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ID        	=	 2308141327281442689
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     -15.076 -44.014  38.259  1.00 27.16
ATOM      2  CA  ASN A  22     -13.884 -44.771  38.620  1.00 31.92
ATOM      3  CB  ASN A  22     -14.298 -45.932  39.540  1.00 35.53
ATOM      4  CG  ASN A  22     -15.128 -46.984  38.820  1.00 37.72
ATOM      5  OD1 ASN A  22     -14.607 -47.769  38.042  1.00 41.73
ATOM      6  ND2 ASN A  22     -16.498 -46.967  38.993  1.00 47.45
ATOM      7  C   ASN A  22     -13.099 -45.237  37.377  1.00 38.19
ATOM      8  O   ASN A  22     -13.549 -45.070  36.242  1.00 32.65
ATOM      9  N   THR A  23     -11.851 -45.854  37.598  1.00 35.89
ATOM     10  CA  THR A  23     -10.963 -46.317  36.520  1.00 37.53
ATOM     11  CB  THR A  23      -9.634 -46.820  37.103  1.00 33.93
ATOM     12  OG1 THR A  23      -8.999 -45.739  37.758  1.00 37.93
ATOM     13  CG2 THR A  23      -8.655 -47.337  36.048  1.00 33.82
ATOM     14  C   THR A  23     -11.603 -47.363  35.608  1.00 39.45
ATOM     15  O   THR A  23     -11.440 -47.280  34.389  1.00 36.58
ATOM     16  N   CYS A  24     -12.398 -48.370  36.180  1.00 38.91
ATOM     17  CA  CYS A  24     -13.061 -49.380  35.360  1.00 37.50
ATOM     18  CB  CYS A  24     -13.653 -50.474  36.259  1.00 40.95
ATOM     19  SG  CYS A  24     -12.332 -51.274  37.214  1.00 71.26
ATOM     20  C   CYS A  24     -14.144 -48.736  34.488  1.00 42.76
ATOM     21  O   CYS A  24     -14.206 -49.001  33.290  1.00 39.15
ATOM     22  N   PHE A  25     -14.993 -47.788  35.091  1.00 37.34
ATOM     23  CA  PHE A  25     -16.056 -47.096  34.367  1.00 38.17
ATOM     24  CB  PHE A  25     -16.846 -46.204  35.336  1.00 40.62
ATOM     25  CG  PHE A  25     -17.866 -45.316  34.648  1.00 43.24
ATOM     26  CD1 PHE A  25     -19.039 -45.878  34.109  1.00 39.98
ATOM     27  CE1 PHE A  25     -19.959 -45.067  33.421  1.00 36.33
ATOM     28  CZ  PHE A  25     -19.710 -43.691  33.271  1.00 32.60
ATOM     29  CE2 PHE A  25     -18.542 -43.126  33.811  1.00 34.73
ATOM     30  CD2 PHE A  25     -17.619 -43.936  34.497  1.00 44.60
ATOM     31  C   PHE A  25     -15.512 -46.290  33.183  1.00 42.74
ATOM     32  O   PHE A  25     -15.947 -46.500  32.054  1.00 38.77
ATOM     33  N   ARG A  26     -14.476 -45.358  33.412  1.00 35.97
ATOM     34  CA  ARG A  26     -13.910 -44.544  32.324  1.00 41.27
ATOM     35  CB  ARG A  26     -13.043 -43.402  32.885  1.00 41.53
ATOM     36  CG  ARG A  26     -11.749 -43.855  33.580  1.00 37.82
ATOM     37  CD  ARG A  26     -11.126 -42.705  34.388  1.00 30.31
ATOM     38  NE  ARG A  26     -10.019 -43.172  35.246  1.00 34.53
ATOM     39  CZ  ARG A  26      -8.735 -43.288  34.931  1.00 36.03
ATOM     40  NH1 ARG A  26      -8.254 -42.885  33.777  1.00 36.20
ATOM     41  NH2 ARG A  26      -7.906 -43.833  35.789  1.00 39.49
ATOM     42  C   ARG A  26     -13.194 -45.388  31.263  1.00 36.04
ATOM     43  O   ARG A  26     -13.163 -45.003  30.096  1.00 31.44
ATOM     44  N   THR A  27     -12.648 -46.623  31.659  1.00 36.48
ATOM     45  CA  THR A  27     -12.072 -47.575  30.701  1.00 37.72
ATOM     46  CB  THR A  27     -11.296 -48.690  31.424  1.00 39.44
ATOM     47  OG1 THR A  27     -10.299 -48.118  32.241  1.00 43.14
ATOM     48  CG2 THR A  27     -10.582 -49.630  30.453  1.00 46.60
ATOM     49  C   THR A  27     -13.155 -48.163  29.793  1.00 34.86
ATOM     50  O   THR A  27     -12.968 -48.210  28.581  1.00 36.58
ATOM     51  N   GLN A  28     -14.374 -48.573  30.370  1.00 34.90
ATOM     52  CA  GLN A  28     -15.501 -49.077  29.579  1.00 36.07
ATOM     53  CB  GLN A  28     -16.560 -49.701  30.506  1.00 40.04
ATOM     54  CG  GLN A  28     -16.094 -51.005  31.178  1.00 47.06
ATOM     55  CD  GLN A  28     -15.842 -52.111  30.158  1.00 48.50
ATOM     56  OE1 GLN A  28     -16.754 -52.820  29.765  1.00 45.46
ATOM     57  NE2 GLN A  28     -14.552 -52.256  29.673  1.00 45.98
ATOM     58  C   GLN A  28     -16.128 -47.996  28.690  1.00 38.14
ATOM     59  O   GLN A  28     -16.553 -48.298  27.578  1.00 30.41
ATOM     60  N   VAL A  29     -16.135 -46.661  29.141  1.00 33.31
ATOM     61  CA  VAL A  29     -16.553 -45.544  28.283  1.00 29.48
ATOM     62  CB  VAL A  29     -16.614 -44.225  29.083  1.00 30.18
ATOM     63  CG1 VAL A  29     -16.825 -42.992  28.193  1.00 26.23
ATOM     64  CG2 VAL A  29     -17.766 -44.264  30.098  1.00 31.73
ATOM     65  C   VAL A  29     -15.630 -45.436  27.065  1.00 28.50
ATOM     66  O   VAL A  29     -16.118 -45.323  25.942  1.00 31.96
ATOM     67  N   LYS A  30     -14.234 -45.534  27.259  1.00 32.06
ATOM     68  CA  LYS A  30     -13.300 -45.549  26.127  1.00 28.85
ATOM     69  CB  LYS A  30     -11.843 -45.458  26.602  1.00 27.56
ATOM     70  CG  LYS A  30     -11.459 -44.013  26.951  1.00 30.38
ATOM     71  CD  LYS A  30      -9.937 -43.873  27.073  1.00 37.35
ATOM     72  CE  LYS A  30      -9.556 -42.395  27.201  1.00 45.14
ATOM     73  NZ  LYS A  30      -8.093 -42.202  27.062  1.00 46.73
ATOM     74  C   LYS A  30     -13.486 -46.762  25.214  1.00 38.78
ATOM     75  O   LYS A  30     -13.377 -46.610  24.002  1.00 35.61
ATOM     76  N   GLU A  31     -13.811 -48.000  25.787  1.00 34.56
ATOM     77  CA  GLU A  31     -14.071 -49.196  24.984  1.00 34.31
ATOM     78  CB  GLU A  31     -14.232 -50.410  25.916  1.00 41.58
ATOM     79  CG  GLU A  31     -14.137 -51.736  25.150  1.00 42.87
ATOM     80  CD  GLU A  31     -14.385 -52.946  26.060  1.00 61.52
ATOM     81  OE1 GLU A  31     -13.724 -53.029  27.122  1.00 52.52
ATOM     82  OE2 GLU A  31     -15.237 -53.781  25.686  1.00 56.48
ATOM     83  C   GLU A  31     -15.297 -49.002  24.079  1.00 33.66
ATOM     84  O   GLU A  31     -15.238 -49.295  22.889  1.00 37.64
ATOM     85  N   ALA A  32     -16.444 -48.401  24.631  1.00 31.05
ATOM     86  CA  ALA A  32     -17.630 -48.090  23.839  1.00 32.46
ATOM     87  CB  ALA A  32     -18.731 -47.589  24.781  1.00 27.81
ATOM     88  C   ALA A  32     -17.333 -47.069  22.728  1.00 35.01
ATOM     89  O   ALA A  32     -17.804 -47.229  21.603  1.00 31.67
ATOM     90  N   ILE A  33     -16.481 -45.986  23.032  1.00 28.12
ATOM     91  CA  ILE A  33     -16.074 -44.986  22.038  1.00 37.28
ATOM     92  CB  ILE A  33     -15.312 -43.826  22.725  1.00 32.15
ATOM     93  CG1 ILE A  33     -16.295 -42.992  23.582  1.00 30.23
ATOM     94  CD1 ILE A  33     -15.604 -42.064  24.590  1.00 26.62
ATOM     95  CG2 ILE A  33     -14.605 -42.911  21.705  1.00 26.76
ATOM     96  C   ILE A  33     -15.265 -45.638  20.906  1.00 29.24
ATOM     97  O   ILE A  33     -15.511 -45.331  19.742  1.00 30.15
ATOM     98  N   ASP A  34     -14.292 -46.604  21.231  1.00 32.20
ATOM     99  CA  ASP A  34     -13.546 -47.346  20.213  1.00 38.87
ATOM    100  CB  ASP A  34     -12.499 -48.259  20.871  1.00 37.00
ATOM    101  CG  ASP A  34     -11.757 -49.096  19.824  1.00 45.45
ATOM    102  OD1 ASP A  34     -10.963 -48.516  19.054  1.00 40.91
ATOM    103  OD2 ASP A  34     -12.013 -50.318  19.729  1.00 45.64
ATOM    104  C   ASP A  34     -14.491 -48.154  19.319  1.00 38.23
ATOM    105  O   ASP A  34     -14.409 -48.051  18.099  1.00 37.68
ATOM    106  N   ILE A  35     -15.472 -48.947  19.940  1.00 35.11
ATOM    107  CA  ILE A  35     -16.414 -49.791  19.199  1.00 37.61
ATOM    108  CB  ILE A  35     -17.280 -50.603  20.194  1.00 34.76
ATOM    109  CG1 ILE A  35     -16.410 -51.674  20.898  1.00 40.89
ATOM    110  CD1 ILE A  35     -17.047 -52.247  22.172  1.00 39.74
ATOM    111  CG2 ILE A  35     -18.477 -51.282  19.499  1.00 33.46
ATOM    112  C   ILE A  35     -17.254 -48.958  18.219  1.00 38.85
ATOM    113  O   ILE A  35     -17.427 -49.364  17.071  1.00 34.35
ATOM    114  N   VAL A  36     -17.782 -47.726  18.652  1.00 29.05
ATOM    115  CA  VAL A  36     -18.616 -46.880  17.786  1.00 33.41
ATOM    116  CB  VAL A  36     -19.351 -45.806  18.618  1.00 28.58
ATOM    117  CG1 VAL A  36     -20.075 -44.770  17.744  1.00 28.71
ATOM    118  CG2 VAL A  36     -20.410 -46.463  19.516  1.00 32.49
ATOM    119  C   VAL A  36     -17.788 -46.249  16.663  1.00 33.24
ATOM    120  O   VAL A  36     -18.147 -46.365  15.491  1.00 31.96
ATOM    121  N   CYS A  37     -16.607 -45.568  17.004  1.00 31.68
ATOM    122  CA  CYS A  37     -15.784 -44.885  16.006  1.00 36.11
ATOM    123  CB  CYS A  37     -14.669 -44.111  16.718  1.00 31.95
ATOM    124  SG  CYS A  37     -15.387 -42.686  17.584  1.00 32.31
ATOM    125  C   CYS A  37     -15.206 -45.859  14.974  1.00 35.53
ATOM    126  O   CYS A  37     -15.103 -45.525  13.794  1.00 30.86
ATOM    127  N   ARG A  38     -14.840 -47.146  15.407  1.00 31.57
ATOM    128  CA  ARG A  38     -14.333 -48.162  14.493  1.00 33.97
ATOM    129  CB  ARG A  38     -13.418 -49.145  15.219  1.00 37.22
ATOM    130  CG  ARG A  38     -12.093 -48.463  15.613  1.00 44.43
ATOM    131  CD  ARG A  38     -10.954 -49.467  15.807  1.00 49.91
ATOM    132  NE  ARG A  38     -11.284 -50.434  16.858  1.00 55.26
ATOM    133  CZ  ARG A  38     -11.787 -51.649  16.706  1.00 65.76
ATOM    134  NH1 ARG A  38     -11.964 -52.222  15.531  1.00 62.80
ATOM    135  NH2 ARG A  38     -12.149 -52.306  17.779  1.00 70.02
ATOM    136  C   ARG A  38     -15.436 -48.881  13.730  1.00 37.46
ATOM    137  O   ARG A  38     -15.201 -49.245  12.586  1.00 41.55
ATOM    138  N   PHE A  39     -16.725 -49.002  14.279  1.00 31.53
ATOM    139  CA  PHE A  39     -17.853 -49.397  13.436  1.00 31.72
ATOM    140  CB  PHE A  39     -19.150 -49.488  14.253  1.00 30.85
ATOM    141  CG  PHE A  39     -20.388 -49.617  13.383  1.00 37.01
ATOM    142  CD1 PHE A  39     -20.706 -50.851  12.783  1.00 39.82
ATOM    143  CE1 PHE A  39     -21.802 -50.948  11.908  1.00 35.05
ATOM    144  CZ  PHE A  39     -22.584 -49.812  11.630  1.00 39.52
ATOM    145  CE2 PHE A  39     -22.271 -48.580  12.230  1.00 36.28
ATOM    146  CD2 PHE A  39     -21.174 -48.482  13.105  1.00 34.49
ATOM    147  C   PHE A  39     -17.997 -48.427  12.256  1.00 36.89
ATOM    148  O   PHE A  39     -18.094 -48.868  11.112  1.00 36.12
ATOM    149  N   LEU A  40     -17.931 -47.043  12.519  1.00 29.02
ATOM    150  CA  LEU A  40     -18.011 -46.040  11.456  1.00 32.06
ATOM    151  CB  LEU A  40     -18.056 -44.626  12.065  1.00 30.11
ATOM    152  CG  LEU A  40     -19.320 -44.328  12.899  1.00 33.79
ATOM    153  CD1 LEU A  40     -19.189 -42.955  13.561  1.00 27.43
ATOM    154  CD2 LEU A  40     -20.599 -44.340  12.053  1.00 29.92
ATOM    155  C   LEU A  40     -16.879 -46.180  10.424  1.00 35.08
ATOM    156  O   LEU A  40     -17.139 -46.063   9.228  1.00 35.74
ATOM    157  N   LYS A  41     -15.582 -46.484  10.890  1.00 35.57
ATOM    158  CA  LYS A  41     -14.400 -46.591  10.017  1.00 39.08
ATOM    159  CB  LYS A  41     -13.134 -46.411  10.869  1.00 30.45
ATOM    160  CG  LYS A  41     -12.932 -44.961  11.334  1.00 31.70
ATOM    161  CD  LYS A  41     -11.900 -44.819  12.465  1.00 34.47
ATOM    162  CE  LYS A  41     -10.494 -45.308  12.084  1.00 31.28
ATOM    163  NZ  LYS A  41     -10.250 -46.713  12.492  1.00 28.17
ATOM    164  C   LYS A  41     -14.284 -47.909   9.238  1.00 40.81
ATOM    165  O   LYS A  41     -13.669 -47.917   8.177  1.00 41.75
ATOM    166  N   GLU A  42     -14.849 -49.077   9.779  1.00 36.47
ATOM    167  CA  GLU A  42     -14.475 -50.428   9.328  1.00 39.36
ATOM    168  CB  GLU A  42     -13.605 -51.126  10.402  1.00 36.07
ATOM    169  CG  GLU A  42     -12.215 -50.489  10.608  1.00 33.61
ATOM    170  CD  GLU A  42     -11.869 -50.220  12.082  1.00 42.98
ATOM    171  OE1 GLU A  42     -11.627 -49.031  12.404  1.00 44.67
ATOM    172  OE2 GLU A  42     -11.797 -51.182  12.884  1.00 46.77
ATOM    173  C   GLU A  42     -15.677 -51.311   8.949  1.00 39.64
ATOM    174  O   GLU A  42     -15.472 -52.401   8.416  1.00 39.49
ATOM    175  N   ARG A  43     -16.996 -50.847   9.184  1.00 38.97
ATOM    176  CA  ARG A  43     -18.176 -51.651   8.816  1.00 37.68
ATOM    177  CB  ARG A  43     -18.510 -52.586   9.998  1.00 35.52
ATOM    178  CG  ARG A  43     -19.656 -53.585   9.755  1.00 36.68
ATOM    179  CD  ARG A  43     -19.433 -54.471   8.519  1.00 42.04
ATOM    180  NE  ARG A  43     -20.571 -55.382   8.294  1.00 48.20
ATOM    181  CZ  ARG A  43     -20.727 -56.607   8.781  1.00 45.13
ATOM    182  NH1 ARG A  43     -19.842 -57.160   9.580  1.00 42.40
ATOM    183  NH2 ARG A  43     -21.794 -57.306   8.470  1.00 43.95
ATOM    184  C   ARG A  43     -19.411 -50.862   8.354  1.00 42.90
ATOM    185  O   ARG A  43     -20.225 -51.417   7.624  1.00 41.77
ATOM    186  N   CYS A  44     -19.576 -49.528   8.756  1.00 38.08
ATOM    187  CA  CYS A  44     -20.755 -48.725   8.439  1.00 36.90
ATOM    188  CB  CYS A  44     -20.634 -47.388   9.175  1.00 39.84
ATOM    189  SG  CYS A  44     -22.156 -46.423   8.971  1.00 41.65
ATOM    190  C   CYS A  44     -20.931 -48.539   6.927  1.00 44.32
ATOM    191  O   CYS A  44     -22.016 -48.757   6.390  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.