Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4OB6-pdb

Name Class
4OB6-pdb
HEADER    HYDROLASE                               07-JAN-14   4OB6              
TITLE     COMPLEX STRUCTURE OF ESTERASE RPPE S159A/W187H AND SUBSTRATE (S)-AC-  
TITLE    2 CPA                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE FOLD-3 DOMAIN PROTEIN;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS;                                    
SOURCE   3 ORGANISM_TAXID: 657346;                                              
SOURCE   4 STRAIN: ECU1011;                                                     
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: PET21A                                    
KEYWDS    A/B HYDROLASE FOLD, ESTERASE, HSL-LIKE FAMILY, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DOU,X.D.KONG,B.D.MA,Q.CHEN,J.H.ZHOU,J.H.XU                          
REVDAT   1   23-JUL-14 4OB6    0                                                
JRNL        AUTH   S.DOU,X.D.KONG,B.D.MA,Q.CHEN,J.ZHANG,J.H.ZHOU,J.H.XU         
JRNL        TITL   CRYSTAL STRUCTURES OF PSEUDOMONAS PUTIDA ESTERASE REVEAL THE 
JRNL        TITL 2 FUNCTIONAL ROLE OF RESIDUES 187 AND 287 IN SUBSTRATE BINDING 
JRNL        TITL 3 AND CHIRAL RECOGNITION                                       
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 446  1145 2014              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   24680822                                                     
JRNL        DOI    10.1016/J.BBRC.2014.03.072                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 45369                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2280                            
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 33.7491 -  4.2816    1.00     2934   136  0.1632 0.1611        
REMARK   3     2  4.2816 -  3.3995    1.00     2764   139  0.1570 0.1517        
REMARK   3     3  3.3995 -  2.9700    1.00     2720   159  0.1739 0.1888        
REMARK   3     4  2.9700 -  2.6986    1.00     2709   144  0.1748 0.2008        
REMARK   3     5  2.6986 -  2.5053    1.00     2709   127  0.1726 0.2025        
REMARK   3     6  2.5053 -  2.3576    1.00     2685   149  0.1700 0.1985        
REMARK   3     7  2.3576 -  2.2395    1.00     2675   140  0.1633 0.1848        
REMARK   3     8  2.2395 -  2.1421    1.00     2688   139  0.1578 0.1777        
REMARK   3     9  2.1421 -  2.0596    1.00     2644   153  0.1581 0.1758        
REMARK   3    10  2.0596 -  1.9886    1.00     2656   139  0.1553 0.1748        
REMARK   3    11  1.9886 -  1.9264    1.00     2680   143  0.1558 0.1830        
REMARK   3    12  1.9264 -  1.8713    1.00     2638   140  0.1508 0.1911        
REMARK   3    13  1.8713 -  1.8221    1.00     2673   137  0.1500 0.2001        
REMARK   3    14  1.8221 -  1.7776    1.00     2624   147  0.1493 0.1964        
REMARK   3    15  1.7776 -  1.7372    1.00     2639   145  0.1728 0.2127        
REMARK   3    16  1.7372 -  1.7002    1.00     2651   143  0.2017 0.2619        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.007           2538                                  
REMARK   3   ANGLE     :  1.191           3451                                  
REMARK   3   CHIRALITY :  0.085            382                                  
REMARK   3   PLANARITY :  0.005            451                                  
REMARK   3   DIHEDRAL  : 13.107            912                                  
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 4OB6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084271.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-13                          
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) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : VARIMAX-HF                         
REMARK 200  OPTICS                         : NULL                               
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                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45435                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.742                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 16.700                             
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 16.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.41200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2YH2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) PEG 8000, 0.04M KH2PO4, 20%    
REMARK 280  GLYCEROL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
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       44.14850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.71900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.71900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       66.22275            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.71900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.71900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       22.07425            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.71900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.71900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       66.22275            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.71900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.71900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       22.07425            
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       44.14850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000      190.87600            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      190.87600            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       44.14850            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 545  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 637  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 686  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 549  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 561  LIES ON A SPECIAL POSITION.                          
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     MET A   -14                                                      
REMARK 465     ALA A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     MET A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLN A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     MET A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     LEU A   319                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A     0     OE1  GLU A    17              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A  89      -32.16     68.44                                   
REMARK 500    ASP A  93     -168.88   -177.75                                   
REMARK 500    ALA A 159     -118.27     65.42                                   
REMARK 500    THR A 177      149.52   -171.43                                   
REMARK 500    PHE A 182      146.02   -174.21                                   
REMARK 500    PHE A 207      -75.73     75.49                                   
REMARK 500    PHE A 255       52.11   -105.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 607        DISTANCE =  5.02 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S2T A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S2T A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S2T A 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OB7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OB8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OU4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OU5   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHOR STATED THE SEQUENCE DATABASE WAS WRONG AT THIS POSITION.      
DBREF  4OB6 A    1   316  UNP    L7PYQ2   L7PYQ2_9PSED     1    316             
SEQADV 4OB6 MET A  -14  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 ALA A  -13  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 SER A  -12  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 MET A  -11  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 THR A  -10  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLY A   -9  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLY A   -8  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLN A   -7  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLN A   -6  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 MET A   -5  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLY A   -4  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 ARG A   -3  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLY A   -2  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 SER A   -1  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 SER A    0  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLN A   10  UNP  L7PYQ2    LYS    10 SEE REMARK 999                 
SEQADV 4OB6 ALA A  159  UNP  L7PYQ2    SER   159 ENGINEERED MUTATION            
SEQADV 4OB6 HIS A  187  UNP  L7PYQ2    TRP   187 ENGINEERED MUTATION            
SEQADV 4OB6 LEU A  317  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLU A  318  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 LEU A  319  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 GLU A  320  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 HIS A  321  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 HIS A  322  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 HIS A  323  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 HIS A  324  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 HIS A  325  UNP  L7PYQ2              EXPRESSION TAG                 
SEQADV 4OB6 HIS A  326  UNP  L7PYQ2              EXPRESSION TAG                 
SEQRES   1 A  341  MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY          
SEQRES   2 A  341  SER SER GLY SER PRO GLY VAL GLU GLN HIS THR GLN ALA          
SEQRES   3 A  341  PHE LEU GLU ALA LEU GLU GLN GLY GLY GLY LYS PRO LEU          
SEQRES   4 A  341  GLU GLN LEU SER PRO LYS ASP ALA ARG ALA VAL LEU THR          
SEQRES   5 A  341  GLY ALA GLN ALA SER VAL LYS VAL ASP LEU SER GLY ILE          
SEQRES   6 A  341  GLU VAL LYS GLU ARG THR ILE GLN ALA ASN GLY GLN SER          
SEQRES   7 A  341  ILE LYS LEU GLN VAL VAL ARG PRO ALA ASN VAL LYS GLY          
SEQRES   8 A  341  GLU LEU PRO VAL PHE MET PHE PHE HIS GLY GLY GLY TRP          
SEQRES   9 A  341  VAL LEU GLY ASP PHE PRO THR HIS GLN ARG LEU ILE ARG          
SEQRES  10 A  341  ASP LEU VAL VAL GLY SER GLY ALA VAL ALA VAL TYR VAL          
SEQRES  11 A  341  ASP TYR THR PRO SER PRO GLU SER HIS TYR PRO THR ALA          
SEQRES  12 A  341  ILE ASN GLN ALA TYR ALA ALA THR GLN TRP VAL ALA GLU          
SEQRES  13 A  341  HIS GLY LYS GLU ILE GLY VAL ASP GLY LYS ARG LEU ALA          
SEQRES  14 A  341  VAL ALA GLY ASN ALA VAL GLY GLY ASN MET ALA ALA VAL          
SEQRES  15 A  341  VAL ALA LEU LYS ALA LYS GLU ALA GLY THR PRO ALA LEU          
SEQRES  16 A  341  ARG PHE GLN LEU LEU LEU HIS PRO VAL THR ASP ALA SER          
SEQRES  17 A  341  PHE GLU THR ALA SER TYR LYS GLN PHE ALA ASP GLY HIS          
SEQRES  18 A  341  PHE LEU THR THR GLY MET MET LYS TRP PHE TRP ASP ASN          
SEQRES  19 A  341  TYR THR THR ASP ALA LYS ALA ARG GLU GLN ILE TYR ALA          
SEQRES  20 A  341  SER PRO LEU ARG ALA SER SER GLU GLN LEU LYS GLY LEU          
SEQRES  21 A  341  PRO PRO ALA LEU VAL GLN THR ALA GLU PHE ASP VAL LEU          
SEQRES  22 A  341  ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ASN ALA          
SEQRES  23 A  341  ALA GLY VAL THR VAL THR SER VAL ARG TYR ASN GLY MET          
SEQRES  24 A  341  ILE HIS ASP TYR GLY LEU LEU ASN PRO LEU SER GLN VAL          
SEQRES  25 A  341  PRO ALA VAL LYS ALA ALA MET ARG GLN ALA GLY THR GLU          
SEQRES  26 A  341  LEU LYS VAL HIS LEU GLN LEU GLU LEU GLU HIS HIS HIS          
SEQRES  27 A  341  HIS HIS HIS                                                  
HET    S2T  A 401      15                                                       
HET    S2T  A 402      15                                                       
HET    S2T  A 403      15                                                       
HETNAM     S2T (2S)-(ACETYLOXY)(2-CHLOROPHENYL)ETHANOIC ACID                    
FORMUL   2  S2T    3(C10 H9 CL O4)                                              
FORMUL   5  HOH   *223(H2 O)                                                    
HELIX    1   1 GLU A    6  GLN A   18  1                                  13    
HELIX    2   2 PRO A   23  LEU A   27  5                                   5    
HELIX    3   3 SER A   28  ALA A   41  1                                  14    
HELIX    4   4 ASP A   93  GLY A  109  1                                  17    
HELIX    5   5 PRO A  126  GLY A  143  1                                  18    
HELIX    6   6 LYS A  144  ILE A  146  5                                   3    
HELIX    7   7 ALA A  159  GLY A  176  1                                  18    
HELIX    8   8 THR A  196  PHE A  202  1                                   7    
HELIX    9   9 THR A  209  THR A  221  1                                  13    
HELIX   10  10 ASP A  223  GLN A  229  1                                   7    
HELIX   11  11 SER A  233  ALA A  237  5                                   5    
HELIX   12  12 SER A  238  LYS A  243  1                                   6    
HELIX   13  13 LEU A  258  ALA A  272  1                                  15    
HELIX   14  14 LEU A  291  SER A  295  5                                   5    
HELIX   15  15 VAL A  297  LEU A  315  1                                  19    
SHEET    1   A 8 ILE A  50  ALA A  59  0                                        
SHEET    2   A 8 GLN A  62  PRO A  71 -1  O  VAL A  68   N  LYS A  53           
SHEET    3   A 8 VAL A 111  VAL A 115 -1  O  ALA A 112   N  VAL A  69           
SHEET    4   A 8 LEU A  78  PHE A  84  1  N  PHE A  81   O  VAL A 111           
SHEET    5   A 8 VAL A 148  ASN A 158  1  O  ALA A 154   N  MET A  82           
SHEET    6   A 8 PHE A 182  LEU A 186  1  O  LEU A 184   N  VAL A 155           
SHEET    7   A 8 ALA A 248  PHE A 255  1  O  LEU A 249   N  LEU A 185           
SHEET    8   A 8 VAL A 276  ILE A 285  1  O  TYR A 281   N  THR A 252           
CISPEP   1 SER A  120    PRO A  121          0         5.26                     
CISPEP   2 TYR A  125    PRO A  126          0         3.85                     
CISPEP   3 THR A  177    PRO A  178          0        -4.55                     
SITE     1 AC1 13 LEU A  36  GLY A  86  GLY A  87  GLY A  88                    
SITE     2 AC1 13 ASN A 158  ALA A 159  VAL A 160  PHE A 207                    
SITE     3 AC1 13 LEU A 208  MET A 213  HIS A 286  ASP A 287                    
SITE     4 AC1 13 LEU A 290                                                     
SITE     1 AC2  5 PHE A  12  VAL A  35  ALA A  39  PHE A 207                    
SITE     2 AC2  5 LEU A 291                                                     
SITE     1 AC3  6 GLN A 296  PRO A 298  LYS A 301  ARG A 305                    
SITE     2 AC3  6 VAL A 313  HIS A 314                                          
CRYST1   95.438   95.438   88.297  90.00  90.00  90.00 P 43 21 2     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      0.010478  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010478  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011325        0.00000                         
TER    2438      GLU A 318                                                      
MASTER      332    0    3   15    8    0    8    6 2690    1   45   27          
END                                                                             

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

Acknowledgements and disclaimer