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Database: PDB
Entry: 5AHX
LinkDB: 5AHX
Original site: 5AHX 
HEADER    HYDROLASE                               10-FEB-15   5AHX              
TITLE     APO STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-548;                                            
COMPND   5 SYNONYM: EPOXIDE HYDRATASE, SOLUBLE EPOXIDE HYDROLASE, SEH, SOLUBLE  
COMPND   6 EPOXIDE HYDROLASE;                                                   
COMPND   7 EC: 3.3.2.10, 3.1.3.76;                                              
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.OSTER,S.TAPANI,Y.XUE,H.KACK                                         
REVDAT   3   04-APR-18 5AHX    1       REMARK                                   
REVDAT   2   23-SEP-15 5AHX    1       JRNL                                     
REVDAT   1   13-MAY-15 5AHX    0                                                
JRNL        AUTH   L.OSTER,S.TAPANI,Y.XUE,H.KACK                                
JRNL        TITL   SUCCESSFUL GENERATION OF STRUCTURAL INFORMATION FOR          
JRNL        TITL 2 FRAGMENT-BASED DRUG DISCOVERY.                               
JRNL        REF    DRUG DISCOV TODAY             V.  20  1104 2015              
JRNL        REFN                   ISSN 1359-6446                               
JRNL        PMID   25931264                                                     
JRNL        DOI    10.1016/J.DRUDIS.2015.04.005                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.5                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 42201                          
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)  : NULL                           
REMARK   3   R VALUE            (WORKING SET)  : 0.171                          
REMARK   3   FREE R VALUE                      : 0.219                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2133                           
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   (ANGSTROMS) : NULL                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : NULL                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : NULL                     
REMARK   3   BIN R VALUE               (WORKING SET) : NULL                     
REMARK   3   BIN FREE R VALUE                        : NULL                     
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : NULL                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
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            : 4323                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 429                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.87330                                             
REMARK   3    B22 (A**2) : -0.87330                                             
REMARK   3    B33 (A**2) : 1.74660                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.198               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.170               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.153               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.154               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.146               
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      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4441   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6017   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1548   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 106    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 631    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4441   ; 20.000 ; 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   : 562    ; 5.000  ; SEMIHARMONI         
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
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   : 5498   ; 4.000  ; SEMIHARMONI         
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.13                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.48                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.03                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5AHX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063015.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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 FR-E+                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN A200                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42307                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 245.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.70                              
REMARK 200  R MERGE                    (I) : 0.18000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
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) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.88000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      163.51533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       81.75767            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      122.63650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.87883            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      204.39417            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      163.51533            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       81.75767            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       40.87883            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      122.63650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      204.39417            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.3 KCAL/MOL                        
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   BIOMT1   2  0.500000  0.866025  0.000000       45.86900            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -79.44744            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -40.87883            
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     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A   548                                                      
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   OD1  ASP A   322     NH2  ARG A   351              1.95            
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    LEU A  10      -73.94    -85.32                                   
REMARK 500    VAL A  13      -74.18   -124.07                                   
REMARK 500    GLN A 204      -90.47   -112.85                                   
REMARK 500    GLU A 269     -146.87   -111.57                                   
REMARK 500    ASP A 335     -125.63     58.51                                   
REMARK 500    ASN A 359      -45.26     72.84                                   
REMARK 500    SER A 415      126.49    -37.40                                   
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 SO4 A 1548                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1549                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1550                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AI0   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AI4   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AI5   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AI6   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AI8   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AI9   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AIA   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AIB   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
REMARK 900 RELATED ID: 5AIC   RELATED DB: PDB                                   
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                
DBREF  5AHX A    1   548  UNP    P34913   HYES_HUMAN       1    548             
SEQADV 5AHX GLY A    0  UNP  P34913              EXPRESSION TAG                 
SEQRES   1 A  549  GLY MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY          
SEQRES   2 A  549  VAL LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG          
SEQRES   3 A  549  THR GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN          
SEQRES   4 A  549  ASP ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR          
SEQRES   5 A  549  ARG LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE          
SEQRES   6 A  549  PRO LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR          
SEQRES   7 A  549  ALA LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU          
SEQRES   8 A  549  ILE PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG          
SEQRES   9 A  549  PRO MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY          
SEQRES  10 A  549  PHE THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP          
SEQRES  11 A  549  ARG ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU          
SEQRES  12 A  549  LEU LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN          
SEQRES  13 A  549  VAL GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE          
SEQRES  14 A  549  LEU LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL          
SEQRES  15 A  549  PHE LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG          
SEQRES  16 A  549  ASP LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP          
SEQRES  17 A  549  THR ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN          
SEQRES  18 A  549  LEU LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN          
SEQRES  19 A  549  PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO          
SEQRES  20 A  549  ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO          
SEQRES  21 A  549  ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR          
SEQRES  22 A  549  SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY          
SEQRES  23 A  549  TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU          
SEQRES  24 A  549  SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU          
SEQRES  25 A  549  VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU          
SEQRES  26 A  549  GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY          
SEQRES  27 A  549  GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU          
SEQRES  28 A  549  ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE          
SEQRES  29 A  549  PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS          
SEQRES  30 A  549  ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU          
SEQRES  31 A  549  PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER          
SEQRES  32 A  549  ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER          
SEQRES  33 A  549  VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU          
SEQRES  34 A  549  PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET          
SEQRES  35 A  549  VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE          
SEQRES  36 A  549  LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG          
SEQRES  37 A  549  ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU          
SEQRES  38 A  549  GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA          
SEQRES  39 A  549  GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS          
SEQRES  40 A  549  MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE          
SEQRES  41 A  549  GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR          
SEQRES  42 A  549  GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP          
SEQRES  43 A  549  ALA ARG ASN                                                  
HET    SO4  A1548       5                                                       
HET    SO4  A1549       5                                                       
HET    GOL  A1550       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *429(H2 O)                                                    
HELIX    1   1 ALA A   18  LEU A   30  1                                  13    
HELIX    2   2 GLY A   35  LYS A   43  1                                   9    
HELIX    3   3 GLY A   44  GLU A   47  5                                   4    
HELIX    4   4 GLY A   48  LYS A   55  1                                   8    
HELIX    5   5 THR A   59  ALA A   78  1                                  20    
HELIX    6   6 SER A   87  ARG A   99  1                                  13    
HELIX    7   7 ASN A  102  LYS A  115  1                                  14    
HELIX    8   8 ARG A  133  MET A  145  1                                  13    
HELIX    9   9 SER A  153  GLY A  157  1                                   5    
HELIX   10  10 GLU A  162  LYS A  174  1                                  13    
HELIX   11  11 SER A  176  SER A  178  5                                   3    
HELIX   12  12 ILE A  186  GLY A  197  1                                  12    
HELIX   13  13 ASP A  205  GLY A  218  1                                  14    
HELIX   14  14 ASN A  233  MET A  237  5                                   5    
HELIX   15  15 SER A  270  ARG A  275  5                                   6    
HELIX   16  16 GLN A  277  ALA A  284  1                                   8    
HELIX   17  17 GLU A  304  TYR A  308  5                                   5    
HELIX   18  18 CYS A  309  GLY A  325  1                                  17    
HELIX   19  19 ASP A  335  TYR A  348  1                                  14    
HELIX   20  20 SER A  370  ALA A  377  1                                   8    
HELIX   21  21 ASN A  378  VAL A  380  5                                   3    
HELIX   22  22 PHE A  381  PHE A  387  1                                   7    
HELIX   23  23 GLY A  391  ASN A  400  1                                  10    
HELIX   24  24 ASN A  400  PHE A  409  1                                  10    
HELIX   25  25 ALA A  411  SER A  415  5                                   5    
HELIX   26  26 LYS A  421  GLY A  426  1                                   6    
HELIX   27  27 THR A  443  LYS A  455  1                                  13    
HELIX   28  28 PHE A  459  TRP A  465  1                                   7    
HELIX   29  29 ASN A  468  LYS A  478  1                                  11    
HELIX   30  30 VAL A  500  GLN A  505  5                                   6    
HELIX   31  31 HIS A  506  TRP A  510  5                                   5    
HELIX   32  32 TRP A  525  LYS A  530  1                                   6    
HELIX   33  33 LYS A  530  ALA A  546  1                                  17    
SHEET    1  AA 5 PHE A 149  GLU A 152  0                                        
SHEET    2  AA 5 THR A 118  THR A 123  1  O  THR A 119   N  PHE A 149           
SHEET    3  AA 5 ALA A   5  PHE A   8  1  O  ALA A   6   N  ALA A 120           
SHEET    4  AA 5 VAL A 180  ASP A 184  1  O  VAL A 181   N  VAL A   7           
SHEET    5  AA 5 VAL A 199  LEU A 202  1  O  VAL A 199   N  PHE A 182           
SHEET    1  AB 2 ALA A  15  LEU A  16  0                                        
SHEET    2  AB 2 LYS A 100  ILE A 101 -1  O  LYS A 100   N  LEU A  16           
SHEET    1  AC 8 SER A 238  LYS A 245  0                                        
SHEET    2  AC 8 VAL A 248  LEU A 255 -1  O  VAL A 248   N  VAL A 244           
SHEET    3  AC 8 ARG A 287  ASP A 292 -1  O  VAL A 288   N  LEU A 255           
SHEET    4  AC 8 ALA A 260  CYS A 264  1  O  VAL A 261   N  LEU A 289           
SHEET    5  AC 8 ALA A 329  HIS A 334  1  O  VAL A 330   N  CYS A 262           
SHEET    6  AC 8 VAL A 352  LEU A 358  1  N  ARG A 353   O  ALA A 329           
SHEET    7  AC 8 ALA A 488  ALA A 493  1  O  LEU A 489   N  SER A 357           
SHEET    8  AC 8 LYS A 515  ILE A 519  1  O  LYS A 515   N  MET A 490           
CISPEP   1 LEU A   16    PRO A   17          0        -2.75                     
CISPEP   2 LYS A  160    PRO A  161          0         7.95                     
CISPEP   3 PHE A  267    PRO A  268          0        -6.29                     
SITE     1 AC1  6 GLN A  42  LYS A  43  GLY A  44  LYS A 191                    
SITE     2 AC1  6 ARG A 194  HOH A2186                                          
SITE     1 AC2  3 PHE A 267  TYR A 383  TRP A 525                               
SITE     1 AC3  7 ALA A 365  ASN A 366  TRP A 473  HOH A2304                    
SITE     2 AC3  7 HOH A2308  HOH A2365  HOH A2429                               
CRYST1   91.738   91.738  245.273  90.00  90.00 120.00 P 65 2 2     12          
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      0.010901  0.006293  0.000000        0.00000                         
SCALE2      0.000000  0.012587  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004077        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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