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*** ***elNémo ID: 2404250214242379641Job options:ID = 2404250214242379641 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 11.976 -18.031 33.229 1.00 66.05 C ANISOU 1 CA SER A 96 6758 6471 11866 927 369 677 C ATOM 2 CA VAL A 97 8.863 -15.832 33.506 1.00 55.21 C ANISOU 2 CA VAL A 97 5731 5520 9726 217 303 944 C ATOM 3 CA PRO A 98 7.985 -13.075 36.042 1.00 44.97 C ANISOU 3 CA PRO A 98 4372 5129 7585 219 60 1354 C ATOM 4 CA SER A 99 4.907 -13.750 38.152 1.00 50.24 C ANISOU 4 CA SER A 99 5167 5882 8039 99 5 2124 C ATOM 5 CA GLN A 100 1.700 -12.105 36.991 1.00 51.34 C ANISOU 5 CA GLN A 100 5348 6383 7776 -282 52 1817 C ATOM 6 CA LYS A 101 -0.358 -13.151 40.031 1.00 49.26 C ANISOU 6 CA LYS A 101 4927 6441 7347 -482 155 2466 C ATOM 7 CA THR A 102 -2.591 -10.465 41.581 1.00 48.00 C ANISOU 7 CA THR A 102 4477 7284 6475 -427 126 2326 C ATOM 8 CA TYR A 103 -1.576 -9.659 45.148 1.00 48.77 C ANISOU 8 CA TYR A 103 4536 7983 6010 -308 135 2787 C ATOM 9 CA GLN A 104 -3.146 -6.782 47.032 1.00 44.39 C ANISOU 9 CA GLN A 104 3724 8352 4790 -249 282 2389 C ATOM 10 CA GLY A 105 -0.702 -7.221 49.891 1.00 53.92 C ANISOU 10 CA GLY A 105 4906 10139 5440 -236 155 2825 C ATOM 11 CA SER A 106 -1.021 -5.698 53.327 1.00 57.39 C ANISOU 11 CA SER A 106 5050 11892 4863 -402 302 2673 C ATOM 12 CA TYR A 107 -1.545 -2.171 51.985 1.00 52.54 C ANISOU 12 CA TYR A 107 4508 10975 4482 -319 616 1508 C ATOM 13 CA GLY A 108 -4.547 -3.215 49.893 1.00 44.52 C ANISOU 13 CA GLY A 108 3467 9444 4006 -146 633 1723 C ATOM 14 CA PHE A 109 -2.882 -2.359 46.588 1.00 40.88 C ANISOU 14 CA PHE A 109 3544 7919 4068 197 495 1479 C ATOM 15 CA ARG A 110 -5.194 -1.880 43.561 1.00 48.34 C ANISOU 15 CA ARG A 110 6464 8803 3101 375 111 967 C ATOM 16 CA LEU A 111 -4.975 -0.214 40.119 1.00 31.35 C ANISOU 16 CA LEU A 111 4098 5860 1954 395 30 308 C ATOM 17 CA GLY A 112 -7.445 2.346 38.754 1.00 39.06 C ANISOU 17 CA GLY A 112 4733 6777 3330 418 321 -266 C ATOM 18 CA PHE A 113 -7.916 4.011 35.370 1.00 27.46 C ANISOU 18 CA PHE A 113 3095 4644 2695 381 159 -459 C ATOM 19 CA LEU A 114 -9.654 7.074 33.964 1.00 28.08 C ANISOU 19 CA LEU A 114 2822 4399 3446 499 38 -819 C ATOM 20 CA HIS A 115 -13.174 6.439 32.556 1.00 28.34 C ANISOU 20 CA HIS A 115 2567 4383 3820 410 127 -678 C ATOM 21 CA SER A 116 -12.339 8.007 29.209 1.00 25.46 C ANISOU 21 CA SER A 116 2302 3508 3864 385 -372 -348 C ATOM 22 CA GLY A 117 -14.814 6.393 26.821 1.00 33.96 C ANISOU 22 CA GLY A 117 3268 4625 5011 281 -564 -124 C ATOM 23 CA THR A 118 -14.271 5.446 23.157 1.00 32.89 C ANISOU 23 CA THR A 118 3370 4632 4493 142 -943 240 C ATOM 24 CA ALA A 119 -14.601 8.667 21.115 1.00 35.97 C ANISOU 24 CA ALA A 119 3755 4791 5121 232 -1498 786 C ATOM 25 CA LYS A 120 -12.183 8.880 18.171 1.00 47.98 C ANISOU 25 CA LYS A 120 5677 6748 5805 -9 -1561 1434 C ATOM 26 CA SER A 121 -10.173 11.630 19.851 1.00 47.85 C ANISOU 26 CA SER A 121 5590 6083 6510 -27 -1393 1683 C ATOM 27 CA VAL A 122 -9.209 9.634 22.961 1.00 40.05 C ANISOU 27 CA VAL A 122 4584 5157 5477 47 -890 826 C ATOM 28 CA THR A 123 -5.483 9.054 23.335 1.00 37.34 C ANISOU 28 CA THR A 123 4400 4897 4892 -127 -524 748 C ATOM 29 CA CYS A 124 -5.773 6.442 26.080 1.00 27.88 C ANISOU 29 CA CYS A 124 3228 3854 3512 11 -339 173 C ATOM 30 CA THR A 125 -8.766 4.319 27.140 1.00 32.06 C ANISOU 30 CA THR A 125 3661 4553 3967 68 -278 34 C ATOM 31 CA TYR A 126 -9.242 1.383 29.509 1.00 27.02 C ANISOU 31 CA TYR A 126 3015 4051 3198 25 -31 7 C ATOM 32 CA SER A 127 -11.692 -1.528 29.155 1.00 30.88 C ANISOU 32 CA SER A 127 3261 4482 3988 -147 56 128 C ATOM 33 CA PRO A 128 -13.087 -2.900 32.455 1.00 32.11 C ANISOU 33 CA PRO A 128 3281 4823 4097 -259 490 486 C ATOM 34 CA ALA A 129 -14.552 -5.909 30.638 1.00 29.79 C ANISOU 34 CA ALA A 129 2636 4060 4622 -499 366 564 C ATOM 35 CA LEU A 130 -11.248 -6.890 29.039 1.00 35.08 C ANISOU 35 CA LEU A 130 3570 4498 5262 -422 -24 348 C ATOM 36 CA ASN A 131 -8.944 -5.481 31.750 1.00 33.24 C ANISOU 36 CA ASN A 131 3733 4537 4360 -279 82 638 C ATOM 37 CA LYS A 132 -7.177 -3.940 28.802 1.00 26.05 C ANISOU 37 CA LYS A 132 2902 3634 3363 -183 -136 104 C ATOM 38 CA AMET A 133 -5.585 -0.592 28.131 0.48 28.51 C ANISOU 38 CA AMET A 133 3376 4113 3342 -71 -149 -48 C ATOM 39 CA BMET A 133 -5.569 -0.597 28.140 0.52 28.48 C ANISOU 39 CA BMET A 133 3373 4109 3339 -71 -149 -48 C ATOM 40 CA PHE A 134 -5.719 0.878 24.631 1.00 27.16 C ANISOU 40 CA PHE A 134 3189 4111 3019 -158 -232 -75 C ATOM 41 CA CYS A 135 -3.282 3.749 24.078 1.00 27.65 C ANISOU 41 CA CYS A 135 3311 4121 3072 -202 -166 95 C ATOM 42 CA GLN A 136 -1.456 5.708 21.401 1.00 30.19 C ANISOU 42 CA GLN A 136 3623 4616 3233 -438 -32 471 C ATOM 43 CA LEU A 137 2.306 5.707 20.819 1.00 32.79 C ANISOU 43 CA LEU A 137 3780 5018 3663 -649 349 304 C ATOM 44 CA ALA A 138 4.357 7.769 23.272 1.00 34.85 C ANISOU 44 CA ALA A 138 3827 4616 4798 -576 289 184 C ATOM 45 CA LYS A 139 1.244 9.413 24.740 1.00 34.20 C ANISOU 45 CA LYS A 139 3849 4234 4912 -328 -91 352 C ATOM 46 CA THR A 140 0.412 9.852 28.402 1.00 29.24 C ANISOU 46 CA THR A 140 3149 3403 4556 44 -351 -255 C ATOM 47 CA ACYS A 141 -1.107 6.716 29.892 0.56 32.01 C ANISOU 47 CA ACYS A 141 3411 4263 4487 627 -305 -102 C ATOM 48 CA BCYS A 141 -1.096 6.709 29.876 0.44 32.19 C ANISOU 48 CA BCYS A 141 3436 4285 4511 625 -306 -101 C ATOM 49 CA PRO A 142 -2.364 7.490 33.411 1.00 33.60 C ANISOU 49 CA PRO A 142 3510 4774 4485 890 -183 -435 C ATOM 50 CA VAL A 143 -2.341 4.478 35.732 1.00 31.71 C ANISOU 50 CA VAL A 143 3043 5081 3925 633 15 -226 C ATOM 51 CA GLN A 144 -3.675 5.048 39.239 1.00 32.39 C ANISOU 51 CA GLN A 144 2876 5939 3493 926 220 -441 C ATOM 52 CA LEU A 145 -2.288 3.457 42.406 1.00 36.94 C ANISOU 52 CA LEU A 145 3375 7144 3517 802 331 -220 C ATOM 53 CA TRP A 146 -4.982 2.869 45.037 1.00 43.57 C ANISOU 53 CA TRP A 146 3664 9200 3689 989 704 -42 C ATOM 54 CA VAL A 147 -4.109 1.756 48.573 1.00 48.76 C ANISOU 54 CA VAL A 147 4216 10671 3640 972 734 274 C ATOM 55 CA ASP A 148 -6.118 1.136 51.769 1.00 57.75 C ANISOU 55 CA ASP A 148 4890 12905 4148 1089 887 577 C ATOM 56 CA SER A 149 -3.198 2.384 53.870 1.00 57.00 C ANISOU 56 CA SER A 149 4990 13063 3605 1364 655 63 C ATOM 57 CA THR A 150 -0.036 4.313 53.019 1.00 56.43 C ANISOU 57 CA THR A 150 5394 12321 3724 1429 307 -714 C ATOM 58 CA PRO A 151 3.077 2.254 52.192 1.00 56.76 C ANISOU 58 CA PRO A 151 5633 11975 3960 1055 128 -106 C ATOM 59 CA PRO A 152 6.107 3.496 54.094 1.00 59.71 C ANISOU 59 CA PRO A 152 6053 12596 4037 1110 -226 -621 C ATOM 60 CA PRO A 153 8.675 5.985 52.703 1.00 62.08 C ANISOU 60 CA PRO A 153 6669 12166 4753 907 -668 -1442 C ATOM 61 CA GLY A 154 11.175 4.375 50.350 1.00 50.14 C ANISOU 61 CA GLY A 154 5190 10142 3720 582 -835 -860 C ATOM 62 CA THR A 155 8.462 2.288 48.728 1.00 41.93 C ANISOU 62 CA THR A 155 4183 8886 2861 658 -470 -179 C ATOM 63 CA ARG A 156 9.000 1.890 44.989 1.00 41.18 C ANISOU 63 CA ARG A 156 4277 7678 3691 429 -468 -7 C ATOM 64 CA VAL A 157 6.717 1.232 42.018 1.00 31.42 C ANISOU 64 CA VAL A 157 3167 5722 3048 348 -251 176 C ATOM 65 CA ARG A 158 7.970 -0.939 39.128 1.00 23.52 C ANISOU 65 CA ARG A 158 2251 4127 2557 259 -272 525 C ATOM 66 CA ALA A 159 6.475 -1.601 35.676 1.00 31.01 C ANISOU 66 CA ALA A 159 3304 4522 3957 176 -210 492 C ATOM 67 CA MET A 160 7.416 -4.462 33.340 1.00 29.94 C ANISOU 67 CA MET A 160 3269 3962 4143 244 -253 603 C ATOM 68 CA ALA A 161 5.903 -5.881 30.115 1.00 28.67 C ANISOU 68 CA ALA A 161 3208 3417 4269 188 -298 364 C ATOM 69 CA ILE A 162 5.661 -9.559 29.224 1.00 31.52 C ANISOU 69 CA ILE A 162 3786 3143 5047 210 -430 317 C ATOM 70 CA TYR A 163 3.971 -11.396 26.350 1.00 35.27 C ANISOU 70 CA TYR A 163 4395 3186 5821 65 -630 -195 C ATOM 71 CA LYS A 164 0.454 -12.578 27.246 1.00 34.69 C ANISOU 71 CA LYS A 164 4223 2846 6113 -605 -717 32 C ATOM 72 CA GLN A 165 0.681 -15.793 25.213 1.00 49.53 C ANISOU 72 CA GLN A 165 6477 3797 8546 -631 -1066 -534 C ATOM 73 CA SER A 166 2.486 -18.690 26.902 1.00 60.82 C ANISOU 73 CA SER A 166 8347 4239 10524 -402 -1137 -169 C ATOM 74 CA GLN A 167 4.448 -19.718 23.798 1.00 63.41 C ANISOU 74 CA GLN A 167 8922 4450 10723 279 -1285 -1177 C ATOM 75 CA HIS A 168 5.967 -16.219 23.762 1.00 51.19 C ANISOU 75 CA HIS A 168 6970 4028 8451 631 -1002 -1050 C ATOM 76 CA MET A 169 6.279 -15.540 27.488 1.00 48.57 C ANISOU 76 CA MET A 169 5416 4374 8664 800 -487 -92 C ATOM 77 CA THR A 170 9.977 -16.365 27.781 1.00 53.50 C ANISOU 77 CA THR A 170 5965 5096 9267 1604 -684 -38 C ATOM 78 CA GLU A 171 10.801 -13.781 25.099 1.00 51.23 C ANISOU 78 CA GLU A 171 5370 5979 8115 1850 -234 -744 C ATOM 79 CA VAL A 172 11.873 -10.353 26.370 1.00 39.26 C ANISOU 79 CA VAL A 172 3694 5438 5786 1300 19 -138 C ATOM 80 CA VAL A 173 9.541 -7.519 25.342 1.00 33.39 C ANISOU 80 CA VAL A 173 3194 4858 4634 848 224 -284 C ATOM 81 CA ARG A 174 11.613 -4.804 23.696 1.00 41.32 C ANISOU 81 CA ARG A 174 4032 6715 4951 628 257 -87 C ATOM 82 CA ARG A 175 11.223 -2.033 21.129 1.00 37.12 C ANISOU 82 CA ARG A 175 3627 6591 3885 278 167 118 C ATOM 83 CA CYS A 176 11.573 -2.905 17.453 1.00 39.21 C ANISOU 83 CA CYS A 176 3769 7728 3400 510 279 -185 C ATOM 84 CA PRO A 177 14.829 -1.688 15.830 1.00 44.16 C ANISOU 84 CA PRO A 177 3852 9807 3118 158 788 390 C ATOM 85 CA HIS A 178 13.071 1.180 14.040 1.00 51.27 C ANISOU 85 CA HIS A 178 5420 10569 3493 -589 194 1129 C ATOM 86 CA HIS A 179 11.698 2.778 17.192 1.00 37.59 C ANISOU 86 CA HIS A 179 4022 7318 2942 -726 -291 1291 C ATOM 87 CA GLU A 180 14.840 1.808 19.098 1.00 49.77 C ANISOU 87 CA GLU A 180 4922 9437 4551 -860 104 1346 C ATOM 88 CA ARG A 181 16.871 3.708 16.482 1.00 71.95 C ANISOU 88 CA ARG A 181 7648 14470 5218 -1920 957 429 C ATOM 89 CA CYS A 182 14.376 6.573 16.373 1.00 75.83 C ANISOU 89 CA CYS A 182 8835 13827 6148 -2487 -38 1994 C ATOM 90 CA SER A 183 15.326 10.031 17.601 1.00 82.23 C ANISOU 90 CA SER A 183 9396 13952 7897 -3165 -151 2947 C ATOM 91 CA ASP A 184 12.691 10.025 20.370 1.00 56.00 C ANISOU 91 CA ASP A 184 6145 8951 6182 -2236 -802 2714 C ATOM 92 CA SER A 185 14.966 9.874 23.425 1.00 56.23 C ANISOU 92 CA SER A 185 5661 8901 6801 -1914 -283 1850 C ATOM 93 CA ASP A 186 14.121 11.750 26.635 1.00 49.98 C ANISOU 93 CA ASP A 186 4984 6620 7385 -1873 -462 1746 C ATOM 94 CA GLY A 187 17.716 11.235 27.773 1.00 48.73 C ANISOU 94 CA GLY A 187 4320 7288 6905 -2016 -148 1227 C ATOM 95 CA LEU A 188 16.617 9.004 30.652 1.00 40.65 C ANISOU 95 CA LEU A 188 3778 5587 6080 -1319 -344 293 C ATOM 96 CA ALA A 189 15.100 5.829 29.144 1.00 30.17 C ANISOU 96 CA ALA A 189 2570 4730 4162 -576 -375 -82 C ATOM 97 CA PRO A 190 17.322 3.271 27.384 1.00 38.15 C ANISOU 97 CA PRO A 190 2959 7009 4526 -190 -223 -639 C ATOM 98 CA PRO A 191 16.498 3.127 23.659 1.00 41.02 C ANISOU 98 CA PRO A 191 3335 8282 3967 -413 120 -304 C ATOM 99 CA GLN A 192 15.412 -0.558 23.836 1.00 38.73 C ANISOU 99 CA GLN A 192 3225 7939 3551 526 -124 -1246 C ATOM 100 CA HIS A 193 12.794 -0.100 26.582 1.00 31.42 C ANISOU 100 CA HIS A 193 2962 5594 3382 680 -593 -1000 C ATOM 101 CA LEU A 194 9.114 -0.268 25.676 1.00 23.46 C ANISOU 101 CA LEU A 194 2426 3917 2570 789 -865 -668 C ATOM 102 CA ILE A 195 7.788 1.360 28.861 1.00 28.71 C ANISOU 102 CA ILE A 195 2760 4151 3997 -66 -394 5 C ATOM 103 CA ARG A 196 8.823 4.860 29.974 1.00 28.35 C ANISOU 103 CA ARG A 196 3104 4095 3573 -33 -267 23 C ATOM 104 CA VAL A 197 7.674 7.087 32.782 1.00 32.08 C ANISOU 104 CA VAL A 197 3481 4723 3986 206 -268 -103 C ATOM 105 CA GLU A 198 6.880 10.670 31.835 1.00 37.34 C ANISOU 105 CA GLU A 198 4890 4866 4432 517 -521 -294 C ATOM 106 CA GLY A 199 7.381 13.684 34.102 1.00 43.98 C ANISOU 106 CA GLY A 199 6109 5447 5154 619 -510 -622 C ATOM 107 CA ASN A 200 9.413 12.179 36.911 1.00 43.63 C ANISOU 107 CA ASN A 200 5575 5963 5039 367 -445 -768 C ATOM 108 CA LEU A 201 13.121 12.935 37.232 1.00 51.74 C ANISOU 108 CA LEU A 201 6453 6746 6461 -258 -647 -1197 C ATOM 109 CA ARG A 202 13.570 10.193 39.825 1.00 39.87 C ANISOU 109 CA ARG A 202 4626 6034 4487 239 -963 -1163 C ATOM 110 CA VAL A 203 12.693 7.486 37.311 1.00 29.57 C ANISOU 110 CA VAL A 203 3035 4788 3413 44 -453 -485 C ATOM 111 CA GLU A 204 15.126 4.548 37.159 1.00 31.20 C ANISOU 111 CA GLU A 204 2781 5220 3855 25 -567 -396 C ATOM 112 CA TYR A 205 15.530 1.921 34.417 1.00 30.34 C ANISOU 112 CA TYR A 205 2453 4972 4104 -174 -189 -86 C ATOM 113 CA LEU A 206 16.785 -1.643 34.816 1.00 33.63 C ANISOU 113 CA LEU A 206 2704 5447 4627 209 -282 102 C ATOM 114 CA ASP A 207 18.138 -4.234 32.404 1.00 29.56 C ANISOU 114 CA ASP A 207 2000 4700 4530 239 -25 70 C ATOM 115 CA ASP A 208 18.072 -7.347 34.580 1.00 41.14 C ANISOU 115 CA ASP A 208 3840 5975 5816 912 -302 474 C ATOM 116 CA ARG A 209 21.574 -8.882 34.510 1.00 48.20 C ANISOU 116 CA ARG A 209 4192 6965 7157 1606 -745 28 C ATOM 117 CA ASN A 210 20.115 -12.390 34.778 1.00 49.04 C ANISOU 117 CA ASN A 210 5268 6283 7083 1983 -548 681 C ATOM 118 CA THR A 211 16.733 -12.483 33.019 1.00 41.37 C ANISOU 118 CA THR A 211 4551 4877 6291 1039 106 899 C ATOM 119 CA PHE A 212 17.529 -9.611 30.603 1.00 36.73 C ANISOU 119 CA PHE A 212 3378 4852 5725 607 158 318 C ATOM 120 CA ARG A 213 14.064 -8.138 31.156 1.00 35.14 C ANISOU 120 CA ARG A 213 3341 4630 5380 123 226 559 C ATOM 121 CA HIS A 214 13.508 -4.387 31.112 1.00 29.35 C ANISOU 121 CA HIS A 214 2815 4993 3342 -95 23 271 C ATOM 122 CA SER A 215 11.643 -2.489 33.795 1.00 30.90 C ANISOU 122 CA SER A 215 2974 5376 3391 104 -240 374 C ATOM 123 CA VAL A 216 11.035 1.062 34.973 1.00 25.39 C ANISOU 123 CA VAL A 216 2823 4545 2277 613 -398 564 C ATOM 124 CA VAL A 217 10.725 2.101 38.621 1.00 31.99 C ANISOU 124 CA VAL A 217 3499 5406 3251 309 -322 524 C ATOM 125 CA VAL A 218 9.846 5.278 40.506 1.00 28.89 C ANISOU 125 CA VAL A 218 3394 4879 2704 661 -331 217 C ATOM 126 CA PRO A 219 9.494 6.157 44.190 1.00 36.92 C ANISOU 126 CA PRO A 219 4140 6282 3607 277 -180 -214 C ATOM 127 CA TYR A 220 5.959 5.746 45.547 1.00 37.68 C ANISOU 127 CA TYR A 220 3529 7271 3517 646 -203 -790 C ATOM 128 CA GLU A 221 4.374 9.074 46.459 1.00 50.55 C ANISOU 128 CA GLU A 221 5396 8644 5168 1313 -69 -1551 C ATOM 129 CA PRO A 222 1.308 9.184 48.707 1.00 47.38 C ANISOU 129 CA PRO A 222 4284 9170 4547 1593 108 -2243 C ATOM 130 CA PRO A 223 -1.725 10.885 47.175 1.00 55.47 C ANISOU 130 CA PRO A 223 5209 9898 5968 2697 71 -2510 C ATOM 131 CA GLU A 224 -2.538 14.456 48.121 1.00 78.98 C ANISOU 131 CA GLU A 224 8417 12131 9463 3277 445 -3278 C ATOM 132 CA VAL A 225 -4.659 14.730 51.266 1.00 77.78 C ANISOU 132 CA VAL A 225 7775 12703 9074 3051 771 -3945 C ATOM 133 CA GLY A 226 -7.556 15.803 49.041 1.00 89.21 C ANISOU 133 CA GLY A 226 9065 13636 11196 3973 695 -3557 C ATOM 134 CA SER A 227 -6.905 12.914 46.662 1.00 73.89 C ANISOU 134 CA SER A 227 7087 12130 8859 3772 122 -2697 C ATOM 135 CA ASP A 228 -7.668 9.185 46.669 1.00 64.08 C ANISOU 135 CA ASP A 228 5414 11797 7137 3160 -204 -2261 C ATOM 136 CA CYS A 229 -4.798 7.893 44.543 1.00 50.98 C ANISOU 136 CA CYS A 229 4118 9870 5383 2860 -449 -1820 C ATOM 137 CA THR A 230 -1.363 8.369 43.040 1.00 41.01 C ANISOU 137 CA THR A 230 4225 7174 4185 1053 -155 -1377 C ATOM 138 CA THR A 231 -1.153 8.703 39.261 1.00 30.78 C ANISOU 138 CA THR A 231 3058 4977 3659 623 -227 -1057 C ATOM 139 CA ILE A 232 1.847 7.545 37.241 1.00 32.97 C ANISOU 139 CA ILE A 232 3364 4998 4166 202 -329 -732 C ATOM 140 CA HIS A 233 2.134 8.712 33.618 1.00 32.48 C ANISOU 140 CA HIS A 233 3361 4407 4574 -82 -367 -463 C ATOM 141 CA TYR A 234 3.470 5.863 31.474 1.00 27.88 C ANISOU 141 CA TYR A 234 2731 4020 3842 -193 -205 -107 C ATOM 142 CA ASN A 235 4.468 6.030 27.795 1.00 31.29 C ANISOU 142 CA ASN A 235 3125 4489 4274 -329 -133 187 C ATOM 143 CA TYR A 236 4.555 2.973 25.530 1.00 27.74 C ANISOU 143 CA TYR A 236 2710 4310 3518 -177 0 134 C ATOM 144 CA MET A 237 7.181 3.562 22.854 1.00 34.34 C ANISOU 144 CA MET A 237 3341 5621 4084 -167 180 377 C ATOM 145 CA CYS A 238 6.311 0.910 20.241 1.00 36.28 C ANISOU 145 CA CYS A 238 3721 6196 3868 142 216 -11 C ATOM 146 CA TYR A 239 3.058 -0.129 18.534 1.00 35.12 C ANISOU 146 CA TYR A 239 3777 6040 3528 171 -60 -356 C ATOM 147 CA SER A 240 1.591 -3.592 19.165 1.00 33.77 C ANISOU 147 CA SER A 240 3776 5342 3712 220 -294 -999 C ATOM 148 CA SER A 241 1.757 -4.112 15.403 1.00 34.71 C ANISOU 148 CA SER A 241 3931 6206 3051 506 -391 -1493 C ATOM 149 CA CYS A 242 5.490 -3.257 14.985 1.00 37.95 C ANISOU 149 CA CYS A 242 4142 7207 3072 807 107 -1182 C ATOM 150 CA MET A 243 7.172 -5.847 12.786 1.00 49.84 C ANISOU 150 CA MET A 243 5676 9218 4044 1446 221 -2055 C ATOM 151 CA GLY A 244 10.376 -7.077 14.370 1.00 49.45 C ANISOU 151 CA GLY A 244 5433 8958 4397 1782 570 -2013 C ATOM 152 CA GLY A 245 9.009 -5.869 17.699 1.00 41.12 C ANISOU 152 CA GLY A 245 4442 7059 4124 1171 386 -1387 C ATOM 153 CA MET A 246 5.859 -7.063 19.494 1.00 38.92 C ANISOU 153 CA MET A 246 4442 5832 4516 817 -12 -1508 C ATOM 154 CA ASN A 247 4.600 -7.996 16.036 1.00 43.41 C ANISOU 154 CA ASN A 247 5154 6806 4534 1017 -243 -2280 C ATOM 155 CA ARG A 248 0.873 -8.197 16.855 1.00 47.24 C ANISOU 155 CA ARG A 248 5714 6698 5539 490 -697 -2250 C ATOM 156 CA ARG A 249 1.514 -10.292 19.986 1.00 45.29 C ANISOU 156 CA ARG A 249 5490 5475 6245 440 -630 -2031 C ATOM 157 CA PRO A 250 -0.485 -9.141 23.039 1.00 36.51 C ANISOU 157 CA PRO A 250 4206 4116 5551 -9 -592 -1214 C ATOM 158 CA ILE A 251 1.364 -8.049 26.171 1.00 35.22 C ANISOU 158 CA ILE A 251 3933 4077 5372 85 -264 -565 C ATOM 159 CA LEU A 252 0.569 -7.494 29.853 1.00 30.73 C ANISOU 159 CA LEU A 252 3188 3557 4931 -35 -129 106 C ATOM 160 CA THR A 253 1.973 -4.702 31.974 1.00 28.86 C ANISOU 160 CA THR A 253 2864 3884 4220 61 15 300 C ATOM 161 CA ILE A 254 2.776 -5.852 35.515 1.00 28.44 C ANISOU 161 CA ILE A 254 2648 4055 4102 229 97 804 C ATOM 162 CA ILE A 255 2.872 -3.200 38.255 1.00 34.00 C ANISOU 162 CA ILE A 255 3242 5459 4219 328 111 770 C ATOM 163 CA THR A 256 4.649 -4.244 41.433 1.00 37.96 C ANISOU 163 CA THR A 256 3544 6563 4314 610 86 1185 C ATOM 164 CA LEU A 257 4.892 -2.443 44.746 1.00 41.92 C ANISOU 164 CA LEU A 257 3894 8060 3972 860 -1 1040 C ATOM 165 CA GLU A 258 8.229 -3.039 46.512 1.00 38.49 C ANISOU 165 CA GLU A 258 3243 8222 3159 1084 -290 1188 C ATOM 166 CA ASP A 259 10.024 -1.866 49.669 1.00 48.04 C ANISOU 166 CA ASP A 259 4297 10300 3656 1268 -515 849 C ATOM 167 CA SER A 260 13.349 0.014 49.560 1.00 54.02 C ANISOU 167 CA SER A 260 4960 11041 4523 1062 -979 191 C ATOM 168 CA SER A 261 15.199 -3.334 49.633 1.00 52.59 C ANISOU 168 CA SER A 261 4577 10877 4528 1277 -858 1100 C ATOM 169 CA GLY A 262 13.192 -4.656 46.671 1.00 48.79 C ANISOU 169 CA GLY A 262 4292 9557 4689 1203 -554 1409 C ATOM 170 CA ASN A 263 10.865 -7.006 48.580 1.00 50.96 C ANISOU 170 CA ASN A 263 4559 10003 4799 1410 -237 2254 C ATOM 171 CA LEU A 264 7.430 -7.510 47.012 1.00 50.85 C ANISOU 171 CA LEU A 264 4693 9442 5187 1240 25 2506 C ATOM 172 CA LEU A 265 4.625 -5.532 48.680 1.00 46.08 C ANISOU 172 CA LEU A 265 4041 9546 3921 1255 211 2262 C ATOM 173 CA GLY A 266 1.903 -5.840 46.051 1.00 40.51 C ANISOU 173 CA GLY A 266 3479 7972 3940 910 410 2274 C ATOM 174 CA ARG A 267 1.212 -6.756 42.421 1.00 40.33 C ANISOU 174 CA ARG A 267 3679 6759 4887 534 364 2027 C ATOM 175 CA ASN A 268 -1.383 -6.063 39.733 1.00 39.35 C ANISOU 175 CA ASN A 268 3646 6087 5219 205 367 1642 C ATOM 176 CA SER A 269 -1.483 -6.277 35.940 1.00 30.55 C ANISOU 176 CA SER A 269 2766 4239 4601 -31 169 1102 C ATOM 177 CA PHE A 270 -3.458 -5.222 32.871 1.00 38.86 C ANISOU 177 CA PHE A 270 3888 5066 5810 -254 12 653 C ATOM 178 CA GLU A 271 -3.348 -6.103 29.192 1.00 30.62 C ANISOU 178 CA GLU A 271 3031 3661 4943 -361 -247 132 C ATOM 179 CA VAL A 272 -2.112 -3.365 26.849 1.00 29.14 C ANISOU 179 CA VAL A 272 2985 3847 4240 -239 -262 -174 C ATOM 180 CA ARG A 273 -2.584 -2.633 23.184 1.00 26.34 C ANISOU 180 CA ARG A 273 2698 3766 3545 -230 -450 -480 C ATOM 181 CA VAL A 274 -0.593 0.230 21.658 1.00 29.73 C ANISOU 181 CA VAL A 274 3135 4646 3515 -116 -302 -255 C ATOM 182 CA CYS A 275 -2.467 1.448 18.587 1.00 34.87 C ANISOU 182 CA CYS A 275 3734 5760 3757 -99 -524 -173 C ATOM 183 CA ALA A 276 -3.341 4.450 16.448 1.00 34.81 C ANISOU 183 CA ALA A 276 3604 6196 3427 -47 -612 417 C ATOM 184 CA ACYS A 277 -7.048 4.653 17.344 0.47 35.06 C ANISOU 184 CA ACYS A 277 3485 6001 3837 -97 -913 398 C ATOM 185 CA BCYS A 277 -7.034 4.674 17.369 0.53 34.89 C ANISOU 185 CA BCYS A 277 3464 5973 3820 -97 -910 402 C ATOM 186 CA PRO A 278 -7.589 3.425 20.932 1.00 35.84 C ANISOU 186 CA PRO A 278 3900 6234 3483 631 -47 -507 C ATOM 187 CA GLY A 279 -11.286 4.387 20.997 1.00 34.92 C ANISOU 187 CA GLY A 279 3559 6612 3099 446 -207 -377 C ATOM 188 CA ARG A 280 -12.270 2.526 17.845 1.00 40.02 C ANISOU 188 CA ARG A 280 4122 7925 3158 -214 -348 -901 C ATOM 189 CA ASP A 281 -10.110 -0.487 18.703 1.00 33.93 C ANISOU 189 CA ASP A 281 3827 6008 3056 -185 276 -1569 C ATOM 190 CA ARG A 282 -11.606 -0.685 22.185 1.00 28.97 C ANISOU 190 CA ARG A 282 2923 5083 3001 90 -35 -1072 C ATOM 191 CA ARG A 283 -15.154 -0.349 20.889 1.00 33.10 C ANISOU 191 CA ARG A 283 3259 6362 2957 -388 -483 -935 C ATOM 192 CA THR A 284 -14.421 -2.972 18.214 1.00 44.51 C ANISOU 192 CA THR A 284 5147 7841 3925 -1332 -25 -2068 C ATOM 193 CA GLU A 285 -12.947 -5.488 20.666 1.00 44.49 C ANISOU 193 CA GLU A 285 5094 6501 5308 -760 785 -2267 C ATOM 194 CA GLU A 286 -15.905 -5.057 23.050 1.00 36.01 C ANISOU 194 CA GLU A 286 3599 5661 4421 -452 -65 -1636 C ATOM 195 CA GLU A 287 -18.574 -5.622 20.390 1.00 58.90 C ANISOU 195 CA GLU A 287 6631 9465 6282 -1653 -486 -1887 C ATOM 196 CA ASN A 288 -17.327 -9.213 20.326 1.00 74.67 C ANISOU 196 CA ASN A 288 8998 10357 9015 -2009 788 -3167 C ATOM 197 CA LEU A 289 -18.707 -9.621 23.861 1.00 57.60 C ANISOU 197 CA LEU A 289 6073 7757 8055 -859 301 -2331 C HETATM 1540 ZN ZN A 401 8.222 -0.219 17.046 1.00 36.37 ZN CONECT 638 1540 CONECT 663 1540 CONECT 1140 1540 CONECT 1170 1540 CONECT 1540 638 663 1140 1170 END If you find results from this site helpful for your research, please 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