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LongText Report for: 2E3J-pdb

Name Class
2E3J-pdb
HEADER    HYDROLASE                               27-NOV-06   2E3J              
TITLE     THE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE B (RV1938) FROM            
TITLE    2 MYCOBACTERIUM TUBERCULOSIS AT 2.1 ANGSTROM                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXIDE HYDROLASE EPHB;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EPOXIDE HYDROLASE B, EPOXIDE HYDRATASE, EPOXIDE             
COMPND   5 HYDROLASE;                                                           
COMPND   6 EC: 3.3.2.3;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 (AI);                             
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST17                                   
KEYWDS    EPOXIDE HYDROLASE B, MYCOBACTERIUM TUBERCULOSIS, X-RAY                
KEYWDS   2 CRYSTALLOGRAPHY, STRUCTURAL GENOMICS, MYCOBACTERIUM                  
KEYWDS   3 TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT, XMTB                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.K.BISWAL,MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS           
AUTHOR   2 PROJECT (XMTB)                                                       
REVDAT   1   04-DEC-07 2E3J    0                                                
JRNL        AUTH   B.K.BISWAL,G.GAREN,M.M.CHERNEY,C.GAREN,M.N.JAMES             
JRNL        TITL   THE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE B                 
JRNL        TITL 2 (RV1938) FROM MYCOBACTERIUM TUBERCULOSIS AT 2.1              
JRNL        TITL 3 ANGSTROM                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.28                          
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)   (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20701                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHT                        
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1038                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3900                       
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 149                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2708                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.28000                                             
REMARK   3    B22 (A**2) : 12.28000                                             
REMARK   3    B33 (A**2) : -24.57000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
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) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.44                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.26                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 2E3J COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB026179.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-2005                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.115869                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
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) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49200                            
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: RESIDUES 245-541 (C-TREMINAL DOMAIN) OF PDB ID       
REMARK 200  1EK1                                                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% 2-PROPANOL, 0.2M CACL2, 0.1M         
REMARK 280  SODIUM ACETATE BUFFER, PROTEIN CONCENTRATION 5-10MG/ML, PH          
REMARK 280  4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,1/2+Z                                             
REMARK 290       3555   1/2-Y,1/2+X,1/4+Z                                       
REMARK 290       4555   1/2+Y,1/2-X,3/4+Z                                       
REMARK 290       5555   1/2-X,1/2+Y,1/4-Z                                       
REMARK 290       6555   1/2+X,1/2-Y,3/4-Z                                       
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,1/2-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.55450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       33.12900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       33.12900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       39.27725            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       33.12900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       33.12900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      117.83175            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       33.12900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       33.12900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       39.27725            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       33.12900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       33.12900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      117.83175            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       78.55450            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: DIMER                             
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       78.55450            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2091   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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     VAL A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     ALA A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     VAL A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     GLU A   213                                                      
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    GLU A  38     -155.33   -117.78                                   
REMARK 500    ASP A 104     -127.30     51.54                                   
REMARK 500    SER A 128      -53.91     78.54                                   
REMARK 500    VAL A 136      -59.15     70.56                                   
REMARK 500    LEU A 154      -81.84    -40.57                                   
REMARK 500    LEU A 156       72.05     60.02                                   
REMARK 500    ALA A 157       -7.86    168.39                                   
REMARK 500    PRO A 159      -71.05    -52.43                                   
REMARK 500    ASP A 172      -72.22   -129.99                                   
REMARK 500    ASP A 181       83.63   -161.87                                   
REMARK 500    ALA A 204       39.39    -79.13                                   
REMARK 500    GLU A 230      131.89    -39.02                                   
REMARK 500    ASP A 284       21.19    -63.83                                   
REMARK 500    ASP A 330       -9.37     67.66                                   
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 A2084        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A2114        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A2137        DISTANCE =  5.25 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: RV1938   RELATED DB: TARGETDB                            
DBREF  2E3J A    2   356  UNP    P95276   P95276_MYCTU     2    356             
SEQADV 2E3J VAL A    1  UNP  P95276              EXPRESSION TAG                 
SEQRES   1 A  356  VAL SER GLN VAL HIS ARG ILE LEU ASN CYS ARG GLY THR          
SEQRES   2 A  356  ARG ILE HIS ALA VAL ALA ASP SER PRO PRO ASP GLN GLN          
SEQRES   3 A  356  GLY PRO LEU VAL VAL LEU LEU HIS GLY PHE PRO GLU SER          
SEQRES   4 A  356  TRP TYR SER TRP ARG HIS GLN ILE PRO ALA LEU ALA GLY          
SEQRES   5 A  356  ALA GLY TYR ARG VAL VAL ALA ILE ASP GLN ARG GLY TYR          
SEQRES   6 A  356  GLY ARG SER SER LYS TYR ARG VAL GLN LYS ALA TYR ARG          
SEQRES   7 A  356  ILE LYS GLU LEU VAL GLY ASP VAL VAL GLY VAL LEU ASP          
SEQRES   8 A  356  SER TYR GLY ALA GLU GLN ALA PHE VAL VAL GLY HIS ASP          
SEQRES   9 A  356  TRP GLY ALA PRO VAL ALA TRP THR PHE ALA TRP LEU HIS          
SEQRES  10 A  356  PRO ASP ARG CYS ALA GLY VAL VAL GLY ILE SER VAL PRO          
SEQRES  11 A  356  PHE ALA GLY ARG GLY VAL ILE GLY LEU PRO GLY SER PRO          
SEQRES  12 A  356  PHE GLY GLU ARG ARG PRO SER ASP TYR HIS LEU GLU LEU          
SEQRES  13 A  356  ALA GLY PRO GLY ARG VAL TRP TYR GLN ASP TYR PHE ALA          
SEQRES  14 A  356  VAL GLN ASP GLY ILE ILE THR GLU ILE GLU GLU ASP LEU          
SEQRES  15 A  356  ARG GLY TRP LEU LEU GLY LEU THR TYR THR VAL SER GLY          
SEQRES  16 A  356  GLU GLY MET MET ALA ALA THR LYS ALA ALA VAL ASP ALA          
SEQRES  17 A  356  GLY VAL ASP LEU GLU SER MET ASP PRO ILE ASP VAL ILE          
SEQRES  18 A  356  ARG ALA GLY PRO LEU CYS MET ALA GLU GLY ALA ARG LEU          
SEQRES  19 A  356  LYS ASP ALA PHE VAL TYR PRO GLU THR MET PRO ALA TRP          
SEQRES  20 A  356  PHE THR GLU ALA ASP LEU ASP PHE TYR THR GLY GLU PHE          
SEQRES  21 A  356  GLU ARG SER GLY PHE GLY GLY PRO LEU SER PHE TYR HIS          
SEQRES  22 A  356  ASN ILE ASP ASN ASP TRP HIS ASP LEU ALA ASP GLN GLN          
SEQRES  23 A  356  GLY LYS PRO LEU THR PRO PRO ALA LEU PHE ILE GLY GLY          
SEQRES  24 A  356  GLN TYR ASP VAL GLY THR ILE TRP GLY ALA GLN ALA ILE          
SEQRES  25 A  356  GLU ARG ALA HIS GLU VAL MET PRO ASN TYR ARG GLY THR          
SEQRES  26 A  356  HIS MET ILE ALA ASP VAL GLY HIS TRP ILE GLN GLN GLU          
SEQRES  27 A  356  ALA PRO GLU GLU THR ASN ARG LEU LEU LEU ASP PHE LEU          
SEQRES  28 A  356  GLY GLY LEU ARG PRO                                          
HET    ACT  A2001       4                                                       
HET    ACT  A2002       4                                                       
HET    ACT  A2003       4                                                       
HET    ACT  A2004       4                                                       
HET    ACT  A2005       4                                                       
HET    ACT  A2006       4                                                       
HET    ACT  A2007       4                                                       
HET    ACT  A2008       4                                                       
HET    ACT  A2009       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   2  ACT    9(C2 H3 O2 1-)                                               
FORMUL  11  HOH   *128(H2 O)                                                    
HELIX    1   1 SER A   39  ARG A   44  5                                   6    
HELIX    2   2 GLN A   46  ALA A   53  1                                   8    
HELIX    3   3 VAL A   73  TYR A   77  5                                   5    
HELIX    4   4 ARG A   78  TYR A   93  1                                  16    
HELIX    5   5 TRP A  105  HIS A  117  1                                  13    
HELIX    6   6 ALA A  132  VAL A  136  5                                   5    
HELIX    7   7 ARG A  148  GLU A  155  1                                   8    
HELIX    8   8 TYR A  164  GLN A  171  1                                   8    
HELIX    9   9 ASP A  172  GLU A  180  1                                   9    
HELIX   10  10 ASP A  181  VAL A  193  1                                  13    
HELIX   11  11 SER A  194  ALA A  204  1                                  11    
HELIX   12  12 ASP A  216  VAL A  220  5                                   5    
HELIX   13  13 ARG A  233  PHE A  238  5                                   6    
HELIX   14  14 THR A  249  GLY A  264  1                                  16    
HELIX   15  15 PHE A  265  ASN A  274  1                                  10    
HELIX   16  16 ASN A  274  LEU A  282  1                                   9    
HELIX   17  17 ALA A  283  GLN A  286  5                                   4    
HELIX   18  18 ASP A  302  GLY A  308  1                                   7    
HELIX   19  19 GLY A  308  ARG A  314  1                                   7    
HELIX   20  20 ARG A  314  MET A  319  1                                   6    
HELIX   21  21 TRP A  334  ALA A  339  1                                   6    
HELIX   22  22 ALA A  339  GLY A  353  1                                  15    
SHEET    1   A 8 HIS A   5  CYS A  10  0                                        
SHEET    2   A 8 THR A  13  ASP A  20 -1  O  THR A  13   N  CYS A  10           
SHEET    3   A 8 ARG A  56  ILE A  60 -1  O  VAL A  57   N  ASP A  20           
SHEET    4   A 8 LEU A  29  LEU A  33  1  N  LEU A  32   O  VAL A  58           
SHEET    5   A 8 ALA A  98  HIS A 103  1  O  VAL A 101   N  LEU A  33           
SHEET    6   A 8 CYS A 121  ILE A 127  1  O  ILE A 127   N  GLY A 102           
SHEET    7   A 8 ALA A 294  GLY A 299  1  O  LEU A 295   N  GLY A 126           
SHEET    8   A 8 TYR A 322  ILE A 328  1  O  ARG A 323   N  ALA A 294           
SHEET    1   B 2 ARG A 161  TRP A 163  0                                        
SHEET    2   B 2 CYS A 227  ALA A 229 -1  O  MET A 228   N  VAL A 162           
CISPEP   1 PHE A   36    PRO A   37          0        -0.59                     
CRYST1   66.258   66.258  157.109  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015093  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015093  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006365        0.00000                         
TER    2709      PRO A 356                                                      
MASTER      304    0    9   22   10    0    0    6 2872    1   36   28          
END                                                                             

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