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LongText Report for: 5ALY-pdb

Name Class
5ALY-pdb
HEADER    HYDROLASE                               08-MAR-15   5ALY              
TITLE     LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EPOXIDE HYDRATASE, SOLUBLE EPOXIDE HYDROLASE, SEH;          
COMPND   5 EC: 3.3.2.10, 3.1.3.76;                                              
COMPND   6 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                                     
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.OSTER,S.TAPANI,Y.XUE,H.KACK                                         
REVDAT   1   13-MAY-15 5ALY    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                          2015              
JRNL        REFN                   ESSN 1878-5832                               
JRNL        PMID   25931264                                                     
JRNL        DOI    10.1016/J.DRUDIS.2015.04.005                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.1                                        
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.12                          
REMARK   3   NUMBER OF REFLECTIONS             : 46296                          
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)  : 0.1979                         
REMARK   3   R VALUE            (WORKING SET)  : 0.1953                         
REMARK   3   FREE R VALUE                      : 0.2463                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.10                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 2360                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.90                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.95                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 94.12                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3249                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.4238                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3077                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.4215                   
REMARK   3   BIN FREE R VALUE                        : 0.4650                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.29                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 172                      
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          : 51                                      
REMARK   3   SOLVENT ATOMS            : 535                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.6667                                               
REMARK   3    B22 (A**2) : 0.6667                                               
REMARK   3    B33 (A**2) : -1.3335                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.181               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.164               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.162               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.155               
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      : 0.9505                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9157                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4501   ; 2.00   ; HARMONIC            
REMARK   3    BOND ANGLES               : 6102   ; 2.00   ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1562   ; 2.00   ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 106    ; 2.00   ; HARMONIC            
REMARK   3    GENERAL PLANES            : 645    ; 5.00   ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4501   ; 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   : 565    ; 5.00   ; SEMIHARMONIC        
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   : 5755   ; 4.00   ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.48                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.59                    
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 5ALY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-63255.                                       
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          : FRE PLUS RIGAKU                    
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 (SATURN A200)                  
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46297                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 12.1                               
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.2                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.32                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.30                               
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: PDB ENTRY 5AHX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
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      162.69667            
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       81.34833            
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      122.02250            
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       40.67417            
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      203.37083            
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      162.69667            
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       81.34833            
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       40.67417            
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      122.02250            
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      203.37083            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 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      -73.17    -90.50                                   
REMARK 500    VAL A  13      -68.89   -121.34                                   
REMARK 500    ASN A  85       31.22    -84.21                                   
REMARK 500    GLN A 204      -83.78   -112.42                                   
REMARK 500    GLU A 269     -142.55   -114.88                                   
REMARK 500    ASP A 335     -121.05     58.31                                   
REMARK 500    ASN A 359      -45.41     72.79                                   
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 132        24.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 312        21.8      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 480        25.0      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 502        24.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 533        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2535        DISTANCE =  5.70 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1553                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1554                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B7H A1555                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AK3   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AK4   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AK5   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AK6   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKE   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKG   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKH   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKI   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKJ   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKK   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKL   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKX   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKY   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AKZ   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALD   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALE   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALF   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALG   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALH   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALI   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALJ   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALK   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALL   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALM   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALN   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALO   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALP   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALQ   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALR   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALS   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALT   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALU   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALV   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALW   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALX   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5ALZ   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AM0   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AM1   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AM2   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AM3   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AM4   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
REMARK 900 RELATED ID: 5AM5   RELATED DB: PDB                                   
REMARK 900  LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE               
DBREF  5ALY A    1   548  UNP    P34913   HYES_HUMAN       1    548             
SEQADV 5ALY 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    DMS  A1550       4                                                       
HET    DMS  A1551       4                                                       
HET    DMS  A1552       4                                                       
HET    DMS  A1553       4                                                       
HET    DMS  A1554       4                                                       
HET    B7H  A1555      21                                                       
HETNAM     B7H 5-(7-FLUORANYL-3,3-DIMETHYL-2-OXIDANYLIDENE-                     
HETNAM   2 B7H  1H-INDOL-5-YL)-4-METHYL-1H-PYRAZOLE-3-                          
HETNAM   3 B7H  CARBONITRILE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  B7H    C15 H13 F N4 O                                               
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4  DMS    5(C2 H6 O S)                                                 
FORMUL   5  HOH   *535(H2 O)                                                    
HELIX    1   1 PHE A   20  ALA A   31  1                                  12    
HELIX    2   2 GLY A   35  GLN A   42  1                                   8    
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  GLN A  399  1                                   9    
HELIX   24  24 ASN A  400  PHE A  409  1                                  10    
HELIX   25  25 LYS A  421  GLY A  426  1                                   6    
HELIX   26  26 THR A  443  LYS A  456  1                                  14    
HELIX   27  27 PHE A  459  TRP A  465  1                                   7    
HELIX   28  28 ASN A  468  LYS A  478  1                                  11    
HELIX   29  29 VAL A  500  GLN A  505  5                                   6    
HELIX   30  30 HIS A  506  TRP A  510  5                                   5    
HELIX   31  31 TRP A  525  LYS A  530  1                                   6    
HELIX   32  32 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  ILE A 121   N  ILE A 151           
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  MET A 291 -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        -5.81                     
CISPEP   2 LYS A  160    PRO A  161          0         8.37                     
CISPEP   3 PHE A  267    PRO A  268          0        -4.16                     
SITE     1 AC1  6 ASP A 335  TRP A 336  MET A 339  GLN A 384                    
SITE     2 AC1  6 LEU A 499  HOH A2359                                          
SITE     1 AC2  8 LEU A 228  ARG A 440  MET A 441  VAL A 442                    
SITE     2 AC2  8 THR A 443  GLU A 446  HOH A2318  HOH A2319                    
SITE     1 AC3  4 LYS A 144  PHE A 147  HOH A2165  HOH A2350                    
SITE     1 AC4  3 LEU A   3  LYS A 115  PHE A 117                               
SITE     1 AC5  4 TYR A 343  TRP A 473  HOH A2373  HOH A2457                    
SITE     1 AC6  7 ARG A  34  GLY A  35  ASP A  39  LEU A 190                    
SITE     2 AC6  7 THR A 200  ILE A 201  LEU A 202                               
SITE     1 AC7  4 GLN A  42  GLY A  44  LYS A 191  ARG A 194                    
SITE     1 AC8 12 PHE A 267  PHE A 387  LEU A 397  LEU A 408                    
SITE     2 AC8 12 LEU A 417  MET A 419  ASP A 496  PHE A 497                    
SITE     3 AC8 12 VAL A 498  HIS A 524  HOH A2311  HOH A2484                    
CRYST1   92.103   92.103  244.045  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      0.010857  0.006269  0.000000        0.00000                         
SCALE2      0.000000  0.012537  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004098        0.00000                         
TER    4348      ARG A 547                                                      
MASTER      432    0    8   32   15    0   13    6 4933    1   51   43          
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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