1.00 11.52 C ANISOU 5715 CD2 LEU D 41 1422 1619 1334 -67 -20 51 C ATOM 5716 N LEU A 42 32.166 67.125 89.236 1.00 9.26 N ANISOU 5716 N LEU D 42 1204 1249 1065 -182 -97 -21 N ATOM 5717 CA LEU A 42 32.123 65.680 89.507 1.00 9.47 C ANISOU 5717 CA LEU D 42 1244 1243 1111 -77 -70 -119 C ATOM 5718 C LEU A 42 30.770 65.094 89.114 1.00 9.22 C ANISOU 5718 C LEU D 42 1213 1084 1207 -82 -39 -129 C ATOM 5719 O LEU A 42 30.678 63.909 88.769 1.00 9.91 O ANISOU 5719 O LEU D 42 1431 1189 1145 -125 -5 -290 O ATOM 5720 CB LEU A 42 32.477 65.363 90.957 1.00 9.25 C ANISOU 5720 CB LEU D 42 1162 1280 1072 -63 -24 -108 C ATOM 5721 CG LEU A 42 33.938 65.596 91.365 1.00 9.07 C ANISOU 5721 CG LEU D 42 1123 1253 1068 -148 -55 -197 C ATOM 5722 CD1 LEU A 42 34.040 65.529 92.858 1.00 9.54 C ANISOU 5722 CD1 LEU D 42 997 1457 1170 -129 -71 -49 C ATOM 5723 CD2 LEU A 42 34.865 64.578 90.703 1.00 10.34 C ANISOU 5723 CD2 LEU D 42 1297 1307 1325 -14 24 -207 C ATOM 5724 N GLN A 43 29.729 65.935 89.097 1.00 10.34 N ANISOU 5724 N GLN D 43 1353 1248 1328 -105 -11 -128 N ATOM 5725 CA GLN A 43 28.409 65.489 88.689 1.00 9.97 C ANISOU 5725 CA GLN D 43 1247 1178 1362 -106 -113 -96 C ATOM 5726 C GLN A 43 28.184 65.513 87.177 1.00 10.48 C ANISOU 5726 C GLN D 43 1255 1306 1422 -80 -107 -81 C ATOM 5727 O GLN A 43 27.605 64.567 86.620 1.00 10.25 O ANISOU 5727 O GLN D 43 1303 1180 1409 -81 -144 -165 O ATOM 5728 CB GLN A 43 27.320 66.314 89.383 1.00 10.99 C ANISOU 5728 CB GLN D 43 1356 1387 1430 -123 -102 -72 C ATOM 5729 CG GLN A 43 27.032 65.872 90.779 1.00 10.17 C ANISOU 5729 CG GLN D 43 1431 1135 1296 -59 -218 -165 C ATOM 5730 CD GLN A 43 26.359 64.506 90.847 1.00 10.07 C ANISOU 5730 CD GLN D 43 1292 1191 1342 -90 -153 -182 C ATOM 5731 OE1 GLN A 43 27.030 63.486 90.879 1.00 9.46 O ANISOU 5731 OE1 GLN D 43 1123 1258 1210 -146 -269 -156 O ATOM 5732 NE2 GLN A 43 25.013 64.490 90.900 1.00 9.82 N ANISOU 5732 NE2 GLN D 43 1058 1369 1300 -84 -219 -169 N ATOM 5733 N VAL A 44 28.651 66.572 86.515 1.00 9.46 N ANISOU 5733 N VAL D 44 1172 1050 1370 -127 -100 -112 N ATOM 5734 CA VAL A 44 28.250 66.847 85.138 1.00 9.64 C ANISOU 5734 CA VAL D 44 1243 1147 1272 -67 -72 -75 C ATOM 5735 C VAL A 44 29.384 66.742 84.111 1.00 9.70 C ANISOU 5735 C VAL D 44 1248 1186 1249 -102 -4 -133 C ATOM 5736 O VAL A 44 29.136 66.641 82.916 1.00 10.30 O ANISOU 5736 O VAL D 44 1476 1239 1197 -163 -121 -187 O ATOM 5737 CB VAL A 44 27.551 68.215 85.035 1.00 11.07 C ANISOU 5737 CB VAL D 44 1348 1430 1428 -87 -22 -14 C ATOM 5738 CG1 VAL A 44 26.458 68.311 86.122 1.00 10.97 C ANISOU 5738 CG1 VAL D 44 1400 1253 1514 -152 -133 -4 C ATOM 5739 CG2 VAL A 44 28.532 69.364 85.178 1.00 10.23 C ANISOU 5739 CG2 VAL D 44 1460 1125 1303 -212 -77 -28 C ATOM 5740 N GLY A 45 30.617 66.731 84.579 1.00 9.45 N ANISOU 5740 N GLY D 45 1271 1155 1165 -15 5 -209 N ATOM 5741 CA GLY A 45 31.744 66.706 83.675 1.00 9.39 C ANISOU 5741 CA GLY D 45 1180 1165 1219 -32 -12 -93 C ATOM 5742 C GLY A 45 32.093 68.074 83.113 1.00 9.29 C ANISOU 5742 C GLY D 45 1219 1016 1292 -73 -74 -93 C ATOM 5743 O GLY A 45 31.510 69.099 83.500 1.00 9.97 O ANISOU 5743 O GLY D 45 1254 1052 1482 -125 -56 -162 O ATOM 5744 N SER A 46 33.093 68.094 82.240 1.00 8.86 N ANISOU 5744 N SER D 46 1171 931 1262 -33 -71 -6 N ATOM 5745 CA SER A 46 33.728 69.330 81.809 1.00 8.21 C ANISOU 5745 CA SER D 46 1089 859 1170 -3 -90 -107 C ATOM 5746 C SER A 46 32.965 70.104 80.764 1.00 8.78 C ANISOU 5746 C SER D 46 1151 993 1191 54 -85 -115 C ATOM 5747 O SER A 46 33.358 71.239 80.461 1.00 8.83 O ANISOU 5747 O SER D 46 1193 946 1215 16 -129 -81 O ATOM 5748 CB SER A 46 35.146 69.054 81.333 1.00 8.57 C ANISOU 5748 CB SER D 46 1150 926 1179 -31 -81 -119 C ATOM 5749 OG SER A 46 35.158 68.279 80.157 1.00 7.12 O ANISOU 5749 OG SER D 46 1103 723 876 -192 -159 -168 O ATOM 5750 N GLU A 47 31.882 69.543 80.194 1.00 9.44 N ANISOU 5750 N GLU D 47 1232 1036 1319 43 -10 -134 N ATOM 5751 CA GLU A 47 31.077 70.315 79.237 1.00 10.34 C ANISOU 5751 CA GLU D 47 1370 1150 1406 -8 -4 -165 C ATOM 5752 C GLU A 47 30.557 71.611 79.877 1.00 10.76 C ANISOU 5752 C GLU D 47 1437 1195 1456 34 23 -198 C ATOM 5753 O GLU A 47 30.440 72.614 79.197 1.00 11.12 O ANISOU 5753 O GLU D 47 1474 1091 1659 0 102 -317 O ATOM 5754 CB GLU A 47 29.933 69.513 78.602 1.00 11.20 C ANISOU 5754 CB GLU D 47 1462 1310 1482 -44 36 -142 C ATOM 5755 CG GLU A 47 29.396 70.193 77.341 1.00 12.78 C ANISOU 5755 CG GLU D 47 1655 1460 1740 36 57 -73 C ATOM 5756 CD GLU A 47 28.405 69.367 76.517 1.00 14.01 C ANISOU 5756 CD GLU D 47 1835 1754 1732 171 124 -73 C ATOM 5757 OE1 GLU A 47 27.818 68.377 77.029 1.00 15.62 O ANISOU 5757 OE1 GLU D 47 2323 1525 2086 37 108 -198 O ATOM 5758 OE2 GLU A 47 28.212 69.737 75.331 1.00 16.75 O ANISOU 5758 OE2 GLU D 47 2094 1976 2291 125 341 112 O ATOM 5759 N LEU A 48 30.271 71.557 81.167 1.00 10.75 N ANISOU 5759 N LEU D 48 1454 1171 1458 40 -21 -297 N ATOM 5760 CA LEU A 48 29.871 72.766 81.911 1.00 11.69 C ANISOU 5760 CA LEU D 48 1569 1300 1569 -11 -24 -213 C ATOM 5761 C LEU A 48 30.823 73.947 81.642 1.00 11.64 C ANISOU 5761 C LEU D 48 1460 1376 1585 -71 -37 -187 C ATOM 5762 O LEU A 48 30.390 75.081 81.458 1.00 11.01 O ANISOU 5762 O LEU D 48 1365 1210 1607 -96 30 -259 O ATOM 5763 CB LEU A 48 29.811 72.458 83.403 1.00 12.78 C ANISOU 5763 CB LEU D 48 1703 1448 1704 55 -66 -238 C ATOM 5764 CG LEU A 48 29.552 73.659 84.328 1.00 14.57 C ANISOU 5764 CG LEU D 48 2001 1623 1912 59 0 -205 C ATOM 5765 CD1 LEU A 48 28.237 74.303 83.991 1.00 15.59 C ANISOU 5765 CD1 LEU D 48 2003 1710 2208 55 -189 -314 C ATOM 5766 CD2 LEU A 48 29.591 73.168 85.759 1.00 16.14 C ANISOU 5766 CD2 LEU D 48 2146 1901 2082 211 -104 -237 C ATOM 5767 N VAL A 49 32.126 73.687 81.628 1.00 10.35 N ANISOU 5767 N VAL D 49 1250 1255 1427 -120 -40 -201 N ATOM 5768 CA VAL A 49 33.088 74.746 81.394 1.00 10.69 C ANISOU 5768 CA VAL D 49 1295 1326 1438 -51 -17 -144 C ATOM 5769 C VAL A 49 32.876 75.386 80.026 1.00 10.42 C ANISOU 5769 C VAL D 49 1161 1334 1463 -89 17 -185 C ATOM 5770 O VAL A 49 32.892 76.594 79.894 1.00 10.33 O ANISOU 5770 O VAL D 49 1242 1184 1495 -87 24 -267 O ATOM 5771 CB VAL A 49 34.535 74.230 81.553 1.00 10.80 C ANISOU 5771 CB VAL D 49 1278 1326 1498 -98 -70 -175 C ATOM 5772 CG1 VAL A 49 35.575 75.272 81.155 1.00 10.88 C ANISOU 5772 CG1 VAL D 49 1533 1254 1344 145 76 -218 C ATOM 5773 CG2 VAL A 49 34.764 73.775 82.950 1.00 11.58 C ANISOU 5773 CG2 VAL D 49 1301 1543 1553 -76 -45 -125 C ATOM 5774 N GLU A 50 32.669 74.564 79.000 1.00 10.17 N ANISOU 5774 N GLU D 50 1233 1221 1410 -106 41 -220 N ATOM 5775 CA GLU A 50 32.453 75.082 77.646 1.00 10.67 C ANISOU 5775 CA GLU D 50 1397 1253 1404 -97 9 -208 C ATOM 5776 C GLU A 50 31.120 75.849 77.520 1.00 10.32 C ANISOU 5776 C GLU D 50 1415 1196 1308 -53 12 -190 C ATOM 5777 O GLU A 50 31.016 76.834 76.783 1.00 10.21 O ANISOU 5777 O GLU D 50 1480 928 1468 -67 -54 -272 O ATOM 5778 CB GLU A 50 32.515 73.906 76.648 1.00 10.37 C ANISOU 5778 CB GLU D 50 1431 1125 1382 -22 50 -269 C ATOM 5779 CG GLU A 50 32.528 74.338 75.196 1.00 13.49 C ANISOU 5779 CG GLU D 50 1803 1652 1670 -204 -92 -155 C ATOM 5780 CD GLU A 50 32.865 73.213 74.229 1.00 15.65 C ANISOU 5780 CD GLU D 50 2418 1754 1771 -261 -76 -108 C ATOM 5781 OE1 GLU A 50 33.395 72.173 74.663 1.00 17.18 O ANISOU 5781 OE1 GLU D 50 2769 2140 1616 -350 -123 -221 O ATOM 5782 OE2 GLU A 50 32.627 73.393 73.023 1.00 18.40 O ANISOU 5782 OE2 GLU D 50 2714 2244 2033 -291 -165 -233 O ATOM 5783 N VAL A 51 30.081 75.359 78.199 1.00 10.91 N ANISOU 5783 N VAL D 51 1466 1228 1449 -79 -4 -74 N ATOM 5784 CA VAL A 51 28.799 76.089 78.241 1.00 10.82 C ANISOU 5784 CA VAL D 51 1389 1266 1456 -87 59 -124 C ATOM 5785 C VAL A 51 28.976 77.474 78.869 1.00 10.90 C ANISOU 5785 C VAL D 51 1436 1221 1482 -87 62 -89 C ATOM 5786 O VAL A 51 28.500 78.465 78.320 1.00 11.45 O ANISOU 5786 O VAL D 51 1538 1245 1566 -171 73 -217 O ATOM 5787 CB VAL A 51 27.742 75.307 78.963 1.00 11.59 C ANISOU 5787 CB VAL D 51 1500 1363 1539 -60 62 -160 C ATOM 5788 CG1 VAL A 51 26.455 76.119 79.057 1.00 12.28 C ANISOU 5788 CG1 VAL D 51 1442 1352 1868 -143 -21 -204 C ATOM 5789 CG2 VAL A 51 27.475 74.009 78.189 1.00 10.83 C ANISOU 5789 CG2 VAL D 51 1529 1098 1486 -83 -10 -179 C ATOM 5790 N LEU A 52 29.685 77.526 79.990 1.00 10.22 N ANISOU 5790 N LEU D 52 1342 1088 1450 -70 68 -169 N ATOM 5791 CA LEU A 52 29.946 78.797 80.673 1.00 11.38 C ANISOU 5791 CA LEU D 52 1475 1295 1552 -98 29 -151 C ATOM 5792 C LEU A 52 30.773 79.724 79.796 1.00 11.70 C ANISOU 5792 C LEU D 52 1486 1327 1632 -47 21 -125 C ATOM 5793 O LEU A 52 30.524 80.927 79.752 1.00 12.25 O ANISOU 5793 O LEU D 52 1733 1251 1668 -13 -7 -185 O ATOM 5794 CB LEU A 52 30.644 78.582 82.015 1.00 11.56 C ANISOU 5794 CB LEU D 52 1491 1328 1570 -127 -7 -153 C ATOM 5795 CG LEU A 52 29.831 77.874 83.091 1.00 12.03 C ANISOU 5795 CG LEU D 52 1657 1270 1643 -112 -44 -142 C ATOM 5796 CD1 LEU A 52 30.702 77.519 84.268 1.00 12.29 C ANISOU 5796 CD1 LEU D 52 1726 1234 1709 -131 8 -117 C ATOM 5797 CD2 LEU A 52 28.626 78.719 83.523 1.00 13.47 C ANISOU 5797 CD2 LEU D 52 1764 1566 1788 -137 -85 -176 C ATOM 5798 N ARG A 53 31.780 79.184 79.100 1.00 11.86 N ANISOU 5798 N ARG D 53 1507 1372 1626 -4 -6 -106 N ATOM 5799 CA ARG A 53 32.573 80.036 78.209 1.00 12.73 C ANISOU 5799 CA ARG D 53 1607 1492 1738 22 -33 -79 C ATOM 5800 C ARG A 53 31.753 80.630 77.073 1.00 12.96 C ANISOU 5800 C ARG D 53 1626 1464 1835 -22 -50 -61 C ATOM 5801 O ARG A 53 31.992 81.774 76.675 1.00 15.10 O ANISOU 5801 O ARG D 53 1898 1765 2072 8 -22 1 O ATOM 5802 CB ARG A 53 33.779 79.276 77.672 1.00 12.29 C ANISOU 5802 CB ARG D 53 1561 1352 1755 6 10 -138 C ATOM 5803 CG ARG A 53 34.526 79.938 76.533 1.00 13.86 C ANISOU 5803 CG ARG D 53 1832 1532 1902 20 -17 -146 C ATOM 5804 CD ARG A 53 35.132 81.283 76.909 1.00 14.59 C ANISOU 5804 CD ARG D 53 1816 1698 2028 135 -17 -204 C ATOM 5805 NE ARG A 53 36.156 81.116 77.917 1.00 15.57 N ANISOU 5805 NE ARG D 53 2097 1725 2091 81 -11 -249 N ATOM 5806 CZ ARG A 53 36.448 82.026 78.849 1.00 16.74 C ANISOU 5806 CZ ARG D 53 2149 2050 2160 -63 41 -217 C ATOM 5807 NH1 ARG A 53 35.748 83.165 78.937 1.00 15.48 N ANISOU 5807 NH1 ARG D 53 2079 1549 2254 -63 63 -241 N ATOM 5808 NH2 ARG A 53 37.419 81.778 79.708 1.00 16.95 N ANISOU 5808 NH2 ARG D 53 2062 2063 2313 6 50 -286 N ATOM 5809 N SER A 54 30.770 79.887 76.569 1.00 12.87 N ANISOU 5809 N SER D 54 1593 1496 1802 -40 -96 -55 N ATOM 5810 CA SER A 54 29.919 80.355 75.489 1.00 12.95 C ANISOU 5810 CA SER D 54 1672 1473 1773 -74 -51 -61 C ATOM 5811 C SER A 54 28.974 81.476 75.966 1.00 12.48 C ANISOU 5811 C SER D 54 1617 1380 1743 -47 -63 -34 C ATOM 5812 O SER A 54 28.728 82.455 75.261 1.00 12.86 O ANISOU 5812 O SER D 54 1688 1488 1707 -120 -50 12 O ATOM 5813 CB SER A 54 29.109 79.170 74.948 1.00 12.91 C ANISOU 5813 CB SER D 54 1675 1379 1851 -25 28 -21 C ATOM 5814 OG SER A 54 28.270 79.499 73.850 1.00 15.31 O ANISOU 5814 OG SER D 54 2256 1424 2137 -164 43 -58 O ATOM 5815 N LEU A 55 28.451 81.300 77.170 1.00 12.29 N ANISOU 5815 N LEU D 55 1629 1350 1690 -64 -35 -115 N ATOM 5816 CA LEU A 55 27.549 82.267 77.790 1.00 12.39 C ANISOU 5816 CA LEU D 55 1647 1311 1750 -42 -41 -160 C ATOM 5817 C LEU A 55 28.281 83.547 78.158 1.00 13.65 C ANISOU 5817 C LEU D 55 1732 1476 1975 1 3 -136 C ATOM 5818 O LEU A 55 27.702 84.640 78.074 1.00 13.64 O ANISOU 5818 O LEU D 55 1665 1425 2092 -79 110 -152 O ATOM 5819 CB LEU A 55 26.934 81.672 79.048 1.00 11.86 C ANISOU 5819 CB LEU D 55 1585 1198 1721 -49 -113 -162 C ATOM 5820 CG LEU A 55 25.818 80.638 78.878 1.00 10.57 C ANISOU 5820 CG LEU D 55 1474 1087 1455 -72 32 -226 C ATOM 5821 CD1 LEU A 55 25.521 79.917 80.186 1.00 11.35 C ANISOU 5821 CD1 LEU D 55 1346 1205 1759 -2 -60 -370 C ATOM 5822 CD2 LEU A 55 24.560 81.295 78.308 1.00 11.69 C ANISOU 5822 CD2 LEU D 55 1324 1341 1775 33 -100 -328 C ATOM 5823 N PHE A 56 29.563 83.408 78.507 1.00 14.41 N ANISOU 5823 N PHE D 56 1835 1529 2108 20 94 -148 N ATOM 5824 CA PHE A 56 30.382 84.523 79.026 1.00 15.94 C ANISOU 5824 CA PHE D 56 2036 1811 2208 72 33 -117 C ATOM 5825 C PHE A 56 31.752 84.597 78.343 1.00 16.69 C ANISOU 5825 C PHE D 56 2088 1935 2318 89 74 -102 C ATOM 5826 O PHE A 56 32.771 84.260 78.949 1.00 17.37 O ANISOU 5826 O PHE D 56 2191 2040 2365 94 60 -67 O ATOM 5827 CB PHE A 56 30.521 84.388 80.527 1.00 16.13 C ANISOU 5827 CB PHE D 56 2035 1809 2283 109 54 -143 C ATOM 5828 CG PHE A 56 29.205 84.360 81.239 1.00 18.50 C ANISOU 5828 CG PHE D 56 2392 2257 2378 36 -29 -180 C ATOM 5829 CD1 PHE A 56 28.448 85.514 81.353 1.00 19.46 C ANISOU 5829 CD1 PHE D 56 2532 2393 2469 31 -27 -92 C ATOM 5830 CD2 PHE A 56 28.716 83.165 81.776 1.00 19.29 C ANISOU 5830 CD2 PHE D 56 2543 2452 2335 57 -103 -75 C ATOM 5831 CE1 PHE A 56 27.226 85.480 81.976 1.00 20.47 C ANISOU 5831 CE1 PHE D 56 2745 2613 2418 16 -31 -206 C ATOM 5832 CE2 PHE A 56 27.494 83.128 82.423 1.00 20.32 C ANISOU 5832 CE2 PHE D 56 2600 2704 2414 72 72 -138 C ATOM 5833 CZ PHE A 56 26.748 84.284 82.521 1.00 20.17 C ANISOU 5833 CZ PHE D 56 2732 2607 2325 31 19 -162 C ATOM 5834 N PRO A 57 31.780 85.016 77.071 1.00 17.45 N ANISOU 5834 N PRO D 57 2235 2040 2356 93 41 -36 N ATOM 5835 CA PRO A 57 33.036 85.019 76.307 1.00 19.38 C ANISOU 5835 CA PRO D 57 2475 2346 2542 34 38 -34 C ATOM 5836 C PRO A 57 34.147 85.842 76.962 1.00 21.22 C ANISOU 5836 C PRO D 57 2643 2684 2732 46 62 20 C ATOM 5837 O PRO A 57 35.320 85.533 76.789 1.00 22.28 O ANISOU 5837 O PRO D 57 2684 2861 2918 19 94 87 O ATOM 5838 CB PRO A 57 32.664 85.626 74.946 1.00 19.23 C ANISOU 5838 CB PRO D 57 2436 2389 2479 26 25 -38 C ATOM 5839 CG PRO A 57 31.210 85.860 74.942 1.00 19.18 C ANISOU 5839 CG PRO D 57 2383 2436 2467 65 13 -29 C ATOM 5840 CD PRO A 57 30.627 85.475 76.282 1.00 17.91 C ANISOU 5840 CD PRO D 57 2288 2114 2400 72 21 -19 C ATOM 5841 N ASP A 58 33.763 86.885 77.685 1.00 22.95 N ANISOU 5841 N ASP D 58 2891 2860 2966 47 96 -13 N ATOM 5842 CA ASP A 58 34.735 87.839 78.213 1.00 24.35 C ANISOU 5842 CA ASP D 58 3075 3024 3152 92 69 -8 C ATOM 5843 C ASP A 58 35.123 87.636 79.687 1.00 23.38 C ANISOU 5843 C ASP D 58 2938 2893 3052 93 72 1 C ATOM 5844 O ASP A 58 36.145 88.170 80.134 1.00 25.28 O ANISOU 5844 O ASP D 58 3184 3143 3276 138 85 5 O ATOM 5845 CB ASP A 58 34.233 89.256 77.929 1.00 25.39 C ANISOU 5845 CB ASP D 58 3248 3124 3272 69 71 6 C ATOM 5846 CG ASP A 58 34.148 89.548 76.430 1.00 29.36 C ANISOU 5846 CG ASP D 58 3725 3713 3716 54 44 15 C ATOM 5847 OD1 ASP A 58 35.178 89.391 75.728 1.00 32.23 O ANISOU 5847 OD1 ASP D 58 4046 4114 4087 -12 -134 -27 O ATOM 5848 OD2 ASP A 58 33.072 89.933 75.906 1.00 32.61 O ANISOU 5848 OD2 ASP D 58 3998 4219 4172 7 125 139 O ATOM 5849 N LYS A 59 34.352 86.852 80.437 1.00 21.67 N ANISOU 5849 N LYS D 59 2730 2650 2851 57 74 -46 N ATOM 5850 CA LYS A 59 34.626 86.636 81.855 1.00 20.20 C ANISOU 5850 CA LYS D 59 2588 2439 2649 24 58 -80 C ATOM 5851 C LYS A 59 35.750 85.625 82.102 1.00 18.51 C ANISOU 5851 C LYS D 59 2375 2244 2414 29 57 -112 C ATOM 5852 O LYS A 59 36.045 84.757 81.271 1.00 18.36 O ANISOU 5852 O LYS D 59 2391 2235 2350 7 134 -210 O ATOM 5853 CB LYS A 59 33.363 86.180 82.609 1.00 20.85 C ANISOU 5853 CB LYS D 59 2629 2525 2765 24 40 -93 C ATOM 5854 CG LYS A 59 32.098 87.029 82.349 1.00 22.96 C ANISOU 5854 CG LYS D 59 2934 2798 2989 13 74 -48 C ATOM 5855 CD LYS A 59 31.821 88.005 83.473 1.00 25.15 C ANISOU 5855 CD LYS D 59 3184 3289 3083 -104 -3 10 C ATOM 5856 CE LYS A 59 31.003 89.183 82.997 1.00 26.19 C ANISOU 5856 CE LYS D 59 3292 3271 3385 16 -87 -23 C ATOM 5857 NZ LYS A 59 31.047 90.297 83.963 1.00 27.00 N ANISOU 5857 NZ LYS D 59 3392 3538 3328 -21 -64 3 N ATOM 5858 N ILE A 60 36.366 85.731 83.267 1.00 16.72 N ANISOU 5858 N ILE D 60 2165 1952 2234 59 72 -80 N ATOM 5859 CA ILE A 60 37.317 84.740 83.721 1.00 16.09 C ANISOU 5859 CA ILE D 60 2030 1967 2113 45 14 -101 C ATOM 5860 C ILE A 60 36.524 83.502 84.182 1.00 15.20 C ANISOU 5860 C ILE D 60 1896 1895 1983 54 -36 -106 C ATOM 5861 O ILE A 60 35.587 83.617 84.984 1.00 15.27 O ANISOU 5861 O ILE D 60 1881 1913 2005 24 -118 -242 O ATOM 5862 CB ILE A 60 38.200 85.315 84.858 1.00 16.68 C ANISOU 5862 CB ILE D 60 2122 2098 2114 24 16 -81 C ATOM 5863 CG1 ILE A 60 39.086 86.431 84.283 1.00 17.84 C ANISOU 5863 CG1 ILE D 60 2302 2163 2311 166 40 -133 C ATOM 5864 CG2 ILE A 60 39.040 84.204 85.493 1.00 16.77 C ANISOU 5864 CG2 ILE D 60 2017 2174 2181 7 7 -67 C ATOM 5865 CD1 ILE A 60 39.623 87.458 85.297 1.00 19.33 C ANISOU 5865 CD1 ILE D 60 2445 2379 2520 86 46 -149 C ATOM 5866 N ILE A 61 36.873 82.332 83.648 1.00 13.86 N ANISOU 5866 N ILE D 61 1770 1709 1785 22 -93 -98 N ATOM 5867 CA ILE A 61 36.220 81.068 84.026 1.00 13.46 C ANISOU 5867 CA ILE D 61 1728 1626 1759 63 -52 -119 C ATOM 5868 C ILE A 61 37.173 80.141 84.751 1.00 12.33 C ANISOU 5868 C ILE D 61 1583 1423 1679 54 -62 -175 C ATOM 5869 O ILE A 61 38.298 79.894 84.285 1.00 12.23 O ANISOU 5869 O ILE D 61 1563 1338 1745 -19 -63 -284 O ATOM 5870 CB ILE A 61 35.678 80.331 82.803 1.00 13.73 C ANISOU 5870 CB ILE D 61 1801 1649 1765 67 -57 -88 C ATOM 5871 CG1 ILE A 61 34.713 81.254 82.057 1.00 16.48 C ANISOU 5871 CG1 ILE D 61 2061 2042 2158 35 110 -97 C ATOM 5872 CG2 ILE A 61 35.044 78.993 83.200 1.00 14.05 C ANISOU 5872 CG2 ILE D 61 1807 1707 1823 -50 -83 -21 C ATOM 5873 CD1 ILE A 61 33.983 80.598 80.981 1.00 20.11 C ANISOU 5873 CD1 ILE D 61 2614 2485 2542 89 111 -48 C ATOM 5874 N VAL A 62 36.722 79.615 85.878 1.00 11.84 N ANISOU 5874 N VAL D 62 1520 1344 1634 46 -48 -184 N ATOM 5875 CA VAL A 62 37.507 78.714 86.716 1.00 11.56 C ANISOU 5875 CA VAL D 62 1412 1423 1556 -10 -58 -158 C ATOM 5876 C VAL A 62 36.942 77.319 86.624 1.00 11.32 C ANISOU 5876 C VAL D 62 1310 1438 1552 -43 -65 -184 C ATOM 5877 O VAL A 62 35.747 77.102 86.782 1.00 11.00 O ANISOU 5877 O VAL D 62 1337 1308 1533 -51 -229 -370 O ATOM 5878 CB VAL A 62 37.490 79.144 88.206 1.00 11.98 C ANISOU 5878 CB VAL D 62 1500 1474 1577 38 -86 -87 C ATOM 5879 CG1 VAL A 62 38.330 78.207 89.072 1.00 12.02 C ANISOU 5879 CG1 VAL D 62 1524 1466 1574 -33 -42 -213 C ATOM 5880 CG2 VAL A 62 37.976 80.599 88.359 1.00 13.44 C ANISOU 5880 CG2 VAL D 62 1647 1576 1881 9 -145 -187 C ATOM 5881 N ALA A 63 37.822 76.357 86.376 1.00 11.02 N ANISOU 5881 N ALA D 63 1208 1450 1528 -74 -95 -159 N ATOM 5882 CA ALA A 63 37.496 74.963 86.475 1.00 10.71 C ANISOU 5882 CA ALA D 63 1196 1431 1440 -82 -59 -185 C ATOM 5883 C ALA A 63 38.077 74.478 87.805 1.00 10.25 C ANISOU 5883 C ALA D 63 1168 1318 1407 -77 -49 -205 C ATOM 5884 O ALA A 63 39.291 74.296 87.945 1.00 10.14 O ANISOU 5884 O ALA D 63 1069 1353 1430 -89 -102 -410 O ATOM 5885 CB ALA A 63 38.096 74.190 85.287 1.00 10.41 C ANISOU 5885 CB ALA D 63 1160 1422 1372 -73 -9 -214 C ATOM 5886 N ASP A 64 37.210 74.327 88.793 1.00 10.06 N ANISOU 5886 N ASP D 64 1173 1268 1378 -124 -103 -206 N ATOM 5887 CA ASP A 64 37.599 73.958 90.158 1.00 10.58 C ANISOU 5887 CA ASP D 64 1211 1445 1363 -120 -160 -160 C ATOM 5888 C ASP A 64 37.721 72.431 90.314 1.00 11.21 C ANISOU 5888 C ASP D 64 1299 1524 1434 -57 -155 -178 C ATOM 5889 O ASP A 64 36.877 71.773 90.910 1.00 11.78 O ANISOU 5889 O ASP D 64 1351 1627 1495 -116 -174 -257 O ATOM 5890 CB ASP A 64 36.569 74.593 91.129 1.00 10.97 C ANISOU 5890 CB ASP D 64 1289 1476 1401 -102 -197 -213 C ATOM 5891 CG ASP A 64 36.829 74.283 92.580 1.00 11.55 C ANISOU 5891 CG ASP D 64 1344 1615 1427 -116 -94 -63 C ATOM 5892 OD1 ASP A 64 37.999 74.020 93.004 1.00 12.06 O ANISOU 5892 OD1 ASP D 64 1371 1704 1504 -36 -223 -203 O ATOM 5893 OD2 ASP A 64 35.842 74.314 93.353 1.00 12.39 O ANISOU 5893 OD2 ASP D 64 1698 1576 1431 -56 -89 -156 O ATOM 5894 N THR A 65 38.799 71.868 89.762 1.00 10.63 N ANISOU 5894 N THR D 65 1257 1454 1327 -80 -116 -155 N ATOM 5895 CA THR A 65 38.999 70.424 89.768 1.00 10.95 C ANISOU 5895 CA THR D 65 1360 1472 1325 -35 -102 -171 C ATOM 5896 C THR A 65 39.707 69.903 91.011 1.00 10.52 C ANISOU 5896 C THR D 65 1358 1400 1239 -6 -42 -145 C ATOM 5897 O THR A 65 39.658 68.690 91.299 1.00 10.62 O ANISOU 5897 O THR D 65 1346 1467 1222 114 53 -274 O ATOM 5898 CB THR A 65 39.792 70.008 88.550 1.00 10.90 C ANISOU 5898 CB THR D 65 1374 1456 1312 4 -122 -100 C ATOM 5899 OG1 THR A 65 41.037 70.719 88.543 1.00 11.45 O ANISOU 5899 OG1 THR D 65 1297 1749 1303 9 -227 -513 O ATOM 5900 CG2 THR A 65 39.030 70.315 87.253 1.00 11.00 C ANISOU 5900 CG2 THR D 65 1319 1327 1533 -117 -139 -166 C ATOM 5901 N LYS A 66 40.360 70.811 91.757 1.00 10.90 N ANISOU 5901 N LYS D 66 1400 1418 1323 -4 -67 -139 N ATOM 5902 CA LYS A 66 41.130 70.424 92.953 1.00 11.16 C ANISOU 5902 CA LYS D 66 1386 1485 1366 -44 -52 -119 C ATOM 5903 C LYS A 66 42.021 69.245 92.597 1.00 11.13 C ANISOU 5903 C LYS D 66 1433 1464 1332 -44 -54 -114 C ATOM 5904 O LYS A 66 42.149 68.252 93.317 1.00 12.32 O ANISOU 5904 O LYS D 66 1555 1636 1488 -75 -150 -183 O ATOM 5905 CB LYS A 66 40.212 70.137 94.159 1.00 11.89 C ANISOU 5905 CB LYS D 66 1512 1522 1483 -28 -64 -83 C ATOM 5906 CG LYS A 66 39.561 71.417 94.707 1.00 12.67 C ANISOU 5906 CG LYS D 66 1535 1645 1632 57 -5 -203 C ATOM 5907 CD LYS A 66 38.669 71.113 95.907 1.00 14.40 C ANISOU 5907 CD LYS D 66 2016 1785 1670 67 20 -212 C ATOM 5908 CE LYS A 66 38.081 72.381 96.511 1.00 14.72 C ANISOU 5908 CE LYS D 66 1892 1964 1738 -181 0 -200 C ATOM 5909 NZ LYS A 66 37.182 73.176 95.607 1.00 14.83 N ANISOU 5909 NZ LYS D 66 1840 2215 1580 -78 149 -298 N ATOM 5910 N CYS A 67 42.678 69.419 91.461 1.00 10.91 N ANISOU 5910 N CYS D 67 1386 1439 1318 -43 -57 -132 N ATOM 5911 CA CYS A 67 43.491 68.360 90.851 1.00 11.09 C ANISOU 5911 CA CYS D 67 1428 1435 1347 -84 -78 -182 C ATOM 5912 C CYS A 67 44.610 67.907 91.796 1.00 11.01 C ANISOU 5912 C CYS D 67 1360 1462 1361 -48 -55 -149 C ATOM 5913 O CYS A 67 45.352 68.744 92.313 1.00 11.30 O ANISOU 5913 O CYS D 67 1306 1633 1352 -120 3 -267 O ATOM 5914 CB CYS A 67 44.041 68.875 89.529 1.00 11.09 C ANISOU 5914 CB CYS D 67 1450 1390 1372 -58 -112 -160 C ATOM 5915 SG CYS A 67 45.243 67.822 88.711 1.00 13.95 S ANISOU 5915 SG CYS D 67 1861 1907 1533 -349 -80 -592 S ATOM 5916 N ALA A 68 44.705 66.593 92.033 1.00 11.61 N ANISOU 5916 N ALA D 68 1428 1565 1416 -27 -27 -227 N ATOM 5917 CA ALA A 68 45.729 66.000 92.909 1.00 12.08 C ANISOU 5917 CA ALA D 68 1493 1659 1435 -67 -39 -134 C ATOM 5918 C ALA A 68 46.798 65.250 92.128 1.00 12.87 C ANISOU 5918 C ALA D 68 1558 1826 1504 -121 -3 -140 C ATOM 5919 O ALA A 68 47.875 64.965 92.656 1.00 13.79 O ANISOU 5919 O ALA D 68 1587 2086 1563 -151 -51 -135 O ATOM 5920 CB ALA A 68 45.101 65.047 93.894 1.00 12.95 C ANISOU 5920 CB ALA D 68 1653 1756 1508 -47 -18 -176 C ATOM 5921 N ASP A 69 46.483 64.900 90.882 1.00 12.14 N ANISOU 5921 N ASP D 69 1513 1710 1387 -160 -41 -173 N ATOM 5922 CA ASP A 69 47.330 63.985 90.107 1.00 11.73 C ANISOU 5922 CA ASP D 69 1465 1582 1407 -135 -51 -152 C ATOM 5923 C ASP A 69 46.925 64.091 88.649 1.00 11.55 C ANISOU 5923 C ASP D 69 1429 1583 1376 -113 5 -142 C ATOM 5924 O ASP A 69 45.868 64.662 88.348 1.00 11.89 O ANISOU 5924 O ASP D 69 1624 1496 1395 -175 1 -265 O ATOM 5925 CB ASP A 69 47.170 62.557 90.629 1.00 11.58 C ANISOU 5925 CB ASP D 69 1426 1607 1364 -181 -53 -115 C ATOM 5926 CG ASP A 69 48.365 61.657 90.324 1.00 12.07 C ANISOU 5926 CG ASP D 69 1616 1408 1562 -73 -96 -80 C ATOM 5927 OD1 ASP A 69 49.318 62.115 89.650 1.00 12.91 O ANISOU 5927 OD1 ASP D 69 1392 1940 1570 -326 57 -212 O ATOM 5928 OD2 ASP A 69 48.352 60.451 90.736 1.00 13.88 O ANISOU 5928 OD2 ASP D 69 1748 1558 1966 -236 -160 -7 O ATOM 5929 N ALA A 70 47.775 63.570 87.752 1.00 11.87 N ANISOU 5929 N ALA D 70 1561 1548 1400 -85 17 -123 N ATOM 5930 CA ALA A 70 47.552 63.647 86.297 1.00 11.62 C ANISOU 5930 CA ALA D 70 1488 1566 1359 -22 -18 -76 C ATOM 5931 C ALA A 70 47.382 65.109 85.859 1.00 11.25 C ANISOU 5931 C ALA D 70 1481 1489 1304 -3 9 -100 C ATOM 5932 O ALA A 70 46.458 65.492 85.119 1.00 10.87 O ANISOU 5932 O ALA D 70 1433 1422 1275 -78 9 -157 O ATOM 5933 CB ALA A 70 46.353 62.764 85.861 1.00 11.75 C ANISOU 5933 CB ALA D 70 1553 1540 1369 -9 5 -77 C ATOM 5934 N GLY A 71 48.277 65.953 86.351 1.00 11.43 N ANISOU 5934 N GLY D 71 1386 1642 1312 -19 -8 -130 N ATOM 5935 CA GLY A 71 48.112 67.382 86.222 1.00 11.40 C ANISOU 5935 CA GLY D 71 1413 1516 1400 23 -17 -105 C ATOM 5936 C GLY A 71 48.027 67.873 84.800 1.00 11.34 C ANISOU 5936 C GLY D 71 1415 1468 1422 -19 -36 -129 C ATOM 5937 O GLY A 71 47.177 68.712 84.465 1.00 10.33 O ANISOU 5937 O GLY D 71 1454 1188 1280 3 -80 -249 O ATOM 5938 N GLY A 72 48.889 67.345 83.928 1.00 10.85 N ANISOU 5938 N GLY D 72 1301 1335 1485 -82 -32 -183 N ATOM 5939 CA GLY A 72 48.857 67.773 82.542 1.00 10.42 C ANISOU 5939 CA GLY D 72 1252 1277 1428 -61 -6 -174 C ATOM 5940 C GLY A 72 47.558 67.405 81.844 1.00 9.84 C ANISOU 5940 C GLY D 72 1248 1228 1263 -74 9 -120 C ATOM 5941 O GLY A 72 47.031 68.186 81.061 1.00 10.52 O ANISOU 5941 O GLY D 72 1287 1330 1379 -116 39 -280 O ATOM 5942 N THR A 73 47.067 66.203 82.114 1.00 9.66 N ANISOU 5942 N THR D 73 1173 1240 1257 -59 71 -197 N ATOM 5943 CA THR A 73 45.822 65.700 81.519 1.00 9.73 C ANISOU 5943 CA THR D 73 1220 1252 1222 -75 24 -176 C ATOM 5944 C THR A 73 44.606 66.480 81.982 1.00 9.71 C ANISOU 5944 C THR D 73 1113 1325 1249 -75 35 -119 C ATOM 5945 O THR A 73 43.802 66.912 81.159 1.00 9.71 O ANISOU 5945 O THR D 73 1271 1251 1164 -67 24 -95 O ATOM 5946 CB THR A 73 45.648 64.198 81.839 1.00 10.18 C ANISOU 5946 CB THR D 73 1313 1283 1272 -58 50 -182 C ATOM 5947 OG1 THR A 73 46.734 63.480 81.234 1.00 12.36 O ANISOU 5947 OG1 THR D 73 1428 1549 1720 -182 -145 -387 O ATOM 5948 CG2 THR A 73 44.334 63.635 81.289 1.00 10.60 C ANISOU 5948 CG2 THR D 73 1376 1376 1272 -118 37 -145 C ATOM 5949 N VAL A 74 44.476 66.644 83.292 1.00 10.01 N ANISOU 5949 N VAL D 74 1208 1350 1245 -148 -6 -91 N ATOM 5950 CA VAL A 74 43.322 67.369 83.815 1.00 10.17 C ANISOU 5950 CA VAL D 74 1153 1452 1259 -106 -24 -111 C ATOM 5951 C VAL A 74 43.354 68.831 83.348 1.00 9.83 C ANISOU 5951 C VAL D 74 1153 1369 1210 -47 -28 -96 C ATOM 5952 O VAL A 74 42.330 69.387 82.914 1.00 9.70 O ANISOU 5952 O VAL D 74 1250 1194 1243 -93 -14 -77 O ATOM 5953 CB VAL A 74 43.224 67.277 85.347 1.00 10.45 C ANISOU 5953 CB VAL D 74 1202 1481 1285 -120 -60 -3 C ATOM 5954 CG1 VAL A 74 42.041 68.083 85.850 1.00 11.49 C ANISOU 5954 CG1 VAL D 74 1240 1635 1488 -88 -157 -111 C ATOM 5955 CG2 VAL A 74 43.101 65.826 85.794 1.00 10.68 C ANISOU 5955 CG2 VAL D 74 1143 1421 1492 -293 -145 -30 C ATOM 5956 N ALA A 75 44.514 69.486 83.428 1.00 9.94 N ANISOU 5956 N ALA D 75 1226 1294 1256 -4 -3 -137 N ATOM 5957 CA ALA A 75 44.626 70.863 82.911 1.00 10.33 C ANISOU 5957 CA ALA D 75 1234 1299 1390 -5 -12 -129 C ATOM 5958 C ALA A 75 44.264 70.982 81.429 1.00 10.38 C ANISOU 5958 C ALA D 75 1269 1282 1392 -31 -93 -148 C ATOM 5959 O ALA A 75 43.466 71.821 81.051 1.00 10.33 O ANISOU 5959 O ALA D 75 1251 1405 1267 -44 -206 -225 O ATOM 5960 CB ALA A 75 46.001 71.417 83.163 1.00 11.31 C ANISOU 5960 CB ALA D 75 1298 1455 1543 1 81 -91 C ATOM 5961 N LYS A 76 44.801 70.088 80.584 1.00 10.27 N ANISOU 5961 N LYS D 76 1265 1336 1298 -52 -75 -210 N ATOM 5962 CA LYS A 76 44.455 70.132 79.169 1.00 10.49 C ANISOU 5962 CA LYS D 76 1327 1330 1326 -45 -99 -129 C ATOM 5963 C LYS A 76 42.960 69.953 78.966 1.00 9.69 C ANISOU 5963 C LYS D 76 1270 1136 1273 3 -72 -156 C ATOM 5964 O LYS A 76 42.327 70.645 78.169 1.00 9.48 O ANISOU 5964 O LYS D 76 1246 1068 1285 -25 -227 -152 O ATOM 5965 CB LYS A 76 45.236 69.067 78.382 1.00 10.63 C ANISOU 5965 CB LYS D 76 1376 1313 1348 -22 -59 -213 C ATOM 5966 CG LYS A 76 44.892 69.069 76.919 1.00 14.41 C ANISOU 5966 CG LYS D 76 1654 2026 1795 -72 0 -63 C ATOM 5967 CD LYS A 76 45.867 68.280 76.045 1.00 18.94 C ANISOU 5967 CD LYS D 76 2390 2502 2302 -163 -145 -134 C ATOM 5968 CE LYS A 76 45.553 68.571 74.583 1.00 21.65 C ANISOU 5968 CE LYS D 76 2759 2892 2572 -166 -50 -101 C ATOM 5969 NZ LYS A 76 46.436 67.818 73.609 1.00 23.54 N ANISOU 5969 NZ LYS D 76 3084 2996 2861 -253 -148 -204 N ATOM 5970 N ASN A 77 42.385 68.979 79.661 1.00 9.25 N ANISOU 5970 N ASN D 77 1138 1177 1198 -36 -86 -104 N ATOM 5971 CA ASN A 77 40.960 68.655 79.464 1.00 9.05 C ANISOU 5971 CA ASN D 77 1095 1115 1225 -45 -20 -166 C ATOM 5972 C ASN A 77 40.046 69.853 79.751 1.00 10.54 C ANISOU 5972 C ASN D 77 1211 1437 1355 -94 -19 -160 C ATOM 5973 O ASN A 77 39.065 70.089 79.047 1.00 11.05 O ANISOU 5973 O ASN D 77 1273 1558 1365 -253 47 -294 O ATOM 5974 CB ASN A 77 40.582 67.476 80.364 1.00 9.17 C ANISOU 5974 CB ASN D 77 1108 1085 1291 -116 -25 -105 C ATOM 5975 CG ASN A 77 41.098 66.124 79.852 1.00 8.37 C ANISOU 5975 CG ASN D 77 1046 997 1136 -95 65 -163 C ATOM 5976 OD1 ASN A 77 41.497 65.987 78.693 1.00 10.03 O ANISOU 5976 OD1 ASN D 77 1264 1279 1268 -203 -30 -215 O ATOM 5977 ND2 ASN A 77 41.030 65.103 80.722 1.00 8.99 N ANISOU 5977 ND2 ASN D 77 987 1223 1206 -7 -3 -134 N ATOM 5978 N ASN A 78 40.406 70.645 80.755 1.00 9.99 N ANISOU 5978 N ASN D 78 1235 1275 1283 -20 -25 -150 N ATOM 5979 CA ASN A 78 39.618 71.840 81.081 1.00 10.17 C ANISOU 5979 CA ASN D 78 1167 1384 1312 -47 -18 -149 C ATOM 5980 C ASN A 78 39.987 73.070 80.269 1.00 10.53 C ANISOU 5980 C ASN D 78 1236 1313 1451 -27 -34 -150 C ATOM 5981 O ASN A 78 39.119 73.881 79.916 1.00 11.26 O ANISOU 5981 O ASN D 78 1216 1413 1647 0 -74 -224 O ATOM 5982 CB ASN A 78 39.655 72.099 82.578 1.00 9.71 C ANISOU 5982 CB ASN D 78 1180 1304 1204 -32 -32 -128 C ATOM 5983 CG ASN A 78 38.883 71.073 83.323 1.00 8.99 C ANISOU 5983 CG ASN D 78 1113 1239 1062 -146 19 -163 C ATOM 5984 OD1 ASN A 78 37.665 71.191 83.444 1.00 11.20 O ANISOU 5984 OD1 ASN D 78 1192 1475 1588 -349 -138 -466 O ATOM 5985 ND2 ASN A 78 39.548 70.017 83.771 1.00 9.66 N ANISOU 5985 ND2 ASN D 78 1214 1253 1202 -283 1 -127 N ATOM 5986 N ALA A 79 41.272 73.210 79.929 1.00 10.45 N ANISOU 5986 N ALA D 79 1197 1360 1411 -69 -80 -175 N ATOM 5987 CA ALA A 79 41.709 74.306 79.051 1.00 11.10 C ANISOU 5987 CA ALA D 79 1406 1407 1404 -51 -32 -109 C ATOM 5988 C ALA A 79 41.071 74.236 77.658 1.00 11.43 C ANISOU 5988 C ALA D 79 1511 1416 1413 -22 -41 -78 C ATOM 5989 O ALA A 79 40.660 75.256 77.110 1.00 11.26 O ANISOU 5989 O ALA D 79 1529 1409 1338 -120 -68 -137 O ATOM 5990 CB ALA A 79 43.226 74.355 78.931 1.00 11.69 C ANISOU 5990 CB ALA D 79 1485 1486 1469 26 -34 -105 C ATOM 5991 N VAL A 80 40.977 73.033 77.082 1.00 11.35 N ANISOU 5991 N VAL D 80 1525 1443 1344 -124 -83 -119 N ATOM 5992 CA VAL A 80 40.341 72.921 75.776 1.00 11.81 C ANISOU 5992 CA VAL D 80 1551 1484 1453 -13 -41 -97 C ATOM 5993 C VAL A 80 38.859 73.251 75.816 1.00 11.27 C ANISOU 5993 C VAL D 80 1509 1377 1395 11 -32 -101 C ATOM 5994 O VAL A 80 38.298 73.599 74.787 1.00 12.27 O ANISOU 5994 O VAL D 80 1619 1603 1440 -45 -88 -101 O ATOM 5995 CB VAL A 80 40.575 71.575 75.090 1.00 12.04 C ANISOU 5995 CB VAL D 80 1526 1513 1533 -62 -132 -76 C ATOM 5996 CG1 VAL A 80 42.076 71.347 74.878 1.00 14.22 C ANISOU 5996 CG1 VAL D 80 1744 1822 1834 -144 46 -106 C ATOM 5997 CG2 VAL A 80 39.957 70.455 75.866 1.00 13.41 C ANISOU 5997 CG2 VAL D 80 1880 1521 1694 -112 -24 -196 C ATOM 5998 N ARG A 81 38.232 73.145 76.991 1.00 10.99 N ANISOU 5998 N ARG D 81 1431 1370 1375 68 -24 -123 N ATOM 5999 CA ARG A 81 36.843 73.592 77.178 1.00 10.90 C ANISOU 5999 CA ARG D 81 1420 1333 1388 58 30 -97 C ATOM 6000 C ARG A 81 36.698 75.120 77.329 1.00 11.26 C ANISOU 6000 C ARG D 81 1442 1364 1469 18 4 -118 C ATOM 6001 O ARG A 81 35.601 75.627 77.247 1.00 12.17 O ANISOU 6001 O ARG D 81 1510 1401 1712 86 11 -200 O ATOM 6002 CB ARG A 81 36.211 72.924 78.395 1.00 10.77 C ANISOU 6002 CB ARG D 81 1377 1375 1339 90 23 -93 C ATOM 6003 CG ARG A 81 36.089 71.406 78.307 1.00 11.25 C ANISOU 6003 CG ARG D 81 1421 1306 1546 -38 96 -25 C ATOM 6004 CD ARG A 81 34.931 70.996 77.472 1.00 10.83 C ANISOU 6004 CD ARG D 81 1546 1168 1398 6 70 -71 C ATOM 6005 NE ARG A 81 34.555 69.599 77.639 1.00 12.59 N ANISOU 6005 NE ARG D 81 1612 1419 1752 32 13 -149 N ATOM 6006 CZ ARG A 81 33.617 69.025 76.911 1.00 12.97 C ANISOU 6006 CZ ARG D 81 1747 1459 1720 -57 -77 -117 C ATOM 6007 NH1 ARG A 81 32.997 69.694 75.960 1.00 13.64 N ANISOU 6007 NH1 ARG D 81 1869 1464 1846 -316 128 -283 N ATOM 6008 NH2 ARG A 81 33.330 67.766 77.105 1.00 13.10 N ANISOU 6008 NH2 ARG D 81 1642 1330 2006 -11 7 -57 N ATOM 6009 N GLY A 82 37.801 75.825 77.559 1.00 11.71 N ANISOU 6009 N GLY D 82 1466 1406 1573 -22 10 -125 N ATOM 6010 CA GLY A 82 37.788 77.285 77.671 1.00 11.52 C ANISOU 6010 CA GLY D 82 1437 1426 1512 30 -3 -69 C ATOM 6011 C GLY A 82 38.136 77.856 79.041 1.00 11.20 C ANISOU 6011 C GLY D 82 1398 1357 1498 -2 10 -89 C ATOM 6012 O GLY A 82 38.059 79.078 79.220 1.00 12.67 O ANISOU 6012 O GLY D 82 1579 1585 1648 -23 35 -160 O ATOM 6013 N ALA A 83 38.538 77.016 80.006 1.00 11.32 N ANISOU 6013 N ALA D 83 1444 1374 1480 65 -36 -122 N ATOM 6014 CA ALA A 83 38.930 77.516 81.330 1.00 11.78 C ANISOU 6014 CA ALA D 83 1501 1447 1524 52 -49 -104 C ATOM 6015 C ALA A 83 40.138 78.458 81.256 1.00 11.67 C ANISOU 6015 C ALA D 83 1496 1395 1542 32 -68 -194 C ATOM 6016 O ALA A 83 41.069 78.274 80.456 1.00 11.97 O ANISOU 6016 O ALA D 83 1691 1312 1543 43 -165 -379 O ATOM 6017 CB ALA A 83 39.232 76.372 82.269 1.00 12.42 C ANISOU 6017 CB ALA D 83 1576 1529 1614 -3 -37 -94 C ATOM 6018 N ASP A 84 40.111 79.474 82.118 1.00 11.93 N ANISOU 6018 N ASP D 84 1524 1386 1620 -29 -72 -258 N ATOM 6019 CA ASP A 84 41.269 80.331 82.372 1.00 12.14 C ANISOU 6019 CA ASP D 84 1485 1448 1677 -30 -70 -148 C ATOM 6020 C ASP A 84 42.100 79.861 83.561 1.00 12.23 C ANISOU 6020 C ASP D 84 1475 1538 1631 -20 -72 -161 C ATOM 6021 O ASP A 84 43.328 79.744 83.467 1.00 13.14 O ANISOU 6021 O ASP D 84 1514 1747 1729 -36 -126 -220 O ATOM 6022 CB ASP A 84 40.832 81.786 82.608 1.00 12.60 C ANISOU 6022 CB ASP D 84 1544 1501 1741 -38 -37 -151 C ATOM 6023 CG ASP A 84 40.129 82.363 81.423 1.00 14.92 C ANISOU 6023 CG ASP D 84 1800 1811 2056 -9 48 -127 C ATOM 6024 OD1 ASP A 84 40.680 82.322 80.290 1.00 15.22 O ANISOU 6024 OD1 ASP D 84 1524 1903 2355 99 -90 -120 O ATOM 6025 OD2 ASP A 84 39.009 82.868 81.591 1.00 17.00 O ANISOU 6025 OD2 ASP D 84 1696 2476 2284 13 -185 -280 O ATOM 6026 N TRP A 85 41.430 79.593 84.674 1.00 11.93 N ANISOU 6026 N TRP D 85 1385 1557 1588 2 -78 -143 N ATOM 6027 CA TRP A 85 42.066 79.130 85.883 1.00 11.75 C ANISOU 6027 CA TRP D 85 1374 1551 1537 46 -49 -148 C ATOM 6028 C TRP A 85 41.595 77.731 86.238 1.00 11.68 C ANISOU 6028 C TRP D 85 1385 1510 1542 23 -1 -242 C ATOM 6029 O TRP A 85 40.418 77.389 86.049 1.00 11.76 O ANISOU 6029 O TRP D 85 1343 1411 1713 60 99 -290 O ATOM 6030 CB TRP A 85 41.794 80.096 87.055 1.00 11.90 C ANISOU 6030 CB TRP D 85 1342 1584 1593 95 -50 -157 C ATOM 6031 CG TRP A 85 42.178 81.561 86.820 1.00 13.39 C ANISOU 6031 CG TRP D 85 1777 1571 1737 -27 -37 -81 C ATOM 6032 CD1 TRP A 85 43.062 82.050 85.897 1.00 14.24 C ANISOU 6032 CD1 TRP D 85 1723 1652 2035 82 -15 -123 C ATOM 6033 CD2 TRP A 85 41.706 82.712 87.554 1.00 14.20 C ANISOU 6033 CD2 TRP D 85 1933 1676 1783 55 -15 -228 C ATOM 6034 NE1 TRP A 85 43.146 83.423 85.989 1.00 14.52 N ANISOU 6034 NE1 TRP D 85 1828 1560 2127 155 -6 -166 N ATOM 6035 CE2 TRP A 85 42.326 83.854 86.995 1.00 14.57 C ANISOU 6035 CE2 TRP D 85 1966 1557 2010 57 16 -243 C ATOM 6036 CE3 TRP A 85 40.787 82.889 88.587 1.00 14.81 C ANISOU 6036 CE3 TRP D 85 1920 1736 1970 60 25 -240 C ATOM 6037 CZ2 TRP A 85 42.082 85.168 87.470 1.00 15.94 C ANISOU 6037 CZ2 TRP D 85 2020 1869 2166 43 -5 -257 C ATOM 6038 CZ3 TRP A 85 40.548 84.199 89.063 1.00 15.99 C ANISOU 6038 CZ3 TRP D 85 2240 1734 2099 52 -20 -215 C ATOM 6039 CH2 TRP A 85 41.182 85.307 88.496 1.00 16.03 C ANISOU 6039 CH2 TRP D 85 2195 1865 2030 98 -53 -221 C ATOM 6040 N MET A 86 42.512 76.930 86.758 1.00 10.88 N ANISOU 6040 N MET D 86 1385 1388 1361 52 27 -244 N ATOM 6041 CA MET A 86 42.199 75.652 87.335 1.00 11.54 C ANISOU 6041 CA MET D 86 1442 1414 1528 -36 -23 -232 C ATOM 6042 C MET A 86 42.793 75.499 88.719 1.00 11.60 C ANISOU 6042 C MET D 86 1422 1418 1566 -7 -42 -266 C ATOM 6043 O MET A 86 43.949 75.869 88.946 1.00 12.67 O ANISOU 6043 O MET D 86 1284 1739 1791 -122 -128 -402 O ATOM 6044 CB MET A 86 42.693 74.520 86.413 1.00 11.22 C ANISOU 6044 CB MET D 86 1495 1339 1427 -30 -47 -236 C ATOM 6045 CG MET A 86 42.157 73.174 86.877 1.00 11.16 C ANISOU 6045 CG MET D 86 1587 1091 1560 -24 -56 -290 C ATOM 6046 SD MET A 86 42.742 71.730 85.999 1.00 13.75 S ANISOU 6046 SD MET D 86 1629 1825 1768 -33 -244 -863 S ATOM 6047 CE MET A 86 44.309 71.536 86.739 1.00 12.58 C ANISOU 6047 CE MET D 86 1498 1667 1613 -131 -61 -482 C ATOM 6048 N THR A 87 42.028 74.916 89.630 1.00 11.74 N ANISOU 6048 N THR D 87 1455 1485 1518 -96 -60 -245 N ATOM 6049 CA THR A 87 42.535 74.594 90.956 1.00 12.09 C ANISOU 6049 CA THR D 87 1448 1635 1509 -4 -8 -194 C ATOM 6050 C THR A 87 43.272 73.245 91.026 1.00 12.43 C ANISOU 6050 C THR D 87 1505 1650 1567 16 -11 -238 C ATOM 6051 O THR A 87 42.834 72.216 90.455 1.00 12.45 O ANISOU 6051 O THR D 87 1502 1619 1607 -58 48 -447 O ATOM 6052 CB THR A 87 41.415 74.644 92.021 1.00 12.20 C ANISOU 6052 CB THR D 87 1431 1645 1556 -17 -40 -182 C ATOM 6053 OG1 THR A 87 40.384 73.713 91.708 1.00 11.74 O ANISOU 6053 OG1 THR D 87 1341 1602 1517 3 -69 -358 O ATOM 6054 CG2 THR A 87 40.749 76.005 92.082 1.00 11.69 C ANISOU 6054 CG2 THR D 87 1381 1577 1480 -20 -52 -231 C ATOM 6055 N CYS A 88 44.405 73.248 91.740 1.00 11.94 N ANISOU 6055 N CYS D 88 1393 1651 1492 -30 15 -237 N ATOM 6056 CA CYS A 88 45.036 72.044 92.242 1.00 12.26 C ANISOU 6056 CA CYS D 88 1432 1743 1484 -2 24 -204 C ATOM 6057 C CYS A 88 44.900 72.079 93.755 1.00 11.77 C ANISOU 6057 C CYS D 88 1318 1704 1447 -50 84 -181 C ATOM 6058 O CYS A 88 45.076 73.133 94.375 1.00 12.92 O ANISOU 6058 O CYS D 88 1499 1858 1550 -167 144 -276 O ATOM 6059 CB CYS A 88 46.518 71.993 91.883 1.00 11.57 C ANISOU 6059 CB CYS D 88 1323 1655 1417 29 48 -254 C ATOM 6060 SG CYS A 88 46.860 71.619 90.156 1.00 13.66 S ANISOU 6060 SG CYS D 88 1333 2151 1705 -171 -125 -681 S ATOM 6061 N ILE A 89 44.602 70.931 94.329 1.00 12.48 N ANISOU 6061 N ILE D 89 1400 1893 1449 -56 89 -129 N ATOM 6062 CA ILE A 89 44.647 70.772 95.774 1.00 13.00 C ANISOU 6062 CA ILE D 89 1555 1899 1484 -57 44 -98 C ATOM 6063 C ILE A 89 46.107 70.912 96.231 1.00 13.66 C ANISOU 6063 C ILE D 89 1580 2026 1584 -47 17 -178 C ATOM 6064 O ILE A 89 47.056 70.521 95.530 1.00 13.36 O ANISOU 6064 O ILE D 89 1571 2047 1458 -149 -44 -337 O ATOM 6065 CB ILE A 89 44.031 69.416 96.203 1.00 13.51 C ANISOU 6065 CB ILE D 89 1632 1896 1606 -57 66 -56 C ATOM 6066 CG1 ILE A 89 43.696 69.414 97.696 1.00 14.07 C ANISOU 6066 CG1 ILE D 89 1807 1862 1673 -60 17 -98 C ATOM 6067 CG2 ILE A 89 44.910 68.220 95.806 1.00 12.26 C ANISOU 6067 CG2 ILE D 89 1539 1717 1402 -42 -36 -111 C ATOM 6068 CD1 ILE A 89 42.649 70.439 98.061 1.00 16.31 C ANISOU 6068 CD1 ILE D 89 1997 2310 1887 -175 -62 -248 C ATOM 6069 N CYS A 90 46.293 71.489 97.408 1.00 14.34 N ANISOU 6069 N CYS D 90 1656 2088 1703 -125 21 -257 N ATOM 6070 CA CYS A 90 47.642 71.787 97.893 1.00 15.12 C ANISOU 6070 CA CYS D 90 1751 2131 1862 -32 17 -240 C ATOM 6071 C CYS A 90 48.469 70.539 98.147 1.00 15.48 C ANISOU 6071 C CYS D 90 1822 2146 1911 -36 51 -182 C ATOM 6072 O CYS A 90 49.678 70.642 98.294 1.00 16.43 O ANISOU 6072 O CYS D 90 1786 2333 2124 -78 87 -208 O ATOM 6073 CB CYS A 90 47.581 72.603 99.179 1.00 15.49 C ANISOU 6073 CB CYS D 90 1818 2107 1959 -62 38 -266 C ATOM 6074 SG CYS A 90 46.519 71.922 100.459 1.00 16.94 S ANISOU 6074 SG CYS D 90 2014 2696 1727 -330 -83 -569 S ATOM 6075 N SER A 91 47.853 69.357 98.201 1.00 16.02 N ANISOU 6075 N SER D 91 1903 2228 1955 -61 19 -69 N ATOM 6076 CA SER A 91 48.632 68.141 98.379 1.00 16.47 C ANISOU 6076 CA SER D 91 2049 2224 1985 -87 22 -91 C ATOM 6077 C SER A 91 49.160 67.552 97.062 1.00 15.54 C ANISOU 6077 C SER D 91 1977 2158 1768 -131 20 -99 C ATOM 6078 O SER A 91 49.883 66.567 97.089 1.00 14.92 O ANISOU 6078 O SER D 91 1852 2163 1653 -166 137 -158 O ATOM 6079 CB SER A 91 47.859 67.081 99.133 1.00 17.23 C ANISOU 6079 CB SER D 91 2152 2282 2114 -43 12 -50 C ATOM 6080 OG SER A 91 46.619 66.859 98.525 1.00 19.34 O ANISOU 6080 OG SER D 91 2275 2539 2532 -42 35 -39 O ATOM 6081 N ALA A 92 48.771 68.147 95.935 1.00 15.04 N ANISOU 6081 N ALA D 92 1826 2110 1778 -149 9 -156 N ATOM 6082 CA ALA A 92 49.359 67.802 94.628 1.00 14.52 C ANISOU 6082 CA ALA D 92 1742 2057 1717 -104 -48 -125 C ATOM 6083 C ALA A 92 50.841 68.071 94.680 1.00 14.73 C ANISOU 6083 C ALA D 92 1753 2040 1803 -71 -4 -147 C ATOM 6084 O ALA A 92 51.270 69.071 95.227 1.00 14.50 O ANISOU 6084 O ALA D 92 1593 2137 1776 -39 -21 -230 O ATOM 6085 CB ALA A 92 48.736 68.649 93.505 1.00 14.37 C ANISOU 6085 CB ALA D 92 1691 1988 1778 -128 -82 -70 C ATOM 6086 N THR A 93 51.637 67.175 94.113 1.00 14.67 N ANISOU 6086 N THR D 93 1757 2043 1772 -32 -17 -196 N ATOM 6087 CA THR A 93 53.083 67.360 94.158 1.00 15.15 C ANISOU 6087 CA THR D 93 1812 2071 1873 -49 -3 -113 C ATOM 6088 C THR A 93 53.495 68.490 93.240 1.00 14.07 C ANISOU 6088 C THR D 93 1727 1900 1715 -57 -22 -168 C ATOM 6089 O THR A 93 52.767 68.858 92.336 1.00 13.11 O ANISOU 6089 O THR D 93 1697 1705 1576 -115 -27 -235 O ATOM 6090 CB THR A 93 53.810 66.103 93.706 1.00 15.52 C ANISOU 6090 CB THR D 93 1848 2127 1919 -16 -50 -91 C ATOM 6091 OG1 THR A 93 53.456 65.836 92.342 1.00 16.57 O ANISOU 6091 OG1 THR D 93 1821 2367 2107 -32 -30 -216 O ATOM 6092 CG2 THR A 93 53.426 64.919 94.535 1.00 16.50 C ANISOU 6092 CG2 THR D 93 1820 2246 2201 -68 10 -6 C ATOM 6093 N ILE A 94 54.690 69.027 93.442 1.00 15.06 N ANISOU 6093 N ILE D 94 1859 2041 1820 -4 57 -158 N ATOM 6094 CA ILE A 94 55.237 70.029 92.542 1.00 15.50 C ANISOU 6094 CA ILE D 94 1887 2153 1847 14 5 -170 C ATOM 6095 C ILE A 94 55.278 69.570 91.056 1.00 14.48 C ANISOU 6095 C ILE D 94 1733 2015 1753 11 -44 -136 C ATOM 6096 O ILE A 94 54.856 70.325 90.181 1.00 13.82 O ANISOU 6096 O ILE D 94 1637 1998 1613 -9 -145 -183 O ATOM 6097 CB ILE A 94 56.608 70.542 93.078 1.00 16.26 C ANISOU 6097 CB ILE D 94 1983 2226 1966 38 2 -185 C ATOM 6098 CG1 ILE A 94 56.397 71.210 94.455 1.00 18.39 C ANISOU 6098 CG1 ILE D 94 2251 2581 2154 -14 63 -260 C ATOM 6099 CG2 ILE A 94 57.271 71.498 92.105 1.00 17.56 C ANISOU 6099 CG2 ILE D 94 2160 2420 2091 74 30 -168 C ATOM 6100 CD1 ILE A 94 55.500 72.442 94.415 1.00 19.92 C ANISOU 6100 CD1 ILE D 94 2472 2562 2535 35 59 -183 C ATOM 6101 N PRO A 95 55.778 68.362 90.763 1.00 14.43 N ANISOU 6101 N PRO D 95 1690 2049 1742 -47 -90 -102 N ATOM 6102 CA PRO A 95 55.700 67.870 89.374 1.00 13.84 C ANISOU 6102 CA PRO D 95 1645 1960 1652 -39 -54 -85 C ATOM 6103 C PRO A 95 54.291 67.896 88.795 1.00 12.89 C ANISOU 6103 C PRO D 95 1535 1802 1558 -84 -111 -55 C ATOM 6104 O PRO A 95 54.118 68.318 87.666 1.00 12.69 O ANISOU 6104 O PRO D 95 1442 1886 1494 -239 -160 -99 O ATOM 6105 CB PRO A 95 56.236 66.435 89.466 1.00 14.82 C ANISOU 6105 CB PRO D 95 1732 2097 1801 -8 -37 -76 C ATOM 6106 CG PRO A 95 57.207 66.504 90.600 1.00 15.50 C ANISOU 6106 CG PRO D 95 1794 2248 1846 -176 -34 -148 C ATOM 6107 CD PRO A 95 56.520 67.426 91.624 1.00 14.91 C ANISOU 6107 CD PRO D 95 1818 2065 1783 -41 -101 -127 C ATOM 6108 N THR A 96 53.300 67.471 89.575 1.00 11.87 N ANISOU 6108 N THR D 96 1435 1611 1461 -50 -97 -90 N ATOM 6109 CA THR A 96 51.914 67.569 89.146 1.00 11.68 C ANISOU 6109 CA THR D 96 1386 1614 1435 -40 -74 -115 C ATOM 6110 C THR A 96 51.471 69.000 88.830 1.00 11.25 C ANISOU 6110 C THR D 96 1294 1564 1416 7 -75 -151 C ATOM 6111 O THR A 96 50.880 69.269 87.770 1.00 11.30 O ANISOU 6111 O THR D 96 1183 1655 1452 3 -139 -347 O ATOM 6112 CB THR A 96 51.020 66.889 90.198 1.00 12.01 C ANISOU 6112 CB THR D 96 1405 1610 1547 16 -47 -49 C ATOM 6113 OG1 THR A 96 51.218 65.484 90.100 1.00 12.64 O ANISOU 6113 OG1 THR D 96 1364 1779 1660 -100 40 -238 O ATOM 6114 CG2 THR A 96 49.529 67.130 89.949 1.00 12.32 C ANISOU 6114 CG2 THR D 96 1376 1824 1479 -145 -168 -73 C ATOM 6115 N MET A 97 51.751 69.927 89.739 1.00 11.41 N ANISOU 6115 N MET D 97 1311 1625 1396 12 -3 -203 N ATOM 6116 CA MET A 97 51.422 71.332 89.542 1.00 11.66 C ANISOU 6116 CA MET D 97 1353 1599 1478 -29 19 -240 C ATOM 6117 C MET A 97 52.113 71.955 88.350 1.00 11.34 C ANISOU 6117 C MET D 97 1343 1486 1477 -55 26 -260 C ATOM 6118 O MET A 97 51.512 72.717 87.612 1.00 10.54 O ANISOU 6118 O MET D 97 1236 1354 1412 -184 -62 -435 O ATOM 6119 CB MET A 97 51.719 72.159 90.809 1.00 12.73 C ANISOU 6119 CB MET D 97 1571 1671 1593 -16 34 -247 C ATOM 6120 CG MET A 97 50.836 71.823 91.976 1.00 12.69 C ANISOU 6120 CG MET D 97 1484 1842 1495 15 -16 -316 C ATOM 6121 SD MET A 97 51.072 72.995 93.332 1.00 17.61 S ANISOU 6121 SD MET D 97 2141 2711 1838 6 -212 -816 S ATOM 6122 CE MET A 97 49.997 72.342 94.559 1.00 15.71 C ANISOU 6122 CE MET D 97 2026 2162 1780 57 -38 -467 C ATOM 6123 N LYS A 98 53.404 71.630 88.175 1.00 10.95 N ANISOU 6123 N LYS D 98 1244 1445 1469 -83 9 -270 N ATOM 6124 CA LYS A 98 54.169 72.114 87.034 1.00 11.64 C ANISOU 6124 CA LYS D 98 1311 1563 1545 -26 32 -178 C ATOM 6125 C LYS A 98 53.595 71.635 85.686 1.00 11.69 C ANISOU 6125 C LYS D 98 1356 1592 1492 -71 -10 -187 C ATOM 6126 O LYS A 98 53.449 72.424 84.747 1.00 11.50 O ANISOU 6126 O LYS D 98 1282 1685 1403 6 -15 -276 O ATOM 6127 CB LYS A 98 55.637 71.701 87.177 1.00 12.38 C ANISOU 6127 CB LYS D 98 1402 1712 1590 -29 15 -148 C ATOM 6128 CG LYS A 98 56.395 72.555 88.200 1.00 12.75 C ANISOU 6128 CG LYS D 98 1369 1839 1635 12 1 -160 C ATOM 6129 CD LYS A 98 57.874 72.099 88.306 1.00 14.55 C ANISOU 6129 CD LYS D 98 1669 2077 1782 6 -34 -140 C ATOM 6130 CE LYS A 98 58.691 73.140 89.053 1.00 16.74 C ANISOU 6130 CE LYS D 98 1928 2191 2239 73 27 -173 C ATOM 6131 NZ LYS A 98 60.153 72.871 88.947 1.00 18.89 N ANISOU 6131 NZ LYS D 98 1974 2783 2418 81 -36 -176 N ATOM 6132 N ALA A 99 53.282 70.342 85.608 1.00 12.14 N ANISOU 6132 N ALA D 99 1402 1669 1539 -88 -56 -131 N ATOM 6133 CA ALA A 99 52.661 69.769 84.403 1.00 11.65 C ANISOU 6133 CA ALA D 99 1365 1600 1459 -70 -38 -90 C ATOM 6134 C ALA A 99 51.301 70.416 84.143 1.00 11.79 C ANISOU 6134 C ALA D 99 1434 1626 1418 -133 -70 -130 C ATOM 6135 O ALA A 99 50.960 70.717 83.000 1.00 11.68 O ANISOU 6135 O ALA D 99 1425 1664 1348 -240 -96 -131 O ATOM 6136 CB ALA A 99 52.512 68.262 84.529 1.00 12.24 C ANISOU 6136 CB ALA D 99 1392 1672 1586 -129 -36 -82 C ATOM 6137 N ALA A 100 50.532 70.646 85.207 1.00 11.38 N ANISOU 6137 N ALA D 100 1430 1535 1356 -76 -107 -134 N ATOM 6138 CA ALA A 100 49.252 71.324 85.044 1.00 10.57 C ANISOU 6138 CA ALA D 100 1289 1415 1309 -41 -67 -108 C ATOM 6139 C ALA A 100 49.438 72.759 84.541 1.00 10.86 C ANISOU 6139 C ALA D 100 1272 1447 1406 31 -87 -147 C ATOM 6140 O ALA A 100 48.746 73.190 83.631 1.00 10.68 O ANISOU 6140 O ALA D 100 1235 1350 1472 -10 -66 -77 O ATOM 6141 CB ALA A 100 48.437 71.300 86.350 1.00 10.32 C ANISOU 6141 CB ALA D 100 1266 1376 1278 8 -112 -204 C ATOM 6142 N ARG A 101 50.396 73.487 85.105 1.00 10.92 N ANISOU 6142 N ARG D 101 1232 1487 1427 -6 -16 -191 N ATOM 6143 CA ARG A 101 50.636 74.846 84.655 1.00 11.41 C ANISOU 6143 CA ARG D 101 1363 1487 1484 -12 -55 -166 C ATOM 6144 C ARG A 101 51.077 74.933 83.207 1.00 11.71 C ANISOU 6144 C ARG D 101 1414 1436 1597 5 -55 -161 C ATOM 6145 O ARG A 101 50.559 75.733 82.449 1.00 12.39 O ANISOU 6145 O ARG D 101 1644 1462 1601 -43 -109 -318 O ATOM 6146 CB ARG A 101 51.659 75.566 85.540 1.00 11.89 C ANISOU 6146 CB ARG D 101 1299 1645 1573 -34 -34 -172 C ATOM 6147 CG ARG A 101 51.833 76.999 85.109 1.00 13.99 C ANISOU 6147 CG ARG D 101 1637 1935 1742 -15 -121 -126 C ATOM 6148 CD ARG A 101 52.626 77.869 86.062 1.00 18.18 C ANISOU 6148 CD ARG D 101 2166 2518 2221 50 32 -110 C ATOM 6149 NE ARG A 101 54.000 77.422 86.187 1.00 22.15 N ANISOU 6149 NE ARG D 101 2640 2905 2867 -30 -70 -49 N ATOM 6150 CZ ARG A 101 54.987 77.771 85.359 1.00 25.32 C ANISOU 6150 CZ ARG D 101 3022 3407 3190 9 -117 73 C ATOM 6151 NH1 ARG A 101 54.769 78.588 84.329 1.00 25.42 N ANISOU 6151 NH1 ARG D 101 2991 3512 3154 29 -54 76 N ATOM 6152 NH2 ARG A 101 56.207 77.304 85.579 1.00 27.17 N ANISOU 6152 NH2 ARG D 101 3214 3733 3376 -110 -59 62 N ATOM 6153 N LYS A 102 52.004 74.065 82.810 1.00 12.36 N ANISOU 6153 N LYS D 102 1478 1568 1648 -11 -91 -143 N ATOM 6154 CA LYS A 102 52.463 74.066 81.434 1.00 12.47 C ANISOU 6154 CA LYS D 102 1498 1622 1618 -25 -99 -77 C ATOM 6155 C LYS A 102 51.313 73.791 80.469 1.00 12.37 C ANISOU 6155 C LYS D 102 1502 1644 1552 -64 -126 -106 C ATOM 6156 O LYS A 102 51.178 74.508 79.474 1.00 12.95 O ANISOU 6156 O LYS D 102 1401 1785 1732 -67 -301 -125 O ATOM 6157 CB LYS A 102 53.624 73.080 81.256 1.00 12.16 C ANISOU 6157 CB LYS D 102 1473 1574 1571 -79 -49 -13 C ATOM 6158 CG LYS A 102 54.168 72.923 79.824 1.00 14.98 C ANISOU 6158 CG LYS D 102 1831 2033 1829 -41 -89 -20 C ATOM 6159 CD LYS A 102 54.540 74.243 79.162 1.00 17.65 C ANISOU 6159 CD LYS D 102 2260 2263 2183 -74 -83 -123 C ATOM 6160 CE LYS A 102 55.493 74.070 77.964 1.00 19.49 C ANISOU 6160 CE LYS D 102 2279 2683 2442 85 -154 -142 C ATOM 6161 NZ LYS A 102 55.094 73.026 76.957 1.00 20.36 N ANISOU 6161 NZ LYS D 102 2380 2875 2481 -18 -196 -295 N ATOM 6162 N ALA A 103 50.470 72.806 80.799 1.00 12.92 N ANISOU 6162 N ALA D 103 1552 1800 1557 -28 -91 -176 N ATOM 6163 CA ALA A 103 49.320 72.432 79.957 1.00 13.11 C ANISOU 6163 CA ALA D 103 1623 1738 1619 -34 -47 -144 C ATOM 6164 C ALA A 103 48.331 73.591 79.775 1.00 13.26 C ANISOU 6164 C ALA D 103 1676 1741 1621 -35 -26 -128 C ATOM 6165 O ALA A 103 47.912 73.889 78.665 1.00 13.23 O ANISOU 6165 O ALA D 103 1690 1753 1581 -147 -50 -170 O ATOM 6166 CB ALA A 103 48.617 71.167 80.492 1.00 13.45 C ANISOU 6166 CB ALA D 103 1689 1803 1619 -30 -36 -139 C ATOM 6167 N ILE A 104 47.987 74.261 80.874 1.00 12.98 N ANISOU 6167 N ILE D 104 1652 1710 1570 -6 -58 -100 N ATOM 6168 CA ILE A 104 47.048 75.351 80.777 1.00 13.14 C ANISOU 6168 CA ILE D 104 1672 1693 1627 0 -62 -117 C ATOM 6169 C ILE A 104 47.663 76.561 80.067 1.00 13.34 C ANISOU 6169 C ILE D 104 1701 1664 1701 -7 -31 -143 C ATOM 6170 O ILE A 104 46.983 77.222 79.303 1.00 13.66 O ANISOU 6170 O ILE D 104 1649 1722 1817 -75 -41 -270 O ATOM 6171 CB ILE A 104 46.392 75.729 82.145 1.00 12.96 C ANISOU 6171 CB ILE D 104 1736 1606 1582 66 -60 -59 C ATOM 6172 CG1 ILE A 104 45.039 76.402 81.887 1.00 13.40 C ANISOU 6172 CG1 ILE D 104 1814 1695 1581 23 -116 -101 C ATOM 6173 CG2 ILE A 104 47.315 76.611 82.996 1.00 12.76 C ANISOU 6173 CG2 ILE D 104 1569 1863 1415 7 -57 -154 C ATOM 6174 CD1 ILE A 104 44.108 76.400 83.068 1.00 13.82 C ANISOU 6174 CD1 ILE D 104 1874 1588 1788 29 -239 -124 C ATOM 6175 N GLU A 105 48.955 76.813 80.273 1.00 13.44 N ANISOU 6175 N GLU D 105 1646 1727 1731 -53 -68 -157 N ATOM 6176 CA GLU A 105 49.654 77.855 79.508 1.00 14.21 C ANISOU 6176 CA GLU D 105 1722 1814 1862 -17 -6 -84 C ATOM 6177 C GLU A 105 49.776 77.535 78.009 1.00 14.30 C ANISOU 6177 C GLU D 105 1683 1873 1877 -13 -28 -89 C ATOM 6178 O GLU A 105 49.728 78.447 77.172 1.00 14.80 O ANISOU 6178 O GLU D 105 1733 1997 1891 -78 -7 -133 O ATOM 6179 CB GLU A 105 51.036 78.150 80.103 1.00 14.42 C ANISOU 6179 CB GLU D 105 1792 1793 1894 0 -16 -63 C ATOM 6180 CG GLU A 105 50.970 78.835 81.474 1.00 16.02 C ANISOU 6180 CG GLU D 105 1969 2055 2060 65 34 -90 C ATOM 6181 CD GLU A 105 52.353 79.204 82.003 1.00 18.88 C ANISOU 6181 CD GLU D 105 2156 2611 2405 65 -66 -120 C ATOM 6182 OE1 GLU A 105 53.348 78.953 81.296 1.00 20.75 O ANISOU 6182 OE1 GLU D 105 2099 3160 2624 22 -267 -171 O ATOM 6183 OE2 GLU A 105 52.454 79.737 83.125 1.00 18.14 O ANISOU 6183 OE2 GLU D 105 2136 2499 2254 326 19 -112 O ATOM 6184 N ASP A 106 49.924 76.253 77.658 1.00 15.22 N ANISOU 6184 N ASP D 106 1825 2004 1953 6 -2 -49 N ATOM 6185 CA ASP A 106 50.055 75.896 76.235 1.00 15.63 C ANISOU 6185 CA ASP D 106 1952 2019 1965 -1 -32 -67 C ATOM 6186 C ASP A 106 48.791 76.243 75.431 1.00 15.50 C ANISOU 6186 C ASP D 106 1975 1956 1957 21 -65 -49 C ATOM 6187 O ASP A 106 48.858 76.673 74.284 1.00 16.19 O ANISOU 6187 O ASP D 106 2024 2129 1997 12 -44 -41 O ATOM 6188 CB ASP A 106 50.382 74.407 76.062 1.00 15.79 C ANISOU 6188 CB ASP D 106 1927 2080 1990 -76 -28 -52 C ATOM 6189 CG ASP A 106 51.852 74.082 76.311 1.00 18.18 C ANISOU 6189 CG ASP D 106 2240 2372 2295 -75 12 -22 C ATOM 6190 OD1 ASP A 106 52.688 74.997 76.390 1.00 19.79 O ANISOU 6190 OD1 ASP D 106 2151 2852 2516 55 -113 59 O ATOM 6191 OD2 ASP A 106 52.199 72.888 76.449 1.00 19.86 O ANISOU 6191 OD2 ASP D 106 2458 2476 2610 -311 -42 -12 O ATOM 6192 N ILE A 107 47.630 76.061 76.058 1.00 14.88 N ANISOU 6192 N ILE D 107 1893 1811 1947 29 -88 -78 N ATOM 6193 CA ILE A 107 46.351 76.247 75.398 1.00 14.80 C ANISOU 6193 CA ILE D 107 1949 1785 1887 8 -62 -10 C ATOM 6194 C ILE A 107 45.915 77.705 75.574 1.00 14.80 C ANISOU 6194 C ILE D 107 1867 1859 1894 -27 -87 -28 C ATOM 6195 O ILE A 107 45.340 78.301 74.675 1.00 15.48 O ANISOU 6195 O ILE D 107 1999 1881 2001 -32 -130 90 O ATOM 6196 CB ILE A 107 45.288 75.258 75.972 1.00 15.00 C ANISOU 6196 CB ILE D 107 1932 1821 1945 32 -45 -64 C ATOM 6197 CG1 ILE A 107 45.680 73.803 75.666 1.00 16.87 C ANISOU 6197 CG1 ILE D 107 2181 2047 2180 -50 -53 -132 C ATOM 6198 CG2 ILE A 107 43.890 75.597 75.486 1.00 13.94 C ANISOU 6198 CG2 ILE D 107 1911 1575 1808 53 -82 -141 C ATOM 6199 CD1 ILE A 107 45.416 73.385 74.261 1.00 21.09 C ANISOU 6199 CD1 ILE D 107 2695 2587 2732 -22 0 -40 C ATOM 6200 N ASN A 108 46.213 78.277 76.729 1.00 14.34 N ANISOU 6200 N ASN D 108 1780 1766 1901 52 -55 -9 N ATOM 6201 CA ASN A 108 45.713 79.612 77.071 1.00 14.75 C ANISOU 6201 CA ASN D 108 1824 1855 1922 -1 -64 -41 C ATOM 6202 C ASN A 108 46.885 80.474 77.574 1.00 15.50 C ANISOU 6202 C ASN D 108 1969 1882 2038 43 -66 -29 C ATOM 6203 O ASN A 108 47.016 80.710 78.768 1.00 14.49 O ANISOU 6203 O ASN D 108 1842 1771 1891 -61 -116 -96 O ATOM 6204 CB ASN A 108 44.599 79.453 78.119 1.00 13.96 C ANISOU 6204 CB ASN D 108 1729 1678 1896 59 -128 -37 C ATOM 6205 CG ASN A 108 43.882 80.766 78.461 1.00 14.98 C ANISOU 6205 CG ASN D 108 1810 1808 2071 40 -196 -6 C ATOM 6206 OD1 ASN A 108 44.332 81.859 78.116 1.00 16.10 O ANISOU 6206 OD1 ASN D 108 2103 1812 2201 121 -316 73 O ATOM 6207 ND2 ASN A 108 42.750 80.647 79.158 1.00 14.87 N ANISOU 6207 ND2 ASN D 108 1643 1971 2034 43 -321 -174 N ATOM 6208 N PRO A 109 47.783 80.897 76.668 1.00 17.03 N ANISOU 6208 N PRO D 109 2143 2137 2187 29 -88 -30 N ATOM 6209 CA PRO A 109 48.925 81.725 77.086 1.00 17.96 C ANISOU 6209 CA PRO D 109 2247 2246 2332 48 -92 -28 C ATOM 6210 C PRO A 109 48.532 83.052 77.729 1.00 19.01 C ANISOU 6210 C PRO D 109 2396 2343 2483 57 -73 -16 C ATOM 6211 O PRO A 109 49.194 83.469 78.674 1.00 19.58 O ANISOU 6211 O PRO D 109 2440 2331 2668 164 -131 -78 O ATOM 6212 CB PRO A 109 49.707 81.951 75.778 1.00 18.12 C ANISOU 6212 CB PRO D 109 2234 2298 2351 39 -101 -3 C ATOM 6213 CG PRO A 109 48.803 81.660 74.713 1.00 17.59 C ANISOU 6213 CG PRO D 109 2187 2261 2236 127 -142 12 C ATOM 6214 CD PRO A 109 47.833 80.604 75.229 1.00 17.38 C ANISOU 6214 CD PRO D 109 2232 2155 2216 119 -65 7 C ATOM 6215 N ASP A 110 47.445 83.659 77.265 1.00 20.57 N ANISOU 6215 N ASP D 110 2603 2528 2685 40 -94 -12 N ATOM 6216 CA ASP A 110 47.060 85.000 77.724 1.00 21.25 C ANISOU 6216 CA ASP D 110 2739 2586 2746 31 -57 -27 C ATOM 6217 C ASP A 110 46.630 85.038 79.193 1.00 20.44 C ANISOU 6217 C ASP D 110 2631 2470 2663 65 -81 -39 C ATOM 6218 O ASP A 110 46.971 85.982 79.912 1.00 21.00 O ANISOU 6218 O ASP D 110 2695 2472 2809 78 -130 -46 O ATOM 6219 CB ASP A 110 45.915 85.568 76.882 1.00 22.71 C ANISOU 6219 CB ASP D 110 2906 2808 2911 25 -36 -32 C ATOM 6220 CG ASP A 110 46.351 85.988 75.495 1.00 25.67 C ANISOU 6220 CG ASP D 110 3362 3174 3215 13 -26 -18 C ATOM 6221 OD1 ASP A 110 47.563 85.918 75.165 1.00 29.45 O ANISOU 6221 OD1 ASP D 110 3746 3707 3737 -26 -126 9 O ATOM 6222 OD2 ASP A 110 45.497 86.405 74.691 1.00 30.37 O ANISOU 6222 OD2 ASP D 110 3941 3851 3747 -93 69 12 O ATOM 6223 N LYS A 111 45.892 84.007 79.633 1.00 18.63 N ANISOU 6223 N LYS D 111 2331 2286 2462 83 -84 -45 N ATOM 6224 CA LYS A 111 45.283 83.999 80.967 1.00 17.35 C ANISOU 6224 CA LYS D 111 2192 2136 2263 43 -9 -107 C ATOM 6225 C LYS A 111 45.462 82.724 81.793 1.00 15.97 C ANISOU 6225 C LYS D 111 2032 1955 2078 -7 -31 -152 C ATOM 6226 O LYS A 111 45.114 82.696 82.965 1.00 16.27 O ANISOU 6226 O LYS D 111 2156 1934 2091 -29 5 -265 O ATOM 6227 CB LYS A 111 43.771 84.283 80.840 1.00 17.63 C ANISOU 6227 CB LYS D 111 2189 2218 2292 -1 -41 -79 C ATOM 6228 CG LYS A 111 43.429 85.657 80.267 1.00 19.39 C ANISOU 6228 CG LYS D 111 2456 2327 2585 81 3 -44 C ATOM 6229 CD LYS A 111 41.968 85.984 80.489 1.00 22.58 C ANISOU 6229 CD LYS D 111 2832 2824 2924 11 -27 -18 C ATOM 6230 CE LYS A 111 41.535 87.185 79.685 1.00 26.00 C ANISOU 6230 CE LYS D 111 3333 3218 3326 21 17 -33 C ATOM 6231 NZ LYS A 111 42.183 88.414 80.210 1.00 28.45 N ANISOU 6231 NZ LYS D 111 3642 3469 3697 76 60 -64 N ATOM 6232 N GLY A 112 45.949 81.640 81.176 1.00 14.21 N ANISOU 6232 N GLY D 112 1791 1668 1937 -33 -58 -73 N ATOM 6233 CA GLY A 112 45.949 80.341 81.844 1.00 13.67 C ANISOU 6233 CA GLY D 112 1696 1631 1866 -15 -52 -126 C ATOM 6234 C GLY A 112 46.797 80.340 83.103 1.00 13.19 C ANISOU 6234 C GLY D 112 1655 1583 1772 0 -55 -147 C ATOM 6235 O GLY A 112 47.985 80.722 83.036 1.00 13.26 O ANISOU 6235 O GLY D 112 1593 1563 1879 98 -95 -256 O ATOM 6236 N GLU A 113 46.200 79.932 84.229 1.00 13.34 N ANISOU 6236 N GLU D 113 1638 1602 1827 -1 -105 -153 N ATOM 6237 CA GLU A 113 46.876 79.821 85.520 1.00 13.42 C ANISOU 6237 CA GLU D 113 1626 1655 1816 7 -77 -187 C ATOM 6238 C GLU A 113 46.346 78.681 86.371 1.00 13.02 C ANISOU 6238 C GLU D 113 1581 1685 1678 -13 -115 -262 C ATOM 6239 O GLU A 113 45.184 78.244 86.223 1.00 13.37 O ANISOU 6239 O GLU D 113 1496 1767 1814 22 -81 -387 O ATOM 6240 CB GLU A 113 46.726 81.095 86.356 1.00 13.62 C ANISOU 6240 CB GLU D 113 1708 1676 1788 3 -75 -144 C ATOM 6241 CG GLU A 113 47.468 82.285 85.826 1.00 15.12 C ANISOU 6241 CG GLU D 113 1911 1842 1990 16 -40 -200 C ATOM 6242 CD GLU A 113 47.434 83.438 86.806 1.00 15.45 C ANISOU 6242 CD GLU D 113 2006 1801 2061 164 37 -236 C ATOM 6243 OE1 GLU A 113 47.847 83.235 87.946 1.00 15.20 O ANISOU 6243 OE1 GLU D 113 1993 1742 2037 304 -95 -465 O ATOM 6244 OE2 GLU A 113 46.981 84.510 86.437 1.00 17.63 O ANISOU 6244 OE2 GLU D 113 2361 1888 2448 113 38 -433 O ATOM 6245 N ILE A 114 47.194 78.250 87.292 1.00 12.67 N ANISOU 6245 N ILE D 114 1563 1571 1677 10 -61 -305 N ATOM 6246 CA ILE A 114 46.842 77.334 88.355 1.00 12.98 C ANISOU 6246 CA ILE D 114 1638 1646 1645 39 -40 -283 C ATOM 6247 C ILE A 114 46.645 78.151 89.622 1.00 13.16 C ANISOU 6247 C ILE D 114 1640 1637 1721 82 -73 -293 C ATOM 6248 O ILE A 114 47.347 79.141 89.847 1.00 13.68 O ANISOU 6248 O ILE D 114 1606 1731 1858 217 -163 -377 O ATOM 6249 CB ILE A 114 47.947 76.251 88.550 1.00 13.10 C ANISOU 6249 CB ILE D 114 1680 1588 1708 42 1 -279 C ATOM 6250 CG1 ILE A 114 48.194 75.512 87.223 1.00 13.48 C ANISOU 6250 CG1 ILE D 114 1736 1774 1611 4 -74 -234 C ATOM 6251 CG2 ILE A 114 47.618 75.311 89.670 1.00 14.00 C ANISOU 6251 CG2 ILE D 114 1693 1925 1701 -53 -4 -288 C ATOM 6252 CD1 ILE A 114 46.950 74.900 86.589 1.00 14.56 C ANISOU 6252 CD1 ILE D 114 1902 2008 1621 -53 0 -124 C ATOM 6253 N GLN A 115 45.666 77.738 90.416 1.00 12.47 N ANISOU 6253 N GLN D 115 1525 1571 1642 35 -117 -311 N ATOM 6254 CA GLN A 115 45.424 78.284 91.756 1.00 11.90 C ANISOU 6254 CA GLN D 115 1369 1583 1568 -25 -71 -265 C ATOM 6255 C GLN A 115 45.543 77.161 92.763 1.00 12.21 C ANISOU 6255 C GLN D 115 1420 1575 1642 -50 -117 -291 C ATOM 6256 O GLN A 115 45.046 76.074 92.528 1.00 13.41 O ANISOU 6256 O GLN D 115 1544 1792 1759 82 -47 -384 O ATOM 6257 CB GLN A 115 44.006 78.868 91.854 1.00 11.50 C ANISOU 6257 CB GLN D 115 1368 1444 1556 -44 -107 -258 C ATOM 6258 CG GLN A 115 43.585 79.764 90.731 1.00 11.96 C ANISOU 6258 CG GLN D 115 1327 1520 1698 -89 -2 -277 C ATOM 6259 CD GLN A 115 42.169 80.255 90.951 1.00 11.87 C ANISOU 6259 CD GLN D 115 1425 1285 1800 -70 -97 -307 C ATOM 6260 OE1 GLN A 115 41.230 79.454 90.967 1.00 13.14 O ANISOU 6260 OE1 GLN D 115 1632 1473 1887 -46 -135 -552 O ATOM 6261 NE2 GLN A 115 42.013 81.570 91.164 1.00 11.74 N ANISOU 6261 NE2 GLN D 115 1648 1109 1704 -90 -89 -497 N ATOM 6262 N VAL A 116 46.191 77.404 93.895 1.00 11.82 N ANISOU 6262 N VAL D 116 1397 1548 1544 -100 -75 -309 N ATOM 6263 CA VAL A 116 46.294 76.377 94.914 1.00 12.19 C ANISOU 6263 CA VAL D 116 1432 1633 1566 17 -96 -254 C ATOM 6264 C VAL A 116 45.140 76.489 95.904 1.00 12.38 C ANISOU 6264 C VAL D 116 1449 1619 1637 -34 -123 -280 C ATOM 6265 O VAL A 116 44.990 77.533 96.538 1.00 13.07 O ANISOU 6265 O VAL D 116 1503 1662 1801 79 -152 -428 O ATOM 6266 CB VAL A 116 47.645 76.419 95.674 1.00 12.37 C ANISOU 6266 CB VAL D 116 1452 1701 1546 -18 -45 -208 C ATOM 6267 CG1 VAL A 116 47.699 75.329 96.705 1.00 13.31 C ANISOU 6267 CG1 VAL D 116 1570 1735 1751 52 3 -343 C ATOM 6268 CG2 VAL A 116 48.781 76.296 94.697 1.00 14.00 C ANISOU 6268 CG2 VAL D 116 1537 1911 1870 154 -19 -214 C ATOM 6269 N GLU A 117 44.361 75.412 96.025 1.00 12.65 N ANISOU 6269 N GLU D 117 1494 1719 1591 -21 -85 -278 N ATOM 6270 CA GLU A 117 43.290 75.298 97.023 1.00 12.81 C ANISOU 6270 CA GLU D 117 1588 1682 1595 35 -56 -252 C ATOM 6271 C GLU A 117 43.862 74.839 98.351 1.00 13.18 C ANISOU 6271 C GLU D 117 1701 1730 1574 -2 -25 -244 C ATOM 6272 O GLU A 117 44.395 73.743 98.465 1.00 13.54 O ANISOU 6272 O GLU D 117 1721 1919 1504 7 -69 -375 O ATOM 6273 CB GLU A 117 42.166 74.365 96.531 1.00 12.54 C ANISOU 6273 CB GLU D 117 1572 1646 1544 42 -25 -242 C ATOM 6274 CG GLU A 117 41.201 75.114 95.641 1.00 13.40 C ANISOU 6274 CG GLU D 117 1640 1786 1662 -96 -21 -340 C ATOM 6275 CD GLU A 117 40.140 75.861 96.428 1.00 15.20 C ANISOU 6275 CD GLU D 117 1802 2186 1785 -201 -19 -264 C ATOM 6276 OE1 GLU A 117 40.287 76.003 97.666 1.00 15.60 O ANISOU 6276 OE1 GLU D 117 1770 2198 1958 -180 -48 -407 O ATOM 6277 OE2 GLU A 117 39.178 76.321 95.803 1.00 16.87 O ANISOU 6277 OE2 GLU D 117 1992 2392 2025 -128 167 -551 O ATOM 6278 N LEU A 118 43.733 75.694 99.379 1.00 13.44 N ANISOU 6278 N LEU D 118 1792 1707 1604 2 -42 -262 N ATOM 6279 CA LEU A 118 44.366 75.439 100.674 1.00 14.70 C ANISOU 6279 CA LEU D 118 1886 1907 1790 -2 12 -202 C ATOM 6280 C LEU A 118 43.449 74.660 101.623 1.00 14.62 C ANISOU 6280 C LEU D 118 1917 1903 1735 19 28 -205 C ATOM 6281 O LEU A 118 42.371 75.155 102.041 1.00 15.48 O ANISOU 6281 O LEU D 118 1957 2044 1880 -10 69 -276 O ATOM 6282 CB LEU A 118 44.798 76.748 101.316 1.00 14.88 C ANISOU 6282 CB LEU D 118 1980 1905 1769 28 14 -194 C ATOM 6283 CG LEU A 118 45.754 77.600 100.495 1.00 16.80 C ANISOU 6283 CG LEU D 118 2130 2197 2056 18 -56 -187 C ATOM 6284 CD1 LEU A 118 45.893 78.969 101.104 1.00 16.68 C ANISOU 6284 CD1 LEU D 118 2263 2057 2015 30 -133 -135 C ATOM 6285 CD2 LEU A 118 47.141 76.938 100.387 1.00 16.93 C ANISOU 6285 CD2 LEU D 118 2052 2363 2014 -84 -24 -126 C ATOM 6286 N TYR A 119 43.874 73.437 101.919 1.00 15.61 N ANISOU 6286 N TYR D 119 1984 2121 1825 -50 65 -229 N ATOM 6287 CA TYR A 119 43.180 72.503 102.801 1.00 16.08 C ANISOU 6287 CA TYR D 119 2072 2101 1936 -10 8 -185 C ATOM 6288 C TYR A 119 44.166 71.794 103.726 1.00 17.81 C ANISOU 6288 C TYR D 119 2231 2378 2158 -15 11 -163 C ATOM 6289 O TYR A 119 45.322 71.555 103.362 1.00 17.83 O ANISOU 6289 O TYR D 119 2183 2421 2170 -35 -8 -226 O ATOM 6290 CB TYR A 119 42.397 71.439 101.999 1.00 16.02 C ANISOU 6290 CB TYR D 119 2034 2136 1914 -42 -2 -224 C ATOM 6291 CG TYR A 119 41.092 71.949 101.435 1.00 14.43 C ANISOU 6291 CG TYR D 119 1895 1863 1725 -51 -29 -190 C ATOM 6292 CD1 TYR A 119 39.884 71.698 102.086 1.00 15.87 C ANISOU 6292 CD1 TYR D 119 1932 2172 1926 0 -48 -159 C ATOM 6293 CD2 TYR A 119 41.065 72.746 100.299 1.00 13.32 C ANISOU 6293 CD2 TYR D 119 1679 1689 1690 8 5 -278 C ATOM 6294 CE1 TYR A 119 38.692 72.211 101.590 1.00 15.28 C ANISOU 6294 CE1 TYR D 119 2017 1927 1861 21 61 -148 C ATOM 6295 CE2 TYR A 119 39.900 73.225 99.801 1.00 13.18 C ANISOU 6295 CE2 TYR D 119 1749 1697 1562 74 81 -271 C ATOM 6296 CZ TYR A 119 38.718 72.974 100.449 1.00 14.14 C ANISOU 6296 CZ TYR D 119 1838 1826 1707 44 36 -195 C ATOM 6297 OH TYR A 119 37.564 73.484 99.914 1.00 12.91 O ANISOU 6297 OH TYR D 119 1795 1467 1642 39 174 -184 O ATOM 6298 N GLY A 120 43.700 71.441 104.924 1.00 19.46 N ANISOU 6298 N GLY D 120 2438 2601 2355 -25 0 -98 N ATOM 6299 CA GLY A 120 44.521 70.719 105.891 1.00 20.31 C ANISOU 6299 CA GLY D 120 2612 2645 2459 -17 15 -39 C ATOM 6300 C GLY A 120 45.736 71.522 106.355 1.00 21.41 C ANISOU 6300 C GLY D 120 2725 2788 2621 19 32 -42 C ATOM 6301 O GLY A 120 45.763 72.758 106.275 1.00 20.73 O ANISOU 6301 O GLY D 120 2646 2749 2480 29 97 -76 O ATOM 6302 N ASP A 121 46.751 70.796 106.812 1.00 22.95 N ANISOU 6302 N ASP D 121 2891 2974 2852 15 33 -46 N ATOM 6303 CA ASP A 121 47.961 71.392 107.378 1.00 24.34 C ANISOU 6303 CA ASP D 121 3064 3124 3056 12 37 -62 C ATOM 6304 C ASP A 121 48.991 71.741 106.311 1.00 24.53 C ANISOU 6304 C ASP D 121 3094 3149 3077 -18 35 -88 C ATOM 6305 O ASP A 121 50.056 71.139 106.260 1.00 25.38 O ANISOU 6305 O ASP D 121 3233 3256 3153 -119 25 -145 O ATOM 6306 CB ASP A 121 48.587 70.449 108.425 1.00 24.85 C ANISOU 6306 CB ASP D 121 3123 3165 3153 12 26 -41 C ATOM 6307 CG ASP A 121 47.597 70.002 109.475 1.00 26.74 C ANISOU 6307 CG ASP D 121 3430 3398 3329 28 30 0 C ATOM 6308 OD1 ASP A 121 46.931 70.869 110.071 1.00 27.36 O ANISOU 6308 OD1 ASP D 121 3506 3567 3323 16 17 -40 O ATOM 6309 OD2 ASP A 121 47.442 68.790 109.732 1.00 29.72 O ANISOU 6309 OD2 ASP D 121 3925 3603 3765 12 56 33 O ATOM 6310 N TRP A 122 48.682 72.724 105.473 1.00 24.44 N ANISOU 6310 N TRP D 122 3090 3139 3057 -11 35 -76 N ATOM 6311 CA TRP A 122 49.653 73.260 104.518 1.00 24.67 C ANISOU 6311 CA TRP D 122 3085 3166 3121 22 31 -71 C ATOM 6312 C TRP A 122 50.666 74.186 105.222 1.00 25.19 C ANISOU 6312 C TRP D 122 3145 3265 3160 32 19 -101 C ATOM 6313 O TRP A 122 50.396 74.692 106.312 1.00 25.48 O ANISOU 6313 O TRP D 122 3125 3373 3183 -2 1 -147 O ATOM 6314 CB TRP A 122 48.943 73.992 103.377 1.00 24.00 C ANISOU 6314 CB TRP D 122 3041 3024 3052 42 27 -58 C ATOM 6315 CG TRP A 122 48.196 75.194 103.830 1.00 23.36 C ANISOU 6315 CG TRP D 122 2916 2992 2965 9 15 -58 C ATOM 6316 CD1 TRP A 122 46.884 75.258 104.241 1.00 22.63 C ANISOU 6316 CD1 TRP D 122 2873 2852 2871 -6 105 -75 C ATOM 6317 CD2 TRP A 122 48.711 76.517 103.927 1.00 23.50 C ANISOU 6317 CD2 TRP D 122 2896 3062 2968 38 48 -118 C ATOM 6318 NE1 TRP A 122 46.564 76.552 104.591 1.00 22.72 N ANISOU 6318 NE1 TRP D 122 2903 2846 2881 -78 63 -191 N ATOM 6319 CE2 TRP A 122 47.668 77.346 104.401 1.00 22.59 C ANISOU 6319 CE2 TRP D 122 2795 2894 2893 -32 30 -117 C ATOM 6320 CE3 TRP A 122 49.964 77.091 103.675 1.00 22.91 C ANISOU 6320 CE3 TRP D 122 2730 3115 2857 -8 -71 -10 C ATOM 6321 CZ2 TRP A 122 47.842 78.710 104.619 1.00 23.79 C ANISOU 6321 CZ2 TRP D 122 3031 3058 2947 46 0 -101 C ATOM 6322 CZ3 TRP A 122 50.132 78.454 103.887 1.00 23.57 C ANISOU 6322 CZ3 TRP D 122 2880 3186 2890 -25 73 -73 C ATOM 6323 CH2 TRP A 122 49.078 79.246 104.354 1.00 23.21 C ANISOU 6323 CH2 TRP D 122 2853 3107 2858 14 32 -154 C ATOM 6324 N THR A 123 51.813 74.415 104.579 1.00 25.74 N ANISOU 6324 N THR D 123 3233 3353 3194 21 0 -91 N ATOM 6325 CA THR A 123 52.948 75.121 105.195 1.00 25.88 C ANISOU 6325 CA THR D 123 3256 3341 3233 14 6 -80 C ATOM 6326 C THR A 123 53.436 76.257 104.319 1.00 25.82 C ANISOU 6326 C THR D 123 3234 3340 3234 -5 12 -61 C ATOM 6327 O THR A 123 53.275 76.224 103.110 1.00 25.72 O ANISOU 6327 O THR D 123 3163 3397 3210 -25 11 -141 O ATOM 6328 CB THR A 123 54.155 74.168 105.485 1.00 25.91 C ANISOU 6328 CB THR D 123 3269 3346 3228 2 5 -50 C ATOM 6329 OG1 THR A 123 54.794 73.776 104.258 1.00 25.82 O ANISOU 6329 OG1 THR D 123 3271 3244 3295 28 20 -81 O ATOM 6330 CG2 THR A 123 53.720 72.881 106.174 1.00 26.76 C ANISOU 6330 CG2 THR D 123 3421 3475 3269 34 42 -71 C ATOM 6331 N TYR A 124 54.063 77.261 104.925 1.00 25.83 N ANISOU 6331 N TYR D 124 3271 3324 3216 19 56 -87 N ATOM 6332 CA TYR A 124 54.635 78.366 104.147 1.00 26.14 C ANISOU 6332 CA TYR D 124 3308 3346 3275 29 39 -71 C ATOM 6333 C TYR A 124 55.827 77.948 103.285 1.00 26.05 C ANISOU 6333 C TYR D 124 3303 3327 3265 32 55 -115 C ATOM 6334 O TYR A 124 56.124 78.613 102.286 1.00 25.80 O ANISOU 6334 O TYR D 124 3230 3337 3233 37 75 -177 O ATOM 6335 CB TYR A 124 55.014 79.555 105.041 1.00 26.35 C ANISOU 6335 CB TYR D 124 3369 3350 3291 17 60 -89 C ATOM 6336 CG TYR A 124 53.809 80.237 105.648 1.00 28.00 C ANISOU 6336 CG TYR D 124 3494 3636 3508 12 15 -41 C ATOM 6337 CD1 TYR A 124 52.871 80.889 104.834 1.00 28.29 C ANISOU 6337 CD1 TYR D 124 3569 3639 3539 24 76 -105 C ATOM 6338 CD2 TYR A 124 53.593 80.218 107.031 1.00 29.66 C ANISOU 6338 CD2 TYR D 124 3723 3913 3633 -52 34 -87 C ATOM 6339 CE1 TYR A 124 51.758 81.503 105.377 1.00 30.07 C ANISOU 6339 CE1 TYR D 124 3743 3941 3740 32 63 -89 C ATOM 6340 CE2 TYR A 124 52.473 80.823 107.588 1.00 30.77 C ANISOU 6340 CE2 TYR D 124 3923 4013 3754 -68 27 -120 C ATOM 6341 CZ TYR A 124 51.559 81.467 106.758 1.00 31.01 C ANISOU 6341 CZ TYR D 124 3914 4038 3828 -9 55 -109 C ATOM 6342 OH TYR A 124 50.444 82.069 107.301 1.00 31.95 O ANISOU 6342 OH TYR D 124 4027 4161 3948 -32 57 -169 O ATOM 6343 N ASP A 125 56.503 76.864 103.660 1.00 26.51 N ANISOU 6343 N ASP D 125 3340 3420 3311 11 55 -120 N ATOM 6344 CA ASP A 125 57.571 76.321 102.811 1.00 27.01 C ANISOU 6344 CA ASP D 125 3399 3508 3354 -3 39 -108 C ATOM 6345 C ASP A 125 56.972 75.704 101.550 1.00 25.72 C ANISOU 6345 C ASP D 125 3224 3363 3184 31 35 -96 C ATOM 6346 O ASP A 125 57.508 75.901 100.461 1.00 25.41 O ANISOU 6346 O ASP D 125 3109 3436 3109 64 43 -141 O ATOM 6347 CB ASP A 125 58.430 75.272 103.525 1.00 28.14 C ANISOU 6347 CB ASP D 125 3592 3600 3498 -9 22 -81 C ATOM 6348 CG ASP A 125 59.669 74.869 102.696 1.00 31.95 C ANISOU 6348 CG ASP D 125 3993 4059 4085 -18 -44 -102 C ATOM 6349 OD1 ASP A 125 60.648 75.657 102.665 1.00 35.69 O ANISOU 6349 OD1 ASP D 125 4385 4407 4768 46 -85 -81 O ATOM 6350 OD2 ASP A 125 59.702 73.787 102.044 1.00 34.18 O ANISOU 6350 OD2 ASP D 125 4501 4108 4377 -87 -92 -204 O ATOM 6351 N GLN A 126 55.870 74.967 101.707 1.00 24.60 N ANISOU 6351 N GLN D 126 3075 3221 3049 -28 44 -116 N ATOM 6352 CA GLN A 126 55.137 74.421 100.559 1.00 23.48 C ANISOU 6352 CA GLN D 126 2904 3103 2915 -6 37 -105 C ATOM 6353 C GLN A 126 54.713 75.583 99.681 1.00 22.34 C ANISOU 6353 C GLN D 126 2740 3014 2734 -27 49 -136 C ATOM 6354 O GLN A 126 54.828 75.522 98.466 1.00 22.56 O ANISOU 6354 O GLN D 126 2635 3223 2714 2 95 -197 O ATOM 6355 CB GLN A 126 53.915 73.601 100.997 1.00 23.52 C ANISOU 6355 CB GLN D 126 2936 3082 2918 0 11 -119 C ATOM 6356 CG GLN A 126 54.240 72.186 101.456 1.00 24.57 C ANISOU 6356 CG GLN D 126 3073 3244 3018 43 0 -63 C ATOM 6357 CD GLN A 126 53.129 71.533 102.291 1.00 25.65 C ANISOU 6357 CD GLN D 126 3219 3207 3318 84 -28 -49 C ATOM 6358 OE1 GLN A 126 52.074 72.134 102.549 1.00 26.30 O ANISOU 6358 OE1 GLN D 126 3314 3326 3352 89 -76 -150 O ATOM 6359 NE2 GLN A 126 53.364 70.291 102.701 1.00 26.73 N ANISOU 6359 NE2 GLN D 126 3331 3419 3404 63 117 -38 N ATOM 6360 N ALA A 127 54.252 76.665 100.299 1.00 21.00 N ANISOU 6360 N ALA D 127 2579 2795 2604 -6 88 -151 N ATOM 6361 CA ALA A 127 53.816 77.831 99.556 1.00 19.86 C ANISOU 6361 CA ALA D 127 2460 2614 2469 52 52 -141 C ATOM 6362 C ALA A 127 54.935 78.440 98.738 1.00 19.90 C ANISOU 6362 C ALA D 127 2416 2638 2504 39 75 -154 C ATOM 6363 O ALA A 127 54.700 78.908 97.626 1.00 19.58 O ANISOU 6363 O ALA D 127 2255 2665 2516 53 116 -256 O ATOM 6364 CB ALA A 127 53.201 78.867 100.484 1.00 20.06 C ANISOU 6364 CB ALA D 127 2516 2614 2490 51 53 -135 C ATOM 6365 N GLN A 128 56.149 78.464 99.293 1.00 19.86 N ANISOU 6365 N GLN D 128 2372 2666 2509 0 82 -138 N ATOM 6366 CA GLN A 128 57.276 79.026 98.560 1.00 20.62 C ANISOU 6366 CA GLN D 128 2505 2739 2590 14 76 -120 C ATOM 6367 C GLN A 128 57.650 78.132 97.368 1.00 19.99 C ANISOU 6367 C GLN D 128 2391 2703 2499 -27 50 -101 C ATOM 6368 O GLN A 128 57.987 78.653 96.309 1.00 20.06 O ANISOU 6368 O GLN D 128 2373 2759 2488 -28 30 -176 O ATOM 6369 CB GLN A 128 58.462 79.291 99.498 1.00 20.89 C ANISOU 6369 CB GLN D 128 2516 2783 2638 12 114 -118 C ATOM 6370 CG GLN A 128 59.654 80.001 98.861 1.00 21.92 C ANISOU 6370 CG GLN D 128 2662 2888 2778 79 71 -147 C ATOM 6371 CD GLN A 128 59.319 81.302 98.166 1.00 22.97 C ANISOU 6371 CD GLN D 128 2665 3027 3036 47 106 -223 C ATOM 6372 OE1 GLN A 128 58.839 82.261 98.789 1.00 24.61 O ANISOU 6372 OE1 GLN D 128 2822 3223 3303 159 122 -458 O ATOM 6373 NE2 GLN A 128 59.583 81.359 96.871 1.00 24.49 N ANISOU 6373 NE2 GLN D 128 2887 3278 3139 108 12 -265 N ATOM 6374 N GLN A 129 57.557 76.813 97.551 1.00 20.21 N ANISOU 6374 N GLN D 129 2389 2762 2526 -31 50 -92 N ATOM 6375 CA GLN A 129 57.670 75.833 96.455 1.00 20.28 C ANISOU 6375 CA GLN D 129 2429 2723 2553 -37 -18 -83 C ATOM 6376 C GLN A 129 56.682 76.120 95.298 1.00 19.31 C ANISOU 6376 C GLN D 129 2252 2629 2452 6 -37 -112 C ATOM 6377 O GLN A 129 57.041 76.067 94.115 1.00 18.68 O ANISOU 6377 O GLN D 129 2034 2606 2455 33 -76 -220 O ATOM 6378 CB GLN A 129 57.472 74.404 96.974 1.00 21.69 C ANISOU 6378 CB GLN D 129 2645 2892 2703 -20 4 -81 C ATOM 6379 CG GLN A 129 58.669 73.869 97.767 1.00 24.73 C ANISOU 6379 CG GLN D 129 3034 3218 3144 -55 79 5 C ATOM 6380 CD GLN A 129 58.460 72.467 98.354 1.00 30.43 C ANISOU 6380 CD GLN D 129 3792 3793 3976 -17 71 69 C ATOM 6381 OE1 GLN A 129 57.386 71.866 98.231 1.00 32.46 O ANISOU 6381 OE1 GLN D 129 4092 3972 4267 60 86 29 O ATOM 6382 NE2 GLN A 129 59.498 71.950 99.006 1.00 32.82 N ANISOU 6382 NE2 GLN D 129 4127 4153 4187 -35 158 40 N ATOM 6383 N TRP A 130 55.438 76.464 95.629 1.00 17.98 N ANISOU 6383 N TRP D 130 2090 2442 2300 -35 -58 -141 N ATOM 6384 CA TRP A 130 54.472 76.835 94.598 1.00 17.04 C ANISOU 6384 CA TRP D 130 1959 2304 2208 -8 -23 -168 C ATOM 6385 C TRP A 130 54.923 78.077 93.822 1.00 17.13 C ANISOU 6385 C TRP D 130 1951 2336 2222 -27 -19 -182 C ATOM 6386 O TRP A 130 54.942 78.076 92.607 1.00 16.75 O ANISOU 6386 O TRP D 130 1825 2369 2170 -9 -40 -275 O ATOM 6387 CB TRP A 130 53.045 77.009 95.174 1.00 16.66 C ANISOU 6387 CB TRP D 130 1895 2286 2148 -61 25 -196 C ATOM 6388 CG TRP A 130 52.597 75.872 96.017 1.00 16.19 C ANISOU 6388 CG TRP D 130 1789 2188 2175 40 39 -180 C ATOM 6389 CD1 TRP A 130 52.916 74.555 95.851 1.00 14.65 C ANISOU 6389 CD1 TRP D 130 1736 1897 1930 -100 85 -120 C ATOM 6390 CD2 TRP A 130 51.745 75.931 97.166 1.00 15.53 C ANISOU 6390 CD2 TRP D 130 1774 2095 2032 112 104 -187 C ATOM 6391 NE1 TRP A 130 52.315 73.786 96.824 1.00 15.85 N ANISOU 6391 NE1 TRP D 130 1792 1933 2298 209 31 -126 N ATOM 6392 CE2 TRP A 130 51.606 74.613 97.660 1.00 16.59 C ANISOU 6392 CE2 TRP D 130 1698 2356 2248 63 133 -69 C ATOM 6393 CE3 TRP A 130 51.100 76.971 97.838 1.00 17.16 C ANISOU 6393 CE3 TRP D 130 1896 2387 2235 40 82 -218 C ATOM 6394 CZ2 TRP A 130 50.845 74.315 98.799 1.00 18.19 C ANISOU 6394 CZ2 TRP D 130 2118 2434 2359 40 55 -127 C ATOM 6395 CZ3 TRP A 130 50.361 76.672 98.984 1.00 16.84 C ANISOU 6395 CZ3 TRP D 130 1903 2283 2211 175 61 -122 C ATOM 6396 CH2 TRP A 130 50.230 75.366 99.437 1.00 17.97 C ANISOU 6396 CH2 TRP D 130 2066 2417 2343 -65 105 -81 C ATOM 6397 N LEU A 131 55.273 79.158 94.520 1.00 17.16 N ANISOU 6397 N LEU D 131 2009 2297 2214 53 -6 -196 N ATOM 6398 CA LEU A 131 55.793 80.341 93.841 1.00 17.81 C ANISOU 6398 CA LEU D 131 2178 2326 2262 35 -27 -143 C ATOM 6399 C LEU A 131 57.020 80.022 92.968 1.00 18.41 C ANISOU 6399 C LEU D 131 2225 2400 2367 39 -44 -137 C ATOM 6400 O LEU A 131 57.143 80.535 91.860 1.00 18.65 O ANISOU 6400 O LEU D 131 2163 2588 2332 16 -62 -237 O ATOM 6401 CB LEU A 131 56.175 81.428 94.856 1.00 17.56 C ANISOU 6401 CB LEU D 131 2149 2224 2297 85 -31 -159 C ATOM 6402 CG LEU A 131 55.027 82.069 95.632 1.00 17.18 C ANISOU 6402 CG LEU D 131 2125 2166 2236 20 32 -187 C ATOM 6403 CD1 LEU A 131 55.622 83.012 96.698 1.00 17.37 C ANISOU 6403 CD1 LEU D 131 2010 2142 2448 57 37 -383 C ATOM 6404 CD2 LEU A 131 54.100 82.786 94.706 1.00 18.02 C ANISOU 6404 CD2 LEU D 131 2217 2264 2363 141 -50 -118 C ATOM 6405 N ASP A 132 57.909 79.185 93.482 1.00 19.48 N ANISOU 6405 N ASP D 132 2368 2585 2448 34 -18 -136 N ATOM 6406 CA ASP A 132 59.115 78.775 92.741 1.00 20.75 C ANISOU 6406 CA ASP D 132 2524 2746 2611 5 -27 -126 C ATOM 6407 C ASP A 132 58.761 77.980 91.484 1.00 20.76 C ANISOU 6407 C ASP D 132 2513 2760 2613 32 -67 -147 C ATOM 6408 O ASP A 132 59.564 77.908 90.547 1.00 21.02 O ANISOU 6408 O ASP D 132 2450 2903 2633 23 -127 -202 O ATOM 6409 CB ASP A 132 60.049 77.938 93.627 1.00 21.35 C ANISOU 6409 CB ASP D 132 2614 2823 2676 -19 22 -105 C ATOM 6410 CG ASP A 132 60.701 78.747 94.748 1.00 23.33 C ANISOU 6410 CG ASP D 132 2840 3077 2946 7 69 -122 C ATOM 6411 OD1 ASP A 132 60.608 79.986 94.742 1.00 23.61 O ANISOU 6411 OD1 ASP D 132 2688 3097 3183 64 151 -163 O ATOM 6412 OD2 ASP A 132 61.311 78.153 95.664 1.00 25.46 O ANISOU 6412 OD2 ASP D 132 2927 3583 3162 -172 108 -113 O ATOM 6413 N ALA A 133 57.556 77.403 91.472 1.00 20.24 N ANISOU 6413 N ALA D 133 2457 2663 2569 57 -55 -189 N ATOM 6414 CA ALA A 133 57.065 76.600 90.355 1.00 19.53 C ANISOU 6414 CA ALA D 133 2382 2568 2467 50 -48 -134 C ATOM 6415 C ALA A 133 56.233 77.437 89.403 1.00 18.90 C ANISOU 6415 C ALA D 133 2205 2527 2450 38 -54 -162 C ATOM 6416 O ALA A 133 55.668 76.914 88.432 1.00 19.65 O ANISOU 6416 O ALA D 133 2195 2713 2558 60 -41 -188 O ATOM 6417 CB ALA A 133 56.273 75.382 90.874 1.00 19.36 C ANISOU 6417 CB ALA D 133 2376 2521 2456 82 -17 -193 C ATOM 6418 N GLY A 134 56.188 78.743 89.655 1.00 17.39 N ANISOU 6418 N GLY D 134 2008 2293 2306 73 -73 -89 N ATOM 6419 CA GLY A 134 55.503 79.680 88.785 1.00 16.69 C ANISOU 6419 CA GLY D 134 1898 2202 2241 24 -78 -135 C ATOM 6420 C GLY A 134 54.018 79.844 89.074 1.00 16.42 C ANISOU 6420 C GLY D 134 1875 2144 2217 14 -59 -149 C ATOM 6421 O GLY A 134 53.302 80.427 88.272 1.00 16.99 O ANISOU 6421 O GLY D 134 1906 2188 2362 -34 -107 -231 O ATOM 6422 N ILE A 135 53.576 79.329 90.212 1.00 16.10 N ANISOU 6422 N ILE D 135 1801 2156 2159 -18 -26 -195 N ATOM 6423 CA ILE A 135 52.148 79.378 90.582 1.00 16.16 C ANISOU 6423 CA ILE D 135 1907 2162 2071 0 -76 -195 C ATOM 6424 C ILE A 135 51.977 80.382 91.720 1.00 16.62 C ANISOU 6424 C ILE D 135 2000 2170 2144 -34 -64 -194 C ATOM 6425 O ILE A 135 52.547 80.200 92.796 1.00 16.85 O ANISOU 6425 O ILE D 135 2040 2252 2108 -69 -200 -279 O ATOM 6426 CB ILE A 135 51.670 78.005 90.974 1.00 16.00 C ANISOU 6426 CB ILE D 135 1867 2142 2068 -39 -19 -154 C ATOM 6427 CG1 ILE A 135 51.787 77.081 89.756 1.00 16.41 C ANISOU 6427 CG1 ILE D 135 2008 2186 2039 -2 -39 -123 C ATOM 6428 CG2 ILE A 135 50.211 78.046 91.487 1.00 16.28 C ANISOU 6428 CG2 ILE D 135 1885 2208 2090 -25 -87 -272 C ATOM 6429 CD1 ILE A 135 51.819 75.654 90.070 1.00 16.63 C ANISOU 6429 CD1 ILE D 135 2064 2244 2007 -2 -110 -43 C ATOM 6430 N SER A 136 51.197 81.427 91.472 1.00 16.71 N ANISOU 6430 N SER D 136 2059 2097 2190 8 -52 -218 N ATOM 6431 CA SER A 136 51.132 82.549 92.414 1.00 17.23 C ANISOU 6431 CA SER D 136 2075 2189 2279 3 -34 -195 C ATOM 6432 C SER A 136 49.708 82.980 92.776 1.00 16.59 C ANISOU 6432 C SER D 136 1984 2062 2254 5 -39 -174 C ATOM 6433 O SER A 136 49.461 84.161 93.095 1.00 17.50 O ANISOU 6433 O SER D 136 1983 2183 2482 35 -35 -276 O ATOM 6434 CB SER A 136 51.914 83.724 91.850 1.00 16.98 C ANISOU 6434 CB SER D 136 2094 2131 2227 10 -52 -170 C ATOM 6435 OG SER A 136 51.328 84.200 90.677 1.00 18.58 O ANISOU 6435 OG SER D 136 2036 2547 2475 99 -27 -347 O ATOM 6436 N GLN A 137 48.782 82.023 92.715 1.00 15.69 N ANISOU 6436 N GLN D 137 1829 1973 2156 1 -27 -256 N ATOM 6437 CA GLN A 137 47.429 82.205 93.244 1.00 14.67 C ANISOU 6437 CA GLN D 137 1728 1900 1943 32 8 -233 C ATOM 6438 C GLN A 137 47.117 81.144 94.284 1.00 14.81 C ANISOU 6438 C GLN D 137 1759 1867 2002 63 21 -215 C ATOM 6439 O GLN A 137 47.495 79.968 94.134 1.00 15.15 O ANISOU 6439 O GLN D 137 1710 1918 2127 192 -16 -264 O ATOM 6440 CB GLN A 137 46.378 82.183 92.126 1.00 14.44 C ANISOU 6440 CB GLN D 137 1675 1909 1900 -41 -7 -259 C ATOM 6441 CG GLN A 137 46.370 83.352 91.167 1.00 14.77 C ANISOU 6441 CG GLN D 137 1834 1896 1882 -15 1 -312 C ATOM 6442 CD GLN A 137 45.023 83.482 90.455 1.00 16.36 C ANISOU 6442 CD GLN D 137 1988 2239 1989 80 21 -219 C ATOM 6443 OE1 GLN A 137 43.992 83.536 91.109 1.00 16.08 O ANISOU 6443 OE1 GLN D 137 1825 2240 2045 115 0 -476 O ATOM 6444 NE2 GLN A 137 45.032 83.536 89.115 1.00 15.95 N ANISOU 6444 NE2 GLN D 137 2094 2110 1857 118 -122 -301 N ATOM 6445 N ALA A 138 46.407 81.556 95.341 1.00 14.10 N ANISOU 6445 N ALA D 138 1747 1700 1909 41 -17 -211 N ATOM 6446 CA ALA A 138 45.998 80.639 96.391 1.00 14.71 C ANISOU 6446 CA ALA D 138 1783 1944 1861 34 14 -178 C ATOM 6447 C ALA A 138 44.615 80.990 96.901 1.00 14.72 C ANISOU 6447 C ALA D 138 1798 1896 1900 -8 -31 -152 C ATOM 6448 O ALA A 138 44.248 82.152 96.918 1.00 15.41 O ANISOU 6448 O ALA D 138 1844 2113 1896 -15 -24 -222 O ATOM 6449 CB ALA A 138 47.002 80.622 97.546 1.00 15.36 C ANISOU 6449 CB ALA D 138 1843 2046 1944 -22 18 -119 C ATOM 6450 N ILE A 139 43.877 79.962 97.313 1.00 14.58 N ANISOU 6450 N ILE D 139 1703 1995 1841 57 -35 -203 N ATOM 6451 CA ILE A 139 42.500 80.110 97.766 1.00 14.11 C ANISOU 6451 CA ILE D 139 1675 1886 1799 68 -33 -190 C ATOM 6452 C ILE A 139 42.452 79.775 99.241 1.00 13.81 C ANISOU 6452 C ILE D 139 1609 1837 1800 115 -44 -216 C ATOM 6453 O ILE A 139 42.664 78.638 99.649 1.00 13.14 O ANISOU 6453 O ILE D 139 1449 1860 1680 132 -86 -369 O ATOM 6454 CB ILE A 139 41.526 79.183 96.989 1.00 14.23 C ANISOU 6454 CB ILE D 139 1689 1954 1763 76 8 -157 C ATOM 6455 CG1 ILE A 139 41.847 79.133 95.488 1.00 14.94 C ANISOU 6455 CG1 ILE D 139 1774 2052 1850 6 5 -124 C ATOM 6456 CG2 ILE A 139 40.078 79.567 97.288 1.00 13.90 C ANISOU 6456 CG2 ILE D 139 1718 1958 1606 79 -6 -249 C ATOM 6457 CD1 ILE A 139 41.634 80.372 94.765 1.00 15.50 C ANISOU 6457 CD1 ILE D 139 1996 2015 1878 181 7 -107 C ATOM 6458 N TYR A 140 42.184 80.801 100.048 1.00 14.02 N ANISOU 6458 N TYR D 140 1671 1788 1866 74 -42 -269 N ATOM 6459 CA TYR A 140 42.124 80.671 101.489 1.00 14.67 C ANISOU 6459 CA TYR D 140 1772 1865 1936 83 -26 -187 C ATOM 6460 C TYR A 140 40.679 80.684 101.991 1.00 13.96 C ANISOU 6460 C TYR D 140 1696 1811 1796 101 11 -251 C ATOM 6461 O TYR A 140 39.914 81.558 101.630 1.00 14.16 O ANISOU 6461 O TYR D 140 1573 1883 1923 251 -30 -355 O ATOM 6462 CB TYR A 140 42.904 81.819 102.150 1.00 15.01 C ANISOU 6462 CB TYR D 140 1829 1839 2032 43 -68 -227 C ATOM 6463 CG TYR A 140 43.081 81.621 103.631 1.00 17.22 C ANISOU 6463 CG TYR D 140 2178 2219 2145 -84 -23 -167 C ATOM 6464 CD1 TYR A 140 44.149 80.872 104.137 1.00 20.13 C ANISOU 6464 CD1 TYR D 140 2540 2708 2400 -150 -14 -140 C ATOM 6465 CD2 TYR A 140 42.139 82.114 104.546 1.00 18.34 C ANISOU 6465 CD2 TYR D 140 2287 2237 2443 -89 -93 -170 C ATOM 6466 CE1 TYR A 140 44.287 80.651 105.504 1.00 22.36 C ANISOU 6466 CE1 TYR D 140 2753 3088 2654 -101 64 -154 C ATOM 6467 CE2 TYR A 140 42.275 81.889 105.903 1.00 19.71 C ANISOU 6467 CE2 TYR D 140 2524 2486 2479 -109 -34 -281 C ATOM 6468 CZ TYR A 140 43.347 81.170 106.382 1.00 22.14 C ANISOU 6468 CZ TYR D 140 2677 3007 2727 -106 0 -90 C ATOM 6469 OH TYR A 140 43.499 80.963 107.732 1.00 24.03 O ANISOU 6469 OH TYR D 140 2797 3423 2909 -103 -40 -229 O ATOM 6470 N HIS A 141 40.356 79.704 102.826 1.00 14.51 N ANISOU 6470 N HIS D 141 1823 1918 1768 53 13 -273 N ATOM 6471 CA HIS A 141 39.006 79.461 103.323 1.00 15.44 C ANISOU 6471 CA HIS D 141 1948 2067 1851 -41 -6 -207 C ATOM 6472 C HIS A 141 38.862 79.900 104.790 1.00 16.30 C ANISOU 6472 C HIS D 141 2093 2195 1903 -73 35 -222 C ATOM 6473 O HIS A 141 39.720 79.609 105.614 1.00 15.78 O ANISOU 6473 O HIS D 141 2067 2056 1871 -148 51 -306 O ATOM 6474 CB HIS A 141 38.694 77.960 103.258 1.00 16.01 C ANISOU 6474 CB HIS D 141 2010 2173 1898 6 -23 -197 C ATOM 6475 CG HIS A 141 38.633 77.418 101.863 1.00 16.29 C ANISOU 6475 CG HIS D 141 2015 2205 1969 -120 -106 -296 C ATOM 6476 ND1 HIS A 141 37.453 77.029 101.272 1.00 16.09 N ANISOU 6476 ND1 HIS D 141 1980 2303 1830 -133 -135 -376 N ATOM 6477 CD2 HIS A 141 39.602 77.213 100.940 1.00 16.98 C ANISOU 6477 CD2 HIS D 141 1999 2385 2065 -10 -73 -212 C ATOM 6478 CE1 HIS A 141 37.697 76.610 100.040 1.00 17.56 C ANISOU 6478 CE1 HIS D 141 2024 2436 2212 -110 -58 -295 C ATOM 6479 NE2 HIS A 141 38.992 76.715 99.813 1.00 15.80 N ANISOU 6479 NE2 HIS D 141 1906 2126 1971 -122 -136 -386 N ATOM 6480 N GLN A 142 37.759 80.572 105.109 1.00 17.17 N ANISOU 6480 N GLN D 142 2146 2314 2064 -95 28 -163 N ATOM 6481 CA GLN A 142 37.391 80.830 106.507 1.00 18.79 C ANISOU 6481 CA GLN D 142 2390 2479 2270 -50 -27 -155 C ATOM 6482 C GLN A 142 37.599 79.580 107.345 1.00 19.05 C ANISOU 6482 C GLN D 142 2356 2516 2366 -56 -54 -161 C ATOM 6483 O GLN A 142 37.100 78.511 106.995 1.00 19.54 O ANISOU 6483 O GLN D 142 2428 2548 2447 -7 -53 -244 O ATOM 6484 CB GLN A 142 35.918 81.245 106.614 1.00 18.72 C ANISOU 6484 CB GLN D 142 2330 2485 2298 -48 -39 -135 C ATOM 6485 CG GLN A 142 35.498 81.651 108.051 1.00 20.86 C ANISOU 6485 CG GLN D 142 2669 2690 2564 -21 -79 -173 C ATOM 6486 CD GLN A 142 33.997 81.647 108.268 1.00 23.12 C ANISOU 6486 CD GLN D 142 2847 2892 3043 -24 -84 -225 C ATOM 6487 OE1 GLN A 142 33.283 80.769 107.772 1.00 23.09 O ANISOU 6487 OE1 GLN D 142 2972 2834 2964 -5 -75 -499 O ATOM 6488 NE2 GLN A 142 33.509 82.628 109.026 1.00 23.32 N ANISOU 6488 NE2 GLN D 142 3065 2850 2943 30 -100 -444 N ATOM 6489 N SER A 143 38.322 79.694 108.456 1.00 19.71 N ANISOU 6489 N SER D 143 2446 2613 2428 -72 -56 -175 N ATOM 6490 CA SER A 143 38.550 78.527 109.284 1.00 20.60 C ANISOU 6490 CA SER D 143 2521 2768 2537 -21 -39 -117 C ATOM 6491 C SER A 143 37.239 78.133 109.906 1.00 21.91 C ANISOU 6491 C SER D 143 2712 2899 2713 -14 -34 -105 C ATOM 6492 O SER A 143 36.537 78.980 110.471 1.00 21.53 O ANISOU 6492 O SER D 143 2607 2958 2613 -15 0 -124 O ATOM 6493 CB SER A 143 39.596 78.808 110.347 1.00 20.89 C ANISOU 6493 CB SER D 143 2533 2810 2591 -12 -29 -131 C ATOM 6494 OG SER A 143 40.871 78.799 109.740 1.00 21.41 O ANISOU 6494 OG SER D 143 2511 2975 2646 13 -34 -225 O ATOM 6495 N ARG A 144 36.892 76.858 109.764 1.00 23.58 N ANISOU 6495 N ARG D 144 2930 3054 2972 22 -69 -109 N ATOM 6496 CA ARG A 144 35.610 76.390 110.255 1.00 25.69 C ANISOU 6496 CA ARG D 144 3203 3261 3296 22 -61 -73 C ATOM 6497 C ARG A 144 35.624 76.272 111.770 1.00 25.63 C ANISOU 6497 C ARG D 144 3198 3217 3320 19 -71 -44 C ATOM 6498 O ARG A 144 34.586 76.487 112.407 1.00 26.42 O ANISOU 6498 O ARG D 144 3232 3328 3475 -15 -91 -109 O ATOM 6499 CB ARG A 144 35.143 75.124 109.527 1.00 26.70 C ANISOU 6499 CB ARG D 144 3358 3368 3415 41 -61 -64 C ATOM 6500 CG ARG A 144 34.301 75.481 108.273 1.00 29.66 C ANISOU 6500 CG ARG D 144 3796 3766 3706 -14 -14 -13 C ATOM 6501 CD ARG A 144 34.220 74.369 107.219 1.00 33.75 C ANISOU 6501 CD ARG D 144 4390 4239 4192 19 23 -48 C ATOM 6502 NE ARG A 144 34.257 74.891 105.844 1.00 35.46 N ANISOU 6502 NE ARG D 144 4624 4470 4377 -33 -12 -12 N ATOM 6503 CZ ARG A 144 34.115 74.140 104.746 1.00 36.69 C ANISOU 6503 CZ ARG D 144 4751 4620 4569 14 33 -2 C ATOM 6504 NH1 ARG A 144 33.916 72.824 104.847 1.00 36.52 N ANISOU 6504 NH1 ARG D 144 4736 4596 4542 38 47 -9 N ATOM 6505 NH2 ARG A 144 34.178 74.705 103.535 1.00 36.61 N ANISOU 6505 NH2 ARG D 144 4746 4491 4671 -5 44 17 N ATOM 6506 N ASP A 145 36.786 75.988 112.357 1.00 25.08 N ANISOU 6506 N ASP D 145 3150 3094 3283 23 -50 -34 N ATOM 6507 CA ASP A 145 36.902 76.020 113.817 1.00 25.06 C ANISOU 6507 CA ASP D 145 3152 3133 3235 -1 -48 -1 C ATOM 6508 C ASP A 145 36.726 77.431 114.415 1.00 23.30 C ANISOU 6508 C ASP D 145 2934 2903 3015 -9 -55 2 C ATOM 6509 O ASP A 145 36.206 77.568 115.529 1.00 23.77 O ANISOU 6509 O ASP D 145 2958 2987 3086 -31 -36 32 O ATOM 6510 CB ASP A 145 38.173 75.320 114.353 1.00 25.92 C ANISOU 6510 CB ASP D 145 3266 3228 3354 -7 -38 27 C ATOM 6511 CG ASP A 145 39.462 75.750 113.640 1.00 29.57 C ANISOU 6511 CG ASP D 145 3690 3715 3830 4 -74 21 C ATOM 6512 OD1 ASP A 145 39.576 76.918 113.212 1.00 33.15 O ANISOU 6512 OD1 ASP D 145 4195 4150 4248 -37 -95 110 O ATOM 6513 OD2 ASP A 145 40.405 74.935 113.501 1.00 32.74 O ANISOU 6513 OD2 ASP D 145 3923 4225 4291 -49 -132 30 O ATOM 6514 N ALA A 146 37.143 78.466 113.677 1.00 21.21 N ANISOU 6514 N ALA D 146 2625 2682 2749 -59 -70 -38 N ATOM 6515 CA ALA A 146 36.933 79.854 114.100 1.00 19.63 C ANISOU 6515 CA ALA D 146 2477 2476 2504 -2 -69 -70 C ATOM 6516 C ALA A 146 35.435 80.191 114.038 1.00 19.30 C ANISOU 6516 C ALA D 146 2459 2430 2442 -31 -68 -107 C ATOM 6517 O ALA A 146 34.890 80.845 114.941 1.00 18.78 O ANISOU 6517 O ALA D 146 2507 2344 2281 -46 -152 -183 O ATOM 6518 CB ALA A 146 37.738 80.821 113.215 1.00 19.34 C ANISOU 6518 CB ALA D 146 2446 2431 2469 -11 -59 -73 C ATOM 6519 N LEU A 147 34.774 79.747 112.968 1.00 19.16 N ANISOU 6519 N LEU D 147 2467 2439 2372 -21 -65 -100 N ATOM 6520 CA LEU A 147 33.327 79.921 112.792 1.00 19.80 C ANISOU 6520 CA LEU D 147 2499 2543 2481 -2 -28 -103 C ATOM 6521 C LEU A 147 32.557 79.332 113.958 1.00 20.40 C ANISOU 6521 C LEU D 147 2537 2639 2576 10 -14 -91 C ATOM 6522 O LEU A 147 31.603 79.934 114.462 1.00 20.32 O ANISOU 6522 O LEU D 147 2463 2609 2645 -54 -65 -156 O ATOM 6523 CB LEU A 147 32.872 79.256 111.488 1.00 19.98 C ANISOU 6523 CB LEU D 147 2500 2617 2473 15 3 -134 C ATOM 6524 N LEU A 148 32.978 78.151 114.390 1.00 20.82 N ANISOU 6524 N LEU D 148 2635 2600 2675 -5 -59 -100 N ATOM 6525 CA LEU A 148 32.322 77.458 115.499 1.00 21.48 C ANISOU 6525 CA LEU D 148 2725 2690 2746 32 -90 -18 C ATOM 6526 C LEU A 148 32.602 78.122 116.863 1.00 20.85 C ANISOU 6526 C LEU D 148 2664 2585 2669 31 -115 0 C ATOM 6527 O LEU A 148 31.795 78.029 117.804 1.00 21.03 O ANISOU 6527 O LEU D 148 2741 2576 2672 48 -218 1 O ATOM 6528 CB LEU A 148 32.658 75.962 115.473 1.00 22.42 C ANISOU 6528 CB LEU D 148 2824 2823 2871 20 -90 -23 C ATOM 6529 CG LEU A 148 32.151 75.235 114.210 1.00 24.72 C ANISOU 6529 CG LEU D 148 3121 3133 3137 58 -62 13 C ATOM 6530 CD1 LEU A 148 32.778 73.853 114.115 1.00 26.67 C ANISOU 6530 CD1 LEU D 148 3489 3235 3408 20 -62 -24 C ATOM 6531 CD2 LEU A 148 30.605 75.158 114.111 1.00 25.85 C ANISOU 6531 CD2 LEU D 148 3297 3307 3215 45 -25 -18 C ATOM 6532 N ALA A 149 33.712 78.829 116.963 1.00 19.39 N ANISOU 6532 N ALA D 149 2535 2379 2450 24 -105 -8 N ATOM 6533 CA ALA A 149 33.965 79.630 118.141 1.00 18.36 C ANISOU 6533 CA ALA D 149 2417 2247 2312 18 -34 7 C ATOM 6534 C ALA A 149 33.234 80.981 118.114 1.00 17.82 C ANISOU 6534 C ALA D 149 2322 2203 2244 0 -74 -25 C ATOM 6535 O ALA A 149 33.245 81.709 119.080 1.00 17.80 O ANISOU 6535 O ALA D 149 2386 2086 2289 14 -65 -49 O ATOM 6536 CB ALA A 149 35.443 79.825 118.310 1.00 18.54 C ANISOU 6536 CB ALA D 149 2466 2269 2310 -24 -41 43 C ATOM 6537 N GLY A 150 32.628 81.304 116.983 1.00 17.09 N ANISOU 6537 N GLY D 150 2113 2141 2237 16 -71 -64 N ATOM 6538 CA GLY A 150 31.867 82.525 116.843 1.00 17.04 C ANISOU 6538 CA GLY D 150 2073 2147 2252 -12 -81 -14 C ATOM 6539 C GLY A 150 32.625 83.718 116.260 1.00 17.61 C ANISOU 6539 C GLY D 150 2145 2243 2303 -16 -76 -23 C ATOM 6540 O GLY A 150 32.162 84.849 116.319 1.00 16.98 O ANISOU 6540 O GLY D 150 1939 2222 2288 -64 -163 -102 O ATOM 6541 N GLU A 151 33.779 83.463 115.662 1.00 18.16 N ANISOU 6541 N GLU D 151 2203 2326 2368 -91 -91 -70 N ATOM 6542 CA GLU A 151 34.442 84.510 114.911 1.00 19.52 C ANISOU 6542 CA GLU D 151 2465 2488 2461 -55 -65 -62 C ATOM 6543 C GLU A 151 33.812 84.608 113.532 1.00 19.50 C ANISOU 6543 C GLU D 151 2488 2457 2462 -73 -60 -102 C ATOM 6544 O GLU A 151 33.093 83.728 113.131 1.00 19.39 O ANISOU 6544 O GLU D 151 2533 2598 2235 -61 -90 -119 O ATOM 6545 CB GLU A 151 35.924 84.220 114.791 1.00 20.38 C ANISOU 6545 CB GLU D 151 2564 2552 2625 -16 -90 -70 C ATOM 6546 CG GLU A 151 36.746 84.899 115.819 1.00 24.93 C ANISOU 6546 CG GLU D 151 3081 3360 3029 -48 -22 -99 C ATOM 6547 CD GLU A 151 37.827 84.008 116.351 1.00 30.82 C ANISOU 6547 CD GLU D 151 3906 3998 3806 -117 4 -2 C ATOM 6548 OE1 GLU A 151 38.545 83.419 115.530 1.00 33.98 O ANISOU 6548 OE1 GLU D 151 4259 4482 4167 -91 -57 -160 O ATOM 6549 OE2 GLU A 151 37.975 83.906 117.582 1.00 32.97 O ANISOU 6549 OE2 GLU D 151 4172 4456 3899 -52 -74 -95 O ATOM 6550 N THR A 152 34.072 85.702 112.842 1.00 20.45 N ANISOU 6550 N THR D 152 2640 2645 2484 -39 -61 -69 N ATOM 6551 CA THR A 152 33.816 85.778 111.427 1.00 21.91 C ANISOU 6551 CA THR D 152 2828 2736 2758 -20 -60 -25 C ATOM 6552 C THR A 152 35.104 85.594 110.632 1.00 22.39 C ANISOU 6552 C THR D 152 2932 2766 2808 -35 -83 -13 C ATOM 6553 O THR A 152 35.506 84.460 110.357 1.00 23.35 O ANISOU 6553 O THR D 152 3068 2803 2999 -8 -111 1 O ATOM 6554 CB THR A 152 33.079 87.074 111.067 1.00 22.04 C ANISOU 6554 CB THR D 152 2849 2773 2752 -10 -65 -65 C ATOM 6555 OG1 THR A 152 33.720 88.171 111.710 1.00 23.38 O ANISOU 6555 OG1 THR D 152 3082 2842 2956 63 -87 -11 O ATOM 6556 CG2 THR A 152 31.641 86.973 111.571 1.00 22.73 C ANISOU 6556 CG2 THR D 152 2898 2834 2902 -53 -48 14 C ATOM 6557 N TRP A 153 35.727 86.713 110.276 1.00 22.09 N ANISOU 6557 N TRP D 153 2850 2692 2850 8 -37 -44 N ATOM 6558 CA TRP A 153 37.125 86.780 109.913 1.00 21.23 C ANISOU 6558 CA TRP D 153 2775 2593 2696 0 7 -90 C ATOM 6559 C TRP A 153 38.002 87.396 110.998 1.00 21.59 C ANISOU 6559 C TRP D 153 2827 2666 2708 5 6 -48 C ATOM 6560 O TRP A 153 38.121 88.598 111.102 1.00 21.95 O ANISOU 6560 O TRP D 153 2982 2614 2743 47 23 -72 O ATOM 6561 CB TRP A 153 37.292 87.504 108.586 1.00 20.75 C ANISOU 6561 CB TRP D 153 2693 2581 2610 9 11 -130 C ATOM 6562 CG TRP A 153 36.838 86.647 107.438 1.00 19.21 C ANISOU 6562 CG TRP D 153 2420 2460 2419 5 -11 -203 C ATOM 6563 CD1 TRP A 153 35.572 86.493 106.981 1.00 18.29 C ANISOU 6563 CD1 TRP D 153 2239 2447 2262 -97 -68 -223 C ATOM 6564 CD2 TRP A 153 37.655 85.777 106.648 1.00 18.09 C ANISOU 6564 CD2 TRP D 153 2280 2385 2205 -60 16 -198 C ATOM 6565 NE1 TRP A 153 35.542 85.607 105.933 1.00 18.48 N ANISOU 6565 NE1 TRP D 153 2166 2554 2302 13 27 -278 N ATOM 6566 CE2 TRP A 153 36.808 85.140 105.720 1.00 18.43 C ANISOU 6566 CE2 TRP D 153 2281 2404 2314 -4 -66 -273 C ATOM 6567 CE3 TRP A 153 39.016 85.489 106.624 1.00 16.46 C ANISOU 6567 CE3 TRP D 153 2146 1891 2215 119 -17 -172 C ATOM 6568 CZ2 TRP A 153 37.290 84.242 104.774 1.00 18.60 C ANISOU 6568 CZ2 TRP D 153 2352 2419 2293 58 -41 -314 C ATOM 6569 CZ3 TRP A 153 39.482 84.599 105.703 1.00 18.33 C ANISOU 6569 CZ3 TRP D 153 2361 2310 2291 91 -104 -211 C ATOM 6570 CH2 TRP A 153 38.624 83.981 104.786 1.00 18.61 C ANISOU 6570 CH2 TRP D 153 2302 2432 2335 -20 33 -241 C ATOM 6571 N GLY A 154 38.586 86.543 111.813 1.00 21.32 N ANISOU 6571 N GLY D 154 2779 2649 2670 -28 19 -59 N ATOM 6572 CA GLY A 154 39.378 87.002 112.924 1.00 21.15 C ANISOU 6572 CA GLY D 154 2765 2650 2620 23 23 -96 C ATOM 6573 C GLY A 154 40.820 87.175 112.522 1.00 21.10 C ANISOU 6573 C GLY D 154 2789 2669 2557 34 -9 -113 C ATOM 6574 O GLY A 154 41.180 86.938 111.403 1.00 19.84 O ANISOU 6574 O GLY D 154 2787 2420 2328 96 -4 -252 O ATOM 6575 N GLU A 155 41.646 87.566 113.483 1.00 21.92 N ANISOU 6575 N GLU D 155 2909 2774 2643 63 15 -151 N ATOM 6576 CA GLU A 155 43.027 87.898 113.230 1.00 22.71 C ANISOU 6576 CA GLU D 155 2940 2911 2776 13 14 -123 C ATOM 6577 C GLU A 155 43.876 86.718 112.788 1.00 22.77 C ANISOU 6577 C GLU D 155 2953 2930 2766 39 30 -136 C ATOM 6578 O GLU A 155 44.781 86.880 111.986 1.00 22.72 O ANISOU 6578 O GLU D 155 2926 2984 2721 9 -1 -206 O ATOM 6579 CB GLU A 155 43.654 88.537 114.462 1.00 23.21 C ANISOU 6579 CB GLU D 155 3012 2942 2865 38 44 -107 C ATOM 6580 CG GLU A 155 43.002 89.840 114.838 1.00 24.25 C ANISOU 6580 CG GLU D 155 3211 3043 2960 -2 13 -191 C ATOM 6581 CD GLU A 155 43.247 90.908 113.804 1.00 25.34 C ANISOU 6581 CD GLU D 155 3401 3185 3040 24 62 -243 C ATOM 6582 OE1 GLU A 155 44.417 91.110 113.462 1.00 27.42 O ANISOU 6582 OE1 GLU D 155 3433 3665 3318 115 1 -179 O ATOM 6583 OE2 GLU A 155 42.282 91.541 113.335 1.00 26.05 O ANISOU 6583 OE2 GLU D 155 3485 3214 3196 -53 161 -397 O ATOM 6584 N LYS A 156 43.611 85.557 113.355 1.00 22.85 N ANISOU 6584 N LYS D 156 2941 2950 2790 10 45 -114 N ATOM 6585 CA LYS A 156 44.306 84.338 112.914 1.00 23.26 C ANISOU 6585 CA LYS D 156 2954 3019 2862 -6 25 -97 C ATOM 6586 C LYS A 156 44.168 84.130 111.398 1.00 22.95 C ANISOU 6586 C LYS D 156 2890 2990 2837 13 4 -121 C ATOM 6587 O LYS A 156 45.170 83.961 110.694 1.00 23.44 O ANISOU 6587 O LYS D 156 2899 3117 2889 3 25 -208 O ATOM 6588 CB LYS A 156 43.793 83.113 113.680 1.00 23.56 C ANISOU 6588 CB LYS D 156 2988 3063 2899 16 25 -85 C ATOM 6589 N ASP A 157 42.940 84.169 110.895 1.00 21.91 N ANISOU 6589 N ASP D 157 2741 2858 2725 -43 -10 -126 N ATOM 6590 CA ASP A 157 42.696 83.983 109.458 1.00 21.36 C ANISOU 6590 CA ASP D 157 2714 2760 2639 -19 -20 -153 C ATOM 6591 C ASP A 157 43.243 85.149 108.631 1.00 20.97 C ANISOU 6591 C ASP D 157 2658 2658 2649 -11 -30 -188 C ATOM 6592 O ASP A 157 43.866 84.953 107.576 1.00 20.19 O ANISOU 6592 O ASP D 157 2585 2554 2530 36 -45 -356 O ATOM 6593 CB ASP A 157 41.195 83.793 109.148 1.00 21.16 C ANISOU 6593 CB ASP D 157 2642 2783 2613 -53 -47 -135 C ATOM 6594 CG ASP A 157 40.702 82.364 109.340 1.00 21.25 C ANISOU 6594 CG ASP D 157 2656 2879 2537 -24 28 -205 C ATOM 6595 OD1 ASP A 157 41.497 81.403 109.457 1.00 20.92 O ANISOU 6595 OD1 ASP D 157 2501 2988 2459 -43 106 -312 O ATOM 6596 OD2 ASP A 157 39.466 82.146 109.366 1.00 20.94 O ANISOU 6596 OD2 ASP D 157 2655 2833 2466 58 -4 -461 O ATOM 6597 N LEU A 158 43.012 86.380 109.093 1.00 20.96 N ANISOU 6597 N LEU D 158 2688 2620 2654 -23 -7 -210 N ATOM 6598 CA LEU A 158 43.470 87.545 108.351 1.00 20.99 C ANISOU 6598 CA LEU D 158 2690 2628 2655 -18 0 -147 C ATOM 6599 C LEU A 158 44.993 87.629 108.291 1.00 21.34 C ANISOU 6599 C LEU D 158 2733 2654 2720 -7 9 -164 C ATOM 6600 O LEU A 158 45.521 88.124 107.310 1.00 20.91 O ANISOU 6600 O LEU D 158 2661 2653 2630 22 32 -217 O ATOM 6601 CB LEU A 158 42.893 88.859 108.922 1.00 20.89 C ANISOU 6601 CB LEU D 158 2703 2565 2669 -50 5 -129 C ATOM 6602 CG LEU A 158 41.385 89.033 108.819 1.00 21.66 C ANISOU 6602 CG LEU D 158 2798 2647 2782 -44 0 -142 C ATOM 6603 CD1 LEU A 158 40.936 90.282 109.643 1.00 22.14 C ANISOU 6603 CD1 LEU D 158 2935 2689 2788 -14 24 -268 C ATOM 6604 CD2 LEU A 158 40.936 89.174 107.368 1.00 20.75 C ANISOU 6604 CD2 LEU D 158 2741 2515 2626 -26 72 -131 C ATOM 6605 N ASN A 159 45.675 87.137 109.328 1.00 21.95 N ANISOU 6605 N ASN D 159 2822 2739 2778 -4 11 -160 N ATOM 6606 CA ASN A 159 47.149 87.133 109.378 1.00 23.05 C ANISOU 6606 CA ASN D 159 2970 2896 2891 -7 1 -137 C ATOM 6607 C ASN A 159 47.758 86.220 108.314 1.00 22.99 C ANISOU 6607 C ASN D 159 2960 2868 2907 7 -9 -149 C ATOM 6608 O ASN A 159 48.764 86.569 107.694 1.00 22.71 O ANISOU 6608 O ASN D 159 2975 2853 2799 20 11 -242 O ATOM 6609 CB ASN A 159 47.674 86.726 110.771 1.00 23.44 C ANISOU 6609 CB ASN D 159 3031 2923 2952 -33 7 -127 C ATOM 6610 CG ASN A 159 47.553 87.845 111.812 1.00 24.71 C ANISOU 6610 CG ASN D 159 3248 3131 3010 0 58 -135 C ATOM 6611 OD1 ASN A 159 47.713 87.598 113.022 1.00 25.61 O ANISOU 6611 OD1 ASN D 159 3428 3257 3044 41 -47 -219 O ATOM 6612 ND2 ASN A 159 47.260 89.067 111.358 1.00 23.96 N ANISOU 6612 ND2 ASN D 159 3297 2908 2897 110 84 -326 N ATOM 6613 N LYS A 160 47.135 85.059 108.120 1.00 23.14 N ANISOU 6613 N LYS D 160 2934 2948 2909 16 0 -157 N ATOM 6614 CA LYS A 160 47.591 84.072 107.130 1.00 22.87 C ANISOU 6614 CA LYS D 160 2893 2887 2907 1 -6 -131 C ATOM 6615 C LYS A 160 47.392 84.622 105.722 1.00 22.28 C ANISOU 6615 C LYS D 160 2816 2838 2808 16 12 -190 C ATOM 6616 O LYS A 160 48.277 84.495 104.876 1.00 22.20 O ANISOU 6616 O LYS D 160 2726 2863 2847 0 -2 -245 O ATOM 6617 CB LYS A 160 46.876 82.724 107.319 1.00 23.17 C ANISOU 6617 CB LYS D 160 2949 2939 2914 -9 -15 -129 C ATOM 6618 CG LYS A 160 47.254 81.997 108.604 1.00 23.17 C ANISOU 6618 CG LYS D 160 2888 2917 2996 -72 -32 -47 C ATOM 6619 CD LYS A 160 46.751 80.582 108.624 1.00 24.77 C ANISOU 6619 CD LYS D 160 3060 3147 3202 -32 -32 -53 C ATOM 6620 CE LYS A 160 47.193 79.865 109.885 1.00 26.95 C ANISOU 6620 CE LYS D 160 3450 3367 3420 20 13 -4 C ATOM 6621 NZ LYS A 160 46.742 78.439 109.882 1.00 28.93 N ANISOU 6621 NZ LYS D 160 3777 3616 3599 32 -27 4 N ATOM 6622 N VAL A 161 46.244 85.260 105.488 1.00 20.70 N ANISOU 6622 N VAL D 161 2718 2549 2598 20 6 -277 N ATOM 6623 CA VAL A 161 45.962 85.939 104.235 1.00 19.58 C ANISOU 6623 CA VAL D 161 2585 2392 2463 46 -14 -243 C ATOM 6624 C VAL A 161 47.031 86.998 103.948 1.00 19.70 C ANISOU 6624 C VAL D 161 2612 2439 2432 84 3 -264 C ATOM 6625 O VAL A 161 47.627 87.032 102.871 1.00 19.69 O ANISOU 6625 O VAL D 161 2625 2463 2390 167 42 -376 O ATOM 6626 CB VAL A 161 44.529 86.525 104.232 1.00 19.29 C ANISOU 6626 CB VAL D 161 2570 2340 2418 79 -34 -212 C ATOM 6627 CG1 VAL A 161 44.308 87.547 103.101 1.00 18.79 C ANISOU 6627 CG1 VAL D 161 2512 2300 2327 55 6 -338 C ATOM 6628 CG2 VAL A 161 43.484 85.391 104.200 1.00 19.52 C ANISOU 6628 CG2 VAL D 161 2476 2467 2471 36 -80 -243 C ATOM 6629 N LYS A 162 47.296 87.859 104.931 1.00 19.58 N ANISOU 6629 N LYS D 162 2575 2471 2390 62 10 -273 N ATOM 6630 CA LYS A 162 48.269 88.942 104.763 1.00 19.88 C ANISOU 6630 CA LYS D 162 2561 2501 2489 66 24 -224 C ATOM 6631 C LYS A 162 49.664 88.436 104.471 1.00 20.15 C ANISOU 6631 C LYS D 162 2628 2553 2473 138 47 -240 C ATOM 6632 O LYS A 162 50.401 89.024 103.662 1.00 20.39 O ANISOU 6632 O LYS D 162 2653 2540 2553 252 117 -355 O ATOM 6633 CB LYS A 162 48.313 89.811 106.036 1.00 19.97 C ANISOU 6633 CB LYS D 162 2530 2570 2486 92 37 -247 C ATOM 6634 CG LYS A 162 47.052 90.645 106.251 1.00 21.26 C ANISOU 6634 CG LYS D 162 2664 2676 2737 -18 12 -148 C ATOM 6635 CD LYS A 162 46.984 91.215 107.666 1.00 24.25 C ANISOU 6635 CD LYS D 162 3038 3140 3033 -14 -11 -174 C ATOM 6636 CE LYS A 162 45.822 92.215 107.781 1.00 25.39 C ANISOU 6636 CE LYS D 162 3180 3207 3259 -41 26 -161 C ATOM 6637 NZ LYS A 162 45.801 92.941 109.099 1.00 27.25 N ANISOU 6637 NZ LYS D 162 3424 3569 3358 52 -20 -193 N ATOM 6638 N LYS A 163 50.017 87.340 105.134 1.00 20.60 N ANISOU 6638 N LYS D 163 2652 2588 2586 111 72 -235 N ATOM 6639 CA LYS A 163 51.325 86.756 104.961 1.00 21.91 C ANISOU 6639 CA LYS D 163 2775 2781 2766 64 27 -181 C ATOM 6640 C LYS A 163 51.442 86.233 103.522 1.00 21.65 C ANISOU 6640 C LYS D 163 2699 2800 2724 102 7 -169 C ATOM 6641 O LYS A 163 52.444 86.476 102.854 1.00 21.47 O ANISOU 6641 O LYS D 163 2585 2844 2727 121 -27 -251 O ATOM 6642 CB LYS A 163 51.582 85.656 105.989 1.00 22.39 C ANISOU 6642 CB LYS D 163 2875 2852 2779 127 54 -173 C ATOM 6643 CG LYS A 163 52.871 84.885 105.711 1.00 25.44 C ANISOU 6643 CG LYS D 163 3252 3159 3253 -21 18 -102 C ATOM 6644 CD LYS A 163 53.676 84.540 106.953 1.00 30.42 C ANISOU 6644 CD LYS D 163 3897 3855 3805 -26 67 -21 C ATOM 6645 CE LYS A 163 55.017 83.904 106.543 1.00 32.52 C ANISOU 6645 CE LYS D 163 4127 4149 4077 -6 34 -25 C ATOM 6646 NZ LYS A 163 56.092 83.979 107.585 1.00 33.62 N ANISOU 6646 NZ LYS D 163 4207 4277 4289 22 110 -37 N ATOM 6647 N LEU A 164 50.410 85.536 103.037 1.00 21.06 N ANISOU 6647 N LEU D 164 2533 2770 2697 84 20 -164 N ATOM 6648 CA LEU A 164 50.491 84.933 101.707 1.00 20.17 C ANISOU 6648 CA LEU D 164 2464 2658 2541 70 30 -180 C ATOM 6649 C LEU A 164 50.628 86.044 100.686 1.00 20.19 C ANISOU 6649 C LEU D 164 2450 2674 2546 89 51 -210 C ATOM 6650 O LEU A 164 51.412 85.926 99.741 1.00 20.34 O ANISOU 6650 O LEU D 164 2510 2762 2454 117 53 -362 O ATOM 6651 CB LEU A 164 49.278 84.020 101.400 1.00 20.17 C ANISOU 6651 CB LEU D 164 2465 2668 2529 52 23 -171 C ATOM 6652 CG LEU A 164 49.143 82.674 102.132 1.00 19.21 C ANISOU 6652 CG LEU D 164 2312 2518 2466 7 -34 -178 C ATOM 6653 CD1 LEU A 164 47.723 82.120 102.062 1.00 19.31 C ANISOU 6653 CD1 LEU D 164 2398 2531 2405 -80 -39 -363 C ATOM 6654 CD2 LEU A 164 50.106 81.591 101.628 1.00 19.74 C ANISOU 6654 CD2 LEU D 164 2465 2601 2434 -59 -83 -265 C ATOM 6655 N ILE A 165 49.913 87.152 100.900 1.00 20.29 N ANISOU 6655 N ILE D 165 2470 2662 2576 52 32 -195 N ATOM 6656 CA ILE A 165 50.009 88.329 100.038 1.00 21.49 C ANISOU 6656 CA ILE D 165 2633 2766 2766 36 11 -144 C ATOM 6657 C ILE A 165 51.425 88.915 100.075 1.00 22.21 C ANISOU 6657 C ILE D 165 2730 2865 2843 76 17 -134 C ATOM 6658 O ILE A 165 51.980 89.255 99.043 1.00 21.99 O ANISOU 6658 O ILE D 165 2668 2838 2846 121 41 -277 O ATOM 6659 CB ILE A 165 48.963 89.416 100.439 1.00 21.50 C ANISOU 6659 CB ILE D 165 2639 2782 2747 8 -5 -132 C ATOM 6660 CG1 ILE A 165 47.549 88.911 100.144 1.00 20.77 C ANISOU 6660 CG1 ILE D 165 2555 2625 2709 29 2 -126 C ATOM 6661 CG2 ILE A 165 49.203 90.723 99.679 1.00 22.00 C ANISOU 6661 CG2 ILE D 165 2702 2722 2935 55 -2 -141 C ATOM 6662 CD1 ILE A 165 46.473 89.623 100.889 1.00 20.84 C ANISOU 6662 CD1 ILE D 165 2541 2596 2779 -31 -55 -173 C ATOM 6663 N GLU A 166 51.985 89.032 101.277 1.00 23.83 N ANISOU 6663 N GLU D 166 2928 3099 3026 51 13 -124 N ATOM 6664 CA GLU A 166 53.391 89.425 101.462 1.00 25.20 C ANISOU 6664 CA GLU D 166 3099 3262 3211 40 -25 -104 C ATOM 6665 C GLU A 166 54.374 88.565 100.657 1.00 24.91 C ANISOU 6665 C GLU D 166 3061 3225 3179 38 -40 -110 C ATOM 6666 O GLU A 166 55.321 89.099 100.062 1.00 24.97 O ANISOU 6666 O GLU D 166 3004 3297 3183 106 -62 -221 O ATOM 6667 CB GLU A 166 53.780 89.321 102.936 1.00 26.04 C ANISOU 6667 CB GLU D 166 3220 3382 3289 31 -3 -60 C ATOM 6668 CG GLU A 166 53.450 90.541 103.774 1.00 30.29 C ANISOU 6668 CG GLU D 166 3805 3804 3897 -30 -29 -61 C ATOM 6669 CD GLU A 166 54.131 90.502 105.129 1.00 35.31 C ANISOU 6669 CD GLU D 166 4452 4536 4427 -19 25 -35 C ATOM 6670 OE1 GLU A 166 55.377 90.422 105.164 1.00 37.08 O ANISOU 6670 OE1 GLU D 166 4422 4816 4850 -24 -55 -12 O ATOM 6671 OE2 GLU A 166 53.421 90.552 106.163 1.00 38.05 O ANISOU 6671 OE2 GLU D 166 4808 4923 4723 -6 -105 35 O ATOM 6672 N MET A 167 54.162 87.248 100.668 1.00 24.44 N ANISOU 6672 N MET D 167 2953 3169 3163 40 -31 -144 N ATOM 6673 CA MET A 167 55.043 86.298 99.965 1.00 23.89 C ANISOU 6673 CA MET D 167 2893 3119 3063 -14 -32 -115 C ATOM 6674 C MET A 167 54.999 86.447 98.441 1.00 23.76 C ANISOU 6674 C MET D 167 2873 3106 3046 -19 -31 -129 C ATOM 6675 O MET A 167 55.928 86.008 97.755 1.00 24.05 O ANISOU 6675 O MET D 167 2844 3214 3079 -4 -82 -169 O ATOM 6676 CB MET A 167 54.702 84.856 100.327 1.00 23.74 C ANISOU 6676 CB MET D 167 2883 3103 3031 -70 -31 -129 C ATOM 6677 CG MET A 167 55.029 84.451 101.740 1.00 24.39 C ANISOU 6677 CG MET D 167 2945 3339 2983 -83 -18 -184 C ATOM 6678 SD MET A 167 54.583 82.742 102.104 1.00 25.67 S ANISOU 6678 SD MET D 167 3024 3682 3045 -118 -5 -591 S ATOM 6679 CE MET A 167 55.837 81.812 101.191 1.00 24.46 C ANISOU 6679 CE MET D 167 2989 3267 3037 -87 -4 -389 C ATOM 6680 N GLY A 168 53.926 87.039 97.914 1.00 22.75 N ANISOU 6680 N GLY D 168 2766 2957 2922 13 -4 -119 N ATOM 6681 CA GLY A 168 53.776 87.289 96.487 1.00 21.71 C ANISOU 6681 CA GLY D 168 2600 2841 2805 62 -10 -89 C ATOM 6682 C GLY A 168 52.566 86.618 95.830 1.00 20.94 C ANISOU 6682 C GLY D 168 2508 2749 2697 89 14 -95 C ATOM 6683 O GLY A 168 52.423 86.659 94.607 1.00 20.80 O ANISOU 6683 O GLY D 168 2376 2790 2738 102 -32 -144 O ATOM 6684 N PHE A 169 51.684 86.041 96.646 1.00 19.83 N ANISOU 6684 N PHE D 169 2356 2604 2572 130 43 -162 N ATOM 6685 CA PHE A 169 50.432 85.451 96.141 1.00 18.71 C ANISOU 6685 CA PHE D 169 2288 2419 2401 107 53 -168 C ATOM 6686 C PHE A 169 49.347 86.482 95.882 1.00 18.19 C ANISOU 6686 C PHE D 169 2269 2304 2337 101 34 -209 C ATOM 6687 O PHE A 169 49.195 87.469 96.626 1.00 18.14 O ANISOU 6687 O PHE D 169 2253 2295 2342 179 94 -449 O ATOM 6688 CB PHE A 169 49.891 84.432 97.132 1.00 18.43 C ANISOU 6688 CB PHE D 169 2216 2394 2393 97 65 -158 C ATOM 6689 CG PHE A 169 50.637 83.137 97.144 1.00 18.73 C ANISOU 6689 CG PHE D 169 2328 2348 2437 54 39 -106 C ATOM 6690 CD1 PHE A 169 50.325 82.125 96.235 1.00 18.07 C ANISOU 6690 CD1 PHE D 169 2251 2287 2328 -8 101 -157 C ATOM 6691 CD2 PHE A 169 51.657 82.911 98.065 1.00 18.67 C ANISOU 6691 CD2 PHE D 169 2293 2405 2394 -13 6 -173 C ATOM 6692 CE1 PHE A 169 51.013 80.902 96.274 1.00 18.36 C ANISOU 6692 CE1 PHE D 169 2200 2413 2362 -98 104 -217 C ATOM 6693 CE2 PHE A 169 52.342 81.701 98.091 1.00 18.94 C ANISOU 6693 CE2 PHE D 169 2325 2434 2436 15 118 -145 C ATOM 6694 CZ PHE A 169 52.020 80.695 97.195 1.00 18.15 C ANISOU 6694 CZ PHE D 169 2308 2348 2237 -104 109 -184 C ATOM 6695 N ARG A 170 48.600 86.254 94.803 1.00 17.54 N ANISOU 6695 N ARG D 170 2188 2175 2300 108 23 -168 N ATOM 6696 CA ARG A 170 47.282 86.837 94.615 1.00 17.30 C ANISOU 6696 CA ARG D 170 2181 2154 2238 62 -23 -154 C ATOM 6697 C ARG A 170 46.317 85.900 95.341 1.00 17.15 C ANISOU 6697 C ARG D 170 2160 2132 2224 92 -83 -194 C ATOM 6698 O ARG A 170 46.112 84.748 94.919 1.00 16.03 O ANISOU 6698 O ARG D 170 1941 2022 2127 125 -191 -388 O ATOM 6699 CB ARG A 170 46.948 86.949 93.133 1.00 17.82 C ANISOU 6699 CB ARG D 170 2253 2210 2308 7 -30 -128 C ATOM 6700 CG ARG A 170 47.416 88.245 92.465 1.00 17.94 C ANISOU 6700 CG ARG D 170 2301 2335 2181 72 -65 -100 C ATOM 6701 CD ARG A 170 47.474 88.161 90.942 1.00 18.72 C ANISOU 6701 CD ARG D 170 2392 2389 2328 40 -45 -97 C ATOM 6702 NE ARG A 170 48.425 87.123 90.571 1.00 18.37 N ANISOU 6702 NE ARG D 170 2257 2320 2402 186 -172 -261 N ATOM 6703 CZ ARG A 170 48.226 86.242 89.592 1.00 18.16 C ANISOU 6703 CZ ARG D 170 2257 2395 2246 49 -92 -160 C ATOM 6704 NH1 ARG A 170 47.149 86.318 88.813 1.00 18.31 N ANISOU 6704 NH1 ARG D 170 2113 2488 2353 -5 -152 -239 N ATOM 6705 NH2 ARG A 170 49.126 85.305 89.377 1.00 17.16 N ANISOU 6705 NH2 ARG D 170 2047 2179 2292 76 -126 -111 N ATOM 6706 N VAL A 171 45.763 86.370 96.464 1.00 17.25 N ANISOU 6706 N VAL D 171 2189 2116 2249 93 -76 -195 N ATOM 6707 CA VAL A 171 44.942 85.537 97.345 1.00 16.98 C ANISOU 6707 CA VAL D 171 2183 2110 2159 58 -31 -211 C ATOM 6708 C VAL A 171 43.459 85.764 97.085 1.00 16.38 C ANISOU 6708 C VAL D 171 2076 1966 2179 77 -39 -234 C ATOM 6709 O VAL A 171 42.971 86.900 97.030 1.00 16.27 O ANISOU 6709 O VAL D 171 2080 1982 2120 11 -9 -480 O ATOM 6710 CB VAL A 171 45.268 85.773 98.862 1.00 16.99 C ANISOU 6710 CB VAL D 171 2181 2103 2170 73 0 -145 C ATOM 6711 CG1 VAL A 171 44.405 84.901 99.754 1.00 16.74 C ANISOU 6711 CG1 VAL D 171 2155 2282 1924 5 77 -206 C ATOM 6712 CG2 VAL A 171 46.732 85.484 99.136 1.00 17.59 C ANISOU 6712 CG2 VAL D 171 2287 2181 2215 60 7 -100 C ATOM 6713 N SER A 172 42.755 84.661 96.864 1.00 15.70 N ANISOU 6713 N SER D 172 1967 1955 2040 77 -42 -369 N ATOM 6714 CA SER A 172 41.317 84.673 96.886 1.00 14.78 C ANISOU 6714 CA SER D 172 1870 1799 1947 66 14 -321 C ATOM 6715 C SER A 172 40.861 84.181 98.237 1.00 14.82 C ANISOU 6715 C SER D 172 1900 1849 1881 39 57 -328 C ATOM 6716 O SER A 172 41.466 83.279 98.816 1.00 15.34 O ANISOU 6716 O SER D 172 1978 1902 1949 -19 11 -510 O ATOM 6717 CB SER A 172 40.783 83.737 95.800 1.00 14.84 C ANISOU 6717 CB SER D 172 1850 1858 1927 141 35 -287 C ATOM 6718 OG SER A 172 41.151 84.192 94.516 1.00 13.75 O ANISOU 6718 OG SER D 172 1834 1532 1856 205 -4 -474 O ATOM 6719 N VAL A 173 39.765 84.742 98.735 1.00 14.28 N ANISOU 6719 N VAL D 173 1812 1801 1810 2 25 -327 N ATOM 6720 CA VAL A 173 39.168 84.283 99.988 1.00 14.71 C ANISOU 6720 CA VAL D 173 1875 1873 1841 -16 -18 -289 C ATOM 6721 C VAL A 173 37.722 83.845 99.809 1.00 14.16 C ANISOU 6721 C VAL D 173 1812 1848 1719 -103 -81 -351 C ATOM 6722 O VAL A 173 37.014 84.333 98.929 1.00 14.99 O ANISOU 6722 O VAL D 173 1857 1982 1854 -230 -144 -522 O ATOM 6723 CB VAL A 173 39.257 85.342 101.137 1.00 14.45 C ANISOU 6723 CB VAL D 173 1850 1833 1805 -6 -6 -269 C ATOM 6724 CG1 VAL A 173 40.704 85.687 101.401 1.00 16.10 C ANISOU 6724 CG1 VAL D 173 1948 2097 2069 -20 -25 -232 C ATOM 6725 CG2 VAL A 173 38.459 86.603 100.826 1.00 15.40 C ANISOU 6725 CG2 VAL D 173 1787 2025 2037 95 0 -235 C ATOM 6726 N THR A 174 37.299 82.934 100.659 1.00 14.95 N ANISOU 6726 N THR D 174 1956 1916 1809 -95 -91 -415 N ATOM 6727 CA THR A 174 35.953 82.401 100.582 1.00 16.14 C ANISOU 6727 CA THR D 174 2080 2107 1943 -39 -50 -327 C ATOM 6728 C THR A 174 35.477 81.899 101.948 1.00 16.35 C ANISOU 6728 C THR D 174 2166 2061 1982 -71 -34 -271 C ATOM 6729 O THR A 174 36.289 81.561 102.801 1.00 16.34 O ANISOU 6729 O THR D 174 2146 2104 1957 -189 -101 -410 O ATOM 6730 CB THR A 174 35.892 81.283 99.485 1.00 15.76 C ANISOU 6730 CB THR D 174 2063 2059 1866 0 -40 -334 C ATOM 6731 OG1 THR A 174 34.520 80.976 99.195 1.00 17.63 O ANISOU 6731 OG1 THR D 174 2282 2461 1954 55 9 -631 O ATOM 6732 CG2 THR A 174 36.535 80.021 99.939 1.00 17.58 C ANISOU 6732 CG2 THR D 174 2306 2310 2063 -25 -28 -281 C ATOM 6733 N GLY A 175 34.159 81.881 102.143 1.00 17.61 N ANISOU 6733 N GLY D 175 2260 2251 2177 -39 -29 -215 N ATOM 6734 CA GLY A 175 33.534 81.496 103.400 1.00 19.00 C ANISOU 6734 CA GLY D 175 2420 2411 2386 -24 -36 -184 C ATOM 6735 C GLY A 175 33.150 82.715 104.240 1.00 20.09 C ANISOU 6735 C GLY D 175 2558 2555 2518 -2 -91 -198 C ATOM 6736 O GLY A 175 33.944 83.620 104.411 1.00 19.10 O ANISOU 6736 O GLY D 175 2446 2379 2430 -21 -177 -338 O ATOM 6737 N GLY A 176 31.921 82.746 104.744 1.00 21.02 N ANISOU 6737 N GLY D 176 2635 2698 2653 -8 -74 -133 N ATOM 6738 CA GLY A 176 31.504 83.828 105.628 1.00 22.42 C ANISOU 6738 CA GLY D 176 2867 2862 2787 -9 -47 -111 C ATOM 6739 C GLY A 176 31.618 85.222 105.029 1.00 23.19 C ANISOU 6739 C GLY D 176 2953 2937 2920 17 -28 -118 C ATOM 6740 O GLY A 176 31.895 86.197 105.745 1.00 23.58 O ANISOU 6740 O GLY D 176 3019 3033 2904 4 -32 -223 O ATOM 6741 N LEU A 177 31.396 85.337 103.722 1.00 23.28 N ANISOU 6741 N LEU D 177 2972 2945 2927 -15 -18 -106 N ATOM 6742 CA LEU A 177 31.513 86.624 103.050 1.00 23.68 C ANISOU 6742 CA LEU D 177 2998 3001 2996 19 11 -62 C ATOM 6743 C LEU A 177 30.145 87.225 102.765 1.00 24.61 C ANISOU 6743 C LEU D 177 3065 3135 3148 9 -2 -75 C ATOM 6744 O LEU A 177 29.277 86.564 102.194 1.00 24.92 O ANISOU 6744 O LEU D 177 3145 3146 3176 69 0 -140 O ATOM 6745 CB LEU A 177 32.275 86.489 101.734 1.00 23.12 C ANISOU 6745 CB LEU D 177 2926 2907 2951 39 12 -81 C ATOM 6746 CG LEU A 177 33.772 86.206 101.773 1.00 22.78 C ANISOU 6746 CG LEU D 177 2883 2866 2903 46 -1 -109 C ATOM 6747 CD1 LEU A 177 34.309 86.071 100.355 1.00 23.01 C ANISOU 6747 CD1 LEU D 177 2934 2915 2893 99 67 -128 C ATOM 6748 CD2 LEU A 177 34.540 87.307 102.523 1.00 23.39 C ANISOU 6748 CD2 LEU D 177 2843 3049 2993 65 -52 -123 C ATOM 6749 N SER A 178 29.967 88.484 103.144 1.00 25.36 N ANISOU 6749 N SER D 178 3182 3225 3227 51 24 -75 N ATOM 6750 CA SER A 178 28.772 89.242 102.781 1.00 26.09 C ANISOU 6750 CA SER D 178 3289 3317 3306 2 -13 -71 C ATOM 6751 C SER A 178 29.163 90.692 102.550 1.00 26.68 C ANISOU 6751 C SER D 178 3383 3368 3384 -3 -10 -52 C ATOM 6752 O SER A 178 30.294 91.085 102.841 1.00 26.51 O ANISOU 6752 O SER D 178 3441 3269 3360 6 -18 -145 O ATOM 6753 CB SER A 178 27.698 89.145 103.881 1.00 26.12 C ANISOU 6753 CB SER D 178 3244 3378 3300 33 -11 -48 C ATOM 6754 OG SER A 178 28.185 89.615 105.129 1.00 26.44 O ANISOU 6754 OG SER D 178 3301 3482 3262 -29 -123 -180 O ATOM 6755 N VAL A 179 28.235 91.483 102.018 1.00 27.48 N ANISOU 6755 N VAL D 179 3484 3495 3462 -8 -1 -51 N ATOM 6756 CA VAL A 179 28.431 92.930 101.910 1.00 28.45 C ANISOU 6756 CA VAL D 179 3629 3592 3586 -17 9 -28 C ATOM 6757 C VAL A 179 28.909 93.515 103.243 1.00 28.35 C ANISOU 6757 C VAL D 179 3601 3580 3591 0 26 -33 C ATOM 6758 O VAL A 179 29.801 94.368 103.264 1.00 28.83 O ANISOU 6758 O VAL D 179 3703 3613 3635 9 38 -63 O ATOM 6759 CB VAL A 179 27.139 93.630 101.443 1.00 28.66 C ANISOU 6759 CB VAL D 179 3642 3613 3632 -3 41 -26 C ATOM 6760 CG1 VAL A 179 27.132 95.133 101.781 1.00 29.72 C ANISOU 6760 CG1 VAL D 179 3788 3758 3743 1 26 -41 C ATOM 6761 CG2 VAL A 179 26.988 93.453 99.971 1.00 29.39 C ANISOU 6761 CG2 VAL D 179 3770 3702 3695 -22 -22 -17 C ATOM 6762 N ASP A 180 28.339 93.033 104.349 1.00 27.88 N ANISOU 6762 N ASP D 180 3547 3515 3528 -8 11 -51 N ATOM 6763 CA ASP A 180 28.655 93.605 105.664 1.00 27.53 C ANISOU 6763 CA ASP D 180 3464 3488 3508 6 -5 -49 C ATOM 6764 C ASP A 180 30.037 93.211 106.198 1.00 26.09 C ANISOU 6764 C ASP D 180 3323 3252 3336 -3 -12 -81 C ATOM 6765 O ASP A 180 30.674 94.002 106.927 1.00 25.16 O ANISOU 6765 O ASP D 180 3177 3130 3250 11 -36 -173 O ATOM 6766 CB ASP A 180 27.544 93.325 106.698 1.00 28.49 C ANISOU 6766 CB ASP D 180 3583 3642 3600 15 -16 -14 C ATOM 6767 CG ASP A 180 26.264 94.133 106.433 1.00 30.39 C ANISOU 6767 CG ASP D 180 3819 3838 3887 -45 -63 -17 C ATOM 6768 OD1 ASP A 180 26.255 95.034 105.554 1.00 32.23 O ANISOU 6768 OD1 ASP D 180 4103 3987 4156 -51 -73 -3 O ATOM 6769 OD2 ASP A 180 25.222 93.886 107.079 1.00 33.04 O ANISOU 6769 OD2 ASP D 180 4119 4192 4241 56 -90 6 O ATOM 6770 N THR A 181 30.528 92.025 105.825 1.00 24.44 N ANISOU 6770 N THR D 181 3148 3003 3134 61 -27 -65 N ATOM 6771 CA THR A 181 31.847 91.596 106.297 1.00 23.21 C ANISOU 6771 CA THR D 181 3018 2854 2947 51 -40 -89 C ATOM 6772 C THR A 181 33.003 91.986 105.395 1.00 21.13 C ANISOU 6772 C THR D 181 2811 2543 2674 26 -30 -160 C ATOM 6773 O THR A 181 34.151 91.742 105.759 1.00 20.96 O ANISOU 6773 O THR D 181 2829 2510 2625 16 -101 -239 O ATOM 6774 CB THR A 181 31.919 90.089 106.631 1.00 23.85 C ANISOU 6774 CB THR D 181 3119 2952 2989 96 -34 -69 C ATOM 6775 OG1 THR A 181 31.769 89.308 105.447 1.00 25.43 O ANISOU 6775 OG1 THR D 181 3372 3065 3222 97 -84 -153 O ATOM 6776 CG2 THR A 181 30.805 89.700 107.595 1.00 25.06 C ANISOU 6776 CG2 THR D 181 3163 3202 3156 90 -89 -79 C ATOM 6777 N LEU A 182 32.724 92.639 104.270 1.00 19.61 N ANISOU 6777 N LEU D 182 2586 2330 2533 72 -14 -246 N ATOM 6778 CA LEU A 182 33.802 93.107 103.396 1.00 19.24 C ANISOU 6778 CA LEU D 182 2512 2325 2473 80 -13 -198 C ATOM 6779 C LEU A 182 34.738 94.074 104.150 1.00 20.17 C ANISOU 6779 C LEU D 182 2556 2536 2571 63 -6 -217 C ATOM 6780 O LEU A 182 35.972 94.021 103.998 1.00 19.93 O ANISOU 6780 O LEU D 182 2476 2537 2557 192 -6 -317 O ATOM 6781 CB LEU A 182 33.245 93.738 102.109 1.00 18.80 C ANISOU 6781 CB LEU D 182 2419 2284 2441 76 -4 -251 C ATOM 6782 CG LEU A 182 32.820 92.743 101.010 1.00 18.05 C ANISOU 6782 CG LEU D 182 2385 2156 2317 118 19 -236 C ATOM 6783 CD1 LEU A 182 32.126 93.413 99.857 1.00 17.86 C ANISOU 6783 CD1 LEU D 182 2430 2013 2342 56 -92 -277 C ATOM 6784 CD2 LEU A 182 34.030 91.951 100.520 1.00 19.41 C ANISOU 6784 CD2 LEU D 182 2498 2375 2501 60 -24 -282 C ATOM 6785 N LYS A 183 34.168 94.909 105.013 1.00 20.81 N ANISOU 6785 N LYS D 183 2617 2636 2653 3 -48 -156 N ATOM 6786 CA LYS A 183 34.964 95.915 105.724 1.00 21.24 C ANISOU 6786 CA LYS D 183 2707 2662 2698 1 -67 -125 C ATOM 6787 C LYS A 183 36.049 95.297 106.617 1.00 20.72 C ANISOU 6787 C LYS D 183 2633 2588 2650 -8 -88 -114 C ATOM 6788 O LYS A 183 37.039 95.959 106.991 1.00 20.67 O ANISOU 6788 O LYS D 183 2632 2598 2621 0 -108 -217 O ATOM 6789 CB LYS A 183 34.068 96.875 106.528 1.00 21.58 C ANISOU 6789 CB LYS D 183 2739 2664 2795 -43 -64 -98 C ATOM 6790 CG LYS A 183 33.267 96.255 107.659 1.00 23.00 C ANISOU 6790 CG LYS D 183 2969 2914 2854 -53 -29 -107 C ATOM 6791 CD LYS A 183 32.378 97.310 108.395 1.00 24.93 C ANISOU 6791 CD LYS D 183 3188 3104 3180 -174 16 -150 C ATOM 6792 CE LYS A 183 31.360 98.021 107.474 1.00 26.97 C ANISOU 6792 CE LYS D 183 3471 3371 3402 11 -14 -77 C ATOM 6793 NZ LYS A 183 30.302 97.124 106.906 1.00 29.06 N ANISOU 6793 NZ LYS D 183 3629 3696 3714 -21 14 -162 N ATOM 6794 N LEU A 184 35.864 94.027 106.977 1.00 20.21 N ANISOU 6794 N LEU D 184 2601 2488 2587 16 -85 -156 N ATOM 6795 CA LEU A 184 36.857 93.345 107.800 1.00 19.98 C ANISOU 6795 CA LEU D 184 2591 2470 2529 37 -47 -134 C ATOM 6796 C LEU A 184 38.203 93.235 107.083 1.00 19.55 C ANISOU 6796 C LEU D 184 2584 2381 2461 19 -59 -177 C ATOM 6797 O LEU A 184 39.246 93.087 107.731 1.00 20.10 O ANISOU 6797 O LEU D 184 2660 2518 2457 76 -88 -294 O ATOM 6798 CB LEU A 184 36.366 91.975 108.265 1.00 19.80 C ANISOU 6798 CB LEU D 184 2569 2474 2477 47 -88 -143 C ATOM 6799 CG LEU A 184 35.147 91.960 109.195 1.00 19.84 C ANISOU 6799 CG LEU D 184 2471 2538 2527 49 -51 -97 C ATOM 6800 CD1 LEU A 184 34.868 90.543 109.583 1.00 21.25 C ANISOU 6800 CD1 LEU D 184 2701 2738 2634 29 -110 -58 C ATOM 6801 CD2 LEU A 184 35.348 92.826 110.446 1.00 19.60 C ANISOU 6801 CD2 LEU D 184 2501 2610 2334 56 -147 -86 C ATOM 6802 N PHE A 185 38.179 93.326 105.753 1.00 19.41 N ANISOU 6802 N PHE D 185 2555 2334 2484 59 -15 -156 N ATOM 6803 CA PHE A 185 39.396 93.243 104.930 1.00 19.43 C ANISOU 6803 CA PHE D 185 2551 2376 2455 51 -50 -136 C ATOM 6804 C PHE A 185 39.962 94.599 104.506 1.00 20.43 C ANISOU 6804 C PHE D 185 2671 2491 2598 74 -55 -148 C ATOM 6805 O PHE A 185 40.873 94.657 103.692 1.00 20.02 O ANISOU 6805 O PHE D 185 2736 2410 2460 131 -102 -268 O ATOM 6806 CB PHE A 185 39.133 92.422 103.653 1.00 18.97 C ANISOU 6806 CB PHE D 185 2453 2340 2413 41 -11 -133 C ATOM 6807 CG PHE A 185 38.782 90.991 103.913 1.00 19.37 C ANISOU 6807 CG PHE D 185 2506 2403 2448 53 -21 -118 C ATOM 6808 CD1 PHE A 185 39.765 90.017 103.938 1.00 19.21 C ANISOU 6808 CD1 PHE D 185 2500 2368 2431 99 99 -97 C ATOM 6809 CD2 PHE A 185 37.475 90.622 104.136 1.00 19.71 C ANISOU 6809 CD2 PHE D 185 2530 2477 2480 26 6 -146 C ATOM 6810 CE1 PHE A 185 39.447 88.691 104.189 1.00 19.87 C ANISOU 6810 CE1 PHE D 185 2644 2452 2454 33 30 -98 C ATOM 6811 CE2 PHE A 185 37.145 89.308 104.381 1.00 20.17 C ANISOU 6811 CE2 PHE D 185 2771 2478 2413 -69 -35 -61 C ATOM 6812 CZ PHE A 185 38.137 88.337 104.407 1.00 19.42 C ANISOU 6812 CZ PHE D 185 2614 2419 2344 16 51 -159 C ATOM 6813 N GLU A 186 39.429 95.694 105.038 1.00 21.63 N ANISOU 6813 N GLU D 186 2876 2586 2753 46 -39 -149 N ATOM 6814 CA GLU A 186 39.959 97.013 104.691 1.00 23.20 C ANISOU 6814 CA GLU D 186 3052 2792 2969 45 -36 -94 C ATOM 6815 C GLU A 186 41.462 97.031 104.874 1.00 22.28 C ANISOU 6815 C GLU D 186 2974 2627 2865 46 5 -169 C ATOM 6816 O GLU A 186 41.986 96.511 105.856 1.00 21.51 O ANISOU 6816 O GLU D 186 2919 2396 2856 118 30 -265 O ATOM 6817 CB GLU A 186 39.315 98.112 105.533 1.00 24.12 C ANISOU 6817 CB GLU D 186 3161 2907 3095 0 -39 -114 C ATOM 6818 CG GLU A 186 39.464 99.531 104.959 1.00 28.32 C ANISOU 6818 CG GLU D 186 3728 3459 3574 43 -46 27 C ATOM 6819 CD GLU A 186 38.361 100.462 105.448 1.00 33.70 C ANISOU 6819 CD GLU D 186 4370 4156 4276 -42 -44 -3 C ATOM 6820 OE1 GLU A 186 37.829 100.217 106.552 1.00 36.19 O ANISOU 6820 OE1 GLU D 186 4690 4612 4448 6 -138 0 O ATOM 6821 OE2 GLU A 186 38.015 101.440 104.738 1.00 36.19 O ANISOU 6821 OE2 GLU D 186 4769 4515 4465 -60 31 91 O ATOM 6822 N GLY A 187 42.150 97.570 103.880 1.00 22.79 N ANISOU 6822 N GLY D 187 2980 2700 2977 65 -21 -140 N ATOM 6823 CA GLY A 187 43.601 97.650 103.901 1.00 23.66 C ANISOU 6823 CA GLY D 187 2997 2923 3066 29 14 -119 C ATOM 6824 C GLY A 187 44.352 96.380 103.545 1.00 24.29 C ANISOU 6824 C GLY D 187 3050 3029 3150 36 -3 -122 C ATOM 6825 O GLY A 187 45.585 96.378 103.553 1.00 24.59 O ANISOU 6825 O GLY D 187 3070 3077 3194 27 68 -209 O ATOM 6826 N VAL A 188 43.641 95.300 103.220 1.00 24.61 N ANISOU 6826 N VAL D 188 3070 3120 3162 28 -11 -90 N ATOM 6827 CA VAL A 188 44.327 94.108 102.736 1.00 24.52 C ANISOU 6827 CA VAL D 188 3123 3085 3109 33 -23 -59 C ATOM 6828 C VAL A 188 44.033 93.869 101.267 1.00 23.93 C ANISOU 6828 C VAL D 188 3019 2996 3076 47 -36 -100 C ATOM 6829 O VAL A 188 42.899 94.039 100.796 1.00 23.52 O ANISOU 6829 O VAL D 188 2985 2948 3001 47 -103 -201 O ATOM 6830 CB VAL A 188 44.195 92.847 103.664 1.00 25.38 C ANISOU 6830 CB VAL D 188 3235 3189 3220 52 -22 -28 C ATOM 6831 CG1 VAL A 188 43.418 93.155 104.955 1.00 25.33 C ANISOU 6831 CG1 VAL D 188 3241 3159 3223 19 -40 -102 C ATOM 6832 CG2 VAL A 188 43.675 91.611 102.930 1.00 25.41 C ANISOU 6832 CG2 VAL D 188 3315 3188 3151 42 -12 -29 C ATOM 6833 N ASP A 189 45.104 93.541 100.550 1.00 23.11 N ANISOU 6833 N ASP D 189 2918 2854 3006 61 -32 -150 N ATOM 6834 CA ASP A 189 45.135 93.543 99.099 1.00 22.57 C ANISOU 6834 CA ASP D 189 2875 2740 2958 71 -11 -143 C ATOM 6835 C ASP A 189 44.538 92.236 98.567 1.00 21.65 C ANISOU 6835 C ASP D 189 2718 2669 2838 78 -11 -213 C ATOM 6836 O ASP A 189 45.225 91.472 97.882 1.00 21.80 O ANISOU 6836 O ASP D 189 2756 2551 2975 68 -2 -319 O ATOM 6837 CB ASP A 189 46.592 93.702 98.636 1.00 23.11 C ANISOU 6837 CB ASP D 189 2926 2842 3011 44 -8 -165 C ATOM 6838 CG ASP A 189 46.718 94.037 97.158 1.00 25.13 C ANISOU 6838 CG ASP D 189 3232 3076 3241 42 26 -116 C ATOM 6839 OD1 ASP A 189 45.734 94.514 96.547 1.00 27.27 O ANISOU 6839 OD1 ASP D 189 3402 3447 3509 14 135 -197 O ATOM 6840 OD2 ASP A 189 47.803 93.836 96.554 1.00 27.93 O ANISOU 6840 OD2 ASP D 189 3509 3556 3545 62 30 -239 O ATOM 6841 N VAL A 190 43.280 91.968 98.910 1.00 19.97 N ANISOU 6841 N VAL D 190 2566 2409 2610 57 -9 -223 N ATOM 6842 CA VAL A 190 42.605 90.739 98.442 1.00 18.88 C ANISOU 6842 CA VAL D 190 2409 2301 2464 77 -20 -177 C ATOM 6843 C VAL A 190 42.496 90.780 96.929 1.00 18.12 C ANISOU 6843 C VAL D 190 2360 2148 2376 30 -66 -202 C ATOM 6844 O VAL A 190 42.186 91.815 96.352 1.00 17.84 O ANISOU 6844 O VAL D 190 2408 2111 2257 25 -103 -270 O ATOM 6845 CB VAL A 190 41.228 90.569 99.118 1.00 18.96 C ANISOU 6845 CB VAL D 190 2408 2319 2474 73 4 -143 C ATOM 6846 CG1 VAL A 190 40.416 89.456 98.447 1.00 19.13 C ANISOU 6846 CG1 VAL D 190 2378 2304 2585 129 7 -223 C ATOM 6847 CG2 VAL A 190 41.413 90.258 100.608 1.00 20.00 C ANISOU 6847 CG2 VAL D 190 2468 2612 2519 106 -46 -89 C ATOM 6848 N PHE A 191 42.786 89.643 96.279 1.00 17.04 N ANISOU 6848 N PHE D 191 2256 2016 2201 61 -71 -210 N ATOM 6849 CA PHE A 191 42.751 89.566 94.828 1.00 15.94 C ANISOU 6849 CA PHE D 191 2055 1926 2074 -10 -21 -201 C ATOM 6850 C PHE A 191 41.319 89.329 94.349 1.00 14.52 C ANISOU 6850 C PHE D 191 1917 1711 1887 -63 -56 -275 C ATOM 6851 O PHE A 191 40.865 89.955 93.410 1.00 14.16 O ANISOU 6851 O PHE D 191 1851 1681 1846 -125 -52 -395 O ATOM 6852 CB PHE A 191 43.703 88.465 94.326 1.00 15.69 C ANISOU 6852 CB PHE D 191 2068 1890 2000 14 -27 -172 C ATOM 6853 CG PHE A 191 43.616 88.207 92.842 1.00 15.49 C ANISOU 6853 CG PHE D 191 2066 1843 1977 -5 -37 -212 C ATOM 6854 CD1 PHE A 191 43.875 89.236 91.933 1.00 15.60 C ANISOU 6854 CD1 PHE D 191 2019 1976 1932 48 -145 -276 C ATOM 6855 CD2 PHE A 191 43.254 86.938 92.358 1.00 15.08 C ANISOU 6855 CD2 PHE D 191 1927 1845 1957 182 -16 -37 C ATOM 6856 CE1 PHE A 191 43.797 89.038 90.570 1.00 16.42 C ANISOU 6856 CE1 PHE D 191 2224 2072 1940 129 -42 -199 C ATOM 6857 CE2 PHE A 191 43.166 86.722 90.976 1.00 13.22 C ANISOU 6857 CE2 PHE D 191 1852 1429 1740 175 -91 -254 C ATOM 6858 CZ PHE A 191 43.420 87.770 90.080 1.00 14.72 C ANISOU 6858 CZ PHE D 191 1895 1738 1958 63 -144 -141 C ATOM 6859 N THR A 192 40.634 88.414 95.016 1.00 14.09 N ANISOU 6859 N THR D 192 1841 1720 1790 -13 -39 -302 N ATOM 6860 CA THR A 192 39.271 88.020 94.649 1.00 13.58 C ANISOU 6860 CA THR D 192 1812 1565 1781 13 5 -297 C ATOM 6861 C THR A 192 38.470 87.560 95.878 1.00 13.16 C ANISOU 6861 C THR D 192 1865 1502 1631 95 67 -362 C ATOM 6862 O THR A 192 38.960 86.790 96.702 1.00 13.72 O ANISOU 6862 O THR D 192 1991 1465 1756 159 102 -461 O ATOM 6863 CB THR A 192 39.317 86.847 93.629 1.00 13.12 C ANISOU 6863 CB THR D 192 1811 1521 1651 35 25 -313 C ATOM 6864 OG1 THR A 192 39.922 87.272 92.410 1.00 14.45 O ANISOU 6864 OG1 THR D 192 1972 1719 1797 -50 -48 -509 O ATOM 6865 CG2 THR A 192 37.904 86.333 93.271 1.00 12.65 C ANISOU 6865 CG2 THR D 192 1725 1323 1758 -146 -42 -318 C ATOM 6866 N PHE A 193 37.222 88.002 95.969 1.00 13.40 N ANISOU 6866 N PHE D 193 1894 1528 1667 69 8 -308 N ATOM 6867 CA PHE A 193 36.287 87.474 96.944 1.00 14.33 C ANISOU 6867 CA PHE D 193 1917 1706 1820 70 -57 -267 C ATOM 6868 C PHE A 193 35.379 86.488 96.248 1.00 13.78 C ANISOU 6868 C PHE D 193 1794 1726 1713 29 -65 -272 C ATOM 6869 O PHE A 193 34.778 86.826 95.237 1.00 13.90 O ANISOU 6869 O PHE D 193 1875 1737 1669 -10 -189 -550 O ATOM 6870 CB PHE A 193 35.429 88.584 97.529 1.00 14.62 C ANISOU 6870 CB PHE D 193 1993 1768 1793 48 -42 -209 C ATOM 6871 CG PHE A 193 36.197 89.554 98.377 1.00 15.90 C ANISOU 6871 CG PHE D 193 2174 1870 1995 101 -20 -210 C ATOM 6872 CD1 PHE A 193 36.517 89.236 99.687 1.00 16.23 C ANISOU 6872 CD1 PHE D 193 2321 1749 2094 54 14 -339 C ATOM 6873 CD2 PHE A 193 36.609 90.783 97.851 1.00 15.07 C ANISOU 6873 CD2 PHE D 193 2188 1686 1852 37 -35 -333 C ATOM 6874 CE1 PHE A 193 37.232 90.143 100.478 1.00 16.08 C ANISOU 6874 CE1 PHE D 193 2112 1837 2161 166 26 -268 C ATOM 6875 CE2 PHE A 193 37.329 91.686 98.648 1.00 15.67 C ANISOU 6875 CE2 PHE D 193 2061 1848 2046 -15 0 -272 C ATOM 6876 CZ PHE A 193 37.633 91.353 99.936 1.00 14.29 C ANISOU 6876 CZ PHE D 193 1988 1495 1946 -46 -26 -257 C ATOM 6877 N ILE A 194 35.240 85.309 96.847 1.00 14.55 N ANISOU 6877 N ILE D 194 1897 1775 1854 50 -54 -269 N ATOM 6878 CA ILE A 194 34.441 84.215 96.267 1.00 14.95 C ANISOU 6878 CA ILE D 194 1985 1772 1922 77 51 -193 C ATOM 6879 C ILE A 194 33.163 84.062 97.079 1.00 15.68 C ANISOU 6879 C ILE D 194 2114 1830 2012 30 21 -209 C ATOM 6880 O ILE A 194 33.184 83.619 98.228 1.00 15.98 O ANISOU 6880 O ILE D 194 2218 1667 2186 43 63 -206 O ATOM 6881 CB ILE A 194 35.200 82.868 96.240 1.00 15.35 C ANISOU 6881 CB ILE D 194 1979 1874 1976 83 73 -244 C ATOM 6882 CG1 ILE A 194 36.532 83.006 95.514 1.00 15.18 C ANISOU 6882 CG1 ILE D 194 2004 1821 1942 82 95 -294 C ATOM 6883 CG2 ILE A 194 34.368 81.821 95.506 1.00 14.83 C ANISOU 6883 CG2 ILE D 194 1941 1840 1853 78 109 -185 C ATOM 6884 CD1 ILE A 194 37.375 81.736 95.503 1.00 14.27 C ANISOU 6884 CD1 ILE D 194 1719 1822 1878 75 59 -305 C ATOM 6885 N ALA A 195 32.056 84.413 96.448 1.00 16.44 N ANISOU 6885 N ALA D 195 2190 1953 2101 6 0 -204 N ATOM 6886 CA ALA A 195 30.721 84.222 96.991 1.00 17.36 C ANISOU 6886 CA ALA D 195 2240 2157 2196 52 -63 -164 C ATOM 6887 C ALA A 195 30.024 83.055 96.290 1.00 17.73 C ANISOU 6887 C ALA D 195 2286 2234 2214 101 -98 -173 C ATOM 6888 O ALA A 195 30.405 82.664 95.190 1.00 17.68 O ANISOU 6888 O ALA D 195 2279 2171 2265 101 -213 -290 O ATOM 6889 CB ALA A 195 29.910 85.497 96.832 1.00 17.83 C ANISOU 6889 CB ALA D 195 2315 2211 2246 25 -46 -109 C ATOM 6890 N GLY A 196 28.988 82.530 96.927 1.00 17.22 N ANISOU 6890 N GLY D 196 2156 2189 2197 117 -112 -213 N ATOM 6891 CA GLY A 196 28.260 81.379 96.416 1.00 16.71 C ANISOU 6891 CA GLY D 196 2059 2139 2149 47 -71 -164 C ATOM 6892 C GLY A 196 26.775 81.593 96.594 1.00 16.48 C ANISOU 6892 C GLY D 196 2069 2082 2109 -12 -82 -165 C ATOM 6893 O GLY A 196 26.215 82.510 96.032 1.00 15.53 O ANISOU 6893 O GLY D 196 1998 1923 1979 -10 -131 -232 O ATOM 6894 N ARG A 197 26.162 80.728 97.388 1.00 17.91 N ANISOU 6894 N ARG D 197 2244 2251 2309 -16 -99 -126 N ATOM 6895 CA ARG A 197 24.722 80.730 97.610 1.00 19.70 C ANISOU 6895 CA ARG D 197 2445 2483 2555 -5 -42 -101 C ATOM 6896 C ARG A 197 24.240 81.996 98.297 1.00 20.00 C ANISOU 6896 C ARG D 197 2494 2518 2587 -25 -48 -70 C ATOM 6897 O ARG A 197 23.097 82.389 98.139 1.00 20.13 O ANISOU 6897 O ARG D 197 2460 2552 2634 -36 -70 -94 O ATOM 6898 CB ARG A 197 24.323 79.496 98.417 1.00 20.68 C ANISOU 6898 CB ARG D 197 2587 2575 2692 41 -81 -54 C ATOM 6899 CG ARG A 197 24.403 78.207 97.584 1.00 24.13 C ANISOU 6899 CG ARG D 197 3037 3001 3127 -28 -70 -93 C ATOM 6900 CD ARG A 197 24.209 76.940 98.410 1.00 29.57 C ANISOU 6900 CD ARG D 197 3751 3668 3815 10 -65 14 C ATOM 6901 NE ARG A 197 24.617 77.083 99.797 1.00 34.82 N ANISOU 6901 NE ARG D 197 4493 4438 4298 22 -35 -25 N ATOM 6902 CZ ARG A 197 24.134 76.346 100.792 1.00 38.62 C ANISOU 6902 CZ ARG D 197 4963 4851 4858 -46 31 15 C ATOM 6903 NH1 ARG A 197 24.550 76.544 102.040 1.00 40.04 N ANISOU 6903 NH1 ARG D 197 5139 5050 5021 -69 -27 -18 N ATOM 6904 NH2 ARG A 197 23.218 75.424 100.547 1.00 40.10 N ANISOU 6904 NH2 ARG D 197 5191 5010 5032 -30 -12 3 N ATOM 6905 N GLY A 198 25.130 82.637 99.042 1.00 20.56 N ANISOU 6905 N GLY D 198 2562 2597 2651 -46 -28 -123 N ATOM 6906 CA GLY A 198 24.819 83.932 99.650 1.00 21.60 C ANISOU 6906 CA GLY D 198 2736 2695 2774 -67 -47 -106 C ATOM 6907 C GLY A 198 24.353 84.956 98.632 1.00 22.23 C ANISOU 6907 C GLY D 198 2833 2786 2827 -88 -41 -115 C ATOM 6908 O GLY A 198 23.529 85.817 98.944 1.00 23.45 O ANISOU 6908 O GLY D 198 3030 2918 2960 -170 -53 -155 O ATOM 6909 N ILE A 199 24.860 84.869 97.407 1.00 21.89 N ANISOU 6909 N ILE D 199 2780 2708 2827 -41 -39 -144 N ATOM 6910 CA ILE A 199 24.371 85.693 96.332 1.00 21.63 C ANISOU 6910 CA ILE D 199 2733 2678 2807 -18 -8 -145 C ATOM 6911 C ILE A 199 23.358 84.966 95.415 1.00 20.90 C ANISOU 6911 C ILE D 199 2614 2560 2765 -28 -5 -141 C ATOM 6912 O ILE A 199 22.334 85.539 95.025 1.00 20.40 O ANISOU 6912 O ILE D 199 2522 2482 2745 -39 -56 -201 O ATOM 6913 CB ILE A 199 25.547 86.290 95.535 1.00 22.30 C ANISOU 6913 CB ILE D 199 2793 2745 2933 39 16 -106 C ATOM 6914 CG1 ILE A 199 26.243 87.371 96.380 1.00 23.58 C ANISOU 6914 CG1 ILE D 199 2988 2969 3001 68 -21 -162 C ATOM 6915 CG2 ILE A 199 25.081 86.897 94.220 1.00 22.74 C ANISOU 6915 CG2 ILE D 199 2911 2751 2975 74 -26 -146 C ATOM 6916 CD1 ILE A 199 27.395 88.072 95.690 1.00 26.78 C ANISOU 6916 CD1 ILE D 199 3330 3432 3412 73 -37 -50 C ATOM 6917 N THR A 200 23.620 83.716 95.053 1.00 19.63 N ANISOU 6917 N THR D 200 2415 2448 2596 -43 -34 -158 N ATOM 6918 CA THR A 200 22.753 83.110 94.047 1.00 18.42 C ANISOU 6918 CA THR D 200 2277 2275 2444 -50 -76 -184 C ATOM 6919 C THR A 200 21.401 82.668 94.599 1.00 18.81 C ANISOU 6919 C THR D 200 2256 2394 2494 -108 -75 -196 C ATOM 6920 O THR A 200 20.477 82.466 93.829 1.00 17.96 O ANISOU 6920 O THR D 200 2049 2324 2451 -276 -133 -275 O ATOM 6921 CB THR A 200 23.436 81.948 93.313 1.00 17.69 C ANISOU 6921 CB THR D 200 2199 2196 2324 -19 -96 -198 C ATOM 6922 OG1 THR A 200 23.790 80.935 94.256 1.00 15.94 O ANISOU 6922 OG1 THR D 200 1961 1831 2265 -49 -55 -396 O ATOM 6923 CG2 THR A 200 24.729 82.423 92.647 1.00 16.78 C ANISOU 6923 CG2 THR D 200 2098 2039 2237 19 -63 -258 C ATOM 6924 N GLU A 201 21.299 82.504 95.917 1.00 19.88 N ANISOU 6924 N GLU D 201 2414 2536 2603 -40 -73 -143 N ATOM 6925 CA GLU A 201 20.022 82.166 96.559 1.00 20.97 C ANISOU 6925 CA GLU D 201 2588 2641 2738 -36 -85 -138 C ATOM 6926 C GLU A 201 19.297 83.398 97.114 1.00 21.39 C ANISOU 6926 C GLU D 201 2649 2668 2807 -31 -85 -107 C ATOM 6927 O GLU A 201 18.244 83.263 97.745 1.00 21.51 O ANISOU 6927 O GLU D 201 2598 2714 2861 -56 -144 -163 O ATOM 6928 CB GLU A 201 20.208 81.118 97.668 1.00 21.34 C ANISOU 6928 CB GLU D 201 2652 2680 2777 -41 -52 -130 C ATOM 6929 CG GLU A 201 20.795 79.779 97.189 1.00 22.94 C ANISOU 6929 CG GLU D 201 2875 2843 2996 -84 -94 -81 C ATOM 6930 CD GLU A 201 20.818 78.675 98.253 1.00 24.40 C ANISOU 6930 CD GLU D 201 3166 3059 3045 -112 -86 -66 C ATOM 6931 OE1 GLU A 201 20.723 78.967 99.475 1.00 25.70 O ANISOU 6931 OE1 GLU D 201 3420 3271 3073 -147 -32 -22 O ATOM 6932 OE2 GLU A 201 20.957 77.492 97.862 1.00 26.34 O ANISOU 6932 OE2 GLU D 201 3476 3302 3229 -17 -116 -51 O ATOM 6933 N ALA A 202 19.849 84.585 96.875 1.00 21.68 N ANISOU 6933 N ALA D 202 2752 2662 2820 -70 -73 -148 N ATOM 6934 CA ALA A 202 19.232 85.817 97.382 1.00 22.42 C ANISOU 6934 CA ALA D 202 2810 2843 2866 -80 -67 -130 C ATOM 6935 C ALA A 202 17.949 86.094 96.610 1.00 23.26 C ANISOU 6935 C ALA D 202 2899 2989 2949 -52 -54 -127 C ATOM 6936 O ALA A 202 17.735 85.530 95.517 1.00 22.49 O ANISOU 6936 O ALA D 202 2768 2941 2834 8 -131 -216 O ATOM 6937 CB ALA A 202 20.188 86.966 97.264 1.00 22.04 C ANISOU 6937 CB ALA D 202 2804 2759 2809 -88 -81 -139 C ATOM 6938 N LYS A 203 17.082 86.933 97.188 1.00 24.06 N ANISOU 6938 N LYS D 203 2969 3095 3076 -81 -63 -109 N ATOM 6939 CA LYS A 203 15.804 87.277 96.556 1.00 24.95 C ANISOU 6939 CA LYS D 203 3113 3205 3161 -57 -28 -54 C ATOM 6940 C LYS A 203 16.019 87.853 95.167 1.00 24.87 C ANISOU 6940 C LYS D 203 3095 3180 3173 -71 -37 -56 C ATOM 6941 O LYS A 203 15.316 87.485 94.228 1.00 25.41 O ANISOU 6941 O LYS D 203 3070 3332 3250 -109 -31 -74 O ATOM 6942 CB LYS A 203 15.009 88.256 97.421 1.00 25.02 C ANISOU 6942 CB LYS D 203 3157 3183 3166 -48 -61 -40 C ATOM 6943 N ASN A 204 16.999 88.742 95.046 1.00 24.49 N ANISOU 6943 N ASN D 204 3045 3113 3146 -60 -34 -72 N ATOM 6944 CA ASN A 204 17.403 89.291 93.757 1.00 24.43 C ANISOU 6944 CA ASN D 204 3038 3084 3160 -55 -36 -76 C ATOM 6945 C ASN A 204 18.905 89.072 93.607 1.00 23.45 C ANISOU 6945 C ASN D 204 2926 2930 3054 -70 -55 -143 C ATOM 6946 O ASN A 204 19.703 89.923 94.013 1.00 23.60 O ANISOU 6946 O ASN D 204 2935 2949 3081 -82 -136 -200 O ATOM 6947 CB ASN A 204 17.046 90.781 93.654 1.00 24.73 C ANISOU 6947 CB ASN D 204 3131 3073 3189 -78 -33 -96 C ATOM 6948 CG ASN A 204 17.434 91.391 92.317 1.00 26.86 C ANISOU 6948 CG ASN D 204 3388 3365 3450 -45 -33 -45 C ATOM 6949 OD1 ASN A 204 18.039 90.732 91.473 1.00 27.94 O ANISOU 6949 OD1 ASN D 204 3478 3524 3612 -132 4 -157 O ATOM 6950 ND2 ASN A 204 17.080 92.667 92.112 1.00 28.83 N ANISOU 6950 ND2 ASN D 204 3725 3479 3750 -52 -35 -128 N ATOM 6951 N PRO A 205 19.298 87.908 93.064 1.00 22.15 N ANISOU 6951 N PRO D 205 2766 2750 2900 -48 -46 -169 N ATOM 6952 CA PRO A 205 20.716 87.559 92.939 1.00 21.12 C ANISOU 6952 CA PRO D 205 2710 2565 2748 -64 -29 -183 C ATOM 6953 C PRO A 205 21.547 88.625 92.247 1.00 20.04 C ANISOU 6953 C PRO D 205 2599 2394 2620 -96 -65 -220 C ATOM 6954 O PRO A 205 22.639 88.896 92.723 1.00 20.14 O ANISOU 6954 O PRO D 205 2732 2276 2643 -95 -42 -308 O ATOM 6955 CB PRO A 205 20.674 86.269 92.103 1.00 20.89 C ANISOU 6955 CB PRO D 205 2676 2545 2716 -53 -45 -168 C ATOM 6956 CG PRO A 205 19.390 85.662 92.482 1.00 21.39 C ANISOU 6956 CG PRO D 205 2716 2595 2814 -35 -37 -130 C ATOM 6957 CD PRO A 205 18.438 86.821 92.557 1.00 21.81 C ANISOU 6957 CD PRO D 205 2728 2706 2852 -63 -15 -157 C ATOM 6958 N ALA A 206 21.058 89.206 91.153 1.00 20.07 N ANISOU 6958 N ALA D 206 2641 2398 2585 -56 -85 -229 N ATOM 6959 CA ALA A 206 21.834 90.231 90.423 1.00 19.74 C ANISOU 6959 CA ALA D 206 2565 2348 2585 -22 -50 -182 C ATOM 6960 C ALA A 206 22.024 91.494 91.256 1.00 20.12 C ANISOU 6960 C ALA D 206 2580 2380 2683 8 -62 -187 C ATOM 6961 O ALA A 206 23.101 92.095 91.250 1.00 20.22 O ANISOU 6961 O ALA D 206 2655 2297 2728 15 -28 -316 O ATOM 6962 CB ALA A 206 21.208 90.571 89.105 1.00 20.22 C ANISOU 6962 CB ALA D 206 2581 2429 2670 -32 -65 -130 C ATOM 6963 N GLY A 207 20.971 91.879 91.965 1.00 20.24 N ANISOU 6963 N GLY D 207 2612 2386 2692 3 -45 -205 N ATOM 6964 CA GLY A 207 21.035 92.997 92.899 1.00 19.98 C ANISOU 6964 CA GLY D 207 2562 2385 2644 -39 -40 -167 C ATOM 6965 C GLY A 207 22.030 92.768 94.018 1.00 19.65 C ANISOU 6965 C GLY D 207 2477 2367 2622 -51 -60 -144 C ATOM 6966 O GLY A 207 22.790 93.670 94.367 1.00 20.11 O ANISOU 6966 O GLY D 207 2447 2406 2785 -107 -113 -233 O ATOM 6967 N ALA A 208 22.031 91.555 94.574 1.00 19.34 N ANISOU 6967 N ALA D 208 2474 2372 2499 -21 -56 -104 N ATOM 6968 CA ALA A 208 22.958 91.186 95.639 1.00 19.24 C ANISOU 6968 CA ALA D 208 2481 2334 2492 -22 -52 -94 C ATOM 6969 C ALA A 208 24.410 91.199 95.144 1.00 19.20 C ANISOU 6969 C ALA D 208 2467 2352 2476 4 -12 -136 C ATOM 6970 O ALA A 208 25.309 91.688 95.837 1.00 19.47 O ANISOU 6970 O ALA D 208 2599 2259 2538 -11 -11 -288 O ATOM 6971 CB ALA A 208 22.583 89.812 96.220 1.00 19.67 C ANISOU 6971 CB ALA D 208 2574 2401 2496 -25 -97 -85 C ATOM 6972 N ALA A 209 24.641 90.680 93.942 1.00 18.11 N ANISOU 6972 N ALA D 209 2328 2165 2385 15 0 -181 N ATOM 6973 CA ALA A 209 25.970 90.664 93.367 1.00 18.96 C ANISOU 6973 CA ALA D 209 2434 2328 2441 4 -25 -126 C ATOM 6974 C ALA A 209 26.452 92.089 93.169 1.00 19.75 C ANISOU 6974 C ALA D 209 2525 2430 2549 -13 -43 -120 C ATOM 6975 O ALA A 209 27.586 92.414 93.530 1.00 19.58 O ANISOU 6975 O ALA D 209 2437 2363 2639 -122 -41 -189 O ATOM 6976 CB ALA A 209 25.981 89.870 92.037 1.00 18.47 C ANISOU 6976 CB ALA D 209 2365 2311 2340 15 -67 -119 C ATOM 6977 N ARG A 210 25.574 92.941 92.635 1.00 21.42 N ANISOU 6977 N ARG D 210 2750 2638 2751 -37 -44 -101 N ATOM 6978 CA ARG A 210 25.889 94.359 92.421 1.00 23.15 C ANISOU 6978 CA ARG D 210 2976 2869 2950 24 -55 -58 C ATOM 6979 C ARG A 210 26.186 95.095 93.733 1.00 23.28 C ANISOU 6979 C ARG D 210 2978 2903 2963 18 -69 -79 C ATOM 6980 O ARG A 210 27.091 95.924 93.785 1.00 23.39 O ANISOU 6980 O ARG D 210 2959 2896 3033 39 -153 -101 O ATOM 6981 CB ARG A 210 24.765 95.073 91.674 1.00 23.93 C ANISOU 6981 CB ARG D 210 3072 2970 3048 -7 -41 -52 C ATOM 6982 CG ARG A 210 24.988 96.597 91.596 1.00 27.00 C ANISOU 6982 CG ARG D 210 3544 3273 3441 60 8 -35 C ATOM 6983 CD ARG A 210 24.155 97.321 90.537 1.00 32.51 C ANISOU 6983 CD ARG D 210 4135 4082 4134 22 28 6 C ATOM 6984 NE ARG A 210 24.726 97.210 89.190 1.00 37.06 N ANISOU 6984 NE ARG D 210 4760 4709 4612 17 -39 34 N ATOM 6985 CZ ARG A 210 25.838 97.823 88.762 1.00 40.40 C ANISOU 6985 CZ ARG D 210 5108 5142 5100 24 -32 5 C ATOM 6986 NH1 ARG A 210 26.554 98.612 89.571 1.00 40.92 N ANISOU 6986 NH1 ARG D 210 5229 5168 5149 15 24 -33 N ATOM 6987 NH2 ARG A 210 26.244 97.637 87.504 1.00 41.52 N ANISOU 6987 NH2 ARG D 210 5332 5322 5120 0 -50 -13 N ATOM 6988 N ALA A 211 25.421 94.791 94.782 1.00 22.95 N ANISOU 6988 N ALA D 211 2923 2857 2938 29 -49 -75 N ATOM 6989 CA ALA A 211 25.661 95.369 96.106 1.00 22.61 C ANISOU 6989 CA ALA D 211 2864 2826 2898 18 -35 -124 C ATOM 6990 C ALA A 211 27.038 94.965 96.647 1.00 22.45 C ANISOU 6990 C ALA D 211 2865 2759 2905 -15 -16 -146 C ATOM 6991 O ALA A 211 27.745 95.789 97.246 1.00 22.14 O ANISOU 6991 O ALA D 211 2741 2771 2899 -33 -52 -360 O ATOM 6992 CB ALA A 211 24.564 94.963 97.083 1.00 22.97 C ANISOU 6992 CB ALA D 211 2954 2853 2919 48 -33 -109 C ATOM 6993 N PHE A 212 27.414 93.701 96.417 1.00 21.66 N ANISOU 6993 N PHE D 212 2786 2632 2809 -22 -7 -219 N ATOM 6994 CA PHE A 212 28.708 93.160 96.813 1.00 20.85 C ANISOU 6994 CA PHE D 212 2751 2480 2690 -19 -3 -178 C ATOM 6995 C PHE A 212 29.804 93.917 96.066 1.00 21.07 C ANISOU 6995 C PHE D 212 2709 2540 2757 -36 13 -155 C ATOM 6996 O PHE A 212 30.747 94.418 96.683 1.00 20.18 O ANISOU 6996 O PHE D 212 2656 2370 2642 18 39 -244 O ATOM 6997 CB PHE A 212 28.761 91.640 96.516 1.00 21.28 C ANISOU 6997 CB PHE D 212 2778 2578 2727 -38 5 -200 C ATOM 6998 CG PHE A 212 29.737 90.876 97.364 1.00 18.86 C ANISOU 6998 CG PHE D 212 2640 2134 2390 -67 -95 -301 C ATOM 6999 CD1 PHE A 212 29.304 90.056 98.401 1.00 20.25 C ANISOU 6999 CD1 PHE D 212 2786 2374 2534 -156 -41 -258 C ATOM 7000 CD2 PHE A 212 31.092 90.967 97.117 1.00 19.32 C ANISOU 7000 CD2 PHE D 212 2610 2313 2418 -38 -10 -219 C ATOM 7001 CE1 PHE A 212 30.211 89.347 99.179 1.00 21.05 C ANISOU 7001 CE1 PHE D 212 2779 2668 2549 -55 -69 -294 C ATOM 7002 CE2 PHE A 212 32.005 90.266 97.896 1.00 19.77 C ANISOU 7002 CE2 PHE D 212 2676 2402 2431 -59 -65 -200 C ATOM 7003 CZ PHE A 212 31.565 89.445 98.921 1.00 20.30 C ANISOU 7003 CZ PHE D 212 2686 2518 2505 54 -104 -180 C ATOM 7004 N LYS A 213 29.669 94.037 94.748 1.00 21.76 N ANISOU 7004 N LYS D 213 2804 2623 2841 -22 33 -119 N ATOM 7005 CA LYS A 213 30.650 94.770 93.945 1.00 23.05 C ANISOU 7005 CA LYS D 213 2966 2805 2985 -12 -29 -103 C ATOM 7006 C LYS A 213 30.743 96.269 94.316 1.00 23.30 C ANISOU 7006 C LYS D 213 2990 2802 3061 17 -28 -141 C ATOM 7007 O LYS A 213 31.841 96.812 94.352 1.00 22.95 O ANISOU 7007 O LYS D 213 3010 2646 3062 -2 -114 -251 O ATOM 7008 CB LYS A 213 30.369 94.604 92.445 1.00 24.10 C ANISOU 7008 CB LYS D 213 3078 3007 3072 -17 -30 -85 C ATOM 7009 CG LYS A 213 31.510 95.062 91.515 1.00 25.99 C ANISOU 7009 CG LYS D 213 3288 3276 3308 36 -43 20 C ATOM 7010 CD LYS A 213 32.858 94.464 91.905 1.00 28.03 C ANISOU 7010 CD LYS D 213 3531 3540 3577 -9 -14 1 C ATOM 7011 CE LYS A 213 33.898 94.569 90.776 1.00 28.71 C ANISOU 7011 CE LYS D 213 3613 3593 3699 22 -9 22 C ATOM 7012 NZ LYS A 213 35.248 94.180 91.254 1.00 28.32 N ANISOU 7012 NZ LYS D 213 3446 3526 3786 -50 3 -25 N ATOM 7013 N ASP A 214 29.606 96.925 94.564 1.00 23.56 N ANISOU 7013 N ASP D 214 3040 2836 3076 21 -46 -170 N ATOM 7014 CA ASP A 214 29.604 98.346 94.968 1.00 24.44 C ANISOU 7014 CA ASP D 214 3133 2974 3177 1 -13 -92 C ATOM 7015 C ASP A 214 30.351 98.546 96.289 1.00 23.99 C ANISOU 7015 C ASP D 214 3071 2934 3107 13 -33 -136 C ATOM 7016 O ASP A 214 31.012 99.570 96.476 1.00 24.66 O ANISOU 7016 O ASP D 214 3173 2982 3212 71 -13 -184 O ATOM 7017 CB ASP A 214 28.175 98.885 95.120 1.00 24.84 C ANISOU 7017 CB ASP D 214 3160 3024 3253 -14 -5 -98 C ATOM 7018 CG ASP A 214 27.467 99.091 93.788 1.00 27.08 C ANISOU 7018 CG ASP D 214 3419 3348 3521 -24 10 -56 C ATOM 7019 OD1 ASP A 214 28.121 99.084 92.724 1.00 29.71 O ANISOU 7019 OD1 ASP D 214 3709 3765 3811 -47 -129 -68 O ATOM 7020 OD2 ASP A 214 26.224 99.257 93.761 1.00 28.92 O ANISOU 7020 OD2 ASP D 214 3557 3492 3939 -200 -12 -155 O ATOM 7021 N GLU A 215 30.232 97.589 97.206 1.00 23.53 N ANISOU 7021 N GLU D 215 3026 2901 3012 -50 -19 -153 N ATOM 7022 CA GLU A 215 30.945 97.682 98.487 1.00 23.01 C ANISOU 7022 CA GLU D 215 2933 2841 2969 -30 -22 -146 C ATOM 7023 C GLU A 215 32.448 97.461 98.328 1.00 22.96 C ANISOU 7023 C GLU D 215 2924 2874 2924 -12 -43 -188 C ATOM 7024 O GLU A 215 33.245 98.090 99.012 1.00 23.05 O ANISOU 7024 O GLU D 215 2955 2775 3028 28 -73 -271 O ATOM 7025 CB GLU A 215 30.355 96.732 99.527 1.00 23.22 C ANISOU 7025 CB GLU D 215 2975 2862 2983 -11 -24 -124 C ATOM 7026 CG GLU A 215 31.024 96.762 100.908 1.00 22.34 C ANISOU 7026 CG GLU D 215 2931 2591 2966 -65 -71 -212 C ATOM 7027 CD GLU A 215 30.753 98.046 101.715 1.00 22.41 C ANISOU 7027 CD GLU D 215 2963 2707 2844 15 -75 -310 C ATOM 7028 OE1 GLU A 215 30.128 98.994 101.189 1.00 21.79 O ANISOU 7028 OE1 GLU D 215 3182 2327 2771 38 -178 -603 O ATOM 7029 OE2 GLU A 215 31.177 98.065 102.879 1.00 20.84 O ANISOU 7029 OE2 GLU D 215 2627 2569 2722 109 -311 -573 O ATOM 7030 N ILE A 216 32.841 96.553 97.430 1.00 21.70 N ANISOU 7030 N ILE D 216 2808 2646 2792 -4 -19 -211 N ATOM 7031 CA ILE A 216 34.246 96.434 97.067 1.00 20.87 C ANISOU 7031 CA ILE D 216 2706 2557 2665 26 -36 -153 C ATOM 7032 C ILE A 216 34.781 97.775 96.575 1.00 21.16 C ANISOU 7032 C ILE D 216 2743 2561 2735 4 -69 -165 C ATOM 7033 O ILE A 216 35.839 98.218 97.036 1.00 20.73 O ANISOU 7033 O ILE D 216 2738 2400 2736 39 -127 -299 O ATOM 7034 CB ILE A 216 34.461 95.354 95.985 1.00 20.35 C ANISOU 7034 CB ILE D 216 2633 2490 2610 0 -9 -139 C ATOM 7035 CG1 ILE A 216 34.232 93.962 96.593 1.00 18.97 C ANISOU 7035 CG1 ILE D 216 2526 2261 2418 12 33 -108 C ATOM 7036 CG2 ILE A 216 35.856 95.448 95.367 1.00 20.67 C ANISOU 7036 CG2 ILE D 216 2699 2599 2555 115 -70 -69 C ATOM 7037 CD1 ILE A 216 34.226 92.850 95.547 1.00 17.79 C ANISOU 7037 CD1 ILE D 216 2250 2133 2374 -74 107 -288 C ATOM 7038 N LYS A 217 34.067 98.388 95.639 1.00 22.43 N ANISOU 7038 N LYS D 217 2857 2757 2905 6 -88 -149 N ATOM 7039 CA LYS A 217 34.441 99.688 95.079 1.00 24.24 C ANISOU 7039 CA LYS D 217 3116 2993 3099 34 -94 -90 C ATOM 7040 C LYS A 217 34.499 100.766 96.153 1.00 24.64 C ANISOU 7040 C LYS D 217 3154 3041 3164 56 -87 -112 C ATOM 7041 O LYS A 217 35.391 101.624 96.135 1.00 24.57 O ANISOU 7041 O LYS D 217 3185 2931 3216 69 -151 -163 O ATOM 7042 CB LYS A 217 33.456 100.133 93.989 1.00 24.67 C ANISOU 7042 CB LYS D 217 3144 3086 3142 24 -81 -60 C ATOM 7043 CG LYS A 217 33.852 101.462 93.339 1.00 27.53 C ANISOU 7043 CG LYS D 217 3569 3383 3506 17 -59 -67 C ATOM 7044 CD LYS A 217 32.816 101.964 92.354 1.00 31.82 C ANISOU 7044 CD LYS D 217 4115 3934 4038 0 19 -17 C ATOM 7045 CE LYS A 217 33.239 103.291 91.746 1.00 33.76 C ANISOU 7045 CE LYS D 217 4394 4152 4281 56 -35 -7 C ATOM 7046 NZ LYS A 217 33.293 104.392 92.769 1.00 35.54 N ANISOU 7046 NZ LYS D 217 4570 4449 4482 11 -66 -16 N ATOM 7047 N ARG A 218 33.558 100.730 97.091 1.00 24.75 N ANISOU 7047 N ARG D 218 3171 3042 3190 40 -62 -124 N ATOM 7048 CA ARG A 218 33.549 101.751 98.142 1.00 24.73 C ANISOU 7048 CA ARG D 218 3210 2999 3187 33 -23 -121 C ATOM 7049 C ARG A 218 34.830 101.676 98.969 1.00 24.93 C ANISOU 7049 C ARG D 218 3221 3025 3225 29 -3 -111 C ATOM 7050 O ARG A 218 35.482 102.709 99.207 1.00 25.76 O ANISOU 7050 O ARG D 218 3340 3055 3390 52 15 -156 O ATOM 7051 CB ARG A 218 32.314 101.642 99.039 1.00 24.69 C ANISOU 7051 CB ARG D 218 3206 2977 3195 22 -35 -132 C ATOM 7052 CG ARG A 218 32.136 102.877 99.951 1.00 24.18 C ANISOU 7052 CG ARG D 218 3217 2890 3081 -4 -13 -154 C ATOM 7053 CD ARG A 218 31.031 102.719 100.989 1.00 23.02 C ANISOU 7053 CD ARG D 218 3090 2691 2964 -29 -77 -132 C ATOM 7054 NE ARG A 218 31.308 101.628 101.923 1.00 23.09 N ANISOU 7054 NE ARG D 218 3178 2722 2872 -85 -112 -271 N ATOM 7055 CZ ARG A 218 32.202 101.660 102.901 1.00 23.80 C ANISOU 7055 CZ ARG D 218 3089 2863 3090 -72 -55 -82 C ATOM 7056 NH1 ARG A 218 32.925 102.750 103.135 1.00 24.81 N ANISOU 7056 NH1 ARG D 218 3142 2957 3326 48 -113 -61 N ATOM 7057 NH2 ARG A 218 32.362 100.598 103.681 1.00 23.46 N ANISOU 7057 NH2 ARG D 218 3160 2721 3030 -7 -154 -93 N ATOM 7058 N ILE A 219 35.209 100.458 99.356 1.00 24.69 N ANISOU 7058 N ILE D 219 3207 3020 3151 72 -16 -117 N ATOM 7059 CA ILE A 219 36.349 100.197 100.233 1.00 24.12 C ANISOU 7059 CA ILE D 219 3109 3004 3051 28 -17 -121 C ATOM 7060 C ILE A 219 37.717 100.307 99.537 1.00 24.45 C ANISOU 7060 C ILE D 219 3141 3040 3108 60 -18 -127 C ATOM 7061 O ILE A 219 38.616 100.968 100.053 1.00 24.72 O ANISOU 7061 O ILE D 219 3148 3057 3188 76 11 -205 O ATOM 7062 CB ILE A 219 36.207 98.823 100.931 1.00 24.15 C ANISOU 7062 CB ILE D 219 3095 3034 3047 66 -34 -128 C ATOM 7063 CG1 ILE A 219 34.982 98.801 101.856 1.00 23.78 C ANISOU 7063 CG1 ILE D 219 3083 3012 2940 -22 -53 -189 C ATOM 7064 CG2 ILE A 219 37.459 98.471 101.715 1.00 23.75 C ANISOU 7064 CG2 ILE D 219 3130 3008 2884 20 3 -105 C ATOM 7065 CD1 ILE A 219 34.500 97.394 102.268 1.00 24.08 C ANISOU 7065 CD1 ILE D 219 3110 3099 2939 131 -50 -118 C ATOM 7066 N TRP A 220 37.875 99.656 98.381 1.00 24.18 N ANISOU 7066 N TRP D 220 3098 2984 3103 47 -27 -139 N ATOM 7067 CA TRP A 220 39.167 99.596 97.681 1.00 24.11 C ANISOU 7067 CA TRP D 220 3115 2973 3070 49 -54 -117 C ATOM 7068 C TRP A 220 39.356 100.674 96.610 1.00 25.42 C ANISOU 7068 C TRP D 220 3306 3120 3233 33 -20 -83 C ATOM 7069 O TRP A 220 40.486 100.887 96.132 1.00 25.55 O ANISOU 7069 O TRP D 220 3351 3105 3248 58 -95 -62 O ATOM 7070 CB TRP A 220 39.418 98.181 97.089 1.00 23.04 C ANISOU 7070 CB TRP D 220 2970 2844 2939 16 -75 -144 C ATOM 7071 CG TRP A 220 39.830 97.202 98.152 1.00 20.07 C ANISOU 7071 CG TRP D 220 2631 2444 2550 42 -82 -326 C ATOM 7072 CD1 TRP A 220 41.102 96.951 98.599 1.00 18.53 C ANISOU 7072 CD1 TRP D 220 2529 2195 2314 47 10 -328 C ATOM 7073 CD2 TRP A 220 38.960 96.379 98.938 1.00 17.65 C ANISOU 7073 CD2 TRP D 220 2416 2073 2216 15 -64 -433 C ATOM 7074 NE1 TRP A 220 41.071 96.016 99.602 1.00 18.21 N ANISOU 7074 NE1 TRP D 220 2456 2077 2383 98 -15 -473 N ATOM 7075 CE2 TRP A 220 39.765 95.655 99.836 1.00 16.20 C ANISOU 7075 CE2 TRP D 220 2339 1755 2060 104 -37 -530 C ATOM 7076 CE3 TRP A 220 37.572 96.175 98.960 1.00 16.94 C ANISOU 7076 CE3 TRP D 220 2304 1998 2132 -3 -45 -428 C ATOM 7077 CZ2 TRP A 220 39.231 94.752 100.762 1.00 17.11 C ANISOU 7077 CZ2 TRP D 220 2356 1971 2174 102 -24 -427 C ATOM 7078 CZ3 TRP A 220 37.041 95.278 99.873 1.00 16.83 C ANISOU 7078 CZ3 TRP D 220 2392 1888 2114 14 -62 -353 C ATOM 7079 CH2 TRP A 220 37.867 94.581 100.765 1.00 17.12 C ANISOU 7079 CH2 TRP D 220 2290 1977 2237 28 -94 -359 C ATOM 7080 N GLY A 221 38.277 101.369 96.265 1.00 26.84 N ANISOU 7080 N GLY D 221 3450 3324 3422 32 10 -76 N ATOM 7081 CA GLY A 221 38.284 102.333 95.164 1.00 28.68 C ANISOU 7081 CA GLY D 221 3715 3566 3613 34 16 -53 C ATOM 7082 C GLY A 221 38.821 103.703 95.519 1.00 29.85 C ANISOU 7082 C GLY D 221 3898 3685 3759 22 17 -23 C ATOM 7083 O GLY A 221 39.168 103.981 96.675 1.00 30.80 O ANISOU 7083 O GLY D 221 4069 3788 3843 59 58 -64 O ATOM 7084 OXT GLY A 221 38.922 104.547 94.632 1.00 30.46 O ANISOU 7084 OXT GLY D 221 3969 3762 3841 11 5 -26 O TER 7085 GLY D 221 END