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Database: PDB
Entry: 1DG1
LinkDB: 1DG1
Original site: 1DG1 
HEADER    RNA BINDING PROTEIN                     22-NOV-99   1DG1              
TITLE     WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: G, H;                                                         
COMPND   4 SYNONYM: EF-TU                                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 OTHER_DETAILS: CELL CYTOPLASM EXTRACT                                
KEYWDS    ELONGATION FACTOR, TRNA BINDING, ALPHA BETA SHIFT, TS                 
KEYWDS   2 BINDING PROTEIN, GTPASE, GDP BINDING, RNA BINDING PROTEIN            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.ABEL,M.YODER,R.HILGENFELD,F.JURNAK                                  
REVDAT   4   24-FEB-09 1DG1    1       VERSN                                    
REVDAT   3   01-APR-03 1DG1    1       JRNL                                     
REVDAT   2   29-MAR-00 1DG1    1       REMARK                                   
REVDAT   1   01-DEC-99 1DG1    0                                                
JRNL        AUTH   K.ABEL,M.D.YODER,R.HILGENFELD,F.JURNAK                       
JRNL        TITL   AN ALPHA TO BETA CONFORMATIONAL SWITCH IN EF-TU.             
JRNL        REF    STRUCTURE                     V.   4  1153 1996              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   8939740                                                      
JRNL        DOI    10.1016/S0969-2126(96)00123-2                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0001                         
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  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2015                            
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            : 5926                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.25                          
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.54                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.28                            
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 1DG1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-NOV-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB010053.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 5.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 5                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE CRYSTAL                   
REMARK 200  OPTICS                         : COLLIMATOR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SDMS                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS                               
REMARK 200  DATA SCALING SOFTWARE          : SDMS                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28782                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.123                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06130                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM CITRATE,              
REMARK 280  AMMONIUM ACETATE, PH 5.75, VAPOR DIFFUSION, TEMPERATURE 298.0K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       52.30000            
REMARK 290   SMTRY3   2  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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER, TU WITH A GDP            
REMARK 300 SUBSTRATE BOUND.                                                     
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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 G     0                                                      
REMARK 465     SER G     1                                                      
REMARK 465     LYS G     2                                                      
REMARK 465     GLU G     3                                                      
REMARK 465     LYS G     4                                                      
REMARK 465     PHE G     5                                                      
REMARK 465     GLU G     6                                                      
REMARK 465     ARG G     7                                                      
REMARK 465     THR G     8                                                      
REMARK 465     MET H     0                                                      
REMARK 465     SER H     1                                                      
REMARK 465     LYS H     2                                                      
REMARK 465     GLU H     3                                                      
REMARK 465     LYS H     4                                                      
REMARK 465     PHE H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     ARG H     7                                                      
REMARK 465     THR H     8                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER G 393    CB   OG                                             
REMARK 470     SER H 393    CB   OG                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP G  21       12.36     59.35                                   
REMARK 500    ARG G  58       62.43     63.69                                   
REMARK 500    TYR G 160       31.65    -97.92                                   
REMARK 500    PRO G 163       63.96    -65.53                                   
REMARK 500    ILE G 247      -73.12     67.99                                   
REMARK 500    LYS G 248     -146.96    -98.77                                   
REMARK 500    MET G 260       85.08   -158.68                                   
REMARK 500    PHE G 261       74.05     54.26                                   
REMARK 500    ARG G 262      -31.11     68.26                                   
REMARK 500    ALA G 270      115.81    -39.35                                   
REMARK 500    GLU G 284       -9.36    -59.28                                   
REMARK 500    LEU G 311      171.74    -59.50                                   
REMARK 500    ARG G 333      -60.99     66.72                                   
REMARK 500    TYR H 160       32.22    -88.66                                   
REMARK 500    PRO H 163       70.89    -69.29                                   
REMARK 500    ILE H 247      -67.63     62.08                                   
REMARK 500    LYS H 248     -157.75   -109.18                                   
REMARK 500    ARG H 262      -29.91     74.74                                   
REMARK 500    ARG H 333      -73.00     63.15                                   
REMARK 500    GLU H 348      -71.89   -118.56                                   
REMARK 500    LYS H 390      136.06   -173.92                                   
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 G1096        DISTANCE =  6.70 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G  25   OG1                                                    
REMARK 620 2 GDP G 999   O2B  80.3                                              
REMARK 620 3 HOH G1003   O    75.0  73.1                                        
REMARK 620 4 HOH G1004   O    80.1 156.0  88.5                                  
REMARK 620 5 HOH G1006   O    73.6  93.1 147.5  94.5                            
REMARK 620 6 HOH G1002   O   156.2  76.0 100.3 123.5 104.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H2029   O                                                      
REMARK 620 2 HOH H2030   O    89.9                                              
REMARK 620 3 THR H  25   OG1  81.4 162.9                                        
REMARK 620 4 HOH H2028   O    77.8  98.2  94.4                                  
REMARK 620 5 HOH H2033   O   156.4  86.0  96.1 125.8                            
REMARK 620 6 GDP H1999   O2B  75.2  78.6  84.9 152.7  81.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 998                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 998                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP G 999                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP H 1999                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AIP   RELATED DB: PDB                                   
REMARK 900 ELONGATION FACTOR COMPLEX                                            
REMARK 900 RELATED ID: 1B23   RELATED DB: PDB                                   
REMARK 900 ELONGATION FACTOR COMPLEX                                            
REMARK 900 RELATED ID: 1D2E   RELATED DB: PDB                                   
REMARK 900 ELONGATION FACTOR TU                                                 
REMARK 900 RELATED ID: 1DAR   RELATED DB: PDB                                   
REMARK 900 ELONGATION FACTOR                                                    
REMARK 900 RELATED ID: 1EFC   RELATED DB: PDB                                   
REMARK 900 ELONGATION FACTOR TU                                                 
REMARK 900 RELATED ID: 1EFM   RELATED DB: PDB                                   
REMARK 900 TRYPSIN MODIFIED EF-TU                                               
DBREF  1DG1 G    0   393  UNP    P0A6N1   EFTU_ECOLI       1    394             
DBREF  1DG1 H    0   393  UNP    P0A6N1   EFTU_ECOLI       1    394             
SEQRES   1 G  394  MET SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL          
SEQRES   2 G  394  ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR          
SEQRES   3 G  394  THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR          
SEQRES   4 G  394  TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN          
SEQRES   5 G  394  ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR          
SEQRES   6 G  394  SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA          
SEQRES   7 G  394  HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN          
SEQRES   8 G  394  MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU          
SEQRES   9 G  394  VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG          
SEQRES  10 G  394  GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR          
SEQRES  11 G  394  ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP          
SEQRES  12 G  394  GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU          
SEQRES  13 G  394  LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO          
SEQRES  14 G  394  ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP          
SEQRES  15 G  394  ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE          
SEQRES  16 G  394  LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP          
SEQRES  17 G  394  LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE          
SEQRES  18 G  394  SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG          
SEQRES  19 G  394  GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY          
SEQRES  20 G  394  ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU          
SEQRES  21 G  394  MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU          
SEQRES  22 G  394  ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU          
SEQRES  23 G  394  ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE          
SEQRES  24 G  394  LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU          
SEQRES  25 G  394  SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS          
SEQRES  26 G  394  GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL          
SEQRES  27 G  394  THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL          
SEQRES  28 G  394  MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE          
SEQRES  29 G  394  HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE          
SEQRES  30 G  394  ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA          
SEQRES  31 G  394  LYS VAL LEU SER                                              
SEQRES   1 H  394  MET SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL          
SEQRES   2 H  394  ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR          
SEQRES   3 H  394  THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR          
SEQRES   4 H  394  TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN          
SEQRES   5 H  394  ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR          
SEQRES   6 H  394  SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA          
SEQRES   7 H  394  HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN          
SEQRES   8 H  394  MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU          
SEQRES   9 H  394  VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG          
SEQRES  10 H  394  GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR          
SEQRES  11 H  394  ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP          
SEQRES  12 H  394  GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU          
SEQRES  13 H  394  LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO          
SEQRES  14 H  394  ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP          
SEQRES  15 H  394  ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE          
SEQRES  16 H  394  LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP          
SEQRES  17 H  394  LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE          
SEQRES  18 H  394  SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG          
SEQRES  19 H  394  GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY          
SEQRES  20 H  394  ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU          
SEQRES  21 H  394  MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU          
SEQRES  22 H  394  ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU          
SEQRES  23 H  394  ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE          
SEQRES  24 H  394  LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU          
SEQRES  25 H  394  SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS          
SEQRES  26 H  394  GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL          
SEQRES  27 H  394  THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL          
SEQRES  28 H  394  MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE          
SEQRES  29 H  394  HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE          
SEQRES  30 H  394  ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA          
SEQRES  31 H  394  LYS VAL LEU SER                                              
HET     MG  G 998       1                                                       
HET     MG  H 998       1                                                       
HET    GDP  G 999      28                                                       
HET    GDP  H1999      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   7  HOH   *193(H2 O)                                                    
HELIX    1   1 GLY G   23  GLY G   40  1                                  18    
HELIX    2   2 ALA G   45  ASN G   51  1                                   7    
HELIX    3   3 GLY G   83  GLY G   94  1                                  12    
HELIX    4   4 MET G  112  GLY G  126  1                                  15    
HELIX    5   5 ASP G  142  TYR G  160  1                                  19    
HELIX    6   6 PRO G  163  THR G  167  5                                   5    
HELIX    7   7 SER G  173  GLY G  180  1                                   8    
HELIX    8   8 ASP G  181  ILE G  199  1                                  19    
HELIX    9   9 ARG G  204  LYS G  208  5                                   5    
HELIX   10  10 LYS G  282  ILE G  286  5                                   5    
HELIX   11  11 SER G  312  GLY G  316  5                                   5    
HELIX   12  12 GLY H   23  GLY H   40  1                                  18    
HELIX   13  13 ALA H   45  ASN H   51  1                                   7    
HELIX   14  14 GLY H   83  THR H   93  1                                  11    
HELIX   15  15 MET H  112  GLY H  126  1                                  15    
HELIX   16  16 ASP H  142  TYR H  160  1                                  19    
HELIX   17  17 PRO H  163  THR H  167  5                                   5    
HELIX   18  18 SER H  173  GLY H  180  1                                   8    
HELIX   19  19 ASP H  181  ILE H  199  1                                  19    
HELIX   20  20 ARG H  204  LYS H  208  5                                   5    
HELIX   21  21 LYS H  282  ILE H  286  5                                   5    
SHEET    1   A 6 SER G  65  ASP G  70  0                                        
SHEET    2   A 6 HIS G  75  ASP G  80 -1  N  TYR G  76   O  TYR G  69           
SHEET    3   A 6 HIS G  11  ILE G  17  1  O  VAL G  12   N  ALA G  77           
SHEET    4   A 6 GLY G 100  ALA G 106  1  N  GLY G 100   O  ASN G  13           
SHEET    5   A 6 TYR G 129  ASN G 135  1  O  TYR G 129   N  ALA G 101           
SHEET    6   A 6 ILE G 169  ARG G 171  1  O  VAL G 170   N  LEU G 134           
SHEET    1   B 2 GLU G  54  ALA G  57  0                                        
SHEET    2   B 2 ILE G  60  ASN G  63 -1  O  ILE G  60   N  ALA G  57           
SHEET    1   C 7 ASP G 216  ILE G 220  0                                        
SHEET    2   C 7 GLY G 224  ARG G 230 -1  O  GLY G 224   N  ILE G 220           
SHEET    3   C 7 ASN G 273  ARG G 279 -1  N  VAL G 274   O  GLY G 229           
SHEET    4   C 7 GLN G 251  MET G 260 -1  O  THR G 254   N  ARG G 279           
SHEET    5   C 7 GLU G 241  VAL G 245 -1  N  VAL G 242   O  SER G 253           
SHEET    6   C 7 VAL G 291  ALA G 293 -1  O  VAL G 291   N  VAL G 245           
SHEET    7   C 7 LEU G 211  PRO G 213 -1  O  LEU G 212   N  LEU G 292           
SHEET    1  C1 5 ASP G 216  ILE G 220  0                                        
SHEET    2  C1 5 GLY G 224  ARG G 230 -1  O  GLY G 224   N  ILE G 220           
SHEET    3  C1 5 ASN G 273  ARG G 279 -1  N  VAL G 274   O  GLY G 229           
SHEET    4  C1 5 GLN G 251  MET G 260 -1  O  THR G 254   N  ARG G 279           
SHEET    5  C1 5 LYS G 263  LEU G 265 -1  O  LYS G 263   N  MET G 260           
SHEET    1   D 2 ILE G 235  LYS G 237  0                                        
SHEET    2   D 2 GLU G 267  ARG G 269 -1  O  GLY G 268   N  ILE G 236           
SHEET    1   E 7 PRO G 300  ILE G 310  0                                        
SHEET    2   E 7 ASN G 355  ALA G 367 -1  O  ILE G 356   N  VAL G 308           
SHEET    3   E 7 THR G 335  GLU G 342 -1  O  THR G 338   N  ILE G 363           
SHEET    4   E 7 GLN G 329  PHE G 332 -1  N  PHE G 330   O  VAL G 337           
SHEET    5   E 7 ARG G 373  GLU G 378 -1  O  ALA G 375   N  TYR G 331           
SHEET    6   E 7 ARG G 381  SER G 393 -1  O  ARG G 381   N  GLU G 378           
SHEET    7   E 7 PRO G 300  ILE G 310 -1  N  THR G 302   O  SER G 393           
SHEET    1   F 6 SER H  65  THR H  71  0                                        
SHEET    2   F 6 ARG H  74  ASP H  80 -1  O  ARG H  74   N  THR H  71           
SHEET    3   F 6 HIS H  11  ILE H  17  1  N  VAL H  12   O  HIS H  75           
SHEET    4   F 6 GLY H 100  ALA H 106  1  N  GLY H 100   O  ASN H  13           
SHEET    5   F 6 ILE H 130  ASN H 135  1  O  ILE H 131   N  LEU H 103           
SHEET    6   F 6 ILE H 169  ARG H 171  1  O  VAL H 170   N  LEU H 134           
SHEET    1   G 2 GLU H  54  ALA H  57  0                                        
SHEET    2   G 2 ILE H  60  ASN H  63 -1  N  ILE H  60   O  ALA H  57           
SHEET    1   H 7 ASP H 216  ILE H 220  0                                        
SHEET    2   H 7 GLY H 224  ARG H 230 -1  O  GLY H 224   N  ILE H 220           
SHEET    3   H 7 ASN H 273  ARG H 279 -1  N  VAL H 274   O  GLY H 229           
SHEET    4   H 7 GLN H 251  MET H 260 -1  O  THR H 254   N  ARG H 279           
SHEET    5   H 7 GLU H 241  VAL H 245 -1  O  VAL H 242   N  SER H 253           
SHEET    6   H 7 VAL H 291  ALA H 293 -1  O  VAL H 291   N  VAL H 245           
SHEET    7   H 7 LEU H 211  PRO H 213 -1  O  LEU H 212   N  LEU H 292           
SHEET    1  H1 5 ASP H 216  ILE H 220  0                                        
SHEET    2  H1 5 GLY H 224  ARG H 230 -1  O  GLY H 224   N  ILE H 220           
SHEET    3  H1 5 ASN H 273  ARG H 279 -1  N  VAL H 274   O  GLY H 229           
SHEET    4  H1 5 GLN H 251  MET H 260 -1  O  THR H 254   N  ARG H 279           
SHEET    5  H1 5 LYS H 263  LEU H 265 -1  O  LYS H 263   N  MET H 260           
SHEET    1   I 2 ILE H 235  LYS H 237  0                                        
SHEET    2   I 2 GLU H 267  ARG H 269 -1  N  GLY H 268   O  ILE H 236           
SHEET    1   J 7 LYS H 299  ILE H 310  0                                        
SHEET    2   J 7 ASN H 355  MET H 368 -1  O  ILE H 356   N  VAL H 308           
SHEET    3   J 7 THR H 335  GLU H 342 -1  O  THR H 338   N  ILE H 363           
SHEET    4   J 7 GLN H 329  PHE H 332 -1  N  PHE H 330   O  VAL H 337           
SHEET    5   J 7 ARG H 373  GLU H 378 -1  O  ALA H 375   N  TYR H 331           
SHEET    6   J 7 ARG H 381  SER H 393 -1  O  ARG H 381   N  GLU H 378           
SHEET    7   J 7 LYS H 299  ILE H 310 -1  N  THR H 302   O  SER H 393           
SHEET    1   K 2 PHE H 322  PHE H 323  0                                        
SHEET    2   K 2 MET H 349  VAL H 350 -1  N  VAL H 350   O  PHE H 322           
LINK        MG    MG G 998                 OG1 THR G  25     1555   1555  2.24  
LINK        MG    MG G 998                 O2B GDP G 999     1555   1555  2.31  
LINK        MG    MG G 998                 O   HOH G1003     1555   1555  2.24  
LINK        MG    MG G 998                 O   HOH G1004     1555   1555  2.11  
LINK        MG    MG G 998                 O   HOH G1006     1555   1555  2.26  
LINK        MG    MG G 998                 O   HOH G1002     1555   1555  2.20  
LINK        MG    MG H 998                 O   HOH H2029     1555   1555  2.22  
LINK        MG    MG H 998                 O   HOH H2030     1555   1555  2.27  
LINK        MG    MG H 998                 OG1 THR H  25     1555   1555  2.17  
LINK        MG    MG H 998                 O   HOH H2028     1555   1555  2.26  
LINK        MG    MG H 998                 O   HOH H2033     1555   1555  2.16  
LINK        MG    MG H 998                 O2B GDP H1999     1555   1555  2.40  
SITE     1 AC1  6 THR G  25  GDP G 999  HOH G1002  HOH G1003                    
SITE     2 AC1  6 HOH G1004  HOH G1006                                          
SITE     1 AC2  7 THR H  25  ASP H  80  GDP H1999  HOH H2028                    
SITE     2 AC2  7 HOH H2029  HOH H2030  HOH H2033                               
SITE     1 AC3 17 VAL G  20  ASP G  21  HIS G  22  GLY G  23                    
SITE     2 AC3 17 LYS G  24  THR G  25  THR G  26  ASN G 135                    
SITE     3 AC3 17 LYS G 136  ASP G 138  MET G 139  SER G 173                    
SITE     4 AC3 17 ALA G 174  LEU G 175   MG G 998  HOH G1002                    
SITE     5 AC3 17 HOH G1003                                                     
SITE     1 AC4 19 VAL H  20  ASP H  21  HIS H  22  GLY H  23                    
SITE     2 AC4 19 LYS H  24  THR H  25  THR H  26  ASN H 135                    
SITE     3 AC4 19 LYS H 136  ASP H 138  SER H 173  ALA H 174                    
SITE     4 AC4 19 LEU H 175   MG H 998  HOH H2029  HOH H2030                    
SITE     5 AC4 19 HOH H2033  HOH H2034  HOH H2035                               
CRYST1   63.600  104.600   67.200  90.00  97.02  90.00 P 1 21 1      4          
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      0.015723  0.000000  0.001936        0.00000                         
SCALE2      0.000000  0.009560  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014993        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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