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LongText Report for: 3FCY-pdb

Name Class
3FCY-pdb
HEADER    HYDROLASE                               24-NOV-08   3FCY              
TITLE     CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE 1 FROM                     
TITLE    2 THERMOANAEROBACTERIUM SP. JW/SL YS485                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: XYLAN ESTERASE 1;                                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 3.1.1.72, 3.1.1.41;                                              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOANAEROBACTERIUM SP. 'JW/SL                
SOURCE   3 YS485';                                                              
SOURCE   4 ORGANISM_TAXID: 60708;                                               
SOURCE   5 STRAIN: JW/SL YS485;                                                 
SOURCE   6 GENE: AXE1;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET                              
KEYWDS    ALPHA/BETA HYDROLASE, CARBOHYDRATE ESTERASE, CE7,                     
KEYWDS   2 THERMOANAEROBACTERIUM SP.                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.KRASTANOVA,A.CASSETTA,D.LAMBA                                       
REVDAT   1   17-NOV-09 3FCY    0                                                
JRNL        AUTH   I.KRASTANOVA,A.CASSETTA,J.WIEGEL,D.LAMBA                     
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF ACETYL XYLAN ESTERASE          
JRNL        TITL 2 1 FROM THERMOANAEROBACTERIUM SP. JW/SL YS485                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.SHAO,J.WIEGEL                                              
REMARK   1  TITL   PURIFICATION AND CHARACTERIZATION OF TWO                     
REMARK   1  TITL 2 THERMOSTABLE ACETYL XYLAN ESTERASES FROM                     
REMARK   1  TITL 3 THERMOANAEROBACTERIUM SP. STRAIN JW/SL-YS485                 
REMARK   1  REF    APPL.ENVIRON.MICROBIOL.       V.  61   729 1995              
REMARK   1  REFN                   ISSN 0099-2240                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.W.LORENZ,J.WIEGEL                                          
REMARK   1  TITL   ISOLATION, ANALYSIS, AND EXPRESSION OF TWO GENES             
REMARK   1  TITL 2 FROM THERMOANAEROBACTERIUM SP. STRAIN JW/SL YS485:           
REMARK   1  TITL 3 A BETA-XYLOSIDASE AND A NOVEL ACETYL XYLAN ESTERASE          
REMARK   1  TITL 4 WITH CEPHALOSPORIN C DEACETYLASE ACTIVITY                    
REMARK   1  REF    J.BACTERIOL.                  V. 179  5436 1997              
REMARK   1  REFN                   ISSN 0021-9193                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 66710                          
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 SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6761                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7572                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 489                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.56                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.70500                                              
REMARK   3    B22 (A**2) : 2.70500                                              
REMARK   3    B33 (A**2) : -5.41000                                             
REMARK   3    B12 (A**2) : 0.70200                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.25                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.124 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.584 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.983 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.894 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 53.97                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3FCY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050435.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66742                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.100                             
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.32900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.300                              
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 3FVR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 400, 0.1M CALCIUM CHLORIDE,      
REMARK 280  0.05M SODIUM HEPES, PH 7.5, MICROBATCH, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.27600            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.63800            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.63800            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       75.27600            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       37.63800            
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 CA    CA A 321  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   -25                                                      
REMARK 465     LYS A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     PRO A   -17                                                      
REMARK 465     MET A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     ASP A   -14                                                      
REMARK 465     TYR A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     ILE A   -11                                                      
REMARK 465     PRO A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     MET B   -25                                                      
REMARK 465     LYS B   -24                                                      
REMARK 465     HIS B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     PRO B   -17                                                      
REMARK 465     MET B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     ASP B   -14                                                      
REMARK 465     TYR B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     ILE B   -11                                                      
REMARK 465     PRO B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     MET C   -25                                                      
REMARK 465     LYS C   -24                                                      
REMARK 465     HIS C   -23                                                      
REMARK 465     HIS C   -22                                                      
REMARK 465     HIS C   -21                                                      
REMARK 465     HIS C   -20                                                      
REMARK 465     HIS C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     PRO C   -17                                                      
REMARK 465     MET C   -16                                                      
REMARK 465     SER C   -15                                                      
REMARK 465     ASP C   -14                                                      
REMARK 465     TYR C   -13                                                      
REMARK 465     ASP C   -12                                                      
REMARK 465     ILE C   -11                                                      
REMARK 465     PRO C   -10                                                      
REMARK 465     THR C    -9                                                      
REMARK 465     THR C    -8                                                      
REMARK 465     GLU C    -7                                                      
REMARK 465     ASN C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     TYR C    -4                                                      
REMARK 465     PHE C    -3                                                      
REMARK 465     GLN C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  92       -3.11     81.54                                   
REMARK 500    SER A  93     -153.26    -92.31                                   
REMARK 500    GLN A 119     -132.34   -102.04                                   
REMARK 500    SER A 182     -118.09     53.81                                   
REMARK 500    TYR A 205       65.61     30.70                                   
REMARK 500    LEU A 208       36.62     74.79                                   
REMARK 500    ASN A 222     -121.95     57.89                                   
REMARK 500    ASP A 235       62.60   -160.88                                   
REMARK 500    SER B  92       -7.07     80.39                                   
REMARK 500    SER B  93     -155.50    -88.14                                   
REMARK 500    GLN B 119     -125.88   -104.44                                   
REMARK 500    SER B 182     -114.03     55.69                                   
REMARK 500    TYR B 205       64.83     31.66                                   
REMARK 500    LEU B 208       33.31     70.01                                   
REMARK 500    ASN B 222     -122.43     59.63                                   
REMARK 500    ASP B 235       59.49   -161.60                                   
REMARK 500    SER C  92       -0.69     79.28                                   
REMARK 500    SER C  93     -156.18    -94.30                                   
REMARK 500    GLN C 119     -129.89    -99.85                                   
REMARK 500    SER C 182     -118.32     54.26                                   
REMARK 500    TYR C 205       67.52     26.77                                   
REMARK 500    LEU C 208       35.91     73.03                                   
REMARK 500    ASN C 222     -122.85     57.66                                   
REMARK 500    ASP C 235       62.94   -161.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 321  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 317   O                                                      
REMARK 620 2 TYR A 319   O    81.6                                              
REMARK 620 3 HOH A 395   O   109.8  88.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 321  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 317   O                                                      
REMARK 620 2 TYR C 319   O    86.9                                              
REMARK 620 3 HOH C 417   O    80.7  74.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 321                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 321                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ODS   RELATED DB: PDB                                   
REMARK 900 CEPHALOSPORIN C DEACETYLASE FROM BACILLUS SUBTILIS                   
REMARK 900 RELATED ID: 1ODT   RELATED DB: PDB                                   
REMARK 900 CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH ACETATE         
REMARK 900 RELATED ID: 1L7A   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF CEPHALOSPORIN C            
REMARK 900 DEACETYLASE                                                          
REMARK 900 RELATED ID: 1VLQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM             
REMARK 900 THERMOTOGA MARITIMA AT 2.10 A RESOLUTION                             
DBREF  3FCY A    1   320  UNP    O30361   O30361_THESJ     1    320             
DBREF  3FCY B    1   320  UNP    O30361   O30361_THESJ     1    320             
DBREF  3FCY C    1   320  UNP    O30361   O30361_THESJ     1    320             
SEQADV 3FCY MET A  -25  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY LYS A  -24  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS A  -23  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS A  -22  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS A  -21  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS A  -20  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS A  -19  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS A  -18  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PRO A  -17  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY MET A  -16  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY SER A  -15  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASP A  -14  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY TYR A  -13  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASP A  -12  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ILE A  -11  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PRO A  -10  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY THR A   -9  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY THR A   -8  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLU A   -7  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASN A   -6  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY LEU A   -5  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY TYR A   -4  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PHE A   -3  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLN A   -2  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLY A   -1  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ALA A    0  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY MET B  -25  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY LYS B  -24  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS B  -23  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS B  -22  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS B  -21  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS B  -20  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS B  -19  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS B  -18  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PRO B  -17  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY MET B  -16  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY SER B  -15  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASP B  -14  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY TYR B  -13  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASP B  -12  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ILE B  -11  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PRO B  -10  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY THR B   -9  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY THR B   -8  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLU B   -7  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASN B   -6  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY LEU B   -5  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY TYR B   -4  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PHE B   -3  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLN B   -2  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLY B   -1  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ALA B    0  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY MET C  -25  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY LYS C  -24  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS C  -23  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS C  -22  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS C  -21  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS C  -20  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS C  -19  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY HIS C  -18  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PRO C  -17  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY MET C  -16  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY SER C  -15  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASP C  -14  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY TYR C  -13  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASP C  -12  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ILE C  -11  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PRO C  -10  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY THR C   -9  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY THR C   -8  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLU C   -7  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ASN C   -6  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY LEU C   -5  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY TYR C   -4  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY PHE C   -3  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLN C   -2  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY GLY C   -1  UNP  O30361              EXPRESSION TAG                 
SEQADV 3FCY ALA C    0  UNP  O30361              EXPRESSION TAG                 
SEQRES   1 A  346  MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR          
SEQRES   2 A  346  ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA          
SEQRES   3 A  346  MET GLY LEU PHE ASP MET PRO LEU GLN LYS LEU ARG GLU          
SEQRES   4 A  346  TYR THR GLY THR ASN PRO CYS PRO GLU ASP PHE ASP GLU          
SEQRES   5 A  346  TYR TRP ASN ARG ALA LEU ASP GLU MET ARG SER VAL ASP          
SEQRES   6 A  346  PRO LYS ILE GLU LEU LYS GLU SER SER PHE GLN VAL SER          
SEQRES   7 A  346  PHE ALA GLU CYS TYR ASP LEU TYR PHE THR GLY VAL ARG          
SEQRES   8 A  346  GLY ALA ARG ILE HIS ALA LYS TYR ILE LYS PRO LYS THR          
SEQRES   9 A  346  GLU GLY LYS HIS PRO ALA LEU ILE ARG PHE HIS GLY TYR          
SEQRES  10 A  346  SER SER ASN SER GLY ASP TRP ASN ASP LYS LEU ASN TYR          
SEQRES  11 A  346  VAL ALA ALA GLY PHE THR VAL VAL ALA MET ASP VAL ARG          
SEQRES  12 A  346  GLY GLN GLY GLY GLN SER GLN ASP VAL GLY GLY VAL THR          
SEQRES  13 A  346  GLY ASN THR LEU ASN GLY HIS ILE ILE ARG GLY LEU ASP          
SEQRES  14 A  346  ASP ASP ALA ASP ASN MET LEU PHE ARG HIS ILE PHE LEU          
SEQRES  15 A  346  ASP THR ALA GLN LEU ALA GLY ILE VAL MET ASN MET PRO          
SEQRES  16 A  346  GLU VAL ASP GLU ASP ARG VAL GLY VAL MET GLY PRO SER          
SEQRES  17 A  346  GLN GLY GLY GLY LEU SER LEU ALA CYS ALA ALA LEU GLU          
SEQRES  18 A  346  PRO ARG VAL ARG LYS VAL VAL SER GLU TYR PRO PHE LEU          
SEQRES  19 A  346  SER ASP TYR LYS ARG VAL TRP ASP LEU ASP LEU ALA LYS          
SEQRES  20 A  346  ASN ALA TYR GLN GLU ILE THR ASP TYR PHE ARG LEU PHE          
SEQRES  21 A  346  ASP PRO ARG HIS GLU ARG GLU ASN GLU VAL PHE THR LYS          
SEQRES  22 A  346  LEU GLY TYR ILE ASP VAL LYS ASN LEU ALA LYS ARG ILE          
SEQRES  23 A  346  LYS GLY ASP VAL LEU MET CYS VAL GLY LEU MET ASP GLN          
SEQRES  24 A  346  VAL CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN ASN          
SEQRES  25 A  346  ILE GLN SER LYS LYS ASP ILE LYS VAL TYR PRO ASP TYR          
SEQRES  26 A  346  GLY HIS GLU PRO MET ARG GLY PHE GLY ASP LEU ALA MET          
SEQRES  27 A  346  GLN PHE MET LEU GLU LEU TYR SER                              
SEQRES   1 B  346  MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR          
SEQRES   2 B  346  ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA          
SEQRES   3 B  346  MET GLY LEU PHE ASP MET PRO LEU GLN LYS LEU ARG GLU          
SEQRES   4 B  346  TYR THR GLY THR ASN PRO CYS PRO GLU ASP PHE ASP GLU          
SEQRES   5 B  346  TYR TRP ASN ARG ALA LEU ASP GLU MET ARG SER VAL ASP          
SEQRES   6 B  346  PRO LYS ILE GLU LEU LYS GLU SER SER PHE GLN VAL SER          
SEQRES   7 B  346  PHE ALA GLU CYS TYR ASP LEU TYR PHE THR GLY VAL ARG          
SEQRES   8 B  346  GLY ALA ARG ILE HIS ALA LYS TYR ILE LYS PRO LYS THR          
SEQRES   9 B  346  GLU GLY LYS HIS PRO ALA LEU ILE ARG PHE HIS GLY TYR          
SEQRES  10 B  346  SER SER ASN SER GLY ASP TRP ASN ASP LYS LEU ASN TYR          
SEQRES  11 B  346  VAL ALA ALA GLY PHE THR VAL VAL ALA MET ASP VAL ARG          
SEQRES  12 B  346  GLY GLN GLY GLY GLN SER GLN ASP VAL GLY GLY VAL THR          
SEQRES  13 B  346  GLY ASN THR LEU ASN GLY HIS ILE ILE ARG GLY LEU ASP          
SEQRES  14 B  346  ASP ASP ALA ASP ASN MET LEU PHE ARG HIS ILE PHE LEU          
SEQRES  15 B  346  ASP THR ALA GLN LEU ALA GLY ILE VAL MET ASN MET PRO          
SEQRES  16 B  346  GLU VAL ASP GLU ASP ARG VAL GLY VAL MET GLY PRO SER          
SEQRES  17 B  346  GLN GLY GLY GLY LEU SER LEU ALA CYS ALA ALA LEU GLU          
SEQRES  18 B  346  PRO ARG VAL ARG LYS VAL VAL SER GLU TYR PRO PHE LEU          
SEQRES  19 B  346  SER ASP TYR LYS ARG VAL TRP ASP LEU ASP LEU ALA LYS          
SEQRES  20 B  346  ASN ALA TYR GLN GLU ILE THR ASP TYR PHE ARG LEU PHE          
SEQRES  21 B  346  ASP PRO ARG HIS GLU ARG GLU ASN GLU VAL PHE THR LYS          
SEQRES  22 B  346  LEU GLY TYR ILE ASP VAL LYS ASN LEU ALA LYS ARG ILE          
SEQRES  23 B  346  LYS GLY ASP VAL LEU MET CYS VAL GLY LEU MET ASP GLN          
SEQRES  24 B  346  VAL CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN ASN          
SEQRES  25 B  346  ILE GLN SER LYS LYS ASP ILE LYS VAL TYR PRO ASP TYR          
SEQRES  26 B  346  GLY HIS GLU PRO MET ARG GLY PHE GLY ASP LEU ALA MET          
SEQRES  27 B  346  GLN PHE MET LEU GLU LEU TYR SER                              
SEQRES   1 C  346  MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR          
SEQRES   2 C  346  ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA          
SEQRES   3 C  346  MET GLY LEU PHE ASP MET PRO LEU GLN LYS LEU ARG GLU          
SEQRES   4 C  346  TYR THR GLY THR ASN PRO CYS PRO GLU ASP PHE ASP GLU          
SEQRES   5 C  346  TYR TRP ASN ARG ALA LEU ASP GLU MET ARG SER VAL ASP          
SEQRES   6 C  346  PRO LYS ILE GLU LEU LYS GLU SER SER PHE GLN VAL SER          
SEQRES   7 C  346  PHE ALA GLU CYS TYR ASP LEU TYR PHE THR GLY VAL ARG          
SEQRES   8 C  346  GLY ALA ARG ILE HIS ALA LYS TYR ILE LYS PRO LYS THR          
SEQRES   9 C  346  GLU GLY LYS HIS PRO ALA LEU ILE ARG PHE HIS GLY TYR          
SEQRES  10 C  346  SER SER ASN SER GLY ASP TRP ASN ASP LYS LEU ASN TYR          
SEQRES  11 C  346  VAL ALA ALA GLY PHE THR VAL VAL ALA MET ASP VAL ARG          
SEQRES  12 C  346  GLY GLN GLY GLY GLN SER GLN ASP VAL GLY GLY VAL THR          
SEQRES  13 C  346  GLY ASN THR LEU ASN GLY HIS ILE ILE ARG GLY LEU ASP          
SEQRES  14 C  346  ASP ASP ALA ASP ASN MET LEU PHE ARG HIS ILE PHE LEU          
SEQRES  15 C  346  ASP THR ALA GLN LEU ALA GLY ILE VAL MET ASN MET PRO          
SEQRES  16 C  346  GLU VAL ASP GLU ASP ARG VAL GLY VAL MET GLY PRO SER          
SEQRES  17 C  346  GLN GLY GLY GLY LEU SER LEU ALA CYS ALA ALA LEU GLU          
SEQRES  18 C  346  PRO ARG VAL ARG LYS VAL VAL SER GLU TYR PRO PHE LEU          
SEQRES  19 C  346  SER ASP TYR LYS ARG VAL TRP ASP LEU ASP LEU ALA LYS          
SEQRES  20 C  346  ASN ALA TYR GLN GLU ILE THR ASP TYR PHE ARG LEU PHE          
SEQRES  21 C  346  ASP PRO ARG HIS GLU ARG GLU ASN GLU VAL PHE THR LYS          
SEQRES  22 C  346  LEU GLY TYR ILE ASP VAL LYS ASN LEU ALA LYS ARG ILE          
SEQRES  23 C  346  LYS GLY ASP VAL LEU MET CYS VAL GLY LEU MET ASP GLN          
SEQRES  24 C  346  VAL CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN ASN          
SEQRES  25 C  346  ILE GLN SER LYS LYS ASP ILE LYS VAL TYR PRO ASP TYR          
SEQRES  26 C  346  GLY HIS GLU PRO MET ARG GLY PHE GLY ASP LEU ALA MET          
SEQRES  27 C  346  GLN PHE MET LEU GLU LEU TYR SER                              
HET     CA  A 321       1                                                       
HET     CA  C 321       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  HOH   *489(H2 O)                                                    
HELIX    1   1 PRO A    7  ARG A   12  1                                   6    
HELIX    2   2 ASP A   23  SER A   37  1                                  15    
HELIX    3   3 VAL A   64  GLY A   66  5                                   3    
HELIX    4   4 TRP A   98  ASP A  100  5                                   3    
HELIX    5   5 LYS A  101  ALA A  106  1                                   6    
HELIX    6   6 ASP A  145  ASN A  148  5                                   4    
HELIX    7   7 MET A  149  ASN A  167  1                                  19    
HELIX    8   8 SER A  182  GLU A  195  1                                  14    
HELIX    9   9 ASP A  210  LEU A  217  1                                   8    
HELIX   10  10 LYS A  221  ALA A  223  5                                   3    
HELIX   11  11 TYR A  224  ASP A  235  1                                  12    
HELIX   12  12 ARG A  240  GLY A  249  1                                  10    
HELIX   13  13 ASP A  252  ALA A  257  1                                   6    
HELIX   14  14 LYS A  258  ILE A  260  5                                   3    
HELIX   15  15 PRO A  276  ASN A  285  1                                  10    
HELIX   16  16 GLY A  306  GLU A  317  1                                  12    
HELIX   17  17 PRO B    7  ARG B   12  1                                   6    
HELIX   18  18 ASP B   23  SER B   37  1                                  15    
HELIX   19  19 VAL B   64  GLY B   66  5                                   3    
HELIX   20  20 TRP B   98  ASP B  100  5                                   3    
HELIX   21  21 LYS B  101  ALA B  106  1                                   6    
HELIX   22  22 ASP B  145  ASN B  148  5                                   4    
HELIX   23  23 MET B  149  MET B  166  1                                  18    
HELIX   24  24 SER B  182  GLU B  195  1                                  14    
HELIX   25  25 ASP B  210  LEU B  217  1                                   8    
HELIX   26  26 LYS B  221  ALA B  223  5                                   3    
HELIX   27  27 TYR B  224  ASP B  235  1                                  12    
HELIX   28  28 ARG B  240  GLY B  249  1                                  10    
HELIX   29  29 ASP B  252  ALA B  257  1                                   6    
HELIX   30  30 LYS B  258  ILE B  260  5                                   3    
HELIX   31  31 PRO B  276  ASN B  286  1                                  11    
HELIX   32  32 GLY B  306  LEU B  316  1                                  11    
HELIX   33  33 GLU B  317  TYR B  319  5                                   3    
HELIX   34  34 PRO C    7  ARG C   12  1                                   6    
HELIX   35  35 ASP C   23  SER C   37  1                                  15    
HELIX   36  36 VAL C   64  GLY C   66  5                                   3    
HELIX   37  37 TRP C   98  ASP C  100  5                                   3    
HELIX   38  38 LYS C  101  ALA C  107  1                                   7    
HELIX   39  39 ASP C  145  ASN C  148  5                                   4    
HELIX   40  40 MET C  149  ASN C  167  1                                  19    
HELIX   41  41 SER C  182  GLU C  195  1                                  14    
HELIX   42  42 ASP C  210  LEU C  217  1                                   8    
HELIX   43  43 LYS C  221  ALA C  223  5                                   3    
HELIX   44  44 TYR C  224  ASP C  235  1                                  12    
HELIX   45  45 ARG C  240  GLY C  249  1                                  10    
HELIX   46  46 ASP C  252  ALA C  257  1                                   6    
HELIX   47  47 LYS C  258  ILE C  260  5                                   3    
HELIX   48  48 PRO C  276  ASN C  285  1                                  10    
HELIX   49  49 GLY C  306  LEU C  316  1                                  11    
HELIX   50  50 GLU C  317  TYR C  319  5                                   3    
SHEET    1   A 9 GLU A  43  GLU A  46  0                                        
SHEET    2   A 9 ALA A  54  THR A  62 -1  O  ASP A  58   N  LYS A  45           
SHEET    3   A 9 ARG A  68  PRO A  76 -1  O  ILE A  69   N  PHE A  61           
SHEET    4   A 9 THR A 110  MET A 114 -1  O  VAL A 111   N  ILE A  74           
SHEET    5   A 9 HIS A  82  PHE A  88  1  N  ARG A  87   O  VAL A 112           
SHEET    6   A 9 VAL A 171  PRO A 181  1  O  GLY A 177   N  ALA A  84           
SHEET    7   A 9 LYS A 200  GLU A 204  1  O  VAL A 202   N  VAL A 178           
SHEET    8   A 9 ASP A 263  GLY A 269  1  O  LEU A 265   N  VAL A 201           
SHEET    9   A 9 LYS A 291  TYR A 296  1  O  LYS A 294   N  MET A 266           
SHEET    1   B 9 GLU B  43  GLU B  46  0                                        
SHEET    2   B 9 ALA B  54  THR B  62 -1  O  ASP B  58   N  LYS B  45           
SHEET    3   B 9 ARG B  68  PRO B  76 -1  O  ILE B  69   N  PHE B  61           
SHEET    4   B 9 THR B 110  MET B 114 -1  O  VAL B 111   N  ILE B  74           
SHEET    5   B 9 HIS B  82  PHE B  88  1  N  ARG B  87   O  VAL B 112           
SHEET    6   B 9 VAL B 171  PRO B 181  1  O  GLY B 177   N  ALA B  84           
SHEET    7   B 9 LYS B 200  GLU B 204  1  O  GLU B 204   N  GLY B 180           
SHEET    8   B 9 ASP B 263  GLY B 269  1  O  LEU B 265   N  VAL B 201           
SHEET    9   B 9 LYS B 291  TYR B 296  1  O  LYS B 294   N  MET B 266           
SHEET    1   C 9 GLU C  43  GLU C  46  0                                        
SHEET    2   C 9 ALA C  54  THR C  62 -1  O  ASP C  58   N  LYS C  45           
SHEET    3   C 9 ARG C  68  PRO C  76 -1  O  ILE C  69   N  PHE C  61           
SHEET    4   C 9 THR C 110  MET C 114 -1  O  VAL C 111   N  ILE C  74           
SHEET    5   C 9 HIS C  82  PHE C  88  1  N  ARG C  87   O  VAL C 112           
SHEET    6   C 9 VAL C 171  PRO C 181  1  O  GLY C 177   N  ALA C  84           
SHEET    7   C 9 LYS C 200  GLU C 204  1  O  VAL C 202   N  VAL C 178           
SHEET    8   C 9 ASP C 263  GLY C 269  1  O  LEU C 265   N  VAL C 201           
SHEET    9   C 9 LYS C 291  TYR C 296  1  O  TYR C 296   N  VAL C 268           
LINK         O   GLU A 317                CA    CA A 321     1555   1555  2.62  
LINK         O   TYR A 319                CA    CA A 321     1555   1555  2.52  
LINK         O   GLU C 317                CA    CA C 321     1555   1555  2.46  
LINK         O   TYR C 319                CA    CA C 321     1555   1555  2.49  
LINK        CA    CA A 321                 O   HOH A 395     1555   1555  2.74  
LINK        CA    CA C 321                 O   HOH C 417     1555   1555  2.89  
SITE     1 AC1  3 GLU A 317  TYR A 319  HOH A 395                               
SITE     1 AC2  7 GLU B 317  TYR B 319  HOH B 321  HOH B 348                    
SITE     2 AC2  7 GLU C 317  TYR C 319  HOH C 417                               
CRYST1  132.263  132.263  112.914  90.00  90.00 120.00 P 32 2 1     18          
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      0.007561  0.004365  0.000000        0.00000                         
SCALE2      0.000000  0.008730  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008856        0.00000                         
TER    2525      SER A 320                                                      
TER    5050      SER B 320                                                      
TER    7575      SER C 320                                                      
MASTER      431    0    2   50   27    0    3    6 8063    3    8   81          
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.
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