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ID        	=	 2308141335261444624
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 3
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0

ATOM      1  N   ASN A  22     -15.422 -44.350  38.175  1.00 27.16
ATOM      2  CA  ASN A  22     -14.064 -44.730  38.539  1.00 31.92
ATOM      3  CB  ASN A  22     -14.139 -45.805  39.646  1.00 35.53
ATOM      4  CG  ASN A  22     -14.381 -47.222  39.132  1.00 37.72
ATOM      5  OD1 ASN A  22     -14.884 -47.429  38.036  1.00 41.73
ATOM      6  ND2 ASN A  22     -13.623 -48.204  39.741  1.00 47.45
ATOM      7  C   ASN A  22     -13.217 -45.157  37.317  1.00 38.19
ATOM      8  O   ASN A  22     -13.612 -44.965  36.167  1.00 32.65
ATOM      9  N   THR A  23     -11.969 -45.767  37.573  1.00 35.89
ATOM     10  CA  THR A  23     -11.071 -46.285  36.528  1.00 37.53
ATOM     11  CB  THR A  23      -9.794 -46.856  37.164  1.00 33.93
ATOM     12  OG1 THR A  23      -9.108 -45.798  37.806  1.00 37.93
ATOM     13  CG2 THR A  23      -8.817 -47.472  36.160  1.00 33.82
ATOM     14  C   THR A  23     -11.734 -47.306  35.604  1.00 39.45
ATOM     15  O   THR A  23     -11.570 -47.211  34.387  1.00 36.58
ATOM     16  N   ASP A  24     -12.535 -48.309  36.169  1.00 38.91
ATOM     17  CA  ASP A  24     -13.203 -49.322  35.353  1.00 37.50
ATOM     18  C   ASP A  24     -14.272 -48.683  34.462  1.00 42.76
ATOM     19  O   ASP A  24     -14.304 -48.931  33.258  1.00 39.15
ATOM     20  CB  ASP A  24     -13.818 -50.395  36.260  1.00 30.00
ATOM     21  CG  ASP A  24     -12.770 -50.973  37.211  1.00 30.00
ATOM     22  OD1 ASP A  24     -12.046 -51.896  36.786  1.00 30.00
ATOM     23  OD2 ASP A  24     -12.678 -50.425  38.335  1.00 30.00
ATOM     24  N   PHE A  25     -15.139 -47.743  35.055  1.00 37.34
ATOM     25  CA  PHE A  25     -16.187 -47.048  34.312  1.00 38.17
ATOM     26  CB  PHE A  25     -16.980 -46.144  35.265  1.00 40.62
ATOM     27  CG  PHE A  25     -17.980 -45.240  34.566  1.00 43.24
ATOM     28  CD1 PHE A  25     -19.115 -45.791  33.941  1.00 39.98
ATOM     29  CE1 PHE A  25     -20.018 -44.958  33.256  1.00 36.33
ATOM     30  CZ  PHE A  25     -19.792 -43.572  33.196  1.00 32.60
ATOM     31  CE2 PHE A  25     -18.659 -43.018  33.820  1.00 34.73
ATOM     32  CD2 PHE A  25     -17.754 -43.850  34.502  1.00 44.60
ATOM     33  C   PHE A  25     -15.621 -46.246  33.136  1.00 42.74
ATOM     34  O   PHE A  25     -16.045 -46.451  32.002  1.00 38.77
ATOM     35  N   ARG A  26     -14.585 -45.317  33.378  1.00 35.97
ATOM     36  CA  ARG A  26     -13.999 -44.510  32.297  1.00 41.27
ATOM     37  CB  ARG A  26     -13.124 -43.377  32.865  1.00 41.53
ATOM     38  CG  ARG A  26     -11.829 -43.843  33.550  1.00 37.82
ATOM     39  CD  ARG A  26     -11.192 -42.700  34.356  1.00 30.31
ATOM     40  NE  ARG A  26     -10.100 -43.182  35.225  1.00 34.53
ATOM     41  CZ  ARG A  26      -8.836 -43.416  34.892  1.00 36.03
ATOM     42  NH1 ARG A  26      -8.357 -43.107  33.710  1.00 36.20
ATOM     43  NH2 ARG A  26      -8.027 -43.983  35.755  1.00 39.49
ATOM     44  C   ARG A  26     -13.273 -45.360  31.248  1.00 36.04
ATOM     45  O   ARG A  26     -13.214 -44.972  30.083  1.00 31.44
ATOM     46  N   THR A  27     -12.744 -46.599  31.653  1.00 36.48
ATOM     47  CA  THR A  27     -12.148 -47.548  30.706  1.00 37.72
ATOM     48  CB  THR A  27     -11.374 -48.653  31.446  1.00 39.44
ATOM     49  OG1 THR A  27     -10.391 -48.066  32.270  1.00 43.14
ATOM     50  CG2 THR A  27     -10.640 -49.596  30.492  1.00 46.60
ATOM     51  C   THR A  27     -13.217 -48.145  29.787  1.00 34.86
ATOM     52  O   THR A  27     -13.012 -48.205  28.579  1.00 36.58
ATOM     53  N   GLN A  28     -14.447 -48.540  30.350  1.00 34.90
ATOM     54  CA  GLN A  28     -15.569 -49.040  29.551  1.00 36.07
ATOM     55  CB  GLN A  28     -16.636 -49.655  30.474  1.00 40.04
ATOM     56  CG  GLN A  28     -16.177 -50.963  31.142  1.00 47.06
ATOM     57  CD  GLN A  28     -15.936 -52.059  30.109  1.00 48.50
ATOM     58  OE1 GLN A  28     -16.863 -52.718  29.667  1.00 45.46
ATOM     59  NE2 GLN A  28     -14.639 -52.245  29.658  1.00 45.98
ATOM     60  C   GLN A  28     -16.187 -47.958  28.658  1.00 38.14
ATOM     61  O   GLN A  28     -16.608 -48.257  27.544  1.00 30.41
ATOM     62  N   VAL A  29     -16.189 -46.623  29.108  1.00 33.31
ATOM     63  CA  VAL A  29     -16.593 -45.505  28.247  1.00 29.48
ATOM     64  CB  VAL A  29     -16.662 -44.184  29.045  1.00 30.18
ATOM     65  CG1 VAL A  29     -16.860 -42.956  28.144  1.00 26.23
ATOM     66  CG2 VAL A  29     -17.829 -44.212  30.043  1.00 31.73
ATOM     67  C   VAL A  29     -15.652 -45.400  27.043  1.00 28.50
ATOM     68  O   VAL A  29     -16.124 -45.275  25.914  1.00 31.96
ATOM     69  N   LYS A  30     -14.258 -45.516  27.252  1.00 32.06
ATOM     70  CA  LYS A  30     -13.314 -45.537  26.128  1.00 28.85
ATOM     71  CB  LYS A  30     -11.860 -45.457  26.615  1.00 27.56
ATOM     72  CG  LYS A  30     -11.475 -44.014  26.970  1.00 30.38
ATOM     73  CD  LYS A  30      -9.957 -43.888  27.135  1.00 37.35
ATOM     74  CE  LYS A  30      -9.578 -42.414  27.305  1.00 45.14
ATOM     75  NZ  LYS A  30      -8.112 -42.219  27.205  1.00 46.73
ATOM     76  C   LYS A  30     -13.502 -46.748  25.213  1.00 38.78
ATOM     77  O   LYS A  30     -13.376 -46.598  24.002  1.00 35.61
ATOM     78  N   GLU A  31     -13.846 -47.983  25.782  1.00 34.56
ATOM     79  CA  GLU A  31     -14.113 -49.175  24.973  1.00 34.31
ATOM     80  CB  GLU A  31     -14.298 -50.392  25.897  1.00 41.58
ATOM     81  CG  GLU A  31     -14.206 -51.716  25.125  1.00 42.87
ATOM     82  CD  GLU A  31     -14.474 -52.928  26.027  1.00 61.52
ATOM     83  OE1 GLU A  31     -13.824 -53.021  27.095  1.00 52.52
ATOM     84  OE2 GLU A  31     -15.326 -53.755  25.637  1.00 56.48
ATOM     85  C   GLU A  31     -15.330 -48.965  24.060  1.00 33.66
ATOM     86  O   GLU A  31     -15.267 -49.261  22.870  1.00 37.64
ATOM     87  N   ALA A  32     -16.472 -48.346  24.603  1.00 31.05
ATOM     88  CA  ALA A  32     -17.648 -48.021  23.803  1.00 32.46
ATOM     89  CB  ALA A  32     -18.749 -47.506  24.736  1.00 27.81
ATOM     90  C   ALA A  32     -17.332 -47.003  22.695  1.00 35.01
ATOM     91  O   ALA A  32     -17.793 -47.161  21.565  1.00 31.67
ATOM     92  N   ILE A  33     -16.476 -45.925  23.007  1.00 28.12
ATOM     93  CA  ILE A  33     -16.044 -44.934  22.013  1.00 37.28
ATOM     94  CB  ILE A  33     -15.264 -43.786  22.701  1.00 32.15
ATOM     95  CG1 ILE A  33     -16.236 -42.928  23.547  1.00 30.23
ATOM     96  CD1 ILE A  33     -15.538 -42.002  24.552  1.00 26.62
ATOM     97  CG2 ILE A  33     -14.544 -42.885  21.677  1.00 26.76
ATOM     98  C   ILE A  33     -15.245 -45.602  20.886  1.00 29.24
ATOM     99  O   ILE A  33     -15.485 -45.298  19.719  1.00 30.15
ATOM    100  N   ASP A  34     -14.285 -46.580  21.216  1.00 32.20
ATOM    101  CA  ASP A  34     -13.550 -47.333  20.199  1.00 38.87
ATOM    102  CB  ASP A  34     -12.517 -48.259  20.861  1.00 37.00
ATOM    103  CG  ASP A  34     -11.787 -49.105  19.813  1.00 45.45
ATOM    104  OD1 ASP A  34     -10.993 -48.531  19.039  1.00 40.91
ATOM    105  OD2 ASP A  34     -12.055 -50.325  19.721  1.00 45.64
ATOM    106  C   ASP A  34     -14.504 -48.130  19.304  1.00 38.23
ATOM    107  O   ASP A  34     -14.417 -48.033  18.085  1.00 37.68
ATOM    108  N   ILE A  35     -15.497 -48.909  19.926  1.00 35.11
ATOM    109  CA  ILE A  35     -16.447 -49.745  19.186  1.00 37.61
ATOM    110  CB  ILE A  35     -17.322 -50.543  20.184  1.00 34.76
ATOM    111  CG1 ILE A  35     -16.461 -51.624  20.884  1.00 40.89
ATOM    112  CD1 ILE A  35     -17.104 -52.200  22.153  1.00 39.74
ATOM    113  CG2 ILE A  35     -18.531 -51.206  19.493  1.00 33.46
ATOM    114  C   ILE A  35     -17.274 -48.909  18.198  1.00 38.85
ATOM    115  O   ILE A  35     -17.441 -49.315  17.050  1.00 34.35
ATOM    116  N   VAL A  36     -17.798 -47.674  18.627  1.00 29.05
ATOM    117  CA  VAL A  36     -18.613 -46.815  17.755  1.00 33.41
ATOM    118  CB  VAL A  36     -19.317 -45.721  18.586  1.00 28.58
ATOM    119  CG1 VAL A  36     -20.017 -44.669  17.710  1.00 28.71
ATOM    120  CG2 VAL A  36     -20.389 -46.346  19.492  1.00 32.49
ATOM    121  C   VAL A  36     -17.770 -46.208  16.630  1.00 33.24
ATOM    122  O   VAL A  36     -18.126 -46.327  15.458  1.00 31.96
ATOM    123  N   CYS A  37     -16.579 -45.543  16.972  1.00 31.68
ATOM    124  CA  CYS A  37     -15.746 -44.875  15.974  1.00 36.11
ATOM    125  CB  CYS A  37     -14.619 -44.121  16.687  1.00 31.95
ATOM    126  SG  CYS A  37     -15.324 -42.687  17.549  1.00 32.31
ATOM    127  C   CYS A  37     -15.189 -45.861  14.941  1.00 35.53
ATOM    128  O   CYS A  37     -15.105 -45.539  13.756  1.00 30.86
ATOM    129  N   ARG A  38     -14.820 -47.143  15.382  1.00 31.57
ATOM    130  CA  ARG A  38     -14.322 -48.169  14.473  1.00 33.97
ATOM    131  CB  ARG A  38     -13.409 -49.152  15.202  1.00 37.22
ATOM    132  CG  ARG A  38     -12.088 -48.468  15.597  1.00 44.43
ATOM    133  CD  ARG A  38     -10.954 -49.474  15.808  1.00 49.91
ATOM    134  NE  ARG A  38     -11.298 -50.440  16.854  1.00 55.26
ATOM    135  CZ  ARG A  38     -11.791 -51.660  16.702  1.00 65.76
ATOM    136  NH1 ARG A  38     -11.964 -52.234  15.528  1.00 62.80
ATOM    137  NH2 ARG A  38     -12.146 -52.321  17.776  1.00 70.02
ATOM    138  C   ARG A  38     -15.427 -48.888  13.715  1.00 37.46
ATOM    139  O   ARG A  38     -15.189 -49.264  12.575  1.00 41.55
ATOM    140  N   PHE A  39     -16.717 -48.998  14.261  1.00 31.53
ATOM    141  CA  PHE A  39     -17.846 -49.397  13.419  1.00 31.72
ATOM    142  CB  PHE A  39     -19.148 -49.468  14.231  1.00 30.85
ATOM    143  CG  PHE A  39     -20.383 -49.625  13.361  1.00 37.01
ATOM    144  CD1 PHE A  39     -20.707 -50.878  12.806  1.00 39.82
ATOM    145  CE1 PHE A  39     -21.803 -51.002  11.933  1.00 35.05
ATOM    146  CZ  PHE A  39     -22.580 -49.875  11.614  1.00 39.52
ATOM    147  CE2 PHE A  39     -22.264 -48.623  12.172  1.00 36.28
ATOM    148  CD2 PHE A  39     -21.166 -48.498  13.042  1.00 34.49
ATOM    149  C   PHE A  39     -17.981 -48.436  12.231  1.00 36.89
ATOM    150  O   PHE A  39     -18.068 -48.885  11.090  1.00 36.12
ATOM    151  N   LEU A  40     -17.923 -47.051  12.489  1.00 29.02
ATOM    152  CA  LEU A  40     -17.998 -46.050  11.424  1.00 32.06
ATOM    153  CB  LEU A  40     -18.047 -44.635  12.031  1.00 30.11
ATOM    154  CG  LEU A  40     -19.319 -44.333  12.852  1.00 33.79
ATOM    155  CD1 LEU A  40     -19.174 -42.976  13.545  1.00 27.43
ATOM    156  CD2 LEU A  40     -20.583 -44.311  11.983  1.00 29.92
ATOM    157  C   LEU A  40     -16.859 -46.193  10.398  1.00 35.08
ATOM    158  O   LEU A  40     -17.110 -46.068   9.202  1.00 35.74
ATOM    159  N   LYS A  41     -15.567 -46.508  10.870  1.00 35.57
ATOM    160  CA  LYS A  41     -14.381 -46.614  10.004  1.00 39.08
ATOM    161  CB  LYS A  41     -13.119 -46.419  10.858  1.00 30.45
ATOM    162  CG  LYS A  41     -12.932 -44.965  11.318  1.00 31.70
ATOM    163  CD  LYS A  41     -11.899 -44.806  12.445  1.00 34.47
ATOM    164  CE  LYS A  41     -10.499 -45.312  12.065  1.00 31.28
ATOM    165  NZ  LYS A  41     -10.265 -46.715  12.483  1.00 28.17
ATOM    166  C   LYS A  41     -14.253 -47.936   9.232  1.00 40.81
ATOM    167  O   LYS A  41     -13.622 -47.947   8.180  1.00 41.75
ATOM    168  N   GLU A  42     -14.830 -49.101   9.766  1.00 36.47
ATOM    169  CA  GLU A  42     -14.457 -50.453   9.319  1.00 39.36
ATOM    170  CB  GLU A  42     -13.587 -51.144  10.397  1.00 36.07
ATOM    171  CG  GLU A  42     -12.196 -50.510  10.605  1.00 33.61
ATOM    172  CD  GLU A  42     -11.853 -50.239  12.079  1.00 42.98
ATOM    173  OE1 GLU A  42     -11.613 -49.050  12.400  1.00 44.67
ATOM    174  OE2 GLU A  42     -11.780 -51.201  12.882  1.00 46.77
ATOM    175  C   GLU A  42     -15.660 -51.339   8.946  1.00 39.64
ATOM    176  O   GLU A  42     -15.455 -52.429   8.412  1.00 39.49
ATOM    177  N   ARG A  43     -16.980 -50.880   9.188  1.00 38.97
ATOM    178  CA  ARG A  43     -18.161 -51.695   8.844  1.00 37.68
ATOM    179  CB  ARG A  43     -18.485 -52.603  10.049  1.00 35.52
ATOM    180  CG  ARG A  43     -19.615 -53.626   9.831  1.00 36.68
ATOM    181  CD  ARG A  43     -19.382 -54.534   8.612  1.00 42.04
ATOM    182  NE  ARG A  43     -20.511 -55.459   8.399  1.00 48.20
ATOM    183  CZ  ARG A  43     -20.653 -56.684   8.890  1.00 45.13
ATOM    184  NH1 ARG A  43     -19.756 -57.230   9.680  1.00 42.40
ATOM    185  NH2 ARG A  43     -21.718 -57.391   8.591  1.00 43.95
ATOM    186  C   ARG A  43     -19.401 -50.918   8.374  1.00 42.90
ATOM    187  O   ARG A  43     -20.222 -51.490   7.664  1.00 41.77
ATOM    188  N   CYS A  44     -19.563 -49.576   8.749  1.00 38.08
ATOM    189  CA  CYS A  44     -20.740 -48.771   8.430  1.00 36.90
ATOM    190  CB  CYS A  44     -20.599 -47.426   9.150  1.00 39.84
ATOM    191  SG  CYS A  44     -22.109 -46.440   8.959  1.00 41.65
ATOM    192  C   CYS A  44     -20.927 -48.600   6.917  1.00 44.32
ATOM    193  O   CYS A  44     -22.019 -48.812   6.392  1.00 45.99
END

• K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
• K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.