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Database: PDB
Entry: 1U75
LinkDB: 1U75
Original site: 1U75 
HEADER    OXIDOREDUCTASE                          02-AUG-04   1U75              
TITLE     ELECTRON TRANSFER COMPLEX BETWEEN HORSE HEART CYTOCHROME C AND ZINC-  
TITLE    2 PORPHYRIN SUBSTITUTED CYTOCHROME C PEROXIDASE                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C PEROXIDASE;                                   
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 1.11.1.5;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CYTOCHROME C;                                              
COMPND   8 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: YEAST;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7CCP;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE  13 ORGANISM_COMMON: HORSE;                                              
SOURCE  14 ORGANISM_TAXID: 9796;                                                
SOURCE  15 OTHER_DETAILS: HORSE HEART                                           
KEYWDS    PROTEIN-PROTEIN COMPLEX, HEME, OXIDOREDUCTASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.R.CRANE,S.A.KANG                                                    
REVDAT   3   13-JUL-11 1U75    1       VERSN                                    
REVDAT   2   24-FEB-09 1U75    1       VERSN                                    
REVDAT   1   28-SEP-04 1U75    0                                                
JRNL        AUTH   S.A.KANG,P.J.MARJAVAARA,B.R.CRANE                            
JRNL        TITL   ELECTRON TRANSFER BETWEEN CYTOCHROME C AND CYTOCHOME C       
JRNL        TITL 2 PEROXIDASE IN SINGLE CRYSTALS.                               
JRNL        REF    J.AM.CHEM.SOC.                V. 126 10836 2004              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   15339156                                                     
JRNL        DOI    10.1021/JA049230U                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.9999                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 32279                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.273                           
REMARK   3   R VALUE            (WORKING SET) : 0.271                           
REMARK   3   FREE R VALUE                     : 0.306                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1685                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2305                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 128                          
REMARK   3   BIN FREE R VALUE                    : 0.4340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5573                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 139                                     
REMARK   3   SOLVENT ATOMS            : 320                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.85000                                             
REMARK   3    B22 (A**2) : -0.85000                                             
REMARK   3    B33 (A**2) : 1.69000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.605         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.343         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.326         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.815        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5890 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7996 ; 2.217 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   689 ; 1.545 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   290 ;43.118 ;24.966       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   971 ;22.602 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;25.815 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   785 ; 0.154 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4594 ; 0.018 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2317 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   157 ; 0.184 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.050 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    42 ; 0.233 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 1.021 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3544 ; 1.586 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5520 ; 2.528 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2775 ; 4.563 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2470 ; 5.905 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     294      5                      
REMARK   3           1     C      1       C     294      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):     72 ;  1.60 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):     60 ;  2.93 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):     72 ;  3.20 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):     60 ;  4.44 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   104                          
REMARK   3    RESIDUE RANGE :   B  1101        B  1101                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2263  52.5677  59.6992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6466 T22:   0.6340                                     
REMARK   3      T33:   0.9773 T12:   0.0102                                     
REMARK   3      T13:   0.3319 T23:  -0.3610                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3473 L22:   5.9370                                     
REMARK   3      L33:  11.3178 L12:   0.4514                                     
REMARK   3      L13:  -3.8025 L23:   4.1218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5952 S12:  -1.2781 S13:   1.4903                       
REMARK   3      S21:   0.5576 S22:   0.8028 S23:  -1.1242                       
REMARK   3      S31:  -1.7368 S32:   1.0713 S33:  -1.3980                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   294                          
REMARK   3    RESIDUE RANGE :   A  1001        A  1001                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.9207  27.5789  40.3568              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1988 T22:  -0.1703                                     
REMARK   3      T33:  -0.2260 T12:   0.0541                                     
REMARK   3      T13:  -0.0029 T23:   0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7245 L22:   2.9650                                     
REMARK   3      L33:   1.9683 L12:   0.0267                                     
REMARK   3      L13:  -0.5743 L23:  -0.6638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1318 S12:  -0.1019 S13:  -0.0080                       
REMARK   3      S21:  -0.1421 S22:   0.1907 S23:   0.2260                       
REMARK   3      S31:   0.1061 S32:   0.0031 S33:  -0.0590                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   294                          
REMARK   3    RESIDUE RANGE :   C  1201        C  1201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.1101   1.0437  33.9368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1070 T22:  -0.1935                                     
REMARK   3      T33:  -0.1417 T12:   0.0215                                     
REMARK   3      T13:   0.1071 T23:   0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6021 L22:   4.1773                                     
REMARK   3      L33:   2.1900 L12:   0.2908                                     
REMARK   3      L13:  -0.4126 L23:  -1.3190                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1421 S12:  -0.0123 S13:  -0.1859                       
REMARK   3      S21:  -0.2388 S22:   0.0875 S23:  -0.1065                       
REMARK   3      S31:  -0.0778 S32:  -0.0491 S33:   0.0546                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1U75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023329.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 78                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9363                             
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34216                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 2PCB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PH 7.0, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.44200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.23250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.23250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      140.16300            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.23250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.23250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       46.72100            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.23250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.23250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      140.16300            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.23250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.23250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       46.72100            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       93.44200            
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: THE BIOLOGICAL ASSEMBLY IS A TRIMER CONTAINING TWO           
REMARK 300 MOLECULES OF CYTOCHROME C PEROXIDASE AND ONE MOLECULE OF CYTOCHROME  
REMARK 300 C                                                                    
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B1982  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -1                                                      
REMARK 465     ILE A     0                                                      
REMARK 465     MET C    -1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1886     O    HOH A  1994              0.25            
REMARK 500   O    ILE B    85     NH1  ARG B    91              1.51            
REMARK 500   O1   PO4 C  2202     NA   ZNH C  1201              1.81            
REMARK 500   O1   PO4 C  2202     ND   ZNH C  1201              1.84            
REMARK 500   CD1  TRP A    51     O2   PO4 A  2201              1.92            
REMARK 500   N    VAL A     7     O    HOH A  2002              2.01            
REMARK 500   OE1  GLU A   135     O    HOH A  2012              2.05            
REMARK 500   O3   PO4 C  2202     NA   ZNH C  1201              2.10            
REMARK 500   SG   CYS B    14     CBB  HEM B  1101              2.15            
REMARK 500   N    SER C    66     O    HOH C  1998              2.16            
REMARK 500   O1   PO4 A  2201     NA   ZNH A  1001              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2017     O    HOH C  1999     8565     0.59            
REMARK 500   O    HOH A  2015     O    HOH C  1401     8565     0.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR A   1   C     THR A   1   O       0.116                       
REMARK 500    THR A   2   C     PRO A   3   N       0.146                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A   3   C   -  N   -  CA  ANGL. DEV. =  31.6 DEGREES          
REMARK 500    PRO A   3   C   -  N   -  CD  ANGL. DEV. = -26.2 DEGREES          
REMARK 500    LEU B  64   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    PHE C  77   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A   2     -176.58     44.66                                   
REMARK 500    PRO A   3       78.56   -117.80                                   
REMARK 500    GLU A  11      108.79    -54.91                                   
REMARK 500    LYS A  12      108.57    -16.65                                   
REMARK 500    SER A  15     -165.33   -105.86                                   
REMARK 500    ASP A  33       43.83    -90.03                                   
REMARK 500    THR A  70        5.90    -67.23                                   
REMARK 500    GLU A 135      -34.13    -35.12                                   
REMARK 500    ASN A 184      -64.32   -101.94                                   
REMARK 500    ALA A 194       76.88   -102.35                                   
REMARK 500    PRO A 277     -169.97    -69.62                                   
REMARK 500    ASP A 279       48.22    -80.05                                   
REMARK 500    LYS B  27     -122.11   -104.59                                   
REMARK 500    ALA B  43      110.42    -39.22                                   
REMARK 500    ALA B  51      -40.85    175.94                                   
REMARK 500    LEU B  64        0.23    147.06                                   
REMARK 500    LYS B 100      -70.85    -86.45                                   
REMARK 500    ASN B 103      -55.93   -145.47                                   
REMARK 500    THR C   1      122.36   -170.50                                   
REMARK 500    LYS C  12       99.79    -48.40                                   
REMARK 500    ASP C  33       47.54    -94.26                                   
REMARK 500    ASP C  34        0.50    -68.04                                   
REMARK 500    MET C 119       31.52    -92.67                                   
REMARK 500    LYS C 149     -151.99   -108.10                                   
REMARK 500    ASN C 196       20.49   -141.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  67         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR B  63         10.29                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A   4        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS A  12        23.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS A  74        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 195        23.9      L          L   OUTSIDE RANGE           
REMARK 500    GLN B  42        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN B  52        23.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  62        23.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU C  35        24.0      L          L   OUTSIDE RANGE           
REMARK 500    TYR C  39        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 239        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1496        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH A1584        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH A1596        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH A1658        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A1747        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A1808        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A1831        DISTANCE =  8.20 ANGSTROMS                       
REMARK 525    HOH A1835        DISTANCE =  7.50 ANGSTROMS                       
REMARK 525    HOH A1867        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A1877        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH A1880        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A1883        DISTANCE =  9.50 ANGSTROMS                       
REMARK 525    HOH A1884        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH A1892        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH A1893        DISTANCE =  9.50 ANGSTROMS                       
REMARK 525    HOH A1894        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH A1895        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A1896        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH A1898        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH A1900        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A1904        DISTANCE =  8.36 ANGSTROMS                       
REMARK 525    HOH A1907        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A1908        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH A1925        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH A1932        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A1981        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH B1667        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH B1670        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH B1683        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH B1748        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B1849        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B1850        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH B1913        DISTANCE =  7.68 ANGSTROMS                       
REMARK 525    HOH B1914        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B1915        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH B1919        DISTANCE =  9.03 ANGSTROMS                       
REMARK 525    HOH B1920        DISTANCE =  7.67 ANGSTROMS                       
REMARK 525    HOH B1939        DISTANCE =  9.22 ANGSTROMS                       
REMARK 525    HOH B1983        DISTANCE = 11.69 ANGSTROMS                       
REMARK 525    HOH B1984        DISTANCE =  8.84 ANGSTROMS                       
REMARK 525    HOH C1556        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH C1709        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH C1778        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH C1787        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH C1853        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH C1905        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH C1936        DISTANCE =  9.22 ANGSTROMS                       
REMARK 525    HOH C1938        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH C1940        DISTANCE = 12.12 ANGSTROMS                       
REMARK 525    HOH C1941        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH C1946        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH C1947        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH C1948        DISTANCE =  8.02 ANGSTROMS                       
REMARK 525    HOH C1951        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH C1955        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH C1957        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH C1959        DISTANCE =  8.30 ANGSTROMS                       
REMARK 525    HOH C1960        DISTANCE =  8.05 ANGSTROMS                       
REMARK 525    HOH C1961        DISTANCE = 12.62 ANGSTROMS                       
REMARK 525    HOH C1964        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH C1968        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH C1969        DISTANCE =  8.61 ANGSTROMS                       
REMARK 525    HOH C1970        DISTANCE = 10.42 ANGSTROMS                       
REMARK 525    HOH C1971        DISTANCE = 10.72 ANGSTROMS                       
REMARK 525    HOH C1972        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH C2001        DISTANCE =  7.73 ANGSTROMS                       
REMARK 525    HOH C2019        DISTANCE =  5.50 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B1101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  18   NE2                                                    
REMARK 620 2 HEM B1101   NA   89.6                                              
REMARK 620 3 HEM B1101   NB   94.3  87.2                                        
REMARK 620 4 HEM B1101   NC  105.1 165.3  92.8                                  
REMARK 620 5 HEM B1101   ND   92.0  90.4 173.2  87.9                            
REMARK 620 6 MET B  80   SD  161.0  71.4  84.1  93.9  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ZNH A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 A2201   O1                                                     
REMARK 620 2 ZNH A1001   NA   73.4                                              
REMARK 620 3 ZNH A1001   NB   42.4  88.4                                        
REMARK 620 4 ZNH A1001   NC   82.8 148.4  87.7                                  
REMARK 620 5 ZNH A1001   ND  113.4  87.2 155.4  83.5                            
REMARK 620 6 HIS A 175   NE2 140.2 110.8  97.8 100.7 106.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ZNH C1201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 C2202   O1                                                     
REMARK 620 2 ZNH C1201   NA   58.7                                              
REMARK 620 3 ZNH C1201   NB   96.7  85.2                                        
REMARK 620 4 ZNH C1201   NC   98.0 154.6  88.3                                  
REMARK 620 5 ZNH C1201   ND   63.0  86.8 159.3  90.8                            
REMARK 620 6 HIS C 175   NE2 158.2 112.8 102.6  92.5  98.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 2202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZNH A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZNH C 1201                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1U74   RELATED DB: PDB                                   
REMARK 900 ELECTRON TRANSFER COMPLEX BETWEEN YEAST CYTOCHROME C AND             
REMARK 900 ZINE-PORPHYRIN SUBSTITUTED CYTOCHROME C PEROXIDASE                   
DBREF  1U75 A    1   294  GB     171177   AAA88709        69    362             
DBREF  1U75 C    1   294  GB     171177   AAA88709        69    362             
DBREF  1U75 B    1   104  UNP    P00004   CYC_HORSE        1    104             
SEQADV 1U75 MET A   -1  GB   171177              CLONING ARTIFACT               
SEQADV 1U75 ILE A    0  GB   171177              CLONING ARTIFACT               
SEQADV 1U75 MET C   -1  GB   171177              CLONING ARTIFACT               
SEQADV 1U75 ILE C    0  GB   171177              CLONING ARTIFACT               
SEQRES   1 A  296  MET ILE THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU          
SEQRES   2 A  296  LYS GLY ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN          
SEQRES   3 A  296  ALA ILE ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP          
SEQRES   4 A  296  ASN TYR ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA          
SEQRES   5 A  296  TRP HIS ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR          
SEQRES   6 A  296  GLY GLY SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU          
SEQRES   7 A  296  PHE ASN ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE          
SEQRES   8 A  296  LYS PHE LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE          
SEQRES   9 A  296  SER SER GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA          
SEQRES  10 A  296  VAL GLN GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS          
SEQRES  11 A  296  GLY ARG VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN          
SEQRES  12 A  296  GLY ARG LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL          
SEQRES  13 A  296  ARG THR PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU          
SEQRES  14 A  296  VAL VAL ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR          
SEQRES  15 A  296  HIS LEU LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA          
SEQRES  16 A  296  ALA ASN ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU          
SEQRES  17 A  296  LEU ASN GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN          
SEQRES  18 A  296  ASN GLU GLN TRP ASP SER LYS SER GLY TYR MET MET LEU          
SEQRES  19 A  296  PRO THR ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU          
SEQRES  20 A  296  SER ILE VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE          
SEQRES  21 A  296  PHE LYS ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU          
SEQRES  22 A  296  ASN GLY ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE          
SEQRES  23 A  296  ILE PHE LYS THR LEU GLU GLU GLN GLY LEU                      
SEQRES   1 B  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 B  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 B  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 B  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 B  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 B  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 B  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 B  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 C  296  MET ILE THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU          
SEQRES   2 C  296  LYS GLY ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN          
SEQRES   3 C  296  ALA ILE ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP          
SEQRES   4 C  296  ASN TYR ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA          
SEQRES   5 C  296  TRP HIS ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR          
SEQRES   6 C  296  GLY GLY SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU          
SEQRES   7 C  296  PHE ASN ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE          
SEQRES   8 C  296  LYS PHE LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE          
SEQRES   9 C  296  SER SER GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA          
SEQRES  10 C  296  VAL GLN GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS          
SEQRES  11 C  296  GLY ARG VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN          
SEQRES  12 C  296  GLY ARG LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL          
SEQRES  13 C  296  ARG THR PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU          
SEQRES  14 C  296  VAL VAL ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR          
SEQRES  15 C  296  HIS LEU LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA          
SEQRES  16 C  296  ALA ASN ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU          
SEQRES  17 C  296  LEU ASN GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN          
SEQRES  18 C  296  ASN GLU GLN TRP ASP SER LYS SER GLY TYR MET MET LEU          
SEQRES  19 C  296  PRO THR ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU          
SEQRES  20 C  296  SER ILE VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE          
SEQRES  21 C  296  PHE LYS ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU          
SEQRES  22 C  296  ASN GLY ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE          
SEQRES  23 C  296  ILE PHE LYS THR LEU GLU GLU GLN GLY LEU                      
HET    PO4  A2201       5                                                       
HET    PO4  C2202       5                                                       
HET    ZNH  A1001      43                                                       
HET    HEM  B1101      43                                                       
HET    ZNH  C1201      43                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ZNH PROTOPORPHYRIN IX CONTAINING ZN                                  
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   4  PO4    2(O4 P 3-)                                                   
FORMUL   6  ZNH    2(C34 H32 N4 O4 ZN)                                          
FORMUL   7  HEM    C34 H32 FE N4 O4                                             
FORMUL   9  HOH   *320(H2 O)                                                    
HELIX    1   1 SER A   15  ASP A   33  1                                  19    
HELIX    2   2 GLU A   35  ILE A   40  1                                   6    
HELIX    3   3 TYR A   42  GLY A   55  1                                  14    
HELIX    4   4 GLY A   69  ARG A   72  5                                   4    
HELIX    5   5 PHE A   73  ASN A   78  1                                   6    
HELIX    6   6 ASP A   79  GLY A   84  5                                   6    
HELIX    7   7 LEU A   85  PHE A   99  1                                  15    
HELIX    8   8 SER A  103  MET A  119  1                                  17    
HELIX    9   9 PRO A  134  THR A  138  5                                   5    
HELIX   10  10 ASP A  150  ARG A  160  1                                  11    
HELIX   11  11 ASN A  164  MET A  172  1                                   9    
HELIX   12  12 GLY A  173  LEU A  177  5                                   5    
HELIX   13  13 HIS A  181  GLY A  186  1                                   6    
HELIX   14  14 ASN A  200  GLU A  209  1                                  10    
HELIX   15  15 LEU A  232  ASP A  241  1                                  10    
HELIX   16  16 ASP A  241  ASP A  254  1                                  14    
HELIX   17  17 ASP A  254  ASN A  272  1                                  19    
HELIX   18  18 THR A  288  GLY A  293  5                                   6    
HELIX   19  19 LYS B    5  CYS B   14  1                                  10    
HELIX   20  20 ASN B   52  GLY B   56  5                                   5    
HELIX   21  21 LYS B   87  THR B  102  1                                  16    
HELIX   22  22 SER C   15  ASP C   33  1                                  19    
HELIX   23  23 GLU C   35  ILE C   40  1                                   6    
HELIX   24  24 TYR C   42  GLY C   55  1                                  14    
HELIX   25  25 GLY C   69  ARG C   72  5                                   4    
HELIX   26  26 PHE C   73  ASN C   78  1                                   6    
HELIX   27  27 ASP C   79  ALA C   83  5                                   5    
HELIX   28  28 LEU C   85  PHE C   99  1                                  15    
HELIX   29  29 SER C  103  MET C  119  1                                  17    
HELIX   30  30 PRO C  134  THR C  138  5                                   5    
HELIX   31  31 ASP C  150  ARG C  160  1                                  11    
HELIX   32  32 ASN C  164  MET C  172  1                                   9    
HELIX   33  33 GLY C  173  LEU C  177  5                                   5    
HELIX   34  34 HIS C  181  GLY C  186  1                                   6    
HELIX   35  35 ASN C  200  GLU C  209  1                                  10    
HELIX   36  36 LEU C  232  SER C  237  1                                   6    
HELIX   37  37 ASP C  241  ASP C  254  1                                  14    
HELIX   38  38 ASP C  254  ASN C  272  1                                  19    
SHEET    1   A 2 HIS A   6  VAL A   7  0                                        
SHEET    2   A 2 ILE A 274  THR A 275  1  O  THR A 275   N  HIS A   6           
SHEET    1   B 2 LYS A 179  THR A 180  0                                        
SHEET    2   B 2 GLY A 189  PRO A 190 -1  O  GLY A 189   N  THR A 180           
SHEET    1   C 3 LYS A 212  LYS A 215  0                                        
SHEET    2   C 3 GLU A 221  ASP A 224 -1  O  ASP A 224   N  LYS A 212           
SHEET    3   C 3 MET A 230  MET A 231 -1  O  MET A 231   N  TRP A 223           
SHEET    1   D 2 LYS C 179  THR C 180  0                                        
SHEET    2   D 2 GLY C 189  PRO C 190 -1  O  GLY C 189   N  THR C 180           
SHEET    1   E 3 TRP C 211  LYS C 215  0                                        
SHEET    2   E 3 GLU C 221  SER C 225 -1  O  ASP C 224   N  LYS C 212           
SHEET    3   E 3 MET C 230  MET C 231 -1  O  MET C 231   N  TRP C 223           
LINK        FE   HEM B1101                 NE2 HIS B  18     1555   1555  2.04  
LINK         NE1 TRP A  51                 O2  PO4 A2201     1555   1555  1.39  
LINK         NB  ZNH A1001                 O1  PO4 A2201     1555   1555  1.36  
LINK        ZN   ZNH A1001                 O1  PO4 A2201     1555   1555  1.57  
LINK        ZN   ZNH A1001                 NE2 HIS A 175     1555   1555  1.95  
LINK         SG  CYS B  14                 CAB HEM B1101     1555   1555  1.71  
LINK        FE   HEM B1101                 SD  MET B  80     1555   1555  2.70  
LINK        ZN   ZNH C1201                 O1  PO4 C2202     1555   1555  1.19  
LINK        ZN   ZNH C1201                 NE2 HIS C 175     1555   1555  2.10  
CISPEP   1 THR A    2    PRO A    3          0        -2.55                     
SITE     1 AC1  6 ARG A  48  TRP A  51  HIS A  52  HIS A 175                    
SITE     2 AC1  6 ZNH A1001  HOH A2004                                          
SITE     1 AC2  5 ARG C  48  TRP C  51  HIS C  52  HIS C 175                    
SITE     2 AC2  5 ZNH C1201                                                     
SITE     1 AC3 20 PRO A  44  ARG A  48  TRP A  51  LEU A 171                    
SITE     2 AC3 20 MET A 172  ALA A 174  HIS A 175  LEU A 177                    
SITE     3 AC3 20 GLY A 178  LYS A 179  THR A 180  HIS A 181                    
SITE     4 AC3 20 ASN A 184  SER A 185  TRP A 191  LEU A 232                    
SITE     5 AC3 20 THR A 234  PHE A 266  HOH A2004  PO4 A2201                    
SITE     1 AC4 17 LYS B  13  CYS B  14  CYS B  17  HIS B  18                    
SITE     2 AC4 17 THR B  28  THR B  40  GLY B  41  GLN B  42                    
SITE     3 AC4 17 TYR B  48  THR B  49  ASN B  52  TRP B  59                    
SITE     4 AC4 17 TYR B  67  THR B  78  LYS B  79  MET B  80                    
SITE     5 AC4 17 PHE B  82                                                     
SITE     1 AC5 17 PRO C  44  ARG C  48  TRP C  51  PRO C 145                    
SITE     2 AC5 17 ASP C 146  LEU C 171  ALA C 174  HIS C 175                    
SITE     3 AC5 17 GLY C 178  LYS C 179  HIS C 181  ASN C 184                    
SITE     4 AC5 17 SER C 185  TRP C 191  HOH C1422  HOH C1534                    
SITE     5 AC5 17 PO4 C2202                                                     
CRYST1  104.465  104.465  186.884  90.00  90.00  90.00 P 43 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009573  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009573  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005351        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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