[Bioperl-guts-l] bioperl-live/t/data 1BPT.pdb, NONE, 1.1 pdb1bpt.ent, 1.1, NONE

Brian Osborne bosborne at dev.open-bio.org
Thu Sep 14 17:34:18 EDT 2006


Update of /home/repository/bioperl/bioperl-live/t/data
In directory dev.open-bio.org:/tmp/cvs-serv28090

Added Files:
	1BPT.pdb 
Removed Files:
	pdb1bpt.ent 
Log Message:
Rename PDB file

--- pdb1bpt.ent DELETED ---

--- NEW FILE: 1BPT.pdb ---
HEADER    PROTEINASE INHIBITOR (TRYPSIN)          11-DEC-91   1BPT      1BPT   2
COMPND    BOVINE PANCREATIC TRYPSIN INHIBITOR (/BPTI$) MUTANT (TYR 23   1BPT   3
COMPND   2 REPLACED BY ALA) (/Y23A$)                                    1BPT   4
SOURCE    BOVINE (BOS $TAURUS) PANCREAS                                 1BPT   5
AUTHOR    D.HOUSSET,A.WLODAWER,F.TAO,J.FUCHS,C.WOODWARD                 1BPT   6
REVDAT   1   15-JAN-93 1BPT    0                                        1BPT   7
JRNL        AUTH   A.T.DANISHEFSKY,D.HOUSSET,K.-S.KIM,F.TAO,J.FUCHS,    1BPT   8
JRNL        AUTH 2 C.WOODWARD,A.WLODAWER                                1BPT   9
JRNL        TITL   CREVICE-FORMING MUTANTS OF BPTI: CRYSTAL STRUCTURES  1BPT  10
JRNL        TITL 2 OF F22A, Y23A, N43G, AND F45A                        1BPT  11
JRNL        REF    TO BE PUBLISHED                                      1BPT  12
JRNL        REFN                                                   353  1BPT  13
REMARK   1                                                              1BPT  14
REMARK   1 REFERENCE 1                                                  1BPT  15
REMARK   1  AUTH   K.S.KIM,F.TAO,J.FUCHS,A.T.DANISHEFSKY,D.HOUSSET,     1BPT  16
REMARK   1  AUTH 2 A.WLODAWER,C.WOODWARD                                1BPT  17
REMARK   1  TITL   CREVICE-FORMING MUTANTS OF BPTI: STABILITY CHANGES   1BPT  18
REMARK   1  TITL 2 AND NEW HYDROPHOBIC SURFACE                          1BPT  19
REMARK   1  REF    TO BE PUBLISHED                                      1BPT  20
REMARK   1  REFN                                                   353  1BPT  21
REMARK   1 REFERENCE 2                                                  1BPT  22
REMARK   1  AUTH   D.HOUSSET,K.-*S.KIM,J.FUCHS,C.WOODWARD,A.WLODAWER    1BPT  23
REMARK   1  TITL   CRYSTAL STRUCTURE OF A /Y35G$ MUTANT OF BOVINE       1BPT  24
REMARK   1  TITL 2 PANCREATIC TRYPSIN INHIBITOR                         1BPT  25
REMARK   1  REF    J.MOL.BIOL.                   V. 220   757 1991      1BPT  26
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836                  070  1BPT  27
REMARK   1 REFERENCE 3                                                  1BPT  28
REMARK   1  AUTH   C.EIGENBROT,M.RANDAL,A.A.KOSSIAKOFF                  1BPT  29
REMARK   1  TITL   STRUCTURAL EFFECTS INDUCED BY REMOVAL OF A           1BPT  30
REMARK   1  TITL 2 DISULFIDE-BRIDGE. THE X-RAY STRUCTURE OF THE         1BPT  31
REMARK   1  TITL 3 /C30A(SLASH)C51A$ MUTANT OF BASIC PANCREATIC         1BPT  32
REMARK   1  TITL 4 TRYPSIN INHIBITOR AT 1.6 ANGSTROMS                   1BPT  33
REMARK   1  REF    PROTEIN ENG.                  V.   3   591 1990      1BPT  34
REMARK   1  REFN   ASTM PRENE9  UK ISSN 0269-2139                  859  1BPT  35
REMARK   1 REFERENCE 4                                                  1BPT  36
REMARK   1  AUTH   T.R.HYNES,M.RANDAL,L.A.KENNEDY,C.EIGENBROT,          1BPT  37
REMARK   1  AUTH 2 A.A.KOSSIAKOFF                                       1BPT  38
REMARK   1  TITL   X-RAY CRYSTAL STRUCTURE OF THE PROTEASE INHIBITOR    1BPT  39
REMARK   1  TITL 2 DOMAIN OF ALZHEIMER'S AMYLOID BETA-*PROTEIN          1BPT  40
REMARK   1  TITL 3 PRECURSOR                                            1BPT  41
REMARK   1  REF    BIOCHEMISTRY                  V.  29 10018 1990      1BPT  42
REMARK   1  REFN   ASTM BICHAW  US ISSN 0006-2960                  033  1BPT  43
REMARK   1 REFERENCE 5                                                  1BPT  44
REMARK   1  AUTH   A.WLODAWER,J.NACHMAN,G.L.GILLILAND,W.GALLAGHER       1BPT  45
REMARK   1  AUTH 2 C.WOODWARD                                           1BPT  46
REMARK   1  TITL   STRUCTURE OF FORM /III$ CRYSTALS OF BOVINE           1BPT  47
REMARK   1  TITL 2 PANCREATIC TRYPSIN INHIBITOR.                        1BPT  48
REMARK   1  REF    J.MOL.BIOL.                   V. 198   469 1987      1BPT  49
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836                  070  1BPT  50
REMARK   1 REFERENCE 6                                                  1BPT  51
REMARK   1  AUTH   A.WLODAWER,J.WALTER,R.HUBER,L.SJOLIN                 1BPT  52
REMARK   1  TITL   STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR.    1BPT  53
REMARK   1  TITL 2 RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT OF     1BPT  54
REMARK   1  TITL 3 CRYSTAL FORM /II$                                    1BPT  55
REMARK   1  REF    J.MOL.BIOL.                   V. 180   307 1984      1BPT  56
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836                  070  1BPT  57
REMARK   1 REFERENCE 7                                                  1BPT  58
REMARK   1  AUTH   A.WLODAWER,J.DEISENHOFER,R.HUBER                     1BPT  59
REMARK   1  TITL   COMPARISON OF TWO HIGHLY REFINED STRUCTURES OF       1BPT  60
REMARK   1  TITL 2 BOVINE PANCREATIC TRYPSIN INHIBITOR                  1BPT  61
REMARK   1  REF    J.MOL.BIOL.                   V. 193   145 1987      1BPT  62
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836                  070  1BPT  63
REMARK   1 REFERENCE 8                                                  1BPT  64
REMARK   1  AUTH   J.WALTER,R.HUBER                                     1BPT  65
REMARK   1  TITL   PANCREATIC TRYPSIN INHIBITOR. A NEW CRYSTAL FORM     1BPT  66
REMARK   1  TITL 2 AND ITS ANALYSIS                                     1BPT  67
REMARK   1  REF    J.MOL.BIOL.                   V. 167   911 1983      1BPT  68
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836                  070  1BPT  69
REMARK   2                                                              1BPT  70
REMARK   2 RESOLUTION. 2.0  ANGSTROMS.                                  1BPT  71
REMARK   3                                                              1BPT  72
REMARK   3 REFINEMENT.                                                  1BPT  73
REMARK   3   PROGRAM                    XPLOR                           1BPT  74
REMARK   3   AUTHORS                    BRUENGER                        1BPT  75
REMARK   3   R VALUE                    0.165                           1BPT  76
REMARK   3   RMSD BOND DISTANCES        0.018  ANGSTROMS                1BPT  77
REMARK   4                                                              1BPT  78
REMARK   4 THERE WAS NO DENSITY FOR THE FINAL TWO CARBOXY-TERMINAL      1BPT  79
REMARK   4 RESIDUES (GLY 57 AND ALA 58) IN THE FINAL MAPS.              1BPT  80
REMARK   5                                                              1BPT  81
REMARK   5 COORDINATES FOR 40 WATER MOLECULES ARE GIVEN FOLLOWING THE   1BPT  82
REMARK   5 MAIN BODY OF THE PROTEIN.  THE NOMENCLATURE OF THE WATER     1BPT  83
REMARK   5 MOLECULES IS THAT OF THE DEPOSITORS.                         1BPT  84
SEQRES   1     58  ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO  1BPT  85
SEQRES   2     58  CYS LYS ALA ARG ILE ILE ARG TYR PHE ALA ASN ALA LYS  1BPT  86
SEQRES   3     58  ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG  1BPT  87
SEQRES   4     58  ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET  1BPT  88
SEQRES   5     58  ARG THR CYS GLY GLY ALA                              1BPT  89
HET    PO4     70       5     PHOSPHATE ION                             1BPT  90
FORMUL   2  PO4    O4 P1 --                                             1BPT  91
FORMUL   3  HOH   *40(H2 O1)                                            1BPT  92
HELIX    1  H1 PRO      2  GLU      7  5 ALL DONORS,ACCEPTORS INCLUDED  1BPT  93
HELIX    2  H2 SER     47  GLY     56  1 ALL DONORS,ACCEPTORS INCLUDED  1BPT  94
SHEET    1  S1 3 LEU    29  TYR    35  0                                1BPT  95
SHEET    2  S1 3 ILE    18  ASN    24 -1  N  ILE    18   O  TYR    35   1BPT  96
SHEET    3  S1 3 PHE    45  PHE    45 -1  N  PHE    45   O  TYR    21   1BPT  97
SSBOND   1 CYS      5    CYS     55                                     1BPT  98
SSBOND   2 CYS     14    CYS     38                                     1BPT  99
SSBOND   3 CYS     30    CYS     51                                     1BPT 100
CRYST1   69.469   23.346   29.188  90.00  90.00  90.00 P 21 21 21    4  1BPT 101
ORIGX1      1.000000  0.000000  0.000000        0.00000                 1BPT 102
ORIGX2      0.000000  1.000000  0.000000        0.00000                 1BPT 103
ORIGX3      0.000000  0.000000  1.000000        0.00000                 1BPT 104
SCALE1      0.014395  0.000000  0.000000        0.00000                 1BPT 105
SCALE2      0.000000  0.042834  0.000000        0.00000                 1BPT 106
SCALE3      0.000000  0.000000  0.034261        0.00000                 1BPT 107
ATOM      1  N   ARG     1      29.292  13.212 -12.751  1.00 33.78      1BPT 108
ATOM      2  CA  ARG     1      29.057  12.019 -11.946  1.00 27.63      1BPT 109
ATOM      3  C   ARG     1      30.419  11.466 -11.478  1.00 29.64      1BPT 110
ATOM      4  O   ARG     1      31.064  10.670 -12.174  1.00 27.67      1BPT 111
ATOM      5  CB  ARG     1      28.297  10.939 -12.700  1.00 28.82      1BPT 112
ATOM      6  CG  ARG     1      27.925   9.695 -11.892  1.00 25.04      1BPT 113
ATOM      7  CD  ARG     1      26.990  10.102 -10.814  1.00 36.35      1BPT 114
ATOM      8  NE  ARG     1      25.671   9.509 -10.875  1.00 43.70      1BPT 115
ATOM      9  CZ  ARG     1      25.299   8.414 -10.207  1.00 44.64      1BPT 116
ATOM     10  NH1 ARG     1      26.105   7.749  -9.392  1.00 44.80      1BPT 117
ATOM     11  NH2 ARG     1      24.055   7.949 -10.340  1.00 51.16      1BPT 118
ATOM     12  N   PRO     2      30.790  11.942 -10.291  1.00 26.52      1BPT 119
ATOM     13  CA  PRO     2      32.005  11.512  -9.585  1.00 25.70      1BPT 120
ATOM     14  C   PRO     2      32.010   9.993  -9.473  1.00 22.30      1BPT 121
ATOM     15  O   PRO     2      30.968   9.316  -9.390  1.00 22.80      1BPT 122
ATOM     16  CB  PRO     2      31.892  12.166  -8.209  1.00 25.93      1BPT 123
ATOM     17  CG  PRO     2      31.000  13.378  -8.442  1.00 26.12      1BPT 124
ATOM     18  CD  PRO     2      29.997  12.890  -9.480  1.00 27.15      1BPT 125
ATOM     19  N   ASP     3      33.188   9.438  -9.467  1.00 21.36      1BPT 126
ATOM     20  CA  ASP     3      33.386   7.984  -9.444  1.00 21.85      1BPT 127
ATOM     21  C   ASP     3      32.859   7.313  -8.187  1.00 18.86      1BPT 128
ATOM     22  O   ASP     3      32.477   6.121  -8.298  1.00  9.03      1BPT 129
ATOM     23  CB  ASP     3      34.849   7.659  -9.800  1.00 30.83      1BPT 130
ATOM     24  CG  ASP     3      35.257   8.386 -11.083  1.00 41.90      1BPT 131
ATOM     25  OD1 ASP     3      34.882   7.832 -12.153  1.00 42.04      1BPT 132
ATOM     26  OD2 ASP     3      35.864   9.473 -10.980  1.00 43.78      1BPT 133
ATOM     27  N   PHE     4      32.841   8.042  -7.067  1.00 14.13      1BPT 134
ATOM     28  CA  PHE     4      32.406   7.481  -5.780  1.00 12.89      1BPT 135
ATOM     29  C   PHE     4      30.894   7.286  -5.768  1.00 12.89      1BPT 136
ATOM     30  O   PHE     4      30.393   6.509  -4.938  1.00 12.42      1BPT 137
ATOM     31  CB  PHE     4      32.998   8.208  -4.578  1.00 13.83      1BPT 138
ATOM     32  CG  PHE     4      32.588   9.662  -4.482  1.00 10.93      1BPT 139
ATOM     33  CD1 PHE     4      31.311   9.973  -3.991  1.00 12.72      1BPT 140
ATOM     34  CD2 PHE     4      33.414  10.650  -4.951  1.00 13.53      1BPT 141
ATOM     35  CE1 PHE     4      30.896  11.308  -3.928  1.00 15.82      1BPT 142
ATOM     36  CE2 PHE     4      33.041  12.001  -4.878  1.00 14.51      1BPT 143
ATOM     37  CZ  PHE     4      31.765  12.300  -4.388  1.00 10.66      1BPT 144
ATOM     38  N   CYS     5      30.213   7.889  -6.711  1.00 11.30      1BPT 145
ATOM     39  CA  CYS     5      28.751   7.756  -6.894  1.00  8.91      1BPT 146
ATOM     40  C   CYS     5      28.333   6.353  -7.318  1.00  9.64      1BPT 147
ATOM     41  O   CYS     5      27.197   5.876  -7.108  1.00  7.73      1BPT 148
ATOM     42  CB  CYS     5      28.387   8.851  -7.898  1.00 11.12      1BPT 149
ATOM     43  SG  CYS     5      28.579  10.549  -7.280  1.00 12.16      1BPT 150
ATOM     44  N   LEU     6      29.193   5.558  -7.897  1.00  4.74      1BPT 151
ATOM     45  CA  LEU     6      29.077   4.189  -8.326  1.00  6.59      1BPT 152
ATOM     46  C   LEU     6      29.483   3.225  -7.187  1.00  9.26      1BPT 153
ATOM     47  O   LEU     6      29.266   1.982  -7.343  1.00 13.32      1BPT 154
ATOM     48  CB  LEU     6      29.823   3.914  -9.616  1.00 11.74      1BPT 155
ATOM     49  CG  LEU     6      29.250   4.089 -11.024  1.00 15.14      1BPT 156
ATOM     50  CD1 LEU     6      28.437   5.346 -11.272  1.00 16.39      1BPT 157
ATOM     51  CD2 LEU     6      30.480   4.138 -11.961  1.00 10.37      1BPT 158
ATOM     52  N   GLU     7      29.975   3.690  -6.075  1.00  9.37      1BPT 159
ATOM     53  CA  GLU     7      30.343   2.830  -4.930  1.00 13.11      1BPT 160
ATOM     54  C   GLU     7      29.096   2.241  -4.249  1.00 10.70      1BPT 161
ATOM     55  O   GLU     7      28.116   2.999  -4.165  1.00  9.68      1BPT 162
ATOM     56  CB  GLU     7      30.967   3.613  -3.776  1.00 19.20      1BPT 163
ATOM     57  CG  GLU     7      32.359   3.902  -3.452  1.00 23.47      1BPT 164
ATOM     58  CD  GLU     7      32.867   5.001  -2.582  1.00 27.28      1BPT 165
ATOM     59  OE1 GLU     7      32.230   5.418  -1.584  1.00 20.35      1BPT 166
ATOM     60  OE2 GLU     7      33.979   5.507  -2.848  1.00 29.04      1BPT 167
ATOM     61  N   PRO     8      29.242   1.021  -3.736  1.00 10.63      1BPT 168
ATOM     62  CA  PRO     8      28.178   0.413  -2.939  1.00 11.56      1BPT 169
ATOM     63  C   PRO     8      28.214   1.124  -1.566  1.00  8.44      1BPT 170
ATOM     64  O   PRO     8      29.236   1.677  -1.137  1.00  6.60      1BPT 171
ATOM     65  CB  PRO     8      28.549  -1.058  -2.811  1.00 11.83      1BPT 172
ATOM     66  CG  PRO     8      30.015  -1.151  -3.101  1.00 11.19      1BPT 173
ATOM     67  CD  PRO     8      30.413   0.125  -3.811  1.00 10.52      1BPT 174
ATOM     68  N   PRO     9      27.095   1.120  -0.895  1.00  8.82      1BPT 175
ATOM     69  CA  PRO     9      27.024   1.732   0.456  1.00  7.22      1BPT 176
ATOM     70  C   PRO     9      27.918   0.926   1.409  1.00  8.58      1BPT 177
ATOM     71  O   PRO     9      28.136  -0.308   1.289  1.00  9.21      1BPT 178
ATOM     72  CB  PRO     9      25.565   1.704   0.830  1.00  8.50      1BPT 179
ATOM     73  CG  PRO     9      24.820   0.922  -0.252  1.00  8.80      1BPT 180
ATOM     74  CD  PRO     9      25.831   0.488  -1.289  1.00  8.43      1BPT 181
ATOM     75  N   TYR    10      28.489   1.597   2.363  1.00  5.10      1BPT 182
ATOM     76  CA  TYR    10      29.355   0.981   3.369  1.00  7.77      1BPT 183
ATOM     77  C   TYR    10      28.862   1.292   4.801  1.00  6.47      1BPT 184
ATOM     78  O   TYR    10      29.004   2.426   5.260  1.00  5.08      1BPT 185
ATOM     79  CB  TYR    10      30.776   1.548   3.188  1.00 10.29      1BPT 186
ATOM     80  CG  TYR    10      31.812   0.865   4.029  1.00  3.16      1BPT 187
ATOM     81  CD1 TYR    10      32.181  -0.458   3.705  1.00  8.41      1BPT 188
ATOM     82  CD2 TYR    10      32.424   1.521   5.086  1.00  6.18      1BPT 189
ATOM     83  CE1 TYR    10      33.149  -1.084   4.464  1.00 15.04      1BPT 190
ATOM     84  CE2 TYR    10      33.412   0.896   5.832  1.00  6.33      1BPT 191
ATOM     85  CZ  TYR    10      33.728  -0.425   5.565  1.00  8.46      1BPT 192
ATOM     86  OH  TYR    10      34.706  -1.029   6.302  1.00 18.91      1BPT 193
ATOM     87  N   THR    11      28.424   0.231   5.434  1.00  6.57      1BPT 194
ATOM     88  CA  THR    11      27.936   0.236   6.812  1.00  8.79      1BPT 195
ATOM     89  C   THR    11      29.135   0.441   7.754  1.00 11.72      1BPT 196
ATOM     90  O   THR    11      29.083   1.299   8.664  1.00  8.91      1BPT 197
ATOM     91  CB  THR    11      27.128  -1.066   7.132  1.00  9.23      1BPT 198
ATOM     92  OG1 THR    11      25.915  -0.877   6.315  1.00 11.90      1BPT 199
ATOM     93  CG2 THR    11      26.632  -1.251   8.598  1.00  9.84      1BPT 200
ATOM     94  N   GLY    12      30.177  -0.374   7.495  1.00  7.42      1BPT 201
ATOM     95  CA  GLY    12      31.386  -0.224   8.306  1.00  5.96      1BPT 202
ATOM     96  C   GLY    12      31.203  -1.147   9.527  1.00 12.57      1BPT 203
ATOM     97  O   GLY    12      30.172  -1.792   9.683  1.00  8.90      1BPT 204
ATOM     98  N   PRO    13      32.259  -1.145  10.334  1.00  9.49      1BPT 205
ATOM     99  CA  PRO    13      32.384  -1.978  11.478  1.00 11.26      1BPT 206
ATOM    100  C   PRO    13      31.761  -1.570  12.787  1.00 10.42      1BPT 207
ATOM    101  O   PRO    13      31.739  -2.455  13.698  1.00  9.05      1BPT 208
ATOM    102  CB  PRO    13      33.930  -2.112  11.625  1.00 12.73      1BPT 209
ATOM    103  CG  PRO    13      34.418  -0.761  11.150  1.00 12.37      1BPT 210
ATOM    104  CD  PRO    13      33.504  -0.375  10.028  1.00  9.04      1BPT 211
ATOM    105  N   CYS    14      31.284  -0.361  12.916  1.00  9.07      1BPT 212
ATOM    106  CA  CYS    14      30.645   0.049  14.197  1.00 10.05      1BPT 213
ATOM    107  C   CYS    14      29.209  -0.417  14.208  1.00 13.02      1BPT 214
ATOM    108  O   CYS    14      28.598  -0.805  13.198  1.00 11.90      1BPT 215
ATOM    109  CB  CYS    14      30.904   1.510  14.446  1.00  7.60      1BPT 216
ATOM    110  SG  CYS    14      32.618   1.798  14.807  1.00 11.36      1BPT 217
ATOM    111  N   LYS    15      28.649  -0.419  15.375  1.00 15.92      1BPT 218
ATOM    112  CA  LYS    15      27.336  -0.923  15.756  1.00 15.34      1BPT 219
ATOM    113  C   LYS    15      26.228   0.042  16.097  1.00 15.21      1BPT 220
ATOM    114  O   LYS    15      25.303  -0.309  16.854  1.00 19.24      1BPT 221
ATOM    115  CB  LYS    15      27.580  -1.878  16.945  1.00 11.46      1BPT 222
ATOM    116  CG  LYS    15      27.956  -3.321  16.572  1.00 19.41      1BPT 223
ATOM    117  CD  LYS    15      29.204  -3.436  15.742  1.00 19.90      1BPT 224
ATOM    118  CE  LYS    15      29.694  -4.836  15.472  1.00 20.37      1BPT 225
ATOM    119  NZ  LYS    15      30.440  -5.364  16.680  1.00 25.63      1BPT 226
ATOM    120  N   ALA    16      26.223   1.260  15.569  1.00 11.74      1BPT 227
ATOM    121  CA  ALA    16      25.109   2.169  15.768  1.00  7.48      1BPT 228
ATOM    122  C   ALA    16      24.174   1.935  14.571  1.00  4.01      1BPT 229
ATOM    123  O   ALA    16      24.497   1.277  13.592  1.00  5.07      1BPT 230
ATOM    124  CB  ALA    16      25.536   3.634  15.859  1.00  5.63      1BPT 231
ATOM    125  N   ARG    17      22.998   2.500  14.683  1.00  8.74      1BPT 232
ATOM    126  CA  ARG    17      21.990   2.475  13.592  1.00 11.74      1BPT 233
ATOM    127  C   ARG    17      21.767   3.981  13.235  1.00  7.15      1BPT 234
ATOM    128  O   ARG    17      21.022   4.658  13.964  1.00 10.78      1BPT 235
ATOM    129  CB  ARG    17      20.614   1.926  13.959  1.00  6.42      1BPT 236
ATOM    130  CG  ARG    17      20.105   0.880  12.983  1.00 15.99      1BPT 237
ATOM    131  CD  ARG    17      19.624  -0.289  13.808  1.00  9.00      1BPT 238
ATOM    132  NE  ARG    17      18.355   0.098  14.439  1.00 18.94      1BPT 239
ATOM    133  CZ  ARG    17      17.708  -0.673  15.324  1.00 17.07      1BPT 240
ATOM    134  NH1 ARG    17      18.221  -1.843  15.720  1.00 10.96      1BPT 241
ATOM    135  NH2 ARG    17      16.495  -0.327  15.731  1.00 15.74      1BPT 242
ATOM    136  N   ILE    18      22.497   4.428  12.250  1.00  8.62      1BPT 243
ATOM    137  CA  ILE    18      22.423   5.788  11.715  1.00 10.26      1BPT 244
ATOM    138  C   ILE    18      21.950   5.730  10.266  1.00  9.38      1BPT 245
ATOM    139  O   ILE    18      22.480   5.004   9.421  1.00  8.61      1BPT 246
ATOM    140  CB  ILE    18      23.762   6.554  11.785  1.00 13.44      1BPT 247
ATOM    141  CG1 ILE    18      24.274   6.512  13.260  1.00 10.02      1BPT 248
ATOM    142  CG2 ILE    18      23.602   8.014  11.254  1.00 10.50      1BPT 249
ATOM    143  CD1 ILE    18      25.764   6.903  13.344  1.00 10.74      1BPT 250
ATOM    144  N   ILE    19      20.867   6.472  10.022  1.00 15.71      1BPT 251
ATOM    145  CA  ILE    19      20.335   6.459   8.640  1.00 13.86      1BPT 252
ATOM    146  C   ILE    19      20.970   7.606   7.855  1.00 13.32      1BPT 253
ATOM    147  O   ILE    19      20.910   8.763   8.262  1.00 11.39      1BPT 254
ATOM    148  CB  ILE    19      18.788   6.485   8.581  1.00 13.72      1BPT 255
ATOM    149  CG1 ILE    19      18.252   5.154   9.150  1.00  6.44      1BPT 256
ATOM    150  CG2 ILE    19      18.282   6.719   7.120  1.00 12.60      1BPT 257
ATOM    151  CD1 ILE    19      18.299   5.180  10.698  1.00 16.15      1BPT 258
ATOM    152  N   ARG    20      21.588   7.204   6.751  1.00 11.35      1BPT 259
ATOM    153  CA  ARG    20      22.236   8.068   5.785  1.00  9.74      1BPT 260
ATOM    154  C   ARG    20      21.695   7.783   4.382  1.00  6.30      1BPT 261
ATOM    155  O   ARG    20      20.944   6.791   4.218  1.00  9.59      1BPT 262
ATOM    156  CB  ARG    20      23.771   7.817   5.751  1.00  9.39      1BPT 263
ATOM    157  CG  ARG    20      24.296   7.949   7.188  1.00  2.00      1BPT 264
ATOM    158  CD  ARG    20      24.046   9.346   7.751  1.00 11.19      1BPT 265
ATOM    159  NE  ARG    20      25.357   9.939   7.653  1.00 16.42      1BPT 266
ATOM    160  CZ  ARG    20      26.326  10.113   8.491  1.00 17.82      1BPT 267
ATOM    161  NH1 ARG    20      26.238  10.069   9.811  1.00 20.52      1BPT 268
ATOM    162  NH2 ARG    20      27.584  10.026   7.945  1.00 11.96      1BPT 269
ATOM    163  N   TYR    21      22.153   8.566   3.449  1.00  3.50      1BPT 270
ATOM    164  CA  TYR    21      21.802   8.399   2.032  1.00  4.17      1BPT 271
ATOM    165  C   TYR    21      23.053   8.021   1.197  1.00  9.33      1BPT 272
ATOM    166  O   TYR    21      24.153   8.520   1.489  1.00  9.71      1BPT 273
ATOM    167  CB  TYR    21      21.233   9.689   1.363  1.00  2.47      1BPT 274
ATOM    168  CG  TYR    21      19.856   9.977   1.902  1.00  5.78      1BPT 275
ATOM    169  CD1 TYR    21      18.714   9.405   1.346  1.00  8.74      1BPT 276
ATOM    170  CD2 TYR    21      19.722  10.802   3.013  1.00  5.70      1BPT 277
ATOM    171  CE1 TYR    21      17.462   9.666   1.913  1.00  8.01      1BPT 278
ATOM    172  CE2 TYR    21      18.482  11.081   3.558  1.00 11.15      1BPT 279
ATOM    173  CZ  TYR    21      17.360  10.496   2.999  1.00  9.06      1BPT 280
ATOM    174  OH  TYR    21      16.131  10.758   3.524  1.00 17.41      1BPT 281
ATOM    175  N   PHE    22      22.829   7.168   0.207  1.00  4.91      1BPT 282
ATOM    176  CA  PHE    22      23.752   6.692  -0.783  1.00  4.40      1BPT 283
ATOM    177  C   PHE    22      23.022   6.846  -2.150  1.00  7.34      1BPT 284
ATOM    178  O   PHE    22      21.797   6.782  -2.278  1.00  6.82      1BPT 285
ATOM    179  CB  PHE    22      24.275   5.290  -0.661  1.00  2.00      1BPT 286
ATOM    180  CG  PHE    22      23.364   4.150  -0.996  1.00  5.18      1BPT 287
ATOM    181  CD1 PHE    22      22.275   3.834  -0.223  1.00  2.00      1BPT 288
ATOM    182  CD2 PHE    22      23.583   3.377  -2.136  1.00  5.44      1BPT 289
ATOM    183  CE1 PHE    22      21.466   2.719  -0.446  1.00  6.36      1BPT 290
ATOM    184  CE2 PHE    22      22.782   2.296  -2.447  1.00  5.66      1BPT 291
ATOM    185  CZ  PHE    22      21.709   1.949  -1.597  1.00 10.45      1BPT 292
ATOM    186  N   ALA    23      23.845   7.069  -3.162  1.00  9.17      1BPT 293
ATOM    187  CA  ALA    23      23.410   7.217  -4.539  1.00  7.19      1BPT 294
ATOM    188  C   ALA    23      23.463   5.773  -5.115  1.00  9.37      1BPT 295
ATOM    189  O   ALA    23      24.506   5.134  -4.936  1.00  8.29      1BPT 296
ATOM    190  CB  ALA    23      24.352   8.087  -5.360  1.00  4.05      1BPT 297
ATOM    191  N   ASN    24      22.400   5.354  -5.693  1.00  7.55      1BPT 298
ATOM    192  CA  ASN    24      22.126   4.088  -6.326  1.00 15.15      1BPT 299
ATOM    193  C   ASN    24      22.120   4.301  -7.848  1.00 14.72      1BPT 300
ATOM    194  O   ASN    24      21.083   4.569  -8.463  1.00 22.72      1BPT 301
ATOM    195  CB  ASN    24      20.788   3.517  -5.804  1.00 19.37      1BPT 302
ATOM    196  CG  ASN    24      20.802   1.994  -5.932  1.00 26.23      1BPT 303
ATOM    197  OD1 ASN    24      21.039   1.448  -7.013  1.00 21.38      1BPT 304
ATOM    198  ND2 ASN    24      20.644   1.338  -4.770  1.00 31.83      1BPT 305
ATOM    199  N   ALA    25      23.301   4.247  -8.411  1.00 17.58      1BPT 306
ATOM    200  CA  ALA    25      23.706   4.425  -9.774  1.00 17.08      1BPT 307
ATOM    201  C   ALA    25      22.839   3.573 -10.736  1.00 21.07      1BPT 308
ATOM    202  O   ALA    25      22.702   3.982 -11.887  1.00 16.65      1BPT 309
ATOM    203  CB  ALA    25      25.187   4.093  -9.933  1.00 11.69      1BPT 310
ATOM    204  N   LYS    26      22.312   2.473 -10.242  1.00 19.28      1BPT 311
ATOM    205  CA  LYS    26      21.466   1.487 -10.891  1.00 22.03      1BPT 312
ATOM    206  C   LYS    26      20.014   1.952 -10.989  1.00 24.09      1BPT 313
ATOM    207  O   LYS    26      19.442   1.857 -12.084  1.00 23.97      1BPT 314
ATOM    208  CB  LYS    26      21.491   0.169 -10.130  1.00 22.95      1BPT 315
ATOM    209  CG  LYS    26      21.106  -1.100 -10.859  1.00 28.77      1BPT 316
ATOM    210  CD  LYS    26      22.013  -1.383 -12.055  1.00 29.92      1BPT 317
ATOM    211  CE  LYS    26      22.610  -2.772 -11.994  1.00 25.89      1BPT 318
ATOM    212  NZ  LYS    26      23.796  -2.860 -12.900  1.00 25.18      1BPT 319
ATOM    213  N   ALA    27      19.497   2.488  -9.874  1.00 22.92      1BPT 320
ATOM    214  CA  ALA    27      18.103   2.961  -9.823  1.00 19.83      1BPT 321
ATOM    215  C   ALA    27      17.967   4.434 -10.123  1.00 20.29      1BPT 322
ATOM    216  O   ALA    27      16.824   4.929 -10.240  1.00 23.87      1BPT 323
ATOM    217  CB  ALA    27      17.441   2.549  -8.518  1.00 16.72      1BPT 324
ATOM    218  N   GLY    28      19.057   5.153 -10.273  1.00 16.11      1BPT 325
ATOM    219  CA  GLY    28      19.062   6.550 -10.586  1.00 17.38      1BPT 326
ATOM    220  C   GLY    28      18.483   7.415  -9.466  1.00 18.84      1BPT 327
ATOM    221  O   GLY    28      18.119   8.579  -9.690  1.00 16.95      1BPT 328
ATOM    222  N   LEU    29      18.443   6.832  -8.287  1.00 21.25      1BPT 329
ATOM    223  CA  LEU    29      17.947   7.407  -7.024  1.00 21.57      1BPT 330
ATOM    224  C   LEU    29      18.945   7.497  -5.866  1.00 18.12      1BPT 331
ATOM    225  O   LEU    29      19.896   6.727  -5.858  1.00 21.34      1BPT 332
ATOM    226  CB  LEU    29      17.024   6.228  -6.528  1.00 23.29      1BPT 333
ATOM    227  CG  LEU    29      15.567   6.158  -6.693  1.00 19.66      1BPT 334
ATOM    228  CD1 LEU    29      15.044   6.893  -7.909  1.00 21.45      1BPT 335
ATOM    229  CD2 LEU    29      15.225   4.662  -6.813  1.00 20.64      1BPT 336
ATOM    230  N   CYS    30      18.644   8.243  -4.834  1.00 15.30      1BPT 337
ATOM    231  CA  CYS    30      19.386   8.332  -3.584  1.00 13.07      1BPT 338
ATOM    232  C   CYS    30      18.461   7.549  -2.587  1.00 11.85      1BPT 339
ATOM    233  O   CYS    30      17.266   7.847  -2.545  1.00  9.49      1BPT 340
ATOM    234  CB  CYS    30      19.618   9.746  -3.030  1.00  7.99      1BPT 341
ATOM    235  SG  CYS    30      20.895  10.605  -3.992  1.00 11.01      1BPT 342
ATOM    236  N   GLN    31      19.006   6.552  -1.970  1.00  8.48      1BPT 343
ATOM    237  CA  GLN    31      18.317   5.700  -1.038  1.00  6.54      1BPT 344
ATOM    238  C   GLN    31      19.100   5.705   0.281  1.00  5.06      1BPT 345
ATOM    239  O   GLN    31      20.258   6.027   0.325  1.00 10.97      1BPT 346
ATOM    240  CB  GLN    31      18.127   4.265  -1.486  1.00  6.08      1BPT 347
ATOM    241  CG  GLN    31      17.649   4.129  -2.917  1.00 10.54      1BPT 348
ATOM    242  CD  GLN    31      17.592   2.652  -3.291  1.00 15.80      1BPT 349
ATOM    243  OE1 GLN    31      18.591   1.933  -3.214  1.00 13.15      1BPT 350
ATOM    244  NE2 GLN    31      16.345   2.282  -3.638  1.00 16.64      1BPT 351
ATOM    245  N   THR    32      18.377   5.323   1.264  1.00  6.87      1BPT 352
ATOM    246  CA  THR    32      18.655   5.165   2.680  1.00  7.62      1BPT 353
ATOM    247  C   THR    32      19.331   3.843   2.925  1.00  4.54      1BPT 354
ATOM    248  O   THR    32      19.028   2.743   2.403  1.00  9.34      1BPT 355
ATOM    249  CB  THR    32      17.212   5.330   3.366  1.00 11.68      1BPT 356
ATOM    250  OG1 THR    32      17.146   6.586   4.121  1.00 16.76      1BPT 357
ATOM    251  CG2 THR    32      16.592   4.169   4.025  1.00 11.13      1BPT 358
ATOM    252  N   PHE    33      20.325   3.905   3.792  1.00  6.01      1BPT 359
ATOM    253  CA  PHE    33      21.049   2.679   4.214  1.00  5.51      1BPT 360
ATOM    254  C   PHE    33      21.391   2.964   5.697  1.00  5.03      1BPT 361
ATOM    255  O   PHE    33      21.307   4.127   6.134  1.00  2.00      1BPT 362
ATOM    256  CB  PHE    33      22.237   2.311   3.301  1.00  6.21      1BPT 363
ATOM    257  CG  PHE    33      23.481   3.115   3.586  1.00  7.37      1BPT 364
ATOM    258  CD1 PHE    33      23.551   4.451   3.178  1.00  3.42      1BPT 365
ATOM    259  CD2 PHE    33      24.548   2.490   4.242  1.00  5.10      1BPT 366
ATOM    260  CE1 PHE    33      24.689   5.209   3.481  1.00  4.87      1BPT 367
ATOM    261  CE2 PHE    33      25.680   3.270   4.545  1.00  3.64      1BPT 368
ATOM    262  CZ  PHE    33      25.736   4.604   4.188  1.00  4.11      1BPT 369
ATOM    263  N   VAL    34      21.791   1.844   6.303  1.00  7.77      1BPT 370
ATOM    264  CA  VAL    34      22.179   1.847   7.727  1.00  7.30      1BPT 371
ATOM    265  C   VAL    34      23.698   2.016   7.870  1.00  5.82      1BPT 372
ATOM    266  O   VAL    34      24.383   1.128   7.464  1.00  7.30      1BPT 373
ATOM    267  CB  VAL    34      21.710   0.602   8.491  1.00 12.10      1BPT 374
ATOM    268  CG1 VAL    34      22.162   0.650   9.973  1.00  9.39      1BPT 375
ATOM    269  CG2 VAL    34      20.174   0.525   8.409  1.00 15.65      1BPT 376
ATOM    270  N   TYR    35      24.091   3.158   8.410  1.00  5.38      1BPT 377
ATOM    271  CA  TYR    35      25.512   3.474   8.630  1.00  4.86      1BPT 378
ATOM    272  C   TYR    35      25.853   3.141  10.089  1.00  6.21      1BPT 379
ATOM    273  O   TYR    35      25.096   3.564  11.002  1.00  5.98      1BPT 380
ATOM    274  CB  TYR    35      25.736   4.938   8.236  1.00  5.98      1BPT 381
ATOM    275  CG  TYR    35      27.123   5.423   8.667  1.00  8.66      1BPT 382
ATOM    276  CD1 TYR    35      28.268   4.755   8.295  1.00  5.52      1BPT 383
ATOM    277  CD2 TYR    35      27.254   6.531   9.488  1.00  5.03      1BPT 384
ATOM    278  CE1 TYR    35      29.512   5.168   8.668  1.00  4.71      1BPT 385
ATOM    279  CE2 TYR    35      28.510   6.966   9.884  1.00  5.81      1BPT 386
ATOM    280  CZ  TYR    35      29.623   6.289   9.481  1.00  3.57      1BPT 387
ATOM    281  OH  TYR    35      30.830   6.742   9.901  1.00 13.53      1BPT 388
ATOM    282  N   GLY    36      26.877   2.383  10.299  1.00  9.83      1BPT 389
ATOM    283  CA  GLY    36      27.457   1.871  11.546  1.00 11.89      1BPT 390
ATOM    284  C   GLY    36      28.028   2.897  12.527  1.00 10.62      1BPT 391
ATOM    285  O   GLY    36      28.257   2.623  13.728  1.00  6.24      1BPT 392
ATOM    286  N   GLY    37      28.306   4.113  12.087  1.00 10.90      1BPT 393
ATOM    287  CA  GLY    37      28.806   5.132  13.062  1.00  8.57      1BPT 394
ATOM    288  C   GLY    37      30.264   5.436  12.901  1.00 11.39      1BPT 395
ATOM    289  O   GLY    37      30.788   6.346  13.587  1.00 12.05      1BPT 396
ATOM    290  N   CYS    38      30.958   4.608  12.100  1.00 11.97      1BPT 397
ATOM    291  CA  CYS    38      32.402   4.846  11.895  1.00 10.71      1BPT 398
ATOM    292  C   CYS    38      32.879   4.309  10.558  1.00  7.26      1BPT 399
ATOM    293  O   CYS    38      32.377   3.284  10.069  1.00 10.85      1BPT 400
ATOM    294  CB  CYS    38      33.254   4.254  13.025  1.00  5.40      1BPT 401
ATOM    295  SG  CYS    38      33.463   2.472  13.064  1.00 11.31      1BPT 402
ATOM    296  N   ARG    39      33.888   5.024  10.044  1.00  7.90      1BPT 403
ATOM    297  CA  ARG    39      34.612   4.645   8.827  1.00  9.16      1BPT 404
ATOM    298  C   ARG    39      33.852   4.820   7.536  1.00  5.75      1BPT 405
ATOM    299  O   ARG    39      33.993   4.050   6.590  1.00  7.37      1BPT 406
ATOM    300  CB  ARG    39      35.284   3.233   8.942  1.00 13.97      1BPT 407
ATOM    301  CG  ARG    39      36.652   3.311   9.588  1.00 23.19      1BPT 408
ATOM    302  CD  ARG    39      37.108   2.346  10.584  1.00 26.99      1BPT 409
ATOM    303  NE  ARG    39      37.383   1.012  10.071  1.00 34.96      1BPT 410
ATOM    304  CZ  ARG    39      38.017   0.015  10.712  1.00 34.64      1BPT 411
ATOM    305  NH1 ARG    39      38.490   0.185  11.953  1.00 32.55      1BPT 412
ATOM    306  NH2 ARG    39      38.178  -1.162  10.082  1.00 31.33      1BPT 413
ATOM    307  N   ALA    40      33.087   5.902   7.525  1.00  6.82      1BPT 414
ATOM    308  CA  ALA    40      32.280   6.346   6.408  1.00  6.05      1BPT 415
ATOM    309  C   ALA    40      33.174   6.463   5.167  1.00 10.08      1BPT 416
ATOM    310  O   ALA    40      34.349   6.857   5.267  1.00  9.96      1BPT 417
ATOM    311  CB  ALA    40      31.763   7.754   6.764  1.00  2.00      1BPT 418
ATOM    312  N   LYS    41      32.572   6.106   4.046  1.00  8.14      1BPT 419
ATOM    313  CA  LYS    41      33.210   6.218   2.716  1.00  6.07      1BPT 420
ATOM    314  C   LYS    41      32.548   7.399   2.044  1.00 12.83      1BPT 421
ATOM    315  O   LYS    41      31.646   8.090   2.693  1.00 10.68      1BPT 422
ATOM    316  CB  LYS    41      33.223   4.867   2.018  1.00 10.37      1BPT 423
ATOM    317  CG  LYS    41      34.398   4.021   2.455  1.00 16.66      1BPT 424
ATOM    318  CD  LYS    41      34.882   2.814   1.760  1.00 24.01      1BPT 425
ATOM    319  CE  LYS    41      35.299   2.810   0.338  1.00 30.41      1BPT 426
ATOM    320  NZ  LYS    41      36.465   3.643  -0.102  1.00 35.07      1BPT 427
ATOM    321  N   ARG    42      32.884   7.785   0.815  1.00 10.98      1BPT 428
ATOM    322  CA  ARG    42      32.283   8.966   0.211  1.00  9.54      1BPT 429
ATOM    323  C   ARG    42      30.805   8.864  -0.204  1.00  6.66      1BPT 430
ATOM    324  O   ARG    42      30.082   9.903  -0.070  1.00  3.97      1BPT 431
ATOM    325  CB  ARG    42      33.012   9.583  -0.935  1.00 15.86      1BPT 432
ATOM    326  CG  ARG    42      34.425  10.106  -0.842  1.00 20.34      1BPT 433
ATOM    327  CD  ARG    42      35.312   9.161  -1.625  1.00 22.25      1BPT 434
ATOM    328  NE  ARG    42      36.086   9.790  -2.633  1.00 21.50      1BPT 435
ATOM    329  CZ  ARG    42      36.767   9.117  -3.589  1.00 27.18      1BPT 436
ATOM    330  NH1 ARG    42      36.779   7.793  -3.734  1.00 24.88      1BPT 437
ATOM    331  NH2 ARG    42      37.511   9.871  -4.403  1.00 23.05      1BPT 438
ATOM    332  N   ASN    43      30.347   7.774  -0.685  1.00  4.96      1BPT 439
ATOM    333  CA  ASN    43      28.913   7.618  -1.084  1.00  5.93      1BPT 440
ATOM    334  C   ASN    43      28.074   7.439   0.214  1.00  6.01      1BPT 441
ATOM    335  O   ASN    43      27.554   6.351   0.508  1.00  5.41      1BPT 442
ATOM    336  CB  ASN    43      28.824   6.464  -2.040  1.00  2.00      1BPT 443
ATOM    337  CG  ASN    43      27.504   6.530  -2.797  1.00  3.64      1BPT 444
ATOM    338  OD1 ASN    43      26.760   7.532  -2.643  1.00  2.67      1BPT 445
ATOM    339  ND2 ASN    43      27.301   5.537  -3.633  1.00  4.58      1BPT 446
ATOM    340  N   ASN    44      27.999   8.522   0.982  1.00  9.31      1BPT 447
ATOM    341  CA  ASN    44      27.314   8.619   2.297  1.00  2.00      1BPT 448
ATOM    342  C   ASN    44      26.927  10.073   2.517  1.00  4.30      1BPT 449
ATOM    343  O   ASN    44      27.772  10.923   2.793  1.00  4.82      1BPT 450
ATOM    344  CB  ASN    44      28.276   8.091   3.338  1.00  8.38      1BPT 451
ATOM    345  CG  ASN    44      27.789   8.066   4.782  1.00  2.00      1BPT 452
ATOM    346  OD1 ASN    44      28.115   7.107   5.498  1.00  3.04      1BPT 453
ATOM    347  ND2 ASN    44      27.094   9.111   5.123  1.00  7.22      1BPT 454
ATOM    348  N   PHE    45      25.640  10.394   2.440  1.00  6.11      1BPT 455
ATOM    349  CA  PHE    45      25.077  11.713   2.604  1.00  6.35      1BPT 456
ATOM    350  C   PHE    45      24.138  11.761   3.822  1.00  5.91      1BPT 457
ATOM    351  O   PHE    45      23.569  10.743   4.220  1.00  7.40      1BPT 458
ATOM    352  CB  PHE    45      24.338  12.182   1.306  1.00  6.75      1BPT 459
ATOM    353  CG  PHE    45      25.243  12.109   0.104  1.00  8.57      1BPT 460
ATOM    354  CD1 PHE    45      26.165  13.134  -0.110  1.00  4.49      1BPT 461
ATOM    355  CD2 PHE    45      25.243  10.988  -0.731  1.00  7.57      1BPT 462
ATOM    356  CE1 PHE    45      27.037  13.057  -1.206  1.00  5.81      1BPT 463
ATOM    357  CE2 PHE    45      26.116  10.886  -1.828  1.00  6.32      1BPT 464
ATOM    358  CZ  PHE    45      27.017  11.915  -2.031  1.00  5.88      1BPT 465
ATOM    359  N   LYS    46      24.017  12.955   4.372  1.00  5.18      1BPT 466
ATOM    360  CA  LYS    46      23.137  13.170   5.515  1.00  7.22      1BPT 467
ATOM    361  C   LYS    46      21.747  13.494   5.037  1.00  8.50      1BPT 468
ATOM    362  O   LYS    46      20.775  13.277   5.777  1.00  8.81      1BPT 469
ATOM    363  CB  LYS    46      23.719  14.097   6.569  1.00 17.67      1BPT 470
ATOM    364  CG  LYS    46      24.807  13.401   7.450  1.00 17.14      1BPT 471
ATOM    365  CD  LYS    46      25.667  14.430   8.162  1.00 22.39      1BPT 472
ATOM    366  CE  LYS    46      26.849  13.763   8.823  1.00 33.75      1BPT 473
ATOM    367  NZ  LYS    46      27.771  13.182   7.778  1.00 39.51      1BPT 474
ATOM    368  N   SER    47      21.567  13.946   3.793  1.00  6.62      1BPT 475
ATOM    369  CA  SER    47      20.237  14.215   3.241  1.00  7.92      1BPT 476
ATOM    370  C   SER    47      20.291  13.788   1.753  1.00  9.35      1BPT 477
ATOM    371  O   SER    47      21.389  13.808   1.198  1.00  6.05      1BPT 478
ATOM    372  CB  SER    47      19.755  15.634   3.248  1.00  8.12      1BPT 479
ATOM    373  OG  SER    47      20.635  16.520   2.615  1.00 10.87      1BPT 480
ATOM    374  N   ALA    48      19.110  13.576   1.248  1.00 13.39      1BPT 481
ATOM    375  CA  ALA    48      18.819  13.216  -0.137  1.00 14.31      1BPT 482
ATOM    376  C   ALA    48      19.222  14.327  -1.097  1.00  9.87      1BPT 483
ATOM    377  O   ALA    48      19.693  14.049  -2.219  1.00 10.59      1BPT 484
ATOM    378  CB  ALA    48      17.317  12.910  -0.257  1.00 14.70      1BPT 485
ATOM    379  N   GLU    49      19.096  15.564  -0.717  1.00 12.65      1BPT 486
ATOM    380  CA  GLU    49      19.425  16.790  -1.459  1.00 16.19      1BPT 487
ATOM    381  C   GLU    49      20.919  16.933  -1.769  1.00 13.71      1BPT 488
ATOM    382  O   GLU    49      21.385  17.262  -2.881  1.00 12.61      1BPT 489
ATOM    383  CB  GLU    49      18.987  18.000  -0.638  1.00 24.93      1BPT 490
ATOM    384  CG  GLU    49      19.603  19.360  -0.977  1.00 32.70      1BPT 491
ATOM    385  CD  GLU    49      18.593  20.478  -0.869  1.00 33.74      1BPT 492
ATOM    386  OE1 GLU    49      17.501  20.301  -0.357  1.00 37.68      1BPT 493
ATOM    387  OE2 GLU    49      19.011  21.524  -1.382  1.00 40.58      1BPT 494
ATOM    388  N   ASP    50      21.678  16.685  -0.752  1.00  8.77      1BPT 495
ATOM    389  CA  ASP    50      23.154  16.618  -0.749  1.00  5.33      1BPT 496
ATOM    390  C   ASP    50      23.557  15.495  -1.741  1.00  7.91      1BPT 497
ATOM    391  O   ASP    50      24.418  15.687  -2.574  1.00 10.59      1BPT 498
ATOM    392  CB  ASP    50      23.469  16.208   0.652  1.00  7.72      1BPT 499
ATOM    393  CG  ASP    50      24.677  16.768   1.310  1.00 22.77      1BPT 500
ATOM    394  OD1 ASP    50      25.784  16.205   1.218  1.00 29.45      1BPT 501
ATOM    395  OD2 ASP    50      24.437  17.805   1.976  1.00 27.42      1BPT 502
ATOM    396  N   CYS    51      22.889  14.372  -1.606  1.00  7.15      1BPT 503
ATOM    397  CA  CYS    51      23.118  13.191  -2.471  1.00  9.78      1BPT 504
ATOM    398  C   CYS    51      22.817  13.463  -3.927  1.00 10.99      1BPT 505
ATOM    399  O   CYS    51      23.624  13.202  -4.878  1.00 10.34      1BPT 506
ATOM    400  CB  CYS    51      22.338  12.044  -1.832  1.00  7.72      1BPT 507
ATOM    401  SG  CYS    51      22.556  10.517  -2.797  1.00  9.28      1BPT 508
ATOM    402  N   MET    52      21.658  14.043  -4.168  1.00 11.69      1BPT 509
ATOM    403  CA  MET    52      21.202  14.431  -5.526  1.00 18.65      1BPT 510
ATOM    404  C   MET    52      22.077  15.525  -6.147  1.00 19.65      1BPT 511
ATOM    405  O   MET    52      22.331  15.528  -7.377  1.00 21.47      1BPT 512
ATOM    406  CB  MET    52      19.733  14.888  -5.520  1.00 18.64      1BPT 513
ATOM    407  CG  MET    52      18.820  13.802  -5.029  1.00 25.08      1BPT 514
ATOM    408  SD  MET    52      18.593  12.518  -6.298  1.00 36.21      1BPT 515
ATOM    409  CE  MET    52      17.140  13.185  -7.164  1.00 31.81      1BPT 516
ATOM    410  N   ARG    53      22.488  16.491  -5.340  1.00 15.68      1BPT 517
ATOM    411  CA  ARG    53      23.357  17.550  -5.895  1.00 14.21      1BPT 518
ATOM    412  C   ARG    53      24.665  16.936  -6.309  1.00 16.12      1BPT 519
ATOM    413  O   ARG    53      25.128  17.198  -7.444  1.00 20.73      1BPT 520
ATOM    414  CB  ARG    53      23.476  18.743  -4.963  1.00 18.66      1BPT 521
ATOM    415  CG  ARG    53      24.712  19.585  -4.904  1.00 20.71      1BPT 522
ATOM    416  CD  ARG    53      24.526  20.881  -4.194  1.00 20.48      1BPT 523
ATOM    417  NE  ARG    53      24.137  20.759  -2.782  1.00 23.67      1BPT 524
ATOM    418  CZ  ARG    53      22.949  21.116  -2.283  1.00 19.89      1BPT 525
ATOM    419  NH1 ARG    53      21.956  21.580  -3.045  1.00 21.51      1BPT 526
ATOM    420  NH2 ARG    53      22.797  21.076  -0.984  1.00 19.67      1BPT 527
ATOM    421  N   THR    54      25.282  16.106  -5.486  1.00 15.94      1BPT 528
ATOM    422  CA  THR    54      26.565  15.457  -5.745  1.00 15.33      1BPT 529
ATOM    423  C   THR    54      26.567  14.390  -6.831  1.00 14.34      1BPT 530
ATOM    424  O   THR    54      27.430  14.320  -7.727  1.00 15.03      1BPT 531
ATOM    425  CB  THR    54      27.103  14.813  -4.378  1.00 15.64      1BPT 532
ATOM    426  OG1 THR    54      26.939  15.842  -3.350  1.00 14.11      1BPT 533
ATOM    427  CG2 THR    54      28.533  14.325  -4.493  1.00 13.03      1BPT 534
ATOM    428  N   CYS    55      25.605  13.478  -6.742  1.00 14.03      1BPT 535
ATOM    429  CA  CYS    55      25.487  12.381  -7.678  1.00 18.90      1BPT 536
ATOM    430  C   CYS    55      24.327  12.243  -8.624  1.00 14.94      1BPT 537
ATOM    431  O   CYS    55      24.416  11.321  -9.464  1.00 17.17      1BPT 538
ATOM    432  CB  CYS    55      25.558  11.073  -6.799  1.00 13.60      1BPT 539
ATOM    433  SG  CYS    55      27.108  10.842  -5.962  1.00 11.32      1BPT 540
ATOM    434  N   GLY    56      23.250  12.959  -8.573  1.00 21.33      1BPT 541
ATOM    435  CA  GLY    56      22.055  12.828  -9.404  1.00 21.71      1BPT 542
ATOM    436  C   GLY    56      22.203  13.318 -10.815  1.00 29.25      1BPT 543
ATOM    437  O   GLY    56      22.062  14.551 -11.007  1.00 36.32      1BPT 544
TER     438      GLY    56                                              1BPT 545
HETATM  439  P   PO4    70      30.706  10.577  10.314  1.00 40.72      1BPT 546
HETATM  440  O1  PO4    70      31.880  11.494  10.318  1.00 40.10      1BPT 547
HETATM  441  O2  PO4    70      29.700  11.094  11.269  1.00 36.93      1BPT 548
HETATM  442  O3  PO4    70      30.132  10.507   8.949  1.00 36.50      1BPT 549
HETATM  443  O4  PO4    70      31.190   9.240  10.783  1.00 33.43      1BPT 550
HETATM  444  O   HOH    80      20.819  13.100   8.431  1.00 24.07      1BPT 551
HETATM  445  O   HOH   102      30.510   0.396  17.550  1.00 19.35      1BPT 552
HETATM  446  O   HOH   110      35.009   6.459  -0.855  1.00 12.67      1BPT 553
HETATM  447  O   HOH   111      30.611   3.654  -0.155  1.00 13.18      1BPT 554
HETATM  448  O   HOH   112      28.828   4.406   1.730  1.00  8.47      1BPT 555
HETATM  449  O   HOH   113      29.841   4.909   4.406  1.00  7.19      1BPT 556
HETATM  450  O   HOH   117      21.848  -0.746   5.060  1.00 16.62      1BPT 557
HETATM  451  O   HOH   119      21.823   5.979 -12.630  1.00 24.84      1BPT 558
HETATM  452  O   HOH   122      30.511   1.654  10.647  1.00  7.89      1BPT 559
HETATM  453  O   HOH   138      25.621  15.094   3.493  1.00 23.48      1BPT 560
HETATM  454  O   HOH   143      26.160   3.139  -5.420  1.00 34.25      1BPT 561
HETATM  455  O   HOH   145      33.316   1.413  18.097  1.00 25.90      1BPT 562
HETATM  456  O   HOH   159      28.583  -2.632   3.791  1.00 39.81      1BPT 563
HETATM  457  O   HOH   160      33.706   3.567  -8.762  1.00 24.53      1BPT 564
HETATM  458  O   HOH   200      14.641   3.645 -11.171  1.00 43.15      1BPT 565
HETATM  459  O   HOH   203      36.110   7.939   7.187  1.00 26.10      1BPT 566
HETATM  460  O   HOH   204      37.573   6.383   4.119  1.00 34.45      1BPT 567
HETATM  461  O   HOH   205      17.114   1.480   5.071  1.00 25.78      1BPT 568
HETATM  462  O   HOH   210      29.293  -0.141  -8.753  1.00 31.97      1BPT 569
HETATM  463  O   HOH   220      38.003  -0.043   7.446  1.00 39.37      1BPT 570
HETATM  464  O   HOH   310      27.894  18.497  -3.763  1.00 43.65      1BPT 571
HETATM  465  O   HOH   400      21.958   7.437  -8.430  1.00 19.20      1BPT 572
HETATM  466  O   HOH   401      31.962   7.677 -12.750  1.00 38.68      1BPT 573
HETATM  467  O   HOH   402      17.664   6.716 -13.231  1.00 33.38      1BPT 574
HETATM  468  O   HOH   403      13.919   2.897  -4.054  1.00 16.38      1BPT 575
HETATM  469  O   HOH   404      21.409  17.309  -9.673  1.00 36.53      1BPT 576
HETATM  470  O   HOH   405      13.834   0.430  16.064  1.00 32.73      1BPT 577
HETATM  471  O   HOH   406      28.339  15.647 -11.514  1.00 41.64      1BPT 578
HETATM  472  O   HOH   407      15.124   9.979  -1.705  1.00 32.62      1BPT 579
HETATM  473  O   HOH   408      15.714   0.107  18.383  1.00 27.81      1BPT 580
HETATM  474  O   HOH   409      28.278  14.368 -14.656  1.00 28.15      1BPT 581
HETATM  475  O   HOH   410      15.105   5.054   0.515  1.00 23.38      1BPT 582
HETATM  476  O   HOH   411      23.761  -2.671   7.342  1.00 35.33      1BPT 583
HETATM  477  O   HOH   412      32.010  -0.303  -0.690  1.00 43.06      1BPT 584
HETATM  478  O   HOH   413      25.967  19.801  -1.055  1.00 37.89      1BPT 585
HETATM  479  O   HOH   414      35.741   2.717  -2.480  1.00 39.48      1BPT 586
HETATM  480  O   HOH   415      22.383  20.755   1.804  1.00 31.50      1BPT 587
HETATM  481  O   HOH   416      26.289  11.963 -15.860  1.00 40.37      1BPT 588
HETATM  482  O   HOH   417      28.681  15.680  -0.316  1.00 48.97      1BPT 589
HETATM  483  O   HOH   418      28.804  19.336  -6.207  1.00 36.73      1BPT 590
CONECT   43   42  433                                                   1BPT 591
CONECT  110  109  295                                                   1BPT 592
CONECT  235  234  401                                                   1BPT 593
CONECT  295  110  294                                                   1BPT 594
CONECT  401  235  400                                                   1BPT 595
CONECT  433   43  432                                                   1BPT 596
CONECT  439  440  441  442  443                                         1BPT 597
CONECT  440  439                                                        1BPT 598
CONECT  441  439                                                        1BPT 599
CONECT  442  439                                                        1BPT 600
CONECT  443  439                                                        1BPT 601
MASTER       71    0    1    2    3    0    0    6  482    1   11    5  1BPT 602
END                                                                     1BPT 603



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