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LongText Report for: 5DJ5-pdb

Name Class
5DJ5-pdb
HEADER    HYDROLASE                               01-SEP-15   5DJ5              
TITLE     CRYSTAL STRUCTURE OF RICE DWARF14 IN COMPLEX WITH SYNTHETIC           
TITLE    2 STRIGOLACTONE GR24                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE STRIGOLACTONE ESTERASE D14;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ALPHA/BETA HYDROLASE RESIDUES 52-318;                      
COMPND   5 SYNONYM: PROTEIN DWARF-14,PROTEIN DWARF-88,PROTEIN HIGH-TILLERING    
COMPND   6 DWARF 2;                                                             
COMPND   7 EC: 3.1.-.-;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA SUBSP. JAPONICA;                   
SOURCE   3 ORGANISM_COMMON: RICE;                                               
SOURCE   4 ORGANISM_TAXID: 39947;                                               
SOURCE   5 GENE: D14, D88, HTD2, OS03G0203200, LOC_OS03G10620;                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSUMO                                     
KEYWDS    ALPHA/BETA, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.E.ZHOU,L.-H.ZHAO,W.YI,Z.-S.WU,Y.LIU,Y.KANG,L.HOU,P.W.DE WAAL,S.LI,  
AUTHOR   2 Y.JIANG,K.MELCHER,H.E.XU                                             
REVDAT   1   28-OCT-15 5DJ5    0                                                
JRNL        AUTH   L.H.ZHAO,X.E.ZHOU,W.YI,Z.WU,Y.LIU,Y.KANG,L.HOU,P.W.DE WAAL,  
JRNL        AUTH 2 S.LI,Y.JIANG,A.SCAFFIDI,G.R.FLEMATTI,S.M.SMITH,V.Q.LAM,      
JRNL        AUTH 3 P.R.GRIFFIN,Y.WANG,J.LI,K.MELCHER,H.E.XU                     
JRNL        TITL   DESTABILIZATION OF STRIGOLACTONE RECEPTOR DWARF14 BY BINDING 
JRNL        TITL 2 OF LIGAND AND E3-LIGASE SIGNALING EFFECTOR DWARF3.           
JRNL        REF    CELL RES.                                  2015              
JRNL        REFN                   ISSN 1001-0602                               
JRNL        PMID   26470846                                                     
JRNL        DOI    10.1038/CR.2015.122                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17868                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1254                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.90                                          
REMARK   3   SHRINKAGE RADIUS   : 0.60                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.740           
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           4258                                  
REMARK   3   ANGLE     :  1.147           5811                                  
REMARK   3   CHIRALITY :  0.123            672                                  
REMARK   3   PLANARITY :  0.006            753                                  
REMARK   3   DIHEDRAL  : 12.713           1533                                  
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 5DJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213301.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17932                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.202                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13600                            
REMARK 200   FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.65400                            
REMARK 200   FOR SHELL         : 1.100                              
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: 4IH9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, ETHYLENE GLYCOL, PH 7.5,        
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
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       24.20000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.28500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.94000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.28500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.20000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.94000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     2                                                      
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    ALA B     4     O    HOH B   301              2.18            
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  97     -117.42     57.59                                   
REMARK 500    SER B  97     -116.21     56.76                                   
REMARK 500    THR B 244      164.69    173.81                                   
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 B 397        DISTANCE =  6.60 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GR2 A 800                 
DBREF  5DJ5 A    2   268  UNP    Q10QA5   D14_ORYSJ       52    318             
DBREF  5DJ5 B    2   268  UNP    Q10QA5   D14_ORYSJ       52    318             
SEQRES   1 A  267  SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL          
SEQRES   2 A  267  VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY          
SEQRES   3 A  267  PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO          
SEQRES   4 A  267  TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU          
SEQRES   5 A  267  VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE          
SEQRES   6 A  267  ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU          
SEQRES   7 A  267  LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA          
SEQRES   8 A  267  PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU          
SEQRES   9 A  267  ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL          
SEQRES  10 A  267  LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP          
SEQRES  11 A  267  TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL          
SEQRES  12 A  267  PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR          
SEQRES  13 A  267  GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA          
SEQRES  14 A  267  ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG          
SEQRES  15 A  267  PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS          
SEQRES  16 A  267  THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO          
SEQRES  17 A  267  CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO          
SEQRES  18 A  267  ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY          
SEQRES  19 A  267  ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU          
SEQRES  20 A  267  PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU          
SEQRES  21 A  267  ARG ARG ALA LEU ALA ARG TYR                                  
SEQRES   1 B  267  SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL          
SEQRES   2 B  267  VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY          
SEQRES   3 B  267  PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO          
SEQRES   4 B  267  TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU          
SEQRES   5 B  267  VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE          
SEQRES   6 B  267  ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU          
SEQRES   7 B  267  LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA          
SEQRES   8 B  267  PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU          
SEQRES   9 B  267  ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL          
SEQRES  10 B  267  LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP          
SEQRES  11 B  267  TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL          
SEQRES  12 B  267  PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR          
SEQRES  13 B  267  GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA          
SEQRES  14 B  267  ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG          
SEQRES  15 B  267  PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS          
SEQRES  16 B  267  THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO          
SEQRES  17 B  267  CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO          
SEQRES  18 B  267  ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY          
SEQRES  19 B  267  ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU          
SEQRES  20 B  267  PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU          
SEQRES  21 B  267  ARG ARG ALA LEU ALA ARG TYR                                  
HET    GR2  A 800      22                                                       
HETNAM     GR2 (3E,3AR,8BS)-3-({[(2R)-4-METHYL-5-OXO-2,5-DIHYDROFURAN-          
HETNAM   2 GR2  2-YL]OXY}METHYLIDENE)-3,3A,4,8B-TETRAHYDRO-2H-                  
HETNAM   3 GR2  INDENO[1,2-B]FURAN-2-ONE                                        
FORMUL   3  GR2    C17 H14 O5                                                   
FORMUL   4  HOH   *163(H2 O)                                                    
HELIX    1 AA1 GLY A    3  LEU A   10  1                                   8    
HELIX    2 AA2 ASP A   31  SER A   36  5                                   6    
HELIX    3 AA3 VAL A   38  THR A   43  1                                   6    
HELIX    4 AA4 ASN A   60  PHE A   64  5                                   5    
HELIX    5 AA5 ARG A   67  ASN A   71  5                                   5    
HELIX    6 AA6 LEU A   72  LEU A   86  1                                  15    
HELIX    7 AA7 SER A   97  ARG A  110  1                                  14    
HELIX    8 AA8 GLU A  137  ASN A  151  1                                  15    
HELIX    9 AA9 ASN A  151  GLY A  165  1                                  15    
HELIX   10 AB1 VAL A  168  ASN A  181  1                                  14    
HELIX   11 AB2 ARG A  183  LYS A  196  1                                  14    
HELIX   12 AB3 LEU A  199  VAL A  206  5                                   8    
HELIX   13 AB4 PRO A  222  LEU A  233  1                                  12    
HELIX   14 AB5 LEU A  248  ALA A  253  1                                   6    
HELIX   15 AB6 ALA A  253  LEU A  265  1                                  13    
HELIX   16 AB7 GLY B    3  LEU B   10  1                                   8    
HELIX   17 AB8 ASP B   31  SER B   36  5                                   6    
HELIX   18 AB9 VAL B   38  ARG B   44  1                                   7    
HELIX   19 AC1 ASN B   60  PHE B   64  5                                   5    
HELIX   20 AC2 ARG B   67  ASP B   70  5                                   4    
HELIX   21 AC3 ASN B   71  LEU B   86  1                                  16    
HELIX   22 AC4 SER B   97  ARG B  110  1                                  14    
HELIX   23 AC5 GLU B  137  ASN B  151  1                                  15    
HELIX   24 AC6 ASN B  151  GLY B  165  1                                  15    
HELIX   25 AC7 VAL B  168  ASN B  181  1                                  14    
HELIX   26 AC8 ARG B  183  LYS B  196  1                                  14    
HELIX   27 AC9 LEU B  199  VAL B  206  5                                   8    
HELIX   28 AD1 PRO B  222  LEU B  233  1                                  12    
HELIX   29 AD2 LEU B  248  ALA B  253  1                                   6    
HELIX   30 AD3 ALA B  253  LEU B  265  1                                  13    
SHEET    1 AA1 7 ARG A  13  VAL A  15  0                                        
SHEET    2 AA1 7 HIS A  46  LEU A  50 -1  O  VAL A  48   N  VAL A  15           
SHEET    3 AA1 7 ARG A  20  SER A  25  1  N  ARG A  20   O  ARG A  47           
SHEET    4 AA1 7 CYS A  91  HIS A  96  1  O  VAL A  94   N  VAL A  23           
SHEET    5 AA1 7 PHE A 114  ILE A 120  1  O  ALA A 115   N  CYS A  91           
SHEET    6 AA1 7 CYS A 210  GLN A 214  1  O  VAL A 213   N  LEU A 119           
SHEET    7 AA1 7 THR A 237  PHE A 241  1  O  THR A 238   N  VAL A 212           
SHEET    1 AA2 7 ARG B  13  GLY B  16  0                                        
SHEET    2 AA2 7 ARG B  47  LEU B  50 -1  O  VAL B  48   N  VAL B  15           
SHEET    3 AA2 7 VAL B  21  SER B  25  1  N  VAL B  22   O  VAL B  49           
SHEET    4 AA2 7 CYS B  91  HIS B  96  1  O  VAL B  94   N  VAL B  23           
SHEET    5 AA2 7 PHE B 114  ILE B 120  1  O  VAL B 118   N  PHE B  93           
SHEET    6 AA2 7 CYS B 210  GLN B 214  1  O  VAL B 213   N  LEU B 119           
SHEET    7 AA2 7 THR B 237  PHE B 241  1  O  THR B 238   N  VAL B 212           
SITE     1 AC1  9 PHE A  28  SER A  97  VAL A  98  VAL A 144                    
SITE     2 AC1  9 TYR A 159  CYS A 191  VAL A 219  SER A 220                    
SITE     3 AC1  9 HIS A 247                                                     
CRYST1   48.400   87.880  118.570  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      0.020661  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011379  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008434        0.00000                         
TER    2068      TYR A 268                                                      
TER    4139      TYR B 268                                                      
MASTER      253    0    1   30   14    0    3    6 4301    2   22   42          
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.
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