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LongText Report for: 5zhr-pdb

Name Class
5zhr-pdb
HEADER    HYDROLASE                               13-MAR-18   5ZHR              
TITLE     CRYSTAL STRUCTURE OF OSD14 IN COMPLEX WITH COVALENTLY BOUND KK094     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STRIGOLACTONE ESTERASE D14;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEIN DWARF 14,PROTEIN DWARF 88,PROTEIN HIGH-TILLERING    
COMPND   5 DWARF 2;                                                             
COMPND   6 EC: 3.1.-.-;                                                         
COMPND   7 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: 562                                         
KEYWDS    PLANT HORMONES, PLANT SIGNALLING, STRIGOLACTONES, RECEPTOR, HYDROLASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HIRABAYASHI,T.MIYAKAWA,M.TANOKURA                                   
REVDAT   1   21-NOV-18 5ZHR    0                                                
JRNL        AUTH   H.NAKAMURA,K.HIRABAYASHI,T.MIYAKAWA,K.KIKUZATO,W.HU,Y.XU,    
JRNL        AUTH 2 K.JIANG,I.TAKAHASHI,R.NIIYAMA,N.DOHMAE,M.TANOKURA,T.ASAMI    
JRNL        TITL   TRIAZOLE UREAS COVALENTLY BIND TO STRIGOLACTONE RECEPTOR AND 
JRNL        TITL 2 ANTAGONIZE STRIGOLACTONE RESPONSES.                          
JRNL        REF    MOL PLANT                                  2018              
JRNL        REFN                   ESSN 1752-9867                               
JRNL        PMID   30391752                                                     
JRNL        DOI    10.1016/J.MOLP.2018.10.006                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 173170                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3809                            
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 49.5396 -  4.3490    1.00     6328   141  0.1547 0.1783        
REMARK   3     2  4.3490 -  3.4522    1.00     6353   142  0.1492 0.2026        
REMARK   3     3  3.4522 -  3.0159    1.00     6354   143  0.1636 0.1873        
REMARK   3     4  3.0159 -  2.7402    1.00     6349   143  0.1700 0.1827        
REMARK   3     5  2.7402 -  2.5438    1.00     6367   145  0.1669 0.1896        
REMARK   3     6  2.5438 -  2.3938    1.00     6335   136  0.1673 0.2006        
REMARK   3     7  2.3938 -  2.2739    1.00     6370   149  0.1636 0.1966        
REMARK   3     8  2.2739 -  2.1749    1.00     6372   139  0.1668 0.2230        
REMARK   3     9  2.1749 -  2.0912    1.00     6347   147  0.1636 0.1870        
REMARK   3    10  2.0912 -  2.0190    1.00     6319   137  0.1659 0.2062        
REMARK   3    11  2.0190 -  1.9559    1.00     6370   140  0.1654 0.2085        
REMARK   3    12  1.9559 -  1.9000    1.00     6386   147  0.1666 0.1937        
REMARK   3    13  1.9000 -  1.8500    1.00     6317   144  0.1687 0.2187        
REMARK   3    14  1.8500 -  1.8048    1.00     6336   142  0.1713 0.1950        
REMARK   3    15  1.8048 -  1.7638    1.00     6414   149  0.1754 0.2067        
REMARK   3    16  1.7638 -  1.7263    1.00     6305   144  0.1734 0.2213        
REMARK   3    17  1.7263 -  1.6917    1.00     6387   143  0.1684 0.2106        
REMARK   3    18  1.6917 -  1.6598    1.00     6304   143  0.1689 0.2138        
REMARK   3    19  1.6598 -  1.6302    1.00     6385   141  0.1731 0.2180        
REMARK   3    20  1.6302 -  1.6025    1.00     6314   146  0.1675 0.1682        
REMARK   3    21  1.6025 -  1.5767    1.00     6414   146  0.1697 0.2145        
REMARK   3    22  1.5767 -  1.5524    1.00     6250   143  0.1755 0.2309        
REMARK   3    23  1.5524 -  1.5296    1.00     6402   142  0.1825 0.1897        
REMARK   3    24  1.5296 -  1.5080    1.00     6324   139  0.1905 0.2160        
REMARK   3    25  1.5080 -  1.4877    0.98     6267   142  0.1965 0.2287        
REMARK   3    26  1.4877 -  1.4683    0.88     5609   127  0.2157 0.2221        
REMARK   3    27  1.4683 -  1.4500    0.80     5083   109  0.2280 0.2750        
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)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.220           
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      :  0.009           4218                                  
REMARK   3   ANGLE     :  1.215           5748                                  
REMARK   3   CHIRALITY :  0.051            662                                  
REMARK   3   PLANARITY :  0.007            744                                  
REMARK   3   DIHEDRAL  : 11.996           1508                                  
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 5ZHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007101.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-1A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : CRYO-COOLED CHANNEL-CUT SI(111)    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 173170                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.511                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 9.300                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 26.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.900                              
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: 3VXK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR            
REMARK 280  DIFFUSION, SITTING 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       24.12500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.69000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.32000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.69000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.12500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.32000            
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 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 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     GLY A    45                                                      
REMARK 465     PRO A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     TYR A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     ASN A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     PRO B    46                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     TYR B    48                                                      
REMARK 465     GLN B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     PRO B    51                                                      
REMARK 465     ASN B    52                                                      
REMARK 465     SER B    53                                                      
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 147     -119.63     58.33                                   
REMARK 500    ARG A 175      121.40   -170.86                                   
REMARK 500    ASN A 201       78.97   -162.73                                   
REMARK 500    GLN A 293       31.82    -88.02                                   
REMARK 500    ALA A 303       55.79   -145.72                                   
REMARK 500    ASP B  81     -167.83   -126.77                                   
REMARK 500    SER B 147     -118.92     57.56                                   
REMARK 500    ARG B 175      120.98   -171.57                                   
REMARK 500    ASP B 181       -8.01     61.50                                   
REMARK 500    ASN B 201       85.26   -154.24                                   
REMARK 500    ALA B 303       57.21   -141.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 883        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B 843        DISTANCE =  6.63 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KOK A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide KOK B 500 and SER B    
REMARK 800  147                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5YZ7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH DIFFERENT LIGAND                               
REMARK 900 RELATED ID: 3VXK   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN (LIGAND-FREE STRUCTURE)                             
REMARK 900 RELATED ID: 3WIO   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH DIFFERENT LIGAND                               
DBREF  5ZHR A   54   318  UNP    Q10QA5   D14_ORYSJ       54    318             
DBREF  5ZHR B   54   318  UNP    Q10QA5   D14_ORYSJ       54    318             
SEQADV 5ZHR GLY A   45  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR PRO A   46  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR GLY A   47  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR TYR A   48  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR GLN A   49  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR ASP A   50  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR PRO A   51  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR ASN A   52  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR SER A   53  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR GLY B   45  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR PRO B   46  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR GLY B   47  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR TYR B   48  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR GLN B   49  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR ASP B   50  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR PRO B   51  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR ASN B   52  UNP  Q10QA5              EXPRESSION TAG                 
SEQADV 5ZHR SER B   53  UNP  Q10QA5              EXPRESSION TAG                 
SEQRES   1 A  274  GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU          
SEQRES   2 A  274  GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG          
SEQRES   3 A  274  VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER          
SEQRES   4 A  274  ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS          
SEQRES   5 A  274  ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL          
SEQRES   6 A  274  ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU          
SEQRES   7 A  274  ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA          
SEQRES   8 A  274  LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL          
SEQRES   9 A  274  SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO          
SEQRES  10 A  274  ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO          
SEQRES  11 A  274  ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU          
SEQRES  12 A  274  LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA          
SEQRES  13 A  274  ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA          
SEQRES  14 A  274  VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER          
SEQRES  15 A  274  ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS          
SEQRES  16 A  274  VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL          
SEQRES  17 A  274  LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR          
SEQRES  18 A  274  THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR          
SEQRES  19 A  274  LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE          
SEQRES  20 A  274  LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO          
SEQRES  21 A  274  SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG          
SEQRES  22 A  274  TYR                                                          
SEQRES   1 B  274  GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU          
SEQRES   2 B  274  GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG          
SEQRES   3 B  274  VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER          
SEQRES   4 B  274  ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS          
SEQRES   5 B  274  ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL          
SEQRES   6 B  274  ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU          
SEQRES   7 B  274  ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA          
SEQRES   8 B  274  LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL          
SEQRES   9 B  274  SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO          
SEQRES  10 B  274  ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO          
SEQRES  11 B  274  ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU          
SEQRES  12 B  274  LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA          
SEQRES  13 B  274  ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA          
SEQRES  14 B  274  VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER          
SEQRES  15 B  274  ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS          
SEQRES  16 B  274  VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL          
SEQRES  17 B  274  LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR          
SEQRES  18 B  274  THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR          
SEQRES  19 B  274  LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE          
SEQRES  20 B  274  LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO          
SEQRES  21 B  274  SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG          
SEQRES  22 B  274  TYR                                                          
HET    KOK  A 500      11                                                       
HET    KOK  B 500      11                                                       
HETNAM     KOK (2,3-DIHYDRO-1H-INDOL-1-YL)(1H-1,2,3-TRIAZOL-1-YL)               
HETNAM   2 KOK  METHANONE                                                       
FORMUL   3  KOK    2(C11 H10 N4 O)                                              
FORMUL   5  HOH   *526(H2 O)                                                    
HELIX    1 AA1 ALA A   54  LEU A   60  1                                   7    
HELIX    2 AA2 ASP A   81  SER A   86  5                                   6    
HELIX    3 AA3 VAL A   88  LEU A   92  5                                   5    
HELIX    4 AA4 ASN A  110  PHE A  114  5                                   5    
HELIX    5 AA5 ARG A  117  ASP A  120  5                                   4    
HELIX    6 AA6 ASN A  121  LEU A  136  1                                  16    
HELIX    7 AA7 SER A  147  ARG A  160  1                                  14    
HELIX    8 AA8 GLU A  187  ASN A  201  1                                  15    
HELIX    9 AA9 ASN A  201  GLY A  215  1                                  15    
HELIX   10 AB1 VAL A  218  MET A  232  1                                  15    
HELIX   11 AB2 ARG A  233  THR A  247  1                                  15    
HELIX   12 AB3 LEU A  249  VAL A  256  5                                   8    
HELIX   13 AB4 SER A  274  LEU A  283  1                                  10    
HELIX   14 AB5 LEU A  298  ALA A  303  1                                   6    
HELIX   15 AB6 ALA A  303  LEU A  315  1                                  13    
HELIX   16 AB7 LYS B   55  LEU B   60  1                                   6    
HELIX   17 AB8 ASP B   81  SER B   86  5                                   6    
HELIX   18 AB9 VAL B   88  LEU B   92  5                                   5    
HELIX   19 AC1 ASN B  110  PHE B  114  5                                   5    
HELIX   20 AC2 ARG B  117  ASP B  120  5                                   4    
HELIX   21 AC3 ASN B  121  LEU B  136  1                                  16    
HELIX   22 AC4 SER B  147  ARG B  160  1                                  14    
HELIX   23 AC5 GLU B  187  ASN B  201  1                                  15    
HELIX   24 AC6 ASN B  201  GLY B  215  1                                  15    
HELIX   25 AC7 VAL B  218  MET B  232  1                                  15    
HELIX   26 AC8 ARG B  233  LYS B  246  1                                  14    
HELIX   27 AC9 LEU B  249  VAL B  256  5                                   8    
HELIX   28 AD1 ALA B  273  LEU B  283  1                                  11    
HELIX   29 AD2 LEU B  298  ALA B  303  1                                   6    
HELIX   30 AD3 ALA B  303  LEU B  315  1                                  13    
SHEET    1 AA1 7 ARG A  63  GLY A  66  0                                        
SHEET    2 AA1 7 ARG A  97  LEU A 100 -1  O  VAL A  98   N  VAL A  65           
SHEET    3 AA1 7 VAL A  71  SER A  75  1  N  VAL A  72   O  ARG A  97           
SHEET    4 AA1 7 CYS A 141  HIS A 146  1  O  VAL A 144   N  VAL A  73           
SHEET    5 AA1 7 PHE A 164  ILE A 170  1  O  ALA A 165   N  CYS A 141           
SHEET    6 AA1 7 CYS A 260  GLN A 264  1  O  VAL A 261   N  LEU A 169           
SHEET    7 AA1 7 THR A 287  PHE A 291  1  O  THR A 288   N  VAL A 262           
SHEET    1 AA2 7 ARG B  63  GLY B  66  0                                        
SHEET    2 AA2 7 ARG B  97  LEU B 100 -1  O  VAL B  98   N  VAL B  65           
SHEET    3 AA2 7 VAL B  71  SER B  75  1  N  VAL B  72   O  VAL B  99           
SHEET    4 AA2 7 CYS B 141  HIS B 146  1  O  VAL B 144   N  VAL B  73           
SHEET    5 AA2 7 PHE B 164  ILE B 170  1  O  ALA B 165   N  CYS B 141           
SHEET    6 AA2 7 CYS B 260  GLN B 264  1  O  VAL B 263   N  LEU B 169           
SHEET    7 AA2 7 THR B 287  PHE B 291  1  O  GLU B 290   N  GLN B 264           
LINK         OG  SER A 147                 CAA KOK A 500     1555   1555  1.40  
LINK         OG  SER B 147                 CAA KOK B 500     1555   1555  1.37  
SITE     1 AC1  8 PHE A  78  SER A 147  VAL A 148  PHE A 176                    
SITE     2 AC1  8 VAL A 244  PHE A 245  SER A 270  HOH A 723                    
SITE     1 AC2 15 PHE B  78  HIS B 146  VAL B 148  SER B 149                    
SITE     2 AC2 15 ALA B 150  MET B 151  ILE B 170  GLY B 171                    
SITE     3 AC2 15 PHE B 176  VAL B 244  PHE B 245  SER B 270                    
SITE     4 AC2 15 HIS B 297  HOH B 689  HOH B 738                               
CRYST1   48.250   88.640  119.380  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      0.020725  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011282  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008377        0.00000                         
TER    2052      TYR A 318                                                      
TER    4104      TYR B 318                                                      
MASTER      305    0    2   30   14    0    6    6 4650    2   24   44          
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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