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LongText Report for: 3BF7-pdb

Name Class
3BF7-pdb
HEADER    HYDROLASE                               21-NOV-07   3BF7              
TITLE     1.1 RESOLUTION STRUCTURE OF YBFF, A NEW ESTERASE FROM                 
TITLE    2 ESCHERICHIA COLI: A UNIQUE SUBSTRATE-BINDING CREVICE                 
TITLE    3 GENERATED BY DOMAIN ARRANGEMENT                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE YBFF;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.-.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 GENE: K12;                                                           
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: B834(DE3);                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PET21A                                     
KEYWDS    ESTERASE, THIOESTERASE, YBFF, HELICAL CAP, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.K.PARK,J.S.KIM                                                      
REVDAT   1   15-JAN-08 3BF7    0                                                
JRNL        AUTH   S.Y.PARK,S.H.LEE,J.LEE,N.KOSUKE,Y.S.KIM,C.H.JUNG,            
JRNL        AUTH 2 J.S.KIM                                                      
JRNL        TITL   1.1 RESOLUTION STRUCTURE OF YBFF, A NEW ESTERASE             
JRNL        TITL 2 FROM ESCHERICHIA COLI: A UNIQUE SUBSTRATE-BINDING            
JRNL        TITL 3 CREVICE GENERATED BY DOMAIN ARRANGEMENT                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.10 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -1.000                         
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 212339                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 21133                           
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) : 1.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.11                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 375                          
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            : 4025                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 1008                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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) : 0.004                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.24                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BF7 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB045444.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-2007                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6C1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99187                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 212392                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03400                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34300                            
REMARK 200   FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% TACSIMATE, PH7.0, VAPOR              
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291.0K                         
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   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-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       33.04500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.44200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.35600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.44200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.04500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.35600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     HIS B   255                                                      
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                             
REMARK 500   OE2  GLU B    59     O    HOH B   898              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   779     O    HOH B   617     4456     1.94            
REMARK 500   O    HOH A   779     O    HOH B   898     4456     2.02            
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  89     -117.81     49.77                                   
REMARK 500    ASP A 107      -88.08    -98.51                                   
REMARK 500    ASP A 113       63.52     37.31                                   
REMARK 500    SER A 137     -168.91    -78.72                                   
REMARK 500    GLN A 223       31.13    -99.50                                   
REMARK 500    ASP A 254       50.56     32.17                                   
REMARK 500    SER B  89     -116.08     49.45                                   
REMARK 500    ASP B 107      -83.80    -91.21                                   
REMARK 500    ASP B 113       63.24     37.54                                   
REMARK 500    TRP B 188      149.78   -171.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;                               
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 404        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A 492        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH B 740        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH B 772        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH B 790        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH A 571        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B 859        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH B 907        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH A 720        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH B 950        DISTANCE = 13.44 ANGSTROMS                       
REMARK 525    HOH A 749        DISTANCE =  8.04 ANGSTROMS                       
REMARK 525    HOH A 751        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A 769        DISTANCE =  6.54 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BF8   RELATED DB: PDB                                   
DBREF  3BF7 A    1   254  UNP    A7ZXU7   A7ZXU7_ECOLX     1    254             
DBREF  3BF7 B    1   254  UNP    A7ZXU7   A7ZXU7_ECOLX     1    254             
SEQADV 3BF7 VAL A   50  UNP  A7ZXU7    MET    50 ENGINEERED                     
SEQADV 3BF7 HIS A  255  UNP  A7ZXU7              EXPRESSION TAG                 
SEQADV 3BF7 VAL B   50  UNP  A7ZXU7    MET    50 ENGINEERED                     
SEQADV 3BF7 HIS B  255  UNP  A7ZXU7              EXPRESSION TAG                 
SEQRES   1 A  255  MET LYS LEU ASN ILE ARG ALA GLN THR ALA GLN ASN GLN          
SEQRES   2 A  255  HIS ASN ASN SER PRO ILE VAL LEU VAL HIS GLY LEU PHE          
SEQRES   3 A  255  GLY SER LEU ASP ASN LEU GLY VAL LEU ALA ARG ASP LEU          
SEQRES   4 A  255  VAL ASN ASP HIS ASN ILE ILE GLN VAL ASP VAL ARG ASN          
SEQRES   5 A  255  HIS GLY LEU SER PRO ARG GLU PRO VAL MET ASN TYR PRO          
SEQRES   6 A  255  ALA MET ALA GLN ASP LEU VAL ASP THR LEU ASP ALA LEU          
SEQRES   7 A  255  GLN ILE ASP LYS ALA THR PHE ILE GLY HIS SER MET GLY          
SEQRES   8 A  255  GLY LYS ALA VAL MET ALA LEU THR ALA LEU ALA PRO ASP          
SEQRES   9 A  255  ARG ILE ASP LYS LEU VAL ALA ILE ASP ILE ALA PRO VAL          
SEQRES  10 A  255  ASP TYR HIS VAL ARG ARG HIS ASP GLU ILE PHE ALA ALA          
SEQRES  11 A  255  ILE ASN ALA VAL SER GLU SER ASP ALA GLN THR ARG GLN          
SEQRES  12 A  255  GLN ALA ALA ALA ILE MET ARG GLN HIS LEU ASN GLU GLU          
SEQRES  13 A  255  GLY VAL ILE GLN PHE LEU LEU LYS SER PHE VAL ASP GLY          
SEQRES  14 A  255  GLU TRP ARG PHE ASN VAL PRO VAL LEU TRP ASP GLN TYR          
SEQRES  15 A  255  PRO HIS ILE VAL GLY TRP GLU LYS ILE PRO ALA TRP ASP          
SEQRES  16 A  255  HIS PRO ALA LEU PHE ILE PRO GLY GLY ASN SER PRO TYR          
SEQRES  17 A  255  VAL SER GLU GLN TYR ARG ASP ASP LEU LEU ALA GLN PHE          
SEQRES  18 A  255  PRO GLN ALA ARG ALA HIS VAL ILE ALA GLY ALA GLY HIS          
SEQRES  19 A  255  TRP VAL HIS ALA GLU LYS PRO ASP ALA VAL LEU ARG ALA          
SEQRES  20 A  255  ILE ARG ARG TYR LEU ASN ASP HIS                              
SEQRES   1 B  255  MET LYS LEU ASN ILE ARG ALA GLN THR ALA GLN ASN GLN          
SEQRES   2 B  255  HIS ASN ASN SER PRO ILE VAL LEU VAL HIS GLY LEU PHE          
SEQRES   3 B  255  GLY SER LEU ASP ASN LEU GLY VAL LEU ALA ARG ASP LEU          
SEQRES   4 B  255  VAL ASN ASP HIS ASN ILE ILE GLN VAL ASP VAL ARG ASN          
SEQRES   5 B  255  HIS GLY LEU SER PRO ARG GLU PRO VAL MET ASN TYR PRO          
SEQRES   6 B  255  ALA MET ALA GLN ASP LEU VAL ASP THR LEU ASP ALA LEU          
SEQRES   7 B  255  GLN ILE ASP LYS ALA THR PHE ILE GLY HIS SER MET GLY          
SEQRES   8 B  255  GLY LYS ALA VAL MET ALA LEU THR ALA LEU ALA PRO ASP          
SEQRES   9 B  255  ARG ILE ASP LYS LEU VAL ALA ILE ASP ILE ALA PRO VAL          
SEQRES  10 B  255  ASP TYR HIS VAL ARG ARG HIS ASP GLU ILE PHE ALA ALA          
SEQRES  11 B  255  ILE ASN ALA VAL SER GLU SER ASP ALA GLN THR ARG GLN          
SEQRES  12 B  255  GLN ALA ALA ALA ILE MET ARG GLN HIS LEU ASN GLU GLU          
SEQRES  13 B  255  GLY VAL ILE GLN PHE LEU LEU LYS SER PHE VAL ASP GLY          
SEQRES  14 B  255  GLU TRP ARG PHE ASN VAL PRO VAL LEU TRP ASP GLN TYR          
SEQRES  15 B  255  PRO HIS ILE VAL GLY TRP GLU LYS ILE PRO ALA TRP ASP          
SEQRES  16 B  255  HIS PRO ALA LEU PHE ILE PRO GLY GLY ASN SER PRO TYR          
SEQRES  17 B  255  VAL SER GLU GLN TYR ARG ASP ASP LEU LEU ALA GLN PHE          
SEQRES  18 B  255  PRO GLN ALA ARG ALA HIS VAL ILE ALA GLY ALA GLY HIS          
SEQRES  19 B  255  TRP VAL HIS ALA GLU LYS PRO ASP ALA VAL LEU ARG ALA          
SEQRES  20 B  255  ILE ARG ARG TYR LEU ASN ASP HIS                              
FORMUL   3  HOH   *1008(H2 O)                                                   
HELIX    1   1 LEU A   32  VAL A   40  1                                   9    
HELIX    2   2 ASN A   63  GLN A   79  1                                  17    
HELIX    3   3 SER A   89  ALA A  102  1                                  14    
HELIX    4   4 HIS A  124  SER A  137  1                                  14    
HELIX    5   5 THR A  141  ARG A  150  1                                  10    
HELIX    6   6 GLU A  155  LYS A  164  1                                  10    
HELIX    7   7 ASN A  174  GLN A  181  1                                   8    
HELIX    8   8 GLN A  181  GLY A  187  1                                   7    
HELIX    9   9 SER A  210  GLN A  212  5                                   3    
HELIX   10  10 TYR A  213  PHE A  221  1                                   9    
HELIX   11  11 TRP A  235  LYS A  240  1                                   6    
HELIX   12  12 LYS A  240  ASP A  254  1                                  15    
HELIX   13  13 LEU B   32  VAL B   40  1                                   9    
HELIX   14  14 ASN B   63  GLN B   79  1                                  17    
HELIX   15  15 SER B   89  ALA B  102  1                                  14    
HELIX   16  16 HIS B  124  SER B  137  1                                  14    
HELIX   17  17 THR B  141  ARG B  150  1                                  10    
HELIX   18  18 GLU B  155  LYS B  164  1                                  10    
HELIX   19  19 ASN B  174  GLN B  181  1                                   8    
HELIX   20  20 GLN B  181  GLY B  187  1                                   7    
HELIX   21  21 SER B  210  GLN B  212  5                                   3    
HELIX   22  22 TYR B  213  PHE B  221  1                                   9    
HELIX   23  23 TRP B  235  LYS B  240  1                                   6    
HELIX   24  24 LYS B  240  ASP B  254  1                                  15    
SHEET    1   A 7 ILE A   5  GLN A   8  0                                        
SHEET    2   A 7 ILE A  45  VAL A  48 -1  O  ILE A  45   N  GLN A   8           
SHEET    3   A 7 ILE A  19  VAL A  22  1  N  LEU A  21   O  ILE A  46           
SHEET    4   A 7 ALA A  83  HIS A  88  1  O  THR A  84   N  VAL A  20           
SHEET    5   A 7 ILE A 106  ILE A 112  1  O  ILE A 112   N  GLY A  87           
SHEET    6   A 7 ALA A 198  ILE A 201  1  O  LEU A 199   N  ALA A 111           
SHEET    7   A 7 ALA A 224  ALA A 226  1  O  ARG A 225   N  PHE A 200           
SHEET    1   B 2 PHE A 166  VAL A 167  0                                        
SHEET    2   B 2 GLU A 170  TRP A 171 -1  O  GLU A 170   N  VAL A 167           
SHEET    1   C 7 ILE B   5  GLN B   8  0                                        
SHEET    2   C 7 ILE B  45  VAL B  48 -1  O  ILE B  45   N  GLN B   8           
SHEET    3   C 7 ILE B  19  VAL B  22  1  N  LEU B  21   O  ILE B  46           
SHEET    4   C 7 ALA B  83  HIS B  88  1  O  THR B  84   N  VAL B  20           
SHEET    5   C 7 ILE B 106  ILE B 112  1  O  ILE B 112   N  GLY B  87           
SHEET    6   C 7 ALA B 198  ILE B 201  1  O  LEU B 199   N  ALA B 111           
SHEET    7   C 7 ALA B 224  ALA B 226  1  O  ARG B 225   N  PHE B 200           
SHEET    1   D 2 PHE B 166  VAL B 167  0                                        
SHEET    2   D 2 GLU B 170  TRP B 171 -1  O  GLU B 170   N  VAL B 167           
CRYST1   66.090   90.712   92.884  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015131  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011024  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010766        0.00000                         
TER    2019      HIS A 255                                                      
TER    4027      ASP B 254                                                      
MASTER      313    0    0   24   18    0    0    6 5033    2    0   40          
END                                                                             

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