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Database: PDB
Entry: 2DLI
LinkDB: 2DLI
Original site: 2DLI 
HEADER    IMMUNE SYSTEM                           08-MAR-99   2DLI              
TITLE     KILLER IMMUNOGLOBULIN RECEPTOR 2DL2,TRIGONAL FORM                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (MHC CLASS I NK CELL RECEPTOR PRECURSOR);          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR HLA-CW3 RECOGNITION DOMAIN;                  
COMPND   5 SYNONYM: P58 NATURAL KILLER CELL RECEPTOR;                           
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 CELL: NATURAL KILLER;                                                
SOURCE   6 CELLULAR_LOCATION: SURFACE;                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET30                                     
KEYWDS    KIR, NATURAL KILLER RECEPTOR, INHIBITORY RECEPTOR,                    
KEYWDS   2 IMMUNOGLOBULIN, IMMUNE SYSTEM                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.SUN,G.A.SNYDER                                                    
REVDAT   3   24-FEB-09 2DLI    1       VERSN                                    
REVDAT   2   05-MAY-00 2DLI    1       COMPND DBREF                             
REVDAT   1   13-JAN-00 2DLI    0                                                
JRNL        AUTH   G.A.SNYDER,A.G.BROOKS,P.D.SUN                                
JRNL        TITL   CRYSTAL STRUCTURE OF THE HLA-CW3 ALLOTYPE-SPECIFIC           
JRNL        TITL 2 KILLER CELL INHIBITORY RECEPTOR KIR2DL2                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  96  3864 1999              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   10097129                                                     
JRNL        DOI    10.1073/PNAS.96.7.3864                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 5690                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.331                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1521                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.37                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DLI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000603.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6169                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.24000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1NKR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.93333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.46667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       20.46667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       40.93333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A     4                                                      
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    ARG A   6      114.79     90.35                                   
REMARK 500    HIS A  13      -57.96    -17.94                                   
REMARK 500    GLU A  21       -8.21     68.78                                   
REMARK 500    SER A  30      136.92   -173.50                                   
REMARK 500    VAL A  32       99.19    -64.79                                   
REMARK 500    ARG A  33       67.18    -45.65                                   
REMARK 500    GLU A  35      -20.92   -143.38                                   
REMARK 500    GLU A  42     -148.23   -122.79                                   
REMARK 500    LYS A  44      -75.71    -78.60                                   
REMARK 500    HIS A  56       73.43    -62.67                                   
REMARK 500    ASP A  57      122.16     62.40                                   
REMARK 500    PRO A  68       95.15    -40.74                                   
REMARK 500    SER A  82     -167.73   -179.03                                   
REMARK 500    GLN A  89      132.02    -26.62                                   
REMARK 500    LEU A 104        1.05   -178.67                                   
REMARK 500    SER A 130      157.19    165.35                                   
REMARK 500    SER A 133       48.72    -70.07                                   
REMARK 500    GLU A 142      103.78     50.95                                   
REMARK 500    ARG A 149      140.95   -172.04                                   
REMARK 500    PRO A 154      170.41    -52.55                                   
REMARK 500    ASN A 157      -38.42   -166.76                                   
REMARK 500    PRO A 168       99.75    -44.30                                   
REMARK 500    THR A 170      -74.92   -113.32                                   
REMARK 500    ASP A 183      -72.22    -68.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2DLI A    4   200  UNP    P43627   KI2L2_HUMAN     25    221             
SEQRES   1 A  197  VAL HIS ARG LYS PRO SER LEU LEU ALA HIS PRO GLY ARG          
SEQRES   2 A  197  LEU VAL LYS SER GLU GLU THR VAL ILE LEU GLN CYS TRP          
SEQRES   3 A  197  SER ASP VAL ARG PHE GLU HIS PHE LEU LEU HIS ARG GLU          
SEQRES   4 A  197  GLY LYS PHE LYS ASP THR LEU HIS LEU ILE GLY GLU HIS          
SEQRES   5 A  197  HIS ASP GLY VAL SER LYS ALA ASN PHE SER ILE GLY PRO          
SEQRES   6 A  197  MET MET GLN ASP LEU ALA GLY THR TYR ARG CYS TYR GLY          
SEQRES   7 A  197  SER VAL THR HIS SER PRO TYR GLN LEU SER ALA PRO SER          
SEQRES   8 A  197  ASP PRO LEU ASP ILE VAL ILE THR GLY LEU TYR GLU LYS          
SEQRES   9 A  197  PRO SER LEU SER ALA GLN PRO GLY PRO THR VAL LEU ALA          
SEQRES  10 A  197  GLY GLU SER VAL THR LEU SER CYS SER SER ARG SER SER          
SEQRES  11 A  197  TYR ASP MET TYR HIS LEU SER ARG GLU GLY GLU ALA HIS          
SEQRES  12 A  197  GLU CYS ARG PHE SER ALA GLY PRO LYS VAL ASN GLY THR          
SEQRES  13 A  197  PHE GLN ALA ASP PHE PRO LEU GLY PRO ALA THR HIS GLY          
SEQRES  14 A  197  GLY THR TYR ARG CYS PHE GLY SER PHE ARG ASP SER PRO          
SEQRES  15 A  197  TYR GLU TRP SER ASN SER SER ASP PRO LEU LEU VAL SER          
SEQRES  16 A  197  VAL ILE                                                      
FORMUL   2  HOH   *10(H2 O)                                                     
SHEET    1   A 3 SER A   9  LEU A  11  0                                        
SHEET    2   A 3 VAL A  24  SER A  30 -1  N  TRP A  29   O  SER A   9           
SHEET    3   A 3 SER A  60  ILE A  66 -1  N  ILE A  66   O  VAL A  24           
SHEET    1   B 2 LEU A  17  LYS A  19  0                                        
SHEET    2   B 2 VAL A 100  THR A 102  1  N  VAL A 100   O  VAL A  18           
SHEET    1   C 3 ARG A  78  SER A  82  0                                        
SHEET    2   C 3 HIS A  36  HIS A  40 -1  N  HIS A  40   O  ARG A  78           
SHEET    3   C 3 THR A  48  LEU A  51 -1  N  LEU A  51   O  PHE A  37           
SHEET    1   D 2 GLY A  75  TYR A  77  0                                        
SHEET    2   D 2 LEU A  97  ILE A  99 -1  N  ILE A  99   O  GLY A  75           
SHEET    1   E 3 SER A 109  ALA A 112  0                                        
SHEET    2   E 3 SER A 123  SER A 129 -1  N  SER A 129   O  SER A 109           
SHEET    3   E 3 ASP A 163  PRO A 168 -1  N  GLY A 167   O  VAL A 124           
SHEET    1   F 2 THR A 117  LEU A 119  0                                        
SHEET    2   F 2 SER A 198  ILE A 200  1  N  SER A 198   O  VAL A 118           
SHEET    1   G 3 CYS A 148  SER A 151  0                                        
SHEET    2   G 3 MET A 136  SER A 140 -1  N  LEU A 139   O  CYS A 148           
SHEET    3   G 3 ARG A 176  SER A 180 -1  N  SER A 180   O  MET A 136           
SHEET    1   H 2 GLY A 173  TYR A 175  0                                        
SHEET    2   H 2 LEU A 195  VAL A 197 -1  N  VAL A 197   O  GLY A 173           
SSBOND   1 CYS A   28    CYS A   79                          1555   1555  2.04  
SSBOND   2 CYS A  128    CYS A  177                          1555   1555  2.01  
CRYST1   91.300   91.300   61.400  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010953  0.006324  0.000000        0.00000                         
SCALE2      0.000000  0.012647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016287        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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