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LongText Report for: 3PDC-pdb

Name Class
3PDC-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           22-OCT-10   3PDC              
TITLE     CRYSTAL STRUCTURE OF HYDROLASE DOMAIN OF HUMAN SOLUBLE EPOXIDE        
TITLE    2 HYDROLASE COMPLEXED WITH A BENZOXAZOLE INHIBITOR                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXIDE HYDROLASE 2;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HYDROLASE DOMAIN (UNP RESIDUES 226 TO 548);                
COMPND   5 SYNONYM: CYTOSOLIC EPOXIDE HYDROLASE, CEH, EPOXIDE HYDRATASE, SOLUBLE
COMPND   6 EPOXIDE HYDROLASE, SEH;                                              
COMPND   7 EC: 3.3.2.10;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EPHX2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    EPOXIDE HYDROLASE, HYDROLASE, HYPERTENSION, BETA BARREL, ALPHA/BETA   
KEYWDS   2 HYDROLASE FOLD; EPOXIDE HYDROLASE FOLD, ACTS ON EPOXIDES (ALKENE     
KEYWDS   3 OXIDES, OXIRANES) AND ARENE OXIDES. PLAYS A ROLE IN XENOBIOTIC       
KEYWDS   4 METABOLISM BY DEGRADING POTENTIALLY TOXIC EPOXIDES. ALSO DETERMINES  
KEYWDS   5 STEADY-STATE LEVELS OF PHYSIOLOGICAL MEDIATORS. HAS LOW PHOSPHATASE  
KEYWDS   6 ACTIVITY, BINDS MG2+, ACETYLATION OF LYSINE, CYTOPLASM; PEROXISOME,  
KEYWDS   7 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.G.KURUMBAIL,J.M.WILLIAMS                                            
REVDAT   1   06-APR-11 3PDC    0                                                
JRNL        AUTH   L.XING,J.J.MCDONALD,S.A.KOLODZIEJ,R.G.KURUMBAIL,             
JRNL        AUTH 2 J.M.WILLIAMS,C.J.WARREN,J.M.O'NEAL,J.E.SKEPNER,S.L.ROBERDS   
JRNL        TITL   DISCOVERY OF POTENT INHIBITORS OF SOLUBLE EPOXIDE HYDROLASE  
JRNL        TITL 2 BY COMBINATORIAL LIBRARY DESIGN AND STRUCTURE-BASED VIRTUAL  
JRNL        TITL 3 SCREENING.                                                   
JRNL        REF    J.MED.CHEM.                   V.  54  1211 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21302953                                                     
JRNL        DOI    10.1021/JM101382T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 18003                          
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 SELECTION OF 5% OF       
REMARK   3                                      REFLECTIONS                     
REMARK   3   R VALUE            (WORKING SET) : 0.279                           
REMARK   3   FREE R VALUE                     : 0.333                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 897                             
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3720                       
REMARK   3   BIN FREE R VALUE                    : 0.4340                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 104                          
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            : 5196                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 191                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.43                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 10.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.55                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 22.80                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ISOTROPIC B FACTOR REFINEMENT             
REMARK   4                                                                      
REMARK   4 3PDC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062239.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 130 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18410                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : 0.12000                            
REMARK 200   FOR THE DATA SET  : 6.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1S80                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30% PEG6K, 0.1M SODIUM CACODYLATE,    
REMARK 280  0.07M AMMONIUM ACETATE, 0.1M MAGNESIUM ACETATE, PH 7.4, VAPOR       
REMARK 280  DIFFUSION, TEMPERATURE 298K                                         
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       39.95100            
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS TWO COPIES OF THE BIOLOGICAL    
REMARK 300 UNIT(UNIT 1)                                                         
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     MET A   203                                                      
REMARK 465     GLY A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     SER A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     HIS A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     PRO A   218                                                      
REMARK 465     ARG A   219                                                      
REMARK 465     GLY A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     HIS A   222                                                      
REMARK 465     MET A   223                                                      
REMARK 465     MET B   203                                                      
REMARK 465     GLY B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     SER B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     HIS B   210                                                      
REMARK 465     HIS B   211                                                      
REMARK 465     HIS B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     SER B   214                                                      
REMARK 465     GLY B   215                                                      
REMARK 465     LEU B   216                                                      
REMARK 465     VAL B   217                                                      
REMARK 465     PRO B   218                                                      
REMARK 465     ARG B   219                                                      
REMARK 465     GLY B   220                                                      
REMARK 465     SER B   221                                                      
REMARK 465     HIS B   222                                                      
REMARK 465     MET B   223                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 408   CD  -  NE  -  CZ  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A 408   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A 408   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    LEU A 488   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG B 408   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG B 408   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG B 408   NE  -  CZ  -  NH2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    LEU B 488   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 229     -164.11   -104.83                                   
REMARK 500    PRO A 266       76.91   -113.67                                   
REMARK 500    GLU A 267     -142.66    -91.68                                   
REMARK 500    SER A 268     -178.82   -176.53                                   
REMARK 500    ASP A 290       51.31   -106.26                                   
REMARK 500    MET A 291      135.45     -7.37                                   
REMARK 500    PRO A 301      -18.72    -49.09                                   
REMARK 500    ASP A 333     -119.71     61.18                                   
REMARK 500    ASN A 357      -47.16     70.47                                   
REMARK 500    PHE A 407       88.92    -64.94                                   
REMARK 500    SER A 413      178.60    -47.18                                   
REMARK 500    VAL A 415      -30.69   -166.59                                   
REMARK 500    HIS A 419      -70.24   -118.48                                   
REMARK 500    ASN A 430       58.83   -105.34                                   
REMARK 500    LYS A 455      -87.37    -94.96                                   
REMARK 500    SER A 478      -22.46   -178.12                                   
REMARK 500    LEU A 479     -102.44     21.65                                   
REMARK 500    LEU A 498       71.92   -112.79                                   
REMARK 500    HIS A 512       50.69   -115.06                                   
REMARK 500    TRP A 524       49.47    -78.40                                   
REMARK 500    THR A 525      -46.02    -25.02                                   
REMARK 500    ARG A 546      -31.94    -34.50                                   
REMARK 500    SER B 229     -163.58   -105.53                                   
REMARK 500    HIS B 263     -168.54    -76.65                                   
REMARK 500    PRO B 266       77.89   -113.47                                   
REMARK 500    GLU B 267     -142.77    -91.47                                   
REMARK 500    SER B 268     -178.15   -176.21                                   
REMARK 500    ARG B 273      -22.85    -39.64                                   
REMARK 500    ASP B 290       51.81   -104.78                                   
REMARK 500    MET B 291      134.92     -7.23                                   
REMARK 500    PRO B 301      -18.63    -48.83                                   
REMARK 500    ASP B 333     -119.64     61.42                                   
REMARK 500    ASN B 357      -48.05     71.15                                   
REMARK 500    PHE B 407       89.64    -65.90                                   
REMARK 500    SER B 413      178.49    -47.87                                   
REMARK 500    VAL B 415      -30.39   -166.23                                   
REMARK 500    ASN B 430       58.91   -104.76                                   
REMARK 500    LYS B 455      -87.63    -94.74                                   
REMARK 500    SER B 478      -22.54   -178.21                                   
REMARK 500    LEU B 479     -102.28     21.35                                   
REMARK 500    LEU B 498       71.90   -113.19                                   
REMARK 500    HIS B 512       50.95   -114.92                                   
REMARK 500    TRP B 524       49.30    -77.93                                   
REMARK 500    THR B 525      -46.15    -24.80                                   
REMARK 500    ARG B 546      -31.65    -35.20                                   
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1202        DISTANCE =  5.96 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYI A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYI B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1S8O   RELATED DB: PDB                                   
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE                                      
REMARK 900 RELATED ID: 1VJ5   RELATED DB: PDB                                   
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE- N-CYCLOHEXYL-N'-(4-                 
REMARK 900 IODOPHENYL)UREA COMPLEX                                              
REMARK 900 RELATED ID: 1ZD2   RELATED DB: PDB                                   
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE 4-(3-CYCLOHEXYLURIEDO)-              
REMARK 900 ETHANOIC ACID COMPLEX                                                
REMARK 900 RELATED ID: 3IIY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                       
REMARK 900 RELATED ID: 3I28   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                       
DBREF  3PDC A  224   547  UNP    P34913   HYES_HUMAN     226    548             
DBREF  3PDC B  224   547  UNP    P34913   HYES_HUMAN     226    548             
SEQADV 3PDC MET A  203  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC GLY A  204  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER A  205  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER A  206  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS A  207  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS A  208  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS A  209  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS A  210  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS A  211  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS A  212  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER A  213  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER A  214  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC GLY A  215  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC LEU A  216  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC VAL A  217  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC PRO A  218  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC ARG A  219  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC GLY A  220  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER A  221  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS A  222  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC MET A  223  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC MET B  203  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC GLY B  204  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER B  205  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER B  206  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS B  207  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS B  208  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS B  209  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS B  210  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS B  211  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS B  212  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER B  213  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER B  214  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC GLY B  215  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC LEU B  216  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC VAL B  217  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC PRO B  218  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC ARG B  219  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC GLY B  220  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC SER B  221  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC HIS B  222  UNP  P34913              EXPRESSION TAG                 
SEQADV 3PDC MET B  223  UNP  P34913              EXPRESSION TAG                 
SEQRES   1 A  344  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  344  LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU PRO THR          
SEQRES   3 A  344  SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR          
SEQRES   4 A  344  VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY          
SEQRES   5 A  344  SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU          
SEQRES   6 A  344  SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA          
SEQRES   7 A  344  GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY          
SEQRES   8 A  344  TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR          
SEQRES   9 A  344  CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU          
SEQRES  10 A  344  ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS          
SEQRES  11 A  344  ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE          
SEQRES  12 A  344  TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR          
SEQRES  13 A  344  PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU          
SEQRES  14 A  344  SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR          
SEQRES  15 A  344  PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN          
SEQRES  16 A  344  ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER          
SEQRES  17 A  344  ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA          
SEQRES  18 A  344  GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU          
SEQRES  19 A  344  SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL          
SEQRES  20 A  344  GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN          
SEQRES  21 A  344  TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS          
SEQRES  22 A  344  LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET          
SEQRES  23 A  344  VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET          
SEQRES  24 A  344  SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG          
SEQRES  25 A  344  GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP          
SEQRES  26 A  344  LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU          
SEQRES  27 A  344  ASP SER ASP ALA ARG ASN                                      
SEQRES   1 B  344  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  344  LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU PRO THR          
SEQRES   3 B  344  SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR          
SEQRES   4 B  344  VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY          
SEQRES   5 B  344  SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU          
SEQRES   6 B  344  SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA          
SEQRES   7 B  344  GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY          
SEQRES   8 B  344  TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR          
SEQRES   9 B  344  CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU          
SEQRES  10 B  344  ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS          
SEQRES  11 B  344  ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE          
SEQRES  12 B  344  TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR          
SEQRES  13 B  344  PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU          
SEQRES  14 B  344  SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR          
SEQRES  15 B  344  PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN          
SEQRES  16 B  344  ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER          
SEQRES  17 B  344  ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA          
SEQRES  18 B  344  GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU          
SEQRES  19 B  344  SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL          
SEQRES  20 B  344  GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN          
SEQRES  21 B  344  TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS          
SEQRES  22 B  344  LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET          
SEQRES  23 B  344  VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET          
SEQRES  24 B  344  SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG          
SEQRES  25 B  344  GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP          
SEQRES  26 B  344  LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU          
SEQRES  27 B  344  ASP SER ASP ALA ARG ASN                                      
HET    ZYI  A   1      19                                                       
HET    ZYI  B   2      19                                                       
HETNAM     ZYI N-(5-CHLORO-1,3-BENZOXAZOL-2-YL)-2-CYCLOPENTYLACETAMIDE          
FORMUL   3  ZYI    2(C14 H15 CL N2 O2)                                          
FORMUL   5  HOH   *191(H2 O)                                                    
HELIX    1   1 ASN A  231  MET A  235  5                                   5    
HELIX    2   2 SER A  268  ARG A  273  5                                   6    
HELIX    3   3 TYR A  274  ALA A  282  1                                   9    
HELIX    4   4 GLU A  302  TYR A  306  5                                   5    
HELIX    5   5 CYS A  307  GLY A  323  1                                  17    
HELIX    6   6 ASP A  333  PHE A  345  1                                  13    
HELIX    7   7 TYR A  346  GLU A  348  5                                   3    
HELIX    8   8 ASN A  376  VAL A  378  5                                   3    
HELIX    9   9 PHE A  379  GLU A  387  1                                   9    
HELIX   10  10 GLY A  389  ASN A  398  1                                  10    
HELIX   11  11 ASN A  398  PHE A  407  1                                  10    
HELIX   12  12 ALA A  409  SER A  413  5                                   5    
HELIX   13  13 LYS A  420  GLY A  425  1                                   6    
HELIX   14  14 THR A  442  PHE A  453  1                                  12    
HELIX   15  15 PHE A  458  TRP A  464  1                                   7    
HELIX   16  16 ASN A  467  LYS A  477  1                                  11    
HELIX   17  17 SER A  503  ASP A  508  5                                   6    
HELIX   18  18 TRP A  524  LYS A  529  1                                   6    
HELIX   19  19 LYS A  529  ASP A  542  1                                  14    
HELIX   20  20 ASN B  231  MET B  235  5                                   5    
HELIX   21  21 SER B  268  ARG B  273  5                                   6    
HELIX   22  22 TYR B  274  ALA B  282  1                                   9    
HELIX   23  23 GLU B  302  TYR B  306  5                                   5    
HELIX   24  24 CYS B  307  GLY B  323  1                                  17    
HELIX   25  25 ASP B  333  PHE B  345  1                                  13    
HELIX   26  26 TYR B  346  GLU B  348  5                                   3    
HELIX   27  27 ASN B  376  VAL B  378  5                                   3    
HELIX   28  28 PHE B  379  GLU B  387  1                                   9    
HELIX   29  29 GLY B  389  ASN B  398  1                                  10    
HELIX   30  30 ASN B  398  PHE B  407  1                                  10    
HELIX   31  31 ALA B  409  SER B  413  5                                   5    
HELIX   32  32 LYS B  420  GLY B  425  1                                   6    
HELIX   33  33 THR B  442  PHE B  453  1                                  12    
HELIX   34  34 PHE B  458  TRP B  464  1                                   7    
HELIX   35  35 ASN B  467  LYS B  477  1                                  11    
HELIX   36  36 SER B  503  ASP B  508  5                                   6    
HELIX   37  37 TRP B  524  LYS B  529  1                                   6    
HELIX   38  38 LYS B  529  ASP B  542  1                                  14    
SHEET    1   A 8 HIS A 237  LYS A 243  0                                        
SHEET    2   A 8 VAL A 246  LEU A 253 -1  O  VAL A 246   N  VAL A 242           
SHEET    3   A 8 ARG A 285  MET A 289 -1  O  ALA A 288   N  VAL A 251           
SHEET    4   A 8 ALA A 258  CYS A 262  1  N  LEU A 261   O  LEU A 287           
SHEET    5   A 8 ALA A 327  HIS A 332  1  O  VAL A 328   N  CYS A 260           
SHEET    6   A 8 VAL A 350  LEU A 356  1  O  ALA A 354   N  PHE A 329           
SHEET    7   A 8 ALA A 487  ALA A 492  1  O  VAL A 490   N  SER A 355           
SHEET    8   A 8 LEU A 513  ILE A 518  1  O  GLY A 516   N  THR A 491           
SHEET    1   B 8 HIS B 237  LYS B 243  0                                        
SHEET    2   B 8 VAL B 246  LEU B 253 -1  O  VAL B 246   N  VAL B 242           
SHEET    3   B 8 ARG B 285  MET B 289 -1  O  ALA B 288   N  VAL B 251           
SHEET    4   B 8 ALA B 258  CYS B 262  1  N  VAL B 259   O  LEU B 287           
SHEET    5   B 8 ALA B 327  HIS B 332  1  O  VAL B 328   N  CYS B 260           
SHEET    6   B 8 VAL B 350  LEU B 356  1  O  ALA B 354   N  PHE B 329           
SHEET    7   B 8 ALA B 487  ALA B 492  1  O  VAL B 490   N  SER B 355           
SHEET    8   B 8 LEU B 513  ILE B 518  1  O  GLY B 516   N  THR B 491           
CISPEP   1 PHE A  265    PRO A  266          0        -0.72                     
CISPEP   2 PHE B  265    PRO B  266          0        -0.77                     
SITE     1 AC1 10 PHE A 265  ASP A 333  MET A 337  TYR A 381                    
SITE     2 AC1 10 GLN A 382  LEU A 406  LEU A 427  TYR A 465                    
SITE     3 AC1 10 HIS A 523  TRP A 524                                          
SITE     1 AC2 11 PHE B 265  ASP B 333  TRP B 334  THR B 358                    
SITE     2 AC2 11 TYR B 381  GLN B 382  LEU B 406  LEU B 427                    
SITE     3 AC2 11 TYR B 465  HIS B 523  TRP B 524                               
CRYST1   46.523   79.902   89.318  90.00  90.22  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      0.021495  0.000000  0.000084        0.00000                         
SCALE2      0.000000  0.012515  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011196        0.00000                         
TER    2599      ASN A 547                                                      
TER    5198      ASN B 547                                                      
MASTER      379    0    2   38   16    0    6    6 5425    2   38   54          
END                                                                             

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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.
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