CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 24041412150577045

Job options:

ID        	=	 24041412150577045
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      12.232 -17.060  32.737  1.00 29.62           C  
ANISOU    1  CA  SER A  96     3702   2999   4553   1218    -36    918       C  
ATOM      2  CA  VAL A  97       8.881 -15.263  32.797  1.00 22.33           C  
ANISOU    2  CA  VAL A  97     3026   2232   3225     59    619     22       C  
ATOM      3  CA  PRO A  98       7.876 -12.600  35.357  1.00 21.08           C  
ANISOU    3  CA  PRO A  98     2584   2655   2769     57    645   -444       C  
ATOM      4  CA  SER A  99       4.789 -13.355  37.474  1.00 21.93           C  
ANISOU    4  CA  SER A  99     2885   2693   2757     -3    857     13       C  
ATOM      5  CA  GLN A 100       1.595 -11.608  36.364  1.00 24.12           C  
ANISOU    5  CA  GLN A 100     3170   3111   2882   -177    607    151       C  
ATOM      6  CA  LYS A 101      -0.450 -12.612  39.404  1.00 20.53           C  
ANISOU    6  CA  LYS A 101     2725   2634   2442   -318    530   -115       C  
ATOM      7  CA  THR A 102      -2.532  -9.758  40.816  1.00 17.74           C  
ANISOU    7  CA  THR A 102     2072   2550   2118   -188    -95    238       C  
ATOM      8  CA  TYR A 103      -1.535  -9.013  44.412  1.00 18.83           C  
ANISOU    8  CA  TYR A 103     2128   3068   1957   -181   -414    543       C  
ATOM      9  CA  GLN A 104      -3.064  -6.051  46.231  1.00 17.53           C  
ANISOU    9  CA  GLN A 104     1608   3352   1701     15    -58    741       C  
ATOM     10  CA  GLY A 105      -0.843  -6.696  49.244  1.00 17.65           C  
ANISOU   10  CA  GLY A 105     2301   3021   1384   -292    135    422       C  
ATOM     11  CA  SER A 106      -0.750  -4.950  52.604  1.00 20.02           C  
ANISOU   11  CA  SER A 106     2608   3406   1594   -265   -304    437       C  
ATOM     12  CA  TYR A 107      -1.438  -1.492  51.187  1.00 17.91           C  
ANISOU   12  CA  TYR A 107     2064   3147   1596   -263    -19    310       C  
ATOM     13  CA  GLY A 108      -4.372  -2.460  48.973  1.00 16.55           C  
ANISOU   13  CA  GLY A 108     1866   3037   1385    309    -96    107       C  
ATOM     14  CA  PHE A 109      -2.570  -1.670  45.730  1.00 15.40           C  
ANISOU   14  CA  PHE A 109     1682   2925   1246     50     20    508       C  
ATOM     15  CA  ARG A 110      -4.894  -1.182  42.741  1.00 16.22           C  
ANISOU   15  CA  ARG A 110     1807   2876   1480     19   -126    398       C  
ATOM     16  CA  LEU A 111      -4.693   0.483  39.334  1.00 12.49           C  
ANISOU   16  CA  LEU A 111     1224   2140   1381   -369     23     90       C  
ATOM     17  CA  GLY A 112      -7.176   3.060  38.082  1.00 12.53           C  
ANISOU   17  CA  GLY A 112     1626   1815   1319     86    -55    221       C  
ATOM     18  CA  PHE A 113      -7.646   4.629  34.666  1.00 12.54           C  
ANISOU   18  CA  PHE A 113     1588   1690   1487    376   -181     19       C  
ATOM     19  CA  LEU A 114      -9.356   7.684  33.188  1.00 13.36           C  
ANISOU   19  CA  LEU A 114     1605   1741   1731     59    -53   -257       C  
ATOM     20  CA  HIS A 115     -12.863   7.186  31.779  1.00 13.48           C  
ANISOU   20  CA  HIS A 115     1551   1851   1719     -9   -271   -375       C  
ATOM     21  CA  SER A 116     -12.091   8.744  28.419  1.00 12.97           C  
ANISOU   21  CA  SER A 116     1338   1895   1696     51   -150    -57       C  
ATOM     22  CA  GLY A 117     -14.608   7.106  26.092  1.00 12.60           C  
ANISOU   22  CA  GLY A 117     1540   1757   1490     72   -174   -176       C  
ATOM     23  CA  THR A 118     -14.071   6.081  22.450  1.00 13.67           C  
ANISOU   23  CA  THR A 118     1507   2288   1399   -109   -115    292       C  
ATOM     24  CA  ALA A 119     -14.526   9.262  20.384  1.00 15.44           C  
ANISOU   24  CA  ALA A 119     1818   2634   1415   -526   -201    690       C  
ATOM     25  CA  LYS A 120     -12.088   9.452  17.455  1.00 23.97           C  
ANISOU   25  CA  LYS A 120     3451   3938   1720   -829   -621    589       C  
ATOM     26  CA  SER A 121     -10.139  12.307  19.057  1.00 26.96           C  
ANISOU   26  CA  SER A 121     3676   3685   2881   -354   -205    329       C  
ATOM     27  CA  VAL A 122      -9.058  10.356  22.180  1.00 21.88           C  
ANISOU   27  CA  VAL A 122     2231   3273   2811   -126    381    391       C  
ATOM     28  CA  THR A 123      -5.328   9.634  22.437  1.00 23.06           C  
ANISOU   28  CA  THR A 123     2341   3498   2922   -279    473    750       C  
ATOM     29  CA  CYS A 124      -5.688   7.109  25.213  1.00 19.19           C  
ANISOU   29  CA  CYS A 124     1683   3209   2399   -354    135    -73       C  
ATOM     30  CA  THR A 125      -8.622   4.982  26.400  1.00 13.33           C  
ANISOU   30  CA  THR A 125     1505   1662   1898   -313   -449     -1       C  
ATOM     31  CA  TYR A 126      -9.024   2.052  28.809  1.00 10.90           C  
ANISOU   31  CA  TYR A 126     1590   1379   1171   -183   -615     77       C  
ATOM     32  CA  SER A 127     -11.437  -0.878  28.463  1.00 12.14           C  
ANISOU   32  CA  SER A 127     1922   1512   1179     13   -417    -21       C  
ATOM     33  CA  PRO A 128     -12.750  -2.223  31.814  1.00 12.27           C  
ANISOU   33  CA  PRO A 128     1867   1207   1587   -228    -79    171       C  
ATOM     34  CA  ALA A 129     -14.383  -5.187  30.082  1.00 13.71           C  
ANISOU   34  CA  ALA A 129     1607   1740   1863    -60    -84    -12       C  
ATOM     35  CA  LEU A 130     -11.102  -6.183  28.395  1.00 13.73           C  
ANISOU   35  CA  LEU A 130     1811   1576   1831   -147    -18    166       C  
ATOM     36  CA  ASN A 131      -8.746  -4.831  31.092  1.00 12.81           C  
ANISOU   36  CA  ASN A 131     1551   1914   1401     59     25    208       C  
ATOM     37  CA  LYS A 132      -7.031  -3.266  28.131  1.00 12.37           C  
ANISOU   37  CA  LYS A 132     1805   1513   1383    111      4   -189       C  
ATOM     38  CA AMET A 133      -5.407   0.061  27.468  0.76 12.69           C  
ANISOU   38  CA AMET A 133     1656   1954   1212    474    -11   -419       C  
ATOM     39  CA BMET A 133      -5.381   0.053  27.470  0.24 13.04           C  
ANISOU   39  CA BMET A 133     1858   1830   1267    586    -24   -342       C  
ATOM     40  CA  PHE A 134      -5.559   1.526  23.953  1.00 11.21           C  
ANISOU   40  CA  PHE A 134     1152   1893   1213    242     -2    129       C  
ATOM     41  CA  CYS A 135      -3.038   4.301  23.398  1.00 17.26           C  
ANISOU   41  CA  CYS A 135     1799   2817   1943      1    464    480       C  
ATOM     42  CA  GLN A 136      -1.046   6.147  20.757  1.00 19.02           C  
ANISOU   42  CA  GLN A 136     2216   2932   2080   -305    428    676       C  
ATOM     43  CA  LEU A 137       2.699   6.022  20.064  1.00 19.79           C  
ANISOU   43  CA  LEU A 137     2240   3245   2035     28    140    -90       C  
ATOM     44  CA  ALA A 138       4.698   8.343  22.358  1.00 19.52           C  
ANISOU   44  CA  ALA A 138     2578   3098   1742    -85   -198     16       C  
ATOM     45  CA  LYS A 139       1.515  10.020  23.681  1.00 19.05           C  
ANISOU   45  CA  LYS A 139     2635   2891   1713   -118   -160    672       C  
ATOM     46  CA  THR A 140       0.639  10.468  27.362  1.00 16.74           C  
ANISOU   46  CA  THR A 140     2077   2216   2066    241   -300    189       C  
ATOM     47  CA ACYS A 141      -0.841   7.385  29.003  0.39 14.90           C  
ANISOU   47  CA ACYS A 141     1742   1945   1975    311   -208    -48       C  
ATOM     48  CA BCYS A 141      -0.830   7.380  28.989  0.61 15.53           C  
ANISOU   48  CA BCYS A 141     1745   2091   2066    332   -265   -147       C  
ATOM     49  CA  PRO A 142      -2.205   8.125  32.472  1.00 14.41           C  
ANISOU   49  CA  PRO A 142     2250   1665   1559    319   -107    -61       C  
ATOM     50  CA  VAL A 143      -2.189   5.271  34.982  1.00 13.81           C  
ANISOU   50  CA  VAL A 143     2041   1382   1823    -70   -139   -260       C  
ATOM     51  CA  GLN A 144      -3.437   5.770  38.532  1.00 13.58           C  
ANISOU   51  CA  GLN A 144     1662   1397   2099    464     89   -285       C  
ATOM     52  CA  LEU A 145      -1.950   4.078  41.577  1.00 13.90           C  
ANISOU   52  CA  LEU A 145     1191   2249   1841    128     71   -591       C  
ATOM     53  CA  TRP A 146      -4.569   3.540  44.313  1.00 15.45           C  
ANISOU   53  CA  TRP A 146     1944   2433   1494    425    495    357       C  
ATOM     54  CA  VAL A 147      -3.747   2.333  47.832  1.00 18.71           C  
ANISOU   54  CA  VAL A 147     2491   3038   1580    530    206    386       C  
ATOM     55  CA  ASP A 148      -5.829   1.799  50.978  1.00 22.43           C  
ANISOU   55  CA  ASP A 148     2866   3692   1963    305    531    -64       C  
ATOM     56  CA  SER A 149      -2.825   2.700  53.148  1.00 24.52           C  
ANISOU   56  CA  SER A 149     3027   3995   2295    316    375    230       C  
ATOM     57  CA  THR A 150       0.270   4.808  52.378  1.00 25.42           C  
ANISOU   57  CA  THR A 150     2713   4087   2861   -202    242   -501       C  
ATOM     58  CA  PRO A 151       3.375   2.632  51.674  1.00 24.46           C  
ANISOU   58  CA  PRO A 151     2435   4482   2376   -578    258   -654       C  
ATOM     59  CA  PRO A 152       6.740   3.213  53.464  1.00 26.65           C  
ANISOU   59  CA  PRO A 152     2839   4929   2356  -1317   -698   -262       C  
ATOM     60  CA  PRO A 153       9.246   5.982  52.648  1.00 28.30           C  
ANISOU   60  CA  PRO A 153     3491   4959   2301  -1496   -139   -666       C  
ATOM     61  CA  GLY A 154      11.402   4.828  49.742  1.00 19.85           C  
ANISOU   61  CA  GLY A 154     2040   3801   1701   -932   -247   -326       C  
ATOM     62  CA  THR A 155       8.702   2.710  48.101  1.00 15.73           C  
ANISOU   62  CA  THR A 155     1518   3123   1335     17   -344    302       C  
ATOM     63  CA  ARG A 156       9.069   2.447  44.304  1.00 13.98           C  
ANISOU   63  CA  ARG A 156     1488   2609   1217     50   -361   -172       C  
ATOM     64  CA  PHE A 157       6.804   1.273  41.484  1.00 11.74           C  
ANISOU   64  CA  PHE A 157     1578   1946    936    376     18   -260       C  
ATOM     65  CA  ARG A 158       8.039  -0.534  38.383  1.00 10.91           C  
ANISOU   65  CA  ARG A 158     1350   1666   1128    453   -178     57       C  
ATOM     66  CA  ALA A 159       6.529  -1.137  34.922  1.00  9.76           C  
ANISOU   66  CA  ALA A 159     1134   1369   1207    140   -157    -15       C  
ATOM     67  CA  MET A 160       7.544  -4.028  32.675  1.00 12.83           C  
ANISOU   67  CA  MET A 160     1409   1658   1807    204   -161   -290       C  
ATOM     68  CA  ALA A 161       6.046  -5.383  29.453  1.00 13.05           C  
ANISOU   68  CA  ALA A 161     1744   1520   1696    392   -176   -376       C  
ATOM     69  CA  ILE A 162       5.664  -9.066  28.568  1.00 13.28           C  
ANISOU   69  CA  ILE A 162     1683   1754   1608    -13     93   -310       C  
ATOM     70  CA  TYR A 163       4.024 -10.830  25.629  1.00 15.74           C  
ANISOU   70  CA  TYR A 163     1753   2318   1910   -210   -273   -333       C  
ATOM     71  CA  LYS A 164       0.473 -11.896  26.455  1.00 19.87           C  
ANISOU   71  CA  LYS A 164     2220   2952   2376   -194   -269    117       C  
ATOM     72  CA  GLN A 165       0.603 -15.150  24.472  1.00 23.57           C  
ANISOU   72  CA  GLN A 165     2910   2929   3117   -253   -475    -74       C  
ATOM     73  CA  SER A 166       2.307 -18.057  26.232  1.00 27.08           C  
ANISOU   73  CA  SER A 166     3897   3001   3391    -95   -889   -335       C  
ATOM     74  CA  GLN A 167       4.193 -19.065  23.072  1.00 28.86           C  
ANISOU   74  CA  GLN A 167     4014   3010   3942    153   -499   -721       C  
ATOM     75  CA  HIS A 168       5.913 -15.650  23.112  1.00 23.66           C  
ANISOU   75  CA  HIS A 168     2813   2879   3299     71   -171  -1284       C  
ATOM     76  CA  MET A 169       6.236 -15.019  26.868  1.00 24.06           C  
ANISOU   76  CA  MET A 169     2923   2939   3280     50   -166   -819       C  
ATOM     77  CA  THR A 170       9.959 -15.859  27.105  1.00 21.46           C  
ANISOU   77  CA  THR A 170     2354   2655   3146    532   -261  -1091       C  
ATOM     78  CA  GLU A 171      10.796 -13.305  24.422  1.00 21.17           C  
ANISOU   78  CA  GLU A 171     2255   3003   2787    293     43   -823       C  
ATOM     79  CA  VAL A 172      11.909  -9.945  25.798  1.00 17.79           C  
ANISOU   79  CA  VAL A 172     1812   2851   2094    139    -14   -371       C  
ATOM     80  CA  VAL A 173       9.633  -7.086  24.740  1.00 15.07           C  
ANISOU   80  CA  VAL A 173     1443   2624   1660    344    -28     -8       C  
ATOM     81  CA  ARG A 174      11.790  -4.411  23.113  1.00 19.48           C  
ANISOU   81  CA  ARG A 174     1630   3637   2135    395     -9     31       C  
ATOM     82  CA  ARG A 175      11.494  -1.683  20.489  1.00 18.81           C  
ANISOU   82  CA  ARG A 175     1907   3773   1468     36     57    -31       C  
ATOM     83  CA  CYS A 176      11.866  -2.566  16.808  1.00 20.36           C  
ANISOU   83  CA  CYS A 176     2019   4309   1410    628    178    172       C  
ATOM     84  CA  PRO A 177      15.235  -1.668  15.216  1.00 22.48           C  
ANISOU   84  CA  PRO A 177     2005   4790   1745    777    354    377       C  
ATOM     85  CA  HIS A 178      13.605   1.307  13.444  1.00 18.98           C  
ANISOU   85  CA  HIS A 178     1423   4425   1363    477    -41   -103       C  
ATOM     86  CA  HIS A 179      12.346   2.915  16.640  1.00 18.99           C  
ANISOU   86  CA  HIS A 179     1467   4559   1189     32    -38    148       C  
ATOM     87  CA  GLU A 180      15.459   1.938  18.575  1.00 25.11           C  
ANISOU   87  CA  GLU A 180     1779   5828   1933   -178    271     59       C  
ATOM     88  CA  ARG A 181      17.402   3.983  16.013  1.00 34.91           C  
ANISOU   88  CA  ARG A 181     3304   6767   3194   -834   -151     58       C  
ATOM     89  CA  CYS A 182      14.841   6.800  15.892  1.00 35.22           C  
ANISOU   89  CA  CYS A 182     3838   6313   3232  -1242   -893    599       C  
ATOM     90  CA  SER A 183      15.964  10.206  17.168  1.00 36.41           C  
ANISOU   90  CA  SER A 183     4266   5698   3870  -1348    265    854       C  
ATOM     91  CA  ASP A 184      13.174  10.314  19.754  1.00 29.49           C  
ANISOU   91  CA  ASP A 184     3518   4554   3132  -1321    184   1082       C  
ATOM     92  CA  SER A 185      15.337  10.161  22.877  1.00 28.63           C  
ANISOU   92  CA  SER A 185     3412   4159   3308   -649    128   1103       C  
ATOM     93  CA  ASP A 186      14.324  12.070  26.003  1.00 25.25           C  
ANISOU   93  CA  ASP A 186     3076   3395   3124   -697   -163    669       C  
ATOM     94  CA  GLY A 187      17.878  11.819  27.303  1.00 22.65           C  
ANISOU   94  CA  GLY A 187     2554   3125   2926   -572   -322    394       C  
ATOM     95  CA  LEU A 188      16.845   9.423  30.069  1.00 19.54           C  
ANISOU   95  CA  LEU A 188     2002   2919   2502   -603   -568    169       C  
ATOM     96  CA  ALA A 189      15.290   6.307  28.539  1.00 16.66           C  
ANISOU   96  CA  ALA A 189     1544   3042   1744    -14   -366    231       C  
ATOM     97  CA  PRO A 190      17.491   3.666  26.850  1.00 16.37           C  
ANISOU   97  CA  PRO A 190     1430   3218   1570   -304   -256    272       C  
ATOM     98  CA  PRO A 191      16.739   3.430  23.116  1.00 18.36           C  
ANISOU   98  CA  PRO A 191     1629   3985   1361   -390    245    139       C  
ATOM     99  CA  GLN A 192      15.678  -0.253  23.335  1.00 17.30           C  
ANISOU   99  CA  GLN A 192     1722   3390   1461    259    353    296       C  
ATOM    100  CA  HIS A 193      13.032   0.362  26.008  1.00 11.51           C  
ANISOU  100  CA  HIS A 193     1018   2382    975    133   -257    100       C  
ATOM    101  CA  LEU A 194       9.360   0.188  25.021  1.00 12.11           C  
ANISOU  101  CA  LEU A 194     1225   2023   1353    166   -237    119       C  
ATOM    102  CA  ILE A 195       7.968   1.873  28.144  1.00 12.96           C  
ANISOU  102  CA  ILE A 195     1334   1840   1749    168    -47    142       C  
ATOM    103  CA  ARG A 196       9.038   5.378  29.238  1.00 13.09           C  
ANISOU  103  CA  ARG A 196     1265   1705   2004   -270   -138    309       C  
ATOM    104  CA  VAL A 197       7.908   7.631  32.051  1.00 14.38           C  
ANISOU  104  CA  VAL A 197     2122   1391   1952   -223   -153    -78       C  
ATOM    105  CA  GLU A 198       6.983  11.180  31.133  1.00 19.66           C  
ANISOU  105  CA  GLU A 198     3100   1638   2733   -224   -338    283       C  
ATOM    106  CA  GLY A 199       7.561  14.251  33.324  1.00 19.65           C  
ANISOU  106  CA  GLY A 199     3118   1557   2792     -9   -406    654       C  
ATOM    107  CA  ASN A 200       9.582  12.707  36.161  1.00 17.87           C  
ANISOU  107  CA  ASN A 200     2364   1827   2598    308   -357     89       C  
ATOM    108  CA  LEU A 201      13.320  13.359  36.460  1.00 21.94           C  
ANISOU  108  CA  LEU A 201     2877   2125   3336   -102   -423    -75       C  
ATOM    109  CA  ARG A 202      13.735  10.687  39.156  1.00 17.53           C  
ANISOU  109  CA  ARG A 202     2056   2100   2506    -27      5   -130       C  
ATOM    110  CA  VAL A 203      12.832   7.961  36.676  1.00 11.38           C  
ANISOU  110  CA  VAL A 203     1361   1327   1635   -355   -312   -137       C  
ATOM    111  CA  GLU A 204      15.191   4.961  36.603  1.00 11.12           C  
ANISOU  111  CA  GLU A 204     1696   1078   1450   -140   -467    405       C  
ATOM    112  CA  TYR A 205      15.595   2.341  33.866  1.00 11.83           C  
ANISOU  112  CA  TYR A 205     1511   1554   1429    149   -422    397       C  
ATOM    113  CA  LEU A 206      16.862  -1.228  34.206  1.00 11.45           C  
ANISOU  113  CA  LEU A 206     1215   1400   1737   -186   -391    315       C  
ATOM    114  CA  ASP A 207      18.222  -3.866  31.857  1.00 13.58           C  
ANISOU  114  CA  ASP A 207     1326   1849   1986    111   -543    255       C  
ATOM    115  CA  ASP A 208      18.093  -6.986  34.020  1.00 17.36           C  
ANISOU  115  CA  ASP A 208     1771   1538   3286    464   -553   -110       C  
ATOM    116  CA  ARG A 209      21.554  -8.547  33.880  1.00 25.72           C  
ANISOU  116  CA  ARG A 209     2629   2703   4440    412   -842   -320       C  
ATOM    117  CA  ASN A 210      20.093 -12.055  34.298  1.00 25.34           C  
ANISOU  117  CA  ASN A 210     2502   2601   4525    702  -1040   -954       C  
ATOM    118  CA  THR A 211      16.714 -12.062  32.534  1.00 22.10           C  
ANISOU  118  CA  THR A 211     2189   2189   4019    -10   -557   -910       C  
ATOM    119  CA  PHE A 212      17.553  -9.217  30.112  1.00 19.49           C  
ANISOU  119  CA  PHE A 212     2125   2149   3133    186    148   -633       C  
ATOM    120  CA  ARG A 213      14.080  -7.775  30.748  1.00 17.37           C  
ANISOU  120  CA  ARG A 213     1974   2079   2548     48    -88   -436       C  
ATOM    121  CA  HIS A 214      13.592  -4.017  30.490  1.00 12.57           C  
ANISOU  121  CA  HIS A 214     1590   1574   1611    -98    252   -185       C  
ATOM    122  CA  SER A 215      11.757  -2.066  33.178  1.00 10.26           C  
ANISOU  122  CA  SER A 215     1069   1579   1250    -15   -136    156       C  
ATOM    123  CA  VAL A 216      11.223   1.476  34.359  1.00 10.65           C  
ANISOU  123  CA  VAL A 216     1301   1818    926    157   -158   -149       C  
ATOM    124  CA  VAL A 217      11.018   2.363  38.043  1.00 13.08           C  
ANISOU  124  CA  VAL A 217     1687   2093   1189    427   -334      3       C  
ATOM    125  CA  VAL A 218       9.895   5.530  39.843  1.00 13.83           C  
ANISOU  125  CA  VAL A 218     1745   2199   1311    309   -279    219       C  
ATOM    126  CA  PRO A 219       9.839   6.716  43.505  1.00 16.27           C  
ANISOU  126  CA  PRO A 219     1784   2652   1744   -130   -413   -385       C  
ATOM    127  CA  TYR A 220       6.299   6.422  44.910  1.00 17.77           C  
ANISOU  127  CA  TYR A 220     2105   3034   1613    154    300   -397       C  
ATOM    128  CA  GLU A 221       4.821   9.695  46.104  1.00 25.83           C  
ANISOU  128  CA  GLU A 221     3323   3825   2665    385    145  -1149       C  
ATOM    129  CA  PRO A 222       1.549   9.685  48.065  1.00 27.48           C  
ANISOU  129  CA  PRO A 222     3473   3773   3197    803     87   -997       C  
ATOM    130  CA  PRO A 223      -1.312  11.773  46.638  1.00 29.54           C  
ANISOU  130  CA  PRO A 223     3505   3920   3800   1190    362  -1322       C  
ATOM    131  CA  GLU A 224      -1.899  15.372  47.709  1.00 36.55           C  
ANISOU  131  CA  GLU A 224     4374   4584   4929   1355    535  -1038       C  
ATOM    132  CA  VAL A 225      -4.011  15.286  50.880  1.00 38.49           C  
ANISOU  132  CA  VAL A 225     4590   4853   5183   1702    452  -1350       C  
ATOM    133  CA  GLY A 226      -7.057  16.353  48.870  1.00 38.33           C  
ANISOU  133  CA  GLY A 226     4433   4702   5427   2162    660  -1492       C  
ATOM    134  CA  SER A 227      -6.385  13.678  46.225  1.00 37.48           C  
ANISOU  134  CA  SER A 227     4189   4608   5442   1521    854  -1036       C  
ATOM    135  CA  ASP A 228      -7.357  10.004  45.933  1.00 33.28           C  
ANISOU  135  CA  ASP A 228     3487   4365   4792    969   1192   -829       C  
ATOM    136  CA  CYS A 229      -4.490   8.577  43.890  1.00 23.48           C  
ANISOU  136  CA  CYS A 229     2329   3512   3082    158    288   -545       C  
ATOM    137  CA  THR A 230      -1.120   9.117  42.269  1.00 19.65           C  
ANISOU  137  CA  THR A 230     2039   3327   2100   -430     61   -551       C  
ATOM    138  CA  THR A 231      -1.052   9.558  38.497  1.00 18.67           C  
ANISOU  138  CA  THR A 231     1837   2722   2533   -432     23   -661       C  
ATOM    139  CA  ILE A 232       1.937   8.412  36.460  1.00 18.94           C  
ANISOU  139  CA  ILE A 232     1972   2779   2444   -340   -371   -346       C  
ATOM    140  CA  HIS A 233       2.326   9.268  32.770  1.00 14.21           C  
ANISOU  140  CA  HIS A 233     1638   1729   2033   -102   -259    -63       C  
ATOM    141  CA  TYR A 234       3.686   6.431  30.659  1.00 11.19           C  
ANISOU  141  CA  TYR A 234     1274   1715   1265    -32   -409    319       C  
ATOM    142  CA  ASN A 235       4.723   6.602  26.996  1.00 13.62           C  
ANISOU  142  CA  ASN A 235     1510   2236   1428   -251   -706    108       C  
ATOM    143  CA  TYR A 236       4.785   3.509  24.787  1.00 11.89           C  
ANISOU  143  CA  TYR A 236     1238   1993   1287   -267    110    652       C  
ATOM    144  CA  MET A 237       7.489   4.008  22.180  1.00 14.32           C  
ANISOU  144  CA  MET A 237     1353   2628   1461   -409    100    210       C  
ATOM    145  CA  CYS A 238       6.488   1.399  19.570  1.00 16.87           C  
ANISOU  145  CA  CYS A 238     1719   3308   1384   -175    -89   -184       C  
ATOM    146  CA  ASN A 239       3.189   0.588  17.858  1.00 17.32           C  
ANISOU  146  CA  ASN A 239     2022   3388   1169   -218    433    101       C  
ATOM    147  CA  SER A 240       1.639  -2.859  18.312  1.00 17.03           C  
ANISOU  147  CA  SER A 240     1904   3401   1163   -335    356    -72       C  
ATOM    148  CA  SER A 241       1.943  -3.153  14.527  1.00 21.75           C  
ANISOU  148  CA  SER A 241     2491   4314   1458   -184    165   -199       C  
ATOM    149  CA  CYS A 242       5.695  -2.423  14.365  1.00 22.44           C  
ANISOU  149  CA  CYS A 242     2220   4686   1619    166    350     24       C  
ATOM    150  CA  MET A 243       7.492  -4.770  11.962  1.00 23.26           C  
ANISOU  150  CA  MET A 243     2687   4630   1522    478    312    193       C  
ATOM    151  CA  GLY A 244      10.476  -6.317  13.734  1.00 23.64           C  
ANISOU  151  CA  GLY A 244     3148   4055   1779    711    434   -449       C  
ATOM    152  CA  GLY A 245       9.211  -5.312  17.161  1.00 24.72           C  
ANISOU  152  CA  GLY A 245     3192   4032   2167    -29    885   -570       C  
ATOM    153  CA  MET A 246       5.987  -6.429  18.817  1.00 22.10           C  
ANISOU  153  CA  MET A 246     2919   3838   1640    -14    537  -1064       C  
ATOM    154  CA  ASN A 247       5.071  -7.500  15.285  1.00 27.16           C  
ANISOU  154  CA  ASN A 247     4383   4134   1802   -171   -137  -1287       C  
ATOM    155  CA  ARG A 248       1.290  -7.418  15.893  1.00 27.29           C  
ANISOU  155  CA  ARG A 248     4294   4064   2012    -49   -330  -1069       C  
ATOM    156  CA  ARG A 249       1.652  -9.433  19.137  1.00 22.90           C  
ANISOU  156  CA  ARG A 249     3360   3510   1830    244   -434   -998       C  
ATOM    157  CA  PRO A 250      -0.428  -8.338  22.173  1.00 19.54           C  
ANISOU  157  CA  PRO A 250     2309   3058   2056   -321   -220   -805       C  
ATOM    158  CA  ILE A 251       1.480  -7.357  25.331  1.00 15.43           C  
ANISOU  158  CA  ILE A 251     1852   2179   1833     67    -99   -672       C  
ATOM    159  CA  LEU A 252       0.714  -6.864  29.025  1.00 15.46           C  
ANISOU  159  CA  LEU A 252     1871   2078   1924     89   -197   -372       C  
ATOM    160  CA  THR A 253       2.176  -4.176  31.239  1.00 12.81           C  
ANISOU  160  CA  THR A 253     1631   1934   1304    458   -143   -116       C  
ATOM    161  CA  ILE A 254       2.918  -5.409  34.768  1.00 11.70           C  
ANISOU  161  CA  ILE A 254     1509   1705   1232     66    -18    -58       C  
ATOM    162  CA  ILE A 255       3.085  -2.763  37.512  1.00 10.92           C  
ANISOU  162  CA  ILE A 255     1575   1608    967   -317     17    200       C  
ATOM    163  CA  THR A 256       4.821  -3.885  40.704  1.00 13.80           C  
ANISOU  163  CA  THR A 256     1999   1829   1416   -464    204    174       C  
ATOM    164  CA  LEU A 257       4.956  -1.964  43.963  1.00 14.17           C  
ANISOU  164  CA  LEU A 257     1809   2261   1313    332   -240     29       C  
ATOM    165  CA  GLU A 258       8.238  -2.601  45.767  1.00 16.41           C  
ANISOU  165  CA  GLU A 258     1637   3081   1518    146     58    171       C  
ATOM    166  CA  ASP A 259      10.028  -1.444  48.912  1.00 17.83           C  
ANISOU  166  CA  ASP A 259     1879   3298   1596   -185   -124    378       C  
ATOM    167  CA  SER A 260      13.360   0.410  48.999  1.00 20.52           C  
ANISOU  167  CA  SER A 260     2063   3558   2174    335   -234    220       C  
ATOM    168  CA  SER A 261      15.138  -2.979  48.913  1.00 20.86           C  
ANISOU  168  CA  SER A 261     1914   3532   2478    479      3    273       C  
ATOM    169  CA  GLY A 262      13.115  -4.176  45.929  1.00 19.87           C  
ANISOU  169  CA  GLY A 262     1839   3283   2427    244    243    390       C  
ATOM    170  CA  ASN A 263      10.887  -6.533  47.923  1.00 20.11           C  
ANISOU  170  CA  ASN A 263     1971   3139   2532    448   -413    679       C  
ATOM    171  CA  LEU A 264       7.451  -7.148  46.360  1.00 18.35           C  
ANISOU  171  CA  LEU A 264     2352   2340   2281    142   -318    306       C  
ATOM    172  CA  LEU A 265       4.608  -5.169  47.985  1.00 13.63           C  
ANISOU  172  CA  LEU A 265     1854   1680   1644   -247   -143    552       C  
ATOM    173  CA  GLY A 266       1.930  -5.386  45.285  1.00 12.20           C  
ANISOU  173  CA  GLY A 266     1557   1619   1458   -151   -180    759       C  
ATOM    174  CA  ARG A 267       1.282  -6.279  41.638  1.00 12.59           C  
ANISOU  174  CA  ARG A 267     1558   1802   1423   -150   -462    696       C  
ATOM    175  CA  ASN A 268      -1.282  -5.412  38.972  1.00 14.68           C  
ANISOU  175  CA  ASN A 268     2060   2392   1125   -504   -212    333       C  
ATOM    176  CA  SER A 269      -1.397  -5.700  35.200  1.00 12.63           C  
ANISOU  176  CA  SER A 269     1760   1828   1213     54   -517     78       C  
ATOM    177  CA  PHE A 270      -3.283  -4.616  32.083  1.00  9.97           C  
ANISOU  177  CA  PHE A 270     1501   1228   1057    -71    177   -202       C  
ATOM    178  CA  GLU A 271      -3.131  -5.494  28.397  1.00 12.90           C  
ANISOU  178  CA  GLU A 271     1865   1757   1280     59   -380   -292       C  
ATOM    179  CA  VAL A 272      -1.923  -2.787  25.997  1.00 14.48           C  
ANISOU  179  CA  VAL A 272     2099   1985   1420   -162   -132   -199       C  
ATOM    180  CA  ARG A 273      -2.477  -2.056  22.328  1.00 13.60           C  
ANISOU  180  CA  ARG A 273     1674   2145   1349    360     74   -267       C  
ATOM    181  CA  VAL A 274      -0.481   0.853  20.930  1.00 13.86           C  
ANISOU  181  CA  VAL A 274     1448   2785   1033    223      1    -66       C  
ATOM    182  CA  CYS A 275      -2.357   2.077  17.843  1.00 17.77           C  
ANISOU  182  CA  CYS A 275     1773   3488   1491     85   -182   -121       C  
ATOM    183  CA  ALA A 276      -3.265   5.044  15.651  1.00 19.67           C  
ANISOU  183  CA  ALA A 276     2131   3890   1452    487    337    212       C  
ATOM    184  CA ACYS A 277      -6.962   5.124  16.630  0.58 20.37           C  
ANISOU  184  CA ACYS A 277     1791   4097   1851   -129   -390    506       C  
ATOM    185  CA BCYS A 277      -6.951   5.145  16.648  0.42 19.97           C  
ANISOU  185  CA BCYS A 277     1633   4012   1941     50   -350    462       C  
ATOM    186  CA  PRO A 278      -7.443   4.004  20.270  1.00 15.16           C  
ANISOU  186  CA  PRO A 278     1194   3046   1521   -133   -314    -60       C  
ATOM    187  CA  GLY A 279     -11.140   4.955  20.384  1.00 16.28           C  
ANISOU  187  CA  GLY A 279     1452   3303   1430    502   -499   -555       C  
ATOM    188  CA  ARG A 280     -12.016   3.143  17.159  1.00 20.38           C  
ANISOU  188  CA  ARG A 280     2552   3936   1254    216   -584   -343       C  
ATOM    189  CA  ASP A 281      -9.980   0.074  18.060  1.00 17.06           C  
ANISOU  189  CA  ASP A 281     2150   3306   1025    342   -293   -500       C  
ATOM    190  CA  ARG A 282     -11.460  -0.175  21.568  1.00 12.51           C  
ANISOU  190  CA  ARG A 282     1510   2174   1068     25     68   -628       C  
ATOM    191  CA  ARG A 283     -15.024   0.170  20.295  1.00 16.61           C  
ANISOU  191  CA  ARG A 283     1581   3036   1695    -84    -77   -121       C  
ATOM    192  CA  THR A 284     -14.337  -2.474  17.637  1.00 19.92           C  
ANISOU  192  CA  THR A 284     2193   3414   1963   -673     71   -784       C  
ATOM    193  CA  GLU A 285     -12.741  -4.966  20.040  1.00 24.58           C  
ANISOU  193  CA  GLU A 285     2703   3939   2699   -436   -284  -1430       C  
ATOM    194  CA  GLU A 286     -15.633  -4.609  22.470  1.00 25.85           C  
ANISOU  194  CA  GLU A 286     2540   4261   3020   -826  -1023   -961       C  
ATOM    195  CA  GLU A 287     -18.087  -5.296  19.624  1.00 37.55           C  
ANISOU  195  CA  GLU A 287     4198   5685   4384  -1123   -669  -1049       C  
ATOM    196  CA  ASN A 288     -17.136  -8.976  20.024  1.00 43.35           C  
ANISOU  196  CA  ASN A 288     5579   5509   5382  -1210    246  -1191       C  
ATOM    197  CA  LEU A 289     -18.534  -9.100  23.577  1.00 38.19           C  
ANISOU  197  CA  LEU A 289     4938   4667   4906  -1730    766  -1121       C  
HETATM 1540 ZN    ZN A 401       8.654   0.295  16.522  1.00 15.70          ZN  
CONECT  642 1540
CONECT  667 1540
CONECT 1144 1540
CONECT 1170 1540
CONECT 1540  642  667 1144 1170
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.