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*** ***elNémo ID: 2404250408192433806Job options:ID = 2404250408192433806 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 HETATM 1566 ZN ZN A 401 23.127 -13.571 5.712 1.00 27.55 ZN CONECT 646 1566 CONECT 671 1566 CONECT 1149 1566 CONECT 1179 1566 CONECT 1566 646 671 1149 1179 END END If you find results from this site helpful for your research, please cite one of our papers:
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