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Database: PDB
Entry: 1OCC
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HEADER    OXIDOREDUCTASE (CYTOCHROME(C)-OXYGEN)   18-APR-96   1OCC              
TITLE     STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY           
TITLE    2 OXIDIZED STATE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND   3 CHAIN: A, N;                                                         
COMPND   4 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND   5 EC: 1.9.3.1;                                                         
COMPND   6 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND   7 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND   8 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND   9 CUA, CUB, MG AND ZN.;                                                
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  12 CHAIN: B, O;                                                         
COMPND  13 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  14 EC: 1.9.3.1;                                                         
COMPND  15 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  16 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  17 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  18 CUA, CUB, MG AND ZN.;                                                
COMPND  19 MOL_ID: 3;                                                           
COMPND  20 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  21 CHAIN: C, P;                                                         
COMPND  22 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  23 EC: 1.9.3.1;                                                         
COMPND  24 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  25 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  26 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  27 CUA, CUB, MG AND ZN.;                                                
COMPND  28 MOL_ID: 4;                                                           
COMPND  29 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  30 CHAIN: D, Q;                                                         
COMPND  31 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  32 EC: 1.9.3.1;                                                         
COMPND  33 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  34 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  35 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  36 CUA, CUB, MG AND ZN.;                                                
COMPND  37 MOL_ID: 5;                                                           
COMPND  38 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  39 CHAIN: E, R;                                                         
COMPND  40 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  41 EC: 1.9.3.1;                                                         
COMPND  42 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  43 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  44 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  45 CUA, CUB, MG AND ZN.;                                                
COMPND  46 MOL_ID: 6;                                                           
COMPND  47 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  48 CHAIN: F, S;                                                         
COMPND  49 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  50 EC: 1.9.3.1;                                                         
COMPND  51 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  52 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  53 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  54 CUA, CUB, MG AND ZN.;                                                
COMPND  55 MOL_ID: 7;                                                           
COMPND  56 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  57 CHAIN: G, T;                                                         
COMPND  58 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  59 EC: 1.9.3.1;                                                         
COMPND  60 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  61 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  62 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  63 CUA, CUB, MG AND ZN.;                                                
COMPND  64 MOL_ID: 8;                                                           
COMPND  65 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  66 CHAIN: H, U;                                                         
COMPND  67 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  68 EC: 1.9.3.1;                                                         
COMPND  69 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  70 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  71 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  72 CUA, CUB, MG AND ZN.;                                                
COMPND  73 MOL_ID: 9;                                                           
COMPND  74 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  75 CHAIN: I, V;                                                         
COMPND  76 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  77 EC: 1.9.3.1;                                                         
COMPND  78 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  79 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  80 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  81 CUA, CUB, MG AND ZN.;                                                
COMPND  82 MOL_ID: 10;                                                          
COMPND  83 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  84 CHAIN: J, W;                                                         
COMPND  85 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  86 EC: 1.9.3.1;                                                         
COMPND  87 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  88 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  89 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  90 CUA, CUB, MG AND ZN.;                                                
COMPND  91 MOL_ID: 11;                                                          
COMPND  92 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND  93 CHAIN: K, X;                                                         
COMPND  94 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND  95 EC: 1.9.3.1;                                                         
COMPND  96 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND  97 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND  98 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND  99 CUA, CUB, MG AND ZN.;                                                
COMPND 100 MOL_ID: 12;                                                          
COMPND 101 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND 102 CHAIN: L, Y;                                                         
COMPND 103 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND 104 EC: 1.9.3.1;                                                         
COMPND 105 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND 106 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND 107 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND 108 CUA, CUB, MG AND ZN.;                                                
COMPND 109 MOL_ID: 13;                                                          
COMPND 110 MOLECULE: CYTOCHROME C OXIDASE;                                      
COMPND 111 CHAIN: M, Z;                                                         
COMPND 112 SYNONYM: FERROCYTOCHROME C\:OXYGEN OXIDOREDUCTASE;                   
COMPND 113 EC: 1.9.3.1;                                                         
COMPND 114 OTHER_DETAILS: THIS ENZYME IS A MULTI COMPONENT PROTEIN              
COMPND 115 COMPLEX AND IS A HOMO DIMER. ONE MONOMER IS COMPOSED OF 13           
COMPND 116 DIFFERENT SUBUNITS AND SIX METAL CENTERS, HEME A, HEME A3,           
COMPND 117 CUA, CUB, MG AND ZN.                                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 ORGAN: HEART;                                                        
SOURCE   6 TISSUE: HEART MUSCLE;                                                
SOURCE   7 ORGANELLE: MITOCHONDRION;                                            
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  10 ORGANISM_COMMON: CATTLE;                                             
SOURCE  11 ORGANISM_TAXID: 9913;                                                
SOURCE  12 ORGAN: HEART;                                                        
SOURCE  13 TISSUE: HEART MUSCLE;                                                
SOURCE  14 ORGANELLE: MITOCHONDRION;                                            
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  17 ORGANISM_COMMON: CATTLE;                                             
SOURCE  18 ORGANISM_TAXID: 9913;                                                
SOURCE  19 ORGAN: HEART;                                                        
SOURCE  20 TISSUE: HEART MUSCLE;                                                
SOURCE  21 ORGANELLE: MITOCHONDRION;                                            
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  24 ORGANISM_COMMON: CATTLE;                                             
SOURCE  25 ORGANISM_TAXID: 9913;                                                
SOURCE  26 ORGAN: HEART;                                                        
SOURCE  27 TISSUE: HEART MUSCLE;                                                
SOURCE  28 ORGANELLE: MITOCHONDRION;                                            
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  31 ORGANISM_COMMON: CATTLE;                                             
SOURCE  32 ORGANISM_TAXID: 9913;                                                
SOURCE  33 ORGAN: HEART;                                                        
SOURCE  34 TISSUE: HEART MUSCLE;                                                
SOURCE  35 ORGANELLE: MITOCHONDRION;                                            
SOURCE  36 MOL_ID: 6;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  38 ORGANISM_COMMON: CATTLE;                                             
SOURCE  39 ORGANISM_TAXID: 9913;                                                
SOURCE  40 ORGAN: HEART;                                                        
SOURCE  41 TISSUE: HEART MUSCLE;                                                
SOURCE  42 ORGANELLE: MITOCHONDRION;                                            
SOURCE  43 MOL_ID: 7;                                                           
SOURCE  44 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  45 ORGANISM_COMMON: CATTLE;                                             
SOURCE  46 ORGANISM_TAXID: 9913;                                                
SOURCE  47 ORGAN: HEART;                                                        
SOURCE  48 TISSUE: HEART MUSCLE;                                                
SOURCE  49 ORGANELLE: MITOCHONDRION;                                            
SOURCE  50 MOL_ID: 8;                                                           
SOURCE  51 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  52 ORGANISM_COMMON: CATTLE;                                             
SOURCE  53 ORGANISM_TAXID: 9913;                                                
SOURCE  54 ORGAN: HEART;                                                        
SOURCE  55 TISSUE: HEART MUSCLE;                                                
SOURCE  56 ORGANELLE: MITOCHONDRION;                                            
SOURCE  57 MOL_ID: 9;                                                           
SOURCE  58 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  59 ORGANISM_COMMON: CATTLE;                                             
SOURCE  60 ORGANISM_TAXID: 9913;                                                
SOURCE  61 ORGAN: HEART;                                                        
SOURCE  62 TISSUE: HEART MUSCLE;                                                
SOURCE  63 ORGANELLE: MITOCHONDRION;                                            
SOURCE  64 MOL_ID: 10;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  66 ORGANISM_COMMON: CATTLE;                                             
SOURCE  67 ORGANISM_TAXID: 9913;                                                
SOURCE  68 ORGAN: HEART;                                                        
SOURCE  69 TISSUE: HEART MUSCLE;                                                
SOURCE  70 ORGANELLE: MITOCHONDRION;                                            
SOURCE  71 MOL_ID: 11;                                                          
SOURCE  72 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  73 ORGANISM_COMMON: CATTLE;                                             
SOURCE  74 ORGANISM_TAXID: 9913;                                                
SOURCE  75 ORGAN: HEART;                                                        
SOURCE  76 TISSUE: HEART MUSCLE;                                                
SOURCE  77 ORGANELLE: MITOCHONDRION;                                            
SOURCE  78 MOL_ID: 12;                                                          
SOURCE  79 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  80 ORGANISM_COMMON: CATTLE;                                             
SOURCE  81 ORGANISM_TAXID: 9913;                                                
SOURCE  82 ORGAN: HEART;                                                        
SOURCE  83 TISSUE: HEART MUSCLE;                                                
SOURCE  84 ORGANELLE: MITOCHONDRION;                                            
SOURCE  85 MOL_ID: 13;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  87 ORGANISM_COMMON: CATTLE;                                             
SOURCE  88 ORGANISM_TAXID: 9913;                                                
SOURCE  89 ORGAN: HEART;                                                        
SOURCE  90 TISSUE: HEART MUSCLE;                                                
SOURCE  91 ORGANELLE: MITOCHONDRION                                             
KEYWDS    CYTOCHROME C OXIDASE, OXIDOREDUCTASE (CYTOCHROME(C)-OXYGEN)           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TSUKIHARA,H.AOYAMA,E.YAMASHITA,T.TOMIZAKI,H.YAMAGUCHI,              
AUTHOR   2 K.SHINZAWA-ITOH,R.NAKASHIMA,R.YAONO,S.YOSHIKAWA                      
REVDAT   3   24-FEB-09 1OCC    1       VERSN                                    
REVDAT   2   30-SEP-03 1OCC    1       DBREF                                    
REVDAT   1   07-DEC-96 1OCC    0                                                
JRNL        AUTH   T.TSUKIHARA,H.AOYAMA,E.YAMASHITA,T.TOMIZAKI,                 
JRNL        AUTH 2 H.YAMAGUCHI,K.SHINZAWA-ITOH,R.NAKASHIMA,R.YAONO,             
JRNL        AUTH 3 S.YOSHIKAWA                                                  
JRNL        TITL   THE WHOLE STRUCTURE OF THE 13-SUBUNIT OXIDIZED               
JRNL        TITL 2 CYTOCHROME C OXIDASE AT 2.8 A.                               
JRNL        REF    SCIENCE                       V. 272  1136 1996              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   8638158                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.TSUKIHARA,H.AOYAMA,E.YAMASHITA,T.TOMIZAKI,                 
REMARK   1  AUTH 2 H.YAMAGUCHI,K.SHINZAWA-ITOH,R.NAKASHIMA,R.YAONO,             
REMARK   1  AUTH 3 S.YOSHIKAWA                                                  
REMARK   1  TITL   STRUCTURES OF METAL SITES OF OXIDIZED BOVINE HEART           
REMARK   1  TITL 2 CYTOCHROME C OXIDASE AT 2.8 A                                
REMARK   1  REF    SCIENCE                       V. 269  1069 1995              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 151622                         
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) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
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            : 14238                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 125                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.00                          
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) : 0.35                            
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) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.58                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.99                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.30                            
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 ELECTRON DENSITY OF REGION FROM       
REMARK   3  G 1 TO G11 IS NOISY AND THE MODEL OF THIS REGION HAS                
REMARK   3  AMBIGUITY. THE REGIONS FROM H 46 TO H 51 AND FROM H 39 TO H 42      
REMARK   3  HAVE WEAK ELECTRON DENSITIES. THE ELECTRON DENSITY OF REGION        
REMARK   3  FROM G 1 TO G11 IS NOISY AND THE MODEL OF THIS REGION HAS           
REMARK   3  AMBIGUITY. THE REGIONS FROM H 46 TO H 51 AND FROM H 39 TO H 42      
REMARK   3  HAVE WEAK ELECTRON DENSITIES.                                       
REMARK   4                                                                      
REMARK   4 1OCC 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        : 01-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 283                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK AND TSUKI SCALE          
REMARK 200                                   (LOCAL)                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 155505                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.78000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: OSCILLATION METHOD                                           
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       94.55000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.30000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      105.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.30000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       94.55000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      105.25000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK:                                                              
REMARK 300 THIS ENZYME IS A MULTI-COMPONENT PROTEIN COMPLEX AND IS A            
REMARK 300 HOMODIMER.  EACH MONOMER IS COMPOSED OF 13 DIFFERENT                 
REMARK 300 SUBUNITS AND SIX METAL CENTERS: HEME A, HEME A3, CUA, CUB,           
REMARK 300 MG, AND ZN.  THE DEPOSITOR PROVIDED THE COORDINATES OF ONE           
REMARK 300 MONOMER.  THE PDB GENERATED THE OTHER MONOMER FROM THE               
REMARK 300 MONOMER THAT WAS DEPOSITED USING THE TRANSFORMATION                  
REMARK 300 PROVIDED BY THE DEPOSITOR.                                           
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: 26-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 26-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 117760 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 121840 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -989.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P, Q, R,            
REMARK 350                    AND CHAINS: S, T, U, V, W, X, Y, Z                
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     ALA D     1                                                      
REMARK 465     HIS D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     GLU H     2                                                      
REMARK 465     ASP H     3                                                      
REMARK 465     ILE H     4                                                      
REMARK 465     GLN H     5                                                      
REMARK 465     ALA H     6                                                      
REMARK 465     LYS H     7                                                      
REMARK 465     ILE H     8                                                      
REMARK 465     LYS H     9                                                      
REMARK 465     ASN H    10                                                      
REMARK 465     HIS J    57                                                      
REMARK 465     LYS J    58                                                      
REMARK 465     LYS J    59                                                      
REMARK 465     ILE K     1                                                      
REMARK 465     HIS K     2                                                      
REMARK 465     GLN K     3                                                      
REMARK 465     LYS K     4                                                      
REMARK 465     ARG K     5                                                      
REMARK 465     GLU K    55                                                      
REMARK 465     GLN K    56                                                      
REMARK 465     SER M    44                                                      
REMARK 465     ALA M    45                                                      
REMARK 465     ALA M    46                                                      
REMARK 465     ALA Q     1                                                      
REMARK 465     HIS Q     2                                                      
REMARK 465     GLY Q     3                                                      
REMARK 465     ALA U     1                                                      
REMARK 465     GLU U     2                                                      
REMARK 465     ASP U     3                                                      
REMARK 465     ILE U     4                                                      
REMARK 465     GLN U     5                                                      
REMARK 465     ALA U     6                                                      
REMARK 465     LYS U     7                                                      
REMARK 465     ILE U     8                                                      
REMARK 465     LYS U     9                                                      
REMARK 465     ASN U    10                                                      
REMARK 465     HIS W    57                                                      
REMARK 465     LYS W    58                                                      
REMARK 465     LYS W    59                                                      
REMARK 465     ILE X     1                                                      
REMARK 465     HIS X     2                                                      
REMARK 465     GLN X     3                                                      
REMARK 465     LYS X     4                                                      
REMARK 465     ARG X     5                                                      
REMARK 465     GLU X    55                                                      
REMARK 465     GLN X    56                                                      
REMARK 465     SER Z    44                                                      
REMARK 465     ALA Z    45                                                      
REMARK 465     ALA Z    46                                                      
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                             HEA A 515  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  61   NE2                                                    
REMARK 620 2 HIS A 378   NE2 168.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 517  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 240   ND1                                                    
REMARK 620 2 HIS A 290   NE2 100.7                                              
REMARK 620 3 HIS A 291   NE2 139.6  97.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 228  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 161   ND1                                                    
REMARK 620 2 CYS B 196   SG  124.5                                              
REMARK 620 3 CYS B 200   SG  106.0 114.4                                        
REMARK 620 4  CU B 229  CU   143.4  58.0  56.5                                  
REMARK 620 5 MET B 207   SD   97.3 111.4  99.0 116.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 229  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 196   SG                                                     
REMARK 620 2 GLU B 198   O    90.4                                              
REMARK 620 3 CYS B 200   SG  118.6 111.8                                        
REMARK 620 4 HIS B 204   ND1 117.4  81.6 121.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEA N 515  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  61   NE2                                                    
REMARK 620 2 HIS N 378   NE2 168.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU N 517  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N 240   ND1                                                    
REMARK 620 2 HIS N 290   NE2 100.6                                              
REMARK 620 3 HIS N 291   NE2 139.6  97.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU O 228  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS O 161   ND1                                                    
REMARK 620 2 CYS O 196   SG  124.5                                              
REMARK 620 3 CYS O 200   SG  106.0 114.5                                        
REMARK 620 4  CU O 229  CU   143.4  58.0  56.5                                  
REMARK 620 5 MET O 207   SD   97.3 111.5  99.0 116.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU O 229  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 196   SG                                                     
REMARK 620 2 GLU O 198   O    90.4                                              
REMARK 620 3 CYS O 200   SG  118.6 111.8                                        
REMARK 620 4 HIS O 204   ND1 117.4  81.6 122.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 518  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 369   OD2                                                    
REMARK 620 2 HIS A 368   NE2  73.0                                              
REMARK 620 3 GLU B 198   OE1  85.0 107.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F  99  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  62   SG                                                     
REMARK 620 2 CYS F  85   SG   92.8                                              
REMARK 620 3 CYS F  60   SG  121.1 120.3                                        
REMARK 620 4 CYS F  82   SG  100.4 102.7 115.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG N 518  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP N 369   OD2                                                    
REMARK 620 2 HIS N 368   NE2  73.0                                              
REMARK 620 3 GLU O 198   OE1  85.0 107.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN S  99  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS S  85   SG                                                     
REMARK 620 2 CYS S  82   SG  102.7                                              
REMARK 620 3 CYS S  62   SG   92.8 100.4                                        
REMARK 620 4 CYS S  60   SG  120.3 115.4 121.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 517                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 518                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 228                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 229                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 99                   
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU N 517                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 518                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU O 228                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU O 229                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 99                   
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 515                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 516                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 515                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 516                 
DBREF  1OCC A    1   514  UNP    P00396   COX1_BOVIN       1    514             
DBREF  1OCC B    1   227  UNP    P68530   COX2_BOVIN       1    227             
DBREF  1OCC C    1   261  UNP    P00415   COX3_BOVIN       1    261             
DBREF  1OCC D    1   147  UNP    P00423   COX41_BOVIN     23    169             
DBREF  1OCC E    1   109  UNP    P00426   COX5A_BOVIN      1    109             
DBREF  1OCC F    1    98  UNP    P00428   COX5B_BOVIN      1     98             
DBREF  1OCC G    1    84  UNP    P07471   CX6A2_BOVIN     13     96             
DBREF  1OCC H    1    85  UNP    P00429   COX6B_BOVIN      1     85             
DBREF  1OCC I    1    73  UNP    P04038   COX6C_BOVIN      1     73             
DBREF  1OCC J    1    59  UNP    P07470   CX7A1_BOVIN     22     80             
DBREF  1OCC K    1    56  UNP    P13183   COX7B_BOVIN     33     88             
DBREF  1OCC L    1    47  UNP    P00430   COX7C_BOVIN     17     63             
DBREF  1OCC M    1    46  UNP    P10175   COX81_BOVIN     25     70             
DBREF  1OCC N    1   514  UNP    P00396   COX1_BOVIN       1    514             
DBREF  1OCC O    1   227  UNP    P68530   COX2_BOVIN       1    227             
DBREF  1OCC P    1   261  UNP    P00415   COX3_BOVIN       1    261             
DBREF  1OCC Q    1   147  UNP    P00423   COX41_BOVIN     23    169             
DBREF  1OCC R    1   109  UNP    P00426   COX5A_BOVIN      1    109             
DBREF  1OCC S    1    98  UNP    P00428   COX5B_BOVIN      1     98             
DBREF  1OCC T    1    84  UNP    P07471   CX6A2_BOVIN     13     96             
DBREF  1OCC U    1    85  UNP    P00429   COX6B_BOVIN      1     85             
DBREF  1OCC V    1    73  UNP    P04038   COX6C_BOVIN      1     73             
DBREF  1OCC W    1    59  UNP    P07470   CX7A1_BOVIN     22     80             
DBREF  1OCC X    1    56  UNP    P13183   COX7B_BOVIN     33     88             
DBREF  1OCC Y    1    47  UNP    P00430   COX7C_BOVIN     17     63             
DBREF  1OCC Z    1    46  UNP    P10175   COX81_BOVIN     25     70             
SEQRES   1 A  514  MET PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS          
SEQRES   2 A  514  ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA          
SEQRES   3 A  514  GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA          
SEQRES   4 A  514  GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN          
SEQRES   5 A  514  ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET          
SEQRES   6 A  514  ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE          
SEQRES   7 A  514  GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP          
SEQRES   8 A  514  MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU          
SEQRES   9 A  514  LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET          
SEQRES  10 A  514  VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO          
SEQRES  11 A  514  PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL          
SEQRES  12 A  514  ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER          
SEQRES  13 A  514  SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE          
SEQRES  14 A  514  ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO          
SEQRES  15 A  514  LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU          
SEQRES  16 A  514  LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET          
SEQRES  17 A  514  LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP          
SEQRES  18 A  514  PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU          
SEQRES  19 A  514  PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE          
SEQRES  20 A  514  LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR          
SEQRES  21 A  514  TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET          
SEQRES  22 A  514  VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE          
SEQRES  23 A  514  VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL          
SEQRES  24 A  514  ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE          
SEQRES  25 A  514  ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA          
SEQRES  26 A  514  THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET          
SEQRES  27 A  514  MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY          
SEQRES  28 A  514  GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP          
SEQRES  29 A  514  ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE          
SEQRES  30 A  514  HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET          
SEQRES  31 A  514  GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR          
SEQRES  32 A  514  THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE          
SEQRES  33 A  514  MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS          
SEQRES  34 A  514  PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP          
SEQRES  35 A  514  TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER          
SEQRES  36 A  514  MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET          
SEQRES  37 A  514  VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU          
SEQRES  38 A  514  VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP          
SEQRES  39 A  514  LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU          
SEQRES  40 A  514  PRO THR TYR VAL ASN LEU LYS                                  
SEQRES   1 B  227  MET ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR          
SEQRES   2 B  227  SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS          
SEQRES   3 B  227  THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU          
SEQRES   4 B  227  TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS          
SEQRES   5 B  227  THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP          
SEQRES   6 B  227  THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU          
SEQRES   7 B  227  PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN          
SEQRES   8 B  227  ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP          
SEQRES   9 B  227  TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER          
SEQRES  10 B  227  PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO          
SEQRES  11 B  227  GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL          
SEQRES  12 B  227  LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER          
SEQRES  13 B  227  GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY          
SEQRES  14 B  227  LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR          
SEQRES  15 B  227  THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN          
SEQRES  16 B  227  CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO          
SEQRES  17 B  227  ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS          
SEQRES  18 B  227  TRP SER ALA SER MET LEU                                      
SEQRES   1 C  261  MET THR HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO          
SEQRES   2 C  261  SER PRO TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU          
SEQRES   3 C  261  MET THR SER GLY LEU THR MET TRP PHE HIS PHE ASN SER          
SEQRES   4 C  261  MET THR LEU LEU MET ILE GLY LEU THR THR ASN MET LEU          
SEQRES   5 C  261  THR MET TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER          
SEQRES   6 C  261  THR PHE GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY          
SEQRES   7 C  261  LEU ARG TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL          
SEQRES   8 C  261  LEU PHE PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER          
SEQRES   9 C  261  SER LEU ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO          
SEQRES  10 C  261  PRO THR GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO          
SEQRES  11 C  261  LEU LEU ASN THR SER VAL LEU LEU ALA SER GLY VAL SER          
SEQRES  12 C  261  ILE THR TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG          
SEQRES  13 C  261  LYS HIS MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU          
SEQRES  14 C  261  GLY VAL TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR          
SEQRES  15 C  261  GLU ALA PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER          
SEQRES  16 C  261  THR PHE PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL          
SEQRES  17 C  261  ILE ILE GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG          
SEQRES  18 C  261  GLN LEU LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY          
SEQRES  19 C  261  PHE GLU ALA GLY ALA TRP TYR TRP HIS PHE VAL ASP VAL          
SEQRES  20 C  261  VAL TRP LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY          
SEQRES  21 C  261  SER                                                          
SEQRES   1 D  147  ALA HIS GLY SER VAL VAL LYS SER GLU ASP TYR ALA LEU          
SEQRES   2 D  147  PRO SER TYR VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP          
SEQRES   3 D  147  VAL ALA HIS VAL LYS ASN LEU SER ALA SER GLN LYS ALA          
SEQRES   4 D  147  LEU LYS GLU LYS GLU LYS ALA SER TRP SER SER LEU SER          
SEQRES   5 D  147  ILE ASP GLU LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS          
SEQRES   6 D  147  GLU SER PHE ALA GLU MET ASN ARG SER THR ASN GLU TRP          
SEQRES   7 D  147  LYS THR VAL VAL GLY ALA ALA MET PHE PHE ILE GLY PHE          
SEQRES   8 D  147  THR ALA LEU LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR          
SEQRES   9 D  147  GLY PRO ILE PRO HIS THR PHE GLU GLU GLU TRP VAL ALA          
SEQRES  10 D  147  LYS GLN THR LYS ARG MET LEU ASP MET LYS VAL ALA PRO          
SEQRES  11 D  147  ILE GLN GLY PHE SER ALA LYS TRP ASP TYR ASP LYS ASN          
SEQRES  12 D  147  GLU TRP LYS LYS                                              
SEQRES   1 E  109  SER HIS GLY SER HIS GLU THR ASP GLU GLU PHE ASP ALA          
SEQRES   2 E  109  ARG TRP VAL THR TYR PHE ASN LYS PRO ASP ILE ASP ALA          
SEQRES   3 E  109  TRP GLU LEU ARG LYS GLY MET ASN THR LEU VAL GLY TYR          
SEQRES   4 E  109  ASP LEU VAL PRO GLU PRO LYS ILE ILE ASP ALA ALA LEU          
SEQRES   5 E  109  ARG ALA CYS ARG ARG LEU ASN ASP PHE ALA SER ALA VAL          
SEQRES   6 E  109  ARG ILE LEU GLU VAL VAL LYS ASP LYS ALA GLY PRO HIS          
SEQRES   7 E  109  LYS GLU ILE TYR PRO TYR VAL ILE GLN GLU LEU ARG PRO          
SEQRES   8 E  109  THR LEU ASN GLU LEU GLY ILE SER THR PRO GLU GLU LEU          
SEQRES   9 E  109  GLY LEU ASP LYS VAL                                          
SEQRES   1 F   98  ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA          
SEQRES   2 F   98  THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS          
SEQRES   3 F   98  GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR          
SEQRES   4 F   98  SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE          
SEQRES   5 F   98  THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP          
SEQRES   6 F   98  ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU          
SEQRES   7 F   98  ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU          
SEQRES   8 F   98  VAL PRO HIS GLN LEU ALA HIS                                  
SEQRES   1 G   84  ALA SER ALA ALA LYS GLY ASP HIS GLY GLY THR GLY ALA          
SEQRES   2 G   84  ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO          
SEQRES   3 G   84  SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER          
SEQRES   4 G   84  GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS          
SEQRES   5 G   84  LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY          
SEQRES   6 G   84  ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU          
SEQRES   7 G   84  PRO THR GLY TYR GLU LYS                                      
SEQRES   1 H   85  ALA GLU ASP ILE GLN ALA LYS ILE LYS ASN TYR GLN THR          
SEQRES   2 H   85  ALA PRO PHE ASP SER ARG PHE PRO ASN GLN ASN GLN THR          
SEQRES   3 H   85  ARG ASN CYS TRP GLN ASN TYR LEU ASP PHE HIS ARG CYS          
SEQRES   4 H   85  GLU LYS ALA MET THR ALA LYS GLY GLY ASP VAL SER VAL          
SEQRES   5 H   85  CYS GLU TRP TYR ARG ARG VAL TYR LYS SER LEU CYS PRO          
SEQRES   6 H   85  ILE SER TRP VAL SER THR TRP ASP ASP ARG ARG ALA GLU          
SEQRES   7 H   85  GLY THR PHE PRO GLY LYS ILE                                  
SEQRES   1 I   73  SER THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU          
SEQRES   2 I   73  ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET          
SEQRES   3 I   73  VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL          
SEQRES   4 I   73  ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG          
SEQRES   5 I   73  ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS          
SEQRES   6 I   73  ALA GLY ILE PHE GLN SER ALA LYS                              
SEQRES   1 J   59  PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN          
SEQRES   2 J   59  GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA          
SEQRES   3 J   59  THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS          
SEQRES   4 J   59  LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP          
SEQRES   5 J   59  ALA SER PHE PRO HIS LYS LYS                                  
SEQRES   1 K   56  ILE HIS GLN LYS ARG ALA PRO ASP PHE HIS ASP LYS TYR          
SEQRES   2 K   56  GLY ASN ALA VAL LEU ALA SER GLY ALA THR PHE CYS VAL          
SEQRES   3 K   56  ALA VAL TRP VAL TYR MET ALA THR GLN ILE GLY ILE GLU          
SEQRES   4 K   56  TRP ASN PRO SER PRO VAL GLY ARG VAL THR PRO LYS GLU          
SEQRES   5 K   56  TRP ARG GLU GLN                                              
SEQRES   1 L   47  SER HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE          
SEQRES   2 L   47  SER VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR          
SEQRES   3 L   47  LEU PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE          
SEQRES   4 L   47  VAL ARG HIS GLN LEU LEU LYS LYS                              
SEQRES   1 M   46  ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS          
SEQRES   2 M   46  GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE          
SEQRES   3 M   46  LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN          
SEQRES   4 M   46  TYR LYS LYS SER SER ALA ALA                                  
SEQRES   1 N  514  MET PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS          
SEQRES   2 N  514  ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA          
SEQRES   3 N  514  GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA          
SEQRES   4 N  514  GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN          
SEQRES   5 N  514  ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET          
SEQRES   6 N  514  ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE          
SEQRES   7 N  514  GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP          
SEQRES   8 N  514  MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU          
SEQRES   9 N  514  LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET          
SEQRES  10 N  514  VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO          
SEQRES  11 N  514  PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL          
SEQRES  12 N  514  ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER          
SEQRES  13 N  514  SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE          
SEQRES  14 N  514  ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO          
SEQRES  15 N  514  LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU          
SEQRES  16 N  514  LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET          
SEQRES  17 N  514  LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP          
SEQRES  18 N  514  PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU          
SEQRES  19 N  514  PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE          
SEQRES  20 N  514  LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR          
SEQRES  21 N  514  TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET          
SEQRES  22 N  514  VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE          
SEQRES  23 N  514  VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL          
SEQRES  24 N  514  ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE          
SEQRES  25 N  514  ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA          
SEQRES  26 N  514  THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET          
SEQRES  27 N  514  MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY          
SEQRES  28 N  514  GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP          
SEQRES  29 N  514  ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE          
SEQRES  30 N  514  HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET          
SEQRES  31 N  514  GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR          
SEQRES  32 N  514  THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE          
SEQRES  33 N  514  MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS          
SEQRES  34 N  514  PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP          
SEQRES  35 N  514  TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER          
SEQRES  36 N  514  MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET          
SEQRES  37 N  514  VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU          
SEQRES  38 N  514  VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP          
SEQRES  39 N  514  LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU          
SEQRES  40 N  514  PRO THR TYR VAL ASN LEU LYS                                  
SEQRES   1 O  227  MET ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR          
SEQRES   2 O  227  SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS          
SEQRES   3 O  227  THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU          
SEQRES   4 O  227  TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS          
SEQRES   5 O  227  THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP          
SEQRES   6 O  227  THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU          
SEQRES   7 O  227  PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN          
SEQRES   8 O  227  ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP          
SEQRES   9 O  227  TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER          
SEQRES  10 O  227  PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO          
SEQRES  11 O  227  GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL          
SEQRES  12 O  227  LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER          
SEQRES  13 O  227  GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY          
SEQRES  14 O  227  LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR          
SEQRES  15 O  227  THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN          
SEQRES  16 O  227  CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO          
SEQRES  17 O  227  ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS          
SEQRES  18 O  227  TRP SER ALA SER MET LEU                                      
SEQRES   1 P  261  MET THR HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO          
SEQRES   2 P  261  SER PRO TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU          
SEQRES   3 P  261  MET THR SER GLY LEU THR MET TRP PHE HIS PHE ASN SER          
SEQRES   4 P  261  MET THR LEU LEU MET ILE GLY LEU THR THR ASN MET LEU          
SEQRES   5 P  261  THR MET TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER          
SEQRES   6 P  261  THR PHE GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY          
SEQRES   7 P  261  LEU ARG TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL          
SEQRES   8 P  261  LEU PHE PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER          
SEQRES   9 P  261  SER LEU ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO          
SEQRES  10 P  261  PRO THR GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO          
SEQRES  11 P  261  LEU LEU ASN THR SER VAL LEU LEU ALA SER GLY VAL SER          
SEQRES  12 P  261  ILE THR TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG          
SEQRES  13 P  261  LYS HIS MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU          
SEQRES  14 P  261  GLY VAL TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR          
SEQRES  15 P  261  GLU ALA PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER          
SEQRES  16 P  261  THR PHE PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL          
SEQRES  17 P  261  ILE ILE GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG          
SEQRES  18 P  261  GLN LEU LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY          
SEQRES  19 P  261  PHE GLU ALA GLY ALA TRP TYR TRP HIS PHE VAL ASP VAL          
SEQRES  20 P  261  VAL TRP LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY          
SEQRES  21 P  261  SER                                                          
SEQRES   1 Q  147  ALA HIS GLY SER VAL VAL LYS SER GLU ASP TYR ALA LEU          
SEQRES   2 Q  147  PRO SER TYR VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP          
SEQRES   3 Q  147  VAL ALA HIS VAL LYS ASN LEU SER ALA SER GLN LYS ALA          
SEQRES   4 Q  147  LEU LYS GLU LYS GLU LYS ALA SER TRP SER SER LEU SER          
SEQRES   5 Q  147  ILE ASP GLU LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS          
SEQRES   6 Q  147  GLU SER PHE ALA GLU MET ASN ARG SER THR ASN GLU TRP          
SEQRES   7 Q  147  LYS THR VAL VAL GLY ALA ALA MET PHE PHE ILE GLY PHE          
SEQRES   8 Q  147  THR ALA LEU LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR          
SEQRES   9 Q  147  GLY PRO ILE PRO HIS THR PHE GLU GLU GLU TRP VAL ALA          
SEQRES  10 Q  147  LYS GLN THR LYS ARG MET LEU ASP MET LYS VAL ALA PRO          
SEQRES  11 Q  147  ILE GLN GLY PHE SER ALA LYS TRP ASP TYR ASP LYS ASN          
SEQRES  12 Q  147  GLU TRP LYS LYS                                              
SEQRES   1 R  109  SER HIS GLY SER HIS GLU THR ASP GLU GLU PHE ASP ALA          
SEQRES   2 R  109  ARG TRP VAL THR TYR PHE ASN LYS PRO ASP ILE ASP ALA          
SEQRES   3 R  109  TRP GLU LEU ARG LYS GLY MET ASN THR LEU VAL GLY TYR          
SEQRES   4 R  109  ASP LEU VAL PRO GLU PRO LYS ILE ILE ASP ALA ALA LEU          
SEQRES   5 R  109  ARG ALA CYS ARG ARG LEU ASN ASP PHE ALA SER ALA VAL          
SEQRES   6 R  109  ARG ILE LEU GLU VAL VAL LYS ASP LYS ALA GLY PRO HIS          
SEQRES   7 R  109  LYS GLU ILE TYR PRO TYR VAL ILE GLN GLU LEU ARG PRO          
SEQRES   8 R  109  THR LEU ASN GLU LEU GLY ILE SER THR PRO GLU GLU LEU          
SEQRES   9 R  109  GLY LEU ASP LYS VAL                                          
SEQRES   1 S   98  ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA          
SEQRES   2 S   98  THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS          
SEQRES   3 S   98  GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR          
SEQRES   4 S   98  SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE          
SEQRES   5 S   98  THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP          
SEQRES   6 S   98  ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU          
SEQRES   7 S   98  ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU          
SEQRES   8 S   98  VAL PRO HIS GLN LEU ALA HIS                                  
SEQRES   1 T   84  ALA SER ALA ALA LYS GLY ASP HIS GLY GLY THR GLY ALA          
SEQRES   2 T   84  ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO          
SEQRES   3 T   84  SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER          
SEQRES   4 T   84  GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS          
SEQRES   5 T   84  LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY          
SEQRES   6 T   84  ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU          
SEQRES   7 T   84  PRO THR GLY TYR GLU LYS                                      
SEQRES   1 U   85  ALA GLU ASP ILE GLN ALA LYS ILE LYS ASN TYR GLN THR          
SEQRES   2 U   85  ALA PRO PHE ASP SER ARG PHE PRO ASN GLN ASN GLN THR          
SEQRES   3 U   85  ARG ASN CYS TRP GLN ASN TYR LEU ASP PHE HIS ARG CYS          
SEQRES   4 U   85  GLU LYS ALA MET THR ALA LYS GLY GLY ASP VAL SER VAL          
SEQRES   5 U   85  CYS GLU TRP TYR ARG ARG VAL TYR LYS SER LEU CYS PRO          
SEQRES   6 U   85  ILE SER TRP VAL SER THR TRP ASP ASP ARG ARG ALA GLU          
SEQRES   7 U   85  GLY THR PHE PRO GLY LYS ILE                                  
SEQRES   1 V   73  SER THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU          
SEQRES   2 V   73  ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET          
SEQRES   3 V   73  VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL          
SEQRES   4 V   73  ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG          
SEQRES   5 V   73  ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS          
SEQRES   6 V   73  ALA GLY ILE PHE GLN SER ALA LYS                              
SEQRES   1 W   59  PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN          
SEQRES   2 W   59  GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA          
SEQRES   3 W   59  THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS          
SEQRES   4 W   59  LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP          
SEQRES   5 W   59  ALA SER PHE PRO HIS LYS LYS                                  
SEQRES   1 X   56  ILE HIS GLN LYS ARG ALA PRO ASP PHE HIS ASP LYS TYR          
SEQRES   2 X   56  GLY ASN ALA VAL LEU ALA SER GLY ALA THR PHE CYS VAL          
SEQRES   3 X   56  ALA VAL TRP VAL TYR MET ALA THR GLN ILE GLY ILE GLU          
SEQRES   4 X   56  TRP ASN PRO SER PRO VAL GLY ARG VAL THR PRO LYS GLU          
SEQRES   5 X   56  TRP ARG GLU GLN                                              
SEQRES   1 Y   47  SER HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE          
SEQRES   2 Y   47  SER VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR          
SEQRES   3 Y   47  LEU PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE          
SEQRES   4 Y   47  VAL ARG HIS GLN LEU LEU LYS LYS                              
SEQRES   1 Z   46  ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS          
SEQRES   2 Z   46  GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE          
SEQRES   3 Z   46  LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN          
SEQRES   4 Z   46  TYR LYS LYS SER SER ALA ALA                                  
HET     CU  A 517       1                                                       
HET     MG  A 518       1                                                       
HET     CU  B 228       1                                                       
HET     CU  B 229       1                                                       
HET     ZN  F  99       1                                                       
HET     CU  N 517       1                                                       
HET     MG  N 518       1                                                       
HET     CU  O 228       1                                                       
HET     CU  O 229       1                                                       
HET     ZN  S  99       1                                                       
HET    HEA  A 515      60                                                       
HET    HEA  A 516      60                                                       
HET    HEA  N 515      60                                                       
HET    HEA  N 516      60                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     HEA HEME-A                                                           
FORMUL  27   CU    6(CU 2+)                                                     
FORMUL  28   MG    2(MG 2+)                                                     
FORMUL  31   ZN    2(ZN 2+)                                                     
FORMUL  37  HEA    4(C49 H56 FE N4 O6)                                          
HELIX    1   1 PHE A    2  TRP A    6  1                                   5    
HELIX    2   2 HIS A   12  LEU A   41  1                                  30    
HELIX    3   3 ASP A   51  PHE A   67  1                                  17    
HELIX    4   4 VAL A   70  ILE A   75  1                                   6    
HELIX    5   5 GLY A   77  ILE A   87  1                                  11    
HELIX    6   6 PRO A   95  SER A  116  1                                  22    
HELIX    7   7 ALA A  141  ASN A  170  1                                  30    
HELIX    8   8 GLN A  178  GLN A  180  5                                   3    
HELIX    9   9 LEU A  183  ASP A  212  1                                  30    
HELIX   10  10 PRO A  222  GLY A  224  5                                   3    
HELIX   11  11 PRO A  228  SER A  262  1                                  35    
HELIX   12  12 TYR A  270  PHE A  285  1                                  16    
HELIX   13  13 TRP A  288  HIS A  291  5                                   4    
HELIX   14  14 VAL A  299  LEU A  327  1                                  29    
HELIX   15  15 PRO A  336  ALA A  359  1                                  24    
HELIX   16  16 SER A  361  LEU A  367  1                                   7    
HELIX   17  17 TYR A  371  SER A  382  1                                  12    
HELIX   18  18 ALA A  385  SER A  401  1                                  17    
HELIX   19  19 ASP A  407  LEU A  433  1                                  27    
HELIX   20  20 ASP A  445  SER A  478  5                                  34    
HELIX   21  21 THR A  488  THR A  490  5                                   3    
HELIX   22  22 LEU A  492  ASN A  496  5                                   5    
HELIX   23  23 PRO B   15  MET B   45  1                                  31    
HELIX   24  24 GLU B   60  MET B   87  1                                  28    
HELIX   25  25 THR B  125  GLU B  127  5                                   3    
HELIX   26  26 PRO B  166  LEU B  168  5                                   3    
HELIX   27  27 LEU B  216  SER B  225  1                                  10    
HELIX   28  28 TRP C   16  PHE C   37  1                                  22    
HELIX   29  29 THR C   41  THR C   66  1                                  26    
HELIX   30  30 PRO C   73  LEU C  106  1                                  34    
HELIX   31  31 PRO C  110  LEU C  112  5                                   3    
HELIX   32  32 VAL C  129  GLU C  153  1                                  25    
HELIX   33  33 ARG C  156  GLU C  183  1                                  28    
HELIX   34  34 GLY C  191  LEU C  223  1                                  33    
HELIX   35  35 PHE C  233  SER C  255  1                                  23    
HELIX   36  36 SER D    8  ALA D   12  5                                   5    
HELIX   37  37 ALA D   35  LYS D   45  1                                  11    
HELIX   38  38 TRP D   48  SER D   50  5                                   3    
HELIX   39  39 ILE D   53  LYS D   63  1                                  11    
HELIX   40  40 PHE D   68  MET D   71  1                                   4    
HELIX   41  41 GLU D   77  TYR D  102  1                                  26    
HELIX   42  42 HIS D  109  PHE D  111  5                                   3    
HELIX   43  43 GLU D  113  ASP D  125  1                                  13    
HELIX   44  44 SER D  135  LYS D  137  5                                   3    
HELIX   45  45 ASP E    8  ASN E   20  1                                  13    
HELIX   46  46 ALA E   26  GLY E   38  1                                  13    
HELIX   47  47 PRO E   45  ARG E   57  1                                  13    
HELIX   48  48 PHE E   61  ALA E   75  1                                  15    
HELIX   49  49 LYS E   79  LEU E   96  1                                  18    
HELIX   50  50 PRO E  101  LEU E  104  1                                   4    
HELIX   51  51 ASP F    9  GLN F   12  1                                   4    
HELIX   52  52 GLY F   15  ARG F   25  1                                  11    
HELIX   53  53 ALA G   13  GLY G   22  1                                  10    
HELIX   54  54 ALA G   24  LEU G   37  1                                  14    
HELIX   55  55 SER H   18  PHE H   20  5                                   3    
HELIX   56  56 THR H   26  THR H   44  1                                  19    
HELIX   57  57 GLU H   54  LEU H   63  1                                  10    
HELIX   58  58 ILE H   66  GLU H   78  1                                  13    
HELIX   59  59 LEU I   12  ALA I   38  1                                  27    
HELIX   60  60 ALA I   40  ASN I   53  1                                  14    
HELIX   61  61 SER I   56  LYS I   65  1                                  10    
HELIX   62  62 VAL J    5  GLN J   13  1                                   9    
HELIX   63  63 ALA J   26  SER J   54  1                                  29    
HELIX   64  64 PHE K    9  GLN K   35  1                                  27    
HELIX   65  65 LYS L   18  LEU L   44  1                                  27    
HELIX   66  66 PRO M   12  TYR M   35  1                                  24    
HELIX   67  67 LEU M   37  LYS M   41  1                                   5    
HELIX   68  68 PHE N    2  TRP N    6  1                                   5    
HELIX   69  69 HIS N   12  LEU N   41  1                                  30    
HELIX   70  70 ASP N   51  PHE N   67  1                                  17    
HELIX   71  71 VAL N   70  ILE N   75  1                                   6    
HELIX   72  72 GLY N   77  ILE N   87  1                                  11    
HELIX   73  73 PRO N   95  SER N  116  1                                  22    
HELIX   74  74 ALA N  141  ASN N  170  1                                  30    
HELIX   75  75 GLN N  178  GLN N  180  5                                   3    
HELIX   76  76 LEU N  183  ASP N  212  1                                  30    
HELIX   77  77 PRO N  222  GLY N  224  5                                   3    
HELIX   78  78 PRO N  228  SER N  262  1                                  35    
HELIX   79  79 TYR N  270  PHE N  285  1                                  16    
HELIX   80  80 TRP N  288  HIS N  291  5                                   4    
HELIX   81  81 VAL N  299  LEU N  327  1                                  29    
HELIX   82  82 PRO N  336  ALA N  359  1                                  24    
HELIX   83  83 SER N  361  LEU N  367  1                                   7    
HELIX   84  84 TYR N  371  SER N  382  1                                  12    
HELIX   85  85 ALA N  385  SER N  401  1                                  17    
HELIX   86  86 ASP N  407  LEU N  433  1                                  27    
HELIX   87  87 ASP N  445  SER N  478  5                                  34    
HELIX   88  88 THR N  488  THR N  490  5                                   3    
HELIX   89  89 LEU N  492  ASN N  496  5                                   5    
HELIX   90  90 PRO O   15  MET O   45  1                                  31    
HELIX   91  91 GLU O   60  MET O   87  1                                  28    
HELIX   92  92 THR O  125  GLU O  127  5                                   3    
HELIX   93  93 PRO O  166  LEU O  168  5                                   3    
HELIX   94  94 LEU O  216  SER O  225  1                                  10    
HELIX   95  95 TRP P   16  PHE P   37  1                                  22    
HELIX   96  96 THR P   41  THR P   66  1                                  26    
HELIX   97  97 PRO P   73  LEU P  106  1                                  34    
HELIX   98  98 PRO P  110  LEU P  112  5                                   3    
HELIX   99  99 VAL P  129  GLU P  153  1                                  25    
HELIX  100 100 ARG P  156  GLU P  183  1                                  28    
HELIX  101 101 GLY P  191  LEU P  223  1                                  33    
HELIX  102 102 PHE P  233  SER P  255  1                                  23    
HELIX  103 103 SER Q    8  ALA Q   12  5                                   5    
HELIX  104 104 ALA Q   35  LYS Q   45  1                                  11    
HELIX  105 105 TRP Q   48  SER Q   50  5                                   3    
HELIX  106 106 ILE Q   53  LYS Q   63  1                                  11    
HELIX  107 107 PHE Q   68  MET Q   71  1                                   4    
HELIX  108 108 GLU Q   77  TYR Q  102  1                                  26    
HELIX  109 109 HIS Q  109  PHE Q  111  5                                   3    
HELIX  110 110 GLU Q  113  ASP Q  125  1                                  13    
HELIX  111 111 SER Q  135  LYS Q  137  5                                   3    
HELIX  112 112 ASP R    8  ASN R   20  1                                  13    
HELIX  113 113 ALA R   26  GLY R   38  1                                  13    
HELIX  114 114 PRO R   45  ARG R   57  1                                  13    
HELIX  115 115 PHE R   61  ALA R   75  1                                  15    
HELIX  116 116 LYS R   79  LEU R   96  1                                  18    
HELIX  117 117 PRO R  101  LEU R  104  1                                   4    
HELIX  118 118 ASP S    9  GLN S   12  1                                   4    
HELIX  119 119 GLY S   15  ARG S   25  1                                  11    
HELIX  120 120 ALA T   13  GLY T   22  1                                  10    
HELIX  121 121 ALA T   24  LEU T   37  1                                  14    
HELIX  122 122 SER U   18  PHE U   20  5                                   3    
HELIX  123 123 THR U   26  THR U   44  1                                  19    
HELIX  124 124 GLU U   54  LEU U   63  1                                  10    
HELIX  125 125 ILE U   66  GLU U   78  1                                  13    
HELIX  126 126 LEU V   12  ALA V   38  1                                  27    
HELIX  127 127 ALA V   40  ASN V   53  1                                  14    
HELIX  128 128 SER V   56  LYS V   65  1                                  10    
HELIX  129 129 VAL W    5  GLN W   13  1                                   9    
HELIX  130 130 ALA W   26  SER W   54  1                                  29    
HELIX  131 131 PHE X    9  GLN X   35  1                                  27    
HELIX  132 132 LYS Y   18  LEU Y   44  1                                  27    
HELIX  133 133 PRO Z   12  TYR Z   35  1                                  24    
HELIX  134 134 LEU Z   37  LYS Z   41  1                                   5    
SHEET    1   A 5 LEU B 116  SER B 120  0                                        
SHEET    2   A 5 TYR B 105  TYR B 110 -1  N  TYR B 110   O  LEU B 116           
SHEET    3   A 5 LEU B  95  HIS B 102 -1  N  HIS B 102   O  TYR B 105           
SHEET    4   A 5 ILE B 150  SER B 156  1  N  ARG B 151   O  LEU B  95           
SHEET    5   A 5 ASN B 180  LEU B 184 -1  N  LEU B 184   O  ILE B 150           
SHEET    1   B 3 VAL B 142  PRO B 145  0                                        
SHEET    2   B 3 ILE B 209  VAL B 214  1  N  GLU B 212   O  VAL B 142           
SHEET    3   B 3 GLY B 190  GLY B 194 -1  N  GLY B 194   O  ILE B 209           
SHEET    1   C 2 HIS B 161  VAL B 165  0                                        
SHEET    2   C 2 LEU B 170  ALA B 174 -1  N  ALA B 174   O  HIS B 161           
SHEET    1   D 3 ASN F  47  SER F  51  0                                        
SHEET    2   D 3 GLY F  86  PRO F  93  1  N  LYS F  90   O  ASN F  47           
SHEET    3   D 3 GLN F  80  CYS F  82 -1  N  CYS F  82   O  GLY F  86           
SHEET    1   E 2 LYS F  55  CYS F  60  0                                        
SHEET    2   E 2 ILE F  70  HIS F  75 -1  N  LEU F  74   O  ARG F  56           
SHEET    1   F 5 LEU O 116  SER O 120  0                                        
SHEET    2   F 5 TYR O 105  TYR O 110 -1  N  TYR O 110   O  LEU O 116           
SHEET    3   F 5 LEU O  95  HIS O 102 -1  N  HIS O 102   O  TYR O 105           
SHEET    4   F 5 ILE O 150  SER O 156  1  N  ARG O 151   O  LEU O  95           
SHEET    5   F 5 ASN O 180  LEU O 184 -1  N  LEU O 184   O  ILE O 150           
SHEET    1   G 3 VAL O 142  PRO O 145  0                                        
SHEET    2   G 3 ILE O 209  VAL O 214  1  N  GLU O 212   O  VAL O 142           
SHEET    3   G 3 GLY O 190  GLY O 194 -1  N  GLY O 194   O  ILE O 209           
SHEET    1   H 2 HIS O 161  VAL O 165  0                                        
SHEET    2   H 2 LEU O 170  ALA O 174 -1  N  ALA O 174   O  HIS O 161           
SHEET    1   I 3 ASN S  47  SER S  51  0                                        
SHEET    2   I 3 GLY S  86  PRO S  93  1  N  LYS S  90   O  ASN S  47           
SHEET    3   I 3 GLN S  80  CYS S  82 -1  N  CYS S  82   O  GLY S  86           
SHEET    1   J 2 LYS S  55  CYS S  60  0                                        
SHEET    2   J 2 ILE S  70  HIS S  75 -1  N  LEU S  74   O  ARG S  56           
SSBOND   1 CYS H   29    CYS H   64                          1555   1555  2.01  
SSBOND   2 CYS H   39    CYS H   53                          1555   1555  2.39  
SSBOND   3 CYS U   29    CYS U   64                          1555   1555  2.01  
SSBOND   4 CYS U   39    CYS U   53                          1555   1555  2.39  
LINK        FE   HEA A 515                 NE2 HIS A  61     1555   1555  1.83  
LINK        FE   HEA A 515                 NE2 HIS A 378     1555   1555  1.90  
LINK        FE   HEA A 516                 NE2 HIS A 376     1555   1555  2.08  
LINK        CU    CU A 517                 ND1 HIS A 240     1555   1555  1.85  
LINK        CU    CU A 517                 NE2 HIS A 290     1555   1555  2.16  
LINK        CU    CU A 517                 NE2 HIS A 291     1555   1555  2.15  
LINK        CU    CU B 228                 ND1 HIS B 161     1555   1555  1.89  
LINK        CU    CU B 228                 SG  CYS B 196     1555   1555  2.27  
LINK        CU    CU B 228                 SG  CYS B 200     1555   1555  2.30  
LINK        CU    CU B 228                CU    CU B 229     1555   1555  2.38  
LINK        CU    CU B 229                 SG  CYS B 196     1555   1555  2.26  
LINK        CU    CU B 229                 O   GLU B 198     1555   1555  2.19  
LINK        CU    CU B 229                 SG  CYS B 200     1555   1555  2.21  
LINK        CU    CU B 229                 ND1 HIS B 204     1555   1555  1.92  
LINK        FE   HEA N 515                 NE2 HIS N  61     1555   1555  1.83  
LINK        FE   HEA N 515                 NE2 HIS N 378     1555   1555  1.90  
LINK        FE   HEA N 516                 NE2 HIS N 376     1555   1555  2.08  
LINK        CU    CU N 517                 ND1 HIS N 240     1555   1555  1.85  
LINK        CU    CU N 517                 NE2 HIS N 290     1555   1555  2.16  
LINK        CU    CU N 517                 NE2 HIS N 291     1555   1555  2.15  
LINK        CU    CU O 228                 ND1 HIS O 161     1555   1555  1.89  
LINK        CU    CU O 228                 SG  CYS O 196     1555   1555  2.27  
LINK        CU    CU O 228                 SG  CYS O 200     1555   1555  2.30  
LINK        CU    CU O 228                CU    CU O 229     1555   1555  2.38  
LINK        CU    CU O 229                 SG  CYS O 196     1555   1555  2.26  
LINK        CU    CU O 229                 O   GLU O 198     1555   1555  2.19  
LINK        CU    CU O 229                 SG  CYS O 200     1555   1555  2.21  
LINK        CU    CU O 229                 ND1 HIS O 204     1555   1555  1.92  
LINK        MG    MG A 518                 OD2 ASP A 369     1555   1555  2.53  
LINK        MG    MG A 518                 NE2 HIS A 368     1555   1555  2.67  
LINK        MG    MG A 518                 OE1 GLU B 198     1555   1555  2.50  
LINK        CU    CU B 228                 SD  MET B 207     1555   1555  2.48  
LINK        ZN    ZN F  99                 SG  CYS F  62     1555   1555  2.50  
LINK        ZN    ZN F  99                 SG  CYS F  85     1555   1555  2.46  
LINK        ZN    ZN F  99                 SG  CYS F  60     1555   1555  2.43  
LINK        ZN    ZN F  99                 SG  CYS F  82     1555   1555  2.46  
LINK        MG    MG N 518                 OD2 ASP N 369     1555   1555  2.53  
LINK        MG    MG N 518                 NE2 HIS N 368     1555   1555  2.67  
LINK        MG    MG N 518                 OE1 GLU O 198     1555   1555  2.50  
LINK        CU    CU O 228                 SD  MET O 207     1555   1555  2.48  
LINK        ZN    ZN S  99                 SG  CYS S  85     1555   1555  2.46  
LINK        ZN    ZN S  99                 SG  CYS S  82     1555   1555  2.46  
LINK        ZN    ZN S  99                 SG  CYS S  62     1555   1555  2.50  
LINK        ZN    ZN S  99                 SG  CYS S  60     1555   1555  2.43  
CISPEP   1 PRO A  130    PRO A  131          0         0.26                     
CISPEP   2 CYS A  498    PRO A  499          0        -0.07                     
CISPEP   3 TRP C  116    PRO C  117          0        -0.09                     
CISPEP   4 PRO N  130    PRO N  131          0         0.22                     
CISPEP   5 CYS N  498    PRO N  499          0        -0.05                     
CISPEP   6 TRP P  116    PRO P  117          0        -0.11                     
SITE     1 AC1  3 HIS A 240  HIS A 290  HIS A 291                               
SITE     1 AC2  3 HIS A 368  ASP A 369  GLU B 198                               
SITE     1 AC3  5 HIS B 161  CYS B 196  CYS B 200  MET B 207                    
SITE     2 AC3  5  CU B 229                                                     
SITE     1 AC4  5 CYS B 196  GLU B 198  CYS B 200  HIS B 204                    
SITE     2 AC4  5  CU B 228                                                     
SITE     1 AC5  4 CYS F  60  CYS F  62  CYS F  82  CYS F  85                    
SITE     1 AC6  3 HIS N 240  HIS N 290  HIS N 291                               
SITE     1 AC7  3 HIS N 368  ASP N 369  GLU O 198                               
SITE     1 AC8  5 HIS O 161  CYS O 196  CYS O 200  MET O 207                    
SITE     2 AC8  5  CU O 229                                                     
SITE     1 AC9  5 CYS O 196  GLU O 198  CYS O 200  HIS O 204                    
SITE     2 AC9  5  CU O 228                                                     
SITE     1 BC1  4 CYS S  60  CYS S  62  CYS S  82  CYS S  85                    
SITE     1 BC2 23 GLY A  27  MET A  28  SER A  34  ILE A  37                    
SITE     2 BC2 23 ARG A  38  TYR A  54  VAL A  58  HIS A  61                    
SITE     3 BC2 23 ALA A  62  MET A  65  ILE A  66  VAL A  70                    
SITE     4 BC2 23 GLY A 125  TRP A 126  TYR A 371  PHE A 377                    
SITE     5 BC2 23 HIS A 378  SER A 382  PHE A 425  GLN A 428                    
SITE     6 BC2 23 ARG A 438  ARG A 439  MET A 468                               
SITE     1 BC3 22 TRP A 126  TRP A 236  VAL A 243  TYR A 244                    
SITE     2 BC3 22 HIS A 290  HIS A 291  THR A 309  ALA A 313                    
SITE     3 BC3 22 THR A 316  GLY A 317  GLY A 352  LEU A 353                    
SITE     4 BC3 22 GLY A 355  ILE A 356  LEU A 358  ALA A 359                    
SITE     5 BC3 22 ASP A 364  HIS A 368  HIS A 376  PHE A 377                    
SITE     6 BC3 22 VAL A 380  ARG A 438                                          
SITE     1 BC4 23 GLY N  27  MET N  28  SER N  34  ILE N  37                    
SITE     2 BC4 23 ARG N  38  TYR N  54  VAL N  58  HIS N  61                    
SITE     3 BC4 23 ALA N  62  MET N  65  ILE N  66  VAL N  70                    
SITE     4 BC4 23 GLY N 125  TRP N 126  TYR N 371  PHE N 377                    
SITE     5 BC4 23 HIS N 378  SER N 382  PHE N 425  GLN N 428                    
SITE     6 BC4 23 ARG N 438  ARG N 439  MET N 468                               
SITE     1 BC5 22 TRP N 126  TRP N 236  VAL N 243  TYR N 244                    
SITE     2 BC5 22 HIS N 290  HIS N 291  THR N 309  ALA N 313                    
SITE     3 BC5 22 THR N 316  GLY N 317  GLY N 352  LEU N 353                    
SITE     4 BC5 22 GLY N 355  ILE N 356  LEU N 358  ALA N 359                    
SITE     5 BC5 22 ASP N 364  HIS N 368  HIS N 376  PHE N 377                    
SITE     6 BC5 22 VAL N 380  ARG N 438                                          
CRYST1  189.100  210.500  178.600  90.00  90.00  90.00 P 21 21 21    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      0.005288  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004751  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005599        0.00000                         
MTRIX1   1 -0.993860 -0.001000  0.110650      170.59108    1                    
MTRIX2   1  0.000890 -1.000000 -0.001010      638.15674    1                    
MTRIX3   1  0.110650 -0.000900  0.993860       -9.16846    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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