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Database: PDB
Entry: 4NFG
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Original site: 4NFG 
HEADER    OXIDOREDUCTASE/ELECTRON TRANSPORT       31-OCT-13   4NFG              
TITLE     K13R MUTANT OF HORSE CYTOCHROME C AND YEAST CYTOCHROME C PEROXIDASE   
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CCP;                                                        
COMPND   5 EC: 1.11.1.5;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYTOCHROME C;                                              
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: CCP1, CCP, CPO, YKR066C;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE  10 ORGANISM_COMMON: DOMESTIC HORSE,EQUINE;                              
SOURCE  11 ORGANISM_TAXID: 9796;                                                
SOURCE  12 GENE: CYCS, CYC;                                                     
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE/ELECTRON TRANSPORT, OXIDOREDUCTASE-ELECTRON TRANSPORT  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.M.MEULENBROEK,Q.BASHIR,M.UBBINK,N.S.PANNU                           
REVDAT   2   12-NOV-14 4NFG    1       JRNL                                     
REVDAT   1   24-SEP-14 4NFG    0                                                
JRNL        AUTH   Q.BASHIR,E.M.MEULENBROEK,N.S.PANNU,M.UBBINK                  
JRNL        TITL   ENGINEERING SPECIFICITY IN A DYNAMIC PROTEIN COMPLEX WITH A  
JRNL        TITL 2 SINGLE CONSERVED MUTATION.                                   
JRNL        REF    FEBS J.                       V. 281  4892 2014              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   25180929                                                     
JRNL        DOI    10.1111/FEBS.13028                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.11 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23185                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1221                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.11                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.17                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1588                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 94                           
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3188                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 302                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.46000                                             
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : 0.45000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.237         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.123         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.542         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3371 ; 0.016 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3106 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4574 ; 1.944 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7169 ; 0.895 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   395 ; 6.135 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   164 ;33.517 ;25.061       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   571 ;15.021 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;24.050 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   451 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3859 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   798 ; 0.008 ; 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):  1586 ; 1.224 ; 1.517       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1585 ; 1.224 ; 1.516       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1979 ; 1.895 ; 2.266       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1785 ; 1.602 ; 1.650       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   294                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3840  10.9550 -14.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0032 T22:   0.0668                                     
REMARK   3      T33:   0.0836 T12:  -0.0015                                     
REMARK   3      T13:  -0.0063 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5763 L22:   1.2488                                     
REMARK   3      L33:   0.7338 L12:   0.0073                                     
REMARK   3      L13:   0.0953 L23:   0.1672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0371 S12:   0.0701 S13:  -0.0153                       
REMARK   3      S21:   0.0118 S22:   0.0206 S23:  -0.0923                       
REMARK   3      S31:   0.0108 S32:   0.0104 S33:  -0.0578                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   104                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2720  16.0850 -41.7640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0805 T22:   0.0654                                     
REMARK   3      T33:   0.0380 T12:   0.0142                                     
REMARK   3      T13:  -0.0022 T23:   0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6742 L22:   1.5706                                     
REMARK   3      L33:   1.9704 L12:  -0.0986                                     
REMARK   3      L13:   0.1929 L23:   0.6564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0266 S12:   0.2033 S13:   0.0199                       
REMARK   3      S21:  -0.0776 S22:   0.0015 S23:  -0.0223                       
REMARK   3      S31:   0.1828 S32:   0.0754 S33:   0.0251                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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                                                           
REMARK   4                                                                      
REMARK   4 4NFG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083135.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24499                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2PCC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 150 MM NACL, 0.5 MM 1:1    
REMARK 280  RATIO OF HORSE CYTOCHROME C AND YEAST CYTOCHROME C PEROXIDASE, PH   
REMARK 280  7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                  
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       22.44500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.37000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.37000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.44500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 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 146   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ASP A 150   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 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    ASP A 254       89.45   -151.45                                   
REMARK 500    LYS B  27     -134.55   -111.68                                   
REMARK 500    LYS B  60     -177.30   -172.88                                   
REMARK 500    ASN B  70       91.10   -163.12                                   
REMARK 500    PHE B  82      113.69   -160.25                                   
REMARK 500    ASN B 103       38.06   -140.23                                   
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                             HEM A 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 175   NE2                                                    
REMARK 620 2 HEM A 301   NA   94.1                                              
REMARK 620 3 HEM A 301   NB   91.1  89.5                                        
REMARK 620 4 HEM A 301   NC   85.9 178.7  89.2                                  
REMARK 620 5 HEM A 301   ND   89.7  90.7 179.2  90.5                            
REMARK 620 6 UNX A 302  UNK  177.8  83.9  87.9  96.0  91.4                      
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   87.3                                              
REMARK 620 3 HEC B 201   NB   90.7  89.9                                        
REMARK 620 4 HEC B 201   NC   92.0 179.2  90.5                                  
REMARK 620 5 HEC B 201   ND   88.5  90.5 179.1  89.2                            
REMARK 620 6 MET B  80   SD  168.5  83.2  95.8  97.4  85.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 201                 
DBREF  4NFG A    4   294  UNP    P00431   CCPR_YEAST      71    361             
DBREF  4NFG B    1   104  UNP    P00004   CYC_HORSE        2    105             
SEQADV 4NFG MET A    1  UNP  P00431              EXPRESSION TAG                 
SEQADV 4NFG LYS A    2  UNP  P00431              EXPRESSION TAG                 
SEQADV 4NFG THR A    3  UNP  P00431              EXPRESSION TAG                 
SEQADV 4NFG ALA A  128  UNP  P00431    CYS   195 CONFLICT                       
SEQADV 4NFG ARG B   13  UNP  P00004    LYS    14 ENGINEERED MUTATION            
SEQADV 4NFG ASN B   26  UNP  P00004    HIS    27 CONFLICT                       
SEQADV 4NFG ASN B   33  UNP  P00004    HIS    34 CONFLICT                       
SEQRES   1 A  294  MET LYS THR LEU VAL HIS VAL ALA SER VAL GLU LYS GLY          
SEQRES   2 A  294  ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE          
SEQRES   3 A  294  ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR          
SEQRES   4 A  294  ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS          
SEQRES   5 A  294  THR SER GLY THR TRP ASP LYS HIS ASP ASN THR GLY GLY          
SEQRES   6 A  294  SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU PHE ASN          
SEQRES   7 A  294  ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE          
SEQRES   8 A  294  LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE SER SER          
SEQRES   9 A  294  GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA VAL GLN          
SEQRES  10 A  294  GLU MET GLN GLY PRO LYS ILE PRO TRP ARG ALA GLY ARG          
SEQRES  11 A  294  VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN GLY ARG          
SEQRES  12 A  294  LEU PRO ASP ALA ASP LYS ASP ALA ASP TYR VAL ARG THR          
SEQRES  13 A  294  PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU VAL VAL          
SEQRES  14 A  294  ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR HIS LEU          
SEQRES  15 A  294  LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA ALA ASN          
SEQRES  16 A  294  ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU LEU ASN          
SEQRES  17 A  294  GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN ASN GLU          
SEQRES  18 A  294  GLN TRP ASP SER LYS SER GLY TYR MET MET LEU PRO THR          
SEQRES  19 A  294  ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU SER ILE          
SEQRES  20 A  294  VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE PHE LYS          
SEQRES  21 A  294  ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU ASN GLY          
SEQRES  22 A  294  ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE ILE PHE          
SEQRES  23 A  294  LYS THR LEU GLU GLU GLN GLY LEU                              
SEQRES   1 B  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN ARG          
SEQRES   2 B  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS ASN          
SEQRES   3 B  104  LYS THR GLY PRO ASN LEU ASN GLY LEU PHE GLY ARG LYS          
SEQRES   4 B  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 B  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 B  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 B  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 B  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
HET    HEM  A 301      43                                                       
HET    UNX  A 302       1                                                       
HET    HEC  B 201      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     HEC HEME C                                                           
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    C34 H32 FE N4 O4                                             
FORMUL   4  UNX    X                                                            
FORMUL   5  HEC    C34 H34 FE N4 O4                                             
FORMUL   6  HOH   *302(H2 O)                                                    
HELIX    1   1 SER A   15  ASP A   33  1                                  19    
HELIX    2   2 GLU A   35  ILE A   40  1                                   6    
HELIX    3   3 TYR A   42  GLY A   55  1                                  14    
HELIX    4   4 GLY A   69  ARG A   72  5                                   4    
HELIX    5   5 PHE A   73  ASN A   78  1                                   6    
HELIX    6   6 ASP A   79  GLY A   84  5                                   6    
HELIX    7   7 LEU A   85  PHE A   99  1                                  15    
HELIX    8   8 SER A  103  MET A  119  1                                  17    
HELIX    9   9 PRO A  134  THR A  138  5                                   5    
HELIX   10  10 ASP A  150  ARG A  160  1                                  11    
HELIX   11  11 ASN A  164  GLY A  173  1                                  10    
HELIX   12  12 ALA A  174  LEU A  177  5                                   4    
HELIX   13  13 HIS A  181  GLY A  186  1                                   6    
HELIX   14  14 ASN A  200  GLU A  209  1                                  10    
HELIX   15  15 LEU A  232  ASP A  241  1                                  10    
HELIX   16  16 ASP A  241  ASP A  254  1                                  14    
HELIX   17  17 ASP A  254  ASN A  272  1                                  19    
HELIX   18  18 ASP B    2  CYS B   14  1                                  13    
HELIX   19  19 THR B   49  ASN B   54  1                                   6    
HELIX   20  20 LYS B   60  ASN B   70  1                                  11    
HELIX   21  21 ASN B   70  ILE B   75  1                                   6    
HELIX   22  22 LYS B   87  THR B  102  1                                  16    
SHEET    1   A 2 LYS A 179  THR A 180  0                                        
SHEET    2   A 2 GLY A 189  PRO A 190 -1  O  GLY A 189   N  THR A 180           
SHEET    1   B 3 LYS A 212  LYS A 215  0                                        
SHEET    2   B 3 GLU A 221  ASP A 224 -1  O  GLN A 222   N  GLU A 214           
SHEET    3   B 3 MET A 230  MET A 231 -1  O  MET A 231   N  TRP A 223           
LINK         NE2 HIS A 175                FE   HEM A 301     1555   1555  1.96  
LINK         NE2 HIS B  18                FE   HEC B 201     1555   1555  2.07  
LINK         SD  MET B  80                FE   HEC B 201     1555   1555  2.25  
LINK        FE   HEM A 301                UNK  UNX A 302     1555   1555  2.37  
LINK         SG  CYS B  14                 CAB HEC B 201     1555   1555  1.79  
LINK         SG  CYS B  17                 CAC HEC B 201     1555   1555  1.80  
SITE     1 AC1 22 PRO A  44  ARG A  48  TRP A  51  PRO A 145                    
SITE     2 AC1 22 ALA A 147  LEU A 171  MET A 172  ALA A 174                    
SITE     3 AC1 22 HIS A 175  LEU A 177  GLY A 178  LYS A 179                    
SITE     4 AC1 22 THR A 180  HIS A 181  ASN A 184  SER A 185                    
SITE     5 AC1 22 TRP A 191  LEU A 232  THR A 234  HOH A 442                    
SITE     6 AC1 22 HOH A 460  HOH A 522                                          
SITE     1 AC2 24 ALA A 193  ARG B  13  CYS B  14  GLN B  16                    
SITE     2 AC2 24 CYS B  17  HIS B  18  THR B  28  GLY B  29                    
SITE     3 AC2 24 PRO B  30  THR B  40  GLY B  41  TYR B  48                    
SITE     4 AC2 24 THR B  49  ASN B  52  TRP B  59  LEU B  64                    
SITE     5 AC2 24 TYR B  67  LEU B  68  THR B  78  LYS B  79                    
SITE     6 AC2 24 MET B  80  PHE B  82  LEU B  94  HOH B 346                    
CRYST1   44.890   87.700  104.740  90.00  90.00  90.00 P 21 21 21    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      0.022277  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009547        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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