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Database: PDB
Entry: 3LC4
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Original site: 3LC4 
HEADER    OXIDOREDUCTASE                          09-JAN-10   3LC4              
TITLE     HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-DODECANOIC 
TITLE    2 ACID                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2E1;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 32-493;                         
COMPND   5 SYNONYM: CYPIIE1, 4-NITROPHENOL 2-HYDROXYLASE, P450-J;               
COMPND   6 EC: 1.14.13.-;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP2E, CYP2E1;                                                 
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: PKK2E1DH                                  
KEYWDS    CYP2E1, P450 2E1, MONOOXYGENASE, ACETAMINOPHEN, HEME, ENDOPLASMIC     
KEYWDS   2 RETICULUM, IRON, MEMBRANE, METAL-BINDING, MICROSOME, OXIDOREDUCTASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.E.SCOTT,P.R.PORUBSKY                                                
REVDAT   2   28-JUL-10 3LC4    1       JRNL                                     
REVDAT   1   12-MAY-10 3LC4    0                                                
JRNL        AUTH   P.R.PORUBSKY,K.P.BATTAILE,E.E.SCOTT                          
JRNL        TITL   HUMAN CYTOCHROME P450 2E1 STRUCTURES WITH FATTY ACID ANALOGS 
JRNL        TITL 2 REVEAL A PREVIOUSLY UNOBSERVED BINDING MODE.                 
JRNL        REF    J.BIOL.CHEM.                  V. 285 22282 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20463018                                                     
JRNL        DOI    10.1074/JBC.M110.109017                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18847                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1018                            
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1313                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7502                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 124                                     
REMARK   3   SOLVENT ATOMS            : 5                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.28000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.543         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.429         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.186        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.848                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7848 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10648 ; 1.504 ; 2.012       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   915 ; 6.345 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   370 ;35.617 ;23.135       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1335 ;23.341 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;21.775 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1125 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6014 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  4609 ; 0.498 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7508 ; 0.975 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3239 ; 1.350 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3140 ; 2.421 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3LC4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057094.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : 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                  : SIDE-SCATTERING CUBEROOT I- BEAM   
REMARK 200                                   BENT SINGLE CRYSTAL. ASYMMETRIC    
REMARK 200                                   CUT 12.2 DEGS                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19925                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.300                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.18900                            
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) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40500                            
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: PDB ENTRY 3E6I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NAHEPES PH 7.5, 5% ISO-PROPANOL, 22%     
REMARK 280  PEG 2000 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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      112.31450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      168.47175            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.15725            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     LYS A   140                                                      
REMARK 465     GLN A   141                                                      
REMARK 465     HIS A   494                                                      
REMARK 465     HIS A   495                                                      
REMARK 465     HIS A   496                                                      
REMARK 465     HIS A   497                                                      
REMARK 465     MET B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     LYS B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     MET B   138                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     LYS B   140                                                      
REMARK 465     GLN B   141                                                      
REMARK 465     HIS B   494                                                      
REMARK 465     HIS B   495                                                      
REMARK 465     HIS B   496                                                      
REMARK 465     HIS B   497                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 104   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  41      -73.55     69.06                                   
REMARK 500    PHE A  97       40.70   -103.71                                   
REMARK 500    ALA A 108      -29.59    -39.22                                   
REMARK 500    ILE A 114      -78.38   -134.89                                   
REMARK 500    LEU A 171      -62.27   -101.08                                   
REMARK 500    ARG A 186       38.59     39.19                                   
REMARK 500    TYR A 191       11.53    -63.80                                   
REMARK 500    CYS A 261       79.17   -106.67                                   
REMARK 500    LYS A 275      -17.41    -42.88                                   
REMARK 500    GLU A 276       37.94   -146.74                                   
REMARK 500    ALA A 280      -72.84    -54.95                                   
REMARK 500    TYR A 318       76.02   -117.44                                   
REMARK 500    SER A 336      -64.70   -126.36                                   
REMARK 500    THR A 362       61.09     38.65                                   
REMARK 500    VAL A 364       79.34   -102.92                                   
REMARK 500    ASN A 367     -178.43     60.32                                   
REMARK 500    ARG A 379     -126.07     54.87                                   
REMARK 500    ASP A 405       70.07     43.94                                   
REMARK 500    SER A 431     -168.30     82.32                                   
REMARK 500    CYS A 437      126.58    -36.73                                   
REMARK 500    PRO A 466       -9.18    -44.43                                   
REMARK 500    PRO A 491      166.94    -38.33                                   
REMARK 500    PRO B  34      179.17    -57.13                                   
REMARK 500    ILE B  41      -46.71     69.06                                   
REMARK 500    ASP B 111       21.71     47.60                                   
REMARK 500    ILE B 114      -71.37   -134.01                                   
REMARK 500    ARG B 186       12.18     53.35                                   
REMARK 500    TYR B 191       16.46    -66.72                                   
REMARK 500    ASN B 192       -9.12   -144.11                                   
REMARK 500    SER B 231       -7.29    -54.43                                   
REMARK 500    SER B 279      120.91    -36.06                                   
REMARK 500    TYR B 318       76.18   -119.98                                   
REMARK 500    SER B 336      -62.84   -109.91                                   
REMARK 500    THR B 362       57.34     37.72                                   
REMARK 500    VAL B 364       75.14   -108.64                                   
REMARK 500    ASN B 367      172.96     61.04                                   
REMARK 500    ASP B 375      126.97    -37.57                                   
REMARK 500    ARG B 379     -115.68     55.03                                   
REMARK 500    ASN B 416      139.75     82.84                                   
REMARK 500    SER B 431     -167.73     78.61                                   
REMARK 500    PRO B 466      -18.67    -44.84                                   
REMARK 500    PRO B 491      164.58    -47.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 437   SG                                                     
REMARK 620 2 HEM B 500   NA   96.8                                              
REMARK 620 3 HEM B 500   NB   82.9  87.3                                        
REMARK 620 4 HEM B 500   NC   83.0 178.7  91.4                                  
REMARK 620 5 HEM B 500   ND   94.9  95.0 177.0  86.3                            
REMARK 620 6 LC4 B 501   N15 164.0  67.3  94.5 112.9  88.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LC4 A 501   N15                                                    
REMARK 620 2 HEM A 500   NA   71.9                                              
REMARK 620 3 HEM A 500   NB   89.1  87.4                                        
REMARK 620 4 HEM A 500   NC  107.6 179.2  92.0                                  
REMARK 620 5 HEM A 500   ND   91.5  93.4 179.2  87.2                            
REMARK 620 6 CYS A 437   SG  167.0  97.2  83.3  83.2  96.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC4 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GPH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-          
REMARK 900 DECANOIC ACID                                                        
REMARK 900 RELATED ID: 3KOH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-          
REMARK 900 OCTANOIC ACID                                                        
REMARK 900 RELATED ID: 3E6I   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH INDAZOLE                   
REMARK 900 RELATED ID: 3E4E   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH 4-METHYLPYRAZOLE           
DBREF  3LC4 A   32   493  UNP    P05181   CP2E1_HUMAN     32    493             
DBREF  3LC4 B   32   493  UNP    P05181   CP2E1_HUMAN     32    493             
SEQADV 3LC4 MET A   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 ALA A   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS A   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS A   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 THR A   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 SER A   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 SER A   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS A   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 GLY A   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS A   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS A  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS A  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS A  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS A  497  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 MET B   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 ALA B   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS B   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS B   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 THR B   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 SER B   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 SER B   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS B   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 GLY B   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 LYS B   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS B  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS B  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS B  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3LC4 HIS B  497  UNP  P05181              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 PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN          
SEQRES   3 A  476  LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU          
SEQRES   4 A  476  ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY          
SEQRES   5 A  476  SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL          
SEQRES   6 A  476  LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY          
SEQRES   7 A  476  ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG          
SEQRES   8 A  476  GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE          
SEQRES   9 A  476  ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET          
SEQRES  10 A  476  GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA          
SEQRES  11 A  476  HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN          
SEQRES  12 A  476  PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS          
SEQRES  13 A  476  ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP          
SEQRES  14 A  476  TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE          
SEQRES  15 A  476  ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN          
SEQRES  16 A  476  LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO          
SEQRES  17 A  476  GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL          
SEQRES  18 A  476  LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN          
SEQRES  19 A  476  SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS          
SEQRES  20 A  476  LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU          
SEQRES  21 A  476  ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA          
SEQRES  22 A  476  ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR          
SEQRES  23 A  476  LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU          
SEQRES  24 A  476  ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE          
SEQRES  25 A  476  GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU          
SEQRES  26 A  476  MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG          
SEQRES  27 A  476  PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA          
SEQRES  28 A  476  THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS          
SEQRES  29 A  476  GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR          
SEQRES  30 A  476  ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO          
SEQRES  31 A  476  GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER          
SEQRES  32 A  476  ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS          
SEQRES  33 A  476  ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU          
SEQRES  34 A  476  LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU          
SEQRES  35 A  476  VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE          
SEQRES  36 A  476  GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL          
SEQRES  37 A  476  ILE PRO ARG SER 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 PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN          
SEQRES   3 B  476  LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU          
SEQRES   4 B  476  ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY          
SEQRES   5 B  476  SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL          
SEQRES   6 B  476  LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY          
SEQRES   7 B  476  ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG          
SEQRES   8 B  476  GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE          
SEQRES   9 B  476  ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET          
SEQRES  10 B  476  GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA          
SEQRES  11 B  476  HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN          
SEQRES  12 B  476  PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS          
SEQRES  13 B  476  ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP          
SEQRES  14 B  476  TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE          
SEQRES  15 B  476  ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN          
SEQRES  16 B  476  LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO          
SEQRES  17 B  476  GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL          
SEQRES  18 B  476  LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN          
SEQRES  19 B  476  SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS          
SEQRES  20 B  476  LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU          
SEQRES  21 B  476  ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA          
SEQRES  22 B  476  ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR          
SEQRES  23 B  476  LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU          
SEQRES  24 B  476  ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE          
SEQRES  25 B  476  GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU          
SEQRES  26 B  476  MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG          
SEQRES  27 B  476  PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA          
SEQRES  28 B  476  THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS          
SEQRES  29 B  476  GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR          
SEQRES  30 B  476  ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO          
SEQRES  31 B  476  GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER          
SEQRES  32 B  476  ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS          
SEQRES  33 B  476  ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU          
SEQRES  34 B  476  LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU          
SEQRES  35 B  476  VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE          
SEQRES  36 B  476  GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL          
SEQRES  37 B  476  ILE PRO ARG SER HIS HIS HIS HIS                              
HET    HEM  A 500      43                                                       
HET    LC4  A 501      19                                                       
HET    HEM  B 500      43                                                       
HET    LC4  B 501      19                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     LC4 12-(1H-IMIDAZOL-1-YL)DODECANOIC ACID                             
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  LC4    2(C15 H26 N2 O2)                                             
FORMUL   7  HOH   *5(H2 O)                                                      
HELIX    1   1 ASN A   44  LEU A   48  5                                   5    
HELIX    2   2 GLU A   49  LYS A   51  5                                   3    
HELIX    3   3 ASN A   52  GLY A   65  1                                  14    
HELIX    4   4 GLY A   82  ASP A   92  1                                  11    
HELIX    5   5 LEU A  103  ARG A  110  5                                   8    
HELIX    6   6 THR A  121  TYR A  136  1                                  16    
HELIX    7   7 GLY A  142  LYS A  160  1                                  19    
HELIX    8   8 PRO A  168  GLY A  173  1                                   6    
HELIX    9   9 GLY A  173  ARG A  186  1                                  14    
HELIX   10  10 ASP A  193  SER A  211  1                                  19    
HELIX   11  11 THR A  212  PHE A  221  1                                  10    
HELIX   12  12 PHE A  221  HIS A  226  1                                   6    
HELIX   13  13 SER A  231  LEU A  257  1                                  27    
HELIX   14  14 ASP A  264  LYS A  275  1                                  12    
HELIX   15  15 THR A  285  TYR A  318  1                                  34    
HELIX   16  16 TYR A  318  ILE A  333  1                                  16    
HELIX   17  17 ALA A  340  GLU A  346  5                                   7    
HELIX   18  18 MET A  347  THR A  362  1                                  16    
HELIX   19  19 LEU A  393  TYR A  398  1                                   6    
HELIX   20  20 LYS A  410  LEU A  415  5                                   6    
HELIX   21  21 THR A  432  VAL A  436  5                                   5    
HELIX   22  22 GLY A  439  HIS A  457  1                                  19    
HELIX   23  23 ASN B   44  LEU B   48  5                                   5    
HELIX   24  24 GLU B   49  LYS B   51  5                                   3    
HELIX   25  25 ASN B   52  GLY B   65  1                                  14    
HELIX   26  26 GLY B   82  TYR B   93  1                                  12    
HELIX   27  27 LYS B   94  SER B   98  5                                   5    
HELIX   28  28 LEU B  103  ARG B  110  5                                   8    
HELIX   29  29 THR B  121  TYR B  136  1                                  16    
HELIX   30  30 GLY B  142  LYS B  160  1                                  19    
HELIX   31  31 ASP B  167  ILE B  172  5                                   6    
HELIX   32  32 GLY B  173  ARG B  186  1                                  14    
HELIX   33  33 ASP B  193  SER B  211  1                                  19    
HELIX   34  34 THR B  212  PHE B  221  1                                  10    
HELIX   35  35 PHE B  221  HIS B  226  1                                   6    
HELIX   36  36 SER B  231  GLN B  255  1                                  25    
HELIX   37  37 ASP B  264  LYS B  275  1                                  12    
HELIX   38  38 THR B  285  TYR B  318  1                                  34    
HELIX   39  39 TYR B  318  GLY B  334  1                                  17    
HELIX   40  40 ALA B  340  GLU B  346  5                                   7    
HELIX   41  41 MET B  347  THR B  362  1                                  16    
HELIX   42  42 THR B  392  TYR B  398  1                                   7    
HELIX   43  43 LYS B  410  LEU B  415  5                                   6    
HELIX   44  44 GLY B  439  HIS B  457  1                                  19    
SHEET    1   A 5 VAL A  67  VAL A  72  0                                        
SHEET    2   A 5 GLN A  75  HIS A  81 -1  O  MET A  77   N  LEU A  70           
SHEET    3   A 5 VAL A 388  THR A 392  1  O  VAL A 390   N  VAL A  78           
SHEET    4   A 5 HIS A 370  GLU A 371 -1  N  HIS A 370   O  VAL A 389           
SHEET    5   A 5 GLY A  99  ARG A 100 -1  N  GLY A  99   O  GLU A 371           
SHEET    1   B 3 PRO A 165  PHE A 166  0                                        
SHEET    2   B 3 LEU A 487  PRO A 491 -1  O  LEU A 487   N  PHE A 166           
SHEET    3   B 3 PHE A 458  PRO A 462 -1  N  LYS A 461   O  CYS A 488           
SHEET    1   C 2 THR A 376  PHE A 378  0                                        
SHEET    2   C 2 TYR A 381  ILE A 383 -1  O  TYR A 381   N  PHE A 378           
SHEET    1   D 2 HIS A 475  ILE A 476  0                                        
SHEET    2   D 2 CYS A 480  ILE A 481 -1  O  ILE A 481   N  HIS A 475           
SHEET    1   E 5 VAL B  67  VAL B  72  0                                        
SHEET    2   E 5 GLN B  75  MET B  80 -1  O  MET B  77   N  LEU B  70           
SHEET    3   E 5 VAL B 388  PRO B 391  1  O  VAL B 390   N  VAL B  78           
SHEET    4   E 5 HIS B 370  GLU B 371 -1  N  HIS B 370   O  VAL B 389           
SHEET    5   E 5 GLY B  99  ARG B 100 -1  N  GLY B  99   O  GLU B 371           
SHEET    1   F 2 THR B 376  PHE B 378  0                                        
SHEET    2   F 2 TYR B 381  ILE B 383 -1  O  ILE B 383   N  THR B 376           
SHEET    1   G 2 PHE B 458  PRO B 462  0                                        
SHEET    2   G 2 LEU B 487  PRO B 491 -1  O  CYS B 488   N  LYS B 461           
SHEET    1   H 2 HIS B 475  ILE B 476  0                                        
SHEET    2   H 2 CYS B 480  ILE B 481 -1  O  ILE B 481   N  HIS B 475           
LINK         SG  CYS B 437                FE   HEM B 500     1555   1555  2.42  
LINK        FE   HEM A 500                 N15 LC4 A 501     1555   1555  2.47  
LINK         SG  CYS A 437                FE   HEM A 500     1555   1555  2.53  
LINK        FE   HEM B 500                 N15 LC4 B 501     1555   1555  2.63  
SITE     1 AC1 20 ARG A 100  ILE A 114  ILE A 115  TRP A 122                    
SITE     2 AC1 20 ARG A 126  ALA A 299  GLY A 300  THR A 303                    
SITE     3 AC1 20 THR A 307  ASN A 367  LEU A 368  HIS A 370                    
SITE     4 AC1 20 LEU A 393  PRO A 429  PHE A 430  SER A 431                    
SITE     5 AC1 20 ARG A 435  CYS A 437  GLY A 439  LC4 A 501                    
SITE     1 AC2  9 HIS A 109  ASN A 206  PHE A 207  VAL A 239                    
SITE     2 AC2  9 VAL A 242  LYS A 243  PHE A 298  THR A 303                    
SITE     3 AC2  9 HEM A 500                                                     
SITE     1 AC3 20 ARG B 100  ILE B 114  ILE B 115  TRP B 122                    
SITE     2 AC3 20 ARG B 126  ALA B 299  GLY B 300  THR B 303                    
SITE     3 AC3 20 ASN B 367  LEU B 368  HIS B 370  LEU B 393                    
SITE     4 AC3 20 PRO B 429  SER B 431  ARG B 435  CYS B 437                    
SITE     5 AC3 20 ALA B 438  GLY B 439  ALA B 443  LC4 B 501                    
SITE     1 AC4 10 HIS B 109  ASN B 206  PHE B 207  VAL B 239                    
SITE     2 AC4 10 VAL B 242  LYS B 243  PHE B 298  THR B 303                    
SITE     3 AC4 10 LEU B 368  HEM B 500                                          
CRYST1   70.779   70.779  224.629  90.00  90.00  90.00 P 43          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      0.014129  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014129  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004452        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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