GenomeNet

Database: PDB
Entry: 3EBS
LinkDB: 3EBS
Original site: 3EBS 
HEADER    OXIDOREDUCTASE                          28-AUG-08   3EBS              
TITLE     HUMAN CYTOCHROME P450 2A6 I208S/I300F/G301A/S369G IN COMPLEX          
TITLE    2 WITH PHENACETIN                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2A6;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 29 TO 494;                                    
COMPND   5 SYNONYM: CYPIIA6, COUMARIN 7-HYDROXYLASE, P450 IIA3,                 
COMPND   6 CYP2A3, P450(I);                                                     
COMPND   7 EC: 1.14.14.1;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP2A6, CYP2A3;                                                
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: PKKA2A6DH                                 
KEYWDS    CYP2A6, P450 2A6, CYP2A13, P450 2A13, MONOOXYGENASE,                  
KEYWDS   2 OXIDOREDUCATASE, HEME, ENDOPLASMIC RETICULUM, IRON,                  
KEYWDS   3 MEMBRANE, METAL-BINDING, MICROSOME, PHENACETIN,                      
KEYWDS   4 OXIDOREDUCTASE, POLYMORPHISM                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.DEVORE,E.E.SCOTT                                                  
REVDAT   4   09-JUN-09 3EBS    1       REVDAT                                   
REVDAT   3   24-FEB-09 3EBS    1       VERSN                                    
REVDAT   2   23-DEC-08 3EBS    1       JRNL                                     
REVDAT   1   23-SEP-08 3EBS    0                                                
JRNL        AUTH   N.M.DEVORE,B.D.SMITH,M.J.URBAN,E.E.SCOTT                     
JRNL        TITL   KEY RESIDUES CONTROLLING PHENACETIN METABOLISM BY            
JRNL        TITL 2 HUMAN CYTOCHROME P4502A ENZYMES.                             
JRNL        REF    DRUG METAB.DISPOS.            V.  36  2582 2008              
JRNL        REFN                                                                
JRNL        PMID   18779312                                                     
JRNL        DOI    10.1124/DMD.108.023770                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 115652                         
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6120                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8518                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 439                          
REMARK   3   BIN FREE R VALUE                    : 0.3740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15033                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 211                                     
REMARK   3   SOLVENT ATOMS            : 276                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.39                          
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) : -0.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.251         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.218         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.172         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.745         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15638 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21116 ; 1.498 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1854 ; 6.597 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   770 ;35.233 ;23.273       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2722 ;17.103 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   128 ;18.713 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2187 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12069 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7288 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10431 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   502 ; 0.329 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    38 ; 0.242 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.241 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9644 ; 0.690 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15001 ; 1.165 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6842 ; 1.862 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6107 ; 2.717 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3EBS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049126.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-08                          
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                         : NULL                               
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   : 121786                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 10.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: CYP2A6 PDB ENTRY 1Z10                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.10 M TRIS, 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       79.56300            
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   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      -58.62     65.07                                   
REMARK 500    PHE A 118       46.84   -102.28                                   
REMARK 500    ASN A 412       97.77   -161.39                                   
REMARK 500    HIS A 415      -35.75    -36.95                                   
REMARK 500    SER A 433     -170.50     63.62                                   
REMARK 500    PRO A 468      -35.68    -36.87                                   
REMARK 500    PHE B  42      -53.42     72.74                                   
REMARK 500    PHE B 118       44.33    -97.24                                   
REMARK 500    ARG B 381       48.95     37.61                                   
REMARK 500    ASP B 382       -7.00     84.30                                   
REMARK 500    ASN B 418      170.96    -56.05                                   
REMARK 500    SER B 433     -165.69     59.94                                   
REMARK 500    PRO B 468      -28.84    -27.65                                   
REMARK 500    HIS B 495        2.37    100.81                                   
REMARK 500    PHE C  42      -56.83     70.80                                   
REMARK 500    LYS C 337        9.26   -166.68                                   
REMARK 500    ARG C 381     -124.46     47.77                                   
REMARK 500    LYS C 387      129.30    -37.69                                   
REMARK 500    SER C 433     -172.27     66.01                                   
REMARK 500    PHE D  42      -56.13     64.92                                   
REMARK 500    PRO D 261      -19.27    -47.04                                   
REMARK 500    ASP D 266     -173.15   -172.01                                   
REMARK 500    MET D 349       74.30   -119.69                                   
REMARK 500    ASP D 364       57.99     37.20                                   
REMARK 500    ARG D 381     -122.97     49.01                                   
REMARK 500    SER D 433     -162.13     65.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     GLU D 103        24.4      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N4E A 1                   
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N4E B 1                   
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 500                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 500                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N4E D 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Z11   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 WITH METHOXSALEN          
REMARK 900 BOUND                                                                
REMARK 900 RELATED ID: 2FDY   RELATED DB: PDB                                   
REMARK 900 MICROSOMAL P450 2A6 WITH THE INHIBITOR ADRITHIOL BOUND               
REMARK 900 RELATED ID: 1Z10   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 WITH                  
REMARK 900 COUMARIN BOUND                                                       
REMARK 900 RELATED ID: 2FDU   RELATED DB: PDB                                   
REMARK 900 MICROSOMAL P450 2A6 WITH THE INHIBITOR N,N-DIMETHYL(5-               
REMARK 900 (PYRIDIN-3-YL)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-          
REMARK 900 3-YL)FURAN-2-YL)METHANAMINE BOUND                                    
REMARK 900 RELATED ID: 2FDW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 WITH THE              
REMARK 900 INHIBITOR (5-(PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE BOUND              
REMARK 900 RELATED ID: 2PG6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 L240C/N297Q           
REMARK 900 RELATED ID: 2PG7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 N297Q/I300V           
REMARK 900 RELATED ID: 2PG5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 N297Q                 
REMARK 900 RELATED ID: 2P85   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN LUNG CYTOCHROME P450 2A13 WITH INDOLE             
REMARK 900 BOUND IN TWO ALTERNATE CONFORMATIONS                                 
DBREF  3EBS A   29   494  UNP    P11509   CP2A6_HUMAN     29    494             
DBREF  3EBS B   29   494  UNP    P11509   CP2A6_HUMAN     29    494             
DBREF  3EBS C   29   494  UNP    P11509   CP2A6_HUMAN     29    494             
DBREF  3EBS D   29   494  UNP    P11509   CP2A6_HUMAN     29    494             
SEQADV 3EBS MET A   23  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS ALA A   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS A   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS A   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS THR A   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER A   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER A  208  UNP  P11509    ILE   208 ENGINEERED                     
SEQADV 3EBS PHE A  300  UNP  P11509    ILE   300 ENGINEERED                     
SEQADV 3EBS ALA A  301  UNP  P11509    GLY   301 ENGINEERED                     
SEQADV 3EBS GLY A  369  UNP  P11509    SER   369 ENGINEERED                     
SEQADV 3EBS HIS A  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS A  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS A  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS A  498  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS MET B   23  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS ALA B   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS B   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS B   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS THR B   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER B   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER B  208  UNP  P11509    ILE   208 ENGINEERED                     
SEQADV 3EBS PHE B  300  UNP  P11509    ILE   300 ENGINEERED                     
SEQADV 3EBS ALA B  301  UNP  P11509    GLY   301 ENGINEERED                     
SEQADV 3EBS GLY B  369  UNP  P11509    SER   369 ENGINEERED                     
SEQADV 3EBS HIS B  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS B  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS B  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS B  498  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS MET C   23  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS ALA C   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS C   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS C   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS THR C   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER C   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER C  208  UNP  P11509    ILE   208 ENGINEERED                     
SEQADV 3EBS PHE C  300  UNP  P11509    ILE   300 ENGINEERED                     
SEQADV 3EBS ALA C  301  UNP  P11509    GLY   301 ENGINEERED                     
SEQADV 3EBS GLY C  369  UNP  P11509    SER   369 ENGINEERED                     
SEQADV 3EBS HIS C  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS C  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS C  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS C  498  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS MET D   23  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS ALA D   24  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS D   25  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS LYS D   26  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS THR D   27  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER D   28  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS SER D  208  UNP  P11509    ILE   208 ENGINEERED                     
SEQADV 3EBS PHE D  300  UNP  P11509    ILE   300 ENGINEERED                     
SEQADV 3EBS ALA D  301  UNP  P11509    GLY   301 ENGINEERED                     
SEQADV 3EBS GLY D  369  UNP  P11509    SER   369 ENGINEERED                     
SEQADV 3EBS HIS D  495  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS D  496  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS HIS D  497  UNP  P11509              EXPRESSION TAG                 
SEQADV 3EBS 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 SER 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 PHE ALA 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 GLY 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 SER 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 PHE ALA 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 GLY 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 SER 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 PHE ALA 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 GLY 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 SER 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 PHE ALA 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 GLY 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    N4E  A   1      13                                                       
HET    HEM  B 500      43                                                       
HET    N4E  B   1      13                                                       
HET    HEM  C 500      43                                                       
HET    HEM  D 500      43                                                       
HET    N4E  D   1      13                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     N4E N-(4-ETHOXYPHENYL)ACETAMIDE                                      
HETSYN     HEM HEME                                                             
HETSYN     N4E PHENACETIN                                                       
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  N4E    3(C10 H13 N O2)                                              
FORMUL  12  HOH   *276(H2 O)                                                    
HELIX    1   1 ASN A   45  LEU A   49  5                                   5    
HELIX    2   2 ASN A   50  GLU A   52  5                                   3    
HELIX    3   3 GLN A   53  GLY A   66  1                                  14    
HELIX    4   4 CYS A   82  VAL A   92  1                                  11    
HELIX    5   5 GLN A  104  LYS A  112  1                                   9    
HELIX    6   6 ASN A  120  PHE A  138  1                                  19    
HELIX    7   7 LYS A  142  GLY A  162  1                                  21    
HELIX    8   8 PRO A  170  GLY A  188  1                                  19    
HELIX    9   9 ASP A  195  THR A  214  1                                  20    
HELIX   10  10 THR A  214  LYS A  228  1                                  15    
HELIX   11  11 GLY A  232  ARG A  257  1                                  26    
HELIX   12  12 ASP A  266  GLU A  278  1                                  13    
HELIX   13  13 TYR A  287  HIS A  320  1                                  34    
HELIX   14  14 HIS A  320  ILE A  335  1                                  16    
HELIX   15  15 LYS A  342  LYS A  348  5                                   7    
HELIX   16  16 MET A  349  ASP A  364  1                                  16    
HELIX   17  17 MET A  394  ARG A  400  1                                   7    
HELIX   18  18 ASN A  412  LEU A  417  5                                   6    
HELIX   19  19 GLY A  441  ASN A  459  1                                  19    
HELIX   20  20 SER A  467  ILE A  471  5                                   5    
HELIX   21  21 ASN B   45  LEU B   49  5                                   5    
HELIX   22  22 GLN B   53  GLY B   66  1                                  14    
HELIX   23  23 CYS B   82  VAL B   92  1                                  11    
HELIX   24  24 GLN B  104  LYS B  112  1                                   9    
HELIX   25  25 ASN B  120  PHE B  138  1                                  19    
HELIX   26  26 LYS B  142  GLY B  162  1                                  21    
HELIX   27  27 ASP B  169  GLY B  188  1                                  20    
HELIX   28  28 ASP B  195  THR B  212  1                                  18    
HELIX   29  29 THR B  214  LYS B  228  1                                  15    
HELIX   30  30 GLY B  232  THR B  258  1                                  27    
HELIX   31  31 ASP B  266  GLU B  278  1                                  13    
HELIX   32  32 TYR B  287  HIS B  320  1                                  34    
HELIX   33  33 HIS B  320  ILE B  335  1                                  16    
HELIX   34  34 LYS B  342  LYS B  348  5                                   7    
HELIX   35  35 MET B  349  ASP B  364  1                                  16    
HELIX   36  36 MET B  394  ARG B  400  1                                   7    
HELIX   37  37 ASN B  412  LEU B  417  5                                   6    
HELIX   38  38 GLY B  441  ASN B  459  1                                  19    
HELIX   39  39 ASN C   45  LEU C   49  5                                   5    
HELIX   40  40 ASN C   50  GLU C   52  5                                   3    
HELIX   41  41 GLN C   53  GLY C   66  1                                  14    
HELIX   42  42 CYS C   82  VAL C   92  1                                  11    
HELIX   43  43 GLN C  104  LYS C  112  1                                   9    
HELIX   44  44 ASN C  120  PHE C  138  1                                  19    
HELIX   45  45 LYS C  142  GLY C  162  1                                  21    
HELIX   46  46 PRO C  170  PHE C  187  1                                  18    
HELIX   47  47 ASP C  195  THR C  212  1                                  18    
HELIX   48  48 THR C  214  LYS C  228  1                                  15    
HELIX   49  49 GLY C  232  ARG C  257  1                                  26    
HELIX   50  50 ASP C  266  GLU C  278  1                                  13    
HELIX   51  51 TYR C  287  HIS C  320  1                                  34    
HELIX   52  52 HIS C  320  ILE C  335  1                                  16    
HELIX   53  53 LYS C  342  LYS C  348  5                                   7    
HELIX   54  54 MET C  349  ASP C  364  1                                  16    
HELIX   55  55 MET C  394  ARG C  400  1                                   7    
HELIX   56  56 ASN C  412  LEU C  417  5                                   6    
HELIX   57  57 GLY C  441  ASN C  459  1                                  19    
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 CYS D   82  VAL D   92  1                                  11    
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 PRO D  170  GLY D  188  1                                  19    
HELIX   66  66 ASP D  195  THR D  212  1                                  18    
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  HIS D  320  1                                  34    
HELIX   71  71 HIS D  320  ILE D  335  1                                  16    
HELIX   72  72 LYS D  342  LYS D  348  5                                   7    
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  ASN D  459  1                                  19    
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  80   N  PHE A  69           
SHEET    3   A 5 GLU A 390  PRO A 393  1  O  TYR A 392   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  SER A 490   N  LYS A 463           
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  TYR B 392   N  LEU B  81           
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 PHE B 460  SER B 464  0                                        
SHEET    2   G 2 MET B 489  PRO B 493 -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  80   N  PHE C  69           
SHEET    3   I 5 GLU C 390  PRO C 393  1  O  GLU C 390   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  LYS C 463  0                                        
SHEET    2   K 2 SER C 490  PRO C 493 -1  O  SER C 490   N  LYS C 463           
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  80   N  PHE D  69           
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 PHE D 460  SER D 464  0                                        
SHEET    2   O 2 MET D 489  PRO D 493 -1  O  SER D 490   N  LYS D 463           
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 A 439                FE   HEM A 500     1555   1555  2.51  
LINK         SG  CYS B 439                FE   HEM B 500     1555   1555  2.57  
LINK         SG  CYS C 439                FE   HEM C 500     1555   1555  2.52  
SITE     1 AC1 20 N4E A   1  ARG A 101  VAL A 117  ARG A 128                    
SITE     2 AC1 20 LEU A 298  ALA A 301  GLY A 302  THR A 305                    
SITE     3 AC1 20 THR A 309  GLN A 360  ARG A 372  PRO A 431                    
SITE     4 AC1 20 PHE A 432  SER A 433  ARG A 437  CYS A 439                    
SITE     5 AC1 20 PHE A 440  GLY A 441  HOH A 811  HOH A 825                    
SITE     1 AC2  7 PHE A 107  PHE A 111  ASN A 297  PHE A 300                    
SITE     2 AC2  7 LEU A 370  PHE A 480  HEM A 500                               
SITE     1 AC3 22 N4E B   1  ARG B 101  VAL B 116  VAL B 117                    
SITE     2 AC3 22 ARG B 128  ALA B 301  GLY B 302  THR B 305                    
SITE     3 AC3 22 VAL B 306  THR B 309  GLN B 360  ARG B 372                    
SITE     4 AC3 22 LEU B 395  PRO B 431  PHE B 432  SER B 433                    
SITE     5 AC3 22 ARG B 437  CYS B 439  PHE B 440  GLY B 441                    
SITE     6 AC3 22 LEU B 444  HOH B 838                                          
SITE     1 AC4 10 PHE B 107  PHE B 111  VAL B 117  ASN B 297                    
SITE     2 AC4 10 PHE B 300  ALA B 301  THR B 305  LEU B 370                    
SITE     3 AC4 10 PHE B 480  HEM B 500                                          
SITE     1 AC5 20 ARG C 101  VAL C 117  ARG C 128  ALA C 301                    
SITE     2 AC5 20 GLY C 302  THR C 305  VAL C 306  THR C 309                    
SITE     3 AC5 20 GLN C 360  LEU C 370  ARG C 372  LEU C 395                    
SITE     4 AC5 20 PRO C 431  PHE C 432  SER C 433  ARG C 437                    
SITE     5 AC5 20 CYS C 439  PHE C 440  GLY C 441  HOH C 720                    
SITE     1 AC6 18 N4E D   1  ARG D 101  VAL D 117  ARG D 128                    
SITE     2 AC6 18 ALA D 301  GLY D 302  THR D 305  THR D 309                    
SITE     3 AC6 18 GLN D 360  ARG D 372  PRO D 431  PHE D 432                    
SITE     4 AC6 18 SER D 433  ARG D 437  CYS D 439  PHE D 440                    
SITE     5 AC6 18 GLY D 441  HOH D 714                                          
SITE     1 AC7  8 PHE D 107  PHE D 111  ASN D 297  PHE D 300                    
SITE     2 AC7  8 THR D 305  LEU D 370  PHE D 480  HEM D 500                    
CRYST1   70.850  159.126  103.993  90.00  92.08  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      0.014114  0.000000  0.000513        0.00000                         
SCALE2      0.000000  0.006284  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009622        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system