CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 240818121738854229

Job options:

ID        	=	 240818121738854229
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  95      20.690  21.163  17.849  1.00 88.39           C  
ANISOU    1  CA  SER A  95    12610   9298  11675   1642   -424    413       C  
ATOM      2  CA  SER A  96      18.636  17.992  17.361  1.00 81.97           C  
ANISOU    2  CA  SER A  96    11054   9145  10947   1727   -523    653       C  
ATOM      3  CA  VAL A  97      21.566  16.373  15.542  1.00 45.25           C  
ANISOU    3  CA  VAL A  97     6666   4514   6012   1137   -748    584       C  
ATOM      4  CA  PRO A  98      22.612  12.996  17.041  1.00 27.09           C  
ANISOU    4  CA  PRO A  98     3986   2643   3663    859   -625    347       C  
ATOM      5  CA  SER A  99      25.570  13.147  19.442  1.00 22.34           C  
ANISOU    5  CA  SER A  99     3611   1963   2913    631   -437      5       C  
ATOM      6  CA  GLN A 100      28.884  11.937  18.033  1.00 19.41           C  
ANISOU    6  CA  GLN A 100     3239   1708   2428     90   -464    -69       C  
ATOM      7  CA  LYS A 101      30.756  12.317  21.322  1.00 16.68           C  
ANISOU    7  CA  LYS A 101     2930   1430   1977      4   -394   -285       C  
ATOM      8  CA  THR A 102      32.908   9.315  22.235  1.00 14.67           C  
ANISOU    8  CA  THR A 102     2221   1598   1757   -152   -354   -247       C  
ATOM      9  CA  TYR A 103      32.165   7.489  25.476  1.00 17.11           C  
ANISOU    9  CA  TYR A 103     2283   2198   2020     81   -310   -182       C  
ATOM     10  CA  GLN A 104      33.666   4.104  26.336  1.00 16.35           C  
ANISOU   10  CA  GLN A 104     1738   2390   2083    100   -293     55       C  
ATOM     11  CA  GLY A 105      31.195   3.850  29.207  1.00 16.16           C  
ANISOU   11  CA  GLY A 105     1728   2535   1875    342   -218    162       C  
ATOM     12  CA  SER A 106      30.880   1.096  31.800  1.00 20.16           C  
ANISOU   12  CA  SER A 106     1945   3362   2355    462   -169    555       C  
ATOM     13  CA  TYR A 107      31.904  -1.690  29.425  1.00 17.15           C  
ANISOU   13  CA  TYR A 107     1335   2689   2494    442   -173    708       C  
ATOM     14  CA  GLY A 108      35.026  -0.043  28.007  1.00 17.78           C  
ANISOU   14  CA  GLY A 108     1438   2802   2516    277   -271    468       C  
ATOM     15  CA  PHE A 109      33.531   0.184  24.528  1.00 14.24           C  
ANISOU   15  CA  PHE A 109     1184   1980   2246    230   -167    236       C  
ATOM     16  CA AARG A 110      36.079   0.602  21.728  0.56 17.46           C  
ANISOU   16  CA AARG A 110     1809   2619   2205    156    -42     81       C  
ATOM     17  CA BARG A 110      36.079   0.610  21.734  0.44 17.46           C  
ANISOU   17  CA BARG A 110     1809   2620   2205    156    -42     80       C  
ATOM     18  CA  LEU A 111      35.978   0.170  17.964  1.00 14.02           C  
ANISOU   18  CA  LEU A 111     1425   1962   1940     79    -13     50       C  
ATOM     19  CA  GLY A 112      38.424  -1.983  16.017  1.00 11.88           C  
ANISOU   19  CA  GLY A 112     1084   1675   1756    109     -7     60       C  
ATOM     20  CA  PHE A 113      39.155  -2.669  12.363  1.00 13.14           C  
ANISOU   20  CA  PHE A 113     1245   1746   2003     71     24    -23       C  
ATOM     21  CA  LEU A 114      41.015  -5.345  10.401  1.00 14.88           C  
ANISOU   21  CA  LEU A 114     1389   1950   2314    164     54    -68       C  
ATOM     22  CA  HIS A 115      44.564  -4.597   9.296  1.00 14.61           C  
ANISOU   22  CA  HIS A 115     1216   2134   2203    152     62   -151       C  
ATOM     23  CA  SER A 116      43.699  -5.158   5.647  1.00 14.67           C  
ANISOU   23  CA  SER A 116     1270   2075   2229    129    116   -260       C  
ATOM     24  CA  GLY A 117      46.294  -3.133   3.746  1.00 13.83           C  
ANISOU   24  CA  GLY A 117     1068   2196   1990     18    180   -310       C  
ATOM     25  CA  THR A 118      45.718  -1.081   0.598  1.00 13.76           C  
ANISOU   25  CA  THR A 118     1137   2247   1846    -97    260   -303       C  
ATOM     26  CA  ALA A 119      46.035  -3.528  -2.307  1.00 15.09           C  
ANISOU   26  CA  ALA A 119     1232   2536   1966     43    295   -459       C  
ATOM     27  CA  LYS A 120      43.735  -3.177  -5.339  1.00 22.09           C  
ANISOU   27  CA  LYS A 120     2207   3495   2690     71    299   -506       C  
ATOM     28  CA  SER A 121      41.680  -6.212  -4.364  1.00 22.61           C  
ANISOU   28  CA  SER A 121     2279   3353   2960    166    205   -673       C  
ATOM     29  CA AVAL A 122      40.804  -4.884  -0.903  0.51 16.99           C  
ANISOU   29  CA AVAL A 122     1647   2445   2363     92    160   -471       C  
ATOM     30  CA BVAL A 122      40.811  -4.870  -0.905  0.49 17.02           C  
ANISOU   30  CA BVAL A 122     1651   2450   2366     91    160   -471       C  
ATOM     31  CA  THR A 123      37.124  -3.943  -0.518  1.00 20.90           C  
ANISOU   31  CA  THR A 123     2237   2850   2853     62     94   -430       C  
ATOM     32  CA ACYS A 124      37.456  -2.375   2.915  0.07 14.16           C  
ANISOU   32  CA ACYS A 124     1435   1885   2058     11     86   -262       C  
ATOM     33  CA BCYS A 124      37.437  -2.438   2.952  0.93 13.91           C  
ANISOU   33  CA BCYS A 124     1403   1852   2031     13     86   -263       C  
ATOM     34  CA  THR A 125      40.472  -0.729   4.506  1.00 12.49           C  
ANISOU   34  CA  THR A 125     1191   1737   1818    -60    117   -194       C  
ATOM     35  CA  TYR A 126      40.804   1.414   7.613  1.00 12.54           C  
ANISOU   35  CA  TYR A 126     1226   1719   1820   -138     93   -138       C  
ATOM     36  CA  SER A 127      43.221   4.293   8.195  1.00 16.21           C  
ANISOU   36  CA  SER A 127     1666   2246   2246   -322    138   -172       C  
ATOM     37  CA  PRO A 128      44.295   4.483  11.866  1.00 19.13           C  
ANISOU   37  CA  PRO A 128     1931   2735   2601   -336     62   -243       C  
ATOM     38  CA  ALA A 129      45.957   7.811  11.077  1.00 23.89           C  
ANISOU   38  CA  ALA A 129     2557   3296   3225   -607    152   -332       C  
ATOM     39  CA  LEU A 130      42.712   9.275   9.730  1.00 20.15           C  
ANISOU   39  CA  LEU A 130     2354   2528   2774   -546    195   -215       C  
ATOM     40  CA  ASN A 131      40.205   7.250  11.746  1.00 16.48           C  
ANISOU   40  CA  ASN A 131     1884   2092   2286   -336     88   -194       C  
ATOM     41  CA  LYS A 132      38.568   6.726   8.369  1.00 16.08           C  
ANISOU   41  CA  LYS A 132     1921   1962   2226   -257    127    -91       C  
ATOM     42  CA AMET A 133      37.158   3.678   6.599  0.64 15.50           C  
ANISOU   42  CA AMET A 133     1786   1951   2153   -124     93    -82       C  
ATOM     43  CA BMET A 133      37.137   3.684   6.603  0.36 15.43           C  
ANISOU   43  CA BMET A 133     1777   1942   2144   -124     93    -82       C  
ATOM     44  CA  PHE A 134      37.508   3.333   2.834  1.00 15.83           C  
ANISOU   44  CA  PHE A 134     1824   2083   2107   -101    137    -84       C  
ATOM     45  CA  CYS A 135      35.132   0.795   1.340  1.00 15.05           C  
ANISOU   45  CA  CYS A 135     1667   2040   2010      9     77   -184       C  
ATOM     46  CA  GLN A 136      33.350  -0.404  -1.776  1.00 16.61           C  
ANISOU   46  CA  GLN A 136     1812   2400   2100     92     39   -308       C  
ATOM     47  CA  LEU A 137      29.632  -0.080  -2.551  1.00 20.10           C  
ANISOU   47  CA  LEU A 137     2225   2947   2467    179    -49   -355       C  
ATOM     48  CA  ALA A 138      27.585  -3.000  -1.159  1.00 17.65           C  
ANISOU   48  CA  ALA A 138     1780   2556   2368    105    -88   -536       C  
ATOM     49  CA ALYS A 139      30.712  -4.873  -0.028  0.49 16.22           C  
ANISOU   49  CA ALYS A 139     1623   2188   2351     47    -14   -534       C  
ATOM     50  CA BLYS A 139      30.704  -4.882  -0.028  0.51 16.24           C  
ANISOU   50  CA BLYS A 139     1625   2190   2354     47    -14   -535       C  
ATOM     51  CA  THR A 140      31.563  -6.389   3.374  1.00 18.15           C  
ANISOU   51  CA  THR A 140     1887   2201   2809     13     35   -423       C  
ATOM     52  CA ACYS A 141      32.726  -3.821   5.940  0.75 13.72           C  
ANISOU   52  CA ACYS A 141     1398   1650   2163     21     37   -223       C  
ATOM     53  CA BCYS A 141      32.719  -3.815   5.940  0.25 13.82           C  
ANISOU   53  CA BCYS A 141     1412   1664   2177     21     37   -223       C  
ATOM     54  CA  PRO A 142      33.910  -5.490   9.164  1.00 13.23           C  
ANISOU   54  CA  PRO A 142     1320   1496   2209     54     67   -104       C  
ATOM     55  CA  VAL A 143      33.624  -3.293  12.253  1.00 12.43           C  
ANISOU   55  CA  VAL A 143     1250   1473   1999     56     49     11       C  
ATOM     56  CA  GLN A 144      34.948  -4.670  15.530  1.00 11.88           C  
ANISOU   56  CA  GLN A 144     1142   1458   1915    145     60    156       C  
ATOM     57  CA  LEU A 145      33.464  -4.142  18.976  1.00 13.40           C  
ANISOU   57  CA  LEU A 145     1335   1760   1996    188     76    281       C  
ATOM     58  CA  TRP A 146      35.997  -4.284  21.798  1.00 14.88           C  
ANISOU   58  CA  TRP A 146     1452   2186   2014    316     32    372       C  
ATOM     59  CA  VAL A 147      34.859  -4.310  25.424  1.00 18.74           C  
ANISOU   59  CA  VAL A 147     1920   2895   2306    422     57    526       C  
ATOM     60  CA  ASP A 148      36.587  -4.560  28.801  1.00 18.42           C  
ANISOU   60  CA  ASP A 148     1782   3240   1976    614      7    647       C  
ATOM     61  CA  SER A 149      33.472  -6.148  30.288  1.00 22.05           C  
ANISOU   61  CA  SER A 149     2305   3628   2444    650    166    916       C  
ATOM     62  CA  THR A 150      30.709  -8.167  28.591  1.00 25.57           C  
ANISOU   62  CA  THR A 150     2828   3684   3204    515    327   1039       C  
ATOM     63  CA  PRO A 151      27.357  -6.384  28.135  1.00 25.46           C  
ANISOU   63  CA  PRO A 151     2790   3674   3208    357    370    877       C  
ATOM     64  CA  PRO A 152      24.432  -8.695  29.013  1.00 31.56           C  
ANISOU   64  CA  PRO A 152     3531   4351   4110    270    584   1120       C  
ATOM     65  CA  PRO A 153      22.376 -10.477  26.319  1.00 34.41           C  
ANISOU   65  CA  PRO A 153     3864   4373   4838     41    671   1037       C  
ATOM     66  CA  GLY A 154      19.681  -8.045  25.245  1.00 26.51           C  
ANISOU   66  CA  GLY A 154     2742   3549   3782    -41    615    768       C  
ATOM     67  CA  THR A 155      22.281  -5.371  24.530  1.00 18.10           C  
ANISOU   67  CA  THR A 155     1776   2551   2550    101    417    593       C  
ATOM     68  CA  ARG A 156      21.967  -3.782  21.078  1.00 15.33           C  
ANISOU   68  CA  ARG A 156     1435   2105   2283     56    295    332       C  
ATOM     69  CA  VAL A 157      24.435  -2.164  18.654  1.00 12.49           C  
ANISOU   69  CA  VAL A 157     1177   1659   1909     84    166    189       C  
ATOM     70  CA  ARG A 158      23.219   0.768  16.553  1.00 14.29           C  
ANISOU   70  CA  ARG A 158     1442   1916   2073    134     92     37       C  
ATOM     71  CA  ALA A 159      24.776   2.366  13.471  1.00 10.74           C  
ANISOU   71  CA  ALA A 159     1091   1383   1605    145     26    -36       C  
ATOM     72  CA  MET A 160      23.866   5.732  11.952  1.00 12.69           C  
ANISOU   72  CA  MET A 160     1451   1611   1760    266     -4    -64       C  
ATOM     73  CA  ALA A 161      25.394   8.013   9.325  1.00 11.09           C  
ANISOU   73  CA  ALA A 161     1407   1299   1508    295     -3    -24       C  
ATOM     74  CA  ILE A 162      25.594  11.802   9.657  1.00 12.52           C  
ANISOU   74  CA  ILE A 162     1802   1281   1674    378     46     12       C  
ATOM     75  CA  TYR A 163      27.238  14.486   7.532  1.00 14.96           C  
ANISOU   75  CA  TYR A 163     2332   1367   1986    366    129    129       C  
ATOM     76  CA  LYS A 164      30.640  15.632   8.790  1.00 22.19           C  
ANISOU   76  CA  LYS A 164     3318   2103   3011     95    211     56       C  
ATOM     77  CA  GLN A 165      30.467  19.310   7.866  1.00 25.64           C  
ANISOU   77  CA  GLN A 165     4043   2175   3523    147    338    160       C  
ATOM     78  CA  SER A 166      28.448  21.660  10.085  1.00 26.72           C  
ANISOU   78  CA  SER A 166     4331   2080   3742    321    352     42       C  
ATOM     79  CA  GLN A 167      26.364  23.114   7.215  1.00 28.06           C  
ANISOU   79  CA  GLN A 167     4681   2139   3842    649    397    332       C  
ATOM     80  CA  HIS A 168      25.092  19.647   6.247  1.00 21.85           C  
ANISOU   80  CA  HIS A 168     3589   1846   2868    716    241    332       C  
ATOM     81  CA AMET A 169      24.766  18.018   9.677  0.50 20.78           C  
ANISOU   81  CA AMET A 169     3262   1856   2776    608    168     80       C  
ATOM     82  CA BMET A 169      24.763  18.015   9.683  0.50 20.77           C  
ANISOU   82  CA BMET A 169     3261   1856   2776    608    168     79       C  
ATOM     83  CA  THR A 170      21.033  18.740   9.963  1.00 22.23           C  
ANISOU   83  CA  THR A 170     3409   2152   2887    964    121     83       C  
ATOM     84  CA  GLU A 171      20.370  17.002   6.645  1.00 17.41           C  
ANISOU   84  CA  GLU A 171     2674   1803   2138   1031     52    231       C  
ATOM     85  CA  VAL A 172      19.421  13.309   6.899  1.00 18.53           C  
ANISOU   85  CA  VAL A 172     2495   2297   2249    902    -42    101       C  
ATOM     86  CA  VAL A 173      21.956  11.038   5.203  1.00 15.60           C  
ANISOU   86  CA  VAL A 173     2075   1966   1886    665    -45    101       C  
ATOM     87  CA AARG A 174      20.041   8.910   2.701  0.63 15.15           C  
ANISOU   87  CA AARG A 174     1800   2241   1715    736   -142     28       C  
ATOM     88  CA BARG A 174      20.061   8.887   2.712  0.37 15.24           C  
ANISOU   88  CA BARG A 174     1811   2252   1728    733   -142     28       C  
ATOM     89  CA  ARG A 175      20.560   7.080  -0.591  1.00 20.40           C  
ANISOU   89  CA  ARG A 175     2356   3142   2253    709   -197    -41       C  
ATOM     90  CA  CYS A 176      20.418   8.898  -3.933  1.00 23.08           C  
ANISOU   90  CA  CYS A 176     2781   3676   2312    951   -218    116       C  
ATOM     91  CA  PRO A 177      17.309   8.634  -6.177  1.00 30.98           C  
ANISOU   91  CA  PRO A 177     3562   5158   3053   1220   -369     32       C  
ATOM     92  CA  HIS A 178      19.071   6.212  -8.568  1.00 28.04           C  
ANISOU   92  CA  HIS A 178     3086   4984   2583   1057   -385   -149       C  
ATOM     93  CA  HIS A 179      19.938   3.753  -5.808  1.00 28.63           C  
ANISOU   93  CA  HIS A 179     3099   4755   3024    725   -336   -343       C  
ATOM     94  CA AGLU A 180      16.763   4.191  -3.744  0.44 39.40           C  
ANISOU   94  CA AGLU A 180     4328   6173   4471    795   -390   -379       C  
ATOM     95  CA BGLU A 180      16.730   4.250  -3.819  0.56 40.06           C  
ANISOU   95  CA BGLU A 180     4412   6265   4546    804   -392   -376       C  
ATOM     96  CA AARG A 181      14.698   3.195  -6.808  0.44 59.24           C  
ANISOU   96  CA AARG A 181     6861   9397   6248    -10   -773   -397       C  
ATOM     97  CA BARG A 181      14.917   3.408  -7.067  0.56 59.72           C  
ANISOU   97  CA BARG A 181     6950   9465   6275      6   -775   -368       C  
ATOM     98  CA  CYS A 182      16.667   0.123  -7.828  1.00 62.82           C  
ANISOU   98  CA  CYS A 182     7487   9733   6649   -352   -551   -771       C  
ATOM     99  CA  SER A 183      15.970  -3.139  -6.050  1.00 69.51           C  
ANISOU   99  CA  SER A 183     8248  10334   7831   -625   -379  -1113       C  
ATOM    100  CA  ASP A 184      19.224  -4.138  -4.427  1.00 63.96           C  
ANISOU  100  CA  ASP A 184     7759   9146   7395   -630    -84  -1148       C  
ATOM    101  CA  SER A 185      16.846  -4.382  -1.489  1.00 52.68           C  
ANISOU  101  CA  SER A 185     6111   7665   6239   -631   -148  -1109       C  
ATOM    102  CA  ASP A 186      17.135  -7.591   0.530  1.00 39.70           C  
ANISOU  102  CA  ASP A 186     4512   5624   4949   -831    128  -1270       C  
ATOM    103  CA  GLY A 187      13.550  -7.383   1.779  1.00 33.49           C  
ANISOU  103  CA  GLY A 187     3457   5074   4196   -871      9  -1242       C  
ATOM    104  CA  LEU A 188      14.652  -6.243   5.235  1.00 30.96           C  
ANISOU  104  CA  LEU A 188     3172   4501   4090   -685     91   -995       C  
ATOM    105  CA  ALA A 189      16.424  -2.955   4.634  1.00 25.41           C  
ANISOU  105  CA  ALA A 189     2583   3840   3232   -370    -57   -758       C  
ATOM    106  CA  PRO A 190      14.317   0.015   3.579  1.00 23.73           C  
ANISOU  106  CA  PRO A 190     2199   3975   2844   -159   -295   -638       C  
ATOM    107  CA  PRO A 191      15.527   0.995   0.085  1.00 23.94           C  
ANISOU  107  CA  PRO A 191     2347   4177   2574   -119   -415   -590       C  
ATOM    108  CA  GLN A 192      16.413   4.510   1.325  1.00 22.66           C  
ANISOU  108  CA  GLN A 192     2296   3818   2497    208   -429   -268       C  
ATOM    109  CA  HIS A 193      18.819   3.348   4.049  1.00 16.64           C  
ANISOU  109  CA  HIS A 193     1675   2672   1975    110   -228   -321       C  
ATOM    110  CA  LEU A 194      22.518   3.876   3.336  1.00 15.81           C  
ANISOU  110  CA  LEU A 194     1777   2341   1889     94   -123   -231       C  
ATOM    111  CA  ILE A 195      23.717   1.421   5.988  1.00 12.99           C  
ANISOU  111  CA  ILE A 195     1406   1788   1741     -7      0   -311       C  
ATOM    112  CA  ARG A 196      22.741  -2.248   6.070  1.00 13.23           C  
ANISOU  112  CA  ARG A 196     1383   1790   1856   -178    119   -489       C  
ATOM    113  CA  VAL A 197      23.959  -5.219   8.083  1.00 16.31           C  
ANISOU  113  CA  VAL A 197     1809   1911   2478   -234    304   -470       C  
ATOM    114  CA  GLU A 198      24.584  -8.475   6.216  1.00 19.60           C  
ANISOU  114  CA  GLU A 198     2290   2133   3023   -379    528   -673       C  
ATOM    115  CA  GLY A 199      24.678 -11.970   7.694  1.00 23.48           C  
ANISOU  115  CA  GLY A 199     2847   2256   3820   -452    790   -670       C  
ATOM    116  CA  ASN A 200      22.228 -11.256  10.517  1.00 21.20           C  
ANISOU  116  CA  ASN A 200     2472   2097   3486   -486    695   -521       C  
ATOM    117  CA  LEU A 201      18.573 -12.347  10.434  1.00 25.58           C  
ANISOU  117  CA  LEU A 201     2907   2760   4054   -774    750   -729       C  
ATOM    118  CA  ARG A 202      17.894 -10.413  13.643  1.00 17.09           C  
ANISOU  118  CA  ARG A 202     1775   1842   2878   -608    664   -456       C  
ATOM    119  CA  VAL A 203      18.756  -7.091  11.998  1.00 13.54           C  
ANISOU  119  CA  VAL A 203     1291   1634   2220   -422    402   -488       C  
ATOM    120  CA  GLU A 204      16.355  -4.216  12.747  1.00 15.99           C  
ANISOU  120  CA  GLU A 204     1444   2243   2389   -314    258   -487       C  
ATOM    121  CA  TYR A 205      15.836  -0.942  10.879  1.00 13.78           C  
ANISOU  121  CA  TYR A 205     1101   2170   1966   -125     50   -489       C  
ATOM    122  CA  LEU A 206      14.506   2.373  12.149  1.00 13.05           C  
ANISOU  122  CA  LEU A 206      951   2170   1838    126    -13   -412       C  
ATOM    123  CA  ASP A 207      13.093   5.506  10.612  1.00 18.26           C  
ANISOU  123  CA  ASP A 207     1519   2962   2456    395   -148   -336       C  
ATOM    124  CA  ASP A 208      13.012   7.913  13.537  1.00 18.80           C  
ANISOU  124  CA  ASP A 208     1688   2856   2599    586    -26   -325       C  
ATOM    125  CA AARG A 209       9.444   9.153  14.026  0.52 25.69           C  
ANISOU  125  CA AARG A 209     2261   3943   3558    821     23   -347       C  
ATOM    126  CA BARG A 209       9.442   9.179  13.952  0.48 25.49           C  
ANISOU  126  CA BARG A 209     2234   3920   3533    824     19   -343       C  
ATOM    127  CA  ASN A 210      10.736  12.629  14.929  1.00 26.77           C  
ANISOU  127  CA  ASN A 210     2676   3732   3765   1070     99   -309       C  
ATOM    128  CA  THR A 211      14.179  13.205  13.373  1.00 21.64           C  
ANISOU  128  CA  THR A 211     2327   2831   3066    945     -3   -210       C  
ATOM    129  CA  PHE A 212      13.515  11.092  10.250  1.00 20.13           C  
ANISOU  129  CA  PHE A 212     1945   2947   2756    857   -180   -117       C  
ATOM    130  CA  ARG A 213      17.012   9.636  10.649  1.00 18.01           C  
ANISOU  130  CA  ARG A 213     1904   2490   2449    586   -145   -163       C  
ATOM    131  CA  HIS A 214      17.812   6.103   9.538  1.00 14.07           C  
ANISOU  131  CA  HIS A 214     1348   2110   1886    334   -155   -237       C  
ATOM    132  CA  SER A 215      19.625   3.581  11.720  1.00 10.85           C  
ANISOU  132  CA  SER A 215     1007   1571   1544    156    -45   -285       C  
ATOM    133  CA  VAL A 216      20.306  -0.146  11.700  1.00 13.75           C  
ANISOU  133  CA  VAL A 216     1364   1880   1982    -32     62   -332       C  
ATOM    134  CA AVAL A 217      20.592  -2.221  14.884  0.78 13.17           C  
ANISOU  134  CA AVAL A 217     1323   1700   1980    -89    191   -248       C  
ATOM    135  CA BVAL A 217      20.596  -2.238  14.883  0.22 13.19           C  
ANISOU  135  CA BVAL A 217     1327   1703   1984    -90    192   -248       C  
ATOM    136  CA  VAL A 218      21.658  -5.778  15.770  1.00 13.93           C  
ANISOU  136  CA  VAL A 218     1478   1587   2226   -183    363   -151       C  
ATOM    137  CA  PRO A 219      21.771  -7.728  19.045  1.00 18.90           C  
ANISOU  137  CA  PRO A 219     2179   2122   2879   -182    503     87       C  
ATOM    138  CA  TYR A 220      25.186  -7.603  20.701  1.00 16.40           C  
ANISOU  138  CA  TYR A 220     1927   1786   2517     -6    394    344       C  
ATOM    139  CA  GLU A 221      26.827 -11.021  20.837  1.00 20.68           C  
ANISOU  139  CA  GLU A 221     2521   2027   3309     71    569    590       C  
ATOM    140  CA  PRO A 222      30.001 -11.814  22.847  1.00 23.54           C  
ANISOU  140  CA  PRO A 222     2859   2414   3671    318    467    982       C  
ATOM    141  CA  PRO A 223      33.334 -12.286  20.966  1.00 27.70           C  
ANISOU  141  CA  PRO A 223     3244   2826   4455    502    442   1019       C  
ATOM    142  CA AGLU A 224      33.521 -15.152  18.450  0.38 27.57           C  
ANISOU  142  CA AGLU A 224     3282   2425   4770    499    759    870       C  
ATOM    143  CA BGLU A 224      33.408 -15.198  18.506  0.23 27.76           C  
ANISOU  143  CA BGLU A 224     3313   2444   4792    494    763    872       C  
ATOM    144  CA CGLU A 224      33.605 -15.098  18.390  0.39 27.50           C  
ANISOU  144  CA CGLU A 224     3267   2419   4761    502    755    867       C  
ATOM    145  CA  VAL A 225      35.715 -18.215  18.912  1.00 33.46           C  
ANISOU  145  CA  VAL A 225     3998   2991   5724    704    911   1089       C  
ATOM    146  CA  GLY A 226      39.307 -17.319  18.058  1.00 37.18           C  
ANISOU  146  CA  GLY A 226     4240   3628   6258    879    792   1140       C  
ATOM    147  CA  SER A 227      38.584 -13.606  18.434  1.00 29.52           C  
ANISOU  147  CA  SER A 227     3207   2979   5029    750    505   1038       C  
ATOM    148  CA  ASP A 228      38.747 -11.110  21.299  1.00 26.17           C  
ANISOU  148  CA  ASP A 228     2693   2953   4297    745    148   1208       C  
ATOM    149  CA  CYS A 229      36.191  -8.801  19.687  1.00 18.05           C  
ANISOU  149  CA  CYS A 229     1793   1924   3142    500    158    846       C  
ATOM    150  CA  THR A 230      32.696  -8.945  18.193  1.00 16.41           C  
ANISOU  150  CA  THR A 230     1772   1566   2897    306    324    571       C  
ATOM    151  CA  THR A 231      32.541  -8.314  14.443  1.00 15.41           C  
ANISOU  151  CA  THR A 231     1650   1362   2845    207    422    262       C  
ATOM    152  CA  ILE A 232      29.631  -6.763  12.526  1.00 13.90           C  
ANISOU  152  CA  ILE A 232     1524   1280   2479     30    392    -16       C  
ATOM    153  CA  HIS A 233      29.408  -6.748   8.724  1.00 14.23           C  
ANISOU  153  CA  HIS A 233     1595   1330   2481    -63    478   -265       C  
ATOM    154  CA  TYR A 234      28.027  -3.455   7.431  1.00 10.26           C  
ANISOU  154  CA  TYR A 234     1093   1076   1729    -87    292   -317       C  
ATOM    155  CA  ASN A 235      27.184  -2.610   3.831  1.00 14.28           C  
ANISOU  155  CA  ASN A 235     1643   1763   2021   -154    278   -461       C  
ATOM    156  CA  TYR A 236      27.161   0.937   2.477  1.00 12.15           C  
ANISOU  156  CA  TYR A 236     1415   1645   1558    -67    143   -321       C  
ATOM    157  CA  MET A 237      24.655   1.134  -0.368  1.00 15.88           C  
ANISOU  157  CA  MET A 237     1881   2427   1728   -106     37   -410       C  
ATOM    158  CA  CYS A 238      25.769   4.374  -2.016  1.00 15.81           C  
ANISOU  158  CA  CYS A 238     1988   2458   1559     22      4   -149       C  
ATOM    159  CA  ASN A 239      29.048   5.799  -3.267  1.00 18.86           C  
ANISOU  159  CA  ASN A 239     2505   2711   1950      7    186     12       C  
ATOM    160  CA  SER A 240      30.267   9.012  -1.639  1.00 26.84           C  
ANISOU  160  CA  SER A 240     3572   3457   3169     75    188    244       C  
ATOM    161  CA  SER A 241      30.171  10.494  -5.151  1.00 30.37           C  
ANISOU  161  CA  SER A 241     4177   4074   3288    115    244    467       C  
ATOM    162  CA  CYS A 242      26.533   9.585  -5.896  1.00 29.46           C  
ANISOU  162  CA  CYS A 242     3980   4296   2918    229     -7    399       C  
ATOM    163  CA  MET A 243      24.856  12.724  -7.241  1.00 36.24           C  
ANISOU  163  CA  MET A 243     4935   5227   3609    485   -133    795       C  
ATOM    164  CA  GLY A 244      21.609  13.661  -5.502  1.00 40.84           C  
ANISOU  164  CA  GLY A 244     5342   5843   4333    734   -353    831       C  
ATOM    165  CA  GLY A 245      22.654  11.740  -2.413  1.00 29.46           C  
ANISOU  165  CA  GLY A 245     3816   4170   3208    533   -253    482       C  
ATOM    166  CA  MET A 246      25.810  12.366  -0.403  1.00 19.63           C  
ANISOU  166  CA  MET A 246     2684   2523   2251    393    -64    438       C  
ATOM    167  CA  ASN A 247      27.224  14.011  -3.557  1.00 21.59           C  
ANISOU  167  CA  ASN A 247     3115   2787   2301    402     44    723       C  
ATOM    168  CA  ARG A 248      30.871  13.871  -2.400  1.00 22.70           C  
ANISOU  168  CA  ARG A 248     3267   2665   2693    164    252    630       C  
ATOM    169  CA  ARG A 249      29.960  15.159   1.065  1.00 18.15           C  
ANISOU  169  CA  ARG A 249     2664   1838   2395    218    160    527       C  
ATOM    170  CA  PRO A 250      31.995  13.397   3.798  1.00 15.80           C  
ANISOU  170  CA  PRO A 250     2213   1513   2279     32    157    287       C  
ATOM    171  CA  ILE A 251      30.066  11.389   6.396  1.00 16.61           C  
ANISOU  171  CA  ILE A 251     2460   1632   2219    351    350    331       C  
ATOM    172  CA  LEU A 252      30.640   9.724   9.755  1.00 15.95           C  
ANISOU  172  CA  LEU A 252     2274   1560   2227    165    247    158       C  
ATOM    173  CA  THR A 253      29.227   6.469  11.070  1.00 10.53           C  
ANISOU  173  CA  THR A 253     1385   1082   1533    167    154     67       C  
ATOM    174  CA  ILE A 254      28.171   6.597  14.711  1.00 11.42           C  
ANISOU  174  CA  ILE A 254     1509   1198   1633    159    121     -2       C  
ATOM    175  CA  ILE A 255      28.207   3.283  16.574  1.00 11.80           C  
ANISOU  175  CA  ILE A 255     1422   1358   1704     72     88     -4       C  
ATOM    176  CA ATHR A 256      26.133   3.222  19.774  0.61 12.11           C  
ANISOU  176  CA ATHR A 256     1418   1530   1654    117     84    -14       C  
ATOM    177  CA BTHR A 256      26.171   3.210  19.786  0.39 12.08           C  
ANISOU  177  CA BTHR A 256     1414   1526   1651    116     83    -14       C  
ATOM    178  CA ALEU A 257      25.939   0.524  22.439  0.57 12.29           C  
ANISOU  178  CA ALEU A 257     1365   1653   1650     63    108     75       C  
ATOM    179  CA BLEU A 257      25.930   0.537  22.464  0.43 12.36           C  
ANISOU  179  CA BLEU A 257     1373   1663   1658     64    108     75       C  
ATOM    180  CA  GLU A 258      22.535   0.477  24.176  1.00 14.82           C  
ANISOU  180  CA  GLU A 258     1577   2216   1837     86    143     91       C  
ATOM    181  CA  ASP A 259      20.709  -1.850  26.566  1.00 14.48           C  
ANISOU  181  CA  ASP A 259     1430   2361   1711    -10    233    230       C  
ATOM    182  CA  SER A 260      17.416  -3.674  25.947  1.00 16.48           C  
ANISOU  182  CA  SER A 260     1533   2805   1922   -237    333    249       C  
ATOM    183  CA  SER A 261      15.591  -0.627  27.326  1.00 16.07           C  
ANISOU  183  CA  SER A 261     1339   3134   1633     24    265    156       C  
ATOM    184  CA  GLY A 262      17.316   1.924  25.097  1.00 13.84           C  
ANISOU  184  CA  GLY A 262     1224   2599   1435    216    167     24       C  
ATOM    185  CA  ASN A 263      19.685   3.286  27.741  1.00 16.93           C  
ANISOU  185  CA  ASN A 263     1732   2884   1815    331    121      8       C  
ATOM    186  CA  LEU A 264      22.977   4.511  26.256  1.00 16.32           C  
ANISOU  186  CA  LEU A 264     1836   2467   1899    301     73    -62       C  
ATOM    187  CA  LEU A 265      26.032   2.476  27.302  1.00 16.75           C  
ANISOU  187  CA  LEU A 265     1876   2473   2015    200     69     25       C  
ATOM    188  CA  GLY A 266      28.727   3.759  24.967  1.00 12.11           C  
ANISOU  188  CA  GLY A 266     1381   1670   1550    125     37    -59       C  
ATOM    189  CA  ARG A 267      29.414   5.556  21.703  1.00 13.28           C  
ANISOU  189  CA  ARG A 267     1645   1597   1802     73     49   -105       C  
ATOM    190  CA  ASN A 268      32.144   5.664  19.076  1.00 10.57           C  
ANISOU  190  CA  ASN A 268     1320   1147   1549    -41     62    -86       C  
ATOM    191  CA  SER A 269      32.479   6.905  15.504  1.00 11.80           C  
ANISOU  191  CA  SER A 269     1560   1167   1758    -57    114    -32       C  
ATOM    192  CA  PHE A 270      34.570   6.792  12.336  1.00 12.12           C  
ANISOU  192  CA  PHE A 270     1568   1212   1824   -123    153     41       C  
ATOM    193  CA  GLU A 271      34.543   8.604   9.005  1.00 13.08           C  
ANISOU  193  CA  GLU A 271     1787   1258   1927    -84    244    160       C  
ATOM    194  CA AVAL A 272      33.683   6.527   5.950  0.63 13.67           C  
ANISOU  194  CA AVAL A 272     1723   1539   1932     74    226    203       C  
ATOM    195  CA BVAL A 272      33.611   6.522   5.944  0.37 14.79           C  
ANISOU  195  CA BVAL A 272     1866   1682   2073     78    226    202       C  
ATOM    196  CA  ARG A 273      34.347   7.032   2.251  1.00  0.00           C  
ATOM    197  CA  VAL A 274      32.573   4.781  -0.217  1.00 14.92           C  
ANISOU  197  CA  VAL A 274     1659   2140   1868    358    239    236       C  
ATOM    198  CA  CYS A 275      34.413   4.326  -3.508  1.00 20.09           C  
ANISOU  198  CA  CYS A 275     2180   3056   2396    433    273    290       C  
ATOM    199  CA  ALA A 276      35.739   2.083  -6.277  1.00 20.37           C  
ANISOU  199  CA  ALA A 276     2008   3426   2308    532    239    176       C  
ATOM    200  CA  CYS A 277      39.374   2.205  -5.133  1.00 20.58           C  
ANISOU  200  CA  CYS A 277     2024   3390   2406    363    265    251       C  
ATOM    201  CA  PRO A 278      39.524   2.095  -1.295  1.00 17.38           C  
ANISOU  201  CA  PRO A 278     1737   2681   2184    190    223    199       C  
ATOM    202  CA  GLY A 279      43.213   1.184  -1.151  1.00 14.54           C  
ANISOU  202  CA  GLY A 279     1215   2546   1763    144    220    191       C  
ATOM    203  CA  ARG A 280      44.177   3.879  -3.647  1.00 19.04           C  
ANISOU  203  CA  ARG A 280     1741   3271   2222     47    347    396       C  
ATOM    204  CA  ASP A 281      42.250   6.571  -1.764  1.00 17.52           C  
ANISOU  204  CA  ASP A 281     1815   2671   2170   -105    404    480       C  
ATOM    205  CA  ARG A 282      43.604   5.604   1.642  1.00 15.08           C  
ANISOU  205  CA  ARG A 282     1455   2326   1949   -255    319    320       C  
ATOM    206  CA  ARG A 283      47.175   5.963   0.353  1.00 16.71           C  
ANISOU  206  CA  ARG A 283     1424   2905   2020   -419    382    373       C  
ATOM    207  CA  THR A 284      46.322   9.337  -1.225  1.00  0.00           C  
ATOM    208  CA  GLU A 285      44.650  10.787   1.821  1.00 25.62           C  
ANISOU  208  CA  GLU A 285     3034   3349   3351   -705    544    493       C  
ATOM    209  CA  GLU A 286      47.449   9.611   4.108  1.00 25.20           C  
ANISOU  209  CA  GLU A 286     2707   3613   3256   -911    457    298       C  
ATOM    210  CA  GLU A 287      49.983  11.539   2.036  1.00 41.62           C  
ANISOU  210  CA  GLU A 287     4688   5871   5254  -1254    631    433       C  
ATOM    211  CA  ASN A 288      47.667  14.594   2.001  1.00 57.03           C  
ANISOU  211  CA  ASN A 288     7111   7188   7369  -1340    785    562       C  
ATOM    212  CA  LEU A 289      48.465  15.182   5.685  1.00 69.10           C  
ANISOU  212  CA  LEU A 289     8618   8658   8978  -1543    674    255       C  
ATOM    213  CA  ARG A 290      52.003  16.178   4.748  1.00 68.04           C  
ANISOU  213  CA  ARG A 290     8261   8831   8759  -1846    737    242       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.