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Database: PDB
Entry: 3RUK
LinkDB: 3RUK
Original site: 3RUK 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 05-MAY-11   3RUK              
TITLE     HUMAN CYTOCHROME P450 CYP17A1 IN COMPLEX WITH ABIRATERONE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 24-508;                                       
COMPND   5 SYNONYM: CYPXVII, CYTOCHROME P450 17A1, CYTOCHROME P450-C17,         
COMPND   6 CYTOCHROME P450C17, STEROID 17-ALPHA-MONOOXYGENASE;                  
COMPND   7 EC: 1.14.99.9;                                                       
COMPND   8 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: CYP17, CYP17A1, S17AH;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI+                                   
KEYWDS    CYTOCHROME P450, CYP17A1, P450 17A1, MONOOXYGENASE, 17A-HYDROXYLASE,  
KEYWDS   2 17, 20-LYASE, HEME PROTEIN, CYTOCHROME P450 OXIDOREDUCTASE,          
KEYWDS   3 ABIRATERONE, ZYTIGA, 17A-HYDROXYLATION, MEMBRANE, MICROSOME,         
KEYWDS   4 ENDOPLASMIC RETICULUM, GALETERONE, OXIDOREDUCTASE-OXIDOREDUCTASE     
KEYWDS   5 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.DEVORE,E.E.SCOTT                                                  
REVDAT   3   08-NOV-17 3RUK    1       REMARK                                   
REVDAT   2   01-FEB-12 3RUK    1       JRNL                                     
REVDAT   1   25-JAN-12 3RUK    0                                                
JRNL        AUTH   N.M.DEVORE,E.E.SCOTT                                         
JRNL        TITL   STRUCTURES OF CYTOCHROME P450 17A1 WITH PROSTATE CANCER      
JRNL        TITL 2 DRUGS ABIRATERONE AND TOK-001.                               
JRNL        REF    NATURE                        V. 482   116 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22266943                                                     
JRNL        DOI    10.1038/NATURE10743                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 6.1.13                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 66758                          
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 + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3531                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14921                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 276                                     
REMARK   3   SOLVENT ATOMS            : 118                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.09000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.368         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.280         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.297        
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000065394.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : RH COATED FLAT MIRROR, TOROIDAL    
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: CYP2R1                                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.175 M TRIS, 0.30 M       
REMARK 280  AMMONIUM SULFATE, 3% GLYCEROL, PH 8.5, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 298K                                              
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       42.90650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.44100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.04900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.44100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.90650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.04900            
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, 3, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     GLY A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     TYR A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     ASP A   274                                                      
REMARK 465     ASN A   275                                                      
REMARK 465     GLY A   276                                                      
REMARK 465     ASN A   277                                                      
REMARK 465     ALA A   278                                                      
REMARK 465     GLY A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     ASP A   281                                                      
REMARK 465     GLN A   282                                                      
REMARK 465     ALA A   504                                                      
REMARK 465     GLU A   505                                                      
REMARK 465     GLY A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     THR A   508                                                      
REMARK 465     HIS A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     HIS A   512                                                      
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     GLY B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     TYR B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     ASN B   275                                                      
REMARK 465     GLY B   276                                                      
REMARK 465     ASN B   277                                                      
REMARK 465     ALA B   278                                                      
REMARK 465     GLY B   279                                                      
REMARK 465     PRO B   280                                                      
REMARK 465     ASP B   281                                                      
REMARK 465     GLN B   282                                                      
REMARK 465     ALA B   504                                                      
REMARK 465     GLU B   505                                                      
REMARK 465     GLY B   506                                                      
REMARK 465     SER B   507                                                      
REMARK 465     THR B   508                                                      
REMARK 465     HIS B   509                                                      
REMARK 465     HIS B   510                                                      
REMARK 465     HIS B   511                                                      
REMARK 465     HIS B   512                                                      
REMARK 465     MET C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     LYS C    21                                                      
REMARK 465     LYS C    22                                                      
REMARK 465     THR C    23                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     LYS C    26                                                      
REMARK 465     TYR C    27                                                      
REMARK 465     PRO C    28                                                      
REMARK 465     LYS C    29                                                      
REMARK 465     SER C    30                                                      
REMARK 465     GLN C   503                                                      
REMARK 465     ALA C   504                                                      
REMARK 465     GLU C   505                                                      
REMARK 465     GLY C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     THR C   508                                                      
REMARK 465     HIS C   509                                                      
REMARK 465     HIS C   510                                                      
REMARK 465     HIS C   511                                                      
REMARK 465     HIS C   512                                                      
REMARK 465     MET D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     LYS D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     LYS D    26                                                      
REMARK 465     TYR D    27                                                      
REMARK 465     PRO D    28                                                      
REMARK 465     LYS D    29                                                      
REMARK 465     SER D    30                                                      
REMARK 465     ALA D   504                                                      
REMARK 465     GLU D   505                                                      
REMARK 465     GLY D   506                                                      
REMARK 465     SER D   507                                                      
REMARK 465     THR D   508                                                      
REMARK 465     HIS D   509                                                      
REMARK 465     HIS D   510                                                      
REMARK 465     HIS D   511                                                      
REMARK 465     HIS D   512                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASN C   275     N    ASN C   277              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 C 280   C   -  N   -  CD  ANGL. DEV. = -19.4 DEGREES          
REMARK 500    PRO D 280   C   -  N   -  CD  ANGL. DEV. = -18.4 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    ILE A  87      -74.44   -105.73                                   
REMARK 500    ASN A 108       62.72     64.56                                   
REMARK 500    LEU A 134       14.77    -58.97                                   
REMARK 500    PHE A 135       25.34   -140.63                                   
REMARK 500    GLN A 140       45.77    -98.23                                   
REMARK 500    PHE A 184       -8.00   -143.50                                   
REMARK 500    ASP A 212     -124.89   -116.81                                   
REMARK 500    VAL A 215       82.51    -67.20                                   
REMARK 500    MET A 271      -74.09    -63.62                                   
REMARK 500    ASN A 272      -39.51    -37.59                                   
REMARK 500    SER A 288      174.65    -56.93                                   
REMARK 500    SER A 345      -16.60    -49.64                                   
REMARK 500    LEU A 370     -140.78     34.04                                   
REMARK 500    SER A 379     -157.22   -169.60                                   
REMARK 500    LYS A 388      123.59    -38.89                                   
REMARK 500    GLN A 408       67.35     82.98                                   
REMARK 500    TYR A 432      115.12   -161.85                                   
REMARK 500    LEU A 433       65.67   -154.93                                   
REMARK 500    ALA A 437      151.24    179.31                                   
REMARK 500    ASP A 469      -35.51    -37.49                                   
REMARK 500    LYS A 481     -156.05   -145.85                                   
REMARK 500    GLU A 501       17.30    -51.59                                   
REMARK 500    ALA A 502       38.60   -147.63                                   
REMARK 500    ILE B  87      -75.74   -112.02                                   
REMARK 500    ARG B 109       38.89     72.39                                   
REMARK 500    LEU B 134       -7.94    -54.56                                   
REMARK 500    ASP B 212     -139.44    -95.17                                   
REMARK 500    ASN B 335      -27.33   -141.82                                   
REMARK 500    LEU B 350       57.01    -96.04                                   
REMARK 500    LEU B 370     -145.20     41.32                                   
REMARK 500    SER B 379     -159.80   -158.90                                   
REMARK 500    GLU B 383       26.32   -146.07                                   
REMARK 500    GLN B 408       66.18     34.92                                   
REMARK 500    MET B 413       78.90   -153.06                                   
REMARK 500    LEU B 433       54.36   -148.67                                   
REMARK 500    LYS B 481     -148.86   -123.38                                   
REMARK 500    GLN B 497      -66.51    -24.25                                   
REMARK 500    LEU C  43       84.05   -151.85                                   
REMARK 500    ARG C 109       36.93     71.45                                   
REMARK 500    ILE C 112      -64.51   -121.89                                   
REMARK 500    ALA C 113      -56.29    -29.75                                   
REMARK 500    LEU C 134        8.17    -69.25                                   
REMARK 500    ASP C 137      129.84    174.55                                   
REMARK 500    PRO C 225       67.97    -66.79                                   
REMARK 500    ASP C 274      -64.07    -91.36                                   
REMARK 500    ALA C 278      -22.48     51.65                                   
REMARK 500    SER C 284      -79.67    -20.31                                   
REMARK 500    SER C 288      165.66    -47.69                                   
REMARK 500    GLN C 334       30.63    -89.35                                   
REMARK 500    ASN C 335      -31.07   -158.58                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 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 C 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 442   SG                                                     
REMARK 620 2 HEM C 600   NA   92.4                                              
REMARK 620 3 HEM C 600   NB   84.9  89.8                                        
REMARK 620 4 HEM C 600   NC   89.6 177.4  88.7                                  
REMARK 620 5 HEM C 600   ND   99.3  90.1 175.8  91.3                            
REMARK 620 6 AER C 601   N22 172.9  89.7  88.3  88.1  87.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AER A 601   N22                                                    
REMARK 620 2 HEM A 600   NA   87.7                                              
REMARK 620 3 HEM A 600   NB   93.9  89.3                                        
REMARK 620 4 HEM A 600   NC   90.9 178.6  91.1                                  
REMARK 620 5 HEM A 600   ND   83.8  92.3 177.1  87.3                            
REMARK 620 6 CYS A 442   SG  177.3  92.1  88.8  89.3  93.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 442   SG                                                     
REMARK 620 2 HEM B 600   NA   90.1                                              
REMARK 620 3 HEM B 600   NB   86.6  83.1                                        
REMARK 620 4 HEM B 600   NC   89.0 178.9  96.3                                  
REMARK 620 5 HEM B 600   ND   93.1  96.1 179.2  84.4                            
REMARK 620 6 AER B 601   N22 178.8  90.1  94.6  90.8  85.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AER D 601   N22                                                    
REMARK 620 2 HEM D 600   NA   84.8                                              
REMARK 620 3 HEM D 600   NB   84.5  92.9                                        
REMARK 620 4 HEM D 600   NC   96.0 178.8  86.4                                  
REMARK 620 5 HEM D 600   ND   97.9  87.7 177.6  92.9                            
REMARK 620 6 CYS D 442   SG  165.3  95.1  80.9  83.8  96.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AER A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AER B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AER C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AER D 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SWZ   RELATED DB: PDB                                   
DBREF  3RUK A   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  3RUK B   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  3RUK C   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  3RUK D   24   508  UNP    P05093   CP17A_HUMAN     24    508             
SEQADV 3RUK MET A   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK ALA A   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS A   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS A   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK THR A   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS A  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS A  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS A  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS A  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK MET B   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK ALA B   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS B   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS B   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK THR B   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS B  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS B  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS B  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS B  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK MET C   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK ALA C   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS C   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS C   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK THR C   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS C  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS C  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS C  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS C  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK MET D   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK ALA D   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS D   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK LYS D   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK THR D   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS D  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS D  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS D  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3RUK HIS D  512  UNP  P05093              EXPRESSION TAG                 
SEQRES   1 A  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 A  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 A  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 A  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 A  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 A  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 A  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 A  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 A  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 A  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 A  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 A  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 A  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 A  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 A  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 A  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 A  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 A  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 A  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 A  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 A  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 A  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 A  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 A  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 A  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 A  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 A  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 A  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 A  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 A  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 A  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 A  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 A  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 A  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 A  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 A  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 A  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 A  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 B  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 B  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 B  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 B  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 B  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 B  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 B  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 B  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 B  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 B  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 B  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 B  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 B  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 B  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 B  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 B  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 B  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 B  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 B  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 B  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 B  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 B  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 B  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 B  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 B  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 B  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 B  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 B  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 B  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 B  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 B  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 B  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 B  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 B  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 B  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 B  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 B  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 B  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 C  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 C  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 C  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 C  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 C  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 C  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 C  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 C  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 C  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 C  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 C  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 C  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 C  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 C  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 C  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 C  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 C  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 C  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 C  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 C  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 C  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 C  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 C  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 C  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 C  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 C  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 C  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 C  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 C  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 C  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 C  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 C  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 C  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 C  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 C  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 C  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 C  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 C  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 D  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 D  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 D  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 D  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 D  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 D  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 D  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 D  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 D  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 D  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 D  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 D  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 D  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 D  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 D  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 D  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 D  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 D  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 D  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 D  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 D  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 D  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 D  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 D  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 D  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 D  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 D  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 D  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 D  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 D  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 D  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 D  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 D  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 D  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 D  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 D  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 D  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 D  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
HET    HEM  A 600      43                                                       
HET    AER  A 601      26                                                       
HET    HEM  B 600      43                                                       
HET    AER  B 601      26                                                       
HET    HEM  C 600      43                                                       
HET    AER  C 601      26                                                       
HET    HEM  D 600      43                                                       
HET    AER  D 601      26                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     AER ABIRATERONE                                                      
HETSYN     HEM HEME                                                             
HETSYN     AER (3S,8R,9S,10R,13S,14S)-10,13-DIMETHYL-17-PYRIDIN-3-YL-           
HETSYN   2 AER  2,3,4,7,8,9,11,12,14,15-DECAHYDRO-1H-                           
HETSYN   3 AER  CYCLOPENTA[A]PHENANTHREN-3-OL                                   
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  AER    4(C24 H31 N O)                                               
FORMUL  13  HOH   *118(H2 O)                                                    
HELIX    1   1 HIS A   48  GLY A   61  1                                  14    
HELIX    2   2 HIS A   78  ILE A   87  1                                  10    
HELIX    3   3 LYS A   89  SER A   94  1                                   6    
HELIX    4   4 MET A   99  SER A  106  1                                   8    
HELIX    5   5 GLY A  118  LEU A  134  1                                  17    
HELIX    6   6 LYS A  141  HIS A  160  1                                  20    
HELIX    7   7 ILE A  167  ASN A  185  1                                  19    
HELIX    8   8 PRO A  193  SER A  210  1                                  18    
HELIX    9   9 PRO A  219  PHE A  224  1                                   6    
HELIX   10  10 LYS A  227  ASN A  249  1                                  23    
HELIX   11  11 ASN A  261  SER A  273  1                                  13    
HELIX   12  12 SER A  284  LEU A  287  5                                   4    
HELIX   13  13 SER A  288  ASN A  321  1                                  34    
HELIX   14  14 ASN A  321  GLY A  337  1                                  17    
HELIX   15  15 THR A  343  ARG A  349  5                                   7    
HELIX   16  16 LEU A  350  ARG A  364  1                                  15    
HELIX   17  17 ASN A  395  ASN A  402  1                                   8    
HELIX   18  18 MET A  413  LEU A  418  5                                   6    
HELIX   19  19 GLY A  444  ARG A  462  1                                  19    
HELIX   20  20 ARG A  496  GLU A  501  1                                   6    
HELIX   21  21 HIS B   48  LEU B   56  1                                   9    
HELIX   22  22 LEU B   56  GLY B   61  1                                   6    
HELIX   23  23 HIS B   78  ILE B   87  1                                  10    
HELIX   24  24 LYS B   89  PHE B   93  5                                   5    
HELIX   25  25 MET B   99  SER B  106  1                                   8    
HELIX   26  26 GLY B  118  LEU B  134  1                                  17    
HELIX   27  27 LYS B  141  ALA B  158  1                                  18    
HELIX   28  28 THR B  159  ASN B  161  5                                   3    
HELIX   29  29 ILE B  167  ASN B  185  1                                  19    
HELIX   30  30 ASP B  192  SER B  210  1                                  19    
HELIX   31  31 PRO B  219  PHE B  224  1                                   6    
HELIX   32  32 LYS B  227  ASN B  249  1                                  23    
HELIX   33  33 ASN B  261  SER B  273  1                                  13    
HELIX   34  34 SER B  288  ASN B  321  1                                  34    
HELIX   35  35 ASN B  321  GLY B  337  1                                  17    
HELIX   36  36 THR B  343  ARG B  349  5                                   7    
HELIX   37  37 LEU B  350  ARG B  364  1                                  15    
HELIX   38  38 ASN B  395  HIS B  400  1                                   6    
HELIX   39  39 MET B  413  LEU B  418  5                                   6    
HELIX   40  40 ALA B  437  SER B  441  5                                   5    
HELIX   41  41 GLY B  444  ARG B  462  1                                  19    
HELIX   42  42 ARG B  496  GLU B  501  1                                   6    
HELIX   43  43 HIS C   48  LEU C   56  1                                   9    
HELIX   44  44 LEU C   56  GLY C   61  1                                   6    
HELIX   45  45 HIS C   78  ILE C   87  1                                  10    
HELIX   46  46 MET C   99  SER C  106  1                                   8    
HELIX   47  47 GLY C  118  THR C  131  1                                  14    
HELIX   48  48 PHE C  132  LYS C  136  5                                   5    
HELIX   49  49 LYS C  141  THR C  159  1                                  19    
HELIX   50  50 ILE C  167  ASN C  185  1                                  19    
HELIX   51  51 PRO C  193  SER C  210  1                                  18    
HELIX   52  52 LYS C  227  PHE C  254  1                                  28    
HELIX   53  53 ASN C  261  ASN C  275  1                                  15    
HELIX   54  54 PRO C  280  LEU C  287  5                                   8    
HELIX   55  55 SER C  288  LEU C  318  1                                  31    
HELIX   56  56 ASN C  321  GLN C  334  1                                  14    
HELIX   57  57 THR C  343  ARG C  349  5                                   7    
HELIX   58  58 LEU C  350  ARG C  364  1                                  15    
HELIX   59  59 ASN C  395  ASN C  402  1                                   8    
HELIX   60  60 MET C  413  LEU C  418  5                                   6    
HELIX   61  61 ALA C  437  SER C  441  5                                   5    
HELIX   62  62 GLY C  444  ARG C  462  1                                  19    
HELIX   63  63 GLN C  497  ARG C  500  5                                   4    
HELIX   64  64 HIS D   48  LEU D   56  1                                   9    
HELIX   65  65 LEU D   56  GLY D   61  1                                   6    
HELIX   66  66 HIS D   78  ILE D   87  1                                  10    
HELIX   67  67 MET D   99  SER D  106  1                                   8    
HELIX   68  68 GLY D  118  PHE D  132  1                                  15    
HELIX   69  69 ALA D  133  LYS D  136  5                                   4    
HELIX   70  70 LYS D  141  HIS D  160  1                                  20    
HELIX   71  71 ILE D  167  ASN D  185  1                                  19    
HELIX   72  72 PRO D  193  SER D  210  1                                  18    
HELIX   73  73 LYS D  227  PHE D  254  1                                  28    
HELIX   74  74 ASN D  261  SER D  273  1                                  13    
HELIX   75  75 PRO D  280  LEU D  287  5                                   8    
HELIX   76  76 SER D  288  ASN D  321  1                                  34    
HELIX   77  77 ASN D  321  VAL D  336  1                                  16    
HELIX   78  78 THR D  343  ASN D  348  5                                   6    
HELIX   79  79 LEU D  350  ARG D  364  1                                  15    
HELIX   80  80 ASN D  395  HIS D  400  1                                   6    
HELIX   81  81 MET D  413  LEU D  418  5                                   6    
HELIX   82  82 ALA D  437  SER D  441  5                                   5    
HELIX   83  83 GLY D  444  ARG D  462  1                                  19    
HELIX   84  84 ARG D  496  GLU D  501  1                                   6    
SHEET    1   A 5 LEU A  36  LEU A  40  0                                        
SHEET    2   A 5 ILE C  63  MET C  68  1  O  ARG C  67   N  GLY A  38           
SHEET    3   A 5 LYS C  71  VAL C  76 -1  O  LYS C  71   N  MET C  68           
SHEET    4   A 5 GLU C 391  ILE C 394  1  O  GLU C 391   N  VAL C  74           
SHEET    5   A 5 HIS C 373  LYS C 374 -1  N  HIS C 373   O  VAL C 392           
SHEET    1   B 5 HIS A 373  LYS A 374  0                                        
SHEET    2   B 5 GLU A 391  ILE A 394 -1  O  VAL A 392   N  HIS A 373           
SHEET    3   B 5 LYS A  71  VAL A  76  1  N  VAL A  74   O  GLU A 391           
SHEET    4   B 5 ILE A  63  MET A  68 -1  N  TYR A  64   O  ILE A  75           
SHEET    5   B 5 LEU C  36  LEU C  40  1  O  GLY C  38   N  ARG A  67           
SHEET    1   C 3 GLN A 163  ILE A 165  0                                        
SHEET    2   C 3 VAL A 491  VAL A 495 -1  O  VAL A 491   N  ILE A 165           
SHEET    3   C 3 PHE A 463  GLU A 466 -1  N  GLU A 466   O  LYS A 492           
SHEET    1   D 2 SER A 379  ILE A 381  0                                        
SHEET    2   D 2 PHE A 384  VAL A 386 -1  O  PHE A 384   N  ILE A 381           
SHEET    1   E 2 ILE A 479  PRO A 480  0                                        
SHEET    2   E 2 PHE A 484  LEU A 485 -1  O  LEU A 485   N  ILE A 479           
SHEET    1   F 5 LEU B  36  LEU B  40  0                                        
SHEET    2   F 5 ILE D  63  MET D  68  1  O  SER D  65   N  VAL B  37           
SHEET    3   F 5 LYS D  71  VAL D  76 -1  O  LYS D  71   N  MET D  68           
SHEET    4   F 5 GLU D 391  ILE D 394  1  O  ILE D 393   N  VAL D  74           
SHEET    5   F 5 HIS D 373  LYS D 374 -1  N  HIS D 373   O  VAL D 392           
SHEET    1   G 5 HIS B 373  LYS B 374  0                                        
SHEET    2   G 5 GLU B 391  ILE B 394 -1  O  VAL B 392   N  HIS B 373           
SHEET    3   G 5 LYS B  71  VAL B  76  1  N  VAL B  74   O  ILE B 393           
SHEET    4   G 5 ILE B  63  MET B  68 -1  N  MET B  68   O  LYS B  71           
SHEET    5   G 5 LEU D  36  LEU D  40  1  O  VAL D  37   N  SER B  65           
SHEET    1   H 3 GLN B 163  ILE B 165  0                                        
SHEET    2   H 3 VAL B 491  VAL B 495 -1  O  ILE B 493   N  GLN B 163           
SHEET    3   H 3 PHE B 463  GLU B 466 -1  N  ASP B 464   O  LYS B 494           
SHEET    1   I 2 SER B 379  ILE B 381  0                                        
SHEET    2   I 2 PHE B 384  VAL B 386 -1  O  VAL B 386   N  SER B 379           
SHEET    1   J 2 ILE B 479  PRO B 480  0                                        
SHEET    2   J 2 PHE B 484  LEU B 485 -1  O  LEU B 485   N  ILE B 479           
SHEET    1   K 3 SER C 164  ILE C 165  0                                        
SHEET    2   K 3 VAL C 491  VAL C 495 -1  O  VAL C 491   N  ILE C 165           
SHEET    3   K 3 PHE C 463  GLU C 466 -1  N  GLU C 466   O  LYS C 492           
SHEET    1   L 2 SER C 379  ILE C 381  0                                        
SHEET    2   L 2 PHE C 384  VAL C 386 -1  O  VAL C 386   N  SER C 379           
SHEET    1   M 2 ILE C 479  PRO C 480  0                                        
SHEET    2   M 2 PHE C 484  LEU C 485 -1  O  LEU C 485   N  ILE C 479           
SHEET    1   N 3 SER D 164  ILE D 165  0                                        
SHEET    2   N 3 VAL D 491  VAL D 495 -1  O  VAL D 491   N  ILE D 165           
SHEET    3   N 3 PHE D 463  GLU D 466 -1  N  GLU D 466   O  LYS D 492           
SHEET    1   O 2 SER D 379  ILE D 381  0                                        
SHEET    2   O 2 PHE D 384  VAL D 386 -1  O  VAL D 386   N  SER D 379           
SHEET    1   P 2 ILE D 479  PRO D 480  0                                        
SHEET    2   P 2 PHE D 484  LEU D 485 -1  O  LEU D 485   N  ILE D 479           
LINK         SG  CYS C 442                FE   HEM C 600     1555   1555  2.01  
LINK        FE   HEM A 600                 N22 AER A 601     1555   1555  2.04  
LINK         SG  CYS B 442                FE   HEM B 600     1555   1555  2.13  
LINK        FE   HEM B 600                 N22 AER B 601     1555   1555  2.19  
LINK        FE   HEM D 600                 N22 AER D 601     1555   1555  2.25  
LINK        FE   HEM C 600                 N22 AER C 601     1555   1555  2.27  
LINK         SG  CYS D 442                FE   HEM D 600     1555   1555  2.40  
LINK         SG  CYS A 442                FE   HEM A 600     1555   1555  1.90  
SITE     1 AC1 20 ARG A  96  ILE A 112  ALA A 113  TRP A 121                    
SITE     2 AC1 20 ARG A 125  ALA A 302  THR A 306  VAL A 310                    
SITE     3 AC1 20 LEU A 361  VAL A 366  LEU A 370  ILE A 371                    
SITE     4 AC1 20 HIS A 373  PRO A 434  PHE A 435  ARG A 440                    
SITE     5 AC1 20 CYS A 442  GLY A 444  ALA A 448  AER A 601                    
SITE     1 AC2  7 ALA A 113  ASN A 202  ILE A 205  ASP A 298                    
SITE     2 AC2  7 ALA A 302  THR A 306  HEM A 600                               
SITE     1 AC3 20 ARG B  96  ILE B 112  ALA B 113  TRP B 121                    
SITE     2 AC3 20 ARG B 125  ILE B 299  ALA B 302  GLY B 303                    
SITE     3 AC3 20 THR B 306  LEU B 361  VAL B 366  LEU B 370                    
SITE     4 AC3 20 ILE B 371  HIS B 373  PRO B 434  PHE B 435                    
SITE     5 AC3 20 ARG B 440  CYS B 442  GLY B 444  AER B 601                    
SITE     1 AC4  9 ALA B 113  PHE B 114  ASN B 202  ILE B 205                    
SITE     2 AC4  9 ILE B 206  LEU B 209  THR B 306  VAL B 482                    
SITE     3 AC4  9 HEM B 600                                                     
SITE     1 AC5 16 ARG C  96  ILE C 112  ALA C 113  TRP C 121                    
SITE     2 AC5 16 ARG C 125  THR C 306  VAL C 366  LEU C 370                    
SITE     3 AC5 16 ILE C 371  HIS C 373  PRO C 434  PHE C 435                    
SITE     4 AC5 16 ARG C 440  CYS C 442  ILE C 443  AER C 601                    
SITE     1 AC6  8 ALA C 113  PHE C 114  TYR C 201  ASN C 202                    
SITE     2 AC6  8 ILE C 205  GLY C 297  ASP C 298  HEM C 600                    
SITE     1 AC7 18 ARG D  96  ILE D 112  ALA D 113  TRP D 121                    
SITE     2 AC7 18 ARG D 125  ILE D 299  GLY D 303  THR D 306                    
SITE     3 AC7 18 VAL D 310  VAL D 366  LEU D 370  ILE D 371                    
SITE     4 AC7 18 HIS D 373  PRO D 434  PHE D 435  ARG D 440                    
SITE     5 AC7 18 CYS D 442  AER D 601                                          
SITE     1 AC8 10 ALA D 113  PHE D 114  TYR D 201  ASN D 202                    
SITE     2 AC8 10 ILE D 205  GLY D 297  ASP D 298  THR D 306                    
SITE     3 AC8 10 VAL D 366  HEM D 600                                          
CRYST1   85.813  152.098  172.882  90.00  90.00  90.00 P 21 21 21   16          
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      0.011653  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006575  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005784        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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