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Database: PDB
Entry: 2NNH
LinkDB: 2NNH
Original site: 2NNH 
HEADER    OXIDOREDUCTASE,ELECTRON TRANSPORT       24-OCT-06   2NNH              
TITLE     CYP2C8DH COMPLEXED WITH 2 MOLECULES OF 9-CIS RETINOIC ACID            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2C8;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYPIIC8; P450 FORM 1; P450 MP-12/MP-20; P450 IIC2; S-       
COMPND   5 MEPHENYTOIN 4-HYDROXYLASE;                                           
COMPND   6 EC: 1.14.14.1;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP2C8;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCW                                       
KEYWDS    CYP2C8; HUMAN P450 2C8; MONOOXYGENASES; SUBSTRATE COMPLEX; PALMITIC   
KEYWDS   2 ACID; 9-CIS RETINOIC ACID; PANRETIN, OXIDOREDUCTASE,ELECTRON         
KEYWDS   3 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.A.SCHOCH,J.K.YANO,C.D.STOUT,E.F.JOHNSON                             
REVDAT   5   16-NOV-16 2NNH    1       HET    HETATM HETNAM VERSN               
REVDAT   4   09-JUN-09 2NNH    1       REVDAT                                   
REVDAT   3   24-FEB-09 2NNH    1       VERSN                                    
REVDAT   2   02-DEC-08 2NNH    1       JRNL                                     
REVDAT   1   23-OCT-07 2NNH    0                                                
JRNL        AUTH   G.A.SCHOCH,J.K.YANO,S.SANSEN,P.M.DANSETTE,C.D.STOUT,         
JRNL        AUTH 2 E.F.JOHNSON                                                  
JRNL        TITL   DETERMINANTS OF CYTOCHROME P450 2C8 SUBSTRATE BINDING:       
JRNL        TITL 2 STRUCTURES OF COMPLEXES WITH MONTELUKAST, TROGLITAZONE,      
JRNL        TITL 3 FELODIPINE, AND 9-CIS-RETINOIC ACID.                         
JRNL        REF    J.BIOL.CHEM.                  V. 283 17227 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18413310                                                     
JRNL        DOI    10.1074/JBC.M802180200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 51297                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 48714                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 220                                     
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.265 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.127 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.761 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.672 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2NNH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040076.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING BENT CUBE-ROOT I   
REMARK 200                                   -BEAM SINGLE CRYSTAL; ASYMMETRIC   
REMARK 200                                   CUT 4.965 DEGS                     
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL FOCUSING);   
REMARK 200                                   SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   MONOCHROMATOR (HO RIZONTAL         
REMARK 200                                   FOCUSING)                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51297                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.45000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1PQ2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, HEPES, LISO4, MEOH, PH 7.5,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       69.90500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.81000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       69.90500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.81000            
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                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     HIS A   491                                                      
REMARK 465     HIS A   492                                                      
REMARK 465     HIS A   493                                                      
REMARK 465     HIS A   494                                                      
REMARK 465     MET B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     HIS B   491                                                      
REMARK 465     HIS B   492                                                      
REMARK 465     HIS B   493                                                      
REMARK 465     HIS B   494                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 363   C   -  N   -  CA  ANGL. DEV. =   9.2 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    LEU A  43       31.41    -83.57                                   
REMARK 500    ALA A  86      -70.74    -74.76                                   
REMARK 500    ILE A  88      -71.53    -90.44                                   
REMARK 500    ASN A  90       39.57    -97.28                                   
REMARK 500    ASN A  99       75.39     66.33                                   
REMARK 500    ILE A 106      -72.06    -94.47                                   
REMARK 500    LYS A 108       28.52     42.52                                   
REMARK 500    GLN A 184      -80.08    -56.25                                   
REMARK 500    ASP A 191       98.39    -67.47                                   
REMARK 500    GLN A 192      -33.50    -37.74                                   
REMARK 500    VAL A 257      -18.99    -48.92                                   
REMARK 500    ASP A 262     -163.46   -167.07                                   
REMARK 500    THR A 299      -70.88    -90.65                                   
REMARK 500    HIS A 316       79.61   -119.62                                   
REMARK 500    ARG A 377      -94.19     46.54                                   
REMARK 500    PRO A 402      127.26    -39.00                                   
REMARK 500    ASN A 403       60.00     60.19                                   
REMARK 500    SER A 429     -158.67     75.44                                   
REMARK 500    CYS A 435      123.72    -34.95                                   
REMARK 500    LYS A 474       46.44   -141.65                                   
REMARK 500    PRO B  31      173.64    -58.04                                   
REMARK 500    ILE B  45     -153.64   -119.97                                   
REMARK 500    ASP B  49       62.80   -108.72                                   
REMARK 500    ILE B  88      -68.48    -96.28                                   
REMARK 500    ASP B  89       37.11    -73.92                                   
REMARK 500    ASN B  90       13.52    179.35                                   
REMARK 500    ASN B  99       80.10     65.92                                   
REMARK 500    ILE B 106      -67.05    -96.02                                   
REMARK 500    PHE B 134       51.92   -108.50                                   
REMARK 500    ALA B 161       17.77     52.22                                   
REMARK 500    ASN B 193      -18.83    -49.42                                   
REMARK 500    PRO B 220      -30.38    -32.23                                   
REMARK 500    ALA B 253       33.25    -75.54                                   
REMARK 500    SER B 254        4.17   -172.46                                   
REMARK 500    ASN B 259      106.44   -171.51                                   
REMARK 500    LYS B 279       57.73   -106.43                                   
REMARK 500    THR B 299      -68.94    -93.71                                   
REMARK 500    ARG B 333       31.49    -96.21                                   
REMARK 500    MET B 345       65.72   -116.11                                   
REMARK 500    ASP B 360       59.91     33.72                                   
REMARK 500    ARG B 377     -120.09     67.36                                   
REMARK 500    LEU B 390       92.45    -63.33                                   
REMARK 500    SER B 429      179.05     74.73                                   
REMARK 500    CYS B 435      123.19    -39.34                                   
REMARK 500    LEU B 467      108.65    -51.78                                   
REMARK 500    LYS B 474      -41.74   -155.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 435   SG                                                     
REMARK 620 2 HEM A 500   NA   93.5                                              
REMARK 620 3 HEM A 500   NB   93.4  89.2                                        
REMARK 620 4 HEM A 500   NC   83.5 177.0  91.7                                  
REMARK 620 5 HEM A 500   ND   91.4  90.3 175.2  89.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 435   SG                                                     
REMARK 620 2 HEM B 500   NA   95.1                                              
REMARK 620 3 HEM B 500   NB   90.1  88.9                                        
REMARK 620 4 HEM B 500   NC   88.6 176.3  91.4                                  
REMARK 620 5 HEM B 500   ND   92.5  90.2 177.3  89.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9CR A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9CR A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9CR B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9CR B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NNI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NNJ   RELATED DB: PDB                                   
DBREF  2NNH A   28   490  UNP    P10632   CP2C8_HUMAN     28    490             
DBREF  2NNH B   28   490  UNP    P10632   CP2C8_HUMAN     28    490             
SEQADV 2NNH MET A   19  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH ALA A   20  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH LYS A   21  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH LYS A   22  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH THR A   23  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH SER A   24  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH SER A   25  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH LYS A   26  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH GLY A   27  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS A  491  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS A  492  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS A  493  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS A  494  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH MET B   19  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH ALA B   20  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH LYS B   21  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH LYS B   22  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH THR B   23  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH SER B   24  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH SER B   25  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH LYS B   26  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH GLY B   27  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS B  491  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS B  492  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS B  493  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNH HIS B  494  UNP  P10632              EXPRESSION TAG                 
SEQRES   1 A  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 A  476  GLY PRO THR PRO LEU PRO ILE ILE GLY ASN MET LEU GLN          
SEQRES   3 A  476  ILE ASP VAL LYS ASP ILE CYS LYS SER PHE THR ASN PHE          
SEQRES   4 A  476  SER LYS VAL TYR GLY PRO VAL PHE THR VAL TYR PHE GLY          
SEQRES   5 A  476  MET ASN PRO ILE VAL VAL PHE HIS GLY TYR GLU ALA VAL          
SEQRES   6 A  476  LYS GLU ALA LEU ILE ASP ASN GLY GLU GLU PHE SER GLY          
SEQRES   7 A  476  ARG GLY ASN SER PRO ILE SER GLN ARG ILE THR LYS GLY          
SEQRES   8 A  476  LEU GLY ILE ILE SER SER ASN GLY LYS ARG TRP LYS GLU          
SEQRES   9 A  476  ILE ARG ARG PHE SER LEU THR THR LEU ARG ASN PHE GLY          
SEQRES  10 A  476  MET GLY LYS ARG SER ILE GLU ASP ARG VAL GLN GLU GLU          
SEQRES  11 A  476  ALA HIS CYS LEU VAL GLU GLU LEU ARG LYS THR LYS ALA          
SEQRES  12 A  476  SER PRO CYS ASP PRO THR PHE ILE LEU GLY CYS ALA PRO          
SEQRES  13 A  476  CYS ASN VAL ILE CYS SER VAL VAL PHE GLN LYS ARG PHE          
SEQRES  14 A  476  ASP TYR LYS ASP GLN ASN PHE LEU THR LEU MET LYS ARG          
SEQRES  15 A  476  PHE ASN GLU ASN PHE ARG ILE LEU ASN SER PRO TRP ILE          
SEQRES  16 A  476  GLN VAL CYS ASN ASN PHE PRO LEU LEU ILE ASP CYS PHE          
SEQRES  17 A  476  PRO GLY THR HIS ASN LYS VAL LEU LYS ASN VAL ALA LEU          
SEQRES  18 A  476  THR ARG SER TYR ILE ARG GLU LYS VAL LYS GLU HIS GLN          
SEQRES  19 A  476  ALA SER LEU ASP VAL ASN ASN PRO ARG ASP PHE ILE ASP          
SEQRES  20 A  476  CYS PHE LEU ILE LYS MET GLU GLN GLU LYS ASP ASN GLN          
SEQRES  21 A  476  LYS SER GLU PHE ASN ILE GLU ASN LEU VAL GLY THR VAL          
SEQRES  22 A  476  ALA ASP LEU PHE VAL ALA GLY THR GLU THR THR SER THR          
SEQRES  23 A  476  THR LEU ARG TYR GLY LEU LEU LEU LEU LEU LYS HIS PRO          
SEQRES  24 A  476  GLU VAL THR ALA LYS VAL GLN GLU GLU ILE ASP HIS VAL          
SEQRES  25 A  476  ILE GLY ARG HIS ARG SER PRO CYS MET GLN ASP ARG SER          
SEQRES  26 A  476  HIS MET PRO TYR THR ASP ALA VAL VAL HIS GLU ILE GLN          
SEQRES  27 A  476  ARG TYR SER ASP LEU VAL PRO THR GLY VAL PRO HIS ALA          
SEQRES  28 A  476  VAL THR THR ASP THR LYS PHE ARG ASN TYR LEU ILE PRO          
SEQRES  29 A  476  LYS GLY THR THR ILE MET ALA LEU LEU THR SER VAL LEU          
SEQRES  30 A  476  HIS ASP ASP LYS GLU PHE PRO ASN PRO ASN ILE PHE ASP          
SEQRES  31 A  476  PRO GLY HIS PHE LEU ASP LYS ASN GLY ASN PHE LYS LYS          
SEQRES  32 A  476  SER ASP TYR PHE MET PRO PHE SER ALA GLY LYS ARG ILE          
SEQRES  33 A  476  CYS ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 A  476  PHE LEU THR THR ILE LEU GLN ASN PHE ASN LEU LYS SER          
SEQRES  35 A  476  VAL ASP ASP LEU LYS ASN LEU ASN THR THR ALA VAL THR          
SEQRES  36 A  476  LYS GLY ILE VAL SER LEU PRO PRO SER TYR GLN ILE CYS          
SEQRES  37 A  476  PHE ILE PRO VAL HIS HIS HIS HIS                              
SEQRES   1 B  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 B  476  GLY PRO THR PRO LEU PRO ILE ILE GLY ASN MET LEU GLN          
SEQRES   3 B  476  ILE ASP VAL LYS ASP ILE CYS LYS SER PHE THR ASN PHE          
SEQRES   4 B  476  SER LYS VAL TYR GLY PRO VAL PHE THR VAL TYR PHE GLY          
SEQRES   5 B  476  MET ASN PRO ILE VAL VAL PHE HIS GLY TYR GLU ALA VAL          
SEQRES   6 B  476  LYS GLU ALA LEU ILE ASP ASN GLY GLU GLU PHE SER GLY          
SEQRES   7 B  476  ARG GLY ASN SER PRO ILE SER GLN ARG ILE THR LYS GLY          
SEQRES   8 B  476  LEU GLY ILE ILE SER SER ASN GLY LYS ARG TRP LYS GLU          
SEQRES   9 B  476  ILE ARG ARG PHE SER LEU THR THR LEU ARG ASN PHE GLY          
SEQRES  10 B  476  MET GLY LYS ARG SER ILE GLU ASP ARG VAL GLN GLU GLU          
SEQRES  11 B  476  ALA HIS CYS LEU VAL GLU GLU LEU ARG LYS THR LYS ALA          
SEQRES  12 B  476  SER PRO CYS ASP PRO THR PHE ILE LEU GLY CYS ALA PRO          
SEQRES  13 B  476  CYS ASN VAL ILE CYS SER VAL VAL PHE GLN LYS ARG PHE          
SEQRES  14 B  476  ASP TYR LYS ASP GLN ASN PHE LEU THR LEU MET LYS ARG          
SEQRES  15 B  476  PHE ASN GLU ASN PHE ARG ILE LEU ASN SER PRO TRP ILE          
SEQRES  16 B  476  GLN VAL CYS ASN ASN PHE PRO LEU LEU ILE ASP CYS PHE          
SEQRES  17 B  476  PRO GLY THR HIS ASN LYS VAL LEU LYS ASN VAL ALA LEU          
SEQRES  18 B  476  THR ARG SER TYR ILE ARG GLU LYS VAL LYS GLU HIS GLN          
SEQRES  19 B  476  ALA SER LEU ASP VAL ASN ASN PRO ARG ASP PHE ILE ASP          
SEQRES  20 B  476  CYS PHE LEU ILE LYS MET GLU GLN GLU LYS ASP ASN GLN          
SEQRES  21 B  476  LYS SER GLU PHE ASN ILE GLU ASN LEU VAL GLY THR VAL          
SEQRES  22 B  476  ALA ASP LEU PHE VAL ALA GLY THR GLU THR THR SER THR          
SEQRES  23 B  476  THR LEU ARG TYR GLY LEU LEU LEU LEU LEU LYS HIS PRO          
SEQRES  24 B  476  GLU VAL THR ALA LYS VAL GLN GLU GLU ILE ASP HIS VAL          
SEQRES  25 B  476  ILE GLY ARG HIS ARG SER PRO CYS MET GLN ASP ARG SER          
SEQRES  26 B  476  HIS MET PRO TYR THR ASP ALA VAL VAL HIS GLU ILE GLN          
SEQRES  27 B  476  ARG TYR SER ASP LEU VAL PRO THR GLY VAL PRO HIS ALA          
SEQRES  28 B  476  VAL THR THR ASP THR LYS PHE ARG ASN TYR LEU ILE PRO          
SEQRES  29 B  476  LYS GLY THR THR ILE MET ALA LEU LEU THR SER VAL LEU          
SEQRES  30 B  476  HIS ASP ASP LYS GLU PHE PRO ASN PRO ASN ILE PHE ASP          
SEQRES  31 B  476  PRO GLY HIS PHE LEU ASP LYS ASN GLY ASN PHE LYS LYS          
SEQRES  32 B  476  SER ASP TYR PHE MET PRO PHE SER ALA GLY LYS ARG ILE          
SEQRES  33 B  476  CYS ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 B  476  PHE LEU THR THR ILE LEU GLN ASN PHE ASN LEU LYS SER          
SEQRES  35 B  476  VAL ASP ASP LEU LYS ASN LEU ASN THR THR ALA VAL THR          
SEQRES  36 B  476  LYS GLY ILE VAL SER LEU PRO PRO SER TYR GLN ILE CYS          
SEQRES  37 B  476  PHE ILE PRO VAL HIS HIS HIS HIS                              
HET    SO4  A 505       5                                                       
HET    HEM  A 500      43                                                       
HET    9CR  A 501      22                                                       
HET    9CR  A 502      22                                                       
HET    PLM  A 503      18                                                       
HET    SO4  B 504       5                                                       
HET    HEM  B 500      43                                                       
HET    9CR  B 501      22                                                       
HET    9CR  B 502      22                                                       
HET    PLM  B 503      18                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     9CR (9CIS)-RETINOIC ACID                                             
HETNAM     PLM PALMITIC ACID                                                    
HETSYN     HEM HEME                                                             
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   5  9CR    4(C20 H28 O2)                                                
FORMUL   7  PLM    2(C16 H32 O2)                                                
FORMUL  13  HOH   *88(H2 O)                                                     
HELIX    1   1 ASN A   41  ILE A   45  5                                   5    
HELIX    2   2 ASP A   49  GLY A   62  1                                  14    
HELIX    3   3 HIS A   78  ILE A   88  1                                  11    
HELIX    4   4 SER A  100  THR A  107  1                                   8    
HELIX    5   5 ASN A  116  LEU A  131  1                                  16    
HELIX    6   6 SER A  140  LYS A  158  1                                  19    
HELIX    7   7 PRO A  166  PHE A  183  1                                  18    
HELIX    8   8 ASP A  191  ASN A  209  1                                  19    
HELIX    9   9 PRO A  211  PHE A  219  1                                   9    
HELIX   10  10 PRO A  220  CYS A  225  5                                   6    
HELIX   11  11 PHE A  226  ALA A  253  1                                  28    
HELIX   12  12 ASP A  262  LYS A  275  1                                  14    
HELIX   13  13 ASN A  283  THR A  299  1                                  17    
HELIX   14  14 THR A  299  HIS A  316  1                                  18    
HELIX   15  15 HIS A  316  ILE A  331  1                                  16    
HELIX   16  16 CYS A  338  HIS A  344  5                                   7    
HELIX   17  17 MET A  345  ASP A  360  1                                  16    
HELIX   18  18 LEU A  390  HIS A  396  1                                   7    
HELIX   19  19 ASP A  408  LEU A  413  5                                   6    
HELIX   20  20 ALA A  430  ILE A  434  5                                   5    
HELIX   21  21 GLY A  437  ASN A  455  1                                  19    
HELIX   22  22 ASN B   41  ILE B   45  5                                   5    
HELIX   23  23 ASP B   49  GLY B   62  1                                  14    
HELIX   24  24 GLY B   79  ILE B   88  1                                  10    
HELIX   25  25 SER B  100  THR B  107  1                                   8    
HELIX   26  26 ASN B  116  LEU B  131  1                                  16    
HELIX   27  27 SER B  140  LYS B  158  1                                  19    
HELIX   28  28 PRO B  166  PHE B  183  1                                  18    
HELIX   29  29 ASP B  191  ASN B  209  1                                  19    
HELIX   30  30 SER B  210  PHE B  219  1                                  10    
HELIX   31  31 PRO B  220  CYS B  225  5                                   6    
HELIX   32  32 PHE B  226  ALA B  253  1                                  28    
HELIX   33  33 ASP B  262  GLN B  273  1                                  12    
HELIX   34  34 ASN B  283  THR B  299  1                                  17    
HELIX   35  35 THR B  299  HIS B  316  1                                  18    
HELIX   36  36 HIS B  316  GLY B  332  1                                  17    
HELIX   37  37 CYS B  338  HIS B  344  5                                   7    
HELIX   38  38 MET B  345  ASP B  360  1                                  16    
HELIX   39  39 LEU B  390  HIS B  396  1                                   7    
HELIX   40  40 ASP B  408  LEU B  413  5                                   6    
HELIX   41  41 GLY B  437  ASN B  455  1                                  19    
SHEET    1   A 4 VAL A  64  PHE A  69  0                                        
SHEET    2   A 4 ASN A  72  PHE A  77 -1  O  ILE A  74   N  VAL A  67           
SHEET    3   A 4 THR A 386  ALA A 389  1  O  MET A 388   N  PHE A  77           
SHEET    4   A 4 HIS A 368  ALA A 369 -1  N  HIS A 368   O  ILE A 387           
SHEET    1   B 3 PRO A 163  CYS A 164  0                                        
SHEET    2   B 3 ILE A 485  PRO A 489 -1  O  ILE A 485   N  CYS A 164           
SHEET    3   B 3 PHE A 456  LYS A 459 -1  N  LYS A 459   O  CYS A 486           
SHEET    1   C 2 THR A 374  PHE A 376  0                                        
SHEET    2   C 2 TYR A 379  ILE A 381 -1  O  ILE A 381   N  THR A 374           
SHEET    1   D 4 VAL B  64  PHE B  69  0                                        
SHEET    2   D 4 ASN B  72  PHE B  77 -1  O  ILE B  74   N  VAL B  67           
SHEET    3   D 4 THR B 386  ALA B 389  1  O  MET B 388   N  PHE B  77           
SHEET    4   D 4 HIS B 368  ALA B 369 -1  N  HIS B 368   O  ILE B 387           
SHEET    1   E 2 THR B 374  PHE B 376  0                                        
SHEET    2   E 2 TYR B 379  ILE B 381 -1  O  ILE B 381   N  THR B 374           
SHEET    1   F 2 PHE B 456  LYS B 459  0                                        
SHEET    2   F 2 CYS B 486  PRO B 489 -1  O  CYS B 486   N  LYS B 459           
LINK         SG  CYS A 435                FE   HEM A 500     1555   1555  2.28  
LINK         SG  CYS B 435                FE   HEM B 500     1555   1555  2.28  
SITE     1 AC1  2 ARG B 132  ASN B 133                                          
SITE     1 AC2  2 ARG A 132  ASN A 133                                          
SITE     1 AC3 21 ARG A  97  ILE A 112  TRP A 120  ARG A 124                    
SITE     2 AC3 21 ILE A 178  ALA A 297  GLY A 298  THR A 301                    
SITE     3 AC3 21 THR A 302  THR A 305  LEU A 361  VAL A 366                    
SITE     4 AC3 21 HIS A 368  PRO A 427  PHE A 428  SER A 429                    
SITE     5 AC3 21 ARG A 433  CYS A 435  LEU A 440  ALA A 441                    
SITE     6 AC3 21 9CR A 501                                                     
SITE     1 AC4 20 ARG B  97  ILE B 112  ILE B 113  TRP B 120                    
SITE     2 AC4 20 ARG B 124  ALA B 297  GLY B 298  THR B 301                    
SITE     3 AC4 20 THR B 302  THR B 305  GLN B 356  LEU B 361                    
SITE     4 AC4 20 VAL B 366  HIS B 368  PRO B 427  PHE B 428                    
SITE     5 AC4 20 SER B 429  ARG B 433  CYS B 435  9CR B 501                    
SITE     1 AC5 11 ARG A  97  GLY A  98  ASN A  99  SER A 100                    
SITE     2 AC5 11 SER A 103  ILE A 113  THR A 301  VAL A 366                    
SITE     3 AC5 11 HEM A 500  9CR A 502  HOH A 541                               
SITE     1 AC6  9 SER A 100  ASN A 204  LEU A 208  ASN A 217                    
SITE     2 AC6  9 VAL A 237  ARG A 241  VAL A 296  ILE A 476                    
SITE     3 AC6  9 9CR A 501                                                     
SITE     1 AC7 10 GLY B  98  ASN B  99  SER B 100  ILE B 113                    
SITE     2 AC7 10 THR B 301  VAL B 366  PRO B 367  HEM B 500                    
SITE     3 AC7 10 9CR B 502  HOH B 534                                          
SITE     1 AC8  7 SER B 100  ASN B 204  LEU B 208  ARG B 241                    
SITE     2 AC8  7 VAL B 296  ILE B 476  9CR B 501                               
SITE     1 AC9 10 ARG A 105  ILE A 106  TRP A 212  CYS A 216                    
SITE     2 AC9 10 THR A 229  HOH A 535  PHE B 226  PRO B 227                    
SITE     3 AC9 10 GLY B 228  THR B 229                                          
SITE     1 BC1 10 PHE A 226  PRO A 227  GLY A 228  THR A 229                    
SITE     2 BC1 10 ILE B 102  ILE B 106  TRP B 212  PHE B 226                    
SITE     3 BC1 10 HIS B 230  LEU B 234                                          
CRYST1  139.810  163.620   73.555  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007153  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013595        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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