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Database: PDB
Entry: 2JFN
LinkDB: 2JFN
Original site: 2JFN 
HEADER    ISOMERASE                               03-FEB-07   2JFN              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GLUTAMATE RACEMASE              
TITLE    2 IN COMPLEX WITH L-GLUTAMATE AND ACTIVATOR UDP-MURNAC-ALA             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RACEMASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 5.1.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CELL WALL, ISOMERASE, CELL SHAPE, UDP- MURNAC-ALA,                    
KEYWDS   2 PEPTIDOGLYCAN BIOSYNTHESIS, GLUTAMATE RACEMASE,                      
KEYWDS   3 PEPTIDOGLYCAN SYNTHESIS                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.LUNDQVIST                                                           
REVDAT   2   24-FEB-09 2JFN    1       VERSN                                    
REVDAT   1   03-JUL-07 2JFN    0                                                
JRNL        AUTH   T.LUNDQVIST,S.L.FISHER,G.KERN,R.H.A.FOLMER,Y.XUE,            
JRNL        AUTH 2 D.T.NEWTON,T.A.KEATING,R.A.ALM,B.L.M.DE JONGE                
JRNL        TITL   EXPLOITATION OF STRUCTURAL AND REGULATORY                    
JRNL        TITL 2 DIVERSITY IN GLUTAMATE RACEMASES                             
JRNL        REF    NATURE                        V. 447   817 2007              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   17568739                                                     
JRNL        DOI    10.1038/NATURE05689                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.9  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2000.2                                           
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  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.9                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 26542                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.2185                          
REMARK   3   FREE R VALUE                     : 0.2440                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.8                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1344                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 2047                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 221                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.991                                                
REMARK   3    B22 (A**2) : -8.126                                               
REMARK   3    B33 (A**2) : 4.136                                                
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : 0.000                                                
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
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) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006037                        
REMARK   3   BOND ANGLES            (DEGREES) : 1.31354                         
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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        : 0.373583                                             
REMARK   3   BSOL        : 48.6342                                              
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  : A                                              
REMARK   3  TOPOLOGY FILE  1   : A                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2JFN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  05-FEB-07.                 
REMARK 100 THE PDBE ID CODE IS EBI-31338.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9456                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 338825                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN FORMULATED AT 10 MG/ML           
REMARK 280  WITH 200MM AMMONIUM ACETATE PH 7.4, 5MM D-L GLUTAMATE, 1            
REMARK 280  MM TCEP AND IN 0.6 MM OF THE ACTIVATOR MUR-NAC-ALA AND              
REMARK 280  CRYSTALLISED WITH 100 MM SODIUM ACETATE PH 4.55-10% MME             
REMARK 280  2000 AND 30% GLYCEROL                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.06000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.06000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       41.52500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.41000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       41.52500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.41000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.06000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       41.52500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.41000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       37.06000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       41.52500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.41000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 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     ALA A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     CYS A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     GLU A    19                                                      
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 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    SER A  96      -76.55    -44.07                                   
REMARK 500    THR A  97      -71.72    -35.08                                   
REMARK 500    ALA A 117       48.99    -72.64                                   
REMARK 500    GLU A 242      -28.24   -145.49                                   
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 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A1287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMA A1286                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2JFO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF E. FAECALIS GLUTAMATE                          
REMARK 900  RACEMASE IN COMPLEX WITH D- AND L-                                  
REMARK 900  GLUTAMATE                                                           
REMARK 900 RELATED ID: 2JFP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF E. FAECALIS GLUTAMATE                          
REMARK 900  RACEMASE IN COMPLEX WITH D-GLUTAMATE                                
REMARK 900 RELATED ID: 2JFQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S. AUREUS GLUTAMATE                            
REMARK 900  RACEMASE IN COMPLEX WITH D-GLUTAMATE                                
REMARK 900 RELATED ID: 2JFU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF E. FAECIUM GLUTAMATE                           
REMARK 900  RACEMASE IN COMPLEX WITH PHOSPHATE                                  
DBREF  2JFN A    1   285  UNP    P22634   MURI_ECOLI       1    285             
SEQRES   1 A  285  MET ALA THR LYS LEU GLN ASP GLY ASN THR PRO CYS LEU          
SEQRES   2 A  285  ALA ALA THR PRO SER GLU PRO ARG PRO THR VAL LEU VAL          
SEQRES   3 A  285  PHE ASP SER GLY VAL GLY GLY LEU SER VAL TYR ASP GLU          
SEQRES   4 A  285  ILE ARG HIS LEU LEU PRO ASP LEU HIS TYR ILE TYR ALA          
SEQRES   5 A  285  PHE ASP ASN VAL ALA PHE PRO TYR GLY GLU LYS SER GLU          
SEQRES   6 A  285  ALA PHE ILE VAL GLU ARG VAL VAL ALA ILE VAL THR ALA          
SEQRES   7 A  285  VAL GLN GLU ARG TYR PRO LEU ALA LEU ALA VAL VAL ALA          
SEQRES   8 A  285  CYS ASN THR ALA SER THR VAL SER LEU PRO ALA LEU ARG          
SEQRES   9 A  285  GLU LYS PHE ASP PHE PRO VAL VAL GLY VAL VAL PRO ALA          
SEQRES  10 A  285  ILE LYS PRO ALA ALA ARG LEU THR ALA ASN GLY ILE VAL          
SEQRES  11 A  285  GLY LEU LEU ALA THR ARG GLY THR VAL LYS ARG SER TYR          
SEQRES  12 A  285  THR HIS GLU LEU ILE ALA ARG PHE ALA ASN GLU CYS GLN          
SEQRES  13 A  285  ILE GLU MET LEU GLY SER ALA GLU MET VAL GLU LEU ALA          
SEQRES  14 A  285  GLU ALA LYS LEU HIS GLY GLU ASP VAL SER LEU ASP ALA          
SEQRES  15 A  285  LEU LYS ARG ILE LEU ARG PRO TRP LEU ARG MET LYS GLU          
SEQRES  16 A  285  PRO PRO ASP THR VAL VAL LEU GLY CYS THR HIS PHE PRO          
SEQRES  17 A  285  LEU LEU GLN GLU GLU LEU LEU GLN VAL LEU PRO GLU GLY          
SEQRES  18 A  285  THR ARG LEU VAL ASP SER GLY ALA ALA ILE ALA ARG ARG          
SEQRES  19 A  285  THR ALA TRP LEU LEU GLU HIS GLU ALA PRO ASP ALA LYS          
SEQRES  20 A  285  SER ALA ASP ALA ASN ILE ALA PHE CYS MET ALA MET THR          
SEQRES  21 A  285  PRO GLY ALA GLU GLN LEU LEU PRO VAL LEU GLN ARG TYR          
SEQRES  22 A  285  GLY PHE GLU THR LEU GLU LYS LEU ALA VAL LEU GLY              
HET    GLU  A1287      10                                                       
HET    UMA  A1286      49                                                       
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     UMA URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-                       
HETNAM   2 UMA  ALANINE                                                         
FORMUL   2  GLU    C5 H9 N O4                                                   
FORMUL   2  UMA    C23 H36 N4 O20 P2                                            
FORMUL   3  HOH   *221(H2 O1)                                                   
HELIX    1   1 GLY A   32  LEU A   44  1                                  13    
HELIX    2   2 SER A   64  TYR A   83  1                                  20    
HELIX    3   3 CYS A   92  PHE A  107  1                                  16    
HELIX    4   4 ALA A  117  THR A  125  1                                   9    
HELIX    5   5 GLY A  137  LYS A  140  5                                   4    
HELIX    6   6 ARG A  141  PHE A  151  1                                  11    
HELIX    7   7 SER A  162  HIS A  174  1                                  13    
HELIX    8   8 SER A  179  LEU A  187  1                                   9    
HELIX    9   9 LEU A  187  ARG A  192  1                                   6    
HELIX   10  10 HIS A  206  LEU A  209  5                                   4    
HELIX   11  11 LEU A  210  LEU A  218  1                                   9    
HELIX   12  12 SER A  227  GLU A  242  1                                  16    
HELIX   13  13 THR A  260  GLN A  265  1                                   6    
HELIX   14  14 LEU A  266  TYR A  273  1                                   8    
SHEET    1  AA 4 VAL A 111  VAL A 112  0                                        
SHEET    2  AA 4 LEU A  87  VAL A  90  1  O  ALA A  88   N  VAL A 112           
SHEET    3  AA 4 ARG A  21  ASP A  28  1  O  LEU A  25   N  VAL A  89           
SHEET    4  AA 4 LYS A 247  SER A 248 -1  O  SER A 248   N  ARG A  21           
SHEET    1  AB 6 VAL A 111  VAL A 112  0                                        
SHEET    2  AB 6 LEU A  87  VAL A  90  1  O  ALA A  88   N  VAL A 112           
SHEET    3  AB 6 ARG A  21  ASP A  28  1  O  LEU A  25   N  VAL A  89           
SHEET    4  AB 6 HIS A  48  PHE A  53  1  O  HIS A  48   N  VAL A  24           
SHEET    5  AB 6 ILE A 253  CYS A 256  1  O  ILE A 253   N  TYR A  51           
SHEET    6  AB 6 THR A 277  LYS A 280  1  O  THR A 277   N  ALA A 254           
SHEET    1  AC 4 GLN A 156  GLY A 161  0                                        
SHEET    2  AC 4 ILE A 129  ALA A 134  1  O  VAL A 130   N  GLU A 158           
SHEET    3  AC 4 THR A 199  LEU A 202  1  O  THR A 199   N  GLY A 131           
SHEET    4  AC 4 ARG A 223  VAL A 225  1  O  ARG A 223   N  VAL A 200           
CISPEP   1 PHE A   58    PRO A   59          0         0.04                     
SITE     1 AC1 13 ASP A  28  SER A  29  PHE A  58  PRO A  59                    
SITE     2 AC1 13 TYR A  60  GLY A  61  CYS A  92  ASN A  93                    
SITE     3 AC1 13 THR A  94  CYS A 204  THR A 205  HIS A 206                    
SITE     4 AC1 13 HOH A2089                                                     
SITE     1 AC2 24 LEU A 100  ARG A 104  VAL A 112  GLY A 113                    
SITE     2 AC2 24 VAL A 114  VAL A 115  PRO A 116  ALA A 117                    
SITE     3 AC2 24 LYS A 119  PRO A 120  SER A 227  ALA A 230                    
SITE     4 AC2 24 ILE A 231  ARG A 233  ARG A 234  HOH A2084                    
SITE     5 AC2 24 HOH A2166  HOH A2213  HOH A2214  HOH A2215                    
SITE     6 AC2 24 HOH A2217  HOH A2218  HOH A2220  HOH A2221                    
CRYST1   83.050  112.820   74.120  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012041  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008864  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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