CNRS Nantes University US2B US2B
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elNémo ID: 2410102203191111079

Job options:

ID        	=	 2410102203191111079
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


SEQRES   1 A  452  THR THR MET ALA SER PRO GLN LEU MET PRO LEU VAL VAL
SEQRES   2 A  452  VAL LEU SER THR ILE CYS LEU VAL THR VAL GLY LEU ASN
SEQRES   3 A  452  LEU LEU VAL LEU TYR ALA VAL ARG SER GLU ARG LYS LEU
SEQRES   4 A  452  HIS THR VAL GLY ASN LEU TYR ILE VAL SER LEU SER VAL
SEQRES   5 A  452  ALA ASP LEU ILE VAL GLY ALA VAL VAL MET PRO MET ASN
SEQRES   6 A  452  ILE LEU TYR LEU LEU MET SER LYS TRP SER LEU GLY ARG
SEQRES   7 A  452  PRO LEU CYS LEU PHE TRP LEU SER MET ASP TYR VAL ALA
SEQRES   8 A  452  SER THR ALA SER ILE PHE SER VAL PHE ILE LEU CYS ILE
SEQRES   9 A  452  ASP ARG TYR ARG SER VAL GLN GLN PRO LEU ARG TYR LEU
SEQRES  10 A  452  LYS TYR ARG THR LYS THR ARG ALA SER ALA THR ILE LEU
SEQRES  11 A  452  GLY ALA TRP PHE LEU SER PHE LEU TRP VAL ILE PRO ILE
SEQRES  12 A  452  LEU GLY TRP ASN HIS PHE MET GLN GLN THR SER VAL ARG
SEQRES  13 A  452  ARG GLU ASP LYS CYS GLU THR ASP PHE TYR ASP VAL THR
SEQRES  14 A  452  TRP PHE LYS VAL MET THR ALA ILE ILE ASN PHE TYR LEU
SEQRES  15 A  452  PRO THR LEU LEU MET LEU TRP PHE TYR ALA LYS ILE TYR
SEQRES  16 A  452  LYS ALA VAL ARG GLN HIS CYS ASN ILE PHE GLU MET LEU
SEQRES  17 A  452  ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP
SEQRES  18 A  452  THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU
SEQRES  19 A  452  THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU
SEQRES  20 A  452  ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR
SEQRES  21 A  452  LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP
SEQRES  22 A  452  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS
SEQRES  23 A  452  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA
SEQRES  24 A  452  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL
SEQRES  25 A  452  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS
SEQRES  26 A  452  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG
SEQRES  27 A  452  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE
SEQRES  28 A  452  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR LEU HIS
SEQRES  29 A  452  MET ASN ARG GLU ARG LYS ALA ALA LYS GLN LEU GLY PHE
SEQRES  30 A  452  ILE MET ALA ALA PHE ILE LEU CYS TRP ILE PRO TYR PHE
SEQRES  31 A  452  ILE PHE PHE MET VAL ILE ALA PHE CYS LYS ASN CYS CYS
SEQRES  32 A  452  ASN GLU HIS LEU HIS MET PHE THR ILE TRP LEU GLY TYR
SEQRES  33 A  452  ILE ASN SER THR LEU ASN PRO LEU ILE TYR PRO LEU CYS
SEQRES  34 A  452  ASN GLU ASN PHE LYS LYS THR PHE LYS ARG ILE LEU HIS
SEQRES  35 A  452  ILE ARG SER GLY GLU ASN LEU TYR PHE GLN
HELIX    1   1 MET A   28  VAL A   31  1                                   4
HELIX    2   2 VAL A   32  GLU A   55  1                                  24
HELIX    3   3 THR A   60  GLY A   62  1                                   3
HELIX    4   4 ASN A   63  ALA A   78  1                                  16
HELIX    5   5 VAL A   79  MET A   90  1                                  12
HELIX    6   6 LEU A   95  GLN A  131  1                                  37
HELIX    7   7 THR A  140  PHE A  156  1                                  17
HELIX    8   8 TRP A  158  GLY A  164  1                                   7
HELIX    9   9 VAL A  187  ASN A  198  1                                  12
HELIX   10  10 PHE A  199  VAL A  217  1                                  19
HELIX   11  11 ASN A 1002  GLY A 1012  1                                  11
HELIX   12  12 SER A 1038  GLY A 1051  1                                  14
HELIX   13  13 THR A 1059  ARG A 1080  1                                  22
HELIX   14  14 LEU A 1084  LEU A 1091  1                                   8
HELIX   15  15 ASP A 1092  MET A 1106  1                                  15
HELIX   16  16 GLY A 1107  ALA A 1112  1                                   6
HELIX   17  17 PHE A 1114  GLN A 1123  1                                  10
HELIX   18  18 ARG A 1125  ALA A 1134  1                                  10
HELIX   19  19 SER A 1136  GLN A 1141  1                                   6
HELIX   20  20 THR A 1142  GLY A 1156  1                                  15
HELIX   21  21 TRP A 1158  LEU A  405  1                                   5
HELIX   22  22 MET A  407  LYS A  442  1                                  36
HELIX   23  23 LEU A  449  CYS A  471  1                                  23
HELIX   24  24 ASN A  472  HIS A  484  1                                  13
SHEET    1   1 1 LEU A1013  LYS A1019  0
SHEET    2   2 1 TYR A1025  ILE A1029  0
SHEET    3   3 1 HIS A1031  LEU A1032  0
SSBOND   1 CYS A  100    CYS A  180                          1555   1555  2.03
SSBOND   2 CYS A  441    CYS A  444                          1555   1555  2.03
CRYST1   88.144   88.144  331.654  90.00  90.00  90.00 I 4 2 2      16
ATOM      1  N   ASP A 107       8.478  36.028  20.891  1.00111.70           N
ANISOU    1  N   ASP A 107    16461  16479   9502    321   -638   1689       N
ATOM      2  CA  ASP A 107       9.705  35.243  21.005  1.00110.09           C
ANISOU    2  CA  ASP A 107    16390  15990   9451    224   -597   1545       C
ATOM      3  C   ASP A 107      10.806  36.150  21.569  1.00111.07           C
ANISOU    3  C   ASP A 107    16531  15861   9810    366   -459   1546       C
ATOM      4  O   ASP A 107      11.526  35.744  22.481  1.00109.62           O
ANISOU    4  O   ASP A 107    16359  15494   9798    315   -454   1457       O
ATOM      5  CB  ASP A 107      10.099  34.647  19.639  1.00113.11           C
ANISOU    5  CB  ASP A 107    16911  16362   9704    170   -572   1487       C
ATOM      6  CG  ASP A 107      11.470  33.999  19.590  1.00122.19           C
ANISOU    6  CG  ASP A 107    18199  17244  10984    151   -499   1349       C
ATOM      7  OD1 ASP A 107      12.431  34.680  19.173  1.00122.29           O
ANISOU    7  OD1 ASP A 107    18237  17143  11083    277   -353   1367       O
ATOM      8  OD2 ASP A 107      11.577  32.801  19.941  1.00127.27           O
ANISOU    8  OD2 ASP A 107    18930  17804  11623     12   -592   1230       O
ATOM      9  N   TYR A 108      10.907  37.385  21.046  1.00106.44           N
ANISOU    9  N   TYR A 108    15954  15271   9217    530   -357   1656       N
ATOM     10  CA  TYR A 108      11.896  38.369  21.476  1.00104.79           C
ANISOU   10  CA  TYR A 108    15786  14829   9200    630   -236   1679       C
ATOM     11  C   TYR A 108      11.567  39.040  22.815  1.00106.69           C
ANISOU   11  C   TYR A 108    15961  15020   9554    710   -267   1708       C
ATOM     12  O   TYR A 108      12.484  39.290  23.596  1.00105.11           O
ANISOU   12  O   TYR A 108    15786  14605   9546    699   -214   1659       O
ATOM     13  CB  TYR A 108      12.179  39.396  20.368  1.00106.73           C
ANISOU   13  CB  TYR A 108    16111  15059   9381    744   -124   1792       C
ATOM     14  CG  TYR A 108      13.174  38.903  19.337  1.00108.22           C
ANISOU   14  CG  TYR A 108    16374  15195   9550    676    -38   1740       C
ATOM     15  CD1 TYR A 108      14.543  38.927  19.591  1.00109.70           C
ANISOU   15  CD1 TYR A 108    16590  15187   9904    637     62   1684       C
ATOM     16  CD2 TYR A 108      12.747  38.402  18.111  1.00109.72           C
ANISOU   16  CD2 TYR A 108    16594  15561   9534    657    -57   1745       C
ATOM     17  CE1 TYR A 108      15.465  38.484  18.642  1.00111.04           C
ANISOU   17  CE1 TYR A 108    16805  15357  10029    606    149   1642       C
ATOM     18  CE2 TYR A 108      13.658  37.944  17.158  1.00110.99           C
ANISOU   18  CE2 TYR A 108    16826  15691   9653    625     25   1690       C
ATOM     19  CZ  TYR A 108      15.018  37.987  17.428  1.00116.95           C
ANISOU   19  CZ  TYR A 108    17597  16270  10570    612    133   1640       C
ATOM     20  OH  TYR A 108      15.927  37.538  16.498  1.00116.63           O
ANISOU   20  OH  TYR A 108    17605  16246  10464    610    222   1591       O
ATOM     21  N   SER A 111      11.787  36.092  25.858  1.00 91.55           N
ANISOU   21  N   SER A 111    13898  12999   7886    331   -512   1406       N
ATOM     22  CA  SER A 111      13.178  35.702  26.099  1.00 89.65           C
ANISOU   22  CA  SER A 111    13729  12515   7818    295   -442   1302       C
ATOM     23  C   SER A 111      13.970  36.818  26.793  1.00 91.64           C
ANISOU   23  C   SER A 111    13963  12605   8252    396   -346   1324       C
ATOM     24  O   SER A 111      14.814  36.523  27.636  1.00 91.05           O
ANISOU   24  O   SER A 111    13876  12387   8330    357   -334   1247       O
ATOM     25  CB  SER A 111      13.857  35.260  24.810  1.00 92.91           C
ANISOU   25  CB  SER A 111    14251  12886   8164    278   -376   1261       C
ATOM     26  OG  SER A 111      13.478  33.938  24.469  1.00 99.48           O
ANISOU   26  OG  SER A 111    15154  13774   8871    152   -479   1186       O
ATOM     27  N   THR A 112      13.665  38.089  26.475  1.00 86.74           N
ANISOU   27  N   THR A 112    13355  12003   7599    521   -291   1429       N
ATOM     28  CA  THR A 112      14.284  39.251  27.115  1.00 85.40           C
ANISOU   28  CA  THR A 112    13215  11661   7572    599   -220   1459       C
ATOM     29  C   THR A 112      13.738  39.348  28.544  1.00 87.53           C
ANISOU   29  C   THR A 112    13409  11948   7901    633   -302   1437       C
ATOM     30  O   THR A 112      14.503  39.604  29.475  1.00 86.57           O
ANISOU   30  O   THR A 112    13290  11666   7938    613   -281   1386       O
ATOM     31  CB  THR A 112      14.017  40.512  26.287  1.00 90.92           C
ANISOU   31  CB  THR A 112    14003  12355   8186    726   -155   1584       C
ATOM     32  OG1 THR A 112      14.575  40.317  24.992  1.00 90.76           O
ANISOU   32  OG1 THR A 112    14037  12342   8107    678    -78   1603       O
ATOM     33  CG2 THR A 112      14.608  41.770  26.904  1.00 88.01           C
ANISOU   33  CG2 THR A 112    13724  11772   7941    785    -98   1621       C
ATOM     34  N   ILE A 115      15.630  36.815  30.807  1.00 76.24           N
ANISOU   34  N   ILE A 115    11867  10299   6801    346   -383   1152       N
ATOM     35  CA  ILE A 115      16.920  37.317  31.304  1.00 75.54           C
ANISOU   35  CA  ILE A 115    11781  10042   6881    345   -302   1115       C
ATOM     36  C   ILE A 115      16.693  38.472  32.281  1.00 79.03           C
ANISOU   36  C   ILE A 115    12210  10427   7390    412   -309   1149       C
ATOM     37  O   ILE A 115      17.425  38.590  33.261  1.00 78.20           O
ANISOU   37  O   ILE A 115    12074  10221   7417    380   -306   1097       O
ATOM     38  CB  ILE A 115      17.979  37.641  30.198  1.00 79.26           C
ANISOU   38  CB  ILE A 115    12307  10446   7361    338   -179   1132       C
ATOM     39  CG1 ILE A 115      19.405  37.759  30.798  1.00 79.28           C
ANISOU   39  CG1 ILE A 115    12266  10338   7519    289   -115   1082       C
ATOM     40  CG2 ILE A 115      17.610  38.877  29.351  1.00 80.96           C
ANISOU   40  CG2 ILE A 115    12595  10663   7503    403   -119   1244       C
ATOM     41  CD1 ILE A 115      20.538  37.371  29.876  1.00 87.76           C
ANISOU   41  CD1 ILE A 115    13336  11428   8579    269    -16   1065       C
ATOM     42  N   TRP A 158      10.855  45.550  22.097  1.00117.56           N
ANISOU   42  N   TRP A 158    17876  15995  10795   1588    -24   2290       N
ATOM     43  CA  TRP A 158      11.157  44.678  20.960  1.00117.28           C
ANISOU   43  CA  TRP A 158    17772  16091  10697   1430      8   2273       C
ATOM     44  C   TRP A 158      10.111  44.745  19.856  1.00122.78           C
ANISOU   44  C   TRP A 158    18440  17068  11143   1561    -19   2383       C
ATOM     45  O   TRP A 158      10.450  44.514  18.697  1.00122.85           O
ANISOU   45  O   TRP A 158    18475  17126  11075   1486     34   2413       O
ATOM     46  CB  TRP A 158      11.365  43.233  21.423  1.00114.19           C
ANISOU   46  CB  TRP A 158    17217  15788  10382   1232    -45   2117       C
ATOM     47  CG  TRP A 158      12.765  42.992  21.874  1.00113.94           C
ANISOU   47  CG  TRP A 158    17217  15509  10564   1067     21   2021       C
ATOM     48  CD1 TRP A 158      13.253  43.134  23.138  1.00115.90           C
ANISOU   48  CD1 TRP A 158    17462  15583  10993   1032     10   1952       C
ATOM     49  CD2 TRP A 158      13.892  42.713  21.037  1.00113.90           C
ANISOU   49  CD2 TRP A 158    17251  15430  10596    938    118   2003       C
ATOM     50  NE1 TRP A 158      14.610  42.912  23.149  1.00114.91           N
ANISOU   50  NE1 TRP A 158    17354  15292  11014    877     88   1892       N
ATOM     51  CE2 TRP A 158      15.029  42.650  21.870  1.00117.00           C
ANISOU   51  CE2 TRP A 158    17639  15626  11191    825    158   1924       C
ATOM     52  CE3 TRP A 158      14.050  42.492  19.660  1.00116.03           C
ANISOU   52  CE3 TRP A 158    17547  15810  10731    916    174   2047       C
ATOM     53  CZ2 TRP A 158      16.306  42.361  21.374  1.00116.36           C
ANISOU   53  CZ2 TRP A 158    17556  15484  11171    700    255   1893       C
ATOM     54  CZ3 TRP A 158      15.317  42.223  19.169  1.00117.50           C
ANISOU   54  CZ3 TRP A 158    17747  15919  10980    800    275   2011       C
ATOM     55  CH2 TRP A 158      16.422  42.139  20.023  1.00117.28           C
ANISOU   55  CH2 TRP A 158    17692  15725  11145    697    315   1937       C
ATOM     56  N   LYS A 179      12.950  31.070  10.033  1.00149.39           N
ANISOU   56  N   LYS A 179    22588  21151  13021    291   -324    968       N
ATOM     57  CA  LYS A 179      11.704  31.363  10.761  1.00148.13           C
ANISOU   57  CA  LYS A 179    22295  21099  12888    143   -457   1072       C
ATOM     58  C   LYS A 179      10.736  32.298   9.980  1.00151.79           C
ANISOU   58  C   LYS A 179    22624  21857  13190    166   -458   1250       C
ATOM     59  O   LYS A 179      10.696  32.234   8.748  1.00152.95           O
ANISOU   59  O   LYS A 179    22847  22141  13125    199   -438   1245       O
ATOM     60  CB  LYS A 179      11.988  31.845  12.210  1.00148.40           C
ANISOU   60  CB  LYS A 179    22190  20982  13215    166   -421   1121       C
ATOM     61  CG  LYS A 179      12.784  33.145  12.345  1.00159.15           C
ANISOU   61  CG  LYS A 179    23415  22297  14757    346   -232   1247       C
ATOM     62  CD  LYS A 179      12.681  33.694  13.765  1.00166.39           C
ANISOU   62  CD  LYS A 179    24197  23112  15912    338   -241   1309       C
ATOM     63  CE  LYS A 179      13.029  35.158  13.856  1.00174.81           C
ANISOU   63  CE  LYS A 179    25149  24167  17105    475   -100   1470       C
ATOM     64  NZ  LYS A 179      14.477  35.401  13.643  1.00183.66           N
ANISOU   64  NZ  LYS A 179    26296  25150  18336    560     63   1447       N
ATOM     65  N   LYS A 191      22.160  43.024  14.780  1.00109.47           N
ANISOU   65  N   LYS A 191    16639  15134   9822    335   1020   2300       N
ATOM     66  CA  LYS A 191      22.083  41.670  15.331  1.00107.59           C
ANISOU   66  CA  LYS A 191    16315  14937   9626    408    953   2087       C
ATOM     67  C   LYS A 191      23.112  41.452  16.448  1.00111.00           C
ANISOU   67  C   LYS A 191    16633  15307  10236    322    969   2010       C
ATOM     68  O   LYS A 191      22.816  40.736  17.404  1.00109.24           O
ANISOU   68  O   LYS A 191    16385  15004  10116    359    876   1868       O
ATOM     69  CB  LYS A 191      22.290  40.622  14.232  1.00110.77           C
ANISOU   69  CB  LYS A 191    16684  15560   9842    503   1000   2002       C
ATOM     70  CG  LYS A 191      21.009  39.990  13.713  1.00123.48           C
ANISOU   70  CG  LYS A 191    18387  17218  11314    606    896   1933       C
ATOM     71  CD  LYS A 191      21.308  38.618  13.104  1.00135.11           C
ANISOU   71  CD  LYS A 191    19854  18834  12648    693    900   1767       C
ATOM     72  CE  LYS A 191      20.135  37.971  12.402  1.00145.97           C
ANISOU   72  CE  LYS A 191    21335  20283  13844    754    798   1704       C
ATOM     73  NZ  LYS A 191      19.083  37.493  13.341  1.00153.27           N
ANISOU   73  NZ  LYS A 191    22295  21095  14847    725    634   1617       N
ATOM     74  N   THR A 194      22.191  43.905  19.712  1.00108.61           N
ANISOU   74  N   THR A 194    16533  14357  10377    148    768   2113       N
ATOM     75  CA  THR A 194      21.102  43.368  20.540  1.00106.61           C
ANISOU   75  CA  THR A 194    16286  14051  10170    268    642   1998       C
ATOM     76  C   THR A 194      21.563  42.094  21.250  1.00109.10           C
ANISOU   76  C   THR A 194    16453  14431  10570    261    611   1823       C
ATOM     77  O   THR A 194      20.990  41.726  22.276  1.00107.41           O
ANISOU   77  O   THR A 194    16223  14148  10440    298    511   1732       O
ATOM     78  CB  THR A 194      19.824  43.127  19.734  1.00112.91           C
ANISOU   78  CB  THR A 194    17143  14953  10806    415    592   2018       C
ATOM     79  OG1 THR A 194      20.102  42.266  18.631  1.00112.10           O
ANISOU   79  OG1 THR A 194    16981  15041  10570    431    647   1983       O
ATOM     80  CG2 THR A 194      19.162  44.417  19.278  1.00112.38           C
ANISOU   80  CG2 THR A 194    17240  14800  10657    476    595   2188       C
ATOM     81  N   ALA A 195      22.598  41.424  20.699  1.00105.70           N
ANISOU   81  N   ALA A 195    15918  14144  10101    230    699   1784       N
ATOM     82  CA  ALA A 195      23.197  40.224  21.276  1.00104.28           C
ANISOU   82  CA  ALA A 195    15619  14024   9978    253    683   1628       C
ATOM     83  C   ALA A 195      23.882  40.590  22.592  1.00106.88           C
ANISOU   83  C   ALA A 195    15876  14245  10490    151    667   1608       C
ATOM     84  O   ALA A 195      23.747  39.858  23.567  1.00105.22           O
ANISOU   84  O   ALA A 195    15622  13990  10368    185    588   1487       O
ATOM     85  CB  ALA A 195      24.206  39.623  20.311  1.00106.32           C
ANISOU   85  CB  ALA A 195    15794  14482  10123    283    795   1611       C
ATOM     86  N   ASN A 198      21.009  42.777  25.172  1.00 96.83           N
ANISOU   86  N   ASN A 198    14904  12471   9416    218    383   1674       N
ATOM     87  CA  ASN A 198      20.013  41.868  25.751  1.00 94.61           C
ANISOU   87  CA  ASN A 198    14572  12248   9125    320    277   1572       C
ATOM     88  C   ASN A 198      20.549  40.548  26.354  1.00 96.45           C
ANISOU   88  C   ASN A 198    14674  12544   9431    286    249   1431       C
ATOM     89  O   ASN A 198      19.799  39.862  27.052  1.00 95.00           O
ANISOU   89  O   ASN A 198    14458  12380   9256    329    150   1356       O
ATOM     90  CB  ASN A 198      18.845  41.637  24.787  1.00 94.18           C
ANISOU   90  CB  ASN A 198    14563  12320   8901    431    246   1615       C
ATOM     91  CG  ASN A 198      18.078  42.896  24.479  1.00113.01           C
ANISOU   91  CG  ASN A 198    17083  14645  11211    522    244   1747       C
ATOM     92  OD1 ASN A 198      17.055  43.194  25.099  1.00106.63           O
ANISOU   92  OD1 ASN A 198    16301  13833  10379    633    161   1754       O
ATOM     93  ND2 ASN A 198      18.566  43.679  23.528  1.00105.12           N
ANISOU   93  ND2 ASN A 198    16178  13607  10158    490    335   1862       N
ATOM     94  N   PHE A 199      21.830  40.199  26.116  1.00 92.61           N
ANISOU   94  N   PHE A 199    14109  12100   8980    216    333   1404       N
ATOM     95  CA  PHE A 199      22.400  38.970  26.671  1.00 91.24           C
ANISOU   95  CA  PHE A 199    13832  11977   8857    224    310   1275       C
ATOM     96  C   PHE A 199      23.798  39.126  27.266  1.00 95.82           C
ANISOU   96  C   PHE A 199    14298  12562   9547    139    372   1260       C
ATOM     97  O   PHE A 199      23.934  38.922  28.466  1.00 94.92           O
ANISOU   97  O   PHE A 199    14131  12389   9546    118    310   1194       O
ATOM     98  CB  PHE A 199      22.299  37.789  25.689  1.00 93.08           C
ANISOU   98  CB  PHE A 199    14081  12330   8953    303    318   1212       C
ATOM     99  CG  PHE A 199      22.787  36.452  26.203  1.00 93.89           C
ANISOU   99  CG  PHE A 199    14140  12453   9082    348    280   1077       C
ATOM    100  CD1 PHE A 199      21.926  35.591  26.875  1.00 95.73           C
ANISOU  100  CD1 PHE A 199    14420  12634   9319    364    152    997       C
ATOM    101  CD2 PHE A 199      24.095  36.033  25.972  1.00 96.70           C
ANISOU  101  CD2 PHE A 199    14413  12895   9432    383    371   1040       C
ATOM    102  CE1 PHE A 199      22.372  34.347  27.330  1.00 96.32           C
ANISOU  102  CE1 PHE A 199    14499  12693   9404    409    109    881       C
ATOM    103  CE2 PHE A 199      24.541  34.791  26.430  1.00 99.27           C
ANISOU  103  CE2 PHE A 199    14728  13228   9762    468    333    917       C
ATOM    104  CZ  PHE A 199      23.676  33.955  27.104  1.00 96.24           C
ANISOU  104  CZ  PHE A 199    14431  12743   9392    479    200    837       C
ATOM    105  N   PHE A 424      20.023  28.933  32.688  1.00 84.51           N
ANISOU  105  N   PHE A 424    13307  10790   8012    202   -602    557       N
ATOM    106  CA  PHE A 424      19.898  29.984  31.673  1.00 84.74           C
ANISOU  106  CA  PHE A 424    13273  10916   8010    222   -502    613       C
ATOM    107  C   PHE A 424      21.162  30.228  30.840  1.00 90.30           C
ANISOU  107  C   PHE A 424    13958  11632   8718    356   -358    584       C
ATOM    108  O   PHE A 424      21.050  30.688  29.708  1.00 90.33           O
ANISOU  108  O   PHE A 424    13982  11702   8639    373   -290    618       O
ATOM    109  CB  PHE A 424      19.412  31.283  32.322  1.00 85.43           C
ANISOU  109  CB  PHE A 424    13194  11075   8190    181   -484    700       C
ATOM    110  CG  PHE A 424      18.684  32.222  31.394  1.00 87.16           C
ANISOU  110  CG  PHE A 424    13399  11389   8330    174   -443    782       C
ATOM    111  CD1 PHE A 424      17.321  32.082  31.167  1.00 90.33           C
ANISOU  111  CD1 PHE A 424    13828  11888   8605     98   -539    831       C
ATOM    112  CD2 PHE A 424      19.350  33.279  30.786  1.00 89.61           C
ANISOU  112  CD2 PHE A 424    13660  11707   8680    237   -314    824       C
ATOM    113  CE1 PHE A 424      16.642  32.961  30.321  1.00 91.63           C
ANISOU  113  CE1 PHE A 424    13973  12161   8682    122   -503    914       C
ATOM    114  CE2 PHE A 424      18.671  34.158  29.939  1.00 92.82           C
ANISOU  114  CE2 PHE A 424    14077  12187   9005    246   -280    910       C
ATOM    115  CZ  PHE A 424      17.319  33.998  29.718  1.00 90.97           C
ANISOU  115  CZ  PHE A 424    13869  12052   8644    207   -373    952       C
ATOM    116  N   TRP A 428      21.094  28.956  26.771  1.00102.93           N
ANISOU  116  N   TRP A 428    15978  13307   9824    514   -273    485       N
ATOM    117  CA  TRP A 428      21.181  30.034  25.795  1.00102.88           C
ANISOU  117  CA  TRP A 428    15872  13432   9786    534   -152    568       C
ATOM    118  C   TRP A 428      22.562  30.351  25.231  1.00109.33           C
ANISOU  118  C   TRP A 428    16603  14333  10606    680     11    563       C
ATOM    119  O   TRP A 428      22.623  30.731  24.061  1.00110.09           O
ANISOU  119  O   TRP A 428    16710  14531  10590    715     93    599       O
ATOM    120  CB  TRP A 428      20.501  31.298  26.319  1.00 99.96           C
ANISOU  120  CB  TRP A 428    15348  13109   9524    427   -151    689       C
ATOM    121  CG  TRP A 428      19.006  31.225  26.336  1.00100.40           C
ANISOU  121  CG  TRP A 428    15454  13195   9497    307   -279    730       C
ATOM    122  CD1 TRP A 428      18.205  31.075  27.430  1.00102.28           C
ANISOU  122  CD1 TRP A 428    15657  13415   9790    208   -396    746       C
ATOM    123  CD2 TRP A 428      18.131  31.342  25.210  1.00100.96           C
ANISOU  123  CD2 TRP A 428    15592  13369   9400    272   -300    774       C
ATOM    124  NE1 TRP A 428      16.882  31.095  27.055  1.00101.97           N
ANISOU  124  NE1 TRP A 428    15640  13483   9619    112   -487    803       N
ATOM    125  CE2 TRP A 428      16.806  31.270  25.698  1.00104.41           C
ANISOU  125  CE2 TRP A 428    16012  13866   9792    148   -433    820       C
ATOM    126  CE3 TRP A 428      18.335  31.511  23.831  1.00103.22           C
ANISOU  126  CE3 TRP A 428    15935  13730   9553    334   -218    785       C
ATOM    127  CZ2 TRP A 428      15.691  31.346  24.856  1.00104.45           C
ANISOU  127  CZ2 TRP A 428    16048  14017   9622     83   -491    877       C
ATOM    128  CZ3 TRP A 428      17.230  31.587  22.998  1.00105.44           C
ANISOU  128  CZ3 TRP A 428    16266  14126   9670    272   -277    835       C
ATOM    129  CH2 TRP A 428      15.927  31.500  23.510  1.00105.59           C
ANISOU  129  CH2 TRP A 428    16259  14214   9645    146   -415    881       C
ATOM    130  N   TYR A 431      23.535  29.030  21.668  1.00115.48           N
ANISOU  130  N   TYR A 431    17704  15314  10860   1034    179    412       N
ATOM    131  CA  TYR A 431      22.812  29.778  20.632  1.00115.85           C
ANISOU  131  CA  TYR A 431    17742  15463  10811    948    207    503       C
ATOM    132  C   TYR A 431      23.432  31.158  20.393  1.00120.39           C
ANISOU  132  C   TYR A 431    18086  16189  11465    931    364    649       C
ATOM    133  O   TYR A 431      23.517  31.586  19.243  1.00121.47           O
ANISOU  133  O   TYR A 431    18217  16462  11474    964    453    705       O
ATOM    134  CB  TYR A 431      21.313  29.894  20.994  1.00115.77           C
ANISOU  134  CB  TYR A 431    17789  15376  10821    753     57    546       C
ATOM    135  CG  TYR A 431      20.538  30.946  20.222  1.00117.24           C
ANISOU  135  CG  TYR A 431    17908  15685  10952    671     88    677       C
ATOM    136  CD1 TYR A 431      20.116  30.713  18.917  1.00120.59           C
ANISOU  136  CD1 TYR A 431    18453  16201  11165    692     87    665       C
ATOM    137  CD2 TYR A 431      20.190  32.158  20.814  1.00116.59           C
ANISOU  137  CD2 TYR A 431    17664  15621  11013    587    110    811       C
ATOM    138  CE1 TYR A 431      19.401  31.677  18.205  1.00121.48           C
ANISOU  138  CE1 TYR A 431    18504  16439  11214    635    114    795       C
ATOM    139  CE2 TYR A 431      19.464  33.124  20.116  1.00117.53           C
ANISOU  139  CE2 TYR A 431    17749  15841  11067    547    134    937       C
ATOM    140  CZ  TYR A 431      19.062  32.874  18.815  1.00125.96           C
ANISOU  140  CZ  TYR A 431    18918  17016  11927    572    136    934       C
ATOM    141  OH  TYR A 431      18.352  33.821  18.118  1.00126.38           O
ANISOU  141  OH  TYR A 431    18937  17181  11903    551    158   1066       O
ATOM    142  N   PHE A 432      23.822  31.863  21.473  1.00116.07           N
ANISOU  142  N   PHE A 432    17370  15614  11119    861    388    714       N
ATOM    143  CA  PHE A 432      24.436  33.187  21.379  1.00116.28           C
ANISOU  143  CA  PHE A 432    17210  15745  11224    800    517    856       C
ATOM    144  C   PHE A 432      25.865  33.126  20.876  1.00123.29           C
ANISOU  144  C   PHE A 432    17980  16817  12047    916    665    857       C
ATOM    145  O   PHE A 432      26.332  34.088  20.261  1.00123.62           O
ANISOU  145  O   PHE A 432    17911  16997  12062    862    783    983       O
ATOM    146  CB  PHE A 432      24.314  33.972  22.690  1.00116.39           C
ANISOU  146  CB  PHE A 432    17117  15655  11450    669    476    918       C
ATOM    147  CG  PHE A 432      22.992  34.690  22.810  1.00116.67           C
ANISOU  147  CG  PHE A 432    17209  15607  11512    562    394    997       C
ATOM    148  CD1 PHE A 432      21.923  34.106  23.478  1.00118.33           C
ANISOU  148  CD1 PHE A 432    17500  15720  11742    529    247    939       C
ATOM    149  CD2 PHE A 432      22.806  35.940  22.230  1.00119.08           C
ANISOU  149  CD2 PHE A 432    17492  15952  11803    503    462   1140       C
ATOM    150  CE1 PHE A 432      20.696  34.766  23.577  1.00118.42           C
ANISOU  150  CE1 PHE A 432    17533  15715  11748    460    177   1019       C
ATOM    151  CE2 PHE A 432      21.574  36.595  22.323  1.00121.08           C
ANISOU  151  CE2 PHE A 432    17802  16147  12055    456    388   1214       C
ATOM    152  CZ  PHE A 432      20.531  36.006  23.003  1.00117.97           C
ANISOU  152  CZ  PHE A 432    17453  15697  11671    446    249   1152       C
ATOM    153  N   PHE A 435      25.523  32.758  17.182  1.00131.61           N
ANISOU  153  N   PHE A 435    19258  18199  12548   1126    813    868       N
ATOM    154  CA  PHE A 435      25.196  34.066  16.627  1.00131.74           C
ANISOU  154  CA  PHE A 435    19202  18285  12570    990    877   1049       C
ATOM    155  C   PHE A 435      26.502  34.804  16.370  1.00137.98           C
ANISOU  155  C   PHE A 435    19789  19278  13359    981   1046   1165       C
ATOM    156  O   PHE A 435      26.593  35.576  15.420  1.00138.49           O
ANISOU  156  O   PHE A 435    19818  19480  13323    935   1140   1299       O
ATOM    157  CB  PHE A 435      24.329  34.848  17.622  1.00131.56           C
ANISOU  157  CB  PHE A 435    19169  18078  12738    819    781   1126       C
ATOM    158  CG  PHE A 435      22.970  35.249  17.104  1.00132.73           C
ANISOU  158  CG  PHE A 435    19431  18184  12817    757    703   1190       C
ATOM    159  CD1 PHE A 435      22.632  36.590  16.960  1.00135.73           C
ANISOU  159  CD1 PHE A 435    19773  18558  13240    661    741   1364       C
ATOM    160  CD2 PHE A 435      22.023  34.287  16.764  1.00134.96           C
ANISOU  160  CD2 PHE A 435    19869  18437  12974    793    584   1081       C
ATOM    161  CE1 PHE A 435      21.373  36.963  16.480  1.00136.56           C
ANISOU  161  CE1 PHE A 435    19970  18657  13260    643    670   1430       C
ATOM    162  CE2 PHE A 435      20.771  34.661  16.269  1.00137.75           C
ANISOU  162  CE2 PHE A 435    20291  18808  13239    734    511   1151       C
ATOM    163  CZ  PHE A 435      20.450  35.996  16.139  1.00135.68           C
ANISOU  163  CZ  PHE A 435    19967  18567  13019    679    558   1326       C
ATOM    164  N   ILE A 454      17.973  26.891  19.272  1.00136.14           N
ANISOU  164  N   ILE A 454    21129  17816  12781    409   -446    319       N
ATOM    165  CA  ILE A 454      16.786  27.710  19.542  1.00134.79           C
ANISOU  165  CA  ILE A 454    20786  17781  12646    227   -504    462       C
ATOM    166  C   ILE A 454      15.829  26.923  20.439  1.00138.10           C
ANISOU  166  C   ILE A 454    21295  18122  13056      9   -702    444       C
ATOM    167  O   ILE A 454      15.138  27.524  21.262  1.00136.45           O
ANISOU  167  O   ILE A 454    20899  17997  12950    -98   -741    552       O
ATOM    168  CB  ILE A 454      16.076  28.302  18.287  1.00138.88           C
ANISOU  168  CB  ILE A 454    21275  18503  12990    196   -484    540       C
ATOM    169  CG1 ILE A 454      15.560  27.225  17.315  1.00141.71           C
ANISOU  169  CG1 ILE A 454    21904  18854  13084    112   -606    432       C
ATOM    170  CG2 ILE A 454      16.936  29.326  17.572  1.00139.45           C
ANISOU  170  CG2 ILE A 454    21212  18676  13098    377   -284    608       C
ATOM    171  CD1 ILE A 454      14.072  27.249  17.121  1.00150.94           C
ANISOU  171  CD1 ILE A 454    23054  20185  14113   -121   -758    511       C
ATOM    172  N   TYR A 458      14.476  27.007  24.507  1.00119.89           N
ANISOU  172  N   TYR A 458    18647  15758  11149   -345   -946    605       N
ATOM    173  CA  TYR A 458      13.080  26.699  24.823  1.00120.08           C
ANISOU  173  CA  TYR A 458    18647  15925  11053   -597  -1115    677       C
ATOM    174  C   TYR A 458      13.044  25.589  25.891  1.00122.39           C
ANISOU  174  C   TYR A 458    19078  16051  11374   -747  -1253    628       C
ATOM    175  O   TYR A 458      12.014  25.398  26.538  1.00121.83           O
ANISOU  175  O   TYR A 458    18933  16108  11247   -964  -1385    708       O
ATOM    176  CB  TYR A 458      12.284  26.272  23.559  1.00123.83           C
ANISOU  176  CB  TYR A 458    19262  16517  11269   -733  -1202    671       C
ATOM    177  CG  TYR A 458      12.138  27.309  22.454  1.00126.44           C
ANISOU  177  CG  TYR A 458    19466  17041  11533   -609  -1088    739       C
ATOM    178  CD1 TYR A 458      11.970  28.661  22.750  1.00127.29           C
ANISOU  178  CD1 TYR A 458    19304  17305  11754   -488   -983    864       C
ATOM    179  CD2 TYR A 458      12.053  26.923  21.116  1.00129.03           C
ANISOU  179  CD2 TYR A 458    19965  17399  11659   -624  -1102    684       C
ATOM    180  CE1 TYR A 458      11.812  29.613  21.738  1.00128.47           C
ANISOU  180  CE1 TYR A 458    19367  17614  11830   -373   -886    940       C
ATOM    181  CE2 TYR A 458      11.894  27.866  20.096  1.00130.15           C
ANISOU  181  CE2 TYR A 458    19994  17730  11729   -512  -1001    759       C
ATOM    182  CZ  TYR A 458      11.765  29.209  20.412  1.00135.54           C
ANISOU  182  CZ  TYR A 458    20415  18551  12534   -390   -894    894       C
ATOM    183  OH  TYR A 458      11.602  30.139  19.413  1.00135.19           O
ANISOU  183  OH  TYR A 458    20288  18672  12408   -277   -800    980       O
TER     184      ILE A 485
HETATM  185  C01A5EH A1200      14.569  31.755  20.378  0.50128.73           C
HETATM  186  N02A5EH A1200      14.525  32.943  19.512  0.50135.70           N
HETATM  187  C03A5EH A1200      14.452  32.511  18.106  0.50 23.95           C
HETATM  188  C04A5EH A1200      15.730  33.765  19.724  0.50108.61           C
HETATM  189  C05A5EH A1200      15.364  35.138  20.280  0.50 60.67           C
HETATM  190  C06A5EH A1200      15.773  35.211  21.734  0.50113.33           C
HETATM  191  C07A5EH A1200      16.751  36.014  22.195  0.50165.91           C
HETATM  192  C08A5EH A1200      17.526  36.943  21.311  0.50153.27           C
HETATM  193  C09A5EH A1200      18.420  36.473  20.347  0.50127.97           C
HETATM  194  C10A5EH A1200      19.149  37.384  19.580  0.50131.79           C
HETATM  195  C11A5EH A1200      18.997  38.757  19.793  0.50 91.15           C
HETATM  196  C12A5EH A1200      18.119  39.218  20.775  0.50 77.62           C
HETATM  197  C13A5EH A1200      17.392  38.303  21.537  0.50 99.53           C
HETATM  198  C14A5EH A1200      16.426  38.762  22.605  0.50 29.88           C
HETATM  199  O15A5EH A1200      16.962  38.468  23.894  0.50129.74           O
HETATM  200  C16A5EH A1200      17.176  37.205  24.405  0.50141.60           C
HETATM  201  C17A5EH A1200      17.517  37.134  25.758  0.50123.84           C
HETATM  202  C18A5EH A1200      17.770  35.908  26.373  0.50140.03           C
HETATM  203  C19A5EH A1200      17.686  34.733  25.630  0.50137.78           C
HETATM  204  C20A5EH A1200      17.350  34.796  24.279  0.50113.47           C
HETATM  205  C21A5EH A1200      17.092  36.021  23.659  0.50159.27           C
HETATM  206  C1 BD7V A1201      14.808  32.837  18.106  0.50 73.17           C
HETATM  207  N1 BD7V A1201      14.677  33.217  19.522  0.50134.26           N
HETATM  208  O1 BD7V A1201      17.822  39.257  22.374  0.50 60.56           O
HETATM  209  C2 BD7V A1201      14.643  32.000  20.349  0.50132.98           C
HETATM  210  C3 BD7V A1201      15.818  34.061  19.915  0.50101.39           C
HETATM  211  C4 BD7V A1201      15.343  35.458  20.304  0.50 63.13           C
HETATM  212  C5 BD7V A1201      15.754  35.727  21.733  0.50 97.28           C
HETATM  213  C6 BD7V A1201      16.832  36.440  22.115  0.50159.20           C
HETATM  214  C7 BD7V A1201      17.090  36.591  23.581  0.50151.60           C
HETATM  215  C8 BD7V A1201      17.401  35.486  24.375  0.50133.41           C
HETATM  216  C9 BD7V A1201      17.654  35.666  25.736  0.50144.02           C
HETATM  217  C10BD7V A1201      17.597  36.946  26.291  0.50124.82           C
HETATM  218  C11BD7V A1201      17.280  38.046  25.491  0.50 95.05           C
HETATM  219  C12BD7V A1201      17.027  37.857  24.132  0.50118.35           C
HETATM  220  C13BD7V A1201      16.702  39.017  23.224  0.50 79.50           C
HETATM  221  C14BD7V A1201      18.247  38.425  21.362  0.50105.70           C
HETATM  222  C15BD7V A1201      17.803  37.105  21.170  0.50154.58           C
HETATM  223  C16BD7V A1201      19.189  38.972  20.486  0.50 61.44           C
HETATM  224  C17BD7V A1201      19.706  38.223  19.432  0.50 50.85           C
HETATM  225  C18BD7V A1201      19.279  36.910  19.253  0.50146.65           C
HETATM  226  C19BD7V A1201      18.351  36.351  20.130  0.50111.98           C
HETATM  227  P   PO4 A1202      17.536  33.739  14.081  1.00172.63           P
HETATM  228  O1  PO4 A1202      18.998  33.196  13.827  1.00178.54           O
HETATM  229  O2  PO4 A1202      17.291  35.061  13.244  1.00178.73           O
HETATM  230  O3  PO4 A1202      16.485  32.632  13.656  1.00178.41           O
HETATM  231  O4  PO4 A1202      17.396  34.078  15.613  1.00178.53           O
CONECT  185  186
CONECT  186  185  187  188
CONECT  187  186
CONECT  188  186  189
CONECT  189  188  190
CONECT  190  189  191
CONECT  191  190  192  205
CONECT  192  191  193  197
CONECT  193  192  194
CONECT  194  193  195
CONECT  195  194  196
CONECT  196  195  197
CONECT  197  192  196  198
CONECT  198  197  199
CONECT  199  198  200
CONECT  200  199  201  205
CONECT  201  200  202
CONECT  202  201  203
CONECT  203  202  204
CONECT  204  203  205
CONECT  205  191  200  204
CONECT  206  207
CONECT  207  206  209  210
CONECT  208  220  221
CONECT  209  207
CONECT  210  207  211
CONECT  211  210  212
CONECT  212  211  213
CONECT  213  212  214  222
CONECT  214  213  215  219
CONECT  215  214  216
CONECT  216  215  217
CONECT  217  216  218
CONECT  218  217  219
CONECT  219  214  218  220
CONECT  220  208  219
CONECT  221  208  222  223
CONECT  222  213  221  226
CONECT  223  221  224
CONECT  224  223  225
CONECT  225  224  226
CONECT  226  222  225
CONECT  227  228  229  230  231
CONECT  228  227
CONECT  229  227
CONECT  230  227
CONECT  231  227
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.