***    ***
Job options:
ID = 240818122744891385
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
END
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elNémo
is maintained by Yves-Henri Sanejouand.
It was developed
by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.
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