Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4C4X-pdb

Name Class
4C4X-pdb
HEADER    HYDROLASE                               09-SEP-13   4C4X              
TITLE     CRYSTAL STRUCTURE OF HUMAN BIFUNCTIONAL EPOXIDE HYDROXYLASE 2         
TITLE    2 COMPLEXED WITH C9                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EPOXIDE HYDROXYLASE DOMAIN RESIDUES 230-555;               
COMPND   5 SYNONYM: BIFUNCTIONAL EPOXIDE HYDROXYLASE 2, CYTOSOLIC EPOXIDE       
COMPND   6  HYDROLASE 2, CEH, EPOXIDE HYDRATASE, SOLUBLE EPOXIDE HYDROLASE,     
COMPND   7  SEH, LIPID-PHOSPHATE PHOSPHATASE;                                   
COMPND   8 EC: 3.3.2.10, 3.1.3.76;                                              
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET16B                                     
KEYWDS    HYDROLASE, DRUG DESIGN, MULTIPLE BINDING MODES                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PILGER,A.MAZUR,P.MONECKE,H.SCHREUDER,B.ELSHORST,T.LANGER,           
AUTHOR   2 A.SCHIFFER,I.KRIMM,M.WEGSTROTH,D.LEE,G.HESSLER,K.-U.WENDT,S.BECKER,  
AUTHOR   3 C.GRIESINGER                                                         
REVDAT   1   01-OCT-14 4C4X    0                                                
JRNL        AUTH   J.PILGER,A.MAZUR,P.MONECKE,H.SCHREUDER,B.ELSHORST,T.LANGER,  
JRNL        AUTH 2 A.SCHIFFER,I.KRIMM,M.WEGSTROTH,D.LEE,G.HESSLER,K.-U.WENDT,   
JRNL        AUTH 3 S.BECKER,C.GRIESINGER                                        
JRNL        TITL   A COMBINATION OF SPIN DIFFUSION METHODS FOR THE              
JRNL        TITL 2 DETERMINATION OF PROTEIN-LIGAND COMPLEX STRUCTURAL           
JRNL        TITL 3 ENSEMBLES                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,WOMACK;       
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.80                          
REMARK   3   NUMBER OF REFLECTIONS             : 34823                          
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)  : 0.2133                         
REMARK   3   R VALUE            (WORKING SET)  : 0.2111                         
REMARK   3   FREE R VALUE                      : 0.2418                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 7.21                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 2512                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.17                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.24                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.80                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2990                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2383                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2774                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2364                   
REMARK   3   BIN FREE R VALUE                        : 0.2635                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 7.22                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 216                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5061                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 445                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.9696                                              
REMARK   3    B22 (A**2) : 11.5946                                              
REMARK   3    B33 (A**2) : -8.6250                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 1.4659                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.287               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.319               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.211               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.304               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.210               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.9089                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.8790                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              :   5267 ;   2.00 ;  HARMONIC           
REMARK   3    BOND ANGLES               :   7141 ;   2.00 ;  HARMONIC           
REMARK   3    TORSION ANGLES            :   1797 ;   2.00 ;  SINUSOIDAL         
REMARK   3    TRIGONAL CARBON PLANES    :    122 ;   2.00 ;  HARMONIC           
REMARK   3    GENERAL PLANES            :    755 ;   5.00 ;  HARMONIC           
REMARK   3    ISOTROPIC THERMAL FACTORS :   5267 ;  20.00 ;  HARMONIC           
REMARK   3    BAD NON-BONDED CONTACTS   :   NULL ;   NULL ;  NULL               
REMARK   3    IMPROPER TORSIONS         :   NULL ;   NULL ;  NULL               
REMARK   3    PSEUDOROTATION ANGLES     :   NULL ;   NULL ;  NULL               
REMARK   3    CHIRAL IMPROPER TORSION   :    629 ;   5.00 ;  SEMIHARMONIC       
REMARK   3    SUM OF OCCUPANCIES        :      2 ;   1.00 ;  HARMONIC           
REMARK   3    UTILITY DISTANCES         :   NULL ;   NULL ;  NULL               
REMARK   3    UTILITY ANGLES            :   NULL ;   NULL ;  NULL               
REMARK   3    UTILITY TORSION           :   NULL ;   NULL ;  NULL               
REMARK   3    IDEAL-DIST CONTACT TERM   :   6357 ;   4.00 ;  SEMIHARMONIC       
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.94                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.13                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.31                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3   ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY.                        
REMARK   3   THE INHIBITOR HAS BEEN MODELED IN TWO ORIENTATIONS                 
REMARK   4                                                                      
REMARK   4 4C4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-SEP-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58281.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS)                    
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35085                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.17                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.31                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.3                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.90                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.41                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3OTQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP. 1 UL PROTEIN               
REMARK 280  SOLUTION (8 MG/ML SEH IN 100 MM NAPO2, PH 7.4, 5 MM DTT             
REMARK 280  AND 15% GLYCEROL) WAS MIXED WITH 1 UL RESERVOIR SOLUTION            
REMARK 280  (100 MM TRIS-HCL, PH 8.3, 26% PEG4000 AND 200 MM LI2SO4             
REMARK 280  AND EQUILIBRATED AT 20C. CRYSTALS APPEARED IN ABOUT 2 WEEKS         
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       39.93500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     CYS A   232                                                      
REMARK 465     ASN A   233                                                      
REMARK 465     PRO A   234                                                      
REMARK 465     ASN A   548                                                      
REMARK 465     PRO A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     VAL A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     LYS A   554                                                      
REMARK 465     MET A   555                                                      
REMARK 465     THR B   230                                                      
REMARK 465     SER B   231                                                      
REMARK 465     CYS B   232                                                      
REMARK 465     ASN B   233                                                      
REMARK 465     ASN B   548                                                      
REMARK 465     PRO B   549                                                      
REMARK 465     PRO B   550                                                      
REMARK 465     VAL B   551                                                      
REMARK 465     VAL B   552                                                      
REMARK 465     SER B   553                                                      
REMARK 465     LYS B   554                                                      
REMARK 465     MET B   555                                                      
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     PRO B 234    CG   CD                                             
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 269     -155.87   -105.31                                   
REMARK 500    ASP A 335     -118.00     59.52                                   
REMARK 500    ASN A 359      -40.95     72.89                                   
REMARK 500    SER A 418       61.98   -112.37                                   
REMARK 500    CYS A 423      132.65     69.42                                   
REMARK 500    GLU A 424      124.51     -8.05                                   
REMARK 500    ALA A 425      -47.61      4.68                                   
REMARK 500    LEU A 480      106.89     38.59                                   
REMARK 500    LEU A 499       67.87   -105.24                                   
REMARK 500    HIS A 513       38.40    -99.22                                   
REMARK 500    PRO B 268       75.58   -100.53                                   
REMARK 500    GLU B 269     -156.83    -99.78                                   
REMARK 500    ASP B 335     -118.98     58.44                                   
REMARK 500    ASN B 359      -45.83     69.92                                   
REMARK 500    PHE B 381       31.36    -92.64                                   
REMARK 500    VAL B 422       63.37   -108.88                                   
REMARK 500    CYS B 423      -44.84   -153.32                                   
REMARK 500    PHE B 429       59.91   -104.75                                   
REMARK 500    LEU B 480      117.25    -10.76                                   
REMARK 500    HIS B 513       32.35    -97.44                                   
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    GLU A 269        24.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 341        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 424        23.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 269        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE W9M A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE W9M B1548                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C4Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BIFUNCTIONAL EPOXIDE                     
REMARK 900  HYDROXYLASE 2 COMPLEXED WITH A4                                     
REMARK 900 RELATED ID: 4C4Z   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BIFUNCTIONAL EPOXIDE                     
REMARK 900  HYDROXYLASE 2 COMPLEXED WITH A8                                     
DBREF  4C4X A  230   555  UNP    P34913   HYES_HUMAN     230    555             
DBREF  4C4X B  230   555  UNP    P34913   HYES_HUMAN     230    555             
SEQRES   1 A  326  THR SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL          
SEQRES   2 A  326  THR VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU          
SEQRES   3 A  326  GLY SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO          
SEQRES   4 A  326  GLU SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU          
SEQRES   5 A  326  ALA GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS          
SEQRES   6 A  326  GLY TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU          
SEQRES   7 A  326  TYR CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE          
SEQRES   8 A  326  LEU ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY          
SEQRES   9 A  326  HIS ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU          
SEQRES  10 A  326  PHE TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN          
SEQRES  11 A  326  THR PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU          
SEQRES  12 A  326  GLU SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU          
SEQRES  13 A  326  TYR PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU          
SEQRES  14 A  326  GLN ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA          
SEQRES  15 A  326  SER ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU          
SEQRES  16 A  326  ALA GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER          
SEQRES  17 A  326  LEU SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR          
SEQRES  18 A  326  VAL GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU          
SEQRES  19 A  326  ASN TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA          
SEQRES  20 A  326  CYS LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU          
SEQRES  21 A  326  MET VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN          
SEQRES  22 A  326  MET SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS          
SEQRES  23 A  326  ARG GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET          
SEQRES  24 A  326  ASP LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP          
SEQRES  25 A  326  LEU ASP SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS          
SEQRES  26 A  326  MET                                                          
SEQRES   1 B  326  THR SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL          
SEQRES   2 B  326  THR VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU          
SEQRES   3 B  326  GLY SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO          
SEQRES   4 B  326  GLU SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU          
SEQRES   5 B  326  ALA GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS          
SEQRES   6 B  326  GLY TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU          
SEQRES   7 B  326  TYR CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE          
SEQRES   8 B  326  LEU ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY          
SEQRES   9 B  326  HIS ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU          
SEQRES  10 B  326  PHE TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN          
SEQRES  11 B  326  THR PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU          
SEQRES  12 B  326  GLU SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU          
SEQRES  13 B  326  TYR PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU          
SEQRES  14 B  326  GLN ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA          
SEQRES  15 B  326  SER ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU          
SEQRES  16 B  326  ALA GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER          
SEQRES  17 B  326  LEU SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR          
SEQRES  18 B  326  VAL GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU          
SEQRES  19 B  326  ASN TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA          
SEQRES  20 B  326  CYS LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU          
SEQRES  21 B  326  MET VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN          
SEQRES  22 B  326  MET SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS          
SEQRES  23 B  326  ARG GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET          
SEQRES  24 B  326  ASP LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP          
SEQRES  25 B  326  LEU ASP SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS          
SEQRES  26 B  326  MET                                                          
HET    W9M  A1548      28                                                       
HET    W9M  B1548      28                                                       
HETNAM     W9M 3-(3,4-DICHLOROPHENYL)-1,1-DIMETHYL-UREA                         
FORMUL   3  W9M    2(C9 H10 CL2 N2 O)                                           
FORMUL   4  HOH   *445(H2 O)                                                    
HELIX    1   1 SER A  270  ARG A  275  5                                   6    
HELIX    2   2 TYR A  276  ALA A  284  1                                   9    
HELIX    3   3 ILE A  305  TYR A  308  5                                   4    
HELIX    4   4 CYS A  309  LEU A  324  1                                  16    
HELIX    5   5 ASP A  335  TYR A  348  1                                  14    
HELIX    6   6 SER A  370  ASN A  378  1                                   9    
HELIX    7   7 PHE A  381  PHE A  387  1                                   7    
HELIX    8   8 GLY A  391  ASN A  400  1                                  10    
HELIX    9   9 ASN A  400  PHE A  409  1                                  10    
HELIX   10  10 THR A  443  LYS A  455  1                                  13    
HELIX   11  11 PHE A  459  ASN A  464  1                                   6    
HELIX   12  12 ASN A  468  LYS A  478  1                                  11    
HELIX   13  13 VAL A  500  GLN A  505  5                                   6    
HELIX   14  14 HIS A  506  TRP A  510  5                                   5    
HELIX   15  15 TRP A  525  LYS A  530  1                                   6    
HELIX   16  16 LYS A  530  ALA A  546  1                                  17    
HELIX   17  17 SER B  270  ARG B  275  5                                   6    
HELIX   18  18 TYR B  276  ALA B  284  1                                   9    
HELIX   19  19 ILE B  305  TYR B  308  5                                   4    
HELIX   20  20 CYS B  309  LEU B  324  1                                  16    
HELIX   21  21 ASP B  335  TYR B  348  1                                  14    
HELIX   22  22 SER B  370  ASN B  378  1                                   9    
HELIX   23  23 PRO B  379  PHE B  381  5                                   3    
HELIX   24  24 ASP B  382  PHE B  387  1                                   6    
HELIX   25  25 GLY B  391  ASN B  400  1                                  10    
HELIX   26  26 ASN B  400  PHE B  409  1                                  10    
HELIX   27  27 THR B  443  LYS B  455  1                                  13    
HELIX   28  28 PHE B  459  ASN B  464  1                                   6    
HELIX   29  29 ASN B  468  CYS B  477  1                                  10    
HELIX   30  30 VAL B  500  GLN B  505  5                                   6    
HELIX   31  31 HIS B  506  TRP B  510  5                                   5    
HELIX   32  32 TRP B  525  LYS B  530  1                                   6    
HELIX   33  33 LYS B  530  ALA B  546  1                                  17    
SHEET    1  AA16 LEU A 514  ILE A 519  0                                        
SHEET    2  AA16 ALA A 488  ALA A 493  1  O  ALA A 488   N  LYS A 515           
SHEET    3  AA16 VAL A 352  LEU A 358  1  O  VAL A 355   N  LEU A 489           
SHEET    4  AA16 ALA A 329  HIS A 334  1  O  ALA A 329   N  ARG A 353           
SHEET    5  AA16 ALA A 260  CYS A 264  1  O  ALA A 260   N  VAL A 330           
SHEET    6  AA16 ARG A 287  ASP A 292  1  O  ARG A 287   N  VAL A 261           
SHEET    7  AA16 VAL A 248  LEU A 255 -1  O  HIS A 251   N  ASP A 292           
SHEET    8  AA16 SER A 238  LYS A 245 -1  O  SER A 238   N  GLU A 254           
SHEET    9  AA16 SER B 238  THR B 243 -1  O  HIS B 239   N  TYR A 241           
SHEET   10  AA16 ARG B 249  LEU B 255 -1  O  LEU B 250   N  VAL B 242           
SHEET   11  AA16 ARG B 287  ASP B 292 -1  O  VAL B 288   N  LEU B 255           
SHEET   12  AA16 ALA B 260  CYS B 264  1  O  VAL B 261   N  LEU B 289           
SHEET   13  AA16 ALA B 329  HIS B 334  1  O  VAL B 330   N  CYS B 262           
SHEET   14  AA16 VAL B 352  LEU B 358  1  N  ARG B 353   O  ALA B 329           
SHEET   15  AA16 ALA B 488  ALA B 493  1  O  LEU B 489   N  SER B 357           
SHEET   16  AA16 LEU B 514  ILE B 519  1  O  LYS B 515   N  MET B 490           
CISPEP   1 PHE A  267    PRO A  268          0        -7.26                     
CISPEP   2 CYS A  423    GLU A  424          0         3.58                     
CISPEP   3 PHE B  267    PRO B  268          0        -6.44                     
SITE     1 AC1  8 PHE A 267  ASP A 335  TYR A 383  LEU A 408                    
SITE     2 AC1  8 MET A 419  TYR A 466  VAL A 498  HIS A 524                    
SITE     1 AC2  8 PHE B 267  ASP B 335  TYR B 383  LEU B 408                    
SITE     2 AC2  8 MET B 419  TYR B 466  VAL B 498  HIS B 524                    
CRYST1   47.690   79.870   88.610  90.00  89.95  90.00 P 1 21 1      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      0.020969  0.000000 -0.000018        0.00000                         
SCALE2      0.000000  0.012520  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011285        0.00000                         
TER    2529      ARG A 547                                                      
TER    5063      ARG B 547                                                      
MASTER      333    0    2   33   16    0    4    6 5562    2   56   52          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer