GenomeNet

Database: PDB
Entry: 5O10
LinkDB: 5O10
Original site: 5O10 
HEADER    ELECTRON TRANSFER, APOPTOSIS            17-MAY-17   5O10              
TITLE     Y48H MUTANT OF HUMAN CYTOCHROME C                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYCS, CYC;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    HEME, HAEM, CYTOCHROME C, METALLOPROTEIN, ELECTRON TRANSFER,          
KEYWDS   2 APOPTOSIS                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MORENO-CHICANO,O.M.DEACON,M.A.HOUGH,J.A.R.WORRALL                   
REVDAT   1   28-MAR-18 5O10    0                                                
JRNL        AUTH   O.M.DEACON,A.I.KARSISIOTIS,T.MORENO-CHICANO,M.A.HOUGH,       
JRNL        AUTH 2 C.MACDONALD,T.M.A.BLUMENSCHEIN,M.T.WILSON,G.R.MOORE,         
JRNL        AUTH 3 J.A.R.WORRALL                                                
JRNL        TITL   HEIGHTENED DYNAMICS OF THE OXIDIZED Y48H VARIANT OF HUMAN    
JRNL        TITL 2 CYTOCHROME C INCREASES ITS PEROXIDATIC ACTIVITY.             
JRNL        REF    BIOCHEMISTRY                  V.  56  6111 2017              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   29083920                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.7B00890                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.36 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 43449                          
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) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2362                            
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) : 1.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3043                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 162                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1628                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 214                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45000                                              
REMARK   3    B22 (A**2) : 0.44000                                              
REMARK   3    B33 (A**2) : -0.34000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.37000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.056         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.052         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.035         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.963         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1800 ; 0.015 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1715 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2434 ; 2.179 ; 2.087       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4009 ; 2.604 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   214 ; 6.386 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    66 ;28.119 ;24.848       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   345 ;12.700 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;25.496 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   236 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1973 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   324 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3515 ; 2.110 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   152 ;22.279 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3524 ; 7.515 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5O10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1200005011.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45812                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.11500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3ZCF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 33% PEG 6000 100MM TRIS PH 7.5, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       18.24900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A    8   NZ                                                  
REMARK 480     LYS A   22   CE   NZ                                             
REMARK 480     LYS A   25   CE   NZ                                             
REMARK 480     LYS A   72   NZ                                                  
REMARK 480     LYS A   86   CD   CE   NZ                                        
REMARK 480     LYS A   87   CD   CE   NZ                                        
REMARK 480     LYS A   88   NZ                                                  
REMARK 480     GLU B    4   CG   CD   OE1  OE2                                  
REMARK 480     LYS B    5   CE   NZ                                             
REMARK 480     MET B   12   CE                                                  
REMARK 480     GLU B   21   CD   OE1  OE2                                       
REMARK 480     LYS B   22   CE   NZ                                             
REMARK 480     LYS B   53   NZ                                                  
REMARK 480     LYS B   86   CG   CD   CE   NZ                                   
REMARK 480     LYS B   87   CD   CE   NZ                                        
REMARK 480     GLU B   89   CG   CD   OE1  OE2                                  
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    GLU B 104   CD    GLU B 104   OE2    -0.073                       
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    ARG B  91   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B  91   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 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     -140.92   -122.41                                   
REMARK 500    ASN A  70       86.67   -163.75                                   
REMARK 500    ASN A  70       86.67   -160.57                                   
REMARK 500    LYS B  27     -141.17   -117.96                                   
REMARK 500    ASN B  70       87.93   -163.86                                   
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 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 HEC A 201   NA   90.7                                              
REMARK 620 3 HEC A 201   NB   87.2  91.9                                        
REMARK 620 4 HEC A 201   NC   90.3 178.8  87.5                                  
REMARK 620 5 HEC A 201   ND   91.5  88.0 178.7  92.5                            
REMARK 620 6 MET A  80   SD  175.9  85.2  93.3  93.8  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  18   NE2                                                    
REMARK 620 2 HEC B 201   NA   88.8                                              
REMARK 620 3 HEC B 201   NB   89.3  89.9                                        
REMARK 620 4 HEC B 201   NC   91.4 179.6  90.5                                  
REMARK 620 5 HEC B 201   ND   89.7  89.6 179.0  90.0                            
REMARK 620 6 MET B  80   SD  174.6  86.3  93.0  93.4  87.8                      
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 HEC A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEC B 201 and CYS B    
REMARK 800  17                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEC B 201 and CYS B    
REMARK 800  14                                                                  
DBREF  5O10 A    1   104  UNP    P99999   CYC_HUMAN        2    105             
DBREF  5O10 B    1   104  UNP    P99999   CYC_HUMAN        2    105             
SEQADV 5O10 HIS A   48  UNP  P99999    TYR    49 ENGINEERED MUTATION            
SEQADV 5O10 HIS B   48  UNP  P99999    TYR    49 ENGINEERED MUTATION            
SEQRES   1 A  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE ILE MET LYS          
SEQRES   2 A  104  CYS SER GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 A  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 A  104  THR GLY GLN ALA PRO GLY TYR SER HIS THR ALA ALA ASN          
SEQRES   5 A  104  LYS ASN LYS GLY ILE ILE TRP GLY GLU ASP THR LEU MET          
SEQRES   6 A  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 A  104  LYS MET ILE PHE VAL GLY ILE LYS LYS LYS GLU GLU ARG          
SEQRES   8 A  104  ALA ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 B  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE ILE MET LYS          
SEQRES   2 B  104  CYS SER 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 TYR SER HIS THR ALA ALA ASN          
SEQRES   5 B  104  LYS ASN LYS GLY ILE ILE TRP GLY GLU ASP 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 VAL GLY ILE LYS LYS LYS GLU GLU ARG          
SEQRES   8 B  104  ALA ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
HET    HEC  A 201      43                                                       
HET    HEC  B 201      43                                                       
HETNAM     HEC HEME C                                                           
FORMUL   3  HEC    2(C34 H34 FE N4 O4)                                          
FORMUL   5  HOH   *214(H2 O)                                                    
HELIX    1 AA1 ASP A    2  CYS A   14  1                                  13    
HELIX    2 AA2 THR A   49  LYS A   55  1                                   7    
HELIX    3 AA3 GLY A   60  ASN A   70  1                                  11    
HELIX    4 AA4 ASN A   70  ILE A   75  1                                   6    
HELIX    5 AA5 LYS A   87  THR A  102  1                                  16    
HELIX    6 AA6 ASP B    2  CYS B   14  1                                  13    
HELIX    7 AA7 THR B   49  LYS B   55  1                                   7    
HELIX    8 AA8 GLY B   60  ASN B   70  1                                  11    
HELIX    9 AA9 ASN B   70  ILE B   75  1                                   6    
HELIX   10 AB1 LYS B   87  THR B  102  1                                  16    
LINK         SG  CYS A  14                 CAB HEC A 201     1555   1555  1.78  
LINK         SG  CYS A  17                 CAC HEC A 201     1555   1555  1.83  
LINK         NE2 HIS A  18                FE   HEC A 201     1555   1555  1.99  
LINK         SD  MET A  80                FE   HEC A 201     1555   1555  2.26  
LINK         SG  CYS B  14                 CAB HEC B 201     1555   1555  1.77  
LINK         SG  CYS B  17                 CAC HEC B 201     1555   1555  1.83  
LINK         NE2 HIS B  18                FE   HEC B 201     1555   1555  2.05  
LINK         SD  MET B  80                FE   HEC B 201     1555   1555  2.33  
SITE     1 AC1 21 LYS A  13  CYS A  14  CYS A  17  HIS A  18                    
SITE     2 AC1 21 THR A  28  GLY A  29  PRO A  30  ARG A  38                    
SITE     3 AC1 21 GLY A  41  TYR A  46  HIS A  48  THR A  49                    
SITE     4 AC1 21 ASN A  52  TRP A  59  TYR A  67  THR A  78                    
SITE     5 AC1 21 LYS A  79  MET A  80  ILE A  81  PHE A  82                    
SITE     6 AC1 21 HOH A 304                                                     
SITE     1 AC2 24 LYS A  55  LYS B  13  CYS B  14  SER B  15                    
SITE     2 AC2 24 GLN B  16  HIS B  18  LYS B  27  THR B  28                    
SITE     3 AC2 24 GLY B  29  PRO B  30  ARG B  38  GLY B  41                    
SITE     4 AC2 24 TYR B  46  HIS B  48  THR B  49  ASN B  52                    
SITE     5 AC2 24 TRP B  59  THR B  78  LYS B  79  MET B  80                    
SITE     6 AC2 24 ILE B  81  PHE B  82  ILE B  85  HOH B 303                    
SITE     1 AC3 24 LYS A  55  PHE B  10  LYS B  13  SER B  15                    
SITE     2 AC3 24 GLN B  16  CYS B  17  HIS B  18  THR B  28                    
SITE     3 AC3 24 GLY B  29  PRO B  30  ARG B  38  GLY B  41                    
SITE     4 AC3 24 TYR B  46  HIS B  48  THR B  49  ASN B  52                    
SITE     5 AC3 24 TRP B  59  THR B  78  LYS B  79  MET B  80                    
SITE     6 AC3 24 ILE B  81  PHE B  82  ILE B  85  HOH B 303                    
CRYST1   56.937   36.498   60.700  90.00 116.65  90.00 P 1 21 1      4          
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      0.017563  0.000000  0.008813        0.00000                         
SCALE2      0.000000  0.027399  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018432        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system