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*** ***elNémo ID: 2404110227203529905Job options:ID = 2404110227203529905 JOBID = USERID = unknown PRIVAT = 0 NMODES = 10 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = -1 CUTOFF = 10 CAONLY = 0 Input data for this run:ATOM 1 CA SER A 96 12.232 -17.060 32.737 1.00 29.62 C ANISOU 1 CA SER A 96 3702 2999 4553 1218 -36 918 C ATOM 2 CA VAL A 97 8.881 -15.263 32.797 1.00 22.33 C ANISOU 2 CA VAL A 97 3026 2232 3225 59 619 22 C ATOM 3 CA PRO A 98 7.876 -12.600 35.357 1.00 21.08 C ANISOU 3 CA PRO A 98 2584 2655 2769 57 645 -444 C ATOM 4 CA SER A 99 4.789 -13.355 37.474 1.00 21.93 C ANISOU 4 CA SER A 99 2885 2693 2757 -3 857 13 C ATOM 5 CA GLN A 100 1.595 -11.608 36.364 1.00 24.12 C ANISOU 5 CA GLN A 100 3170 3111 2882 -177 607 151 C ATOM 6 CA LYS A 101 -0.450 -12.612 39.404 1.00 20.53 C ANISOU 6 CA LYS A 101 2725 2634 2442 -318 530 -115 C ATOM 7 CA THR A 102 -2.532 -9.758 40.816 1.00 17.74 C ANISOU 7 CA THR A 102 2072 2550 2118 -188 -95 238 C ATOM 8 CA TYR A 103 -1.535 -9.013 44.412 1.00 18.83 C ANISOU 8 CA TYR A 103 2128 3068 1957 -181 -414 543 C ATOM 9 CA GLN A 104 -3.064 -6.051 46.231 1.00 17.53 C ANISOU 9 CA GLN A 104 1608 3352 1701 15 -58 741 C ATOM 10 CA GLY A 105 -0.843 -6.696 49.244 1.00 17.65 C ANISOU 10 CA GLY A 105 2301 3021 1384 -292 135 422 C ATOM 11 CA SER A 106 -0.750 -4.950 52.604 1.00 20.02 C ANISOU 11 CA SER A 106 2608 3406 1594 -265 -304 437 C ATOM 12 CA TYR A 107 -1.438 -1.492 51.187 1.00 17.91 C ANISOU 12 CA TYR A 107 2064 3147 1596 -263 -19 310 C ATOM 13 CA GLY A 108 -4.372 -2.460 48.973 1.00 16.55 C ANISOU 13 CA GLY A 108 1866 3037 1385 309 -96 107 C ATOM 14 CA PHE A 109 -2.570 -1.670 45.730 1.00 15.40 C ANISOU 14 CA PHE A 109 1682 2925 1246 50 20 508 C ATOM 15 CA ARG A 110 -4.894 -1.182 42.741 1.00 16.22 C ANISOU 15 CA ARG A 110 1807 2876 1480 19 -126 398 C ATOM 16 CA LEU A 111 -4.693 0.483 39.334 1.00 12.49 C ANISOU 16 CA LEU A 111 1224 2140 1381 -369 23 90 C ATOM 17 CA GLY A 112 -7.176 3.060 38.082 1.00 12.53 C ANISOU 17 CA GLY A 112 1626 1815 1319 86 -55 221 C ATOM 18 CA PHE A 113 -7.646 4.629 34.666 1.00 12.54 C ANISOU 18 CA PHE A 113 1588 1690 1487 376 -181 19 C ATOM 19 CA LEU A 114 -9.356 7.684 33.188 1.00 13.36 C ANISOU 19 CA LEU A 114 1605 1741 1731 59 -53 -257 C ATOM 20 CA HIS A 115 -12.863 7.186 31.779 1.00 13.48 C ANISOU 20 CA HIS A 115 1551 1851 1719 -9 -271 -375 C ATOM 21 CA SER A 116 -12.091 8.744 28.419 1.00 12.97 C ANISOU 21 CA SER A 116 1338 1895 1696 51 -150 -57 C ATOM 22 CA GLY A 117 -14.608 7.106 26.092 1.00 12.60 C ANISOU 22 CA GLY A 117 1540 1757 1490 72 -174 -176 C ATOM 23 CA THR A 118 -14.071 6.081 22.450 1.00 13.67 C ANISOU 23 CA THR A 118 1507 2288 1399 -109 -115 292 C ATOM 24 CA ALA A 119 -14.526 9.262 20.384 1.00 15.44 C ANISOU 24 CA ALA A 119 1818 2634 1415 -526 -201 690 C ATOM 25 CA LYS A 120 -12.088 9.452 17.455 1.00 23.97 C ANISOU 25 CA LYS A 120 3451 3938 1720 -829 -621 589 C ATOM 26 CA SER A 121 -10.139 12.307 19.057 1.00 26.96 C ANISOU 26 CA SER A 121 3676 3685 2881 -354 -205 329 C ATOM 27 CA VAL A 122 -9.058 10.356 22.180 1.00 21.88 C ANISOU 27 CA VAL A 122 2231 3273 2811 -126 381 391 C ATOM 28 CA THR A 123 -5.328 9.634 22.437 1.00 23.06 C ANISOU 28 CA THR A 123 2341 3498 2922 -279 473 750 C ATOM 29 CA CYS A 124 -5.688 7.109 25.213 1.00 19.19 C ANISOU 29 CA CYS A 124 1683 3209 2399 -354 135 -73 C ATOM 30 CA THR A 125 -8.622 4.982 26.400 1.00 13.33 C ANISOU 30 CA THR A 125 1505 1662 1898 -313 -449 -1 C ATOM 31 CA TYR A 126 -9.024 2.052 28.809 1.00 10.90 C ANISOU 31 CA TYR A 126 1590 1379 1171 -183 -615 77 C ATOM 32 CA SER A 127 -11.437 -0.878 28.463 1.00 12.14 C ANISOU 32 CA SER A 127 1922 1512 1179 13 -417 -21 C ATOM 33 CA PRO A 128 -12.750 -2.223 31.814 1.00 12.27 C ANISOU 33 CA PRO A 128 1867 1207 1587 -228 -79 171 C ATOM 34 CA ALA A 129 -14.383 -5.187 30.082 1.00 13.71 C ANISOU 34 CA ALA A 129 1607 1740 1863 -60 -84 -12 C ATOM 35 CA LEU A 130 -11.102 -6.183 28.395 1.00 13.73 C ANISOU 35 CA LEU A 130 1811 1576 1831 -147 -18 166 C ATOM 36 CA ASN A 131 -8.746 -4.831 31.092 1.00 12.81 C ANISOU 36 CA ASN A 131 1551 1914 1401 59 25 208 C ATOM 37 CA LYS A 132 -7.031 -3.266 28.131 1.00 12.37 C ANISOU 37 CA LYS A 132 1805 1513 1383 111 4 -189 C ATOM 38 CA AMET A 133 -5.407 0.061 27.468 0.76 12.69 C ANISOU 38 CA AMET A 133 1656 1954 1212 474 -11 -419 C ATOM 39 CA BMET A 133 -5.381 0.053 27.470 0.24 13.04 C ANISOU 39 CA BMET A 133 1858 1830 1267 586 -24 -342 C ATOM 40 CA PHE A 134 -5.559 1.526 23.953 1.00 11.21 C ANISOU 40 CA PHE A 134 1152 1893 1213 242 -2 129 C ATOM 41 CA CYS A 135 -3.038 4.301 23.398 1.00 17.26 C ANISOU 41 CA CYS A 135 1799 2817 1943 1 464 480 C ATOM 42 CA GLN A 136 -1.046 6.147 20.757 1.00 19.02 C ANISOU 42 CA GLN A 136 2216 2932 2080 -305 428 676 C ATOM 43 CA LEU A 137 2.699 6.022 20.064 1.00 19.79 C ANISOU 43 CA LEU A 137 2240 3245 2035 28 140 -90 C ATOM 44 CA ALA A 138 4.698 8.343 22.358 1.00 19.52 C ANISOU 44 CA ALA A 138 2578 3098 1742 -85 -198 16 C ATOM 45 CA LYS A 139 1.515 10.020 23.681 1.00 19.05 C ANISOU 45 CA LYS A 139 2635 2891 1713 -118 -160 672 C ATOM 46 CA THR A 140 0.639 10.468 27.362 1.00 16.74 C ANISOU 46 CA THR A 140 2077 2216 2066 241 -300 189 C ATOM 47 CA ACYS A 141 -0.841 7.385 29.003 0.39 14.90 C ANISOU 47 CA ACYS A 141 1742 1945 1975 311 -208 -48 C ATOM 48 CA BCYS A 141 -0.830 7.380 28.989 0.61 15.53 C ANISOU 48 CA BCYS A 141 1745 2091 2066 332 -265 -147 C ATOM 49 CA PRO A 142 -2.205 8.125 32.472 1.00 14.41 C ANISOU 49 CA PRO A 142 2250 1665 1559 319 -107 -61 C ATOM 50 CA VAL A 143 -2.189 5.271 34.982 1.00 13.81 C ANISOU 50 CA VAL A 143 2041 1382 1823 -70 -139 -260 C ATOM 51 CA GLN A 144 -3.437 5.770 38.532 1.00 13.58 C ANISOU 51 CA GLN A 144 1662 1397 2099 464 89 -285 C ATOM 52 CA LEU A 145 -1.950 4.078 41.577 1.00 13.90 C ANISOU 52 CA LEU A 145 1191 2249 1841 128 71 -591 C ATOM 53 CA TRP A 146 -4.569 3.540 44.313 1.00 15.45 C ANISOU 53 CA TRP A 146 1944 2433 1494 425 495 357 C ATOM 54 CA VAL A 147 -3.747 2.333 47.832 1.00 18.71 C ANISOU 54 CA VAL A 147 2491 3038 1580 530 206 386 C ATOM 55 CA ASP A 148 -5.829 1.799 50.978 1.00 22.43 C ANISOU 55 CA ASP A 148 2866 3692 1963 305 531 -64 C ATOM 56 CA SER A 149 -2.825 2.700 53.148 1.00 24.52 C ANISOU 56 CA SER A 149 3027 3995 2295 316 375 230 C ATOM 57 CA THR A 150 0.270 4.808 52.378 1.00 25.42 C ANISOU 57 CA THR A 150 2713 4087 2861 -202 242 -501 C ATOM 58 CA PRO A 151 3.375 2.632 51.674 1.00 24.46 C ANISOU 58 CA PRO A 151 2435 4482 2376 -578 258 -654 C ATOM 59 CA PRO A 152 6.740 3.213 53.464 1.00 26.65 C ANISOU 59 CA PRO A 152 2839 4929 2356 -1317 -698 -262 C ATOM 60 CA PRO A 153 9.246 5.982 52.648 1.00 28.30 C ANISOU 60 CA PRO A 153 3491 4959 2301 -1496 -139 -666 C ATOM 61 CA GLY A 154 11.402 4.828 49.742 1.00 19.85 C ANISOU 61 CA GLY A 154 2040 3801 1701 -932 -247 -326 C ATOM 62 CA THR A 155 8.702 2.710 48.101 1.00 15.73 C ANISOU 62 CA THR A 155 1518 3123 1335 17 -344 302 C ATOM 63 CA ARG A 156 9.069 2.447 44.304 1.00 13.98 C ANISOU 63 CA ARG A 156 1488 2609 1217 50 -361 -172 C ATOM 64 CA PHE A 157 6.804 1.273 41.484 1.00 11.74 C ANISOU 64 CA PHE A 157 1578 1946 936 376 18 -260 C ATOM 65 CA ARG A 158 8.039 -0.534 38.383 1.00 10.91 C ANISOU 65 CA ARG A 158 1350 1666 1128 453 -178 57 C ATOM 66 CA ALA A 159 6.529 -1.137 34.922 1.00 9.76 C ANISOU 66 CA ALA A 159 1134 1369 1207 140 -157 -15 C ATOM 67 CA MET A 160 7.544 -4.028 32.675 1.00 12.83 C ANISOU 67 CA MET A 160 1409 1658 1807 204 -161 -290 C ATOM 68 CA ALA A 161 6.046 -5.383 29.453 1.00 13.05 C ANISOU 68 CA ALA A 161 1744 1520 1696 392 -176 -376 C ATOM 69 CA ILE A 162 5.664 -9.066 28.568 1.00 13.28 C ANISOU 69 CA ILE A 162 1683 1754 1608 -13 93 -310 C ATOM 70 CA TYR A 163 4.024 -10.830 25.629 1.00 15.74 C ANISOU 70 CA TYR A 163 1753 2318 1910 -210 -273 -333 C ATOM 71 CA LYS A 164 0.473 -11.896 26.455 1.00 19.87 C ANISOU 71 CA LYS A 164 2220 2952 2376 -194 -269 117 C ATOM 72 CA GLN A 165 0.603 -15.150 24.472 1.00 23.57 C ANISOU 72 CA GLN A 165 2910 2929 3117 -253 -475 -74 C ATOM 73 CA SER A 166 2.307 -18.057 26.232 1.00 27.08 C ANISOU 73 CA SER A 166 3897 3001 3391 -95 -889 -335 C ATOM 74 CA GLN A 167 4.193 -19.065 23.072 1.00 28.86 C ANISOU 74 CA GLN A 167 4014 3010 3942 153 -499 -721 C ATOM 75 CA HIS A 168 5.913 -15.650 23.112 1.00 23.66 C ANISOU 75 CA HIS A 168 2813 2879 3299 71 -171 -1284 C ATOM 76 CA MET A 169 6.236 -15.019 26.868 1.00 24.06 C ANISOU 76 CA MET A 169 2923 2939 3280 50 -166 -819 C ATOM 77 CA THR A 170 9.959 -15.859 27.105 1.00 21.46 C ANISOU 77 CA THR A 170 2354 2655 3146 532 -261 -1091 C ATOM 78 CA GLU A 171 10.796 -13.305 24.422 1.00 21.17 C ANISOU 78 CA GLU A 171 2255 3003 2787 293 43 -823 C ATOM 79 CA VAL A 172 11.909 -9.945 25.798 1.00 17.79 C ANISOU 79 CA VAL A 172 1812 2851 2094 139 -14 -371 C ATOM 80 CA VAL A 173 9.633 -7.086 24.740 1.00 15.07 C ANISOU 80 CA VAL A 173 1443 2624 1660 344 -28 -8 C ATOM 81 CA ARG A 174 11.790 -4.411 23.113 1.00 19.48 C ANISOU 81 CA ARG A 174 1630 3637 2135 395 -9 31 C ATOM 82 CA ARG A 175 11.494 -1.683 20.489 1.00 18.81 C ANISOU 82 CA ARG A 175 1907 3773 1468 36 57 -31 C ATOM 83 CA CYS A 176 11.866 -2.566 16.808 1.00 20.36 C ANISOU 83 CA CYS A 176 2019 4309 1410 628 178 172 C ATOM 84 CA PRO A 177 15.235 -1.668 15.216 1.00 22.48 C ANISOU 84 CA PRO A 177 2005 4790 1745 777 354 377 C ATOM 85 CA HIS A 178 13.605 1.307 13.444 1.00 18.98 C ANISOU 85 CA HIS A 178 1423 4425 1363 477 -41 -103 C ATOM 86 CA HIS A 179 12.346 2.915 16.640 1.00 18.99 C ANISOU 86 CA HIS A 179 1467 4559 1189 32 -38 148 C ATOM 87 CA GLU A 180 15.459 1.938 18.575 1.00 25.11 C ANISOU 87 CA GLU A 180 1779 5828 1933 -178 271 59 C ATOM 88 CA ARG A 181 17.402 3.983 16.013 1.00 34.91 C ANISOU 88 CA ARG A 181 3304 6767 3194 -834 -151 58 C ATOM 89 CA CYS A 182 14.841 6.800 15.892 1.00 35.22 C ANISOU 89 CA CYS A 182 3838 6313 3232 -1242 -893 599 C ATOM 90 CA SER A 183 15.964 10.206 17.168 1.00 36.41 C ANISOU 90 CA SER A 183 4266 5698 3870 -1348 265 854 C ATOM 91 CA ASP A 184 13.174 10.314 19.754 1.00 29.49 C ANISOU 91 CA ASP A 184 3518 4554 3132 -1321 184 1082 C ATOM 92 CA SER A 185 15.337 10.161 22.877 1.00 28.63 C ANISOU 92 CA SER A 185 3412 4159 3308 -649 128 1103 C ATOM 93 CA ASP A 186 14.324 12.070 26.003 1.00 25.25 C ANISOU 93 CA ASP A 186 3076 3395 3124 -697 -163 669 C ATOM 94 CA GLY A 187 17.878 11.819 27.303 1.00 22.65 C ANISOU 94 CA GLY A 187 2554 3125 2926 -572 -322 394 C ATOM 95 CA LEU A 188 16.845 9.423 30.069 1.00 19.54 C ANISOU 95 CA LEU A 188 2002 2919 2502 -603 -568 169 C ATOM 96 CA ALA A 189 15.290 6.307 28.539 1.00 16.66 C ANISOU 96 CA ALA A 189 1544 3042 1744 -14 -366 231 C ATOM 97 CA PRO A 190 17.491 3.666 26.850 1.00 16.37 C ANISOU 97 CA PRO A 190 1430 3218 1570 -304 -256 272 C ATOM 98 CA PRO A 191 16.739 3.430 23.116 1.00 18.36 C ANISOU 98 CA PRO A 191 1629 3985 1361 -390 245 139 C ATOM 99 CA GLN A 192 15.678 -0.253 23.335 1.00 17.30 C ANISOU 99 CA GLN A 192 1722 3390 1461 259 353 296 C ATOM 100 CA HIS A 193 13.032 0.362 26.008 1.00 11.51 C ANISOU 100 CA HIS A 193 1018 2382 975 133 -257 100 C ATOM 101 CA LEU A 194 9.360 0.188 25.021 1.00 12.11 C ANISOU 101 CA LEU A 194 1225 2023 1353 166 -237 119 C ATOM 102 CA ILE A 195 7.968 1.873 28.144 1.00 12.96 C ANISOU 102 CA ILE A 195 1334 1840 1749 168 -47 142 C ATOM 103 CA ARG A 196 9.038 5.378 29.238 1.00 13.09 C ANISOU 103 CA ARG A 196 1265 1705 2004 -270 -138 309 C ATOM 104 CA VAL A 197 7.908 7.631 32.051 1.00 14.38 C ANISOU 104 CA VAL A 197 2122 1391 1952 -223 -153 -78 C ATOM 105 CA GLU A 198 6.983 11.180 31.133 1.00 19.66 C ANISOU 105 CA GLU A 198 3100 1638 2733 -224 -338 283 C ATOM 106 CA GLY A 199 7.561 14.251 33.324 1.00 19.65 C ANISOU 106 CA GLY A 199 3118 1557 2792 -9 -406 654 C ATOM 107 CA ASN A 200 9.582 12.707 36.161 1.00 17.87 C ANISOU 107 CA ASN A 200 2364 1827 2598 308 -357 89 C ATOM 108 CA LEU A 201 13.320 13.359 36.460 1.00 21.94 C ANISOU 108 CA LEU A 201 2877 2125 3336 -102 -423 -75 C ATOM 109 CA ARG A 202 13.735 10.687 39.156 1.00 17.53 C ANISOU 109 CA ARG A 202 2056 2100 2506 -27 5 -130 C ATOM 110 CA VAL A 203 12.832 7.961 36.676 1.00 11.38 C ANISOU 110 CA VAL A 203 1361 1327 1635 -355 -312 -137 C ATOM 111 CA GLU A 204 15.191 4.961 36.603 1.00 11.12 C ANISOU 111 CA GLU A 204 1696 1078 1450 -140 -467 405 C ATOM 112 CA TYR A 205 15.595 2.341 33.866 1.00 11.83 C ANISOU 112 CA TYR A 205 1511 1554 1429 149 -422 397 C ATOM 113 CA LEU A 206 16.862 -1.228 34.206 1.00 11.45 C ANISOU 113 CA LEU A 206 1215 1400 1737 -186 -391 315 C ATOM 114 CA ASP A 207 18.222 -3.866 31.857 1.00 13.58 C ANISOU 114 CA ASP A 207 1326 1849 1986 111 -543 255 C ATOM 115 CA ASP A 208 18.093 -6.986 34.020 1.00 17.36 C ANISOU 115 CA ASP A 208 1771 1538 3286 464 -553 -110 C ATOM 116 CA ARG A 209 21.554 -8.547 33.880 1.00 25.72 C ANISOU 116 CA ARG A 209 2629 2703 4440 412 -842 -320 C ATOM 117 CA ASN A 210 20.093 -12.055 34.298 1.00 25.34 C ANISOU 117 CA ASN A 210 2502 2601 4525 702 -1040 -954 C ATOM 118 CA THR A 211 16.714 -12.062 32.534 1.00 22.10 C ANISOU 118 CA THR A 211 2189 2189 4019 -10 -557 -910 C ATOM 119 CA PHE A 212 17.553 -9.217 30.112 1.00 19.49 C ANISOU 119 CA PHE A 212 2125 2149 3133 186 148 -633 C ATOM 120 CA ARG A 213 14.080 -7.775 30.748 1.00 17.37 C ANISOU 120 CA ARG A 213 1974 2079 2548 48 -88 -436 C ATOM 121 CA HIS A 214 13.592 -4.017 30.490 1.00 12.57 C ANISOU 121 CA HIS A 214 1590 1574 1611 -98 252 -185 C ATOM 122 CA SER A 215 11.757 -2.066 33.178 1.00 10.26 C ANISOU 122 CA SER A 215 1069 1579 1250 -15 -136 156 C ATOM 123 CA VAL A 216 11.223 1.476 34.359 1.00 10.65 C ANISOU 123 CA VAL A 216 1301 1818 926 157 -158 -149 C ATOM 124 CA VAL A 217 11.018 2.363 38.043 1.00 13.08 C ANISOU 124 CA VAL A 217 1687 2093 1189 427 -334 3 C ATOM 125 CA VAL A 218 9.895 5.530 39.843 1.00 13.83 C ANISOU 125 CA VAL A 218 1745 2199 1311 309 -279 219 C ATOM 126 CA PRO A 219 9.839 6.716 43.505 1.00 16.27 C ANISOU 126 CA PRO A 219 1784 2652 1744 -130 -413 -385 C ATOM 127 CA TYR A 220 6.299 6.422 44.910 1.00 17.77 C ANISOU 127 CA TYR A 220 2105 3034 1613 154 300 -397 C ATOM 128 CA GLU A 221 4.821 9.695 46.104 1.00 25.83 C ANISOU 128 CA GLU A 221 3323 3825 2665 385 145 -1149 C ATOM 129 CA PRO A 222 1.549 9.685 48.065 1.00 27.48 C ANISOU 129 CA PRO A 222 3473 3773 3197 803 87 -997 C ATOM 130 CA PRO A 223 -1.312 11.773 46.638 1.00 29.54 C ANISOU 130 CA PRO A 223 3505 3920 3800 1190 362 -1322 C ATOM 131 CA GLU A 224 -1.899 15.372 47.709 1.00 36.55 C ANISOU 131 CA GLU A 224 4374 4584 4929 1355 535 -1038 C ATOM 132 CA VAL A 225 -4.011 15.286 50.880 1.00 38.49 C ANISOU 132 CA VAL A 225 4590 4853 5183 1702 452 -1350 C ATOM 133 CA GLY A 226 -7.057 16.353 48.870 1.00 38.33 C ANISOU 133 CA GLY A 226 4433 4702 5427 2162 660 -1492 C ATOM 134 CA SER A 227 -6.385 13.678 46.225 1.00 37.48 C ANISOU 134 CA SER A 227 4189 4608 5442 1521 854 -1036 C ATOM 135 CA ASP A 228 -7.357 10.004 45.933 1.00 33.28 C ANISOU 135 CA ASP A 228 3487 4365 4792 969 1192 -829 C ATOM 136 CA CYS A 229 -4.490 8.577 43.890 1.00 23.48 C ANISOU 136 CA CYS A 229 2329 3512 3082 158 288 -545 C ATOM 137 CA THR A 230 -1.120 9.117 42.269 1.00 19.65 C ANISOU 137 CA THR A 230 2039 3327 2100 -430 61 -551 C ATOM 138 CA THR A 231 -1.052 9.558 38.497 1.00 18.67 C ANISOU 138 CA THR A 231 1837 2722 2533 -432 23 -661 C ATOM 139 CA ILE A 232 1.937 8.412 36.460 1.00 18.94 C ANISOU 139 CA ILE A 232 1972 2779 2444 -340 -371 -346 C ATOM 140 CA HIS A 233 2.326 9.268 32.770 1.00 14.21 C ANISOU 140 CA HIS A 233 1638 1729 2033 -102 -259 -63 C ATOM 141 CA TYR A 234 3.686 6.431 30.659 1.00 11.19 C ANISOU 141 CA TYR A 234 1274 1715 1265 -32 -409 319 C ATOM 142 CA ASN A 235 4.723 6.602 26.996 1.00 13.62 C ANISOU 142 CA ASN A 235 1510 2236 1428 -251 -706 108 C ATOM 143 CA TYR A 236 4.785 3.509 24.787 1.00 11.89 C ANISOU 143 CA TYR A 236 1238 1993 1287 -267 110 652 C ATOM 144 CA MET A 237 7.489 4.008 22.180 1.00 14.32 C ANISOU 144 CA MET A 237 1353 2628 1461 -409 100 210 C ATOM 145 CA CYS A 238 6.488 1.399 19.570 1.00 16.87 C ANISOU 145 CA CYS A 238 1719 3308 1384 -175 -89 -184 C ATOM 146 CA ASN A 239 3.189 0.588 17.858 1.00 17.32 C ANISOU 146 CA ASN A 239 2022 3388 1169 -218 433 101 C ATOM 147 CA SER A 240 1.639 -2.859 18.312 1.00 17.03 C ANISOU 147 CA SER A 240 1904 3401 1163 -335 356 -72 C ATOM 148 CA SER A 241 1.943 -3.153 14.527 1.00 21.75 C ANISOU 148 CA SER A 241 2491 4314 1458 -184 165 -199 C ATOM 149 CA CYS A 242 5.695 -2.423 14.365 1.00 22.44 C ANISOU 149 CA CYS A 242 2220 4686 1619 166 350 24 C ATOM 150 CA MET A 243 7.492 -4.770 11.962 1.00 23.26 C ANISOU 150 CA MET A 243 2687 4630 1522 478 312 193 C ATOM 151 CA GLY A 244 10.476 -6.317 13.734 1.00 23.64 C ANISOU 151 CA GLY A 244 3148 4055 1779 711 434 -449 C ATOM 152 CA GLY A 245 9.211 -5.312 17.161 1.00 24.72 C ANISOU 152 CA GLY A 245 3192 4032 2167 -29 885 -570 C ATOM 153 CA MET A 246 5.987 -6.429 18.817 1.00 22.10 C ANISOU 153 CA MET A 246 2919 3838 1640 -14 537 -1064 C ATOM 154 CA ASN A 247 5.071 -7.500 15.285 1.00 27.16 C ANISOU 154 CA ASN A 247 4383 4134 1802 -171 -137 -1287 C ATOM 155 CA ARG A 248 1.290 -7.418 15.893 1.00 27.29 C ANISOU 155 CA ARG A 248 4294 4064 2012 -49 -330 -1069 C ATOM 156 CA ARG A 249 1.652 -9.433 19.137 1.00 22.90 C ANISOU 156 CA ARG A 249 3360 3510 1830 244 -434 -998 C ATOM 157 CA PRO A 250 -0.428 -8.338 22.173 1.00 19.54 C ANISOU 157 CA PRO A 250 2309 3058 2056 -321 -220 -805 C ATOM 158 CA ILE A 251 1.480 -7.357 25.331 1.00 15.43 C ANISOU 158 CA ILE A 251 1852 2179 1833 67 -99 -672 C ATOM 159 CA LEU A 252 0.714 -6.864 29.025 1.00 15.46 C ANISOU 159 CA LEU A 252 1871 2078 1924 89 -197 -372 C ATOM 160 CA THR A 253 2.176 -4.176 31.239 1.00 12.81 C ANISOU 160 CA THR A 253 1631 1934 1304 458 -143 -116 C ATOM 161 CA ILE A 254 2.918 -5.409 34.768 1.00 11.70 C ANISOU 161 CA ILE A 254 1509 1705 1232 66 -18 -58 C ATOM 162 CA ILE A 255 3.085 -2.763 37.512 1.00 10.92 C ANISOU 162 CA ILE A 255 1575 1608 967 -317 17 200 C ATOM 163 CA THR A 256 4.821 -3.885 40.704 1.00 13.80 C ANISOU 163 CA THR A 256 1999 1829 1416 -464 204 174 C ATOM 164 CA LEU A 257 4.956 -1.964 43.963 1.00 14.17 C ANISOU 164 CA LEU A 257 1809 2261 1313 332 -240 29 C ATOM 165 CA GLU A 258 8.238 -2.601 45.767 1.00 16.41 C ANISOU 165 CA GLU A 258 1637 3081 1518 146 58 171 C ATOM 166 CA ASP A 259 10.028 -1.444 48.912 1.00 17.83 C ANISOU 166 CA ASP A 259 1879 3298 1596 -185 -124 378 C ATOM 167 CA SER A 260 13.360 0.410 48.999 1.00 20.52 C ANISOU 167 CA SER A 260 2063 3558 2174 335 -234 220 C ATOM 168 CA SER A 261 15.138 -2.979 48.913 1.00 20.86 C ANISOU 168 CA SER A 261 1914 3532 2478 479 3 273 C ATOM 169 CA GLY A 262 13.115 -4.176 45.929 1.00 19.87 C ANISOU 169 CA GLY A 262 1839 3283 2427 244 243 390 C ATOM 170 CA ASN A 263 10.887 -6.533 47.923 1.00 20.11 C ANISOU 170 CA ASN A 263 1971 3139 2532 448 -413 679 C ATOM 171 CA LEU A 264 7.451 -7.148 46.360 1.00 18.35 C ANISOU 171 CA LEU A 264 2352 2340 2281 142 -318 306 C ATOM 172 CA LEU A 265 4.608 -5.169 47.985 1.00 13.63 C ANISOU 172 CA LEU A 265 1854 1680 1644 -247 -143 552 C ATOM 173 CA GLY A 266 1.930 -5.386 45.285 1.00 12.20 C ANISOU 173 CA GLY A 266 1557 1619 1458 -151 -180 759 C ATOM 174 CA ARG A 267 1.282 -6.279 41.638 1.00 12.59 C ANISOU 174 CA ARG A 267 1558 1802 1423 -150 -462 696 C ATOM 175 CA ASN A 268 -1.282 -5.412 38.972 1.00 14.68 C ANISOU 175 CA ASN A 268 2060 2392 1125 -504 -212 333 C ATOM 176 CA SER A 269 -1.397 -5.700 35.200 1.00 12.63 C ANISOU 176 CA SER A 269 1760 1828 1213 54 -517 78 C ATOM 177 CA PHE A 270 -3.283 -4.616 32.083 1.00 9.97 C ANISOU 177 CA PHE A 270 1501 1228 1057 -71 177 -202 C ATOM 178 CA GLU A 271 -3.131 -5.494 28.397 1.00 12.90 C ANISOU 178 CA GLU A 271 1865 1757 1280 59 -380 -292 C ATOM 179 CA VAL A 272 -1.923 -2.787 25.997 1.00 14.48 C ANISOU 179 CA VAL A 272 2099 1985 1420 -162 -132 -199 C ATOM 180 CA ARG A 273 -2.477 -2.056 22.328 1.00 13.60 C ANISOU 180 CA ARG A 273 1674 2145 1349 360 74 -267 C ATOM 181 CA VAL A 274 -0.481 0.853 20.930 1.00 13.86 C ANISOU 181 CA VAL A 274 1448 2785 1033 223 1 -66 C ATOM 182 CA CYS A 275 -2.357 2.077 17.843 1.00 17.77 C ANISOU 182 CA CYS A 275 1773 3488 1491 85 -182 -121 C ATOM 183 CA ALA A 276 -3.265 5.044 15.651 1.00 19.67 C ANISOU 183 CA ALA A 276 2131 3890 1452 487 337 212 C ATOM 184 CA ACYS A 277 -6.962 5.124 16.630 0.58 20.37 C ANISOU 184 CA ACYS A 277 1791 4097 1851 -129 -390 506 C ATOM 185 CA BCYS A 277 -6.951 5.145 16.648 0.42 19.97 C ANISOU 185 CA BCYS A 277 1633 4012 1941 50 -350 462 C ATOM 186 CA PRO A 278 -7.443 4.004 20.270 1.00 15.16 C ANISOU 186 CA PRO A 278 1194 3046 1521 -133 -314 -60 C ATOM 187 CA GLY A 279 -11.140 4.955 20.384 1.00 16.28 C ANISOU 187 CA GLY A 279 1452 3303 1430 502 -499 -555 C ATOM 188 CA ARG A 280 -12.016 3.143 17.159 1.00 20.38 C ANISOU 188 CA ARG A 280 2552 3936 1254 216 -584 -343 C ATOM 189 CA ASP A 281 -9.980 0.074 18.060 1.00 17.06 C ANISOU 189 CA ASP A 281 2150 3306 1025 342 -293 -500 C ATOM 190 CA ARG A 282 -11.460 -0.175 21.568 1.00 12.51 C ANISOU 190 CA ARG A 282 1510 2174 1068 25 68 -628 C ATOM 191 CA ARG A 283 -15.024 0.170 20.295 1.00 16.61 C ANISOU 191 CA ARG A 283 1581 3036 1695 -84 -77 -121 C ATOM 192 CA THR A 284 -14.337 -2.474 17.637 1.00 19.92 C ANISOU 192 CA THR A 284 2193 3414 1963 -673 71 -784 C ATOM 193 CA GLU A 285 -12.741 -4.966 20.040 1.00 24.58 C ANISOU 193 CA GLU A 285 2703 3939 2699 -436 -284 -1430 C ATOM 194 CA GLU A 286 -15.633 -4.609 22.470 1.00 25.85 C ANISOU 194 CA GLU A 286 2540 4261 3020 -826 -1023 -961 C ATOM 195 CA GLU A 287 -18.087 -5.296 19.624 1.00 37.55 C ANISOU 195 CA GLU A 287 4198 5685 4384 -1123 -669 -1049 C ATOM 196 CA ASN A 288 -17.136 -8.976 20.024 1.00 43.35 C ANISOU 196 CA ASN A 288 5579 5509 5382 -1210 246 -1191 C ATOM 197 CA LEU A 289 -18.534 -9.100 23.577 1.00 38.19 C ANISOU 197 CA LEU A 289 4938 4667 4906 -1730 766 -1121 C END If you find results from this site helpful for your research, please cite one of our papers:
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