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*** ***elNémo ID: 2404111543003695203Job options:ID = 2404111543003695203 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 94 5.280 2.932 -11.544 1.00 33.63 C ANISOU 1 CA SER A 94 5202 5048 2527 43 -709 242 C ATOM 2 CA SER A 95 9.017 2.978 -10.849 1.00 39.80 C ANISOU 2 CA SER A 95 5954 5993 3175 121 -284 213 C ATOM 3 CA SER A 96 9.662 0.206 -8.335 1.00 37.66 C ANISOU 3 CA SER A 96 5719 5335 3255 201 -225 -264 C ATOM 4 CA VAL A 97 12.940 1.840 -7.338 1.00 30.01 C ANISOU 4 CA VAL A 97 4622 4450 2330 193 123 -20 C ATOM 5 CA PRO A 98 12.469 4.114 -4.286 1.00 27.95 C ANISOU 5 CA PRO A 98 4243 3777 2600 53 122 215 C ATOM 6 CA SER A 99 13.910 7.604 -4.632 1.00 31.43 C ANISOU 6 CA SER A 99 4486 4220 3235 -52 199 667 C ATOM 7 CA GLN A 100 16.706 8.482 -2.229 1.00 38.46 C ANISOU 7 CA GLN A 100 5229 4913 4471 -86 315 642 C ATOM 8 CA LYS A 101 16.679 12.265 -2.399 1.00 37.32 C ANISOU 8 CA LYS A 101 4832 4510 4837 -225 193 1048 C ATOM 9 CA THR A 102 16.864 13.924 1.023 1.00 32.38 C ANISOU 9 CA THR A 102 4098 3423 4780 -254 46 727 C ATOM 10 CA TYR A 103 13.877 16.134 1.706 1.00 31.79 C ANISOU 10 CA TYR A 103 3925 2979 5174 -246 -155 628 C ATOM 11 CA GLN A 104 13.433 17.402 5.236 1.00 28.17 C ANISOU 11 CA GLN A 104 3391 2225 5088 -172 -261 22 C ATOM 12 CA GLY A 105 9.863 18.381 4.395 1.00 25.05 C ANISOU 12 CA GLY A 105 2912 1680 4927 -104 -327 60 C ATOM 13 CA SER A 106 7.460 20.834 5.988 1.00 30.94 C ANISOU 13 CA SER A 106 3391 2242 6123 26 -424 -310 C ATOM 14 CA TYR A 107 7.849 19.160 9.389 1.00 28.02 C ANISOU 14 CA TYR A 107 3198 2154 5294 131 -245 -911 C ATOM 15 CA GLY A 108 11.629 19.471 9.440 1.00 32.45 C ANISOU 15 CA GLY A 108 3785 2668 5878 17 -357 -821 C ATOM 16 CA PHE A 109 12.505 15.795 9.397 1.00 22.43 C ANISOU 16 CA PHE A 109 2818 1765 3940 -25 -160 -716 C ATOM 17 CA ARG A 110 16.150 15.142 10.276 1.00 28.52 C ANISOU 17 CA ARG A 110 3613 2637 4586 -108 -218 -704 C ATOM 18 CA LEU A 111 18.176 12.157 11.518 1.00 20.46 C ANISOU 18 CA LEU A 111 2742 1987 3047 -126 -142 -670 C ATOM 19 CA GLY A 112 20.554 12.078 14.465 1.00 19.22 C ANISOU 19 CA GLY A 112 2545 1971 2786 -152 -332 -948 C ATOM 20 CA PHE A 113 23.207 9.533 15.419 1.00 17.83 C ANISOU 20 CA PHE A 113 2388 2031 2357 -202 -380 -744 C ATOM 21 CA LEU A 114 24.882 8.802 18.730 1.00 22.22 C ANISOU 21 CA LEU A 114 2923 2896 2622 -236 -643 -917 C ATOM 22 CA HIS A 115 28.457 9.932 19.074 1.00 28.00 C ANISOU 22 CA HIS A 115 3438 3414 3789 -339 -961 -907 C ATOM 23 CA SER A 116 30.703 6.885 18.901 1.00 29.17 C ANISOU 23 CA SER A 116 3506 3671 3905 -365 -949 -449 C ATOM 24 CA GLY A 117 34.361 6.167 18.481 1.00 33.42 C ANISOU 24 CA GLY A 117 3748 4041 4909 -425 -1099 -147 C ATOM 25 CA THR A 118 36.224 3.580 16.472 1.00 24.01 C ANISOU 25 CA THR A 118 2364 2749 4011 -343 -861 258 C ATOM 26 CA ALA A 119 37.145 1.238 19.310 1.00 29.05 C ANISOU 26 CA ALA A 119 2958 3589 4492 -375 -1210 424 C ATOM 27 CA LYS A 120 37.497 -2.257 17.869 1.00 30.39 C ANISOU 27 CA LYS A 120 3015 3625 4907 -227 -998 716 C ATOM 28 CA SER A 121 34.809 -3.575 20.242 1.00 29.46 C ANISOU 28 CA SER A 121 3142 3817 4234 -289 -1152 814 C ATOM 29 CA VAL A 122 32.122 -1.031 19.269 1.00 21.83 C ANISOU 29 CA VAL A 122 2463 2930 2900 -283 -893 419 C ATOM 30 CA THR A 123 28.994 -2.758 18.041 1.00 19.33 C ANISOU 30 CA THR A 123 2325 2601 2418 -208 -627 464 C ATOM 31 CA CYS A 124 27.611 0.289 16.249 1.00 17.13 C ANISOU 31 CA CYS A 124 2191 2249 2067 -187 -413 119 C ATOM 32 CA THR A 125 29.392 3.417 14.986 1.00 24.86 C ANISOU 32 CA THR A 125 3052 3037 3356 -224 -415 -23 C ATOM 33 CA TYR A 126 28.325 6.314 12.746 1.00 18.44 C ANISOU 33 CA TYR A 126 2245 2038 2724 -235 -266 -107 C ATOM 34 CA SER A 127 30.723 8.290 10.539 1.00 18.91 C ANISOU 34 CA SER A 127 2016 1892 3276 -295 -201 141 C ATOM 35 CA PRO A 128 29.414 11.838 9.954 1.00 21.51 C ANISOU 35 CA PRO A 128 2276 1951 3946 -383 -308 101 C ATOM 36 CA ALA A 129 32.044 12.326 7.223 1.00 30.69 C ANISOU 36 CA ALA A 129 3096 3104 5463 -440 -104 645 C ATOM 37 CA LEU A 130 30.750 9.314 5.284 1.00 24.07 C ANISOU 37 CA LEU A 130 2507 2644 3992 -261 262 655 C ATOM 38 CA ASN A 131 27.159 9.571 6.496 1.00 22.46 C ANISOU 38 CA ASN A 131 2625 2372 3538 -245 125 334 C ATOM 39 CA LYS A 132 27.595 5.889 6.997 1.00 15.84 C ANISOU 39 CA LYS A 132 1913 1732 2373 -123 222 217 C ATOM 40 CA MET A 133 26.661 3.541 9.781 1.00 18.03 C ANISOU 40 CA MET A 133 2337 2063 2448 -98 64 33 C ATOM 41 CA PHE A 134 28.971 0.658 10.598 1.00 18.63 C ANISOU 41 CA PHE A 134 2278 2148 2652 -41 8 135 C ATOM 42 CA CYS A 135 27.458 -2.097 12.672 1.00 17.25 C ANISOU 42 CA CYS A 135 2191 2023 2339 -40 -145 195 C ATOM 43 CA GLN A 136 27.707 -5.708 13.692 1.00 23.33 C ANISOU 43 CA GLN A 136 2849 2697 3319 -2 -294 418 C ATOM 44 CA LEU A 137 25.242 -8.425 12.708 1.00 18.79 C ANISOU 44 CA LEU A 137 2320 1935 2886 57 -290 442 C ATOM 45 CA ALA A 138 22.023 -8.612 14.800 1.00 23.86 C ANISOU 45 CA ALA A 138 3044 2777 3244 -84 -357 682 C ATOM 46 CA LYS A 139 23.212 -5.718 16.942 1.00 26.82 C ANISOU 46 CA LYS A 139 3469 3527 3194 -164 -375 617 C ATOM 47 CA THR A 140 21.131 -2.684 17.791 1.00 27.27 C ANISOU 47 CA THR A 140 3679 3868 2815 -190 -252 335 C ATOM 48 CA CYS A 141 21.791 0.704 16.087 1.00 23.05 C ANISOU 48 CA CYS A 141 3211 3165 2382 -153 -171 -45 C ATOM 49 CA PRO A 142 20.066 3.644 17.798 1.00 21.79 C ANISOU 49 CA PRO A 142 3093 3195 1990 -148 -174 -406 C ATOM 50 CA VAL A 143 19.032 6.222 15.221 1.00 23.12 C ANISOU 50 CA VAL A 143 3272 3016 2498 -112 -78 -575 C ATOM 51 CA GLN A 144 17.503 9.522 16.298 1.00 24.27 C ANISOU 51 CA GLN A 144 3356 3089 2775 -59 -132 -1020 C ATOM 52 CA LEU A 145 14.507 10.817 14.413 1.00 27.06 C ANISOU 52 CA LEU A 145 3684 3213 3386 2 -5 -1026 C ATOM 53 CA TRP A 146 13.916 14.549 14.836 1.00 26.22 C ANISOU 53 CA TRP A 146 3393 2774 3795 66 -153 -1410 C ATOM 54 CA VAL A 147 10.867 16.516 13.675 1.00 29.87 C ANISOU 54 CA VAL A 147 3701 2977 4670 153 -118 -1417 C ATOM 55 CA ASP A 148 10.924 20.305 13.996 1.00 28.90 C ANISOU 55 CA ASP A 148 3282 2502 5198 199 -345 -1620 C ATOM 56 CA SER A 149 7.160 20.697 13.772 1.00 30.44 C ANISOU 56 CA SER A 149 3360 2687 5518 317 -213 -1698 C ATOM 57 CA THR A 150 4.575 18.244 15.050 1.00 34.98 C ANISOU 57 CA THR A 150 4038 3689 5563 417 95 -1799 C ATOM 58 CA PRO A 151 3.282 16.017 12.186 1.00 21.93 C ANISOU 58 CA PRO A 151 2484 1918 3929 345 169 -1328 C ATOM 59 CA PRO A 152 -0.359 14.985 11.664 1.00 31.75 C ANISOU 59 CA PRO A 152 3576 3205 5283 421 320 -1199 C ATOM 60 CA PRO A 153 -1.800 12.038 13.675 1.00 36.67 C ANISOU 60 CA PRO A 153 4194 4396 5341 434 618 -1130 C ATOM 61 CA GLY A 154 -1.019 8.599 12.274 1.00 18.39 C ANISOU 61 CA GLY A 154 2109 2177 2702 235 533 -609 C ATOM 62 CA THR A 155 2.359 9.692 10.991 1.00 18.96 C ANISOU 62 CA THR A 155 2404 2044 2755 174 346 -655 C ATOM 63 CA ARG A 156 4.966 6.953 10.761 1.00 27.65 C ANISOU 63 CA ARG A 156 3135 3374 3995 1784 303 -113 C ATOM 64 CA PHE A 157 8.666 6.354 10.168 1.00 30.66 C ANISOU 64 CA PHE A 157 3941 3519 4188 1115 -70 -346 C ATOM 65 CA ARG A 158 9.504 3.736 7.508 1.00 17.52 C ANISOU 65 CA ARG A 158 1906 2193 2557 636 -374 -147 C ATOM 66 CA ALA A 159 12.969 2.190 7.168 1.00 18.29 C ANISOU 66 CA ALA A 159 2126 2260 2564 183 -509 -309 C ATOM 67 CA MET A 160 13.889 0.472 3.917 1.00 12.95 C ANISOU 67 CA MET A 160 1343 1746 1833 -60 -592 -228 C ATOM 68 CA ALA A 161 17.203 -0.723 2.535 1.00 23.14 C ANISOU 68 CA ALA A 161 2638 3056 3097 -265 -474 -311 C ATOM 69 CA ILE A 162 18.220 -0.279 -1.095 1.00 19.12 C ANISOU 69 CA ILE A 162 2286 2664 2315 -360 -294 -193 C ATOM 70 CA TYR A 163 21.422 -0.963 -3.007 1.00 24.28 C ANISOU 70 CA TYR A 163 2879 3461 2884 -425 156 -187 C ATOM 71 CA LYS A 164 23.653 2.076 -3.225 1.00 22.37 C ANISOU 71 CA LYS A 164 2475 3136 2887 -711 381 172 C ATOM 72 CA GLN A 165 25.123 1.180 -6.626 1.00 28.03 C ANISOU 72 CA GLN A 165 3307 4204 3140 -653 1000 296 C ATOM 73 CA SER A 166 23.086 2.260 -9.631 1.00 38.82 C ANISOU 73 CA SER A 166 5354 5690 3705 -623 973 560 C ATOM 74 CA GLN A 167 23.758 -1.086 -11.302 1.00 34.59 C ANISOU 74 CA GLN A 167 5034 5464 2646 -359 1337 60 C ATOM 75 CA HIS A 168 22.079 -2.979 -8.419 1.00 27.39 C ANISOU 75 CA HIS A 168 3895 4250 2262 -292 738 -354 C ATOM 76 CA MET A 169 19.339 -0.453 -7.527 1.00 24.35 C ANISOU 76 CA MET A 169 3534 3751 1966 -418 146 -23 C ATOM 77 CA THR A 170 16.526 -2.515 -9.091 1.00 30.17 C ANISOU 77 CA THR A 170 4608 4682 2175 -426 -321 -318 C ATOM 78 CA GLU A 171 17.422 -5.487 -6.872 1.00 31.38 C ANISOU 78 CA GLU A 171 4543 4546 2834 -392 -185 -763 C ATOM 79 CA VAL A 172 15.386 -6.001 -3.692 1.00 18.62 C ANISOU 79 CA VAL A 172 2543 2748 1783 -450 -543 -718 C ATOM 80 CA VAL A 173 17.632 -6.086 -0.615 1.00 17.06 C ANISOU 80 CA VAL A 173 2041 2365 2075 -291 -310 -652 C ATOM 81 CA ARG A 174 16.993 -9.327 1.281 1.00 22.76 C ANISOU 81 CA ARG A 174 2773 2808 3068 -275 -362 -775 C ATOM 82 CA ARG A 175 18.661 -11.607 3.783 1.00 21.01 C ANISOU 82 CA ARG A 175 2486 2307 3189 -40 -258 -686 C ATOM 83 CA CYS A 176 20.686 -14.467 2.350 1.00 21.22 C ANISOU 83 CA CYS A 176 2757 1944 3362 271 49 -922 C ATOM 84 CA PRO A 177 18.983 -17.899 2.211 1.00 27.29 C ANISOU 84 CA PRO A 177 4058 2005 4307 124 19 -1118 C ATOM 85 CA HIS A 178 21.241 -19.355 4.927 1.00 28.05 C ANISOU 85 CA HIS A 178 3978 1847 4832 675 127 -690 C ATOM 86 CA HIS A 179 20.247 -16.757 7.494 1.00 27.52 C ANISOU 86 CA HIS A 179 3500 2389 4568 436 -184 -299 C ATOM 87 CA GLU A 180 16.599 -16.744 6.397 1.00 27.36 C ANISOU 87 CA GLU A 180 3659 2304 4432 -161 -275 -464 C ATOM 88 CA ARG A 181 16.302 -20.438 7.368 1.00 38.82 C ANISOU 88 CA ARG A 181 5528 2944 6277 -184 -173 -300 C ATOM 89 CA CYS A 182 18.397 -20.279 10.547 1.00 42.36 C ANISOU 89 CA CYS A 182 5793 3580 6721 351 -185 269 C ATOM 90 CA SER A 183 15.242 -19.584 12.576 1.00 29.81 C ANISOU 90 CA SER A 183 4123 2261 4941 -131 -175 619 C ATOM 91 CA ASP A 184 16.166 -16.409 14.475 1.00 33.30 C ANISOU 91 CA ASP A 184 4301 3469 4881 125 -313 681 C ATOM 92 CA SER A 185 12.941 -14.421 14.083 1.00 29.75 C ANISOU 92 CA SER A 185 3620 3373 4309 -227 -164 559 C ATOM 93 CA ASP A 186 11.620 -12.659 17.183 1.00 27.30 C ANISOU 93 CA ASP A 186 3329 3536 3510 -73 65 806 C ATOM 94 CA GLY A 187 8.226 -14.112 16.322 1.00 25.90 C ANISOU 94 CA GLY A 187 2790 3289 3761 -525 364 1043 C ATOM 95 CA LEU A 188 7.284 -10.868 14.520 1.00 29.22 C ANISOU 95 CA LEU A 188 2870 4071 4163 -381 246 643 C ATOM 96 CA ALA A 189 10.043 -10.081 11.997 1.00 17.21 C ANISOU 96 CA ALA A 189 1562 2338 2638 -314 -168 211 C ATOM 97 CA PRO A 190 9.712 -12.187 8.809 1.00 24.92 C ANISOU 97 CA PRO A 190 2538 3022 3907 -697 -394 13 C ATOM 98 CA PRO A 191 12.892 -14.301 8.471 1.00 19.75 C ANISOU 98 CA PRO A 191 2293 1902 3309 -522 -386 -127 C ATOM 99 CA GLN A 192 13.797 -12.779 5.048 1.00 29.83 C ANISOU 99 CA GLN A 192 3615 3330 4390 -510 -499 -535 C ATOM 100 CA HIS A 193 13.837 -9.202 6.367 1.00 20.39 C ANISOU 100 CA HIS A 193 2175 2544 3029 -324 -510 -375 C ATOM 101 CA LEU A 194 17.204 -7.468 6.670 1.00 13.68 C ANISOU 101 CA LEU A 194 1309 1758 2132 -124 -484 -420 C ATOM 102 CA ILE A 195 16.065 -4.583 8.859 1.00 21.62 C ANISOU 102 CA ILE A 195 2333 2882 3000 -76 -550 -362 C ATOM 103 CA ARG A 196 14.419 -5.206 12.239 1.00 20.33 C ANISOU 103 CA ARG A 196 2260 2809 2654 56 -455 -225 C ATOM 104 CA VAL A 197 13.400 -2.882 15.054 1.00 22.42 C ANISOU 104 CA VAL A 197 2796 3175 2548 280 -327 -316 C ATOM 105 CA GLU A 198 13.801 -3.645 18.739 1.00 20.36 C ANISOU 105 CA GLU A 198 2902 3108 1725 422 -288 -237 C ATOM 106 CA GLY A 199 12.354 -1.832 21.745 1.00 26.48 C ANISOU 106 CA GLY A 199 4199 4047 1815 743 45 -424 C ATOM 107 CA ASN A 200 9.217 -0.642 19.999 1.00 29.00 C ANISOU 107 CA ASN A 200 4105 4321 2593 971 541 -375 C ATOM 108 CA LEU A 201 5.753 -2.008 20.864 1.00 35.65 C ANISOU 108 CA LEU A 201 4467 5555 3522 1165 1257 81 C ATOM 109 CA ARG A 202 4.123 -0.990 17.583 1.00 28.38 C ANISOU 109 CA ARG A 202 2873 4567 3341 1176 1109 139 C ATOM 110 CA VAL A 203 6.480 -2.296 14.893 1.00 21.45 C ANISOU 110 CA VAL A 203 2007 3431 2711 652 431 66 C ATOM 111 CA GLU A 204 5.140 -3.515 11.547 1.00 26.85 C ANISOU 111 CA GLU A 204 4156 3722 2323 832 1079 1328 C ATOM 112 CA TYR A 205 6.954 -5.412 8.833 1.00 19.46 C ANISOU 112 CA TYR A 205 3121 2076 2197 163 269 1075 C ATOM 113 CA LEU A 206 6.010 -4.948 5.186 1.00 20.10 C ANISOU 113 CA LEU A 206 2945 2282 2410 319 161 976 C ATOM 114 CA ASP A 207 6.587 -6.812 1.910 1.00 22.68 C ANISOU 114 CA ASP A 207 3131 2506 2981 -237 -484 455 C ATOM 115 CA ASP A 208 5.295 -4.428 -0.741 1.00 26.25 C ANISOU 115 CA ASP A 208 3465 3697 2810 173 -249 807 C ATOM 116 CA ARG A 209 2.801 -6.251 -2.947 1.00 38.61 C ANISOU 116 CA ARG A 209 4365 6163 4141 -520 -1086 1130 C ATOM 117 CA ASN A 210 3.982 -4.594 -6.165 1.00 35.04 C ANISOU 117 CA ASN A 210 4237 6230 2846 -422 -961 857 C ATOM 118 CA THR A 211 7.709 -3.989 -5.545 1.00 30.21 C ANISOU 118 CA THR A 211 4357 4656 2466 -97 -322 -13 C ATOM 119 CA PHE A 212 8.520 -6.950 -3.273 1.00 22.66 C ANISOU 119 CA PHE A 212 3494 2740 2375 -440 -626 -685 C ATOM 120 CA ARG A 213 10.628 -4.549 -1.220 1.00 34.64 C ANISOU 120 CA ARG A 213 5375 3663 4123 67 7 -451 C ATOM 121 CA HIS A 214 10.721 -4.934 2.564 1.00 16.64 C ANISOU 121 CA HIS A 214 2353 833 3136 -52 425 25 C ATOM 122 CA SER A 215 10.464 -2.228 5.139 1.00 14.54 C ANISOU 122 CA SER A 215 1621 792 3112 -32 285 -9 C ATOM 123 CA VAL A 216 9.829 -1.791 8.818 1.00 20.19 C ANISOU 123 CA VAL A 216 2464 1547 3659 153 -75 67 C ATOM 124 CA VAL A 217 7.566 0.900 10.255 1.00 15.32 C ANISOU 124 CA VAL A 217 1706 1280 2836 -137 136 -50 C ATOM 125 CA VAL A 218 6.958 2.521 13.633 1.00 20.21 C ANISOU 125 CA VAL A 218 2477 2316 2887 -26 66 -384 C ATOM 126 CA PRO A 219 4.428 5.256 14.500 1.00 27.24 C ANISOU 126 CA PRO A 219 3169 3334 3845 -180 655 -711 C ATOM 127 CA TYR A 220 5.450 8.778 15.251 1.00 28.39 C ANISOU 127 CA TYR A 220 2964 3410 4411 -85 511 -1578 C ATOM 128 CA GLU A 221 4.737 9.756 18.847 1.00 40.59 C ANISOU 128 CA GLU A 221 5152 5300 4971 78 727 -2222 C ATOM 129 CA PRO A 222 5.368 13.140 20.469 1.00 47.72 C ANISOU 129 CA PRO A 222 6161 6019 5953 164 564 -3070 C ATOM 130 CA PRO A 223 8.597 12.944 22.511 1.00 62.52 C ANISOU 130 CA PRO A 223 8638 8062 7054 86 -484 -3376 C ATOM 131 CA GLU A 224 8.266 12.729 26.311 1.00 84.72 C ANISOU 131 CA GLU A 224 12710 11249 8229 -46 -445 -3759 C ATOM 132 CA VAL A 225 8.408 15.617 28.792 1.00 95.10 C ANISOU 132 CA VAL A 225 14857 12273 9003 -179 -423 -4546 C ATOM 133 CA GLY A 226 12.144 15.030 29.163 1.00101.56 C ANISOU 133 CA GLY A 226 15471 13300 9816 -657 -1800 -4313 C ATOM 134 CA SER A 227 12.889 13.620 25.695 1.00 88.23 C ANISOU 134 CA SER A 227 12610 11442 9472 -286 -2010 -3599 C ATOM 135 CA ASP A 228 13.732 15.740 22.628 1.00 67.14 C ANISOU 135 CA ASP A 228 8822 8283 8406 -154 -1995 -3433 C ATOM 136 CA CYS A 229 13.441 13.209 19.764 1.00 47.18 C ANISOU 136 CA CYS A 229 5617 5822 6488 37 -1727 -2787 C ATOM 137 CA THR A 230 12.542 9.669 18.800 1.00 35.07 C ANISOU 137 CA THR A 230 5620 4158 3549 301 258 -458 C ATOM 138 CA THR A 231 15.173 6.964 19.129 1.00 31.34 C ANISOU 138 CA THR A 231 5091 4018 2800 459 -45 -469 C ATOM 139 CA ILE A 232 14.594 3.726 17.204 1.00 24.09 C ANISOU 139 CA ILE A 232 3914 2960 2279 305 212 10 C ATOM 140 CA HIS A 233 16.864 0.744 17.723 1.00 23.85 C ANISOU 140 CA HIS A 233 3864 3138 2059 567 155 166 C ATOM 141 CA TYR A 234 17.300 -0.820 14.306 1.00 19.16 C ANISOU 141 CA TYR A 234 2891 2344 2045 95 95 149 C ATOM 142 CA LYS A 235 19.097 -4.162 13.708 1.00 22.81 C ANISOU 142 CA LYS A 235 3223 2781 2662 203 195 318 C ATOM 143 CA TYR A 236 20.597 -5.511 10.505 1.00 14.94 C ANISOU 143 CA TYR A 236 2009 1714 1954 -64 45 126 C ATOM 144 CA MET A 237 20.260 -9.270 10.130 1.00 19.76 C ANISOU 144 CA MET A 237 2467 1939 3103 44 421 257 C ATOM 145 CA CYS A 238 22.888 -10.077 7.489 1.00 18.37 C ANISOU 145 CA CYS A 238 2257 1883 2840 -24 221 40 C ATOM 146 CA TYR A 239 26.491 -9.107 6.828 1.00 19.44 C ANISOU 146 CA TYR A 239 2384 2350 2653 29 75 117 C ATOM 147 CA SER A 240 27.166 -6.883 3.839 1.00 20.24 C ANISOU 147 CA SER A 240 2548 2521 2620 -45 20 -33 C ATOM 148 CA SER A 241 29.182 -9.839 2.608 1.00 23.43 C ANISOU 148 CA SER A 241 2937 2816 3151 155 254 25 C ATOM 149 CA CYS A 242 26.439 -12.486 2.970 1.00 19.87 C ANISOU 149 CA CYS A 242 2496 2040 3015 131 269 -239 C ATOM 150 CA MET A 243 26.497 -14.757 -0.087 1.00 25.93 C ANISOU 150 CA MET A 243 3377 2584 3892 332 295 -731 C ATOM 151 CA GLY A 244 23.057 -15.037 -1.705 1.00 26.37 C ANISOU 151 CA GLY A 244 3368 2473 4180 325 -155 -1535 C ATOM 152 CA GLY A 245 22.192 -11.830 0.108 1.00 21.02 C ANISOU 152 CA GLY A 245 2691 2088 3209 126 -219 -1070 C ATOM 153 CA MET A 246 23.833 -8.411 -0.038 1.00 25.30 C ANISOU 153 CA MET A 246 3446 3038 3127 183 -163 -625 C ATOM 154 CA ASN A 247 26.829 -10.078 -1.778 1.00 24.28 C ANISOU 154 CA ASN A 247 3449 2904 2874 469 126 -539 C ATOM 155 CA ARG A 248 29.321 -7.368 -0.610 1.00 24.86 C ANISOU 155 CA ARG A 248 3350 3084 3010 344 379 1 C ATOM 156 CA ARG A 249 27.128 -4.595 -2.102 1.00 19.12 C ANISOU 156 CA ARG A 249 2861 2477 1926 487 308 -54 C ATOM 157 CA PRO A 250 26.833 -1.281 -0.192 1.00 17.35 C ANISOU 157 CA PRO A 250 2421 2189 1981 167 336 137 C ATOM 158 CA ILE A 251 23.284 -0.428 0.848 1.00 20.02 C ANISOU 158 CA ILE A 251 2837 2589 2181 37 -9 -85 C ATOM 159 CA LEU A 252 21.464 2.735 1.828 1.00 17.86 C ANISOU 159 CA LEU A 252 2556 2254 1977 -80 16 -13 C ATOM 160 CA THR A 253 18.904 2.839 4.621 1.00 24.76 C ANISOU 160 CA THR A 253 3370 3080 2959 -314 -201 -162 C ATOM 161 CA ILE A 254 16.144 5.189 3.516 1.00 13.57 C ANISOU 161 CA ILE A 254 2026 1655 1474 -162 -173 -101 C ATOM 162 CA ILE A 255 13.992 6.493 6.322 1.00 16.83 C ANISOU 162 CA ILE A 255 2406 1906 2081 -337 -116 -103 C ATOM 163 CA THR A 256 10.851 8.312 5.260 1.00 15.06 C ANISOU 163 CA THR A 256 2144 1658 1920 -143 -95 -9 C ATOM 164 CA LEU A 257 8.466 10.333 7.371 1.00 22.28 C ANISOU 164 CA LEU A 257 3058 2347 3062 -184 152 107 C ATOM 165 CA GLU A 258 5.041 9.286 6.018 1.00 24.63 C ANISOU 165 CA GLU A 258 2982 2674 3703 19 -106 43 C ATOM 166 CA ASP A 259 1.375 9.729 6.782 1.00 26.04 C ANISOU 166 CA ASP A 259 2764 2619 4510 109 -22 109 C ATOM 167 CA SER A 260 -0.621 6.601 7.609 1.00 31.46 C ANISOU 167 CA SER A 260 2825 2927 6200 -29 -40 -100 C ATOM 168 CA SER A 261 -1.411 5.988 3.907 1.00 32.94 C ANISOU 168 CA SER A 261 2611 3512 6393 266 -974 -708 C ATOM 169 CA GLY A 262 2.269 6.138 2.977 1.00 38.39 C ANISOU 169 CA GLY A 262 4005 4571 6012 294 -962 -607 C ATOM 170 CA ASN A 263 2.400 9.604 1.412 1.00 25.53 C ANISOU 170 CA ASN A 263 2758 3285 3656 759 -866 -228 C ATOM 171 CA LEU A 264 5.832 11.256 1.595 1.00 27.33 C ANISOU 171 CA LEU A 264 3544 3484 3356 672 -316 177 C ATOM 172 CA LEU A 265 6.305 13.916 4.306 1.00 24.13 C ANISOU 172 CA LEU A 265 3297 2655 3215 332 307 460 C ATOM 173 CA GLY A 266 10.082 13.771 4.409 1.00 22.09 C ANISOU 173 CA GLY A 266 3199 2320 2875 107 480 419 C ATOM 174 CA ARG A 267 13.034 11.557 3.536 1.00 16.32 C ANISOU 174 CA ARG A 267 2476 1733 1990 29 333 297 C ATOM 175 CA ASN A 268 16.510 10.959 4.936 1.00 15.57 C ANISOU 175 CA ASN A 268 2283 1502 2133 -306 380 128 C ATOM 176 CA SER A 269 19.169 8.357 4.283 1.00 21.22 C ANISOU 176 CA SER A 269 2923 2363 2779 -332 244 63 C ATOM 177 CA PHE A 270 22.489 6.959 5.430 1.00 15.48 C ANISOU 177 CA PHE A 270 1961 1626 2296 -515 140 -96 C ATOM 178 CA GLU A 271 24.828 4.309 4.085 1.00 20.86 C ANISOU 178 CA GLU A 271 2574 2421 2931 -400 162 1 C ATOM 179 CA VAL A 272 25.181 1.098 6.097 1.00 14.30 C ANISOU 179 CA VAL A 272 1726 1797 1908 -414 -177 -139 C ATOM 180 CA ARG A 273 27.925 -1.503 6.279 1.00 15.56 C ANISOU 180 CA ARG A 273 1713 2040 2161 -311 -194 -72 C ATOM 181 CA VAL A 274 27.183 -4.563 8.363 1.00 15.94 C ANISOU 181 CA VAL A 274 1867 2196 1995 -124 -271 7 C ATOM 182 CA CYS A 275 30.499 -6.159 9.229 1.00 18.75 C ANISOU 182 CA CYS A 275 1963 2712 2450 92 -340 119 C ATOM 183 CA ALA A 276 32.315 -8.053 11.976 1.00 22.62 C ANISOU 183 CA ALA A 276 2343 3524 2727 582 -523 282 C ATOM 184 CA CYS A 277 34.454 -5.138 13.104 1.00 26.46 C ANISOU 184 CA CYS A 277 2376 4250 3429 516 -1149 -230 C ATOM 185 CA PRO A 278 32.657 -1.756 12.665 1.00 18.43 C ANISOU 185 CA PRO A 278 3423 2288 1293 504 -266 -512 C ATOM 186 CA GLY A 279 35.278 0.155 14.648 1.00 21.10 C ANISOU 186 CA GLY A 279 3065 3005 1947 444 -919 -237 C ATOM 187 CA ARG A 280 38.230 -0.832 12.450 1.00 25.38 C ANISOU 187 CA ARG A 280 3164 3420 3058 842 -278 616 C ATOM 188 CA ASP A 281 36.282 -0.627 9.213 1.00 23.71 C ANISOU 188 CA ASP A 281 3758 2576 2676 724 239 64 C ATOM 189 CA ARG A 282 35.120 2.906 10.015 1.00 18.55 C ANISOU 189 CA ARG A 282 2947 2095 2005 337 -509 -407 C ATOM 190 CA ARG A 283 38.632 4.034 10.927 1.00 24.86 C ANISOU 190 CA ARG A 283 2995 3167 3285 85 -830 91 C ATOM 191 CA THR A 284 39.813 2.462 7.706 1.00 31.26 C ANISOU 191 CA THR A 284 3813 3599 4463 638 24 623 C ATOM 192 CA GLU A 285 37.253 4.213 5.471 1.00 24.65 C ANISOU 192 CA GLU A 285 3543 2451 3372 454 112 21 C ATOM 193 CA GLU A 286 37.807 7.566 7.192 1.00 22.91 C ANISOU 193 CA GLU A 286 3126 2192 3386 39 -406 -203 C ATOM 194 CA GLU A 287 41.579 7.248 6.814 1.00 34.76 C ANISOU 194 CA GLU A 287 3822 3972 5413 -101 -444 520 C ATOM 195 CA ASN A 288 41.255 6.561 3.079 1.00 36.71 C ANISOU 195 CA ASN A 288 4355 3744 5850 462 337 701 C ATOM 196 CA LEU A 289 39.224 9.757 3.037 1.00 42.68 C ANISOU 196 CA LEU A 289 5470 4244 6501 203 180 178 C ATOM 197 CA ARG A 290 42.171 11.886 4.153 1.00 66.02 C ANISOU 197 CA ARG A 290 8031 7154 9900 -519 -100 309 C ATOM 198 CA LYS A 291 45.222 10.165 2.683 1.00 73.07 C ANISOU 198 CA LYS A 291 8037 8461 11265 -228 61 1257 C END If you find results from this site helpful for your research, please cite one of our papers:
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