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*** ***elNémo ID: 2404140106454101830Job options:ID = 2404140106454101830 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 -6.411 8.590 -2.131 1.00 29.58 C ANISOU 1 CA VAL A 97 3470 3825 3942 34 58 47 C ATOM 2 CA PRO A 98 -4.811 12.061 -2.300 1.00 26.91 C ANISOU 2 CA PRO A 98 3048 3491 3685 -471 245 141 C ATOM 3 CA SER A 99 -7.106 14.802 -3.588 1.00 29.22 C ANISOU 3 CA SER A 99 3662 3456 3981 -384 554 217 C ATOM 4 CA GLN A 100 -6.727 16.128 -7.121 1.00 28.04 C ANISOU 4 CA GLN A 100 3247 2955 4452 261 -9 -53 C ATOM 5 CA LYS A 101 -8.930 19.164 -6.451 1.00 19.30 C ANISOU 5 CA LYS A 101 2289 2232 2812 331 173 60 C ATOM 6 CA THR A 102 -7.596 22.423 -7.897 1.00 15.49 C ANISOU 6 CA THR A 102 1672 2266 1945 30 -68 -301 C ATOM 7 CA TYR A 103 -6.781 24.803 -5.045 1.00 13.47 C ANISOU 7 CA TYR A 103 1670 1869 1577 238 32 -107 C ATOM 8 CA GLN A 104 -5.184 28.041 -6.178 1.00 16.71 C ANISOU 8 CA GLN A 104 2152 1795 2401 43 102 497 C ATOM 9 CA GLY A 105 -4.851 29.074 -2.534 1.00 17.85 C ANISOU 9 CA GLY A 105 2367 1665 2748 103 305 -137 C ATOM 10 CA ASER A 106 -3.610 32.349 -1.074 0.50 18.70 C ANISOU 10 CA ASER A 106 2584 1664 2854 65 261 -213 C ATOM 11 CA BSER A 106 -3.637 32.359 -1.098 0.50 20.00 C ANISOU 11 CA BSER A 106 2708 1921 2970 18 238 -197 C ATOM 12 CA TYR A 107 -0.671 32.603 -3.489 1.00 18.12 C ANISOU 12 CA TYR A 107 2319 1820 2743 -3 284 86 C ATOM 13 CA GLY A 108 -2.659 32.180 -6.732 1.00 18.81 C ANISOU 13 CA GLY A 108 2783 1534 2827 63 405 -36 C ATOM 14 CA PHE A 109 -0.874 28.972 -7.685 1.00 15.80 C ANISOU 14 CA PHE A 109 2090 1551 2361 -96 236 -210 C ATOM 15 CA AARG A 110 -1.292 27.563 -11.162 0.50 19.75 C ANISOU 15 CA AARG A 110 2383 2335 2785 -99 94 -343 C ATOM 16 CA BARG A 110 -1.291 27.757 -11.281 0.50 13.92 C ANISOU 16 CA BARG A 110 1708 1466 2115 -66 233 218 C ATOM 17 CA LEU A 111 0.586 25.506 -13.717 1.00 13.16 C ANISOU 17 CA LEU A 111 1721 1453 1827 -31 107 0 C ATOM 18 CA GLY A 112 1.860 26.310 -17.165 1.00 14.78 C ANISOU 18 CA GLY A 112 2127 1688 1799 -165 -143 460 C ATOM 19 CA PHE A 113 3.310 24.229 -19.953 1.00 17.38 C ANISOU 19 CA PHE A 113 2477 2348 1778 -351 -16 196 C ATOM 20 CA LEU A 114 5.455 25.043 -22.994 1.00 27.17 C ANISOU 20 CA LEU A 114 3661 3869 2793 -315 249 501 C TER 21 LEU A 114 ATOM 22 CA VAL A 122 8.211 15.790 -30.004 1.00 30.48 C ANISOU 22 CA VAL A 122 4357 4135 3088 -28 80 -164 C ATOM 23 CA THR A 123 9.460 14.641 -26.589 1.00 24.75 C ANISOU 23 CA THR A 123 3484 3306 2613 -192 379 359 C ATOM 24 CA ACYS A 124 6.810 16.468 -24.510 0.70 18.76 C ANISOU 24 CA ACYS A 124 2406 1996 2724 -371 -69 378 C ATOM 25 CA BCYS A 124 6.802 16.457 -24.525 0.30 22.61 C ANISOU 25 CA BCYS A 124 2931 2634 3025 -96 65 303 C ATOM 26 CA THR A 125 3.596 18.207 -25.622 1.00 17.63 C ANISOU 26 CA THR A 125 2757 1800 2139 -516 21 238 C ATOM 27 CA TYR A 126 0.662 19.578 -23.642 1.00 15.48 C ANISOU 27 CA TYR A 126 2732 1427 1721 -78 -394 333 C ATOM 28 CA SER A 127 -2.997 19.814 -24.653 1.00 16.64 C ANISOU 28 CA SER A 127 3041 1541 1738 -372 -556 421 C ATOM 29 CA PRO A 128 -4.856 22.617 -22.866 1.00 18.89 C ANISOU 29 CA PRO A 128 3334 1399 2442 223 -761 278 C ATOM 30 CA ALA A 129 -8.171 21.249 -24.227 1.00 21.63 C ANISOU 30 CA ALA A 129 3486 2070 2660 71 -1009 199 C ATOM 31 CA LEU A 130 -7.542 17.878 -22.558 1.00 17.21 C ANISOU 31 CA LEU A 130 2931 1570 2038 31 -831 134 C ATOM 32 CA ASN A 131 -5.457 19.267 -19.643 1.00 15.88 C ANISOU 32 CA ASN A 131 2615 1687 1732 289 -749 -15 C ATOM 33 CA LYS A 132 -3.103 16.489 -20.643 1.00 12.96 C ANISOU 33 CA LYS A 132 1977 1249 1699 -58 -317 234 C ATOM 34 CA AMET A 133 0.629 16.101 -21.100 0.70 13.21 C ANISOU 34 CA AMET A 133 2355 1362 1300 -461 -148 242 C ATOM 35 CA BMET A 133 0.631 16.106 -21.097 0.30 14.09 C ANISOU 35 CA BMET A 133 2273 1547 1531 -252 -123 134 C ATOM 36 CA PHE A 134 1.939 13.621 -23.672 1.00 14.44 C ANISOU 36 CA PHE A 134 2465 1552 1468 -75 -257 25 C ATOM 37 CA ACYS A 135 5.599 12.715 -23.185 0.80 15.14 C ANISOU 37 CA ACYS A 135 2440 1601 1709 -19 198 42 C ATOM 38 CA BCYS A 135 5.599 12.717 -23.124 0.20 16.39 C ANISOU 38 CA BCYS A 135 2406 1800 2019 22 106 92 C ATOM 39 CA GLN A 136 8.261 10.110 -23.914 1.00 16.16 C ANISOU 39 CA GLN A 136 2221 2024 1891 67 313 88 C ATOM 40 CA LEU A 137 9.757 7.879 -21.223 1.00 16.91 C ANISOU 40 CA LEU A 137 2587 1969 1869 177 172 -43 C ATOM 41 CA ALA A 138 12.725 9.488 -19.401 1.00 18.69 C ANISOU 41 CA ALA A 138 2467 2257 2374 395 353 222 C ATOM 42 CA LYS A 139 12.565 12.699 -21.452 1.00 16.51 C ANISOU 42 CA LYS A 139 2399 1934 1940 71 249 131 C ATOM 43 CA THR A 140 12.445 16.223 -20.053 1.00 17.15 C ANISOU 43 CA THR A 140 2581 2076 1856 82 302 309 C ATOM 44 CA ACYS A 141 8.929 17.359 -19.134 0.70 14.70 C ANISOU 44 CA ACYS A 141 2019 1987 1578 -145 199 398 C ATOM 45 CA BCYS A 141 8.921 17.326 -19.130 0.30 15.74 C ANISOU 45 CA BCYS A 141 2081 1897 2003 -35 85 158 C ATOM 46 CA PRO A 142 8.930 21.041 -18.235 1.00 15.20 C ANISOU 46 CA PRO A 142 2118 1585 2071 94 180 88 C ATOM 47 CA VAL A 143 6.212 22.062 -15.811 1.00 12.68 C ANISOU 47 CA VAL A 143 1611 1510 1694 -165 -41 113 C ATOM 48 CA GLN A 144 5.887 25.754 -14.939 1.00 13.16 C ANISOU 48 CA GLN A 144 2025 1316 1656 -236 91 89 C ATOM 49 CA LEU A 145 4.836 27.068 -11.565 1.00 12.67 C ANISOU 49 CA LEU A 145 1720 1402 1692 -297 -2 56 C ATOM 50 CA TRP A 146 3.091 30.431 -11.590 1.00 14.97 C ANISOU 50 CA TRP A 146 2158 1274 2255 -173 -28 176 C ATOM 51 CA VAL A 147 2.219 32.364 -8.426 1.00 16.21 C ANISOU 51 CA VAL A 147 2369 1317 2472 -134 219 -61 C ATOM 52 CA ASP A 148 0.670 35.800 -7.817 1.00 20.85 C ANISOU 52 CA ASP A 148 3150 1738 3032 33 1 -122 C ATOM 53 CA ASER A 149 2.638 36.328 -4.588 0.50 25.24 C ANISOU 53 CA ASER A 149 3490 2684 3414 -98 13 -79 C ATOM 54 CA BSER A 149 2.592 36.312 -4.541 0.50 25.32 C ANISOU 54 CA BSER A 149 3501 2727 3393 -71 16 -78 C ATOM 55 CA THR A 150 5.817 34.914 -3.029 1.00 28.19 C ANISOU 55 CA THR A 150 3672 3213 3827 -245 -173 247 C ATOM 56 CA PRO A 151 5.261 31.693 -1.015 1.00 24.52 C ANISOU 56 CA PRO A 151 3156 2812 3346 -28 -281 -120 C ATOM 57 CA PRO A 152 6.733 31.579 2.532 1.00 24.39 C ANISOU 57 CA PRO A 152 3477 2866 2921 -168 -454 -503 C ATOM 58 CA PRO A 153 10.340 30.555 3.293 1.00 24.02 C ANISOU 58 CA PRO A 153 3324 2722 3079 -474 -187 -415 C ATOM 59 CA GLY A 154 10.923 26.835 2.947 1.00 20.30 C ANISOU 59 CA GLY A 154 2251 2945 2516 -917 -515 -341 C ATOM 60 CA THR A 155 7.986 26.228 0.606 1.00 15.13 C ANISOU 60 CA THR A 155 1961 1808 1980 -539 12 -403 C ATOM 61 CA ARG A 156 8.206 22.896 -1.193 1.00 14.33 C ANISOU 61 CA ARG A 156 1405 2098 1938 -317 -95 -329 C ATOM 62 CA VAL A 157 6.795 21.475 -4.416 1.00 11.15 C ANISOU 62 CA VAL A 157 1475 1495 1264 -291 -216 26 C ATOM 63 CA ARG A 158 5.523 17.876 -4.461 1.00 10.93 C ANISOU 63 CA ARG A 158 1414 1406 1333 -360 -115 107 C ATOM 64 CA ALA A 159 4.598 15.744 -7.470 1.00 10.85 C ANISOU 64 CA ALA A 159 1581 1131 1409 -284 -21 193 C ATOM 65 CA AMET A 160 2.576 12.543 -7.151 0.50 12.73 C ANISOU 65 CA AMET A 160 1788 1413 1635 -391 -276 98 C ATOM 66 CA BMET A 160 2.602 12.523 -7.178 0.50 10.50 C ANISOU 66 CA BMET A 160 1556 1013 1418 -312 -228 217 C ATOM 67 CA ALA A 161 0.762 10.318 -9.648 1.00 11.30 C ANISOU 67 CA ALA A 161 1644 1110 1539 -358 -278 94 C ATOM 68 CA ILE A 162 -2.699 8.798 -9.116 1.00 12.78 C ANISOU 68 CA ILE A 162 1788 1485 1583 -481 -133 42 C ATOM 69 CA TYR A 163 -5.026 6.898 -11.418 1.00 12.86 C ANISOU 69 CA TYR A 163 1527 1636 1724 -413 -109 62 C ATOM 70 CA LYS A 164 -7.638 9.136 -13.044 1.00 17.26 C ANISOU 70 CA LYS A 164 1749 2290 2518 -311 -145 134 C ATOM 71 CA GLN A 165 -10.464 6.581 -12.924 1.00 18.60 C ANISOU 71 CA GLN A 165 1971 2231 2862 -414 -240 -3 C ATOM 72 CA ASER A 166 -12.284 6.387 -9.590 0.50 20.94 C ANISOU 72 CA ASER A 166 2211 2476 3266 -61 154 -127 C ATOM 73 CA BSER A 166 -12.282 6.387 -9.590 0.50 21.82 C ANISOU 73 CA BSER A 166 2357 2612 3320 -94 162 -109 C ATOM 74 CA AGLN A 167 -12.383 2.582 -9.811 0.50 19.20 C ANISOU 74 CA AGLN A 167 2287 2018 2988 -324 43 -173 C ATOM 75 CA BGLN A 167 -12.382 2.581 -9.821 0.50 18.86 C ANISOU 75 CA BGLN A 167 2228 1938 2997 -374 68 -203 C ATOM 76 CA HIS A 168 -8.558 2.404 -9.774 1.00 16.15 C ANISOU 76 CA HIS A 168 2061 1887 2187 -107 295 -304 C ATOM 77 CA MET A 169 -7.790 5.367 -7.540 1.00 17.35 C ANISOU 77 CA MET A 169 2250 1982 2358 -513 285 -52 C ATOM 78 CA THR A 170 -6.872 3.321 -4.469 1.00 19.89 C ANISOU 78 CA THR A 170 2738 2633 2185 -161 423 240 C ATOM 79 CA GLU A 171 -4.136 1.598 -6.494 1.00 16.86 C ANISOU 79 CA GLU A 171 1996 2003 2407 -267 146 330 C ATOM 80 CA VAL A 172 -0.661 3.066 -6.030 1.00 13.92 C ANISOU 80 CA VAL A 172 1959 1480 1850 -135 161 174 C ATOM 81 CA VAL A 173 0.966 4.224 -9.262 1.00 13.02 C ANISOU 81 CA VAL A 173 2106 1071 1769 -53 65 26 C ATOM 82 CA ARG A 174 4.397 2.618 -9.542 1.00 15.82 C ANISOU 82 CA ARG A 174 2464 1803 1742 342 -25 -140 C ATOM 83 CA AARG A 175 6.776 1.338 -12.189 0.60 16.04 C ANISOU 83 CA AARG A 175 2812 1513 1770 378 188 -30 C ATOM 84 CA BARG A 175 6.767 1.339 -12.194 0.40 16.21 C ANISOU 84 CA BARG A 175 2658 1630 1870 326 189 -35 C ATOM 85 CA CYS A 176 6.101 -2.014 -13.843 1.00 16.55 C ANISOU 85 CA CYS A 176 2801 1377 2109 309 279 50 C ATOM 86 CA PRO A 177 8.169 -5.060 -12.809 1.00 21.19 C ANISOU 86 CA PRO A 177 3352 1922 2778 528 333 171 C ATOM 87 CA HIS A 178 10.433 -4.796 -15.874 1.00 20.14 C ANISOU 87 CA HIS A 178 2720 2571 2362 828 129 -142 C ATOM 88 CA HIS A 179 11.304 -1.128 -15.354 1.00 20.36 C ANISOU 88 CA HIS A 179 2835 2658 2241 -26 -259 175 C ATOM 89 CA GLU A 180 11.638 -1.467 -11.566 1.00 21.32 C ANISOU 89 CA GLU A 180 2919 2595 2584 425 -588 163 C ATOM 90 CA ARG A 181 14.340 -4.092 -12.220 1.00 27.19 C ANISOU 90 CA ARG A 181 3398 3403 3529 556 -323 315 C TER 91 ARG A 181 ATOM 92 CA LEU A 188 18.913 9.170 -6.117 1.00 24.27 C ANISOU 92 CA LEU A 188 2568 3432 3219 -179 -175 90 C ATOM 93 CA ALA A 189 15.522 7.823 -7.177 1.00 21.87 C ANISOU 93 CA ALA A 189 2531 2260 3518 73 -371 -5 C ATOM 94 CA PRO A 190 14.194 4.570 -5.748 1.00 21.25 C ANISOU 94 CA PRO A 190 2965 1775 3333 361 -540 -73 C ATOM 95 CA PRO A 191 13.655 2.152 -8.665 1.00 20.28 C ANISOU 95 CA PRO A 191 2500 1846 3357 778 -415 -268 C ATOM 96 CA GLN A 192 9.899 1.898 -8.002 1.00 17.45 C ANISOU 96 CA GLN A 192 2557 1472 2600 198 -192 316 C ATOM 97 CA HIS A 193 9.181 5.610 -8.477 1.00 13.90 C ANISOU 97 CA HIS A 193 2302 1273 1706 195 -258 163 C ATOM 98 CA LEU A 194 7.456 6.666 -11.692 1.00 12.50 C ANISOU 98 CA LEU A 194 1931 1255 1563 9 17 209 C ATOM 99 CA ILE A 195 8.267 10.387 -11.420 1.00 11.72 C ANISOU 99 CA ILE A 195 1449 1373 1628 -113 -1 39 C ATOM 100 CA ARG A 196 11.793 11.769 -11.161 1.00 12.51 C ANISOU 100 CA ARG A 196 1493 1453 1808 40 25 94 C ATOM 101 CA VAL A 197 13.167 15.304 -11.209 1.00 12.93 C ANISOU 101 CA VAL A 197 1423 1656 1833 -255 12 163 C ATOM 102 CA GLU A 198 16.242 16.212 -13.223 1.00 17.10 C ANISOU 102 CA GLU A 198 2000 2212 2284 -77 428 18 C ATOM 103 CA GLY A 199 18.423 19.328 -12.935 1.00 18.44 C ANISOU 103 CA GLY A 199 2255 2337 2411 -630 114 183 C ATOM 104 CA ASN A 200 17.828 19.842 -9.214 1.00 16.13 C ANISOU 104 CA ASN A 200 1481 2302 2342 -180 -98 278 C ATOM 105 CA LEU A 201 20.296 19.317 -6.362 1.00 15.56 C ANISOU 105 CA LEU A 201 1491 2271 2150 -290 -200 367 C ATOM 106 CA ARG A 202 17.689 19.072 -3.597 1.00 15.43 C ANISOU 106 CA ARG A 202 1491 2071 2300 -170 -211 -3 C ATOM 107 CA VAL A 203 15.359 16.301 -4.733 1.00 14.28 C ANISOU 107 CA VAL A 203 1201 2158 2066 -140 -108 104 C ATOM 108 CA GLU A 204 13.612 14.185 -2.105 1.00 14.45 C ANISOU 108 CA GLU A 204 1582 1823 2083 -122 -334 147 C ATOM 109 CA TYR A 205 12.066 10.847 -2.968 1.00 14.41 C ANISOU 109 CA TYR A 205 1828 1935 1709 -187 -259 369 C ATOM 110 CA LEU A 206 9.347 10.036 -0.491 1.00 15.47 C ANISOU 110 CA LEU A 206 2131 1992 1753 -389 -426 172 C ATOM 111 CA ASP A 207 7.329 6.930 0.285 1.00 19.61 C ANISOU 111 CA ASP A 207 3055 2302 2092 -545 -359 342 C ATOM 112 CA ASP A 208 4.196 7.543 2.375 1.00 23.20 C ANISOU 112 CA ASP A 208 3735 2656 2421 -383 136 291 C ATOM 113 CA ARG A 209 4.269 5.328 5.488 1.00 27.51 C ANISOU 113 CA ARG A 209 4396 3673 2381 -215 -203 754 C ATOM 114 CA ASN A 210 0.489 4.708 5.465 1.00 32.92 C ANISOU 114 CA ASN A 210 4448 4477 3581 -31 207 166 C ATOM 115 CA THR A 211 -0.550 4.822 1.789 1.00 24.88 C ANISOU 115 CA THR A 211 3324 3365 2765 37 415 420 C ATOM 116 CA PHE A 212 2.762 3.639 0.256 1.00 17.13 C ANISOU 116 CA PHE A 212 2787 1680 2040 -171 339 529 C ATOM 117 CA ARG A 213 2.338 6.306 -2.404 1.00 14.67 C ANISOU 117 CA ARG A 213 2515 1504 1551 -267 112 372 C ATOM 118 CA HIS A 214 5.443 7.767 -3.978 1.00 12.92 C ANISOU 118 CA HIS A 214 2065 1328 1514 -294 -302 248 C ATOM 119 CA SER A 215 6.199 11.404 -4.431 1.00 12.87 C ANISOU 119 CA SER A 215 1760 1202 1926 -353 -242 274 C ATOM 120 CA VAL A 216 9.084 13.604 -5.424 1.00 12.07 C ANISOU 120 CA VAL A 216 1618 1306 1659 -203 -237 213 C ATOM 121 CA VAL A 217 9.719 16.944 -3.753 1.00 11.42 C ANISOU 121 CA VAL A 217 1193 1462 1684 -208 -190 135 C ATOM 122 CA VAL A 218 11.952 19.924 -4.508 1.00 12.49 C ANISOU 122 CA VAL A 218 1233 1798 1711 -454 -89 85 C ATOM 123 CA PRO A 219 12.225 23.305 -2.813 1.00 13.12 C ANISOU 123 CA PRO A 219 1416 1533 2034 -344 32 59 C ATOM 124 CA TYR A 220 10.161 26.063 -4.351 1.00 13.76 C ANISOU 124 CA TYR A 220 1572 1626 2027 -478 47 -18 C ATOM 125 CA GLU A 221 12.453 28.601 -6.017 1.00 15.83 C ANISOU 125 CA GLU A 221 1678 1988 2346 -413 -156 383 C ATOM 126 CA APRO A 222 11.278 31.916 -7.448 0.50 15.12 C ANISOU 126 CA APRO A 222 2210 1183 2351 -355 -100 14 C ATOM 127 CA BPRO A 222 11.246 31.939 -7.423 0.50 20.89 C ANISOU 127 CA BPRO A 222 2773 2249 2914 -236 -115 53 C ATOM 128 CA PRO A 223 11.663 32.525 -11.197 1.00 17.62 C ANISOU 128 CA PRO A 223 2326 1805 2561 -676 -12 332 C ATOM 129 CA GLU A 224 15.209 33.137 -12.394 1.00 18.58 C ANISOU 129 CA GLU A 224 2251 1733 3073 -655 266 18 C ATOM 130 CA VAL A 225 16.076 36.689 -13.404 1.00 17.51 C ANISOU 130 CA VAL A 225 2427 1715 2510 -551 237 100 C ATOM 131 CA GLY A 226 14.596 37.108 -16.917 1.00 21.52 C ANISOU 131 CA GLY A 226 2874 2504 2796 -739 234 360 C ATOM 132 CA SER A 227 11.703 34.695 -16.276 1.00 17.60 C ANISOU 132 CA SER A 227 2436 1520 2731 -516 109 91 C ATOM 133 CA ASP A 228 8.075 34.967 -15.077 1.00 17.80 C ANISOU 133 CA ASP A 228 2353 1636 2772 -106 79 270 C ATOM 134 CA CYS A 229 7.704 31.406 -13.803 1.00 15.46 C ANISOU 134 CA CYS A 229 1874 1525 2473 -251 -73 96 C ATOM 135 CA THR A 230 9.575 28.577 -12.159 1.00 14.21 C ANISOU 135 CA THR A 230 1780 1519 2100 -163 -89 84 C ATOM 136 CA THR A 231 10.240 25.489 -14.242 1.00 14.46 C ANISOU 136 CA THR A 231 1883 1556 2053 -198 -35 294 C ATOM 137 CA ILE A 232 10.709 21.976 -12.910 1.00 13.33 C ANISOU 137 CA ILE A 232 1675 1538 1851 -317 -55 300 C ATOM 138 CA HIS A 233 11.933 19.235 -15.239 1.00 13.85 C ANISOU 138 CA HIS A 233 1892 1568 1801 -191 268 144 C ATOM 139 CA TYR A 234 10.079 16.007 -14.533 1.00 12.34 C ANISOU 139 CA TYR A 234 1563 1393 1731 -116 194 281 C ATOM 140 CA ASN A 235 10.889 12.612 -16.020 1.00 13.00 C ANISOU 140 CA ASN A 235 1770 1407 1762 141 161 71 C ATOM 141 CA TYR A 236 8.377 9.740 -16.230 1.00 13.00 C ANISOU 141 CA TYR A 236 1834 1373 1729 82 -10 123 C ATOM 142 CA MET A 237 10.092 6.385 -16.017 1.00 15.20 C ANISOU 142 CA MET A 237 2210 1433 2129 358 40 -133 C ATOM 143 CA ACYS A 238 7.384 3.986 -17.215 0.50 17.98 C ANISOU 143 CA ACYS A 238 2471 1982 2378 -39 199 14 C ATOM 144 CA BCYS A 238 7.433 3.987 -17.301 0.50 14.12 C ANISOU 144 CA BCYS A 238 2203 1365 1796 -32 491 68 C ATOM 145 CA AASN A 239 5.096 4.070 -20.280 0.50 17.17 C ANISOU 145 CA AASN A 239 2404 1870 2250 -152 231 -305 C ATOM 146 CA BASN A 239 5.096 4.060 -20.286 0.50 17.56 C ANISOU 146 CA BASN A 239 2480 1888 2302 -151 193 -293 C ATOM 147 CA SER A 240 1.324 4.335 -19.824 1.00 16.37 C ANISOU 147 CA SER A 240 2376 1483 2359 -158 -181 209 C ATOM 148 CA SER A 241 1.088 1.061 -21.750 1.00 19.83 C ANISOU 148 CA SER A 241 3108 2005 2418 76 -124 -333 C ATOM 149 CA CYS A 242 3.389 -0.863 -19.399 1.00 19.30 C ANISOU 149 CA CYS A 242 2245 2192 2894 -20 19 305 C ATOM 150 CA MET A 243 1.487 -3.998 -18.403 1.00 21.53 C ANISOU 150 CA MET A 243 2898 2487 2794 -272 -80 -200 C ATOM 151 CA GLY A 244 1.790 -4.971 -14.739 1.00 26.23 C ANISOU 151 CA GLY A 244 3934 2561 3470 -14 81 40 C ATOM 152 CA GLY A 245 1.819 -1.232 -14.081 1.00 25.39 C ANISOU 152 CA GLY A 245 3553 2532 3562 477 -133 -283 C ATOM 153 CA MET A 246 -0.400 1.503 -15.489 1.00 20.40 C ANISOU 153 CA MET A 246 2734 2238 2776 -87 50 65 C ATOM 154 CA ASN A 247 -1.951 -0.983 -17.943 1.00 21.15 C ANISOU 154 CA ASN A 247 2801 2407 2826 -236 95 -184 C ATOM 155 CA ARG A 248 -2.937 1.756 -20.455 1.00 22.84 C ANISOU 155 CA ARG A 248 3012 3138 2527 103 -440 -103 C ATOM 156 CA SER A 249 -5.048 3.413 -17.728 1.00 22.44 C ANISOU 156 CA SER A 249 3376 2347 2801 34 -288 -331 C ATOM 157 CA APRO A 250 -4.822 7.238 -17.509 0.50 17.99 C ANISOU 157 CA APRO A 250 2737 2207 1891 -216 -538 -152 C ATOM 158 CA BPRO A 250 -4.794 7.226 -17.510 0.50 17.79 C ANISOU 158 CA BPRO A 250 2756 2215 1786 -159 -629 -103 C ATOM 159 CA ILE A 251 -2.939 8.864 -14.664 1.00 13.11 C ANISOU 159 CA ILE A 251 1871 1517 1593 -338 -413 97 C ATOM 160 CA LEU A 252 -2.970 12.321 -13.167 1.00 13.25 C ANISOU 160 CA LEU A 252 2106 1313 1614 -418 -417 204 C ATOM 161 CA THR A 253 0.048 14.149 -11.856 1.00 10.67 C ANISOU 161 CA THR A 253 1587 1042 1422 -216 -84 50 C ATOM 162 CA AILE A 254 -0.825 16.211 -8.788 0.50 10.82 C ANISOU 162 CA AILE A 254 1396 1265 1448 -235 -4 65 C ATOM 163 CA BILE A 254 -0.827 16.213 -8.790 0.50 11.21 C ANISOU 163 CA BILE A 254 1448 1331 1481 -262 -53 38 C ATOM 164 CA ILE A 255 1.447 19.175 -8.056 1.00 10.71 C ANISOU 164 CA ILE A 255 1379 1356 1333 -192 -69 -70 C ATOM 165 CA ATHR A 256 1.199 20.518 -4.512 0.50 11.72 C ANISOU 165 CA ATHR A 256 1255 1526 1672 -199 73 -86 C ATOM 166 CA BTHR A 256 1.184 20.605 -4.571 0.50 12.80 C ANISOU 166 CA BTHR A 256 1501 1690 1670 -345 25 -109 C ATOM 167 CA LEU A 257 2.726 23.680 -3.093 1.00 12.08 C ANISOU 167 CA LEU A 257 1411 1547 1630 -280 79 -59 C ATOM 168 CA GLU A 258 3.409 23.021 0.591 1.00 13.77 C ANISOU 168 CA GLU A 258 1639 1701 1891 -366 -257 -179 C ATOM 169 CA ASP A 259 4.843 25.055 3.444 1.00 16.74 C ANISOU 169 CA ASP A 259 1651 2746 1964 -342 -156 -548 C ATOM 170 CA SER A 260 7.916 23.943 5.421 1.00 21.39 C ANISOU 170 CA SER A 260 1462 3905 2760 -181 -416 -178 C ATOM 171 CA ASER A 261 5.672 22.012 7.847 0.70 22.47 C ANISOU 171 CA ASER A 261 2317 3785 2434 -186 -376 86 C ATOM 172 CA BSER A 261 5.698 21.994 7.843 0.30 23.52 C ANISOU 172 CA BSER A 261 2572 3588 2773 -139 -238 86 C ATOM 173 CA GLY A 262 3.956 20.165 4.978 1.00 20.37 C ANISOU 173 CA GLY A 262 1513 3150 3075 209 -198 13 C ATOM 174 CA ASN A 263 0.710 22.144 5.019 1.00 16.26 C ANISOU 174 CA ASN A 263 1655 2652 1871 -136 -356 93 C ATOM 175 CA LEU A 264 -1.167 22.607 1.781 1.00 14.00 C ANISOU 175 CA LEU A 264 1616 1994 1710 -311 38 81 C ATOM 176 CA LEU A 265 -0.710 25.990 0.100 1.00 13.69 C ANISOU 176 CA LEU A 265 1950 1553 1696 -186 -108 -189 C ATOM 177 CA GLY A 266 -1.944 25.155 -3.393 1.00 12.81 C ANISOU 177 CA GLY A 266 1705 1608 1554 -88 -71 -82 C ATOM 178 CA AARG A 267 -2.773 22.289 -5.731 0.50 11.43 C ANISOU 178 CA AARG A 267 1479 1475 1387 -38 -55 -50 C ATOM 179 CA BARG A 267 -2.723 22.268 -5.731 0.50 12.75 C ANISOU 179 CA BARG A 267 1565 1564 1714 -52 49 -87 C ATOM 180 CA ASN A 268 -3.069 21.701 -9.459 1.00 11.33 C ANISOU 180 CA ASN A 268 1541 1379 1384 -97 6 11 C ATOM 181 CA SER A 269 -3.114 18.597 -11.634 1.00 13.31 C ANISOU 181 CA SER A 269 2004 1505 1544 8 -131 10 C ATOM 182 CA PHE A 270 -2.837 17.401 -15.191 1.00 12.07 C ANISOU 182 CA PHE A 270 2076 1274 1233 1 -228 13 C ATOM 183 CA GLU A 271 -3.410 14.107 -16.937 1.00 12.29 C ANISOU 183 CA GLU A 271 1961 1274 1435 -201 -206 129 C ATOM 184 CA AVAL A 272 -0.306 12.382 -18.353 0.50 11.69 C ANISOU 184 CA AVAL A 272 2405 957 1080 15 -187 171 C ATOM 185 CA BVAL A 272 -0.351 12.429 -18.419 0.50 13.48 C ANISOU 185 CA BVAL A 272 2359 1281 1481 135 -138 -191 C ATOM 186 CA ARG A 273 0.240 9.837 -21.108 1.00 13.76 C ANISOU 186 CA ARG A 273 2354 1351 1523 189 -89 -30 C ATOM 187 CA VAL A 274 3.757 8.498 -21.370 1.00 16.12 C ANISOU 187 CA VAL A 274 2793 1598 1732 88 85 -51 C ATOM 188 CA CYS A 275 4.079 7.203 -24.908 1.00 18.83 C ANISOU 188 CA CYS A 275 3255 2041 1857 -90 344 -309 C ATOM 189 CA ALA A 276 6.433 6.693 -27.852 1.00 22.16 C ANISOU 189 CA ALA A 276 3199 2831 2390 260 519 -99 C ATOM 190 CA ACYS A 277 4.822 9.300 -30.109 0.50 19.76 C ANISOU 190 CA ACYS A 277 2859 2955 1692 -73 6 -197 C ATOM 191 CA BCYS A 277 4.831 9.321 -30.094 0.50 21.92 C ANISOU 191 CA BCYS A 277 3188 3100 2041 -4 36 -144 C ATOM 192 CA PRO A 278 3.423 12.208 -27.993 1.00 19.04 C ANISOU 192 CA PRO A 278 2701 2921 1613 -182 -5 -139 C ATOM 193 CA GLY A 279 2.523 14.444 -30.950 1.00 21.74 C ANISOU 193 CA GLY A 279 3129 2940 2188 -653 -360 231 C ATOM 194 CA ARG A 280 0.625 11.682 -32.704 1.00 22.12 C ANISOU 194 CA ARG A 280 3118 3356 1929 -620 -141 -165 C ATOM 195 CA ASP A 281 -1.227 10.547 -29.590 1.00 18.76 C ANISOU 195 CA ASP A 281 2659 2396 2070 -278 188 -49 C ATOM 196 CA AARG A 282 -2.182 14.122 -28.685 0.50 16.62 C ANISOU 196 CA AARG A 282 2818 1966 1529 -418 -298 -28 C ATOM 197 CA BARG A 282 -2.180 14.126 -28.684 0.50 19.89 C ANISOU 197 CA BARG A 282 3038 2432 2087 -280 -230 -56 C ATOM 198 CA ARG A 283 -3.607 14.600 -32.174 1.00 23.93 C ANISOU 198 CA ARG A 283 3323 3321 2446 -230 -576 -190 C ATOM 199 CA THR A 284 -5.544 11.315 -31.925 1.00 25.20 C ANISOU 199 CA THR A 284 2884 3280 3412 -161 -284 -581 C ATOM 200 CA GLU A 285 -6.957 12.062 -28.451 1.00 23.16 C ANISOU 200 CA GLU A 285 3063 2540 3195 47 -222 -94 C ATOM 201 CA GLU A 286 -7.874 15.597 -29.565 1.00 25.35 C ANISOU 201 CA GLU A 286 3512 2865 3253 60 -308 -31 C ATOM 202 CA GLU A 287 -9.616 14.270 -32.692 1.00 34.99 C ANISOU 202 CA GLU A 287 4245 4798 4252 212 -378 -231 C ATOM 203 CA ASN A 288 -11.555 11.828 -30.479 1.00 39.17 C ANISOU 203 CA ASN A 288 4759 5055 5067 74 -8 39 C END If you find results from this site helpful for your research, please cite one of our papers:
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