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Database: PDB
Entry: 5PRC
LinkDB: 5PRC
Original site: 5PRC 
HEADER    PHOTOSYNTHETIC REACTION CENTER          01-AUG-97   5PRC              
TITLE     PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS (ATRAZINE
TITLE    2 COMPLEX)                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;                            
COMPND   3 CHAIN: C;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;                            
COMPND   6 CHAIN: L;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;                            
COMPND   9 CHAIN: M;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;                            
COMPND  12 CHAIN: H                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;                          
SOURCE   3 ORGANISM_TAXID: 1079;                                                
SOURCE   4 ATCC: DSM 133;                                                       
SOURCE   5 COLLECTION: DSM 133;                                                 
SOURCE   6 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM);                  
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;                          
SOURCE   9 ORGANISM_TAXID: 1079;                                                
SOURCE  10 COLLECTION: DSM 133;                                                 
SOURCE  11 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM);                  
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;                          
SOURCE  14 ORGANISM_TAXID: 1079;                                                
SOURCE  15 COLLECTION: DSM 133;                                                 
SOURCE  16 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM);                  
SOURCE  17 MOL_ID: 4;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;                          
SOURCE  19 ORGANISM_TAXID: 1079;                                                
SOURCE  20 COLLECTION: DSM 133;                                                 
SOURCE  21 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM)                   
KEYWDS    PHOTOSYNTHETIC REACTION CENTER, SECONDARY QUINONE (QB), TRIAZINE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.D.LANCASTER,H.MICHEL                                              
REVDAT   6   09-AUG-23 5PRC    1       REMARK LINK                              
REVDAT   5   16-NOV-11 5PRC    1       HETATM                                   
REVDAT   4   13-JUL-11 5PRC    1       VERSN                                    
REVDAT   3   31-MAR-09 5PRC    1       HETNAM                                   
REVDAT   2   24-FEB-09 5PRC    1       VERSN                                    
REVDAT   1   06-APR-99 5PRC    0                                                
JRNL        AUTH   C.R.LANCASTER,H.MICHEL                                       
JRNL        TITL   REFINED CRYSTAL STRUCTURES OF REACTION CENTRES FROM          
JRNL        TITL 2 RHODOPSEUDOMONAS VIRIDIS IN COMPLEXES WITH THE HERBICIDE     
JRNL        TITL 3 ATRAZINE AND TWO CHIRAL ATRAZINE DERIVATIVES ALSO LEAD TO A  
JRNL        TITL 4 NEW MODEL OF THE BOUND CAROTENOID.                           
JRNL        REF    J.MOL.BIOL.                   V. 286   883 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10024457                                                     
JRNL        DOI    10.1006/JMBI.1998.2532                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.R.D.LANCASTER                                              
REMARK   1  TITL   UBIQUINONE REDUCTION AND PROTONATION IN THE REACTION CENTRE  
REMARK   1  TITL 2 OF RHODOPSEUDOMONAS VIRIDIS: X-RAY STRUCTURES AND THEIR      
REMARK   1  TITL 3 FUNCTIONAL IMPLICATIONS                                      
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1365   143 1998              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.R.LANCASTER,H.MICHEL                                       
REMARK   1  TITL   THE COUPLING OF LIGHT-INDUCED ELECTRON TRANSFER AND PROTON   
REMARK   1  TITL 2 UPTAKE AS DERIVED FROM CRYSTAL STRUCTURES OF REACTION        
REMARK   1  TITL 3 CENTRES FROM RHODOPSEUDOMONAS VIRIDIS MODIFIED AT THE        
REMARK   1  TITL 4 BINDING SITE OF THE SECONDARY QUINONE, QB                    
REMARK   1  REF    STRUCTURE                     V.   5  1339 1997              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.DEISENHOFER,O.EPP,I.SINNING,H.MICHEL                       
REMARK   1  TITL   CRYSTALLOGRAPHIC REFINEMENT AT 2.3 A RESOLUTION AND REFINED  
REMARK   1  TITL 2 MODEL OF THE PHOTOSYNTHETIC REACTION CENTRE FROM             
REMARK   1  TITL 3 RHODOPSEUDOMONAS VIRIDIS                                     
REMARK   1  REF    J.MOL.BIOL.                   V. 246   429 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.DEISENHOFER,H.MICHEL                                       
REMARK   1  TITL   THE PHOTOSYNTHETIC REACTION CENTER FROM THE PURPLE BACTERIUM 
REMARK   1  TITL 2 RHODOPSEUDOMONAS VIRIDIS                                     
REMARK   1  REF    SCIENCE                       V. 245  1463 1989              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   J.DEISENHOFER,O.EPP,K.MIKI,R.HUBER,H.MICHEL                  
REMARK   1  TITL   STRUCTURE OF THE PROTEIN SUBUNITS IN THE PHOTOSYNTHETIC      
REMARK   1  TITL 2 REACTION CENTRE OF RHODOPSEUDOMONAS VIRIDIS AT 3 ANGSTROMS   
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    NATURE                        V. 318   618 1985              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   J.DEISENHOFER,O.EPP,K.MIKI,R.HUBER,H.MICHEL                  
REMARK   1  TITL   X-RAY STRUCTURE ANALYSIS OF A MEMBRANE PROTEIN COMPLEX.      
REMARK   1  TITL 2 ELECTRON DENSITY MAP AT 3 A RESOLUTION AND A MODEL OF THE    
REMARK   1  TITL 3 CHROMOPHORES OF THE PHOTOSYNTHETIC REACTION CENTER FROM      
REMARK   1  TITL 4 RHODOPSEUDOMONAS VIRIDIS                                     
REMARK   1  REF    J.MOL.BIOL.                   V. 180   385 1984              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   H.MICHEL                                                     
REMARK   1  TITL   THREE-DIMENSIONAL CRYSTALS OF A MEMBRANE PROTEIN COMPLEX.    
REMARK   1  TITL 2 THE PHOTOSYNTHETIC REACTION CENTRE FROM RHODOPSEUDOMONAS     
REMARK   1  TITL 3 VIRIDIS                                                      
REMARK   1  REF    J.MOL.BIOL.                   V. 158   567 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
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)   (%) : 78.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 92322                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : A POSTERIORI                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 9237                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 57.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7493                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 854                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9342                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 785                                     
REMARK   3   SOLVENT ATOMS            : 343                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.40                          
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) : 0.26                            
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.220                           
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) : 1.500 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 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  : PARHCSDX_TEST.PRO                              
REMARK   3  PARAMETER FILE  2  : PARAM19.ION                                    
REMARK   3  PARAMETER FILE  3  : PARHCSDX_IUB.RCV                               
REMARK   3  PARAMETER FILE  4  : PARAM19.SOL, PARHCSDX.TRZ                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.ION                                     
REMARK   3  TOPOLOGY FILE  3   : TOPHCSDX_IUB.RCV                               
REMARK   3  TOPOLOGY FILE  4   : TOPH19.SOL, TOPHCSDX.TRZ                       
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: N(OBS)/N(PAR) = 2.20                      
REMARK   4                                                                      
REMARK   4 5PRC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000179759.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : SEP-93                             
REMARK 200  TEMPERATURE           (KELVIN) : 263                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 6                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (ROTAVATA, AGROVATA           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96950                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 76.2                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 48.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.28200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER / SA      
REMARK 200  OMIT MAPS                                                           
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 6PRC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0                                   
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       56.80000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000      111.75000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      111.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       85.20000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      111.75000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000      111.75000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.40000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      111.75000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      111.75000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       85.20000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000      111.75000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      111.75000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       28.40000            
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       56.80000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 49460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -417.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, L, M, H                            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH H1094  LIES ON A SPECIAL POSITION.                          
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     ALA C   333                                                      
REMARK 465     ALA C   334                                                      
REMARK 465     ALA C   335                                                      
REMARK 465     LYS C   336                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS C 332    CG   CD   CE   NZ                                   
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     PRO H    46                                                      
REMARK 475     LEU H    47                                                      
REMARK 475     GLY H    48                                                      
REMARK 475     LEU H    49                                                      
REMARK 475     VAL H    50                                                      
REMARK 475     LYS H    51                                                      
REMARK 475     LEU H    52                                                      
REMARK 475     ALA H    53                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS C   32   CD   CE   NZ                                        
REMARK 480     LYS C   46   CD   CE   NZ                                        
REMARK 480     GLU C   48   CG   CD   OE1  OE2                                  
REMARK 480     GLN C   54   CD   OE1  NE2                                       
REMARK 480     LYS C   57   CD   CE   NZ                                        
REMARK 480     LYS C   60   CD   CE   NZ                                        
REMARK 480     ASN C   64   OD1  ND2                                            
REMARK 480     GLU C   93   CD   OE1  OE2                                       
REMARK 480     ASN C   94   OD1  ND2                                            
REMARK 480     GLN C  127   CD   OE1  NE2                                       
REMARK 480     THR C  159   CB   OG1  CG2                                       
REMARK 480     ARG C  165   NH1  NH2                                            
REMARK 480     ARG C  169   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS C  198   CD   CE   NZ                                        
REMARK 480     ARG C  199   CZ   NH1  NH2                                       
REMARK 480     LYS C  218   CD   CE   NZ                                        
REMARK 480     LYS C  323   CE   NZ                                             
REMARK 480     ILE L   17   CD1                                                 
REMARK 480     PRO L   57   O                                                   
REMARK 480     LYS L   72   CE   NZ                                             
REMARK 480     ASP L  202   OD1  OD2                                            
REMARK 480     LYS L  205   CD   CE   NZ                                        
REMARK 480     ILE L  269   CD1                                                 
REMARK 480     PHE L  271   CD1  CD2  CE1  CE2  CZ                              
REMARK 480     GLU M   22   CD   OE1  OE2                                       
REMARK 480     ASP M   25   OD1  OD2                                            
REMARK 480     ASN M   26   OD1  ND2                                            
REMARK 480     LYS M   31   CG   CD   CE   NZ                                   
REMARK 480     ILE M  104   CD1                                                 
REMARK 480     ARG M  136   NH1  NH2                                            
REMARK 480     LYS M  298   NZ                                                  
REMARK 480     LYS M  323   CG   CD   CE   NZ                                   
REMARK 480     GLN H    8   CB   CG   CD   OE1  NE2                             
REMARK 480     HIS H    9   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLU H   45   C    O    CG   CD   OE1  OE2                        
REMARK 480     GLU H   55   CD   OE1  OE2                                       
REMARK 480     ARG H   81   CD   NE   CZ   NH1  NH2                             
REMARK 480     THR H   85   CB   OG1  CG2                                       
REMARK 480     GLU H   87   CG   CD   OE1  OE2                                  
REMARK 480     LYS H   89   CD   CE   NZ                                        
REMARK 480     GLN H   92   CD   OE1  NE2                                       
REMARK 480     ASP H   94   CB   CG   OD1  OD2                                  
REMARK 480     GLU H   97   OE1  OE2                                            
REMARK 480     LYS H  131   CE   NZ                                             
REMARK 480     GLU H  147   CG   CD   OE1  OE2                                  
REMARK 480     LYS H  205   CD   CE   NZ                                        
REMARK 480     LYS H  207   NZ                                                  
REMARK 480     GLU H  216   CD   OE1  OE2                                       
REMARK 480     ARG H  223   NH1  NH2                                            
REMARK 480     GLN H  225   OE1  NE2                                            
REMARK 480     ARG H  227   CG   CD   NE   CZ   NH1  NH2                        
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    LEU M 318   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ALA H  53   CB  -  CA  -  C   ANGL. DEV. = -15.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR C  38      107.94    -48.10                                   
REMARK 500    ALA C  43      140.70    -33.85                                   
REMARK 500    ASN C  58       47.99   -108.43                                   
REMARK 500    ALA C 126     -131.67     55.72                                   
REMARK 500    ASN C 186       43.15    -86.95                                   
REMARK 500    TRP C 256     -153.81   -111.82                                   
REMARK 500    LEU C 285        0.59    -65.24                                   
REMARK 500    ASP C 304     -154.92   -126.46                                   
REMARK 500    ASP L  23       79.16    -68.07                                   
REMARK 500    VAL L  31      -87.86    -93.85                                   
REMARK 500    LEU L 165      -59.70     62.36                                   
REMARK 500    ASP L 202     -126.33     42.11                                   
REMARK 500    LYS L 207     -157.66    -86.50                                   
REMARK 500    LEU M  51     -110.79    -71.99                                   
REMARK 500    CYS M 160      -60.01   -122.35                                   
REMARK 500    ASN M 193       96.12     82.04                                   
REMARK 500    ASP M 238       78.86   -153.19                                   
REMARK 500    ARG M 239      125.47    -35.72                                   
REMARK 500    PRO M 319      106.61    -54.59                                   
REMARK 500    PRO M 322     -171.34    -56.10                                   
REMARK 500    HIS H   9       36.14   -151.83                                   
REMARK 500    TYR H  31      -75.89    -99.94                                   
REMARK 500    PRO H  46     -173.96    -65.99                                   
REMARK 500    LEU H  52       -3.95   -141.65                                   
REMARK 500    PRO H  54       71.54    -65.76                                   
REMARK 500    ASP H  94     -144.03   -123.99                                   
REMARK 500    ASP H 142        4.26    -68.88                                   
REMARK 500    HIS H 178       62.45     62.78                                   
REMARK 500    ALA H 191       60.31   -113.04                                   
REMARK 500    SER H 256      124.96    -33.88                                   
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 C  15         0.09    SIDE CHAIN                              
REMARK 500    PHE C 190         0.08    SIDE CHAIN                              
REMARK 500    TYR C 227         0.10    SIDE CHAIN                              
REMARK 500    ARG C 272         0.08    SIDE CHAIN                              
REMARK 500    TYR C 325         0.06    SIDE CHAIN                              
REMARK 500    TYR L  51         0.13    SIDE CHAIN                              
REMARK 500    TYR L 148         0.07    SIDE CHAIN                              
REMARK 500    TYR L 164         0.07    SIDE CHAIN                              
REMARK 500    HIS L 230         0.10    SIDE CHAIN                              
REMARK 500    ARG M  28         0.08    SIDE CHAIN                              
REMARK 500    TYR M 208         0.06    SIDE CHAIN                              
REMARK 500    TYR H  18         0.10    SIDE CHAIN                              
REMARK 500    ARG H  34         0.08    SIDE CHAIN                              
REMARK 500    TYR H  64         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    TRP C 121        -10.87                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     LDA L   705                                                      
REMARK 615     BPB M   401                                                      
REMARK 615     NS5 M   600                                                      
REMARK 615     LDA M   706                                                      
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 C 337  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET C  74   SD                                                     
REMARK 620 2 HEM C 337   NA   89.0                                              
REMARK 620 3 HEM C 337   NB   92.2  90.9                                        
REMARK 620 4 HEM C 337   NC   93.3 177.3  90.3                                  
REMARK 620 5 HEM C 337   ND   86.7  88.5 178.8  90.3                            
REMARK 620 6 HIS C  91   NE2 175.4  90.5  92.4  87.1  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 338  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET C 110   SD                                                     
REMARK 620 2 HEM C 338   NA   88.4                                              
REMARK 620 3 HEM C 338   NB   88.0  94.6                                        
REMARK 620 4 HEM C 338   NC   91.3 179.7  85.3                                  
REMARK 620 5 HEM C 338   ND   88.7  89.0 174.9  91.0                            
REMARK 620 6 HIS C 136   NE2 175.8  87.4  92.1  92.9  91.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 340  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 124   NE2                                                    
REMARK 620 2 HEM C 340   NA   87.6                                              
REMARK 620 3 HEM C 340   NB   89.8  90.7                                        
REMARK 620 4 HEM C 340   NC   91.2 177.9  87.5                                  
REMARK 620 5 HEM C 340   ND   86.6  90.6 176.1  91.1                            
REMARK 620 6 HIS C 309   NE2 177.7  90.1  90.0  91.1  93.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 339  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET C 233   SD                                                     
REMARK 620 2 HEM C 339   NA   89.7                                              
REMARK 620 3 HEM C 339   NB   85.1  91.2                                        
REMARK 620 4 HEM C 339   NC   91.7 178.4  89.7                                  
REMARK 620 5 HEM C 339   ND   90.6  87.5 175.6  91.7                            
REMARK 620 6 HIS C 248   NE2 175.2  85.9  92.9  92.7  91.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCB L 304  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L 153   NE2                                                    
REMARK 620 2 BCB L 304   NA   97.7                                              
REMARK 620 3 BCB L 304   NB   98.4  90.6                                        
REMARK 620 4 BCB L 304   NC   93.3 168.5  91.3                                  
REMARK 620 5 BCB L 304   ND   96.2  87.6 165.5  87.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCB L 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L 173   NE2                                                    
REMARK 620 2 BCB L 302   NA   86.3                                              
REMARK 620 3 BCB L 302   NB   87.2  90.9                                        
REMARK 620 4 BCB L 302   NC  104.3 169.3  91.0                                  
REMARK 620 5 BCB L 302   ND   99.8  89.2 173.0  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 M 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L 190   NE2                                                    
REMARK 620 2 HIS L 230   NE2  87.2                                              
REMARK 620 3 HIS M 217   NE2 110.1  91.6                                        
REMARK 620 4 GLU M 232   OE2 148.1  81.7 100.0                                  
REMARK 620 5 GLU M 232   OE1  94.4  96.2 154.7  57.7                            
REMARK 620 6 HIS M 264   NE2  90.3 174.7  84.9 102.8  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCB M 805  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M 180   NE2                                                    
REMARK 620 2 BCB M 805   NA   93.4                                              
REMARK 620 3 BCB M 805   NB   98.8  89.4                                        
REMARK 620 4 BCB M 805   NC   99.2 167.1  91.1                                  
REMARK 620 5 BCB M 805   ND   94.6  89.5 166.6  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCB M 806  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M 200   NE2                                                    
REMARK 620 2 BCB M 806   NA   97.5                                              
REMARK 620 3 BCB M 806   NB   96.9  90.0                                        
REMARK 620 4 BCB M 806   NC   95.4 166.8  91.5                                  
REMARK 620 5 BCB M 806   ND   96.4  88.1 166.7  87.5                            
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 FE2 M 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB M 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB L 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB M 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB L 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPB M 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPB L 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQ7 M 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 338                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 339                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 340                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NS5 M 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATZ L 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA H 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA L 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA H 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA M 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA L 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA M 706                 
DBREF  5PRC C    1   336  UNP    P07173   CYCR_RHOVI      21    356             
DBREF  5PRC L    1   273  UNP    P06009   RCEL_RHOVI       1    273             
DBREF  5PRC M    1   323  UNP    P06010   RCEM_RHOVI       1    323             
DBREF  5PRC H    2   258  UNP    P06008   RCEH_RHOVI       2    258             
SEQRES   1 C  336  CYS PHE GLU PRO PRO PRO ALA THR THR THR GLN THR GLY          
SEQRES   2 C  336  PHE ARG GLY LEU SER MET GLY GLU VAL LEU HIS PRO ALA          
SEQRES   3 C  336  THR VAL LYS ALA LYS LYS GLU ARG ASP ALA GLN TYR PRO          
SEQRES   4 C  336  PRO ALA LEU ALA ALA VAL LYS ALA GLU GLY PRO PRO VAL          
SEQRES   5 C  336  SER GLN VAL TYR LYS ASN VAL LYS VAL LEU GLY ASN LEU          
SEQRES   6 C  336  THR GLU ALA GLU PHE LEU ARG THR MET THR ALA ILE THR          
SEQRES   7 C  336  GLU TRP VAL SER PRO GLN GLU GLY CYS THR TYR CYS HIS          
SEQRES   8 C  336  ASP GLU ASN ASN LEU ALA SER GLU ALA LYS TYR PRO TYR          
SEQRES   9 C  336  VAL VAL ALA ARG ARG MET LEU GLU MET THR ARG ALA ILE          
SEQRES  10 C  336  ASN THR ASN TRP THR GLN HIS VAL ALA GLN THR GLY VAL          
SEQRES  11 C  336  THR CYS TYR THR CYS HIS ARG GLY THR PRO LEU PRO PRO          
SEQRES  12 C  336  TYR VAL ARG TYR LEU GLU PRO THR LEU PRO LEU ASN ASN          
SEQRES  13 C  336  ARG GLU THR PRO THR HIS VAL GLU ARG VAL GLU THR ARG          
SEQRES  14 C  336  SER GLY TYR VAL VAL ARG LEU ALA LYS TYR THR ALA TYR          
SEQRES  15 C  336  SER ALA LEU ASN TYR ASP PRO PHE THR MET PHE LEU ALA          
SEQRES  16 C  336  ASN ASP LYS ARG GLN VAL ARG VAL VAL PRO GLN THR ALA          
SEQRES  17 C  336  LEU PRO LEU VAL GLY VAL SER ARG GLY LYS GLU ARG ARG          
SEQRES  18 C  336  PRO LEU SER ASP ALA TYR ALA THR PHE ALA LEU MET MET          
SEQRES  19 C  336  SER ILE SER ASP SER LEU GLY THR ASN CYS THR PHE CYS          
SEQRES  20 C  336  HIS ASN ALA GLN THR PHE GLU SER TRP GLY LYS LYS SER          
SEQRES  21 C  336  THR PRO GLN ARG ALA ILE ALA TRP TRP GLY ILE ARG MET          
SEQRES  22 C  336  VAL ARG ASP LEU ASN MET ASN TYR LEU ALA PRO LEU ASN          
SEQRES  23 C  336  ALA SER LEU PRO ALA SER ARG LEU GLY ARG GLN GLY GLU          
SEQRES  24 C  336  ALA PRO GLN ALA ASP CYS ARG THR CYS HIS GLN GLY VAL          
SEQRES  25 C  336  THR LYS PRO LEU PHE GLY ALA SER ARG LEU LYS ASP TYR          
SEQRES  26 C  336  PRO GLU LEU GLY PRO ILE LYS ALA ALA ALA LYS                  
SEQRES   1 L  273  ALA LEU LEU SER PHE GLU ARG LYS TYR ARG VAL ARG GLY          
SEQRES   2 L  273  GLY THR LEU ILE GLY GLY ASP LEU PHE ASP PHE TRP VAL          
SEQRES   3 L  273  GLY PRO TYR PHE VAL GLY PHE PHE GLY VAL SER ALA ILE          
SEQRES   4 L  273  PHE PHE ILE PHE LEU GLY VAL SER LEU ILE GLY TYR ALA          
SEQRES   5 L  273  ALA SER GLN GLY PRO THR TRP ASP PRO PHE ALA ILE SER          
SEQRES   6 L  273  ILE ASN PRO PRO ASP LEU LYS TYR GLY LEU GLY ALA ALA          
SEQRES   7 L  273  PRO LEU LEU GLU GLY GLY PHE TRP GLN ALA ILE THR VAL          
SEQRES   8 L  273  CYS ALA LEU GLY ALA PHE ILE SER TRP MET LEU ARG GLU          
SEQRES   9 L  273  VAL GLU ILE SER ARG LYS LEU GLY ILE GLY TRP HIS VAL          
SEQRES  10 L  273  PRO LEU ALA PHE CYS VAL PRO ILE PHE MET PHE CYS VAL          
SEQRES  11 L  273  LEU GLN VAL PHE ARG PRO LEU LEU LEU GLY SER TRP GLY          
SEQRES  12 L  273  HIS ALA PHE PRO TYR GLY ILE LEU SER HIS LEU ASP TRP          
SEQRES  13 L  273  VAL ASN ASN PHE GLY TYR GLN TYR LEU ASN TRP HIS TYR          
SEQRES  14 L  273  ASN PRO GLY HIS MET SER SER VAL SER PHE LEU PHE VAL          
SEQRES  15 L  273  ASN ALA MET ALA LEU GLY LEU HIS GLY GLY LEU ILE LEU          
SEQRES  16 L  273  SER VAL ALA ASN PRO GLY ASP GLY ASP LYS VAL LYS THR          
SEQRES  17 L  273  ALA GLU HIS GLU ASN GLN TYR PHE ARG ASP VAL VAL GLY          
SEQRES  18 L  273  TYR SER ILE GLY ALA LEU SER ILE HIS ARG LEU GLY LEU          
SEQRES  19 L  273  PHE LEU ALA SER ASN ILE PHE LEU THR GLY ALA PHE GLY          
SEQRES  20 L  273  THR ILE ALA SER GLY PRO PHE TRP THR ARG GLY TRP PRO          
SEQRES  21 L  273  GLU TRP TRP GLY TRP TRP LEU ASP ILE PRO PHE TRP SER          
SEQRES   1 M  323  ALA ASP TYR GLN THR ILE TYR THR GLN ILE GLN ALA ARG          
SEQRES   2 M  323  GLY PRO HIS ILE THR VAL SER GLY GLU TRP GLY ASP ASN          
SEQRES   3 M  323  ASP ARG VAL GLY LYS PRO PHE TYR SER TYR TRP LEU GLY          
SEQRES   4 M  323  LYS ILE GLY ASP ALA GLN ILE GLY PRO ILE TYR LEU GLY          
SEQRES   5 M  323  ALA SER GLY ILE ALA ALA PHE ALA PHE GLY SER THR ALA          
SEQRES   6 M  323  ILE LEU ILE ILE LEU PHE ASN MET ALA ALA GLU VAL HIS          
SEQRES   7 M  323  PHE ASP PRO LEU GLN PHE PHE ARG GLN PHE PHE TRP LEU          
SEQRES   8 M  323  GLY LEU TYR PRO PRO LYS ALA GLN TYR GLY MET GLY ILE          
SEQRES   9 M  323  PRO PRO LEU HIS ASP GLY GLY TRP TRP LEU MET ALA GLY          
SEQRES  10 M  323  LEU PHE MET THR LEU SER LEU GLY SER TRP TRP ILE ARG          
SEQRES  11 M  323  VAL TYR SER ARG ALA ARG ALA LEU GLY LEU GLY THR HIS          
SEQRES  12 M  323  ILE ALA TRP ASN PHE ALA ALA ALA ILE PHE PHE VAL LEU          
SEQRES  13 M  323  CYS ILE GLY CYS ILE HIS PRO THR LEU VAL GLY SER TRP          
SEQRES  14 M  323  SER GLU GLY VAL PRO PHE GLY ILE TRP PRO HIS ILE ASP          
SEQRES  15 M  323  TRP LEU THR ALA PHE SER ILE ARG TYR GLY ASN PHE TYR          
SEQRES  16 M  323  TYR CYS PRO TRP HIS GLY PHE SER ILE GLY PHE ALA TYR          
SEQRES  17 M  323  GLY CYS GLY LEU LEU PHE ALA ALA HIS GLY ALA THR ILE          
SEQRES  18 M  323  LEU ALA VAL ALA ARG PHE GLY GLY ASP ARG GLU ILE GLU          
SEQRES  19 M  323  GLN ILE THR ASP ARG GLY THR ALA VAL GLU ARG ALA ALA          
SEQRES  20 M  323  LEU PHE TRP ARG TRP THR ILE GLY PHE ASN ALA THR ILE          
SEQRES  21 M  323  GLU SER VAL HIS ARG TRP GLY TRP PHE PHE SER LEU MET          
SEQRES  22 M  323  VAL MET VAL SER ALA SER VAL GLY ILE LEU LEU THR GLY          
SEQRES  23 M  323  THR PHE VAL ASP ASN TRP TYR LEU TRP CYS VAL LYS HIS          
SEQRES  24 M  323  GLY ALA ALA PRO ASP TYR PRO ALA TYR LEU PRO ALA THR          
SEQRES  25 M  323  PRO ASP PRO ALA SER LEU PRO GLY ALA PRO LYS                  
SEQRES   1 H  258  FME TYR HIS GLY ALA LEU ALA GLN HIS LEU ASP ILE ALA          
SEQRES   2 H  258  GLN LEU VAL TRP TYR ALA GLN TRP LEU VAL ILE TRP THR          
SEQRES   3 H  258  VAL VAL LEU LEU TYR LEU ARG ARG GLU ASP ARG ARG GLU          
SEQRES   4 H  258  GLY TYR PRO LEU VAL GLU PRO LEU GLY LEU VAL LYS LEU          
SEQRES   5 H  258  ALA PRO GLU ASP GLY GLN VAL TYR GLU LEU PRO TYR PRO          
SEQRES   6 H  258  LYS THR PHE VAL LEU PRO HIS GLY GLY THR VAL THR VAL          
SEQRES   7 H  258  PRO ARG ARG ARG PRO GLU THR ARG GLU LEU LYS LEU ALA          
SEQRES   8 H  258  GLN THR ASP GLY PHE GLU GLY ALA PRO LEU GLN PRO THR          
SEQRES   9 H  258  GLY ASN PRO LEU VAL ASP ALA VAL GLY PRO ALA SER TYR          
SEQRES  10 H  258  ALA GLU ARG ALA GLU VAL VAL ASP ALA THR VAL ASP GLY          
SEQRES  11 H  258  LYS ALA LYS ILE VAL PRO LEU ARG VAL ALA THR ASP PHE          
SEQRES  12 H  258  SER ILE ALA GLU GLY ASP VAL ASP PRO ARG GLY LEU PRO          
SEQRES  13 H  258  VAL VAL ALA ALA ASP GLY VAL GLU ALA GLY THR VAL THR          
SEQRES  14 H  258  ASP LEU TRP VAL ASP ARG SER GLU HIS TYR PHE ARG TYR          
SEQRES  15 H  258  LEU GLU LEU SER VAL ALA GLY SER ALA ARG THR ALA LEU          
SEQRES  16 H  258  ILE PRO LEU GLY PHE CYS ASP VAL LYS LYS ASP LYS ILE          
SEQRES  17 H  258  VAL VAL THR SER ILE LEU SER GLU GLN PHE ALA ASN VAL          
SEQRES  18 H  258  PRO ARG LEU GLN SER ARG ASP GLN ILE THR LEU ARG GLU          
SEQRES  19 H  258  GLU ASP LYS VAL SER ALA TYR TYR ALA GLY GLY LEU LEU          
SEQRES  20 H  258  TYR ALA THR PRO GLU ARG ALA GLU SER LEU LEU                  
MODRES 5PRC FME H    1  MET  N-FORMYLMETHIONINE                                 
HET    FME  H   1      10                                                       
HET    HEM  C 337      43                                                       
HET    HEM  C 338      43                                                       
HET    HEM  C 339      43                                                       
HET    HEM  C 340      43                                                       
HET    BCB  L 302      66                                                       
HET    BCB  L 304      66                                                       
HET    BPB  L 402      65                                                       
HET    ATZ  L 502      14                                                       
HET    LDA  L 702      16                                                       
HET    LDA  L 705      16                                                       
HET    FE2  M 500       1                                                       
HET    SO4  M 802       5                                                       
HET    SO4  M 803       5                                                       
HET    SO4  M 804       5                                                       
HET    BCB  M 805      66                                                       
HET    BCB  M 806      66                                                       
HET    BPB  M 401      65                                                       
HET    MQ7  M 501      48                                                       
HET    NS5  M 600      40                                                       
HET    LDA  M 704      16                                                       
HET    LDA  M 706      16                                                       
HET    SO4  H 801       5                                                       
HET    LDA  H 701      16                                                       
HET    LDA  H 703      16                                                       
HETNAM     FME N-FORMYLMETHIONINE                                               
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     BCB BACTERIOCHLOROPHYLL B                                            
HETNAM     BPB BACTERIOPHEOPHYTIN B                                             
HETNAM     ATZ 2-CHLORO-4-ISOPROPYLAMINO-6-ETHYLAMINO -1,3,5-TRIAZINE           
HETNAM     LDA LAURYL DIMETHYLAMINE-N-OXIDE                                     
HETNAM     FE2 FE (II) ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MQ7 MENAQUINONE-7                                                    
HETNAM     NS5 15-CIS-1,2-DIHYDRONEUROSPORENE                                   
HETSYN     HEM HEME                                                             
HETSYN     ATZ ATRAZINE                                                         
FORMUL   4  FME    C6 H11 N O3 S                                                
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   9  BCB    4(C55 H72 MG N4 O6 2+)                                       
FORMUL  11  BPB    2(C55 H74 N4 O6)                                             
FORMUL  12  ATZ    C8 H14 CL N5                                                 
FORMUL  13  LDA    6(C14 H31 N O)                                               
FORMUL  15  FE2    FE 2+                                                        
FORMUL  16  SO4    4(O4 S 2-)                                                   
FORMUL  22  MQ7    C46 H64 O2                                                   
FORMUL  23  NS5    C40 H60                                                      
FORMUL  29  HOH   *343(H2 O)                                                    
HELIX    1   1 PRO C   25  GLN C   37  1N-TERMINAL HELIX                  13    
HELIX    2   3 GLU C   67  TRP C   80  1ASSOCIATED WITH HEME 1            14    
HELIX    3   5 TYR C  102  ASN C  120  1ASSOCIATED WITH HEME 2            19    
HELIX    4   7 CYS C  132  HIS C  136  1HEME 2 ATTACHMENT SITE             5    
HELIX    5   8 ARG C  169  TYR C  179  5                                  11    
HELIX    6   9 PRO C  189  PHE C  193  1                                   5    
HELIX    7  11 LEU C  223  LEU C  240  5ASSOCIATED WITH HEME 3            18    
HELIX    8  15 PRO C  262  ASN C  280  1ASSOCIATED WITH HEME 4            19    
HELIX    9  16 ALA C  283  ALA C  287  5                                   5    
HELIX   10  18 CYS C  305  HIS C  309  1HEME 4 ATTACHMENT SITE             5    
HELIX   11  22 GLY L   32  GLN L   55  1TRANSMEMBRANE HELIX LA            24    
HELIX   12  25 GLY L   84  LEU L  111  1TRANSMEMBRANE HELIX LB            28    
HELIX   13  26 HIS L  116  LEU L  139  1TRANSMEMBRANE HELIX LC            24    
HELIX   14  29 SER L  152  TYR L  164  1PERIPLASMIC HELIX LCD             13    
HELIX   15  31 PRO L  171  ALA L  198  1TRANSMEMBRANE HELIX LD            28    
HELIX   16  32 ALA L  209  VAL L  220  1CYTOPLASMIC HELIX LDE             12    
HELIX   17  33 ALA L  226  PRO L  253  1TRANSMEMBRANE HELIX LE            28    
HELIX   18  34 TRP L  259  LEU L  267  1PERIPLASMIC C-TERMINAL             9    
HELIX   19  37 ALA M   53  VAL M   77  1TRANSMEMBRANE HELIX MA            25    
HELIX   20  38 PRO M   81  ARG M   86  1PERIPLASMIC HELIX MAB              6    
HELIX   21  41 GLY M  111  LEU M  138  1TRANSMEMBRANE HELIX MB            28    
HELIX   22  42 HIS M  143  VAL M  166  1TRANSMEMBRANE HELIX MC            24    
HELIX   23  45 ILE M  177  ARG M  190  1PERIPLASMIC HELIX MCD             14    
HELIX   24  47 PRO M  198  PHE M  227  1TRANSMEMBRANE HELIX MD            30    
HELIX   25  48 GLU M  232  THR M  237  1CYTOPLASMIC HELIX                  6    
HELIX   26  49 THR M  241  ILE M  254  1CYTOPLASMIC HELIX MDE             14    
HELIX   27  50 SER M  262  LEU M  284  1TRANSMEMBRANE HELIX ME            23    
HELIX   28  51 TRP M  292  HIS M  299  1PERIPLASMIC C-TERMINAL             8    
HELIX   29  53 ILE H   12  LEU H   30  1TRANSMEMBRANE HELIX               19    
HELIX   30  54 LEU H   32  ARG H   37  1PI-HELICAL EXTENSION OF TM         6    
HELIX   31  55 ASP H   56  TYR H   60  1SHORT HELIX                        5    
HELIX   32  56 PRO H  107  ASP H  110  1SHORT HELIX                        4    
HELIX   33  59 SER H  215  ASN H  220  5SHORT HELIX                        6    
HELIX   34  60 LEU H  232  TYR H  248  1C-TERMINAL HELIX                  17    
SHEET    1   A 2 ALA C   7  THR C   9  0                                        
SHEET    2   A 2 VAL C  22  HIS C  24 -1  N  LEU C  23   O  THR C   8           
SHEET    1   B 2 LYS H  66  VAL H  69  0                                        
SHEET    2   B 2 THR H  75  VAL H  78 -1  N  VAL H  78   O  LYS H  66           
SHEET    1   C 2 LEU H  90  GLN H  92  0                                        
SHEET    2   C 2 LEU H 101  PRO H 103 -1  N  GLN H 102   O  ALA H  91           
SHEET    1   D 4 ILE H 134  PRO H 136  0                                        
SHEET    2   D 4 GLY H 166  ASP H 174 -1  N  VAL H 173   O  VAL H 135           
SHEET    3   D 4 TYR H 182  VAL H 187 -1  N  SER H 186   O  THR H 167           
SHEET    4   D 4 THR H 193  PRO H 197 -1  N  ILE H 196   O  LEU H 183           
SHEET    1   E 2 CYS H 201  VAL H 203  0                                        
SHEET    2   E 2 ILE H 208  VAL H 210 -1  N  VAL H 209   O  ASP H 202           
SHEET    1   F 2 PRO H 156  VAL H 158  0                                        
SHEET    2   F 2 GLU H 164  THR H 167 -1  N  GLY H 166   O  VAL H 157           
LINK         SG  CYS C  87                 CAB HEM C 337     1555   1555  1.75  
LINK         SG  CYS C  90                 CAC HEM C 337     1555   1555  1.79  
LINK         SG  CYS C 132                 CAB HEM C 338     1555   1555  1.81  
LINK         SG  CYS C 135                 CAC HEM C 338     1555   1555  1.78  
LINK         SG  CYS C 244                 CAB HEM C 339     1555   1555  1.77  
LINK         SG  CYS C 247                 CAC HEM C 339     1555   1555  1.79  
LINK         SG  CYS C 305                 CAB HEM C 340     1555   1555  1.76  
LINK         SG  CYS C 308                 CAC HEM C 340     1555   1555  1.76  
LINK         C   FME H   1                 N   TYR H   2     1555   1555  1.33  
LINK         SD  MET C  74                FE   HEM C 337     1555   1555  2.18  
LINK         NE2 HIS C  91                FE   HEM C 337     1555   1555  1.90  
LINK         SD  MET C 110                FE   HEM C 338     1555   1555  2.16  
LINK         NE2 HIS C 124                FE   HEM C 340     1555   1555  1.94  
LINK         NE2 HIS C 136                FE   HEM C 338     1555   1555  1.97  
LINK         SD  MET C 233                FE   HEM C 339     1555   1555  2.09  
LINK         NE2 HIS C 248                FE   HEM C 339     1555   1555  1.94  
LINK         NE2 HIS C 309                FE   HEM C 340     1555   1555  1.98  
LINK         NE2 HIS L 153                MG   BCB L 304     1555   1555  2.11  
LINK         NE2 HIS L 173                MG   BCB L 302     1555   1555  2.04  
LINK         NE2 HIS L 190                FE   FE2 M 500     1555   1555  1.86  
LINK         NE2 HIS L 230                FE   FE2 M 500     1555   1555  2.25  
LINK         NE2 HIS M 180                MG   BCB M 805     1555   1555  2.06  
LINK         NE2 HIS M 200                MG   BCB M 806     1555   1555  2.06  
LINK         NE2 HIS M 217                FE   FE2 M 500     1555   1555  2.00  
LINK         OE2 GLU M 232                FE   FE2 M 500     1555   1555  1.99  
LINK         OE1 GLU M 232                FE   FE2 M 500     1555   1555  2.45  
LINK         NE2 HIS M 264                FE   FE2 M 500     1555   1555  2.10  
CISPEP   1 PRO C    5    PRO C    6          0        -1.18                     
CISPEP   2 LEU C  152    PRO C  153          0       -16.13                     
CISPEP   3 GLY C  329    PRO C  330          0         7.41                     
CISPEP   4 GLY M   47    PRO M   48          0       -11.89                     
CISPEP   5 TYR H   41    PRO H   42          0         8.44                     
CISPEP   6 VAL H   78    PRO H   79          0         1.83                     
SITE     1 AC1  5 HIS L 190  HIS L 230  HIS M 217  GLU M 232                    
SITE     2 AC1  5 HIS M 264                                                     
SITE     1 AC2  7 ARG H  33  ARG H  37  TYR H  41  HOH H1059                    
SITE     2 AC2  7 HOH H1060  HOH H1061  ARG M 251                               
SITE     1 AC3  5 HOH H1224  ASN L 199  HOH L1127  HIS M 143                    
SITE     2 AC3  5 ARG M 265                                                     
SITE     1 AC4  4 LEU H 246  ALA M   1  ARG M 226  HOH M1226                    
SITE     1 AC5  8 TRP M  23  TYR M  50  ALA M  53  SER M  54                    
SITE     2 AC5  8 SER M 133  LDA M 704  HOH M1030  HOH M1064                    
SITE     1 AC6 19 HIS L 168  MET L 174  VAL L 177  SER L 178                    
SITE     2 AC6 19 VAL L 182  MET L 185  VAL L 220  BCB L 302                    
SITE     3 AC6 19 HOH L 993  MET M 120  VAL M 155  ILE M 177                    
SITE     4 AC6 19 TRP M 178  HIS M 180  ILE M 181  LEU M 184                    
SITE     5 AC6 19 BPB M 401  NS5 M 600  BCB M 806                               
SITE     1 AC7 20 PRO L 124  MET L 127  PHE L 128  VAL L 157                    
SITE     2 AC7 20 PHE L 160  GLY L 161  TRP L 167  HIS L 168                    
SITE     3 AC7 20 HIS L 173  SER L 176  VAL L 177  PHE L 241                    
SITE     4 AC7 20 GLY L 244  THR L 248  BCB L 304  BPB L 402                    
SITE     5 AC7 20 TYR M 195  TYR M 208  BCB M 805  BCB M 806                    
SITE     1 AC8 22 VAL L 157  TYR L 162  PHE L 181  BCB L 302                    
SITE     2 AC8 22 BCB L 304  PHE M 148  PHE M 154  VAL M 155                    
SITE     3 AC8 22 LEU M 184  PHE M 187  SER M 188  PHE M 194                    
SITE     4 AC8 22 TYR M 195  HIS M 200  SER M 203  ILE M 204                    
SITE     5 AC8 22 TYR M 208  MET M 275  ALA M 278  ILE M 282                    
SITE     6 AC8 22 BPB M 401  BCB M 805                                          
SITE     1 AC9 15 PHE L 128  PHE L 146  ILE L 150  HIS L 153                    
SITE     2 AC9 15 LEU L 154  VAL L 157  BCB L 302  BPB L 402                    
SITE     3 AC9 15 GLY M 201  ILE M 204  GLY M 205  TYR M 208                    
SITE     4 AC9 15 GLY M 209  BCB M 806  HOH M 991                               
SITE     1 BC1 17 PHE L 181  MET L 185  LEU L 189  VAL L 220                    
SITE     2 BC1 17 PHE M  59  SER M  63  ILE M  66  SER M 123                    
SITE     3 BC1 17 LEU M 124  TRP M 127  ILE M 144  ASN M 147                    
SITE     4 BC1 17 PHE M 148  SER M 271  MET M 275  BCB M 805                    
SITE     5 BC1 17 BCB M 806                                                     
SITE     1 BC2 16 PHE L  97  TRP L 100  GLU L 104  VAL L 117                    
SITE     2 BC2 16 PHE L 121  PRO L 124  TYR L 148  HIS L 153                    
SITE     3 BC2 16 ALA L 237  BCB L 302  BCB L 304  TYR M 208                    
SITE     4 BC2 16 LEU M 212  TRP M 250  ILE M 254  MQ7 M 501                    
SITE     1 BC3 10 TYR L  29  BPB L 402  ALA M 216  HIS M 217                    
SITE     2 BC3 10 THR M 220  ALA M 246  TRP M 250  ALA M 258                    
SITE     3 BC3 10 VAL M 263  PHE M 270                                          
SITE     1 BC4 21 TYR C  56  LYS C  57  ASN C  58  VAL C  59                    
SITE     2 BC4 21 LYS C  60  VAL C  61  LEU C  62  PHE C  70                    
SITE     3 BC4 21 LEU C  71  MET C  74  THR C  78  SER C  82                    
SITE     4 BC4 21 CYS C  87  CYS C  90  HIS C  91  LEU C  96                    
SITE     5 BC4 21 ALA C  97  TYR C 104  ALA C 107  ARG C 108                    
SITE     6 BC4 21 VAL C 212                                                     
SITE     1 BC5 16 TYR C  89  TYR C 102  VAL C 106  MET C 110                    
SITE     2 BC5 16 LEU C 111  MET C 113  THR C 114  CYS C 132                    
SITE     3 BC5 16 CYS C 135  HIS C 136  PRO C 140  LEU C 141                    
SITE     4 BC5 16 PRO C 142  LEU C 289  ARG C 293  PRO C 301                    
SITE     1 BC6 20 VAL C 201  ARG C 202  VAL C 203  VAL C 204                    
SITE     2 BC6 20 MET C 233  SER C 237  LEU C 240  ASN C 243                    
SITE     3 BC6 20 CYS C 244  CYS C 247  HIS C 248  PHE C 253                    
SITE     4 BC6 20 GLU C 254  ARG C 264  ALA C 267  TRP C 268                    
SITE     5 BC6 20 ARG C 272  HOH C 938  HOH C 940  HOH C 973                    
SITE     1 BC7 21 HIS C 124  THR C 128  GLY C 129  VAL C 130                    
SITE     2 BC7 21 ILE C 236  GLN C 263  ILE C 266  GLY C 270                    
SITE     3 BC7 21 ILE C 271  MET C 273  VAL C 274  ASP C 304                    
SITE     4 BC7 21 CYS C 305  CYS C 308  HIS C 309  THR C 313                    
SITE     5 BC7 21 LYS C 314  PRO C 315  HOH C 967  HOH C1203                    
SITE     6 BC7 21 HOH C1235                                                     
SITE     1 BC8  8 GLY M 117  THR M 121  GLY M 159  CYS M 160                    
SITE     2 BC8  8 VAL M 173  GLY M 176  HIS M 180  BCB M 805                    
SITE     1 BC9  8 GLU L 212  ASN L 213  PHE L 216  TYR L 222                    
SITE     2 BC9  8 SER L 223  ILE L 224  GLY L 225  ALA L 226                    
SITE     1 CC1  5 ARG H  33  PRO H  54  ASP H  56  LDA L 705                    
SITE     2 CC1  5 TRP M 266                                                     
SITE     1 CC2  6 ASP L  60  PHE L  62  TYR M 195  TRP M 295                    
SITE     2 CC2  6 CYS M 296  ALA M 301                                          
SITE     1 CC3  7 PRO H  42  VAL H  59  TYR H  60  LEU H  62                    
SITE     2 CC3  7 TYR H  64  PRO H  65  ARG H  80                               
SITE     1 CC4  7 TRP M  23  ALA M  53  SER M  54  ALA M  57                    
SITE     2 CC4  7 SER M 126  SER M 133  SO4 M 804                               
SITE     1 CC5  3 LDA H 701  HOH H1060  PHE M 256                               
SITE     1 CC6  3 PHE M  71  ASN M  72  TRP M 112                               
CRYST1  223.500  223.500  113.600  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004474  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008803        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system