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LongText Report for: 5AOB-pdb

Name Class
5AOB-pdb
HEADER    HYDROLASE                               10-SEP-15   5AOB              
TITLE     THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM THE               
TITLE    2 PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-               
TITLE    3 BUTYRATE BOUND                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOGUTTA TERRIFONTIS;                        
SOURCE   3 ORGANISM_TAXID: 1331910;                                             
SOURCE   4 STRAIN: R1;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PLATE31                                    
KEYWDS    HYDROLASE, CARBOXYL ESTERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SAYER,Z.SZABO,M.N.ISUPOV,C.INGHAM,J.A.LITTLECHILD                   
REVDAT   1   09-DEC-15 5AOB    0                                                
JRNL        AUTH   C.SAYER,Z.SZABO,M.N.ISUPOV,C.INGHAM,J.A.LITTLECHILD          
JRNL        TITL   THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM THE      
JRNL        TITL 2 PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS REVEALS AN   
JRNL        TITL 3 OPEN ACTIVE SITE DUE TO A MINIMAL 'CAP' DOMAIN               
JRNL        REF    FRONT.MICROBIOL.                           2015              
JRNL        REFN                   ESSN 1664-302X                               
JRNL        DOI    10.3389/FMICB.2015.01294                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.25                          
REMARK   3   NUMBER OF REFLECTIONS             : 29842                          
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) : 0.17779                         
REMARK   3   R VALUE            (WORKING SET) : 0.17550                         
REMARK   3   FREE R VALUE                     : 0.22086                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1581                            
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) : 1.790                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.836                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2159                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.337                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.355                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2297                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.984                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.10                                                 
REMARK   3    B22 (A**2) : -1.75                                                
REMARK   3    B33 (A**2) : 0.65                                                 
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): 0.116         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.401         
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):  2429 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2357 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3290 ; 1.459 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5448 ; 0.980 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   319 ; 5.875 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   121 ;31.478 ;23.058       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   404 ;15.606 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;17.852 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   337 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2768 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   578 ; 0.002 ; 0.020       
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):  1153 ; 4.910 ; 7.369       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1152 ; 4.912 ; 7.356       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1450 ; 6.660 ;12.342       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1276 ; 5.917 ; 9.048       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 5AOB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-64897.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91731                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.79                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.60                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.3                                
REMARK 200  R MERGE                    (I) : 0.01                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.60                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 1.22                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1EVQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       30.84200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.65250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.28900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.65250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.84200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.28900            
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 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLU A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     GLN A   285                                                      
REMARK 465     PRO A   286                                                      
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   OE2B GLU A   186     O    HOH A  2085              1.89            
REMARK 500   OE2B GLU A   186     O    HOH A  2123              1.93            
REMARK 500   NE A ARG A   255     O    HOH A  2169              2.18            
REMARK 500   CZ A ARG A   255     O    HOH A  2169              1.16            
REMARK 500   NH1A ARG A   255     O    HOH A  2169              2.10            
REMARK 500   NH2A ARG A   255     O    HOH A  2169              0.34            
REMARK 500   O    HOH A  2085     O    HOH A  2123              1.82            
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    SER A 126     -117.40     57.24                                   
REMARK 500    ASP A 147       50.10     70.25                                   
REMARK 500    ASN A 161       63.94     20.95                                   
REMARK 500    LYS A 172       44.86    -97.93                                   
REMARK 500    ARG A 177       64.77   -113.43                                   
REMARK 500    ASN A 258       19.28     57.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 161        24.4      L          L   OUTSIDE RANGE           
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 PG4 A1283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BUA A1285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1292                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AO9   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM                 
REMARK 900  THE PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-          
REMARK 900  NATIVE                                                              
REMARK 900 RELATED ID: 5AOA   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM                 
REMARK 900  THE PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-          
REMARK 900  PROPIONATE BOUND                                                    
REMARK 900 RELATED ID: 5AOC   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM                 
REMARK 900  THE PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-          
REMARK 900  VALERATE BOUND                                                      
DBREF  5AOB A    1   286  PDB    5AOB     5AOB             1    286             
SEQRES   1 A  286  ALA GLU VAL GLY ARG LEU ARG TYR PRO PRO GLU MET PRO          
SEQRES   2 A  286  GLY ALA GLU VAL LYS VAL TYR LYS LYS VAL ASP ASN VAL          
SEQRES   3 A  286  ASP LEU LYS LEU TYR ILE TYR LYS PRO ALA ASP TRP LYS          
SEQRES   4 A  286  PRO ALA ASP ARG ARG SER ALA ILE VAL PHE PHE PHE GLY          
SEQRES   5 A  286  GLY GLY TRP GLN SER GLY SER PRO ALA GLN PHE ARG PRO          
SEQRES   6 A  286  GLN CYS GLU TYR PHE ALA GLY ARG GLY MET VAL ALA MET          
SEQRES   7 A  286  ALA ALA ASP TYR ARG VAL GLY SER ARG HIS ASN VAL LYS          
SEQRES   8 A  286  VAL ALA ASP CYS VAL ALA ASP ALA LYS SER ALA ILE ARG          
SEQRES   9 A  286  TRP VAL ARG GLN HIS ALA ALA GLU LEU GLY VAL ASP PRO          
SEQRES  10 A  286  GLN LYS ILE VAL ALA SER GLY GLY SER ALA GLY GLY HIS          
SEQRES  11 A  286  LEU ALA ALA CYS THR VAL MET VAL PRO ASP LEU GLU ALA          
SEQRES  12 A  286  PRO GLU GLU ASP HIS THR ILE SER SER GLN ALA ASN ALA          
SEQRES  13 A  286  ALA ILE LEU PHE ASN PRO VAL LEU ILE LEU SER ARG GLU          
SEQRES  14 A  286  GLY LEU LYS ASP HIS VAL PRO ARG GLN ASP TRP GLU GLU          
SEQRES  15 A  286  ARG LEU ARG GLU ARG LEU GLY THR GLU PRO LYS ALA VAL          
SEQRES  16 A  286  SER PRO TYR HIS HIS ILE ARG ALA GLY LEU PRO PRO MET          
SEQRES  17 A  286  ILE ILE PHE HIS GLY THR ALA ASP ASN THR VAL PRO PHE          
SEQRES  18 A  286  GLU THR ILE ARG LEU PHE ALA GLU ALA MET LYS LYS ALA          
SEQRES  19 A  286  GLY ASN ARG CYS GLU LEU VAL PRO PHE GLU GLY ALA ALA          
SEQRES  20 A  286  HIS GLY PHE PHE ASN PHE GLY ARG GLY ASP ASN LEU ALA          
SEQRES  21 A  286  TYR GLN LYS THR LEU GLU LEU ALA ASP GLU PHE LEU VAL          
SEQRES  22 A  286  GLU ILE GLY PHE LEU ALA PRO LYS GLY GLU SER GLN PRO          
HET    PG4  A1283      13                                                       
HET    PG4  A1284      13                                                       
HET    BUA  A1285       6                                                       
HET    EDO  A1286       4                                                       
HET    EDO  A1287       4                                                       
HET    EDO  A1288       4                                                       
HET    EDO  A1289       4                                                       
HET     CL  A1290       1                                                       
HET    PEG  A1291       7                                                       
HET    PEG  A1292       7                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     BUA BUTANOIC ACID                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  PG4    2(C8 H18 O5)                                                 
FORMUL   3  EDO    4(C2 H6 O2)                                                  
FORMUL   4  BUA    C4 H8 O2                                                     
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  PEG    2(C4 H10 O3)                                                 
FORMUL   7  HOH   *193(H2 O)                                                    
HELIX    1   1 SER A   59  GLN A   62  5                                   4    
HELIX    2   2 PHE A   63  ARG A   73  1                                  11    
HELIX    3   3 VAL A   84  ASN A   89  1                                   6    
HELIX    4   4 LYS A   91  HIS A  109  1                                  19    
HELIX    5   5 HIS A  109  GLY A  114  1                                   6    
HELIX    6   6 SER A  126  VAL A  138  1                                  13    
HELIX    7   7 ARG A  177  GLY A  189  1                                  13    
HELIX    8   8 GLU A  191  SER A  196  5                                   6    
HELIX    9   9 SER A  196  ILE A  201  5                                   6    
HELIX   10  10 PRO A  220  ALA A  234  1                                  15    
HELIX   11  11 ARG A  255  ASP A  257  5                                   3    
HELIX   12  12 ASN A  258  ILE A  275  1                                  18    
SHEET    1  AA 8 GLU A  16  VAL A  23  0                                        
SHEET    2  AA 8 VAL A  26  TYR A  33 -1  O  VAL A  26   N  VAL A  23           
SHEET    3  AA 8 VAL A  76  ALA A  80 -1  O  ALA A  77   N  TYR A  33           
SHEET    4  AA 8 ARG A  44  PHE A  50  1  O  SER A  45   N  VAL A  76           
SHEET    5  AA 8 VAL A 115  GLY A 125  1  N  ASP A 116   O  ARG A  44           
SHEET    6  AA 8 ALA A 156  PHE A 160  1  O  ALA A 156   N  ALA A 122           
SHEET    7  AA 8 MET A 208  GLY A 213  1  O  ILE A 209   N  LEU A 159           
SHEET    8  AA 8 CYS A 238  PHE A 243  1  O  GLU A 239   N  ILE A 210           
CISPEP   1 TYR A    8    PRO A    9          0        -4.41                     
SITE     1 AC1  7 MET A 137  VAL A 138  PRO A 139  ASP A 140                    
SITE     2 AC1  7 GLN A 153  HOH A2111  HOH A2190                               
SITE     1 AC2  8 GLN A 118  THR A 149  GLN A 153  ASN A 155                    
SITE     2 AC2  8 HIS A 174  VAL A 175  HOH A2102  HOH A2112                    
SITE     1 AC3  7 GLY A  53  GLY A  54  SER A 126  ALA A 127                    
SITE     2 AC3  7 HIS A 248  HOH A2065  HOH A2191                               
SITE     1 AC4  1 ARG A 168                                                     
SITE     1 AC5  1 PRO A  35                                                     
SITE     1 AC6  4 GLN A  56  VAL A  90  PEG A1292  HOH A2080                    
SITE     1 AC7  2 ARG A  87  HOH A2082                                          
SITE     1 AC8  5 ASN A 217  ALA A 247  HIS A 248  HOH A2147                    
SITE     2 AC8  5 HOH A2148                                                     
SITE     1 AC9  3 ARG A  43  HOH A2049  HOH A2104                               
SITE     1 BC1  5 GLN A  56  ARG A 187  EDO A1288  HOH A2059                    
SITE     2 BC1  5 HOH A2088                                                     
CRYST1   61.684   70.578   75.305  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016212  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014169  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013279        0.00000                         
TER    2298      GLY A 282                                                      
MASTER      357    0   10   12    8    0   15    6 2553    1   62   22          
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:
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