GenomeNet

Database: PDB
Entry: 1KLA
LinkDB: 1KLA
Original site: 1KLA 
HEADER    GROWTH FACTOR                           16-JAN-96   1KLA              
TITLE     SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 1-17 OF 33 STRUCTURES       
SPLIT      1KLA 1KLD                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING GROWTH FACTOR-BETA 1;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TGF-B1;                                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: 1 MM (IN DIMER), PH 4.2                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: OVARY;                                                        
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    GROWTH FACTOR, MITOGEN, GLYCOPROTEIN                                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    17                                                                    
AUTHOR    A.P.HINCK,S.J.ARCHER,S.W.QIAN,A.B.ROBERTS,M.B.SPORN,J.A.WEATHERBEE,   
AUTHOR   2 M.L.-S.TSANG,R.LUCAS,B.-L.ZHANG,J.WENKER,D.A.TORCHIA                 
REVDAT   5   29-NOV-17 1KLA    1       HELIX                                    
REVDAT   4   24-NOV-10 1KLA    1       REMARK                                   
REVDAT   3   24-FEB-09 1KLA    1       VERSN                                    
REVDAT   2   01-APR-03 1KLA    1       JRNL                                     
REVDAT   1   17-AUG-96 1KLA    0                                                
JRNL        AUTH   A.P.HINCK,S.J.ARCHER,S.W.QIAN,A.B.ROBERTS,M.B.SPORN,         
JRNL        AUTH 2 J.A.WEATHERBEE,M.L.TSANG,R.LUCAS,B.L.ZHANG,J.WENKER,         
JRNL        AUTH 3 D.A.TORCHIA                                                  
JRNL        TITL   TRANSFORMING GROWTH FACTOR BETA 1: THREE-DIMENSIONAL         
JRNL        TITL 2 STRUCTURE IN SOLUTION AND COMPARISON WITH THE X-RAY          
JRNL        TITL 3 STRUCTURE OF TRANSFORMING GROWTH FACTOR BETA 2.              
JRNL        REF    BIOCHEMISTRY                  V.  35  8517 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8679613                                                      
JRNL        DOI    10.1021/BI9604946                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KLA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174451.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : 4.2                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XPLOR 3.1                          
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 33                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 17                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: THIS ENTRY CONTAINS 1 - 17 OF 33 MODELS. 1 MM (IN DIMER).    
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 LEU A   2       53.99    -91.33                                   
REMARK 500  1 PHE A   8       42.51    -90.52                                   
REMARK 500  1 GLU A  12      164.35    175.71                                   
REMARK 500  1 CYS A  15      159.47    -45.06                                   
REMARK 500  1 CYS A  16      115.19   -177.79                                   
REMARK 500  1 LEU A  20       46.59   -156.38                                   
REMARK 500  1 PHE A  24      -57.26    -15.61                                   
REMARK 500  1 TYR A  39     -178.68    179.47                                   
REMARK 500  1 ASN A  42      175.16     52.91                                   
REMARK 500  1 PHE A  43     -178.18    179.97                                   
REMARK 500  1 PRO A  49     -145.91    -76.04                                   
REMARK 500  1 TYR A  50      -87.83    -91.07                                   
REMARK 500  1 ILE A  51      -28.07    -36.46                                   
REMARK 500  1 TRP A  52       88.11    -59.30                                   
REMARK 500  1 SER A  53       96.46     34.69                                   
REMARK 500  1 ASP A  55      -66.36    -94.57                                   
REMARK 500  1 ALA A  75     -177.10    -52.04                                   
REMARK 500  1 PRO A  76     -162.33    -78.69                                   
REMARK 500  1 LEU A  83     -169.96   -125.73                                   
REMARK 500  1 PRO A  85     -166.71    -74.70                                   
REMARK 500  1 LEU A  86      110.06   -164.22                                   
REMARK 500  1 ILE A  88     -161.83   -125.14                                   
REMARK 500  1 VAL A  89      110.96   -164.01                                   
REMARK 500  1 ARG A  94       -4.27   -141.51                                   
REMARK 500  1 GLU A  99     -159.05   -134.05                                   
REMARK 500  1 SER A 108      139.15   -177.91                                   
REMARK 500  1 LYS A 110     -128.89   -137.34                                   
REMARK 500  1 LEU B   2       54.71    -91.05                                   
REMARK 500  1 PHE B   8       42.58    -90.53                                   
REMARK 500  1 GLU B  12      164.70    175.80                                   
REMARK 500  1 CYS B  15      159.86    -44.94                                   
REMARK 500  1 CYS B  16      115.30   -178.11                                   
REMARK 500  1 LEU B  20       46.42   -156.30                                   
REMARK 500  1 PHE B  24      -57.11    -14.97                                   
REMARK 500  1 TYR B  39     -179.12    178.98                                   
REMARK 500  1 ASN B  42      175.18     52.97                                   
REMARK 500  1 PHE B  43     -178.26   -179.89                                   
REMARK 500  1 PRO B  49     -145.74    -75.95                                   
REMARK 500  1 TYR B  50      -87.74    -91.40                                   
REMARK 500  1 ILE B  51      -28.08    -36.53                                   
REMARK 500  1 TRP B  52       88.04    -59.33                                   
REMARK 500  1 SER B  53       96.35     34.77                                   
REMARK 500  1 ASP B  55      -66.07    -94.55                                   
REMARK 500  1 ALA B  75     -177.49    -51.63                                   
REMARK 500  1 PRO B  76     -161.85    -78.34                                   
REMARK 500  1 LEU B  83     -169.93   -125.88                                   
REMARK 500  1 PRO B  85     -167.09    -75.04                                   
REMARK 500  1 LEU B  86      110.25   -163.74                                   
REMARK 500  1 ILE B  88     -162.09   -124.20                                   
REMARK 500  1 VAL B  89      110.88   -163.91                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     910 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 ARG A  18         0.24    SIDE CHAIN                              
REMARK 500  1 ARG A  25         0.14    SIDE CHAIN                              
REMARK 500  1 ARG A  94         0.20    SIDE CHAIN                              
REMARK 500  1 ARG A 107         0.27    SIDE CHAIN                              
REMARK 500  1 ARG B  18         0.25    SIDE CHAIN                              
REMARK 500  1 ARG B  25         0.14    SIDE CHAIN                              
REMARK 500  1 ARG B  94         0.20    SIDE CHAIN                              
REMARK 500  1 ARG B 107         0.28    SIDE CHAIN                              
REMARK 500  2 ARG A  18         0.13    SIDE CHAIN                              
REMARK 500  2 ARG A  25         0.26    SIDE CHAIN                              
REMARK 500  2 ARG A  94         0.28    SIDE CHAIN                              
REMARK 500  2 ARG A 107         0.23    SIDE CHAIN                              
REMARK 500  2 ARG B  18         0.14    SIDE CHAIN                              
REMARK 500  2 ARG B  25         0.26    SIDE CHAIN                              
REMARK 500  2 ARG B  94         0.28    SIDE CHAIN                              
REMARK 500  2 ARG B 107         0.23    SIDE CHAIN                              
REMARK 500  3 ARG A  94         0.27    SIDE CHAIN                              
REMARK 500  3 ARG A 107         0.32    SIDE CHAIN                              
REMARK 500  3 ARG B  94         0.27    SIDE CHAIN                              
REMARK 500  3 ARG B 107         0.32    SIDE CHAIN                              
REMARK 500  4 ARG A  18         0.21    SIDE CHAIN                              
REMARK 500  4 ARG A  25         0.23    SIDE CHAIN                              
REMARK 500  4 ARG A  94         0.27    SIDE CHAIN                              
REMARK 500  4 ARG A 107         0.31    SIDE CHAIN                              
REMARK 500  4 ARG B  18         0.20    SIDE CHAIN                              
REMARK 500  4 ARG B  25         0.22    SIDE CHAIN                              
REMARK 500  4 ARG B  94         0.27    SIDE CHAIN                              
REMARK 500  4 ARG B 107         0.31    SIDE CHAIN                              
REMARK 500  5 ARG A  18         0.19    SIDE CHAIN                              
REMARK 500  5 ARG A  25         0.12    SIDE CHAIN                              
REMARK 500  5 ARG A  94         0.31    SIDE CHAIN                              
REMARK 500  5 ARG A 107         0.29    SIDE CHAIN                              
REMARK 500  5 ARG B  18         0.18    SIDE CHAIN                              
REMARK 500  5 ARG B  25         0.32    SIDE CHAIN                              
REMARK 500  5 ARG B  94         0.31    SIDE CHAIN                              
REMARK 500  5 ARG B 107         0.29    SIDE CHAIN                              
REMARK 500  6 ARG A  18         0.17    SIDE CHAIN                              
REMARK 500  6 ARG A  25         0.17    SIDE CHAIN                              
REMARK 500  6 ARG A  94         0.21    SIDE CHAIN                              
REMARK 500  6 ARG A 107         0.23    SIDE CHAIN                              
REMARK 500  6 ARG B  18         0.16    SIDE CHAIN                              
REMARK 500  6 ARG B  25         0.18    SIDE CHAIN                              
REMARK 500  6 ARG B  94         0.21    SIDE CHAIN                              
REMARK 500  6 ARG B 107         0.27    SIDE CHAIN                              
REMARK 500  7 ARG A  18         0.23    SIDE CHAIN                              
REMARK 500  7 ARG A  25         0.13    SIDE CHAIN                              
REMARK 500  7 ARG A  94         0.32    SIDE CHAIN                              
REMARK 500  7 ARG A 107         0.28    SIDE CHAIN                              
REMARK 500  7 ARG B  18         0.23    SIDE CHAIN                              
REMARK 500  7 ARG B  25         0.23    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     130 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KLC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1KLD   RELATED DB: PDB                                   
DBREF  1KLA A    1   112  UNP    P01137   TGFB1_HUMAN    279    390             
DBREF  1KLA B    1   112  UNP    P01137   TGFB1_HUMAN    279    390             
SEQRES   1 A  112  ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS          
SEQRES   2 A  112  ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS          
SEQRES   3 A  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 A  112  HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP          
SEQRES   5 A  112  SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR          
SEQRES   6 A  112  ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS          
SEQRES   7 A  112  VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR          
SEQRES   8 A  112  VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 A  112  ILE VAL ARG SER CYS LYS CYS SER                              
SEQRES   1 B  112  ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS          
SEQRES   2 B  112  ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS          
SEQRES   3 B  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 B  112  HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP          
SEQRES   5 B  112  SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR          
SEQRES   6 B  112  ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS          
SEQRES   7 B  112  VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR          
SEQRES   8 B  112  VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 B  112  ILE VAL ARG SER CYS LYS CYS SER                              
HELIX    1   1 GLN A   57  HIS A   68  1                                  12    
HELIX    2   2 GLN B   57  HIS B   68  1                                  12    
SHEET    1   A 2 CYS A  16  ARG A  18  0                                        
SHEET    2   A 2 PHE A  43  LEU A  45 -1  N  LEU A  45   O  CYS A  16           
SHEET    1   B 2 TYR A  90  VAL A  92  0                                        
SHEET    2   B 2 LYS A  95  LYS A  97 -1  N  LYS A  97   O  TYR A  90           
SHEET    1   C 2 CYS B  16  ARG B  18  0                                        
SHEET    2   C 2 PHE B  43  LEU B  45 -1  N  LEU B  45   O  CYS B  16           
SHEET    1   D 2 TYR B  90  VAL B  92  0                                        
SHEET    2   D 2 LYS B  95  LYS B  97 -1  N  LYS B  97   O  TYR B  90           
SHEET    1   E 2 CYS A  77  ALA A  82  0                                        
SHEET    2   E 2 SER A 108  SER A 112 -1  N  SER A 112   O  CYS A  77           
SHEET    1   F 2 CYS B  77  ALA B  82  0                                        
SHEET    2   F 2 SER B 108  SER B 112 -1  N  SER B 112   O  CYS B  77           
SSBOND   1 CYS A    7    CYS A   16                          1555   1555  2.02  
SSBOND   2 CYS A   15    CYS A   78                          1555   1555  2.02  
SSBOND   3 CYS A   44    CYS A  109                          1555   1555  2.01  
SSBOND   4 CYS A   48    CYS A  111                          1555   1555  2.02  
SSBOND   5 CYS A   77    CYS B   77                          1555   1555  2.02  
SSBOND   6 CYS B    7    CYS B   16                          1555   1555  2.02  
SSBOND   7 CYS B   15    CYS B   78                          1555   1555  2.02  
SSBOND   8 CYS B   44    CYS B  109                          1555   1555  2.01  
SSBOND   9 CYS B   48    CYS B  111                          1555   1555  2.02  
CISPEP   1 GLU A   35    PRO A   36          1        -0.21                     
CISPEP   2 GLU B   35    PRO B   36          1        -0.21                     
CISPEP   3 GLU A   35    PRO A   36          2        -0.07                     
CISPEP   4 GLU B   35    PRO B   36          2        -0.07                     
CISPEP   5 GLU A   35    PRO A   36          3         0.11                     
CISPEP   6 GLU B   35    PRO B   36          3         0.02                     
CISPEP   7 GLU A   35    PRO A   36          4         0.15                     
CISPEP   8 GLU B   35    PRO B   36          4         0.11                     
CISPEP   9 GLU A   35    PRO A   36          5        -0.04                     
CISPEP  10 GLU B   35    PRO B   36          5        -0.13                     
CISPEP  11 GLU A   35    PRO A   36          6        -0.21                     
CISPEP  12 GLU B   35    PRO B   36          6        -0.20                     
CISPEP  13 GLU A   35    PRO A   36          7        -0.05                     
CISPEP  14 GLU B   35    PRO B   36          7         0.12                     
CISPEP  15 GLU A   35    PRO A   36          8        -0.27                     
CISPEP  16 GLU B   35    PRO B   36          8        -0.34                     
CISPEP  17 GLU A   35    PRO A   36          9        -0.01                     
CISPEP  18 GLU B   35    PRO B   36          9        -0.16                     
CISPEP  19 GLU A   35    PRO A   36         10        -0.06                     
CISPEP  20 GLU B   35    PRO B   36         10         0.00                     
CISPEP  21 GLU A   35    PRO A   36         11         0.09                     
CISPEP  22 GLU B   35    PRO B   36         11         0.00                     
CISPEP  23 GLU A   35    PRO A   36         12        -0.32                     
CISPEP  24 GLU B   35    PRO B   36         12        -0.32                     
CISPEP  25 GLU A   35    PRO A   36         13        -0.23                     
CISPEP  26 GLU B   35    PRO B   36         13        -0.16                     
CISPEP  27 GLU A   35    PRO A   36         14         0.15                     
CISPEP  28 GLU B   35    PRO B   36         14        -0.09                     
CISPEP  29 GLU A   35    PRO A   36         15         0.04                     
CISPEP  30 GLU B   35    PRO B   36         15         0.15                     
CISPEP  31 GLU A   35    PRO A   36         16         0.44                     
CISPEP  32 GLU B   35    PRO B   36         16         0.34                     
CISPEP  33 GLU A   35    PRO A   36         17        -0.04                     
CISPEP  34 GLU B   35    PRO B   36         17        -0.05                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system