GenomeNet

Database: PDB
Entry: 1EFM
LinkDB: 1EFM
Original site: 1EFM 
HEADER    ELONGATION FACTOR                       29-MAY-87   1EFM              
TITLE     STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE              
TITLE    2 AMINO ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    ELONGATION FACTOR                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
MDLTYP    CA ATOMS ONLY, CHAIN A                                                
AUTHOR    F.JURNAK                                                              
REVDAT   3   24-FEB-09 1EFM    1       VERSN                                    
REVDAT   2   15-OCT-91 1EFM    1       REMARK                                   
REVDAT   1   16-JUL-87 1EFM    0                                                
JRNL        AUTH   F.JURNAK                                                     
JRNL        TITL   STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION            
JRNL        TITL 2 OF THE AMINO ACIDS HOMOLOGOUS TO RAS ONCOGENE                
JRNL        TITL 3 PROTEINS.                                                    
JRNL        REF    SCIENCE                       V. 230    32 1985              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   3898365                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.JURNAK,A.MCPHERSON,A.H.J.WANG,A.RICH                       
REMARK   1  TITL   BIOCHEMICAL AND STRUCTURAL STUDIES OF THE                    
REMARK   1  TITL 2 TETRAGONAL CRYSTALLINE MODIFICATION OF THE                   
REMARK   1  TITL 3 ESCHERICHIA COLI ELONGATION FACTOR TU                        
REMARK   1  REF    J.BIOL.CHEM.                  V. 255  6751 1980              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   F.JURNAK,A.RICH,D.MILLER                                     
REMARK   1  TITL   PRELIMINARY X-RAY DIFFRACTION DATA FOR TETRAGONAL            
REMARK   1  TITL 2 CRYSTALS OF TRYPSINIZED ESCHERICHIA COLI                     
REMARK   1  TITL 3 ELONGATION FACTOR                                            
REMARK   1  REF    J.MOL.BIOL.                   V. 115   103 1977              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.ARAI,B.F.C.CLARK,L.DUFFY,M.D.JONES,Y.KAZIRO,               
REMARK   1  AUTH 2 R.A.LAURSEN,J.L'ITALIEN,D.L.MILLER,S.NAGARKATTI,             
REMARK   1  AUTH 3 S.NAKAMURA,K.M.NIELSEN,T.E.PETERSEN,K.TAKAHASHI,             
REMARK   1  AUTH 4 M.WADE                                                       
REMARK   1  TITL   PRIMARY STRUCTURE OF ELONGATION FACTOR TU FROM               
REMARK   1  TITL 2 ESCHERICHIA COLI                                             
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  77  1326 1980              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
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             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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) : 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            : 158                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : 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) : 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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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  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 1EFM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       81.23250            
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       81.23250            
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       49.30450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.40350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       49.30450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.40350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       81.23250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       49.30450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.40350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       81.23250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       49.30450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.40350            
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 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 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 TRYPSIN-MODIFIED EF-TU CONTAINS TWO MAJOR FRAGMENTS                  
REMARK 400 CONSISTING OF RESIDUES 1-44 AND 59-393.  RESIDUES 45-58              
REMARK 400 HAVE BEEN EXCISED.  TO CLARIFY THIS RELATIONSHIP, THE                
REMARK 400 PROTEIN IS REPRESENTED BY ONE SET OF SEQRES RECORDS WITH             
REMARK 400 EXC IN PLACE OF RESIDUES 45-58.                                      
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     SER A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     ILE A    60                                                      
REMARK 465     LEU A   191                                                      
REMARK 465     ALA A   192                                                      
REMARK 465     GLY A   193                                                      
REMARK 465     PHE A   194                                                      
REMARK 465     LEU A   195                                                      
REMARK 465     ASP A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     TYR A   198                                                      
REMARK 465     ILE A   199                                                      
REMARK 465     PRO A   200                                                      
REMARK 465     GLU A   201                                                      
REMARK 465     PRO A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     ARG A   204                                                      
REMARK 465     ALA A   205                                                      
REMARK 465     ILE A   206                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     LYS A   208                                                      
REMARK 465     PRO A   209                                                      
REMARK 465     PHE A   210                                                      
REMARK 465     LEU A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     ILE A   214                                                      
REMARK 465     GLU A   215                                                      
REMARK 465     ASP A   216                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     ILE A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     ARG A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     THR A   225                                                      
REMARK 465     VAL A   226                                                      
REMARK 465     VAL A   227                                                      
REMARK 465     THR A   228                                                      
REMARK 465     GLY A   229                                                      
REMARK 465     ARG A   230                                                      
REMARK 465     VAL A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     ARG A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     ILE A   235                                                      
REMARK 465     ILE A   236                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     VAL A   238                                                      
REMARK 465     GLY A   239                                                      
REMARK 465     GLU A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     VAL A   242                                                      
REMARK 465     GLU A   243                                                      
REMARK 465     ILE A   244                                                      
REMARK 465     VAL A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     ILE A   247                                                      
REMARK 465     LYS A   248                                                      
REMARK 465     GLU A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     GLN A   251                                                      
REMARK 465     LYS A   252                                                      
REMARK 465     SER A   253                                                      
REMARK 465     THR A   254                                                      
REMARK 465     CYS A   255                                                      
REMARK 465     THR A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     VAL A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     MET A   260                                                      
REMARK 465     PHE A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     LYS A   263                                                      
REMARK 465     LEU A   264                                                      
REMARK 465     LEU A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     GLU A   267                                                      
REMARK 465     GLY A   268                                                      
REMARK 465     ARG A   269                                                      
REMARK 465     ALA A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     GLU A   272                                                      
REMARK 465     ASN A   273                                                      
REMARK 465     VAL A   274                                                      
REMARK 465     GLY A   275                                                      
REMARK 465     VAL A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     LEU A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     GLY A   280                                                      
REMARK 465     ILE A   281                                                      
REMARK 465     LYS A   282                                                      
REMARK 465     ARG A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     ILE A   286                                                      
REMARK 465     GLU A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLN A   290                                                      
REMARK 465     VAL A   291                                                      
REMARK 465     LEU A   292                                                      
REMARK 465     ALA A   293                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     PRO A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     THR A   297                                                      
REMARK 465     ILE A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     PRO A   300                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     THR A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     VAL A   308                                                      
REMARK 465     TYR A   309                                                      
REMARK 465     ILE A   310                                                      
REMARK 465     LEU A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     ASP A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     ARG A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     PHE A   322                                                      
REMARK 465     PHE A   323                                                      
REMARK 465     LYS A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     TYR A   326                                                      
REMARK 465     ARG A   327                                                      
REMARK 465     PRO A   328                                                      
REMARK 465     GLN A   329                                                      
REMARK 465     PHE A   330                                                      
REMARK 465     TYR A   331                                                      
REMARK 465     PHE A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     THR A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     ASP A   336                                                      
REMARK 465     VAL A   337                                                      
REMARK 465     THR A   338                                                      
REMARK 465     GLY A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     GLU A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     PRO A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     VAL A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     MET A   349                                                      
REMARK 465     VAL A   350                                                      
REMARK 465     MET A   351                                                      
REMARK 465     PRO A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     ASN A   355                                                      
REMARK 465     ILE A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     VAL A   359                                                      
REMARK 465     VAL A   360                                                      
REMARK 465     THR A   361                                                      
REMARK 465     LEU A   362                                                      
REMARK 465     ILE A   363                                                      
REMARK 465     HIS A   364                                                      
REMARK 465     PRO A   365                                                      
REMARK 465     ILE A   366                                                      
REMARK 465     ALA A   367                                                      
REMARK 465     MET A   368                                                      
REMARK 465     ASP A   369                                                      
REMARK 465     ASP A   370                                                      
REMARK 465     GLY A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     ARG A   373                                                      
REMARK 465     PHE A   374                                                      
REMARK 465     ALA A   375                                                      
REMARK 465     ILE A   376                                                      
REMARK 465     ARG A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     GLY A   380                                                      
REMARK 465     ARG A   381                                                      
REMARK 465     THR A   382                                                      
REMARK 465     VAL A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     ALA A   385                                                      
REMARK 465     GLY A   386                                                      
REMARK 465     VAL A   387                                                      
REMARK 465     VAL A   388                                                      
REMARK 465     ALA A   389                                                      
REMARK 465     LYS A   390                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     LEU A   392                                                      
REMARK 465     SER A   393                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 394                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 395                 
DBREF  1EFM A    1   393  UNP    P02990   EFTU_ECOLI       1    393             
SEQADV 1EFM     A       UNP  P02990    ALA    43 DELETION                       
SEQADV 1EFM     A       UNP  P02990    ARG    44 DELETION                       
SEQADV 1EFM     A       UNP  P02990    ALA    45 DELETION                       
SEQADV 1EFM     A       UNP  P02990    PHE    46 DELETION                       
SEQADV 1EFM     A       UNP  P02990    ASP    47 DELETION                       
SEQADV 1EFM     A       UNP  P02990    GLN    48 DELETION                       
SEQADV 1EFM     A       UNP  P02990    ILE    49 DELETION                       
SEQADV 1EFM     A       UNP  P02990    ASP    50 DELETION                       
SEQADV 1EFM     A       UNP  P02990    ASN    51 DELETION                       
SEQADV 1EFM     A       UNP  P02990    ALA    52 DELETION                       
SEQADV 1EFM     A       UNP  P02990    PRO    53 DELETION                       
SEQADV 1EFM     A       UNP  P02990    GLU    54 DELETION                       
SEQADV 1EFM     A       UNP  P02990    GLU    55 DELETION                       
SEQADV 1EFM     A       UNP  P02990    LYS    56 DELETION                       
SEQRES   1 A  379  SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 A  379  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 A  379  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 A  379  GLY GLY ALA ALA ARG GLY ILE THR ILE ASN THR SER HIS          
SEQRES   5 A  379  VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS VAL          
SEQRES   6 A  379  ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET ILE          
SEQRES   7 A  379  THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL VAL          
SEQRES   8 A  379  ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU HIS          
SEQRES   9 A  379  ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE ILE          
SEQRES  10 A  379  VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU GLU          
SEQRES  11 A  379  LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU LEU          
SEQRES  12 A  379  SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE VAL          
SEQRES  13 A  379  ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA GLU          
SEQRES  14 A  379  TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU ASP          
SEQRES  15 A  379  SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS PRO          
SEQRES  16 A  379  PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER GLY          
SEQRES  17 A  379  ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY ILE          
SEQRES  18 A  379  ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE LYS          
SEQRES  19 A  379  GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET PHE          
SEQRES  20 A  379  ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN VAL          
SEQRES  21 A  379  GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE GLU          
SEQRES  22 A  379  ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS PRO          
SEQRES  23 A  379  HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER LYS          
SEQRES  24 A  379  ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY TYR          
SEQRES  25 A  379  ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY          
SEQRES  26 A  379  THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET PRO          
SEQRES  27 A  379  GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS PRO          
SEQRES  28 A  379  ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG GLU          
SEQRES  29 A  379  GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS VAL          
SEQRES  30 A  379  LEU SER                                                      
HET     MG  A 394       1                                                       
HET    GDP  A 395      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
SITE     1 AC1  1 GDP A 395                                                     
SITE     1 AC2  7 VAL A  20  ASP A  21  GLY A  23  LYS A  24                    
SITE     2 AC2  7 THR A  25  LEU A 175   MG A 394                               
CRYST1   98.609  100.807  162.465  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      0.010141  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009920  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006155        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system