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Database: PDB
Entry: 2WIO
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Original site: 2WIO 
HEADER    OXIDOREDUCTASE                          14-MAY-09   2WIO              
TITLE     STRUCTURE OF THE  HISTIDINE TAGGED, OPEN CYTOCHROME                   
TITLE    2 P450 ERYK FROM S. ERYTHRAEA                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ERYTHROMYCIN B/D C-12 HYDROXYLASE;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 2-397;                                            
COMPND   5 SYNONYM: CYTOCHROME P450 CYP113A1;                                   
COMPND   6 EC: 1.14.-.-;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;                    
SOURCE   3 ORGANISM_TAXID: 1836;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 (STAR);                               
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PET28B;                                    
SOURCE   8 OTHER_DETAILS: CDNA                                                  
KEYWDS    SUBSTRATE SPECIFICITY, ANTIBIOTIC BIOSYNTHESIS,                       
KEYWDS   2 METAL-BINDING, OXIDOREDUCTASE, CYTOCHROME P450, IRON,                
KEYWDS   3 HEME, ERYTHROMICYN, MONOOXYGENASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SAVINO,L.C.MONTEMIGLIO,G.SCIARA,A.E.MIELE,S.G.KEDREW,               
AUTHOR   2 S.GIANNI,B.VALLONE                                                   
REVDAT   4   20-OCT-09 2WIO    1       JRNL                                     
REVDAT   3   04-AUG-09 2WIO    1       JRNL                                     
REVDAT   2   28-JUL-09 2WIO    1       TITLE                                    
REVDAT   1   21-JUL-09 2WIO    0                                                
JRNL        AUTH   C.SAVINO,L.C.MONTEMIGLIO,G.SCIARA,A.E.MIELE,                 
JRNL        AUTH 2 S.G.KENDREW,P.JEMTH,S.GIANNI,B.VALLONE                       
JRNL        TITL   INVESTIGATING THE STRUCTURAL PLASTICITY OF A                 
JRNL        TITL 2 CYTOCHROME P450: THREE-DIMENSIONAL STRUCTURES OF             
JRNL        TITL 3 P450 ERYK AND BINDING TO ITS PHYSIOLOGICAL                   
JRNL        TITL 4 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.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 81.77                          
REMARK   3   NUMBER OF REFLECTIONS             : 21300                          
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) : 0.18587                         
REMARK   3   R VALUE            (WORKING SET) : 0.18341                         
REMARK   3   FREE R VALUE                     : 0.23202                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1115                            
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) : 2.000                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.052                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1653                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.200                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.267                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3053                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 308                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.901                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.08                                                
REMARK   3    B22 (A**2) : -1.54                                                
REMARK   3    B33 (A**2) : 1.61                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.266         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.202         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.007         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3173 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4346 ; 1.543 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   392 ; 6.279 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   149 ;34.134 ;23.087       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   491 ;17.156 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;20.234 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   485 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2475 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1720 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2166 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   295 ; 0.187 ; 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):    73 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.229 ; 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):  2028 ; 0.874 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3194 ; 1.315 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1285 ; 2.133 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1150 ; 3.152 ; 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   3  THE PDB STARTS FROM A.A. 19 SINCE THERE WAS NO                      
REMARK   3  INTERPRETABLE ELECTRON DENSITY FOR PREVIOUS RESIDUES                
REMARK   4                                                                      
REMARK   4 2WIO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAY-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-39810.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22549                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.2                               
REMARK 200  DATA REDUNDANCY                : 4.8                                
REMARK 200  R MERGE                    (I) : 0.19                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.90                              
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) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.44                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.10                               
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 1OXA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2M NACL, 0.1M             
REMARK 280  TRIS PH 8.0                                                         
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       18.96612            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.77850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.67062            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.77850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.96604            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.67050            
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 GENERATING THE BIOMOLECULE                                           
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: 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 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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
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   OE2  GLU A   229  -  O    HOH A  2185              2.15            
REMARK 500   O    HOH A  2025  -  O    HOH A  2229              1.97            
REMARK 500   O    HOH A  2058  -  O    HOH A  2123              2.17            
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 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       71.86   -154.29                                   
REMARK 500    ASP A 210       74.44   -101.63                                   
REMARK 500    VAL A 221      -75.44   -111.36                                   
REMARK 500    ASP A 222       67.73   -115.79                                   
REMARK 500    ASP A 309       33.51     70.42                                   
REMARK 500    CYS A 353      116.75    -28.33                                   
REMARK 500    GLN A 391      -80.63   -133.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLN A 391        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
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 A1412  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 353   SG                                                     
REMARK 620 2 HEM A1412   NA  102.8                                              
REMARK 620 3 HEM A1412   NB   92.8  86.7                                        
REMARK 620 4 HEM A1412   ND   98.8  93.1 168.1                                  
REMARK 620 5 HOH A2307   O   165.7  75.1  73.0  95.4                            
REMARK 620 6 HEM A1412   NC   90.4 166.2  88.7  88.7  91.2                      
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 A1412                 
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: 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)                                   
REMARK 900 RELATED ID: 2JJO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX                        
REMARK 900   WITH ITS NATURAL SUBSTRATE ERD                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MGSSHHHHHHSSGLVPRGSH ADDED BECAUSE OF THE EXPRESSION                 
REMARK 999 VECTOR                                                               
DBREF  2WIO A  -19    15  PDB    2WIO     2WIO           -19     15             
DBREF  2WIO A   16   411  UNP    P48635   CPXQ_SACEN       2    397             
SEQADV 2WIO LEU A  344  UNP  P48635    PHE   330 CONFLICT                       
SEQRES   1 A  431  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  431  LEU VAL PRO ARG GLY SER HIS MET PHE ALA ASP VAL GLU          
SEQRES   3 A  431  THR THR CYS CYS ALA ARG ARG THR LEU THR THR ILE ASP          
SEQRES   4 A  431  GLU VAL PRO GLY MET ALA ASP GLU THR ALA LEU LEU ASP          
SEQRES   5 A  431  TRP LEU GLY THR MET ARG GLU LYS GLN PRO VAL TRP GLN          
SEQRES   6 A  431  ASP ARG TYR GLY VAL TRP HIS VAL PHE ARG HIS ALA ASP          
SEQRES   7 A  431  VAL GLN THR VAL LEU ARG ASP THR ALA THR PHE SER SER          
SEQRES   8 A  431  ASP PRO THR ARG VAL ILE GLU GLY ALA SER PRO THR PRO          
SEQRES   9 A  431  GLY MET ILE HIS GLU ILE ASP PRO PRO GLU HIS ARG ALA          
SEQRES  10 A  431  LEU ARG LYS VAL VAL SER SER ALA PHE THR PRO ARG THR          
SEQRES  11 A  431  ILE SER ASP LEU GLU PRO ARG ILE ARG ASP VAL THR ARG          
SEQRES  12 A  431  SER LEU LEU ALA ASP ALA GLY GLU SER PHE ASP LEU VAL          
SEQRES  13 A  431  ASP VAL LEU ALA PHE PRO LEU PRO VAL THR ILE VAL ALA          
SEQRES  14 A  431  GLU LEU LEU GLY LEU PRO PRO MET ASP HIS GLU GLN PHE          
SEQRES  15 A  431  GLY ASP TRP SER GLY ALA LEU VAL ASP ILE GLN MET ASP          
SEQRES  16 A  431  ASP PRO THR ASP PRO ALA LEU ALA GLU ARG ILE ALA ASP          
SEQRES  17 A  431  VAL LEU ASN PRO LEU THR ALA TYR LEU LYS ALA ARG CYS          
SEQRES  18 A  431  ALA GLU ARG ARG ALA ASP PRO GLY ASP ASP LEU ILE SER          
SEQRES  19 A  431  ARG LEU VAL LEU ALA GLU VAL ASP GLY ARG ALA LEU ASP          
SEQRES  20 A  431  ASP GLU GLU ALA ALA ASN PHE SER THR ALA LEU LEU LEU          
SEQRES  21 A  431  ALA GLY HIS ILE THR THR THR VAL LEU LEU GLY ASN ILE          
SEQRES  22 A  431  VAL ARG THR LEU ASP GLU HIS PRO ALA HIS TRP ASP ALA          
SEQRES  23 A  431  ALA ALA GLU ASP PRO GLY ARG ILE PRO ALA ILE VAL GLU          
SEQRES  24 A  431  GLU VAL LEU ARG TYR ARG PRO PRO PHE PRO GLN MET GLN          
SEQRES  25 A  431  ARG THR THR THR LYS ALA THR GLU VAL ALA GLY VAL PRO          
SEQRES  26 A  431  ILE PRO ALA ASP VAL MET VAL ASN THR TRP VAL LEU SER          
SEQRES  27 A  431  ALA ASN ARG ASP SER ASP ALA HIS ASP ASP PRO ASP ARG          
SEQRES  28 A  431  PHE ASP PRO SER ARG LYS SER GLY GLY ALA ALA GLN LEU          
SEQRES  29 A  431  SER PHE GLY HIS GLY VAL HIS PHE CYS LEU GLY ALA PRO          
SEQRES  30 A  431  LEU ALA ARG LEU GLU ASN ARG VAL ALA LEU GLU GLU ILE          
SEQRES  31 A  431  ILE ALA ARG PHE GLY ARG LEU THR VAL ASP ARG ASP ASP          
SEQRES  32 A  431  GLU ARG LEU ARG HIS PHE GLU GLN ILE VAL LEU GLY THR          
SEQRES  33 A  431  ARG HIS LEU PRO VAL LEU ALA GLY SER SER PRO ARG GLN          
SEQRES  34 A  431  SER ALA                                                      
HET    HEM  A1412      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  HOH   *308(H2 O1)                                                   
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 PRO A  155  MET A  157  5                                   3    
HELIX   11  11 ASP A  158  GLN A  173  1                                  16    
HELIX   12  12 ALA A  181  ASP A  207  1                                  27    
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           
SHEET    1  AD 2 ARG A 387  HIS A 388  0                                        
SHEET    2  AD 2 THR A 396  HIS A 398 -1  N  ARG A 397   O  ARG A 387           
LINK        FE   HEM A1412                 SG  CYS A 353     1555   1555  2.31  
LINK        FE   HEM A1412                 O   HOH A2307     1555   1555  2.29  
CISPEP   1 PRO A   92    PRO A   93          0        -2.55                     
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  PHE A 288                    
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 A2078  HOH A2306  HOH A2307                    
SITE     7 AC1 25 HOH A2308                                                     
CRYST1   37.932   57.341  179.557  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      0.026363  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017440  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005569        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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