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LongText Report for: 4LYE-pdb

Name Class
4LYE-pdb
HEADER    HYDROLASE                               31-JUL-13   4LYE              
TITLE     CRYSTAL STRUCTURE OF THE S105A MUTANT OF A C-C HYDROLASE, DXNB2 FROM  
TITLE    2 SPHINGOMONAS WITTICHII RW1, IN COMPLEX WITH SUBSTRATE HOPDA          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MCP HYDROLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA/BETA HYDROLASE FOLD;                                  
COMPND   5 EC: 3.7.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SPHINGOMONAS WITTICHII;                         
SOURCE   3 ORGANISM_TAXID: 392499;                                              
SOURCE   4 STRAIN: RW1;                                                         
SOURCE   5 GENE: DXNB2, SWIT_3055;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PEMDXN1                                   
KEYWDS    META-CLEAVAGE PRODUCT HYDROLASE, C-C BOND HYDROLASE, ALPHA-BETA       
KEYWDS   2 HYDROLASE, DIBENZO-P-DIOXIN DEGRADATION, DIBENZOFURAN DEGRADATION,   
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GHOSH,J.T.BOLIN                                                     
REVDAT   1   09-OCT-13 4LYE    0                                                
JRNL        AUTH   A.C.RUZZINI,S.BHOWMIK,S.GHOSH,K.C.YAM,J.T.BOLIN,L.D.ELTIS    
JRNL        TITL   A SUBSTRATE-ASSISTED MECHANISM OF NUCLEOPHILE ACTIVATION IN  
JRNL        TITL 2 A SER-HIS-ASP CONTAINING C-C BOND HYDROLASE.                 
JRNL        REF    BIOCHEMISTRY                               2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24067021                                                     
JRNL        DOI    10.1021/BI401156A                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19693                          
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) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1006                            
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) : 2.33                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1331                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2108                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 72                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.58000                                              
REMARK   3    B22 (A**2) : 0.58000                                              
REMARK   3    B33 (A**2) : -1.88000                                             
REMARK   3    B12 (A**2) : 0.58000                                              
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): 0.207         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.190         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.332         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2174 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2044 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2947 ; 1.415 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4699 ; 0.764 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   275 ; 5.895 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    94 ;34.462 ;23.936       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   344 ;15.924 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;16.502 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   322 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2494 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   504 ; 0.001 ; 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):  1103 ; 2.916 ; 4.598       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1102 ; 2.915 ; 4.594       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1377 ; 4.312 ; 6.890       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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 4LYE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081241.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : GE(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19800                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 10.700                             
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.45900                            
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   (%): 64.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M SODIUM MALONATE, PH 6.8, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      226.16800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      113.08400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      169.62600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.54200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      282.71000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      226.16800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      113.08400            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       56.54200            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      169.62600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      282.71000            
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 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  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       56.54200            
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     ASP A   277                                                      
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  13       59.94     32.41                                   
REMARK 500    ALA A  70       79.19   -118.18                                   
REMARK 500    ALA A 105     -121.75     51.11                                   
REMARK 500    ASN A 133       32.89   -146.41                                   
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 HPK A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LXG   RELATED DB: PDB                                   
REMARK 900 DXNB2 WILD TYPE                                                      
REMARK 900 RELATED ID: 4LYD   RELATED DB: PDB                                   
REMARK 900 DXNB2 S105A                                                          
REMARK 900 RELATED ID: 4LXH   RELATED DB: PDB                                   
REMARK 900 DXNB2 S105A IN COMPLEX WITH 3-CL-HOPDA                               
REMARK 900 RELATED ID: 4LXI   RELATED DB: PDB                                   
REMARK 900 DXNB2 S105A IN COMPLEX WITH 5,8-DIF-HOPDA                            
DBREF  4LYE A    1   277  UNP    A5VAT9   A5VAT9_SPHWW     1    277             
SEQADV 4LYE ALA A  105  UNP  A5VAT9    SER   105 ENGINEERED MUTATION            
SEQRES   1 A  277  MET PHE GLU GLN PHE GLU SER LYS PHE ILE ASP CYS ASP          
SEQRES   2 A  277  GLY ILE ARG THR HIS TYR ILE GLU MET GLY GLU GLY ASP          
SEQRES   3 A  277  PRO LEU VAL LEU VAL HIS GLY GLY GLY ALA GLY ALA ASP          
SEQRES   4 A  277  GLY ARG SER ASN PHE ALA ASP ASN PHE PRO ILE PHE ALA          
SEQRES   5 A  277  ARG HIS MET ARG VAL ILE ALA TYR ASP MET VAL GLY PHE          
SEQRES   6 A  277  GLY GLN THR ASP ALA PRO ASP PRO ALA GLY PHE ALA TYR          
SEQRES   7 A  277  THR GLN ALA ALA ARG THR ASP HIS LEU ILE SER PHE ILE          
SEQRES   8 A  277  LYS ALA LEU GLY LEU SER LYS ILE CYS LEU ILE GLY ASN          
SEQRES   9 A  277  ALA MET GLY GLY THR THR ALA CYS GLY ALA ALA LEU LYS          
SEQRES  10 A  277  ALA PRO GLU LEU ILE ASP ARG LEU VAL LEU MET GLY ALA          
SEQRES  11 A  277  ALA VAL ASN ILE SER PRO ASP ASP MET VAL ALA ASN ARG          
SEQRES  12 A  277  ASP ASP LEU ALA ALA VAL MET SER TYR ASP GLY SER GLU          
SEQRES  13 A  277  GLU GLY MET ARG LYS ILE ILE ALA ALA LEU THR HIS SER          
SEQRES  14 A  277  TYR GLN PRO THR ASP ASP ILE VAL HIS TYR ARG HIS GLU          
SEQRES  15 A  277  ALA SER LEU ARG PRO THR THR THR ALA ALA TYR LYS ALA          
SEQRES  16 A  277  THR MET GLY TRP ALA LYS GLN ASN GLY LEU TYR TYR SER          
SEQRES  17 A  277  PRO GLU GLN LEU ALA SER LEU THR MET PRO VAL LEU VAL          
SEQRES  18 A  277  LEU GLY GLY LYS ASN ASP VAL MET VAL PRO VAL ARG LYS          
SEQRES  19 A  277  VAL ILE ASP GLN ILE LEU ALA ILE PRO GLN ALA ILE GLY          
SEQRES  20 A  277  HIS VAL PHE PRO ASN CYS GLY HIS TRP VAL MET ILE GLU          
SEQRES  21 A  277  TYR PRO GLU GLU PHE CYS THR GLN THR LEU HIS PHE PHE          
SEQRES  22 A  277  GLY LYS LEU ASP                                              
HET    HPK  A 301      16                                                       
HETNAM     HPK (3E)-2,6-DIOXO-6-PHENYLHEX-3-ENOATE                              
FORMUL   2  HPK    C12 H9 O4 1-                                                 
FORMUL   3  HOH   *72(H2 O)                                                     
HELIX    1   1 ASP A   39  ALA A   45  1                                   7    
HELIX    2   2 ASN A   47  ARG A   53  1                                   7    
HELIX    3   3 THR A   79  LEU A   94  1                                  16    
HELIX    4   4 ALA A  105  ALA A  118  1                                  14    
HELIX    5   5 SER A  135  ASN A  142  1                                   8    
HELIX    6   6 ASN A  142  SER A  151  1                                  10    
HELIX    7   7 SER A  155  THR A  167  1                                  13    
HELIX    8   8 THR A  173  LEU A  185  1                                  13    
HELIX    9   9 ARG A  186  GLY A  204  1                                  19    
HELIX   10  10 SER A  208  SER A  214  1                                   7    
HELIX   11  11 PRO A  231  ILE A  242  1                                  12    
HELIX   12  12 TRP A  256  TYR A  261  1                                   6    
HELIX   13  13 TYR A  261  PHE A  273  1                                  13    
SHEET    1   A 8 LYS A   8  CYS A  12  0                                        
SHEET    2   A 8 ILE A  15  MET A  22 -1  O  ILE A  15   N  CYS A  12           
SHEET    3   A 8 ARG A  56  TYR A  60 -1  O  VAL A  57   N  MET A  22           
SHEET    4   A 8 PRO A  27  VAL A  31  1  N  LEU A  30   O  ILE A  58           
SHEET    5   A 8 ILE A  99  ASN A 104  1  O  ILE A 102   N  VAL A  31           
SHEET    6   A 8 ILE A 122  MET A 128  1  O  MET A 128   N  GLY A 103           
SHEET    7   A 8 VAL A 219  GLY A 224  1  O  LEU A 222   N  LEU A 127           
SHEET    8   A 8 ILE A 246  PHE A 250  1  O  ILE A 246   N  VAL A 219           
SHEET    1   B 2 ASN A 133  ILE A 134  0                                        
SHEET    2   B 2 LEU A 205  TYR A 206 -1  O  LEU A 205   N  ILE A 134           
SITE     1 AC1 16 GLY A  33  GLY A  34  GLY A  35  ALA A  38                    
SITE     2 AC1 16 ASN A  43  ASN A 104  ALA A 105  MET A 106                    
SITE     3 AC1 16 LEU A 146  MET A 150  LEU A 166  ARG A 180                    
SITE     4 AC1 16 MET A 229  HIS A 255  TRP A 256  HOH A 469                    
CRYST1   65.715   65.715  339.252  90.00  90.00 120.00 P 65 2 2     12          
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      0.015217  0.008786  0.000000        0.00000                         
SCALE2      0.000000  0.017571  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002948        0.00000                         
TER    2109      LEU A 276                                                      
MASTER      312    0    1   13   10    0    4    6 2196    1   16   22          
END                                                                             

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