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Database: PDB
Entry: 1KEW
LinkDB: 1KEW
Original site: 1KEW 
HEADER    LYASE                                   17-NOV-01   1KEW              
TITLE     THE CRYSTAL STRUCTURE OF DTDP-D-GLUCOSE 4,6-DEHYDRATASE (RMLB) FROM   
TITLE    2 SALMONELLA ENTERICA SEROVAR TYPHIMURIUM WITH THYMIDINE DIPHOSPHATE   
TITLE    3 BOUND                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DTDP-D-GLUCOSE 4,6-DEHYDRATASE;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DTDP-GLUCOSE 4,6-DEHYDRATASE; RMLB;                         
COMPND   5 EC: 4.2.1.46;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR     
SOURCE   3 TYPHIMURIUM;                                                         
SOURCE   4 ORGANISM_TAXID: 90371;                                               
SOURCE   5 STRAIN: SUBSP. ENTERICA SEROVAR TYPHIMURIUM;                         
SOURCE   6 GENE: RMLB;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    ROSSMANN FOLD, LYASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.T.M.ALLARD,K.BEIS,M.-F.GIRAUD,A.D.HEGEMAN,J.W.GROSS,C.WHITFIELD,    
AUTHOR   2 M.GRANINGER,P.MESSNER,A.G.ALLEN,J.H.NAISMITH                         
REVDAT   4   13-JUL-11 1KEW    1       VERSN                                    
REVDAT   3   24-FEB-09 1KEW    1       VERSN                                    
REVDAT   2   01-APR-03 1KEW    1       JRNL                                     
REVDAT   1   25-JAN-02 1KEW    0                                                
JRNL        AUTH   S.T.ALLARD,K.BEIS,M.F.GIRAUD,A.D.HEGEMAN,J.W.GROSS,          
JRNL        AUTH 2 R.C.WILMOUTH,C.WHITFIELD,M.GRANINGER,P.MESSNER,A.G.ALLEN,    
JRNL        AUTH 3 D.J.MASKELL,J.H.NAISMITH                                     
JRNL        TITL   TOWARD A STRUCTURAL UNDERSTANDING OF THE DEHYDRATASE         
JRNL        TITL 2 MECHANISM.                                                   
JRNL        REF    STRUCTURE                     V.  10    81 2002              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   11796113                                                     
JRNL        DOI    10.1016/S0969-2126(01)00694-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 500.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 140818                         
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 SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7022                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.03                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2463                       
REMARK   3   BIN FREE R VALUE                    : 0.2896                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 696                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5758                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 156                                     
REMARK   3   SOLVENT ATOMS            : 701                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.23                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.43                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.89                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KEW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-NOV-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014879.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.32                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 140877                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : 0.05300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
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) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.18500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1G1A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.32, 1.5M LITHIUM           
REMARK 280  SULPHATE, VAPOR DIFFUSION, HANGING DROP AT 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       30.94467            
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       61.88933            
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       46.41700            
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       77.36167            
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       15.47233            
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: 6880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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 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    THR A  35     -165.96    -79.77                                   
REMARK 500    ILE A 101      -63.99    -93.39                                   
REMARK 500    ASN A 148       12.38    -60.91                                   
REMARK 500    ALA A 162       60.32   -162.28                                   
REMARK 500    PRO A 204       32.71    -57.68                                   
REMARK 500    ILE B 101      -64.04    -94.68                                   
REMARK 500    ASN B 148        7.34    -62.29                                   
REMARK 500    ALA B 162       58.42   -161.51                                   
REMARK 500    PRO B 204       31.60    -60.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2876        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH A2926        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A2934        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A2941        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH A2952        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH B2959        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH B2967        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH B3010        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH B3025        DISTANCE =  6.61 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYD A 2600                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYD B 2700                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 1400                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1473                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1474                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1475                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KEP   RELATED DB: PDB                                   
REMARK 900 RMLB FROM STREPTOCOCCUS SUIS WITH DTDP-XYLOSE BOUND                  
REMARK 900 RELATED ID: 1KER   RELATED DB: PDB                                   
REMARK 900 RMLB FROM STREPTOCOCCUS SUIS WITH DTDP-D-GLUCOSE BOUND               
REMARK 900 RELATED ID: 1KET   RELATED DB: PDB                                   
REMARK 900 RMLB FROM STREPTOCOCCUS SUIS WITH THYMIDINE DIPHOSPHATE              
REMARK 900 BOUND                                                                
REMARK 900 RELATED ID: 1KEU   RELATED DB: PDB                                   
REMARK 900 RMLB FROM SALMONELLA ENTERICA SEROVAR TYPHIMURIUM WITH DTDP          
REMARK 900 -D-GLUCOSE BOUND                                                     
REMARK 900 RELATED ID: 1G1A   RELATED DB: PDB                                   
REMARK 900 RMLB FROM SALMONELLA ENTERICA SEROVAR TYPHIMURIUM WITH NAD+          
REMARK 900 BOUND                                                                
DBREF  1KEW A    1   361  UNP    P26391   RFBB_SALTY       1    361             
DBREF  1KEW B    1   361  UNP    P26391   RFBB_SALTY       1    361             
SEQRES   1 A  361  MET LYS ILE LEU ILE THR GLY GLY ALA GLY PHE ILE GLY          
SEQRES   2 A  361  SER ALA VAL VAL ARG HIS ILE ILE LYS ASN THR GLN ASP          
SEQRES   3 A  361  THR VAL VAL ASN ILE ASP LYS LEU THR TYR ALA GLY ASN          
SEQRES   4 A  361  LEU GLU SER LEU SER ASP ILE SER GLU SER ASN ARG TYR          
SEQRES   5 A  361  ASN PHE GLU HIS ALA ASP ILE CYS ASP SER ALA GLU ILE          
SEQRES   6 A  361  THR ARG ILE PHE GLU GLN TYR GLN PRO ASP ALA VAL MET          
SEQRES   7 A  361  HIS LEU ALA ALA GLU SER HIS VAL ASP ARG SER ILE THR          
SEQRES   8 A  361  GLY PRO ALA ALA PHE ILE GLU THR ASN ILE VAL GLY THR          
SEQRES   9 A  361  TYR ALA LEU LEU GLU VAL ALA ARG LYS TYR TRP SER ALA          
SEQRES  10 A  361  LEU GLY GLU ASP LYS LYS ASN ASN PHE ARG PHE HIS HIS          
SEQRES  11 A  361  ILE SER THR ASP GLU VAL TYR GLY ASP LEU PRO HIS PRO          
SEQRES  12 A  361  ASP GLU VAL GLU ASN SER VAL THR LEU PRO LEU PHE THR          
SEQRES  13 A  361  GLU THR THR ALA TYR ALA PRO SER SER PRO TYR SER ALA          
SEQRES  14 A  361  SER LYS ALA SER SER ASP HIS LEU VAL ARG ALA TRP ARG          
SEQRES  15 A  361  ARG THR TYR GLY LEU PRO THR ILE VAL THR ASN CYS SER          
SEQRES  16 A  361  ASN ASN TYR GLY PRO TYR HIS PHE PRO GLU LYS LEU ILE          
SEQRES  17 A  361  PRO LEU VAL ILE LEU ASN ALA LEU GLU GLY LYS PRO LEU          
SEQRES  18 A  361  PRO ILE TYR GLY LYS GLY ASP GLN ILE ARG ASP TRP LEU          
SEQRES  19 A  361  TYR VAL GLU ASP HIS ALA ARG ALA LEU HIS MET VAL VAL          
SEQRES  20 A  361  THR GLU GLY LYS ALA GLY GLU THR TYR ASN ILE GLY GLY          
SEQRES  21 A  361  HIS ASN GLU LYS LYS ASN LEU ASP VAL VAL PHE THR ILE          
SEQRES  22 A  361  CYS ASP LEU LEU ASP GLU ILE VAL PRO LYS ALA THR SER          
SEQRES  23 A  361  TYR ARG GLU GLN ILE THR TYR VAL ALA ASP ARG PRO GLY          
SEQRES  24 A  361  HIS ASP ARG ARG TYR ALA ILE ASP ALA GLY LYS ILE SER          
SEQRES  25 A  361  ARG GLU LEU GLY TRP LYS PRO LEU GLU THR PHE GLU SER          
SEQRES  26 A  361  GLY ILE ARG LYS THR VAL GLU TRP TYR LEU ALA ASN THR          
SEQRES  27 A  361  GLN TRP VAL ASN ASN VAL LYS SER GLY ALA TYR GLN SER          
SEQRES  28 A  361  TRP ILE GLU GLN ASN TYR GLU GLY ARG GLN                      
SEQRES   1 B  361  MET LYS ILE LEU ILE THR GLY GLY ALA GLY PHE ILE GLY          
SEQRES   2 B  361  SER ALA VAL VAL ARG HIS ILE ILE LYS ASN THR GLN ASP          
SEQRES   3 B  361  THR VAL VAL ASN ILE ASP LYS LEU THR TYR ALA GLY ASN          
SEQRES   4 B  361  LEU GLU SER LEU SER ASP ILE SER GLU SER ASN ARG TYR          
SEQRES   5 B  361  ASN PHE GLU HIS ALA ASP ILE CYS ASP SER ALA GLU ILE          
SEQRES   6 B  361  THR ARG ILE PHE GLU GLN TYR GLN PRO ASP ALA VAL MET          
SEQRES   7 B  361  HIS LEU ALA ALA GLU SER HIS VAL ASP ARG SER ILE THR          
SEQRES   8 B  361  GLY PRO ALA ALA PHE ILE GLU THR ASN ILE VAL GLY THR          
SEQRES   9 B  361  TYR ALA LEU LEU GLU VAL ALA ARG LYS TYR TRP SER ALA          
SEQRES  10 B  361  LEU GLY GLU ASP LYS LYS ASN ASN PHE ARG PHE HIS HIS          
SEQRES  11 B  361  ILE SER THR ASP GLU VAL TYR GLY ASP LEU PRO HIS PRO          
SEQRES  12 B  361  ASP GLU VAL GLU ASN SER VAL THR LEU PRO LEU PHE THR          
SEQRES  13 B  361  GLU THR THR ALA TYR ALA PRO SER SER PRO TYR SER ALA          
SEQRES  14 B  361  SER LYS ALA SER SER ASP HIS LEU VAL ARG ALA TRP ARG          
SEQRES  15 B  361  ARG THR TYR GLY LEU PRO THR ILE VAL THR ASN CYS SER          
SEQRES  16 B  361  ASN ASN TYR GLY PRO TYR HIS PHE PRO GLU LYS LEU ILE          
SEQRES  17 B  361  PRO LEU VAL ILE LEU ASN ALA LEU GLU GLY LYS PRO LEU          
SEQRES  18 B  361  PRO ILE TYR GLY LYS GLY ASP GLN ILE ARG ASP TRP LEU          
SEQRES  19 B  361  TYR VAL GLU ASP HIS ALA ARG ALA LEU HIS MET VAL VAL          
SEQRES  20 B  361  THR GLU GLY LYS ALA GLY GLU THR TYR ASN ILE GLY GLY          
SEQRES  21 B  361  HIS ASN GLU LYS LYS ASN LEU ASP VAL VAL PHE THR ILE          
SEQRES  22 B  361  CYS ASP LEU LEU ASP GLU ILE VAL PRO LYS ALA THR SER          
SEQRES  23 B  361  TYR ARG GLU GLN ILE THR TYR VAL ALA ASP ARG PRO GLY          
SEQRES  24 B  361  HIS ASP ARG ARG TYR ALA ILE ASP ALA GLY LYS ILE SER          
SEQRES  25 B  361  ARG GLU LEU GLY TRP LYS PRO LEU GLU THR PHE GLU SER          
SEQRES  26 B  361  GLY ILE ARG LYS THR VAL GLU TRP TYR LEU ALA ASN THR          
SEQRES  27 B  361  GLN TRP VAL ASN ASN VAL LYS SER GLY ALA TYR GLN SER          
SEQRES  28 B  361  TRP ILE GLU GLN ASN TYR GLU GLY ARG GLN                      
HET    TYD  A2600      25                                                       
HET    TYD  B2700      25                                                       
HET    NAD  A1400      44                                                       
HET    NAD  B1500      44                                                       
HET    GOL  A1473       6                                                       
HET    GOL  A1474       6                                                       
HET    GOL  A1475       6                                                       
HETNAM     TYD THYMIDINE-5'-DIPHOSPHATE                                         
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  TYD    2(C10 H16 N2 O11 P2)                                         
FORMUL   5  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   7  GOL    3(C3 H8 O3)                                                  
FORMUL  10  HOH   *701(H2 O)                                                    
HELIX    1   1 GLY A   10  THR A   24  1                                  15    
HELIX    2   2 ASN A   39  SER A   44  5                                   6    
HELIX    3   3 ASP A   61  GLN A   73  1                                  13    
HELIX    4   4 HIS A   85  GLY A   92  1                                   8    
HELIX    5   5 PRO A   93  ILE A  101  1                                   9    
HELIX    6   6 ILE A  101  ALA A  117  1                                  17    
HELIX    7   7 GLY A  119  PHE A  126  1                                   8    
HELIX    8   8 GLU A  135  GLY A  138  5                                   4    
HELIX    9   9 HIS A  142  VAL A  146  5                                   5    
HELIX   10  10 SER A  165  GLY A  186  1                                  22    
HELIX   11  11 LYS A  206  GLY A  218  1                                  13    
HELIX   12  12 VAL A  236  GLY A  250  1                                  15    
HELIX   13  13 ASN A  266  VAL A  281  1                                  16    
HELIX   14  14 SER A  286  GLU A  289  5                                   4    
HELIX   15  15 ALA A  308  GLY A  316  1                                   9    
HELIX   16  16 THR A  322  ASN A  337  1                                  16    
HELIX   17  17 ASN A  337  VAL A  344  1                                   8    
HELIX   18  18 SER A  346  GLU A  358  1                                  13    
HELIX   19  19 GLY B   10  THR B   24  1                                  15    
HELIX   20  20 ASN B   39  SER B   44  5                                   6    
HELIX   21  21 ASP B   61  GLN B   73  1                                  13    
HELIX   22  22 HIS B   85  GLY B   92  1                                   8    
HELIX   23  23 PRO B   93  ILE B  101  1                                   9    
HELIX   24  24 ILE B  101  ALA B  117  1                                  17    
HELIX   25  25 GLY B  119  PHE B  126  1                                   8    
HELIX   26  26 GLU B  135  GLY B  138  5                                   4    
HELIX   27  27 HIS B  142  VAL B  146  5                                   5    
HELIX   28  28 SER B  165  GLY B  186  1                                  22    
HELIX   29  29 LYS B  206  GLU B  217  1                                  12    
HELIX   30  30 VAL B  236  GLY B  250  1                                  15    
HELIX   31  31 ASN B  266  VAL B  281  1                                  16    
HELIX   32  32 SER B  286  GLU B  289  5                                   4    
HELIX   33  33 ALA B  308  GLY B  316  1                                   9    
HELIX   34  34 THR B  322  ASN B  337  1                                  16    
HELIX   35  35 ASN B  337  LYS B  345  1                                   9    
HELIX   36  36 SER B  346  GLU B  358  1                                  13    
SHEET    1   A 7 TYR A  52  HIS A  56  0                                        
SHEET    2   A 7 THR A  27  ASP A  32  1  N  ASN A  30   O  GLU A  55           
SHEET    3   A 7 LYS A   2  THR A   6  1  N  ILE A   5   O  ILE A  31           
SHEET    4   A 7 ALA A  76  HIS A  79  1  O  ALA A  76   N  LEU A   4           
SHEET    5   A 7 ARG A 127  THR A 133  1  O  HIS A 129   N  VAL A  77           
SHEET    6   A 7 THR A 189  CYS A 194  1  O  ILE A 190   N  HIS A 130           
SHEET    7   A 7 THR A 255  ILE A 258  1  O  ILE A 258   N  ASN A 193           
SHEET    1   B 3 ASN A 196  TYR A 198  0                                        
SHEET    2   B 3 ILE A 230  TYR A 235  1  O  LEU A 234   N  ASN A 196           
SHEET    3   B 3 GLU A 263  LYS A 265 -1  O  LYS A 264   N  ARG A 231           
SHEET    1   C 2 LEU A 221  TYR A 224  0                                        
SHEET    2   C 2 ILE A 291  VAL A 294  1  O  THR A 292   N  ILE A 223           
SHEET    1   D 7 TYR B  52  HIS B  56  0                                        
SHEET    2   D 7 THR B  27  ASP B  32  1  N  ASN B  30   O  GLU B  55           
SHEET    3   D 7 LYS B   2  THR B   6  1  N  ILE B   5   O  ILE B  31           
SHEET    4   D 7 ALA B  76  HIS B  79  1  O  ALA B  76   N  LEU B   4           
SHEET    5   D 7 ARG B 127  THR B 133  1  O  HIS B 129   N  VAL B  77           
SHEET    6   D 7 THR B 189  CYS B 194  1  O  ILE B 190   N  HIS B 130           
SHEET    7   D 7 THR B 255  ILE B 258  1  O  ILE B 258   N  ASN B 193           
SHEET    1   E 3 ASN B 196  TYR B 198  0                                        
SHEET    2   E 3 ILE B 230  TYR B 235  1  O  LEU B 234   N  ASN B 196           
SHEET    3   E 3 GLU B 263  LYS B 265 -1  O  LYS B 264   N  ARG B 231           
SHEET    1   F 2 LEU B 221  TYR B 224  0                                        
SHEET    2   F 2 ILE B 291  VAL B 294  1  O  THR B 292   N  ILE B 223           
SITE     1 AC1 20 HIS A  85  VAL A  86  GLU A 135  ASN A 196                    
SITE     2 AC1 20 GLU A 205  LYS A 206  LEU A 207  LEU A 210                    
SITE     3 AC1 20 PRO A 222  TYR A 224  ARG A 231  ASN A 266                    
SITE     4 AC1 20 ARG A 297  HIS A 300  TYR A 357  HOH A2604                    
SITE     5 AC1 20 HOH A2615  HOH A2624  HOH A2636  HOH A2741                    
SITE     1 AC2 20 HIS B  85  VAL B  86  GLU B 135  ASN B 196                    
SITE     2 AC2 20 GLU B 205  LYS B 206  LEU B 207  LEU B 210                    
SITE     3 AC2 20 PRO B 222  TYR B 224  ARG B 231  ASN B 266                    
SITE     4 AC2 20 ARG B 297  HIS B 300  TYR B 357  HOH B2708                    
SITE     5 AC2 20 HOH B2712  HOH B2723  HOH B2726  HOH B2826                    
SITE     1 AC3 36 ALA A   9  GLY A  10  PHE A  11  ILE A  12                    
SITE     2 AC3 36 ASP A  32  LYS A  33  LEU A  34  THR A  35                    
SITE     3 AC3 36 ALA A  37  GLY A  38  ALA A  57  ASP A  58                    
SITE     4 AC3 36 ILE A  59  LEU A  80  ALA A  81  ALA A  82                    
SITE     5 AC3 36 SER A  84  THR A  99  ILE A 131  SER A 132                    
SITE     6 AC3 36 THR A 133  TYR A 167  LYS A 171  CYS A 194                    
SITE     7 AC3 36 SER A 195  ASN A 196  ASN A 197  HOH A2601                    
SITE     8 AC3 36 HOH A2611  HOH A2613  HOH A2627  HOH A2628                    
SITE     9 AC3 36 HOH A2633  HOH A2639  HOH A2645  HOH A2674                    
SITE     1 AC4 36 ALA B   9  GLY B  10  PHE B  11  ILE B  12                    
SITE     2 AC4 36 ASP B  32  LYS B  33  LEU B  34  THR B  35                    
SITE     3 AC4 36 ALA B  37  GLY B  38  ALA B  57  ASP B  58                    
SITE     4 AC4 36 ILE B  59  LEU B  80  ALA B  81  ALA B  82                    
SITE     5 AC4 36 SER B  84  THR B  99  ILE B 131  SER B 132                    
SITE     6 AC4 36 THR B 133  TYR B 167  LYS B 171  CYS B 194                    
SITE     7 AC4 36 SER B 195  ASN B 196  ASN B 197  HOH B2702                    
SITE     8 AC4 36 HOH B2714  HOH B2715  HOH B2720  HOH B2728                    
SITE     9 AC4 36 HOH B2736  HOH B2747  HOH B2750  HOH B2761                    
SITE     1 AC5  2 HOH A2811  ARG B 288                                          
SITE     1 AC6  7 ARG A 179  GLY A 253  GLU A 254  THR A 255                    
SITE     2 AC6  7 LYS A 310  HOH A2714  HOH A2732                               
SITE     1 AC7  5 ASN A 262  LYS A 264  THR A 322  PHE A 323                    
SITE     2 AC7  5 HOH A2900                                                     
CRYST1  169.897  169.897   92.834  90.00  90.00 120.00 P 61         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      0.005886  0.003398  0.000000        0.00000                         
SCALE2      0.000000  0.006796  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010772        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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