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Database: PDB
Entry: 1A30
LinkDB: 1A30
Original site: 1A30 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           27-JAN-98   1A30              
TITLE     HIV-1 PROTEASE COMPLEXED WITH A TRIPEPTIDE INHIBITOR                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIV-1 PROTEASE;                                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.23.16;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRIPEPTIDE GLU-ASP-LEU;                                    
COMPND   9 CHAIN: C;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 STRAIN: ISOLATE HXB2;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET-11 A;                                  
SOURCE   9 MOL_ID: 2                                                            
KEYWDS    ASPARTIC PROTEASE, HIV PROTEASE, HYDROLASE-HYDROLASE INHIBITOR        
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.LOUIS,F.DYDA,N.T.NASHED,A.R.KIMMEL,D.R.DAVIES                     
REVDAT   5   07-FEB-24 1A30    1       REMARK                                   
REVDAT   4   03-NOV-21 1A30    1       SEQADV                                   
REVDAT   3   13-JUL-11 1A30    1       VERSN                                    
REVDAT   2   24-FEB-09 1A30    1       VERSN                                    
REVDAT   1   29-APR-98 1A30    0                                                
JRNL        AUTH   J.M.LOUIS,F.DYDA,N.T.NASHED,A.R.KIMMEL,D.R.DAVIES            
JRNL        TITL   HYDROPHILIC PEPTIDES DERIVED FROM THE TRANSFRAME REGION OF   
JRNL        TITL 2 GAG-POL INHIBIT THE HIV-1 PROTEASE.                          
JRNL        REF    BIOCHEMISTRY                  V.  37  2105 1998              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9485357                                                      
JRNL        DOI    10.1021/BI972059X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 13987                          
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) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 724                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.97                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1238                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700                       
REMARK   3   BIN FREE R VALUE                    : 0.2998                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.31                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 59                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.003                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1536                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 216                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.00000                                              
REMARK   3    B22 (A**2) : 1.00000                                              
REMARK   3    B33 (A**2) : 1.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.381                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.39                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.230                           
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000170328.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAY-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14128                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.7                               
REMARK 200  DATA REDUNDANCY                : 4.630                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.12100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.12100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: USING ISOMORPHOUS TO         
REMARK 200  PREVIOUS STRUCTURE                                                  
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.2                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       29.23500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.22000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.23500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.22000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9280 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  41    CG   CD   NE   CZ   NH1  NH2                        
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    GLU A  35      116.96    -34.48                                   
REMARK 500    PRO A  79       50.80    -69.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF TRIPEPTIDE GLU-ASP     
REMARK 800  -LEU                                                                
DBREF  1A30 A    1    99  UNP    P04585   POL_HV1H2       69    167             
DBREF  1A30 B    1    99  UNP    P04585   POL_HV1H2       69    167             
DBREF  1A30 C  506   508  PDB    1A30     1A30           506    508             
SEQADV 1A30 LYS A    7  UNP  P04585    GLN    75 ENGINEERED MUTATION            
SEQADV 1A30 ILE A   33  UNP  P04585    LEU   101 ENGINEERED MUTATION            
SEQADV 1A30 ILE A   63  UNP  P04585    LEU   131 ENGINEERED MUTATION            
SEQADV 1A30 LYS B    7  UNP  P04585    GLN    75 ENGINEERED MUTATION            
SEQADV 1A30 ILE B   33  UNP  P04585    LEU   101 ENGINEERED MUTATION            
SEQADV 1A30 ILE B   63  UNP  P04585    LEU   131 ENGINEERED MUTATION            
SEQRES   1 A   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 A   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 A   99  GLY ALA ASP ASP THR VAL ILE GLU GLU MET SER LEU PRO          
SEQRES   4 A   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 A   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE ILE ILE GLU          
SEQRES   6 A   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 A   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 A   99  GLN ILE GLY CYS THR LEU ASN PHE                              
SEQRES   1 B   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 B   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 B   99  GLY ALA ASP ASP THR VAL ILE GLU GLU MET SER LEU PRO          
SEQRES   4 B   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 B   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE ILE ILE GLU          
SEQRES   6 B   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 B   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 B   99  GLN ILE GLY CYS THR LEU ASN PHE                              
SEQRES   1 C    3  GLU ASP LEU                                                  
FORMUL   4  HOH   *216(H2 O)                                                    
HELIX    1   1 ARG A   87  LEU A   90  1                                   4    
HELIX    2   2 ARG B   87  LEU B   90  1                                   4    
SHEET    1   A 4 GLN A  18  LEU A  23  0                                        
SHEET    2   A 4 LEU A  10  ILE A  15 -1  N  ILE A  15   O  GLN A  18           
SHEET    3   A 4 ILE A  62  ILE A  66 -1  N  GLU A  65   O  LYS A  14           
SHEET    4   A 4 HIS A  69  GLY A  73 -1  N  GLY A  73   O  ILE A  62           
SHEET    1   B 4 VAL A  32  GLU A  34  0                                        
SHEET    2   B 4 VAL A  75  GLY A  78  1  N  LEU A  76   O  ILE A  33           
SHEET    3   B 4 GLY A  52  TYR A  59 -1  N  TYR A  59   O  VAL A  75           
SHEET    4   B 4 TRP A  42  GLY A  49 -1  N  GLY A  49   O  GLY A  52           
SHEET    1   C 2 LEU B  10  ILE B  15  0                                        
SHEET    2   C 2 GLN B  18  LEU B  23 -1  N  ALA B  22   O  VAL B  11           
SHEET    1   D 3 LYS B  43  GLY B  48  0                                        
SHEET    2   D 3 PHE B  53  TYR B  59 -1  N  GLN B  58   O  LYS B  43           
SHEET    3   D 3 VAL B  75  GLY B  78 -1  N  VAL B  77   O  ARG B  57           
SHEET    1   E 2 ILE B  62  ILE B  66  0                                        
SHEET    2   E 2 HIS B  69  GLY B  73 -1  N  GLY B  73   O  ILE B  62           
SITE     1 AC1 15 ASP A  25  GLY A  27  ALA A  28  ASP A  29                    
SITE     2 AC1 15 ASP A  30  ILE A  47  GLY A  48  ILE A  50                    
SITE     3 AC1 15 HOH A1076  ARG B   8  ASP B  25  VAL B  82                    
SITE     4 AC1 15 HOH C1075  HOH C1092  HOH C1097                               
CRYST1   58.470   86.440   45.810  90.00  90.00  90.00 P 21 21 2     8          
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      0.017103  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011569  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021829        0.00000                         
MTRIX1   1 -0.341600  0.828700 -0.443400        0.45720    1                    
MTRIX2   1  0.828700  0.043000 -0.558100       14.52920    1                    
MTRIX3   1 -0.443400 -0.558100 -0.701400       27.83140    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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