CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 210201174800131912

Job options:

ID        	=	 210201174800131912
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:

ATOM      1  N   PRO A 148     -57.761 -37.236  42.507  1.00313.69           N  
ANISOU    1  N   PRO A 148    40595  40493  38100  -1626    -57    132       N  
ATOM      2  CA  PRO A 148     -57.133 -35.920  42.422  1.00316.53           C  
ANISOU    2  CA  PRO A 148    40811  40886  38568  -1506    -54    118       C  
ATOM      3  C   PRO A 148     -55.655 -35.936  41.981  1.00303.08           C  
ANISOU    3  C   PRO A 148    39128  39105  36923  -1354   -147    164       C  
ATOM      4  O   PRO A 148     -55.050 -37.010  41.848  1.00201.96           O  
ANISOU    4  O   PRO A 148    26457  26209  24066  -1338   -219    206       O  
ATOM      5  CB  PRO A 148     -57.301 -35.381  43.846  1.00224.98           C  
ANISOU    5  CB  PRO A 148    29241  29316  26923  -1585    -16     87       C  
ATOM      6  CG  PRO A 148     -58.605 -35.985  44.297  1.00229.02           C  
ANISOU    6  CG  PRO A 148    29809  29868  27339  -1755     52     57       C  
ATOM      7  CD  PRO A 148     -58.860 -37.243  43.492  1.00193.05           C  
ANISOU    7  CD  PRO A 148    25342  25269  22737  -1787     20     89       C  
ATOM      8  N   GLY A 149     -55.104 -34.741  41.743  1.00306.72           N  
ANISOU    8  N   GLY A 149    39451  39600  37488  -1245   -142    152       N  
ATOM      9  CA  GLY A 149     -53.753 -34.562  41.195  1.00277.48           C  
ANISOU    9  CA  GLY A 149    35729  35842  33859  -1097   -216    186       C  
ATOM     10  C   GLY A 149     -53.781 -33.767  39.895  1.00257.51           C  
ANISOU   10  C   GLY A 149    33032  33361  31445   -998   -190    177       C  
ATOM     11  O   GLY A 149     -54.236 -32.617  39.868  1.00177.59           O  
ANISOU   11  O   GLY A 149    22773  23315  21386   -989   -131    141       O  
ATOM     12  N   ILE A 150     -53.295 -34.379  38.815  1.00249.55           N  
ANISOU   12  N   ILE A 150    32042  32309  30466   -925   -235    208       N  
ATOM     13  CA  ILE A 150     -53.416 -33.803  37.474  1.00189.51           C  
ANISOU   13  CA  ILE A 150    24300  24746  22958   -846   -211    202       C  
ATOM     14  C   ILE A 150     -54.863 -33.362  37.228  1.00221.36           C  
ANISOU   14  C   ILE A 150    28238  28870  26998   -928   -128    164       C  
ATOM     15  O   ILE A 150     -55.119 -32.194  36.933  1.00203.11           O  
ANISOU   15  O   ILE A 150    25782  26623  24766   -887    -86    136       O  
ATOM     16  CB  ILE A 150     -52.963 -34.789  36.371  1.00133.49           C  
ANISOU   16  CB  ILE A 150    17265  17589  15864   -790   -260    238       C  
ATOM     17  N   ALA A 151     -55.803 -34.292  37.404  1.00222.53           N  
ANISOU   17  N   ALA A 151    28467  29021  27060  -1045   -107    160       N  
ATOM     18  CA  ALA A 151     -57.236 -34.036  37.190  1.00272.21           C  
ANISOU   18  CA  ALA A 151    34675  35400  33351  -1135    -32    120       C  
ATOM     19  C   ALA A 151     -57.832 -32.934  38.082  1.00260.31           C  
ANISOU   19  C   ALA A 151    33072  33969  31863  -1178     33     71       C  
ATOM     20  O   ALA A 151     -58.955 -32.466  37.846  1.00237.16           O  
ANISOU   20  O   ALA A 151    30034  31118  28956  -1228     97     31       O  
ATOM     21  CB  ALA A 151     -58.026 -35.329  37.339  1.00229.94           C  
ANISOU   21  CB  ALA A 151    29446  30029  27892  -1262    -26    126       C  
ATOM     22  N   TRP A 152     -57.076 -32.523  39.098  1.00210.91           N  
ANISOU   22  N   TRP A 152    26852  27686  25595  -1158     16     72       N  
ATOM     23  CA  TRP A 152     -57.514 -31.468  40.000  1.00217.85           C  
ANISOU   23  CA  TRP A 152    27652  28629  26490  -1193     76     25       C  
ATOM     24  C   TRP A 152     -57.245 -30.088  39.384  1.00210.86           C  
ANISOU   24  C   TRP A 152    26602  27787  25728  -1078     90      8       C  
ATOM     25  O   TRP A 152     -58.054 -29.166  39.518  1.00185.55           O  
ANISOU   25  O   TRP A 152    23280  24657  22563  -1100    155    -38       O  
ATOM     26  CB  TRP A 152     -56.846 -31.638  41.373  1.00263.13           C  
ANISOU   26  CB  TRP A 152    33508  34315  32153  -1230     48     33       C  
ATOM     27  CG  TRP A 152     -57.818 -31.832  42.532  1.00342.85           C  
ANISOU   27  CG  TRP A 152    43659  44448  42158  -1380    111     -4       C  
ATOM     28  CD1 TRP A 152     -57.637 -31.434  43.834  1.00280.62           C  
ANISOU   28  CD1 TRP A 152    35823  36565  34231  -1428    126    -24       C  
ATOM     29  CD2 TRP A 152     -59.112 -32.469  42.487  1.00353.27           C  
ANISOU   29  CD2 TRP A 152    44994  45813  43417  -1508    169    -30       C  
ATOM     30  NE1 TRP A 152     -58.731 -31.784  44.595  1.00220.50           N  
ANISOU   30  NE1 TRP A 152    28254  28992  26531  -1577    194    -61       N  
ATOM     31  CE2 TRP A 152     -59.650 -32.416  43.794  1.00332.57           C  
ANISOU   31  CE2 TRP A 152    42427  43217  40716  -1629    222    -66       C  
ATOM     32  CE3 TRP A 152     -59.868 -33.078  41.467  1.00296.31           C  
ANISOU   32  CE3 TRP A 152    37753  38621  36207  -1534    181    -27       C  
ATOM     33  CZ2 TRP A 152     -60.912 -32.948  44.106  1.00275.37           C  
ANISOU   33  CZ2 TRP A 152    35205  36023  33398  -1777    291   -102       C  
ATOM     34  CZ3 TRP A 152     -61.120 -33.606  41.782  1.00234.23           C  
ANISOU   34  CZ3 TRP A 152    29913  30809  28273  -1680    245    -61       C  
ATOM     35  CH2 TRP A 152     -61.627 -33.536  43.088  1.00216.80           C  
ANISOU   35  CH2 TRP A 152    27754  28629  25990  -1800    300    -99       C  
ATOM     36  N   ILE A 153     -56.116 -29.964  38.690  1.00201.36           N  
ANISOU   36  N   ILE A 153    25390  26533  24582   -958     30     45       N  
ATOM     37  CA  ILE A 153     -55.803 -28.767  37.911  1.00206.45           C  
ANISOU   37  CA  ILE A 153    25890  27210  25339   -848     37     37       C  
ATOM     38  C   ILE A 153     -56.768 -28.707  36.740  1.00187.77           C  
ANISOU   38  C   ILE A 153    23431  24894  23015   -850     70     24       C  
ATOM     39  O   ILE A 153     -57.290 -27.638  36.402  1.00144.23           O  
ANISOU   39  O   ILE A 153    17784  19442  17574   -821    111     -7       O  
ATOM     40  CB  ILE A 153     -54.375 -28.813  37.332  1.00206.14           C  
ANISOU   40  CB  ILE A 153    25872  27104  25345   -728    -33     80       C  
ATOM     41  CG1 ILE A 153     -53.530 -29.866  38.049  1.00198.53           C  
ANISOU   41  CG1 ILE A 153    25068  26061  24304   -744    -95    114       C  
ATOM     42  CG2 ILE A 153     -53.727 -27.438  37.383  1.00183.08           C  
ANISOU   42  CG2 ILE A 153    22846  24203  22511   -639    -28     66       C  
ATOM     43  CD1 ILE A 153     -52.346 -30.364  37.251  1.00221.07           C  
ANISOU   43  CD1 ILE A 153    27959  28846  27189   -641   -165    157       C  
ATOM     44  N   ALA A 154     -56.991 -29.871  36.129  1.00141.26           N  
ANISOU   44  N   ALA A 154    17618  18974  17078   -884     47     50       N  
ATOM     45  CA  ALA A 154     -57.926 -30.009  35.019  1.00189.61           C  
ANISOU   45  CA  ALA A 154    23673  25139  23228   -899     69     42       C  
ATOM     46  C   ALA A 154     -59.214 -29.290  35.374  1.00229.85           C  
ANISOU   46  C   ALA A 154    28662  30327  28340   -968    142    -12       C  
ATOM     47  O   ALA A 154     -59.548 -28.269  34.764  1.00196.00           O  
ANISOU   47  O   ALA A 154    24241  26090  24139   -911    164    -34       O  
ATOM     48  CB  ALA A 154     -58.188 -31.480  34.722  1.00163.84           C  
ANISOU   48  CB  ALA A 154    20533  21835  19882   -969     45     69       C  
ATOM     49  N   LEU A 155     -59.905 -29.823  36.382  1.00213.87           N  
ANISOU   49  N   LEU A 155    26703  28322  26233  -1090    178    -36       N  
ATOM     50  CA  LEU A 155     -61.042 -29.173  37.016  1.00158.23           C  
ANISOU   50  CA  LEU A 155    19568  21361  19192  -1165    254    -96       C  
ATOM     51  C   LEU A 155     -60.802 -27.657  37.202  1.00209.04           C  
ANISOU   51  C   LEU A 155    25876  27831  25718  -1081    276   -126       C  
ATOM     52  O   LEU A 155     -61.546 -26.853  36.629  1.00176.76           O  
ANISOU   52  O   LEU A 155    21651  23806  21703  -1055    310   -159       O  
ATOM     53  CB  LEU A 155     -61.357 -29.886  38.345  1.00190.20           C  
ANISOU   53  CB  LEU A 155    23733  25402  23129  -1296    281   -111       C  
ATOM     54  CG  LEU A 155     -61.823 -29.157  39.621  1.00239.12           C  
ANISOU   54  CG  LEU A 155    29895  31649  29308  -1360    347   -166       C  
ATOM     55  CD1 LEU A 155     -63.247 -28.607  39.538  1.00181.92           C  
ANISOU   55  CD1 LEU A 155    22515  24508  22098  -1420    428   -231       C  
ATOM     56  CD2 LEU A 155     -61.672 -30.073  40.829  1.00177.70           C  
ANISOU   56  CD2 LEU A 155    22283  23828  21406  -1471    346   -157       C  
ATOM     57  N   LEU A 156     -59.756 -27.288  37.959  1.00180.05           N  
ANISOU   57  N   LEU A 156    22253  24115  22042  -1037    252   -112       N  
ATOM     58  CA  LEU A 156     -59.413 -25.883  38.268  1.00166.08           C  
ANISOU   58  CA  LEU A 156    20384  22369  20348   -963    271   -138       C  
ATOM     59  C   LEU A 156     -59.457 -24.979  37.043  1.00187.10           C  
ANISOU   59  C   LEU A 156    22911  25056  23119   -859    265   -139       C  
ATOM     60  O   LEU A 156     -60.030 -23.881  37.076  1.00153.17           O  
ANISOU   60  O   LEU A 156    18494  20816  18884   -838    308   -183       O  
ATOM     61  CB  LEU A 156     -58.009 -25.796  38.885  1.00140.84           C  
ANISOU   61  CB  LEU A 156    17269  19103  17138   -908    220   -105       C  
ATOM     62  CG  LEU A 156     -57.181 -24.540  38.511  1.00190.35           C  
ANISOU   62  CG  LEU A 156    23446  25369  23506   -784    202   -102       C  
ATOM     63  CD1 LEU A 156     -57.469 -23.283  39.340  1.00126.68           C  
ANISOU   63  CD1 LEU A 156    15303  17353  15477   -787    255   -153       C  
ATOM     64  CD2 LEU A 156     -55.694 -24.846  38.525  1.00206.37           C  
ANISOU   64  CD2 LEU A 156    25558  27320  25531   -713    129    -52       C  
ATOM     65  N   LEU A 157     -58.814 -25.462  35.981  1.00154.84           N  
ANISOU   65  N   LEU A 157    18854  20924  19052   -793    209    -91       N  
ATOM     66  CA  LEU A 157     -58.698 -24.769  34.711  1.00179.62           C  
ANISOU   66  CA  LEU A 157    21893  24072  22282   -695    192    -81       C  
ATOM     67  C   LEU A 157     -60.047 -24.560  34.033  1.00195.30           C  
ANISOU   67  C   LEU A 157    23776  26126  24300   -727    229   -114       C  
ATOM     68  O   LEU A 157     -60.344 -23.469  33.525  1.00137.00           O  
ANISOU   68  O   LEU A 157    16274  18780  16999   -666    243   -136       O  
ATOM     69  CB  LEU A 157     -57.773 -25.570  33.792  1.00161.07           C  
ANISOU   69  CB  LEU A 157    19617  21655  19926   -639    129    -24       C  
ATOM     70  CG  LEU A 157     -57.859 -25.296  32.291  1.00146.78           C  
ANISOU   70  CG  LEU A 157    17734  19850  18183   -568    111     -9       C  
ATOM     71  CD1 LEU A 157     -57.375 -23.896  31.924  1.00173.63           C  
ANISOU   71  CD1 LEU A 157    21031  23260  21677   -469    111    -17       C  
ATOM     72  CD2 LEU A 157     -57.064 -26.351  31.550  1.00124.28           C  
ANISOU   72  CD2 LEU A 157    14981  16934  15305   -540     59     40       C  
ATOM     73  N   LEU A 158     -60.840 -25.628  34.020  1.00188.01           N  
ANISOU   73  N   LEU A 158    22905  25218  23311   -823    241   -116       N  
ATOM     74  CA  LEU A 158     -62.152 -25.648  33.394  1.00156.90           C  
ANISOU   74  CA  LEU A 158    18879  21344  19391   -867    271   -146       C  
ATOM     75  C   LEU A 158     -63.113 -24.773  34.196  1.00185.46           C  
ANISOU   75  C   LEU A 158    22394  25038  23034   -910    338   -213       C  
ATOM     76  O   LEU A 158     -63.984 -24.104  33.634  1.00208.32           O  
ANISOU   76  O   LEU A 158    25164  27991  25994   -891    359   -247       O  
ATOM     77  CB  LEU A 158     -62.649 -27.083  33.303  1.00136.90           C  
ANISOU   77  CB  LEU A 158    16444  18801  16771   -969    266   -131       C  
ATOM     78  CG  LEU A 158     -61.571 -28.124  32.969  1.00198.90           C  
ANISOU   78  CG  LEU A 158    24436  26564  24573   -945    205    -69       C  
ATOM     79  CD1 LEU A 158     -62.145 -29.530  33.025  1.00245.09           C  
ANISOU   79  CD1 LEU A 158    30391  32403  30328  -1057    204    -58       C  
ATOM     80  CD2 LEU A 158     -60.858 -27.879  31.638  1.00224.10           C  
ANISOU   80  CD2 LEU A 158    27598  29718  27829   -830    155    -30       C  
ATOM     81  N   VAL A 159     -62.940 -24.792  35.514  1.00160.11           N  
ANISOU   81  N   VAL A 159    19240  21823  19770   -966    369   -233       N  
ATOM     82  CA  VAL A 159     -63.409 -23.723  36.391  1.00214.43           C  
ANISOU   82  CA  VAL A 159    26033  28757  26682   -975    428   -293       C  
ATOM     83  C   VAL A 159     -63.023 -22.350  35.799  1.00214.42           C  
ANISOU   83  C   VAL A 159    25919  28758  26790   -847    413   -298       C  
ATOM     84  O   VAL A 159     -63.891 -21.587  35.350  1.00154.51           O  
ANISOU   84  O   VAL A 159    18205  21229  19272   -824    439   -338       O  
ATOM     85  CB  VAL A 159     -62.821 -23.921  37.810  1.00194.62           C  
ANISOU   85  CB  VAL A 159    23630  26216  24098  -1029    444   -296       C  
ATOM     86  CG1 VAL A 159     -62.709 -22.608  38.574  1.00191.07           C  
ANISOU   86  CG1 VAL A 159    23108  25792  23698   -990    482   -339       C  
ATOM     87  CG2 VAL A 159     -63.637 -24.949  38.576  1.00206.30           C  
ANISOU   87  CG2 VAL A 159    25185  27720  25477  -1176    486   -319       C  
ATOM     88  N   ILE A 160     -61.715 -22.079  35.761  1.00192.98           N  
ANISOU   88  N   ILE A 160    23255  25979  24089   -766    367   -256       N  
ATOM     89  CA  ILE A 160     -61.138 -20.852  35.192  1.00203.85           C  
ANISOU   89  CA  ILE A 160    24549  27344  25558   -648    347   -251       C  
ATOM     90  C   ILE A 160     -61.775 -20.439  33.856  1.00193.80           C  
ANISOU   90  C   ILE A 160    23171  26100  24360   -593    334   -253       C  
ATOM     91  O   ILE A 160     -61.900 -19.242  33.537  1.00141.74           O  
ANISOU   91  O   ILE A 160    16478  19527  17848   -521    340   -275       O  
ATOM     92  CB  ILE A 160     -59.610 -21.016  34.997  1.00182.45           C  
ANISOU   92  CB  ILE A 160    21923  24555  22844   -577    287   -192       C  
ATOM     93  CG1 ILE A 160     -58.942 -21.383  36.324  1.00169.55           C  
ANISOU   93  CG1 ILE A 160    20393  22888  21139   -625    289   -189       C  
ATOM     94  CG2 ILE A 160     -58.980 -19.767  34.375  1.00142.69           C  
ANISOU   94  CG2 ILE A 160    16809  19507  17900   -463    267   -186       C  
ATOM     95  CD1 ILE A 160     -57.551 -21.956  36.159  1.00175.36           C  
ANISOU   95  CD1 ILE A 160    21228  23546  21852   -576    224   -130       C  
ATOM     96  N   PHE A 161     -62.186 -21.436  33.084  1.00147.13           N  
ANISOU   96  N   PHE A 161    17292  20191  18421   -630    313   -229       N  
ATOM     97  CA  PHE A 161     -62.644 -21.188  31.737  1.00192.25           C  
ANISOU   97  CA  PHE A 161    22928  25921  24195   -579    288   -220       C  
ATOM     98  C   PHE A 161     -64.049 -20.634  31.794  1.00203.54           C  
ANISOU   98  C   PHE A 161    24236  27432  25666   -612    332   -281       C  
ATOM     99  O   PHE A 161     -64.328 -19.551  31.255  1.00163.97           O  
ANISOU   99  O   PHE A 161    19120  22443  20739   -538    327   -301       O  
ATOM    100  CB  PHE A 161     -62.615 -22.478  30.924  1.00210.84           C  
ANISOU  100  CB  PHE A 161    25363  28247  26500   -613    251   -176       C  
ATOM    101  CG  PHE A 161     -62.175 -22.280  29.511  1.00250.74           C  
ANISOU  101  CG  PHE A 161    30397  33268  31604   -527    200   -136       C  
ATOM    102  CD1 PHE A 161     -63.044 -21.749  28.565  1.00233.07           C  
ANISOU  102  CD1 PHE A 161    28056  31072  29426   -501    194   -152       C  
ATOM    103  CD2 PHE A 161     -60.883 -22.612  29.127  1.00278.88           C  
ANISOU  103  CD2 PHE A 161    34045  36760  35155   -471    157    -84       C  
ATOM    104  CE1 PHE A 161     -62.632 -21.563  27.258  1.00253.31           C  
ANISOU  104  CE1 PHE A 161    30612  33603  32031   -426    146   -114       C  
ATOM    105  CE2 PHE A 161     -60.463 -22.425  27.824  1.00287.62           C  
ANISOU  105  CE2 PHE A 161    35138  37838  36305   -396    117    -50       C  
ATOM    106  CZ  PHE A 161     -61.339 -21.900  26.890  1.00277.77           C  
ANISOU  106  CZ  PHE A 161    33798  36629  35111   -377    111    -64       C  
ATOM    107  N   TYR A 162     -64.912 -21.395  32.471  1.00198.03           N  
ANISOU  107  N   TYR A 162    23556  26777  24907   -724    374   -313       N  
ATOM    108  CA  TYR A 162     -66.308 -21.046  32.696  1.00199.11           C  
ANISOU  108  CA  TYR A 162    23580  26999  25071   -775    426   -380       C  
ATOM    109  C   TYR A 162     -66.401 -19.710  33.402  1.00191.27           C  
ANISOU  109  C   TYR A 162    22499  26034  24139   -728    465   -432       C  
ATOM    110  O   TYR A 162     -67.176 -18.851  32.997  1.00187.57           O  
ANISOU  110  O   TYR A 162    21904  25613  23748   -685    476   -472       O  
ATOM    111  CB  TYR A 162     -67.005 -22.150  33.502  1.00149.98           C  
ANISOU  111  CB  TYR A 162    17417  20810  18757   -915    471   -404       C  
ATOM    112  CG  TYR A 162     -68.104 -21.689  34.445  1.00223.07           C  
ANISOU  112  CG  TYR A 162    26584  30148  28021   -983    550   -485       C  
ATOM    113  CD1 TYR A 162     -69.378 -21.353  33.971  1.00187.14           C  
ANISOU  113  CD1 TYR A 162    21898  25677  23528   -995    573   -537       C  
ATOM    114  CD2 TYR A 162     -67.872 -21.617  35.820  1.00285.00           C  
ANISOU  114  CD2 TYR A 162    34482  37991  35813  -1039    601   -513       C  
ATOM    115  CE1 TYR A 162     -70.378 -20.947  34.840  1.00207.91           C  
ANISOU  115  CE1 TYR A 162    24441  28385  26169  -1057    649   -617       C  
ATOM    116  CE2 TYR A 162     -68.866 -21.209  36.696  1.00323.50           C  
ANISOU  116  CE2 TYR A 162    39280  42942  40693  -1105    680   -592       C  
ATOM    117  CZ  TYR A 162     -70.114 -20.876  36.203  1.00305.13           C  
ANISOU  117  CZ  TYR A 162    36811  40695  38427  -1113    706   -646       C  
ATOM    118  OH  TYR A 162     -71.095 -20.473  37.078  1.00381.95           O  
ANISOU  118  OH  TYR A 162    46457  50502  48164  -1178    789   -730       O  
ATOM    119  N   VAL A 163     -65.585 -19.544  34.439  1.00139.08           N  
ANISOU  119  N   VAL A 163    15959  19389  17493   -733    483   -429       N  
ATOM    120  CA  VAL A 163     -65.503 -18.289  35.182  1.00150.22           C  
ANISOU  120  CA  VAL A 163    17307  20815  18953   -688    519   -474       C  
ATOM    121  C   VAL A 163     -65.106 -17.085  34.295  1.00200.70           C  
ANISOU  121  C   VAL A 163    23622  27188  25447   -557    479   -462       C  
ATOM    122  O   VAL A 163     -65.385 -15.931  34.623  1.00181.44           O  
ANISOU  122  O   VAL A 163    21096  24772  23068   -512    507   -508       O  
ATOM    123  CB  VAL A 163     -64.547 -18.421  36.393  1.00178.87           C  
ANISOU  123  CB  VAL A 163    21044  24400  22516   -718    532   -462       C  
ATOM    124  CG1 VAL A 163     -64.981 -19.564  37.303  1.00230.10           C  
ANISOU  124  CG1 VAL A 163    27619  30906  28901   -852    571   -476       C  
ATOM    125  CG2 VAL A 163     -63.110 -18.634  35.948  1.00189.33           C  
ANISOU  125  CG2 VAL A 163    22460  25641  23832   -649    463   -389       C  
ATOM    126  N   PHE A 164     -64.466 -17.357  33.165  1.00202.65           N  
ANISOU  126  N   PHE A 164    23902  27387  25708   -498    415   -400       N  
ATOM    127  CA  PHE A 164     -64.044 -16.293  32.273  1.00163.24           C  
ANISOU  127  CA  PHE A 164    18851  22370  20801   -383    375   -384       C  
ATOM    128  C   PHE A 164     -64.980 -16.062  31.107  1.00199.72           C  
ANISOU  128  C   PHE A 164    23376  27025  25482   -352    352   -393       C  
ATOM    129  O   PHE A 164     -65.120 -14.932  30.650  1.00203.92           O  
ANISOU  129  O   PHE A 164    23825  27560  26093   -270    338   -409       O  
ATOM    130  CB  PHE A 164     -62.667 -16.591  31.733  1.00173.74           C  
ANISOU  130  CB  PHE A 164    20274  23624  22114   -332    320   -313       C  
ATOM    131  CG  PHE A 164     -61.624 -15.665  32.236  1.00198.09           C  
ANISOU  131  CG  PHE A 164    23373  26669  25223   -269    317   -308       C  
ATOM    132  CD1 PHE A 164     -61.797 -14.290  32.137  1.00170.98           C  
ANISOU  132  CD1 PHE A 164    19850  23247  21868   -199    325   -339       C  
ATOM    133  CD2 PHE A 164     -60.460 -16.164  32.804  1.00177.44           C  
ANISOU  133  CD2 PHE A 164    20861  24001  22553   -280    303   -273       C  
ATOM    134  CE1 PHE A 164     -60.820 -13.423  32.595  1.00203.67           C  
ANISOU  134  CE1 PHE A 164    24007  27348  26029   -146    322   -334       C  
ATOM    135  CE2 PHE A 164     -59.474 -15.303  33.259  1.00156.69           C  
ANISOU  135  CE2 PHE A 164    18245  21340  19949   -225    297   -268       C  
ATOM    136  CZ  PHE A 164     -59.654 -13.929  33.153  1.00160.66           C  
ANISOU  136  CZ  PHE A 164    18660  21855  20527   -161    309   -299       C  
ATOM    137  N   ALA A 165     -65.582 -17.140  30.605  1.00222.56           N  
ANISOU  137  N   ALA A 165    26287  29939  28335   -415    341   -380       N  
ATOM    138  CA  ALA A 165     -66.575 -17.062  29.528  1.00229.40           C  
ANISOU  138  CA  ALA A 165    27066  30845  29251   -400    317   -390       C  
ATOM    139  C   ALA A 165     -67.862 -16.530  30.114  1.00210.62           C  
ANISOU  139  C   ALA A 165    24567  28546  26910   -432    369   -470       C  
ATOM    140  O   ALA A 165     -68.706 -15.975  29.406  1.00206.55           O  
ANISOU  140  O   ALA A 165    23945  28068  26464   -392    351   -495       O  
ATOM    141  CB  ALA A 165     -66.798 -18.428  28.902  1.00211.70           C  
ANISOU  141  CB  ALA A 165    24887  28600  26947   -468    292   -354       C  
ATOM    142  N   VAL A 166     -67.989 -16.753  31.422  1.00166.38           N  
ANISOU  142  N   VAL A 166    18988  22969  21259   -506    432   -508       N  
ATOM    143  CA  VAL A 166     -68.928 -16.077  32.304  1.00212.08           C  
ANISOU  143  CA  VAL A 166    24675  28823  27079   -531    498   -591       C  
ATOM    144  C   VAL A 166     -68.964 -14.569  32.039  1.00214.14           C  
ANISOU  144  C   VAL A 166    24836  29082  27442   -417    486   -618       C  
ATOM    145  O   VAL A 166     -70.028 -13.993  31.814  1.00200.58           O  
ANISOU  145  O   VAL A 166    22995  27422  25791   -397    498   -673       O  
ATOM    146  CB  VAL A 166     -68.512 -16.324  33.782  1.00231.68           C  
ANISOU  146  CB  VAL A 166    27236  31301  29489   -604    559   -611       C  
ATOM    147  CG1 VAL A 166     -68.793 -15.116  34.666  1.00201.44           C  
ANISOU  147  CG1 VAL A 166    23327  27501  25710   -573    614   -680       C  
ATOM    148  CG2 VAL A 166     -69.158 -17.582  34.347  1.00203.92           C  
ANISOU  148  CG2 VAL A 166    23768  27825  25885   -741    601   -628       C  
ATOM    149  N   MET A 167     -67.784 -13.957  32.063  1.00208.18           N  
ANISOU  149  N   MET A 167    24139  28261  26699   -344    460   -580       N  
ATOM    150  CA  MET A 167     -67.640 -12.514  32.001  1.00209.25           C  
ANISOU  150  CA  MET A 167    24205  28383  26918   -242    454   -604       C  
ATOM    151  C   MET A 167     -67.815 -11.980  30.598  1.00196.02           C  
ANISOU  151  C   MET A 167    22470  26691  25315   -153    386   -579       C  
ATOM    152  O   MET A 167     -68.507 -10.998  30.409  1.00167.22           O  
ANISOU  152  O   MET A 167    18718  23070  21746    -94    385   -624       O  
ATOM    153  CB  MET A 167     -66.270 -12.099  32.534  1.00235.11           C  
ANISOU  153  CB  MET A 167    27568  31591  30172   -206    449   -570       C  
ATOM    154  CG  MET A 167     -66.015 -12.495  33.974  1.00169.32           C  
ANISOU  154  CG  MET A 167    19300  23265  21766   -288    509   -594       C  
ATOM    155  SD  MET A 167     -67.332 -11.910  35.063  1.00319.80           S  
ANISOU  155  SD  MET A 167    38251  42407  40850   -335    598   -701       S  
ATOM    156  CE  MET A 167     -67.020 -10.146  35.134  1.00295.82           C  
ANISOU  156  CE  MET A 167    35148  39344  37906   -215    594   -730       C  
ATOM    157  N   GLY A 168     -67.172 -12.621  29.625  1.00191.36           N  
ANISOU  157  N   GLY A 168    21952  26054  24698   -141    329   -507       N  
ATOM    158  CA  GLY A 168     -67.276 -12.213  28.231  1.00199.82           C  
ANISOU  158  CA  GLY A 168    22988  27106  25828    -65    261   -476       C  
ATOM    159  C   GLY A 168     -68.726 -12.011  27.845  1.00224.78           C  
ANISOU  159  C   GLY A 168    26026  30335  29044    -67    258   -528       C  
ATOM    160  O   GLY A 168     -69.070 -11.026  27.184  1.00162.69           O  
ANISOU  160  O   GLY A 168    18087  22467  21258     15    221   -540       O  
ATOM    161  N   THR A 169     -69.567 -12.936  28.312  1.00211.86           N  
ANISOU  161  N   THR A 169    24370  28760  27365   -165    299   -560       N  
ATOM    162  CA  THR A 169     -70.995 -12.996  27.996  1.00183.25           C  
ANISOU  162  CA  THR A 169    20630  25212  23784   -189    301   -612       C  
ATOM    163  C   THR A 169     -71.853 -11.997  28.751  1.00203.91           C  
ANISOU  163  C   THR A 169    23122  27885  26468   -165    349   -699       C  
ATOM    164  O   THR A 169     -72.818 -11.446  28.212  1.00176.44           O  
ANISOU  164  O   THR A 169    19526  24446  23064   -121    325   -738       O  
ATOM    165  CB  THR A 169     -71.571 -14.352  28.380  1.00180.28           C  
ANISOU  165  CB  THR A 169    20280  24887  23331   -317    338   -623       C  
ATOM    166  OG1 THR A 169     -70.718 -15.393  27.902  1.00186.15           O  
ANISOU  166  OG1 THR A 169    21153  25574  23999   -350    305   -547       O  
ATOM    167  CG2 THR A 169     -72.952 -14.498  27.790  1.00255.93           C  
ANISOU  167  CG2 THR A 169    29745  34541  32956   -339    325   -664       C  
ATOM    168  N   LYS A 170     -71.544 -11.834  30.030  1.00169.98           N  
ANISOU  168  N   LYS A 170    18851  23592  22139   -200    419   -733       N  
ATOM    169  CA  LYS A 170     -72.143 -10.776  30.812  1.00197.52           C  
ANISOU  169  CA  LYS A 170    22238  27119  25690   -167    470   -814       C  
ATOM    170  C   LYS A 170     -71.659  -9.423  30.296  1.00197.82           C  
ANISOU  170  C   LYS A 170    22252  27102  25808    -35    421   -802       C  
ATOM    171  O   LYS A 170     -72.330  -8.418  30.490  1.00253.34           O  
ANISOU  171  O   LYS A 170    29177  34161  32916     21    436   -866       O  
ATOM    172  CB  LYS A 170     -71.774 -10.942  32.284  1.00176.63           C  
ANISOU  172  CB  LYS A 170    19650  24480  22981   -238    553   -845       C  
ATOM    173  N   LEU A 171     -70.529  -9.420  29.586  1.00186.61           N  
ANISOU  173  N   LEU A 171    20927  25603  24370     11    362   -722       N  
ATOM    174  CA  LEU A 171     -69.759  -8.202  29.328  1.00209.75           C  
ANISOU  174  CA  LEU A 171    23872  28469  27353    118    328   -703       C  
ATOM    175  C   LEU A 171     -69.625  -7.637  27.905  1.00211.14           C  
ANISOU  175  C   LEU A 171    24036  28599  27586    211    239   -657       C  
ATOM    176  O   LEU A 171     -69.673  -6.415  27.712  1.00235.31           O  
ANISOU  176  O   LEU A 171    27050  31637  30719    302    217   -677       O  
ATOM    177  CB  LEU A 171     -68.355  -8.451  29.812  1.00222.97           C  
ANISOU  177  CB  LEU A 171    25674  30082  28961    100    338   -651       C  
ATOM    178  CG  LEU A 171     -67.834  -7.425  30.770  1.00210.11           C  
ANISOU  178  CG  LEU A 171    24051  28429  27350    137    377   -682       C  
ATOM    179  CD1 LEU A 171     -66.599  -8.112  31.328  1.00141.33           C  
ANISOU  179  CD1 LEU A 171    15468  19676  18555     87    390   -632       C  
ATOM    180  CD2 LEU A 171     -67.564  -6.086  30.071  1.00160.74           C  
ANISOU  180  CD2 LEU A 171    17768  22127  21177    254    327   -674       C  
ATOM    181  N   PHE A 172     -69.354  -8.495  26.929  1.00147.19           N  
ANISOU  181  N   PHE A 172    15995  20480  19450    190    189   -593       N  
ATOM    182  CA  PHE A 172     -69.085  -8.012  25.566  1.00243.05           C  
ANISOU  182  CA  PHE A 172    28147  32569  31631    270    105   -542       C  
ATOM    183  C   PHE A 172     -70.255  -8.452  24.710  1.00229.23           C  
ANISOU  183  C   PHE A 172    26321  30867  29906    257     65   -553       C  
ATOM    184  O   PHE A 172     -70.220  -8.415  23.476  1.00199.31           O  
ANISOU  184  O   PHE A 172    22548  27047  26134    297     -7   -508       O  
ATOM    185  CB  PHE A 172     -67.753  -8.558  25.014  1.00205.84           C  
ANISOU  185  CB  PHE A 172    23564  27786  26857    265     76   -459       C  
ATOM    186  CG  PHE A 172     -66.566  -8.322  25.914  1.00221.49           C  
ANISOU  186  CG  PHE A 172    25622  29727  28805    264    116   -447       C  
ATOM    187  CD1 PHE A 172     -65.920  -7.086  25.936  1.00180.69           C  
ANISOU  187  CD1 PHE A 172    20461  24510  23683    344    103   -445       C  
ATOM    188  CD2 PHE A 172     -66.084  -9.344  26.730  1.00177.54           C  
ANISOU  188  CD2 PHE A 172    20127  24168  23161    183    161   -436       C  
ATOM    189  CE1 PHE A 172     -64.829  -6.871  26.768  1.00169.57           C  
ANISOU  189  CE1 PHE A 172    19118  23065  22242    340    137   -434       C  
ATOM    190  CE2 PHE A 172     -64.996  -9.129  27.570  1.00158.51           C  
ANISOU  190  CE2 PHE A 172    17784  21720  20720    183    190   -425       C  
ATOM    191  CZ  PHE A 172     -64.363  -7.893  27.584  1.00152.15           C  
ANISOU  191  CZ  PHE A 172    16976  20870  19961    260    179   -425       C  
ATOM    192  N   ALA A 173     -71.309  -8.843  25.411  1.00204.02           N  
ANISOU  192  N   ALA A 173    23046  27754  26715    195    115   -618       N  
ATOM    193  CA  ALA A 173     -72.427  -9.524  24.820  1.00191.94           C  
ANISOU  193  CA  ALA A 173    21449  26285  25194    153     91   -633       C  
ATOM    194  C   ALA A 173     -73.196  -8.641  23.835  1.00229.56           C  
ANISOU  194  C   ALA A 173    26117  31053  30051    242     17   -648       C  
ATOM    195  O   ALA A 173     -73.229  -8.944  22.639  1.00213.89           O  
ANISOU  195  O   ALA A 173    24157  29046  28065    256    -55   -598       O  
ATOM    196  CB  ALA A 173     -73.330 -10.058  25.914  1.00148.54           C  
ANISOU  196  CB  ALA A 173    15883  20874  19679     63    171   -706       C  
ATOM    197  N   GLN A 174     -73.784  -7.547  24.326  1.00217.57           N  
ANISOU  197  N   GLN A 174    24496  29558  28611    305     34   -717       N  
ATOM    198  CA  GLN A 174     -74.625  -6.676  23.492  1.00204.41           C  
ANISOU  198  CA  GLN A 174    22728  27898  27039    394    -37   -741       C  
ATOM    199  C   GLN A 174     -73.939  -6.405  22.154  1.00225.90           C  
ANISOU  199  C   GLN A 174    25531  30538  29762    459   -132   -659       C  
ATOM    200  O   GLN A 174     -74.586  -6.394  21.095  1.00169.77           O  
ANISOU  200  O   GLN A 174    18379  23435  22689    488   -210   -646       O  
ATOM    201  CB  GLN A 174     -74.935  -5.342  24.205  1.00154.18           C  
ANISOU  201  CB  GLN A 174    16282  21540  20759    476    -10   -812       C  
ATOM    202  CG  GLN A 174     -75.696  -5.465  25.540  1.00305.99           C  
ANISOU  202  CG  GLN A 174    35417  40851  39992    418     89   -905       C  
ATOM    203  CD  GLN A 174     -77.197  -5.161  25.464  1.00323.69           C  
ANISOU  203  CD  GLN A 174    37491  43173  42320    441     81   -989       C  
ATOM    204  OE1 GLN A 174     -77.642  -4.351  24.648  1.00317.49           O  
ANISOU  204  OE1 GLN A 174    36643  42370  41617    539      2   -994       O  
ATOM    205  NE2 GLN A 174     -77.982  -5.796  26.346  1.00283.88           N  
ANISOU  205  NE2 GLN A 174    32377  38223  37262    351    163  -1057       N  
ATOM    206  N   SER A 175     -72.611  -6.289  22.227  1.00219.84           N  
ANISOU  206  N   SER A 175    24884  29696  28947    469   -123   -603       N  
ATOM    207  CA  SER A 175     -71.784  -5.583  21.242  1.00187.27           C  
ANISOU  207  CA  SER A 175    20834  25482  24835    548   -194   -540       C  
ATOM    208  C   SER A 175     -70.837  -6.437  20.436  1.00216.70           C  
ANISOU  208  C   SER A 175    24687  29161  28487    510   -223   -454       C  
ATOM    209  O   SER A 175     -70.577  -6.084  19.273  1.00173.21           O  
ANISOU  209  O   SER A 175    19220  23599  22993    560   -298   -405       O  
ATOM    210  CB  SER A 175     -70.941  -4.561  21.972  1.00197.80           C  
ANISOU  210  CB  SER A 175    22202  26767  26185    601   -160   -549       C  
ATOM    211  OG  SER A 175     -70.862  -5.018  23.335  1.00141.29           O  
ANISOU  211  OG  SER A 175    15039  19654  18990    532    -65   -591       O  
ATOM    212  N   PHE A 176     -70.285  -7.506  21.049  1.00163.21           N  
ANISOU  212  N   PHE A 176    17979  22399  21634    424   -164   -437       N  
ATOM    213  CA  PHE A 176     -69.357  -8.488  20.374  1.00180.73           C  
ANISOU  213  CA  PHE A 176    20319  24574  23776    380   -182   -361       C  
ATOM    214  C   PHE A 176     -70.026  -9.824  20.516  1.00213.96           C  
ANISOU  214  C   PHE A 176    24517  28844  27935    283   -159   -371       C  
ATOM    215  O   PHE A 176     -69.588 -10.662  21.301  1.00227.72           O  
ANISOU  215  O   PHE A 176    26313  30597  29613    212   -102   -367       O  
ATOM    216  CB  PHE A 176     -67.892  -8.496  20.942  1.00201.63           C  
ANISOU  216  CB  PHE A 176    23072  27165  26373    376   -141   -326       C  
ATOM    217  CG  PHE A 176     -67.277  -7.113  20.977  1.00178.62           C  
ANISOU  217  CG  PHE A 176    20162  24196  23509    464   -154   -326       C  
ATOM    218  CD1 PHE A 176     -66.939  -6.433  19.715  1.00167.17           C  
ANISOU  218  CD1 PHE A 176    18746  22684  22086    533   -228   -281       C  
ATOM    219  CD2 PHE A 176     -67.117  -6.394  22.243  1.00156.75           C  
ANISOU  219  CD2 PHE A 176    17361  21435  20760    479    -95   -376       C  
ATOM    220  CE1 PHE A 176     -66.508  -5.071  19.704  1.00192.94           C  
ANISOU  220  CE1 PHE A 176    22010  25897  25399    613   -244   -285       C  
ATOM    221  CE2 PHE A 176     -66.652  -5.021  22.229  1.00156.56           C  
ANISOU  221  CE2 PHE A 176    17338  21360  20787    563   -111   -380       C  
ATOM    222  CZ  PHE A 176     -66.362  -4.364  20.952  1.00167.79           C  
ANISOU  222  CZ  PHE A 176    18793  22721  22238    630   -187   -334       C  
ATOM    223  N   PRO A 177     -71.137  -9.997  19.786  1.00222.10           N  
ANISOU  223  N   PRO A 177    25475  29917  28997    278   -207   -385       N  
ATOM    224  CA  PRO A 177     -72.000 -11.128  19.970  1.00150.38           C  
ANISOU  224  CA  PRO A 177    16355  20902  19877    184   -185   -408       C  
ATOM    225  C   PRO A 177     -71.519 -12.274  19.095  1.00240.44           C  
ANISOU  225  C   PRO A 177    27869  32277  31209    132   -216   -340       C  
ATOM    226  O   PRO A 177     -71.857 -13.433  19.386  1.00218.51           O  
ANISOU  226  O   PRO A 177    25108  29540  28374     38   -185   -345       O  
ATOM    227  CB  PRO A 177     -73.370 -10.598  19.509  1.00228.46           C  
ANISOU  227  CB  PRO A 177    26109  30846  29846    219   -231   -457       C  
ATOM    228  CG  PRO A 177     -73.158  -9.156  19.141  1.00190.16           C  
ANISOU  228  CG  PRO A 177    21232  25946  25071    336   -278   -458       C  
ATOM    229  CD  PRO A 177     -71.708  -9.087  18.787  1.00216.64           C  
ANISOU  229  CD  PRO A 177    24723  29210  28377    360   -287   -386       C  
ATOM    230  N   GLU A 178     -70.744 -11.929  18.051  1.00264.37           N  
ANISOU  230  N   GLU A 178    30973  35234  34239    190   -275   -279       N  
ATOM    231  CA  GLU A 178     -69.982 -12.880  17.233  1.00296.12           C  
ANISOU  231  CA  GLU A 178    35115  39208  38188    154   -298   -211       C  
ATOM    232  C   GLU A 178     -69.047 -13.668  18.162  1.00281.47           C  
ANISOU  232  C   GLU A 178    33346  37337  36262     99   -229   -198       C  
ATOM    233  O   GLU A 178     -68.955 -14.906  18.097  1.00185.77           O  
ANISOU  233  O   GLU A 178    21289  25221  24071     23   -216   -175       O  
ATOM    234  CB  GLU A 178     -69.190 -12.145  16.119  1.00269.75           C  
ANISOU  234  CB  GLU A 178    31837  35789  34865    233   -359   -157       C  
ATOM    235  CG  GLU A 178     -68.690 -13.054  14.977  1.00376.40           C  
ANISOU  235  CG  GLU A 178    45450  49253  48309    201   -397    -92       C  
ATOM    236  CD  GLU A 178     -68.077 -12.312  13.779  1.00325.68           C  
ANISOU  236  CD  GLU A 178    39082  42758  41902    270   -460    -44       C  
ATOM    237  OE1 GLU A 178     -67.713 -12.972  12.760  1.00196.83           O  
ANISOU  237  OE1 GLU A 178    22848  26402  25534    247   -492      5       O  
ATOM    238  OE2 GLU A 178     -67.958 -11.067  13.847  1.00296.82           O  
ANISOU  238  OE2 GLU A 178    35391  39080  38305    345   -475    -57       O  
ATOM    239  N   TRP A 179     -68.389 -12.947  19.064  1.00186.90           N  
ANISOU  239  N   TRP A 179    21370  25342  24302    135   -186   -215       N  
ATOM    240  CA  TRP A 179     -67.479 -13.579  20.006  1.00222.70           C  
ANISOU  240  CA  TRP A 179    25982  29858  28774     91   -128   -204       C  
ATOM    241  C   TRP A 179     -68.134 -13.906  21.376  1.00214.80           C  
ANISOU  241  C   TRP A 179    24929  28924  27760     24    -59   -264       C  
ATOM    242  O   TRP A 179     -68.177 -15.079  21.774  1.00142.93           O  
ANISOU  242  O   TRP A 179    15876  19839  18589    -60    -30   -259       O  
ATOM    243  CB  TRP A 179     -66.167 -12.759  20.124  1.00276.27           C  
ANISOU  243  CB  TRP A 179    32822  36575  35569    159   -124   -177       C  
ATOM    244  CG  TRP A 179     -65.667 -12.171  18.780  1.00184.36           C  
ANISOU  244  CG  TRP A 179    21217  24876  23954    228   -188   -129       C  
ATOM    245  CD1 TRP A 179     -65.726 -12.767  17.547  1.00209.14           C  
ANISOU  245  CD1 TRP A 179    24400  27994  27067    217   -238    -86       C  
ATOM    246  CD2 TRP A 179     -65.036 -10.896  18.571  1.00137.48           C  
ANISOU  246  CD2 TRP A 179    15279  18890  18064    311   -206   -121       C  
ATOM    247  NE1 TRP A 179     -65.192 -11.943  16.590  1.00155.63           N  
ANISOU  247  NE1 TRP A 179    17651  21160  20318    285   -284    -53       N  
ATOM    248  CE2 TRP A 179     -64.763 -10.788  17.186  1.00129.22           C  
ANISOU  248  CE2 TRP A 179    14279  17797  17018    343   -267    -73       C  
ATOM    249  CE3 TRP A 179     -64.684  -9.822  19.422  1.00173.31           C  
ANISOU  249  CE3 TRP A 179    19787  23419  22642    357   -177   -151       C  
ATOM    250  CZ2 TRP A 179     -64.151  -9.654  16.623  1.00169.04           C  
ANISOU  250  CZ2 TRP A 179    19343  22785  22098    416   -298    -52       C  
ATOM    251  CZ3 TRP A 179     -64.068  -8.655  18.862  1.00189.00           C  
ANISOU  251  CZ3 TRP A 179    21791  25349  24670    434   -210   -131       C  
ATOM    252  CH2 TRP A 179     -63.811  -8.604  17.471  1.00236.42           C  
ANISOU  252  CH2 TRP A 179    27846  31310  30672    460   -269    -81       C  
ATOM    253  N   PHE A 180     -68.675 -12.884  22.051  1.00210.15           N  
ANISOU  253  N   PHE A 180    24243  28368  27233     61    -35   -322       N  
ATOM    254  CA  PHE A 180     -69.152 -12.987  23.449  1.00224.57           C  
ANISOU  254  CA  PHE A 180    26024  30251  29049      5     38   -383       C  
ATOM    255  C   PHE A 180     -70.657 -12.847  23.670  1.00224.14           C  
ANISOU  255  C   PHE A 180    25839  30282  29041    -20     53   -453       C  
ATOM    256  O   PHE A 180     -71.115 -12.769  24.831  1.00158.78           O  
ANISOU  256  O   PHE A 180    17511  22054  20763    -61    120   -513       O  
ATOM    257  CB  PHE A 180     -68.464 -11.933  24.312  1.00189.96           C  
ANISOU  257  CB  PHE A 180    21639  25840  24694     61     72   -403       C  
ATOM    258  CG  PHE A 180     -66.986 -11.959  24.214  1.00165.08           C  
ANISOU  258  CG  PHE A 180    18602  22613  21507     88     61   -344       C  
ATOM    259  CD1 PHE A 180     -66.281 -13.104  24.558  1.00135.10           C  
ANISOU  259  CD1 PHE A 180    14906  18797  17628     21     82   -309       C  
ATOM    260  CD2 PHE A 180     -66.298 -10.849  23.749  1.00168.23           C  
ANISOU  260  CD2 PHE A 180    19008  22958  21954    179     28   -323       C  
ATOM    261  CE1 PHE A 180     -64.903 -13.133  24.450  1.00222.59           C  
ANISOU  261  CE1 PHE A 180    26083  29810  28681     51     70   -258       C  
ATOM    262  CE2 PHE A 180     -64.922 -10.866  23.644  1.00199.59           C  
ANISOU  262  CE2 PHE A 180    23077  26864  25894    201     21   -272       C  
ATOM    263  CZ  PHE A 180     -64.224 -12.014  23.990  1.00244.06           C  
ANISOU  263  CZ  PHE A 180    28799  32482  31450    139     42   -240       C  
ATOM    264  N   GLY A 181     -71.414 -12.808  22.574  1.00169.66           N  
ANISOU  264  N   GLY A 181    18884  23399  22180      2     -7   -448       N  
ATOM    265  CA  GLY A 181     -72.863 -12.624  22.629  1.00238.79           C  
ANISOU  265  CA  GLY A 181    27502  32236  30990    -12     -5   -514       C  
ATOM    266  C   GLY A 181     -73.535 -13.522  23.643  1.00282.09           C  
ANISOU  266  C   GLY A 181    32959  37793  36427   -125     69   -564       C  
ATOM    267  O   GLY A 181     -74.270 -13.059  24.521  1.00278.32           O  
ANISOU  267  O   GLY A 181    32383  37376  35988   -134    122   -638       O  
ATOM    268  N   THR A 182     -73.279 -14.817  23.518  1.00267.31           N  
ANISOU  268  N   THR A 182    31180  35914  34469   -213     74   -523       N  
ATOM    269  CA  THR A 182     -73.742 -15.771  24.508  1.00258.38           C  
ANISOU  269  CA  THR A 182    30056  34840  33275   -332    146   -560       C  
ATOM    270  C   THR A 182     -72.587 -16.637  24.944  1.00239.72           C  
ANISOU  270  C   THR A 182    27845  32418  30816   -381    169   -506       C  
ATOM    271  O   THR A 182     -71.485 -16.555  24.389  1.00152.92           O  
ANISOU  271  O   THR A 182    16944  21348  19810   -324    129   -443       O  
ATOM    272  CB  THR A 182     -74.861 -16.695  23.988  1.00238.97           C  
ANISOU  272  CB  THR A 182    27550  32446  30799   -415    130   -575       C  
ATOM    273  OG1 THR A 182     -74.342 -18.020  23.793  1.00272.95           O  
ANISOU  273  OG1 THR A 182    31985  36716  35004   -497    127   -518       O  
ATOM    274  CG2 THR A 182     -75.466 -16.165  22.691  1.00340.66           C  
ANISOU  274  CG2 THR A 182    40349  45332  43753   -344     46   -567       C  
ATOM    275  N   LEU A 183     -72.890 -17.493  25.915  1.00246.94           N  
ANISOU  275  N   LEU A 183    28787  33372  31664   -491    234   -535       N  
ATOM    276  CA  LEU A 183     -71.927 -18.331  26.595  1.00208.72           C  
ANISOU  276  CA  LEU A 183    24087  28486  26732   -548    264   -497       C  
ATOM    277  C   LEU A 183     -71.241 -19.337  25.668  1.00233.55           C  
ANISOU  277  C   LEU A 183    27352  31569  29816   -562    210   -419       C  
ATOM    278  O   LEU A 183     -70.028 -19.262  25.478  1.00221.85           O  
ANISOU  278  O   LEU A 183    25961  30011  28317   -507    185   -366       O  
ATOM    279  CB  LEU A 183     -72.614 -19.027  27.770  1.00205.51           C  
ANISOU  279  CB  LEU A 183    23675  28140  26266   -671    341   -551       C  
ATOM    280  CG  LEU A 183     -71.768 -19.456  28.970  1.00231.91           C  
ANISOU  280  CG  LEU A 183    27133  31448  29531   -723    392   -541       C  
ATOM    281  CD1 LEU A 183     -71.083 -20.783  28.679  1.00215.18           C  
ANISOU  281  CD1 LEU A 183    25164  29274  27318   -781    364   -474       C  
ATOM    282  CD2 LEU A 183     -70.761 -18.393  29.402  1.00226.04           C  
ANISOU  282  CD2 LEU A 183    26406  30654  28825   -627    393   -532       C  
ATOM    283  N   GLY A 184     -72.010 -20.256  25.083  1.00279.47           N  
ANISOU  283  N   GLY A 184    33166  37418  35602   -634    192   -416       N  
ATOM    284  CA  GLY A 184     -71.467 -21.265  24.152  1.00358.47           C  
ANISOU  284  CA  GLY A 184    43285  47368  45549   -652    143   -346       C  
ATOM    285  C   GLY A 184     -70.675 -20.700  22.978  1.00301.51           C  
ANISOU  285  C   GLY A 184    36095  40087  38376   -543     74   -291       C  
ATOM    286  O   GLY A 184     -70.111 -21.450  22.164  1.00226.60           O  
ANISOU  286  O   GLY A 184    26706  30548  28844   -547     35   -234       O  
ATOM    287  N   ALA A 185     -70.641 -19.371  22.902  1.00186.43           N  
ANISOU  287  N   ALA A 185    21435  25514  23885   -447     63   -311       N  
ATOM    288  CA  ALA A 185     -69.908 -18.649  21.877  1.00280.89           C  
ANISOU  288  CA  ALA A 185    33416  37416  35891   -342      4   -266       C  
ATOM    289  C   ALA A 185     -68.668 -17.995  22.481  1.00219.70           C  
ANISOU  289  C   ALA A 185    25718  29610  28148   -279     24   -250       C  
ATOM    290  O   ALA A 185     -67.632 -17.934  21.820  1.00167.90           O  
ANISOU  290  O   ALA A 185    19233  22981  21579   -226     -9   -196       O  
ATOM    291  CB  ALA A 185     -70.799 -17.614  21.207  1.00301.10           C  
ANISOU  291  CB  ALA A 185    35849  40012  38543   -278    -35   -296       C  
ATOM    292  N   SER A 186     -68.783 -17.495  23.717  1.00197.63           N  
ANISOU  292  N   SER A 186    22879  26844  25365   -288     81   -299       N  
ATOM    293  CA  SER A 186     -67.608 -17.122  24.513  1.00164.28           C  
ANISOU  293  CA  SER A 186    18718  22571  21126   -255    108   -286       C  
ATOM    294  C   SER A 186     -66.799 -18.368  24.749  1.00183.82           C  
ANISOU  294  C   SER A 186    21325  25005  23511   -315    115   -242       C  
ATOM    295  O   SER A 186     -65.600 -18.376  24.519  1.00196.83           O  
ANISOU  295  O   SER A 186    23054  26587  25143   -269     94   -195       O  
ATOM    296  CB  SER A 186     -67.964 -16.515  25.873  1.00114.44           C  
ANISOU  296  CB  SER A 186    12346  16303  14832   -273    172   -349       C  
ATOM    297  OG  SER A 186     -68.027 -15.103  25.784  1.00178.89           O  
ANISOU  297  OG  SER A 186    20424  24465  23080   -181    163   -375       O  
ATOM    298  N   MET A 187     -67.462 -19.427  25.200  1.00140.33           N  
ANISOU  298  N   MET A 187    15838  19535  17942   -418    143   -259       N  
ATOM    299  CA  MET A 187     -66.801 -20.719  25.379  1.00235.52           C  
ANISOU  299  CA  MET A 187    28028  31550  29908   -480    144   -217       C  
ATOM    300  C   MET A 187     -65.897 -20.994  24.195  1.00213.08           C  
ANISOU  300  C   MET A 187    25259  28638  27060   -423     87   -153       C  
ATOM    301  O   MET A 187     -64.685 -21.191  24.348  1.00175.71           O  
ANISOU  301  O   MET A 187    20617  23843  22300   -392     80   -115       O  
ATOM    302  CB  MET A 187     -67.831 -21.841  25.490  1.00269.56           C  
ANISOU  302  CB  MET A 187    32347  35910  34163   -595    162   -236       C  
ATOM    303  CG  MET A 187     -68.548 -21.891  26.825  1.00256.20           C  
ANISOU  303  CG  MET A 187    30617  34279  32447   -677    230   -297       C  
ATOM    304  SD  MET A 187     -67.456 -22.301  28.198  1.00274.55           S  
ANISOU  304  SD  MET A 187    33065  36553  34696   -710    267   -284       S  
ATOM    305  CE  MET A 187     -67.534 -24.088  28.170  1.00338.59           C  
ANISOU  305  CE  MET A 187    41310  44643  42694   -827    262   -251       C  
ATOM    306  N   TYR A 188     -66.514 -20.972  23.015  1.00201.94           N  
ANISOU  306  N   TYR A 188    23805  27241  25679   -408     46   -143       N  
ATOM    307  CA  TYR A 188     -65.833 -21.169  21.750  1.00188.93           C  
ANISOU  307  CA  TYR A 188    22219  25536  24030   -358     -6    -87       C  
ATOM    308  C   TYR A 188     -64.731 -20.146  21.527  1.00162.06           C  
ANISOU  308  C   TYR A 188    18820  22080  20673   -255    -22    -65       C  
ATOM    309  O   TYR A 188     -63.606 -20.512  21.213  1.00205.46           O  
ANISOU  309  O   TYR A 188    24408  27515  26141   -228    -36    -21       O  
ATOM    310  CB  TYR A 188     -66.820 -21.108  20.571  1.00244.82           C  
ANISOU  310  CB  TYR A 188    29235  32645  31140   -358    -49    -88       C  
ATOM    311  CG  TYR A 188     -66.108 -21.288  19.252  1.00218.03           C  
ANISOU  311  CG  TYR A 188    25911  29189  27739   -311   -102    -31       C  
ATOM    312  CD1 TYR A 188     -65.730 -22.559  18.821  1.00167.24           C  
ANISOU  312  CD1 TYR A 188    19589  22719  21234   -359   -113      6       C  
ATOM    313  CD2 TYR A 188     -65.761 -20.195  18.460  1.00178.00           C  
ANISOU  313  CD2 TYR A 188    20805  24092  22732   -219   -137    -16       C  
ATOM    314  CE1 TYR A 188     -65.051 -22.746  17.630  1.00166.92           C  
ANISOU  314  CE1 TYR A 188    19616  22621  21184   -318   -153     54       C  
ATOM    315  CE2 TYR A 188     -65.071 -20.370  17.268  1.00191.60           C  
ANISOU  315  CE2 TYR A 188    22598  25757  24442   -182   -178     33       C  
ATOM    316  CZ  TYR A 188     -64.721 -21.649  16.856  1.00225.25           C  
ANISOU  316  CZ  TYR A 188    26964  29987  28632   -232   -184     67       C  
ATOM    317  OH  TYR A 188     -64.042 -21.856  15.675  1.00175.04           O  
ANISOU  317  OH  TYR A 188    20678  23571  22259   -199   -219    112       O  
ATOM    318  N   THR A 189     -65.090 -18.868  21.621  1.00171.17           N  
ANISOU  318  N   THR A 189    19874  23260  21901   -198    -20    -96       N  
ATOM    319  CA  THR A 189     -64.147 -17.763  21.519  1.00167.25           C  
ANISOU  319  CA  THR A 189    19374  22720  21453   -107    -30    -83       C  
ATOM    320  C   THR A 189     -63.041 -18.015  22.523  1.00169.01           C  
ANISOU  320  C   THR A 189    19670  22908  21636   -113      2    -73       C  
ATOM    321  O   THR A 189     -61.851 -18.011  22.182  1.00146.22           O  
ANISOU  321  O   THR A 189    16851  19963  18741    -69    -13    -34       O  
ATOM    322  CB  THR A 189     -64.854 -16.426  21.841  1.00201.61           C  
ANISOU  322  CB  THR A 189    23607  27112  25883    -61    -22   -132       C  
ATOM    323  OG1 THR A 189     -65.889 -16.193  20.877  1.00247.16           O  
ANISOU  323  OG1 THR A 189    29305  32911  31692    -50    -63   -140       O  
ATOM    324  CG2 THR A 189     -63.875 -15.232  21.870  1.00110.35           C  
ANISOU  324  CG2 THR A 189    12050  15508  14371     26    -28   -121       C  
ATOM    325  N   LEU A 190     -63.448 -18.283  23.759  1.00118.93           N  
ANISOU  325  N   LEU A 190    13316  16604  15267   -173     48   -111       N  
ATOM    326  CA  LEU A 190     -62.487 -18.385  24.850  1.00196.08           C  
ANISOU  326  CA  LEU A 190    23149  26346  25004   -179     77   -108       C  
ATOM    327  C   LEU A 190     -61.423 -19.440  24.579  1.00199.69           C  
ANISOU  327  C   LEU A 190    23728  26744  25402   -188     56    -56       C  
ATOM    328  O   LEU A 190     -60.227 -19.220  24.826  1.00136.51           O  
ANISOU  328  O   LEU A 190    15774  18695  17399   -143     52    -34       O  
ATOM    329  CB  LEU A 190     -63.198 -18.543  26.207  1.00116.71           C  
ANISOU  329  CB  LEU A 190    13071  16345  14925   -253    131   -159       C  
ATOM    330  CG  LEU A 190     -63.493 -17.126  26.740  1.00127.04           C  
ANISOU  330  CG  LEU A 190    14281  17683  16304   -204    155   -206       C  
ATOM    331  CD1 LEU A 190     -63.156 -16.978  28.217  1.00114.54           C  
ANISOU  331  CD1 LEU A 190    12721  16105  14693   -235    204   -235       C  
ATOM    332  CD2 LEU A 190     -62.772 -16.020  25.955  1.00109.86           C  
ANISOU  332  CD2 LEU A 190    12082  15465  14193    -99    119   -182       C  
ATOM    333  N   PHE A 191     -61.879 -20.554  24.014  1.00159.74           N  
ANISOU  333  N   PHE A 191    18712  21686  20295   -243     41    -39       N  
ATOM    334  CA  PHE A 191     -61.019 -21.634  23.566  1.00165.26           C  
ANISOU  334  CA  PHE A 191    19524  22328  20938   -250     18      8       C  
ATOM    335  C   PHE A 191     -60.146 -21.178  22.416  1.00168.38           C  
ANISOU  335  C   PHE A 191    19931  22675  21371   -166    -17     45       C  
ATOM    336  O   PHE A 191     -58.996 -21.601  22.283  1.00171.02           O  
ANISOU  336  O   PHE A 191    20343  22953  21681   -138    -29     77       O  
ATOM    337  CB  PHE A 191     -61.895 -22.801  23.132  1.00169.49           C  
ANISOU  337  CB  PHE A 191    20092  22882  21421   -330     10     12       C  
ATOM    338  CG  PHE A 191     -61.175 -23.881  22.363  1.00176.05           C  
ANISOU  338  CG  PHE A 191    21033  23653  22202   -331    -19     60       C  
ATOM    339  CD1 PHE A 191     -60.296 -24.752  22.993  1.00154.29           C  
ANISOU  339  CD1 PHE A 191    18382  20850  19388   -349    -16     80       C  
ATOM    340  CD2 PHE A 191     -61.425 -24.063  21.011  1.00243.53           C  
ANISOU  340  CD2 PHE A 191    29580  32190  30758   -316    -53     83       C  
ATOM    341  CE1 PHE A 191     -59.664 -25.763  22.282  1.00139.77           C  
ANISOU  341  CE1 PHE A 191    16644  18955  17506   -346    -43    119       C  
ATOM    342  CE2 PHE A 191     -60.794 -25.076  20.298  1.00267.10           C  
ANISOU  342  CE2 PHE A 191    32669  35120  33696   -319    -77    123       C  
ATOM    343  CZ  PHE A 191     -59.913 -25.930  20.936  1.00186.86           C  
ANISOU  343  CZ  PHE A 191    22607  24910  23479   -331    -70    140       C  
ATOM    344  N   GLN A 192     -60.706 -20.314  21.582  1.00143.89           N  
ANISOU  344  N   GLN A 192    16751  19594  18327   -127    -35     38       N  
ATOM    345  CA  GLN A 192     -59.977 -19.785  20.443  1.00200.08           C  
ANISOU  345  CA  GLN A 192    23877  26666  25477    -53    -67     70       C  
ATOM    346  C   GLN A 192     -58.889 -18.881  20.998  1.00199.56           C  
ANISOU  346  C   GLN A 192    23806  26572  25443      7    -54     70       C  
ATOM    347  O   GLN A 192     -57.715 -18.941  20.582  1.00157.48           O  
ANISOU  347  O   GLN A 192    18532  21191  20110     49    -65    101       O  
ATOM    348  CB  GLN A 192     -60.920 -18.991  19.539  1.00170.11           C  
ANISOU  348  CB  GLN A 192    19999  22900  21734    -29    -93     60       C  
ATOM    349  CG  GLN A 192     -60.406 -18.777  18.130  1.00150.89           C  
ANISOU  349  CG  GLN A 192    17596  20420  19314     20   -132     99       C  
ATOM    350  CD  GLN A 192     -60.742 -17.394  17.595  1.00231.02           C  
ANISOU  350  CD  GLN A 192    27666  30577  29534     81   -155     89       C  
ATOM    351  OE1 GLN A 192     -60.213 -16.383  18.076  1.00147.48           O  
ANISOU  351  OE1 GLN A 192    17056  19986  18993    131   -142     77       O  
ATOM    352  NE2 GLN A 192     -61.617 -17.340  16.590  1.00217.33           N  
ANISOU  352  NE2 GLN A 192    25903  28858  27813     77   -194     94       N  
ATOM    353  N   VAL A 193     -59.293 -18.077  21.978  1.00164.24           N  
ANISOU  353  N   VAL A 193    19265  22134  21001      8    -28     31       N  
ATOM    354  CA  VAL A 193     -58.406 -17.106  22.593  1.00190.17           C  
ANISOU  354  CA  VAL A 193    22537  25400  24320     61    -14     24       C  
ATOM    355  C   VAL A 193     -57.337 -17.825  23.404  1.00144.91           C  
ANISOU  355  C   VAL A 193    16885  19634  18538     45     -2     39       C  
ATOM    356  O   VAL A 193     -56.180 -17.425  23.389  1.00113.10           O  
ANISOU  356  O   VAL A 193    12880  15566  14525     94     -8     57       O  
ATOM    357  CB  VAL A 193     -59.196 -16.072  23.422  1.00156.63           C  
ANISOU  357  CB  VAL A 193    18197  21198  20115     64     11    -24       C  
ATOM    358  CG1 VAL A 193     -58.270 -15.279  24.330  1.00143.10           C  
ANISOU  358  CG1 VAL A 193    16486  19464  18420     99     31    -34       C  
ATOM    359  CG2 VAL A 193     -59.947 -15.129  22.484  1.00145.74           C  
ANISOU  359  CG2 VAL A 193    16740  19834  18799    108    -13    -34       C  
ATOM    360  N   MET A 194     -57.742 -18.895  24.083  1.00177.94           N  
ANISOU  360  N   MET A 194    21112  23833  22663    -26     11     32       N  
ATOM    361  CA  MET A 194     -56.831 -19.790  24.796  1.00164.85           C  
ANISOU  361  CA  MET A 194    19544  22139  20950    -47     13     50       C  
ATOM    362  C   MET A 194     -55.670 -20.157  23.870  1.00163.91           C  
ANISOU  362  C   MET A 194    19486  21962  20828      2    -16     93       C  
ATOM    363  O   MET A 194     -54.500 -20.023  24.239  1.00178.63           O  
ANISOU  363  O   MET A 194    21383  23791  22697     40    -21    104       O  
ATOM    364  CB  MET A 194     -57.609 -21.042  25.259  1.00159.20           C  
ANISOU  364  CB  MET A 194    18879  21443  20165   -138     23     43       C  
ATOM    365  CG  MET A 194     -56.905 -22.002  26.209  1.00125.54           C  
ANISOU  365  CG  MET A 194    14715  17147  15837   -174     24     56       C  
ATOM    366  SD  MET A 194     -55.908 -23.264  25.379  1.00315.6



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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: October 18th, 2018.