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LongText Report for: 5jkf-pdb

Name Class
5jkf-pdb
HEADER    HYDROLASE                               26-APR-16   5JKF              
TITLE     CRYSTAL STRUCTURE OF ESTERASE E22                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE E22;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3)PLYSS AG;                    
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    ESTERASE E32, HYDROLASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,P.WANG,Q.YAO                                                  
REVDAT   1   26-APR-17 5JKF    0                                                
JRNL        AUTH   Y.ZHANG,Q.YAO,P.WANG                                         
JRNL        TITL   STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION AND CATALYSIS OF  
JRNL        TITL 2 A NOVEL ESTERASE E22 WITH A HOMOSERINE TRANSACETYLASE-LIKE   
JRNL        TITL 3 FOLD                                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 24105                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1173                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.7554 -  4.7838    0.92     3089   151  0.1476 0.1808        
REMARK   3     2  4.7838 -  3.7978    0.88     2817   153  0.1352 0.2100        
REMARK   3     3  3.7978 -  3.3179    0.89     2805   164  0.1683 0.2430        
REMARK   3     4  3.3179 -  3.0146    0.90     2842   132  0.1918 0.3353        
REMARK   3     5  3.0146 -  2.7986    0.92     2859   144  0.1997 0.2936        
REMARK   3     6  2.7986 -  2.6336    0.92     2843   145  0.2056 0.2760        
REMARK   3     7  2.6336 -  2.5018    0.91     2849   147  0.2118 0.2875        
REMARK   3     8  2.5018 -  2.3929    0.90     2828   137  0.2213 0.3619        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.550           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           5826                                  
REMARK   3   ANGLE     :  0.954           7939                                  
REMARK   3   CHIRALITY :  0.054            893                                  
REMARK   3   PLANARITY :  0.006           1026                                  
REMARK   3   DIHEDRAL  : 13.387           3437                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5JKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220782.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24115                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.393                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 27.1300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3I1I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CHES (PH 9.5), 16% (W/V) PEG        
REMARK 280  8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.14750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.70850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.84100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.70850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.14750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.84100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   394                                                      
REMARK 465     ASN B   393                                                      
REMARK 465     ASP B   394                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER B   175     O    HOH B   401              1.84            
REMARK 500   O    HOH A   463     O    HOH A   481              1.96            
REMARK 500   NH2  ARG A   150     O    GLY A   316              2.08            
REMARK 500   O    HOH A   466     O    HOH B   476              2.11            
REMARK 500   CB   MET B    25     O    HOH B   482              2.12            
REMARK 500   O    SER A   166     O    HOH A   401              2.12            
REMARK 500   O    LEU B   221     O    HOH B   402              2.13            
REMARK 500   NZ   LYS B    42     O    HOH B   403              2.15            
REMARK 500   OD2  ASP B   151     O    HOH B   404              2.16            
REMARK 500   O    ALA A   100     O    HOH A   402              2.17            
REMARK 500   O    HOH A   456     O    HOH B   476              2.19            
REMARK 500   O    HOH A   468     O    HOH B   474              2.19            
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 175     -120.80     67.75                                   
REMARK 500    ILE A 199       48.47     36.28                                   
REMARK 500    LEU A 252     -157.84   -121.10                                   
REMARK 500    VAL A 269       73.46   -101.78                                   
REMARK 500    HIS A 317       42.85     75.03                                   
REMARK 500    GLN A 318     -158.68    -95.36                                   
REMARK 500    ASP A 361       96.65    -61.55                                   
REMARK 500    PRO B  88     -169.21    -79.95                                   
REMARK 500    SER B 175     -118.17     57.70                                   
REMARK 500    ILE B 199       56.16     30.92                                   
REMARK 500    LEU B 252     -153.46   -116.95                                   
REMARK 500    GLN B 318     -159.37   -110.46                                   
REMARK 500    ASP B 361       92.01    -64.13                                   
REMARK 500    VAL B 377      -69.11   -102.62                                   
REMARK 500    ASN B 379       52.73   -142.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JKJ   RELATED DB: PDB                                   
DBREF  5JKF A   25   394  PDB    5JKF     5JKF            25    394             
DBREF  5JKF B   25   394  PDB    5JKF     5JKF            25    394             
SEQRES   1 A  370  MET VAL GLU LYS ARG VAL PHE GLU MET PRO HIS PHE THR          
SEQRES   2 A  370  THR PHE GLY GLY LYS GLN ILE LYS ASN VAL LYS VAL GLY          
SEQRES   3 A  370  TRP GLU ALA TYR GLY THR LEU ASN ASP ALA LYS SER ASN          
SEQRES   4 A  370  VAL ILE LEU ILE THR HIS TYR PHE SER GLY SER SER HIS          
SEQRES   5 A  370  ALA ALA GLY LYS TYR ASP GLU ASN ASP PRO ALA PRO GLY          
SEQRES   6 A  370  TYR TRP ASP SER ILE ILE GLY PRO GLY LYS ALA ILE ASP          
SEQRES   7 A  370  THR ASP ARG PHE TYR VAL ILE SER VAL ASP THR LEU ALA          
SEQRES   8 A  370  ASN LEU ASN ALA TYR ASP PRO HIS VAL ILE THR THR GLY          
SEQRES   9 A  370  PRO THR SER ILE ASN PRO ASP THR GLY LYS PRO TYR GLY          
SEQRES  10 A  370  LEU ASP PHE PRO VAL VAL THR ILE ARG ASP PHE VAL ASN          
SEQRES  11 A  370  VAL GLN LYS ALA LEU LEU GLU SER LEU GLY ILE SER LYS          
SEQRES  12 A  370  LEU TYR ALA VAL ILE GLY PRO SER MET GLY SER MET GLN          
SEQRES  13 A  370  ALA ILE ASP TRP ALA SER ALA TYR PRO GLY TRP VAL GLU          
SEQRES  14 A  370  ARG MET ILE SER VAL ILE GLY ALA GLY GLN SER ASP ALA          
SEQRES  15 A  370  TRP THR THR ALA ALA LEU GLU HIS TRP ALA THR PRO ILE          
SEQRES  16 A  370  THR LEU ASP LYS ASN TRP ASN ASN GLY ALA TYR SER LYS          
SEQRES  17 A  370  GLU GLN ALA PRO LEU ASN GLY LEU ALA ALA SER LEU MET          
SEQRES  18 A  370  LEU ILE THR GLN ASN ALA LEU THR PRO SER PHE PHE ASN          
SEQRES  19 A  370  GLN THR GLY ASN THR LEU GLY TYR LYS ASN VAL GLU SER          
SEQRES  20 A  370  ALA PRO LEU ASN ASP ILE ARG GLN SER HIS SER ILE VAL          
SEQRES  21 A  370  ASN TRP LEU ARG GLU ARG ALA LYS THR ARG ALA LYS SER          
SEQRES  22 A  370  MET ASP ALA ASN HIS LEU LEU TYR LEU VAL ARG ALA CYS          
SEQRES  23 A  370  GLN LEU PHE VAL ALA GLY HIS GLN GLY ASN LEU GLU GLN          
SEQRES  24 A  370  GLY LEU ALA SER ILE LYS ALA LYS THR LEU PHE ILE PRO          
SEQRES  25 A  370  ALA GLN THR ASP LEU LEU LEU MET PRO TYR LEU SER GLN          
SEQRES  26 A  370  SER ALA HIS GLN GLY LEU THR SER MET ASN ASN ASP SER          
SEQRES  27 A  370  THR LEU VAL THR LEU ASN GLY LYS LEU GLY HIS LEU GLU          
SEQRES  28 A  370  GLY VAL THR ASN VAL SER ALA GLN ALA GLN ALA ILE ARG          
SEQRES  29 A  370  GLN PHE LEU GLU ASN ASP                                      
SEQRES   1 B  370  MET VAL GLU LYS ARG VAL PHE GLU MET PRO HIS PHE THR          
SEQRES   2 B  370  THR PHE GLY GLY LYS GLN ILE LYS ASN VAL LYS VAL GLY          
SEQRES   3 B  370  TRP GLU ALA TYR GLY THR LEU ASN ASP ALA LYS SER ASN          
SEQRES   4 B  370  VAL ILE LEU ILE THR HIS TYR PHE SER GLY SER SER HIS          
SEQRES   5 B  370  ALA ALA GLY LYS TYR ASP GLU ASN ASP PRO ALA PRO GLY          
SEQRES   6 B  370  TYR TRP ASP SER ILE ILE GLY PRO GLY LYS ALA ILE ASP          
SEQRES   7 B  370  THR ASP ARG PHE TYR VAL ILE SER VAL ASP THR LEU ALA          
SEQRES   8 B  370  ASN LEU ASN ALA TYR ASP PRO HIS VAL ILE THR THR GLY          
SEQRES   9 B  370  PRO THR SER ILE ASN PRO ASP THR GLY LYS PRO TYR GLY          
SEQRES  10 B  370  LEU ASP PHE PRO VAL VAL THR ILE ARG ASP PHE VAL ASN          
SEQRES  11 B  370  VAL GLN LYS ALA LEU LEU GLU SER LEU GLY ILE SER LYS          
SEQRES  12 B  370  LEU TYR ALA VAL ILE GLY PRO SER MET GLY SER MET GLN          
SEQRES  13 B  370  ALA ILE ASP TRP ALA SER ALA TYR PRO GLY TRP VAL GLU          
SEQRES  14 B  370  ARG MET ILE SER VAL ILE GLY ALA GLY GLN SER ASP ALA          
SEQRES  15 B  370  TRP THR THR ALA ALA LEU GLU HIS TRP ALA THR PRO ILE          
SEQRES  16 B  370  THR LEU ASP LYS ASN TRP ASN ASN GLY ALA TYR SER LYS          
SEQRES  17 B  370  GLU GLN ALA PRO LEU ASN GLY LEU ALA ALA SER LEU MET          
SEQRES  18 B  370  LEU ILE THR GLN ASN ALA LEU THR PRO SER PHE PHE ASN          
SEQRES  19 B  370  GLN THR GLY ASN THR LEU GLY TYR LYS ASN VAL GLU SER          
SEQRES  20 B  370  ALA PRO LEU ASN ASP ILE ARG GLN SER HIS SER ILE VAL          
SEQRES  21 B  370  ASN TRP LEU ARG GLU ARG ALA LYS THR ARG ALA LYS SER          
SEQRES  22 B  370  MET ASP ALA ASN HIS LEU LEU TYR LEU VAL ARG ALA CYS          
SEQRES  23 B  370  GLN LEU PHE VAL ALA GLY HIS GLN GLY ASN LEU GLU GLN          
SEQRES  24 B  370  GLY LEU ALA SER ILE LYS ALA LYS THR LEU PHE ILE PRO          
SEQRES  25 B  370  ALA GLN THR ASP LEU LEU LEU MET PRO TYR LEU SER GLN          
SEQRES  26 B  370  SER ALA HIS GLN GLY LEU THR SER MET ASN ASN ASP SER          
SEQRES  27 B  370  THR LEU VAL THR LEU ASN GLY LYS LEU GLY HIS LEU GLU          
SEQRES  28 B  370  GLY VAL THR ASN VAL SER ALA GLN ALA GLN ALA ILE ARG          
SEQRES  29 B  370  GLN PHE LEU GLU ASN ASP                                      
FORMUL   3  HOH   *170(H2 O)                                                    
HELIX    1 AA1 TYR A  140  PHE A  144  5                                   5    
HELIX    2 AA2 THR A  148  LEU A  163  1                                  16    
HELIX    3 AA3 SER A  175  TYR A  188  1                                  14    
HELIX    4 AA4 PRO A  189  VAL A  192  5                                   4    
HELIX    5 AA5 ASP A  205  ASP A  222  1                                  18    
HELIX    6 AA6 LYS A  223  ALA A  229  5                                   7    
HELIX    7 AA7 SER A  231  ALA A  235  5                                   5    
HELIX    8 AA8 PRO A  236  ALA A  251  1                                  16    
HELIX    9 AA9 THR A  253  LEU A  264  1                                  12    
HELIX   10 AB1 GLU A  270  ASP A  276  1                                   7    
HELIX   11 AB2 HIS A  281  ALA A  295  1                                  15    
HELIX   12 AB3 ASP A  299  LEU A  312  1                                  14    
HELIX   13 AB4 ASN A  320  SER A  327  1                                   8    
HELIX   14 AB5 MET A  344  MET A  358  1                                  15    
HELIX   15 AB6 LEU A  371  HIS A  373  5                                   3    
HELIX   16 AB7 LEU A  374  ASN A  379  1                                   6    
HELIX   17 AB8 VAL A  380  ALA A  382  5                                   3    
HELIX   18 AB9 GLN A  383  GLU A  392  1                                  10    
HELIX   19 AC1 TRP B   91  SER B   93  5                                   3    
HELIX   20 AC2 TYR B  140  PHE B  144  5                                   5    
HELIX   21 AC3 THR B  148  SER B  162  1                                  15    
HELIX   22 AC4 SER B  175  TYR B  188  1                                  14    
HELIX   23 AC5 PRO B  189  VAL B  192  5                                   4    
HELIX   24 AC6 ASP B  205  ASP B  222  1                                  18    
HELIX   25 AC7 LYS B  223  ALA B  229  5                                   7    
HELIX   26 AC8 PRO B  236  ALA B  251  1                                  16    
HELIX   27 AC9 THR B  253  GLY B  265  1                                  13    
HELIX   28 AD1 GLU B  270  ASP B  276  1                                   7    
HELIX   29 AD2 HIS B  281  ALA B  295  1                                  15    
HELIX   30 AD3 ASP B  299  LEU B  312  1                                  14    
HELIX   31 AD4 VAL B  314  GLN B  318  5                                   5    
HELIX   32 AD5 ASN B  320  SER B  327  1                                   8    
HELIX   33 AD6 MET B  344  MET B  358  1                                  15    
HELIX   34 AD7 LEU B  371  HIS B  373  5                                   3    
HELIX   35 AD8 LEU B  374  ASN B  379  1                                   6    
HELIX   36 AD9 VAL B  380  ALA B  382  5                                   3    
HELIX   37 AE1 GLN B  383  GLU B  392  1                                  10    
SHEET    1 AA1 8 ARG A  29  THR A  37  0                                        
SHEET    2 AA1 8 GLN A  43  TYR A  54 -1  O  TRP A  51   N  ARG A  29           
SHEET    3 AA1 8 TYR A 107  VAL A 111 -1  O  VAL A 108   N  TYR A  54           
SHEET    4 AA1 8 VAL A  64  ILE A  67  1  N  ILE A  65   O  TYR A 107           
SHEET    5 AA1 8 ALA A 170  PRO A 174  1  O  ILE A 172   N  LEU A  66           
SHEET    6 AA1 8 ARG A 194  VAL A 198  1  O  ILE A 196   N  VAL A 171           
SHEET    7 AA1 8 LYS A 331  ILE A 335  1  O  LEU A 333   N  SER A 197           
SHEET    8 AA1 8 SER A 362  LEU A 364  1  O  THR A 363   N  THR A 332           
SHEET    1 AA2 2 ILE A  95  GLY A  96  0                                        
SHEET    2 AA2 2 ILE A 101  ASP A 102  1  O  ILE A 101   N  GLY A  96           
SHEET    1 AA3 8 ARG B  29  THR B  37  0                                        
SHEET    2 AA3 8 GLN B  43  TYR B  54 -1  O  VAL B  49   N  PHE B  31           
SHEET    3 AA3 8 TYR B 107  VAL B 111 -1  O  VAL B 108   N  TYR B  54           
SHEET    4 AA3 8 VAL B  64  ILE B  67  1  N  ILE B  67   O  ILE B 109           
SHEET    5 AA3 8 ALA B 170  PRO B 174  1  O  ILE B 172   N  LEU B  66           
SHEET    6 AA3 8 ARG B 194  VAL B 198  1  O  ILE B 196   N  VAL B 171           
SHEET    7 AA3 8 LYS B 331  ILE B 335  1  O  ILE B 335   N  SER B 197           
SHEET    8 AA3 8 SER B 362  LEU B 364  1  O  THR B 363   N  PHE B 334           
SHEET    1 AA4 2 ILE B  95  GLY B  96  0                                        
SHEET    2 AA4 2 ILE B 101  ASP B 102  1  O  ILE B 101   N  GLY B  96           
CRYST1   58.295   67.682  165.417  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      0.017154  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014775  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006045        0.00000                         
TER    2850      ASN A 393                                                      
TER    5684      GLU B 392                                                      
MASTER      265    0    0   37   20    0    0    6 5844    2    0   58          
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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