CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 240818122744891385

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.