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Database: PDB
Entry: 1Q8K
LinkDB: 1Q8K
Original site: 1Q8K 
HEADER    TRANSLATION                             21-AUG-03   1Q8K              
TITLE     SOLUTION STRUCTURE OF ALPHA SUBUNIT OF HUMAN EIF2                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1;      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EUKARYOTIC TRANSLATION INITIATION FACTOR 2 ALPHA SUBUNIT,   
COMPND   5 EIF-2-ALPHA, EIF- 2ALPHA, EIF-2A;                                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EIF2S1 OR EIF2A;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSLATION, TRANSLATION INITIATION, EUKARYOTIC TRANSLATION           
KEYWDS   2 INITIATION FACTOR 2                                                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    15                                                                    
AUTHOR    T.ITO,A.MARINTCHEV,G.WAGNER                                           
REVDAT   4   27-OCT-21 1Q8K    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 1Q8K    1       VERSN                                    
REVDAT   2   05-OCT-04 1Q8K    1       JRNL                                     
REVDAT   1   07-SEP-04 1Q8K    0                                                
JRNL        AUTH   T.ITO,A.MARINTCHEV,G.WAGNER                                  
JRNL        TITL   SOLUTION STRUCTURE OF HUMAN INITIATION FACTOR EIF2ALPHA      
JRNL        TITL 2 REVEALS HOMOLOGY TO THE ELONGATION FACTOR EEF1B.             
JRNL        REF    STRUCTURE                     V.  12  1693 2004              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15341733                                                     
JRNL        DOI    10.1016/J.STR.2004.07.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NIH-XPLOR1 2.1                                       
REMARK   3   AUTHORS     : JONES,ZOU,COWAN,KJELDGAARD                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Q8K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020051.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 1.1                                
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : 750 MHZ; 600 MHZ; 500 MHZ          
REMARK 210  SPECTROMETER MODEL             : VARIAN INOVA; BRUKER DRX           
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN; BRUKER                     
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NIH-XPLOR1 2.1                     
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 51                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 15                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-15                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     LEU A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 SER A   4      -67.67   -102.03                                   
REMARK 500  1 CYS A   5      156.80    -46.58                                   
REMARK 500  1 ARG A   6      -46.51   -168.49                                   
REMARK 500  1 TYR A   8       28.32    179.64                                   
REMARK 500  1 GLN A   9       26.30     46.14                                   
REMARK 500  1 HIS A  10      107.05     67.75                                   
REMARK 500  1 LYS A  11       78.06   -175.93                                   
REMARK 500  1 PRO A  13     -162.95    -72.30                                   
REMARK 500  1 GLU A  16       32.26   -179.69                                   
REMARK 500  1 VAL A  23      151.72    -45.60                                   
REMARK 500  1 ARG A  24      -64.89   -131.29                                   
REMARK 500  1 LEU A  36      110.39     55.95                                   
REMARK 500  1 GLU A  37       40.26    -74.94                                   
REMARK 500  1 TYR A  38      -57.87   -148.49                                   
REMARK 500  1 ASN A  40      -92.31   -155.02                                   
REMARK 500  1 ILE A  41     -151.88    173.12                                   
REMARK 500  1 GLU A  42     -159.04    -81.92                                   
REMARK 500  1 ARG A  52     -179.03    -57.73                                   
REMARK 500  1 ARG A  53     -159.99     55.19                                   
REMARK 500  1 ARG A  56      -62.55   -120.22                                   
REMARK 500  1 SER A  57       26.90   -164.72                                   
REMARK 500  1 ILE A  58       37.49     34.75                                   
REMARK 500  1 ILE A  64       81.35     30.28                                   
REMARK 500  1 ARG A  74      131.56   -176.67                                   
REMARK 500  1 LYS A  79      -36.64   -166.33                                   
REMARK 500  1 ARG A  88       74.76     64.58                                   
REMARK 500  1 GLU A 119       67.15     65.44                                   
REMARK 500  1 ASP A 123      -80.55     59.55                                   
REMARK 500  1 THR A 133      -72.89   -149.96                                   
REMARK 500  1 ASP A 158       72.42   -118.10                                   
REMARK 500  1 LEU A 183      -70.00   -118.31                                   
REMARK 500  1 PRO A 185     -167.34    -74.27                                   
REMARK 500  1 ALA A 187      147.82     58.22                                   
REMARK 500  1 TYR A 199      101.78    -49.78                                   
REMARK 500  1 SER A 218     -163.42    -60.88                                   
REMARK 500  1 PRO A 231      -74.96    -72.63                                   
REMARK 500  1 PRO A 232       49.83    -78.76                                   
REMARK 500  1 THR A 238     -176.82   -176.98                                   
REMARK 500  1 LEU A 241      175.11    -53.45                                   
REMARK 500  1 GLU A 242      130.95     70.17                                   
REMARK 500  1 ARG A 265       64.47     61.04                                   
REMARK 500  1 MET A 272       16.21   -145.70                                   
REMARK 500  1 GLU A 273      176.53     51.15                                   
REMARK 500  1 GLN A 288      -74.68    -86.12                                   
REMARK 500  1 MET A 289     -158.83     56.03                                   
REMARK 500  1 GLU A 290       91.05     53.52                                   
REMARK 500  1 GLU A 298       57.87   -112.63                                   
REMARK 500  2 CYS A   5      118.51     62.32                                   
REMARK 500  2 GLN A   9        5.65    -67.29                                   
REMARK 500  2 HIS A  10       96.00     70.11                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     587 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   6         0.26    SIDE CHAIN                              
REMARK 500  1 ARG A  24         0.27    SIDE CHAIN                              
REMARK 500  1 ARG A  52         0.15    SIDE CHAIN                              
REMARK 500  1 ARG A  53         0.19    SIDE CHAIN                              
REMARK 500  1 ARG A  54         0.25    SIDE CHAIN                              
REMARK 500  1 ARG A  56         0.17    SIDE CHAIN                              
REMARK 500  1 ARG A  63         0.32    SIDE CHAIN                              
REMARK 500  1 ARG A  66         0.28    SIDE CHAIN                              
REMARK 500  1 ARG A  74         0.16    SIDE CHAIN                              
REMARK 500  1 ARG A  87         0.29    SIDE CHAIN                              
REMARK 500  1 ARG A  88         0.32    SIDE CHAIN                              
REMARK 500  1 ARG A 112         0.31    SIDE CHAIN                              
REMARK 500  1 ARG A 132         0.29    SIDE CHAIN                              
REMARK 500  1 ARG A 143         0.18    SIDE CHAIN                              
REMARK 500  1 ARG A 172         0.14    SIDE CHAIN                              
REMARK 500  1 ARG A 181         0.23    SIDE CHAIN                              
REMARK 500  1 ARG A 182         0.23    SIDE CHAIN                              
REMARK 500  1 ARG A 191         0.26    SIDE CHAIN                              
REMARK 500  1 ARG A 212         0.30    SIDE CHAIN                              
REMARK 500  1 ARG A 233         0.11    SIDE CHAIN                              
REMARK 500  1 ARG A 243         0.28    SIDE CHAIN                              
REMARK 500  1 ARG A 265         0.23    SIDE CHAIN                              
REMARK 500  1 ARG A 287         0.14    SIDE CHAIN                              
REMARK 500  1 ARG A 291         0.27    SIDE CHAIN                              
REMARK 500  1 ARG A 294         0.21    SIDE CHAIN                              
REMARK 500  2 ARG A   6         0.22    SIDE CHAIN                              
REMARK 500  2 ARG A  24         0.23    SIDE CHAIN                              
REMARK 500  2 ARG A  52         0.10    SIDE CHAIN                              
REMARK 500  2 ARG A  53         0.17    SIDE CHAIN                              
REMARK 500  2 ARG A  54         0.18    SIDE CHAIN                              
REMARK 500  2 ARG A  56         0.29    SIDE CHAIN                              
REMARK 500  2 ARG A  63         0.23    SIDE CHAIN                              
REMARK 500  2 ARG A  66         0.22    SIDE CHAIN                              
REMARK 500  2 ARG A  74         0.17    SIDE CHAIN                              
REMARK 500  2 ARG A  87         0.30    SIDE CHAIN                              
REMARK 500  2 ARG A  88         0.13    SIDE CHAIN                              
REMARK 500  2 ARG A 112         0.32    SIDE CHAIN                              
REMARK 500  2 ARG A 132         0.16    SIDE CHAIN                              
REMARK 500  2 ARG A 172         0.26    SIDE CHAIN                              
REMARK 500  2 ARG A 181         0.29    SIDE CHAIN                              
REMARK 500  2 ARG A 182         0.28    SIDE CHAIN                              
REMARK 500  2 ARG A 191         0.31    SIDE CHAIN                              
REMARK 500  2 ARG A 212         0.20    SIDE CHAIN                              
REMARK 500  2 ARG A 233         0.28    SIDE CHAIN                              
REMARK 500  2 ARG A 243         0.18    SIDE CHAIN                              
REMARK 500  2 ARG A 287         0.31    SIDE CHAIN                              
REMARK 500  2 ARG A 291         0.21    SIDE CHAIN                              
REMARK 500  2 ARG A 294         0.26    SIDE CHAIN                              
REMARK 500  3 ARG A   6         0.32    SIDE CHAIN                              
REMARK 500  3 ARG A  24         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     360 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1Q8K A    4   302  UNP    P05198   IF2A_HUMAN       4    302             
SEQADV 1Q8K MET A    3  UNP  P05198              CLONING ARTIFACT               
SEQADV 1Q8K GLN A   27  UNP  P05198    ALA    27 ENGINEERED MUTATION            
SEQADV 1Q8K HIS A   46  UNP  P05198    LEU    46 ENGINEERED MUTATION            
SEQADV 1Q8K LYS A   71  UNP  P05198    VAL    71 ENGINEERED MUTATION            
SEQADV 1Q8K LEU A  303  UNP  P05198              CLONING ARTIFACT               
SEQADV 1Q8K GLU A  304  UNP  P05198              CLONING ARTIFACT               
SEQADV 1Q8K HIS A  305  UNP  P05198              EXPRESSION TAG                 
SEQADV 1Q8K HIS A  306  UNP  P05198              EXPRESSION TAG                 
SEQADV 1Q8K HIS A  307  UNP  P05198              EXPRESSION TAG                 
SEQADV 1Q8K HIS A  308  UNP  P05198              EXPRESSION TAG                 
SEQADV 1Q8K HIS A  309  UNP  P05198              EXPRESSION TAG                 
SEQADV 1Q8K HIS A  310  UNP  P05198              EXPRESSION TAG                 
SEQRES   1 A  308  MET SER CYS ARG PHE TYR GLN HIS LYS PHE PRO GLU VAL          
SEQRES   2 A  308  GLU ASP VAL VAL MET VAL ASN VAL ARG SER ILE GLN GLU          
SEQRES   3 A  308  MET GLY ALA TYR VAL SER LEU LEU GLU TYR ASN ASN ILE          
SEQRES   4 A  308  GLU GLY MET ILE HIS LEU SER GLU LEU SER ARG ARG ARG          
SEQRES   5 A  308  ILE ARG SER ILE ASN LYS LEU ILE ARG ILE GLY ARG ASN          
SEQRES   6 A  308  GLU CYS VAL LYS VAL ILE ARG VAL ASP LYS GLU LYS GLY          
SEQRES   7 A  308  TYR ILE ASP LEU SER LYS ARG ARG VAL SER PRO GLU GLU          
SEQRES   8 A  308  ALA ILE LYS CYS GLU ASP LYS PHE THR LYS SER LYS THR          
SEQRES   9 A  308  VAL TYR SER ILE LEU ARG HIS VAL ALA GLU VAL LEU GLU          
SEQRES  10 A  308  TYR THR LYS ASP GLU GLN LEU GLU SER LEU PHE GLN ARG          
SEQRES  11 A  308  THR ALA TRP VAL PHE ASP ASP LYS TYR LYS ARG PRO GLY          
SEQRES  12 A  308  TYR GLY ALA TYR ASP ALA PHE LYS HIS ALA VAL SER ASP          
SEQRES  13 A  308  PRO SER ILE LEU ASP SER LEU ASP LEU ASN GLU ASP GLU          
SEQRES  14 A  308  ARG GLU VAL LEU ILE ASN ASN ILE ASN ARG ARG LEU THR          
SEQRES  15 A  308  PRO GLN ALA VAL LYS ILE ARG ALA ASP ILE GLU VAL ALA          
SEQRES  16 A  308  CYS TYR GLY TYR GLU GLY ILE ASP ALA VAL LYS GLU ALA          
SEQRES  17 A  308  LEU ARG ALA GLY LEU ASN CYS SER THR GLU ASN MET PRO          
SEQRES  18 A  308  ILE LYS ILE ASN LEU ILE ALA PRO PRO ARG TYR VAL MET          
SEQRES  19 A  308  THR THR THR THR LEU GLU ARG THR GLU GLY LEU SER VAL          
SEQRES  20 A  308  LEU SER GLN ALA MET ALA VAL ILE LYS GLU LYS ILE GLU          
SEQRES  21 A  308  GLU LYS ARG GLY VAL PHE ASN VAL GLN MET GLU PRO LYS          
SEQRES  22 A  308  VAL VAL THR ASP THR ASP GLU THR GLU LEU ALA ARG GLN          
SEQRES  23 A  308  MET GLU ARG LEU GLU ARG GLU ASN ALA GLU VAL ASP GLY          
SEQRES  24 A  308  ASP LEU GLU HIS HIS HIS HIS HIS HIS                          
HELIX    1   1 LEU A   47  LEU A   50  5                                   4    
HELIX    2   3 PRO A   91  LEU A  118  1                                  28    
HELIX    3   4 ASP A  123  GLN A  131  1                                   9    
HELIX    4   5 ALA A  134  TYR A  141  1                                   8    
HELIX    5   6 TYR A  146  HIS A  154  1                                   9    
HELIX    6   8 GLU A  169  LEU A  183  1                                  15    
HELIX    7   9 ILE A  204  ASN A  216  1                                  13    
HELIX    8  10 ARG A  243  GLU A  262  1                                  20    
HELIX    9  11 ASP A  281  GLN A  288  1                                   8    
SHEET    1   A 6 VAL A  18  ILE A  26  0                                        
SHEET    2   A 6 ALA A  31  LEU A  35 -1  O  TYR A  32   N  SER A  25           
SHEET    3   A 6 ILE A  41  ILE A  45 -1  O  ILE A  45   N  ALA A  31           
SHEET    4   A 6 TYR A  81  SER A  85  1  O  ILE A  82   N  MET A  44           
SHEET    5   A 6 ASN A  67  ASP A  76 -1  N  LYS A  71   O  SER A  85           
SHEET    6   A 6 VAL A  18  ILE A  26 -1  N  VAL A  21   O  GLU A  68           
SHEET    1   B 5 ILE A 224  ALA A 230  0                                        
SHEET    2   B 5 ARG A 233  THR A 240 -1  O  THR A 237   N  LYS A 225           
SHEET    3   B 5 VAL A 188  ALA A 197 -1  N  ILE A 190   O  THR A 238           
SHEET    4   B 5 VAL A 267  VAL A 270 -1  O  VAL A 267   N  ALA A 197           
SHEET    5   B 5 LYS A 275  VAL A 277  1  O  LYS A 275   N  ARG A 191           
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                                                                             
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