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LongText Report for: 3V1N-pdb

Name Class
3V1N-pdb
HEADER    HYDROLASE                               09-DEC-11   3V1N              
TITLE     CRYSTAL STRUCTURE OF THE H265Q MUTANT OF A C-C HYDROLASE, BPHD FROM   
TITLE    2 BURKHOLDERIA XENOVORANS LB400, AFTER EXPOSURE TO ITS SUBSTRATE HOPDA 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE HYDROLASE;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HOPDA HYDROLASE, 2,6-DIOXO-6-PHENYLHEXA-3-ENOATE HYDROLASE; 
COMPND   5 EC: 3.7.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;                        
SOURCE   3 ORGANISM_TAXID: 266265;                                              
SOURCE   4 STRAIN: LB400;                                                       
SOURCE   5 GENE: BPHD, BXENO_C1120, BXE_C1186;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    C-C BOND HYDROLASE, ALPHA/BETA HYDROLASE FOLD, BPHD, ALPHA/BETA       
KEYWDS   2 HYDROLASE, PCB DEGRADATION, META CLEAVAGE PRODUCT HYDROLASE, MCP     
KEYWDS   3 HYDROLASE, 2-HYDROXY-6-OXO-6-PHENYL-HEXA-2,4-DIENOATE HYDROLASE,     
KEYWDS   4 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GHOSH,J.T.BOLIN                                                     
REVDAT   1   21-MAR-12 3V1N    0                                                
JRNL        AUTH   A.C.RUZZINI,S.GHOSH,G.P.HORSMAN,L.J.FOSTER,J.T.BOLIN,        
JRNL        AUTH 2 L.D.ELTIS                                                    
JRNL        TITL   IDENTIFICATION OF AN ACYL-ENZYME INTERMEDIATE IN A           
JRNL        TITL 2 META-CLEAVAGE PRODUCT HYDROLASE REVEALS THE VERSATILITY OF   
JRNL        TITL 3 THE CATALYTIC TRIAD.                                         
JRNL        REF    J.AM.CHEM.SOC.                             2012              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   22339283                                                     
JRNL        DOI    10.1021/JA208544G                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 82.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40814                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2046                            
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) : 1.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2627                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 149                          
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2239                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 176                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.66000                                              
REMARK   3    B22 (A**2) : 0.66000                                              
REMARK   3    B33 (A**2) : -1.32000                                             
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): 0.088         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.088         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.747         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2375 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1621 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3220 ; 1.387 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3934 ; 0.947 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   296 ; 5.672 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   110 ;36.594 ;23.909       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   398 ;13.321 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;16.279 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   334 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2703 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   522 ; 0.007 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   : 1.20                                          
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; U VALUES: REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 3V1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB069481.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40851                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.000                             
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.82400                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, 10 MM CALCIUM     
REMARK 280  CHLORIDE DIHYDRATE, PH 6.4, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       58.32050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       58.32050            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.79550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       58.32050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       21.89775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       58.32050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.69325            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       58.32050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       65.69325            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.32050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       21.89775            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       58.32050            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       58.32050            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.79550            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       58.32050            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       58.32050            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       43.79550            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       58.32050            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       65.69325            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       58.32050            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       21.89775            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       58.32050            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       21.89775            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       58.32050            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       65.69325            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       58.32050            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       58.32050            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       43.79550            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12620 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
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   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  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     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 200   CG    HIS A 200   CD2     0.063                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  18     -119.67     46.59                                   
REMARK 500    ASN A  75     -123.32     46.83                                   
REMARK 500    SER A 112     -111.17     57.31                                   
REMARK 500    LEU A 140       35.59    -89.87                                   
REMARK 500    TRP A 266       72.95   -115.85                                   
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 MLA A 287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPK A 289                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OG1   RELATED DB: PDB                                   
REMARK 900 BPHD WILD TYPE                                                       
REMARK 900 RELATED ID: 2RI6   RELATED DB: PDB                                   
REMARK 900 BPHD S112A MUTANT                                                    
REMARK 900 RELATED ID: 2PU7   RELATED DB: PDB                                   
REMARK 900 BPHD S112A/H265A MUTANT                                              
REMARK 900 RELATED ID: 2PUH   RELATED DB: PDB                                   
REMARK 900 BPHD S112A MUTANT IN COMPLEX WITH SUBSTRATE HOPDA                    
REMARK 900 RELATED ID: 2PUJ   RELATED DB: PDB                                   
REMARK 900 BPHD S112A/H265Q MUTANT IN COMPLEX WITH SUBSTRATE HOPDA              
REMARK 900 RELATED ID: 2RHW   RELATED DB: PDB                                   
REMARK 900 BPHD S112A MUTANT IN COMPLEX WITH 3, 10 - DIFLUORO HOPDA             
REMARK 900 RELATED ID: 2RHT   RELATED DB: PDB                                   
REMARK 900 BPHD S112A MUTANT IN COMPLEX WITH 3-CL HOPDA                         
REMARK 900 RELATED ID: 3V1K   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3V1L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3V1M   RELATED DB: PDB                                   
DBREF  3V1N A    1   286  UNP    P47229   BPHD_BURXL       1    286             
SEQADV 3V1N GLN A  265  UNP  P47229    HIS   265 ENGINEERED MUTATION            
SEQRES   1 A  286  MET THR ALA LEU THR GLU SER SER THR SER LYS PHE VAL          
SEQRES   2 A  286  LYS ILE ASN GLU LYS GLY PHE SER ASP PHE ASN ILE HIS          
SEQRES   3 A  286  TYR ASN GLU ALA GLY ASN GLY GLU THR VAL ILE MET LEU          
SEQRES   4 A  286  HIS GLY GLY GLY PRO GLY ALA GLY GLY TRP SER ASN TYR          
SEQRES   5 A  286  TYR ARG ASN VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG          
SEQRES   6 A  286  VAL ILE LEU LYS ASP SER PRO GLY PHE ASN LYS SER ASP          
SEQRES   7 A  286  ALA VAL VAL MET ASP GLU GLN ARG GLY LEU VAL ASN ALA          
SEQRES   8 A  286  ARG ALA VAL LYS GLY LEU MET ASP ALA LEU ASP ILE ASP          
SEQRES   9 A  286  ARG ALA HIS LEU VAL GLY ASN SER MET GLY GLY ALA THR          
SEQRES  10 A  286  ALA LEU ASN PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY          
SEQRES  11 A  286  LYS LEU ILE LEU MET GLY PRO GLY GLY LEU GLY PRO SER          
SEQRES  12 A  286  MET PHE ALA PRO MET PRO MET GLU GLY ILE LYS LEU LEU          
SEQRES  13 A  286  PHE LYS LEU TYR ALA GLU PRO SER TYR GLU THR LEU LYS          
SEQRES  14 A  286  GLN MET LEU GLN VAL PHE LEU TYR ASP GLN SER LEU ILE          
SEQRES  15 A  286  THR GLU GLU LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN          
SEQRES  16 A  286  ARG GLN PRO GLU HIS LEU LYS ASN PHE LEU ILE SER ALA          
SEQRES  17 A  286  GLN LYS ALA PRO LEU SER THR TRP ASP VAL THR ALA ARG          
SEQRES  18 A  286  LEU GLY GLU ILE LYS ALA LYS THR PHE ILE THR TRP GLY          
SEQRES  19 A  286  ARG ASP ASP ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS          
SEQRES  20 A  286  LEU LEU TRP ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE          
SEQRES  21 A  286  SER LYS CYS GLY GLN TRP ALA GLN TRP GLU HIS ALA ASP          
SEQRES  22 A  286  GLU PHE ASN ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA          
HET    MLA  A 287       7                                                       
HET    BEZ  A 288       8                                                       
HET    HPK  A 289      16                                                       
HETNAM     MLA MALONIC ACID                                                     
HETNAM     BEZ BENZOIC ACID                                                     
HETNAM     HPK (3E)-2,6-DIOXO-6-PHENYLHEX-3-ENOATE                              
HETSYN     MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;                        
HETSYN   2 MLA  METAHNEDICARBOXYLIC ACID                                        
FORMUL   2  MLA    C3 H4 O4                                                     
FORMUL   3  BEZ    C7 H6 O2                                                     
FORMUL   4  HPK    C12 H9 O4 1-                                                 
FORMUL   5  HOH   *176(H2 O)                                                    
HELIX    1   1 THR A    5  THR A    9  1                                   5    
HELIX    2   2 GLY A   47  TYR A   53  1                                   7    
HELIX    3   3 ASN A   55  ALA A   62  1                                   8    
HELIX    4   4 GLN A   85  ASP A  102  1                                  18    
HELIX    5   5 SER A  112  TYR A  125  1                                  14    
HELIX    6   6 MET A  150  GLU A  162  1                                  13    
HELIX    7   7 SER A  164  LEU A  176  1                                  13    
HELIX    8   8 ASP A  178  ILE A  182  5                                   5    
HELIX    9   9 THR A  183  GLN A  197  1                                  15    
HELIX   10  10 GLN A  197  ALA A  211  1                                  15    
HELIX   11  11 PRO A  212  ASP A  217  5                                   6    
HELIX   12  12 VAL A  218  ILE A  225  5                                   8    
HELIX   13  13 LEU A  242  ILE A  252  1                                  11    
HELIX   14  14 TRP A  266  HIS A  271  1                                   6    
HELIX   15  15 HIS A  271  ALA A  286  1                                  16    
SHEET    1   A 8 SER A  10  GLU A  17  0                                        
SHEET    2   A 8 PHE A  20  ALA A  30 -1  O  PHE A  23   N  ILE A  15           
SHEET    3   A 8 TYR A  64  LYS A  69 -1  O  LEU A  68   N  ASN A  28           
SHEET    4   A 8 GLU A  34  LEU A  39  1  N  MET A  38   O  ILE A  67           
SHEET    5   A 8 ALA A 106  ASN A 111  1  O  VAL A 109   N  LEU A  39           
SHEET    6   A 8 ILE A 129  MET A 135  1  O  MET A 135   N  GLY A 110           
SHEET    7   A 8 THR A 229  GLY A 234  1  O  THR A 232   N  LEU A 134           
SHEET    8   A 8 ALA A 255  PHE A 260  1  O  ARG A 256   N  ILE A 231           
LINK         OG  SER A 112                 C   BEZ A 288     1555   1555  1.42  
CISPEP   1 MET A  148    PRO A  149          0        10.76                     
SITE     1 AC1 13 GLU A  34  THR A  35  ARG A  65  ASP A 102                    
SITE     2 AC1 13 ILE A 103  ASP A 104  ARG A 105  SER A 180                    
SITE     3 AC1 13 ILE A 182  HOH A 297  HOH A 356  HOH A 425                    
SITE     4 AC1 13 HOH A 443                                                     
SITE     1 AC2  7 GLY A  41  GLY A  42  SER A 112  MET A 113                    
SITE     2 AC2  7 ILE A 153  LEU A 213  VAL A 240                               
SITE     1 AC3 13 HIS A  40  GLY A  41  ALA A  46  GLY A  47                    
SITE     2 AC3 13 SER A  50  ASN A  51  LEU A 176  LEU A 181                    
SITE     3 AC3 13 LEU A 186  ARG A 190  TRP A 266  HOH A 440                    
SITE     4 AC3 13 HOH A 455                                                     
CRYST1  116.641  116.641   87.591  90.00  90.00  90.00 I 41 2 2     16          
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      0.008573  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008573  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011417        0.00000                         
TER    2281      ALA A 286                                                      
MASTER      374    0    3   15    8    0   10    6 2446    1   32   22          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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