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Entry: 1CRC
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HEADER    MITOCHONDRIAL ELECTRON TRANSPORT        22-MAR-95   1CRC              
TITLE     CYTOCHROME C AT LOW IONIC STRENGTH                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C;                                              
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   3 ORGANISM_COMMON: HORSE;                                              
SOURCE   4 ORGANISM_TAXID: 9796;                                                
SOURCE   5 ORGAN: HEART                                                         
KEYWDS    FERRIC FORM, LOW IONIC STRENGTH, MITOCHONDRIAL ELECTRON               
KEYWDS   2 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.SANISHVILI,K.W.VOLZ,E.M.WESTBROOK,E.MARGOLIASH                      
REVDAT   2   24-FEB-09 1CRC    1       VERSN                                    
REVDAT   1   08-MAR-96 1CRC    0                                                
JRNL        AUTH   R.SANISHVILI,K.W.VOLZ,E.M.WESTBROOK,E.MARGOLIASH             
JRNL        TITL   THE LOW IONIC STRENGTH CRYSTAL STRUCTURE OF HORSE            
JRNL        TITL 2 CYTOCHROME C AT 2.1 A RESOLUTION AND COMPARISON              
JRNL        TITL 3 WITH ITS HIGH IONIC STRENGTH COUNTERPART.                    
JRNL        REF    STRUCTURE                     V.   3   707 1995              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   8591047                                                      
JRNL        DOI    10.1016/S0969-2126(01)00205-2                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.SANISHVILI,E.MARGOLIASH,M.L.WESTBROOK,                     
REMARK   1  AUTH 2 E.M.WESTBROOK,K.W.VOLZ                                       
REMARK   1  TITL   CRYSTALLIZATION OF WILD-TYPE AND MUTANT                      
REMARK   1  TITL 2 FERRICYTOCHROMES C AT LOW IONIC STRENGTH: SEEDING            
REMARK   1  TITL 3 TECHNIQUE AND X-RAY DIFFRACTION ANALYSIS                     
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  50   687 1994              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT, PROLSQ                                       
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 60.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 7684                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1727                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.017 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.057 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.060 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.012 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.182 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.244 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.354 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.323 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.000 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 22.000; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.080 ; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 0.100 ; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 0.070 ; 1.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 0.100 ; 0.150               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE SIDE CHAINS OF RESIDUES LYS 72        
REMARK   3  AND LYS 87 IN MOLECULE A COULD BE FITTED TO THE ELECTRON            
REMARK   3  DENSITY IN MORE THAN ONE CONFORMATION BUT THESE ARE NOT             
REMARK   3  CLEARLY EXPRESSED ROTAMERS. THEY ARE IDENTIFIED AS 'C' IN THE       
REMARK   3  ALTERNATE LOCATIONS COLUMN. THE SIDE CHAINS OF RESIDUES LYS 8,      
REMARK   3  LYS 53, GLU 61, LYS 86 AND LYS 100 IN MOLECULE B HAVE               
REMARK   3  ROTAMERS. THEY ARE DESIGNATED 'D' IN THE ALTERNATE                  
REMARK   3  CONFORMATIONS COLUMN. THE SIDE CHAINS OF RESIDUES LYS 22, LYS       
REMARK   3  72 AND LYS 88 IN MOLECULE B COULD BE FITTED TO THE ELECTRON         
REMARK   3  DENSITY IN MORE THAN ONE CONFORMATION BUT THESE ARE NOT             
REMARK   3  CLEARLY EXPRESSED ROTAMERS. THEY ARE IDENTIFIED AS 'D' IN THE       
REMARK   3  ALTERNATE LOCATIONS COLUMN.                                         
REMARK   4                                                                      
REMARK   4 1CRC 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-JUL-92                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : XENTRONICS                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8803                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 65.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.03960                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       27.81000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       17.55500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.50500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       17.55500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.81000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.50500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    LYS B    39     O    HOH B   110              1.70            
REMARK 500   OG1  THR A    49     O2D  HEM A   105              2.07            
REMARK 500   OD1  ASN B    52     O    HOH B   109              2.16            
REMARK 500   O    THR A    47     NZ   LYS A    79              2.18            
REMARK 500   OE1  GLU B     4     O    HOH B   155              2.18            
REMARK 500   O    THR B    40     O    HOH B   123              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   OE2  GLU B    62     NZ   LYS B    86     2654     2.08            
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    ASP A   2   CB  -  CG  -  OD2 ANGL. DEV. =  10.9 DEGREES          
REMARK 500    GLU A   4   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    VAL A  11   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ALA A  15   CB  -  CA  -  C   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    HIS A  18   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    GLU A  21   CG  -  CD  -  OE2 ANGL. DEV. =  12.5 DEGREES          
REMARK 500    LYS A  22   CD  -  CE  -  NZ  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    ARG A  38   N   -  CA  -  CB  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    ARG A  38   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    THR A  40   CA  -  CB  -  CG2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    GLN A  42   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    THR A  47   CA  -  CB  -  CG2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP A  50   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ASP A  50   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    LYS A  53   N   -  CA  -  CB  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    TYR A  67   CB  -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    GLU A  69   CG  -  CD  -  OE1 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    GLU A  69   CG  -  CD  -  OE2 ANGL. DEV. = -21.4 DEGREES          
REMARK 500    PHE A  82   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A  91   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A  93   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TYR A  97   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    VAL B  11   CG1 -  CB  -  CG2 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    GLN B  16   O   -  C   -  N   ANGL. DEV. =  11.6 DEGREES          
REMARK 500    LYS B  25   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    PRO B  30   O   -  C   -  N   ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG B  38   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    PHE B  46   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    THR B  49   N   -  CA  -  CB  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ASP B  50   CA  -  CB  -  CG  ANGL. DEV. =  37.1 DEGREES          
REMARK 500    ASP B  50   CB  -  CG  -  OD1 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ALA B  51   N   -  CA  -  CB  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    TRP B  59   O   -  C   -  N   ANGL. DEV. =  11.1 DEGREES          
REMARK 500    GLU B  61   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    GLU B  62   CG  -  CD  -  OE1 ANGL. DEV. =  13.6 DEGREES          
REMARK 500    GLU B  62   O   -  C   -  N   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    TYR B  67   O   -  C   -  N   ANGL. DEV. =   9.9 DEGREES          
REMARK 500    LYS B  88   CA  -  C   -  O   ANGL. DEV. =  14.1 DEGREES          
REMARK 500    THR B  89   N   -  CA  -  CB  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ARG B  91   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG B  91   NE  -  CZ  -  NH2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    GLU B  90   O   -  C   -  N   ANGL. DEV. =  10.1 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    LYS A  27     -142.25   -115.53                                   
REMARK 500    PHE A  36      104.54    -51.22                                   
REMARK 500    ASN A  70       86.87   -159.81                                   
REMARK 500    PHE A  82      117.32   -165.43                                   
REMARK 500    LYS A 100      -70.21    -69.70                                   
REMARK 500    LYS B  13       -9.37   -165.20                                   
REMARK 500    HIS B  26      135.28    -38.55                                   
REMARK 500    LYS B  27     -147.94   -112.24                                   
REMARK 500    HIS B  33      103.95    -46.78                                   
REMARK 500    TYR B  48     -177.31    -60.49                                   
REMARK 500    THR B  49     -115.49    -69.99                                   
REMARK 500    ASP B  50      -12.34   -167.01                                   
REMARK 500    GLU B  61      -28.50    -38.40                                   
REMARK 500    ASN B  70       82.96   -168.47                                   
REMARK 500    TYR B  74      -72.57    -81.20                                   
REMARK 500    ILE B  75       67.19   -112.22                                   
REMARK 500    LYS B 100     -104.33    -69.73                                   
REMARK 500    ALA B 101      -46.42    -22.57                                   
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 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: (11X,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     GLU A  61        24.9      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 B 107        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH B 146        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH A 158        DISTANCE =  5.74 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 COMPND                                                               
REMARK 600   MOLECULE: CYTOCHROME C.  THE HEME IS OXIDIZED (FE 3+).             
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 A 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 MET A  80   SD  171.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  18   NE2                                                    
REMARK 620 2 MET B  80   SD  174.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 105                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 105                 
DBREF  1CRC A    1   104  UNP    P00004   CYC_HORSE        1    104             
DBREF  1CRC B    1   104  UNP    P00004   CYC_HORSE        1    104             
SEQRES   1 A  105  ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN          
SEQRES   2 A  105  LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS          
SEQRES   3 A  105  HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG          
SEQRES   4 A  105  LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA          
SEQRES   5 A  105  ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU          
SEQRES   6 A  105  MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY          
SEQRES   7 A  105  THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU          
SEQRES   8 A  105  ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN          
SEQRES   9 A  105  GLU                                                          
SEQRES   1 B  105  ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN          
SEQRES   2 B  105  LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS          
SEQRES   3 B  105  HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG          
SEQRES   4 B  105  LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA          
SEQRES   5 B  105  ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU          
SEQRES   6 B  105  MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY          
SEQRES   7 B  105  THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU          
SEQRES   8 B  105  ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN          
SEQRES   9 B  105  GLU                                                          
HET    ACE  A   0       3                                                       
HET    ACE  B   0       3                                                       
HET    HEM  A 105      43                                                       
HET    HEM  B 105      43                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   1  ACE    2(C2 H4 O)                                                   
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   5  HOH   *120(H2 O)                                                    
HELIX    1   1 ASP A    2  CYS A   14  1                                  13    
HELIX    2   2 THR A   49  LYS A   55  1                                   7    
HELIX    3   3 LYS A   60  GLU A   69  1                                  10    
HELIX    4   4 ASN A   70  ILE A   75  1                                   6    
HELIX    5   5 LYS A   87  GLU A  104  1                                  18    
HELIX    6   6 ASP B    2  CYS B   14  1                                  13    
HELIX    7   7 LYS B   60  GLU B   69  1                                  10    
HELIX    8   8 ASN B   70  ILE B   75  1                                   6    
HELIX    9   9 LYS B   87  GLU B  104  1                                  18    
LINK         C   ACE A   0                 N   GLY A   1     1555   1555  1.37  
LINK         C   ACE B   0                 N   GLY B   1     1555   1555  1.35  
LINK         SG  CYS A  14                 CAB HEM A 105     1555   1555  1.81  
LINK         SG  CYS A  17                 CAC HEM A 105     1555   1555  1.86  
LINK        FE   HEM A 105                 NE2 HIS A  18     1555   1555  2.17  
LINK        FE   HEM A 105                 SD  MET A  80     1555   1555  2.66  
LINK         SG  CYS B  14                 CAB HEM B 105     1555   1555  1.73  
LINK         SG  CYS B  17                 CAC HEM B 105     1555   1555  1.79  
LINK         NE2 HIS B  18                FE   HEM B 105     1555   1555  1.96  
LINK         SD  MET B  80                FE   HEM B 105     1555   1555  2.02  
SITE     1 AC1 20 LYS A  13  CYS A  14  CYS A  17  HIS A  18                    
SITE     2 AC1 20 GLY A  29  PRO A  30  THR A  40  GLY A  41                    
SITE     3 AC1 20 TYR A  48  THR A  49  ASN A  52  TRP A  59                    
SITE     4 AC1 20 TYR A  67  THR A  78  LYS A  79  MET A  80                    
SITE     5 AC1 20 ILE A  81  PHE A  82  HOH A 107  HOH A 110                    
SITE     1 AC2 24 LYS A  55  LYS B  13  CYS B  14  CYS B  17                    
SITE     2 AC2 24 HIS B  18  THR B  28  PRO B  30  LEU B  32                    
SITE     3 AC2 24 LEU B  35  THR B  40  GLY B  41  GLN B  42                    
SITE     4 AC2 24 PHE B  46  TYR B  48  THR B  49  ASN B  52                    
SITE     5 AC2 24 TRP B  59  TYR B  67  THR B  78  LYS B  79                    
SITE     6 AC2 24 MET B  80  ILE B  81  PHE B  82  HOH B 112                    
CRYST1   55.620  105.010   35.110  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      0.017979  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.028482        0.00000                         
HETATM    1  C   ACE A   0       6.678  30.002  -8.077  1.00 18.66           C  
HETATM    2  O   ACE A   0       5.617  30.099  -8.722  1.00 17.70           O  
HETATM    3  CH3 ACE A   0       8.016  30.384  -8.645  1.00 18.46           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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