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Database: PDB
Entry: 3SWZ
LinkDB: 3SWZ
Original site: 3SWZ 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 14-JUL-11   3SWZ              
TITLE     HUMAN CYTOCHROME P450 17A1 IN COMPLEX WITH TOK-001                    
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, P450, CYP17A1, P450C17, P450 17A1, MONOOXYGENASE,    
KEYWDS   2 17A-HYDROXYLASE, 17, 20-LYASE, HEME PROTEIN, CYTOCHROME P450         
KEYWDS   3 OXIDOREDUCTASE, GALETERONE, MEMBRANE, TOK-001, VN/124-1, MICROSOME,  
KEYWDS   4 ENDOPLASMIC RETICULUM, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR       
KEYWDS   5 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.DEVORE,E.E.SCOTT                                                  
REVDAT   3   08-NOV-17 3SWZ    1       REMARK                                   
REVDAT   2   01-FEB-12 3SWZ    1       JRNL                                     
REVDAT   1   25-JAN-12 3SWZ    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.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 6.1.13                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 87320                          
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
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      : 4600                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6376                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 326                          
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14914                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 288                                     
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.294         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.218         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.339         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15568 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21166 ; 1.760 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1866 ; 6.968 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   677 ;38.796 ;24.564       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2776 ;19.506 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    80 ;21.151 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2374 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11539 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9346 ; 0.887 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15178 ; 1.569 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6222 ; 2.136 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5987 ; 3.434 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3SWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066756.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-11                          
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   : 92007                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 15.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 15.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER MR                                             
REMARK 200 STARTING MODEL: PDB ENTRY 3RUK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
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       45.70750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.82800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.04500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.82800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.70750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.04500            
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     ASN A   277                                                      
REMARK 465     ALA A   278                                                      
REMARK 465     GLY A   279                                                      
REMARK 465     PRO A   280                                                      
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     ASN C   277                                                      
REMARK 465     ALA C   278                                                      
REMARK 465     GLY C   279                                                      
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     ASN D   275                                                      
REMARK 465     GLY D   276                                                      
REMARK 465     ASN D   277                                                      
REMARK 465     ALA D   278                                                      
REMARK 465     GLY D   279                                                      
REMARK 465     PRO D   280                                                      
REMARK 465     ASP D   281                                                      
REMARK 465     GLN D   282                                                      
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: 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 D  41   CA  -  N   -  CD  ANGL. DEV. = -12.9 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    ARG A  45       26.35     49.97                                   
REMARK 500    ASN A 107       61.14     38.72                                   
REMARK 500    ASN A 108       72.43     54.98                                   
REMARK 500    ASP A 137      109.34   -177.77                                   
REMARK 500    GLN A 140       57.19   -105.48                                   
REMARK 500    ASP A 212     -121.23   -118.02                                   
REMARK 500    ASN A 272       30.51    -75.32                                   
REMARK 500    SER A 273       51.54   -140.55                                   
REMARK 500    LEU A 370     -142.19     45.96                                   
REMARK 500    PHE A 412       95.53    -69.49                                   
REMARK 500    LYS A 481     -152.71   -133.60                                   
REMARK 500    ALA A 502       22.36    -64.34                                   
REMARK 500    LYS B  71      108.78    -47.85                                   
REMARK 500    ASN B 108       63.39     71.72                                   
REMARK 500    ASP B 212     -121.45   -111.09                                   
REMARK 500    LYS B 251      -39.37    -39.69                                   
REMARK 500    SER B 273     -152.45    -83.17                                   
REMARK 500    LEU B 287       31.24   -146.16                                   
REMARK 500    SER B 288      173.33    -57.01                                   
REMARK 500    LEU B 370     -134.20     42.09                                   
REMARK 500    SER B 379     -159.99   -131.38                                   
REMARK 500    GLN B 408       65.96     30.20                                   
REMARK 500    TYR B 432      105.85   -160.80                                   
REMARK 500    LEU B 433       58.47   -141.03                                   
REMARK 500    ALA B 437      161.59    179.57                                   
REMARK 500    LYS B 481     -154.69   -127.04                                   
REMARK 500    ALA B 502       37.74    -90.22                                   
REMARK 500    PRO C  44     -160.85    -62.26                                   
REMARK 500    ARG C  45      -54.65    158.08                                   
REMARK 500    HIS C  46       85.16    -58.01                                   
REMARK 500    ILE C  87      -71.14   -108.90                                   
REMARK 500    ILE C 112      -65.40   -127.39                                   
REMARK 500    LEU C 134       16.58   -164.78                                   
REMARK 500    GLN C 140       44.27    -90.43                                   
REMARK 500    ASN C 161      110.80    -34.14                                   
REMARK 500    ASN C 275      162.22    -35.58                                   
REMARK 500    SER C 284      -78.07    -60.99                                   
REMARK 500    VAL C 336      -47.55   -131.14                                   
REMARK 500    LEU C 370     -142.78     54.19                                   
REMARK 500    LEU C 433       56.35   -144.66                                   
REMARK 500    LYS C 481     -159.80   -148.93                                   
REMARK 500    GLN C 497      -71.32    -50.67                                   
REMARK 500    LEU D  31      -21.78     82.67                                   
REMARK 500    HIS D  46       15.71     51.14                                   
REMARK 500    ILE D  87      -66.56    -99.61                                   
REMARK 500    LYS D  89       45.53    -98.91                                   
REMARK 500    ASN D 108       48.96     75.29                                   
REMARK 500    LEU D 134       10.33    -68.31                                   
REMARK 500    ASN D 161      115.90    -36.92                                   
REMARK 500    PRO D 225       58.15    -66.89                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 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 D 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TOK D 601   N51                                                    
REMARK 620 2 HEM D 600   NA   86.0                                              
REMARK 620 3 HEM D 600   NB   92.4  87.9                                        
REMARK 620 4 HEM D 600   NC   94.9 177.8  90.1                                  
REMARK 620 5 HEM D 600   ND   89.3  94.1 177.5  87.9                            
REMARK 620 6 CYS D 442   SG  172.8  97.2  81.3  81.6  96.8                      
REMARK 620 N                    1     2     3     4     5                       
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 TOK C 601   N51                                                    
REMARK 620 2 HEM C 600   NA   89.8                                              
REMARK 620 3 HEM C 600   NB   89.0  89.2                                        
REMARK 620 4 HEM C 600   NC   91.5 178.6  90.5                                  
REMARK 620 5 HEM C 600   ND   90.3  92.8 177.9  87.5                            
REMARK 620 6 CYS C 442   SG  172.7  95.0  85.6  83.7  94.9                      
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 TOK A 601   N51                                                    
REMARK 620 2 HEM A 600   NA   88.7                                              
REMARK 620 3 HEM A 600   NB   97.5  88.7                                        
REMARK 620 4 HEM A 600   NC   91.1 178.6  92.7                                  
REMARK 620 5 HEM A 600   ND   82.6  89.5 178.2  89.1                            
REMARK 620 6 CYS A 442   SG  175.3  96.0  82.4  84.2  97.7                      
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 TOK B 601   N51                                                    
REMARK 620 2 HEM B 600   NA   95.5                                              
REMARK 620 3 HEM B 600   NB   89.4  96.1                                        
REMARK 620 4 HEM B 600   NC   84.5 178.5  85.3                                  
REMARK 620 5 HEM B 600   ND   91.8  84.6 178.4  93.9                            
REMARK 620 6 CYS B 442   SG  168.9  93.1  82.6  87.1  96.0                      
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 TOK 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 TOK 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 TOK 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 TOK D 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RUK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CYTOCHROME P450 17A1 WITH ABIRATERONE             
DBREF  3SWZ A   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  3SWZ B   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  3SWZ C   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  3SWZ D   24   508  UNP    P05093   CP17A_HUMAN     24    508             
SEQADV 3SWZ MET A   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ ALA A   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS A   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS A   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ THR A   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS A  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS A  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS A  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS A  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ MET B   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ ALA B   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS B   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS B   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ THR B   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS B  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS B  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS B  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS B  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ MET C   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ ALA C   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS C   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS C   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ THR C   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS C  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS C  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS C  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS C  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ MET D   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ ALA D   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS D   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ LYS D   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ THR D   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS D  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS D  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ HIS D  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 3SWZ 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    TOK  A 601      29                                                       
HET    HEM  B 600      43                                                       
HET    TOK  B 601      29                                                       
HET    HEM  C 600      43                                                       
HET    TOK  C 601      29                                                       
HET    HEM  D 600      43                                                       
HET    TOK  D 601      29                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     TOK (3ALPHA,8ALPHA)-17-(1H-BENZIMIDAZOL-1-YL)ANDROSTA-5,16-          
HETNAM   2 TOK  DIEN-3-OL                                                       
HETSYN     HEM HEME                                                             
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  TOK    4(C26 H32 N2 O)                                              
FORMUL  13  HOH   *88(H2 O)                                                     
HELIX    1   1 HIS A   48  LEU A   56  1                                   9    
HELIX    2   2 LEU A   56  GLY A   61  1                                   6    
HELIX    3   3 HIS A   78  ILE A   87  1                                  10    
HELIX    4   4 MET A   99  SER A  106  1                                   8    
HELIX    5   5 GLY A  118  PHE A  132  1                                  15    
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  ILE A  223  5                                   5    
HELIX   10  10 LYS A  227  LYS A  251  1                                  25    
HELIX   11  11 ASN A  261  ASN A  272  1                                  12    
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  VAL A  336  1                                  16    
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 ALA A  437  SER A  441  5                                   5    
HELIX   20  20 GLY A  444  ARG A  462  1                                  19    
HELIX   21  21 ARG A  496  ALA A  502  1                                   7    
HELIX   22  22 HIS B   48  LEU B   56  1                                   9    
HELIX   23  23 LEU B   56  GLY B   61  1                                   6    
HELIX   24  24 HIS B   78  ILE B   87  1                                  10    
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  THR B  159  1                                  19    
HELIX   28  28 ILE B  167  ASN B  185  1                                  19    
HELIX   29  29 PRO B  193  SER B  210  1                                  18    
HELIX   30  30 PRO B  219  PHE B  224  1                                   6    
HELIX   31  31 LYS B  227  PHE B  254  1                                  28    
HELIX   32  32 ASN B  261  SER B  273  1                                  13    
HELIX   33  33 SER B  284  LEU B  287  5                                   4    
HELIX   34  34 SER B  288  ASN B  321  1                                  34    
HELIX   35  35 ASN B  321  VAL B  336  1                                  16    
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  401  1                                   7    
HELIX   39  39 MET B  413  LEU B  418  5                                   6    
HELIX   40  40 GLY B  444  ARG B  462  1                                  19    
HELIX   41  41 ARG B  496  ALA B  502  1                                   7    
HELIX   42  42 HIS C   48  LEU C   56  1                                   9    
HELIX   43  43 LEU C   56  GLY C   61  1                                   6    
HELIX   44  44 HIS C   78  ILE C   87  1                                  10    
HELIX   45  45 MET C   99  SER C  106  1                                   8    
HELIX   46  46 GLY C  118  ALA C  133  1                                  16    
HELIX   47  47 LYS C  141  THR C  159  1                                  19    
HELIX   48  48 ILE C  167  ASN C  185  1                                  19    
HELIX   49  49 PRO C  193  SER C  210  1                                  18    
HELIX   50  50 LYS C  227  PHE C  254  1                                  28    
HELIX   51  51 ASN C  261  ASN C  275  1                                  15    
HELIX   52  52 SER C  284  LEU C  287  5                                   4    
HELIX   53  53 SER C  288  HIS C  320  1                                  33    
HELIX   54  54 ASN C  321  VAL C  336  1                                  16    
HELIX   55  55 THR C  343  ARG C  349  5                                   7    
HELIX   56  56 LEU C  350  ARG C  364  1                                  15    
HELIX   57  57 ASN C  395  HIS C  401  1                                   7    
HELIX   58  58 MET C  413  LEU C  418  5                                   6    
HELIX   59  59 ALA C  437  SER C  441  5                                   5    
HELIX   60  60 GLY C  444  ARG C  462  1                                  19    
HELIX   61  61 ARG C  496  GLN C  503  1                                   8    
HELIX   62  62 HIS D   48  LEU D   56  1                                   9    
HELIX   63  63 LEU D   56  GLY D   61  1                                   6    
HELIX   64  64 HIS D   78  ILE D   87  1                                  10    
HELIX   65  65 GLY D   90  SER D   94  5                                   5    
HELIX   66  66 MET D   99  SER D  106  1                                   8    
HELIX   67  67 GLY D  118  LEU D  134  1                                  17    
HELIX   68  68 LYS D  141  ALA D  158  1                                  18    
HELIX   69  69 THR D  159  ASN D  161  5                                   3    
HELIX   70  70 ILE D  167  ASN D  185  1                                  19    
HELIX   71  71 PRO D  193  SER D  210  1                                  18    
HELIX   72  72 LYS D  227  ASN D  249  1                                  23    
HELIX   73  73 ASN D  261  ASN D  272  1                                  12    
HELIX   74  74 SER D  288  LEU D  319  1                                  32    
HELIX   75  75 ASN D  321  VAL D  336  1                                  16    
HELIX   76  76 THR D  343  ASN D  348  5                                   6    
HELIX   77  77 LEU D  350  ARG D  364  1                                  15    
HELIX   78  78 ASN D  395  HIS D  400  1                                   6    
HELIX   79  79 HIS D  401  TRP D  406  5                                   6    
HELIX   80  80 MET D  413  LEU D  418  5                                   6    
HELIX   81  81 ALA D  437  SER D  441  5                                   5    
HELIX   82  82 GLY D  444  PHE D  463  1                                  20    
HELIX   83  83 ARG D  496  ALA D  502  1                                   7    
SHEET    1   A 5 LEU A  36  LEU A  40  0                                        
SHEET    2   A 5 ILE D  63  MET D  68  1  O  ARG D  67   N  LEU A  40           
SHEET    3   A 5 LYS D  71  VAL D  76 -1  O  ILE D  75   N  TYR D  64           
SHEET    4   A 5 GLU D 391  ILE D 394  1  O  ILE D 393   N  VAL D  74           
SHEET    5   A 5 HIS D 373  LYS D 374 -1  N  HIS D 373   O  VAL D 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  MET A  68   O  LYS A  71           
SHEET    5   B 5 LEU D  36  LEU D  40  1  O  GLY D  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  ILE A 493   N  GLN A 163           
SHEET    3   C 3 PHE A 463  GLU A 466 -1  N  ASP A 464   O  LYS A 494           
SHEET    1   D 2 SER A 379  ILE A 381  0                                        
SHEET    2   D 2 PHE A 384  VAL A 386 -1  O  VAL A 386   N  SER A 379           
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 C  63  MET C  68  1  O  ARG C  67   N  LEU B  40           
SHEET    3   F 5 LYS C  71  VAL C  76 -1  O  ILE C  75   N  TYR C  64           
SHEET    4   F 5 GLU C 391  ILE C 394  1  O  GLU C 391   N  VAL C  74           
SHEET    5   F 5 HIS C 373  LYS C 374 -1  N  HIS C 373   O  VAL C 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  GLU B 391           
SHEET    4   G 5 ILE B  63  MET B  68 -1  N  VAL B  66   O  THR B  73           
SHEET    5   G 5 LEU C  36  LEU C  40  1  O  LEU C  40   N  ARG B  67           
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  PHE B 384   N  ILE B 381           
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 SER D 164  ILE D 165  0                                        
SHEET    2   M 2 VAL D 491  LYS D 492 -1  O  VAL D 491   N  ILE D 165           
SHEET    1   N 2 SER D 379  ILE D 381  0                                        
SHEET    2   N 2 PHE D 384  VAL D 386 -1  O  VAL D 386   N  SER D 379           
SHEET    1   O 2 ILE D 479  PRO D 480  0                                        
SHEET    2   O 2 PHE D 484  LEU D 485 -1  O  LEU D 485   N  ILE D 479           
LINK        FE   HEM D 600                 N51 TOK D 601     1555   1555  2.14  
LINK        FE   HEM C 600                 N51 TOK C 601     1555   1555  2.21  
LINK        FE   HEM A 600                 N51 TOK A 601     1555   1555  2.23  
LINK        FE   HEM B 600                 N51 TOK B 601     1555   1555  2.26  
LINK         SG  CYS B 442                FE   HEM B 600     1555   1555  2.28  
LINK         SG  CYS C 442                FE   HEM C 600     1555   1555  2.36  
LINK         SG  CYS D 442                FE   HEM D 600     1555   1555  2.50  
LINK         SG  CYS A 442                FE   HEM A 600     1555   1555  2.64  
SITE     1 AC1 22 ARG A  96  ILE A 112  ALA A 113  TRP A 121                    
SITE     2 AC1 22 ARG A 125  PHE A 132  ALA A 302  THR A 306                    
SITE     3 AC1 22 VAL A 310  VAL A 366  LEU A 370  ILE A 371                    
SITE     4 AC1 22 HIS A 373  PRO A 434  PHE A 435  ARG A 440                    
SITE     5 AC1 22 SER A 441  CYS A 442  ILE A 443  GLY A 444                    
SITE     6 AC1 22 ALA A 448  TOK A 601                                          
SITE     1 AC2 10 ALA A 113  PHE A 114  ASN A 202  ILE A 205                    
SITE     2 AC2 10 ALA A 302  THR A 306  VAL A 366  ALA A 367                    
SITE     3 AC2 10 VAL A 482  HEM A 600                                          
SITE     1 AC3 19 ARG B  96  ILE B 112  ALA B 113  TRP B 121                    
SITE     2 AC3 19 ARG B 125  ILE B 299  GLY B 303  THR B 306                    
SITE     3 AC3 19 VAL B 366  LEU B 370  ILE B 371  HIS B 373                    
SITE     4 AC3 19 PRO B 434  PHE B 435  ARG B 440  CYS B 442                    
SITE     5 AC3 19 GLY B 444  ALA B 448  TOK B 601                               
SITE     1 AC4 13 ALA B 113  PHE B 114  TYR B 201  ASN B 202                    
SITE     2 AC4 13 ILE B 205  GLY B 297  ASP B 298  ALA B 302                    
SITE     3 AC4 13 THR B 306  VAL B 366  ALA B 367  VAL B 482                    
SITE     4 AC4 13 HEM B 600                                                     
SITE     1 AC5 22 ARG C  96  ILE C 112  ALA C 113  TRP C 121                    
SITE     2 AC5 22 ARG C 125  PHE C 132  ALA C 302  GLY C 303                    
SITE     3 AC5 22 THR C 306  VAL C 366  LEU C 370  ILE C 371                    
SITE     4 AC5 22 HIS C 373  PRO C 434  PHE C 435  ARG C 440                    
SITE     5 AC5 22 SER C 441  CYS C 442  ILE C 443  GLY C 444                    
SITE     6 AC5 22 ALA C 448  TOK C 601                                          
SITE     1 AC6 12 ALA C 113  PHE C 114  TYR C 201  ASN C 202                    
SITE     2 AC6 12 ILE C 205  GLY C 297  ASP C 298  THR C 306                    
SITE     3 AC6 12 ALA C 367  VAL C 482  VAL C 483  HEM C 600                    
SITE     1 AC7 20 ARG D  96  ILE D 112  ALA D 113  TRP D 121                    
SITE     2 AC7 20 ARG D 125  ALA D 302  THR D 306  VAL D 310                    
SITE     3 AC7 20 VAL D 366  LEU D 370  ILE D 371  HIS D 373                    
SITE     4 AC7 20 PRO D 434  PHE D 435  ARG D 440  CYS D 442                    
SITE     5 AC7 20 ILE D 443  GLY D 444  ALA D 448  TOK D 601                    
SITE     1 AC8 13 ALA D 113  PHE D 114  TYR D 201  ASN D 202                    
SITE     2 AC8 13 ILE D 205  GLY D 297  ASP D 298  ALA D 302                    
SITE     3 AC8 13 THR D 306  VAL D 366  ALA D 367  VAL D 482                    
SITE     4 AC8 13 HEM D 600                                                     
CRYST1   91.415  152.090  167.656  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      0.010939  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006575  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005965        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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