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*** ***elNémo ID: 24041412150577045Job options:ID = 24041412150577045 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 HETATM 1540 ZN ZN A 401 8.654 0.295 16.522 1.00 15.70 ZN CONECT 642 1540 CONECT 667 1540 CONECT 1144 1540 CONECT 1170 1540 CONECT 1540 642 667 1144 1170 END If you find results from this site helpful for your research, please cite one of our papers:
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