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Database: PDB
Entry: 2JJN
LinkDB: 2JJN
Original site: 2JJN 
HEADER    OXIDOREDUCTASE                          15-APR-08   2JJN              
TITLE     STRUCTURE OF CLOSED CYTOCHROME P450 ERYK                              
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    OXIDOREDUCTASE, IRON, HEME, MONOOXYGENASE, METAL-BINDING, ANTIBIOTIC  
KEYWDS   2 BIOSYNTHESIS, TIE-ROD MECHANISM OF ACTION, CYTOCHROME P450,          
KEYWDS   3 SUBSTRATE SPECIFICITY                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SAVINO,G.SCIARA,A.E.MIELE,S.G.KENDREW,B.VALLONE                     
REVDAT   5   13-JUL-11 2JJN    1       VERSN                                    
REVDAT   4   20-OCT-09 2JJN    1       JRNL                                     
REVDAT   3   04-AUG-09 2JJN    1       JRNL                                     
REVDAT   2   21-JUL-09 2JJN    1       JRNL                                     
REVDAT   1   14-JUL-09 2JJN    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.    1.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 50735                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2725                            
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) : 1.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3455                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 202                          
REMARK   3   BIN FREE R VALUE                    : 0.2270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3223                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 551                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 16.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.57000                                             
REMARK   3    B22 (A**2) : 1.47000                                              
REMARK   3    B33 (A**2) : -0.89000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.803         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3365 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4597 ; 1.636 ; 2.014       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   394 ; 5.893 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   170 ;32.328 ;23.353       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   576 ;14.311 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;21.138 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   505 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2584 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1841 ; 0.247 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2323 ; 0.317 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   480 ; 0.181 ; 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):   123 ; 0.307 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    77 ; 0.186 ; 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):  2031 ; 1.222 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3273 ; 1.943 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1473 ; 2.547 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1322 ; 3.755 ; 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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 16                                   
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    27        A    40                          
REMARK   3    RESIDUE RANGE :   A    56        A    64                          
REMARK   3    RESIDUE RANGE :   A    93        A   105                          
REMARK   3    RESIDUE RANGE :   A   108        A   113                          
REMARK   3    RESIDUE RANGE :   A   115        A   128                          
REMARK   3    RESIDUE RANGE :   A   135        A   141                          
REMARK   3    RESIDUE RANGE :   A   143        A   152                          
REMARK   3    RESIDUE RANGE :   A   160        A   171                          
REMARK   3    RESIDUE RANGE :   A   180        A   191                          
REMARK   3    RESIDUE RANGE :   A   192        A   206                          
REMARK   3    RESIDUE RANGE :   A   212        A   218                          
REMARK   3    RESIDUE RANGE :   A   228        A   259                          
REMARK   3    RESIDUE RANGE :   A   261        A   269                          
REMARK   3    RESIDUE RANGE :   A   274        A   284                          
REMARK   3    RESIDUE RANGE :   A   316        A   320                          
REMARK   3    RESIDUE RANGE :   A   356        A   373                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4790  -0.2710   9.3400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1200 T22:  -0.1210                                     
REMARK   3      T33:  -0.0723 T12:   0.0083                                     
REMARK   3      T13:  -0.0100 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4976 L22:   0.0954                                     
REMARK   3      L33:   0.3685 L12:   0.0212                                     
REMARK   3      L13:  -0.0854 L23:   0.0354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0057 S12:  -0.0115 S13:   0.0532                       
REMARK   3      S21:  -0.0004 S22:  -0.0082 S23:  -0.0389                       
REMARK   3      S31:  -0.0252 S32:   0.0511 S33:   0.0139                       
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. COORDINATES START FROM A.A. 17 BECAUSE THERE      
REMARK   3  WAS NOT ELECTRON DENSITY FOR PREVIOUS RESIDUES                      
REMARK   4                                                                      
REMARK   4 2JJN 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-35933.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
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   : 53926                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.60                               
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.1                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.19                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 19.10                              
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 2VRU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.9                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.9                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULPHATE, 0.1M             
REMARK 280  BIS-TRIS PH 6.5                                                     
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       34.00200            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 400 ENGINEERED RESIDUE IN CHAIN A, PHE 330 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A 157    CG   SD   CE                                        
REMARK 470     ASP A 158    CG   OD1  OD2                                       
REMARK 470     HIS A 159    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 160    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2105     O    HOH A  2533              2.11            
REMARK 500   O    HOH A  2106     O    HOH A  2107              2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD1  ILE A    18     O    ALA A   411     1554     1.72            
REMARK 500   O    HOH A  2162     O    HOH A  2282     1655     1.99            
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    PRO A 156   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG A 273   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 376   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 408   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 408   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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    GLN A  41       71.23   -157.04                                   
REMARK 500    LEU A 139      -51.12   -131.98                                   
REMARK 500    PRO A 156      -68.78    -22.60                                   
REMARK 500    ASP A 158       50.81    -97.86                                   
REMARK 500    HIS A 159       73.61    -65.24                                   
REMARK 500    SER A 338       46.96     27.81                                   
REMARK 500    ILE A 392      -63.14     74.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   17     ILE A   18                  147.27                    
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   NA                                                     
REMARK 620 2 CYS A 353   SG   99.0                                              
REMARK 620 3 HEM A 412   NB   89.3  92.8                                        
REMARK 620 4 HEM A 412   ND   90.0  96.9 170.3                                  
REMARK 620 5 HEM A 412   NC  171.8  89.2  90.2  89.1                            
REMARK 620 6 HOH A2539   O    85.8 172.9  81.9  88.4  86.0                      
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 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 417                 
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: 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)                                   
REMARK 900 RELATED ID: 2JJO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX                        
REMARK 900   WITH ITS NATURAL SUBSTRATE ERD                                     
DBREF  2JJN A    1    14  PDB    2JJN     2JJN             1     14             
DBREF  2JJN A   15   411  UNP    P48635   CPXQ_SACEN       1    397             
SEQADV 2JJN LEU A   15  UNP  P48635    MET     1 ENGINEERED MUTATION            
SEQADV 2JJN LEU A  344  UNP  P48635    PHE   330 ENGINEERED MUTATION            
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    SO4  A 413       5                                                       
HET    SO4  A 414       5                                                       
HET    SO4  A 415       5                                                       
HET    SO4  A 416       5                                                       
HET    SO4  A 417       5                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   4  HOH   *551(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  PHE A  106  1                                  14    
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  GLY A  153  1                                  13    
HELIX   10  10 ASP A  164  ILE A  172  1                                   9    
HELIX   11  11 ASP A  179  ASP A  207  1                                  29    
HELIX   12  12 ASP A  211  ALA A  219  1                                   9    
HELIX   13  13 ASP A  227  HIS A  260  1                                  34    
HELIX   14  14 PRO A  261  ASP A  270  1                                  10    
HELIX   15  15 ARG A  273  ARG A  285  1                                  13    
HELIX   16  16 VAL A  316  ARG A  321  1                                   6    
HELIX   17  17 GLN A  343  GLY A  347  5                                   5    
HELIX   18  18 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  LEU A 402 -1  O  VAL A 401   N  PHE A 133           
SHEET    3  AB 3 THR A 378  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  
LINK        FE   HEM A 412                 O   HOH A2539     1555   1555  2.22  
CISPEP   1 PRO A   92    PRO A   93          0         5.15                     
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  LEU A 358                    
SITE     6 AC1 25 ALA A 359  HOH A2131  HOH A2537  HOH A2538                    
SITE     7 AC1 25 HOH A2539                                                     
SITE     1 AC2  6 ARG A 381  ARG A 385  LEU A 386  HIS A 388                    
SITE     2 AC2  6 HOH A2540  HOH A2541                                          
SITE     1 AC3  6 HIS A 326  ASP A 327  ARG A 336  SER A 338                    
SITE     2 AC3  6 HOH A2542  HOH A2543                                          
SITE     1 AC4  4 ARG A  55  HOH A2424  HOH A2544  HOH A2545                    
SITE     1 AC5  5 ARG A  99  SER A 103  LEU A 354  HOH A2546                    
SITE     2 AC5  5 HOH A2547                                                     
SITE     1 AC6 10 HIS A  56  HIS A 326  ALA A 342  LEU A 344                    
SITE     2 AC6 10 HOH A2434  HOH A2464  HOH A2548  HOH A2549                    
SITE     3 AC6 10 HOH A2550  HOH A2551                                          
CRYST1   53.460   68.004   57.407  90.00 101.05  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      0.018706  0.000000  0.003653        0.00000                         
SCALE2      0.000000  0.014705  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017749        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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