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LongText Report for: 7d78-pdb

Name Class
7d78-pdb
HEADER    HYDROLASE                               03-OCT-20   7D78              
TITLE     THE STRUCTURE OF THIOESTERASE DCSB                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DLTD DOMAIN-CONTAINING PROTEIN;                            
COMPND   3 CHAIN: D, A;                                                         
COMPND   4 SYNONYM: THIOESTERASE;                                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BEAUVERIA BASSIANA (STRAIN ARSEF 2860);         
SOURCE   3 ORGANISM_COMMON: WHITE MUSCARDINE DISEASE FUNGUS;                    
SOURCE   4 ORGANISM_TAXID: 655819;                                              
SOURCE   5 STRAIN: ARSEF 2860;                                                  
SOURCE   6 GENE: BBA_03809;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693                                      
KEYWDS    THIOESTERASE, POLYKETIDES, LACTONES, HYDROLASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.TANG,J.H.ZHOU,G.Q.WANG                                              
REVDAT   1   27-JAN-21 7D78    0                                                
JRNL        AUTH   D.W.GAO,C.S.JAMIESON,G.WANG,Y.YAN,J.ZHOU,K.N.HOUK,Y.TANG     
JRNL        TITL   A POLYKETIDE CYCLASE THAT FORMS MEDIUM-RING LACTONES.        
JRNL        REF    J.AM.CHEM.SOC.                V. 143    80 2021              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   33351624                                                     
JRNL        DOI    10.1021/JACS.0C11226                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.363                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 42956                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.026                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2159                            
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  4.8442 -  4.8442    0.98     2799   168  0.1358 0.1677        
REMARK   3     2  4.8442 -  3.8461    1.00     2781   141  0.1234 0.1350        
REMARK   3     3  3.8461 -  3.3603    1.00     2754   146  0.1388 0.1716        
REMARK   3     4  3.3603 -  3.0532    1.00     2738   150  0.1533 0.1985        
REMARK   3     5  3.0532 -  2.8344    1.00     2744   157  0.1616 0.1945        
REMARK   3     6  2.8344 -  2.6673    1.00     2717   126  0.1573 0.1825        
REMARK   3     7  2.6673 -  2.5338    1.00     2748   120  0.1592 0.2302        
REMARK   3     8  2.5338 -  2.4235    1.00     2724   147  0.1567 0.1899        
REMARK   3     9  2.4235 -  2.3302    1.00     2695   161  0.1531 0.2224        
REMARK   3    10  2.3302 -  2.2498    1.00     2708   124  0.1501 0.1982        
REMARK   3    11  2.2498 -  2.1795    0.99     2707   163  0.1482 0.2135        
REMARK   3    12  2.1795 -  2.1172    1.00     2741   126  0.1493 0.1880        
REMARK   3    13  2.1172 -  2.0614    0.99     2662   154  0.1475 0.2162        
REMARK   3    14  2.0614 -  2.0111    0.99     2708   138  0.1566 0.1863        
REMARK   3    15  2.0111 -  1.9700    0.96     2571   138  0.1657 0.2421        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.172            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.746           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.18                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.08                          
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      :  0.007           4702                                  
REMARK   3   ANGLE     :  0.812           6360                                  
REMARK   3   CHIRALITY :  0.056            701                                  
REMARK   3   PLANARITY :  0.006            832                                  
REMARK   3   DIHEDRAL  :  4.805           3972                                  
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 7D78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300018870.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL18U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43010                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.960                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 26.4400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
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: SAD                          
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MIB, 25% PEG 1500, PH 7.0, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289.2K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       89.35350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.78450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       89.35350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.78450            
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: 4880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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 CL    CL D 404  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D 552  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     GLY A   302                                                      
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   O    HOH D   563     O    HOH D   598              2.06            
REMARK 500   O    HOH D   529     O    HOH D   598              2.06            
REMARK 500   O    HOH D   715     O    HOH D   735              2.07            
REMARK 500   O    HOH A   542     O    HOH A   735              2.10            
REMARK 500   OE1  GLU D    11     O    HOH D   501              2.15            
REMARK 500   O    HOH D   504     O    HOH A   593              2.17            
REMARK 500   O    HOH D   501     O    HOH D   726              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    LEU D  47      -44.53     69.48                                   
REMARK 500    SER D 114     -133.58     62.60                                   
REMARK 500    CYS D 137       55.02     39.02                                   
REMARK 500    PHE D 142      -37.93   -140.63                                   
REMARK 500    VAL D 202       33.22    -80.57                                   
REMARK 500    LEU D 246       41.33   -106.28                                   
REMARK 500    VAL D 300       75.22   -113.32                                   
REMARK 500    LEU A  47      -48.07     67.09                                   
REMARK 500    SER A 114     -136.84     59.52                                   
REMARK 500    CYS A 137       56.58     36.42                                   
REMARK 500    PHE A 142      -44.34   -142.31                                   
REMARK 500    ASN A 209        8.13    -67.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 146   O                                                      
REMARK 620 2 HOH D 624   O    68.8                                              
REMARK 620 3 HOH D 728   O   122.2  98.3                                        
REMARK 620 N                    1     2                                         
DBREF  7D78 D    1   302  UNP    J4WAT9   J4WAT9_BEAB2    17    318             
DBREF  7D78 A    1   302  UNP    J4WAT9   J4WAT9_BEAB2    17    318             
SEQADV 7D78 MET D  -19  UNP  J4WAT9              INITIATING METHIONINE          
SEQADV 7D78 GLY D  -18  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER D  -17  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER D  -16  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS D  -15  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS D  -14  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS D  -13  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS D  -12  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS D  -11  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS D  -10  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER D   -9  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER D   -8  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 GLY D   -7  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 LEU D   -6  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 VAL D   -5  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 PRO D   -4  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 ARG D   -3  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 GLY D   -2  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER D   -1  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS D    0  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 MET A  -19  UNP  J4WAT9              INITIATING METHIONINE          
SEQADV 7D78 GLY A  -18  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER A  -17  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER A  -16  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS A  -15  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS A  -14  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS A  -13  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS A  -12  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS A  -11  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS A  -10  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER A   -9  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER A   -8  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 GLY A   -7  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 LEU A   -6  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 VAL A   -5  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 PRO A   -4  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 ARG A   -3  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 GLY A   -2  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 SER A   -1  UNP  J4WAT9              EXPRESSION TAG                 
SEQADV 7D78 HIS A    0  UNP  J4WAT9              EXPRESSION TAG                 
SEQRES   1 D  322  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  322  LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU SER SER          
SEQRES   3 D  322  PHE GLN VAL VAL GLU CYS LYS THR ILE ASP GLY ILE ILE          
SEQRES   4 D  322  ILE ARG GLY ARG PHE TYR ALA VAL ASP GLY LYS GLY PRO          
SEQRES   5 D  322  ALA ILE ILE MET THR PRO GLY PHE ASN CYS VAL LYS GLU          
SEQRES   6 D  322  MET LEU LEU PRO ASP ILE ALA GLU THR PHE GLN SER GLN          
SEQRES   7 D  322  GLY PHE ASN THR TYR ILE TYR ASP PRO ARG SER ILE GLY          
SEQRES   8 D  322  ASP SER ASP GLY SER PRO LYS ASN LEU ILE ASP PRO LEU          
SEQRES   9 D  322  GLN GLN ALA GLU ASP LEU ALA ASP ILE VAL THR HIS ILE          
SEQRES  10 D  322  SER SER LEU PRO SER VAL ASP SER SER LYS ILE THR LEU          
SEQRES  11 D  322  TRP GLY MET SER PHE GLY GLY THR VAL SER ALA CYS ALA          
SEQRES  12 D  322  ALA ALA VAL ASP ARG ARG VAL LYS ALA LEU VAL MET VAL          
SEQRES  13 D  322  CYS PRO ILE LEU SER PHE TYR GLN ALA GLU LYS ARG ASP          
SEQRES  14 D  322  LYS ALA PHE LEU GLN LEU ILE ARG ASP ARG GLN SER GLN          
SEQRES  15 D  322  LEU ARG GLY ASN GLU PRO PHE MET LEU PRO PRO PHE ASN          
SEQRES  16 D  322  SER LYS GLY GLU ASN PRO ILE GLY MET ALA GLY SER GLY          
SEQRES  17 D  322  GLY PRO GLY GLY ILE GLU ALA TYR GLY PHE MET GLY ALA          
SEQRES  18 D  322  VAL ILE ASP ARG GLY ALA PRO ASN PHE ARG ASN LYS ILE          
SEQRES  19 D  322  ALA LEU GLN THR TYR GLN LYS LEU ALA TRP TRP GLN PRO          
SEQRES  20 D  322  LYS GLU ILE LEU LYS LEU VAL ASP LYS THR PRO VAL LEU          
SEQRES  21 D  322  MET VAL THR PRO GLU LEU ASP THR MET SER PRO PRO GLU          
SEQRES  22 D  322  GLU GLN LYS ALA ALA PHE GLU LEU PHE PRO GLN THR LYS          
SEQRES  23 D  322  LYS PHE LEU GLU ALA LYS GLY LYS GLY HIS LEU THR VAL          
SEQRES  24 D  322  LEU SER GLY GLU GLY SER VAL GLU VAL VAL ASP ALA MET          
SEQRES  25 D  322  THR GLU PHE ILE ARG GLU ASN VAL ALA GLY                      
SEQRES   1 A  322  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  322  LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU SER SER          
SEQRES   3 A  322  PHE GLN VAL VAL GLU CYS LYS THR ILE ASP GLY ILE ILE          
SEQRES   4 A  322  ILE ARG GLY ARG PHE TYR ALA VAL ASP GLY LYS GLY PRO          
SEQRES   5 A  322  ALA ILE ILE MET THR PRO GLY PHE ASN CYS VAL LYS GLU          
SEQRES   6 A  322  MET LEU LEU PRO ASP ILE ALA GLU THR PHE GLN SER GLN          
SEQRES   7 A  322  GLY PHE ASN THR TYR ILE TYR ASP PRO ARG SER ILE GLY          
SEQRES   8 A  322  ASP SER ASP GLY SER PRO LYS ASN LEU ILE ASP PRO LEU          
SEQRES   9 A  322  GLN GLN ALA GLU ASP LEU ALA ASP ILE VAL THR HIS ILE          
SEQRES  10 A  322  SER SER LEU PRO SER VAL ASP SER SER LYS ILE THR LEU          
SEQRES  11 A  322  TRP GLY MET SER PHE GLY GLY THR VAL SER ALA CYS ALA          
SEQRES  12 A  322  ALA ALA VAL ASP ARG ARG VAL LYS ALA LEU VAL MET VAL          
SEQRES  13 A  322  CYS PRO ILE LEU SER PHE TYR GLN ALA GLU LYS ARG ASP          
SEQRES  14 A  322  LYS ALA PHE LEU GLN LEU ILE ARG ASP ARG GLN SER GLN          
SEQRES  15 A  322  LEU ARG GLY ASN GLU PRO PHE MET LEU PRO PRO PHE ASN          
SEQRES  16 A  322  SER LYS GLY GLU ASN PRO ILE GLY MET ALA GLY SER GLY          
SEQRES  17 A  322  GLY PRO GLY GLY ILE GLU ALA TYR GLY PHE MET GLY ALA          
SEQRES  18 A  322  VAL ILE ASP ARG GLY ALA PRO ASN PHE ARG ASN LYS ILE          
SEQRES  19 A  322  ALA LEU GLN THR TYR GLN LYS LEU ALA TRP TRP GLN PRO          
SEQRES  20 A  322  LYS GLU ILE LEU LYS LEU VAL ASP LYS THR PRO VAL LEU          
SEQRES  21 A  322  MET VAL THR PRO GLU LEU ASP THR MET SER PRO PRO GLU          
SEQRES  22 A  322  GLU GLN LYS ALA ALA PHE GLU LEU PHE PRO GLN THR LYS          
SEQRES  23 A  322  LYS PHE LEU GLU ALA LYS GLY LYS GLY HIS LEU THR VAL          
SEQRES  24 A  322  LEU SER GLY GLU GLY SER VAL GLU VAL VAL ASP ALA MET          
SEQRES  25 A  322  THR GLU PHE ILE ARG GLU ASN VAL ALA GLY                      
HET     NA  D 401       1                                                       
HET    GOL  D 402       6                                                       
HET     CL  D 403       1                                                       
HET     CL  D 404       1                                                       
HET    GOL  A 401       6                                                       
HET    GOL  A 402       6                                                       
HET    EDO  A 403       4                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   9  EDO    C2 H6 O2                                                     
FORMUL  10  HOH   *524(H2 O)                                                    
HELIX    1 AA1 LEU D   47  GLN D   58  1                                  12    
HELIX    2 AA2 ASP D   82  SER D   99  1                                  18    
HELIX    3 AA3 SER D  114  ASP D  127  1                                  14    
HELIX    4 AA4 GLN D  144  GLU D  146  5                                   3    
HELIX    5 AA5 LYS D  147  ARG D  164  1                                  18    
HELIX    6 AA6 GLY D  189  ALA D  201  1                                  13    
HELIX    7 AA7 GLN D  217  TRP D  225  1                                   9    
HELIX    8 AA8 GLN D  226  LYS D  232  1                                   7    
HELIX    9 AA9 PRO D  251  PHE D  262  1                                  12    
HELIX   10 AB1 GLY D  284  VAL D  300  1                                  17    
HELIX   11 AB2 LEU A   47  GLN A   58  1                                  12    
HELIX   12 AB3 ASP A   82  LEU A  100  1                                  19    
HELIX   13 AB4 SER A  114  ASP A  127  1                                  14    
HELIX   14 AB5 GLN A  144  GLU A  146  5                                   3    
HELIX   15 AB6 LYS A  147  ARG A  164  1                                  18    
HELIX   16 AB7 GLY A  189  ALA A  201  1                                  13    
HELIX   17 AB8 VAL A  202  GLY A  206  5                                   5    
HELIX   18 AB9 GLN A  217  TRP A  225  1                                   9    
HELIX   19 AC1 GLN A  226  LYS A  232  1                                   7    
HELIX   20 AC2 PRO A  251  PHE A  262  1                                  12    
HELIX   21 AC3 GLY A  284  VAL A  300  1                                  17    
SHEET    1 AA1 8 GLN D   8  LYS D  13  0                                        
SHEET    2 AA1 8 ILE D  19  TYR D  25 -1  O  PHE D  24   N  GLN D   8           
SHEET    3 AA1 8 ASN D  61  ASP D  66 -1  O  THR D  62   N  TYR D  25           
SHEET    4 AA1 8 GLY D  31  THR D  37  1  N  MET D  36   O  TYR D  63           
SHEET    5 AA1 8 VAL D 103  MET D 113  1  O  TRP D 111   N  ILE D  35           
SHEET    6 AA1 8 VAL D 130  VAL D 136  1  O  LYS D 131   N  ILE D 108           
SHEET    7 AA1 8 VAL D 239  PRO D 244  1  O  LEU D 240   N  MET D 135           
SHEET    8 AA1 8 LYS D 266  ALA D 271  1  O  LEU D 269   N  THR D 243           
SHEET    1 AA2 2 MET D 170  LEU D 171  0                                        
SHEET    2 AA2 2 ILE D 214  ALA D 215 -1  O  ILE D 214   N  LEU D 171           
SHEET    1 AA3 8 GLN A   8  LYS A  13  0                                        
SHEET    2 AA3 8 ILE A  19  TYR A  25 -1  O  PHE A  24   N  GLN A   8           
SHEET    3 AA3 8 ASN A  61  TYR A  65 -1  O  THR A  62   N  TYR A  25           
SHEET    4 AA3 8 GLY A  31  THR A  37  1  N  MET A  36   O  TYR A  63           
SHEET    5 AA3 8 VAL A 103  MET A 113  1  O  ASP A 104   N  GLY A  31           
SHEET    6 AA3 8 VAL A 130  VAL A 136  1  O  LYS A 131   N  ILE A 108           
SHEET    7 AA3 8 VAL A 239  PRO A 244  1  O  LEU A 240   N  MET A 135           
SHEET    8 AA3 8 LYS A 266  ALA A 271  1  O  LEU A 269   N  MET A 241           
SHEET    1 AA4 2 MET A 170  LEU A 171  0                                        
SHEET    2 AA4 2 ILE A 214  ALA A 215 -1  O  ILE A 214   N  LEU A 171           
LINK         O   GLU D 146                NA    NA D 401     1555   1555  2.82  
LINK        NA    NA D 401                 O   HOH D 624     1555   1555  3.14  
LINK        NA    NA D 401                 O   HOH D 728     1555   1555  3.00  
CISPEP   1 SER D   76    PRO D   77          0        -0.05                     
CISPEP   2 SER A   76    PRO A   77          0         0.02                     
CRYST1  178.707   47.569   71.695  90.00  93.19  90.00 C 1 2 1       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      0.005596  0.000000  0.000312        0.00000                         
SCALE2      0.000000  0.021022  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013970        0.00000                         
TER    2306      GLY D 302                                                      
TER    4584      VAL A 300                                                      
MASTER      331    0    7   21   20    0    0    6 5100    2   26   50          
END                                                                             

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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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