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Database: PDB
Entry: 1LHY
LinkDB: 1LHY
Original site: 1LHY 
HEADER    HYDROLASE                               17-APR-02   1LHY              
TITLE     CRYSTAL STRUCTURE OF TEM-30 BETA-LACTAMASE AT 2.0 ANGSTROM            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CLASS A BETA-LACTAMASE- TEM 30;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.5.2.6;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: BLA;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: SF120;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PALTER EX II                              
KEYWDS    BETA-LACTAMASE, ANTIBIOTIC RESISTANCE, TEM-30, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.WANG,G.MINASOV,B.K.SHOICHET                                         
REVDAT   5   16-AUG-23 1LHY    1       REMARK                                   
REVDAT   4   27-OCT-21 1LHY    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 1LHY    1       VERSN                                    
REVDAT   2   01-APR-03 1LHY    1       JRNL                                     
REVDAT   1   11-SEP-02 1LHY    0                                                
JRNL        AUTH   X.WANG,G.MINASOV,B.K.SHOICHET                                
JRNL        TITL   THE STRUCTURAL BASES OF ANTIBIOTIC RESISTANCE IN THE         
JRNL        TITL 2 CLINICALLY DERIVED MUTANT BETA-LACTAMASES TEM-30, TEM-32,    
JRNL        TITL 3 AND TEM-34.                                                  
JRNL        REF    J.BIOL.CHEM.                  V. 277 32149 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12058046                                                     
JRNL        DOI    10.1074/JBC.M204212200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 14112                          
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) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1400                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 0.88                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 135                          
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            : 2022                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.30100                                              
REMARK   3    B22 (A**2) : -11.43500                                            
REMARK   3    B33 (A**2) : 9.13400                                              
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) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.990                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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:                                           
REMARK   3  CRYSTALLOGRAPHIC CONJUGATE GRADIENT MINIMIZATION REFINEMENT USING   
REMARK   3  MAXIMUM                                                             
REMARK   3  LIKELIHOOD TARGET FOR AMPLITUDES                                    
REMARK   4                                                                      
REMARK   4 1LHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000015956.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 5ID-B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 14828                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
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: PDB ID 1JWP                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM-POTASSIUM BUFFER, PH 8.0, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       20.76600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.04850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.83500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.04850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.76600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.83500            
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: 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 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    MET A  69     -150.75     56.10                                   
REMARK 500    TYR A 105       81.24     60.22                                   
REMARK 500    ASN A 175       -1.86     71.60                                   
REMARK 500    LEU A 220     -128.62    -95.27                                   
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 RESIDUE PO4 A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LI0   RELATED DB: PDB                                   
REMARK 900 CLASS A BETA-LACTAMASE-TEM 32                                        
REMARK 900 RELATED ID: 1LI9   RELATED DB: PDB                                   
REMARK 900 CLASS A BETA-LACTAMASE-TEM 34                                        
DBREF  1LHY A   26   288  UNP    P62593   BLAT_ECOLI      24    286             
SEQADV 1LHY SER A  243  UNP  P62593    ARG   241 ENGINEERED MUTATION            
SEQRES   1 A  263  HIS PRO GLU THR LEU VAL LYS VAL LYS ASP ALA GLU ASP          
SEQRES   2 A  263  GLN LEU GLY ALA ARG VAL GLY TYR ILE GLU LEU ASP LEU          
SEQRES   3 A  263  ASN SER GLY LYS ILE LEU GLU SER PHE ARG PRO GLU GLU          
SEQRES   4 A  263  ARG PHE PRO MET MET SER THR PHE LYS VAL LEU LEU CYS          
SEQRES   5 A  263  GLY ALA VAL LEU SER ARG VAL ASP ALA GLY GLN GLU GLN          
SEQRES   6 A  263  LEU GLY ARG ARG ILE HIS TYR SER GLN ASN ASP LEU VAL          
SEQRES   7 A  263  GLU TYR SER PRO VAL THR GLU LYS HIS LEU THR ASP GLY          
SEQRES   8 A  263  MET THR VAL ARG GLU LEU CYS SER ALA ALA ILE THR MET          
SEQRES   9 A  263  SER ASP ASN THR ALA ALA ASN LEU LEU LEU THR THR ILE          
SEQRES  10 A  263  GLY GLY PRO LYS GLU LEU THR ALA PHE LEU HIS ASN MET          
SEQRES  11 A  263  GLY ASP HIS VAL THR ARG LEU ASP ARG TRP GLU PRO GLU          
SEQRES  12 A  263  LEU ASN GLU ALA ILE PRO ASN ASP GLU ARG ASP THR THR          
SEQRES  13 A  263  MET PRO ALA ALA MET ALA THR THR LEU ARG LYS LEU LEU          
SEQRES  14 A  263  THR GLY GLU LEU LEU THR LEU ALA SER ARG GLN GLN LEU          
SEQRES  15 A  263  ILE ASP TRP MET GLU ALA ASP LYS VAL ALA GLY PRO LEU          
SEQRES  16 A  263  LEU ARG SER ALA LEU PRO ALA GLY TRP PHE ILE ALA ASP          
SEQRES  17 A  263  LYS SER GLY ALA GLY GLU ARG GLY SER SER GLY ILE ILE          
SEQRES  18 A  263  ALA ALA LEU GLY PRO ASP GLY LYS PRO SER ARG ILE VAL          
SEQRES  19 A  263  VAL ILE TYR THR THR GLY SER GLN ALA THR MET ASP GLU          
SEQRES  20 A  263  ARG ASN ARG GLN ILE ALA GLU ILE GLY ALA SER LEU ILE          
SEQRES  21 A  263  LYS HIS TRP                                                  
HET    PO4  A   1       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2  PO4    O4 P 3-                                                      
FORMUL   3  HOH   *224(H2 O)                                                    
HELIX    1   1 HIS A   26  GLY A   41  1                                  16    
HELIX    2   2 THR A   71  ALA A   86  1                                  16    
HELIX    3   3 SER A   98  LEU A  102  5                                   5    
HELIX    4   4 VAL A  119  SER A  130  1                                  12    
HELIX    5   5 ASP A  131  GLY A  143  1                                  13    
HELIX    6   6 GLY A  143  MET A  155  1                                  13    
HELIX    7   7 PRO A  167  GLU A  171  5                                   5    
HELIX    8   8 MET A  182  GLY A  196  1                                  15    
HELIX    9   9 THR A  200  ALA A  213  1                                  14    
HELIX   10  10 LEU A  220  LEU A  225  5                                   6    
HELIX   11  11 THR A  271  HIS A  289  1                                  19    
SHEET    1   A 5 ILE A  56  PHE A  60  0                                        
SHEET    2   A 5 ARG A  43  ASP A  50 -1  N  TYR A  46   O  PHE A  60           
SHEET    3   A 5 ARG A 259  THR A 266 -1  O  ILE A 260   N  LEU A  49           
SHEET    4   A 5 SER A 243  GLY A 251 -1  N  ILE A 246   O  ILE A 263           
SHEET    5   A 5 PHE A 230  GLY A 238 -1  N  PHE A 230   O  GLY A 251           
SHEET    1   B 2 PHE A  66  PRO A  67  0                                        
SHEET    2   B 2 THR A 180  THR A 181 -1  O  THR A 181   N  PHE A  66           
SHEET    1   C 2 ARG A  94  ILE A  95  0                                        
SHEET    2   C 2 MET A 117  THR A 118 -1  O  MET A 117   N  ILE A  95           
SSBOND   1 CYS A   77    CYS A  123                          1555   1555  2.04  
CISPEP   1 GLU A  166    PRO A  167          0         0.00                     
SITE     1 AC1  2 GLY A  92  ARG A 120                                          
CRYST1   41.532   59.670   88.097  90.00  90.00  90.00 P 21 21 21    4          
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      0.024078  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016759  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011351        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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