DOMAINER documentation


 

CONTENTS

1.0 SUMMARY
2.0 INPUTS & OUTPUTS
3.0 INPUT FILE FORMAT
4.0 OUTPUT FILE FORMAT
5.0 DATA FILES
6.0 USAGE
7.0 KNOWN BUGS & WARNINGS
8.0 NOTES
9.0 DESCRIPTION
10.0 ALGORITHM
11.0 RELATED APPLICATIONS
12.0 DIAGNOSTIC ERROR MESSAGES
13.0 AUTHORS
14.0 REFERENCES



1.0 SUMMARY

Generates domain CCF files from protein CCF files


2.0 INPUTS & OUTPUTS

DOMAINER reads a DCF file (domain classification file) and a directory of protein CCF files (clean coordinate files) and writes, for each domain in the DCF file, a domain CCF file and domain PDB file. Each domain CCF file contains coordinates for a single SCOP domain. The paths and extensions for the protein (input) and domain (output) coordinate files are specified by the user (path) and in the ACD file (extension). The SCOP domain identifier codes are used to name the output files. A log file for each of the DCF and PDB format builds is written.


3.0 INPUT FILE FORMAT

The format of the protein CCF file is described in the PDBPARSE documentation.

Input files for usage example

File: ../scopparse-keep/all.scop

ID   D1CS4A_
XX
EN   1CS4
XX
TY   SCOP
XX
SI   53931 CL; 54861 FO; 55073 SF; 55074 FA; 55077 DO; 55078 SO; 39418 DD;
XX
CL   Alpha and beta proteins (a+b)
XX
FO   Ferredoxin-like
XX
SF   Adenylyl and guanylyl cyclase catalytic domain
XX
FA   Adenylyl and guanylyl cyclase catalytic domain
XX
DO   Adenylyl cyclase VC1, domain C1a
XX
OS   Dog (Canis familiaris)
XX
NC   1
XX
CN   [1]
XX
CH   A CHAIN; . START; . END;
//
ID   D1II7A_
XX
EN   1II7
XX
TY   SCOP
XX
SI   53931 CL; 56299 FO; 56300 SF; 64427 FA; 64428 DO; 64429 SO; 62415 DD;
XX
CL   Alpha and beta proteins (a+b)
XX
FO   Metallo-dependent phosphatases
XX
SF   Metallo-dependent phosphatases
XX
FA   DNA double-strand break repair nuclease
XX
DO   Mre11
XX
OS   Archaeon Pyrococcus furiosus
XX
NC   1
XX
CN   [1]
XX
CH   A CHAIN; . START; . END;
//




4.0 OUTPUT FILE FORMAT

The format used for domain CCF files is exactly the same as that used for protein CCF files and is described the PDBPARSE documentation.

Output files for usage example

File: domainer_embl.log





File: domainer_pdb.log








File: d1cs4a_.ent




HEADER     CLEANED-UP PDB FILE FOR SCOP DOMAIN D1CS4A_                          
TITLE      THIS FILE IS MISSING MOST RECORDS FROM THE ORIGINAL PDB FILE         
COMPND     MOL_ID: 1; MOLECULE: TYPE V ADENYLATE CYCLASE;                       
SOURCE     MOL_ID: 1; ORGANISM_SCIENTIFIC: CANIS FAMILIARIS;                    
REMARK                                                                          
REMARK     RESOLUTION. 2.50  ANGSTROMS.                                         
REMARK                                                                          
SEQRES   1 A   52  ALA ASP ILE GLU GLY PHE THR SER LEU ALA SER GLN CYS          
SEQRES   2 A   52  THR ALA GLN GLU LEU VAL MET THR LEU ASN GLU LEU PHE          
SEQRES   3 A   52  ALA ARG PHE ASP LYS LEU ALA ALA GLU ASN HIS CYS LEU          
SEQRES   4 A   52  ARG ILE LYS ILE LEU GLY ASP CYS TYR TYR CYS VAL SER          
ATOM      1  N   ASP A 396      51.711 -11.782  62.798  1.00 51.17           N  
ATOM      2  CA  ASP A 396      52.810 -11.644  61.848  1.00 54.45           C  
ATOM      3  C   ASP A 396      54.137 -11.314  62.530  1.00 55.11           C  
ATOM      4  O   ASP A 396      54.175 -10.524  63.469  1.00 55.34           O  
ATOM      5  CB  ASP A 396      52.437 -10.555  60.831  1.00 57.50           C  
ATOM      6  CG  ASP A 396      53.460 -10.391  59.729  1.00 61.38           C  
ATOM      7  OD1 ASP A 396      54.316  -9.485  59.841  1.00 65.55           O  
ATOM      8  OD2 ASP A 396      53.390 -11.146  58.736  1.00 63.68           O  
ATOM      9  N   ILE A 397      55.216 -11.941  62.066  1.00 57.14           N  
ATOM     10  CA  ILE A 397      56.546 -11.705  62.624  1.00 59.46           C  
ATOM     11  C   ILE A 397      57.020 -10.305  62.230  1.00 60.12           C  
ATOM     12  O   ILE A 397      56.963  -9.927  61.060  1.00 59.12           O  
ATOM     13  CB  ILE A 397      57.583 -12.722  62.094  1.00 60.84           C  
ATOM     14  CG1 ILE A 397      57.184 -14.163  62.447  1.00 63.12           C  
ATOM     15  CG2 ILE A 397      58.975 -12.384  62.632  1.00 61.24           C  
ATOM     16  CD1 ILE A 397      57.408 -14.554  63.895  1.00 63.92           C  
ATOM     17  N   GLU A 398      57.492  -9.548  63.212  1.00 60.23           N  
ATOM     18  CA  GLU A 398      57.975  -8.198  62.971  1.00 62.14           C  
ATOM     19  C   GLU A 398      59.401  -8.277  62.424  1.00 60.59           C  
ATOM     20  O   GLU A 398      60.244  -8.972  62.987  1.00 61.84           O  
ATOM     21  CB  GLU A 398      57.917  -7.386  64.272  1.00 65.47           C  
ATOM     22  CG  GLU A 398      58.037  -5.874  64.091  1.00 70.25           C  
ATOM     23  CD  GLU A 398      57.588  -5.089  65.324  1.00 72.94           C  
ATOM     24  OE1 GLU A 398      58.262  -5.175  66.377  1.00 70.76           O  
ATOM     25  OE2 GLU A 398      56.555  -4.380  65.232  1.00 74.36           O  
ATOM     26  N   GLY A 399      59.642  -7.608  61.298  1.00 57.58           N  
ATOM     27  CA  GLY A 399      60.956  -7.615  60.681  1.00 56.14           C  
ATOM     28  C   GLY A 399      61.452  -8.993  60.265  1.00 58.03           C  
ATOM     29  O   GLY A 399      62.620  -9.322  60.480  1.00 57.47           O  
ATOM     30  N   PHE A 400      60.576  -9.789  59.649  1.00 58.00           N  
ATOM     31  CA  PHE A 400      60.914 -11.143  59.200  1.00 58.07           C  
ATOM     32  C   PHE A 400      61.995 -11.219  58.117  1.00 58.57           C  
ATOM     33  O   PHE A 400      62.862 -12.091  58.161  1.00 59.44           O  
ATOM     34  CB  PHE A 400      59.657 -11.881  58.734  1.00 59.18           C  
ATOM     35  CG  PHE A 400      59.900 -13.316  58.322  1.00 58.53           C  
ATOM     36  CD1 PHE A 400      60.377 -14.251  59.237  1.00 57.59           C  
ATOM     37  CD2 PHE A 400      59.613 -13.736  57.024  1.00 57.95           C  
ATOM     38  CE1 PHE A 400      60.557 -15.583  58.864  1.00 59.98           C  
ATOM     39  CE2 PHE A 400      59.790 -15.063  56.643  1.00 58.52           C  


  [Part of this file has been deleted for brevity]

ATOM    308  C   ILE A 435      45.128 -21.768  57.354  1.00 49.27           C  
ATOM    309  O   ILE A 435      45.316 -22.911  56.925  1.00 50.94           O  
ATOM    310  CB  ILE A 435      43.255 -20.038  57.551  1.00 47.15           C  
ATOM    311  CG1 ILE A 435      41.973 -19.706  58.315  1.00 45.98           C  
ATOM    312  CG2 ILE A 435      42.947 -20.058  56.062  1.00 48.42           C  
ATOM    313  CD1 ILE A 435      40.863 -20.738  58.156  1.00 43.91           C  
ATOM    314  N   LYS A 436      46.066 -20.824  57.308  1.00 48.78           N  
ATOM    315  CA  LYS A 436      47.382 -21.114  56.741  1.00 45.74           C  
ATOM    316  C   LYS A 436      48.551 -20.279  57.227  1.00 44.92           C  
ATOM    317  O   LYS A 436      48.382 -19.355  58.023  1.00 45.05           O  
ATOM    318  CB  LYS A 436      47.364 -21.306  55.217  1.00 47.03           C  
ATOM    319  CG  LYS A 436      46.733 -20.214  54.377  1.00 45.37           C  
ATOM    320  CD  LYS A 436      46.225 -20.811  53.058  1.00 40.72           C  
ATOM    321  CE  LYS A 436      46.260 -19.807  51.913  1.00 44.25           C  
ATOM    322  NZ  LYS A 436      45.622 -20.326  50.664  1.00 45.35           N  
ATOM    323  N   ILE A 437      49.751 -20.706  56.849  1.00 44.66           N  
ATOM    324  CA  ILE A 437      50.969 -20.017  57.239  1.00 45.23           C  
ATOM    325  C   ILE A 437      51.637 -19.439  55.998  1.00 46.08           C  
ATOM    326  O   ILE A 437      52.033 -20.177  55.093  1.00 48.18           O  
ATOM    327  CB  ILE A 437      51.950 -20.971  57.958  1.00 45.87           C  
ATOM    328  CG1 ILE A 437      51.241 -21.704  59.099  1.00 46.15           C  
ATOM    329  CG2 ILE A 437      53.147 -20.193  58.503  1.00 43.43           C  
ATOM    330  CD1 ILE A 437      52.124 -22.722  59.814  1.00 46.81           C  
ATOM    331  N   LEU A 438      51.729 -18.114  55.951  1.00 46.84           N  
ATOM    332  CA  LEU A 438      52.348 -17.415  54.830  1.00 44.42           C  
ATOM    333  C   LEU A 438      53.758 -16.989  55.211  1.00 44.90           C  
ATOM    334  O   LEU A 438      54.061 -15.795  55.283  1.00 42.12           O  
ATOM    335  CB  LEU A 438      51.507 -16.200  54.427  1.00 41.59           C  
ATOM    336  CG  LEU A 438      50.063 -16.485  54.001  1.00 42.78           C  
ATOM    337  CD1 LEU A 438      49.345 -15.182  53.690  1.00 41.92           C  
ATOM    338  CD2 LEU A 438      49.993 -17.430  52.810  1.00 39.08           C  
ATOM    339  N   GLY A 439      54.619 -17.980  55.437  1.00 46.64           N  
ATOM    340  CA  GLY A 439      55.996 -17.717  55.814  1.00 48.31           C  
ATOM    341  C   GLY A 439      56.099 -17.326  57.273  1.00 49.55           C  
ATOM    342  O   GLY A 439      56.500 -18.130  58.108  1.00 50.85           O  
ATOM    343  N   ASP A 440      55.690 -16.096  57.569  1.00 51.02           N  
ATOM    344  CA  ASP A 440      55.712 -15.540  58.917  1.00 50.96           C  
ATOM    345  C   ASP A 440      54.334 -15.024  59.352  1.00 50.15           C  
ATOM    346  O   ASP A 440      54.193 -14.464  60.438  1.00 51.63           O  
ATOM    347  CB  ASP A 440      56.724 -14.394  58.985  1.00 51.43           C  
ATOM    348  CG  ASP A 440      56.280 -13.162  58.196  1.00 55.29           C  
ATOM    349  OD1 ASP A 440      56.528 -12.030  58.669  1.00 57.12           O  
ATOM    350  OD2 ASP A 440      55.685 -13.319  57.108  1.00 52.55           O  
ATOM    351  N   CYS A 441      53.333 -15.191  58.493  1.00 49.26           N  
ATOM    352  CA  CYS A 441      51.971 -14.737  58.775  1.00 49.62           C  
ATOM    353  C   CYS A 441      51.077 -15.923  59.132  1.00 48.96           C  
ATOM    354  O   CYS A 441      50.803 -16.789  58.301  1.00 50.50           O  
ATOM    355  CB  CYS A 441      51.409 -13.972  57.565  1.00 51.82           C  
ATOM    356  SG  CYS A 441      49.727 -13.277  57.723  1.00 54.53           S  
TER     357      CYS A  47                                                      
END                                                                             





File: d1cs4a_.ccf




ID   D1CS4A_
XX
DE   Co-ordinates for SCOP domain D1CS4A_
XX
OS   See Escop.dat for domain classification
XX
EX   METHOD xray; RESO 2.50; NMOD 1; NCHN 1; NGRP 0;
XX
CN   [1]
XX
IN   ID A; NRES 52; NL 0; NH 0; NE 2;
XX
SQ   SEQUENCE    52 AA;   5817 MW;  D8CCAE0E1FC0849A CRC64;
     ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR IKILGDCYYC VS
XX
RE   1    1    2    396   D ASP   .    .    .    .    .    C      360.00  138.76  146.70  139.38   99.30   65.52   63.80   73.85  195.90   37.10   75.30  102.28  112.20
RE   1    1    3    397   I ILE   .    .    .    .    .    T      -70.66  130.71   41.60   42.25   24.10   39.03   28.30    3.22    8.70   39.03   28.10    3.22    9.00
RE   1    1    4    398   E GLU   .    .    .    .    .    T      -80.63  128.14  189.80  172.42  100.10  152.25  113.00   20.18   53.80   71.11  118.00  101.31   90.50
RE   1    1    5    399   G GLY   1    1    H    1    .    T       60.62   44.06   47.30   46.32   57.80   33.67  104.20   12.64   26.50   33.67   89.70   12.64   29.70
RE   1    1    6    400   F PHE   1    1    H    1    1    H      -63.71  -43.06   38.10   42.33   21.20   38.88   23.70    3.46    9.80   38.88   23.50    3.46   10.10
RE   1    1    7    401   T THR   1    1    H    1    1    H      -63.13  -33.45  122.50  117.00   84.00  113.46  111.60    3.54    9.40   81.54  107.70   35.46   55.80
RE   1    1    8    402   S SER   1    1    H    1    1    H      -69.61  -44.64   76.80   69.25   59.40   66.11   84.60    3.14    8.20   36.50   75.20   32.75   48.20
RE   1    1    9    403   L LEU   1    1    H    1    1    H      -63.95  -53.38   81.30   81.72   45.70   81.25   57.60    0.47    1.30   81.25   57.10    0.47    1.30
RE   1    1    10   404   A ALA   1    1    H    1    1    H      -67.72  -13.25   35.90   35.58   33.00   16.63   24.00   18.95   49.20   18.20   25.50   17.38   47.50
RE   1    1    11   405   S SER   1    1    H    1    .    T      -82.48  -15.19  100.90   90.08   77.30   61.12   78.20   28.96   75.40   25.90   53.40   64.18   94.40
RE   1    1    12   406   Q GLN   .    .    .    .    .    T      -95.87  -61.03  151.90  142.66   79.90  109.97   78.00   32.69   87.10   49.16   94.10   93.49   74.00
RE   1    1    13   407   C CYS   .    .    .    .    .    T      -79.87  165.96   32.00   36.35   27.10   27.88   28.80    8.47   22.60   29.04   29.70    7.31   20.10
RE   1    1    14   408   T THR   2    2    H    1    .    C      -67.21  155.23   79.50   78.09   56.10   73.27   72.00    4.82   12.80   53.17   70.20   24.92   39.20
RE   1    1    15   409   A ALA   2    2    H    1    2    H      -61.46  -26.61   74.80   80.21   74.30   71.49  103.00    8.72   22.60   72.91  102.10    7.31   20.00
RE   1    1    16   410   Q GLN   2    2    H    1    2    H      -69.67  -54.28  138.50  127.16   71.20  124.25   88.10    2.91    7.80   46.24   88.60   80.92   64.10
RE   1    1    17   411   E GLU   2    2    H    1    2    H      -57.11  -42.09  104.70   89.88   52.20   89.35   66.30    0.53    1.40   31.77   52.70   58.11   51.90
RE   1    1    18   412   L LEU   2    2    H    1    2    H      -57.70  -47.91   25.70   25.00   14.00   25.00   17.70    0.00    0.00   25.00   17.60    0.00    0.00
RE   1    1    19   413   V VAL   2    2    H    1    2    H      -66.05  -30.11   88.20   90.90   60.00   90.80   79.50    0.10    0.30   90.90   78.70    0.00    0.00
RE   1    1    20   414   M MET   2    2    H    1    2    H      -69.27  -42.21  124.20  127.92   65.90  122.84   78.40    5.08   13.50  124.37   78.80    3.54    9.80
RE   1    1    21   415   T THR   2    2    H    1    2    H      -65.51  -37.49   81.70   78.15   56.10   76.18   74.90    1.96    5.20   56.58   74.70   21.56   33.90
RE   1    1    22   416   L LEU   2    2    H    1    2    H      -74.87  -41.05   26.30   23.57   13.20   23.31   16.50    0.26    0.70   23.57   16.60    0.00    0.00
RE   1    1    23   417   N ASN   2    2    H    1    2    H      -67.86  -35.26  113.60  101.30   70.40   99.87   94.00    1.43    3.80   18.39   39.80   82.91   84.80
RE   1    1    24   418   E GLU   2    2    H    1    2    H      -65.83  -40.82  113.30  100.53   58.40   99.74   74.00    0.79    2.10   38.76   64.30   61.77   55.20
RE   1    1    25   419   L LEU   2    2    H    1    2    H      -72.73  -52.39   57.40   57.47   32.20   57.33   40.60    0.14    0.40   57.33   40.30    0.14    0.40
RE   1    1    26   420   F PHE   2    2    H    1    2    H      -70.80  -21.35   27.00   28.81   14.40   27.76   16.90    1.06    3.00   28.81   17.40    0.00    0.00
RE   1    1    27   421   A ALA   2    2    H    1    2    H      -69.34  -45.28   29.90   35.82   33.20   34.83   50.20    1.00    2.60   34.83   48.80    1.00    2.70
RE   1    1    28   422   R ARG   2    2    H    1    2    H      -61.82  -45.79  136.10  134.66   56.40  134.62   66.90    0.03    0.10   47.36   60.90   87.30   54.20
RE   1    1    29   423   F PHE   2    2    H    1    2    H      -57.44  -43.57  101.50   99.54   49.90   95.45   58.20    4.09   11.60   96.26   58.30    3.28    9.60
RE   1    1    30   424   D ASP   2    2    H    1    2    H      -62.18  -31.31   60.50   54.34   38.70   42.49   41.40   11.84   31.40   25.02   50.80   29.31   32.20
RE   1    1    31   425   K LYS   2    2    H    1    2    H      -78.40  -41.15  135.60  131.47   65.50  129.94   79.60    1.53    4.10   94.19   80.80   37.29   44.30
RE   1    1    32   426   L LEU   2    2    H    1    2    H      -64.72  -26.22   81.20   86.96   48.70   86.30   61.20    0.66    1.80   86.96   61.10    0.00    0.00
RE   1    1    33   427   A ALA   2    2    H    1    2    H      -69.69  -37.04   17.80   18.88   17.50   18.70   26.90    0.18    0.50   18.70   26.20    0.18    0.50
RE   1    1    34   428   A ALA   2    2    H    1    2    H      -70.19  -38.47   77.30   79.34   73.50   60.25   86.80   19.09   49.50   61.54   86.20   17.79   48.60
RE   1    1    35   429   E GLU   2    2    H    1    2    H      -66.66  -43.34  133.10  123.38   71.60  108.84   80.80   14.54   38.80   51.79   85.90   71.59   63.90
RE   1    1    36   430   N ASN   2    2    H    1    2    H      -85.82   10.44  105.20   96.15   66.80   83.39   78.50   12.75   33.80   21.86   47.30   74.28   76.00


  [Part of this file has been deleted for brevity]

AT   1    1    .    41   435   I ILE   P CA       43.791  -21.405   58.007    1.00   47.94
AT   1    1    .    41   435   I ILE   P C        45.128  -21.768   57.354    1.00   49.27
AT   1    1    .    41   435   I ILE   P O        45.316  -22.911   56.925    1.00   50.94
AT   1    1    .    41   435   I ILE   P CB       43.255  -20.038   57.551    1.00   47.15
AT   1    1    .    41   435   I ILE   P CG1      41.973  -19.706   58.315    1.00   45.98
AT   1    1    .    41   435   I ILE   P CG2      42.947  -20.058   56.062    1.00   48.42
AT   1    1    .    41   435   I ILE   P CD1      40.863  -20.738   58.156    1.00   43.91
AT   1    1    .    42   436   K LYS   P N        46.066  -20.824   57.308    1.00   48.78
AT   1    1    .    42   436   K LYS   P CA       47.382  -21.114   56.741    1.00   45.74
AT   1    1    .    42   436   K LYS   P C        48.551  -20.279   57.227    1.00   44.92
AT   1    1    .    42   436   K LYS   P O        48.382  -19.355   58.023    1.00   45.05
AT   1    1    .    42   436   K LYS   P CB       47.364  -21.306   55.217    1.00   47.03
AT   1    1    .    42   436   K LYS   P CG       46.733  -20.214   54.377    1.00   45.37
AT   1    1    .    42   436   K LYS   P CD       46.225  -20.811   53.058    1.00   40.72
AT   1    1    .    42   436   K LYS   P CE       46.260  -19.807   51.913    1.00   44.25
AT   1    1    .    42   436   K LYS   P NZ       45.622  -20.326   50.664    1.00   45.35
AT   1    1    .    43   437   I ILE   P N        49.751  -20.706   56.849    1.00   44.66
AT   1    1    .    43   437   I ILE   P CA       50.969  -20.017   57.239    1.00   45.23
AT   1    1    .    43   437   I ILE   P C        51.637  -19.439   55.998    1.00   46.08
AT   1    1    .    43   437   I ILE   P O        52.033  -20.177   55.093    1.00   48.18
AT   1    1    .    43   437   I ILE   P CB       51.950  -20.971   57.958    1.00   45.87
AT   1    1    .    43   437   I ILE   P CG1      51.241  -21.704   59.099    1.00   46.15
AT   1    1    .    43   437   I ILE   P CG2      53.147  -20.193   58.503    1.00   43.43
AT   1    1    .    43   437   I ILE   P CD1      52.124  -22.722   59.814    1.00   46.81
AT   1    1    .    44   438   L LEU   P N        51.729  -18.114   55.951    1.00   46.84
AT   1    1    .    44   438   L LEU   P CA       52.348  -17.415   54.830    1.00   44.42
AT   1    1    .    44   438   L LEU   P C        53.758  -16.989   55.211    1.00   44.90
AT   1    1    .    44   438   L LEU   P O        54.061  -15.795   55.283    1.00   42.12
AT   1    1    .    44   438   L LEU   P CB       51.507  -16.200   54.427    1.00   41.59
AT   1    1    .    44   438   L LEU   P CG       50.063  -16.485   54.001    1.00   42.78
AT   1    1    .    44   438   L LEU   P CD1      49.345  -15.182   53.690    1.00   41.92
AT   1    1    .    44   438   L LEU   P CD2      49.993  -17.430   52.810    1.00   39.08
AT   1    1    .    45   439   G GLY   P N        54.619  -17.980   55.437    1.00   46.64
AT   1    1    .    45   439   G GLY   P CA       55.996  -17.717   55.814    1.00   48.31
AT   1    1    .    45   439   G GLY   P C        56.099  -17.326   57.273    1.00   49.55
AT   1    1    .    45   439   G GLY   P O        56.500  -18.130   58.108    1.00   50.85
AT   1    1    .    46   440   D ASP   P N        55.690  -16.096   57.569    1.00   51.02
AT   1    1    .    46   440   D ASP   P CA       55.712  -15.540   58.917    1.00   50.96
AT   1    1    .    46   440   D ASP   P C        54.334  -15.024   59.352    1.00   50.15
AT   1    1    .    46   440   D ASP   P O        54.193  -14.464   60.438    1.00   51.63
AT   1    1    .    46   440   D ASP   P CB       56.724  -14.394   58.985    1.00   51.43
AT   1    1    .    46   440   D ASP   P CG       56.280  -13.162   58.196    1.00   55.29
AT   1    1    .    46   440   D ASP   P OD1      56.528  -12.030   58.669    1.00   57.12
AT   1    1    .    46   440   D ASP   P OD2      55.685  -13.319   57.108    1.00   52.55
AT   1    1    .    47   441   C CYS   P N        53.333  -15.191   58.493    1.00   49.26
AT   1    1    .    47   441   C CYS   P CA       51.971  -14.737   58.775    1.00   49.62
AT   1    1    .    47   441   C CYS   P C        51.077  -15.923   59.132    1.00   48.96
AT   1    1    .    47   441   C CYS   P O        50.803  -16.789   58.301    1.00   50.50
AT   1    1    .    47   441   C CYS   P CB       51.409  -13.972   57.565    1.00   51.82
AT   1    1    .    47   441   C CYS   P SG       49.727  -13.277   57.723    1.00   54.53
//





File: d1ii7a_.ent




HEADER     CLEANED-UP PDB FILE FOR SCOP DOMAIN D1II7A_                          
TITLE      THIS FILE IS MISSING MOST RECORDS FROM THE ORIGINAL PDB FILE         
COMPND     MOL_ID: 1; MOLECULE: MRE11 NUCLEASE;                                 
SOURCE     MOL_ID: 1; ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;                 
REMARK                                                                          
REMARK     RESOLUTION. 2.20  ANGSTROMS.                                         
REMARK                                                                          
SEQRES   1 A   65  MET LYS PHE ALA HIS LEU ALA ASP ILE HIS LEU GLY TYR          
SEQRES   2 A   65  GLU GLN PHE HIS LYS PRO GLN ARG GLU GLU GLU PHE ALA          
SEQRES   3 A   65  GLU ALA PHE LYS ASN ALA LEU GLU ILE ALA VAL GLN GLU          
SEQRES   4 A   65  ASN VAL ASP PHE ILE LEU ILE ALA GLY ASP LEU PHE HIS          
SEQRES   5 A   65  SER SER ARG PRO SER PRO GLY THR LEU LYS LYS ALA ILE          
ATOM      1  N   ASP A   8       7.977  32.254  19.055  1.00 26.65           N  
ATOM      2  CA  ASP A   8       8.882  31.149  19.290  1.00 28.34           C  
ATOM      3  C   ASP A   8      10.273  31.305  18.659  1.00 27.71           C  
ATOM      4  O   ASP A   8      10.740  30.453  17.907  1.00 29.27           O  
ATOM      5  CB  ASP A   8       8.186  29.886  18.777  1.00 30.25           C  
ATOM      6  CG  ASP A   8       6.918  29.584  19.554  1.00 34.25           C  
ATOM      7  OD1 ASP A   8       7.041  29.177  20.724  1.00 33.37           O  
ATOM      8  OD2 ASP A   8       5.801  29.770  19.010  1.00 35.77           O  
ATOM      9  N   ILE A   9      10.913  32.423  18.967  1.00 26.84           N  
ATOM     10  CA  ILE A   9      12.236  32.739  18.477  1.00 26.52           C  
ATOM     11  C   ILE A   9      13.285  31.864  19.173  1.00 28.22           C  
ATOM     12  O   ILE A   9      14.257  31.426  18.550  1.00 28.01           O  
ATOM     13  CB  ILE A   9      12.520  34.214  18.759  1.00 27.25           C  
ATOM     14  CG1 ILE A   9      11.338  35.051  18.249  1.00 26.35           C  
ATOM     15  CG2 ILE A   9      13.823  34.640  18.094  1.00 26.40           C  
ATOM     16  CD1 ILE A   9      11.011  34.845  16.725  1.00 25.85           C  
ATOM     17  N   HIS A  10      13.072  31.599  20.462  1.00 26.69           N  
ATOM     18  CA  HIS A  10      14.009  30.787  21.254  1.00 28.02           C  
ATOM     19  C   HIS A  10      15.483  31.203  21.181  1.00 27.57           C  
ATOM     20  O   HIS A  10      16.357  30.359  21.019  1.00 23.99           O  
ATOM     21  CB  HIS A  10      13.867  29.284  20.899  1.00 27.15           C  
ATOM     22  CG  HIS A  10      12.599  28.681  21.415  1.00 28.59           C  
ATOM     23  ND1 HIS A  10      12.536  27.980  22.603  1.00 30.06           N  
ATOM     24  CD2 HIS A  10      11.319  28.794  20.978  1.00 26.35           C  
ATOM     25  CE1 HIS A  10      11.276  27.691  22.875  1.00 27.36           C  
ATOM     26  NE2 HIS A  10      10.519  28.180  21.909  1.00 28.44           N  
ATOM     27  N   LEU A  11      15.758  32.503  21.303  1.00 26.85           N  
ATOM     28  CA  LEU A  11      17.152  32.972  21.286  1.00 27.57           C  
ATOM     29  C   LEU A  11      17.879  32.257  22.409  1.00 28.11           C  
ATOM     30  O   LEU A  11      17.323  32.093  23.505  1.00 29.47           O  
ATOM     31  CB  LEU A  11      17.225  34.494  21.530  1.00 25.89           C  
ATOM     32  CG  LEU A  11      16.526  35.348  20.465  1.00 23.73           C  
ATOM     33  CD1 LEU A  11      16.604  36.805  20.823  1.00 24.72           C  
ATOM     34  CD2 LEU A  11      17.179  35.102  19.081  1.00 22.96           C  
ATOM     35  N   GLY A  12      19.113  31.830  22.152  1.00 28.05           N  
ATOM     36  CA  GLY A  12      19.871  31.143  23.179  1.00 29.54           C  
ATOM     37  C   GLY A  12      19.713  29.623  23.181  1.00 31.92           C  
ATOM     38  O   GLY A  12      20.382  28.937  23.948  1.00 32.60           O  


  [Part of this file has been deleted for brevity]

ATOM    305  N   ILE A  44       5.655  45.232  15.043  1.00 33.36           N  
ATOM    306  CA  ILE A  44       6.014  43.831  15.094  1.00 31.77           C  
ATOM    307  C   ILE A  44       5.453  43.198  16.344  1.00 30.94           C  
ATOM    308  O   ILE A  44       5.512  43.792  17.415  1.00 33.03           O  
ATOM    309  CB  ILE A  44       7.565  43.721  15.081  1.00 32.37           C  
ATOM    310  CG1 ILE A  44       8.089  44.316  13.772  1.00 30.80           C  
ATOM    311  CG2 ILE A  44       8.025  42.282  15.324  1.00 28.46           C  
ATOM    312  CD1 ILE A  44       9.598  44.467  13.698  1.00 31.28           C  
ATOM    313  N   LEU A  45       4.884  42.008  16.199  1.00 28.70           N  
ATOM    314  CA  LEU A  45       4.353  41.265  17.326  1.00 26.34           C  
ATOM    315  C   LEU A  45       5.192  40.020  17.558  1.00 30.16           C  
ATOM    316  O   LEU A  45       5.498  39.290  16.600  1.00 29.17           O  
ATOM    317  CB  LEU A  45       2.947  40.775  17.043  1.00 26.78           C  
ATOM    318  CG  LEU A  45       1.836  41.790  16.769  1.00 29.15           C  
ATOM    319  CD1 LEU A  45       0.527  41.024  16.428  1.00 25.64           C  
ATOM    320  CD2 LEU A  45       1.662  42.668  18.008  1.00 25.27           C  
ATOM    321  N   ILE A  46       5.543  39.761  18.814  1.00 28.08           N  
ATOM    322  CA  ILE A  46       6.290  38.558  19.155  1.00 28.84           C  
ATOM    323  C   ILE A  46       5.452  37.904  20.240  1.00 29.18           C  
ATOM    324  O   ILE A  46       5.461  38.305  21.416  1.00 27.33           O  
ATOM    325  CB  ILE A  46       7.727  38.853  19.664  1.00 29.60           C  
ATOM    326  CG1 ILE A  46       8.493  39.680  18.626  1.00 27.78           C  
ATOM    327  CG2 ILE A  46       8.457  37.542  19.893  1.00 27.75           C  
ATOM    328  CD1 ILE A  46       9.988  39.865  18.927  1.00 28.95           C  
ATOM    329  N   ALA A  47       4.700  36.902  19.798  1.00 29.10           N  
ATOM    330  CA  ALA A  47       3.770  36.163  20.619  1.00 26.51           C  
ATOM    331  C   ALA A  47       4.372  35.106  21.553  1.00 27.03           C  
ATOM    332  O   ALA A  47       3.939  33.951  21.580  1.00 27.39           O  
ATOM    333  CB  ALA A  47       2.691  35.541  19.702  1.00 26.11           C  
ATOM    334  N   GLY A  48       5.381  35.500  22.316  1.00 26.07           N  
ATOM    335  CA  GLY A  48       5.935  34.587  23.293  1.00 27.20           C  
ATOM    336  C   GLY A  48       7.112  33.736  22.884  1.00 29.30           C  
ATOM    337  O   GLY A  48       7.283  33.381  21.709  1.00 29.25           O  
ATOM    338  N   ASP A  49       7.899  33.373  23.889  1.00 28.57           N  
ATOM    339  CA  ASP A  49       9.091  32.554  23.699  1.00 28.10           C  
ATOM    340  C   ASP A  49      10.100  33.250  22.827  1.00 27.16           C  
ATOM    341  O   ASP A  49      10.601  32.676  21.869  1.00 29.08           O  
ATOM    342  CB  ASP A  49       8.735  31.200  23.093  1.00 27.86           C  
ATOM    343  CG  ASP A  49       8.155  30.221  24.124  1.00 32.19           C  
ATOM    344  OD1 ASP A  49       7.861  29.073  23.740  1.00 29.67           O  
ATOM    345  OD2 ASP A  49       7.992  30.586  25.313  1.00 31.41           O  
ATOM    346  N   LEU A  50      10.375  34.509  23.128  1.00 27.16           N  
ATOM    347  CA  LEU A  50      11.393  35.247  22.386  1.00 27.68           C  
ATOM    348  C   LEU A  50      12.754  34.607  22.792  1.00 27.01           C  
ATOM    349  O   LEU A  50      13.642  34.421  21.963  1.00 27.43           O  
ATOM    350  CB  LEU A  50      11.351  36.724  22.771  1.00 28.02           C  
ATOM    351  CG  LEU A  50      12.576  37.551  22.355  1.00 30.11           C  
ATOM    352  CD1 LEU A  50      12.751  37.437  20.827  1.00 28.61           C  
ATOM    353  CD2 LEU A  50      12.425  39.035  22.798  1.00 23.77           C  
TER     354      LEU A  50                                                      
END                                                                             





File: d1ii7a_.ccf




ID   D1II7A_
XX
DE   Co-ordinates for SCOP domain D1II7A_
XX
OS   See Escop.dat for domain classification
XX
EX   METHOD xray; RESO 2.20; NMOD 1; NCHN 1; NGRP 0;
XX
CN   [1]
XX
IN   ID A; NRES 65; NL 0; NH 0; NE 1;
XX
SQ   SEQUENCE    65 AA;   7395 MW;  75FBE75B22FD3678 CRC64;
     MKFAHLADIH LGYEQFHKPQ REEEFAEAFK NALEIAVQEN VDFILIAGDL FHSSRPSPGT
     LKKAI
XX
RE   1    1    8    8     D ASP   .    .    .    .    .    C      360.00   53.69  128.30  117.77   83.90   84.46   82.20   33.31   88.40   34.39   69.80   83.38   91.50
RE   1    1    9    9     I ILE   .    .    .    .    .    C      -72.50  -37.00   42.90   42.38   24.20   41.07   29.80    1.31    3.50   41.07   29.50    1.31    3.60
RE   1    1    10   10    H HIS   .    .    .    .    .    T       50.63   45.81   76.20   75.98   41.50   75.67   51.40    0.31    0.90   48.67   50.10   27.31   31.90
RE   1    1    11   11    L LEU   .    .    .    .    .    T      -57.60  139.21   78.50   79.58   44.50   55.49   39.30   24.09   64.20   56.43   39.70   23.15   63.70
RE   1    1    12   12    G GLY   .    .    .    .    .    T       91.01   -4.77   47.80   51.11   63.80   23.22   71.80   27.90   58.40   27.09   72.10   24.02   56.50
RE   1    1    13   13    Y TYR   .    .    .    .    .    T      -74.99  115.31  107.80  100.62   47.30  100.09   56.40    0.52    1.50   66.13   48.50   34.48   45.20
RE   1    1    14   14    E GLU   1    1    H    5    .    C      -96.17   74.41   82.00   71.84   41.70   61.45   45.60   10.39   27.70   17.84   29.60   54.00   48.20
RE   1    1    15   15    Q GLN   1    1    H    5    .    G      -56.45  130.81   34.70   33.39   18.70   33.39   23.70    0.00    0.00    0.31    0.60   33.08   26.20
RE   1    1    16   16    F PHE   1    1    H    5    .    G       57.56   29.90  146.10  150.86   75.60  136.18   83.00   14.68   41.50  136.40   82.50   14.46   42.20
RE   1    1    17   17    H HIS   1    1    H    5    .    G       55.61   29.81  160.00  158.76   86.80  143.03   97.20   15.72   43.90   93.02   95.70   65.74   76.70
RE   1    1    18   18    K LYS   2    A    E    .    .    C     -111.48  108.83  115.50  109.57   54.60  109.57   67.10    0.00    0.00   67.34   57.80   42.23   50.10
RE   1    1    19   19    P PRO   2    A    E    .    1    H      -54.76  -17.53   74.50   83.79   61.60   82.99   69.20    0.80    4.90   82.99   68.60    0.80    5.30
RE   1    1    20   20    Q GLN   2    A    E    .    1    H      -73.35  -35.75  120.10  112.90   63.30  111.79   79.30    1.11    3.00   28.62   54.80   84.28   66.70
RE   1    1    21   21    R ARG   2    A    E    .    1    H      -68.53  -38.89   82.60   84.22   35.30   84.22   41.80    0.00    0.00   22.91   29.40   61.31   38.10
RE   1    1    22   22    E GLU   2    A    E    .    1    H      -56.60  -42.19   71.00   59.66   34.60   59.41   44.10    0.25    0.70   17.46   29.00   42.20   37.70
RE   1    1    23   23    E GLU   2    A    E    .    1    H      -66.34  -36.55  123.60  108.67   63.10  104.55   77.60    4.12   11.00   54.20   89.90   54.47   48.60
RE   1    1    24   24    E GLU   2    A    E    .    1    H      -71.24  -35.34   80.40   71.99   41.80   67.32   50.00    4.67   12.40   41.76   69.30   30.23   27.00
RE   1    1    25   25    F PHE   2    A    E    .    1    H      -63.59  -40.62   41.80   41.19   20.60   39.81   24.30    1.38    3.90   39.81   24.10    1.38    4.00
RE   1    1    26   26    A ALA   2    A    E    .    1    H      -66.25  -43.69   46.10   46.40   43.00   41.37   59.60    5.03   13.10   42.55   59.60    3.85   10.50
RE   1    1    27   27    E GLU   2    A    E    .    1    H      -60.95  -39.89   91.00   84.33   49.00   83.96   62.30    0.36    1.00   41.68   69.10   42.65   38.10
RE   1    1    28   28    A ALA   2    A    E    .    1    H      -58.03  -47.16   55.00   58.08   53.80   52.98   76.30    5.10   13.20   54.38   76.20    3.70   10.10
RE   1    1    29   29    F PHE   2    A    E    .    1    H      -61.12  -42.56   38.50   33.87   17.00   33.36   20.30    0.51    1.40   33.36   20.20    0.51    1.50
RE   1    1    30   30    K LYS   2    A    E    .    1    H      -63.44  -42.40  104.70  105.98   52.80  105.45   64.60    0.53    1.40   58.41   50.10   47.56   56.50
RE   1    1    31   31    N ASN   2    A    E    .    1    H      -60.26  -47.05   77.00   73.22   50.90   72.53   68.30    0.70    1.80   23.06   49.90   50.16   51.30
RE   1    1    32   32    A ALA   2    A    E    .    1    H      -58.51  -48.57   56.20   56.15   52.00   49.87   71.80    6.28   16.30   51.18   71.70    4.97   13.60
RE   1    1    33   33    L LEU   2    A    E    .    1    H      -61.69  -37.59   59.70   59.93   33.60   59.56   42.20    0.38    1.00   59.93   42.10    0.00    0.00
RE   1    1    34   34    E GLU   2    A    E    .    1    H      -68.18  -35.02   87.40   76.92   44.70   76.19   56.50    0.74    2.00   33.77   56.00   43.15   38.50
RE   1    1    35   35    I ILE   2    A    E    .    1    H      -69.89  -35.85   89.80   96.84   55.30   96.84   70.20    0.00    0.00   96.84   69.60    0.00    0.00
RE   1    1    36   36    A ALA   2    A    E    .    1    H      -61.30  -45.01   19.20   19.50   18.10   19.22   27.70    0.27    0.70   19.22   26.90    0.27    0.70
RE   1    1    37   37    V VAL   2    A    E    .    1    H      -64.92  -44.30  109.50  111.44   73.60  102.58   89.80    8.87   23.90  102.58   88.80    8.87   24.70
RE   1    1    38   38    Q GLN   2    A    E    .    1    H      -59.93  -32.77  145.80  140.48   78.70  113.02   80.20   27.46   73.20   49.34   94.50   91.14   72.20
RE   1    1    39   39    E GLU   2    A    E    .    1    H      -83.49    5.97  133.40  118.49   68.80   99.06   73.50   19.43   51.80   31.08   51.60   87.41   78.10
RE   1    1    40   40    N ASN   .    .    .    .    .    C       54.97   43.05  136.50  126.77   88.10  116.79  109.90    9.98   26.50   31.92   69.00   94.86   97.10
RE   1    1    41   41    V VAL   .    .    .    .    .    C      -70.50  156.23   65.90   69.23   45.70   50.82   44.50   18.40   49.50   50.86   44.00   18.36   51.10


  [Part of this file has been deleted for brevity]

AT   1    1    .    43   43    F PHE   P CZ       -0.112   46.150   14.681    1.00   26.24
AT   1    1    .    44   44    I ILE   P N         5.655   45.232   15.043    1.00   33.36
AT   1    1    .    44   44    I ILE   P CA        6.014   43.831   15.094    1.00   31.77
AT   1    1    .    44   44    I ILE   P C         5.453   43.198   16.344    1.00   30.94
AT   1    1    .    44   44    I ILE   P O         5.512   43.792   17.415    1.00   33.03
AT   1    1    .    44   44    I ILE   P CB        7.565   43.721   15.081    1.00   32.37
AT   1    1    .    44   44    I ILE   P CG1       8.089   44.316   13.772    1.00   30.80
AT   1    1    .    44   44    I ILE   P CG2       8.025   42.282   15.324    1.00   28.46
AT   1    1    .    44   44    I ILE   P CD1       9.598   44.467   13.698    1.00   31.28
AT   1    1    .    45   45    L LEU   P N         4.884   42.008   16.199    1.00   28.70
AT   1    1    .    45   45    L LEU   P CA        4.353   41.265   17.326    1.00   26.34
AT   1    1    .    45   45    L LEU   P C         5.192   40.020   17.558    1.00   30.16
AT   1    1    .    45   45    L LEU   P O         5.498   39.290   16.600    1.00   29.17
AT   1    1    .    45   45    L LEU   P CB        2.947   40.775   17.043    1.00   26.78
AT   1    1    .    45   45    L LEU   P CG        1.836   41.790   16.769    1.00   29.15
AT   1    1    .    45   45    L LEU   P CD1       0.527   41.024   16.428    1.00   25.64
AT   1    1    .    45   45    L LEU   P CD2       1.662   42.668   18.008    1.00   25.27
AT   1    1    .    46   46    I ILE   P N         5.543   39.761   18.814    1.00   28.08
AT   1    1    .    46   46    I ILE   P CA        6.290   38.558   19.155    1.00   28.84
AT   1    1    .    46   46    I ILE   P C         5.452   37.904   20.240    1.00   29.18
AT   1    1    .    46   46    I ILE   P O         5.461   38.305   21.416    1.00   27.33
AT   1    1    .    46   46    I ILE   P CB        7.727   38.853   19.664    1.00   29.60
AT   1    1    .    46   46    I ILE   P CG1       8.493   39.680   18.626    1.00   27.78
AT   1    1    .    46   46    I ILE   P CG2       8.457   37.542   19.893    1.00   27.75
AT   1    1    .    46   46    I ILE   P CD1       9.988   39.865   18.927    1.00   28.95
AT   1    1    .    47   47    A ALA   P N         4.700   36.902   19.798    1.00   29.10
AT   1    1    .    47   47    A ALA   P CA        3.770   36.163   20.619    1.00   26.51
AT   1    1    .    47   47    A ALA   P C         4.372   35.106   21.553    1.00   27.03
AT   1    1    .    47   47    A ALA   P O         3.939   33.951   21.580    1.00   27.39
AT   1    1    .    47   47    A ALA   P CB        2.691   35.541   19.702    1.00   26.11
AT   1    1    .    48   48    G GLY   P N         5.381   35.500   22.316    1.00   26.07
AT   1    1    .    48   48    G GLY   P CA        5.935   34.587   23.293    1.00   27.20
AT   1    1    .    48   48    G GLY   P C         7.112   33.736   22.884    1.00   29.30
AT   1    1    .    48   48    G GLY   P O         7.283   33.381   21.709    1.00   29.25
AT   1    1    .    49   49    D ASP   P N         7.899   33.373   23.889    1.00   28.57
AT   1    1    .    49   49    D ASP   P CA        9.091   32.554   23.699    1.00   28.10
AT   1    1    .    49   49    D ASP   P C        10.100   33.250   22.827    1.00   27.16
AT   1    1    .    49   49    D ASP   P O        10.601   32.676   21.869    1.00   29.08
AT   1    1    .    49   49    D ASP   P CB        8.735   31.200   23.093    1.00   27.86
AT   1    1    .    49   49    D ASP   P CG        8.155   30.221   24.124    1.00   32.19
AT   1    1    .    49   49    D ASP   P OD1       7.861   29.073   23.740    1.00   29.67
AT   1    1    .    49   49    D ASP   P OD2       7.992   30.586   25.313    1.00   31.41
AT   1    1    .    50   50    L LEU   P N        10.375   34.509   23.128    1.00   27.16
AT   1    1    .    50   50    L LEU   P CA       11.393   35.247   22.386    1.00   27.68
AT   1    1    .    50   50    L LEU   P C        12.754   34.607   22.792    1.00   27.01
AT   1    1    .    50   50    L LEU   P O        13.642   34.421   21.963    1.00   27.43
AT   1    1    .    50   50    L LEU   P CB       11.351   36.724   22.771    1.00   28.02
AT   1    1    .    50   50    L LEU   P CG       12.576   37.551   22.355    1.00   30.11
AT   1    1    .    50   50    L LEU   P CD1      12.751   37.437   20.827    1.00   28.61
AT   1    1    .    50   50    L LEU   P CD2      12.425   39.035   22.798    1.00   23.77
//














 5.0   DATA FILES                

None.








 6.0   USAGE                     


 

 6.1   COMMAND LINE ARGUMENTS 



   Standard (Mandatory) qualifiers:
  [-scopfile]          infile     This option specifies the DCF file (domain
                                  classification file) (input). A 'domain
                                  classification file' contains classification
                                  and other data for domains from SCOP or
                                  CATH, in DCF format (EMBL-like). The files
                                  are generated by using SCOPPARSE and
                                  CATHPARSE. Domain sequence information can
                                  be added to the file by using DOMAINSEQS.
  [-ccfpdir]           directory  This option specifies the location of
                                  protein CCF file (clean coordinate files)
                                  (input). A 'clean cordinate file' contains
                                  protein coordinate and derived data for a
                                  single PDB file ('protein clean coordinate
                                  file') or a single domain from SCOP or CATH
                                  ('domain clean coordinate file'), in CCF
                                  format (EMBL-like). The files, generated by
                                  using PDBPARSE (PDB files) or DOMAINER
                                  (domains), contain 'cleaned-up' data that is
                                  self-consistent and error-corrected.
                                  Records for residue solvent accessibility
                                  and secondary structure are added to the
                                  file by using PDBPLUS. default: "./
  [-ccfoutdir]         outdir     [./] This option specifies the location of
                                  domain CCF files (clean coordinate files)
                                  (output). A 'domain coordinate file'
                                  contains coordinate and other data for a
                                  single scop domain. The files are generated
                                  by DOMAINER and are in embl-like and pdb
                                  formats.
  [-pdboutdir]         outdir     [./] This option specifies the location of
                                  domain PDB files (output). A 'domain
                                  coordinate file' contains coordinate and
                                  other data for a single scop domain. The
                                  files are generated by DOMAINER and are in
                                  embl-like and pdb formats.
   -mode               menu       [1] This option specifies the operational
                                  mode of DOMAINER. This determines which sort
                                  of residue number is written to the PDB
                                  file. (Values: 1 (Use original PDB residue
                                  number); 2 (Use corrected residue number
                                  (index into SEQRES sequence)))
   -cpdblogfile        outfile    [domainer_embl.log] This option specifies
                                  the log file, which contains messages about
                                  any errors arising while DOMAINER generated
                                  CCF format files
   -pdblogfile         outfile    [domainer_pdb.log] This option specifies the
                                  the log file, which contains messages about
                                  any errors arising while DOMAINER generated
                                  PDB format files

   Additional (Optional) qualifiers: (none)
   Advanced (Unprompted) qualifiers: (none)
   Associated qualifiers:

   "-cpdblogfile" associated qualifiers
   -odirectory         string     Output directory

   "-pdblogfile" associated qualifiers
   -odirectory         string     Output directory

   General qualifiers:
   -auto               boolean    Turn off prompts
   -stdout             boolean    Write first file to standard output
   -filter             boolean    Read first file from standard input, write
                                  first file to standard output
   -options            boolean    Prompt for standard and additional values
   -debug              boolean    Write debug output to program.dbg
   -verbose            boolean    Report some/full command line options
   -help               boolean    Report command line options. More
                                  information on associated and general
                                  qualifiers can be found with -help -verbose
   -warning            boolean    Report warnings
   -error              boolean    Report errors
   -fatal              boolean    Report fatal errors
   -die                boolean    Report dying program messages










Standard (Mandatory) qualifiers
Allowed values
Default





[-scopfile]
(Parameter 1)		
This option specifies the DCF file (domain classification file) (input). A 'domain classification file' contains classification and other data for domains from SCOP or CATH, in DCF format (EMBL-like). The files are generated by using SCOPPARSE and CATHPARSE. Domain sequence information can be added to the file by using DOMAINSEQS.
Input file
Required





[-ccfpdir]
(Parameter 2)		
This option specifies the location of protein CCF file (clean coordinate files) (input). A 'clean cordinate file' contains protein coordinate and derived data for a single PDB file ('protein clean coordinate file') or a single domain from SCOP or CATH ('domain clean coordinate file'), in CCF format (EMBL-like). The files, generated by using PDBPARSE (PDB files) or DOMAINER (domains), contain 'cleaned-up' data that is self-consistent and error-corrected. Records for residue solvent accessibility and secondary structure are added to the file by using PDBPLUS. default: "./
Directory
 





[-ccfoutdir]
(Parameter 3)		
This option specifies the location of domain CCF files (clean coordinate files) (output). A 'domain coordinate file' contains coordinate and other data for a single scop domain. The files are generated by DOMAINER and are in embl-like and pdb formats.
Output directory
./





[-pdboutdir]
(Parameter 4)		
This option specifies the location of domain PDB files (output). A 'domain coordinate file' contains coordinate and other data for a single scop domain. The files are generated by DOMAINER and are in embl-like and pdb formats.
Output directory
./





-mode
This option specifies the operational mode of DOMAINER. This determines which sort of residue number is written to the PDB file.

1 (Use original PDB residue number)
2 (Use corrected residue number (index into SEQRES sequence))

1





-cpdblogfile
This option specifies the log file, which contains messages about any errors arising while DOMAINER generated CCF format files
Output file
domainer_embl.log





-pdblogfile
This option specifies the the log file, which contains messages about any errors arising while DOMAINER generated PDB format files
Output file
domainer_pdb.log





Additional (Optional) qualifiers
Allowed values
Default





(none)





Advanced (Unprompted) qualifiers
Allowed values
Default





(none)







 6.2 EXAMPLE SESSION 


An example of interactive use of DOMAINER is shown below.

Here is a sample session with domainer







% domainer 
Generates domain CCF files from protein CCF files.
Domain classification file: ../scopparse-keep/all.scop
Clean protein structure coordinates directory [.]: ../pdbplus-keep/
Clean domain coordinates file output directory [./]: 
Domain pdb file output directory [./]: 
Residue number mode
         1 : Use original PDB residue number
         2 : Use corrected residue number (index into SEQRES sequence)
Select mode of operation [1]: 1
Domainatrix CCF generation log output file [domainer_embl.log]: domainer_embl.log
Domainatrix PDB generation log output file [domainer_pdb.log]: domainer_pdb.log

D1CS4A_
D1II7A_





Go to the input files for this example
Go to the output files for this example














 7.0   KNOWN BUGS & WARNINGS     

Wildcard matching of SCOP domain start and end points

SCOP treats PDB residue numbers as integers and this is a potential source
of error in the domain ranges. It means that DOMAINER (via library calls)
must use wild card strings when matching a SCOP start / end point to the
PDB residue number strings.









 8.0   NOTES                     

Where coordinates for multiple models are given in a protein coordinate 
file, the domain CCF file will contain coordinates for the first 
model.  



In the rare cases where a domain is comprised of segments from more than 
one chain, the data in the domain CCF file will be presented as 
belonging to a single chain with a chain identifier of '.'.  A single 
sequence will be given.



The start and end positions of domains in SCOP coincide in several cases 
to residues which either lack a CA atom or for which coordinates for a 
single atom only are given in the PDB file.  To ensure these domains are
processed during a DOMAINER run, it is important to use protein CCF
files which have NOT been masked to remove such residues.
Otherwise errors of the following type may occur in the log file:



//
D1QFUL1
ERROR Domain end not found in ajXyzCpdbWriteDomain 

//
D1QFUL1
ERROR Domain start not found in ajXyzCpdbWriteDomain 




None


 8.1   DATA FILES    





FILE TYPE
FORMAT
DESCRIPTION
CREATED BY 
SEE ALSO




 Domain classification file (for SCOP)
 DCF format (EMBL-like). 
 Classification and other data for domains from SCOP.  
 SCOPPARSE 
 Domain sequence information can be added to the file by using DOMAINSEQS.  




 Domain classification file (for CATH)
 DCF format (EMBL-like). 
 Classification and other data for domains from CATH.  
 CATHPARSE 
 Domain sequence information can be added to the file by using DOMAINSEQS.  




 Clean coordinate file (for protein) 
 CCF format (EMBL-like).
 Protein coordinate and derived data for a single PDB file.  The data are 'cleaned-up': self-consistent and error-corrected.  
 PDBPARSE 
 Records for residue solvent accessibility and secondary structure are added to the file by using PDBPLUS. 




 Clean coordinate file (for domain)
 CCF format (EMBL-like).
 Protein coordinate and derived data for a single domain from SCOP or CATH. The data are 'cleaned-up': self-consistent and error-corrected. 
 DOMAINER
 Records for residue solvent accessibility and secondary structure are added to the file by using PDBPLUS.




Domain PDB file 
 PDB format. 
 Protein coordinate data for a single domain from SCOP or CATH. 
 DOMAINER 
 N.A. 














 9.0   DESCRIPTION               

  
 DOMAINER fills the need for a convenient source of protein coordinate data which 
 includes protein strucutral domain definitions and is therefore appropriate 
 for domain-centred approaches.  DOMAINER reads protein CCF files and
 writes files of coordinate data for individual SCOP domains in clean 
 and PDB formats. Domain definitions are taken from  a DCF file (domain classification file).  For example, SCOPPARSE parses the raw SCOP classification files (dir.cla.scop.txt and dir.des.scop.txt) available at URL (http://scop.mrc-lmb.cam.ac.uk/scop/parse/) and generate a DCF output file suitable for use with DOMAINER.












 10.0  ALGORITHM                 

We wrote the DOMAINER application to read protein CCF files and generate files of coordinates for single SCOP domains in the "clean" format (domain CCF files, Figure 1) and the PDB format.  DOMAINER reads a file of domain classification data (e.g. prepared by using the application SCOPPARSE or CATHPARSE), and generates a domain CCF and domain PDB file for each domain listed.  Where coordinates for multiple models were determined, data in the output files are given for the first model only.  In cases where a domain consists of sections from more than one polypeptide chain, the data are presented as belonging to a single chain only (a single sequence with a chain identifier of is given).  










 11.0  RELATED APPLICATIONS      



See also




Program name
Description



aaindexextract
Extract amino acid property data from AAINDEX





allversusall
Sequence similarity data from all-versus-all comparison





cathparse
Generates DCF file from raw CATH files





cutgextract
Extract codon usage tables from from CUTG database





domainnr
Removes redundant domains from a DCF file





domainseqs
Adds sequence records to a DCF file





domainsse
Add secondary structure records to a DCF file





hetparse
Converts heterogen group dictionary to EMBL-like format





jaspextract
Extract data from JASPAR





pdbparse
Parses PDB files and writes protein CCF files





pdbplus
Add accessibility & secondary structure to a CCF file





pdbtosp
Convert swissprot:PDB codes file to EMBL-like format





printsextract
Extract data from PRINTS database for use by pscan





prosextract
Processes the PROSITE motif database for use by patmatmotifs





rebaseextract
Process the REBASE database for use by restriction enzyme applications





scopparse
Generate DCF file from raw SCOP files





seqnr
Removes redundancy from DHF files





sites
Generate residue-ligand CON files from CCF files





ssematch
Search a DCF file for secondary structure matches





tfextract
Process TRANSFAC transcription factor database for use by tfscan












 12.0  DIAGNOSTIC ERROR MESSAGES 

DOMAINER generates a log file an excerpt of which is shown (Figure 2). If there is a problem in processing a domain, three lines containing the record '//', the domain identifier code and an error message respectively are written. The following messages may then be given.



WARN  filename not found (A CCF file could not be found).


ERROR filename file read error (An error was encountered during a file read or write respectively.)


ERROR filename file write error (An error was encountered during a file read or write respectively.)  


ERROR Domain start found by wildcard match only (Wildcard matching was needed to find the start (or end) of a domain in a PDB file: see below).



Various other error messages may also be given (in case of difficulty email Jon Ison, jison@ebi.ac.uk).



Figure 2  Excerpt of log file

//
DS002__
WARN  Could not open for reading cpdb file s002.pxyz
//
DS003__
WARN  Could not open for reading cpdb file s003.pxyz



Messages of the type below can appear in the log file if 
(i)  The domain is of a PDB file which is in holding, but has not made it into the main PDB release yet.
(ii) The domain is of a PDB file that is now obsolete - having been replaced by a more recent entry.
There may be other cases too.



//
D0LPC_1
WARN  0lpc.pxyz not found

 


Messages of the type below indicate that residues for the start or end of a domain are missing from 
the protein CCF file (see 'Notes' above).

//
D1QFUL1
ERROR Domain start not found in ajXyzCpdbWriteDomain 
//
D1QFUL1
ERROR Domain end not found in ajXyzCpdbWriteDomain 










 13.0  AUTHORS                   

Jon Ison (jison@ebi.ac.uk)


The European Bioinformatics Institute 
Wellcome Trust Genome Campus 
Cambridge CB10 1SD 
UK 









 14.0  REFERENCES                


Please cite the authors and EMBOSS.



Rice P, Longden I and Bleasby A (2000) "EMBOSS - The European
Molecular Biology Open Software Suite"  Trends in Genetics,
15:276-278.



See also http://emboss.sourceforge.net/




14.1 Other useful references