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Database: PDB
Entry: 1CTY
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Original site: 1CTY 
HEADER    ELECTRON TRANSPORT (HEME PROTEIN)       15-FEB-93   1CTY              
TITLE     MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL
TITLE    2 HEME ENVIRONMENT                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932                                                 
KEYWDS    ELECTRON TRANSPORT (HEME PROTEIN)                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.BERGHUIS,G.D.BRAYER                                               
REVDAT   4   03-MAR-21 1CTY    1       COMPND REMARK SEQADV HET                 
REVDAT   4 2                   1       HETNAM HETSYN FORMUL LINK                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   29-NOV-17 1CTY    1       HELIX                                    
REVDAT   2   24-FEB-09 1CTY    1       VERSN                                    
REVDAT   1   15-JUL-93 1CTY    0                                                
JRNL        AUTH   A.M.BERGHUIS,J.G.GUILLEMETTE,M.SMITH,G.D.BRAYER              
JRNL        TITL   MUTATION OF TYROSINE-67 TO PHENYLALANINE IN CYTOCHROME C     
JRNL        TITL 2 SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT.             
JRNL        REF    J.MOL.BIOL.                   V. 235  1326 1994              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8308895                                                      
JRNL        DOI    10.1006/JMBI.1994.1086                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.M.BERGHUIS,G.D.BRAYER                                      
REMARK   1  TITL   OXIDATION STATE-DEPENDENT CONFORMATIONAL CHANGES IN          
REMARK   1  TITL 2 CYTOCHROME C                                                 
REMARK   1  REF    J.MOL.BIOL.                   V. 223   959 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.V.LOUIE,G.D.BRAYER                                         
REMARK   1  TITL   HIGH-RESOLUTION REFINEMENT OF YEAST ISO-1-CYTOCHROME C AND   
REMARK   1  TITL 2 COMPARISONS WITH OTHER EUKARYOTIC CYTOCHROMES C              
REMARK   1  REF    J.MOL.BIOL.                   V. 214   527 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   G.V.LOUIE,G.D.BRAYER                                         
REMARK   1  TITL   A POLYPEPTIDE CHAIN-REFOLDING EVENT OCCURS IN THE GLY82      
REMARK   1  TITL 2 VARIANT OF YEAST ISO-1-CYTOCHROME C                          
REMARK   1  REF    J.MOL.BIOL.                   V. 210   313 1989              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   C.J.LEUNG,B.T.NALL,G.D.BRAYER                                
REMARK   1  TITL   CRYSTALLIZATION OF YEAST ISO-2-CYTOCHROME C USING A NOVEL    
REMARK   1  TITL 2 HAIR SEEDING TECHNIQUE                                       
REMARK   1  REF    J.MOL.BIOL.                   V. 206   783 1989              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   G.V.LOUIE,W.L.B.HUTCHEON,G.D.BRAYER                          
REMARK   1  TITL   YEAST ISO-1-CYTOCHROME C. A 2.8 ANGSTROM RESOLUTION          
REMARK   1  TITL 2 THREE-DIMENSIONAL STRUCTURE DETERMINATION                    
REMARK   1  REF    J.MOL.BIOL.                   V. 199   295 1988              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   G.V.LOUIE,G.J.PIELAK,M.SMITH,G.D.BRAYER                      
REMARK   1  TITL   ROLE OF PHENYLALANINE-82 IN YEAST ISO-1-CYTOCHROME C AND     
REMARK   1  TITL 2 REMOTE CONFORMATIONAL CHANGES INDUCED BY A SERINE RESIDUE AT 
REMARK   1  TITL 3 THIS POSITION                                                
REMARK   1  REF    BIOCHEMISTRY                  V.  27  7870 1988              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
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            : 850                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 30                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.020 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.046 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000172532.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.54000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       18.23500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       18.23500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      104.31000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       18.23500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       18.23500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       34.77000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       18.23500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       18.23500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      104.31000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       18.23500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       18.23500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       34.77000            
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       69.54000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THIS PROTEIN HAS BEEN STABILIZED FOR ANALYSES BY THE                 
REMARK 400 MUTATION OF CYSTEINE 102 TO A THREONINE RESIDUE.                     
REMARK 400                                                                      
REMARK 400 IN TURN T5 THE H-BOND IS MEDIATED THROUGH A WATER MOLECULE.          
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   CG2  THR A    -5     O    ASN A    56     7555     1.66            
REMARK 500   CG2  THR A    -5     C    ASN A    56     7555     1.88            
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    GLY A  29   N     GLY A  29   CA      0.094                       
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    LEU A   9   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    LEU A   9   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    PHE A  10   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    CYS A  14   CA  -  CB  -  SG  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    GLU A  21   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    GLU A  21   OE1 -  CD  -  OE2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG A  38   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    GLU A  44   OE1 -  CD  -  OE2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    GLU A  44   CG  -  CD  -  OE2 ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ASP A  50   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    LEU A  58   CB  -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    ASP A  60   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TYR A  74   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LYS A  89   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A  91   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ASP A  93   CB  -  CG  -  OD1 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ASP A  93   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 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    GLU A  -4       40.54   -147.71                                   
REMARK 500    LYS A  27     -131.15   -134.58                                   
REMARK 500    ASN A  70      102.12   -163.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                             HEC A 104  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 HEC A 104   NA   90.4                                              
REMARK 620 3 HEC A 104   NB   90.9  89.7                                        
REMARK 620 4 HEC A 104   NC   88.8 178.9  89.5                                  
REMARK 620 5 HEC A 104   ND   87.6  91.9 177.8  88.9                            
REMARK 620 6 MET A  80   SD  172.0  95.6  94.4  85.3  86.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 THE END OF THE 50 HELIX (RESIDUE 55) IS DISTORTED.                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 RESIDUES IN SHEET S1 FORM A HIGHLY DISTORTED BETA TYPE               
REMARK 700 CONFORMATION.                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 104                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YCC   RELATED DB: PDB                                   
REMARK 900 REDUCED - WILD-TYPE                                                  
REMARK 900 RELATED ID: 2YCC   RELATED DB: PDB                                   
REMARK 900 OXIDIZED - C102T MUTANT                                              
REMARK 900 RELATED ID: 1CTZ   RELATED DB: PDB                                   
REMARK 900 REDUCED - Y67F, C102T MUTANT                                         
DBREF  1CTY A   -5   103  UNP    P00044   CYC1_YEAST       1    108             
SEQADV 1CTY PHE A   67  UNP  P00044    TYR    72 CONFLICT                       
SEQADV 1CTY THR A  102  UNP  P00044    CYS   107 CONFLICT                       
SEQRES   1 A  108  THR GLU PHE LYS ALA GLY SER ALA LYS LYS GLY ALA THR          
SEQRES   2 A  108  LEU PHE LYS THR ARG CYS LEU GLN CYS HIS THR VAL GLU          
SEQRES   3 A  108  LYS GLY GLY PRO HIS LYS VAL GLY PRO ASN LEU HIS GLY          
SEQRES   4 A  108  ILE PHE GLY ARG HIS SER GLY GLN ALA GLU GLY TYR SER          
SEQRES   5 A  108  TYR THR ASP ALA ASN ILE LYS LYS ASN VAL LEU TRP ASP          
SEQRES   6 A  108  GLU ASN ASN MET SER GLU PHE LEU THR ASN PRO M3L LYS          
SEQRES   7 A  108  TYR ILE PRO GLY THR LYS MET ALA PHE GLY GLY LEU LYS          
SEQRES   8 A  108  LYS GLU LYS ASP ARG ASN ASP LEU ILE THR TYR LEU LYS          
SEQRES   9 A  108  LYS ALA THR GLU                                              
MODRES 1CTY M3L A   72  LYS  N-TRIMETHYLLYSINE                                  
HET    M3L  A  72      12                                                       
HET    SO4  A 117       5                                                       
HET    HEC  A 104      43                                                       
HETNAM     M3L N-TRIMETHYLLYSINE                                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEC HEME C                                                           
FORMUL   1  M3L    C9 H21 N2 O2 1+                                              
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  HEC    C34 H34 FE N4 O4                                             
FORMUL   4  HOH   *30(H2 O)                                                     
HELIX    1  NT SER A    2  CYS A   14  1                                  13    
HELIX    2  50 THR A   49  LYS A   55  1RESIDUE 55 DISTORTED               7    
HELIX    3  60 ASP A   60  ASN A   70  1                                  11    
HELIX    4  70 ASN A   70  ILE A   75  1                                   6    
HELIX    5  CT LYS A   87  THR A  102  1                                  16    
SHEET    1  S1 2 GLY A  37  SER A  40  0                                        
SHEET    2  S1 2 VAL A  57  TRP A  59 -1  O  VAL A  57   N  SER A  40           
LINK         SG  CYS A  14                 CAB HEC A 104     1555   1555  1.79  
LINK         SG  CYS A  17                 CAC HEC A 104     1555   1555  1.77  
LINK         C   PRO A  71                 N   M3L A  72     1555   1555  1.31  
LINK         C   M3L A  72                 N   LYS A  73     1555   1555  1.29  
LINK         NE2 HIS A  18                FE   HEC A 104     1555   1555  2.05  
LINK         SD  MET A  80                FE   HEC A 104     1555   1555  2.44  
SITE     1 AC1  7 GLY A   1  SER A   2  ALA A   3  LYS A   4                    
SITE     2 AC1  7 SER A  47  LYS A  73  HOH A 164                               
SITE     1 AC2 21 ARG A  13  CYS A  14  CYS A  17  HIS A  18                    
SITE     2 AC2 21 GLY A  23  GLY A  29  ILE A  35  SER A  40                    
SITE     3 AC2 21 GLY A  41  TYR A  48  THR A  49  ASN A  52                    
SITE     4 AC2 21 TRP A  59  MET A  64  PHE A  67  LEU A  68                    
SITE     5 AC2 21 THR A  78  LYS A  79  MET A  80  LEU A  94                    
SITE     6 AC2 21 HOH A 121                                                     
CRYST1   36.470   36.470  139.080  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.027420  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.027420  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007190        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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