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LongText Report for: 2WKW-pdb

Name Class
2WKW-pdb
HEADER    HYDROLASE                               18-JUN-09   2WKW              
TITLE     ALCALIGENES ESTERASE COMPLEXED WITH PRODUCT ANALOGUE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLESTERASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ESTERASE;                                                   
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ALCALIGENES SP.;                                
SOURCE   3 ORGANISM_TAXID: 512;                                                 
SOURCE   4 EXPRESSION_SYSTEM: AGROBACTERIUM SP.;                                
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 361                                         
KEYWDS    HYDROLASE, HYDROLASE(CARBOXYLIC ESTERASE), ESTERASE, ATOMIC           
KEYWDS   2 RESOLUTION, ALPHA/BETA HYDROLASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD                                 
REVDAT   1   30-JUN-09 2WKW    0                                                
JRNL        AUTH   P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD                        
JRNL        TITL   ALCALIGENES ESTERASE COMPLEXED WITH PRODUCT                  
JRNL        TITL 2 ANALOGUE                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD                        
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION            
REMARK   1  TITL 2 STUDIES OF A NOVEL BACTERIAL ESTERASE                        
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55   915 1999              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   10089333                                                     
REMARK   1  DOI    10.1107/S0907444998018459                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD                        
REMARK   1  TITL   THE ATOMIC-RESOLUTION STRUCTURE OF A NOVEL                   
REMARK   1  TITL 2 BACTERIAL ESTERASE.                                          
REMARK   1  REF    STRUCTURE                     V.   8   143 2000              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  PMID   10673440                                                     
REMARK   1  DOI    10.1016/S0969-2126(00)00090-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
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) : 2.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 54468                          
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) : 0.15700                         
REMARK   3   R VALUE            (WORKING SET) : 0.15498                         
REMARK   3   FREE R VALUE                     : 0.19430                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2910                            
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) : 2.030                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.082                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3942                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.184                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 211                          
REMARK   3   BIN FREE R VALUE                    : 0.233                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4932                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 111                                     
REMARK   3   SOLVENT ATOMS            : 700                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.0                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.412                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.10                                                 
REMARK   3    B22 (A**2) : -2.37                                                
REMARK   3    B33 (A**2) : -1.73                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.137         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.130         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.060         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5188 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7094 ; 1.242 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   666 ; 5.700 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   212 ;35.912 ;23.679       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   812 ;12.613 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;11.668 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   768 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3967 ; 0.006 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3199 ; 2.021 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5185 ; 2.960 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1989 ; 4.470 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1890 ; 5.424 ;10.000       
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 : BABINET MODEL WITH 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   3   THE CRYSTALS WERE SOAKED WITH THE PRODUCT ANALOGUE                 
REMARK   3   IODINATED AT THE PHENOL RING. HOWEVER NO TRACE OF                  
REMARK   3   IODINATION WAS OBSERVED IN THE STRUCTURE                           
REMARK   4                                                                      
REMARK   4 2WKW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-40158.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9076                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57445                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.03                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.3                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.25                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1QLW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (NH4)2SO4, 10 MM TRIS HCL,           
REMARK 280  PH 7.0                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       28.79859            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.57200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.90559            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.57200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.79858            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.90550            
REMARK 290   SMTRY3   4  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 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: 8390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.35 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     ALA A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     ARG A   328                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LYS B   323                                                      
REMARK 465     PRO B   324                                                      
REMARK 465     ALA B   325                                                      
REMARK 465     HIS B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     ARG 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 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    ASP A  48       -8.36     80.60                                   
REMARK 500    THR A  74     -166.72   -128.99                                   
REMARK 500    GLU A  79     -153.61    -89.85                                   
REMARK 500    PRO A 152       40.25   -107.26                                   
REMARK 500    SER A 206     -112.04     61.04                                   
REMARK 500    GLU A 230       58.98     38.63                                   
REMARK 500    MET A 299       51.63    -95.94                                   
REMARK 500    PRO B   9      104.10    -58.55                                   
REMARK 500    ASP B  48       -5.99     79.04                                   
REMARK 500    GLU B  79     -155.88    -86.67                                   
REMARK 500    ALA B 125      149.84   -174.45                                   
REMARK 500    SER B 206     -114.96     60.93                                   
REMARK 500    ASN B 219      117.47   -162.54                                   
REMARK 500    GLU B 230       60.95     37.38                                   
REMARK 500    MET B 299       51.60    -90.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A  102     ASP A  103                  148.85                    
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE W22 A 577                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE W22 B 577                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1325                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1325                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1326                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1326                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1328                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1329                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1328                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1330                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QLW   RELATED DB: PDB                                   
REMARK 900  THE ATOMIC RESOLUTION STRUCTURE OF A NOVEL                          
REMARK 900  BACTERIAL ESTERASE                                                  
DBREF  2WKW A    1   328  UNP    Q7SIA5   Q7SIA5_ALCSP     1    328             
DBREF  2WKW B    1   328  UNP    Q7SIA5   Q7SIA5_ALCSP     1    328             
SEQRES   1 A  328  ALA PRO PRO PRO VAL PRO LYS THR PRO ALA GLY PRO LEU          
SEQRES   2 A  328  THR LEU SER GLY GLN GLY SER PHE PHE VAL GLY GLY ARG          
SEQRES   3 A  328  ASP VAL THR SER GLU THR LEU SER LEU SER PRO LYS TYR          
SEQRES   4 A  328  ASP ALA HIS GLY THR VAL THR VAL ASP GLN MET TYR VAL          
SEQRES   5 A  328  ARG TYR GLN ILE PRO GLN ARG ALA LYS ARG TYR PRO ILE          
SEQRES   6 A  328  THR LEU ILE HIS GLY CYS CYS LEU THR GLY MET THR TRP          
SEQRES   7 A  328  GLU THR THR PRO ASP GLY ARG MET GLY TRP ASP GLU TYR          
SEQRES   8 A  328  PHE LEU ARG LYS GLY TYR SER THR TYR VAL ILE ASP GLN          
SEQRES   9 A  328  SER GLY ARG GLY ARG SER ALA THR ASP ILE SER ALA ILE          
SEQRES  10 A  328  ASN ALA VAL LYS LEU GLY LYS ALA PRO ALA SER SER LEU          
SEQRES  11 A  328  PRO ASP LEU PHE ALA ALA GLY HIS GLU ALA ALA TRP ALA          
SEQRES  12 A  328  ILE PHE ARG PHE GLY PRO ARG TYR PRO ASP ALA PHE LYS          
SEQRES  13 A  328  ASP THR GLN PHE PRO VAL GLN ALA GLN ALA GLU LEU TRP          
SEQRES  14 A  328  GLN GLN MET VAL PRO ASP TRP LEU GLY SER MET PRO THR          
SEQRES  15 A  328  PRO ASN PRO THR VAL ALA ASN LEU SER LYS LEU ALA ILE          
SEQRES  16 A  328  LYS LEU ASP GLY THR VAL LEU LEU SER HIS SER GLN SER          
SEQRES  17 A  328  GLY ILE TYR PRO PHE GLN THR ALA ALA MET ASN PRO LYS          
SEQRES  18 A  328  GLY ILE THR ALA ILE VAL SER VAL GLU PRO GLY GLU CYS          
SEQRES  19 A  328  PRO LYS PRO GLU ASP VAL LYS PRO LEU THR SER ILE PRO          
SEQRES  20 A  328  VAL LEU VAL VAL PHE GLY ASP HIS ILE GLU GLU PHE PRO          
SEQRES  21 A  328  ARG TRP ALA PRO ARG LEU LYS ALA CYS HIS ALA PHE ILE          
SEQRES  22 A  328  ASP ALA LEU ASN ALA ALA GLY GLY LYS GLY GLN LEU MET          
SEQRES  23 A  328  SER LEU PRO ALA LEU GLY VAL HIS GLY ASN SER HIS MET          
SEQRES  24 A  328  MET MET GLN ASP ARG ASN ASN LEU GLN VAL ALA ASP LEU          
SEQRES  25 A  328  ILE LEU ASP TRP ILE GLY ARG ASN THR ALA LYS PRO ALA          
SEQRES  26 A  328  HIS GLY ARG                                                  
SEQRES   1 B  328  ALA PRO PRO PRO VAL PRO LYS THR PRO ALA GLY PRO LEU          
SEQRES   2 B  328  THR LEU SER GLY GLN GLY SER PHE PHE VAL GLY GLY ARG          
SEQRES   3 B  328  ASP VAL THR SER GLU THR LEU SER LEU SER PRO LYS TYR          
SEQRES   4 B  328  ASP ALA HIS GLY THR VAL THR VAL ASP GLN MET TYR VAL          
SEQRES   5 B  328  ARG TYR GLN ILE PRO GLN ARG ALA LYS ARG TYR PRO ILE          
SEQRES   6 B  328  THR LEU ILE HIS GLY CYS CYS LEU THR GLY MET THR TRP          
SEQRES   7 B  328  GLU THR THR PRO ASP GLY ARG MET GLY TRP ASP GLU TYR          
SEQRES   8 B  328  PHE LEU ARG LYS GLY TYR SER THR TYR VAL ILE ASP GLN          
SEQRES   9 B  328  SER GLY ARG GLY ARG SER ALA THR ASP ILE SER ALA ILE          
SEQRES  10 B  328  ASN ALA VAL LYS LEU GLY LYS ALA PRO ALA SER SER LEU          
SEQRES  11 B  328  PRO ASP LEU PHE ALA ALA GLY HIS GLU ALA ALA TRP ALA          
SEQRES  12 B  328  ILE PHE ARG PHE GLY PRO ARG TYR PRO ASP ALA PHE LYS          
SEQRES  13 B  328  ASP THR GLN PHE PRO VAL GLN ALA GLN ALA GLU LEU TRP          
SEQRES  14 B  328  GLN GLN MET VAL PRO ASP TRP LEU GLY SER MET PRO THR          
SEQRES  15 B  328  PRO ASN PRO THR VAL ALA ASN LEU SER LYS LEU ALA ILE          
SEQRES  16 B  328  LYS LEU ASP GLY THR VAL LEU LEU SER HIS SER GLN SER          
SEQRES  17 B  328  GLY ILE TYR PRO PHE GLN THR ALA ALA MET ASN PRO LYS          
SEQRES  18 B  328  GLY ILE THR ALA ILE VAL SER VAL GLU PRO GLY GLU CYS          
SEQRES  19 B  328  PRO LYS PRO GLU ASP VAL LYS PRO LEU THR SER ILE PRO          
SEQRES  20 B  328  VAL LEU VAL VAL PHE GLY ASP HIS ILE GLU GLU PHE PRO          
SEQRES  21 B  328  ARG TRP ALA PRO ARG LEU LYS ALA CYS HIS ALA PHE ILE          
SEQRES  22 B  328  ASP ALA LEU ASN ALA ALA GLY GLY LYS GLY GLN LEU MET          
SEQRES  23 B  328  SER LEU PRO ALA LEU GLY VAL HIS GLY ASN SER HIS MET          
SEQRES  24 B  328  MET MET GLN ASP ARG ASN ASN LEU GLN VAL ALA ASP LEU          
SEQRES  25 B  328  ILE LEU ASP TRP ILE GLY ARG ASN THR ALA LYS PRO ALA          
SEQRES  26 B  328  HIS GLY ARG                                                  
HET    SO4  B1323       5                                                       
HET    SO4  A1323       5                                                       
HET    W22  A 577      17                                                       
HET    W22  B 577      17                                                       
HET    GOL  B1324       6                                                       
HET    GOL  B1325       6                                                       
HET    SO4  A1324       5                                                       
HET    GOL  A1325       6                                                       
HET    SO4  B1326       5                                                       
HET    GOL  A1326       6                                                       
HET    GOL  A1327       6                                                       
HET    GOL  B1327       6                                                       
HET    SO4  A1328       5                                                       
HET    SO4  A1329       5                                                       
HET    SO4  B1328       5                                                       
HET    GOL  A1330       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     W22 [(2S)-4-METHYL-3-OXO-2,3,4,5-TETRAHYDRO-1H-1,                    
HETNAM   2 W22  4-BENZODIAZEPIN-2-YL]ACETIC ACID                                
HETNAM     GOL GLYCEROL                                                         
FORMUL   3  SO4    7(O4 S 2-)                                                   
FORMUL   4  W22    2(C12 H14 N2 O3)                                             
FORMUL   5  GOL    7(C3 H8 O3)                                                  
FORMUL   6  HOH   *700(H2 O1)                                                   
HELIX    1   1 THR A   74  GLU A   79  5                                   6    
HELIX    2   2 GLY A   87  LYS A   95  1                                   9    
HELIX    3   3 ILE A  114  LEU A  122  1                                   9    
HELIX    4   4 PRO A  126  LEU A  130  5                                   5    
HELIX    5   5 GLY A  137  PHE A  145  1                                   9    
HELIX    6   6 PRO A  161  GLN A  163  5                                   3    
HELIX    7   7 ALA A  164  MET A  172  1                                   9    
HELIX    8   8 TRP A  176  MET A  180  5                                   5    
HELIX    9   9 ASN A  184  ASP A  198  1                                  15    
HELIX   10  10 GLN A  207  GLY A  209  5                                   3    
HELIX   11  11 ILE A  210  ASN A  219  1                                  10    
HELIX   12  12 LYS A  236  VAL A  240  5                                   5    
HELIX   13  13 VAL A  240  THR A  244  5                                   5    
HELIX   14  14 TRP A  262  ALA A  279  1                                  18    
HELIX   15  15 PRO A  289  GLY A  292  5                                   4    
HELIX   16  16 MET A  299  ASP A  303  5                                   5    
HELIX   17  17 ASN A  305  ALA A  322  1                                  18    
HELIX   18  18 THR B   74  GLU B   79  5                                   6    
HELIX   19  19 GLY B   87  LYS B   95  1                                   9    
HELIX   20  20 ILE B  114  GLY B  123  1                                  10    
HELIX   21  21 PRO B  126  LEU B  130  5                                   5    
HELIX   22  22 GLY B  137  PHE B  145  1                                   9    
HELIX   23  23 PRO B  161  GLN B  163  5                                   3    
HELIX   24  24 ALA B  164  GLN B  171  1                                   8    
HELIX   25  25 TRP B  176  MET B  180  5                                   5    
HELIX   26  26 ASN B  184  ASP B  198  1                                  15    
HELIX   27  27 GLN B  207  GLY B  209  5                                   3    
HELIX   28  28 ILE B  210  ASN B  219  1                                  10    
HELIX   29  29 LYS B  236  VAL B  240  5                                   5    
HELIX   30  30 VAL B  240  THR B  244  5                                   5    
HELIX   31  31 TRP B  262  ALA B  279  1                                  18    
HELIX   32  32 PRO B  289  GLY B  292  5                                   4    
HELIX   33  33 MET B  299  ASP B  303  5                                   5    
HELIX   34  34 ASN B  305  THR B  321  1                                  17    
SHEET    1  AA16 GLY A 283  SER A 287  0                                        
SHEET    2  AA16 VAL A 248  PHE A 252  1  O  VAL A 248   N  GLN A 284           
SHEET    3  AA16 ILE A 223  VAL A 229  1  O  ILE A 226   N  LEU A 249           
SHEET    4  AA16 THR A 200  HIS A 205  1  O  THR A 200   N  THR A 224           
SHEET    5  AA16 ILE A  65  ILE A  68  1  O  THR A  66   N  LEU A 203           
SHEET    6  AA16 THR A  99  ASP A 103  1  O  TYR A 100   N  LEU A  67           
SHEET    7  AA16 MET A  50  PRO A  57 -1  O  TYR A  51   N  ASP A 103           
SHEET    8  AA16 LEU A  13  VAL A  23 -1  N  SER A  16   O  ILE A  56           
SHEET    9  AA16 LEU B  13  VAL B  23 -1  O  LEU B  13   N  LEU A  15           
SHEET   10  AA16 MET B  50  PRO B  57 -1  O  MET B  50   N  VAL B  23           
SHEET   11  AA16 THR B  99  ASP B 103 -1  O  THR B  99   N  GLN B  55           
SHEET   12  AA16 ILE B  65  ILE B  68  1  O  ILE B  65   N  TYR B 100           
SHEET   13  AA16 THR B 200  HIS B 205  1  O  VAL B 201   N  THR B  66           
SHEET   14  AA16 ILE B 223  VAL B 229  1  N  THR B 224   O  THR B 200           
SHEET   15  AA16 VAL B 248  PHE B 252  1  O  LEU B 249   N  SER B 228           
SHEET   16  AA16 GLY B 283  SER B 287  1  O  GLN B 284   N  VAL B 250           
SHEET    1  AB 2 ARG A  26  SER A  30  0                                        
SHEET    2  AB 2 GLY A  43  VAL A  47 -1  O  GLY A  43   N  SER A  30           
SHEET    1  BA 2 ARG B  26  SER B  30  0                                        
SHEET    2  BA 2 GLY B  43  VAL B  47 -1  O  GLY B  43   N  SER B  30           
SSBOND   1 CYS A   71    CYS A   72                          1555   1555  2.05  
SSBOND   2 CYS A  234    CYS A  269                          1555   1555  2.02  
SSBOND   3 CYS B   71    CYS B   72                          1555   1555  2.06  
SSBOND   4 CYS B  234    CYS B  269                          1555   1555  2.05  
CISPEP   1 TYR A  151    PRO A  152          0        -1.49                     
CISPEP   2 THR A  182    PRO A  183          0        -1.10                     
CISPEP   3 TYR B  151    PRO B  152          0        -3.35                     
CISPEP   4 THR B  182    PRO B  183          0        -0.10                     
SITE     1 AC1  5 SER B  16  GLN B  58  ARG B  59  HOH B2077                    
SITE     2 AC1  5 HOH B2330                                                     
SITE     1 AC2  4 SER A  16  ARG A  59  HOH A2352  HOH A2353                    
SITE     1 AC3 10 CYS A  71  ALA A 136  ILE A 144  PHE A 145                    
SITE     2 AC3 10 SER A 206  GLN A 207  ARG A 261  ARG A 265                    
SITE     3 AC3 10 HIS A 298  HOH A2351                                          
SITE     1 AC4 10 CYS B  71  ALA B 136  ILE B 144  PHE B 145                    
SITE     2 AC4 10 SER B 206  GLN B 207  ARG B 261  ARG B 265                    
SITE     3 AC4 10 HIS B 298  HOH B2328                                          
SITE     1 AC5  6 ASP B 254  HIS B 255  ILE B 256  GLU B 257                    
SITE     2 AC5  6 GLU B 258  HOH B2331                                          
SITE     1 AC6  4 PHE B 155  LYS B 156  ASP B 157  HIS B 255                    
SITE     1 AC7  5 TYR A  54  HOH A2354  HOH A2356  THR B  80                    
SITE     2 AC7  5 GLY B  84                                                     
SITE     1 AC8  8 ASP A 254  HIS A 255  ILE A 256  GLU A 257                    
SITE     2 AC8  8 GLU A 258  HOH A2357  HOH A2358  HOH A2359                    
SITE     1 AC9  4 THR A  80  GLY A  84  TYR B  54  HOH B2333                    
SITE     1 BC1  5 PRO A  82  ASP A  83  GLU A 167  HOH A2360                    
SITE     2 BC1  5 HOH B2333                                                     
SITE     1 BC2  6 THR A  80  GLU A  90  HOH A2123  HOH A2125                    
SITE     2 BC2  6 GLN B  18  GLY B  19                                          
SITE     1 BC3  7 GLN A  18  GLY A  19  HOH A2011  THR B  80                    
SITE     2 BC3  7 GLU B  90  HOH B2126  HOH B2335                               
SITE     1 BC4 10 ILE A 210  PHE A 213  GLN A 214  PRO A 235                    
SITE     2 BC4 10 ASP A 239  HOH A2264  HOH A2284  HOH A2361                    
SITE     3 BC4 10 PRO B 126  SER B 128                                          
SITE     1 BC5  7 ARG A 319  HOH A2362  HOH A2363  GLN B 284                    
SITE     2 BC5  7 LEU B 285  HOH B2286  HOH B2288                               
SITE     1 BC6  8 ILE A 273  GLN A 284  LEU A 285  HOH A2312                    
SITE     2 BC6  8 HOH A2316  ARG B 319  HOH B2336  HOH B2337                    
SITE     1 BC7  5 GLY A 123  ALA A 125  PRO A 126  GLN A 163                    
SITE     2 BC7  5 GLN A 165                                                     
CRYST1   57.597  115.811  131.144  90.00  90.00  90.00 P 21 21 21    8          
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      0.017362  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007625        0.00000                         
MTRIX1   1 -0.972180 -0.010390 -0.234000        8.01847    1                    
MTRIX2   1  0.003150 -0.999500  0.031310       73.07857    1                    
MTRIX3   1 -0.234210  0.029700  0.971730       -0.18449    1                    
TER    2465      ALA A 322                                                      
TER    4934      ALA B 322                                                      
MASTER      411    0   16   34   20    0   32    9 5743    2  119   52          
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.
For technical information about these pages see:
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