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*** ***elNémo ID: 240414132917104863Job options:ID = 240414132917104863 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 96 12.255 -17.300 32.999 1.00 71.26 C ANISOU 1 CA SER A 96 8545 8095 10437 -573 433 -2462 C ATOM 2 CA VAL A 97 9.072 -15.197 33.108 1.00 49.22 C ANISOU 2 CA VAL A 97 6035 5686 6980 -863 558 -1514 C ATOM 3 CA PRO A 98 8.110 -12.448 35.610 1.00 40.30 C ANISOU 3 CA PRO A 98 4950 4585 5776 -588 400 -997 C ATOM 4 CA SER A 99 4.905 -13.036 37.618 1.00 47.78 C ANISOU 4 CA SER A 99 6330 5518 6305 -529 167 -312 C ATOM 5 CA GLN A 100 1.639 -11.381 36.600 1.00 48.96 C ANISOU 5 CA GLN A 100 6365 6266 5970 -817 275 104 C ATOM 6 CA LYS A 101 -0.461 -12.504 39.544 1.00 36.35 C ANISOU 6 CA LYS A 101 5083 4248 4482 -880 329 296 C ATOM 7 CA THR A 102 -2.508 -9.666 40.983 1.00 40.15 C ANISOU 7 CA THR A 102 5411 5067 4776 -799 219 708 C ATOM 8 CA TYR A 103 -1.490 -8.801 44.581 1.00 37.61 C ANISOU 8 CA TYR A 103 5484 4345 4461 -304 96 985 C ATOM 9 CA GLN A 104 -3.103 -5.953 46.493 1.00 38.77 C ANISOU 9 CA GLN A 104 5413 4727 4593 -262 69 1204 C ATOM 10 CA GLY A 105 -0.813 -6.427 49.484 1.00 37.36 C ANISOU 10 CA GLY A 105 5592 4484 4118 623 -275 950 C ATOM 11 CA SER A 106 -0.827 -4.601 52.804 1.00 37.27 C ANISOU 11 CA SER A 106 5503 4885 3771 1274 -547 672 C ATOM 12 CA TYR A 107 -1.602 -1.280 51.191 1.00 32.58 C ANISOU 12 CA TYR A 107 3959 4328 4093 435 -221 527 C ATOM 13 CA GLY A 108 -4.582 -2.282 49.087 1.00 26.35 C ANISOU 13 CA GLY A 108 3471 3372 3171 -164 94 1274 C ATOM 14 CA PHE A 109 -2.833 -1.555 45.787 1.00 33.94 C ANISOU 14 CA PHE A 109 4132 6107 2658 -398 262 57 C ATOM 15 CA ARG A 110 -5.159 -1.123 42.772 1.00 36.97 C ANISOU 15 CA ARG A 110 4060 6592 3394 -754 531 397 C ATOM 16 CA LEU A 111 -4.947 0.405 39.272 1.00 35.91 C ANISOU 16 CA LEU A 111 3642 6216 3788 -1020 436 451 C ATOM 17 CA GLY A 112 -7.250 3.091 37.861 1.00 38.82 C ANISOU 17 CA GLY A 112 3751 6600 4398 -902 494 511 C ATOM 18 CA PHE A 113 -7.832 4.799 34.488 1.00 32.47 C ANISOU 18 CA PHE A 113 2725 5647 3966 -1052 422 743 C ATOM 19 CA LEU A 114 -9.490 7.770 32.833 1.00 35.96 C ANISOU 19 CA LEU A 114 2990 5921 4751 -928 286 848 C ATOM 20 CA HIS A 115 -13.005 6.909 31.589 1.00 36.12 C ANISOU 20 CA HIS A 115 2811 6255 4659 -908 419 970 C ATOM 21 CA SER A 116 -12.338 8.486 28.155 1.00 37.64 C ANISOU 21 CA SER A 116 3016 6240 5044 -983 225 1303 C ATOM 22 CA GLY A 117 -14.858 6.829 25.811 1.00 35.76 C ANISOU 22 CA GLY A 117 2689 6253 4645 -967 165 1402 C ATOM 23 CA THR A 118 -14.311 5.817 22.188 1.00 34.98 C ANISOU 23 CA THR A 118 2741 6316 4235 -896 12 1644 C ATOM 24 CA ALA A 119 -14.761 9.015 20.212 1.00 42.35 C ANISOU 24 CA ALA A 119 3722 7084 5286 -722 -132 2008 C ATOM 25 CA LYS A 120 -12.505 9.090 17.127 1.00 49.87 C ANISOU 25 CA LYS A 120 4868 8321 5758 -580 -18 2543 C ATOM 26 CA SER A 121 -10.194 11.804 18.523 1.00 54.08 C ANISOU 26 CA SER A 121 5242 8447 6859 -854 139 2935 C ATOM 27 CA VAL A 122 -9.216 10.265 21.897 1.00 47.80 C ANISOU 27 CA VAL A 122 4379 7542 6240 -1057 227 2363 C ATOM 28 CA THR A 123 -5.500 9.562 22.300 1.00 43.11 C ANISOU 28 CA THR A 123 3835 6876 5668 -1118 392 2345 C ATOM 29 CA CYS A 124 -5.869 7.044 25.085 1.00 35.97 C ANISOU 29 CA CYS A 124 4842 4668 4156 -198 -641 1030 C ATOM 30 CA THR A 125 -8.726 4.905 26.373 1.00 32.08 C ANISOU 30 CA THR A 125 4445 4459 3284 35 -509 242 C ATOM 31 CA TYR A 126 -9.275 1.952 28.680 1.00 27.65 C ANISOU 31 CA TYR A 126 3790 4087 2628 -61 -269 -29 C ATOM 32 CA SER A 127 -11.632 -1.010 28.432 1.00 29.72 C ANISOU 32 CA SER A 127 3893 4498 2902 19 183 -462 C ATOM 33 CA PRO A 128 -12.952 -2.388 31.753 1.00 26.44 C ANISOU 33 CA PRO A 128 3475 4160 2410 -152 388 -458 C ATOM 34 CA ALA A 129 -14.491 -5.369 29.940 1.00 31.88 C ANISOU 34 CA ALA A 129 3858 4644 3610 -212 884 -807 C ATOM 35 CA LEU A 130 -11.185 -6.322 28.285 1.00 40.59 C ANISOU 35 CA LEU A 130 4918 5549 4954 -77 828 -389 C ATOM 36 CA ASN A 131 -8.876 -4.966 31.031 1.00 34.22 C ANISOU 36 CA ASN A 131 4336 4844 3823 -153 553 308 C ATOM 37 CA LYS A 132 -7.091 -3.433 28.095 1.00 28.66 C ANISOU 37 CA LYS A 132 3539 4247 3104 -39 334 329 C ATOM 38 CA MET A 133 -5.473 -0.110 27.360 1.00 32.77 C ANISOU 38 CA MET A 133 4114 4828 3509 -130 -47 627 C ATOM 39 CA PHE A 134 -5.599 1.331 23.868 1.00 32.74 C ANISOU 39 CA PHE A 134 4009 5037 3394 96 3 756 C ATOM 40 CA CYS A 135 -3.225 4.234 23.250 1.00 39.31 C ANISOU 40 CA CYS A 135 4783 5708 4447 -172 -196 1500 C ATOM 41 CA GLN A 136 -1.350 6.058 20.521 1.00 42.89 C ANISOU 41 CA GLN A 136 4964 6368 4966 -197 -39 2405 C ATOM 42 CA LEU A 137 2.374 5.856 19.755 1.00 44.61 C ANISOU 42 CA LEU A 137 4603 6938 5407 -487 129 2998 C ATOM 43 CA ALA A 138 4.442 8.188 21.960 1.00 46.80 C ANISOU 43 CA ALA A 138 4769 6530 6481 -1243 -219 3278 C ATOM 44 CA LYS A 139 1.388 9.810 23.554 1.00 44.17 C ANISOU 44 CA LYS A 139 5074 5397 6311 -1200 -611 2766 C ATOM 45 CA THR A 140 0.768 10.195 27.280 1.00 45.36 C ANISOU 45 CA THR A 140 6349 5789 5096 -613 -1132 280 C ATOM 46 CA CYS A 141 -1.120 7.278 28.757 1.00 46.88 C ANISOU 46 CA CYS A 141 6497 5637 5680 -136 -999 -116 C ATOM 47 CA PRO A 142 -2.214 8.066 32.340 1.00 36.82 C ANISOU 47 CA PRO A 142 4732 4135 5124 262 -785 -161 C ATOM 48 CA VAL A 143 -2.256 5.196 34.817 1.00 28.29 C ANISOU 48 CA VAL A 143 3533 3131 4085 543 -370 -319 C ATOM 49 CA GLN A 144 -3.731 5.689 38.281 1.00 32.78 C ANISOU 49 CA GLN A 144 3624 3873 4958 886 -9 -256 C ATOM 50 CA LEU A 145 -2.353 4.230 41.478 1.00 29.86 C ANISOU 50 CA LEU A 145 3295 3796 4253 1101 420 -308 C ATOM 51 CA TRP A 146 -4.959 3.634 44.231 1.00 34.10 C ANISOU 51 CA TRP A 146 3314 4831 4812 1220 860 40 C ATOM 52 CA VAL A 147 -4.146 2.588 47.820 1.00 39.44 C ANISOU 52 CA VAL A 147 4096 6031 4858 1348 1296 173 C ATOM 53 CA ASP A 148 -6.165 1.863 50.980 1.00 49.74 C ANISOU 53 CA ASP A 148 4927 8331 5642 1393 1970 684 C ATOM 54 CA SER A 149 -3.158 2.889 53.094 1.00 52.52 C ANISOU 54 CA SER A 149 6090 8681 5184 1688 1893 121 C ATOM 55 CA THR A 150 -0.141 5.112 52.324 1.00 45.26 C ANISOU 55 CA THR A 150 5776 7251 4171 1717 1309 -591 C ATOM 56 CA PRO A 151 3.008 3.084 51.542 1.00 37.02 C ANISOU 56 CA PRO A 151 4664 6183 3217 1457 777 -189 C ATOM 57 CA PRO A 152 6.258 3.998 53.399 1.00 45.43 C ANISOU 57 CA PRO A 152 5861 7827 3573 1209 226 -181 C ATOM 58 CA PRO A 153 8.717 6.556 52.012 1.00 46.55 C ANISOU 58 CA PRO A 153 5886 8083 3718 600 -404 -371 C ATOM 59 CA GLY A 154 11.281 5.063 49.658 1.00 41.82 C ANISOU 59 CA GLY A 154 4269 8139 3481 773 -503 224 C ATOM 60 CA THR A 155 8.571 3.028 47.965 1.00 39.55 C ANISOU 60 CA THR A 155 4279 6984 3763 1451 108 41 C ATOM 61 CA ARG A 156 9.146 2.637 44.214 1.00 39.43 C ANISOU 61 CA ARG A 156 5392 5539 4052 60 -850 132 C ATOM 62 CA VAL A 157 6.817 1.945 41.243 1.00 36.17 C ANISOU 62 CA VAL A 157 4761 5193 3789 434 -435 395 C ATOM 63 CA ARG A 158 8.078 -0.263 38.397 1.00 28.67 C ANISOU 63 CA ARG A 158 3094 4442 3357 166 -373 375 C ATOM 64 CA ALA A 159 6.498 -0.904 34.972 1.00 34.01 C ANISOU 64 CA ALA A 159 3619 5304 3997 365 -153 383 C ATOM 65 CA MET A 160 7.460 -3.854 32.775 1.00 32.83 C ANISOU 65 CA MET A 160 3014 5284 4178 257 -149 176 C ATOM 66 CA ALA A 161 6.195 -5.335 29.512 1.00 32.17 C ANISOU 66 CA ALA A 161 2869 5438 3918 371 -136 -104 C ATOM 67 CA ILE A 162 5.743 -8.985 28.567 1.00 30.52 C ANISOU 67 CA ILE A 162 2510 5092 3996 214 -279 -509 C ATOM 68 CA TYR A 163 4.013 -10.732 25.645 1.00 37.40 C ANISOU 68 CA TYR A 163 3500 6144 4566 102 -523 -1079 C ATOM 69 CA LYS A 164 0.509 -11.985 26.480 1.00 47.75 C ANISOU 69 CA LYS A 164 4422 7661 6058 -360 -1000 -1078 C ATOM 70 CA GLN A 165 0.570 -15.272 24.542 1.00 51.85 C ANISOU 70 CA GLN A 165 5265 7694 6740 -793 -1205 -1907 C ATOM 71 CA SER A 166 2.337 -18.048 26.433 1.00 53.96 C ANISOU 71 CA SER A 166 5728 6894 7880 -881 -818 -1901 C ATOM 72 CA GLN A 167 4.476 -19.122 23.458 1.00 62.18 C ANISOU 72 CA GLN A 167 7556 7612 8457 -529 -569 -2623 C ATOM 73 CA HIS A 168 6.086 -15.667 23.406 1.00 49.36 C ANISOU 73 CA HIS A 168 5669 6728 6357 60 -319 -2025 C ATOM 74 CA MET A 169 6.519 -14.879 27.108 1.00 46.66 C ANISOU 74 CA MET A 169 4616 6538 6576 664 -18 -1003 C ATOM 75 CA THR A 170 10.256 -15.666 27.341 1.00 44.54 C ANISOU 75 CA THR A 170 4486 6292 6146 1086 366 -1068 C ATOM 76 CA GLU A 171 11.105 -13.267 24.511 1.00 44.37 C ANISOU 76 CA GLU A 171 4583 6632 5645 1266 459 -1207 C ATOM 77 CA VAL A 172 12.053 -9.815 25.815 1.00 40.88 C ANISOU 77 CA VAL A 172 3922 6624 4985 949 592 -868 C ATOM 78 CA VAL A 173 9.718 -7.025 24.685 1.00 38.25 C ANISOU 78 CA VAL A 173 3786 6205 4542 915 622 -926 C ATOM 79 CA ARG A 174 11.843 -4.271 23.116 1.00 46.76 C ANISOU 79 CA ARG A 174 5061 7607 5098 786 665 -783 C ATOM 80 CA ARG A 175 11.500 -1.546 20.474 1.00 39.91 C ANISOU 80 CA ARG A 175 4335 6891 3940 866 669 -708 C ATOM 81 CA CYS A 176 11.767 -2.595 16.833 1.00 41.54 C ANISOU 81 CA CYS A 176 4234 7560 3990 1163 454 -886 C ATOM 82 CA PRO A 177 15.011 -1.853 14.971 1.00 44.08 C ANISOU 82 CA PRO A 177 4388 8558 3803 1253 523 -602 C ATOM 83 CA HIS A 178 13.600 1.249 13.286 1.00 41.49 C ANISOU 83 CA HIS A 178 4182 8244 3338 1065 389 -464 C ATOM 84 CA HIS A 179 12.351 2.946 16.464 1.00 43.33 C ANISOU 84 CA HIS A 179 4959 7720 3785 791 597 -337 C ATOM 85 CA GLU A 180 15.362 1.763 18.395 1.00 42.08 C ANISOU 85 CA GLU A 180 4717 7861 3411 318 457 -138 C ATOM 86 CA ARG A 181 17.358 3.809 15.904 1.00 56.32 C ANISOU 86 CA ARG A 181 4703 11701 4997 -1850 241 -1060 C ATOM 87 CA CYS A 182 14.958 6.787 15.941 1.00 51.18 C ANISOU 87 CA CYS A 182 4421 10602 4422 -2195 -275 644 C ATOM 88 CA SER A 183 15.902 10.275 17.072 1.00 59.61 C ANISOU 88 CA SER A 183 5736 11252 5663 -2384 -424 1512 C ATOM 89 CA ASP A 184 13.182 10.519 19.694 1.00 50.23 C ANISOU 89 CA ASP A 184 4544 8794 5748 -1452 -508 2183 C ATOM 90 CA SER A 185 15.250 10.277 22.842 1.00 44.12 C ANISOU 90 CA SER A 185 4116 7298 5351 -1012 -101 1477 C ATOM 91 CA ASP A 186 14.211 12.518 25.746 1.00 37.64 C ANISOU 91 CA ASP A 186 4221 4907 5174 -586 189 2019 C ATOM 92 CA GLY A 187 17.716 12.167 27.149 1.00 45.99 C ANISOU 92 CA GLY A 187 5489 6156 5828 -1068 84 1403 C ATOM 93 CA LEU A 188 16.748 9.702 29.851 1.00 40.19 C ANISOU 93 CA LEU A 188 5133 4564 5575 -527 100 851 C ATOM 94 CA ALA A 189 15.287 6.580 28.279 1.00 34.58 C ANISOU 94 CA ALA A 189 3662 4470 5006 -125 -75 371 C ATOM 95 CA PRO A 190 17.482 3.858 26.735 1.00 34.06 C ANISOU 95 CA PRO A 190 2849 5253 4840 30 -498 -611 C ATOM 96 CA PRO A 191 16.862 3.640 22.950 1.00 42.21 C ANISOU 96 CA PRO A 191 3360 7426 5251 -294 -234 -680 C ATOM 97 CA GLN A 192 15.575 0.019 23.098 1.00 41.51 C ANISOU 97 CA GLN A 192 3429 7003 5340 85 -555 -1430 C ATOM 98 CA HIS A 193 13.048 0.581 25.917 1.00 35.01 C ANISOU 98 CA HIS A 193 3219 5132 4951 114 -624 -665 C ATOM 99 CA LEU A 194 9.343 0.378 24.972 1.00 27.23 C ANISOU 99 CA LEU A 194 2003 4387 3955 -219 -554 10 C ATOM 100 CA ILE A 195 7.946 2.061 28.095 1.00 31.38 C ANISOU 100 CA ILE A 195 3612 5623 2689 -439 -907 250 C ATOM 101 CA ARG A 196 8.983 5.573 29.177 1.00 31.51 C ANISOU 101 CA ARG A 196 4167 4875 2931 -258 -900 768 C ATOM 102 CA VAL A 197 7.740 7.941 31.894 1.00 37.13 C ANISOU 102 CA VAL A 197 4845 4948 4313 255 -1014 482 C ATOM 103 CA GLU A 198 7.593 11.664 31.091 1.00 48.11 C ANISOU 103 CA GLU A 198 7054 5108 6117 750 -1496 962 C ATOM 104 CA GLY A 199 7.761 14.701 33.360 1.00 52.38 C ANISOU 104 CA GLY A 199 8045 4300 7558 1085 -1554 441 C ATOM 105 CA ASN A 200 9.759 13.083 36.163 1.00 41.45 C ANISOU 105 CA ASN A 200 6306 3605 5839 249 -977 -308 C ATOM 106 CA LEU A 201 13.458 13.949 36.546 1.00 45.44 C ANISOU 106 CA LEU A 201 7143 3571 6551 -883 -940 -208 C ATOM 107 CA ARG A 202 13.898 11.085 39.016 1.00 42.42 C ANISOU 107 CA ARG A 202 6167 4456 5495 -979 -856 -746 C ATOM 108 CA VAL A 203 12.975 8.418 36.484 1.00 26.86 C ANISOU 108 CA VAL A 203 3788 3182 3233 -834 -609 -50 C ATOM 109 CA GLU A 204 15.251 5.380 36.404 1.00 28.91 C ANISOU 109 CA GLU A 204 3559 4036 3392 -1215 -548 78 C ATOM 110 CA TYR A 205 15.670 2.690 33.716 1.00 30.78 C ANISOU 110 CA TYR A 205 3435 4675 3584 -1222 -256 253 C ATOM 111 CA LEU A 206 16.884 -0.909 34.117 1.00 30.90 C ANISOU 111 CA LEU A 206 3023 4806 3912 -1071 -325 59 C ATOM 112 CA ASP A 207 18.365 -3.620 31.947 1.00 29.55 C ANISOU 112 CA ASP A 207 2387 4685 4155 -881 -38 -393 C ATOM 113 CA ASP A 208 18.210 -6.667 34.196 1.00 32.71 C ANISOU 113 CA ASP A 208 2914 4407 5107 -513 -610 -245 C ATOM 114 CA ARG A 209 21.675 -8.212 34.206 1.00 49.84 C ANISOU 114 CA ARG A 209 4257 6325 8355 132 -921 -662 C ATOM 115 CA ASN A 210 20.201 -11.722 34.354 1.00 47.01 C ANISOU 115 CA ASN A 210 4522 4819 8520 433 -1182 -606 C ATOM 116 CA THR A 211 16.867 -11.599 32.535 1.00 43.83 C ANISOU 116 CA THR A 211 4586 4659 7410 -302 -580 -860 C ATOM 117 CA PHE A 212 17.691 -8.813 30.082 1.00 35.30 C ANISOU 117 CA PHE A 212 3082 4768 5563 -442 25 -1300 C ATOM 118 CA ARG A 213 14.183 -7.443 30.573 1.00 30.93 C ANISOU 118 CA ARG A 213 3000 4476 4275 -918 -114 -807 C ATOM 119 CA HIS A 214 13.535 -3.707 30.506 1.00 28.76 C ANISOU 119 CA HIS A 214 4218 3767 2943 10 -218 392 C ATOM 120 CA SER A 215 11.649 -1.794 33.142 1.00 25.20 C ANISOU 120 CA SER A 215 3300 3563 2711 133 -529 54 C ATOM 121 CA VAL A 216 11.132 1.786 34.320 1.00 26.53 C ANISOU 121 CA VAL A 216 3423 3433 3223 681 -585 162 C ATOM 122 CA VAL A 217 10.812 2.804 37.946 1.00 29.41 C ANISOU 122 CA VAL A 217 3527 3628 4021 337 -600 -180 C ATOM 123 CA VAL A 218 9.996 6.121 39.689 1.00 29.20 C ANISOU 123 CA VAL A 218 3564 3214 4315 667 -443 -258 C ATOM 124 CA PRO A 219 9.685 7.069 43.385 1.00 37.26 C ANISOU 124 CA PRO A 219 4460 4040 5658 190 -380 -700 C ATOM 125 CA TYR A 220 6.125 6.512 44.693 1.00 34.71 C ANISOU 125 CA TYR A 220 3670 4426 5092 302 -533 -1234 C ATOM 126 CA GLU A 221 4.437 9.817 45.503 1.00 47.47 C ANISOU 126 CA GLU A 221 5365 5778 6892 1001 -259 -1292 C ATOM 127 CA PRO A 222 1.510 10.009 47.928 1.00 46.06 C ANISOU 127 CA PRO A 222 4703 6047 6750 943 -159 -1972 C ATOM 128 CA PRO A 223 -1.672 11.733 46.698 1.00 55.20 C ANISOU 128 CA PRO A 223 5286 7949 7737 2284 -204 -2145 C ATOM 129 CA GLU A 224 -2.236 15.149 48.237 1.00 71.93 C ANISOU 129 CA GLU A 224 7988 9213 10130 2953 408 -1988 C ATOM 130 CA VAL A 225 -4.902 14.899 50.997 1.00 73.34 C ANISOU 130 CA VAL A 225 7538 9865 10462 2520 619 -2742 C ATOM 131 CA GLY A 226 -7.510 16.223 48.518 1.00 86.75 C ANISOU 131 CA GLY A 226 8784 12419 11757 3915 319 -2414 C ATOM 132 CA SER A 227 -6.924 13.591 45.830 1.00 83.06 C ANISOU 132 CA SER A 227 7932 12818 10810 3641 -399 -2433 C ATOM 133 CA ASP A 228 -7.583 9.841 45.961 1.00 73.86 C ANISOU 133 CA ASP A 228 6047 12542 9474 2357 -670 -3299 C ATOM 134 CA CYS A 229 -4.871 8.430 43.691 1.00 45.60 C ANISOU 134 CA CYS A 229 6431 4723 6173 1320 515 -764 C ATOM 135 CA THR A 230 -1.440 9.004 42.227 1.00 37.21 C ANISOU 135 CA THR A 230 5210 3945 4984 428 -93 -961 C ATOM 136 CA THR A 231 -1.031 9.488 38.465 1.00 36.93 C ANISOU 136 CA THR A 231 4647 4034 5352 134 -233 -541 C ATOM 137 CA ILE A 232 1.962 8.295 36.453 1.00 35.80 C ANISOU 137 CA ILE A 232 3910 4561 5133 -375 -571 -392 C ATOM 138 CA HIS A 233 2.203 9.425 32.822 1.00 40.18 C ANISOU 138 CA HIS A 233 4172 5237 5859 -494 -551 93 C ATOM 139 CA TYR A 234 3.415 6.531 30.701 1.00 30.85 C ANISOU 139 CA TYR A 234 2444 4856 4421 -428 -555 180 C ATOM 140 CA LYS A 235 4.501 6.512 27.055 1.00 34.26 C ANISOU 140 CA LYS A 235 2592 5823 4604 -423 -467 590 C ATOM 141 CA TYR A 236 4.712 3.546 24.643 1.00 30.21 C ANISOU 141 CA TYR A 236 1935 5943 3601 -167 -298 410 C ATOM 142 CA MET A 237 7.397 4.167 22.018 1.00 41.67 C ANISOU 142 CA MET A 237 3202 7916 4715 -126 -11 967 C ATOM 143 CA CYS A 238 6.674 1.482 19.452 1.00 45.98 C ANISOU 143 CA CYS A 238 3985 8966 4518 211 186 519 C ATOM 144 CA ASN A 239 3.499 0.377 17.631 1.00 47.76 C ANISOU 144 CA ASN A 239 4487 9480 4180 216 -185 -49 C ATOM 145 CA SER A 240 1.738 -2.969 18.030 1.00 45.97 C ANISOU 145 CA SER A 240 4515 8993 3958 66 -279 -1038 C ATOM 146 CA SER A 241 1.928 -3.273 14.253 1.00 49.37 C ANISOU 146 CA SER A 241 5326 10255 3177 175 -299 -1229 C ATOM 147 CA CYS A 242 5.682 -2.562 14.040 1.00 56.95 C ANISOU 147 CA CYS A 242 6235 11286 4116 621 485 -550 C ATOM 148 CA MET A 243 7.314 -5.264 11.966 1.00 60.55 C ANISOU 148 CA MET A 243 7343 11799 3862 994 1182 -1093 C ATOM 149 CA GLY A 244 10.501 -6.463 13.640 1.00 59.67 C ANISOU 149 CA GLY A 244 7036 11098 4538 1334 2000 -638 C ATOM 150 CA GLY A 245 9.216 -5.652 17.087 1.00 51.49 C ANISOU 150 CA GLY A 245 5417 9795 4353 963 1511 -588 C ATOM 151 CA MET A 246 6.064 -6.741 18.852 1.00 48.66 C ANISOU 151 CA MET A 246 5145 8877 4468 555 962 -1317 C ATOM 152 CA ASN A 247 4.827 -7.475 15.337 1.00 61.97 C ANISOU 152 CA ASN A 247 7429 11039 5079 493 814 -1972 C ATOM 153 CA ARG A 248 1.079 -7.638 16.029 1.00 61.26 C ANISOU 153 CA ARG A 248 7191 10787 5300 -99 -53 -2460 C ATOM 154 CA ARG A 249 1.663 -9.728 19.174 1.00 53.29 C ANISOU 154 CA ARG A 249 6062 8816 5369 -10 466 -2589 C ATOM 155 CA PRO A 250 -0.360 -8.514 22.192 1.00 42.02 C ANISOU 155 CA PRO A 250 4067 7081 4819 -171 47 -2174 C ATOM 156 CA ILE A 251 1.460 -7.438 25.385 1.00 36.21 C ANISOU 156 CA ILE A 251 3550 6408 3799 551 271 58 C ATOM 157 CA LEU A 252 0.738 -6.876 29.069 1.00 37.42 C ANISOU 157 CA LEU A 252 3757 6061 4400 535 255 127 C ATOM 158 CA THR A 253 2.134 -4.159 31.304 1.00 35.17 C ANISOU 158 CA THR A 253 3377 5639 4348 474 286 369 C ATOM 159 CA ILE A 254 2.971 -5.263 34.824 1.00 30.66 C ANISOU 159 CA ILE A 254 2893 4816 3938 504 336 241 C ATOM 160 CA ILE A 255 2.987 -2.606 37.548 1.00 38.32 C ANISOU 160 CA ILE A 255 3837 5605 5117 373 326 310 C ATOM 161 CA THR A 256 4.722 -3.565 40.788 1.00 29.35 C ANISOU 161 CA THR A 256 2775 4422 3953 312 338 258 C ATOM 162 CA LEU A 257 4.846 -1.740 44.069 1.00 36.50 C ANISOU 162 CA LEU A 257 3718 5247 4902 122 334 174 C ATOM 163 CA GLU A 258 8.200 -2.190 45.856 1.00 32.29 C ANISOU 163 CA GLU A 258 3158 4862 4250 52 222 289 C ATOM 164 CA ASP A 259 10.142 -0.827 48.880 1.00 34.13 C ANISOU 164 CA ASP A 259 3389 5199 4379 -206 103 273 C ATOM 165 CA SER A 260 13.540 0.931 48.793 1.00 39.29 C ANISOU 165 CA SER A 260 3779 6140 5010 -423 -40 410 C ATOM 166 CA SER A 261 15.310 -2.470 48.856 1.00 45.09 C ANISOU 166 CA SER A 261 4331 7181 5620 -15 -180 498 C ATOM 167 CA GLY A 262 13.301 -3.809 45.886 1.00 37.67 C ANISOU 167 CA GLY A 262 3485 6041 4787 282 1 446 C ATOM 168 CA ASN A 263 11.002 -6.125 47.911 1.00 37.87 C ANISOU 168 CA ASN A 263 3976 5670 4745 283 -87 425 C ATOM 169 CA LEU A 264 7.487 -6.730 46.448 1.00 33.60 C ANISOU 169 CA LEU A 264 3624 4890 4254 206 97 326 C ATOM 170 CA LEU A 265 4.618 -4.780 48.084 1.00 30.04 C ANISOU 170 CA LEU A 265 3160 4486 3768 -129 294 152 C ATOM 171 CA GLY A 266 1.968 -4.991 45.365 1.00 42.23 C ANISOU 171 CA GLY A 266 4604 6008 5432 -31 400 60 C ATOM 172 CA ARG A 267 1.320 -6.082 41.790 1.00 39.33 C ANISOU 172 CA ARG A 267 4211 5603 5129 162 367 99 C ATOM 173 CA ASN A 268 -1.289 -5.413 39.120 1.00 31.25 C ANISOU 173 CA ASN A 268 3013 4694 4167 218 376 27 C ATOM 174 CA SER A 269 -1.403 -5.746 35.352 1.00 30.79 C ANISOU 174 CA SER A 269 2925 4736 4040 357 293 92 C ATOM 175 CA PHE A 270 -3.280 -4.758 32.173 1.00 34.10 C ANISOU 175 CA PHE A 270 3200 5353 4404 411 159 153 C ATOM 176 CA GLU A 271 -3.126 -5.619 28.465 1.00 30.51 C ANISOU 176 CA GLU A 271 2784 5170 3638 409 67 203 C ATOM 177 CA VAL A 272 -1.942 -2.986 25.985 1.00 33.52 C ANISOU 177 CA VAL A 272 3131 5763 3844 377 -54 584 C ATOM 178 CA ARG A 273 -2.417 -2.194 22.317 1.00 34.24 C ANISOU 178 CA ARG A 273 3240 6259 3509 223 -262 855 C ATOM 179 CA VAL A 274 -0.459 0.720 20.826 1.00 38.64 C ANISOU 179 CA VAL A 274 3911 6953 3818 -98 -400 1443 C ATOM 180 CA CYS A 275 -2.203 1.830 17.655 1.00 41.67 C ANISOU 180 CA CYS A 275 4427 7585 3822 -278 -825 1853 C ATOM 181 CA ALA A 276 -3.535 4.641 15.546 1.00 48.45 C ANISOU 181 CA ALA A 276 5592 8287 4531 -464 -1483 2567 C ATOM 182 CA CYS A 277 -7.046 5.571 16.671 1.00 57.91 C ANISOU 182 CA CYS A 277 6713 8916 6375 168 -1984 2436 C ATOM 183 CA PRO A 278 -7.555 3.737 20.025 1.00 49.51 C ANISOU 183 CA PRO A 278 3208 8780 6823 91 -1038 -141 C ATOM 184 CA GLY A 279 -11.175 4.878 20.140 1.00 43.95 C ANISOU 184 CA GLY A 279 3099 8037 5560 -268 -804 -270 C ATOM 185 CA ARG A 280 -12.087 2.949 17.006 1.00 45.16 C ANISOU 185 CA ARG A 280 3141 8995 5023 -27 -377 -448 C ATOM 186 CA ASP A 281 -10.060 -0.128 17.931 1.00 40.79 C ANISOU 186 CA ASP A 281 3005 7979 4515 438 -555 -860 C ATOM 187 CA ARG A 282 -11.616 -0.267 21.389 1.00 41.51 C ANISOU 187 CA ARG A 282 3731 7405 4635 2 -1075 -959 C ATOM 188 CA ARG A 283 -15.231 -0.103 20.136 1.00 41.39 C ANISOU 188 CA ARG A 283 3816 7834 4075 -676 -831 -997 C ATOM 189 CA THR A 284 -14.433 -2.703 17.456 1.00 49.71 C ANISOU 189 CA THR A 284 5347 8900 4640 -595 -613 -1619 C ATOM 190 CA GLU A 285 -12.755 -5.161 19.808 1.00 51.29 C ANISOU 190 CA GLU A 285 6457 7879 5151 -50 -567 -1752 C ATOM 191 CA GLU A 286 -15.575 -4.726 22.352 1.00 45.71 C ANISOU 191 CA GLU A 286 5887 6976 4505 -797 -815 -1492 C ATOM 192 CA GLU A 287 -18.182 -5.410 19.652 1.00 67.22 C ANISOU 192 CA GLU A 287 8514 10322 6702 -1926 -807 -1863 C ATOM 193 CA ASN A 288 -17.203 -9.084 19.603 1.00 79.66 C ANISOU 193 CA ASN A 288 11728 10347 8194 -1949 -463 -2582 C ATOM 194 CA LEU A 289 -18.713 -9.483 23.035 1.00 70.28 C ANISOU 194 CA LEU A 289 10374 8810 7518 -1850 -456 -1757 C HETATM 1526 ZN ZN A 401 8.710 0.208 16.282 1.00 40.65 ZN CONECT 630 1526 CONECT 655 1526 CONECT 1133 1526 CONECT 1159 1526 CONECT 1526 630 655 1133 1159 END If you find results from this site helpful for your research, please cite one of our papers:
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