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*** ***elNémo ID: 2404111304113650248Job options:ID = 2404111304113650248 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 END If you find results from this site helpful for your research, please cite one of our papers:
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