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Database: PDB
Entry: 2PCB
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HEADER    OXIDOREDUCTASE/ELECTRON TRANSPORT       14-APR-93   2PCB              
TITLE     CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ELECTRON TRANSFER              
TITLE    2 PARTNERS, CYTOCHROME C PEROXIDASE AND CYTOCHROME C                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C PEROXIDASE (CCP);                             
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CYTOCHROME C;                                              
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 ORGAN: HEART;                                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   8 ORGANISM_COMMON: HORSE;                                              
SOURCE   9 ORGANISM_TAXID: 9796;                                                
SOURCE  10 ORGAN: HEART                                                         
KEYWDS    OXIDOREDUCTASE/ELECTRON TRANSPORT                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.PELLETIER,J.KRAUT                                                   
REVDAT   2   24-FEB-09 2PCB    1       VERSN                                    
REVDAT   1   15-JUL-93 2PCB    0                                                
JRNL        AUTH   H.PELLETIER,J.KRAUT                                          
JRNL        TITL   CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ELECTRON              
JRNL        TITL 2 TRANSFER PARTNERS, CYTOCHROME C PEROXIDASE AND               
JRNL        TITL 3 CYTOCHROME C.                                                
JRNL        REF    SCIENCE                       V. 258  1748 1992              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   1334573                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.WANG,J.M.MAURO,S.L.EDWARDS,S.J.OATLEY,L.A.FISHEL,          
REMARK   1  AUTH 2 V.A.ASHFORD,N.-H.XUONG,J.KRAUT                               
REMARK   1  TITL   X-RAY STRUCTURES OF RECOMBINANT YEAST CYTOCHROME C           
REMARK   1  TITL 2 PEROXIDASE AND THREE HEME-CLEFT MUTANTS PREPARED             
REMARK   1  TITL 3 BY SITE-DIRECTED MUTAGENESIS                                 
REMARK   1  REF    BIOCHEMISTRY                  V.  29  7160 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.W.BUSHNELL,G.V.LOUIE,G.D.BRAYER                            
REMARK   1  TITL   HIGH-RESOLUTION THREE DIMENSIONAL STRUCTURE OF               
REMARK   1  TITL 2 HORSE HEART CYTOCHROME C                                     
REMARK   1  REF    J.MOL.BIOL.                   V. 214   585 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   T.L.POULOS,S.SHERIFF,A.J.HOWARD                              
REMARK   1  TITL   CO-CRYSTALS OF YEAST CYTOCHROME C PEROXIDASE AND             
REMARK   1  TITL 2 HORSE HEART CYTOCHROME C                                     
REMARK   1  REF    J.BIOL.CHEM.                  V. 262 13881 1987              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
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 SET) : 0.178                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 129                                     
REMARK   3   SOLVENT ATOMS            : 337                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  THE YEAST CCP USED HERE IS A             
REMARK   3  RECOMBINANT (CALLED CCP(MI) AND EXPRESSED IN E. COLI) WHICH         
REMARK   3  HAS A MET-ILE DIPEPTIDE FUSED TO THE N-TERMINUS. THIS MET-ILE       
REMARK   3  DIPEPTIDE WAS NOT INCLUDED IN THIS STRUCTURE DUE TO DISORDER.       
REMARK   3  AFTER FINAL REFINEMENT THERE WAS ADDITIONAL ELECTRON DENSITY        
REMARK   3  FOUND IN THE ASYMMETRIC UNIT WHICH HAS BEEN ATTRIBUTED TO A         
REMARK   3  PARTIALLY OCCUPIED SECOND CYTOCHROME C MOLECULE. THE                
REMARK   3  COORDINATES FOR A POSSIBLE SECOND CYTOCHROME C SITE HAVE NOT        
REMARK   3  BEEN INCLUDED IN THIS ENTRY. SEE REFERENCE 1 FOR DETAILS.           
REMARK   4                                                                      
REMARK   4 2PCB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.10000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.65000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      139.65000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.65000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       46.55000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.65000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      139.65000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.65000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       46.55000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       93.10000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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    -1                                                      
REMARK 465     ILE A     0                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     ILE C     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA A   176     O    HOH A   303              1.92            
REMARK 500   O    PHE B    82     O    HOH B   325              2.02            
REMARK 500   O    HOH A   313     O    HOH A   405              2.09            
REMARK 500   O    HOH C   603     O    HOH C   712              2.09            
REMARK 500   O    SER C   225     O    HOH C   441              2.10            
REMARK 500   N    LYS C    74     O    HOH C   725              2.13            
REMARK 500   O    LEU A   294     O    HOH A   361              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   444     O    HOH A   444     8665     1.51            
REMARK 500   O    HOH A   376     O    HOH C   607     6455     1.61            
REMARK 500   CA   ASP C   279     O    HOH B   466     8655     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 175   CG    HIS A 175   CD2     0.059                       
REMARK 500    GLY A 192   N     GLY A 192   CA      0.101                       
REMARK 500    SER C 104   CB    SER C 104   OG      0.081                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  14   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP A  18   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ASP A  18   CB  -  CG  -  OD2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    VAL A  22   CB  -  CA  -  C   ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ARG A  31   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    GLU A  32   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    ASP A  33   CB  -  CG  -  OD1 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ASP A  33   CB  -  CG  -  OD2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    TYR A  36   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    TYR A  36   CB  -  CG  -  CD1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    TYR A  39   CA  -  CB  -  CG  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ARG A  48   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  48   O   -  C   -  N   ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ASP A  61   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    PHE A  73   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    LYS A  74   N   -  CA  -  CB  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    LYS A  75   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    GLU A  98   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    ASP A 106   CB  -  CA  -  C   ANGL. DEV. =  12.0 DEGREES          
REMARK 500    VAL A 113   CA  -  CB  -  CG1 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    GLN A 120   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    THR A 138   CA  -  CB  -  CG2 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    GLY A 142   N   -  CA  -  C   ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLY A 152   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A 155   NH1 -  CZ  -  NH2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 155   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    GLN A 159   CA  -  CB  -  CG  ANGL. DEV. =  22.0 DEGREES          
REMARK 500    ARG A 160   CD  -  NE  -  CZ  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG A 160   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    LEU A 161   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    MET A 163   CA  -  CB  -  CG  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ASN A 184   N   -  CA  -  CB  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    TYR A 187   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    GLY A 192   C   -  N   -  CA  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ASP A 210   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASN A 219   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES          
REMARK 500    ASN A 219   C   -  N   -  CA  ANGL. DEV. =  19.6 DEGREES          
REMARK 500    TRP A 223   CA  -  C   -  O   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ASP A 224   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TYR A 229   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    GLN A 240   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ASP A 241   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TYR A 251   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ASP A 279   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 279   CB  -  CG  -  OD2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    PHE A 286   CA  -  C   -  N   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    PHE A 286   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     125 ANGLE DEVIATIONS.                             
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    SER A   9      117.29   -167.46                                   
REMARK 500    LYS A  12      114.01    -20.62                                   
REMARK 500    ASP A  33       27.26    -71.77                                   
REMARK 500    ASP A  34       17.88    -68.61                                   
REMARK 500    TYR A  36      143.37    -37.72                                   
REMARK 500    TYR A  39       22.73     81.96                                   
REMARK 500    PHE A  99       73.73   -118.45                                   
REMARK 500    GLU A 135      -31.18    -24.76                                   
REMARK 500    LYS A 149     -168.58   -104.68                                   
REMARK 500    ALA A 151      -30.55    -39.92                                   
REMARK 500    ASN A 219       37.87     70.69                                   
REMARK 500    LEU A 232      162.36    -47.72                                   
REMARK 500    PRO A 277     -168.02    -44.93                                   
REMARK 500    GLU B   4      -70.85    -53.01                                   
REMARK 500    CYS B  14      -38.22   -139.44                                   
REMARK 500    ALA B  15      -14.05    -48.78                                   
REMARK 500    LYS B  27     -131.85   -100.99                                   
REMARK 500    LEU B  35      -78.20    -74.49                                   
REMARK 500    TYR B  48      172.70    -51.82                                   
REMARK 500    ASP B  50      -52.81    -29.19                                   
REMARK 500    GLU B  61      -85.49    -23.98                                   
REMARK 500    MET B  65      -31.71    -28.89                                   
REMARK 500    ILE B  75       95.11   -161.12                                   
REMARK 500    ALA B  96      -78.97    -52.24                                   
REMARK 500    LYS B 100      -95.99    -57.80                                   
REMARK 500    ALA B 101      -37.15    -27.02                                   
REMARK 500    ASN B 103      -57.88   -148.50                                   
REMARK 500    ASP C  33       52.35    -91.93                                   
REMARK 500    ASP C  34       -6.33    -59.55                                   
REMARK 500    TYR C  36      128.87    -38.99                                   
REMARK 500    LYS C  59       12.04    -63.22                                   
REMARK 500    LYS C  74      -75.39    -37.15                                   
REMARK 500    LYS C  75      -58.95    -27.45                                   
REMARK 500    LEU C  85      -23.19    -38.57                                   
REMARK 500    LYS C 149     -133.07   -106.02                                   
REMARK 500    ASN C 162       55.04     73.49                                   
REMARK 500    LYS C 183        2.30    -59.68                                   
REMARK 500    ASN C 195       45.41    -92.95                                   
REMARK 500    ASN C 196       20.16   -158.07                                   
REMARK 500    ASN C 216     -157.59   -110.92                                   
REMARK 500    ASN C 219       30.50     71.48                                   
REMARK 500    TYR C 229     -170.18    -62.60                                   
REMARK 500    MET C 230      138.60   -174.10                                   
REMARK 500    ASP C 254       87.30   -155.07                                   
REMARK 500    GLU C 291       -5.59    -59.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 127         0.09    SIDE_CHAIN                              
REMARK 500    ARG A 166         0.14    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 305        DISTANCE =  5.96 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  18   NE2                                                    
REMARK 620 2 MET B  80   SD  171.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 295  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 175   NE2                                                    
REMARK 620 2 HOH C 616   O   171.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 295                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 295                 
DBREF  2PCB A    1   294  UNP    P00431   CCPR_YEAST      68    361             
DBREF  2PCB B    1   104  UNP    P00004   CYC_HORSE        1    104             
DBREF  2PCB C    1   294  UNP    P00431   CCPR_YEAST      68    361             
SEQADV 2PCB ILE A   53  UNP  P00431    THR   120 CONFLICT                       
SEQADV 2PCB GLY A  152  UNP  P00431    ASP   219 CONFLICT                       
SEQADV 2PCB ILE C   53  UNP  P00431    THR   120 CONFLICT                       
SEQADV 2PCB GLY C  152  UNP  P00431    ASP   219 CONFLICT                       
SEQRES   1 A  296  MET ILE THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU          
SEQRES   2 A  296  LYS GLY ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN          
SEQRES   3 A  296  ALA ILE ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP          
SEQRES   4 A  296  ASN TYR ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA          
SEQRES   5 A  296  TRP HIS ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR          
SEQRES   6 A  296  GLY GLY SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU          
SEQRES   7 A  296  PHE ASN ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE          
SEQRES   8 A  296  LYS PHE LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE          
SEQRES   9 A  296  SER SER GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA          
SEQRES  10 A  296  VAL GLN GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS          
SEQRES  11 A  296  GLY ARG VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN          
SEQRES  12 A  296  GLY ARG LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL          
SEQRES  13 A  296  ARG THR PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU          
SEQRES  14 A  296  VAL VAL ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR          
SEQRES  15 A  296  HIS LEU LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA          
SEQRES  16 A  296  ALA ASN ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU          
SEQRES  17 A  296  LEU ASN GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN          
SEQRES  18 A  296  ASN GLU GLN TRP ASP SER LYS SER GLY TYR MET MET LEU          
SEQRES  19 A  296  PRO THR ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU          
SEQRES  20 A  296  SER ILE VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE          
SEQRES  21 A  296  PHE LYS ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU          
SEQRES  22 A  296  ASN GLY ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE          
SEQRES  23 A  296  ILE PHE LYS THR LEU GLU GLU GLN GLY LEU                      
SEQRES   1 B  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 B  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 B  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 B  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 B  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 B  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 B  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 B  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 C  296  MET ILE THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU          
SEQRES   2 C  296  LYS GLY ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN          
SEQRES   3 C  296  ALA ILE ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP          
SEQRES   4 C  296  ASN TYR ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA          
SEQRES   5 C  296  TRP HIS ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR          
SEQRES   6 C  296  GLY GLY SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU          
SEQRES   7 C  296  PHE ASN ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE          
SEQRES   8 C  296  LYS PHE LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE          
SEQRES   9 C  296  SER SER GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA          
SEQRES  10 C  296  VAL GLN GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS          
SEQRES  11 C  296  GLY ARG VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN          
SEQRES  12 C  296  GLY ARG LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL          
SEQRES  13 C  296  ARG THR PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU          
SEQRES  14 C  296  VAL VAL ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR          
SEQRES  15 C  296  HIS LEU LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA          
SEQRES  16 C  296  ALA ASN ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU          
SEQRES  17 C  296  LEU ASN GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN          
SEQRES  18 C  296  ASN GLU GLN TRP ASP SER LYS SER GLY TYR MET MET LEU          
SEQRES  19 C  296  PRO THR ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU          
SEQRES  20 C  296  SER ILE VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE          
SEQRES  21 C  296  PHE LYS ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU          
SEQRES  22 C  296  ASN GLY ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE          
SEQRES  23 C  296  ILE PHE LYS THR LEU GLU GLU GLN GLY LEU                      
HET    HEM  A 295      43                                                       
HET    HEM  B 105      43                                                       
HET    HEM  C 295      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   4  HEM    3(C34 H32 FE N4 O4)                                          
FORMUL   7  HOH   *337(H2 O)                                                    
HELIX    1   1 SER A   15  ASP A   33  1                                  19    
HELIX    2   2 GLU A   35  ILE A   40  1                                   6    
HELIX    3   3 TYR A   42  GLY A   55  1                                  14    
HELIX    4   4 GLY A   69  ARG A   72  5                                   4    
HELIX    5   5 PHE A   73  ASP A   79  1                                   7    
HELIX    6   6 PRO A   80  ALA A   83  5                                   4    
HELIX    7   7 GLY A   84  GLY A   84  5                                   1    
HELIX    8   8 LEU A   85  PHE A   99  1                                  15    
HELIX    9   9 SER A  103  MET A  119  1                                  17    
HELIX   10  10 PRO A  134  THR A  138  5                                   5    
HELIX   11  11 ASP A  150  ARG A  160  1                                  11    
HELIX   12  12 ASN A  164  GLY A  173  1                                  10    
HELIX   13  13 ALA A  174  LEU A  177  5                                   4    
HELIX   14  14 HIS A  181  GLY A  186  1                                   6    
HELIX   15  15 ASN A  200  GLU A  209  1                                  10    
HELIX   16  16 LEU A  232  LEU A  238  1                                   7    
HELIX   17  17 ASP A  241  ASP A  254  1                                  14    
HELIX   18  18 ASP A  254  ASN A  272  1                                  19    
HELIX   19  19 THR A  288  GLN A  292  5                                   5    
HELIX   20  20 VAL B    3  CYS B   14  1                                  12    
HELIX   21  21 THR B   49  ASN B   54  1                                   6    
HELIX   22  22 LYS B   60  LEU B   68  1                                   9    
HELIX   23  23 ASN B   70  ILE B   75  1                                   6    
HELIX   24  24 LYS B   88  THR B  102  1                                  15    
HELIX   25  25 SER C   15  ASP C   33  1                                  19    
HELIX   26  26 GLU C   35  ILE C   40  1                                   6    
HELIX   27  27 TYR C   42  GLY C   55  1                                  14    
HELIX   28  28 GLY C   69  ARG C   72  5                                   4    
HELIX   29  29 PHE C   73  ASN C   78  1                                   6    
HELIX   30  30 ASP C   79  ALA C   83  5                                   5    
HELIX   31  31 LEU C   85  GLU C   98  1                                  14    
HELIX   32  32 SER C  103  MET C  119  1                                  17    
HELIX   33  33 ASP C  150  ARG C  160  1                                  11    
HELIX   34  34 ASN C  164  MET C  172  1                                   9    
HELIX   35  35 GLY C  173  LEU C  177  5                                   5    
HELIX   36  36 HIS C  181  GLY C  186  1                                   6    
HELIX   37  37 ASN C  200  GLU C  209  1                                  10    
HELIX   38  38 LEU C  232  SER C  237  1                                   6    
HELIX   39  39 TYR C  236  ASP C  241  1                                   6    
HELIX   40  40 ASP C  241  ASP C  254  1                                  14    
HELIX   41  41 ASP C  254  ASN C  272  1                                  19    
HELIX   42  42 THR C  288  GLY C  293  1                                   6    
SHEET    1   A 2 HIS A   6  VAL A   7  0                                        
SHEET    2   A 2 ILE A 274  THR A 275  1  N  THR A 275   O  HIS A   6           
SHEET    1   B 2 LYS A 179  THR A 180  0                                        
SHEET    2   B 2 GLY A 189  PRO A 190 -1  O  GLY A 189   N  THR A 180           
SHEET    1   C 3 LYS A 212  LYS A 215  0                                        
SHEET    2   C 3 GLU A 221  ASP A 224 -1  N  GLN A 222   O  GLU A 214           
SHEET    3   C 3 MET A 230  MET A 231 -1  O  MET A 231   N  TRP A 223           
SHEET    1   D 3 TRP C 211  LYS C 215  0                                        
SHEET    2   D 3 GLU C 221  SER C 225 -1  N  GLN C 222   O  GLU C 214           
SHEET    3   D 3 MET C 230  MET C 231 -1  O  MET C 231   N  TRP C 223           
LINK         NE2 HIS A 175                FE   HEM A 295     1555   1555  1.94  
LINK        FE   HEM B 105                 NE2 HIS B  18     1555   1555  2.14  
LINK        FE   HEM B 105                 SD  MET B  80     1555   1555  2.33  
LINK        FE   HEM C 295                 NE2 HIS C 175     1555   1555  2.14  
LINK        FE   HEM C 295                 O   HOH C 616     1555   1555  2.49  
SITE     1 AC1 21 PRO A  44  ARG A  48  TRP A  51  PRO A 145                    
SITE     2 AC1 21 ASP A 146  MET A 172  ALA A 174  HIS A 175                    
SITE     3 AC1 21 LEU A 177  GLY A 178  LYS A 179  THR A 180                    
SITE     4 AC1 21 HIS A 181  ASN A 184  SER A 185  TRP A 191                    
SITE     5 AC1 21 LEU A 232  THR A 234  PHE A 266  HOH A 364                    
SITE     6 AC1 21 HOH A 397                                                     
SITE     1 AC2 18 LYS B  13  CYS B  14  CYS B  17  HIS B  18                    
SITE     2 AC2 18 THR B  28  LYS B  39  THR B  40  GLY B  41                    
SITE     3 AC2 18 PHE B  46  TYR B  48  THR B  49  ASN B  52                    
SITE     4 AC2 18 TRP B  59  TYR B  67  THR B  78  LYS B  79                    
SITE     5 AC2 18 MET B  80  PHE B  82                                          
SITE     1 AC3 22 PRO C  44  VAL C  47  ARG C  48  TRP C  51                    
SITE     2 AC3 22 ASP C 146  PHE C 158  MET C 172  ALA C 174                    
SITE     3 AC3 22 HIS C 175  LEU C 177  GLY C 178  LYS C 179                    
SITE     4 AC3 22 THR C 180  HIS C 181  ASN C 184  SER C 185                    
SITE     5 AC3 22 TRP C 191  THR C 234  HOH C 603  HOH C 606                    
SITE     6 AC3 22 HOH C 610  HOH C 616                                          
CRYST1  105.300  105.300  186.200  90.00  90.00  90.00 P 43 21 2    16          
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      0.009497  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005371        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system