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*** ***elNémo ID: 2404140250094149148Job options:ID = 2404140250094149148 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 VAL A 97 12.653 -25.296 -26.802 1.00 26.70 C ANISOU 1 CA VAL A 97 3649 3248 3250 99 -24 -51 C ATOM 2 CA PRO A 98 11.820 -21.995 -25.035 1.00 22.99 C ANISOU 2 CA PRO A 98 3102 2815 2820 134 -19 -82 C ATOM 3 CA SER A 99 8.819 -21.967 -22.707 1.00 23.86 C ANISOU 3 CA SER A 99 3178 2976 2912 125 -4 -70 C ATOM 4 CA GLN A 100 5.531 -20.680 -24.079 1.00 19.83 C ANISOU 4 CA GLN A 100 2619 2486 2430 85 -5 -44 C ATOM 5 CA LYS A 101 3.782 -21.068 -20.715 1.00 21.10 C ANISOU 5 CA LYS A 101 2759 2702 2557 99 14 -44 C ATOM 6 CA THR A 102 1.528 -18.107 -19.914 1.00 15.36 C ANISOU 6 CA THR A 102 1952 2018 1865 114 15 -58 C ATOM 7 CA TYR A 103 2.489 -16.337 -16.702 1.00 17.76 C ANISOU 7 CA TYR A 103 2218 2358 2170 182 20 -108 C ATOM 8 CA GLN A 104 0.888 -13.057 -15.623 1.00 12.32 C ANISOU 8 CA GLN A 104 1450 1709 1523 213 18 -139 C ATOM 9 CA GLY A 105 3.203 -12.695 -12.636 1.00 10.29 C ANISOU 9 CA GLY A 105 1190 1471 1248 280 20 -193 C ATOM 10 CA SER A 106 3.500 -9.940 -10.059 1.00 17.47 C ANISOU 10 CA SER A 106 2040 2415 2181 339 15 -251 C ATOM 11 CA TYR A 107 2.618 -7.231 -12.525 1.00 17.62 C ANISOU 11 CA TYR A 107 2023 2398 2273 313 2 -247 C ATOM 12 CA GLY A 108 -0.472 -8.959 -13.928 1.00 14.29 C ANISOU 12 CA GLY A 108 1603 2002 1823 266 13 -190 C ATOM 13 CA PHE A 109 1.043 -9.120 -17.416 1.00 12.55 C ANISOU 13 CA PHE A 109 1417 1712 1639 232 2 -171 C ATOM 14 CA ARG A 110 -1.362 -9.847 -20.256 1.00 14.06 C ANISOU 14 CA ARG A 110 1613 1896 1832 169 2 -113 C ATOM 15 CA LEU A 111 -1.375 -9.077 -23.988 1.00 13.65 C ANISOU 15 CA LEU A 111 1562 1802 1823 137 -9 -87 C ATOM 16 CA GLY A 112 -3.826 -7.061 -26.027 1.00 6.12 C ANISOU 16 CA GLY A 112 558 860 909 119 -12 -64 C ATOM 17 CA PHE A 113 -4.410 -6.081 -29.624 1.00 11.91 C ANISOU 17 CA PHE A 113 1279 1568 1678 94 -20 -32 C ATOM 18 CA LEU A 114 -6.264 -3.353 -31.528 1.00 10.57 C ANISOU 18 CA LEU A 114 1050 1407 1559 97 -21 -16 C ATOM 19 CA HIS A 115 -9.847 -4.288 -32.470 1.00 12.42 C ANISOU 19 CA HIS A 115 1268 1691 1760 52 -19 24 C ATOM 20 CA SER A 116 -9.020 -3.779 -36.143 1.00 14.00 C ANISOU 20 CA SER A 116 1475 1857 1989 41 -27 52 C ATOM 21 CA GLY A 117 -11.634 -5.807 -38.000 1.00 8.69 C ANISOU 21 CA GLY A 117 810 1220 1272 -15 -30 92 C ATOM 22 CA THR A 118 -10.956 -7.706 -41.213 1.00 10.57 C ANISOU 22 CA THR A 118 1088 1437 1490 -49 -41 120 C ATOM 23 CA ALA A 119 -11.358 -5.172 -44.058 1.00 14.02 C ANISOU 23 CA ALA A 119 1481 1875 1971 -28 -44 142 C ATOM 24 CA LYS A 120 -9.202 -5.618 -47.176 1.00 18.56 C ANISOU 24 CA LYS A 120 2084 2415 2553 -24 -53 160 C ATOM 25 CA SER A 121 -7.033 -2.688 -46.170 1.00 17.44 C ANISOU 25 CA SER A 121 1916 2235 2476 31 -44 140 C ATOM 26 CA VAL A 122 -6.097 -4.036 -42.724 1.00 14.64 C ANISOU 26 CA VAL A 122 1592 1872 2098 30 -42 101 C ATOM 27 CA THR A 123 -2.362 -4.360 -42.126 1.00 16.17 C ANISOU 27 CA THR A 123 1825 2012 2305 56 -44 74 C ATOM 28 CA CYS A 124 -2.669 -6.305 -38.902 1.00 17.11 C ANISOU 28 CA CYS A 124 1973 2149 2378 45 -41 48 C ATOM 29 CA THR A 125 -5.688 -8.008 -37.343 1.00 9.05 C ANISOU 29 CA THR A 125 952 1179 1309 9 -36 58 C ATOM 30 CA TYR A 126 -6.056 -10.222 -34.298 1.00 9.21 C ANISOU 30 CA TYR A 126 1001 1218 1278 -3 -29 45 C ATOM 31 CA SER A 127 -8.461 -13.118 -33.878 1.00 9.98 C ANISOU 31 CA SER A 127 1123 1350 1321 -58 -25 72 C ATOM 32 CA PRO A 128 -9.514 -13.506 -30.211 1.00 12.46 C ANISOU 32 CA PRO A 128 1424 1702 1608 -46 -10 59 C ATOM 33 CA ALA A 129 -11.115 -16.868 -31.041 1.00 14.63 C ANISOU 33 CA ALA A 129 1739 1983 1836 -111 -9 96 C ATOM 34 CA LEU A 130 -7.898 -18.335 -32.431 1.00 20.85 C ANISOU 34 CA LEU A 130 2591 2712 2621 -107 -20 88 C ATOM 35 CA ASN A 131 -5.540 -16.258 -30.300 1.00 14.72 C ANISOU 35 CA ASN A 131 1800 1925 1867 -41 -15 48 C ATOM 36 CA LYS A 132 -3.853 -15.547 -33.569 1.00 12.29 C ANISOU 36 CA LYS A 132 1504 1575 1590 -41 -30 51 C ATOM 37 CA AMET A 133 -2.430 -12.545 -35.393 0.23 10.98 C ANISOU 37 CA AMET A 133 1303 1386 1483 -4 -38 40 C ATOM 38 CA BMET A 133 -2.549 -12.485 -35.379 0.77 11.79 C ANISOU 38 CA BMET A 133 1403 1490 1586 -5 -38 40 C ATOM 39 CA PHE A 134 -2.731 -12.087 -39.168 1.00 12.26 C ANISOU 39 CA PHE A 134 1459 1537 1665 -23 -49 69 C ATOM 40 CA CYS A 135 -0.372 -9.484 -40.582 1.00 14.56 C ANISOU 40 CA CYS A 135 1728 1793 2013 21 -51 59 C ATOM 41 CA GLN A 136 1.439 -8.253 -43.675 1.00 10.29 C ANISOU 41 CA GLN A 136 1181 1220 1507 38 -58 76 C ATOM 42 CA LEU A 137 5.189 -8.615 -44.217 1.00 14.56 C ANISOU 42 CA LEU A 137 1760 1715 2058 63 -62 62 C ATOM 43 CA ALA A 138 7.177 -5.619 -42.917 1.00 18.85 C ANISOU 43 CA ALA A 138 2264 2230 2668 113 -55 31 C ATOM 44 CA LYS A 139 4.022 -3.718 -41.972 1.00 11.01 C ANISOU 44 CA LYS A 139 1213 1272 1699 111 -47 35 C ATOM 45 CA THR A 140 3.377 -2.276 -38.506 1.00 14.79 C ANISOU 45 CA THR A 140 1658 1765 2196 137 -40 -8 C ATOM 46 CA ACYS A 141 2.017 -4.746 -35.940 0.67 10.73 C ANISOU 46 CA ACYS A 141 1175 1289 1615 115 -39 -20 C ATOM 47 CA BCYS A 141 2.036 -4.709 -35.973 0.33 11.03 C ANISOU 47 CA BCYS A 141 1212 1326 1654 115 -39 -20 C ATOM 48 CA PRO A 142 0.720 -3.170 -32.717 1.00 15.80 C ANISOU 48 CA PRO A 142 1772 1962 2270 143 -32 -56 C ATOM 49 CA VAL A 143 1.069 -5.520 -29.758 1.00 12.14 C ANISOU 49 CA VAL A 143 1346 1522 1746 143 -28 -77 C ATOM 50 CA GLN A 144 -0.243 -4.059 -26.512 1.00 12.59 C ANISOU 50 CA GLN A 144 1356 1621 1806 176 -21 -113 C ATOM 51 CA LEU A 145 1.178 -4.722 -23.053 1.00 16.54 C ANISOU 51 CA LEU A 145 1868 2140 2276 214 -18 -159 C ATOM 52 CA TRP A 146 -1.330 -4.712 -20.191 1.00 16.40 C ANISOU 52 CA TRP A 146 1818 2189 2224 226 -9 -167 C ATOM 53 CA VAL A 147 -0.254 -4.617 -16.532 1.00 15.83 C ANISOU 53 CA VAL A 147 1737 2149 2127 278 -5 -217 C ATOM 54 CA ASP A 148 -2.067 -4.409 -13.153 1.00 15.91 C ANISOU 54 CA ASP A 148 1724 2225 2096 297 4 -228 C ATOM 55 CA SER A 149 0.981 -2.576 -11.784 1.00 20.47 C ANISOU 55 CA SER A 149 2332 2754 2691 302 -8 -255 C ATOM 56 CA ATHR A 150 3.893 -0.813 -13.475 0.40 24.87 C ANISOU 56 CA ATHR A 150 2914 3244 3292 284 -18 -256 C ATOM 57 CA BTHR A 150 3.922 -0.765 -13.402 0.60 24.21 C ANISOU 57 CA BTHR A 150 2829 3160 3207 284 -18 -256 C ATOM 58 CA PRO A 151 7.145 -2.819 -13.557 1.00 23.40 C ANISOU 58 CA PRO A 151 2774 3034 3083 283 -20 -260 C ATOM 59 CA PRO A 152 10.354 -1.239 -12.081 1.00 26.55 C ANISOU 59 CA PRO A 152 3186 3416 3488 280 -30 -277 C ATOM 60 CA PRO A 153 12.727 0.955 -14.103 1.00 42.04 C ANISOU 60 CA PRO A 153 5147 5335 5492 260 -42 -279 C ATOM 61 CA GLY A 154 14.929 -1.039 -16.449 1.00 19.17 C ANISOU 61 CA GLY A 154 2287 2409 2588 245 -38 -255 C ATOM 62 CA THR A 155 12.261 -3.560 -17.402 1.00 7.22 C ANISOU 62 CA THR A 155 783 905 1056 251 -25 -236 C ATOM 63 CA ARG A 156 12.623 -5.051 -20.856 1.00 12.21 C ANISOU 63 CA ARG A 156 1698 1270 1673 44 -343 -35 C ATOM 64 CA VAL A 157 10.177 -6.739 -23.228 1.00 10.79 C ANISOU 64 CA VAL A 157 1543 1092 1464 35 -321 -24 C ATOM 65 CA ARG A 158 11.398 -9.621 -25.396 1.00 11.67 C ANISOU 65 CA ARG A 158 1685 1195 1554 42 -298 -14 C ATOM 66 CA ALA A 159 9.743 -11.235 -28.434 1.00 7.38 C ANISOU 66 CA ALA A 159 1164 652 989 35 -277 -5 C ATOM 67 CA MET A 160 10.692 -14.584 -29.958 1.00 11.40 C ANISOU 67 CA MET A 160 1706 1154 1471 45 -259 3 C ATOM 68 CA ALA A 161 9.122 -16.869 -32.553 1.00 9.60 C ANISOU 68 CA ALA A 161 1510 922 1213 40 -250 7 C ATOM 69 CA ILE A 162 8.996 -20.647 -32.225 1.00 12.02 C ANISOU 69 CA ILE A 162 1859 1226 1484 44 -247 7 C ATOM 70 CA TYR A 163 7.256 -23.236 -34.427 1.00 14.94 C ANISOU 70 CA TYR A 163 2266 1592 1818 38 -242 8 C ATOM 71 CA LYS A 164 3.831 -24.231 -33.111 1.00 18.24 C ANISOU 71 CA LYS A 164 2702 2019 2211 18 -256 4 C ATOM 72 CA GLN A 165 3.933 -27.877 -34.171 1.00 21.72 C ANISOU 72 CA GLN A 165 3187 2451 2615 22 -250 3 C ATOM 73 CA SER A 166 5.831 -30.193 -31.854 1.00 24.16 C ANISOU 73 CA SER A 166 3514 2754 2912 36 -249 1 C ATOM 74 CA GLN A 167 7.776 -31.765 -34.740 1.00 20.40 C ANISOU 74 CA GLN A 167 3058 2267 2426 51 -233 4 C ATOM 75 CA HIS A 168 9.332 -28.415 -35.672 1.00 14.23 C ANISOU 75 CA HIS A 168 2234 1488 1685 58 -227 10 C ATOM 76 CA MET A 169 9.577 -26.922 -32.219 1.00 19.26 C ANISOU 76 CA MET A 169 2261 2511 2546 472 -144 -176 C ATOM 77 CA THR A 170 13.348 -27.448 -31.990 1.00 18.00 C ANISOU 77 CA THR A 170 2086 2423 2328 515 -142 -304 C ATOM 78 CA GLU A 171 13.987 -25.855 -35.376 1.00 14.44 C ANISOU 78 CA GLU A 171 1607 2045 1834 461 -124 -325 C ATOM 79 CA VAL A 172 15.027 -22.217 -35.110 1.00 15.48 C ANISOU 79 CA VAL A 172 1704 2230 1949 423 -42 -317 C ATOM 80 CA VAL A 173 12.578 -19.802 -36.728 1.00 15.35 C ANISOU 80 CA VAL A 173 1676 2203 1953 351 -8 -218 C ATOM 81 CA AARG A 174 14.471 -17.708 -39.268 0.27 13.44 C ANISOU 81 CA AARG A 174 1400 2053 1655 309 29 -270 C ATOM 82 CA BARG A 174 14.469 -17.693 -39.251 0.73 12.71 C ANISOU 82 CA BARG A 174 1308 1960 1562 309 30 -270 C ATOM 83 CA ARG A 175 13.984 -15.822 -42.526 1.00 11.05 C ANISOU 83 CA ARG A 175 1077 1797 1326 240 50 -250 C ATOM 84 CA CYS A 176 14.081 -17.599 -45.876 1.00 13.63 C ANISOU 84 CA CYS A 176 1407 2151 1619 225 -5 -290 C ATOM 85 CA PRO A 177 17.245 -17.319 -48.022 1.00 19.45 C ANISOU 85 CA PRO A 177 2119 2988 2285 221 1 -402 C ATOM 86 CA HIS A 178 15.523 -14.891 -50.397 1.00 17.20 C ANISOU 86 CA HIS A 178 1820 2715 2000 145 33 -330 C ATOM 87 CA HIS A 179 14.472 -12.483 -47.666 1.00 20.67 C ANISOU 87 CA HIS A 179 2255 3119 2481 137 94 -254 C ATOM 88 CA GLU A 180 17.620 -12.815 -45.549 1.00 25.37 C ANISOU 88 CA GLU A 180 2840 3754 3046 192 110 -351 C ATOM 89 CA ARG A 181 19.481 -11.746 -48.697 1.00 25.18 C ANISOU 89 CA ARG A 181 2946 3533 3089 358 -48 171 C ATOM 90 CA CYS A 182 17.001 -8.952 -49.505 1.00 28.17 C ANISOU 90 CA CYS A 182 3373 3786 3544 272 -148 144 C ATOM 91 CA SER A 183 18.186 -5.347 -49.296 1.00 49.61 C ANISOU 91 CA SER A 183 6069 6520 6261 140 -238 246 C ATOM 92 CA ASP A 184 15.787 -4.389 -46.500 1.00 36.17 C ANISOU 92 CA ASP A 184 4415 4649 4678 115 -278 149 C ATOM 93 CA SER A 185 18.280 -3.804 -43.660 1.00 28.39 C ANISOU 93 CA SER A 185 3387 3726 3676 57 -266 217 C ATOM 94 CA ASP A 186 17.615 -1.054 -41.113 1.00 24.59 C ANISOU 94 CA ASP A 186 2945 3133 3265 -34 -349 204 C ATOM 95 CA GLY A 187 21.184 -1.289 -39.846 1.00 17.04 C ANISOU 95 CA GLY A 187 1919 2323 2232 -82 -319 322 C ATOM 96 CA LEU A 188 20.060 -2.703 -36.519 1.00 18.85 C ANISOU 96 CA LEU A 188 2166 2475 2522 -40 -269 222 C ATOM 97 CA ALA A 189 18.299 -5.997 -37.158 1.00 12.98 C ANISOU 97 CA ALA A 189 1427 1710 1793 85 -180 123 C ATOM 98 CA PRO A 190 20.344 -8.982 -38.305 1.00 14.85 C ANISOU 98 CA PRO A 190 1612 2084 1947 172 -89 167 C ATOM 99 CA PRO A 191 19.202 -10.076 -41.786 1.00 19.98 C ANISOU 99 CA PRO A 191 2282 2742 2569 243 -76 139 C ATOM 100 CA AGLN A 192 18.239 -13.539 -40.497 0.54 18.72 C ANISOU 100 CA AGLN A 192 2146 2542 2424 344 3 49 C ATOM 101 CA BGLN A 192 18.258 -13.542 -40.482 0.46 18.81 C ANISOU 101 CA BGLN A 192 2157 2554 2436 344 4 49 C ATOM 102 CA HIS A 193 15.800 -12.283 -37.844 1.00 11.91 C ANISOU 102 CA HIS A 193 1320 1541 1665 286 -34 -31 C ATOM 103 CA LEU A 194 12.083 -12.668 -38.540 1.00 14.30 C ANISOU 103 CA LEU A 194 1701 1730 2003 260 -38 -115 C ATOM 104 CA ILE A 195 10.881 -10.135 -35.983 1.00 11.28 C ANISOU 104 CA ILE A 195 1322 1282 1684 195 -91 -152 C ATOM 105 CA ARG A 196 11.951 -6.496 -35.875 1.00 9.87 C ANISOU 105 CA ARG A 196 1123 1069 1556 148 -191 -114 C ATOM 106 CA VAL A 197 10.730 -3.631 -33.735 1.00 13.39 C ANISOU 106 CA VAL A 197 1604 1418 2066 88 -264 -153 C ATOM 107 CA GLU A 198 9.930 -0.446 -35.625 1.00 23.35 C ANISOU 107 CA GLU A 198 2903 2629 3341 44 -369 -129 C ATOM 108 CA GLY A 199 10.239 3.093 -34.283 1.00 24.03 C ANISOU 108 CA GLY A 199 3031 2688 3411 -12 -435 -86 C ATOM 109 CA ASN A 200 12.485 2.359 -31.287 1.00 15.27 C ANISOU 109 CA ASN A 200 1906 1605 2290 -57 -409 -65 C ATOM 110 CA LEU A 201 16.132 3.430 -31.308 1.00 16.61 C ANISOU 110 CA LEU A 201 2053 1850 2410 -170 -467 71 C ATOM 111 CA ARG A 202 16.814 1.377 -28.173 1.00 14.52 C ANISOU 111 CA ARG A 202 1756 1622 2139 -147 -383 39 C ATOM 112 CA VAL A 203 15.941 -1.941 -29.825 1.00 13.47 C ANISOU 112 CA VAL A 203 1580 1538 1999 -43 -282 1 C ATOM 113 CA GLU A 204 18.322 -4.817 -29.059 1.00 9.75 C ANISOU 113 CA GLU A 204 1045 1193 1466 -8 -188 57 C ATOM 114 CA TYR A 205 18.797 -8.019 -31.053 1.00 9.83 C ANISOU 114 CA TYR A 205 1019 1284 1433 91 -103 63 C ATOM 115 CA LEU A 206 20.105 -11.320 -29.702 1.00 7.70 C ANISOU 115 CA LEU A 206 718 1083 1126 162 -12 67 C ATOM 116 CA ASP A 207 21.440 -14.471 -31.282 1.00 16.32 C ANISOU 116 CA ASP A 207 1790 2258 2151 260 61 86 C ATOM 117 CA ASP A 208 21.450 -16.854 -28.325 1.00 15.43 C ANISOU 117 CA ASP A 208 1716 2099 2046 256 98 37 C ATOM 118 CA ARG A 209 24.995 -18.148 -27.829 1.00 20.43 C ANISOU 118 CA ARG A 209 2321 2845 2595 271 124 127 C ATOM 119 CA ASN A 210 23.724 -21.639 -26.970 1.00 18.34 C ANISOU 119 CA ASN A 210 2127 2493 2349 292 142 46 C ATOM 120 CA THR A 211 20.223 -22.211 -28.412 1.00 19.49 C ANISOU 120 CA THR A 211 2316 2530 2560 271 127 -46 C ATOM 121 CA PHE A 212 20.874 -20.126 -31.540 1.00 18.38 C ANISOU 121 CA PHE A 212 2151 2448 2384 301 116 -2 C ATOM 122 CA ARG A 213 17.398 -18.602 -31.195 1.00 13.82 C ANISOU 122 CA ARG A 213 1592 1756 1903 254 96 -69 C ATOM 123 CA HIS A 214 16.697 -15.070 -32.367 1.00 12.33 C ANISOU 123 CA HIS A 214 1379 1573 1731 263 54 -48 C ATOM 124 CA SER A 215 14.895 -12.519 -30.252 1.00 7.45 C ANISOU 124 CA SER A 215 777 880 1172 206 -2 -103 C ATOM 125 CA VAL A 216 14.314 -8.768 -30.122 1.00 9.09 C ANISOU 125 CA VAL A 216 988 1029 1439 137 -95 -106 C ATOM 126 CA VAL A 217 14.039 -6.726 -26.935 1.00 10.81 C ANISOU 126 CA VAL A 217 1225 1190 1693 70 -134 -130 C ATOM 127 CA VAL A 218 13.012 -3.146 -26.139 1.00 9.58 C ANISOU 127 CA VAL A 218 1117 943 1580 5 -231 -155 C ATOM 128 CA PRO A 219 12.842 -1.103 -22.944 1.00 13.21 C ANISOU 128 CA PRO A 219 1615 1392 2014 -32 -243 -160 C ATOM 129 CA TYR A 220 9.455 -1.300 -21.320 1.00 14.75 C ANISOU 129 CA TYR A 220 1819 1606 2182 16 -182 -216 C ATOM 130 CA GLU A 221 7.931 2.154 -21.127 1.00 11.18 C ANISOU 130 CA GLU A 221 1408 1116 1725 11 -232 -224 C ATOM 131 CA PRO A 222 4.753 3.084 -19.209 1.00 19.10 C ANISOU 131 CA PRO A 222 2395 2111 2750 51 -237 -284 C ATOM 132 CA PRO A 223 1.446 3.524 -21.106 1.00 21.04 C ANISOU 132 CA PRO A 223 2604 2361 3031 94 -264 -318 C ATOM 133 CA GLU A 224 1.320 6.555 -23.402 1.00 29.68 C ANISOU 133 CA GLU A 224 3737 3402 4136 100 -349 -302 C ATOM 134 CA VAL A 225 -1.281 9.305 -23.128 1.00 32.58 C ANISOU 134 CA VAL A 225 4118 3730 4531 137 -415 -347 C ATOM 135 CA GLY A 226 -4.690 8.130 -24.313 1.00 42.88 C ANISOU 135 CA GLY A 226 5356 5070 5866 175 -407 -393 C ATOM 136 CA SER A 227 -3.999 4.455 -23.639 1.00 27.58 C ANISOU 136 CA SER A 227 3372 3193 3913 151 -318 -381 C ATOM 137 CA ASP A 228 -4.248 2.071 -20.686 1.00 23.11 C ANISOU 137 CA ASP A 228 2774 2669 3338 138 -246 -402 C ATOM 138 CA CYS A 229 -1.457 0.020 -22.233 1.00 16.16 C ANISOU 138 CA CYS A 229 1903 1805 2432 111 -214 -347 C ATOM 139 CA THR A 230 1.993 0.133 -23.794 1.00 13.32 C ANISOU 139 CA THR A 230 1639 1416 2008 -110 -86 -64 C ATOM 140 CA THR A 231 2.219 -0.521 -27.518 1.00 12.29 C ANISOU 140 CA THR A 231 1476 1286 1907 -119 -110 -42 C ATOM 141 CA ILE A 232 5.141 -2.054 -29.360 1.00 14.69 C ANISOU 141 CA ILE A 232 1762 1584 2236 -120 -138 -12 C ATOM 142 CA HIS A 233 5.248 -1.993 -33.152 1.00 14.16 C ANISOU 142 CA HIS A 233 1642 1590 2148 -108 -160 48 C ATOM 143 CA TYR A 234 6.568 -5.267 -34.499 1.00 10.70 C ANISOU 143 CA TYR A 234 1257 1217 1593 -56 -134 33 C ATOM 144 CA ASN A 235 7.328 -6.095 -38.143 1.00 10.64 C ANISOU 144 CA ASN A 235 1221 1311 1510 -14 -141 85 C ATOM 145 CA TYR A 236 7.490 -9.649 -39.464 1.00 10.46 C ANISOU 145 CA TYR A 236 1265 1335 1376 34 -116 41 C ATOM 146 CA MET A 237 9.978 -9.832 -42.311 1.00 16.32 C ANISOU 146 CA MET A 237 1968 2189 2044 87 -125 121 C ATOM 147 CA ACYS A 238 8.973 -13.102 -43.972 0.50 16.18 C ANISOU 147 CA ACYS A 238 2014 2203 1931 126 -109 65 C ATOM 148 CA BCYS A 238 8.991 -13.101 -43.973 0.50 16.20 C ANISOU 148 CA BCYS A 238 2016 2205 1933 126 -109 65 C ATOM 149 CA ASN A 239 5.680 -14.553 -45.168 1.00 14.18 C ANISOU 149 CA ASN A 239 1794 1925 1668 116 -109 -3 C ATOM 150 CA SER A 240 4.395 -17.741 -43.553 1.00 15.27 C ANISOU 150 CA SER A 240 2030 2004 1767 118 -82 -106 C ATOM 151 CA SER A 241 4.296 -19.206 -47.070 1.00 21.56 C ANISOU 151 CA SER A 241 2825 2887 2481 168 -94 -91 C ATOM 152 CA CYS A 242 7.948 -18.392 -47.790 1.00 15.07 C ANISOU 152 CA CYS A 242 1963 2147 1615 211 -95 -6 C ATOM 153 CA MET A 243 10.021 -21.087 -49.430 1.00 31.49 C ANISOU 153 CA MET A 243 4085 4308 3572 284 -84 -4 C ATOM 154 CA GLY A 244 13.208 -21.959 -47.580 1.00 25.76 C ANISOU 154 CA GLY A 244 3388 3594 2806 311 -62 10 C ATOM 155 CA GLY A 245 11.727 -20.356 -44.487 1.00 21.37 C ANISOU 155 CA GLY A 245 2831 2931 2357 241 -58 -24 C ATOM 156 CA MET A 246 8.590 -21.074 -42.486 1.00 11.33 C ANISOU 156 CA MET A 246 1609 1554 1141 190 -48 -115 C ATOM 157 CA ASN A 247 7.062 -22.852 -45.505 1.00 15.75 C ANISOU 157 CA ASN A 247 2186 2162 1638 222 -59 -137 C ATOM 158 CA ARG A 248 3.477 -22.427 -44.253 1.00 21.07 C ANISOU 158 CA ARG A 248 2872 2742 2394 161 -61 -200 C ATOM 159 CA ARG A 249 4.339 -23.880 -40.826 1.00 15.17 C ANISOU 159 CA ARG A 249 2187 1928 1650 150 -29 -252 C ATOM 160 CA PRO A 250 2.516 -21.947 -38.087 1.00 17.78 C ANISOU 160 CA PRO A 250 2507 2163 2085 87 -26 -278 C ATOM 161 CA ILE A 251 4.562 -20.089 -35.487 1.00 13.05 C ANISOU 161 CA ILE A 251 1760 1429 1768 150 29 72 C ATOM 162 CA LEU A 252 3.922 -18.550 -32.103 1.00 14.29 C ANISOU 162 CA LEU A 252 1878 1633 1918 134 26 97 C ATOM 163 CA THR A 253 5.340 -15.280 -30.889 1.00 9.30 C ANISOU 163 CA THR A 253 1201 1075 1260 136 17 101 C ATOM 164 CA ILE A 254 6.348 -15.451 -27.232 1.00 10.92 C ANISOU 164 CA ILE A 254 1376 1324 1449 144 31 143 C ATOM 165 CA ILE A 255 6.419 -12.144 -25.401 1.00 8.21 C ANISOU 165 CA ILE A 255 983 1050 1087 119 26 136 C ATOM 166 CA THR A 256 8.340 -12.084 -22.149 1.00 11.95 C ANISOU 166 CA THR A 256 1418 1590 1531 133 40 173 C ATOM 167 CA LEU A 257 8.529 -9.336 -19.575 1.00 10.48 C ANISOU 167 CA LEU A 257 1178 1481 1324 103 44 168 C ATOM 168 CA GLU A 258 11.946 -9.384 -17.816 1.00 9.45 C ANISOU 168 CA GLU A 258 1012 1432 1148 136 59 195 C ATOM 169 CA ASP A 259 13.726 -7.094 -15.362 1.00 11.75 C ANISOU 169 CA ASP A 259 1240 1827 1397 120 72 191 C ATOM 170 CA SER A 260 17.047 -5.348 -16.028 1.00 11.15 C ANISOU 170 CA SER A 260 1135 1820 1282 135 83 171 C ATOM 171 CA SER A 261 18.978 -8.274 -14.570 1.00 11.14 C ANISOU 171 CA SER A 261 1127 1855 1252 189 89 228 C ATOM 172 CA GLY A 262 17.319 -10.962 -16.676 1.00 9.19 C ANISOU 172 CA GLY A 262 946 1497 1049 213 80 244 C ATOM 173 CA ASN A 263 14.705 -12.305 -14.257 1.00 14.37 C ANISOU 173 CA ASN A 263 1602 2132 1725 194 82 271 C ATOM 174 CA LEU A 264 11.402 -13.497 -15.766 1.00 17.36 C ANISOU 174 CA LEU A 264 2033 2405 2157 172 71 258 C ATOM 175 CA LEU A 265 8.489 -11.242 -14.779 1.00 11.62 C ANISOU 175 CA LEU A 265 1288 1677 1449 109 59 227 C ATOM 176 CA GLY A 266 5.751 -12.438 -17.104 1.00 7.20 C ANISOU 176 CA GLY A 266 780 1022 934 94 47 208 C ATOM 177 CA ARG A 267 5.025 -14.351 -20.288 1.00 11.41 C ANISOU 177 CA ARG A 267 1368 1473 1496 108 42 193 C ATOM 178 CA ASN A 268 2.343 -14.623 -22.951 1.00 10.13 C ANISOU 178 CA ASN A 268 1242 1242 1367 81 28 156 C ATOM 179 CA SER A 269 2.053 -15.869 -26.521 1.00 9.93 C ANISOU 179 CA SER A 269 1259 1157 1357 90 22 128 C ATOM 180 CA PHE A 270 -0.062 -15.615 -29.659 1.00 9.69 C ANISOU 180 CA PHE A 270 1251 1086 1345 66 7 84 C ATOM 181 CA GLU A 271 -0.072 -17.399 -33.018 1.00 12.31 C ANISOU 181 CA GLU A 271 1623 1367 1686 77 6 57 C ATOM 182 CA VAL A 272 1.016 -15.497 -36.146 1.00 11.97 C ANISOU 182 CA VAL A 272 1577 1342 1630 90 -8 27 C ATOM 183 CA CYS A 273 0.369 -15.808 -39.841 1.00 10.50 C ANISOU 183 CA CYS A 273 1412 1132 1446 89 -19 -13 C ATOM 184 CA VAL A 274 2.312 -13.392 -42.018 1.00 10.75 C ANISOU 184 CA VAL A 274 1431 1197 1457 116 -28 -25 C ATOM 185 CA CYS A 275 0.307 -13.117 -45.229 1.00 12.54 C ANISOU 185 CA CYS A 275 1664 1416 1685 100 -43 -65 C ATOM 186 CA ALA A 276 -0.824 -10.918 -48.124 1.00 12.90 C ANISOU 186 CA ALA A 276 1693 1490 1718 99 -58 -94 C ATOM 187 CA ACYS A 277 -4.454 -10.530 -47.049 0.38 14.35 C ANISOU 187 CA ACYS A 277 1859 1683 1911 55 -65 -101 C ATOM 188 CA BCYS A 277 -4.468 -10.555 -47.046 0.62 14.56 C ANISOU 188 CA BCYS A 277 1886 1709 1938 55 -65 -101 C ATOM 189 CA PRO A 278 -4.738 -10.674 -43.219 1.00 11.91 C ANISOU 189 CA PRO A 278 1542 1370 1615 38 -56 -71 C ATOM 190 CA GLY A 279 -8.464 -9.837 -43.119 1.00 12.22 C ANISOU 190 CA GLY A 279 1561 1424 1659 -2 -66 -85 C ATOM 191 CA ARG A 280 -9.511 -12.595 -45.480 1.00 16.81 C ANISOU 191 CA ARG A 280 2168 1976 2243 -15 -71 -118 C ATOM 192 CA ASP A 281 -7.248 -15.184 -43.887 1.00 11.31 C ANISOU 192 CA ASP A 281 1504 1234 1560 0 -53 -98 C ATOM 193 CA ARG A 282 -8.642 -14.336 -40.458 1.00 16.11 C ANISOU 193 CA ARG A 282 2091 1853 2178 -23 -51 -71 C ATOM 194 CA ARG A 283 -12.252 -14.750 -41.638 1.00 18.26 C ANISOU 194 CA ARG A 283 2357 2127 2454 -66 -62 -105 C ATOM 195 CA THR A 284 -11.403 -18.116 -43.217 1.00 17.37 C ANISOU 195 CA THR A 284 2286 1965 2351 -64 -48 -126 C ATOM 196 CA GLU A 285 -9.529 -19.614 -40.270 1.00 21.27 C ANISOU 196 CA GLU A 285 2798 2425 2860 -45 -26 -85 C ATOM 197 CA GLU A 286 -12.439 -18.626 -38.014 1.00 21.76 C ANISOU 197 CA GLU A 286 2834 2505 2930 -85 -34 -79 C ATOM 198 CA GLU A 287 -14.989 -19.968 -40.492 1.00 24.32 C ANISOU 198 CA GLU A 287 3168 2818 3256 -123 -39 -129 C ATOM 199 CA ASN A 288 -13.794 -23.485 -39.735 1.00 37.49 C ANISOU 199 CA ASN A 288 4880 4418 4946 -118 -5 -122 C END If you find results from this site helpful for your research, please cite one of 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