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LongText Report for: 4IO0-pdb

Name Class
4IO0-pdb
HEADER    HYDROLASE                               07-JAN-13   4IO0              
TITLE     CRYSTAL STRUCTURE OF F128A MUTANT OF AN EPOXIDE HYDROLASE FROM        
TITLE    2 BACILLUS MEGATERIUM COMPLEXED WITH ITS PRODUCT (R)-3-[1]NAPHTHYLOXY- 
TITLE    3 PROPANE-1,2-DIOL                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUBLE EPOXIDE HYDROLASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.2.2.10;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;                            
SOURCE   3 ORGANISM_TAXID: 1404;                                                
SOURCE   4 STRAIN: ECU1001;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    A/B HYDROLASE FOLD, EPOXIDE HYDROLASE, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.D.KONG,J.H.ZHOU,J.H.XU                                              
REVDAT   1   12-FEB-14 4IO0    0                                                
JRNL        AUTH   X.D.KONG,J.H.ZHOU,J.H.XU                                     
JRNL        TITL   CRYSTAL STRUCTURE OF F128A MUTANT OF AN EPOXIDE HYDROLASE    
JRNL        TITL 2 FROM BACILLUS MEGATERIUM COMPLEXED WITH ITS PRODUCT          
JRNL        TITL 3 (R)-3-[1]NAPHTHYLOXY-PROPANE-1,2-DIOL                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_637)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.25                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15898                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 804                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.2559 -  5.2676    0.99     2752   122  0.1733 0.2174        
REMARK   3     2  5.2676 -  4.1820    0.99     2580   136  0.1165 0.1785        
REMARK   3     3  4.1820 -  3.6537    0.98     2524   132  0.1235 0.1939        
REMARK   3     4  3.6537 -  3.3197    0.97     2489   131  0.1606 0.2581        
REMARK   3     5  3.3197 -  3.0818    0.95     2442   129  0.2022 0.2986        
REMARK   3     6  3.0818 -  2.9002    0.92     2307   154  0.2171 0.3205        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.06                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 22.97                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.33440                                             
REMARK   3    B22 (A**2) : -0.33440                                             
REMARK   3    B33 (A**2) : 0.66880                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4912                                  
REMARK   3   ANGLE     :  1.117           6666                                  
REMARK   3   CHIRALITY :  0.075            681                                  
REMARK   3   PLANARITY :  0.004            870                                  
REMARK   3   DIHEDRAL  : 16.365           1810                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4IO0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076991.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121961                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.22100                            
REMARK 200  R SYM                      (I) : 0.22100                            
REMARK 200   FOR THE DATA SET  : 8.3370                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79000                            
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: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4G00                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 2.0 M (NH4)2SO4, 0.2 M       
REMARK 280  LI2SO4, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.74800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       54.82000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       54.82000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.37400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       54.82000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       54.82000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       88.12200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       54.82000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.82000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       29.37400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       54.82000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.82000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       88.12200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       58.74800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     MET A   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     MET A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     MET A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     GLY B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     ALA B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     GLN B    -5                                                      
REMARK 465     MET B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LYS B     3                                                      
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  31       50.75   -105.50                                   
REMARK 500    ASP A  32     -150.89   -100.33                                   
REMARK 500    SER A  34      -35.41    -34.06                                   
REMARK 500    ASN A  59     -115.65     43.85                                   
REMARK 500    GLU A  62      152.10    -45.25                                   
REMARK 500    ASP A  97     -132.64     59.75                                   
REMARK 500    TYR A 110       51.15   -141.49                                   
REMARK 500    PHE A 148       -4.09    -59.26                                   
REMARK 500    LYS A 207       68.54   -100.93                                   
REMARK 500    ASN A 256       20.59     82.39                                   
REMARK 500    SER A 266     -136.84   -111.87                                   
REMARK 500    ALA A 268       67.88   -114.22                                   
REMARK 500    ASN B   9       35.65     36.52                                   
REMARK 500    LYS B  18      114.05   -173.82                                   
REMARK 500    PRO B  31       53.18   -101.65                                   
REMARK 500    ASP B  32     -146.00   -101.06                                   
REMARK 500    PHE B  33     -173.44    178.72                                   
REMARK 500    ASN B  59     -124.59     58.43                                   
REMARK 500    LYS B  63       66.03   -113.94                                   
REMARK 500    ASP B  97     -120.17     59.12                                   
REMARK 500    ASP B 160       65.49     61.65                                   
REMARK 500    LYS B 207       76.12   -103.63                                   
REMARK 500    SER B 266     -118.40   -122.10                                   
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RN1 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RN1 B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G00   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE WILD TYPE ENZYME                                    
REMARK 900 RELATED ID: 4G02   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE WILD TYPE ENZYME COMPLEXED WITH A                   
REMARK 900 SUBSTRATE ANALOGUE                                                   
REMARK 900 RELATED ID: 4INZ   RELATED DB: PDB                                   
DBREF  4IO0 A    1   287  UNP    G9BEX6   G9BEX6_BACME     1    287             
DBREF  4IO0 B    1   287  UNP    G9BEX6   G9BEX6_BACME     1    287             
SEQADV 4IO0 GLY A  -16  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 SER A  -15  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 HIS A  -14  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 MET A  -13  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 ALA A  -12  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 SER A  -11  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 MET A  -10  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 THR A   -9  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY A   -8  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY A   -7  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLN A   -6  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLN A   -5  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 MET A   -4  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY A   -3  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 ARG A   -2  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY A   -1  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 SER A    0  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 ALA A  128  UNP  G9BEX6    PHE   128 ENGINEERED MUTATION            
SEQADV 4IO0 GLY B  -16  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 SER B  -15  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 HIS B  -14  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 MET B  -13  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 ALA B  -12  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 SER B  -11  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 MET B  -10  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 THR B   -9  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY B   -8  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY B   -7  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLN B   -6  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLN B   -5  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 MET B   -4  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY B   -3  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 ARG B   -2  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 GLY B   -1  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 SER B    0  UNP  G9BEX6              EXPRESSION TAG                 
SEQADV 4IO0 ALA B  128  UNP  G9BEX6    PHE   128 ENGINEERED MUTATION            
SEQRES   1 A  304  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 A  304  GLY ARG GLY SER MET SER LYS GLN TYR ILE ASN VAL ASN          
SEQRES   3 A  304  GLY VAL ASN LEU HIS TYR ILE SER LYS GLY GLN GLY GLU          
SEQRES   4 A  304  LEU MET LEU PHE LEU HIS GLY PHE PRO ASP PHE SER HIS          
SEQRES   5 A  304  ILE TRP ARG HIS GLN ILE ASP GLU PHE SER ASN ASP PHE          
SEQRES   6 A  304  HIS THR VAL ALA LEU ASP LEU ARG GLY TYR ASN LEU SER          
SEQRES   7 A  304  GLU LYS PRO SER GLY LEU GLU SER TYR GLU ILE ASP VAL          
SEQRES   8 A  304  LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU GLY LEU GLY          
SEQRES   9 A  304  TYR SER SER CYS THR LEU VAL VAL HIS ASP TRP GLY ALA          
SEQRES  10 A  304  GLY ILE GLY TRP THR PHE ALA TYR ARG TYR PRO GLU TYR          
SEQRES  11 A  304  VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO HIS PRO TYR          
SEQRES  12 A  304  THR ALA MET ARG GLU LEU ARG THR ASN LYS ASN GLN GLN          
SEQRES  13 A  304  LYS ALA SER GLU TYR MET LYS TRP PHE GLN LYS GLN GLU          
SEQRES  14 A  304  VAL GLN ASP TYR MET GLU ARG ASP ASN PHE SER GLY LEU          
SEQRES  15 A  304  ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS LYS GLY TYR          
SEQRES  16 A  304  LEU THR ALA ASP ASP VAL GLN ALA TYR MET ASN SER TRP          
SEQRES  17 A  304  GLU ASN GLY SER VAL LEU SER MET LEU SER TYR TYR ARG          
SEQRES  18 A  304  ASN LEU LYS ILE PHE THR GLU GLU ASP LEU ARG ARG LYS          
SEQRES  19 A  304  SER LEU PHE PRO LEU GLU GLU GLU VAL LEU ASN ILE PRO          
SEQRES  20 A  304  VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO THR PHE MET          
SEQRES  21 A  304  PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR VAL PRO ASN          
SEQRES  22 A  304  ILE SER VAL HIS ARG LEU ALA GLU ALA SER HIS ALA PRO          
SEQRES  23 A  304  GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN VAL MET TRP          
SEQRES  24 A  304  ASN PHE LEU ASN LYS                                          
SEQRES   1 B  304  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 B  304  GLY ARG GLY SER MET SER LYS GLN TYR ILE ASN VAL ASN          
SEQRES   3 B  304  GLY VAL ASN LEU HIS TYR ILE SER LYS GLY GLN GLY GLU          
SEQRES   4 B  304  LEU MET LEU PHE LEU HIS GLY PHE PRO ASP PHE SER HIS          
SEQRES   5 B  304  ILE TRP ARG HIS GLN ILE ASP GLU PHE SER ASN ASP PHE          
SEQRES   6 B  304  HIS THR VAL ALA LEU ASP LEU ARG GLY TYR ASN LEU SER          
SEQRES   7 B  304  GLU LYS PRO SER GLY LEU GLU SER TYR GLU ILE ASP VAL          
SEQRES   8 B  304  LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU GLY LEU GLY          
SEQRES   9 B  304  TYR SER SER CYS THR LEU VAL VAL HIS ASP TRP GLY ALA          
SEQRES  10 B  304  GLY ILE GLY TRP THR PHE ALA TYR ARG TYR PRO GLU TYR          
SEQRES  11 B  304  VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO HIS PRO TYR          
SEQRES  12 B  304  THR ALA MET ARG GLU LEU ARG THR ASN LYS ASN GLN GLN          
SEQRES  13 B  304  LYS ALA SER GLU TYR MET LYS TRP PHE GLN LYS GLN GLU          
SEQRES  14 B  304  VAL GLN ASP TYR MET GLU ARG ASP ASN PHE SER GLY LEU          
SEQRES  15 B  304  ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS LYS GLY TYR          
SEQRES  16 B  304  LEU THR ALA ASP ASP VAL GLN ALA TYR MET ASN SER TRP          
SEQRES  17 B  304  GLU ASN GLY SER VAL LEU SER MET LEU SER TYR TYR ARG          
SEQRES  18 B  304  ASN LEU LYS ILE PHE THR GLU GLU ASP LEU ARG ARG LYS          
SEQRES  19 B  304  SER LEU PHE PRO LEU GLU GLU GLU VAL LEU ASN ILE PRO          
SEQRES  20 B  304  VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO THR PHE MET          
SEQRES  21 B  304  PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR VAL PRO ASN          
SEQRES  22 B  304  ILE SER VAL HIS ARG LEU ALA GLU ALA SER HIS ALA PRO          
SEQRES  23 B  304  GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN VAL MET TRP          
SEQRES  24 B  304  ASN PHE LEU ASN LYS                                          
HET    SO4  A 301       5                                                       
HET    RN1  A 302      16                                                       
HET    SO4  B 301       5                                                       
HET    RN1  B 302      16                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     RN1 (2R)-3-(NAPHTHALEN-1-YLOXY)PROPANE-1,2-DIOL                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4  RN1    2(C13 H14 O3)                                                
FORMUL   7  HOH   *100(H2 O)                                                    
HELIX    1   1 PHE A   33  ILE A   36  5                                   4    
HELIX    2   2 TRP A   37  SER A   45  1                                   9    
HELIX    3   3 GLY A   66  TYR A   70  5                                   5    
HELIX    4   4 GLU A   71  LEU A   86  1                                  16    
HELIX    5   5 ASP A   97  TYR A  110  1                                  14    
HELIX    6   6 TYR A  126  ASN A  135  1                                  10    
HELIX    7   7 ASN A  135  PHE A  148  1                                  14    
HELIX    8   8 GLN A  149  GLN A  151  5                                   3    
HELIX    9   9 GLU A  152  LYS A  176  1                                  25    
HELIX   10  10 THR A  180  GLY A  194  1                                  15    
HELIX   11  11 SER A  195  TYR A  202  1                                   8    
HELIX   12  12 TYR A  203  LEU A  206  5                                   4    
HELIX   13  13 THR A  210  ARG A  215  1                                   6    
HELIX   14  14 MET A  243  ASP A  248  5                                   6    
HELIX   15  15 GLY A  249  TYR A  253  5                                   5    
HELIX   16  16 ALA A  268  LYS A  273  1                                   6    
HELIX   17  17 LYS A  273  LYS A  287  1                                  15    
HELIX   18  18 PHE B   33  ILE B   36  5                                   4    
HELIX   19  19 TRP B   37  SER B   45  1                                   9    
HELIX   20  20 GLY B   66  TYR B   70  5                                   5    
HELIX   21  21 GLU B   71  LEU B   86  1                                  16    
HELIX   22  22 ASP B   97  TYR B  110  1                                  14    
HELIX   23  23 TYR B  126  ASN B  135  1                                  10    
HELIX   24  24 ASN B  135  PHE B  148  1                                  14    
HELIX   25  25 LYS B  150  LYS B  176  1                                  27    
HELIX   26  26 THR B  180  GLY B  194  1                                  15    
HELIX   27  27 SER B  195  TYR B  202  1                                   8    
HELIX   28  28 TYR B  203  LEU B  206  5                                   4    
HELIX   29  29 THR B  210  ARG B  215  1                                   6    
HELIX   30  30 MET B  243  ASP B  248  5                                   6    
HELIX   31  31 GLY B  249  TYR B  253  5                                   5    
HELIX   32  32 ALA B  268  LYS B  273  1                                   6    
HELIX   33  33 LYS B  273  LYS B  287  1                                  15    
SHEET    1   A 8 SER A   2  VAL A   8  0                                        
SHEET    2   A 8 VAL A  11  LYS A  18 -1  O  SER A  17   N  SER A   2           
SHEET    3   A 8 HIS A  49  LEU A  53 -1  O  ALA A  52   N  ILE A  16           
SHEET    4   A 8 LEU A  23  LEU A  27  1  N  MET A  24   O  VAL A  51           
SHEET    5   A 8 CYS A  91  VAL A  95  1  O  VAL A  94   N  LEU A  25           
SHEET    6   A 8 VAL A 114  ALA A 119  1  O  ILE A 118   N  VAL A  95           
SHEET    7   A 8 VAL A 231  GLY A 236  1  O  GLN A 232   N  ALA A 119           
SHEET    8   A 8 ILE A 257  LEU A 262  1  O  HIS A 260   N  ILE A 233           
SHEET    1   B 8 TYR B   5  VAL B   8  0                                        
SHEET    2   B 8 VAL B  11  GLY B  19 -1  O  LEU B  13   N  ILE B   6           
SHEET    3   B 8 HIS B  49  LEU B  53 -1  O  ALA B  52   N  ILE B  16           
SHEET    4   B 8 LEU B  23  LEU B  27  1  N  PHE B  26   O  VAL B  51           
SHEET    5   B 8 CYS B  91  VAL B  95  1  O  VAL B  94   N  LEU B  27           
SHEET    6   B 8 VAL B 114  ALA B 119  1  O  GLN B 115   N  CYS B  91           
SHEET    7   B 8 VAL B 231  GLY B 236  1  O  GLN B 232   N  LEU B 117           
SHEET    8   B 8 ILE B 257  LEU B 262  1  O  SER B 258   N  VAL B 231           
CISPEP   1 PHE A   30    PRO A   31          0       -10.04                     
CISPEP   2 PHE B   30    PRO B   31          0        -5.02                     
SITE     1 AC1  6 GLU A 272  LYS A 273  PRO A 274  GLN A 275                    
SITE     2 AC1  6 GLU A 276  ASN B 161                                          
SITE     1 AC2 10 ASP A  97  TRP A  98  ALA A 128  LEU A 132                    
SITE     2 AC2 10 GLN A 138  SER A 142  TYR A 144  MET A 145                    
SITE     3 AC2 10 LEU A 206  PHE A 242                                          
SITE     1 AC3  4 LYS B 273  PRO B 274  GLN B 275  GLU B 276                    
SITE     1 AC4  8 ASP B  97  TRP B  98  ALA B 128  SER B 142                    
SITE     2 AC4  8 TYR B 144  LEU B 219  PHE B 242  ASN B 246                    
CRYST1  109.640  109.640  117.496  90.00  90.00  90.00 P 41 21 2    16          
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      0.009121  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009121  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008511        0.00000                         
TER    2381      LYS A 287                                                      
TER    4739      LYS B 287                                                      
MASTER      328    0    4   33   16    0    8    6 4861    2   42   48          
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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