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Database: PDB
Entry: 2NNJ
LinkDB: 2NNJ
Original site: 2NNJ 
HEADER    OXIDOREDUCTASE,ELECTRON TRANSPORT       24-OCT-06   2NNJ              
TITLE     CYP2C8DH COMPLEXED WITH FELODIPINE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2C8;                                       
COMPND   3 CHAIN: A;                                                            
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; FELODIPINE; PLENDIL;          
KEYWDS   2 INHIBITOR COMPLEX; PALMITIC ACID, OXIDOREDUCTASE,ELECTRON TRANSPORT  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.A.SCHOCH,J.K.YANO,C.D.STOUT,E.F.JOHNSON                             
REVDAT   6   13-JUL-11 2NNJ    1       VERSN                                    
REVDAT   5   11-AUG-10 2NNJ    1       HETSYN                                   
REVDAT   4   09-JUN-09 2NNJ    1       REVDAT                                   
REVDAT   3   24-FEB-09 2NNJ    1       VERSN                                    
REVDAT   2   02-DEC-08 2NNJ    1       JRNL                                     
REVDAT   1   23-OCT-07 2NNJ    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.    2.28 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) : 2.28                           
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)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 38962                          
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) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 36898                           
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            : 3693                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 101                                     
REMARK   3   SOLVENT ATOMS            : 179                                     
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
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) : 1.437 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.344 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.208 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.227 ; 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 2NNJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040078.                                      
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                       : BL1-5                              
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                  : DOUBLE-CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : DOUBLE-CRYSTAL MONOCHROMATOR, 1M   
REMARK 200                                   LONG RH COATED BENT CYLINDRICAL    
REMARK 200                                   MIRROR FOR HORIZONTAL AND          
REMARK 200                                   VERTICAL FOCUSSING                 
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   : 38962                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.280                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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   (%): 68.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.91                     
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: I 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.20500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.61000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       81.61500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.20500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.61000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       81.61500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.20500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.61000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       81.61500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.20500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       69.61000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       81.61500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 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    ASP A  49       68.42   -153.40                                   
REMARK 500    MET A 136       45.32   -142.26                                   
REMARK 500    GLN A 184      -52.62     71.66                                   
REMARK 500    SER A 254       17.30   -154.58                                   
REMARK 500    ARG A 377     -123.24     55.84                                   
REMARK 500    SER A 429     -165.33     76.48                                   
REMARK 500    CYS A 435      122.72    -32.82                                   
REMARK 500    ILE A 476      -45.65     91.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 585        DISTANCE =  5.41 ANGSTROMS                       
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   98.3                                              
REMARK 620 3 HEM A 500   NB   93.7  88.6                                        
REMARK 620 4 HEM A 500   NC   86.1 175.6  91.0                                  
REMARK 620 5 HEM A 500   ND   93.7  90.7 172.6  89.1                            
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 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 225 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NNH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NNI   RELATED DB: PDB                                   
DBREF  2NNJ A   28   490  UNP    P10632   CP2C8_HUMAN     28    490             
SEQADV 2NNJ MET A   19  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ ALA A   20  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ LYS A   21  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ LYS A   22  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ THR A   23  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ SER A   24  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ SER A   25  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ LYS A   26  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ GLY A   27  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ HIS A  491  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ HIS A  492  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ HIS A  493  UNP  P10632              EXPRESSION TAG                 
SEQADV 2NNJ HIS A  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                              
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    HEM  A 500      43                                                       
HET    225  A 501      25                                                       
HET    PLM  A 502      18                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     225 FELODIPINE                                                       
HETNAM     PLM PALMITIC ACID                                                    
HETSYN     HEM HEME                                                             
HETSYN     225 ETHYL METHYL (4R)-4-(2,3-DICHLOROPHENYL)-2,6-DIMETHYL-           
HETSYN   2 225  1,4-DIHYDROPYRIDINE-3,5-DICARBOXYLATE                           
FORMUL   2  SO4    3(O4 S 2-)                                                   
FORMUL   5  HEM    C34 H32 FE N4 O4                                             
FORMUL   6  225    C18 H19 CL2 N O4                                             
FORMUL   7  PLM    C16 H32 O2                                                   
FORMUL   8  HOH   *179(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 GLY A   79  ILE A   88  1                                  10    
HELIX    4   4 SER A  100  LYS A  108  1                                   9    
HELIX    5   5 ASN A  116  LEU A  131  1                                  16    
HELIX    6   6 SER A  140  LYS A  158  1                                  19    
HELIX    7   7 PRO A  166  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  GLU A  274  1                                  13    
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 ASP A  463  LEU A  467  5                                   5    
SHEET    1   A 5 VAL A  64  PHE A  69  0                                        
SHEET    2   A 5 ASN A  72  PHE A  77 -1  O  VAL A  76   N  PHE A  65           
SHEET    3   A 5 THR A 386  ALA A 389  1  O  MET A 388   N  PHE A  77           
SHEET    4   A 5 HIS A 368  ALA A 369 -1  N  HIS A 368   O  ILE A 387           
SHEET    5   A 5 GLY A  96  ARG A  97 -1  N  GLY A  96   O  ALA A 369           
SHEET    1   B 2 THR A 374  PHE A 376  0                                        
SHEET    2   B 2 TYR A 379  ILE A 381 -1  O  ILE A 381   N  THR A 374           
SHEET    1   C 2 PHE A 456  LYS A 459  0                                        
SHEET    2   C 2 CYS A 486  PRO A 489 -1  O  CYS A 486   N  LYS A 459           
SHEET    1   D 2 THR A 473  LYS A 474  0                                        
SHEET    2   D 2 SER A 478  LEU A 479 -1  O  LEU A 479   N  THR A 473           
LINK         SG  CYS A 435                FE   HEM A 500     1555   1555  2.32  
SITE     1 AC1  5 ARG A 125  GLY A 332  ARG A 333  HIS A 334                    
SITE     2 AC1  5 HOH A 670                                                     
SITE     1 AC2  4 ARG A 132  ASN A 133  HOH A 560  HOH A 631                    
SITE     1 AC3  5 VAL A 330  ILE A 331  ARG A 335  HOH A 578                    
SITE     2 AC3  5 HOH A 579                                                     
SITE     1 AC4 19 ARG A  97  ILE A 112  TRP A 120  ARG A 124                    
SITE     2 AC4 19 ALA A 297  GLY A 298  THR A 301  THR A 302                    
SITE     3 AC4 19 LEU A 361  VAL A 366  HIS A 368  PRO A 427                    
SITE     4 AC4 19 PHE A 428  SER A 429  ARG A 433  CYS A 435                    
SITE     5 AC4 19 ALA A 436  225 A 501  HOH A 583                               
SITE     1 AC5  5 VAL A 296  THR A 301  GLY A 365  VAL A 366                    
SITE     2 AC5  5 HEM A 500                                                     
SITE     1 AC6  8 ILE A 106  PHE A 226  PRO A 227  GLY A 228                    
SITE     2 AC6  8 THR A 229  HIS A 230  LEU A 234  HOH A 660                    
CRYST1   74.410  139.220  163.230  90.00  90.00  90.00 I 2 2 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      0.013439  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007183  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006126        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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