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Database: PDB
Entry: 4EJJ
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Original site: 4EJJ 
HEADER    OXIDOREDUCTASE                          06-APR-12   4EJJ              
TITLE     HUMAN CYTOCHROME P450 2A6 IN COMPLEX WITH NICOTINE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2A6;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 30-494;                                       
COMPND   5 SYNONYM: CYPIIA6, COUMARIN 7-HYDROXYLASE, CYTOCHROME P450 IIA3,      
COMPND   6 CYTOCHROME P450(I);                                                  
COMPND   7 EC: 1.14.14.1;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP2A3, CYP2A6;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOPP3;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKK2A6DH                                  
KEYWDS    CYTOCHROME P450 2A6, P450 2A6, HEME PROTEIN, MONOXYGENASE, DRUG       
KEYWDS   2 METABOLISM, XENOBIOTIC METABOLISM, ENDOPLASMIC RETICULUM, MEMBRANE,  
KEYWDS   3 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.DEVORE,E.E.SCOTT                                                  
REVDAT   3   15-NOV-17 4EJJ    1       REMARK                                   
REVDAT   2   02-JAN-13 4EJJ    1       JRNL                                     
REVDAT   1   06-JUN-12 4EJJ    0                                                
JRNL        AUTH   N.M.DEVORE,E.E.SCOTT                                         
JRNL        TITL   NICOTINE AND 4-(METHYLNITROSAMINO)-1-(3-PYRIDYL)-1-BUTANONE  
JRNL        TITL 2 BINDING AND ACCESS CHANNEL IN HUMAN CYTOCHROME P450 2A6 AND  
JRNL        TITL 3 2A13 ENZYMES.                                                
JRNL        REF    J.BIOL.CHEM.                  V. 287 26576 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22700965                                                     
JRNL        DOI    10.1074/JBC.M112.372813                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 6.1.13                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 97.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 100359                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5273                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15013                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 220                                     
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.300         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.242         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.174         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4EJJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071697.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : RH COATED FLAT MIRROR, TOROIDAL    
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 105683                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : 0.09300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER MR                                             
REMARK 200 STARTING MODEL: CYP2A6 PDB ENTRY 2FDV                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.175 M TRIS, AND 0.2 M    
REMARK 280  AMMONIUM SULFATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       97.01900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     HIS A   495                                                      
REMARK 465     HIS A   496                                                      
REMARK 465     HIS A   497                                                      
REMARK 465     HIS A   498                                                      
REMARK 465     MET B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     LYS B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     SER B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     HIS B   495                                                      
REMARK 465     HIS B   496                                                      
REMARK 465     HIS B   497                                                      
REMARK 465     HIS B   498                                                      
REMARK 465     MET C    23                                                      
REMARK 465     ALA C    24                                                      
REMARK 465     LYS C    25                                                      
REMARK 465     LYS C    26                                                      
REMARK 465     THR C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     SER C    29                                                      
REMARK 465     LYS C    30                                                      
REMARK 465     HIS C   495                                                      
REMARK 465     HIS C   496                                                      
REMARK 465     HIS C   497                                                      
REMARK 465     HIS C   498                                                      
REMARK 465     MET D    23                                                      
REMARK 465     ALA D    24                                                      
REMARK 465     LYS D    25                                                      
REMARK 465     LYS D    26                                                      
REMARK 465     THR D    27                                                      
REMARK 465     SER D    28                                                      
REMARK 465     SER D    29                                                      
REMARK 465     LYS D    30                                                      
REMARK 465     HIS D   495                                                      
REMARK 465     HIS D   496                                                      
REMARK 465     HIS D   497                                                      
REMARK 465     HIS D   498                                                      
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    PHE A  42      -59.62     71.36                                   
REMARK 500    VAL A  92      -69.08   -100.33                                   
REMARK 500    GLN A  94       50.41   -119.15                                   
REMARK 500    ASP A 195      115.44    -13.40                                   
REMARK 500    ILE A 366       77.38   -115.45                                   
REMARK 500    SER A 369     -161.15     50.12                                   
REMARK 500    SER A 433     -157.23     62.49                                   
REMARK 500    ARG A 485      150.40    -48.99                                   
REMARK 500    PHE B  42      -64.81     68.76                                   
REMARK 500    GLN B  48       35.37    -99.24                                   
REMARK 500    ALA B  90      -71.88    -74.89                                   
REMARK 500    PRO B 261       -8.74    -59.81                                   
REMARK 500    THR B 303      -63.99    -96.79                                   
REMARK 500    ILE B 366       79.11   -115.66                                   
REMARK 500    SER B 369     -158.83     57.39                                   
REMARK 500    LYS B 387      135.18    -36.98                                   
REMARK 500    ASN B 418     -152.75    -91.48                                   
REMARK 500    SER B 433     -168.51     56.53                                   
REMARK 500    LEU C  33      145.69    -30.17                                   
REMARK 500    PHE C  42      -60.83     71.74                                   
REMARK 500    GLN C  53       58.58   -146.64                                   
REMARK 500    VAL C 181      -74.45    -62.71                                   
REMARK 500    GLU C 277        7.44    -64.47                                   
REMARK 500    THR C 303      -70.62    -96.47                                   
REMARK 500    HIS C 320       78.07   -116.82                                   
REMARK 500    MET C 349       71.68   -115.37                                   
REMARK 500    SER C 369     -153.33     59.67                                   
REMARK 500    ASP C 377      114.99    -38.45                                   
REMARK 500    ASP C 382       -7.49     92.64                                   
REMARK 500    LYS C 387      123.70    -31.06                                   
REMARK 500    LYS C 425      151.61    -43.65                                   
REMARK 500    VAL C 430       43.29   -145.95                                   
REMARK 500    SER C 433     -175.63     70.00                                   
REMARK 500    PRO C 468      -48.81    -29.81                                   
REMARK 500    PHE D  42      -56.65     68.00                                   
REMARK 500    PHE D 198      -72.06    -47.56                                   
REMARK 500    THR D 303      -63.96    -94.63                                   
REMARK 500    ASN D 338      -78.02    -74.89                                   
REMARK 500    ILE D 366       79.79   -110.70                                   
REMARK 500    SER D 369     -162.82     57.77                                   
REMARK 500    ASP D 382       18.98     56.95                                   
REMARK 500    LYS D 387      125.89    -33.81                                   
REMARK 500    ASN D 418     -162.45    -69.96                                   
REMARK 500    LYS D 420        1.54    -66.99                                   
REMARK 500    SER D 433     -164.92     57.27                                   
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 B 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 439   SG                                                     
REMARK 620 2 HEM B 500   NA   98.2                                              
REMARK 620 3 HEM B 500   NB   87.9  86.7                                        
REMARK 620 4 HEM B 500   NC   84.9 176.9  94.1                                  
REMARK 620 5 HEM B 500   ND   93.3  92.6 178.6  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 502  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 439   SG                                                     
REMARK 620 2 HEM D 502   NA   98.7                                              
REMARK 620 3 HEM D 502   NB   88.5  88.1                                        
REMARK 620 4 HEM D 502   NC   82.6 178.7  91.9                                  
REMARK 620 5 HEM D 502   ND   92.7  91.6 178.7  88.3                            
REMARK 620 N                    1     2     3     4                             
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 439   SG                                                     
REMARK 620 2 HEM A 500   NA  101.4                                              
REMARK 620 3 HEM A 500   NB   90.2  88.8                                        
REMARK 620 4 HEM A 500   NC   82.4 176.0  92.3                                  
REMARK 620 5 HEM A 500   ND   93.2  91.2 176.5  87.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 439   SG                                                     
REMARK 620 2 HEM C 500   NA   96.1                                              
REMARK 620 3 HEM C 500   NB   90.6  92.4                                        
REMARK 620 4 HEM C 500   NC   84.0 178.7  88.9                                  
REMARK 620 5 HEM C 500   ND   90.3  88.0 179.0  90.7                            
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 HEM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCT A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCT B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCT C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCT D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3T3R   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2A6 IN COMPLEX WITH PILOCARPINE                
REMARK 900 RELATED ID: 3EBS   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2A6 I208S/I300F/G301A/S369G IN COMPLEX WITH    
REMARK 900 PHENACETIN                                                           
REMARK 900 RELATED ID: 2FDY   RELATED DB: PDB                                   
REMARK 900 MICROSOMAL P450 2A6 WITH THE INHIBITOR ADRITHIOL BOUND               
REMARK 900 RELATED ID: 1Z11   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 WITH METHOXSALEN      
REMARK 900 BOUND                                                                
REMARK 900 RELATED ID: 1Z10   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 WITH COUMARIN BOUND   
REMARK 900 RELATED ID: 2FDU   RELATED DB: PDB                                   
REMARK 900 MICROSOMAL P450 2A6 WITH THE INHIBITOR N,N-DIMETHYL(5-(OYRIDIN-3-YL) 
REMARK 900 FURAN-2-YL)METHANAMINE BOUND                                         
REMARK 900 RELATED ID: 2FDV   RELATED DB: PDB                                   
REMARK 900 MICROSOMAL P450 2A6 WITH THE INHIBITOR N-METHYL(5-(PYRIDIN-3-YL)     
REMARK 900 FURAN-2-YL)METHANAMINE BOUND                                         
REMARK 900 RELATED ID: 2PG7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 N297Q/I300V           
REMARK 900 RELATED ID: 2PG6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 L240C/N297Q           
REMARK 900 RELATED ID: 2PG5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 N297Q                 
REMARK 900 RELATED ID: 2FDW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 WITH THE INHIBITOR    
REMARK 900 (5-(PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE BOUND                        
REMARK 900 RELATED ID: 4EJG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EJH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EJI   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS STATE THAT THE AMINOACID AT                                  
REMARK 999 POSITION 392 OF THE UNIPROT ENTRY P11509 SHOULD BE A TYR 2           
DBREF  4EJJ A   29   494  UNP    P11509   CP2A6_HUMAN     30    495             
DBREF  4EJJ B   29   494  UNP    P11509   CP2A6_HUMAN     30    495             
DBREF  4EJJ C   29   494  UNP    P11509   CP2A6_HUMAN     30    495             
DBREF  4EJJ D   29   494  UNP    P11509   CP2A6_HUMAN     30    495             
SEQADV 4EJJ MET A   23  UNP  P11509              INITIATING METHIONINE          
SEQADV 4EJJ ALA A   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS A   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS A   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ THR A   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ SER A   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ TYR A  392  UNP  P11509    PHE   393 SEE REMARK 999                 
SEQADV 4EJJ HIS A  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS A  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS A  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS A  498  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ MET B   23  UNP  P11509              INITIATING METHIONINE          
SEQADV 4EJJ ALA B   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS B   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS B   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ THR B   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ SER B   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ TYR B  392  UNP  P11509    PHE   393 SEE REMARK 999                 
SEQADV 4EJJ HIS B  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS B  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS B  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS B  498  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ MET C   23  UNP  P11509              INITIATING METHIONINE          
SEQADV 4EJJ ALA C   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS C   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS C   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ THR C   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ SER C   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ TYR C  392  UNP  P11509    PHE   393 SEE REMARK 999                 
SEQADV 4EJJ HIS C  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS C  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS C  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS C  498  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ MET D   23  UNP  P11509              INITIATING METHIONINE          
SEQADV 4EJJ ALA D   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS D   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ LYS D   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ THR D   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ SER D   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ TYR D  392  UNP  P11509    PHE   393 SEE REMARK 999                 
SEQADV 4EJJ HIS D  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS D  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS D  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 4EJJ HIS D  498  UNP  P11509              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 PHE ILE GLY ASN TYR LEU GLN          
SEQRES   3 A  476  LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE          
SEQRES   4 A  476  SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY          
SEQRES   5 A  476  PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL          
SEQRES   6 A  476  ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY          
SEQRES   7 A  476  ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY          
SEQRES   8 A  476  TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN          
SEQRES   9 A  476  LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY          
SEQRES  10 A  476  VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU          
SEQRES  11 A  476  ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY          
SEQRES  12 A  476  ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL          
SEQRES  13 A  476  SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE          
SEQRES  14 A  476  ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET          
SEQRES  15 A  476  MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY          
SEQRES  16 A  476  GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU          
SEQRES  17 A  476  PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY          
SEQRES  18 A  476  LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN          
SEQRES  19 A  476  ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP          
SEQRES  20 A  476  SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO          
SEQRES  21 A  476  ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR          
SEQRES  22 A  476  LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR          
SEQRES  23 A  476  THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO          
SEQRES  24 A  476  GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL          
SEQRES  25 A  476  ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA          
SEQRES  26 A  476  LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN          
SEQRES  27 A  476  ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG          
SEQRES  28 A  476  VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO          
SEQRES  29 A  476  LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU          
SEQRES  30 A  476  ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN          
SEQRES  31 A  476  PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS          
SEQRES  32 A  476  SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN          
SEQRES  33 A  476  CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 A  476  PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER          
SEQRES  35 A  476  SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS          
SEQRES  36 A  476  VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER          
SEQRES  37 A  476  PHE LEU PRO ARG 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 PHE ILE GLY ASN TYR LEU GLN          
SEQRES   3 B  476  LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE          
SEQRES   4 B  476  SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY          
SEQRES   5 B  476  PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL          
SEQRES   6 B  476  ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY          
SEQRES   7 B  476  ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY          
SEQRES   8 B  476  TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN          
SEQRES   9 B  476  LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY          
SEQRES  10 B  476  VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU          
SEQRES  11 B  476  ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY          
SEQRES  12 B  476  ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL          
SEQRES  13 B  476  SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE          
SEQRES  14 B  476  ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET          
SEQRES  15 B  476  MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY          
SEQRES  16 B  476  GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU          
SEQRES  17 B  476  PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY          
SEQRES  18 B  476  LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN          
SEQRES  19 B  476  ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP          
SEQRES  20 B  476  SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO          
SEQRES  21 B  476  ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR          
SEQRES  22 B  476  LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR          
SEQRES  23 B  476  THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO          
SEQRES  24 B  476  GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL          
SEQRES  25 B  476  ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA          
SEQRES  26 B  476  LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN          
SEQRES  27 B  476  ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG          
SEQRES  28 B  476  VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO          
SEQRES  29 B  476  LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU          
SEQRES  30 B  476  ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN          
SEQRES  31 B  476  PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS          
SEQRES  32 B  476  SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN          
SEQRES  33 B  476  CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 B  476  PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER          
SEQRES  35 B  476  SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS          
SEQRES  36 B  476  VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER          
SEQRES  37 B  476  PHE LEU PRO ARG HIS HIS HIS HIS                              
SEQRES   1 C  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 C  476  GLY PRO THR PRO LEU PRO PHE ILE GLY ASN TYR LEU GLN          
SEQRES   3 C  476  LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE          
SEQRES   4 C  476  SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY          
SEQRES   5 C  476  PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL          
SEQRES   6 C  476  ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY          
SEQRES   7 C  476  ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY          
SEQRES   8 C  476  TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN          
SEQRES   9 C  476  LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY          
SEQRES  10 C  476  VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU          
SEQRES  11 C  476  ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY          
SEQRES  12 C  476  ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL          
SEQRES  13 C  476  SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE          
SEQRES  14 C  476  ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET          
SEQRES  15 C  476  MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY          
SEQRES  16 C  476  GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU          
SEQRES  17 C  476  PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY          
SEQRES  18 C  476  LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN          
SEQRES  19 C  476  ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP          
SEQRES  20 C  476  SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO          
SEQRES  21 C  476  ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR          
SEQRES  22 C  476  LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR          
SEQRES  23 C  476  THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO          
SEQRES  24 C  476  GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL          
SEQRES  25 C  476  ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA          
SEQRES  26 C  476  LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN          
SEQRES  27 C  476  ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG          
SEQRES  28 C  476  VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO          
SEQRES  29 C  476  LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU          
SEQRES  30 C  476  ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN          
SEQRES  31 C  476  PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS          
SEQRES  32 C  476  SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN          
SEQRES  33 C  476  CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 C  476  PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER          
SEQRES  35 C  476  SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS          
SEQRES  36 C  476  VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER          
SEQRES  37 C  476  PHE LEU PRO ARG HIS HIS HIS HIS                              
SEQRES   1 D  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 D  476  GLY PRO THR PRO LEU PRO PHE ILE GLY ASN TYR LEU GLN          
SEQRES   3 D  476  LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE          
SEQRES   4 D  476  SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY          
SEQRES   5 D  476  PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL          
SEQRES   6 D  476  ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY          
SEQRES   7 D  476  ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY          
SEQRES   8 D  476  TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN          
SEQRES   9 D  476  LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY          
SEQRES  10 D  476  VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU          
SEQRES  11 D  476  ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY          
SEQRES  12 D  476  ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL          
SEQRES  13 D  476  SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE          
SEQRES  14 D  476  ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET          
SEQRES  15 D  476  MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY          
SEQRES  16 D  476  GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU          
SEQRES  17 D  476  PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY          
SEQRES  18 D  476  LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN          
SEQRES  19 D  476  ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP          
SEQRES  20 D  476  SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO          
SEQRES  21 D  476  ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR          
SEQRES  22 D  476  LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR          
SEQRES  23 D  476  THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO          
SEQRES  24 D  476  GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL          
SEQRES  25 D  476  ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA          
SEQRES  26 D  476  LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN          
SEQRES  27 D  476  ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG          
SEQRES  28 D  476  VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO          
SEQRES  29 D  476  LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU          
SEQRES  30 D  476  ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN          
SEQRES  31 D  476  PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS          
SEQRES  32 D  476  SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN          
SEQRES  33 D  476  CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU          
SEQRES  34 D  476  PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER          
SEQRES  35 D  476  SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS          
SEQRES  36 D  476  VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER          
SEQRES  37 D  476  PHE LEU PRO ARG HIS HIS HIS HIS                              
HET    HEM  A 500      43                                                       
HET    NCT  A 501      12                                                       
HET    HEM  B 500      43                                                       
HET    NCT  B 501      12                                                       
HET    HEM  C 500      43                                                       
HET    NCT  C 501      12                                                       
HET    NCT  D 501      12                                                       
HET    HEM  D 502      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE                          
HETSYN     HEM HEME                                                             
HETSYN     NCT (S)-(-)-NICOTINE, 3-[(2S)-1-METHYL-2-PYRROLIDINYL]               
HETSYN   2 NCT  PYRIDINE                                                        
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  NCT    4(C10 H14 N2)                                                
FORMUL  13  HOH   *138(H2 O)                                                    
HELIX    1   1 ASN A   45  LEU A   49  5                                   5    
HELIX    2   2 GLN A   53  GLY A   66  1                                  14    
HELIX    3   3 CYS A   82  VAL A   92  1                                  11    
HELIX    4   4 GLN A  104  LYS A  112  1                                   9    
HELIX    5   5 ASN A  120  PHE A  138  1                                  19    
HELIX    6   6 LYS A  142  GLY A  162  1                                  21    
HELIX    7   7 PRO A  170  GLY A  188  1                                  19    
HELIX    8   8 ASP A  195  THR A  212  1                                  18    
HELIX    9   9 THR A  214  LYS A  228  1                                  15    
HELIX   10  10 GLY A  232  THR A  258  1                                  27    
HELIX   11  11 ASP A  266  GLU A  278  1                                  13    
HELIX   12  12 TYR A  287  HIS A  320  1                                  34    
HELIX   13  13 HIS A  320  ILE A  335  1                                  16    
HELIX   14  14 LYS A  342  LYS A  348  5                                   7    
HELIX   15  15 MET A  349  ASP A  364  1                                  16    
HELIX   16  16 MET A  394  ARG A  400  1                                   7    
HELIX   17  17 ASN A  412  LEU A  417  5                                   6    
HELIX   18  18 GLY A  441  ASN A  459  1                                  19    
HELIX   19  19 SER A  467  ILE A  471  5                                   5    
HELIX   20  20 ASN B   45  LEU B   49  5                                   5    
HELIX   21  21 GLN B   53  GLY B   66  1                                  14    
HELIX   22  22 CYS B   82  VAL B   92  1                                  11    
HELIX   23  23 GLN B  104  LYS B  112  1                                   9    
HELIX   24  24 ASN B  120  PHE B  138  1                                  19    
HELIX   25  25 LYS B  142  GLY B  162  1                                  21    
HELIX   26  26 PRO B  170  GLY B  188  1                                  19    
HELIX   27  27 ASP B  195  THR B  212  1                                  18    
HELIX   28  28 THR B  214  LYS B  228  1                                  15    
HELIX   29  29 GLY B  232  ARG B  257  1                                  26    
HELIX   30  30 ASP B  266  GLU B  277  1                                  12    
HELIX   31  31 TYR B  287  HIS B  320  1                                  34    
HELIX   32  32 HIS B  320  ILE B  335  1                                  16    
HELIX   33  33 LYS B  342  LYS B  348  5                                   7    
HELIX   34  34 MET B  349  ASP B  364  1                                  16    
HELIX   35  35 MET B  394  ARG B  400  1                                   7    
HELIX   36  36 ASN B  412  LEU B  417  5                                   6    
HELIX   37  37 GLY B  441  PHE B  460  1                                  20    
HELIX   38  38 ASN C   45  LEU C   49  5                                   5    
HELIX   39  39 ASN C   50  GLU C   52  5                                   3    
HELIX   40  40 GLN C   53  GLY C   66  1                                  14    
HELIX   41  41 GLY C   83  VAL C   92  1                                  10    
HELIX   42  42 GLN C  104  LYS C  112  1                                   9    
HELIX   43  43 ASN C  120  PHE C  138  1                                  19    
HELIX   44  44 LYS C  142  GLY C  162  1                                  21    
HELIX   45  45 PRO C  170  GLY C  188  1                                  19    
HELIX   46  46 ASP C  195  SER C  213  1                                  19    
HELIX   47  47 THR C  214  LYS C  228  1                                  15    
HELIX   48  48 GLY C  232  ARG C  257  1                                  26    
HELIX   49  49 ASP C  266  GLU C  277  1                                  12    
HELIX   50  50 TYR C  287  HIS C  320  1                                  34    
HELIX   51  51 HIS C  320  GLY C  336  1                                  17    
HELIX   52  52 LYS C  342  LYS C  348  5                                   7    
HELIX   53  53 MET C  349  ASP C  364  1                                  16    
HELIX   54  54 MET C  394  LEU C  399  1                                   6    
HELIX   55  55 ASN C  412  LEU C  417  5                                   6    
HELIX   56  56 GLY C  441  ASN C  459  1                                  19    
HELIX   57  57 SER C  467  ILE C  471  5                                   5    
HELIX   58  58 ASN D   45  LEU D   49  5                                   5    
HELIX   59  59 ASN D   50  GLU D   52  5                                   3    
HELIX   60  60 GLN D   53  GLY D   66  1                                  14    
HELIX   61  61 GLY D   83  VAL D   92  1                                  10    
HELIX   62  62 GLN D  104  LYS D  112  1                                   9    
HELIX   63  63 ASN D  120  PHE D  138  1                                  19    
HELIX   64  64 LYS D  142  GLY D  162  1                                  21    
HELIX   65  65 ASP D  169  GLY D  188  1                                  20    
HELIX   66  66 ASP D  195  SER D  213  1                                  19    
HELIX   67  67 THR D  214  LYS D  228  1                                  15    
HELIX   68  68 GLY D  232  THR D  258  1                                  27    
HELIX   69  69 ASP D  266  GLU D  278  1                                  13    
HELIX   70  70 TYR D  287  MET D  318  1                                  32    
HELIX   71  71 HIS D  320  ILE D  335  1                                  16    
HELIX   72  72 LYS D  342  ALA D  347  5                                   6    
HELIX   73  73 MET D  349  ASP D  364  1                                  16    
HELIX   74  74 MET D  394  ARG D  400  1                                   7    
HELIX   75  75 ASN D  412  LEU D  417  5                                   6    
HELIX   76  76 GLY D  441  PHE D  460  1                                  20    
HELIX   77  77 SER D  467  ILE D  471  5                                   5    
SHEET    1   A 5 VAL A  68  LEU A  73  0                                        
SHEET    2   A 5 ARG A  76  LEU A  81 -1  O  VAL A  78   N  ILE A  71           
SHEET    3   A 5 GLU A 390  PRO A 393  1  O  GLU A 390   N  VAL A  79           
SHEET    4   A 5 ARG A 372  ARG A 373 -1  N  ARG A 372   O  VAL A 391           
SHEET    5   A 5 GLY A 100  ARG A 101 -1  N  GLY A 100   O  ARG A 373           
SHEET    1   B 2 THR A 378  PHE A 380  0                                        
SHEET    2   B 2 PHE A 383  LEU A 385 -1  O  LEU A 385   N  THR A 378           
SHEET    1   C 2 PHE A 460  SER A 464  0                                        
SHEET    2   C 2 MET A 489  PRO A 493 -1  O  LEU A 492   N  ARG A 461           
SHEET    1   D 2 PRO A 475  VAL A 478  0                                        
SHEET    2   D 2 THR A 482  PRO A 484 -1  O  ILE A 483   N  HIS A 477           
SHEET    1   E 5 VAL B  68  LEU B  73  0                                        
SHEET    2   E 5 ARG B  76  LEU B  81 -1  O  VAL B  78   N  ILE B  71           
SHEET    3   E 5 GLU B 390  PRO B 393  1  O  GLU B 390   N  VAL B  79           
SHEET    4   E 5 ARG B 372  ARG B 373 -1  N  ARG B 372   O  VAL B 391           
SHEET    5   E 5 GLY B 100  ARG B 101 -1  N  GLY B 100   O  ARG B 373           
SHEET    1   F 2 THR B 378  PHE B 380  0                                        
SHEET    2   F 2 PHE B 383  LEU B 385 -1  O  LEU B 385   N  THR B 378           
SHEET    1   G 2 ARG B 461  SER B 464  0                                        
SHEET    2   G 2 MET B 489  LEU B 492 -1  O  LEU B 492   N  ARG B 461           
SHEET    1   H 2 PRO B 475  VAL B 478  0                                        
SHEET    2   H 2 THR B 482  PRO B 484 -1  O  ILE B 483   N  LYS B 476           
SHEET    1   I 5 VAL C  68  LEU C  73  0                                        
SHEET    2   I 5 ARG C  76  LEU C  81 -1  O  VAL C  78   N  ILE C  71           
SHEET    3   I 5 GLU C 390  PRO C 393  1  O  TYR C 392   N  VAL C  79           
SHEET    4   I 5 ARG C 372  ARG C 373 -1  N  ARG C 372   O  VAL C 391           
SHEET    5   I 5 GLY C 100  ARG C 101 -1  N  GLY C 100   O  ARG C 373           
SHEET    1   J 2 THR C 378  PHE C 380  0                                        
SHEET    2   J 2 PHE C 383  LEU C 385 -1  O  LEU C 385   N  THR C 378           
SHEET    1   K 2 PHE C 460  SER C 464  0                                        
SHEET    2   K 2 MET C 489  PRO C 493 -1  O  LEU C 492   N  ARG C 461           
SHEET    1   L 2 PRO C 475  VAL C 478  0                                        
SHEET    2   L 2 THR C 482  PRO C 484 -1  O  ILE C 483   N  HIS C 477           
SHEET    1   M 5 VAL D  68  LEU D  73  0                                        
SHEET    2   M 5 ARG D  76  LEU D  81 -1  O  VAL D  78   N  ILE D  71           
SHEET    3   M 5 GLU D 390  PRO D 393  1  O  GLU D 390   N  VAL D  79           
SHEET    4   M 5 ARG D 372  ARG D 373 -1  N  ARG D 372   O  VAL D 391           
SHEET    5   M 5 GLY D 100  ARG D 101 -1  N  GLY D 100   O  ARG D 373           
SHEET    1   N 2 THR D 378  PHE D 380  0                                        
SHEET    2   N 2 PHE D 383  LEU D 385 -1  O  LEU D 385   N  THR D 378           
SHEET    1   O 2 ARG D 461  SER D 464  0                                        
SHEET    2   O 2 MET D 489  LEU D 492 -1  O  LEU D 492   N  ARG D 461           
SHEET    1   P 2 PRO D 475  VAL D 478  0                                        
SHEET    2   P 2 THR D 482  PRO D 484 -1  O  ILE D 483   N  HIS D 477           
LINK         SG  CYS B 439                FE   HEM B 500     1555   1555  2.23  
LINK         SG  CYS D 439                FE   HEM D 502     1555   1555  2.28  
LINK         SG  CYS A 439                FE   HEM A 500     1555   1555  2.36  
LINK         SG  CYS C 439                FE   HEM C 500     1555   1555  2.39  
SITE     1 AC1 18 ARG A 101  VAL A 117  ARG A 128  GLY A 301                    
SITE     2 AC1 18 GLY A 302  THR A 305  ARG A 372  LEU A 395                    
SITE     3 AC1 18 PRO A 431  PHE A 432  SER A 433  ARG A 437                    
SITE     4 AC1 18 ASN A 438  CYS A 439  PHE A 440  GLY A 441                    
SITE     5 AC1 18 NCT A 501  HOH A 647                                          
SITE     1 AC2  7 PHE A 107  PHE A 209  ASN A 297  GLY A 301                    
SITE     2 AC2  7 THR A 305  PHE A 480  HEM A 500                               
SITE     1 AC3 19 ARG B 101  VAL B 117  ARG B 128  GLY B 301                    
SITE     2 AC3 19 GLY B 302  THR B 305  GLN B 360  SER B 369                    
SITE     3 AC3 19 ARG B 372  LEU B 395  PRO B 431  PHE B 432                    
SITE     4 AC3 19 SER B 433  ILE B 434  ARG B 437  ASN B 438                    
SITE     5 AC3 19 CYS B 439  PHE B 440  NCT B 501                               
SITE     1 AC4  4 PHE B 107  ASN B 297  THR B 305  HEM B 500                    
SITE     1 AC5 19 ARG C 101  VAL C 117  ARG C 128  GLY C 301                    
SITE     2 AC5 19 GLY C 302  THR C 305  VAL C 306  THR C 309                    
SITE     3 AC5 19 LEU C 370  ARG C 372  LEU C 395  PRO C 431                    
SITE     4 AC5 19 PHE C 432  SER C 433  ARG C 437  ASN C 438                    
SITE     5 AC5 19 CYS C 439  PHE C 440  NCT C 501                               
SITE     1 AC6  5 PHE C 107  PHE C 209  ASN C 297  GLY C 301                    
SITE     2 AC6  5 HEM C 500                                                     
SITE     1 AC7  5 GLY D 301  THR D 305  LEU D 370  PHE D 480                    
SITE     2 AC7  5 HEM D 502                                                     
SITE     1 AC8 21 ARG D 101  VAL D 117  ARG D 128  GLY D 301                    
SITE     2 AC8 21 GLY D 302  THR D 305  VAL D 306  SER D 369                    
SITE     3 AC8 21 LEU D 370  ARG D 372  LEU D 395  PRO D 431                    
SITE     4 AC8 21 PHE D 432  SER D 433  ARG D 437  CYS D 439                    
SITE     5 AC8 21 PHE D 440  GLY D 441  ALA D 445  NCT D 501                    
SITE     6 AC8 21 HOH D 618                                                     
CRYST1   71.214  194.038   90.266  90.00 102.70  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014042  0.000000  0.003165        0.00000                         
SCALE2      0.000000  0.005154  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011356        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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