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Database: PDB
Entry: 2JJP
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Original site: 2JJP 
HEADER    OXIDOREDUCTASE                          15-APR-08   2JJP              
TITLE     STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX WITH INHIBITOR           
TITLE    2 KETOCONAZOLE (KC)                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 113A1;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ERYTHROMYCIN B/D C-12 HYDROXYLASE, CYTOCROME P450           
COMPND   5  CYP113A1;                                                           
COMPND   6 EC: 1.14.-.-;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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   2   22-AUG-12 2JJP    1       KEYWDS JRNL   REMARK VERSN               
REVDAT   2 2                           HETSYN FORMUL                            
REVDAT   1   14-JUL-09 2JJP    0                                                
JRNL        AUTH   L.C.MONTEMIGLIO,S.GIANNI,B.VALLONE,C.SAVINO                  
JRNL        TITL   AZOLE DRUGS TRAP CYTOCHROME P450 ERYK IN ALTERNATIVE         
JRNL        TITL 2 CONFORMATIONAL STATES.                                       
JRNL        REF    BIOCHEMISTRY                  V.  49  9199 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20845962                                                     
JRNL        DOI    10.1021/BI101062V                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.1  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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20602                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1109                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1500                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3152                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 89                                      
REMARK   3   SOLVENT ATOMS            : 229                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.02000                                             
REMARK   3    B22 (A**2) : 4.54000                                              
REMARK   3    B33 (A**2) : -2.81000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.79000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.309         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.237         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.176         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.695         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3320 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4545 ; 1.611 ; 2.025       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   396 ; 6.349 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   167 ;34.527 ;23.832       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   529 ;18.058 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;22.980 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   498 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2590 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1684 ; 0.238 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2229 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   214 ; 0.211 ; 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):    87 ; 0.198 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.168 ; 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):  2046 ; 1.096 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3250 ; 1.775 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1425 ; 2.380 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1293 ; 3.475 ; 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. COORDINATE START FROM A.A. 15 BECAUSE THERE       
REMARK   3  WAS NOT ELECTRON DENSITY FOR PREVIOUS RESIDUES                      
REMARK   4                                                                      
REMARK   4 2JJP 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-35935.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-06                          
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                       : ID14-2                             
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   : 25326                              
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     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY                : 3.9                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.50                              
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     (%) : 85.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.19                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 12.70                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC5                                               
REMARK 200 STARTING MODEL: PDB ENTRY 2JJN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.3                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULHATE, 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       34.01900            
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 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 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   OE1B GLU A   390     O    HOH A  2218              2.09            
REMARK 500   O    HOH A  2010     O    HOH A  2017              1.87            
REMARK 500   O    HOH A  2018     O    HOH A  2195              2.17            
REMARK 500   O    HOH A  2138     O    HOH A  2139              2.09            
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      -86.37   -112.17                                   
REMARK 500    VAL A  21       95.06     75.14                                   
REMARK 500    THR A  74        6.97    -63.84                                   
REMARK 500    ALA A  80       69.02    -64.50                                   
REMARK 500    SER A  81       74.85   -106.22                                   
REMARK 500    LEU A 139      -54.34   -126.73                                   
REMARK 500    GLU A 160       98.61   -178.42                                   
REMARK 500    GLN A 161       29.32   -144.00                                   
REMARK 500    GLN A 173       96.16    -62.98                                   
REMARK 500    ASP A 175      -46.12   -143.21                                   
REMARK 500    ARG A 336       96.57    -69.29                                   
REMARK 500    ALA A 341       94.20    -55.77                                   
REMARK 500    ARG A 381       50.25   -103.16                                   
REMARK 500    ASP A 383      -44.36   -143.16                                   
REMARK 500    GLN A 391      -71.15   -136.59                                   
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
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        24.2      L          L   OUTSIDE RANGE           
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 CYS A 353   SG                                                     
REMARK 620 2 HEM A 412   NA   91.0                                              
REMARK 620 3 HEM A 412   NB   84.1  92.3                                        
REMARK 620 4 HEM A 412   NC   88.4 175.5  83.3                                  
REMARK 620 5 KLN A 413   N2  170.3  91.4  86.4  88.4                            
REMARK 620 6 HEM A 412   ND   96.8  89.2 178.2  95.2  92.6                      
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 KLN 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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 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: 2JJO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX                        
REMARK 900   WITH ITS NATURAL SUBSTRATE ERD                                     
DBREF  2JJP A    1    14  PDB    2JJP     2JJP             1     14             
DBREF  2JJP A   15   411  UNP    P48635   CPXQ_SACEN       1    397             
SEQADV 2JJP LEU A   15  UNP  P48635    MET     1 ENGINEERED MUTATION            
SEQADV 2JJP 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    KLN  A 413      36                                                       
HET    SO4  A 414       5                                                       
HET    SO4  A 415       5                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     KLN 1-ACETYL-4-(4-{[(2S,4R)-2-(2,4-                                  
HETNAM   2 KLN  DICHLOROPHENYL)-2-(1H-IMIDAZOL-1-YLMETHYL)-1,3-DIOXOLAN-4-      
HETNAM   3 KLN  YL]METHOXY}PHENYL)PIPERAZINE                                    
HETSYN     HEM  HEME                                                            
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4  KLN    C26 H28 CL2 N4 O4                                            
FORMUL   5  HOH   *229(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  VAL A   76  5                                   5    
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 GLY A  163  ASP A  171  1                                   9    
HELIX   11  11 PRO A  180  ASP A  207  1                                  28    
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  2.24  
LINK        FE   HEM A 412                 N2  KLN A 413     1555   1555  1.96  
CISPEP   1 PRO A   92    PRO A   93          0         6.09                     
SITE     1 AC1 20 ILE A  87  HIS A  88  HIS A  95  ARG A  99                    
SITE     2 AC1 20 ALA A 241  THR A 245  MET A 291  ARG A 293                    
SITE     3 AC1 20 SER A 345  PHE A 346  GLY A 347  VAL A 350                    
SITE     4 AC1 20 HIS A 351  CYS A 353  GLY A 355  ALA A 359                    
SITE     5 AC1 20 KLN A 413  HOH A2064  HOH A2065  HOH A2228                    
SITE     1 AC2 14 HIS A  88  MET A 174  ALA A 237  LEU A 240                    
SITE     2 AC2 14 ALA A 241  PHE A 288  GLN A 290  MET A 291                    
SITE     3 AC2 14 GLN A 292  ILE A 392  HEM A 412  HOH A2114                    
SITE     4 AC2 14 HOH A2174  HOH A2219                                          
SITE     1 AC3  4 ARG A 381  ARG A 385  LEU A 386  HIS A 388                    
SITE     1 AC4  5 HIS A 326  ASP A 327  ARG A 336  LYS A 337                    
SITE     2 AC4  5 SER A 338                                                     
CRYST1   53.243   68.038   57.687  90.00 100.71  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      0.018782  0.000000  0.003552        0.00000                         
SCALE2      0.000000  0.014698  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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