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Database: PDB
Entry: 4DVQ
LinkDB: 4DVQ
Original site: 4DVQ 
HEADER    OXIDOREDUCTASE                          23-FEB-12   4DVQ              
TITLE     STRUCTURE OF HUMAN ALDOSTERONE SYNTHASE, CYP11B2, IN COMPLEX WITH     
TITLE    2 DEOXYCORTICOSTERONE                                                  
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, CORTICOSTEROID, MITOCHONDRIA, MEMBRANE,  
KEYWDS   3 OXIDOREDUCTASE                                                       
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 4DVQ    1       JRNL                                     
REVDAT   1   30-JAN-13 4DVQ    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.    2.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 245706                         
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.973                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 12220                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 15486                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 838                          
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 45085                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 849                                     
REMARK   3   SOLVENT ATOMS            : 260                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.33600                                              
REMARK   3    B22 (A**2) : 0.56500                                              
REMARK   3    B33 (A**2) : -0.46400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.57900                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.240         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.859        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 47254 ; 0.011 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A): 32605 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 64368 ; 1.319 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 78990 ; 0.886 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  5526 ; 5.899 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2183 ;34.081 ;22.863       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  7953 ;17.844 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   384 ;16.480 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7000 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 51416 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  9936 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 27816 ; 0.739 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 44974 ; 1.452 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 19403 ; 2.295 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 19341 ; 3.784 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   4                                                                      
REMARK   4 4DVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070842.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 245749                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.240                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7435                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% 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       99.81450            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 106890 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -199.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 106590 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, L, H, K, I, J                      
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     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   437                                                      
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     ARG B   432                                                      
REMARK 465     GLY B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     GLY B   435                                                      
REMARK 465     ARG B   436                                                      
REMARK 465     ASN B   437                                                      
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     ILE D   431                                                      
REMARK 465     ARG D   432                                                      
REMARK 465     GLY D   433                                                      
REMARK 465     SER D   434                                                      
REMARK 465     GLY D   435                                                      
REMARK 465     ARG D   436                                                      
REMARK 465     ASN D   437                                                      
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   437                                                      
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     LEU K   429                                                      
REMARK 465     ASP K   430                                                      
REMARK 465     ILE K   431                                                      
REMARK 465     ARG K   432                                                      
REMARK 465     GLY K   433                                                      
REMARK 465     SER K   434                                                      
REMARK 465     GLY K   435                                                      
REMARK 465     ARG K   436                                                      
REMARK 465     ASN K   437                                                      
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     PHE L   438                                                      
REMARK 465     HIS L   439                                                      
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    HIS A  63   CG    HIS A  63   CD2     0.057                       
REMARK 500    HIS B 225   CG    HIS B 225   CD2     0.058                       
REMARK 500    HIS D  63   CG    HIS D  63   CD2     0.056                       
REMARK 500    HIS F 225   CG    HIS F 225   CD2     0.056                       
REMARK 500    HIS G 440   CG    HIS G 440   CD2     0.061                       
REMARK 500    HIS K 440   CG    HIS K 440   CD2     0.058                       
REMARK 500    HIS L 440   CG    HIS L 440   CD2     0.058                       
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       53.11   -155.27                                   
REMARK 500    PRO A  77       21.72    -77.36                                   
REMARK 500    MET A  92       11.08   -149.97                                   
REMARK 500    SER A 105     -167.28    -69.02                                   
REMARK 500    SER A 249       55.00   -140.99                                   
REMARK 500    LEU A 362       57.13   -118.22                                   
REMARK 500    ALA A 399      131.85    -34.31                                   
REMARK 500    CYS A 450      128.05    -36.95                                   
REMARK 500    THR A 477       81.01    -62.31                                   
REMARK 500    SER A 486       57.03   -149.39                                   
REMARK 500    PHE A 487      -49.39     72.58                                   
REMARK 500    ARG B  48      -38.54    -36.10                                   
REMARK 500    TYR B  61       54.41   -150.23                                   
REMARK 500    ASN B  82       96.67    -62.41                                   
REMARK 500    MET B  92       24.85   -160.51                                   
REMARK 500    SER B 105     -164.60    -69.26                                   
REMARK 500    SER B 243      -59.07    -29.68                                   
REMARK 500    VAL B 316      -79.01   -100.19                                   
REMARK 500    ALA B 349      -71.03    -37.97                                   
REMARK 500    ARG B 427      -37.70    -24.61                                   
REMARK 500    GLN B 449      151.82    -47.92                                   
REMARK 500    CYS B 450      120.79    -37.44                                   
REMARK 500    PHE B 487      -59.17     68.93                                   
REMARK 500    TYR C  61       53.00   -163.33                                   
REMARK 500    MET C  92       10.66   -151.21                                   
REMARK 500    GLU C  95      -55.82    -22.42                                   
REMARK 500    SER C 105     -159.33    -77.09                                   
REMARK 500    SER C 249       53.63   -142.14                                   
REMARK 500    ASN C 413       96.43    -65.65                                   
REMARK 500    PHE C 487      -59.75     66.84                                   
REMARK 500    TYR D  61       54.78   -157.25                                   
REMARK 500    SER D 249       45.62   -142.23                                   
REMARK 500    ALA D 297       29.76     46.99                                   
REMARK 500    VAL D 316      -68.03   -104.93                                   
REMARK 500    ASN D 333       74.42   -110.74                                   
REMARK 500    ASN D 413       93.76    -64.98                                   
REMARK 500    ARG D 419       71.25     56.70                                   
REMARK 500    ARG D 427       -3.67    -57.53                                   
REMARK 500    GLN D 449      152.97    -46.40                                   
REMARK 500    PHE D 487      -46.93     71.04                                   
REMARK 500    TYR E  61       61.50   -159.20                                   
REMARK 500    PRO E  77        0.58    -66.79                                   
REMARK 500    ASN E  82       88.07    -63.49                                   
REMARK 500    MET E  92       10.75   -151.15                                   
REMARK 500    GLU E  95      -50.54    -25.25                                   
REMARK 500    SER E 105     -162.75    -73.48                                   
REMARK 500    VAL E 316      -68.12   -100.23                                   
REMARK 500    ARG E 419       60.76     66.79                                   
REMARK 500    PHE E 438       29.30    -71.23                                   
REMARK 500    CYS E 450      122.46    -37.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     126 RAMACHANDRAN OUTLIERS.                        
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 G 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 450   SG                                                     
REMARK 620 2 HEM G 601   NA   99.8                                              
REMARK 620 3 HEM G 601   NB   89.9  88.9                                        
REMARK 620 4 HEM G 601   NC   84.0 176.0  89.8                                  
REMARK 620 5 HEM G 601   ND   94.2  90.8 175.9  90.3                            
REMARK 620 N                    1     2     3     4                             
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   98.9                                              
REMARK 620 3 HEM A 601   NB   89.3  88.8                                        
REMARK 620 4 HEM A 601   NC   83.7 177.1  90.0                                  
REMARK 620 5 HEM A 601   ND   94.0  91.8 176.5  89.3                            
REMARK 620 N                    1     2     3     4                             
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   93.3                                              
REMARK 620 3 HEM F 601   NB   80.8  87.8                                        
REMARK 620 4 HEM F 601   NC   89.6 176.5  90.8                                  
REMARK 620 5 HEM F 601   ND  102.4  91.8 176.8  89.4                            
REMARK 620 N                    1     2     3     4                             
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   97.9                                              
REMARK 620 3 HEM H 601   NB   88.2  90.1                                        
REMARK 620 4 HEM H 601   NC   85.4 176.6  89.0                                  
REMARK 620 5 HEM H 601   ND   95.7  89.5 176.2  91.1                            
REMARK 620 N                    1     2     3     4                             
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   95.9                                              
REMARK 620 3 HEM I 601   NB   86.3  86.7                                        
REMARK 620 4 HEM I 601   NC   86.3 177.7  92.8                                  
REMARK 620 5 HEM I 601   ND   96.5  93.5 177.1  86.9                            
REMARK 620 N                    1     2     3     4                             
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   85.2  89.9                                        
REMARK 620 4 HEM E 601   NC   83.7 176.4  89.2                                  
REMARK 620 5 HEM E 601   ND   99.5  89.1 175.3  91.6                            
REMARK 620 N                    1     2     3     4                             
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   97.1                                              
REMARK 620 3 HEM D 601   NB   89.8  92.5                                        
REMARK 620 4 HEM D 601   NC   85.9 177.0  87.0                                  
REMARK 620 5 HEM D 601   ND   93.8  87.0 176.4  93.3                            
REMARK 620 N                    1     2     3     4                             
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   98.6                                              
REMARK 620 3 HEM C 601   NB   90.0  93.7                                        
REMARK 620 4 HEM C 601   NC   84.7 176.7  86.2                                  
REMARK 620 5 HEM C 601   ND   93.9  86.3 176.1  93.6                            
REMARK 620 N                    1     2     3     4                             
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   98.4                                              
REMARK 620 3 HEM L 601   NB   88.4  89.7                                        
REMARK 620 4 HEM L 601   NC   83.1 178.3  89.7                                  
REMARK 620 5 HEM L 601   ND   93.6  90.2 178.0  90.3                            
REMARK 620 N                    1     2     3     4                             
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   99.3                                              
REMARK 620 3 HEM B 601   NB   88.3  91.0                                        
REMARK 620 4 HEM B 601   NC   83.4 177.0  87.7                                  
REMARK 620 5 HEM B 601   ND   94.5  89.8 176.9  91.3                            
REMARK 620 N                    1     2     3     4                             
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   99.8                                              
REMARK 620 3 HEM K 601   NB   82.9  89.7                                        
REMARK 620 4 HEM K 601   NC   81.4 178.7  89.9                                  
REMARK 620 5 HEM K 601   ND   98.1  90.8 178.8  89.7                            
REMARK 620 N                    1     2     3     4                             
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   96.2                                              
REMARK 620 3 HEM J 601   NB   86.6  86.4                                        
REMARK 620 4 HEM J 601   NC   84.8 178.5  92.6                                  
REMARK 620 5 HEM J 601   ND   95.2  92.9 178.1  88.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA G 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM H 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA H 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA I 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM J 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA J 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA K 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM L 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA L 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 603                 
DBREF  4DVQ A   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ B   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ C   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ D   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ E   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ F   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ G   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ H   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ I   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ J   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ K   34   503  UNP    P19099   C11B2_HUMAN     34    503             
DBREF  4DVQ L   34   503  UNP    P19099   C11B2_HUMAN     34    503             
SEQADV 4DVQ MET A   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA A   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS A   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS A   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR A   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER A   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER A   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS A  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS A  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS A  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS A  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS A  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS A  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET B   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA B   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS B   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS B   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR B   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER B   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER B   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS B  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS B  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS B  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS B  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS B  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS B  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET C   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA C   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS C   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS C   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR C   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER C   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER C   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS C  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS C  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS C  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS C  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS C  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS C  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET D   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA D   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS D   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS D   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR D   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER D   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER D   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS D  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS D  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS D  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS D  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS D  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS D  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET E   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA E   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS E   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS E   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR E   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER E   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER E   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS E  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS E  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS E  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS E  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS E  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS E  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET F   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA F   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS F   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS F   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR F   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER F   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER F   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS F  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS F  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS F  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS F  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS F  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS F  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET G   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA G   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS G   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS G   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR G   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER G   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER G   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS G  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS G  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS G  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS G  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS G  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS G  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET H   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA H   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS H   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS H   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR H   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER H   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER H   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS H  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS H  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS H  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS H  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS H  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS H  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET I   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA I   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS I   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS I   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR I   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER I   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER I   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS I  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS I  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS I  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS I  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS I  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS I  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET J   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA J   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS J   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS J   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR J   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER J   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER J   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS J  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS J  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS J  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS J  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS J  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS J  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET K   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA K   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS K   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS K   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR K   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER K   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER K   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS K  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS K  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS K  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS K  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS K  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS K  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ MET L   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ ALA L   28  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS L   29  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ LYS L   30  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ THR L   31  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER L   32  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ SER L   33  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS L  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS L  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS L  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS L  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ HIS L  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4DVQ 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    1CA  A 602      24                                                       
HET    HEM  B 601      43                                                       
HET    SO4  A 603       5                                                       
HET    1CA  B 602      24                                                       
HET    HEM  C 601      43                                                       
HET    1CA  C 602      24                                                       
HET    SO4  B 603       5                                                       
HET    HEM  D 601      43                                                       
HET    1CA  D 602      24                                                       
HET    HEM  E 601      43                                                       
HET    SO4  C 603       5                                                       
HET    1CA  E 602      24                                                       
HET    HEM  F 601      43                                                       
HET    1CA  F 602      24                                                       
HET    SO4  D 603       5                                                       
HET    HEM  G 601      43                                                       
HET    1CA  G 602      24                                                       
HET    HEM  H 601      43                                                       
HET    SO4  E 603       5                                                       
HET    1CA  H 602      24                                                       
HET    HEM  I 601      43                                                       
HET    1CA  I 602      24                                                       
HET    SO4  F 603       5                                                       
HET    HEM  J 601      43                                                       
HET    1CA  J 602      24                                                       
HET    HEM  K 601      43                                                       
HET    SO4  G 603       5                                                       
HET    1CA  K 602      24                                                       
HET    HEM  L 601      43                                                       
HET    1CA  L 602      24                                                       
HET    SO4  K 603       5                                                       
HET    SO4  L 603       5                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     1CA DESOXYCORTICOSTERONE                                             
HETNAM     SO4 SULFATE ION                                                      
HETSYN     HEM HEME                                                             
HETSYN     1CA 4-PREGNEN-21-OL-3,20-DIONE; DOC; 21-HYDROXYPROGESTERONE          
FORMUL  13  HEM    12(C34 H32 FE N4 O4)                                         
FORMUL  14  1CA    12(C21 H30 O3)                                               
FORMUL  16  SO4    9(O4 S 2-)                                                   
FORMUL  46  HOH   *260(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  ASP A  104  1                                  12    
HELIX    5   5 LEU A  113  GLY A  124  1                                  12    
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  ASN A  179  1                                  30    
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  GLY A  314  1                                  15    
HELIX   16  16 VAL A  316  ASN A  333  1                                  18    
HELIX   17  17 ASN A  333  HIS A  354  1                                  22    
HELIX   18  18 LYS A  357  LEU A  362  1                                   6    
HELIX   19  19 LEU A  362  TYR A  376  1                                  15    
HELIX   20  20 LEU A  407  GLY A  411  1                                   5    
HELIX   21  21 GLN A  426  ILE A  431  1                                   6    
HELIX   22  22 GLY A  452  HIS A  470  1                                  19    
HELIX   23  23 PRO B   37  MET B   41  5                                   5    
HELIX   24  24 ASN B   47  GLN B   59  1                                  13    
HELIX   25  25 HIS B   63  GLY B   76  1                                  14    
HELIX   26  26 LEU B   93  GLN B  102  1                                  10    
HELIX   27  27 LEU B  113  GLY B  124  1                                  12    
HELIX   28  28 GLY B  128  LEU B  132  5                                   5    
HELIX   29  29 ASN B  133  ARG B  143  1                                  11    
HELIX   30  30 LEU B  144  LEU B  149  1                                   6    
HELIX   31  31 SER B  150  GLN B  178  1                                  29    
HELIX   32  32 VAL B  188  GLY B  206  1                                  19    
HELIX   33  33 SER B  217  PHE B  239  1                                  23    
HELIX   34  34 PRO B  241  SER B  249  1                                   9    
HELIX   35  35 SER B  249  ASN B  281  1                                  33    
HELIX   36  36 GLY B  288  ALA B  297  1                                  10    
HELIX   37  37 SER B  300  SER B  315  1                                  16    
HELIX   38  38 VAL B  316  ASN B  333  1                                  18    
HELIX   39  39 ASN B  333  HIS B  354  1                                  22    
HELIX   40  40 LYS B  357  LEU B  362  1                                   6    
HELIX   41  41 LEU B  362  TYR B  376  1                                  15    
HELIX   42  42 LEU B  407  ARG B  412  1                                   6    
HELIX   43  43 PRO B  425  ILE B  431  1                                   7    
HELIX   44  44 GLY B  452  HIS B  470  1                                  19    
HELIX   45  45 PRO C   37  MET C   41  5                                   5    
HELIX   46  46 ASN C   47  GLN C   59  1                                  13    
HELIX   47  47 HIS C   63  GLY C   76  1                                  14    
HELIX   48  48 LEU C   93  VAL C  103  1                                  11    
HELIX   49  49 LEU C  113  GLY C  124  1                                  12    
HELIX   50  50 GLY C  128  LEU C  132  5                                   5    
HELIX   51  51 ASN C  133  LEU C  149  1                                  17    
HELIX   52  52 SER C  150  ASN C  179  1                                  30    
HELIX   53  53 VAL C  188  GLY C  206  1                                  19    
HELIX   54  54 SER C  217  PHE C  239  1                                  23    
HELIX   55  55 PRO C  241  SER C  249  1                                   9    
HELIX   56  56 SER C  249  ASN C  281  1                                  33    
HELIX   57  57 GLY C  288  ALA C  297  1                                  10    
HELIX   58  58 SER C  300  GLY C  314  1                                  15    
HELIX   59  59 VAL C  316  ASN C  333  1                                  18    
HELIX   60  60 ASN C  333  ALA C  347  1                                  15    
HELIX   61  61 ALA C  347  HIS C  354  1                                   8    
HELIX   62  62 LYS C  357  LEU C  362  1                                   6    
HELIX   63  63 LEU C  362  TYR C  376  1                                  15    
HELIX   64  64 LEU C  407  ASN C  413  1                                   7    
HELIX   65  65 ASN C  424  LEU C  429  5                                   6    
HELIX   66  66 PHE C  445  GLN C  449  5                                   5    
HELIX   67  67 GLY C  452  HIS C  470  1                                  19    
HELIX   68  68 ASN D   47  GLN D   59  1                                  13    
HELIX   69  69 HIS D   63  GLY D   76  1                                  14    
HELIX   70  70 LEU D   93  VAL D  103  1                                  11    
HELIX   71  71 LEU D  113  GLY D  124  1                                  12    
HELIX   72  72 GLY D  128  LEU D  132  5                                   5    
HELIX   73  73 ASN D  133  LEU D  149  1                                  17    
HELIX   74  74 SER D  150  GLN D  178  1                                  29    
HELIX   75  75 VAL D  188  GLY D  206  1                                  19    
HELIX   76  76 SER D  217  PHE D  239  1                                  23    
HELIX   77  77 PRO D  241  SER D  249  1                                   9    
HELIX   78  78 SER D  249  ASN D  281  1                                  33    
HELIX   79  79 GLY D  288  ALA D  297  1                                  10    
HELIX   80  80 SER D  300  GLY D  314  1                                  15    
HELIX   81  81 VAL D  316  ASN D  333  1                                  18    
HELIX   82  82 ASN D  333  HIS D  354  1                                  22    
HELIX   83  83 LYS D  357  LEU D  362  1                                   6    
HELIX   84  84 LEU D  362  TYR D  376  1                                  15    
HELIX   85  85 LEU D  407  GLY D  411  1                                   5    
HELIX   86  86 ASN D  424  LEU D  429  5                                   6    
HELIX   87  87 PHE D  445  GLN D  449  5                                   5    
HELIX   88  88 GLY D  452  HIS D  470  1                                  19    
HELIX   89  89 PRO E   37  MET E   41  5                                   5    
HELIX   90  90 ASN E   47  GLN E   59  1                                  13    
HELIX   91  91 HIS E   63  GLY E   76  1                                  14    
HELIX   92  92 LEU E   93  VAL E  103  1                                  11    
HELIX   93  93 LEU E  113  GLY E  124  1                                  12    
HELIX   94  94 GLY E  128  LEU E  132  5                                   5    
HELIX   95  95 ASN E  133  LEU E  149  1                                  17    
HELIX   96  96 SER E  150  ASN E  179  1                                  30    
HELIX   97  97 VAL E  188  GLY E  206  1                                  19    
HELIX   98  98 SER E  217  PHE E  239  1                                  23    
HELIX   99  99 PRO E  241  SER E  249  1                                   9    
HELIX  100 100 SER E  249  ASN E  281  1                                  33    
HELIX  101 101 GLY E  288  ALA E  297  1                                  10    
HELIX  102 102 SER E  300  SER E  315  1                                  16    
HELIX  103 103 VAL E  316  ASN E  333  1                                  18    
HELIX  104 104 ASN E  333  HIS E  354  1                                  22    
HELIX  105 105 LYS E  357  LEU E  362  1                                   6    
HELIX  106 106 LEU E  362  TYR E  376  1                                  15    
HELIX  107 107 LEU E  407  GLY E  411  1                                   5    
HELIX  108 108 ASN E  424  LEU E  429  5                                   6    
HELIX  109 109 PHE E  445  GLN E  449  5                                   5    
HELIX  110 110 GLY E  452  HIS E  470  1                                  19    
HELIX  111 111 PRO F   37  MET F   41  5                                   5    
HELIX  112 112 ASN F   47  GLN F   59  1                                  13    
HELIX  113 113 HIS F   63  GLY F   76  1                                  14    
HELIX  114 114 LEU F   93  VAL F  103  1                                  11    
HELIX  115 115 LEU F  113  ARG F  123  1                                  11    
HELIX  116 116 ASN F  133  ARG F  143  1                                  11    
HELIX  117 117 LEU F  144  LEU F  149  1                                   6    
HELIX  118 118 SER F  150  ASN F  179  1                                  30    
HELIX  119 119 VAL F  188  GLY F  206  1                                  19    
HELIX  120 120 SER F  217  PHE F  239  1                                  23    
HELIX  121 121 PRO F  241  SER F  249  1                                   9    
HELIX  122 122 SER F  249  ASN F  281  1                                  33    
HELIX  123 123 GLY F  288  ALA F  297  1                                  10    
HELIX  124 124 SER F  300  SER F  315  1                                  16    
HELIX  125 125 VAL F  316  ASN F  333  1                                  18    
HELIX  126 126 ASN F  333  HIS F  354  1                                  22    
HELIX  127 127 LYS F  357  LEU F  362  1                                   6    
HELIX  128 128 LEU F  362  TYR F  376  1                                  15    
HELIX  129 129 LEU F  407  GLY F  411  1                                   5    
HELIX  130 130 ASN F  424  LEU F  429  5                                   6    
HELIX  131 131 PHE F  445  GLN F  449  5                                   5    
HELIX  132 132 GLY F  452  HIS F  470  1                                  19    
HELIX  133 133 PRO G   37  MET G   41  5                                   5    
HELIX  134 134 ASN G   47  GLN G   59  1                                  13    
HELIX  135 135 HIS G   63  GLY G   76  1                                  14    
HELIX  136 136 LEU G   93  GLN G  102  1                                  10    
HELIX  137 137 LEU G  113  ARG G  123  1                                  11    
HELIX  138 138 GLY G  128  LEU G  132  5                                   5    
HELIX  139 139 ASN G  133  LEU G  149  1                                  17    
HELIX  140 140 SER G  150  LEU G  177  1                                  28    
HELIX  141 141 VAL G  188  GLY G  206  1                                  19    
HELIX  142 142 SER G  217  PHE G  239  1                                  23    
HELIX  143 143 PRO G  241  SER G  249  1                                   9    
HELIX  144 144 SER G  249  ASN G  281  1                                  33    
HELIX  145 145 GLY G  288  ALA G  297  1                                  10    
HELIX  146 146 SER G  300  SER G  315  1                                  16    
HELIX  147 147 VAL G  316  ASN G  333  1                                  18    
HELIX  148 148 ASN G  333  HIS G  354  1                                  22    
HELIX  149 149 PRO G  355  THR G  360  5                                   6    
HELIX  150 150 LEU G  362  TYR G  376  1                                  15    
HELIX  151 151 LEU G  407  GLY G  411  1                                   5    
HELIX  152 152 ASN G  424  LEU G  429  5                                   6    
HELIX  153 153 PHE G  445  GLN G  449  5                                   5    
HELIX  154 154 GLY G  452  HIS G  470  1                                  19    
HELIX  155 155 PRO H   37  MET H   41  5                                   5    
HELIX  156 156 ASN H   47  GLN H   59  1                                  13    
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  128  LEU H  132  5                                   5    
HELIX  161 161 ASN H  133  LEU H  149  1                                  17    
HELIX  162 162 SER H  150  GLN H  178  1                                  29    
HELIX  163 163 VAL H  188  GLY H  206  1                                  19    
HELIX  164 164 SER H  217  GLN H  236  1                                  20    
HELIX  165 165 PRO H  241  SER H  249  1                                   9    
HELIX  166 166 SER H  249  ASN H  281  1                                  33    
HELIX  167 167 GLY H  288  ALA H  297  1                                  10    
HELIX  168 168 SER H  300  SER H  315  1                                  16    
HELIX  169 169 VAL H  316  ASN H  333  1                                  18    
HELIX  170 170 ASN H  333  HIS H  354  1                                  22    
HELIX  171 171 LYS H  357  LEU H  362  1                                   6    
HELIX  172 172 LEU H  362  TYR H  376  1                                  15    
HELIX  173 173 LEU H  407  ARG H  412  1                                   6    
HELIX  174 174 ASN H  424  LEU H  429  5                                   6    
HELIX  175 175 PHE H  445  GLN H  449  5                                   5    
HELIX  176 176 GLY H  452  HIS H  470  1                                  19    
HELIX  177 177 PRO I   37  MET I   41  5                                   5    
HELIX  178 178 ASN I   47  GLN I   59  1                                  13    
HELIX  179 179 HIS I   63  PHE I   72  1                                  10    
HELIX  180 180 LEU I   93  VAL I  103  1                                  11    
HELIX  181 181 LEU I  113  GLY I  124  1                                  12    
HELIX  182 182 ASN I  133  ARG I  143  1                                  11    
HELIX  183 183 LEU I  144  LEU I  149  1                                   6    
HELIX  184 184 SER I  150  ASN I  179  1                                  30    
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  ASN I  281  1                                  33    
HELIX  189 189 GLY I  288  ALA I  297  1                                  10    
HELIX  190 190 SER I  300  SER I  315  1                                  16    
HELIX  191 191 VAL I  316  ASN I  333  1                                  18    
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  GLY J   76  1                                  14    
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  ARG J  143  1                                  11    
HELIX  208 208 LEU J  144  LEU J  149  1                                   6    
HELIX  209 209 SER J  150  ASN J  179  1                                  30    
HELIX  210 210 VAL J  188  GLY J  206  1                                  19    
HELIX  211 211 SER J  217  PHE J  239  1                                  23    
HELIX  212 212 PRO J  241  SER J  249  1                                   9    
HELIX  213 213 SER J  249  ASN J  281  1                                  33    
HELIX  214 214 GLY J  288  ALA J  297  1                                  10    
HELIX  215 215 SER J  300  SER J  315  1                                  16    
HELIX  216 216 VAL J  316  ASN J  333  1                                  18    
HELIX  217 217 ASN J  333  HIS J  354  1                                  22    
HELIX  218 218 LYS J  357  LEU J  362  1                                   6    
HELIX  219 219 LEU J  362  TYR J  376  1                                  15    
HELIX  220 220 LEU J  407  ASN J  413  1                                   7    
HELIX  221 221 ASN J  424  ASP J  430  5                                   7    
HELIX  222 222 PHE J  445  GLN J  449  5                                   5    
HELIX  223 223 GLY J  452  HIS J  470  1                                  19    
HELIX  224 224 PRO K   37  MET K   41  5                                   5    
HELIX  225 225 ASN K   47  GLN K   59  1                                  13    
HELIX  226 226 HIS K   63  GLY K   76  1                                  14    
HELIX  227 227 LEU K   93  VAL K  103  1                                  11    
HELIX  228 228 LEU K  113  GLY K  124  1                                  12    
HELIX  229 229 GLY K  134  ARG K  143  1                                  10    
HELIX  230 230 LEU K  144  LEU K  149  1                                   6    
HELIX  231 231 SER K  150  LEU K  177  1                                  28    
HELIX  232 232 VAL K  188  GLY K  206  1                                  19    
HELIX  233 233 SER K  217  PHE K  239  1                                  23    
HELIX  234 234 PRO K  241  SER K  249  1                                   9    
HELIX  235 235 SER K  249  ALA K  279  1                                  31    
HELIX  236 236 GLY K  288  ALA K  297  1                                  10    
HELIX  237 237 SER K  300  SER K  315  1                                  16    
HELIX  238 238 VAL K  316  ASN K  333  1                                  18    
HELIX  239 239 ASN K  333  ALA K  346  1                                  14    
HELIX  240 240 ALA K  347  HIS K  354  1                                   8    
HELIX  241 241 PRO K  355  THR K  360  5                                   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 ASN K  424  TRP K  428  5                                   5    
HELIX  245 245 PHE K  445  GLN K  449  5                                   5    
HELIX  246 246 GLY K  452  HIS K  470  1                                  19    
HELIX  247 247 PRO L   37  MET L   41  5                                   5    
HELIX  248 248 TRP L   49  GLN L   59  1                                  11    
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  GLN L  178  1                                  29    
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 LYS L  357  LEU L  362  1                                   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  LEU L  429  5                                   6    
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  ARG A  80  0                                        
SHEET    2   A 4 MET A  88  VAL A  91 -1  O  CYS A  90   N  PHE A  79           
SHEET    3   A 4 LEU A 402  PHE A 406  1  O  LEU A 402   N  VAL A  89           
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  LEU D 497   N  LEU D 186           
SHEET    3   N 3 PHE D 471  GLU D 474 -1  N  LEU D 472   O  ARG D 500           
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  GLN E 404   N  VAL E  89           
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  ARG F  80  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  LEU F 402   N  VAL F  89           
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  LEU F 392  0                                        
SHEET    2   W 2 TYR F 395  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  TYR G  81  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  GLN G 404   N  VAL G  89           
SHEET    4   Y 4 PHE G 381  VAL G 385 -1  N  ARG G 384   O  VAL G 403           
SHEET    1   Z 3 SER G 183  LEU G 186  0                                        
SHEET    2   Z 3 LEU G 497  ALA G 501 -1  O  PHE G 499   N  LEU G 184           
SHEET    3   Z 3 PHE G 471  GLU G 474 -1  N  GLU G 474   O  THR G 498           
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  TYR H  81  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  89           
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  TYR I  81  0                                        
SHEET    2  AG 4 MET I  88  VAL I  91 -1  O  CYS I  90   N  PHE I  79           
SHEET    3  AG 4 LEU I 402  PHE I 406  1  O  LEU I 402   N  VAL I  89           
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  PHE I 499   N  LEU I 184           
SHEET    3  AH 3 PHE I 471  GLU I 474 -1  N  GLU I 474   O  THR I 498           
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  TYR J  81  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  PHE J 499   N  LEU J 184           
SHEET    3  AL 3 PHE J 471  GLU J 474 -1  N  GLU J 474   O  THR J 498           
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  ASN K  82  0                                        
SHEET    2  AO 4 ARG K  87  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  ARG K  87           
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  GLN L 404   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 G 450                FE   HEM G 601     1555   1555  2.24  
LINK         SG  CYS A 450                FE   HEM A 601     1555   1555  2.25  
LINK         SG  CYS F 450                FE   HEM F 601     1555   1555  2.25  
LINK         SG  CYS H 450                FE   HEM H 601     1555   1555  2.26  
LINK         SG  CYS I 450                FE   HEM I 601     1555   1555  2.31  
LINK         SG  CYS E 450                FE   HEM E 601     1555   1555  2.32  
LINK         SG  CYS D 450                FE   HEM D 601     1555   1555  2.32  
LINK         SG  CYS C 450                FE   HEM C 601     1555   1555  2.34  
LINK         SG  CYS L 450                FE   HEM L 601     1555   1555  2.37  
LINK         SG  CYS B 450                FE   HEM B 601     1555   1555  2.38  
LINK         SG  CYS K 450                FE   HEM K 601     1555   1555  2.47  
LINK         SG  CYS J 450                FE   HEM J 601     1555   1555  2.52  
SITE     1 AC1 17 ARG A 110  TRP A 137  ARG A 141  LEU A 311                    
SITE     2 AC1 17 GLY A 314  SER A 315  THR A 318  LEU A 382                    
SITE     3 AC1 17 ARG A 384  PRO A 442  PHE A 443  GLY A 444                    
SITE     4 AC1 17 PHE A 445  ARG A 448  CYS A 450  GLY A 452                    
SITE     5 AC1 17 1CA A 602                                                     
SITE     1 AC2  7 GLU A 310  GLY A 314  GLY A 379  PHE A 381                    
SITE     2 AC2  7 PHE A 487  ILE A 488  HEM A 601                               
SITE     1 AC3  4 ARG A 366  ARG A 453  ARG A 454  HOH A 728                    
SITE     1 AC4 16 ARG B 110  VAL B 129  TRP B 137  ARG B 141                    
SITE     2 AC4 16 GLY B 314  SER B 315  THR B 318  LEU B 382                    
SITE     3 AC4 16 ARG B 384  PRO B 442  PHE B 443  GLY B 444                    
SITE     4 AC4 16 PHE B 445  ARG B 448  CYS B 450  1CA B 602                    
SITE     1 AC5  8 TRP B 116  PHE B 130  GLU B 310  GLY B 314                    
SITE     2 AC5  8 GLY B 379  PHE B 381  PHE B 487  HEM B 601                    
SITE     1 AC6  3 ARG B 366  ARG B 453  ARG B 454                               
SITE     1 AC7 20 ARG C 110  VAL C 129  TRP C 137  ARG C 141                    
SITE     2 AC7 20 LEU C 311  GLY C 314  SER C 315  THR C 318                    
SITE     3 AC7 20 THR C 319  LEU C 382  ARG C 384  PRO C 442                    
SITE     4 AC7 20 PHE C 443  GLY C 444  PHE C 445  ARG C 448                    
SITE     5 AC7 20 CYS C 450  LEU C 451  GLY C 452  1CA C 602                    
SITE     1 AC8  6 TRP C 116  GLU C 310  GLY C 379  PHE C 381                    
SITE     2 AC8  6 PHE C 487  HEM C 601                                          
SITE     1 AC9  3 ARG C 366  ARG C 453  ARG C 454                               
SITE     1 BC1 19 ARG D 110  TRP D 137  ARG D 141  LEU D 311                    
SITE     2 BC1 19 GLY D 314  SER D 315  THR D 318  THR D 319                    
SITE     3 BC1 19 VAL D 378  ARG D 384  PRO D 442  PHE D 443                    
SITE     4 BC1 19 GLY D 444  PHE D 445  ARG D 448  CYS D 450                    
SITE     5 BC1 19 GLY D 452  1CA D 602  HOH D 713                               
SITE     1 BC2  8 TRP D 116  PHE D 130  GLU D 310  GLY D 379                    
SITE     2 BC2  8 PHE D 381  PHE D 487  HEM D 601  HOH D 713                    
SITE     1 BC3  3 ARG D 366  ARG D 453  ARG D 454                               
SITE     1 BC4 18 ARG E 110  VAL E 129  TRP E 137  ARG E 141                    
SITE     2 BC4 18 LEU E 311  SER E 315  THR E 318  VAL E 378                    
SITE     3 BC4 18 LEU E 382  ARG E 384  PRO E 442  PHE E 443                    
SITE     4 BC4 18 GLY E 444  PHE E 445  ARG E 448  CYS E 450                    
SITE     5 BC4 18 GLY E 452  1CA E 602                                          
SITE     1 BC5  7 TRP E 116  PHE E 130  GLU E 310  GLY E 379                    
SITE     2 BC5  7 PHE E 381  PHE E 487  HEM E 601                               
SITE     1 BC6  3 ARG E 366  ARG E 453  ARG E 454                               
SITE     1 BC7 20 ARG F 110  VAL F 129  TRP F 137  ARG F 141                    
SITE     2 BC7 20 GLU F 310  LEU F 311  GLY F 314  SER F 315                    
SITE     3 BC7 20 THR F 318  LEU F 382  ARG F 384  PRO F 442                    
SITE     4 BC7 20 PHE F 443  GLY F 444  PHE F 445  ARG F 448                    
SITE     5 BC7 20 GLN F 449  CYS F 450  GLY F 452  1CA F 602                    
SITE     1 BC8  7 TRP F 116  PHE F 130  GLU F 310  GLY F 379                    
SITE     2 BC8  7 PHE F 381  PHE F 487  HEM F 601                               
SITE     1 BC9  3 ARG F 366  ARG F 453  ARG F 454                               
SITE     1 CC1 18 ARG G 110  VAL G 129  TRP G 137  ARG G 141                    
SITE     2 CC1 18 LEU G 311  SER G 315  THR G 318  LEU G 382                    
SITE     3 CC1 18 ARG G 384  PRO G 442  PHE G 443  GLY G 444                    
SITE     4 CC1 18 PHE G 445  ARG G 448  CYS G 450  GLY G 452                    
SITE     5 CC1 18 1CA G 602  HOH G 716                                          
SITE     1 CC2  9 TRP G 116  GLU G 310  GLY G 314  GLY G 379                    
SITE     2 CC2  9 PHE G 381  PHE G 487  ILE G 488  HEM G 601                    
SITE     3 CC2  9 HOH G 716                                                     
SITE     1 CC3  3 ARG G 366  ARG G 453  ARG G 454                               
SITE     1 CC4 19 ARG H 110  VAL H 129  PHE H 130  TRP H 137                    
SITE     2 CC4 19 ARG H 141  GLU H 310  GLY H 314  SER H 315                    
SITE     3 CC4 19 THR H 318  VAL H 378  LEU H 382  ARG H 384                    
SITE     4 CC4 19 PRO H 442  PHE H 443  GLY H 444  PHE H 445                    
SITE     5 CC4 19 ARG H 448  CYS H 450  1CA H 602                               
SITE     1 CC5  7 TRP H 116  PHE H 130  GLU H 310  GLY H 379                    
SITE     2 CC5  7 PHE H 381  PHE H 487  HEM H 601                               
SITE     1 CC6 17 ARG I 110  VAL I 129  TRP I 137  ARG I 141                    
SITE     2 CC6 17 GLY I 314  SER I 315  THR I 318  LEU I 382                    
SITE     3 CC6 17 ARG I 384  PRO I 442  PHE I 443  GLY I 444                    
SITE     4 CC6 17 PHE I 445  ARG I 448  CYS I 450  GLY I 452                    
SITE     5 CC6 17 1CA I 602                                                     
SITE     1 CC7  8 TRP I 116  PHE I 130  GLU I 310  GLY I 379                    
SITE     2 CC7  8 LEU I 380  PHE I 381  PHE I 487  HEM I 601                    
SITE     1 CC8 16 ARG J 110  VAL J 129  TRP J 137  ARG J 141                    
SITE     2 CC8 16 GLY J 314  SER J 315  THR J 318  LEU J 382                    
SITE     3 CC8 16 ARG J 384  PRO J 442  PHE J 443  GLY J 444                    
SITE     4 CC8 16 PHE J 445  ARG J 448  CYS J 450  1CA J 602                    
SITE     1 CC9  7 GLU J 310  GLY J 314  GLY J 379  LEU J 380                    
SITE     2 CC9  7 PHE J 381  PHE J 487  HEM J 601                               
SITE     1 DC1 20 ARG K 110  VAL K 129  TRP K 137  ARG K 141                    
SITE     2 DC1 20 SER K 315  THR K 318  VAL K 378  LEU K 382                    
SITE     3 DC1 20 ARG K 384  PRO K 442  PHE K 443  GLY K 444                    
SITE     4 DC1 20 PHE K 445  ARG K 448  GLN K 449  CYS K 450                    
SITE     5 DC1 20 LEU K 451  GLY K 452  1CA K 602  HOH K 704                    
SITE     1 DC2  9 ARG K 110  GLU K 310  GLY K 314  GLY K 379                    
SITE     2 DC2  9 PHE K 381  PHE K 487  ILE K 488  HEM K 601                    
SITE     3 DC2  9 HOH K 704                                                     
SITE     1 DC3  3 ARG K 366  ARG K 453  ARG K 454                               
SITE     1 DC4 17 ARG L 110  VAL L 129  TRP L 137  ARG L 141                    
SITE     2 DC4 17 SER L 315  THR L 318  VAL L 378  LEU L 382                    
SITE     3 DC4 17 ARG L 384  PRO L 442  PHE L 443  GLY L 444                    
SITE     4 DC4 17 PHE L 445  ARG L 448  CYS L 450  GLY L 452                    
SITE     5 DC4 17 1CA L 602                                                     
SITE     1 DC5 10 TRP L 116  PHE L 130  GLU L 310  GLY L 314                    
SITE     2 DC5 10 GLY L 379  PHE L 381  LEU L 382  PHE L 487                    
SITE     3 DC5 10 ILE L 488  HEM L 601                                          
SITE     1 DC6  3 ARG L 366  ARG L 453  ARG L 454                               
CRYST1  130.347  199.629  150.153  90.00 112.18  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      0.007672  0.000000  0.003128        0.00000                         
SCALE2      0.000000  0.005009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007192        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system