HEADER    CYTOKINE                                07-NOV-96   XXXX              
TITLE     RECOMBINANT HUMAN INTERFERON-ALPHA 2B                                 
KEYWDS    INTERFERON, CYTOKINE, ANTI-VIRAL, IMMUNOMODULATOR, 4 HELIX BUNDLE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.R.WALTER                                                            
JRNL        AUTH   R.RADHAKRISHNAN, L.J.WALTER, A.HRUZA, P.REICHERT,            
JRNL        AUTH 2 P.P.TROTTA, T.L.NAGABHUSHAN, M.R.WALTER                      
JRNL        TITL   ZINC MEDIATED DIMER OF HUMAN INTERFERON-ALPHA 2B REVEALED BY 
JRNL        TITL 2 X-RAY CRYSTALLOGRAPHY.                                       
JRNL        REF    STRUCTURE                     V.   4  1453 1996              
JRNL        REFN   ASTM STRUE6  UK ISSN 0969-2126                               
JRNL        PMID   8994971                                                      
JRNL        DOI    10.1016/S0969-2126(96)00152-9                                
SEQRES   1 A  165  CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG          
SEQRES   2 A  165  THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU          
SEQRES   3 A  165  PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO          
SEQRES   4 A  165  GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR          
SEQRES   5 A  165  ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN          
SEQRES   6 A  165  LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU          
SEQRES   7 A  165  THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN          
SEQRES   8 A  165  LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY          
SEQRES   9 A  165  VAL THR GLU THR PRO LEU MET ASN GLU ASP SER ILE LEU          
SEQRES  10 A  165  ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU          
SEQRES  11 A  165  LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL          
SEQRES  12 A  165  ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN          
SEQRES  13 A  165  LEU GLN GLU SER LEU ARG SER LYS GLU                          
SEQRES   1 B  165  CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG          
SEQRES   2 B  165  THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU          
SEQRES   3 B  165  PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO          
SEQRES   4 B  165  GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR          
SEQRES   5 B  165  ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN          
SEQRES   6 B  165  LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU          
SEQRES   7 B  165  THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN          
SEQRES   8 B  165  LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY          
SEQRES   9 B  165  VAL THR GLU THR PRO LEU MET ASN GLU ASP SER ILE LEU          
SEQRES  10 B  165  ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU          
SEQRES  11 B  165  LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL          
SEQRES  12 B  165  ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN          
SEQRES  13 B  165  LEU GLN GLU SER LEU ARG SER LYS GLU                          
SEQRES   1 C  165  CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG          
SEQRES   2 C  165  THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU          
SEQRES   3 C  165  PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO          
SEQRES   4 C  165  GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR          
SEQRES   5 C  165  ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN          
SEQRES   6 C  165  LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU          
SEQRES   7 C  165  THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN          
SEQRES   8 C  165  LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY          
SEQRES   9 C  165  VAL THR GLU THR PRO LEU MET ASN GLU ASP SER ILE LEU          
SEQRES  10 C  165  ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU          
SEQRES  11 C  165  LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL          
SEQRES  12 C  165  ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN          
SEQRES  13 C  165  LEU GLN GLU SER LEU ARG SER LYS GLU                          
SEQRES   1 D  165  CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG          
SEQRES   2 D  165  THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU          
SEQRES   3 D  165  PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO          
SEQRES   4 D  165  GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR          
SEQRES   5 D  165  ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN          
SEQRES   6 D  165  LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU          
SEQRES   7 D  165  THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN          
SEQRES   8 D  165  LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY          
SEQRES   9 D  165  VAL THR GLU THR PRO LEU MET ASN GLU ASP SER ILE LEU          
SEQRES  10 D  165  ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU          
SEQRES  11 D  165  LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL          
SEQRES  12 D  165  ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN          
SEQRES  13 D  165  LEU GLN GLU SER LEU ARG SER LYS GLU                          
SEQRES   1 E  165  CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG          
SEQRES   2 E  165  THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU          
SEQRES   3 E  165  PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO          
SEQRES   4 E  165  GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR          
SEQRES   5 E  165  ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN          
SEQRES   6 E  165  LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU          
SEQRES   7 E  165  THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN          
SEQRES   8 E  165  LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY          
SEQRES   9 E  165  VAL THR GLU THR PRO LEU MET ASN GLU ASP SER ILE LEU          
SEQRES  10 E  165  ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU          
SEQRES  11 E  165  LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL          
SEQRES  12 E  165  ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN          
SEQRES  13 E  165  LEU GLN GLU SER LEU ARG SER LYS GLU                          
SEQRES   1 F  165  CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG          
SEQRES   2 F  165  THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER LEU          
SEQRES   3 F  165  PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO          
SEQRES   4 F  165  GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR          
SEQRES   5 F  165  ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN          
SEQRES   6 F  165  LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU          
SEQRES   7 F  165  THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN          
SEQRES   8 F  165  LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY          
SEQRES   9 F  165  VAL THR GLU THR PRO LEU MET ASN GLU ASP SER ILE LEU          
SEQRES  10 F  165  ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU          
SEQRES  11 F  165  LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL          
SEQRES  12 F  165  ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN          
SEQRES  13 F  165  LEU GLN GLU SER LEU ARG SER LYS GLU                          
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    4(ZN 2+)                                                     
CRYST1   62.400   75.500  148.200  90.00  90.80  90.00 P 1 21 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016026  0.000000  0.000224        0.00000                         
SCALE2      0.000000  0.013245  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006748        0.00000                         
MTRIX1   1 -0.998000 -0.045000 -0.036000       86.80400    1                    
MTRIX2   1  0.042000 -0.128000 -0.991000      124.76500    1                    
MTRIX3   1  0.040000 -0.991000  0.129000      109.34000    1                    
MTRIX1   2 -0.984000 -0.105000 -0.142000      120.79500    1                    
MTRIX2   2  0.058000 -0.952000  0.302000       60.64400    1                    
MTRIX3   2 -0.167000  0.289000  0.943000      -39.30100    1                    
MTRIX1   3  0.997000  0.067000  0.025000       19.05000    1                    
MTRIX2   3 -0.017000 -0.126000  0.992000      -25.90300    1                    
MTRIX3   3  0.070000 -0.990000 -0.125000       90.21100    1                    
MTRIX1   4  0.991000  0.119000  0.055000       -7.07800    1                    
MTRIX2   4 -0.119000  0.993000  0.002000       -5.13700    1                    
MTRIX3   4 -0.055000 -0.009000  0.998000      -72.18800    1                    
MTRIX1   5 -0.971000 -0.114000 -0.209000      104.10800    1                    
MTRIX2   5  0.224000 -0.142000 -0.964000      105.49100    1                    
MTRIX3   5  0.080000 -0.983000  0.164000       29.86300    1                    
MODEL        1                                                                  
ATOM      1  CA  SER D   8      68.305  45.761  12.147  1.00 47.18           C  
ATOM      2  CA  LEU D   9      68.432  49.334  10.987  1.00 29.39           C  
ATOM      3  CA  GLY D  10      65.183  50.075  12.795  1.00 37.89           C  
ATOM      4  CA  SER D  11      66.882  49.268  16.113  1.00 50.64           C  
ATOM      5  CA  ARG D  12      69.654  51.745  15.338  1.00 33.37           C  
ATOM      6  CA  ARG D  13      67.121  54.428  14.446  1.00 45.05           C  
ATOM      7  CA  THR D  14      65.214  53.630  17.658  1.00 41.67           C  
ATOM      8  CA  LEU D  15      68.289  54.074  19.874  1.00 30.06           C  
ATOM      9  CA  MET D  16      69.104  57.199  17.916  1.00 26.15           C  
ATOM     10  CA  LEU D  17      65.678  58.791  18.621  1.00 26.53           C  
ATOM     11  CA  LEU D  18      66.021  57.931  22.327  1.00 35.75           C  
ATOM     12  CA  ALA D  19      69.452  59.561  22.301  1.00 25.04           C  
ATOM     13  CA  GLN D  20      67.924  62.673  20.722  1.00 29.78           C  
ATOM     14  CA  MET D  21      65.099  62.706  23.204  1.00 29.96           C  
ATOM     15  CA  ARG D  22      67.543  63.488  26.065  1.00 27.73           C  
ATOM     16  CA  ARG D  23      66.675  66.747  27.820  1.00 28.70           C  
ATOM     17  CA  ILE D  24      68.591  66.923  31.095  1.00 21.23           C  
ATOM     18  CA  SER D  25      71.500  65.051  32.576  1.00 52.25           C  
ATOM     19  CA  LEU D  26      71.265  61.610  34.150  1.00 77.67           C  
ATOM     20  CA  PHE D  27      74.137  62.849  36.294  1.00 70.56           C  
ATOM     21  CA  SER D  28      72.123  65.817  37.526  1.00 60.65           C  
ATOM     22  CA  CYS D  29      69.690  63.179  38.877  1.00 77.18           C  
ATOM     23  CA  LEU D  30      71.948  60.745  40.761  1.00 80.01           C  
ATOM     24  CA  LYS D  31      69.548  60.890  43.736  1.00 63.93           C  
ATOM     25  CA  ASP D  32      67.071  59.119  41.409  1.00 71.15           C  
ATOM     26  CA  ARG D  33      69.549  56.491  40.243  1.00 60.26           C  
ATOM     27  CA  HIS D  34      67.817  53.053  40.242  1.00 39.70           C  
ATOM     28  CA  ASP D  35      68.345  49.386  39.235  1.00  8.33           C  
ATOM     29  CA  PHE D  36      65.212  47.933  37.599  1.00 16.41           C  
ATOM     30  CA  GLY D  37      66.538  44.347  37.439  1.00 13.66           C  
ATOM     31  CA  PHE D  38      66.183  43.896  33.637  1.00 22.45           C  
ATOM     32  CA  PRO D  39      66.185  40.176  32.730  1.00 28.12           C  
ATOM     33  CA  GLN D  40      68.981  40.194  30.213  1.00 34.23           C  
ATOM     34  CA  GLU D  41      69.301  36.412  30.559  1.00 28.21           C  
ATOM     35  CA  GLU D  42      66.152  36.089  28.484  1.00 20.01           C  
ATOM     36  CA  PHE D  43      67.828  37.305  25.311  1.00 18.20           C  
ATOM     37  CA  GLY D  44      70.590  34.734  25.298  1.00 47.83           C  
ATOM     38  CA  ALA D  50      65.118  32.099  17.855  1.00 39.13           C  
ATOM     39  CA  GLU D  51      62.723  31.446  20.773  1.00 62.82           C  
ATOM     40  CA  THR D  52      63.857  34.864  22.006  1.00 44.87           C  
ATOM     41  CA  ILE D  53      61.891  36.534  19.254  1.00 32.32           C  
ATOM     42  CA  PRO D  54      58.789  36.456  21.472  1.00 39.08           C  
ATOM     43  CA  VAL D  55      60.588  38.234  24.306  1.00 17.61           C  
ATOM     44  CA  LEU D  56      62.187  40.784  21.997  1.00 25.58           C  
ATOM     45  CA  HIS D  57      58.888  41.436  20.293  1.00 18.79           C  
ATOM     46  CA  GLU D  58      57.383  41.829  23.794  1.00 29.61           C  
ATOM     47  CA  MET D  59      60.233  44.195  24.691  1.00 23.96           C  
ATOM     48  CA  ILE D  60      59.305  46.371  21.770  1.00 26.61           C  
ATOM     49  CA  GLN D  61      55.534  46.296  22.410  1.00 27.46           C  
ATOM     50  CA  GLN D  62      56.366  47.381  25.911  1.00 27.14           C  
ATOM     51  CA  ILE D  63      58.711  50.173  24.804  1.00 32.69           C  
ATOM     52  CA  PHE D  64      55.859  51.535  22.663  1.00 39.12           C  
ATOM     53  CA  ASN D  65      53.450  51.212  25.589  1.00 18.24           C  
ATOM     54  CA  LEU D  66      55.826  53.173  27.924  1.00 10.00           C  
ATOM     55  CA  PHE D  67      56.352  56.094  25.554  1.00 28.73           C  
ATOM     56  CA  SER D  68      52.863  56.423  24.140  1.00 25.68           C  
ATOM     57  CA  THR D  69      51.139  57.592  27.287  1.00 27.45           C  
ATOM     58  CA  LYS D  70      49.955  61.102  28.083  1.00 48.66           C  
ATOM     59  CA  ASP D  71      52.838  61.347  30.560  1.00 24.93           C  
ATOM     60  CA  SER D  72      55.191  60.488  27.755  1.00 23.75           C  
ATOM     61  CA  SER D  73      53.658  63.100  25.606  1.00 43.87           C  
ATOM     62  CA  ALA D  74      54.082  65.708  28.304  1.00 41.26           C  
ATOM     63  CA  ALA D  75      57.739  64.707  28.662  1.00 34.13           C  
ATOM     64  CA  TRP D  76      59.300  64.022  25.282  1.00 29.58           C  
ATOM     65  CA  ASP D  77      59.385  65.867  22.008  1.00 28.40           C  
ATOM     66  CA  GLU D  78      56.331  65.152  19.811  1.00 28.12           C  
ATOM     67  CA  THR D  79      58.276  64.961  16.562  1.00 51.60           C  
ATOM     68  CA  LEU D  80      60.874  62.645  18.097  1.00 38.52           C  
ATOM     69  CA  LEU D  81      58.157  60.509  19.690  1.00 25.79           C  
ATOM     70  CA  ASP D  82      56.158  60.241  16.448  1.00 40.71           C  
ATOM     71  CA  LYS D  83      59.296  59.154  14.604  1.00 53.46           C  
ATOM     72  CA  PHE D  84      60.053  56.787  17.484  1.00 35.58           C  
ATOM     73  CA  TYR D  85      56.745  54.966  17.309  1.00 35.37           C  
ATOM     74  CA  THR D  86      57.121  54.290  13.606  1.00 29.14           C  
ATOM     75  CA  GLU D  87      60.353  52.490  14.333  1.00 25.05           C  
ATOM     76  CA  LEU D  88      58.530  50.399  16.940  1.00 53.32           C  
ATOM     77  CA  TYR D  89      55.670  49.407  14.630  1.00 31.42           C  
ATOM     78  CA  GLN D  90      58.113  48.459  11.881  1.00 47.00           C  
ATOM     79  CA  GLN D  91      60.106  46.174  14.150  1.00 28.90           C  
ATOM     80  CA  LEU D  92      56.944  44.686  15.603  1.00  5.00           C  
ATOM     81  CA  ASN D  93      55.971  43.920  12.020  1.00 28.28           C  
ATOM     82  CA  ASP D  94      59.266  42.283  11.122  1.00 36.27           C  
ATOM     83  CA  LEU D  95      59.417  40.017  14.179  1.00 21.30           C  
ATOM     84  CA  GLU D  96      55.904  38.990  13.248  1.00 22.70           C  
ATOM     85  CA  ASN D 112      57.703  31.303  26.798  1.00 54.56           C  
ATOM     86  CA  GLU D 113      54.989  32.951  28.942  1.00 27.98           C  
ATOM     87  CA  ASP D 114      57.469  33.188  31.875  1.00 31.03           C  
ATOM     88  CA  SER D 115      60.072  35.058  29.899  1.00 19.13           C  
ATOM     89  CA  ILE D 116      57.378  37.249  28.265  1.00 28.57           C  
ATOM     90  CA  LEU D 117      56.025  37.906  31.782  1.00 20.97           C  
ATOM     91  CA  ALA D 118      59.603  38.592  32.881  1.00 22.40           C  
ATOM     92  CA  VAL D 119      59.803  41.377  30.351  1.00 32.70           C  
ATOM     93  CA  ARG D 120      56.443  42.856  31.432  1.00 22.90           C  
ATOM     94  CA  LYS D 121      57.181  42.885  35.112  1.00 18.89           C  
ATOM     95  CA  TYR D 122      60.362  44.698  34.187  1.00 21.15           C  
ATOM     96  CA  PHE D 123      58.413  47.478  32.611  1.00 25.37           C  
ATOM     97  CA  GLN D 124      55.905  47.288  35.457  1.00 12.13           C  
ATOM     98  CA  ARG D 125      58.732  48.293  37.769  1.00 17.46           C  
ATOM     99  CA  ILE D 126      59.696  51.009  35.349  1.00 32.04           C  
ATOM    100  CA  THR D 127      56.332  52.702  35.268  1.00 24.75           C  
ATOM    101  CA  LEU D 128      55.714  52.325  39.032  1.00 19.33           C  
ATOM    102  CA  TYR D 129      59.080  53.939  39.604  1.00 34.99           C  
ATOM    103  CA  LEU D 130      57.847  56.779  37.332  1.00 31.33           C  
ATOM    104  CA  LYS D 131      54.438  57.006  39.065  1.00 26.27           C  
ATOM    105  CA  GLU D 132      56.188  57.040  42.402  1.00 29.82           C  
ATOM    106  CA  LYS D 133      58.420  59.900  41.247  1.00 28.29           C  
ATOM    107  CA  LYS D 134      55.524  61.961  39.974  1.00 43.60           C  
ATOM    108  CA  TYR D 135      57.100  61.785  36.476  1.00 26.96           C  
ATOM    109  CA  SER D 136      59.803  64.327  37.416  1.00 20.83           C  
ATOM    110  CA  PRO D 137      62.202  65.288  34.603  1.00 41.66           C  
ATOM    111  CA  CYS D 138      64.929  63.394  36.403  1.00 28.34           C  
ATOM    112  CA  ALA D 139      62.879  60.193  36.883  1.00 30.09           C  
ATOM    113  CA  TRP D 140      61.981  60.380  33.236  1.00 22.72           C  
ATOM    114  CA  GLU D 141      65.651  60.664  32.285  1.00 30.38           C  
ATOM    115  CA  VAL D 142      66.617  57.683  34.426  1.00 28.53           C  
ATOM    116  CA  VAL D 143      63.861  55.834  32.579  1.00 26.46           C  
ATOM    117  CA  ARG D 144      65.131  57.031  29.166  1.00 53.88           C  
ATOM    118  CA  ALA D 145      68.729  55.992  29.903  1.00 34.63           C  
ATOM    119  CA  GLU D 146      67.512  52.677  31.261  1.00 29.16           C  
ATOM    120  CA  ILE D 147      65.563  51.900  28.065  1.00 27.40           C  
ATOM    121  CA  MET D 148      68.613  52.664  25.969  1.00 44.24           C  
ATOM    122  CA  ARG D 149      70.783  50.457  28.181  1.00 28.76           C  
ATOM    123  CA  SER D 150      68.326  47.533  28.072  1.00 34.70           C  
ATOM    124  CA  PHE D 151      67.357  48.077  24.454  1.00 20.60           C  
ATOM    125  CA  SER D 152      70.949  47.984  23.318  1.00 44.74           C  
ATOM    126  CA  LEU D 153      71.587  44.883  25.452  1.00 25.69           C  
ATOM    127  CA  SER D 154      68.556  42.949  24.249  1.00 54.96           C  
ATOM    128  CA  THR D 155      69.194  43.778  20.574  1.00 36.59           C  
ATOM    129  CA  ASN D 156      72.923  42.976  20.532  1.00 51.65           C  
ATOM    130  CA  LEU D 157      72.287  39.828  22.529  1.00 40.84           C  
ATOM    131  CA  GLN D 158      69.137  38.501  20.974  1.00 53.45           C  
TER     132      GLN D 158                                                      
ENDMDL                                                                          
MASTER        0    0    0    0    0    0    0   21  791    6    0   78          
END                                                                             
