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*** ***elNémo ID: 2404260151392809221Job options:ID = 2404260151392809221 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 95 20.690 21.163 17.849 1.00 88.39 C ANISOU 1 CA SER A 95 12610 9298 11675 1642 -424 413 C ATOM 2 CA SER A 96 18.636 17.992 17.361 1.00 81.97 C ANISOU 2 CA SER A 96 11054 9145 10947 1727 -523 653 C ATOM 3 CA VAL A 97 21.566 16.373 15.542 1.00 45.25 C ANISOU 3 CA VAL A 97 6666 4514 6012 1137 -748 584 C ATOM 4 CA PRO A 98 22.612 12.996 17.041 1.00 27.09 C ANISOU 4 CA PRO A 98 3986 2643 3663 859 -625 347 C ATOM 5 CA SER A 99 25.570 13.147 19.442 1.00 22.34 C ANISOU 5 CA SER A 99 3611 1963 2913 631 -437 5 C ATOM 6 CA GLN A 100 28.884 11.937 18.033 1.00 19.41 C ANISOU 6 CA GLN A 100 3239 1708 2428 90 -464 -69 C ATOM 7 CA LYS A 101 30.756 12.317 21.322 1.00 16.68 C ANISOU 7 CA LYS A 101 2930 1430 1977 4 -394 -285 C ATOM 8 CA THR A 102 32.908 9.315 22.235 1.00 14.67 C ANISOU 8 CA THR A 102 2221 1598 1757 -152 -354 -247 C ATOM 9 CA TYR A 103 32.165 7.489 25.476 1.00 17.11 C ANISOU 9 CA TYR A 103 2283 2198 2020 81 -310 -182 C ATOM 10 CA GLN A 104 33.666 4.104 26.336 1.00 16.35 C ANISOU 10 CA GLN A 104 1738 2390 2083 100 -293 55 C ATOM 11 CA GLY A 105 31.195 3.850 29.207 1.00 16.16 C ANISOU 11 CA GLY A 105 1728 2535 1875 342 -218 162 C ATOM 12 CA SER A 106 30.880 1.096 31.800 1.00 20.16 C ANISOU 12 CA SER A 106 1945 3362 2355 462 -169 555 C ATOM 13 CA TYR A 107 31.904 -1.690 29.425 1.00 17.15 C ANISOU 13 CA TYR A 107 1335 2689 2494 442 -173 708 C ATOM 14 CA GLY A 108 35.026 -0.043 28.007 1.00 17.78 C ANISOU 14 CA GLY A 108 1438 2802 2516 277 -271 468 C ATOM 15 CA PHE A 109 33.531 0.184 24.528 1.00 14.24 C ANISOU 15 CA PHE A 109 1184 1980 2246 230 -167 236 C ATOM 16 CA AARG A 110 36.079 0.602 21.728 0.56 17.46 C ANISOU 16 CA AARG A 110 1809 2619 2205 156 -42 81 C ATOM 17 CA BARG A 110 36.079 0.610 21.734 0.44 17.46 C ANISOU 17 CA BARG A 110 1809 2620 2205 156 -42 80 C ATOM 18 CA LEU A 111 35.978 0.170 17.964 1.00 14.02 C ANISOU 18 CA LEU A 111 1425 1962 1940 79 -13 50 C ATOM 19 CA GLY A 112 38.424 -1.983 16.017 1.00 11.88 C ANISOU 19 CA GLY A 112 1084 1675 1756 109 -7 60 C ATOM 20 CA PHE A 113 39.155 -2.669 12.363 1.00 13.14 C ANISOU 20 CA PHE A 113 1245 1746 2003 71 24 -23 C ATOM 21 CA LEU A 114 41.015 -5.345 10.401 1.00 14.88 C ANISOU 21 CA LEU A 114 1389 1950 2314 164 54 -68 C ATOM 22 CA HIS A 115 44.564 -4.597 9.296 1.00 14.61 C ANISOU 22 CA HIS A 115 1216 2134 2203 152 62 -151 C ATOM 23 CA SER A 116 43.699 -5.158 5.647 1.00 14.67 C ANISOU 23 CA SER A 116 1270 2075 2229 129 116 -260 C ATOM 24 CA GLY A 117 46.294 -3.133 3.746 1.00 13.83 C ANISOU 24 CA GLY A 117 1068 2196 1990 18 180 -310 C ATOM 25 CA THR A 118 45.718 -1.081 0.598 1.00 13.76 C ANISOU 25 CA THR A 118 1137 2247 1846 -97 260 -303 C ATOM 26 CA ALA A 119 46.035 -3.528 -2.307 1.00 15.09 C ANISOU 26 CA ALA A 119 1232 2536 1966 43 295 -459 C ATOM 27 CA LYS A 120 43.735 -3.177 -5.339 1.00 22.09 C ANISOU 27 CA LYS A 120 2207 3495 2690 71 299 -506 C ATOM 28 CA SER A 121 41.680 -6.212 -4.364 1.00 22.61 C ANISOU 28 CA SER A 121 2279 3353 2960 166 205 -673 C ATOM 29 CA AVAL A 122 40.804 -4.884 -0.903 0.51 16.99 C ANISOU 29 CA AVAL A 122 1647 2445 2363 92 160 -471 C ATOM 30 CA BVAL A 122 40.811 -4.870 -0.905 0.49 17.02 C ANISOU 30 CA BVAL A 122 1651 2450 2366 91 160 -471 C ATOM 31 CA THR A 123 37.124 -3.943 -0.518 1.00 20.90 C ANISOU 31 CA THR A 123 2237 2850 2853 62 94 -430 C ATOM 32 CA ACYS A 124 37.456 -2.375 2.915 0.07 14.16 C ANISOU 32 CA ACYS A 124 1435 1885 2058 11 86 -262 C ATOM 33 CA BCYS A 124 37.437 -2.438 2.952 0.93 13.91 C ANISOU 33 CA BCYS A 124 1403 1852 2031 13 86 -263 C ATOM 34 CA THR A 125 40.472 -0.729 4.506 1.00 12.49 C ANISOU 34 CA THR A 125 1191 1737 1818 -60 117 -194 C ATOM 35 CA TYR A 126 40.804 1.414 7.613 1.00 12.54 C ANISOU 35 CA TYR A 126 1226 1719 1820 -138 93 -138 C ATOM 36 CA SER A 127 43.221 4.293 8.195 1.00 16.21 C ANISOU 36 CA SER A 127 1666 2246 2246 -322 138 -172 C ATOM 37 CA PRO A 128 44.295 4.483 11.866 1.00 19.13 C ANISOU 37 CA PRO A 128 1931 2735 2601 -336 62 -243 C ATOM 38 CA ALA A 129 45.957 7.811 11.077 1.00 23.89 C ANISOU 38 CA ALA A 129 2557 3296 3225 -607 152 -332 C ATOM 39 CA LEU A 130 42.712 9.275 9.730 1.00 20.15 C ANISOU 39 CA LEU A 130 2354 2528 2774 -546 195 -215 C ATOM 40 CA ASN A 131 40.205 7.250 11.746 1.00 16.48 C ANISOU 40 CA ASN A 131 1884 2092 2286 -336 88 -194 C ATOM 41 CA LYS A 132 38.568 6.726 8.369 1.00 16.08 C ANISOU 41 CA LYS A 132 1921 1962 2226 -257 127 -91 C ATOM 42 CA AMET A 133 37.158 3.678 6.599 0.64 15.50 C ANISOU 42 CA AMET A 133 1786 1951 2153 -124 93 -82 C ATOM 43 CA BMET A 133 37.137 3.684 6.603 0.36 15.43 C ANISOU 43 CA BMET A 133 1777 1942 2144 -124 93 -82 C ATOM 44 CA PHE A 134 37.508 3.333 2.834 1.00 15.83 C ANISOU 44 CA PHE A 134 1824 2083 2107 -101 137 -84 C ATOM 45 CA CYS A 135 35.132 0.795 1.340 1.00 15.05 C ANISOU 45 CA CYS A 135 1667 2040 2010 9 77 -184 C ATOM 46 CA GLN A 136 33.350 -0.404 -1.776 1.00 16.61 C ANISOU 46 CA GLN A 136 1812 2400 2100 92 39 -308 C ATOM 47 CA LEU A 137 29.632 -0.080 -2.551 1.00 20.10 C ANISOU 47 CA LEU A 137 2225 2947 2467 179 -49 -355 C ATOM 48 CA ALA A 138 27.585 -3.000 -1.159 1.00 17.65 C ANISOU 48 CA ALA A 138 1780 2556 2368 105 -88 -536 C ATOM 49 CA ALYS A 139 30.712 -4.873 -0.028 0.49 16.22 C ANISOU 49 CA ALYS A 139 1623 2188 2351 47 -14 -534 C ATOM 50 CA BLYS A 139 30.704 -4.882 -0.028 0.51 16.24 C ANISOU 50 CA BLYS A 139 1625 2190 2354 47 -14 -535 C ATOM 51 CA THR A 140 31.563 -6.389 3.374 1.00 18.15 C ANISOU 51 CA THR A 140 1887 2201 2809 13 35 -423 C ATOM 52 CA ACYS A 141 32.726 -3.821 5.940 0.75 13.72 C ANISOU 52 CA ACYS A 141 1398 1650 2163 21 37 -223 C ATOM 53 CA BCYS A 141 32.719 -3.815 5.940 0.25 13.82 C ANISOU 53 CA BCYS A 141 1412 1664 2177 21 37 -223 C ATOM 54 CA PRO A 142 33.910 -5.490 9.164 1.00 13.23 C ANISOU 54 CA PRO A 142 1320 1496 2209 54 67 -104 C ATOM 55 CA VAL A 143 33.624 -3.293 12.253 1.00 12.43 C ANISOU 55 CA VAL A 143 1250 1473 1999 56 49 11 C ATOM 56 CA GLN A 144 34.948 -4.670 15.530 1.00 11.88 C ANISOU 56 CA GLN A 144 1142 1458 1915 145 60 156 C ATOM 57 CA LEU A 145 33.464 -4.142 18.976 1.00 13.40 C ANISOU 57 CA LEU A 145 1335 1760 1996 188 76 281 C ATOM 58 CA TRP A 146 35.997 -4.284 21.798 1.00 14.88 C ANISOU 58 CA TRP A 146 1452 2186 2014 316 32 372 C ATOM 59 CA VAL A 147 34.859 -4.310 25.424 1.00 18.74 C ANISOU 59 CA VAL A 147 1920 2895 2306 422 57 526 C ATOM 60 CA ASP A 148 36.587 -4.560 28.801 1.00 18.42 C ANISOU 60 CA ASP A 148 1782 3240 1976 614 7 647 C ATOM 61 CA SER A 149 33.472 -6.148 30.288 1.00 22.05 C ANISOU 61 CA SER A 149 2305 3628 2444 650 166 916 C ATOM 62 CA THR A 150 30.709 -8.167 28.591 1.00 25.57 C ANISOU 62 CA THR A 150 2828 3684 3204 515 327 1039 C ATOM 63 CA PRO A 151 27.357 -6.384 28.135 1.00 25.46 C ANISOU 63 CA PRO A 151 2790 3674 3208 357 370 877 C ATOM 64 CA PRO A 152 24.432 -8.695 29.013 1.00 31.56 C ANISOU 64 CA PRO A 152 3531 4351 4110 270 584 1120 C ATOM 65 CA PRO A 153 22.376 -10.477 26.319 1.00 34.41 C ANISOU 65 CA PRO A 153 3864 4373 4838 41 671 1037 C ATOM 66 CA GLY A 154 19.681 -8.045 25.245 1.00 26.51 C ANISOU 66 CA GLY A 154 2742 3549 3782 -41 615 768 C ATOM 67 CA THR A 155 22.281 -5.371 24.530 1.00 18.10 C ANISOU 67 CA THR A 155 1776 2551 2550 101 417 593 C ATOM 68 CA ARG A 156 21.967 -3.782 21.078 1.00 15.33 C ANISOU 68 CA ARG A 156 1435 2105 2283 56 295 332 C ATOM 69 CA VAL A 157 24.435 -2.164 18.654 1.00 12.49 C ANISOU 69 CA VAL A 157 1177 1659 1909 84 166 189 C ATOM 70 CA ARG A 158 23.219 0.768 16.553 1.00 14.29 C ANISOU 70 CA ARG A 158 1442 1916 2073 134 92 37 C ATOM 71 CA ALA A 159 24.776 2.366 13.471 1.00 10.74 C ANISOU 71 CA ALA A 159 1091 1383 1605 145 26 -36 C ATOM 72 CA MET A 160 23.866 5.732 11.952 1.00 12.69 C ANISOU 72 CA MET A 160 1451 1611 1760 266 -4 -64 C ATOM 73 CA ALA A 161 25.394 8.013 9.325 1.00 11.09 C ANISOU 73 CA ALA A 161 1407 1299 1508 295 -3 -24 C ATOM 74 CA ILE A 162 25.594 11.802 9.657 1.00 12.52 C ANISOU 74 CA ILE A 162 1802 1281 1674 378 46 12 C ATOM 75 CA TYR A 163 27.238 14.486 7.532 1.00 14.96 C ANISOU 75 CA TYR A 163 2332 1367 1986 366 129 129 C ATOM 76 CA LYS A 164 30.640 15.632 8.790 1.00 22.19 C ANISOU 76 CA LYS A 164 3318 2103 3011 95 211 56 C ATOM 77 CA GLN A 165 30.467 19.310 7.866 1.00 25.64 C ANISOU 77 CA GLN A 165 4043 2175 3523 147 338 160 C ATOM 78 CA SER A 166 28.448 21.660 10.085 1.00 26.72 C ANISOU 78 CA SER A 166 4331 2080 3742 321 352 42 C ATOM 79 CA GLN A 167 26.364 23.114 7.215 1.00 28.06 C ANISOU 79 CA GLN A 167 4681 2139 3842 649 397 332 C ATOM 80 CA HIS A 168 25.092 19.647 6.247 1.00 21.85 C ANISOU 80 CA HIS A 168 3589 1846 2868 716 241 332 C ATOM 81 CA AMET A 169 24.766 18.018 9.677 0.50 20.78 C ANISOU 81 CA AMET A 169 3262 1856 2776 608 168 80 C ATOM 82 CA BMET A 169 24.763 18.015 9.683 0.50 20.77 C ANISOU 82 CA BMET A 169 3261 1856 2776 608 168 79 C ATOM 83 CA THR A 170 21.033 18.740 9.963 1.00 22.23 C ANISOU 83 CA THR A 170 3409 2152 2887 964 121 83 C ATOM 84 CA GLU A 171 20.370 17.002 6.645 1.00 17.41 C ANISOU 84 CA GLU A 171 2674 1803 2138 1031 52 231 C ATOM 85 CA VAL A 172 19.421 13.309 6.899 1.00 18.53 C ANISOU 85 CA VAL A 172 2495 2297 2249 902 -42 101 C ATOM 86 CA VAL A 173 21.956 11.038 5.203 1.00 15.60 C ANISOU 86 CA VAL A 173 2075 1966 1886 665 -45 101 C ATOM 87 CA AARG A 174 20.041 8.910 2.701 0.63 15.15 C ANISOU 87 CA AARG A 174 1800 2241 1715 736 -142 28 C ATOM 88 CA BARG A 174 20.061 8.887 2.712 0.37 15.24 C ANISOU 88 CA BARG A 174 1811 2252 1728 733 -142 28 C ATOM 89 CA ARG A 175 20.560 7.080 -0.591 1.00 20.40 C ANISOU 89 CA ARG A 175 2356 3142 2253 709 -197 -41 C ATOM 90 CA CYS A 176 20.418 8.898 -3.933 1.00 23.08 C ANISOU 90 CA CYS A 176 2781 3676 2312 951 -218 116 C ATOM 91 CA PRO A 177 17.309 8.634 -6.177 1.00 30.98 C ANISOU 91 CA PRO A 177 3562 5158 3053 1220 -369 32 C ATOM 92 CA HIS A 178 19.071 6.212 -8.568 1.00 28.04 C ANISOU 92 CA HIS A 178 3086 4984 2583 1057 -385 -149 C ATOM 93 CA HIS A 179 19.938 3.753 -5.808 1.00 28.63 C ANISOU 93 CA HIS A 179 3099 4755 3024 725 -336 -343 C ATOM 94 CA AGLU A 180 16.763 4.191 -3.744 0.44 39.40 C ANISOU 94 CA AGLU A 180 4328 6173 4471 795 -390 -379 C ATOM 95 CA BGLU A 180 16.730 4.250 -3.819 0.56 40.06 C ANISOU 95 CA BGLU A 180 4412 6265 4546 804 -392 -376 C ATOM 96 CA AARG A 181 14.698 3.195 -6.808 0.44 59.24 C ANISOU 96 CA AARG A 181 6861 9397 6248 -10 -773 -397 C ATOM 97 CA BARG A 181 14.917 3.408 -7.067 0.56 59.72 C ANISOU 97 CA BARG A 181 6950 9465 6275 6 -775 -368 C ATOM 98 CA CYS A 182 16.667 0.123 -7.828 1.00 62.82 C ANISOU 98 CA CYS A 182 7487 9733 6649 -352 -551 -771 C ATOM 99 CA SER A 183 15.970 -3.139 -6.050 1.00 69.51 C ANISOU 99 CA SER A 183 8248 10334 7831 -625 -379 -1113 C ATOM 100 CA ASP A 184 19.224 -4.138 -4.427 1.00 63.96 C ANISOU 100 CA ASP A 184 7759 9146 7395 -630 -84 -1148 C ATOM 101 CA SER A 185 16.846 -4.382 -1.489 1.00 52.68 C ANISOU 101 CA SER A 185 6111 7665 6239 -631 -148 -1109 C ATOM 102 CA ASP A 186 17.135 -7.591 0.530 1.00 39.70 C ANISOU 102 CA ASP A 186 4512 5624 4949 -831 128 -1270 C ATOM 103 CA GLY A 187 13.550 -7.383 1.779 1.00 33.49 C ANISOU 103 CA GLY A 187 3457 5074 4196 -871 9 -1242 C ATOM 104 CA LEU A 188 14.652 -6.243 5.235 1.00 30.96 C ANISOU 104 CA LEU A 188 3172 4501 4090 -685 91 -995 C ATOM 105 CA ALA A 189 16.424 -2.955 4.634 1.00 25.41 C ANISOU 105 CA ALA A 189 2583 3840 3232 -370 -57 -758 C ATOM 106 CA PRO A 190 14.317 0.015 3.579 1.00 23.73 C ANISOU 106 CA PRO A 190 2199 3975 2844 -159 -295 -638 C ATOM 107 CA PRO A 191 15.527 0.995 0.085 1.00 23.94 C ANISOU 107 CA PRO A 191 2347 4177 2574 -119 -415 -590 C ATOM 108 CA GLN A 192 16.413 4.510 1.325 1.00 22.66 C ANISOU 108 CA GLN A 192 2296 3818 2497 208 -429 -268 C ATOM 109 CA HIS A 193 18.819 3.348 4.049 1.00 16.64 C ANISOU 109 CA HIS A 193 1675 2672 1975 110 -228 -321 C ATOM 110 CA LEU A 194 22.518 3.876 3.336 1.00 15.81 C ANISOU 110 CA LEU A 194 1777 2341 1889 94 -123 -231 C ATOM 111 CA ILE A 195 23.717 1.421 5.988 1.00 12.99 C ANISOU 111 CA ILE A 195 1406 1788 1741 -7 0 -311 C ATOM 112 CA ARG A 196 22.741 -2.248 6.070 1.00 13.23 C ANISOU 112 CA ARG A 196 1383 1790 1856 -178 119 -489 C ATOM 113 CA VAL A 197 23.959 -5.219 8.083 1.00 16.31 C ANISOU 113 CA VAL A 197 1809 1911 2478 -234 304 -470 C ATOM 114 CA GLU A 198 24.584 -8.475 6.216 1.00 19.60 C ANISOU 114 CA GLU A 198 2290 2133 3023 -379 528 -673 C ATOM 115 CA GLY A 199 24.678 -11.970 7.694 1.00 23.48 C ANISOU 115 CA GLY A 199 2847 2256 3820 -452 790 -670 C ATOM 116 CA ASN A 200 22.228 -11.256 10.517 1.00 21.20 C ANISOU 116 CA ASN A 200 2472 2097 3486 -486 695 -521 C ATOM 117 CA LEU A 201 18.573 -12.347 10.434 1.00 25.58 C ANISOU 117 CA LEU A 201 2907 2760 4054 -774 750 -729 C ATOM 118 CA ARG A 202 17.894 -10.413 13.643 1.00 17.09 C ANISOU 118 CA ARG A 202 1775 1842 2878 -608 664 -456 C ATOM 119 CA VAL A 203 18.756 -7.091 11.998 1.00 13.54 C ANISOU 119 CA VAL A 203 1291 1634 2220 -422 402 -488 C ATOM 120 CA GLU A 204 16.355 -4.216 12.747 1.00 15.99 C ANISOU 120 CA GLU A 204 1444 2243 2389 -314 258 -487 C ATOM 121 CA TYR A 205 15.836 -0.942 10.879 1.00 13.78 C ANISOU 121 CA TYR A 205 1101 2170 1966 -125 50 -489 C ATOM 122 CA LEU A 206 14.506 2.373 12.149 1.00 13.05 C ANISOU 122 CA LEU A 206 951 2170 1838 126 -13 -412 C ATOM 123 CA ASP A 207 13.093 5.506 10.612 1.00 18.26 C ANISOU 123 CA ASP A 207 1519 2962 2456 395 -148 -336 C ATOM 124 CA ASP A 208 13.012 7.913 13.537 1.00 18.80 C ANISOU 124 CA ASP A 208 1688 2856 2599 586 -26 -325 C ATOM 125 CA AARG A 209 9.444 9.153 14.026 0.52 25.69 C ANISOU 125 CA AARG A 209 2261 3943 3558 821 23 -347 C ATOM 126 CA BARG A 209 9.442 9.179 13.952 0.48 25.49 C ANISOU 126 CA BARG A 209 2234 3920 3533 824 19 -343 C ATOM 127 CA ASN A 210 10.736 12.629 14.929 1.00 26.77 C ANISOU 127 CA ASN A 210 2676 3732 3765 1070 99 -309 C ATOM 128 CA THR A 211 14.179 13.205 13.373 1.00 21.64 C ANISOU 128 CA THR A 211 2327 2831 3066 945 -3 -210 C ATOM 129 CA PHE A 212 13.515 11.092 10.250 1.00 20.13 C ANISOU 129 CA PHE A 212 1945 2947 2756 857 -180 -117 C ATOM 130 CA ARG A 213 17.012 9.636 10.649 1.00 18.01 C ANISOU 130 CA ARG A 213 1904 2490 2449 586 -145 -163 C ATOM 131 CA HIS A 214 17.812 6.103 9.538 1.00 14.07 C ANISOU 131 CA HIS A 214 1348 2110 1886 334 -155 -237 C ATOM 132 CA SER A 215 19.625 3.581 11.720 1.00 10.85 C ANISOU 132 CA SER A 215 1007 1571 1544 156 -45 -285 C ATOM 133 CA VAL A 216 20.306 -0.146 11.700 1.00 13.75 C ANISOU 133 CA VAL A 216 1364 1880 1982 -32 62 -332 C ATOM 134 CA AVAL A 217 20.592 -2.221 14.884 0.78 13.17 C ANISOU 134 CA AVAL A 217 1323 1700 1980 -89 191 -248 C ATOM 135 CA BVAL A 217 20.596 -2.238 14.883 0.22 13.19 C ANISOU 135 CA BVAL A 217 1327 1703 1984 -90 192 -248 C ATOM 136 CA VAL A 218 21.658 -5.778 15.770 1.00 13.93 C ANISOU 136 CA VAL A 218 1478 1587 2226 -183 363 -151 C ATOM 137 CA PRO A 219 21.771 -7.728 19.045 1.00 18.90 C ANISOU 137 CA PRO A 219 2179 2122 2879 -182 503 87 C ATOM 138 CA TYR A 220 25.186 -7.603 20.701 1.00 16.40 C ANISOU 138 CA TYR A 220 1927 1786 2517 -6 394 344 C ATOM 139 CA GLU A 221 26.827 -11.021 20.837 1.00 20.68 C ANISOU 139 CA GLU A 221 2521 2027 3309 71 569 590 C ATOM 140 CA PRO A 222 30.001 -11.814 22.847 1.00 23.54 C ANISOU 140 CA PRO A 222 2859 2414 3671 318 467 982 C ATOM 141 CA PRO A 223 33.334 -12.286 20.966 1.00 27.70 C ANISOU 141 CA PRO A 223 3244 2826 4455 502 442 1019 C ATOM 142 CA AGLU A 224 33.521 -15.152 18.450 0.38 27.57 C ANISOU 142 CA AGLU A 224 3282 2425 4770 499 759 870 C ATOM 143 CA BGLU A 224 33.408 -15.198 18.506 0.23 27.76 C ANISOU 143 CA BGLU A 224 3313 2444 4792 494 763 872 C ATOM 144 CA CGLU A 224 33.605 -15.098 18.390 0.39 27.50 C ANISOU 144 CA CGLU A 224 3267 2419 4761 502 755 867 C ATOM 145 CA VAL A 225 35.715 -18.215 18.912 1.00 33.46 C ANISOU 145 CA VAL A 225 3998 2991 5724 704 911 1089 C ATOM 146 CA GLY A 226 39.307 -17.319 18.058 1.00 37.18 C ANISOU 146 CA GLY A 226 4240 3628 6258 879 792 1140 C ATOM 147 CA SER A 227 38.584 -13.606 18.434 1.00 29.52 C ANISOU 147 CA SER A 227 3207 2979 5029 750 505 1038 C ATOM 148 CA ASP A 228 38.747 -11.110 21.299 1.00 26.17 C ANISOU 148 CA ASP A 228 2693 2953 4297 745 148 1208 C ATOM 149 CA CYS A 229 36.191 -8.801 19.687 1.00 18.05 C ANISOU 149 CA CYS A 229 1793 1924 3142 500 158 846 C ATOM 150 CA THR A 230 32.696 -8.945 18.193 1.00 16.41 C ANISOU 150 CA THR A 230 1772 1566 2897 306 324 571 C ATOM 151 CA THR A 231 32.541 -8.314 14.443 1.00 15.41 C ANISOU 151 CA THR A 231 1650 1362 2845 207 422 262 C ATOM 152 CA ILE A 232 29.631 -6.763 12.526 1.00 13.90 C ANISOU 152 CA ILE A 232 1524 1280 2479 30 392 -16 C ATOM 153 CA HIS A 233 29.408 -6.748 8.724 1.00 14.23 C ANISOU 153 CA HIS A 233 1595 1330 2481 -63 478 -265 C ATOM 154 CA TYR A 234 28.027 -3.455 7.431 1.00 10.26 C ANISOU 154 CA TYR A 234 1093 1076 1729 -87 292 -317 C ATOM 155 CA ASN A 235 27.184 -2.610 3.831 1.00 14.28 C ANISOU 155 CA ASN A 235 1643 1763 2021 -154 278 -461 C ATOM 156 CA TYR A 236 27.161 0.937 2.477 1.00 12.15 C ANISOU 156 CA TYR A 236 1415 1645 1558 -67 143 -321 C ATOM 157 CA MET A 237 24.655 1.134 -0.368 1.00 15.88 C ANISOU 157 CA MET A 237 1881 2427 1728 -106 37 -410 C ATOM 158 CA CYS A 238 25.769 4.374 -2.016 1.00 15.81 C ANISOU 158 CA CYS A 238 1988 2458 1559 22 4 -149 C ATOM 159 CA ASN A 239 29.048 5.799 -3.267 1.00 18.86 C ANISOU 159 CA ASN A 239 2505 2711 1950 7 186 12 C ATOM 160 CA SER A 240 30.267 9.012 -1.639 1.00 26.84 C ANISOU 160 CA SER A 240 3572 3457 3169 75 188 244 C ATOM 161 CA SER A 241 30.171 10.494 -5.151 1.00 30.37 C ANISOU 161 CA SER A 241 4177 4074 3288 115 244 467 C ATOM 162 CA CYS A 242 26.533 9.585 -5.896 1.00 29.46 C ANISOU 162 CA CYS A 242 3980 4296 2918 229 -7 399 C ATOM 163 CA MET A 243 24.856 12.724 -7.241 1.00 36.24 C ANISOU 163 CA MET A 243 4935 5227 3609 485 -133 795 C ATOM 164 CA GLY A 244 21.609 13.661 -5.502 1.00 40.84 C ANISOU 164 CA GLY A 244 5342 5843 4333 734 -353 831 C ATOM 165 CA GLY A 245 22.654 11.740 -2.413 1.00 29.46 C ANISOU 165 CA GLY A 245 3816 4170 3208 533 -253 482 C ATOM 166 CA LEU A 246 25.809 12.375 -0.410 1.00 0.00 C ATOM 167 CA ASN A 247 27.224 14.011 -3.557 1.00 21.59 C ANISOU 167 CA ASN A 247 3115 2787 2301 402 44 723 C ATOM 168 CA ARG A 248 30.871 13.871 -2.400 1.00 22.70 C ANISOU 168 CA ARG A 248 3267 2665 2693 164 252 630 C ATOM 169 CA ARG A 249 29.960 15.159 1.065 1.00 18.15 C ANISOU 169 CA ARG A 249 2664 1838 2395 218 160 527 C ATOM 170 CA PRO A 250 31.995 13.397 3.798 1.00 15.80 C ANISOU 170 CA PRO A 250 2213 1513 2279 32 157 287 C ATOM 171 CA ILE A 251 30.066 11.389 6.396 1.00 16.61 C ANISOU 171 CA ILE A 251 2460 1632 2219 351 350 331 C ATOM 172 CA LEU A 252 30.640 9.724 9.755 1.00 15.95 C ANISOU 172 CA LEU A 252 2274 1560 2227 165 247 158 C ATOM 173 CA THR A 253 29.227 6.469 11.070 1.00 10.53 C ANISOU 173 CA THR A 253 1385 1082 1533 167 154 67 C ATOM 174 CA ILE A 254 28.171 6.597 14.711 1.00 11.42 C ANISOU 174 CA ILE A 254 1509 1198 1633 159 121 -2 C ATOM 175 CA ILE A 255 28.207 3.283 16.574 1.00 11.80 C ANISOU 175 CA ILE A 255 1422 1358 1704 72 88 -4 C ATOM 176 CA ATHR A 256 26.133 3.222 19.774 0.61 12.11 C ANISOU 176 CA ATHR A 256 1418 1530 1654 117 84 -14 C ATOM 177 CA BTHR A 256 26.171 3.210 19.786 0.39 12.08 C ANISOU 177 CA BTHR A 256 1414 1526 1651 116 83 -14 C ATOM 178 CA ALEU A 257 25.939 0.524 22.439 0.57 12.29 C ANISOU 178 CA ALEU A 257 1365 1653 1650 63 108 75 C ATOM 179 CA BLEU A 257 25.930 0.537 22.464 0.43 12.36 C ANISOU 179 CA BLEU A 257 1373 1663 1658 64 108 75 C ATOM 180 CA GLU A 258 22.535 0.477 24.176 1.00 14.82 C ANISOU 180 CA GLU A 258 1577 2216 1837 86 143 91 C ATOM 181 CA ASP A 259 20.709 -1.850 26.566 1.00 14.48 C ANISOU 181 CA ASP A 259 1430 2361 1711 -10 233 230 C ATOM 182 CA SER A 260 17.416 -3.674 25.947 1.00 16.48 C ANISOU 182 CA SER A 260 1533 2805 1922 -237 333 249 C ATOM 183 CA SER A 261 15.591 -0.627 27.326 1.00 16.07 C ANISOU 183 CA SER A 261 1339 3134 1633 24 265 156 C ATOM 184 CA GLY A 262 17.316 1.924 25.097 1.00 13.84 C ANISOU 184 CA GLY A 262 1224 2599 1435 216 167 24 C ATOM 185 CA ASN A 263 19.685 3.286 27.741 1.00 16.93 C ANISOU 185 CA ASN A 263 1732 2884 1815 331 121 8 C ATOM 186 CA LEU A 264 22.977 4.511 26.256 1.00 16.32 C ANISOU 186 CA LEU A 264 1836 2467 1899 301 73 -62 C ATOM 187 CA LEU A 265 26.032 2.476 27.302 1.00 16.75 C ANISOU 187 CA LEU A 265 1876 2473 2015 200 69 25 C ATOM 188 CA GLY A 266 28.727 3.759 24.967 1.00 12.11 C ANISOU 188 CA GLY A 266 1381 1670 1550 125 37 -59 C ATOM 189 CA ARG A 267 29.414 5.556 21.703 1.00 13.28 C ANISOU 189 CA ARG A 267 1645 1597 1802 73 49 -105 C ATOM 190 CA ASN A 268 32.144 5.664 19.076 1.00 10.57 C ANISOU 190 CA ASN A 268 1320 1147 1549 -41 62 -86 C ATOM 191 CA SER A 269 32.479 6.905 15.504 1.00 11.80 C ANISOU 191 CA SER A 269 1560 1167 1758 -57 114 -32 C ATOM 192 CA PHE A 270 34.570 6.792 12.336 1.00 12.12 C ANISOU 192 CA PHE A 270 1568 1212 1824 -123 153 41 C ATOM 193 CA GLU A 271 34.543 8.604 9.005 1.00 13.08 C ANISOU 193 CA GLU A 271 1787 1258 1927 -84 244 160 C ATOM 194 CA AVAL A 272 33.683 6.527 5.950 0.63 13.67 C ANISOU 194 CA AVAL A 272 1723 1539 1932 74 226 203 C ATOM 195 CA BVAL A 272 33.611 6.522 5.944 0.37 14.79 C ANISOU 195 CA BVAL A 272 1866 1682 2073 78 226 202 C ATOM 196 CA ARG A 273 34.347 7.032 2.251 1.00 0.00 C ATOM 197 CA VAL A 274 32.573 4.781 -0.217 1.00 14.92 C ANISOU 197 CA VAL A 274 1659 2140 1868 358 239 236 C ATOM 198 CA CYS A 275 34.413 4.326 -3.508 1.00 20.09 C ANISOU 198 CA CYS A 275 2180 3056 2396 433 273 290 C ATOM 199 CA ALA A 276 35.739 2.083 -6.277 1.00 20.37 C ANISOU 199 CA ALA A 276 2008 3426 2308 532 239 176 C ATOM 200 CA CYS A 277 39.374 2.205 -5.133 1.00 20.58 C ANISOU 200 CA CYS A 277 2024 3390 2406 363 265 251 C ATOM 201 CA PRO A 278 39.524 2.095 -1.295 1.00 17.38 C ANISOU 201 CA PRO A 278 1737 2681 2184 190 223 199 C ATOM 202 CA GLY A 279 43.213 1.184 -1.151 1.00 14.54 C ANISOU 202 CA GLY A 279 1215 2546 1763 144 220 191 C ATOM 203 CA ARG A 280 44.177 3.879 -3.647 1.00 19.04 C ANISOU 203 CA ARG A 280 1741 3271 2222 47 347 396 C ATOM 204 CA ASP A 281 42.250 6.571 -1.764 1.00 17.52 C ANISOU 204 CA ASP A 281 1815 2671 2170 -105 404 480 C ATOM 205 CA ARG A 282 43.604 5.604 1.642 1.00 15.08 C ANISOU 205 CA ARG A 282 1455 2326 1949 -255 319 320 C ATOM 206 CA ARG A 283 47.175 5.963 0.353 1.00 16.71 C ANISOU 206 CA ARG A 283 1424 2905 2020 -419 382 373 C ATOM 207 CA THR A 284 46.322 9.337 -1.225 1.00 0.00 C ATOM 208 CA GLU A 285 44.650 10.787 1.821 1.00 25.62 C ANISOU 208 CA GLU A 285 3034 3349 3351 -705 544 493 C ATOM 209 CA GLU A 286 47.449 9.611 4.108 1.00 25.20 C ANISOU 209 CA GLU A 286 2707 3613 3256 -911 457 298 C ATOM 210 CA GLU A 287 49.983 11.539 2.036 1.00 41.62 C ANISOU 210 CA GLU A 287 4688 5871 5254 -1254 631 433 C ATOM 211 CA ASN A 288 47.667 14.594 2.001 1.00 57.03 C ANISOU 211 CA ASN A 288 7111 7188 7369 -1340 785 562 C ATOM 212 CA LEU A 289 48.465 15.182 5.685 1.00 69.10 C ANISOU 212 CA LEU A 289 8618 8658 8978 -1543 674 255 C ATOM 213 CA ARG A 290 52.003 16.178 4.748 1.00 68.04 C ANISOU 213 CA ARG A 290 8261 8831 8759 -1846 737 242 C HETATM 1657 ZN ZN A 301 23.732 6.250 -4.804 1.00 21.79 ZN CONECT 688 1657 CONECT 713 1657 CONECT 1243 1657 CONECT 1269 1657 CONECT 1657 688 713 1243 1269 END If you find results from this site helpful for your research, please cite one of our papers:
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