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LongText Report for: 3STU-pdb

Name Class
3STU-pdb
HEADER    HYDROLASE                               11-JUL-11   3STU              
TITLE     CRYSTAL STRUCTURE OF TOMATO METHYLKETONE SYNTHASE I COMPLEXED WITH    
TITLE    2 METHYL-3-HYDROXYDODECANOATE                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHYLKETONE SYNTHASE 1;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LYCOPERSICON HIRSUTUM F. GLABRATUM;             
SOURCE   3 ORGANISM_TAXID: 283673;                                              
SOURCE   4 GENE: MKS1;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHIS9GW                                   
KEYWDS    METHYLKETONE, ALPHA/BETA HYDROLASE, DECARBOXYLASE, HYDROLASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.AULDRIDGE,M.B.AUSTIN,J.P.NOEL                                     
REVDAT   1   02-MAY-12 3STU    0                                                
JRNL        AUTH   M.E.AULDRIDGE,Y.GUO,M.B.AUSTIN,J.RAMSEY,E.FRIDMAN,           
JRNL        AUTH 2 E.PICHERSKY,J.P.NOEL                                         
JRNL        TITL   EMERGENT DECARBOXYLASE ACTIVITY AND ATTENUATION OF           
JRNL        TITL 2 {ALPHA}/{BETA}-HYDROLASE ACTIVITY DURING THE EVOLUTION OF    
JRNL        TITL 3 METHYLKETONE BIOSYNTHESIS IN TOMATO                          
JRNL        REF    PLANT CELL                                 2012              
JRNL        REFN                   ESSN 1532-298X                               
JRNL        DOI    10.1105/TPC.111.093997                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 43407                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2186                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.93                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.4160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3969                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 246                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.149         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4099 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5567 ; 1.042 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   519 ; 5.179 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   146 ;33.864 ;25.068       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   707 ;12.943 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;11.222 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   654 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2986 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2594 ; 0.495 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4208 ; 0.939 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1505 ; 1.165 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1357 ; 1.959 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3STU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066643.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAY-05                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 24.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49900                            
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 7YAS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PIPES-NA+, 22% (W/V) PEG 8000,      
REMARK 280  0.3M NABR, 2MM DITHIOTHREITOL, 2 HR SOAK IN 1MM METHYL-3-           
REMARK 280  HYDROXYDODECANOATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
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       52.85800            
REMARK 290   SMTRY3   2  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: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     SER B     6                                                      
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    PHE A  20      -18.02     75.62                                   
REMARK 500    ALA A  87     -112.39     50.19                                   
REMARK 500    LEU A 136     -118.45     42.19                                   
REMARK 500    ARG A 201      -73.60   -101.32                                   
REMARK 500    ASP A 216       85.78   -151.16                                   
REMARK 500    VAL A 244       77.41   -107.80                                   
REMARK 500    TYR A 264       62.96   -113.75                                   
REMARK 500    PHE B  20      -16.20     76.87                                   
REMARK 500    ALA B  87     -109.78     47.18                                   
REMARK 500    LEU B 136     -114.81     46.70                                   
REMARK 500    ARG B 201      -77.93   -108.10                                   
REMARK 500    ASP B 242     -169.50    -79.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DKA A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DK3 B 266                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3STT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3STV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3STW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3STX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3STY   RELATED DB: PDB                                   
DBREF  3STU A    1   265  UNP    E0YCS2   E0YCS2_SOLHA     1    265             
DBREF  3STU B    1   265  UNP    E0YCS2   E0YCS2_SOLHA     1    265             
SEQADV 3STU GLY A   -1  UNP  E0YCS2              EXPRESSION TAG                 
SEQADV 3STU SER A    0  UNP  E0YCS2              EXPRESSION TAG                 
SEQADV 3STU GLY B   -1  UNP  E0YCS2              EXPRESSION TAG                 
SEQADV 3STU SER B    0  UNP  E0YCS2              EXPRESSION TAG                 
SEQRES   1 A  267  GLY SER MET GLU LYS SER MET SER PRO PHE VAL LYS LYS          
SEQRES   2 A  267  HIS PHE VAL LEU VAL HIS THR ALA PHE HIS GLY ALA TRP          
SEQRES   3 A  267  CYS TRP TYR LYS ILE VAL ALA LEU MET ARG SER SER GLY          
SEQRES   4 A  267  HIS ASN VAL THR ALA LEU ASP LEU GLY ALA SER GLY ILE          
SEQRES   5 A  267  ASN PRO LYS GLN ALA LEU GLN ILE PRO ASN PHE SER ASP          
SEQRES   6 A  267  TYR LEU SER PRO LEU MET GLU PHE MET ALA SER LEU PRO          
SEQRES   7 A  267  ALA ASN GLU LYS ILE ILE LEU VAL GLY HIS ALA LEU GLY          
SEQRES   8 A  267  GLY LEU ALA ILE SER LYS ALA MET GLU THR PHE PRO GLU          
SEQRES   9 A  267  LYS ILE SER VAL ALA VAL PHE LEU SER GLY LEU MET PRO          
SEQRES  10 A  267  GLY PRO ASN ILE ASP ALA THR THR VAL CYS THR LYS ALA          
SEQRES  11 A  267  GLY SER ALA VAL LEU GLY GLN LEU ASP ASN CYS VAL THR          
SEQRES  12 A  267  TYR GLU ASN GLY PRO THR ASN PRO PRO THR THR LEU ILE          
SEQRES  13 A  267  ALA GLY PRO LYS PHE LEU ALA THR ASN VAL TYR HIS LEU          
SEQRES  14 A  267  SER PRO ILE GLU ASP LEU ALA LEU ALA THR ALA LEU VAL          
SEQRES  15 A  267  ARG PRO LEU TYR LEU TYR LEU ALA GLU ASP ILE SER LYS          
SEQRES  16 A  267  GLU VAL VAL LEU SER SER LYS ARG TYR GLY SER VAL LYS          
SEQRES  17 A  267  ARG VAL PHE ILE VAL ALA THR GLU ASN ASP ALA LEU LYS          
SEQRES  18 A  267  LYS GLU PHE LEU LYS LEU MET ILE GLU LYS ASN PRO PRO          
SEQRES  19 A  267  ASP GLU VAL LYS GLU ILE GLU GLY SER ASP HIS VAL THR          
SEQRES  20 A  267  MET MET SER LYS PRO GLN GLN LEU PHE THR THR LEU LEU          
SEQRES  21 A  267  SER ILE ALA ASN LYS TYR LYS                                  
SEQRES   1 B  267  GLY SER MET GLU LYS SER MET SER PRO PHE VAL LYS LYS          
SEQRES   2 B  267  HIS PHE VAL LEU VAL HIS THR ALA PHE HIS GLY ALA TRP          
SEQRES   3 B  267  CYS TRP TYR LYS ILE VAL ALA LEU MET ARG SER SER GLY          
SEQRES   4 B  267  HIS ASN VAL THR ALA LEU ASP LEU GLY ALA SER GLY ILE          
SEQRES   5 B  267  ASN PRO LYS GLN ALA LEU GLN ILE PRO ASN PHE SER ASP          
SEQRES   6 B  267  TYR LEU SER PRO LEU MET GLU PHE MET ALA SER LEU PRO          
SEQRES   7 B  267  ALA ASN GLU LYS ILE ILE LEU VAL GLY HIS ALA LEU GLY          
SEQRES   8 B  267  GLY LEU ALA ILE SER LYS ALA MET GLU THR PHE PRO GLU          
SEQRES   9 B  267  LYS ILE SER VAL ALA VAL PHE LEU SER GLY LEU MET PRO          
SEQRES  10 B  267  GLY PRO ASN ILE ASP ALA THR THR VAL CYS THR LYS ALA          
SEQRES  11 B  267  GLY SER ALA VAL LEU GLY GLN LEU ASP ASN CYS VAL THR          
SEQRES  12 B  267  TYR GLU ASN GLY PRO THR ASN PRO PRO THR THR LEU ILE          
SEQRES  13 B  267  ALA GLY PRO LYS PHE LEU ALA THR ASN VAL TYR HIS LEU          
SEQRES  14 B  267  SER PRO ILE GLU ASP LEU ALA LEU ALA THR ALA LEU VAL          
SEQRES  15 B  267  ARG PRO LEU TYR LEU TYR LEU ALA GLU ASP ILE SER LYS          
SEQRES  16 B  267  GLU VAL VAL LEU SER SER LYS ARG TYR GLY SER VAL LYS          
SEQRES  17 B  267  ARG VAL PHE ILE VAL ALA THR GLU ASN ASP ALA LEU LYS          
SEQRES  18 B  267  LYS GLU PHE LEU LYS LEU MET ILE GLU LYS ASN PRO PRO          
SEQRES  19 B  267  ASP GLU VAL LYS GLU ILE GLU GLY SER ASP HIS VAL THR          
SEQRES  20 B  267  MET MET SER LYS PRO GLN GLN LEU PHE THR THR LEU LEU          
SEQRES  21 B  267  SER ILE ALA ASN LYS TYR LYS                                  
HET    DKA  A 266      12                                                       
HET    DK3  B 266      16                                                       
HETNAM     DKA DECANOIC ACID                                                    
HETNAM     DK3 METHYL (3S)-3-HYDROXYDODECANOATE                                 
FORMUL   3  DKA    C10 H20 O2                                                   
FORMUL   4  DK3    C13 H26 O3                                                   
FORMUL   5  HOH   *246(H2 O)                                                    
HELIX    1   1 GLY A   22  CYS A   25  5                                   4    
HELIX    2   2 TRP A   26  SER A   36  1                                  11    
HELIX    3   3 GLN A   54  ILE A   58  5                                   5    
HELIX    4   4 ASN A   60  SER A   74  1                                  15    
HELIX    5   5 LEU A   88  PHE A  100  1                                  13    
HELIX    6   6 ASP A  120  ALA A  131  1                                  12    
HELIX    7   7 GLY A  156  VAL A  164  1                                   9    
HELIX    8   8 PRO A  169  VAL A  180  1                                  12    
HELIX    9   9 LEU A  187  VAL A  195  1                                   9    
HELIX   10  10 ARG A  201  VAL A  205  5                                   5    
HELIX   11  11 ASP A  216  ASN A  230  1                                  15    
HELIX   12  12 VAL A  244  LYS A  249  1                                   6    
HELIX   13  13 LYS A  249  TYR A  264  1                                  16    
HELIX   14  14 GLY B   22  CYS B   25  5                                   4    
HELIX   15  15 TRP B   26  SER B   36  1                                  11    
HELIX   16  16 GLN B   54  ILE B   58  5                                   5    
HELIX   17  17 ASN B   60  SER B   74  1                                  15    
HELIX   18  18 LEU B   88  PHE B  100  1                                  13    
HELIX   19  19 ASP B  120  ALA B  131  1                                  12    
HELIX   20  20 GLY B  156  VAL B  164  1                                   9    
HELIX   21  21 PRO B  169  ALA B  178  1                                  10    
HELIX   22  22 LEU B  187  VAL B  195  1                                   9    
HELIX   23  23 ARG B  201  VAL B  205  5                                   5    
HELIX   24  24 LYS B  219  ASN B  230  1                                  12    
HELIX   25  25 VAL B  244  LYS B  249  1                                   6    
HELIX   26  26 LYS B  249  TYR B  264  1                                  16    
SHEET    1   A 6 ASN A  39  LEU A  43  0                                        
SHEET    2   A 6 HIS A  12  VAL A  16  1  N  LEU A  15   O  THR A  41           
SHEET    3   A 6 ILE A  81  HIS A  86  1  O  VAL A  84   N  VAL A  14           
SHEET    4   A 6 ILE A 104  LEU A 110  1  O  VAL A 108   N  LEU A  83           
SHEET    5   A 6 LYS A 206  VAL A 211  1  O  VAL A 208   N  PHE A 109           
SHEET    6   A 6 GLU A 234  GLU A 237  1  O  LYS A 236   N  VAL A 211           
SHEET    1   B 3 CYS A 139  THR A 141  0                                        
SHEET    2   B 3 THR A 152  ILE A 154 -1  O  ILE A 154   N  CYS A 139           
SHEET    3   B 3 LEU A 183  TYR A 184 -1  O  LEU A 183   N  LEU A 153           
SHEET    1   C 6 ASN B  39  LEU B  43  0                                        
SHEET    2   C 6 HIS B  12  VAL B  16  1  N  PHE B  13   O  ASN B  39           
SHEET    3   C 6 ILE B  81  HIS B  86  1  O  VAL B  84   N  VAL B  14           
SHEET    4   C 6 ILE B 104  LEU B 110  1  O  VAL B 108   N  LEU B  83           
SHEET    5   C 6 ARG B 207  ALA B 212  1  O  ILE B 210   N  PHE B 109           
SHEET    6   C 6 GLU B 234  ILE B 238  1  O  LYS B 236   N  PHE B 209           
SHEET    1   D 3 CYS B 139  THR B 141  0                                        
SHEET    2   D 3 THR B 152  ILE B 154 -1  O  ILE B 154   N  CYS B 139           
SHEET    3   D 3 LEU B 183  TYR B 184 -1  O  LEU B 183   N  LEU B 153           
SITE     1 AC1  5 THR A  18  CYS A 125  TYR A 186  HIS A 243                    
SITE     2 AC1  5 HOH A 371                                                     
SITE     1 AC2  8 THR B  18  ALA B  19  PHE B  20  HIS B  21                    
SITE     2 AC2  8 ALA B  87  VAL B 132  LEU B 218  HIS B 243                    
CRYST1   48.197  105.716   59.888  90.00  96.51  90.00 P 1 21 1      4          
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      0.020748  0.000000  0.002368        0.00000                         
SCALE2      0.000000  0.009459  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016806        0.00000                         
TER    1988      LYS A 265                                                      
TER    3982      LYS B 265                                                      
MASTER      295    0    2   26   18    0    4    6 4243    2   28   42          
END                                                                             

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