GenomeNet

Database: PDB
Entry: 3PM0
LinkDB: 3PM0
Original site: 3PM0 
HEADER    OXIDOREDUCTASE                          15-NOV-10   3PM0              
TITLE     STRUCTURAL CHARACTERIZATION OF THE COMPLEX BETWEEN ALPHA-             
TITLE    2 NAPHTHOFLAVONE AND HUMAN CYTOCHROME P450 1B1 (CYP1B1)                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 1B1;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYPIB1;                                                     
COMPND   5 EC: 1.14.14.1;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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: CYP1B1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    CYP1B1, P450 1B1, P450, MONOOXYGENASE, ALPHA-NAPHTHOFLAVONE, HEME,    
KEYWDS   2 17BETA-ESTRADIOL, OXIDOREDUCTASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.WANG,C.D.STOUT,E.F.JOHNSON                                          
REVDAT   3   02-MAR-11 3PM0    1       JRNL                                     
REVDAT   2   05-JAN-11 3PM0    1       JRNL                                     
REVDAT   1   08-DEC-10 3PM0    0                                                
JRNL        AUTH   A.WANG,U.SAVAS,C.D.STOUT,E.F.JOHNSON                         
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF THE COMPLEX BETWEEN           
JRNL        TITL 2 {ALPHA}-NAPHTHOFLAVONE AND HUMAN CYTOCHROME P450 1B1.        
JRNL        REF    J.BIOL.CHEM.                  V. 286  5736 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21147782                                                     
JRNL        DOI    10.1074/JBC.M110.204420                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.21                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 15654                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 781                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.80                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3187                       
REMARK   3   BIN FREE R VALUE                    : 0.3274                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 82                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.060                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3655                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 33                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.39                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -17.14500                                            
REMARK   3    B22 (A**2) : 27.70100                                             
REMARK   3    B33 (A**2) : -10.55700                                            
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.43                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.44                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 51.99                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : XDICT_HEME_RELAX.PAR                           
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : BHF.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3PM0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062537.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING BENT CUBE-ROOT I   
REMARK 200                                   -BEAM SINGLE CRYSTAL               
REMARK 200  OPTICS                         : RH COATED FLAT MIRROR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15741                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.43800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-3350, AMMONIUM DIBASIC CITRATE,      
REMARK 280  POTASSIUM PHOSPHATE, NACL, GLYCEROL, BETA-MERCAPTOETHANOL, ALPHA-   
REMARK 280  NAPHTHOFLAVONE, CHAPS, PH 5.1, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       42.08500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.99000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.08500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.99000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     LYS A    44                                                      
REMARK 465     THR A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     LYS A    48                                                      
REMARK 465     GLY A    49                                                      
REMARK 465     LYS A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     PRO A    54                                                      
REMARK 465     PHE A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     TRP A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     LEU A    59                                                      
REMARK 465     ILE A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     ALA A    63                                                      
REMARK 465     ALA A    64                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     VAL A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     SER A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     SER A   531                                                      
REMARK 465     ALA A   532                                                      
REMARK 465     VAL A   533                                                      
REMARK 465     GLN A   534                                                      
REMARK 465     ASN A   535                                                      
REMARK 465     LEU A   536                                                      
REMARK 465     GLN A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     LYS A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     THR A   541                                                      
REMARK 465     CYS A   542                                                      
REMARK 465     GLN A   543                                                      
REMARK 465     HIS A   544                                                      
REMARK 465     HIS A   545                                                      
REMARK 465     HIS A   546                                                      
REMARK 465     HIS A   547                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  80      -33.23   -138.35                                   
REMARK 500    VAL A 108      -71.76   -102.09                                   
REMARK 500    SER A 112      -35.77    121.87                                   
REMARK 500    THR A 157       18.65     86.91                                   
REMARK 500    ASP A 218      108.93    -47.79                                   
REMARK 500    PRO A 285      -81.76    -29.61                                   
REMARK 500    LYS A 454      -36.68    -35.68                                   
REMARK 500    SER A 464     -169.08     66.38                                   
REMARK 500    PRO A 500      -74.05    -59.85                                   
REMARK 500    ALA A 501      158.14    -46.72                                   
REMARK 500    LEU A 509      -79.31     71.61                                   
REMARK 500    SER A 515      138.35    -38.42                                   
REMARK 500    LEU A 529       86.12    -67.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 494         0.19    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 900  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 470   SG                                                     
REMARK 620 2 HEM A 900   NA   98.0                                              
REMARK 620 3 HEM A 900   NB   90.7  88.0                                        
REMARK 620 4 HEM A 900   NC   86.2 175.7  90.8                                  
REMARK 620 5 HEM A 900   ND   93.7  91.2 175.6  89.7                            
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 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHF A 800                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HI4   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 1A2 (CYP1A2)                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS AMINO ACID SUBSTITUTION IS A NATURALLY OCCURRING ALLELIC        
REMARK 999 VARIANT FOR THE ENZYME. IT ARISES FROM A SINGLE NUCLEOTIDE           
REMARK 999 POLYMORPHISM (SNP) WHICH IS DESCRIBED IN THE SNP DATABASE WITH       
REMARK 999 ACCESSION NUMBER RS1056827 WITH AN ALLELE FREQUENCY OF ABOUT 35%.    
DBREF  3PM0 A   51   543  UNP    Q16678   CP1B1_HUMAN     51    543             
SEQADV 3PM0 MET A   41  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 ALA A   42  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 LYS A   43  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 LYS A   44  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 THR A   45  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 SER A   46  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 SER A   47  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 LYS A   48  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 GLY A   49  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 LYS A   50  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 SER A  119  UNP  Q16678    ALA   119 SEE REMARK 999                 
SEQADV 3PM0 HIS A  544  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 HIS A  545  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 HIS A  546  UNP  Q16678              EXPRESSION TAG                 
SEQADV 3PM0 HIS A  547  UNP  Q16678              EXPRESSION TAG                 
SEQRES   1 A  507  MET ALA LYS LYS THR SER SER LYS GLY LYS PRO PRO GLY          
SEQRES   2 A  507  PRO PHE ALA TRP PRO LEU ILE GLY ASN ALA ALA ALA VAL          
SEQRES   3 A  507  GLY GLN ALA ALA HIS LEU SER PHE ALA ARG LEU ALA ARG          
SEQRES   4 A  507  ARG TYR GLY ASP VAL PHE GLN ILE ARG LEU GLY SER CYS          
SEQRES   5 A  507  PRO ILE VAL VAL LEU ASN GLY GLU ARG ALA ILE HIS GLN          
SEQRES   6 A  507  ALA LEU VAL GLN GLN GLY SER ALA PHE ALA ASP ARG PRO          
SEQRES   7 A  507  SER PHE ALA SER PHE ARG VAL VAL SER GLY GLY ARG SER          
SEQRES   8 A  507  MET ALA PHE GLY HIS TYR SER GLU HIS TRP LYS VAL GLN          
SEQRES   9 A  507  ARG ARG ALA ALA HIS SER MET MET ARG ASN PHE PHE THR          
SEQRES  10 A  507  ARG GLN PRO ARG SER ARG GLN VAL LEU GLU GLY HIS VAL          
SEQRES  11 A  507  LEU SER GLU ALA ARG GLU LEU VAL ALA LEU LEU VAL ARG          
SEQRES  12 A  507  GLY SER ALA ASP GLY ALA PHE LEU ASP PRO ARG PRO LEU          
SEQRES  13 A  507  THR VAL VAL ALA VAL ALA ASN VAL MET SER ALA VAL CYS          
SEQRES  14 A  507  PHE GLY CYS ARG TYR SER HIS ASP ASP PRO GLU PHE ARG          
SEQRES  15 A  507  GLU LEU LEU SER HIS ASN GLU GLU PHE GLY ARG THR VAL          
SEQRES  16 A  507  GLY ALA GLY SER LEU VAL ASP VAL MET PRO TRP LEU GLN          
SEQRES  17 A  507  TYR PHE PRO ASN PRO VAL ARG THR VAL PHE ARG GLU PHE          
SEQRES  18 A  507  GLU GLN LEU ASN ARG ASN PHE SER ASN PHE ILE LEU ASP          
SEQRES  19 A  507  LYS PHE LEU ARG HIS CYS GLU SER LEU ARG PRO GLY ALA          
SEQRES  20 A  507  ALA PRO ARG ASP MET MET ASP ALA PHE ILE LEU SER ALA          
SEQRES  21 A  507  GLU LYS LYS ALA ALA GLY ASP SER HIS GLY GLY GLY ALA          
SEQRES  22 A  507  ARG LEU ASP LEU GLU ASN VAL PRO ALA THR ILE THR ASP          
SEQRES  23 A  507  ILE PHE GLY ALA SER GLN ASP THR LEU SER THR ALA LEU          
SEQRES  24 A  507  GLN TRP LEU LEU LEU LEU PHE THR ARG TYR PRO ASP VAL          
SEQRES  25 A  507  GLN THR ARG VAL GLN ALA GLU LEU ASP GLN VAL VAL GLY          
SEQRES  26 A  507  ARG ASP ARG LEU PRO CYS MET GLY ASP GLN PRO ASN LEU          
SEQRES  27 A  507  PRO TYR VAL LEU ALA PHE LEU TYR GLU ALA MET ARG PHE          
SEQRES  28 A  507  SER SER PHE VAL PRO VAL THR ILE PRO HIS ALA THR THR          
SEQRES  29 A  507  ALA ASN THR SER VAL LEU GLY TYR HIS ILE PRO LYS ASP          
SEQRES  30 A  507  THR VAL VAL PHE VAL ASN GLN TRP SER VAL ASN HIS ASP          
SEQRES  31 A  507  PRO LEU LYS TRP PRO ASN PRO GLU ASN PHE ASP PRO ALA          
SEQRES  32 A  507  ARG PHE LEU ASP LYS ASP GLY LEU ILE ASN LYS ASP LEU          
SEQRES  33 A  507  THR SER ARG VAL MET ILE PHE SER VAL GLY LYS ARG ARG          
SEQRES  34 A  507  CYS ILE GLY GLU GLU LEU SER LYS MET GLN LEU PHE LEU          
SEQRES  35 A  507  PHE ILE SER ILE LEU ALA HIS GLN CYS ASP PHE ARG ALA          
SEQRES  36 A  507  ASN PRO ASN GLU PRO ALA LYS MET ASN PHE SER TYR GLY          
SEQRES  37 A  507  LEU THR ILE LYS PRO LYS SER PHE LYS VAL ASN VAL THR          
SEQRES  38 A  507  LEU ARG GLU SER MET GLU LEU LEU ASP SER ALA VAL GLN          
SEQRES  39 A  507  ASN LEU GLN ALA LYS GLU THR CYS GLN HIS HIS HIS HIS          
HET    HEM  A 900      43                                                       
HET    BHF  A 800      21                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     BHF 2-PHENYL-4H-BENZO[H]CHROMEN-4-ONE                                
HETSYN     HEM HEME                                                             
HETSYN     BHF 7,8-BENZOFLAVONE; ALPHA-NAPHTHOFLAVONE                           
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  BHF    C19 H12 O2                                                   
FORMUL   4  HOH   *33(H2 O)                                                     
HELIX    1   1 ALA A   69  GLY A   82  1                                  14    
HELIX    2   2 GLY A   99  VAL A  108  1                                  10    
HELIX    3   3 PHE A  120  VAL A  126  1                                   7    
HELIX    4   4 SER A  127  ARG A  130  5                                   4    
HELIX    5   5 SER A  138  PHE A  155  1                                  18    
HELIX    6   6 ARG A  161  GLY A  184  1                                  24    
HELIX    7   7 SER A  185  ALA A  189  5                                   5    
HELIX    8   8 PRO A  193  PHE A  210  1                                  18    
HELIX    9   9 ASP A  218  LEU A  225  1                                   8    
HELIX   10  10 HIS A  227  GLY A  236  1                                  10    
HELIX   11  11 MET A  244  PHE A  250  5                                   7    
HELIX   12  12 ASN A  252  LEU A  283  1                                  32    
HELIX   13  13 ASP A  291  ALA A  305  1                                  15    
HELIX   14  14 ASP A  316  GLU A  318  5                                   3    
HELIX   15  15 ASN A  319  TYR A  349  1                                  31    
HELIX   16  16 TYR A  349  VAL A  364  1                                  16    
HELIX   17  17 CYS A  371  ASN A  377  5                                   7    
HELIX   18  18 LEU A  378  SER A  393  1                                  16    
HELIX   19  19 GLN A  424  HIS A  429  1                                   6    
HELIX   20  20 ASP A  441  LEU A  446  5                                   6    
HELIX   21  21 ASN A  453  SER A  458  1                                   6    
HELIX   22  22 GLY A  472  GLN A  490  1                                  19    
SHEET    1   A 4 VAL A  84  LEU A  89  0                                        
SHEET    2   A 4 CYS A  92  LEU A  97 -1  O  ILE A  94   N  ILE A  87           
SHEET    3   A 4 VAL A 419  VAL A 422  1  O  PHE A 421   N  LEU A  97           
SHEET    4   A 4 HIS A 401  ALA A 402 -1  N  HIS A 401   O  VAL A 420           
SHEET    1   B 2 THR A 407  VAL A 409  0                                        
SHEET    2   B 2 TYR A 412  ILE A 414 -1  O  ILE A 414   N  THR A 407           
SHEET    1   C 2 CYS A 491  ALA A 495  0                                        
SHEET    2   C 2 VAL A 518  LEU A 522 -1  O  ASN A 519   N  ARG A 494           
SHEET    1   D 2 PHE A 505  TYR A 507  0                                        
SHEET    2   D 2 ILE A 511  PRO A 513 -1  O  LYS A 512   N  SER A 506           
LINK         SG  CYS A 470                FE   HEM A 900     1555   1555  2.35  
SITE     1 AC1 25 ARG A 117  MET A 132  ALA A 133  TRP A 141                    
SITE     2 AC1 25 ARG A 145  MET A 152  ILE A 327  ALA A 330                    
SITE     3 AC1 25 SER A 331  THR A 334  LEU A 335  PHE A 394                    
SITE     4 AC1 25 VAL A 395  THR A 398  ILE A 399  HIS A 401                    
SITE     5 AC1 25 GLN A 424  ILE A 462  PHE A 463  SER A 464                    
SITE     6 AC1 25 ARG A 468  CYS A 470  ILE A 471  SER A 476                    
SITE     7 AC1 25 BHF A 800                                                     
SITE     1 AC2  9 PHE A 134  ASN A 228  PHE A 231  LEU A 264                    
SITE     2 AC2  9 ASP A 326  ALA A 330  THR A 334  LEU A 509                    
SITE     3 AC2  9 HEM A 900                                                     
CRYST1   84.170  103.980   62.970  90.00  90.00  90.00 P 21 21 2     4          
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      0.011881  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009617  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015881        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system