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Database: PDB
Entry: 3E4E
LinkDB: 3E4E
Original site: 3E4E 
HEADER    OXIDOREDUCTASE                          11-AUG-08   3E4E              
TITLE     HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH THE INHIBITOR 4-            
TITLE    2 METHYLPYRAZOLE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2E1;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32 TO 493;                                    
COMPND   5 SYNONYM: CYPIIE1, P450-J;                                            
COMPND   6 EC: 1.14.14.1;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP2E1, CYP2E;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOPP-3;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKK2E1DH                                  
KEYWDS    CYP2E1, P450 2E1, MONOOXYGENASE, ACETAMINOPHEN,                       
KEYWDS   2 OXIDOREDUCTASE, HEME, ENDOPLASMIC RETICULUM, IRON,                   
KEYWDS   3 MEMBRANE, METAL-BINDING, MICROSOME                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.MENEELY,P.R.PORUBSKY,E.E.SCOTT                                    
REVDAT   4   09-JUN-09 3E4E    1       REVDAT                                   
REVDAT   3   24-FEB-09 3E4E    1       VERSN                                    
REVDAT   2   02-DEC-08 3E4E    1       JRNL                                     
REVDAT   1   16-SEP-08 3E4E    0                                                
JRNL        AUTH   P.R.PORUBSKY,K.M.MENEELY,E.E.SCOTT                           
JRNL        TITL   STRUCTURES OF HUMAN CYTOCHROME P450 2E1: INSIGHTS            
JRNL        TITL 2 INTO THE BINDING OF INHIBITORS AND BOTH SMALL                
JRNL        TITL 3 MOLECULAR WEIGHT AND FATTY ACID SUBSTRATES.                  
JRNL        REF    J.BIOL.CHEM.                  V. 283 33698 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18818195                                                     
JRNL        DOI    10.1074/JBC.M805999200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 32629                          
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) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1767                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2396                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 141                          
REMARK   3   BIN FREE R VALUE                    : 0.3980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7543                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 98                                      
REMARK   3   SOLVENT ATOMS            : 66                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.077         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.357         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.276         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.893        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7866 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10681 ; 2.021 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   920 ; 9.719 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;36.878 ;23.120       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1341 ;21.916 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;23.696 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1129 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6051 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3902 ; 0.255 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5317 ; 0.324 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   304 ; 0.185 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    41 ; 0.226 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.450 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4737 ; 0.843 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7543 ; 1.485 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3485 ; 2.392 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3138 ; 3.822 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3E4E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048860.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-08                          
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                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SIDE-SCATTERING CUBEROOT I-        
REMARK 200                                   BEAM BENT SINGLE CRYSTAL;          
REMARK 200                                   ASYMETRIC 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   : 32629                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 113.200                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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: CYP2E1 IN COMPLEX WITH INDAZOLE (PDB ENTRY 3E6I)     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% ISO-PROPANOL, 14% PEG 2000 MME,      
REMARK 280  0.1 M NAHEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  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      112.94400            
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      169.41600            
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       56.47200            
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 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 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     MET A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     LYS A   140                                                      
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     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    THR A 285   N   -  CA  -  CB  ANGL. DEV. =  15.8 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      -54.70     73.94                                   
REMARK 500    ASN A  52       64.88   -158.02                                   
REMARK 500    TYR A  93       55.53   -108.71                                   
REMARK 500    LEU A 103       78.92   -161.10                                   
REMARK 500    PRO A 104      -38.76    -38.49                                   
REMARK 500    LEU A 171      -61.31   -102.69                                   
REMARK 500    TYR A 191       -6.38    -52.80                                   
REMARK 500    ASN A 192       41.79   -140.47                                   
REMARK 500    ASP A 264     -165.26   -168.00                                   
REMARK 500    PRO A 335        1.87    -69.32                                   
REMARK 500    MET A 347       69.62   -119.16                                   
REMARK 500    THR A 362       60.69     38.66                                   
REMARK 500    VAL A 364       78.32   -117.56                                   
REMARK 500    ASN A 367     -174.65     59.66                                   
REMARK 500    ASP A 399      109.89    -45.38                                   
REMARK 500    ASN A 418       31.54    -86.41                                   
REMARK 500    SER A 431     -163.09     66.40                                   
REMARK 500    ILE B  41      -56.61     75.26                                   
REMARK 500    ASN B  52       63.25   -163.30                                   
REMARK 500    TYR B  93       51.82    -98.03                                   
REMARK 500    LEU B 103       80.85   -156.71                                   
REMARK 500    ILE B 114      -59.04   -123.75                                   
REMARK 500    PRO B 120      -18.37    -47.33                                   
REMARK 500    LEU B 171      -70.86   -103.94                                   
REMARK 500    GLN B 255      -15.29    -48.33                                   
REMARK 500    ASP B 264     -167.65   -175.27                                   
REMARK 500    TYR B 318       79.10   -119.48                                   
REMARK 500    MET B 347       71.17   -112.56                                   
REMARK 500    THR B 362       65.48     35.40                                   
REMARK 500    ASN B 367     -178.83     59.59                                   
REMARK 500    ARG B 379       44.78     31.35                                   
REMARK 500    SER B 431     -167.13     67.90                                   
REMARK 500    CYS B 437      117.56    -32.05                                   
REMARK 500    PRO B 466      -39.00    -34.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A  120     THR A  121                 -140.73                    
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 359         0.21    SIDE_CHAIN                              
REMARK 500    ARG B 359         0.20    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ASN A 117        21.8      L          L   OUTSIDE RANGE          
REMARK 500     THR A 169        24.7      L          L   OUTSIDE RANGE          
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 4PZ B 501   N2  175.4                                              
REMARK 620 N                    1                                               
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 4PZ A 501   N2                                                     
REMARK 620 2 CYS A 437   SG  172.7                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PZ A 501                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PZ B 501                 
DBREF  3E4E A   32   493  UNP    P05181   CP2E1_HUMAN     32    493             
DBREF  3E4E B   32   493  UNP    P05181   CP2E1_HUMAN     32    493             
SEQADV 3E4E MET A   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E ALA A   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS A   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS A   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E THR A   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E SER A   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E SER A   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS A   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E GLY A   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS A   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E HIS A  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E HIS A  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E HIS A  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E HIS A  497  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E MET B   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E ALA B   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS B   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS B   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E THR B   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E SER B   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E SER B   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS B   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E GLY B   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E LYS B   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E HIS B  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E HIS B  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E HIS B  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3E4E 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    4PZ  A 501       6                                                       
HET    HEM  B 500      43                                                       
HET    4PZ  B 501       6                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     4PZ 4-METHYL-1H-PYRAZOLE                                             
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  4PZ    2(C4 H6 N2)                                                  
FORMUL   7  HOH   *66(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  GLY A  137  1                                  17    
HELIX    7   7 GLY A  142  LYS A  160  1                                  19    
HELIX    8   8 ASP A  167  ILE A  172  5                                   6    
HELIX    9   9 GLY A  173  ARG A  186  1                                  14    
HELIX   10  10 ASP A  193  LEU A  210  1                                  18    
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 GLY A  230  GLN A  255  1                                  26    
HELIX   14  14 ASP A  264  GLU A  276  1                                  13    
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 GLY A  439  HIS A  457  1                                  19    
HELIX   22  22 ASP A  465  ILE A  469  5                                   5    
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  ASP B   92  1                                  11    
HELIX   27  27 LEU B  103  ARG B  110  5                                   8    
HELIX   28  28 THR B  121  GLY B  137  1                                  17    
HELIX   29  29 GLY B  142  LYS B  160  1                                  19    
HELIX   30  30 PRO B  168  GLY B  173  1                                   6    
HELIX   31  31 GLY B  173  ARG B  186  1                                  14    
HELIX   32  32 ASP B  193  LEU B  210  1                                  18    
HELIX   33  33 THR B  212  PHE B  221  1                                  10    
HELIX   34  34 PHE B  221  HIS B  226  1                                   6    
HELIX   35  35 SER B  231  GLN B  255  1                                  25    
HELIX   36  36 ASP B  264  GLU B  276  1                                  13    
HELIX   37  37 THR B  285  TYR B  318  1                                  34    
HELIX   38  38 TYR B  318  ILE B  333  1                                  16    
HELIX   39  39 ALA B  340  GLU B  346  5                                   7    
HELIX   40  40 MET B  347  THR B  362  1                                  16    
HELIX   41  41 LEU B  393  TYR B  398  1                                   6    
HELIX   42  42 LYS B  410  LEU B  415  5                                   6    
HELIX   43  43 GLY B  439  HIS B  457  1                                  19    
HELIX   44  44 ASP B  465  ILE B  469  5                                   5    
SHEET    1   A 5 VAL A  67  VAL A  72  0                                        
SHEET    2   A 5 GLN A  75  MET A  80 -1  O  MET A  77   N  LEU A  70           
SHEET    3   A 5 VAL A 388  PRO A 391  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 2 THR A 376  PHE A 378  0                                        
SHEET    2   B 2 TYR A 381  ILE A 383 -1  O  ILE A 383   N  THR A 376           
SHEET    1   C 2 PHE A 458  PRO A 462  0                                        
SHEET    2   C 2 LEU A 487  PRO A 491 -1  O  CYS A 488   N  LYS A 461           
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  GLN B  75   N  VAL B  72           
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  TYR B 381   N  PHE B 378           
SHEET    1   G 2 PHE B 458  PRO B 462  0                                        
SHEET    2   G 2 LEU B 487  PRO B 491 -1  O  ILE B 490   N  ASN B 459           
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  2.00  
LINK        FE   HEM B 500                 N2  4PZ B 501     1555   1555  1.72  
LINK        FE   HEM A 500                 N2  4PZ A 501     1555   1555  1.58  
LINK         SG  CYS A 437                FE   HEM A 500     1555   1555  1.67  
SITE     1 AC1 18 ARG A 100  ILE A 114  ILE A 115  TRP A 122                    
SITE     2 AC1 18 ARG A 126  ALA A 299  GLY A 300  THR A 303                    
SITE     3 AC1 18 THR A 307  ASN A 367  LEU A 368  HIS A 370                    
SITE     4 AC1 18 PRO A 429  PHE A 430  SER A 431  ARG A 435                    
SITE     5 AC1 18 CYS A 437  ALA A 438                                          
SITE     1 AC2  3 ALA A 299  THR A 303  CYS A 437                               
SITE     1 AC3 19 ARG B 100  ILE B 114  ILE B 115  TRP B 122                    
SITE     2 AC3 19 ARG B 126  ALA B 299  GLY B 300  THR B 303                    
SITE     3 AC3 19 THR B 307  ASN B 367  LEU B 368  HIS B 370                    
SITE     4 AC3 19 PRO B 429  PHE B 430  SER B 431  ARG B 435                    
SITE     5 AC3 19 CYS B 437  ALA B 438  GLY B 439                               
SITE     1 AC4  2 ALA B 299  THR B 303                                          
CRYST1   71.193   71.193  225.888  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      0.014046  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014046  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004427        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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