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*** HIVp_CA ***elNémo ID: 2602061615123036985Job options:ID = 2602061615123036985 JOBID = HIVp_CA USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER HIVp_CA CRYST1 50.746 57.807 62.006 90.00 90.00 90.00 P 21 21 21 1 ATOM 1 CA PRO A 1 27.719 22.265 34.525 1.00 24.79 C ANISOU 1 CA PRO A 1 2833 3634 2950 238 -116 -18 C ATOM 2 CA GLN A 2 23.872 22.620 34.516 1.00 17.82 C ANISOU 2 CA GLN A 2 2575 2782 1411 284 -61 121 C ATOM 3 CA ILE A 3 22.953 25.808 32.633 1.00 16.67 C ANISOU 3 CA ILE A 3 2552 2337 1442 458 -7 -249 C ATOM 4 CA THR A 4 19.503 27.351 32.833 1.00 15.75 C ANISOU 4 CA THR A 4 2575 2027 1382 491 29 -180 C ATOM 5 CA LEU A 5 18.036 29.497 30.073 1.00 13.94 C ANISOU 5 CA LEU A 5 2308 1907 1082 331 97 -220 C ATOM 6 CA TRP A 6 16.707 32.666 31.611 1.00 17.05 C ANISOU 6 CA TRP A 6 2845 2216 1417 514 101 -445 C ATOM 7 CA LYS A 7 19.868 34.291 30.152 1.00 18.47 C ANISOU 7 CA LYS A 7 2899 2250 1865 354 -194 -724 C ATOM 8 CA ARG A 8 21.751 33.512 26.958 1.00 14.08 C ANISOU 8 CA ARG A 8 2189 1788 1372 217 -258 -291 C ATOM 9 CA PRO A 9 24.058 30.507 27.473 1.00 12.81 C ANISOU 9 CA PRO A 9 2230 1621 1016 43 -352 -232 C ATOM 10 CA LEU A 10 27.264 32.344 26.801 1.00 14.99 C ANISOU 10 CA LEU A 10 2194 1917 1581 -90 -250 -271 C ATOM 11 CA VAL A 11 30.473 30.664 27.715 1.00 16.59 C ANISOU 11 CA VAL A 11 2390 2079 1833 -215 -869 353 C ATOM 12 CA THR A 12 34.172 31.223 27.350 1.00 16.58 C ANISOU 12 CA THR A 12 2279 2090 1931 -287 -1005 193 C ATOM 13 CA ILE A 13 36.036 29.162 24.798 1.00 16.14 C ANISOU 13 CA ILE A 13 1954 1921 2258 -305 -830 425 C ATOM 14 CA ARG A 14 39.740 28.714 23.796 1.00 19.48 C ANISOU 14 CA ARG A 14 1845 2023 3531 -149 -998 564 C ATOM 15 CA ILE A 15 40.664 28.280 20.005 1.00 18.93 C ANISOU 15 CA ILE A 15 1883 2053 3253 -116 -482 584 C ATOM 16 CA GLY A 16 43.870 28.844 17.943 1.00 21.12 C ANISOU 16 CA GLY A 16 2402 2552 3067 -217 -98 18 C ATOM 17 CA GLY A 17 45.383 29.828 21.189 1.00 25.17 C ANISOU 17 CA GLY A 17 3543 2677 3341 -8 -401 -247 C ATOM 18 CA GLN A 18 42.946 32.713 21.880 1.00 22.92 C ANISOU 18 CA GLN A 18 2392 2618 3697 -262 -558 -156 C ATOM 19 CA ALEU A 19 39.800 33.235 24.388 0.50 24.41 C ANISOU 19 CA ALEU A 19 2879 2841 3553 -77 -788 560 C ATOM 20 CA BLEU A 19 39.837 33.221 24.286 0.50 21.98 C ANISOU 20 CA BLEU A 19 2692 2479 3181 -99 -904 521 C ATOM 21 CA LYS A 20 36.328 34.205 23.109 1.00 17.88 C ANISOU 21 CA LYS A 20 2219 1964 2607 -365 -938 741 C ATOM 22 CA AGLU A 21 32.820 34.252 24.177 0.50 15.90 C ANISOU 22 CA AGLU A 21 2119 1922 2000 -385 -886 251 C ATOM 23 CA BGLU A 21 32.684 34.357 24.231 0.50 16.10 C ANISOU 23 CA BGLU A 21 2280 1912 1925 -331 -890 262 C ATOM 24 CA ALA A 22 30.334 31.986 22.363 1.00 11.08 C ANISOU 24 CA ALA A 22 1562 1226 1420 -198 -365 126 C ATOM 25 CA LEU A 23 26.747 30.934 22.555 1.00 10.58 C ANISOU 25 CA LEU A 23 1559 1343 1117 -160 -295 -55 C ATOM 26 CA LEU A 24 25.804 27.311 23.210 1.00 9.65 C ANISOU 26 CA LEU A 24 1327 1398 941 75 -60 -57 C ATOM 27 CA ASP A 25 23.340 26.812 20.393 1.00 8.39 C ANISOU 27 CA ASP A 25 1218 1203 766 39 -19 -18 C ATOM 28 CA THR A 26 21.386 23.566 20.190 1.00 8.04 C ANISOU 28 CA THR A 26 1083 1070 899 -36 35 -40 C ATOM 29 CA GLY A 27 19.612 24.838 17.068 1.00 8.65 C ANISOU 29 CA GLY A 27 1189 1097 999 55 -18 109 C ATOM 30 CA ALA A 28 22.892 25.033 15.169 1.00 8.59 C ANISOU 30 CA ALA A 28 1209 1028 1027 142 19 67 C ATOM 31 CA ASP A 29 24.191 21.928 13.416 1.00 9.24 C ANISOU 31 CA ASP A 29 1275 1238 995 95 212 -179 C ATOM 32 CA ASP A 30 27.545 23.670 12.985 1.00 10.48 C ANISOU 32 CA ASP A 30 1304 1484 1191 210 186 62 C ATOM 33 CA THR A 31 29.929 25.874 14.976 1.00 9.68 C ANISOU 33 CA THR A 31 1241 1267 1167 192 88 62 C ATOM 34 CA VAL A 32 30.273 29.340 13.384 1.00 9.86 C ANISOU 34 CA VAL A 32 1187 1260 1297 93 128 208 C ATOM 35 CA LEU A 33 32.664 31.982 14.629 1.00 10.43 C ANISOU 35 CA LEU A 33 1263 1393 1305 76 118 298 C ATOM 36 CA GLU A 34 33.059 35.623 13.638 1.00 13.57 C ANISOU 36 CA GLU A 34 1652 1630 1872 -22 -190 530 C ATOM 37 CA GLU A 35 35.990 36.650 11.528 1.00 17.77 C ANISOU 37 CA GLU A 35 2129 2233 2388 -136 -72 817 C ATOM 38 CA MET A 36 39.325 35.509 12.967 1.00 19.59 C ANISOU 38 CA MET A 36 2029 2473 2941 -508 -356 319 C ATOM 39 CA ASN A 37 42.570 33.987 11.732 1.00 21.71 C ANISOU 39 CA ASN A 37 2469 2807 2972 -340 84 586 C ATOM 40 CA LEU A 38 43.145 30.242 12.191 1.00 20.76 C ANISOU 40 CA LEU A 38 2193 2897 2795 112 -204 158 C ATOM 41 CA PRO A 39 46.090 28.159 11.052 1.00 26.48 C ANISOU 41 CA PRO A 39 2840 3798 3422 238 -352 -351 C ATOM 42 CA GLY A 40 46.069 25.598 8.306 1.00 27.90 C ANISOU 42 CA GLY A 40 3076 3764 3757 99 -9 -439 C ATOM 43 CA LYS A 41 44.077 24.731 5.314 1.00 24.79 C ANISOU 43 CA LYS A 41 2387 3698 3332 438 162 -450 C ATOM 44 CA TRP A 42 40.471 25.831 4.864 1.00 17.40 C ANISOU 44 CA TRP A 42 1587 2739 2285 16 285 131 C ATOM 45 CA LYS A 43 37.784 25.272 2.263 1.00 18.91 C ANISOU 45 CA LYS A 43 2093 2902 2189 508 112 -57 C ATOM 46 CA PRO A 44 35.176 27.666 1.004 1.00 16.12 C ANISOU 46 CA PRO A 44 1659 2405 2059 325 84 -74 C ATOM 47 CA LYS A 45 31.672 26.614 2.032 1.00 14.58 C ANISOU 47 CA LYS A 45 1824 2015 1700 215 -17 -386 C ATOM 48 CA MET A 46 28.178 28.123 2.243 1.00 13.59 C ANISOU 48 CA MET A 46 1745 1681 1738 190 114 -146 C ATOM 49 CA AILE A 47 25.721 27.757 5.045 0.50 12.92 C ANISOU 49 CA AILE A 47 1587 1489 1832 117 146 -136 C ATOM 50 CA BILE A 47 25.632 27.730 5.008 0.50 12.13 C ANISOU 50 CA BILE A 47 1575 1368 1666 160 110 -196 C ATOM 51 CA GLY A 48 22.140 28.930 5.627 1.00 12.49 C ANISOU 51 CA GLY A 48 1436 1594 1714 56 51 48 C ATOM 52 CA GLY A 49 20.531 30.386 8.694 1.00 11.10 C ANISOU 52 CA GLY A 49 1370 1496 1348 281 43 287 C ATOM 53 CA ILE A 50 17.245 32.068 9.435 1.00 10.92 C ANISOU 53 CA ILE A 50 1388 1290 1471 189 103 103 C ATOM 54 CA GLY A 51 17.999 35.016 7.146 1.00 12.75 C ANISOU 54 CA GLY A 51 1534 1597 1711 182 -62 192 C ATOM 55 CA GLY A 52 19.580 33.270 4.143 1.00 15.11 C ANISOU 55 CA GLY A 52 1764 2319 1656 119 -157 -11 C ATOM 56 CA PHE A 53 22.973 32.032 3.102 1.00 10.60 C ANISOU 56 CA PHE A 53 1484 1388 1152 16 25 -43 C ATOM 57 CA ILE A 54 26.504 33.162 3.817 1.00 10.77 C ANISOU 57 CA ILE A 54 1300 1547 1244 95 -44 -57 C ATOM 58 CA LYS A 55 29.984 32.258 2.741 1.00 11.78 C ANISOU 58 CA LYS A 55 1477 1615 1381 113 -4 44 C ATOM 59 CA VAL A 56 32.262 30.783 5.368 1.00 11.33 C ANISOU 59 CA VAL A 56 1299 1617 1388 88 -148 110 C ATOM 60 CA ARG A 57 35.747 29.317 5.648 1.00 12.54 C ANISOU 60 CA ARG A 57 1269 2070 1426 139 19 139 C ATOM 61 CA GLN A 58 35.655 25.697 6.859 1.00 14.73 C ANISOU 61 CA GLN A 58 1477 2142 1976 342 399 307 C ATOM 62 CA TYR A 59 38.467 24.614 9.068 1.00 15.20 C ANISOU 62 CA TYR A 59 1497 2301 1978 181 537 525 C ATOM 63 CA ASP A 60 38.545 20.953 9.994 1.00 19.11 C ANISOU 63 CA ASP A 60 2053 2252 2955 407 473 164 C ATOM 64 CA GLN A 61 39.825 19.080 12.997 1.00 20.18 C ANISOU 64 CA GLN A 61 1986 2824 2858 401 289 124 C ATOM 65 CA ILE A 62 40.319 22.184 15.069 1.00 14.81 C ANISOU 65 CA ILE A 62 1095 2098 2431 417 120 412 C ATOM 66 CA PRO A 63 40.838 21.982 18.915 1.00 17.34 C ANISOU 66 CA PRO A 63 1263 2326 2999 385 -220 474 C ATOM 67 CA VAL A 64 38.362 24.033 20.905 1.00 14.86 C ANISOU 67 CA VAL A 64 1567 1881 2198 -361 -292 338 C ATOM 68 CA GLU A 65 38.066 24.113 24.779 1.00 17.76 C ANISOU 68 CA GLU A 65 1878 2032 2837 -455 -810 182 C ATOM 69 CA ILE A 66 34.543 24.984 25.984 1.00 17.69 C ANISOU 69 CA ILE A 66 2245 1623 2852 -251 -479 49 C ATOM 70 CA CYS A 67 34.069 25.709 29.704 1.00 24.95 C ANISOU 70 CA CYS A 67 3519 2883 3078 -146 -438 -372 C ATOM 71 CA GLY A 68 37.120 23.554 30.275 1.00 22.70 C ANISOU 71 CA GLY A 68 3441 2494 2687 63 -907 -326 C ATOM 72 CA HIS A 69 35.898 20.596 28.135 1.00 16.56 C ANISOU 72 CA HIS A 69 2185 1818 2288 -71 -656 372 C ATOM 73 CA LYS A 70 37.874 19.557 25.090 1.00 18.05 C ANISOU 73 CA LYS A 70 2256 1958 2643 324 -180 463 C ATOM 74 CA ALA A 71 36.590 19.188 21.546 1.00 13.87 C ANISOU 74 CA ALA A 71 1437 1644 2187 225 213 244 C ATOM 75 CA ILE A 72 38.308 18.847 18.169 1.00 14.64 C ANISOU 75 CA ILE A 72 1696 1547 2318 491 426 406 C ATOM 76 CA GLY A 73 36.213 19.418 15.104 1.00 15.04 C ANISOU 76 CA GLY A 73 1585 1593 2533 307 409 257 C ATOM 77 CA THR A 74 34.984 21.623 12.362 1.00 13.41 C ANISOU 77 CA THR A 74 1360 1669 2065 214 459 383 C ATOM 78 CA VAL A 75 34.819 25.377 12.818 1.00 12.87 C ANISOU 78 CA VAL A 75 1333 1670 1885 106 438 341 C ATOM 79 CA LEU A 76 33.255 27.664 10.242 1.00 11.68 C ANISOU 79 CA LEU A 76 1164 1543 1729 115 282 199 C ATOM 80 CA VAL A 77 34.415 31.270 10.144 1.00 11.76 C ANISOU 80 CA VAL A 77 1241 1609 1615 -66 -4 428 C ATOM 81 CA GLY A 78 32.274 34.021 8.626 1.00 13.32 C ANISOU 81 CA GLY A 78 1880 1633 1548 -174 -159 294 C ATOM 82 CA PRO A 79 29.646 36.704 9.175 1.00 13.49 C ANISOU 82 CA PRO A 79 2109 1251 1763 171 -574 66 C ATOM 83 CA THR A 80 27.599 35.138 11.841 1.00 16.10 C ANISOU 83 CA THR A 80 1967 1995 2153 -342 -623 542 C ATOM 84 CA PRO A 81 25.849 37.615 14.204 1.00 15.89 C ANISOU 84 CA PRO A 81 2202 1453 2381 -123 -486 541 C ATOM 85 CA AVAL A 82 27.455 35.976 17.262 0.50 15.62 C ANISOU 85 CA AVAL A 82 2095 1661 2177 117 71 451 C ATOM 86 CA BVAL A 82 27.548 36.039 17.293 0.50 13.59 C ANISOU 86 CA BVAL A 82 1945 1246 1970 0 36 427 C ATOM 87 CA ASN A 83 29.918 33.163 17.868 1.00 10.18 C ANISOU 87 CA ASN A 83 1259 1146 1462 14 -90 233 C ATOM 88 CA ILE A 84 27.874 29.936 18.121 1.00 9.20 C ANISOU 88 CA ILE A 84 1207 1142 1144 32 100 77 C ATOM 89 CA ILE A 85 28.828 26.486 19.351 1.00 9.36 C ANISOU 89 CA ILE A 85 1212 1079 1263 84 30 93 C ATOM 90 CA GLY A 86 26.758 23.991 17.406 1.00 8.51 C ANISOU 90 CA GLY A 86 1171 1046 1014 21 -25 73 C ATOM 91 CA ARG A 87 25.947 20.365 17.846 1.00 8.66 C ANISOU 91 CA ARG A 87 1113 1003 1173 34 -27 -1 C ATOM 92 CA ASN A 88 29.106 19.153 16.155 1.00 10.08 C ANISOU 92 CA ASN A 88 1207 1216 1407 34 94 51 C ATOM 93 CA LEU A 89 31.034 20.331 19.239 1.00 10.55 C ANISOU 93 CA LEU A 89 1178 1226 1604 43 1 148 C ATOM 94 CA LEU A 90 28.258 20.161 21.849 1.00 9.36 C ANISOU 94 CA LEU A 90 1235 1093 1225 95 -43 9 C ATOM 95 CA THR A 91 28.120 16.392 21.315 1.00 10.34 C ANISOU 95 CA THR A 91 1214 1275 1439 89 125 143 C ATOM 96 CA GLN A 92 31.878 16.096 21.906 1.00 11.30 C ANISOU 96 CA GLN A 92 1264 1254 1773 244 -154 128 C ATOM 97 CA ILE A 93 31.625 17.763 25.302 1.00 12.60 C ANISOU 97 CA ILE A 93 1496 1662 1627 -2 -239 12 C ATOM 98 CA GLY A 94 28.703 15.562 26.316 1.00 13.46 C ANISOU 98 CA GLY A 94 1855 1569 1690 153 -123 499 C ATOM 99 CA ACYS A 95 25.865 18.124 26.160 0.50 13.40 C ANISOU 99 CA ACYS A 95 1927 1922 1240 345 172 161 C ATOM 100 CA BCYS A 95 26.063 18.261 26.299 0.50 12.64 C ANISOU 100 CA BCYS A 95 1716 1820 1265 422 -59 373 C ATOM 101 CA THR A 96 22.378 17.248 26.480 1.00 13.59 C ANISOU 101 CA THR A 96 1925 1811 1428 442 261 377 C ATOM 102 CA LEU A 97 19.041 19.029 26.932 1.00 12.96 C ANISOU 102 CA LEU A 97 1845 1731 1346 368 47 369 C ATOM 103 CA ASN A 98 17.076 18.128 30.058 1.00 15.60 C ANISOU 103 CA ASN A 98 2273 2117 1537 518 459 512 C ATOM 104 CA PHE A 99 13.679 18.998 31.345 1.00 18.40 C ANISOU 104 CA PHE A 99 2316 2335 2339 405 542 390 C TER ATOM 105 CA PRO B 1 13.702 13.683 29.741 1.00 27.13 C ANISOU 105 CA PRO B 1 3384 3299 3624 -425 522 226 C ATOM 106 CA GLN B 2 17.042 13.870 28.261 1.00 22.76 C ANISOU 106 CA GLN B 2 3099 2655 2893 33 833 489 C ATOM 107 CA ILE B 3 17.585 14.885 24.634 1.00 20.06 C ANISOU 107 CA ILE B 3 2973 2275 2373 -274 668 -250 C ATOM 108 CA THR B 4 20.674 13.936 22.871 1.00 19.54 C ANISOU 108 CA THR B 4 3027 1726 2670 524 834 443 C ATOM 109 CA LEU B 5 22.356 16.291 20.383 1.00 9.93 C ANISOU 109 CA LEU B 5 1468 972 1331 28 79 98 C ATOM 110 CA TRP B 6 23.524 13.655 17.876 1.00 11.27 C ANISOU 110 CA TRP B 6 1414 1160 1708 261 80 -141 C ATOM 111 CA LYS B 7 20.574 14.755 15.767 1.00 10.96 C ANISOU 111 CA LYS B 7 1382 1343 1437 143 18 -323 C ATOM 112 CA ARG B 8 18.504 17.931 15.739 1.00 10.03 C ANISOU 112 CA ARG B 8 1209 1321 1279 141 -48 -279 C ATOM 113 CA PRO B 9 16.482 18.214 18.959 1.00 10.43 C ANISOU 113 CA PRO B 9 1158 1132 1672 95 53 127 C ATOM 114 CA LEU B 10 13.067 18.190 17.302 1.00 11.46 C ANISOU 114 CA LEU B 10 1145 1432 1774 -82 -96 -195 C ATOM 115 CA VAL B 11 10.054 17.653 19.463 1.00 13.10 C ANISOU 115 CA VAL B 11 1309 1635 2032 80 152 194 C ATOM 116 CA THR B 12 6.309 17.838 19.125 1.00 16.16 C ANISOU 116 CA THR B 12 1377 2226 2537 -304 -124 105 C ATOM 117 CA ILE B 13 4.528 20.982 20.170 1.00 15.98 C ANISOU 117 CA ILE B 13 1315 2047 2708 -76 97 82 C ATOM 118 CA ARG B 14 0.890 22.087 20.207 1.00 20.16 C ANISOU 118 CA ARG B 14 1511 2131 4017 -137 209 185 C ATOM 119 CA ILE B 15 -0.056 25.637 19.395 1.00 19.19 C ANISOU 119 CA ILE B 15 2019 2188 3082 254 578 484 C ATOM 120 CA GLY B 16 -3.192 27.291 18.219 1.00 22.97 C ANISOU 120 CA GLY B 16 2553 2912 3261 145 -298 32 C ATOM 121 CA GLY B 17 -4.576 23.593 18.116 1.00 22.44 C ANISOU 121 CA GLY B 17 1566 3576 3385 -977 261 -33 C ATOM 122 CA GLN B 18 -2.092 22.379 15.603 1.00 24.41 C ANISOU 122 CA GLN B 18 2784 2803 3686 55 -169 87 C ATOM 123 CA LEU B 19 0.629 19.842 16.456 1.00 20.03 C ANISOU 123 CA LEU B 19 1905 2374 3330 -239 -306 146 C ATOM 124 CA LYS B 20 3.968 20.718 14.943 1.00 19.04 C ANISOU 124 CA LYS B 20 2227 2344 2660 -130 -342 304 C ATOM 125 CA GLU B 21 7.724 19.613 15.052 1.00 16.17 C ANISOU 125 CA GLU B 21 1897 2006 2237 -336 -685 30 C ATOM 126 CA ALA B 22 10.031 22.247 16.434 1.00 12.58 C ANISOU 126 CA ALA B 22 1587 1293 1899 66 -437 8 C ATOM 127 CA LEU B 23 13.662 22.627 17.505 1.00 9.96 C ANISOU 127 CA LEU B 23 1292 1040 1451 90 -79 140 C ATOM 128 CA LEU B 24 14.536 23.029 21.136 1.00 10.42 C ANISOU 128 CA LEU B 24 1146 1145 1667 23 -38 -12 C ATOM 129 CA ASP B 25 16.906 25.958 20.533 1.00 9.04 C ANISOU 129 CA ASP B 25 1140 1074 1219 166 -4 64 C ATOM 130 CA THR B 26 19.064 27.393 23.266 1.00 9.41 C ANISOU 130 CA THR B 26 1337 1249 989 247 73 -142 C ATOM 131 CA GLY B 27 20.481 29.841 20.709 1.00 10.14 C ANISOU 131 CA GLY B 27 1266 1360 1224 -70 36 -56 C ATOM 132 CA ALA B 28 17.115 31.482 20.082 1.00 10.67 C ANISOU 132 CA ALA B 28 1555 1182 1314 220 150 114 C ATOM 133 CA ASP B 29 15.920 34.212 22.459 1.00 11.21 C ANISOU 133 CA ASP B 29 1847 1179 1232 250 134 -46 C ATOM 134 CA ASP B 30 12.337 33.876 21.321 1.00 12.45 C ANISOU 134 CA ASP B 30 1756 1625 1348 373 46 89 C ATOM 135 CA THR B 31 10.194 31.210 19.777 1.00 10.95 C ANISOU 135 CA THR B 31 1411 1216 1534 428 131 388 C ATOM 136 CA AVAL B 32 9.677 31.536 15.998 0.50 10.27 C ANISOU 136 CA AVAL B 32 1039 1455 1406 52 -196 185 C ATOM 137 CA BVAL B 32 9.595 31.576 16.039 0.50 10.37 C ANISOU 137 CA BVAL B 32 1182 1368 1390 18 -248 147 C ATOM 138 CA LEU B 33 7.216 29.418 14.074 1.00 11.24 C ANISOU 138 CA LEU B 33 1406 1489 1376 72 15 218 C ATOM 139 CA GLU B 34 6.660 28.878 10.440 1.00 13.58 C ANISOU 139 CA GLU B 34 1749 1808 1600 -196 16 156 C ATOM 140 CA GLU B 35 4.008 30.894 8.764 1.00 14.57 C ANISOU 140 CA GLU B 35 1929 2190 1414 77 -230 238 C ATOM 141 CA MET B 36 0.527 30.139 10.236 1.00 17.36 C ANISOU 141 CA MET B 36 1988 2200 2408 -478 -279 146 C ATOM 142 CA ASN B 37 -2.638 32.231 10.517 1.00 21.01 C ANISOU 142 CA ASN B 37 2125 3453 2404 -119 -174 367 C ATOM 143 CA LEU B 38 -3.034 32.656 14.287 1.00 19.95 C ANISOU 143 CA LEU B 38 2009 2797 2771 -395 -92 571 C ATOM 144 CA PRO B 39 -5.876 34.619 15.681 1.00 22.44 C ANISOU 144 CA PRO B 39 2471 2940 3113 -47 -201 266 C ATOM 145 CA GLY B 40 -5.375 37.721 17.748 1.00 25.65 C ANISOU 145 CA GLY B 40 3273 3280 3192 -731 500 147 C ATOM 146 CA LYS B 41 -3.396 41.006 17.797 1.00 22.18 C ANISOU 146 CA LYS B 41 2118 2784 3526 164 377 97 C ATOM 147 CA TRP B 42 0.227 41.166 16.820 1.00 16.77 C ANISOU 147 CA TRP B 42 1782 2153 2434 519 385 416 C ATOM 148 CA LYS B 43 3.093 43.659 16.384 1.00 17.00 C ANISOU 148 CA LYS B 43 1564 2182 2712 536 551 372 C ATOM 149 CA PRO B 44 5.751 43.669 13.585 1.00 16.08 C ANISOU 149 CA PRO B 44 1850 1879 2378 228 227 406 C ATOM 150 CA LYS B 45 9.294 42.745 14.409 1.00 13.22 C ANISOU 150 CA LYS B 45 1638 1631 1754 306 163 46 C ATOM 151 CA AMET B 46 12.615 41.969 12.670 0.50 10.47 C ANISOU 151 CA AMET B 46 1472 1202 1302 -16 83 -247 C ATOM 152 CA BMET B 46 12.502 41.909 12.624 0.50 10.99 C ANISOU 152 CA BMET B 46 1512 1341 1321 96 122 -176 C ATOM 153 CA ILE B 47 14.813 39.177 13.940 1.00 11.08 C ANISOU 153 CA ILE B 47 1332 1584 1293 -57 89 -142 C ATOM 154 CA GLY B 48 18.320 38.474 12.794 1.00 13.20 C ANISOU 154 CA GLY B 48 1515 1521 1978 142 177 -70 C ATOM 155 CA GLY B 49 20.538 35.477 12.381 1.00 11.55 C ANISOU 155 CA GLY B 49 1590 1385 1410 234 26 197 C ATOM 156 CA ILE B 50 22.936 33.957 9.913 1.00 10.38 C ANISOU 156 CA ILE B 50 1104 1567 1270 206 145 143 C ATOM 157 CA GLY B 51 22.117 35.473 6.544 1.00 11.38 C ANISOU 157 CA GLY B 51 1455 1657 1211 331 122 383 C ATOM 158 CA GLY B 52 20.416 38.577 7.923 1.00 11.90 C ANISOU 158 CA GLY B 52 1319 1420 1783 19 184 369 C ATOM 159 CA PHE B 53 16.957 39.462 9.112 1.00 11.56 C ANISOU 159 CA PHE B 53 1218 1684 1488 120 26 -9 C ATOM 160 CA ILE B 54 13.400 38.256 8.561 1.00 12.23 C ANISOU 160 CA ILE B 54 1475 1658 1513 288 -275 -370 C ATOM 161 CA LYS B 55 10.174 39.996 9.260 1.00 11.43 C ANISOU 161 CA LYS B 55 1470 1319 1553 139 -3 180 C ATOM 162 CA VAL B 56 7.844 38.344 11.760 1.00 12.25 C ANISOU 162 CA VAL B 56 1484 1255 1914 72 111 388 C ATOM 163 CA ARG B 57 4.560 38.942 13.570 1.00 13.08 C ANISOU 163 CA ARG B 57 1257 1556 2156 194 146 351 C ATOM 164 CA GLN B 58 4.841 39.000 17.350 1.00 13.81 C ANISOU 164 CA GLN B 58 1578 1698 1968 561 430 173 C ATOM 165 CA TYR B 59 1.911 37.412 19.242 1.00 15.48 C ANISOU 165 CA TYR B 59 1634 2017 2231 622 517 535 C ATOM 166 CA ASP B 60 1.731 37.530 22.961 1.00 19.83 C ANISOU 166 CA ASP B 60 2552 2332 2648 238 529 337 C ATOM 167 CA GLN B 61 0.439 35.145 25.614 1.00 19.30 C ANISOU 167 CA GLN B 61 2504 2451 2375 430 784 418 C ATOM 168 CA ILE B 62 -0.064 32.232 23.229 1.00 14.75 C ANISOU 168 CA ILE B 62 1560 1903 2141 311 270 539 C ATOM 169 CA PRO B 63 -0.478 28.785 24.834 1.00 15.81 C ANISOU 169 CA PRO B 63 1830 2048 2128 266 179 641 C ATOM 170 CA VAL B 64 2.082 26.260 23.472 1.00 20.00 C ANISOU 170 CA VAL B 64 2943 1840 2815 427 482 684 C ATOM 171 CA AGLU B 65 2.536 22.729 24.809 0.50 19.38 C ANISOU 171 CA AGLU B 65 2293 2306 2762 555 804 562 C ATOM 172 CA BGLU B 65 2.279 22.520 24.628 0.50 18.85 C ANISOU 172 CA BGLU B 65 2211 1999 2952 436 704 597 C ATOM 173 CA ILE B 66 5.835 21.110 24.258 1.00 18.93 C ANISOU 173 CA ILE B 66 2336 2447 2406 640 877 476 C ATOM 174 CA CYS B 67 6.182 17.375 24.873 1.00 24.28 C ANISOU 174 CA CYS B 67 3267 2554 3403 799 405 313 C ATOM 175 CA GLY B 68 3.290 17.572 27.238 1.00 27.05 C ANISOU 175 CA GLY B 68 3637 3121 3517 -175 659 604 C ATOM 176 CA HIS B 69 4.559 20.500 29.180 1.00 21.59 C ANISOU 176 CA HIS B 69 3153 2228 2823 631 653 734 C ATOM 177 CA LYS B 70 2.416 23.604 29.142 1.00 17.00 C ANISOU 177 CA LYS B 70 2124 2080 2253 448 730 424 C ATOM 178 CA ALA B 71 3.816 26.993 28.324 1.00 17.47 C ANISOU 178 CA ALA B 71 1820 2147 2670 477 427 558 C ATOM 179 CA ILE B 72 2.384 30.403 27.471 1.00 14.64 C ANISOU 179 CA ILE B 72 1661 1733 2167 410 516 341 C ATOM 180 CA GLY B 73 4.132 33.324 25.987 1.00 15.71 C ANISOU 180 CA GLY B 73 1714 1946 2308 540 443 265 C ATOM 181 CA THR B 74 5.407 35.125 22.969 1.00 15.05 C ANISOU 181 CA THR B 74 1914 1773 2030 335 324 387 C ATOM 182 CA VAL B 75 5.382 33.457 19.636 1.00 13.36 C ANISOU 182 CA VAL B 75 1530 1596 1950 315 6 532 C ATOM 183 CA LEU B 76 6.872 35.022 16.525 1.00 11.76 C ANISOU 183 CA LEU B 76 1270 1314 1884 314 -55 269 C ATOM 184 CA VAL B 77 5.465 33.952 13.192 1.00 11.32 C ANISOU 184 CA VAL B 77 1211 1438 1652 108 -110 165 C ATOM 185 CA GLY B 78 7.126 34.368 9.834 1.00 12.40 C ANISOU 185 CA GLY B 78 1401 1653 1655 7 -121 232 C ATOM 186 CA PRO B 79 9.089 32.809 7.052 1.00 12.58 C ANISOU 186 CA PRO B 79 1713 1617 1449 187 -251 150 C ATOM 187 CA THR B 80 11.514 30.801 9.145 1.00 12.42 C ANISOU 187 CA THR B 80 1455 1854 1410 109 -41 246 C ATOM 188 CA PRO B 81 12.663 27.593 7.545 1.00 16.83 C ANISOU 188 CA PRO B 81 2549 2327 1516 624 -283 13 C ATOM 189 CA AVAL B 82 12.115 25.636 10.800 0.50 15.75 C ANISOU 189 CA AVAL B 82 2267 2012 1703 438 -396 23 C ATOM 190 CA BVAL B 82 12.203 25.650 10.810 0.50 15.48 C ANISOU 190 CA BVAL B 82 2321 1891 1669 405 -477 49 C ATOM 191 CA ASN B 83 9.913 25.948 13.859 1.00 13.03 C ANISOU 191 CA ASN B 83 1851 1439 1659 116 -438 -29 C ATOM 192 CA ILE B 84 12.066 27.097 16.740 1.00 10.30 C ANISOU 192 CA ILE B 84 1441 1185 1286 132 -238 35 C ATOM 193 CA ILE B 85 11.297 26.930 20.476 1.00 10.72 C ANISOU 193 CA ILE B 85 1419 1255 1398 246 186 73 C ATOM 194 CA GLY B 86 13.383 29.610 22.055 1.00 9.99 C ANISOU 194 CA GLY B 86 1661 1230 901 271 169 92 C ATOM 195 CA ARG B 87 14.458 30.370 25.564 1.00 10.61 C ANISOU 195 CA ARG B 87 1486 1670 872 412 78 -27 C ATOM 196 CA ASN B 88 11.272 32.266 26.405 1.00 12.83 C ANISOU 196 CA ASN B 88 1802 1709 1362 426 377 -222 C ATOM 197 CA LEU B 89 9.413 28.958 26.411 1.00 13.92 C ANISOU 197 CA LEU B 89 1803 2000 1484 535 568 385 C ATOM 198 CA LEU B 90 12.274 26.603 27.228 1.00 12.48 C ANISOU 198 CA LEU B 90 1770 1769 1200 355 328 375 C ATOM 199 CA THR B 91 12.514 28.086 30.712 1.00 16.50 C ANISOU 199 CA THR B 91 2097 3000 1169 869 320 220 C ATOM 200 CA GLN B 92 8.791 27.545 31.232 1.00 18.14 C ANISOU 200 CA GLN B 92 2286 2876 1729 894 674 310 C ATOM 201 CA ILE B 93 9.050 23.771 30.601 1.00 20.74 C ANISOU 201 CA ILE B 93 2331 2779 2770 675 841 740 C ATOM 202 CA GLY B 94 12.074 23.324 32.808 1.00 21.76 C ANISOU 202 CA GLY B 94 2784 3149 2335 1338 723 983 C ATOM 203 CA CYS B 95 14.751 22.865 30.121 1.00 17.40 C ANISOU 203 CA CYS B 95 2586 2300 1725 914 679 421 C ATOM 204 CA THR B 96 18.489 23.082 30.938 1.00 16.44 C ANISOU 204 CA THR B 96 2701 2136 1407 669 157 266 C ATOM 205 CA LEU B 97 21.738 22.344 29.161 1.00 13.67 C ANISOU 205 CA LEU B 97 2119 1810 1264 401 163 44 C ATOM 206 CA ASN B 98 23.929 19.848 30.932 1.00 16.84 C ANISOU 206 CA ASN B 98 2654 2145 1598 619 143 359 C ATOM 207 CA PHE B 99 27.477 18.594 30.495 1.00 19.26 C ANISOU 207 CA PHE B 99 2428 2636 2254 497 51 213 C TER END If you find results from this site helpful for your research, please cite one of our papers:
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