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Database: PDB
Entry: 4FDH
LinkDB: 4FDH
Original site: 4FDH 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 28-MAY-12   4FDH              
TITLE     STRUCTURE OF HUMAN ALDOSTERONE SYNTHASE, CYP11B2, IN COMPLEX WITH     
TITLE    2 FADROZOLE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 11B2, MITOCHONDRIAL;                       
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: ALDOSTERONE SYNTHASE, ALDOS, ALDOSTERONE-SYNTHESIZING       
COMPND   5 ENZYME, CYPXIB2, CYTOCHROME P-450ALDO, CYTOCHROME P-450C18, STEROID  
COMPND   6 18-HYDROXYLASE;                                                      
COMPND   7 EC: 1.14.15.4, 1.14.15.5;                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALDOSTERONE SYNTHASE, CYP11B2;                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCW                                       
KEYWDS    CYTOCHROME P450, CYP11B2, ALDOSTERONE SYNTHASE, MONOOXYGENASE, HEME   
KEYWDS   2 PROTEIN, MINERALOCORTICOID, INHIBITOR, MITOCHONDRIA, MEMBRANE,       
KEYWDS   3 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.STRUSHKEVICH,L.SHEN,W.TEMPEL,C.ARROWSMITH,A.EDWARDS,S.A.USANOV,H.-  
AUTHOR   2 W.PARK                                                               
REVDAT   2   13-FEB-13 4FDH    1       JRNL                                     
REVDAT   1   30-JAN-13 4FDH    0                                                
JRNL        AUTH   N.STRUSHKEVICH,A.A.GILEP,L.SHEN,C.H.ARROWSMITH,A.M.EDWARDS,  
JRNL        AUTH 2 S.A.USANOV,H.W.PARK                                          
JRNL        TITL   STRUCTURAL INSIGHTS INTO ALDOSTERONE SYNTHASE SUBSTRATE      
JRNL        TITL 2 SPECIFICITY AND TARGETED INHIBITION.                         
JRNL        REF    MOL.ENDOCRINOL.               V.  27   315 2013              
JRNL        REFN                   ISSN 0888-8809                               
JRNL        PMID   23322723                                                     
JRNL        DOI    10.1210/ME.2012-1287                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC5                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 179030                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 45228                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 720                                     
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FDH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072763.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97931                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 179030                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5434                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.24                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 0.1M TRIS, PH 8.5, 0.2M    
REMARK 280  LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       99.54300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 108260 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F, D, E                      
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19870 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 108310 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, L, H, I, J, K                      
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    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     LYS A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     ILE A   431                                                      
REMARK 465     ARG A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     SER A   434                                                      
REMARK 465     GLY A   435                                                      
REMARK 465     ARG A   436                                                      
REMARK 465     ASN A   503                                                      
REMARK 465     HIS A   504                                                      
REMARK 465     HIS A   505                                                      
REMARK 465     HIS A   506                                                      
REMARK 465     HIS A   507                                                      
REMARK 465     HIS A   508                                                      
REMARK 465     HIS A   509                                                      
REMARK 465     MET B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     THR B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     GLY B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     GLY B   435                                                      
REMARK 465     ARG B   436                                                      
REMARK 465     ASN B   503                                                      
REMARK 465     HIS B   504                                                      
REMARK 465     HIS B   505                                                      
REMARK 465     HIS B   506                                                      
REMARK 465     HIS B   507                                                      
REMARK 465     HIS B   508                                                      
REMARK 465     HIS B   509                                                      
REMARK 465     MET C    27                                                      
REMARK 465     ALA C    28                                                      
REMARK 465     LYS C    29                                                      
REMARK 465     LYS C    30                                                      
REMARK 465     THR C    31                                                      
REMARK 465     SER C    32                                                      
REMARK 465     SER C    33                                                      
REMARK 465     ILE C   431                                                      
REMARK 465     ARG C   432                                                      
REMARK 465     GLY C   433                                                      
REMARK 465     SER C   434                                                      
REMARK 465     GLY C   435                                                      
REMARK 465     ARG C   436                                                      
REMARK 465     ASN C   437                                                      
REMARK 465     ASN C   503                                                      
REMARK 465     HIS C   504                                                      
REMARK 465     HIS C   505                                                      
REMARK 465     HIS C   506                                                      
REMARK 465     HIS C   507                                                      
REMARK 465     HIS C   508                                                      
REMARK 465     HIS C   509                                                      
REMARK 465     MET D    27                                                      
REMARK 465     ALA D    28                                                      
REMARK 465     LYS D    29                                                      
REMARK 465     LYS D    30                                                      
REMARK 465     THR D    31                                                      
REMARK 465     SER D    32                                                      
REMARK 465     SER D    33                                                      
REMARK 465     ARG D   432                                                      
REMARK 465     GLY D   433                                                      
REMARK 465     SER D   434                                                      
REMARK 465     GLY D   435                                                      
REMARK 465     ASN D   503                                                      
REMARK 465     HIS D   504                                                      
REMARK 465     HIS D   505                                                      
REMARK 465     HIS D   506                                                      
REMARK 465     HIS D   507                                                      
REMARK 465     HIS D   508                                                      
REMARK 465     HIS D   509                                                      
REMARK 465     MET E    27                                                      
REMARK 465     ALA E    28                                                      
REMARK 465     LYS E    29                                                      
REMARK 465     LYS E    30                                                      
REMARK 465     THR E    31                                                      
REMARK 465     SER E    32                                                      
REMARK 465     SER E    33                                                      
REMARK 465     ILE E   431                                                      
REMARK 465     ARG E   432                                                      
REMARK 465     GLY E   433                                                      
REMARK 465     SER E   434                                                      
REMARK 465     GLY E   435                                                      
REMARK 465     ARG E   436                                                      
REMARK 465     MET F    27                                                      
REMARK 465     ALA F    28                                                      
REMARK 465     LYS F    29                                                      
REMARK 465     LYS F    30                                                      
REMARK 465     THR F    31                                                      
REMARK 465     SER F    32                                                      
REMARK 465     SER F    33                                                      
REMARK 465     ILE F   431                                                      
REMARK 465     ARG F   432                                                      
REMARK 465     GLY F   433                                                      
REMARK 465     SER F   434                                                      
REMARK 465     GLY F   435                                                      
REMARK 465     ARG F   436                                                      
REMARK 465     ASN F   437                                                      
REMARK 465     MET G    27                                                      
REMARK 465     ALA G    28                                                      
REMARK 465     LYS G    29                                                      
REMARK 465     LYS G    30                                                      
REMARK 465     THR G    31                                                      
REMARK 465     SER G    32                                                      
REMARK 465     SER G    33                                                      
REMARK 465     ILE G   431                                                      
REMARK 465     ARG G   432                                                      
REMARK 465     GLY G   433                                                      
REMARK 465     SER G   434                                                      
REMARK 465     GLY G   435                                                      
REMARK 465     ARG G   436                                                      
REMARK 465     ASN G   503                                                      
REMARK 465     HIS G   504                                                      
REMARK 465     HIS G   505                                                      
REMARK 465     HIS G   506                                                      
REMARK 465     HIS G   507                                                      
REMARK 465     HIS G   508                                                      
REMARK 465     HIS G   509                                                      
REMARK 465     MET H    27                                                      
REMARK 465     ALA H    28                                                      
REMARK 465     LYS H    29                                                      
REMARK 465     LYS H    30                                                      
REMARK 465     THR H    31                                                      
REMARK 465     SER H    32                                                      
REMARK 465     SER H    33                                                      
REMARK 465     ILE H   431                                                      
REMARK 465     ARG H   432                                                      
REMARK 465     GLY H   433                                                      
REMARK 465     SER H   434                                                      
REMARK 465     GLY H   435                                                      
REMARK 465     ARG H   436                                                      
REMARK 465     ASN H   437                                                      
REMARK 465     ASN H   503                                                      
REMARK 465     HIS H   504                                                      
REMARK 465     HIS H   505                                                      
REMARK 465     HIS H   506                                                      
REMARK 465     HIS H   507                                                      
REMARK 465     HIS H   508                                                      
REMARK 465     HIS H   509                                                      
REMARK 465     MET I    27                                                      
REMARK 465     ALA I    28                                                      
REMARK 465     LYS I    29                                                      
REMARK 465     LYS I    30                                                      
REMARK 465     THR I    31                                                      
REMARK 465     SER I    32                                                      
REMARK 465     SER I    33                                                      
REMARK 465     ILE I   431                                                      
REMARK 465     ARG I   432                                                      
REMARK 465     GLY I   433                                                      
REMARK 465     SER I   434                                                      
REMARK 465     GLY I   435                                                      
REMARK 465     ARG I   436                                                      
REMARK 465     ASN I   437                                                      
REMARK 465     ASN I   503                                                      
REMARK 465     HIS I   504                                                      
REMARK 465     HIS I   505                                                      
REMARK 465     HIS I   506                                                      
REMARK 465     HIS I   507                                                      
REMARK 465     HIS I   508                                                      
REMARK 465     HIS I   509                                                      
REMARK 465     MET J    27                                                      
REMARK 465     ALA J    28                                                      
REMARK 465     LYS J    29                                                      
REMARK 465     LYS J    30                                                      
REMARK 465     THR J    31                                                      
REMARK 465     SER J    32                                                      
REMARK 465     SER J    33                                                      
REMARK 465     ILE J   431                                                      
REMARK 465     ARG J   432                                                      
REMARK 465     GLY J   433                                                      
REMARK 465     SER J   434                                                      
REMARK 465     GLY J   435                                                      
REMARK 465     ARG J   436                                                      
REMARK 465     ASN J   437                                                      
REMARK 465     ASN J   503                                                      
REMARK 465     HIS J   504                                                      
REMARK 465     HIS J   505                                                      
REMARK 465     HIS J   506                                                      
REMARK 465     HIS J   507                                                      
REMARK 465     HIS J   508                                                      
REMARK 465     HIS J   509                                                      
REMARK 465     MET K    27                                                      
REMARK 465     ALA K    28                                                      
REMARK 465     LYS K    29                                                      
REMARK 465     LYS K    30                                                      
REMARK 465     THR K    31                                                      
REMARK 465     SER K    32                                                      
REMARK 465     SER K    33                                                      
REMARK 465     ASN K   503                                                      
REMARK 465     HIS K   504                                                      
REMARK 465     HIS K   505                                                      
REMARK 465     HIS K   506                                                      
REMARK 465     HIS K   507                                                      
REMARK 465     HIS K   508                                                      
REMARK 465     HIS K   509                                                      
REMARK 465     MET L    27                                                      
REMARK 465     ALA L    28                                                      
REMARK 465     LYS L    29                                                      
REMARK 465     LYS L    30                                                      
REMARK 465     THR L    31                                                      
REMARK 465     SER L    32                                                      
REMARK 465     SER L    33                                                      
REMARK 465     THR L    34                                                      
REMARK 465     VAL L    35                                                      
REMARK 465     ASN L    82                                                      
REMARK 465     LEU L    83                                                      
REMARK 465     GLY L    84                                                      
REMARK 465     GLY L    85                                                      
REMARK 465     ILE L   431                                                      
REMARK 465     ARG L   432                                                      
REMARK 465     GLY L   433                                                      
REMARK 465     SER L   434                                                      
REMARK 465     GLY L   435                                                      
REMARK 465     ARG L   436                                                      
REMARK 465     ASN L   437                                                      
REMARK 465     ASN L   503                                                      
REMARK 465     HIS L   504                                                      
REMARK 465     HIS L   505                                                      
REMARK 465     HIS L   506                                                      
REMARK 465     HIS L   507                                                      
REMARK 465     HIS L   508                                                      
REMARK 465     HIS L   509                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS H 270   CB    CYS H 270   SG     -0.102                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 H  77   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO I  77   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    PRO J  77   C   -  N   -  CA  ANGL. DEV. =  13.7 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    TYR A  61       47.91   -157.08                                   
REMARK 500    MET A  92       11.13   -151.90                                   
REMARK 500    SER A 105     -161.64    -62.30                                   
REMARK 500    ALA A 180      -38.87    -37.84                                   
REMARK 500    LEU A 202      -72.05    -62.39                                   
REMARK 500    VAL A 316      -74.87   -103.81                                   
REMARK 500    ASN A 333       75.11   -117.91                                   
REMARK 500    ARG A 419       63.53     65.48                                   
REMARK 500    THR A 477       86.45    -51.39                                   
REMARK 500    SER A 486       56.43   -140.03                                   
REMARK 500    PHE A 487      -47.13     74.69                                   
REMARK 500    VAL B  35       73.12   -118.21                                   
REMARK 500    ARG B  48      -53.93    -28.88                                   
REMARK 500    TYR B  61       45.28   -155.55                                   
REMARK 500    GLU B  67      -70.00    -57.27                                   
REMARK 500    PRO B  77        0.83    -61.61                                   
REMARK 500    ASN B  82       87.64    -66.89                                   
REMARK 500    MET B  92       10.59   -167.86                                   
REMARK 500    SER B 105     -144.34    -78.66                                   
REMARK 500    SER B 243      -47.43    -25.42                                   
REMARK 500    SER B 249       49.08   -144.97                                   
REMARK 500    ASN B 281      108.88   -161.53                                   
REMARK 500    ALA B 297       33.73     33.55                                   
REMARK 500    VAL B 316      -82.54   -104.21                                   
REMARK 500    ASN B 413      106.26    -52.29                                   
REMARK 500    ARG B 427      -31.14    -32.84                                   
REMARK 500    ILE B 431      100.01    -58.62                                   
REMARK 500    PHE B 438       24.92    -77.48                                   
REMARK 500    VAL B 441       34.53   -142.23                                   
REMARK 500    CYS B 450      111.65    -30.64                                   
REMARK 500    PHE B 487      -61.62     72.70                                   
REMARK 500    TYR C  61       52.62   -160.22                                   
REMARK 500    SER C 105     -134.16    -80.50                                   
REMARK 500    THR C 287       32.86   -142.44                                   
REMARK 500    TYR C 376       59.51   -116.59                                   
REMARK 500    ASN C 413       90.92    -66.91                                   
REMARK 500    ARG C 427      -32.24    -25.11                                   
REMARK 500    VAL C 441       30.27   -145.08                                   
REMARK 500    CYS C 450      122.68    -15.74                                   
REMARK 500    ASP C 480      146.75    -35.83                                   
REMARK 500    PHE C 487      -48.13     66.26                                   
REMARK 500    TYR D  61       51.90   -143.96                                   
REMARK 500    SER D 105     -151.40    -77.88                                   
REMARK 500    HIS D 214     -156.07   -146.47                                   
REMARK 500    THR D 287       29.37   -140.22                                   
REMARK 500    ALA D 297       16.57     55.68                                   
REMARK 500    VAL D 316      -72.49   -117.27                                   
REMARK 500    ASN D 413       93.36    -63.64                                   
REMARK 500    ARG D 419       68.18     62.84                                   
REMARK 500    ARG D 427      -32.78    -21.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     206 RAMACHANDRAN OUTLIERS.                        
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 ALA G  501     ILE G  502                  147.94                    
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
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: (10X,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    PHE C 157        24.2      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 211        24.8      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 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 450   SG                                                     
REMARK 620 2 HEM B 601   NA   98.3                                              
REMARK 620 3 HEM B 601   NB   89.5  92.4                                        
REMARK 620 4 HEM B 601   NC   82.5 178.5  86.4                                  
REMARK 620 5 HEM B 601   ND   91.5  86.8 178.8  94.4                            
REMARK 620 6 0T3 B 602   N06 166.1  95.1  93.4  84.1  85.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 450   SG                                                     
REMARK 620 2 HEM A 601   NA  100.5                                              
REMARK 620 3 HEM A 601   NB   90.7  87.8                                        
REMARK 620 4 HEM A 601   NC   79.4 179.4  91.7                                  
REMARK 620 5 HEM A 601   ND   90.5  91.4 178.7  89.2                            
REMARK 620 6 0T3 A 602   N06 164.1  94.8  94.4  85.4  84.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 450   SG                                                     
REMARK 620 2 HEM D 601   NA   97.8                                              
REMARK 620 3 HEM D 601   NB   88.7  89.3                                        
REMARK 620 4 HEM D 601   NC   81.3 177.5  88.3                                  
REMARK 620 5 HEM D 601   ND   91.6  89.2 178.5  93.2                            
REMARK 620 6 0T3 D 602   N06 165.8  96.3  93.0  84.7  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 450   SG                                                     
REMARK 620 2 HEM C 601   NA   97.6                                              
REMARK 620 3 HEM C 601   NB   90.7  91.9                                        
REMARK 620 4 HEM C 601   NC   82.1 179.7  88.0                                  
REMARK 620 5 HEM C 601   ND   90.0  88.1 179.2  91.9                            
REMARK 620 6 0T3 C 602   N06 163.3  99.0  90.7  81.3  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM H 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H 450   SG                                                     
REMARK 620 2 HEM H 601   NA   93.9                                              
REMARK 620 3 HEM H 601   NB   88.4  88.1                                        
REMARK 620 4 HEM H 601   NC   86.0 177.9  89.8                                  
REMARK 620 5 HEM H 601   ND   91.5  90.5 178.5  91.6                            
REMARK 620 6 0T3 H 602   N06 173.0  92.4  94.9  87.9  85.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 450   SG                                                     
REMARK 620 2 HEM F 601   NA   95.9                                              
REMARK 620 3 HEM F 601   NB   85.3  94.5                                        
REMARK 620 4 HEM F 601   NC   85.8 177.8  84.3                                  
REMARK 620 5 HEM F 601   ND   95.2  85.7 179.5  95.6                            
REMARK 620 6 0T3 F 602   N06 170.2  93.3  97.5  85.1  81.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 450   SG                                                     
REMARK 620 2 HEM E 601   NA   99.6                                              
REMARK 620 3 HEM E 601   NB   83.7  93.3                                        
REMARK 620 4 HEM E 601   NC   82.1 177.4  84.8                                  
REMARK 620 5 HEM E 601   ND   99.1  85.3 177.1  96.5                            
REMARK 620 6 0T3 E 602   N06 168.9  90.9  92.0  87.3  85.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM I 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS I 450   SG                                                     
REMARK 620 2 HEM I 601   NA   99.0                                              
REMARK 620 3 HEM I 601   NB   91.4  93.5                                        
REMARK 620 4 HEM I 601   NC   82.3 178.6  87.0                                  
REMARK 620 5 HEM I 601   ND   89.8  88.3 177.7  91.3                            
REMARK 620 6 0T3 I 602   N06 165.4  94.1  94.0  84.5  84.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 450   SG                                                     
REMARK 620 2 HEM G 601   NA  101.8                                              
REMARK 620 3 HEM G 601   NB   92.0  89.1                                        
REMARK 620 4 HEM G 601   NC   78.5 177.9  88.7                                  
REMARK 620 5 HEM G 601   ND   87.2  90.5 179.1  91.6                            
REMARK 620 6 0T3 G 602   N06 158.6  98.3  95.4  81.7  85.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM L 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L 450   SG                                                     
REMARK 620 2 HEM L 601   NA  102.3                                              
REMARK 620 3 HEM L 601   NB   86.5  90.5                                        
REMARK 620 4 HEM L 601   NC   78.4 178.9  90.4                                  
REMARK 620 5 HEM L 601   ND   94.3  90.3 178.8  88.9                            
REMARK 620 6 0T3 L 602   N06 156.9 100.6  95.9  78.6  83.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 450   SG                                                     
REMARK 620 2 HEM K 601   NA   99.7                                              
REMARK 620 3 HEM K 601   NB   81.1  91.9                                        
REMARK 620 4 HEM K 601   NC   79.6 179.2  87.6                                  
REMARK 620 5 HEM K 601   ND   98.2  89.8 178.3  90.7                            
REMARK 620 6 0T3 K 602   N06 163.2  96.4  93.7  84.3  86.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM J 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 450   SG                                                     
REMARK 620 2 HEM J 601   NA  101.7                                              
REMARK 620 3 HEM J 601   NB   88.4  92.5                                        
REMARK 620 4 HEM J 601   NC   78.1 178.1  85.6                                  
REMARK 620 5 HEM J 601   ND   91.4  88.3 179.2  93.6                            
REMARK 620 6 0T3 J 602   N06 161.1  94.9  99.8  85.6  80.1                      
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 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 G 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM H 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 H 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 I 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM J 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 J 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 K 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM L 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T3 L 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DVQ   RELATED DB: PDB                                   
DBREF  4FDH A   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH B   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH C   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH D   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH E   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH F   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH G   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH H   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH I   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH J   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH K   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4FDH L   34   503  UNP    P19099   C11B2_HUMAN     34    503             
SEQADV 4FDH MET A   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA A   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS A   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS A   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR A   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER A   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER A   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS A  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS A  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS A  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS A  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS A  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS A  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET B   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA B   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS B   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS B   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR B   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER B   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER B   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS B  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS B  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS B  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS B  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS B  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS B  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET C   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA C   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS C   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS C   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR C   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER C   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER C   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS C  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS C  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS C  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS C  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS C  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS C  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET D   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA D   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS D   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS D   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR D   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER D   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER D   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS D  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS D  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS D  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS D  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS D  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS D  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET E   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA E   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS E   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS E   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR E   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER E   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER E   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS E  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS E  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS E  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS E  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS E  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS E  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET F   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA F   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS F   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS F   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR F   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER F   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER F   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS F  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS F  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS F  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS F  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS F  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS F  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET G   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA G   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS G   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS G   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR G   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER G   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER G   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS G  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS G  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS G  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS G  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS G  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS G  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET H   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA H   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS H   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS H   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR H   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER H   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER H   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS H  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS H  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS H  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS H  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS H  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS H  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET I   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA I   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS I   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS I   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR I   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER I   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER I   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS I  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS I  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS I  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS I  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS I  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS I  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET J   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA J   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS J   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS J   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR J   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER J   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER J   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS J  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS J  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS J  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS J  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS J  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS J  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET K   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA K   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS K   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS K   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR K   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER K   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER K   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS K  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS K  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS K  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS K  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS K  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS K  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH MET L   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH ALA L   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS L   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH LYS L   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH THR L   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER L   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH SER L   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS L  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS L  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS L  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS L  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS L  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4FDH HIS L  509  UNP  P19099              EXPRESSION TAG                 
SEQRES   1 A  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 A  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 A  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 A  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 A  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 A  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 A  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 A  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 A  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 A  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 A  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 A  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 A  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 A  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 A  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 A  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 A  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 A  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 A  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 A  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 A  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 A  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 A  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 A  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 A  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 A  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 A  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 A  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 A  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 A  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 A  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 A  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 A  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 A  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 A  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 A  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 A  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 A  483  HIS HIS                                                      
SEQRES   1 B  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 B  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 B  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 B  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 B  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 B  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 B  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 B  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 B  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 B  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 B  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 B  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 B  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 B  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 B  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 B  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 B  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 B  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 B  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 B  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 B  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 B  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 B  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 B  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 B  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 B  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 B  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 B  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 B  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 B  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 B  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 B  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 B  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 B  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 B  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 B  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 B  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 B  483  HIS HIS                                                      
SEQRES   1 C  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 C  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 C  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 C  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 C  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 C  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 C  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 C  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 C  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 C  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 C  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 C  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 C  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 C  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 C  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 C  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 C  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 C  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 C  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 C  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 C  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 C  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 C  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 C  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 C  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 C  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 C  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 C  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 C  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 C  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 C  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 C  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 C  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 C  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 C  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 C  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 C  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 C  483  HIS HIS                                                      
SEQRES   1 D  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 D  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 D  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 D  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 D  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 D  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 D  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 D  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 D  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 D  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 D  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 D  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 D  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 D  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 D  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 D  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 D  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 D  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 D  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 D  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 D  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 D  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 D  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 D  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 D  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 D  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 D  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 D  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 D  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 D  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 D  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 D  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 D  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 D  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 D  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 D  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 D  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 D  483  HIS HIS                                                      
SEQRES   1 E  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 E  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 E  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 E  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 E  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 E  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 E  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 E  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 E  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 E  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 E  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 E  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 E  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 E  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 E  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 E  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 E  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 E  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 E  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 E  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 E  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 E  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 E  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 E  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 E  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 E  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 E  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 E  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 E  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 E  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 E  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 E  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 E  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 E  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 E  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 E  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 E  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 E  483  HIS HIS                                                      
SEQRES   1 F  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 F  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 F  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 F  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 F  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 F  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 F  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 F  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 F  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 F  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 F  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 F  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 F  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 F  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 F  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 F  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 F  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 F  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 F  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 F  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 F  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 F  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 F  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 F  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 F  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 F  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 F  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 F  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 F  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 F  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 F  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 F  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 F  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 F  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 F  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 F  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 F  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 F  483  HIS HIS                                                      
SEQRES   1 G  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 G  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 G  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 G  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 G  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 G  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 G  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 G  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 G  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 G  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 G  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 G  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 G  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 G  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 G  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 G  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 G  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 G  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 G  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 G  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 G  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 G  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 G  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 G  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 G  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 G  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 G  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 G  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 G  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 G  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 G  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 G  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 G  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 G  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 G  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 G  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 G  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 G  483  HIS HIS                                                      
SEQRES   1 H  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 H  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 H  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 H  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 H  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 H  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 H  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 H  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 H  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 H  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 H  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 H  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 H  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 H  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 H  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 H  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 H  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 H  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 H  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 H  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 H  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 H  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 H  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 H  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 H  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 H  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 H  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 H  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 H  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 H  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 H  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 H  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 H  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 H  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 H  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 H  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 H  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 H  483  HIS HIS                                                      
SEQRES   1 I  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 I  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 I  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 I  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 I  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 I  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 I  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 I  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 I  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 I  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 I  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 I  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 I  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 I  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 I  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 I  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 I  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 I  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 I  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 I  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 I  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 I  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 I  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 I  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 I  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 I  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 I  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 I  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 I  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 I  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 I  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 I  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 I  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 I  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 I  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 I  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 I  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 I  483  HIS HIS                                                      
SEQRES   1 J  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 J  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 J  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 J  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 J  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 J  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 J  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 J  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 J  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 J  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 J  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 J  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 J  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 J  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 J  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 J  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 J  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 J  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 J  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 J  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 J  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 J  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 J  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 J  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 J  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 J  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 J  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 J  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 J  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 J  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 J  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 J  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 J  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 J  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 J  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 J  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 J  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 J  483  HIS HIS                                                      
SEQRES   1 K  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 K  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 K  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 K  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 K  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 K  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 K  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 K  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 K  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 K  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 K  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 K  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 K  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 K  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 K  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 K  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 K  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 K  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 K  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 K  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 K  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 K  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 K  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 K  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 K  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 K  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 K  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 K  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 K  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 K  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 K  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 K  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 K  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 K  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 K  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 K  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 K  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 K  483  HIS HIS                                                      
SEQRES   1 L  483  MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU          
SEQRES   2 L  483  ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU          
SEQRES   3 L  483  LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS          
SEQRES   4 L  483  LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE          
SEQRES   5 L  483  PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL          
SEQRES   6 L  483  MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP          
SEQRES   7 L  483  SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL          
SEQRES   8 L  483  ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE          
SEQRES   9 L  483  LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG          
SEQRES  10 L  483  LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG          
SEQRES  11 L  483  PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER          
SEQRES  12 L  483  GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY          
SEQRES  13 L  483  SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR          
SEQRES  14 L  483  THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG          
SEQRES  15 L  483  LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU          
SEQRES  16 L  483  ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR          
SEQRES  17 L  483  VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP          
SEQRES  18 L  483  ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP          
SEQRES  19 L  483  ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS          
SEQRES  20 L  483  ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR          
SEQRES  21 L  483  THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU          
SEQRES  22 L  483  SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR          
SEQRES  23 L  483  ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET          
SEQRES  24 L  483  THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN          
SEQRES  25 L  483  ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE          
SEQRES  26 L  483  SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU          
SEQRES  27 L  483  LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO          
SEQRES  28 L  483  VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU          
SEQRES  29 L  483  VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL          
SEQRES  30 L  483  GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU          
SEQRES  31 L  483  PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU          
SEQRES  32 L  483  ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO          
SEQRES  33 L  483  PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU          
SEQRES  34 L  483  ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU          
SEQRES  35 L  483  LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE          
SEQRES  36 L  483  LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER          
SEQRES  37 L  483  PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS          
SEQRES  38 L  483  HIS HIS                                                      
HET    HEM  A 601      43                                                       
HET    0T3  A 602      17                                                       
HET    HEM  B 601      43                                                       
HET    0T3  B 602      17                                                       
HET    HEM  C 601      43                                                       
HET    0T3  C 602      17                                                       
HET    HEM  D 601      43                                                       
HET    0T3  D 602      17                                                       
HET    HEM  E 601      43                                                       
HET    0T3  E 602      17                                                       
HET    HEM  F 601      43                                                       
HET    0T3  F 602      17                                                       
HET    HEM  G 601      43                                                       
HET    0T3  G 602      17                                                       
HET    HEM  H 601      43                                                       
HET    0T3  H 602      17                                                       
HET    HEM  I 601      43                                                       
HET    0T3  I 602      17                                                       
HET    HEM  J 601      43                                                       
HET    0T3  J 602      17                                                       
HET    HEM  K 601      43                                                       
HET    0T3  K 602      17                                                       
HET    HEM  L 601      43                                                       
HET    0T3  L 602      17                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     0T3 4-[(5R)-5,6,7,8-TETRAHYDROIMIDAZO[1,5-A]PYRIDIN-5-               
HETNAM   2 0T3  YL]BENZONITRILE                                                 
HETSYN     HEM HEME                                                             
HETSYN     0T3 FADROZOLE                                                        
FORMUL  13  HEM    12(C34 H32 FE N4 O4)                                         
FORMUL  14  0T3    12(C14 H13 N3)                                               
FORMUL  37  HOH   *127(H2 O)                                                    
HELIX    1   1 PRO A   37  MET A   41  5                                   5    
HELIX    2   2 ASN A   47  GLN A   59  1                                  13    
HELIX    3   3 HIS A   63  GLY A   76  1                                  14    
HELIX    4   4 LEU A   93  VAL A  103  1                                  11    
HELIX    5   5 LEU A  113  ARG A  123  1                                  11    
HELIX    6   6 GLY A  128  LEU A  132  5                                   5    
HELIX    7   7 ASN A  133  ARG A  143  1                                  11    
HELIX    8   8 LEU A  144  LEU A  149  1                                   6    
HELIX    9   9 SER A  150  LEU A  177  1                                  28    
HELIX   10  10 VAL A  188  GLY A  206  1                                  19    
HELIX   11  11 SER A  217  PHE A  239  1                                  23    
HELIX   12  12 PRO A  241  SER A  249  1                                   9    
HELIX   13  13 SER A  249  ASN A  281  1                                  33    
HELIX   14  14 GLY A  288  ALA A  297  1                                  10    
HELIX   15  15 SER A  300  SER A  315  1                                  16    
HELIX   16  16 VAL A  316  ASN A  333  1                                  18    
HELIX   17  17 ASN A  333  ALA A  347  1                                  15    
HELIX   18  18 ALA A  347  HIS A  354  1                                   8    
HELIX   19  19 LYS A  357  LEU A  362  1                                   6    
HELIX   20  20 LEU A  362  TYR A  376  1                                  15    
HELIX   21  21 LEU A  407  ARG A  412  1                                   6    
HELIX   22  22 ASN A  424  LEU A  429  5                                   6    
HELIX   23  23 PHE A  445  GLN A  449  5                                   5    
HELIX   24  24 GLY A  452  LYS A  469  1                                  18    
HELIX   25  25 PRO B   37  MET B   41  5                                   5    
HELIX   26  26 ASN B   47  GLN B   59  1                                  13    
HELIX   27  27 HIS B   63  GLY B   76  1                                  14    
HELIX   28  28 LEU B   93  VAL B  103  1                                  11    
HELIX   29  29 LEU B  113  GLY B  124  1                                  12    
HELIX   30  30 GLY B  128  LEU B  132  5                                   5    
HELIX   31  31 ASN B  133  ARG B  143  1                                  11    
HELIX   32  32 LEU B  144  LEU B  149  1                                   6    
HELIX   33  33 SER B  150  LEU B  177  1                                  28    
HELIX   34  34 VAL B  188  GLY B  206  1                                  19    
HELIX   35  35 SER B  217  MET B  238  1                                  22    
HELIX   36  36 PRO B  241  SER B  249  1                                   9    
HELIX   37  37 SER B  249  ASN B  281  1                                  33    
HELIX   38  38 GLY B  288  ALA B  297  1                                  10    
HELIX   39  39 SER B  300  SER B  315  1                                  16    
HELIX   40  40 VAL B  316  ASN B  333  1                                  18    
HELIX   41  41 ASN B  333  HIS B  354  1                                  22    
HELIX   42  42 LYS B  357  LEU B  362  1                                   6    
HELIX   43  43 LEU B  362  TYR B  376  1                                  15    
HELIX   44  44 LEU B  407  ARG B  412  1                                   6    
HELIX   45  45 GLN B  426  ILE B  431  1                                   6    
HELIX   46  46 GLY B  452  LYS B  469  1                                  18    
HELIX   47  47 PRO C   37  MET C   41  5                                   5    
HELIX   48  48 ASN C   47  GLN C   59  1                                  13    
HELIX   49  49 HIS C   63  GLY C   76  1                                  14    
HELIX   50  50 LEU C   93  GLN C  102  1                                  10    
HELIX   51  51 LEU C  113  GLY C  124  1                                  12    
HELIX   52  52 GLY C  134  LEU C  149  1                                  16    
HELIX   53  53 SER C  150  LEU C  177  1                                  28    
HELIX   54  54 VAL C  188  GLY C  206  1                                  19    
HELIX   55  55 SER C  217  PHE C  239  1                                  23    
HELIX   56  56 PRO C  241  SER C  249  1                                   9    
HELIX   57  57 SER C  249  LEU C  278  1                                  30    
HELIX   58  58 GLY C  288  ALA C  297  1                                  10    
HELIX   59  59 SER C  300  SER C  315  1                                  16    
HELIX   60  60 VAL C  316  ARG C  332  1                                  17    
HELIX   61  61 ASN C  333  ALA C  347  1                                  15    
HELIX   62  62 ALA C  347  HIS C  354  1                                   8    
HELIX   63  63 LYS C  357  LEU C  362  1                                   6    
HELIX   64  64 LEU C  362  TYR C  376  1                                  15    
HELIX   65  65 LEU C  407  GLY C  411  1                                   5    
HELIX   66  66 ASN C  424  LEU C  429  5                                   6    
HELIX   67  67 PHE C  445  GLN C  449  5                                   5    
HELIX   68  68 GLY C  452  HIS C  470  1                                  19    
HELIX   69  69 PRO D   37  MET D   41  5                                   5    
HELIX   70  70 ASN D   47  GLN D   59  1                                  13    
HELIX   71  71 HIS D   63  GLY D   76  1                                  14    
HELIX   72  72 LEU D   93  VAL D  103  1                                  11    
HELIX   73  73 LEU D  113  GLY D  124  1                                  12    
HELIX   74  74 GLY D  134  ARG D  143  1                                  10    
HELIX   75  75 LEU D  144  LEU D  149  1                                   6    
HELIX   76  76 SER D  150  LEU D  177  1                                  28    
HELIX   77  77 VAL D  188  GLY D  206  1                                  19    
HELIX   78  78 SER D  217  PHE D  239  1                                  23    
HELIX   79  79 PRO D  241  SER D  249  1                                   9    
HELIX   80  80 SER D  249  ASN D  281  1                                  33    
HELIX   81  81 GLY D  288  ALA D  297  1                                  10    
HELIX   82  82 SER D  300  GLY D  314  1                                  15    
HELIX   83  83 VAL D  316  ASN D  333  1                                  18    
HELIX   84  84 ASN D  333  HIS D  354  1                                  22    
HELIX   85  85 LYS D  357  LEU D  362  1                                   6    
HELIX   86  86 LEU D  362  TYR D  376  1                                  15    
HELIX   87  87 LEU D  407  ASN D  413  1                                   7    
HELIX   88  88 ASN D  424  LEU D  429  5                                   6    
HELIX   89  89 ARG D  436  HIS D  440  5                                   5    
HELIX   90  90 PHE D  445  GLN D  449  5                                   5    
HELIX   91  91 GLY D  452  HIS D  470  1                                  19    
HELIX   92  92 PRO E   37  MET E   41  5                                   5    
HELIX   93  93 ASN E   47  GLN E   59  1                                  13    
HELIX   94  94 HIS E   63  GLY E   76  1                                  14    
HELIX   95  95 LEU E   93  VAL E  103  1                                  11    
HELIX   96  96 LEU E  113  GLY E  124  1                                  12    
HELIX   97  97 ASN E  133  LEU E  149  1                                  17    
HELIX   98  98 SER E  150  LEU E  177  1                                  28    
HELIX   99  99 VAL E  188  GLY E  206  1                                  19    
HELIX  100 100 SER E  217  PHE E  239  1                                  23    
HELIX  101 101 PRO E  241  SER E  249  1                                   9    
HELIX  102 102 SER E  249  ASN E  281  1                                  33    
HELIX  103 103 GLY E  288  LYS E  296  1                                   9    
HELIX  104 104 SER E  300  SER E  315  1                                  16    
HELIX  105 105 VAL E  316  ARG E  332  1                                  17    
HELIX  106 106 ASN E  333  HIS E  354  1                                  22    
HELIX  107 107 LYS E  357  LEU E  362  1                                   6    
HELIX  108 108 LEU E  362  TYR E  376  1                                  15    
HELIX  109 109 LEU E  407  ARG E  412  1                                   6    
HELIX  110 110 ASN E  424  LEU E  429  5                                   6    
HELIX  111 111 PHE E  445  GLN E  449  5                                   5    
HELIX  112 112 GLY E  452  HIS E  470  1                                  19    
HELIX  113 113 PRO F   37  MET F   41  5                                   5    
HELIX  114 114 ASN F   47  GLN F   59  1                                  13    
HELIX  115 115 HIS F   63  LEU F   75  1                                  13    
HELIX  116 116 LEU F   93  VAL F  103  1                                  11    
HELIX  117 117 LEU F  113  ARG F  123  1                                  11    
HELIX  118 118 ASN F  133  LEU F  149  1                                  17    
HELIX  119 119 SER F  150  GLN F  178  1                                  29    
HELIX  120 120 VAL F  188  GLY F  206  1                                  19    
HELIX  121 121 SER F  217  MET F  238  1                                  22    
HELIX  122 122 PRO F  241  SER F  249  1                                   9    
HELIX  123 123 SER F  249  ASN F  281  1                                  33    
HELIX  124 124 GLY F  288  ALA F  297  1                                  10    
HELIX  125 125 SER F  300  SER F  315  1                                  16    
HELIX  126 126 VAL F  316  ASN F  333  1                                  18    
HELIX  127 127 ASN F  333  ALA F  347  1                                  15    
HELIX  128 128 ALA F  347  HIS F  354  1                                   8    
HELIX  129 129 LYS F  357  LEU F  362  1                                   6    
HELIX  130 130 LEU F  362  TYR F  376  1                                  15    
HELIX  131 131 LEU F  407  GLY F  411  1                                   5    
HELIX  132 132 ASN F  424  ASP F  430  5                                   7    
HELIX  133 133 PHE F  445  GLN F  449  5                                   5    
HELIX  134 134 GLY F  452  HIS F  470  1                                  19    
HELIX  135 135 PRO G   37  MET G   41  5                                   5    
HELIX  136 136 TRP G   49  GLN G   59  1                                  11    
HELIX  137 137 HIS G   63  GLY G   76  1                                  14    
HELIX  138 138 LEU G   93  GLN G  102  1                                  10    
HELIX  139 139 LEU G  113  HIS G  122  1                                  10    
HELIX  140 140 ASN G  133  LEU G  149  1                                  17    
HELIX  141 141 SER G  150  GLN G  178  1                                  29    
HELIX  142 142 VAL G  188  GLY G  206  1                                  19    
HELIX  143 143 SER G  217  PHE G  239  1                                  23    
HELIX  144 144 PRO G  241  SER G  249  1                                   9    
HELIX  145 145 SER G  249  ASN G  281  1                                  33    
HELIX  146 146 GLY G  288  LEU G  295  1                                   8    
HELIX  147 147 SER G  300  SER G  315  1                                  16    
HELIX  148 148 VAL G  316  ASN G  333  1                                  18    
HELIX  149 149 ASN G  333  HIS G  354  1                                  22    
HELIX  150 150 PRO G  355  THR G  360  5                                   6    
HELIX  151 151 LEU G  362  TYR G  376  1                                  15    
HELIX  152 152 LEU G  407  ASN G  413  1                                   7    
HELIX  153 153 ASN G  424  LEU G  429  5                                   6    
HELIX  154 154 PHE G  445  GLN G  449  5                                   5    
HELIX  155 155 GLY G  452  LYS G  469  1                                  18    
HELIX  156 156 TRP H   49  GLN H   59  1                                  11    
HELIX  157 157 HIS H   63  GLY H   76  1                                  14    
HELIX  158 158 LEU H   93  VAL H  103  1                                  11    
HELIX  159 159 LEU H  113  ARG H  123  1                                  11    
HELIX  160 160 GLY H  134  LEU H  149  1                                  16    
HELIX  161 161 SER H  150  LEU H  177  1                                  28    
HELIX  162 162 VAL H  188  GLY H  206  1                                  19    
HELIX  163 163 SER H  217  PHE H  239  1                                  23    
HELIX  164 164 PRO H  241  SER H  249  1                                   9    
HELIX  165 165 SER H  249  ASN H  281  1                                  33    
HELIX  166 166 GLY H  288  ALA H  297  1                                  10    
HELIX  167 167 SER H  300  SER H  315  1                                  16    
HELIX  168 168 VAL H  316  ASN H  333  1                                  18    
HELIX  169 169 ASN H  333  ALA H  347  1                                  15    
HELIX  170 170 ALA H  347  SER H  352  1                                   6    
HELIX  171 171 HIS H  354  GLN H  356  5                                   3    
HELIX  172 172 LYS H  357  LEU H  362  1                                   6    
HELIX  173 173 LEU H  362  TYR H  376  1                                  15    
HELIX  174 174 LEU H  407  ARG H  412  1                                   6    
HELIX  175 175 PRO H  425  LEU H  429  5                                   5    
HELIX  176 176 GLY H  452  LYS H  469  1                                  18    
HELIX  177 177 PRO I   37  MET I   41  5                                   5    
HELIX  178 178 ARG I   51  GLN I   59  1                                   9    
HELIX  179 179 HIS I   63  GLY I   76  1                                  14    
HELIX  180 180 LEU I   93  ASP I  104  1                                  12    
HELIX  181 181 LEU I  113  GLY I  124  1                                  12    
HELIX  182 182 GLU I  136  LEU I  142  1                                   7    
HELIX  183 183 LEU I  144  LEU I  149  1                                   6    
HELIX  184 184 SER I  150  LEU I  177  1                                  28    
HELIX  185 185 VAL I  188  GLY I  206  1                                  19    
HELIX  186 186 SER I  217  PHE I  239  1                                  23    
HELIX  187 187 PRO I  241  SER I  249  1                                   9    
HELIX  188 188 SER I  249  ALA I  279  1                                  31    
HELIX  189 189 GLY I  288  ALA I  297  1                                  10    
HELIX  190 190 SER I  300  GLY I  314  1                                  15    
HELIX  191 191 VAL I  316  ARG I  332  1                                  17    
HELIX  192 192 ASN I  333  ALA I  347  1                                  15    
HELIX  193 193 ALA I  347  HIS I  354  1                                   8    
HELIX  194 194 LYS I  357  LEU I  362  1                                   6    
HELIX  195 195 LEU I  362  TYR I  376  1                                  15    
HELIX  196 196 LEU I  407  ASN I  413  1                                   7    
HELIX  197 197 ASN I  424  LEU I  429  5                                   6    
HELIX  198 198 PHE I  445  GLN I  449  5                                   5    
HELIX  199 199 GLY I  452  HIS I  470  1                                  19    
HELIX  200 200 PRO J   37  MET J   41  5                                   5    
HELIX  201 201 ARG J   48  LEU J   53  1                                   6    
HELIX  202 202 LEU J   53  GLN J   59  1                                   7    
HELIX  203 203 HIS J   63  LEU J   75  1                                  13    
HELIX  204 204 LEU J   93  VAL J  103  1                                  11    
HELIX  205 205 LEU J  113  ARG J  123  1                                  11    
HELIX  206 206 GLY J  128  LEU J  132  5                                   5    
HELIX  207 207 ASN J  133  LEU J  142  1                                  10    
HELIX  208 208 LEU J  144  LEU J  149  1                                   6    
HELIX  209 209 SER J  150  LEU J  177  1                                  28    
HELIX  210 210 VAL J  188  GLY J  206  1                                  19    
HELIX  211 211 SER J  217  MET J  238  1                                  22    
HELIX  212 212 PRO J  241  SER J  249  1                                   9    
HELIX  213 213 SER J  249  ALA J  279  1                                  31    
HELIX  214 214 GLY J  288  LYS J  296  1                                   9    
HELIX  215 215 SER J  300  SER J  315  1                                  16    
HELIX  216 216 VAL J  316  ARG J  332  1                                  17    
HELIX  217 217 ASN J  333  ALA J  346  1                                  14    
HELIX  218 218 ALA J  347  HIS J  354  1                                   8    
HELIX  219 219 LYS J  357  LEU J  362  1                                   6    
HELIX  220 220 LEU J  362  TYR J  376  1                                  15    
HELIX  221 221 LEU J  407  ARG J  412  1                                   6    
HELIX  222 222 ASN J  424  ASP J  430  5                                   7    
HELIX  223 223 PHE J  445  GLN J  449  5                                   5    
HELIX  224 224 GLY J  452  HIS J  470  1                                  19    
HELIX  225 225 PRO K   37  MET K   41  5                                   5    
HELIX  226 226 ASN K   47  GLN K   59  1                                  13    
HELIX  227 227 HIS K   63  GLY K   76  1                                  14    
HELIX  228 228 LEU K   93  VAL K  103  1                                  11    
HELIX  229 229 LEU K  113  GLY K  124  1                                  12    
HELIX  230 230 GLY K  134  LEU K  142  1                                   9    
HELIX  231 231 LEU K  144  LEU K  149  1                                   6    
HELIX  232 232 SER K  150  LEU K  177  1                                  28    
HELIX  233 233 VAL K  188  GLY K  206  1                                  19    
HELIX  234 234 SER K  217  PHE K  239  1                                  23    
HELIX  235 235 PRO K  241  SER K  249  1                                   9    
HELIX  236 236 SER K  249  ASN K  281  1                                  33    
HELIX  237 237 GLY K  288  ALA K  297  1                                  10    
HELIX  238 238 SER K  300  SER K  315  1                                  16    
HELIX  239 239 VAL K  316  ASN K  333  1                                  18    
HELIX  240 240 ASN K  333  HIS K  354  1                                  22    
HELIX  241 241 LYS K  357  LEU K  362  1                                   6    
HELIX  242 242 LEU K  362  TYR K  376  1                                  15    
HELIX  243 243 LEU K  407  ARG K  412  1                                   6    
HELIX  244 244 PRO K  425  ASP K  430  1                                   6    
HELIX  245 245 PHE K  445  GLN K  449  5                                   5    
HELIX  246 246 GLY K  452  LYS K  469  1                                  18    
HELIX  247 247 PRO L   37  MET L   41  5                                   5    
HELIX  248 248 ARG L   48  GLN L   59  1                                  12    
HELIX  249 249 HIS L   63  GLY L   76  1                                  14    
HELIX  250 250 LEU L   93  VAL L  103  1                                  11    
HELIX  251 251 LEU L  113  ARG L  123  1                                  11    
HELIX  252 252 ASN L  133  ARG L  143  1                                  11    
HELIX  253 253 LEU L  144  LEU L  149  1                                   6    
HELIX  254 254 SER L  150  LEU L  177  1                                  28    
HELIX  255 255 VAL L  188  GLY L  206  1                                  19    
HELIX  256 256 SER L  217  MET L  238  1                                  22    
HELIX  257 257 PRO L  241  SER L  249  1                                   9    
HELIX  258 258 SER L  249  ASN L  281  1                                  33    
HELIX  259 259 GLY L  288  ALA L  297  1                                  10    
HELIX  260 260 SER L  300  SER L  315  1                                  16    
HELIX  261 261 VAL L  316  ASN L  333  1                                  18    
HELIX  262 262 ASN L  333  HIS L  354  1                                  22    
HELIX  263 263 PRO L  355  THR L  360  5                                   6    
HELIX  264 264 LEU L  362  TYR L  376  1                                  15    
HELIX  265 265 LEU L  407  GLY L  411  1                                   5    
HELIX  266 266 ASN L  424  TRP L  428  5                                   5    
HELIX  267 267 PHE L  445  GLN L  449  5                                   5    
HELIX  268 268 GLY L  452  LYS L  469  1                                  18    
SHEET    1   A 4 ILE A  78  ASN A  82  0                                        
SHEET    2   A 4 ARG A  87  VAL A  91 -1  O  CYS A  90   N  PHE A  79           
SHEET    3   A 4 LEU A 402  PHE A 406  1  O  GLN A 404   N  VAL A  91           
SHEET    4   A 4 PHE A 381  VAL A 385 -1  N  ARG A 384   O  VAL A 403           
SHEET    1   B 3 SER A 183  LEU A 186  0                                        
SHEET    2   B 3 LEU A 497  ALA A 501 -1  O  PHE A 499   N  LEU A 184           
SHEET    3   B 3 PHE A 471  GLU A 474 -1  N  LEU A 472   O  ARG A 500           
SHEET    1   C 2 LEU A 390  LEU A 392  0                                        
SHEET    2   C 2 TYR A 395  ILE A 397 -1  O  ILE A 397   N  LEU A 390           
SHEET    1   D 2 MET A 483  TYR A 485  0                                        
SHEET    2   D 2 LEU A 489  PRO A 491 -1  O  ARG A 490   N  VAL A 484           
SHEET    1   E 4 ILE B  78  ASN B  82  0                                        
SHEET    2   E 4 ARG B  87  VAL B  91 -1  O  CYS B  90   N  PHE B  79           
SHEET    3   E 4 LEU B 402  PHE B 406  1  O  LEU B 402   N  ARG B  87           
SHEET    4   E 4 PHE B 381  VAL B 385 -1  N  ARG B 384   O  VAL B 403           
SHEET    1   F 3 SER B 183  LEU B 186  0                                        
SHEET    2   F 3 LEU B 497  ALA B 501 -1  O  PHE B 499   N  LEU B 184           
SHEET    3   F 3 PHE B 471  GLU B 474 -1  N  LEU B 472   O  ARG B 500           
SHEET    1   G 2 LEU B 390  LEU B 392  0                                        
SHEET    2   G 2 TYR B 395  ILE B 397 -1  O  ILE B 397   N  LEU B 390           
SHEET    1   H 2 MET B 483  TYR B 485  0                                        
SHEET    2   H 2 LEU B 489  PRO B 491 -1  O  ARG B 490   N  VAL B 484           
SHEET    1   I 4 ILE C  78  ASN C  82  0                                        
SHEET    2   I 4 ARG C  87  VAL C  91 -1  O  CYS C  90   N  PHE C  79           
SHEET    3   I 4 LEU C 402  PHE C 406  1  O  GLN C 404   N  VAL C  89           
SHEET    4   I 4 PHE C 381  VAL C 385 -1  N  ARG C 384   O  VAL C 403           
SHEET    1   J 3 SER C 183  LEU C 186  0                                        
SHEET    2   J 3 LEU C 497  ALA C 501 -1  O  PHE C 499   N  LEU C 184           
SHEET    3   J 3 PHE C 471  GLU C 474 -1  N  LEU C 472   O  ARG C 500           
SHEET    1   K 2 LEU C 390  LEU C 392  0                                        
SHEET    2   K 2 TYR C 395  ILE C 397 -1  O  ILE C 397   N  LEU C 390           
SHEET    1   L 2 MET C 483  TYR C 485  0                                        
SHEET    2   L 2 LEU C 489  PRO C 491 -1  O  ARG C 490   N  VAL C 484           
SHEET    1   M 4 ILE D  78  ASN D  82  0                                        
SHEET    2   M 4 ARG D  87  VAL D  91 -1  O  CYS D  90   N  PHE D  79           
SHEET    3   M 4 LEU D 402  PHE D 406  1  O  GLN D 404   N  VAL D  89           
SHEET    4   M 4 PHE D 381  VAL D 385 -1  N  ARG D 384   O  VAL D 403           
SHEET    1   N 3 SER D 183  LEU D 186  0                                        
SHEET    2   N 3 LEU D 497  ALA D 501 -1  O  PHE D 499   N  LEU D 184           
SHEET    3   N 3 PHE D 471  GLU D 474 -1  N  GLU D 474   O  THR D 498           
SHEET    1   O 2 LEU D 390  LEU D 392  0                                        
SHEET    2   O 2 TYR D 395  ILE D 397 -1  O  ILE D 397   N  LEU D 390           
SHEET    1   P 2 MET D 483  TYR D 485  0                                        
SHEET    2   P 2 LEU D 489  PRO D 491 -1  O  ARG D 490   N  VAL D 484           
SHEET    1   Q 5 GLN E  43  HIS E  44  0                                        
SHEET    2   Q 5 ILE E  78  TYR E  81  1  O  ARG E  80   N  HIS E  44           
SHEET    3   Q 5 MET E  88  VAL E  91 -1  O  CYS E  90   N  PHE E  79           
SHEET    4   Q 5 LEU E 402  PHE E 406  1  O  PHE E 406   N  VAL E  91           
SHEET    5   Q 5 PHE E 381  VAL E 385 -1  N  ARG E 384   O  VAL E 403           
SHEET    1   R 3 SER E 183  LEU E 186  0                                        
SHEET    2   R 3 LEU E 497  ALA E 501 -1  O  PHE E 499   N  LEU E 184           
SHEET    3   R 3 PHE E 471  GLU E 474 -1  N  LEU E 472   O  ARG E 500           
SHEET    1   S 2 LEU E 390  LEU E 392  0                                        
SHEET    2   S 2 TYR E 395  ILE E 397 -1  O  ILE E 397   N  LEU E 390           
SHEET    1   T 2 MET E 483  TYR E 485  0                                        
SHEET    2   T 2 LEU E 489  PRO E 491 -1  O  ARG E 490   N  VAL E 484           
SHEET    1   U 4 ILE F  78  TYR F  81  0                                        
SHEET    2   U 4 MET F  88  VAL F  91 -1  O  CYS F  90   N  PHE F  79           
SHEET    3   U 4 LEU F 402  PHE F 406  1  O  GLN F 404   N  VAL F  91           
SHEET    4   U 4 PHE F 381  VAL F 385 -1  N  ARG F 384   O  VAL F 403           
SHEET    1   V 3 SER F 183  LEU F 186  0                                        
SHEET    2   V 3 LEU F 497  ALA F 501 -1  O  PHE F 499   N  LEU F 184           
SHEET    3   V 3 PHE F 471  GLU F 474 -1  N  GLU F 474   O  THR F 498           
SHEET    1   W 2 LEU F 390  VAL F 391  0                                        
SHEET    2   W 2 HIS F 396  ILE F 397 -1  O  ILE F 397   N  LEU F 390           
SHEET    1   X 2 MET F 483  TYR F 485  0                                        
SHEET    2   X 2 LEU F 489  PRO F 491 -1  O  ARG F 490   N  VAL F 484           
SHEET    1   Y 4 ILE G  78  ARG G  80  0                                        
SHEET    2   Y 4 MET G  88  VAL G  91 -1  O  CYS G  90   N  PHE G  79           
SHEET    3   Y 4 LEU G 402  PHE G 406  1  O  LEU G 402   N  VAL G  89           
SHEET    4   Y 4 PHE G 381  VAL G 385 -1  N  LEU G 382   O  VAL G 405           
SHEET    1   Z 3 SER G 183  LEU G 186  0                                        
SHEET    2   Z 3 LEU G 497  ALA G 501 -1  O  LEU G 497   N  LEU G 186           
SHEET    3   Z 3 PHE G 471  GLU G 474 -1  N  LEU G 472   O  ARG G 500           
SHEET    1  AA 2 LEU G 390  LEU G 392  0                                        
SHEET    2  AA 2 TYR G 395  ILE G 397 -1  O  ILE G 397   N  LEU G 390           
SHEET    1  AB 2 MET G 483  TYR G 485  0                                        
SHEET    2  AB 2 LEU G 489  PRO G 491 -1  O  ARG G 490   N  VAL G 484           
SHEET    1  AC 4 ILE H  78  ARG H  80  0                                        
SHEET    2  AC 4 MET H  88  VAL H  91 -1  O  CYS H  90   N  PHE H  79           
SHEET    3  AC 4 LEU H 402  PHE H 406  1  O  GLN H 404   N  VAL H  91           
SHEET    4  AC 4 PHE H 381  VAL H 385 -1  N  ARG H 384   O  VAL H 403           
SHEET    1  AD 3 SER H 183  LEU H 186  0                                        
SHEET    2  AD 3 LEU H 497  ALA H 501 -1  O  PHE H 499   N  LEU H 184           
SHEET    3  AD 3 PHE H 471  GLU H 474 -1  N  GLU H 474   O  THR H 498           
SHEET    1  AE 2 LEU H 390  LEU H 392  0                                        
SHEET    2  AE 2 TYR H 395  ILE H 397 -1  O  ILE H 397   N  LEU H 390           
SHEET    1  AF 2 MET H 483  TYR H 485  0                                        
SHEET    2  AF 2 LEU H 489  PRO H 491 -1  O  ARG H 490   N  VAL H 484           
SHEET    1  AG 4 ILE I  78  ASN I  82  0                                        
SHEET    2  AG 4 ARG I  87  VAL I  91 -1  O  CYS I  90   N  PHE I  79           
SHEET    3  AG 4 LEU I 402  PHE I 406  1  O  PHE I 406   N  VAL I  91           
SHEET    4  AG 4 PHE I 381  VAL I 385 -1  N  ARG I 384   O  VAL I 403           
SHEET    1  AH 3 SER I 183  LEU I 186  0                                        
SHEET    2  AH 3 LEU I 497  ALA I 501 -1  O  LEU I 497   N  LEU I 186           
SHEET    3  AH 3 PHE I 471  GLU I 474 -1  N  LEU I 472   O  ARG I 500           
SHEET    1  AI 2 LEU I 390  VAL I 391  0                                        
SHEET    2  AI 2 HIS I 396  ILE I 397 -1  O  ILE I 397   N  LEU I 390           
SHEET    1  AJ 2 MET I 483  TYR I 485  0                                        
SHEET    2  AJ 2 LEU I 489  PRO I 491 -1  O  ARG I 490   N  VAL I 484           
SHEET    1  AK 4 ILE J  78  ARG J  80  0                                        
SHEET    2  AK 4 MET J  88  VAL J  91 -1  O  CYS J  90   N  PHE J  79           
SHEET    3  AK 4 LEU J 402  PHE J 406  1  O  LEU J 402   N  VAL J  89           
SHEET    4  AK 4 PHE J 381  VAL J 385 -1  N  ARG J 384   O  VAL J 403           
SHEET    1  AL 3 SER J 183  LEU J 186  0                                        
SHEET    2  AL 3 LEU J 497  ALA J 501 -1  O  LEU J 497   N  LEU J 186           
SHEET    3  AL 3 PHE J 471  GLU J 474 -1  N  LEU J 472   O  ARG J 500           
SHEET    1  AM 2 LEU J 390  LEU J 392  0                                        
SHEET    2  AM 2 TYR J 395  ILE J 397 -1  O  ILE J 397   N  LEU J 390           
SHEET    1  AN 2 MET J 483  TYR J 485  0                                        
SHEET    2  AN 2 LEU J 489  PRO J 491 -1  O  ARG J 490   N  VAL J 484           
SHEET    1  AO 4 ILE K  78  TYR K  81  0                                        
SHEET    2  AO 4 MET K  88  VAL K  91 -1  O  CYS K  90   N  PHE K  79           
SHEET    3  AO 4 LEU K 402  PHE K 406  1  O  LEU K 402   N  VAL K  89           
SHEET    4  AO 4 PHE K 381  VAL K 385 -1  N  ARG K 384   O  VAL K 403           
SHEET    1  AP 3 SER K 183  LEU K 186  0                                        
SHEET    2  AP 3 LEU K 497  ALA K 501 -1  O  PHE K 499   N  LEU K 184           
SHEET    3  AP 3 PHE K 471  GLU K 474 -1  N  LEU K 472   O  ARG K 500           
SHEET    1  AQ 2 LEU K 390  LEU K 392  0                                        
SHEET    2  AQ 2 TYR K 395  ILE K 397 -1  O  ILE K 397   N  LEU K 390           
SHEET    1  AR 2 MET K 483  TYR K 485  0                                        
SHEET    2  AR 2 LEU K 489  PRO K 491 -1  O  ARG K 490   N  VAL K 484           
SHEET    1  AS 4 ILE L  78  ARG L  80  0                                        
SHEET    2  AS 4 MET L  88  VAL L  91 -1  O  CYS L  90   N  PHE L  79           
SHEET    3  AS 4 LEU L 402  PHE L 406  1  O  LEU L 402   N  VAL L  89           
SHEET    4  AS 4 PHE L 381  VAL L 385 -1  N  ARG L 384   O  VAL L 403           
SHEET    1  AT 3 SER L 183  LEU L 186  0                                        
SHEET    2  AT 3 LEU L 497  ALA L 501 -1  O  PHE L 499   N  LEU L 184           
SHEET    3  AT 3 PHE L 471  GLU L 474 -1  N  GLU L 474   O  THR L 498           
SHEET    1  AU 2 LEU L 390  LEU L 392  0                                        
SHEET    2  AU 2 TYR L 395  ILE L 397 -1  O  ILE L 397   N  LEU L 390           
SHEET    1  AV 2 MET L 483  TYR L 485  0                                        
SHEET    2  AV 2 LEU L 489  PRO L 491 -1  O  ARG L 490   N  VAL L 484           
LINK         SG  CYS B 450                FE   HEM B 601     1555   1555  2.13  
LINK         SG  CYS A 450                FE   HEM A 601     1555   1555  2.14  
LINK         SG  CYS D 450                FE   HEM D 601     1555   1555  2.15  
LINK         SG  CYS C 450                FE   HEM C 601     1555   1555  2.16  
LINK         SG  CYS H 450                FE   HEM H 601     1555   1555  2.17  
LINK         SG  CYS F 450                FE   HEM F 601     1555   1555  2.18  
LINK         SG  CYS E 450                FE   HEM E 601     1555   1555  2.23  
LINK         SG  CYS I 450                FE   HEM I 601     1555   1555  2.27  
LINK         SG  CYS G 450                FE   HEM G 601     1555   1555  2.35  
LINK         SG  CYS L 450                FE   HEM L 601     1555   1555  2.51  
LINK         SG  CYS K 450                FE   HEM K 601     1555   1555  2.54  
LINK         SG  CYS J 450                FE   HEM J 601     1555   1555  2.57  
LINK        FE   HEM B 601                 N06 0T3 B 602     1555   1555  1.81  
LINK        FE   HEM A 601                 N06 0T3 A 602     1555   1555  1.87  
LINK        FE   HEM L 601                 N06 0T3 L 602     1555   1555  1.91  
LINK        FE   HEM H 601                 N06 0T3 H 602     1555   1555  1.93  
LINK        FE   HEM C 601                 N06 0T3 C 602     1555   1555  1.95  
LINK        FE   HEM G 601                 N06 0T3 G 602     1555   1555  1.98  
LINK        FE   HEM D 601                 N06 0T3 D 602     1555   1555  1.99  
LINK        FE   HEM F 601                 N06 0T3 F 602     1555   1555  1.99  
LINK        FE   HEM E 601                 N06 0T3 E 602     1555   1555  2.03  
LINK        FE   HEM K 601                 N06 0T3 K 602     1555   1555  2.10  
LINK        FE   HEM I 601                 N06 0T3 I 602     1555   1555  2.13  
LINK        FE   HEM J 601                 N06 0T3 J 602     1555   1555  2.17  
SITE     1 AC1 21 ARG A 110  VAL A 129  PHE A 130  TRP A 137                    
SITE     2 AC1 21 ARG A 141  LEU A 311  GLY A 314  SER A 315                    
SITE     3 AC1 21 THR A 318  THR A 319  LEU A 382  ARG A 384                    
SITE     4 AC1 21 PRO A 442  PHE A 443  GLY A 444  PHE A 445                    
SITE     5 AC1 21 ARG A 448  CYS A 450  GLY A 452  LEU A 455                    
SITE     6 AC1 21 0T3 A 602                                                     
SITE     1 AC2 10 TRP A 116  ARG A 120  TRP A 260  GLU A 310                    
SITE     2 AC2 10 ALA A 313  GLY A 314  THR A 318  PHE A 487                    
SITE     3 AC2 10 ILE A 488  HEM A 601                                          
SITE     1 AC3 19 ARG B 110  VAL B 129  PHE B 130  TRP B 137                    
SITE     2 AC3 19 ARG B 141  LEU B 311  GLY B 314  SER B 315                    
SITE     3 AC3 19 THR B 318  LEU B 382  ARG B 384  PRO B 442                    
SITE     4 AC3 19 PHE B 443  GLY B 444  PHE B 445  ARG B 448                    
SITE     5 AC3 19 CYS B 450  GLY B 452  0T3 B 602                               
SITE     1 AC4  8 TRP B 116  ARG B 120  GLU B 310  GLY B 314                    
SITE     2 AC4  8 THR B 318  PHE B 487  ILE B 488  HEM B 601                    
SITE     1 AC5 18 ARG C 110  VAL C 129  PHE C 130  TRP C 137                    
SITE     2 AC5 18 ARG C 141  LEU C 311  GLY C 314  SER C 315                    
SITE     3 AC5 18 THR C 318  THR C 319  ARG C 384  PRO C 442                    
SITE     4 AC5 18 PHE C 443  ARG C 448  CYS C 450  GLY C 452                    
SITE     5 AC5 18 ALA C 456  0T3 C 602                                          
SITE     1 AC6  9 TRP C 116  ARG C 120  TRP C 260  GLU C 310                    
SITE     2 AC6  9 GLY C 314  THR C 318  PHE C 487  ILE C 488                    
SITE     3 AC6  9 HEM C 601                                                     
SITE     1 AC7 18 ARG D 110  VAL D 129  PHE D 130  TRP D 137                    
SITE     2 AC7 18 ARG D 141  GLY D 314  SER D 315  THR D 318                    
SITE     3 AC7 18 THR D 319  LEU D 382  ARG D 384  PRO D 442                    
SITE     4 AC7 18 PHE D 443  PHE D 445  ARG D 448  CYS D 450                    
SITE     5 AC7 18 GLY D 452  0T3 D 602                                          
SITE     1 AC8 11 TRP D 116  ARG D 120  PHE D 130  TRP D 260                    
SITE     2 AC8 11 GLU D 310  ALA D 313  GLY D 314  THR D 318                    
SITE     3 AC8 11 PHE D 487  ILE D 488  HEM D 601                               
SITE     1 AC9 21 ARG E 110  VAL E 129  PHE E 130  TRP E 137                    
SITE     2 AC9 21 ARG E 141  LEU E 311  GLY E 314  SER E 315                    
SITE     3 AC9 21 THR E 318  THR E 319  VAL E 378  LEU E 382                    
SITE     4 AC9 21 ARG E 384  PRO E 442  PHE E 443  GLY E 444                    
SITE     5 AC9 21 PHE E 445  ARG E 448  CYS E 450  GLY E 452                    
SITE     6 AC9 21 0T3 E 602                                                     
SITE     1 BC1  8 TRP E 116  ARG E 120  TRP E 260  GLU E 310                    
SITE     2 BC1  8 GLY E 314  THR E 318  PHE E 487  HEM E 601                    
SITE     1 BC2 19 ARG F 110  VAL F 129  PHE F 130  TRP F 137                    
SITE     2 BC2 19 ARG F 141  LEU F 311  GLY F 314  SER F 315                    
SITE     3 BC2 19 THR F 318  ARG F 384  PRO F 442  PHE F 443                    
SITE     4 BC2 19 GLY F 444  PHE F 445  ARG F 448  GLN F 449                    
SITE     5 BC2 19 CYS F 450  GLY F 452  0T3 F 602                               
SITE     1 BC3 10 TRP F 116  ARG F 120  PHE F 130  GLU F 310                    
SITE     2 BC3 10 ALA F 313  GLY F 314  THR F 318  PHE F 487                    
SITE     3 BC3 10 ILE F 488  HEM F 601                                          
SITE     1 BC4 19 ARG G 110  VAL G 129  PHE G 130  TRP G 137                    
SITE     2 BC4 19 ARG G 141  LEU G 311  SER G 315  THR G 318                    
SITE     3 BC4 19 LEU G 382  ARG G 384  PRO G 442  PHE G 443                    
SITE     4 BC4 19 GLY G 444  PHE G 445  ARG G 448  GLN G 449                    
SITE     5 BC4 19 CYS G 450  GLY G 452  0T3 G 602                               
SITE     1 BC5  9 TRP G 116  ARG G 120  GLU G 310  ALA G 313                    
SITE     2 BC5  9 GLY G 314  THR G 318  PHE G 487  ILE G 488                    
SITE     3 BC5  9 HEM G 601                                                     
SITE     1 BC6 20 ARG H 110  VAL H 129  PHE H 130  TRP H 137                    
SITE     2 BC6 20 ARG H 141  LEU H 311  GLY H 314  SER H 315                    
SITE     3 BC6 20 THR H 318  THR H 319  ARG H 384  PRO H 442                    
SITE     4 BC6 20 PHE H 443  GLY H 444  PHE H 445  ARG H 448                    
SITE     5 BC6 20 CYS H 450  GLY H 452  LEU H 455  0T3 H 602                    
SITE     1 BC7  7 TRP H 116  ARG H 120  GLY H 314  THR H 318                    
SITE     2 BC7  7 PHE H 487  ILE H 488  HEM H 601                               
SITE     1 BC8 18 ARG I 110  VAL I 129  PHE I 130  TRP I 137                    
SITE     2 BC8 18 ARG I 141  GLY I 314  SER I 315  THR I 318                    
SITE     3 BC8 18 LEU I 382  ARG I 384  PRO I 442  PHE I 443                    
SITE     4 BC8 18 GLY I 444  PHE I 445  ARG I 448  CYS I 450                    
SITE     5 BC8 18 GLY I 452  0T3 I 602                                          
SITE     1 BC9  9 TRP I 116  ARG I 120  PHE I 231  TRP I 260                    
SITE     2 BC9  9 GLY I 314  THR I 318  PHE I 487  ILE I 488                    
SITE     3 BC9  9 HEM I 601                                                     
SITE     1 CC1 22 ARG J 110  VAL J 129  PHE J 130  TRP J 137                    
SITE     2 CC1 22 ARG J 141  LEU J 311  GLY J 314  SER J 315                    
SITE     3 CC1 22 THR J 318  THR J 319  PRO J 322  VAL J 378                    
SITE     4 CC1 22 LEU J 382  ARG J 384  PRO J 442  PHE J 443                    
SITE     5 CC1 22 GLY J 444  PHE J 445  ARG J 448  CYS J 450                    
SITE     6 CC1 22 GLY J 452  0T3 J 602                                          
SITE     1 CC2  9 TRP J 116  ARG J 120  TRP J 260  GLU J 310                    
SITE     2 CC2  9 GLY J 314  THR J 318  PHE J 487  ILE J 488                    
SITE     3 CC2  9 HEM J 601                                                     
SITE     1 CC3 20 ARG K 110  VAL K 129  PHE K 130  TRP K 137                    
SITE     2 CC3 20 ARG K 141  LEU K 311  SER K 315  THR K 318                    
SITE     3 CC3 20 THR K 319  VAL K 378  LEU K 382  ARG K 384                    
SITE     4 CC3 20 PRO K 442  PHE K 443  ARG K 448  CYS K 450                    
SITE     5 CC3 20 GLY K 452  LEU K 455  ALA K 456  0T3 K 602                    
SITE     1 CC4  8 TRP K 116  ARG K 120  GLU K 310  GLY K 314                    
SITE     2 CC4  8 THR K 318  PHE K 487  ILE K 488  HEM K 601                    
SITE     1 CC5 17 ARG L 110  VAL L 129  PHE L 130  TRP L 137                    
SITE     2 CC5 17 ARG L 141  LEU L 311  SER L 315  THR L 318                    
SITE     3 CC5 17 VAL L 378  LEU L 382  ARG L 384  PRO L 442                    
SITE     4 CC5 17 PHE L 443  ARG L 448  CYS L 450  GLY L 452                    
SITE     5 CC5 17 0T3 L 602                                                     
SITE     1 CC6  8 TRP L 116  ARG L 120  GLU L 310  GLY L 314                    
SITE     2 CC6  8 THR L 318  PHE L 487  ILE L 488  HEM L 601                    
CRYST1  129.751  199.086  150.018  90.00 112.08  90.00 P 1 21 1     24          
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      0.007707  0.000000  0.003126        0.00000                         
SCALE2      0.000000  0.005023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007193        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system