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Database: PDB
Entry: 1PQ2
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Original site: 1PQ2 
HEADER    OXIDOREDUCTASE                          17-JUN-03   1PQ2              
TITLE     CRYSTAL STRUCTURE OF HUMAN DRUG METABOLIZING CYTOCHROME P450 2C8      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2C8;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYPIIC8, P450 FORM 1, P450 MP- 12/MP-20, P450 IIC2, S-      
COMPND   5 MEPHENYTOIN 4-HYDROXYLASE;                                           
COMPND   6 EC: 1.14.14.1;                                                       
COMPND   7 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: CYP2C8;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYTOCHROME P450, CYP2C8, MEMBRANE PROTEIN, TAXOL 6-HYDROXYLASE,       
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.A.SCHOCH,J.K.YANO,M.R.WESTER,K.J.GRIFFIN,C.D.STOUT,E.F.JOHNSON      
REVDAT   4   27-OCT-21 1PQ2    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 1PQ2    1       VERSN                                    
REVDAT   2   30-MAR-04 1PQ2    1       JRNL                                     
REVDAT   1   13-JAN-04 1PQ2    0                                                
JRNL        AUTH   G.A.SCHOCH,J.K.YANO,M.R.WESTER,K.J.GRIFFIN,C.D.STOUT,        
JRNL        AUTH 2 E.F.JOHNSON                                                  
JRNL        TITL   STRUCTURE OF HUMAN MICROSOMAL CYTOCHROME P450 2C8. EVIDENCE  
JRNL        TITL 2 FOR A PERIPHERAL FATTY ACID BINDING SITE                     
JRNL        REF    J.BIOL.CHEM.                  V. 279  9497 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14676196                                                     
JRNL        DOI    10.1074/JBC.M312516200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
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)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34573                          
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) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1751                            
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            : 7386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 127                                     
REMARK   3   SOLVENT ATOMS            : 37                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.49                            
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) : 0.50                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.55                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.652                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.03                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.562                           
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  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: NULL                                      
REMARK   4                                                                      
REMARK   4 1PQ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019487.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38682                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1N6B                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ETHANOL, PEG 4000, HEPES, SODIUM         
REMARK 280  CHLORIDE, CYMAL-6 , PH 7.5, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       52.99400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.70250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       52.99400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       68.70250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     HIS A   491                                                      
REMARK 465     HIS A   492                                                      
REMARK 465     HIS A   493                                                      
REMARK 465     HIS A   494                                                      
REMARK 465     MET B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     HIS B   491                                                      
REMARK 465     HIS B   492                                                      
REMARK 465     HIS B   493                                                      
REMARK 465     HIS B   494                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  35   C   -  N   -  CD  ANGL. DEV. = -20.2 DEGREES          
REMARK 500    PRO A  35   CA  -  N   -  CD  ANGL. DEV. = -20.7 DEGREES          
REMARK 500    PRO A  63   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ASN A  99   CA  -  C   -  N   ANGL. DEV. = -14.4 DEGREES          
REMARK 500    PRO A 101   CA  -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PRO B  37   CA  -  N   -  CD  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    PRO B  37   N   -  CA  -  C   ANGL. DEV. =  19.7 DEGREES          
REMARK 500    GLY B  70   N   -  CA  -  C   ANGL. DEV. = -16.0 DEGREES          
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    PRO A  31      174.55    -57.79                                   
REMARK 500    MET A  42      -14.15    -41.59                                   
REMARK 500    LYS A  48      -87.01    -75.97                                   
REMARK 500    ILE A  88      -71.28    -94.80                                   
REMARK 500    ILE A 106      -71.83    -60.85                                   
REMARK 500    LYS A 160       29.45     49.93                                   
REMARK 500    LYS A 185      127.95   -179.28                                   
REMARK 500    TYR A 189      -16.09    -41.69                                   
REMARK 500    PRO A 220      -11.79    -47.97                                   
REMARK 500    ALA A 253        0.03    -68.87                                   
REMARK 500    SER A 254       27.16   -140.94                                   
REMARK 500    ASP A 276      -86.50    -77.68                                   
REMARK 500    ASN A 277      -44.17      9.55                                   
REMARK 500    GLN A 278       60.89     10.20                                   
REMARK 500    LYS A 279      -16.28   -172.09                                   
REMARK 500    THR A 299      -74.23    -97.04                                   
REMARK 500    ARG A 377       83.61     20.16                                   
REMARK 500    ASN A 378       -0.49     80.00                                   
REMARK 500    LYS A 383      122.78    -35.85                                   
REMARK 500    HIS A 396       31.20    -98.28                                   
REMARK 500    ASN A 403       63.37     60.55                                   
REMARK 500    ASP A 408      109.92   -169.36                                   
REMARK 500    LYS A 415      -10.69    -46.64                                   
REMARK 500    SER A 429      172.63     75.92                                   
REMARK 500    ARG A 433       43.32    -99.42                                   
REMARK 500    VAL A 461       32.45    -89.29                                   
REMARK 500    ASP A 462     -169.82    174.31                                   
REMARK 500    THR A 473       49.17    -97.32                                   
REMARK 500    PRO B  37      -33.26    -39.44                                   
REMARK 500    LYS B  48      -95.45    -67.40                                   
REMARK 500    VAL B  60      -65.40    -93.36                                   
REMARK 500    PHE B  69      -83.70   -108.84                                   
REMARK 500    ILE B  88      -81.36    -87.82                                   
REMARK 500    ILE B 106      -75.62    -74.87                                   
REMARK 500    ILE B 112      -60.89    -98.60                                   
REMARK 500    LYS B 160       46.37     76.42                                   
REMARK 500    GLN B 184       -3.55     95.06                                   
REMARK 500    TYR B 189       37.87    -70.11                                   
REMARK 500    LYS B 190      -29.37   -152.10                                   
REMARK 500    ASP B 191      108.70    -41.29                                   
REMARK 500    SER B 210      136.19    -38.04                                   
REMARK 500    LYS B 275      -73.82     -5.47                                   
REMARK 500    ASP B 276       68.78   -107.59                                   
REMARK 500    GLN B 278      -86.85     50.06                                   
REMARK 500    LYS B 279      -17.70    -42.95                                   
REMARK 500    THR B 299      -75.65    -85.96                                   
REMARK 500    ARG B 333       28.00   -144.22                                   
REMARK 500    ASP B 360       45.40     36.57                                   
REMARK 500    ARG B 377       79.23     20.20                                   
REMARK 500    ASN B 378       -5.80     88.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 435   SG                                                     
REMARK 620 2 HEM A 500   NA   96.0                                              
REMARK 620 3 HEM A 500   NB   90.4  90.0                                        
REMARK 620 4 HEM A 500   NC   83.4 178.3  91.6                                  
REMARK 620 5 HEM A 500   ND   89.9  89.3 179.4  89.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 435   SG                                                     
REMARK 620 2 HEM B 500   NA   93.7                                              
REMARK 620 3 HEM B 500   NB   84.5  89.0                                        
REMARK 620 4 HEM B 500   NC   86.3 179.1  91.9                                  
REMARK 620 5 HEM B 500   ND   96.3  89.7 178.5  89.4                            
REMARK 620 N                    1     2     3     4                             
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 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DT6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF MAMMALIAN CYTOCHROME P450                               
REMARK 900 RELATED ID: 1N6B   RELATED DB: PDB                                   
REMARK 900 MICROSOMAL CYTOCHROME P450 2C5/3LVDH COMPLEX WITH A DIMETHYL         
REMARK 900 DERIVATIVE OF SULFAPHENAZOLE                                         
DBREF  1PQ2 A   28   490  UNP    P10632   CP2C8_HUMAN     28    490             
DBREF  1PQ2 B   28   490  UNP    P10632   CP2C8_HUMAN     28    490             
SEQADV 1PQ2 MET A   19  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 ALA A   20  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 LYS A   21  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 LYS A   22  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 THR A   23  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 SER A   24  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 SER A   25  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 LYS A   26  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 GLY A   27  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 HIS A  491  UNP  P10632              EXPRESSION TAG                 
SEQADV 1PQ2 HIS A  492  UNP  P10632              EXPRESSION TAG                 
SEQADV 1PQ2 HIS A  493  UNP  P10632              EXPRESSION TAG                 
SEQADV 1PQ2 HIS A  494  UNP  P10632              EXPRESSION TAG                 
SEQADV 1PQ2 MET B   19  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 ALA B   20  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 LYS B   21  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 LYS B   22  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 THR B   23  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 SER B   24  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 SER B   25  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 LYS B   26  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 GLY B   27  UNP  P10632              ENGINEERED MUTATION            
SEQADV 1PQ2 HIS B  491  UNP  P10632              EXPRESSION TAG                 
SEQADV 1PQ2 HIS B  492  UNP  P10632              EXPRESSION TAG                 
SEQADV 1PQ2 HIS B  493  UNP  P10632              EXPRESSION TAG                 
SEQADV 1PQ2 HIS B  494  UNP  P10632              EXPRESSION TAG                 
SEQRES   1 A  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 A  476  GLY PRO THR PRO LEU PRO ILE ILE GLY ASN MET LEU GLN          
SEQRES   3 A  476  ILE ASP VAL LYS ASP ILE CYS LYS SER PHE THR ASN PHE          
SEQRES   4 A  476  SER LYS VAL TYR GLY PRO VAL PHE THR VAL TYR PHE GLY          
SEQRES   5 A  476  MET ASN PRO ILE VAL VAL PHE HIS GLY TYR GLU ALA VAL          
SEQRES   6 A  476  LYS GLU ALA LEU ILE ASP ASN GLY GLU GLU PHE SER GLY          
SEQRES   7 A  476  ARG GLY ASN SER PRO ILE SER GLN ARG ILE THR LYS GLY          
SEQRES   8 A  476  LEU GLY ILE ILE SER SER ASN GLY LYS ARG TRP LYS GLU          
SEQRES   9 A  476  ILE ARG ARG PHE SER LEU THR THR LEU ARG ASN PHE GLY          
SEQRES  10 A  476  MET GLY LYS ARG SER ILE GLU ASP ARG VAL GLN GLU GLU          
SEQRES  11 A  476  ALA HIS CYS LEU VAL GLU GLU LEU ARG LYS THR LYS ALA          
SEQRES  12 A  476  SER PRO CYS ASP PRO THR PHE ILE LEU GLY CYS ALA PRO          
SEQRES  13 A  476  CYS ASN VAL ILE CYS SER VAL VAL PHE GLN LYS ARG PHE          
SEQRES  14 A  476  ASP TYR LYS ASP GLN ASN PHE LEU THR LEU MET LYS ARG          
SEQRES  15 A  476  PHE ASN GLU ASN PHE ARG ILE LEU ASN SER PRO TRP ILE          
SEQRES  16 A  476  GLN VAL CYS ASN ASN PHE PRO LEU LEU ILE ASP CYS PHE          
SEQRES  17 A  476  PRO GLY THR HIS ASN LYS VAL LEU LYS ASN VAL ALA LEU          
SEQRES  18 A  476  THR ARG SER TYR ILE ARG GLU LYS VAL LYS GLU HIS GLN          
SEQRES  19 A  476  ALA SER LEU ASP VAL ASN ASN PRO ARG ASP PHE ILE ASP          
SEQRES  20 A  476  CYS PHE LEU ILE LYS MET GLU GLN GLU LYS ASP ASN GLN          
SEQRES  21 A  476  LYS SER GLU PHE ASN ILE GLU ASN LEU VAL GLY THR VAL          
SEQRES  22 A  476  ALA ASP LEU PHE VAL ALA GLY THR GLU THR THR SER THR          
SEQRES  23 A  476  THR LEU ARG TYR GLY LEU LEU LEU LEU LEU LYS HIS PRO          
SEQRES  24 A  476  GLU VAL THR ALA LYS VAL GLN GLU GLU ILE ASP HIS VAL          
SEQRES  25 A  476  ILE GLY ARG HIS ARG SER PRO CYS MET GLN ASP ARG SER          
SEQRES  26 A  476  HIS MET PRO TYR THR ASP ALA VAL VAL HIS GLU ILE GLN          
SEQRES  27 A  476  ARG TYR SER ASP LEU VAL PRO THR GLY VAL PRO HIS ALA          
SEQRES  28 A  476  VAL THR THR ASP THR LYS PHE ARG ASN TYR LEU ILE PRO          
SEQRES  29 A  476  LYS GLY THR THR ILE MET ALA LEU LEU THR SER VAL LEU          
SEQRES  30 A  476  HIS ASP ASP LYS GLU PHE PRO ASN PRO ASN ILE PHE ASP          
SEQRES  31 A  476  PRO GLY HIS PHE LEU ASP LYS ASN GLY ASN PHE LYS LYS          
SEQRES  32 A  476  SER ASP TYR PHE MET PRO PHE SER ALA GLY LYS ARG ILE          
SEQRES  33 A  476  CYS ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 A  476  PHE LEU THR THR ILE LEU GLN ASN PHE ASN LEU LYS SER          
SEQRES  35 A  476  VAL ASP ASP LEU LYS ASN LEU ASN THR THR ALA VAL THR          
SEQRES  36 A  476  LYS GLY ILE VAL SER LEU PRO PRO SER TYR GLN ILE CYS          
SEQRES  37 A  476  PHE ILE PRO VAL HIS HIS HIS HIS                              
SEQRES   1 B  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 B  476  GLY PRO THR PRO LEU PRO ILE ILE GLY ASN MET LEU GLN          
SEQRES   3 B  476  ILE ASP VAL LYS ASP ILE CYS LYS SER PHE THR ASN PHE          
SEQRES   4 B  476  SER LYS VAL TYR GLY PRO VAL PHE THR VAL TYR PHE GLY          
SEQRES   5 B  476  MET ASN PRO ILE VAL VAL PHE HIS GLY TYR GLU ALA VAL          
SEQRES   6 B  476  LYS GLU ALA LEU ILE ASP ASN GLY GLU GLU PHE SER GLY          
SEQRES   7 B  476  ARG GLY ASN SER PRO ILE SER GLN ARG ILE THR LYS GLY          
SEQRES   8 B  476  LEU GLY ILE ILE SER SER ASN GLY LYS ARG TRP LYS GLU          
SEQRES   9 B  476  ILE ARG ARG PHE SER LEU THR THR LEU ARG ASN PHE GLY          
SEQRES  10 B  476  MET GLY LYS ARG SER ILE GLU ASP ARG VAL GLN GLU GLU          
SEQRES  11 B  476  ALA HIS CYS LEU VAL GLU GLU LEU ARG LYS THR LYS ALA          
SEQRES  12 B  476  SER PRO CYS ASP PRO THR PHE ILE LEU GLY CYS ALA PRO          
SEQRES  13 B  476  CYS ASN VAL ILE CYS SER VAL VAL PHE GLN LYS ARG PHE          
SEQRES  14 B  476  ASP TYR LYS ASP GLN ASN PHE LEU THR LEU MET LYS ARG          
SEQRES  15 B  476  PHE ASN GLU ASN PHE ARG ILE LEU ASN SER PRO TRP ILE          
SEQRES  16 B  476  GLN VAL CYS ASN ASN PHE PRO LEU LEU ILE ASP CYS PHE          
SEQRES  17 B  476  PRO GLY THR HIS ASN LYS VAL LEU LYS ASN VAL ALA LEU          
SEQRES  18 B  476  THR ARG SER TYR ILE ARG GLU LYS VAL LYS GLU HIS GLN          
SEQRES  19 B  476  ALA SER LEU ASP VAL ASN ASN PRO ARG ASP PHE ILE ASP          
SEQRES  20 B  476  CYS PHE LEU ILE LYS MET GLU GLN GLU LYS ASP ASN GLN          
SEQRES  21 B  476  LYS SER GLU PHE ASN ILE GLU ASN LEU VAL GLY THR VAL          
SEQRES  22 B  476  ALA ASP LEU PHE VAL ALA GLY THR GLU THR THR SER THR          
SEQRES  23 B  476  THR LEU ARG TYR GLY LEU LEU LEU LEU LEU LYS HIS PRO          
SEQRES  24 B  476  GLU VAL THR ALA LYS VAL GLN GLU GLU ILE ASP HIS VAL          
SEQRES  25 B  476  ILE GLY ARG HIS ARG SER PRO CYS MET GLN ASP ARG SER          
SEQRES  26 B  476  HIS MET PRO TYR THR ASP ALA VAL VAL HIS GLU ILE GLN          
SEQRES  27 B  476  ARG TYR SER ASP LEU VAL PRO THR GLY VAL PRO HIS ALA          
SEQRES  28 B  476  VAL THR THR ASP THR LYS PHE ARG ASN TYR LEU ILE PRO          
SEQRES  29 B  476  LYS GLY THR THR ILE MET ALA LEU LEU THR SER VAL LEU          
SEQRES  30 B  476  HIS ASP ASP LYS GLU PHE PRO ASN PRO ASN ILE PHE ASP          
SEQRES  31 B  476  PRO GLY HIS PHE LEU ASP LYS ASN GLY ASN PHE LYS LYS          
SEQRES  32 B  476  SER ASP TYR PHE MET PRO PHE SER ALA GLY LYS ARG ILE          
SEQRES  33 B  476  CYS ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 B  476  PHE LEU THR THR ILE LEU GLN ASN PHE ASN LEU LYS SER          
SEQRES  35 B  476  VAL ASP ASP LEU LYS ASN LEU ASN THR THR ALA VAL THR          
SEQRES  36 B  476  LYS GLY ILE VAL SER LEU PRO PRO SER TYR GLN ILE CYS          
SEQRES  37 B  476  PHE ILE PRO VAL HIS HIS HIS HIS                              
HET    PO4  A 504       5                                                       
HET    HEM  A 500      43                                                       
HET    PLM  A 502      18                                                       
HET    PLM  B 501      18                                                       
HET    HEM  B 500      43                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     PLM PALMITIC ACID                                                    
HETSYN     HEM HEME                                                             
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   5  PLM    2(C16 H32 O2)                                                
FORMUL   8  HOH   *37(H2 O)                                                     
HELIX    1   1 ASP A   49  GLY A   62  1                                  14    
HELIX    2   2 GLY A   79  ILE A   88  1                                  10    
HELIX    3   3 ASN A   90  SER A   95  1                                   6    
HELIX    4   4 SER A  100  LYS A  108  1                                   9    
HELIX    5   5 ASN A  116  LEU A  131  1                                  16    
HELIX    6   6 SER A  140  LYS A  158  1                                  19    
HELIX    7   7 PRO A  166  GLN A  184  1                                  19    
HELIX    8   8 ASP A  191  ASN A  209  1                                  19    
HELIX    9   9 TRP A  212  ASN A  217  1                                   6    
HELIX   10  10 LEU A  221  CYS A  225  5                                   5    
HELIX   11  11 PHE A  226  ALA A  253  1                                  28    
HELIX   12  12 ASP A  262  GLN A  273  1                                  12    
HELIX   13  13 ASN A  283  THR A  299  1                                  17    
HELIX   14  14 THR A  299  HIS A  316  1                                  18    
HELIX   15  15 HIS A  316  ILE A  331  1                                  16    
HELIX   16  16 CYS A  338  HIS A  344  5                                   7    
HELIX   17  17 MET A  345  ASP A  360  1                                  16    
HELIX   18  18 LEU A  390  HIS A  396  1                                   7    
HELIX   19  19 ASP A  408  LEU A  413  5                                   6    
HELIX   20  20 GLY A  437  PHE A  456  1                                  20    
HELIX   21  21 ASN B   41  ILE B   45  5                                   5    
HELIX   22  22 ASP B   49  GLY B   62  1                                  14    
HELIX   23  23 GLY B   79  ILE B   88  1                                  10    
HELIX   24  24 GLU B   92  GLY B   96  5                                   5    
HELIX   25  25 SER B  100  LYS B  108  1                                   9    
HELIX   26  26 ASN B  116  LEU B  131  1                                  16    
HELIX   27  27 SER B  140  LEU B  156  1                                  17    
HELIX   28  28 PHE B  168  PHE B  183  1                                  16    
HELIX   29  29 ASP B  191  LYS B  199  1                                   9    
HELIX   30  30 ARG B  200  SER B  210  1                                  11    
HELIX   31  31 PRO B  211  PHE B  219  1                                   9    
HELIX   32  32 PRO B  220  CYS B  225  5                                   6    
HELIX   33  33 PHE B  226  LEU B  255  1                                  30    
HELIX   34  34 ASP B  262  GLU B  274  1                                  13    
HELIX   35  35 ASN B  283  THR B  299  1                                  17    
HELIX   36  36 THR B  299  HIS B  316  1                                  18    
HELIX   37  37 HIS B  316  ILE B  331  1                                  16    
HELIX   38  38 GLN B  340  HIS B  344  5                                   5    
HELIX   39  39 MET B  345  ASP B  360  1                                  16    
HELIX   40  40 LEU B  390  HIS B  396  1                                   7    
HELIX   41  41 ASP B  408  LEU B  413  5                                   6    
HELIX   42  42 ALA B  430  ILE B  434  5                                   5    
HELIX   43  43 GLY B  437  ASN B  455  1                                  19    
HELIX   44  44 ASP B  463  LEU B  467  5                                   5    
SHEET    1   A 4 VAL A  64  PHE A  69  0                                        
SHEET    2   A 4 ASN A  72  PHE A  77 -1  O  ILE A  74   N  VAL A  67           
SHEET    3   A 4 THR A 386  ALA A 389  1  O  MET A 388   N  VAL A  75           
SHEET    4   A 4 HIS A 368  ALA A 369 -1  N  HIS A 368   O  ILE A 387           
SHEET    1   B 3 PRO A 163  CYS A 164  0                                        
SHEET    2   B 3 ILE A 485  ILE A 488 -1  O  ILE A 485   N  CYS A 164           
SHEET    3   B 3 ASN A 457  SER A 460 -1  N  ASN A 457   O  ILE A 488           
SHEET    1   C 2 THR A 374  PHE A 376  0                                        
SHEET    2   C 2 TYR A 379  ILE A 381 -1  O  ILE A 381   N  THR A 374           
SHEET    1   D 4 VAL B  64  TYR B  68  0                                        
SHEET    2   D 4 PRO B  73  PHE B  77 -1  O  VAL B  76   N  PHE B  65           
SHEET    3   D 4 THR B 386  ALA B 389  1  O  MET B 388   N  PHE B  77           
SHEET    4   D 4 HIS B 368  ALA B 369 -1  N  HIS B 368   O  ILE B 387           
SHEET    1   E 2 THR B 374  PHE B 376  0                                        
SHEET    2   E 2 TYR B 379  ILE B 381 -1  O  ILE B 381   N  THR B 374           
SHEET    1   F 2 PHE B 456  LYS B 459  0                                        
SHEET    2   F 2 CYS B 486  PRO B 489 -1  O  CYS B 486   N  LYS B 459           
LINK         SG  CYS A 435                FE   HEM A 500     1555   1555  2.23  
LINK         SG  CYS B 435                FE   HEM B 500     1555   1555  2.20  
SITE     1 AC1  3 ILE A 331  HIS A 334  ARG A 335                               
SITE     1 AC2 18 ARG A  97  ILE A 112  TRP A 120  ARG A 124                    
SITE     2 AC2 18 LEU A 131  ALA A 297  GLY A 298  THR A 301                    
SITE     3 AC2 18 GLN A 356  LEU A 361  VAL A 366  HIS A 368                    
SITE     4 AC2 18 PHE A 428  SER A 429  ARG A 433  CYS A 435                    
SITE     5 AC2 18 ALA A 436  ALA A 441                                          
SITE     1 AC3 10 ARG A 105  ILE A 106  THR A 229  HIS A 230                    
SITE     2 AC3 10 LEU A 234  PHE B 226  PRO B 227  GLY B 228                    
SITE     3 AC3 10 THR B 229  HOH B 601                                          
SITE     1 AC4 21 ARG B  97  ILE B 112  ILE B 113  TRP B 120                    
SITE     2 AC4 21 ARG B 124  LEU B 294  ALA B 297  GLY B 298                    
SITE     3 AC4 21 THR B 301  THR B 302  THR B 305  LEU B 361                    
SITE     4 AC4 21 HIS B 368  PRO B 427  PHE B 428  SER B 429                    
SITE     5 AC4 21 ARG B 433  CYS B 435  ALA B 436  GLY B 437                    
SITE     6 AC4 21 ALA B 441                                                     
SITE     1 AC5 11 PHE A 226  PRO A 227  GLY A 228  THR A 229                    
SITE     2 AC5 11 ARG B 105  ILE B 106  TRP B 212  CYS B 216                    
SITE     3 AC5 11 ILE B 223  THR B 229  LEU B 234                               
CRYST1  105.988  137.405   97.322  90.00 112.51  90.00 C 1 2 1       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      0.009435  0.000000  0.003910        0.00000                         
SCALE2      0.000000  0.007278  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011123        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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