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LongText Report for: 6jra-pdb

Name Class
6jra-pdb
HEADER    HYDROLASE                               03-APR-19   6JRA              
TITLE     ZHD/W183F COMPLEX WITH HYDROLYZED AZOL                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZEARALENONE HYDROLASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLONOSTACHYS ROSEA;                             
SOURCE   3 ORGANISM_TAXID: 29856;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LACTONASE, HYDROLASE, ALPHA-BETA FOLD, ZEARALENONE DEGRADE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.J.HU                                                                
REVDAT   1   08-APR-20 6JRA    0                                                
JRNL        AUTH   X.J.HU,H.J.ZHOU,L.LI                                         
JRNL        TITL   STRUCTURE OF ZHD COMPLEX                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 67020                          
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) : 0.145                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.166                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3664                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4801                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 282                          
REMARK   3   BIN FREE R VALUE                    : 0.2280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4104                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 415                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.75000                                             
REMARK   3    B22 (A**2) : 0.54000                                              
REMARK   3    B33 (A**2) : 0.21000                                              
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): 0.082         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.081         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.559         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4385 ; 0.014 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  3994 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5997 ; 1.732 ; 1.655       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9294 ; 1.619 ; 1.583       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   559 ; 6.380 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   200 ;34.150 ;22.600       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   679 ;11.314 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ; 8.810 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   586 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4951 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   889 ; 0.005 ; 0.020       
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):  2206 ; 1.805 ; 1.882       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2205 ; 1.799 ; 1.880       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2775 ; 2.356 ; 2.813       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2776 ; 2.356 ; 2.814       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2179 ; 3.541 ; 2.266       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2180 ; 3.541 ; 2.267       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3223 ; 5.198 ; 3.243       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5114 ; 5.817 ;24.035       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5058 ; 5.754 ;23.764       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6JRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300011621.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97776                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 13.30                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 32.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5C8Z                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE, IMIDAZOLE,           
REMARK 280  POTASSIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  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       37.25700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.37600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.89800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.37600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.25700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.89800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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     VAL A   270                                                      
REMARK 465     ASP A   271                                                      
REMARK 465     LYS A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ALA A   274                                                      
REMARK 465     ALA A   275                                                      
REMARK 465     ALA A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     GLU A   278                                                      
REMARK 465     HIS A   279                                                      
REMARK 465     HIS A   280                                                      
REMARK 465     HIS A   281                                                      
REMARK 465     HIS A   282                                                      
REMARK 465     HIS A   283                                                      
REMARK 465     HIS A   284                                                      
REMARK 465     SER B   269                                                      
REMARK 465     VAL B   270                                                      
REMARK 465     ASP B   271                                                      
REMARK 465     LYS B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     ALA B   274                                                      
REMARK 465     ALA B   275                                                      
REMARK 465     ALA B   276                                                      
REMARK 465     LEU B   277                                                      
REMARK 465     GLU B   278                                                      
REMARK 465     HIS B   279                                                      
REMARK 465     HIS B   280                                                      
REMARK 465     HIS B   281                                                      
REMARK 465     HIS B   282                                                      
REMARK 465     HIS B   283                                                      
REMARK 465     HIS B   284                                                      
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    ASP A  31     -178.84    -65.22                                   
REMARK 500    SER A  62     -120.67     47.07                                   
REMARK 500    SER A 102     -127.22     66.29                                   
REMARK 500    GLU A 126       72.91     49.66                                   
REMARK 500    PRO A 196       46.90    -84.18                                   
REMARK 500    MET A 241     -112.60   -130.31                                   
REMARK 500    ASP B  31     -179.20    -67.38                                   
REMARK 500    SER B  62     -124.03     46.03                                   
REMARK 500    SER B 102     -125.91     65.94                                   
REMARK 500    GLU B 126       72.46     47.89                                   
REMARK 500    PRO B 196       37.63    -84.57                                   
REMARK 500    MET B 241     -112.17   -130.43                                   
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 C3L A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 304                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C3L B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 303                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5C8Z   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME                                                          
REMARK 900 RELATED ID: 6JQZ   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME                                                          
REMARK 900 RELATED ID: 6JR2   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME                                                          
REMARK 900 RELATED ID: 6JR5   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME                                                          
REMARK 900 RELATED ID: 6JR9   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME                                                          
DBREF  6JRA A    1   284  PDB    6JRA     6JRA             1    284             
DBREF  6JRA B    1   284  PDB    6JRA     6JRA             1    284             
SEQRES   1 A  284  MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE          
SEQRES   2 A  284  THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE          
SEQRES   3 A  284  VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE          
SEQRES   4 A  284  ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG          
SEQRES   5 A  284  VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA          
SEQRES   6 A  284  LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN          
SEQRES   7 A  284  LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU          
SEQRES   8 A  284  ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY          
SEQRES   9 A  284  ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP          
SEQRES  10 A  284  ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS          
SEQRES  11 A  284  LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP          
SEQRES  12 A  284  GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MET LEU ASN          
SEQRES  13 A  284  ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY          
SEQRES  14 A  284  VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL          
SEQRES  15 A  284  PHE ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA          
SEQRES  16 A  284  PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU          
SEQRES  17 A  284  ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE          
SEQRES  18 A  284  PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN          
SEQRES  19 A  284  ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER          
SEQRES  20 A  284  HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR          
SEQRES  21 A  284  GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU          
SEQRES  22 A  284  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  284  MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE          
SEQRES   2 B  284  THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE          
SEQRES   3 B  284  VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE          
SEQRES   4 B  284  ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG          
SEQRES   5 B  284  VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA          
SEQRES   6 B  284  LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN          
SEQRES   7 B  284  LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU          
SEQRES   8 B  284  ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY          
SEQRES   9 B  284  ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP          
SEQRES  10 B  284  ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS          
SEQRES  11 B  284  LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP          
SEQRES  12 B  284  GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MET LEU ASN          
SEQRES  13 B  284  ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY          
SEQRES  14 B  284  VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL          
SEQRES  15 B  284  PHE ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA          
SEQRES  16 B  284  PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU          
SEQRES  17 B  284  ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE          
SEQRES  18 B  284  PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN          
SEQRES  19 B  284  ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER          
SEQRES  20 B  284  HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR          
SEQRES  21 B  284  GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU          
SEQRES  22 B  284  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
HET    C3L  A 301      24                                                       
HET    GOL  A 302       6                                                       
HET    GOL  A 303       6                                                       
HET      K  A 304       1                                                       
HET    C3L  B 301      24                                                       
HET    GOL  B 302       6                                                       
HET      K  B 303       1                                                       
HETNAM     C3L 2-[(~{E},6~{R},10~{S})-6,10-BIS(OXIDANYL)UNDEC-1-ENYL]-          
HETNAM   2 C3L  4,6-BIS(OXIDANYL)BENZOIC ACID                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM       K POTASSIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  C3L    2(C18 H26 O6)                                                
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   6    K    2(K 1+)                                                      
FORMUL  10  HOH   *415(H2 O)                                                    
HELIX    1 AA1 GLU A   35  MET A   38  5                                   4    
HELIX    2 AA2 PHE A   39  ALA A   48  1                                  10    
HELIX    3 AA3 MET A   61  ALA A   65  5                                   5    
HELIX    4 AA4 PRO A   68  TYR A   72  5                                   5    
HELIX    5 AA5 THR A   76  LEU A   91  1                                  16    
HELIX    6 AA6 SER A  102  TYR A  115  1                                  14    
HELIX    7 AA7 LEU A  132  ASN A  137  1                                   6    
HELIX    8 AA8 THR A  138  LEU A  141  5                                   4    
HELIX    9 AA9 GLU A  142  ASP A  157  1                                  16    
HELIX   10 AB1 GLY A  161  ALA A  167  1                                   7    
HELIX   11 AB2 GLY A  169  TYR A  187  1                                  19    
HELIX   12 AB3 ILE A  191  ALA A  195  5                                   5    
HELIX   13 AB4 ASP A  199  ARG A  204  1                                   6    
HELIX   14 AB5 PRO A  217  ALA A  231  1                                  15    
HELIX   15 AB6 PHE A  243  HIS A  248  1                                   6    
HELIX   16 AB7 HIS A  248  SER A  268  1                                  21    
HELIX   17 AB8 GLU B   35  MET B   38  5                                   4    
HELIX   18 AB9 PHE B   39  ALA B   48  1                                  10    
HELIX   19 AC1 MET B   61  ALA B   65  5                                   5    
HELIX   20 AC2 PRO B   68  TYR B   72  5                                   5    
HELIX   21 AC3 THR B   76  LEU B   91  1                                  16    
HELIX   22 AC4 SER B  102  TYR B  115  1                                  14    
HELIX   23 AC5 LEU B  132  ASN B  137  1                                   6    
HELIX   24 AC6 THR B  138  LEU B  141  5                                   4    
HELIX   25 AC7 GLU B  142  VAL B  158  1                                  17    
HELIX   26 AC8 GLY B  161  ALA B  167  1                                   7    
HELIX   27 AC9 LEU B  168  TYR B  187  1                                  20    
HELIX   28 AD1 ILE B  191  ALA B  195  5                                   5    
HELIX   29 AD2 ASP B  199  ARG B  204  1                                   6    
HELIX   30 AD3 PRO B  217  GLY B  232  1                                  16    
HELIX   31 AD4 PHE B  243  HIS B  248  1                                   6    
HELIX   32 AD5 HIS B  248  SER B  268  1                                  21    
SHEET    1 AA1 8 THR A   3  SER A   8  0                                        
SHEET    2 AA1 8 THR A  14  GLU A  20 -1  O  GLN A  19   N  THR A   3           
SHEET    3 AA1 8 ARG A  52  PHE A  56 -1  O  VAL A  53   N  GLU A  20           
SHEET    4 AA1 8 ASP A  25  VAL A  29  1  N  ILE A  26   O  ARG A  52           
SHEET    5 AA1 8 ALA A  96  CYS A 101  1  O  THR A  97   N  VAL A  27           
SHEET    6 AA1 8 ILE A 119  HIS A 125  1  O  MET A 123   N  VAL A  98           
SHEET    7 AA1 8 LEU A 208  GLY A 213  1  O  THR A 211   N  CYS A 124           
SHEET    8 AA1 8 ASN A 234  LEU A 238  1  O  ASN A 234   N  TRP A 210           
SHEET    1 AA2 8 THR B   3  SER B   8  0                                        
SHEET    2 AA2 8 THR B  14  GLU B  20 -1  O  TRP B  15   N  ILE B   7           
SHEET    3 AA2 8 ARG B  52  PHE B  56 -1  O  VAL B  53   N  GLU B  20           
SHEET    4 AA2 8 ASP B  25  VAL B  29  1  N  ILE B  26   O  ARG B  52           
SHEET    5 AA2 8 ALA B  96  CYS B 101  1  O  TRP B  99   N  VAL B  29           
SHEET    6 AA2 8 ILE B 119  HIS B 125  1  O  MET B 123   N  VAL B  98           
SHEET    7 AA2 8 LEU B 208  GLY B 213  1  O  THR B 211   N  CYS B 124           
SHEET    8 AA2 8 ASN B 234  LEU B 238  1  O  ASN B 234   N  TRP B 210           
SITE     1 AC1 12 GLY A  32  SER A 102  SER A 103  HIS A 134                    
SITE     2 AC1 12 ILE A 149  VAL A 153  PHE A 183  TYR A 187                    
SITE     3 AC1 12 PRO A 188  PRO A 192  HIS A 242  HOH A 407                    
SITE     1 AC2  6 PRO A 128  THR A 129  LYS A 130  LEU A 132                    
SITE     2 AC2  6 SER A 220  HOH A 459                                          
SITE     1 AC3  6 GLN A  19  ARG A  52  LEU A  91  HOH A 409                    
SITE     2 AC3  6 SER B 162  GLU B 163                                          
SITE     1 AC4  4 HIS A 248  PRO A 249  ASP A 250  VAL A 251                    
SITE     1 AC5 11 GLY B  32  SER B 102  SER B 103  HIS B 134                    
SITE     2 AC5 11 VAL B 153  PHE B 183  TYR B 187  PRO B 188                    
SITE     3 AC5 11 PRO B 192  HIS B 242  HOH B 403                               
SITE     1 AC6  6 PRO B 128  THR B 129  LYS B 130  LEU B 132                    
SITE     2 AC6  6 SER B 220  HOH B 454                                          
SITE     1 AC7  4 HIS B 248  PRO B 249  ASP B 250  VAL B 251                    
CRYST1   74.514   89.796  112.752  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      0.013420  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011136  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008869        0.00000                         
TER    2098      SER A 269                                                      
TER    4199      SER B 268                                                      
MASTER      348    0    7   32   16    0   14    6 4587    2   66   44          
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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