Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 3G0I-pdb

Name Class
3G0I-pdb
HEADER    HYDROLASE                               28-JAN-09   3G0I              
TITLE     COMPLEX OF ASPERGILLUS NIGER EPOXIDE HYDROLASE WITH                   
TITLE    2 VALPROMIDE (2-PROPYLPENTANAMIDE)                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXIDE HYDROLASE;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 5-396;                                        
COMPND   5 EC: 3.3.2.9;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;                              
SOURCE   3 ORGANISM_TAXID: 5061;                                                
SOURCE   4 STRAIN: LCP521;                                                      
SOURCE   5 GENE: HYL1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEF-ANEH336                              
KEYWDS    EPOXIDE HYDROLASE, ALPHA/BETA HYDROLASE FOLD, VALPROMIDE, 2-          
KEYWDS   2 PROPYLPENTANAMIDE, HYDROLASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZOU,S.L.MOWBRAY                                                     
REVDAT   1   09-JUN-09 3G0I    0                                                
JRNL        AUTH   M.T.REETZ,M.BOCOLA,L.W.WANG,J.SANCHIS,A.CRONIN,              
JRNL        AUTH 2 M.ARAND,J.ZOU,A.ARCHELAS,A.L.BOTTALLA,A.NAWORYTA,            
JRNL        AUTH 3 S.L.MOWBRAY                                                  
JRNL        TITL   DIRECTED EVOLUTION OF AN ENANTIOSELECTIVE EPOXIDE            
JRNL        TITL 2 HYDROLASE: UNCOVERING THE SOURCE OF                          
JRNL        TITL 3 ENANTIOSELECTIVITY AT EACH EVOLUTIONARY STAGE                
JRNL        REF    J.AM.CHEM.SOC.                V. 131  7334 2009              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   19469578                                                     
JRNL        DOI    10.1021/JA809673D                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.ZOU,B.M.HALLBERG,T.BERGFORS,F.OESCH,M.ARAND,               
REMARK   1  AUTH 2 S.L.MOWBRAY,T.A.JONES                                        
REMARK   1  TITL   STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE AT          
REMARK   1  TITL 2 1.8 A RESOLUTION: IMPLICATIONS FOR THE STRUCTURE             
REMARK   1  TITL 3 AND FUNCTION OF THE MAMMALIAN MICROSOMAL CLASS OF            
REMARK   1  TITL 4 EPOXIDE HYDROLASES                                           
REMARK   1  REF    STRUCTURE                     V.   8   111 2000              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  PMID   10673439                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 47296                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1214                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3226                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.2440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6218                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 454                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.10000                                              
REMARK   3    B33 (A**2) : -0.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.03000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.218         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.179         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.231         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6439 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8771 ; 1.189 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   788 ; 5.862 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   280 ;35.419 ;23.214       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1031 ;13.657 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;17.375 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   940 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4979 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3144 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4431 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   517 ; 0.134 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.158 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.128 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4041 ; 0.563 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6379 ; 0.931 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2767 ; 1.441 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2392 ; 2.283 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3G0I COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051268.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47596                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.9470                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21300                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1QO7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000, 0.1M MES, PH6.0, 0.1M       
REMARK 280  UNBUFFERED SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
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       44.82750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: N/A                                                          
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: 5620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     SER A   322                                                      
REMARK 465     ALA A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     ASN A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     ALA A   327                                                      
REMARK 465     THR A   328                                                      
REMARK 465     THR B   320                                                      
REMARK 465     ALA B   321                                                      
REMARK 465     SER B   322                                                      
REMARK 465     ALA B   323                                                      
REMARK 465     PRO B   324                                                      
REMARK 465     ASN B   325                                                      
REMARK 465     GLY B   326                                                      
REMARK 465     ALA B   327                                                      
REMARK 465     THR B   328                                                      
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    PRO A 118       41.06    -94.39                                   
REMARK 500    THR A 153     -115.46     43.45                                   
REMARK 500    ASP A 192     -137.83     53.15                                   
REMARK 500    ASP A 286      -73.39    -83.20                                   
REMARK 500    LYS A 332      -88.25   -120.02                                   
REMARK 500    PRO B 118       39.25    -94.48                                   
REMARK 500    SER B 120     -177.71   -173.13                                   
REMARK 500    THR B 153     -113.00     45.44                                   
REMARK 500    ASP B 192     -138.48     56.12                                   
REMARK 500    ASP B 286      -77.75    -83.27                                   
REMARK 500    LYS B 332      -90.81   -123.93                                   
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 VPR A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VPR B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QO7   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE                     
DBREF  3G0I A    5   396  UNP    Q9UR30   Q9UR30_ASPNG     5    396             
DBREF  3G0I B    5   396  UNP    Q9UR30   Q9UR30_ASPNG     5    396             
SEQADV 3G0I LYS A    3  UNP  Q9UR30              EXPRESSION TAG                 
SEQADV 3G0I ALA A    4  UNP  Q9UR30              EXPRESSION TAG                 
SEQADV 3G0I LYS B    3  UNP  Q9UR30              EXPRESSION TAG                 
SEQADV 3G0I ALA B    4  UNP  Q9UR30              EXPRESSION TAG                 
SEQRES   1 A  394  LYS ALA PHE ALA LYS PHE PRO SER SER ALA SER ILE SER          
SEQRES   2 A  394  PRO ASN PRO PHE THR VAL SER ILE PRO ASP GLU GLN LEU          
SEQRES   3 A  394  ASP ASP LEU LYS THR LEU VAL ARG LEU SER LYS ILE ALA          
SEQRES   4 A  394  PRO PRO THR TYR GLU SER LEU GLN ALA ASP GLY ARG PHE          
SEQRES   5 A  394  GLY ILE THR SER GLU TRP LEU THR THR MET ARG GLU LYS          
SEQRES   6 A  394  TRP LEU SER GLU PHE ASP TRP ARG PRO PHE GLU ALA ARG          
SEQRES   7 A  394  LEU ASN SER PHE PRO GLN PHE THR THR GLU ILE GLU GLY          
SEQRES   8 A  394  LEU THR ILE HIS PHE ALA ALA LEU PHE SER GLU ARG GLU          
SEQRES   9 A  394  ASP ALA VAL PRO ILE ALA LEU LEU HIS GLY TRP PRO GLY          
SEQRES  10 A  394  SER PHE VAL GLU PHE TYR PRO ILE LEU GLN LEU PHE ARG          
SEQRES  11 A  394  GLU GLU TYR THR PRO GLU THR LEU PRO PHE HIS LEU VAL          
SEQRES  12 A  394  VAL PRO SER LEU PRO GLY TYR THR PHE SER SER GLY PRO          
SEQRES  13 A  394  PRO LEU ASP LYS ASP PHE GLY LEU MET ASP ASN ALA ARG          
SEQRES  14 A  394  VAL VAL ASP GLN LEU MET LYS ASP LEU GLY PHE GLY SER          
SEQRES  15 A  394  GLY TYR ILE ILE GLN GLY GLY ASP ILE GLY SER PHE VAL          
SEQRES  16 A  394  GLY ARG LEU LEU GLY VAL GLY PHE ASP ALA CYS LYS ALA          
SEQRES  17 A  394  VAL HIS LEU ASN LEU CYS ALA MET ARG ALA PRO PRO GLU          
SEQRES  18 A  394  GLY PRO SER ILE GLU SER LEU SER ALA ALA GLU LYS GLU          
SEQRES  19 A  394  GLY ILE ALA ARG MET GLU LYS PHE MET THR ASP GLY LEU          
SEQRES  20 A  394  ALA TYR ALA MET GLU HIS SER THR ARG PRO SER THR ILE          
SEQRES  21 A  394  GLY HIS VAL LEU SER SER SER PRO ILE ALA LEU LEU ALA          
SEQRES  22 A  394  TRP ILE GLY GLU LYS TYR LEU GLN TRP VAL ASP LYS PRO          
SEQRES  23 A  394  LEU PRO SER GLU THR ILE LEU GLU MET VAL SER LEU TYR          
SEQRES  24 A  394  TRP LEU THR GLU SER PHE PRO ARG ALA ILE HIS THR TYR          
SEQRES  25 A  394  ARG GLU THR THR PRO THR ALA SER ALA PRO ASN GLY ALA          
SEQRES  26 A  394  THR MET LEU GLN LYS GLU LEU TYR ILE HIS LYS PRO PHE          
SEQRES  27 A  394  GLY PHE SER PHE PHE PRO LYS ASP LEU CYS PRO VAL PRO          
SEQRES  28 A  394  ARG SER TRP ILE ALA THR THR GLY ASN LEU VAL PHE PHE          
SEQRES  29 A  394  ARG ASP HIS ALA GLU GLY GLY HIS PHE ALA ALA LEU GLU          
SEQRES  30 A  394  ARG PRO ARG GLU LEU LYS THR ASP LEU THR ALA PHE VAL          
SEQRES  31 A  394  GLU GLN VAL TRP                                              
SEQRES   1 B  394  LYS ALA PHE ALA LYS PHE PRO SER SER ALA SER ILE SER          
SEQRES   2 B  394  PRO ASN PRO PHE THR VAL SER ILE PRO ASP GLU GLN LEU          
SEQRES   3 B  394  ASP ASP LEU LYS THR LEU VAL ARG LEU SER LYS ILE ALA          
SEQRES   4 B  394  PRO PRO THR TYR GLU SER LEU GLN ALA ASP GLY ARG PHE          
SEQRES   5 B  394  GLY ILE THR SER GLU TRP LEU THR THR MET ARG GLU LYS          
SEQRES   6 B  394  TRP LEU SER GLU PHE ASP TRP ARG PRO PHE GLU ALA ARG          
SEQRES   7 B  394  LEU ASN SER PHE PRO GLN PHE THR THR GLU ILE GLU GLY          
SEQRES   8 B  394  LEU THR ILE HIS PHE ALA ALA LEU PHE SER GLU ARG GLU          
SEQRES   9 B  394  ASP ALA VAL PRO ILE ALA LEU LEU HIS GLY TRP PRO GLY          
SEQRES  10 B  394  SER PHE VAL GLU PHE TYR PRO ILE LEU GLN LEU PHE ARG          
SEQRES  11 B  394  GLU GLU TYR THR PRO GLU THR LEU PRO PHE HIS LEU VAL          
SEQRES  12 B  394  VAL PRO SER LEU PRO GLY TYR THR PHE SER SER GLY PRO          
SEQRES  13 B  394  PRO LEU ASP LYS ASP PHE GLY LEU MET ASP ASN ALA ARG          
SEQRES  14 B  394  VAL VAL ASP GLN LEU MET LYS ASP LEU GLY PHE GLY SER          
SEQRES  15 B  394  GLY TYR ILE ILE GLN GLY GLY ASP ILE GLY SER PHE VAL          
SEQRES  16 B  394  GLY ARG LEU LEU GLY VAL GLY PHE ASP ALA CYS LYS ALA          
SEQRES  17 B  394  VAL HIS LEU ASN LEU CYS ALA MET ARG ALA PRO PRO GLU          
SEQRES  18 B  394  GLY PRO SER ILE GLU SER LEU SER ALA ALA GLU LYS GLU          
SEQRES  19 B  394  GLY ILE ALA ARG MET GLU LYS PHE MET THR ASP GLY LEU          
SEQRES  20 B  394  ALA TYR ALA MET GLU HIS SER THR ARG PRO SER THR ILE          
SEQRES  21 B  394  GLY HIS VAL LEU SER SER SER PRO ILE ALA LEU LEU ALA          
SEQRES  22 B  394  TRP ILE GLY GLU LYS TYR LEU GLN TRP VAL ASP LYS PRO          
SEQRES  23 B  394  LEU PRO SER GLU THR ILE LEU GLU MET VAL SER LEU TYR          
SEQRES  24 B  394  TRP LEU THR GLU SER PHE PRO ARG ALA ILE HIS THR TYR          
SEQRES  25 B  394  ARG GLU THR THR PRO THR ALA SER ALA PRO ASN GLY ALA          
SEQRES  26 B  394  THR MET LEU GLN LYS GLU LEU TYR ILE HIS LYS PRO PHE          
SEQRES  27 B  394  GLY PHE SER PHE PHE PRO LYS ASP LEU CYS PRO VAL PRO          
SEQRES  28 B  394  ARG SER TRP ILE ALA THR THR GLY ASN LEU VAL PHE PHE          
SEQRES  29 B  394  ARG ASP HIS ALA GLU GLY GLY HIS PHE ALA ALA LEU GLU          
SEQRES  30 B  394  ARG PRO ARG GLU LEU LYS THR ASP LEU THR ALA PHE VAL          
SEQRES  31 B  394  GLU GLN VAL TRP                                              
HET    VPR  A   1      10                                                       
HET    VPR  B   1      10                                                       
HETNAM     VPR 2-PROPYLPENTANAMIDE                                              
HETSYN     VPR VALPROMIDE                                                       
FORMUL   3  VPR    2(C8 H17 N O)                                                
FORMUL   5  HOH   *454(H2 O)                                                    
HELIX    1   1 PRO A   24  SER A   38  1                                  15    
HELIX    2   2 TYR A   45  GLN A   49  5                                   5    
HELIX    3   3 THR A   57  GLU A   71  1                                  15    
HELIX    4   4 ASP A   73  ASN A   82  1                                  10    
HELIX    5   5 SER A  120  GLU A  123  5                                   4    
HELIX    6   6 PHE A  124  TYR A  135  1                                  12    
HELIX    7   7 GLY A  165  LEU A  180  1                                  16    
HELIX    8   8 ASP A  192  PHE A  205  1                                  14    
HELIX    9   9 SER A  226  LEU A  230  5                                   5    
HELIX   10  10 SER A  231  GLY A  248  1                                  18    
HELIX   11  11 LEU A  249  ARG A  258  1                                  10    
HELIX   12  12 ARG A  258  SER A  268  1                                  11    
HELIX   13  13 SER A  269  TRP A  284  1                                  16    
HELIX   14  14 PRO A  290  THR A  304  1                                  15    
HELIX   15  15 GLU A  305  ILE A  311  1                                   7    
HELIX   16  16 THR A  313  THR A  318  1                                   6    
HELIX   17  17 PRO A  353  ALA A  358  1                                   6    
HELIX   18  18 PHE A  375  ARG A  380  1                                   6    
HELIX   19  19 ARG A  380  TRP A  396  1                                  17    
HELIX   20  20 PRO B   24  SER B   38  1                                  15    
HELIX   21  21 TYR B   45  GLN B   49  5                                   5    
HELIX   22  22 THR B   57  GLU B   71  1                                  15    
HELIX   23  23 ASP B   73  ASN B   82  1                                  10    
HELIX   24  24 SER B  120  GLU B  123  5                                   4    
HELIX   25  25 PHE B  124  TYR B  135  1                                  12    
HELIX   26  26 GLY B  165  LEU B  180  1                                  16    
HELIX   27  27 ASP B  192  PHE B  205  1                                  14    
HELIX   28  28 SER B  231  GLY B  248  1                                  18    
HELIX   29  29 LEU B  249  ARG B  258  1                                  10    
HELIX   30  30 ARG B  258  SER B  269  1                                  12    
HELIX   31  31 SER B  269  TRP B  284  1                                  16    
HELIX   32  32 PRO B  290  THR B  304  1                                  15    
HELIX   33  33 GLU B  305  ILE B  311  1                                   7    
HELIX   34  34 THR B  313  THR B  318  1                                   6    
HELIX   35  35 PRO B  353  ALA B  358  1                                   6    
HELIX   36  36 PHE B  375  ARG B  380  1                                   6    
HELIX   37  37 ARG B  380  TRP B  396  1                                  17    
SHEET    1   A 8 GLN A  86  ILE A  91  0                                        
SHEET    2   A 8 LEU A  94  LEU A 101 -1  O  ILE A  96   N  THR A  89           
SHEET    3   A 8 PHE A 142  PRO A 147 -1  O  VAL A 146   N  ALA A  99           
SHEET    4   A 8 VAL A 109  LEU A 114  1  N  ILE A 111   O  VAL A 145           
SHEET    5   A 8 TYR A 186  GLY A 190  1  O  GLN A 189   N  LEU A 114           
SHEET    6   A 8 CYS A 208  LEU A 213  1  O  LYS A 209   N  TYR A 186           
SHEET    7   A 8 ILE A 336  PHE A 344  1  O  GLY A 341   N  VAL A 211           
SHEET    8   A 8 GLY A 361  ASP A 368  1  O  ARG A 367   N  PHE A 344           
SHEET    1   B 8 GLN B  86  ILE B  91  0                                        
SHEET    2   B 8 LEU B  94  LEU B 101 -1  O  ILE B  96   N  THR B  89           
SHEET    3   B 8 PHE B 142  PRO B 147 -1  O  VAL B 146   N  ALA B  99           
SHEET    4   B 8 VAL B 109  LEU B 114  1  N  ILE B 111   O  VAL B 145           
SHEET    5   B 8 TYR B 186  GLY B 190  1  O  GLN B 189   N  LEU B 114           
SHEET    6   B 8 CYS B 208  LEU B 213  1  O  HIS B 212   N  ILE B 188           
SHEET    7   B 8 ILE B 336  PHE B 344  1  O  GLY B 341   N  LEU B 213           
SHEET    8   B 8 GLY B 361  ASP B 368  1  O  ARG B 367   N  PHE B 344           
CISPEP   1 TRP A  117    PRO A  118          0         3.83                     
CISPEP   2 GLY A  157    PRO A  158          0        -2.88                     
CISPEP   3 GLY A  224    PRO A  225          0         2.73                     
CISPEP   4 TRP B  117    PRO B  118          0         2.80                     
CISPEP   5 GLY B  157    PRO B  158          0         1.38                     
CISPEP   6 GLY B  224    PRO B  225          0        -4.36                     
SITE     1 AC1  6 TRP A 117  ASP A 192  ILE A 193  PHE A 196                    
SITE     2 AC1  6 TYR A 251  TYR A 314                                          
SITE     1 AC2  8 TRP B 117  ASP B 192  ILE B 193  PHE B 244                    
SITE     2 AC2  8 TYR B 251  TRP B 284  TYR B 314  THR B 317                    
CRYST1   62.985   89.655   75.812  90.00 105.31  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      0.015877  0.000000  0.004345        0.00000                         
SCALE2      0.000000  0.011154  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013676        0.00000                         
TER    3103      TRP A 396                                                      
TER    6220      TRP B 396                                                      
MASTER      303    0    2   37   16    0    4    6 6692    2   20   62          
END                                                                             

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

Acknowledgements and disclaimer