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Database: PDB
Entry: 2JJO
LinkDB: 2JJO
Original site: 2JJO 
HEADER    OXIDOREDUCTASE                          15-APR-08   2JJO              
TITLE     STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX WITH ITS                 
TITLE    2 NATURAL SUBSTRATE ERD                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 113A1;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOCROME P450 CYP113A1, ERYTHROMYCIN B/D C-12 HYDROXYLASE; 
COMPND   5 EC: 1.14.-.-;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;                    
SOURCE   3 ORGANISM_TAXID: 1836;                                                
SOURCE   4 STRAIN: NRRL 23338;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21STAR;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET28B;                                    
SOURCE   9 OTHER_DETAILS: CDNA                                                  
KEYWDS    IRON, HEME, MONOOXYGENASE, METAL-BINDING, ANTIBIOTIC BIOSYNTHESIS,    
KEYWDS   2 TIE-ROD MECHANISM OF ACTION, OXIDOREDUCTASE, SUBSTRATE SPECIFICITY   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SAVINO,G.SCIARA,A.E.MIELE,S.G.KENDREW,B.VALLONE                     
REVDAT   5   06-FEB-13 2JJO    1       COMPND KEYWDS JRNL   REMARK              
REVDAT   5 2                           VERSN  HET    HETNAM HETSYN              
REVDAT   5 3                           FORMUL LINK   SITE   ATOM                
REVDAT   5 4                           HETATM CONECT MASTER                     
REVDAT   4   20-OCT-09 2JJO    1       JRNL                                     
REVDAT   3   04-AUG-09 2JJO    1       JRNL                                     
REVDAT   2   21-JUL-09 2JJO    1       JRNL                                     
REVDAT   1   14-JUL-09 2JJO    0                                                
JRNL        AUTH   C.SAVINO,L.C.MONTEMIGLIO,G.SCIARA,A.E.MIELE,S.G.KENDREW,     
JRNL        AUTH 2 P.JEMTH,S.GIANNI,B.VALLONE                                   
JRNL        TITL   INVESTIGATING THE STRUCTURAL PLASTICITY OF A CYTOCHROME      
JRNL        TITL 2 P450: THREE-DIMENSIONAL STRUCTURES OF P450 ERYK AND BINDING  
JRNL        TITL 3 TO ITS PHYSIOLOGICAL SUBSTRATE.                              
JRNL        REF    J.BIOL.CHEM.                  V. 284 29170 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19625248                                                     
JRNL        DOI    10.1074/JBC.M109.003590                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 24282                          
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) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1281                            
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) : 1.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1539                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3089                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 113                                     
REMARK   3   SOLVENT ATOMS            : 335                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.21000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : 1.07000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.54000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.200         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.180         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.990         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3260 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):    21 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4470 ; 1.577 ; 2.026       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    59 ; 1.211 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   392 ; 5.710 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   156 ;34.991 ;23.141       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   508 ;15.329 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;18.496 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   506 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2517 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1640 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    42 ; 0.257 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2229 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):    20 ; 0.126 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   282 ; 0.155 ; 0.200       
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):    75 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.148 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2045 ; 0.893 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3208 ; 1.439 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1359 ; 2.302 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1260 ; 3.295 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 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 : BABINET MODEL WITH 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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2JJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-35934.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27953                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY                : 4.0                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.24                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.90                              
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: PDB ENTRY 2JJN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2M AMMONIUM              
REMARK 280  ACETATE, 0.1M TRIS PH 8.5                                           
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       18.26300            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 ENGINEERED RESIDUE IN CHAIN A, MET 1 TO LEU                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     CYS A     9                                                      
REMARK 465     CYS A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   166     O    HOH A  2169              2.19            
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 A 200   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 200   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 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    GLU A  20       97.15     54.97                                   
REMARK 500    GLN A  41       70.01   -154.81                                   
REMARK 500    ASP A 175      -82.77   -135.62                                   
REMARK 500    HIS A 243      -35.37   -133.05                                   
REMARK 500    CYS A 353      115.35    -38.13                                   
REMARK 500    ILE A 392      -54.91     71.76                                   
REMARK 500    SER A 410     -160.48   -105.01                                   
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 412  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM A 412   NB                                                     
REMARK 620 2 HEM A 412   NA   88.8                                              
REMARK 620 3 HEM A 412   NC   88.9 168.2                                        
REMARK 620 4 HEM A 412   ND  169.7  91.6  88.5                                  
REMARK 620 5 CYS A 353   SG   89.3 103.6  88.0 100.6                            
REMARK 620 N                    1     2     3     4                             
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 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EY5 A 413                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VRU   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF OPEN HISTIDINE TAGGED CYTOCHROME                       
REMARK 900   P450 ERYK                                                          
REMARK 900 RELATED ID: 2WIO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE OPEN HISTIDINE TAGGED C.                           
REMARK 900  SAVINO, CYTOCHROME P450 ERYK                                        
REMARK 900 RELATED ID: 2JJN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CLOSED CYTOCHROME P450 ERYK                            
REMARK 900 RELATED ID: 2VRV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HISTIDINE TAGGED CYTOCHROME P450                       
REMARK 900   ERYK IN COMPLEX WITH INHIBITOR CLOTRIMAZOLE                        
REMARK 900   (CLT)                                                              
REMARK 900 RELATED ID: 2JJP   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX                        
REMARK 900   WITH INHIBITOR KETOCONAZOLE (KC)                                   
DBREF  2JJO A    1    14  PDB    2JJO     2JJO             1     14             
DBREF  2JJO A   15   411  UNP    P48635   CPXQ_SACEN       1    397             
SEQADV 2JJO LEU A   15  UNP  P48635    MET     1 ENGINEERED MUTATION            
SEQADV 2JJO LEU A  344  UNP  P48635    PHE   330 CONFLICT                       
SEQRES   1 A  411  MET PHE ALA ASP VAL GLU THR THR CYS CYS ALA ARG ARG          
SEQRES   2 A  411  THR LEU THR THR ILE ASP GLU VAL PRO GLY MET ALA ASP          
SEQRES   3 A  411  GLU THR ALA LEU LEU ASP TRP LEU GLY THR MET ARG GLU          
SEQRES   4 A  411  LYS GLN PRO VAL TRP GLN ASP ARG TYR GLY VAL TRP HIS          
SEQRES   5 A  411  VAL PHE ARG HIS ALA ASP VAL GLN THR VAL LEU ARG ASP          
SEQRES   6 A  411  THR ALA THR PHE SER SER ASP PRO THR ARG VAL ILE GLU          
SEQRES   7 A  411  GLY ALA SER PRO THR PRO GLY MET ILE HIS GLU ILE ASP          
SEQRES   8 A  411  PRO PRO GLU HIS ARG ALA LEU ARG LYS VAL VAL SER SER          
SEQRES   9 A  411  ALA PHE THR PRO ARG THR ILE SER ASP LEU GLU PRO ARG          
SEQRES  10 A  411  ILE ARG ASP VAL THR ARG SER LEU LEU ALA ASP ALA GLY          
SEQRES  11 A  411  GLU SER PHE ASP LEU VAL ASP VAL LEU ALA PHE PRO LEU          
SEQRES  12 A  411  PRO VAL THR ILE VAL ALA GLU LEU LEU GLY LEU PRO PRO          
SEQRES  13 A  411  MET ASP HIS GLU GLN PHE GLY ASP TRP SER GLY ALA LEU          
SEQRES  14 A  411  VAL ASP ILE GLN MET ASP ASP PRO THR ASP PRO ALA LEU          
SEQRES  15 A  411  ALA GLU ARG ILE ALA ASP VAL LEU ASN PRO LEU THR ALA          
SEQRES  16 A  411  TYR LEU LYS ALA ARG CYS ALA GLU ARG ARG ALA ASP PRO          
SEQRES  17 A  411  GLY ASP ASP LEU ILE SER ARG LEU VAL LEU ALA GLU VAL          
SEQRES  18 A  411  ASP GLY ARG ALA LEU ASP ASP GLU GLU ALA ALA ASN PHE          
SEQRES  19 A  411  SER THR ALA LEU LEU LEU ALA GLY HIS ILE THR THR THR          
SEQRES  20 A  411  VAL LEU LEU GLY ASN ILE VAL ARG THR LEU ASP GLU HIS          
SEQRES  21 A  411  PRO ALA HIS TRP ASP ALA ALA ALA GLU ASP PRO GLY ARG          
SEQRES  22 A  411  ILE PRO ALA ILE VAL GLU GLU VAL LEU ARG TYR ARG PRO          
SEQRES  23 A  411  PRO PHE PRO GLN MET GLN ARG THR THR THR LYS ALA THR          
SEQRES  24 A  411  GLU VAL ALA GLY VAL PRO ILE PRO ALA ASP VAL MET VAL          
SEQRES  25 A  411  ASN THR TRP VAL LEU SER ALA ASN ARG ASP SER ASP ALA          
SEQRES  26 A  411  HIS ASP ASP PRO ASP ARG PHE ASP PRO SER ARG LYS SER          
SEQRES  27 A  411  GLY GLY ALA ALA GLN LEU SER PHE GLY HIS GLY VAL HIS          
SEQRES  28 A  411  PHE CYS LEU GLY ALA PRO LEU ALA ARG LEU GLU ASN ARG          
SEQRES  29 A  411  VAL ALA LEU GLU GLU ILE ILE ALA ARG PHE GLY ARG LEU          
SEQRES  30 A  411  THR VAL ASP ARG ASP ASP GLU ARG LEU ARG HIS PHE GLU          
SEQRES  31 A  411  GLN ILE VAL LEU GLY THR ARG HIS LEU PRO VAL LEU ALA          
SEQRES  32 A  411  GLY SER SER PRO ARG GLN SER ALA                              
HET    HEM  A 412      43                                                       
HET    EY5  A 413      70                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     EY5 ERYTHROMYCIN D                                                   
HETSYN     HEM HEME                                                             
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  EY5    C36 H65 N O12                                                
FORMUL   4  HOH   *335(H2 O)                                                    
HELIX    1   1 ASP A   26  GLN A   41  1                                  16    
HELIX    2   2 ARG A   55  ASP A   65  1                                  11    
HELIX    3   3 ASP A   72  ILE A   77  5                                   6    
HELIX    4   4 MET A   86  ILE A   90  5                                   5    
HELIX    5   5 PRO A   93  SER A  104  1                                  12    
HELIX    6   6 THR A  107  ASP A  113  1                                   7    
HELIX    7   7 LEU A  114  ASP A  128  1                                  15    
HELIX    8   8 LEU A  135  LEU A  139  1                                   5    
HELIX    9   9 PHE A  141  LEU A  152  1                                  12    
HELIX   10  10 PRO A  155  MET A  157  5                                   3    
HELIX   11  11 ASP A  158  ASP A  171  1                                  14    
HELIX   12  12 ASP A  179  ASP A  207  1                                  29    
HELIX   13  13 ASP A  211  ALA A  219  1                                   9    
HELIX   14  14 ASP A  227  HIS A  260  1                                  34    
HELIX   15  15 PRO A  261  ASP A  270  1                                  10    
HELIX   16  16 ARG A  273  ARG A  285  1                                  13    
HELIX   17  17 VAL A  316  ARG A  321  1                                   6    
HELIX   18  18 GLY A  339  GLN A  343  5                                   5    
HELIX   19  19 GLN A  343  GLY A  347  5                                   5    
HELIX   20  20 GLY A  355  GLY A  375  1                                  21    
SHEET    1  AA 5 VAL A  43  GLN A  45  0                                        
SHEET    2  AA 5 TRP A  51  VAL A  53 -1  O  HIS A  52   N  TRP A  44           
SHEET    3  AA 5 MET A 311  TRP A 315  1  O  MET A 311   N  TRP A  51           
SHEET    4  AA 5 GLN A 290  THR A 295 -1  O  MET A 291   N  THR A 314           
SHEET    5  AA 5 PHE A  69  SER A  70 -1  O  SER A  70   N  THR A 294           
SHEET    1  AB 3 SER A 132  ASP A 134  0                                        
SHEET    2  AB 3 PRO A 400  ALA A 403 -1  O  VAL A 401   N  PHE A 133           
SHEET    3  AB 3 LEU A 377  VAL A 379 -1  O  THR A 378   N  LEU A 402           
SHEET    1  AC 2 THR A 299  VAL A 301  0                                        
SHEET    2  AC 2 VAL A 304  ILE A 306 -1  O  VAL A 304   N  VAL A 301           
LINK        FE   HEM A 412                 SG  CYS A 353     1555   1555  2.32  
CISPEP   1 PRO A   92    PRO A   93          0         0.71                     
SITE     1 AC1 25 ILE A  87  HIS A  88  HIS A  95  ARG A  99                    
SITE     2 AC1 25 PHE A 106  LEU A 238  ALA A 241  GLY A 242                    
SITE     3 AC1 25 THR A 245  THR A 246  LEU A 249  MET A 291                    
SITE     4 AC1 25 ARG A 293  SER A 345  PHE A 346  GLY A 347                    
SITE     5 AC1 25 HIS A 351  CYS A 353  GLY A 355  ALA A 359                    
SITE     6 AC1 25 EY5 A 413  HOH A2080  HOH A2331  HOH A2332                    
SITE     7 AC1 25 HOH A2333                                                     
SITE     1 AC2 18 HIS A  88  GLU A  89  LEU A 169  ILE A 172                    
SITE     2 AC2 18 MET A 174  PRO A 177  ILE A 186  LEU A 240                    
SITE     3 AC2 18 ALA A 241  THR A 245  PHE A 288  GLN A 292                    
SITE     4 AC2 18 HEM A 412  HOH A2217  HOH A2238  HOH A2332                    
SITE     5 AC2 18 HOH A2334  HOH A2335                                          
CRYST1   57.840   36.526   96.004  90.00  93.92  90.00 P 1 21 1      2          
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      0.017289  0.000000  0.001185        0.00000                         
SCALE2      0.000000  0.027378  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010441        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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