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Database: PDB
Entry: 1EFC
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HEADER    RNA BINDING PROTEIN                     24-NOV-98   1EFC              
TITLE     INTACT ELONGATION FACTOR FROM E.COLI                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (ELONGATION FACTOR);                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: EFTU;                                                       
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    TRANSPORT AND PROTECTION PROTEIN, RNA BINDING PROTEIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SONG,M.R.PARSONS,S.ROWSELL,G.LEONARD,S.E.V.PHILLIPS                 
REVDAT   4   24-FEB-09 1EFC    1       VERSN                                    
REVDAT   3   01-APR-03 1EFC    1       JRNL                                     
REVDAT   2   09-JUL-99 1EFC    1       HEADER DBREF                             
REVDAT   1   18-MAR-99 1EFC    0                                                
JRNL        AUTH   H.SONG,M.R.PARSONS,S.ROWSELL,G.LEONARD,S.E.PHILLIPS          
JRNL        TITL   CRYSTAL STRUCTURE OF INTACT ELONGATION FACTOR                
JRNL        TITL 2 EF-TU FROM ESCHERICHIA COLI IN GDP CONFORMATION AT           
JRNL        TITL 3 2.05 A RESOLUTION.                                           
JRNL        REF    J.MOL.BIOL.                   V. 285  1245 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9918724                                                      
JRNL        DOI    10.1006/JMBI.1998.2387                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.ABEL,M.D.YODER,R.HILGENFELD,F.JURNAK                       
REMARK   1  TITL   AN ALPHA TO BETA CONFORMATIONAL SWITCH IN EF-TU              
REMARK   1  REF    STRUCTURE                     V.   4  1153 1996              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.POLEKHINA,S.THIRUP,M.KJELDGAARD,P.NISSEN,                  
REMARK   1  AUTH 2 C.LIPPMANN,J.NYBORG                                          
REMARK   1  TITL   HELIX UNWINDING IN THE EFFECTOR REGION OF                    
REMARK   1  TITL 2 ELONGATION FACTOR EF-TU-GDP                                  
REMARK   1  REF    STRUCTURE                     V.   4  1141 1996              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.NISSEN,M.KJELDGAARD,S.THIRUP,G.POLEKHINA,                  
REMARK   1  AUTH 2 L.RESHETNIKOVA,B.F.C.CLARK,J.NYBORG                          
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF                  
REMARK   1  TITL 2 PHE-TRNA, EF-TU AND GTP ANALOGUE                             
REMARK   1  REF    SCIENCE                       V. 270  1464 1995              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   M.KJELDGAARD,P.NISSEN,S.THIRUP,J.NYBORG                      
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU             
REMARK   1  TITL 2 FROM T. AQUATICUS IN THE GTP CONFORMATION                    
REMARK   1  REF    STRUCTURE                     V.   1    35 1993              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.KJELDGAARD,J.NYBORG                                        
REMARK   1  TITL   REFINED STRUCTURE OF ELONGATION FACTOR EF-TU FROM            
REMARK   1  TITL 2 E. COLI                                                      
REMARK   1  REF    J.MOL.BIOL.                   V. 223   721 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 52808                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2640                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5940                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 446                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.00                          
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.010 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.020 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EFC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-98.                  
REMARK 100 THE RCSB ID CODE IS RCSB000160.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97899,0.97916,0.91850            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61876                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.08200                            
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) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      121.56000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.54000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      121.56000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.54000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     PHE B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ARG B     7                                                      
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 A 393    CB   OG                                             
REMARK 470     SER B 393    CB   OG                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   564     O    HOH B   627              2.13            
REMARK 500   OE1  GLU A   152     O    HOH A   632              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   702     O    HOH B   702     2585     1.44            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A  20   CB  -  CA  -  C   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ASP A  80   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 116   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 204   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG A 204   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 262   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    THR A 302   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ASP A 314   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A 318   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG A 318   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 327   CD  -  NE  -  CZ  ANGL. DEV. =  27.6 DEGREES          
REMARK 500    ARG A 327   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG A 327   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    THR A 334   N   -  CA  -  CB  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    ASP A 369   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    VAL B  20   CB  -  CA  -  C   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    ASP B  21   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    TYR B  69   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    CYS B  81   CA  -  CB  -  SG  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ASP B 109   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG B 116   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLU B 117   OE1 -  CD  -  OE2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG B 171   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP B 181   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 262   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG B 269   CD  -  NE  -  CZ  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG B 269   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 269   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B 288   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG B 327   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 333   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG B 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG B 381   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A  58       13.46     55.12                                   
REMARK 500    THR A  93     -108.50    -66.39                                   
REMARK 500    ALA A  96     -147.52    -85.52                                   
REMARK 500    GLN A  97       58.42    157.79                                   
REMARK 500    ASP A 142      103.59    -25.71                                   
REMARK 500    SER A 221     -112.73     11.65                                   
REMARK 500    ARG A 223       -7.42   -179.34                                   
REMARK 500    ILE A 247      -53.87     66.55                                   
REMARK 500    PHE A 261     -112.58     63.22                                   
REMARK 500    ALA A 270      123.65    -38.63                                   
REMARK 500    ARG A 333      -54.62     70.78                                   
REMARK 500    THR A 334      -12.46   -141.35                                   
REMARK 500    GLU A 348      -20.80   -140.24                                   
REMARK 500    ALA B  57      117.20   -168.80                                   
REMARK 500    THR B  93      -83.22   -112.74                                   
REMARK 500    SER B 221      146.13    -38.24                                   
REMARK 500    ARG B 223       38.06     39.05                                   
REMARK 500    ILE B 247      -64.44     63.66                                   
REMARK 500    PHE B 261     -110.67     62.67                                   
REMARK 500    ARG B 333      -64.52     58.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 GDP A 513   O2B 100.6                                              
REMARK 620 3 HOH A 514   O    90.0 100.1                                        
REMARK 620 4 HOH A 518   O    91.9  85.0 174.1                                  
REMARK 620 5 HOH A 523   O   166.7  92.4  89.9  87.0                            
REMARK 620 6 HOH A 525   O    82.7 165.2  94.2  80.5  84.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 521   O                                                      
REMARK 620 2 HOH B 523   O   176.8                                              
REMARK 620 3 HOH B 520   O    87.8  90.0                                        
REMARK 620 4 HOH B 522   O    89.4  92.8  86.5                                  
REMARK 620 5 GDP B 514   O2B  96.1  86.2 174.2  89.3                            
REMARK 620 6 THR B  25   OG1  84.6  93.0  87.1 171.4  97.5                      
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 A 501                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 502                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 513                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 514                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 EF-TU IS CODED FOR BY TWO DIFFERENT GENES. THE SEQUENCE              
REMARK 999 STRUCTURE ANALYSIS CARRIED OUT ON THIS MIXTURE SHOWS THAT            
REMARK 999 THE C-TERMINAL RESIDUE OCCURS AS GLY/SER IN THE RATIO OF 3/          
REMARK 999 1. THIS RESIDUE IS IDENTIFIED AS GLY ON THE *SEQRES*                 
REMARK 999 RECORDS BELOW.                                                       
DBREF  1EFC A    1   393  UNP    P0A6N1   EFTU_ECOLI       2    394             
DBREF  1EFC B    1   393  UNP    P0A6N1   EFTU_ECOLI       2    394             
SEQRES   1 A  393  SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 A  393  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 A  393  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 A  393  GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA          
SEQRES   5 A  393  PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER          
SEQRES   6 A  393  HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS          
SEQRES   7 A  393  VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET          
SEQRES   8 A  393  ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL          
SEQRES   9 A  393  VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU          
SEQRES  10 A  393  HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE          
SEQRES  11 A  393  ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU          
SEQRES  12 A  393  GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU          
SEQRES  13 A  393  LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE          
SEQRES  14 A  393  VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA          
SEQRES  15 A  393  GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU          
SEQRES  16 A  393  ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS          
SEQRES  17 A  393  PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER          
SEQRES  18 A  393  GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY          
SEQRES  19 A  393  ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE          
SEQRES  20 A  393  LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET          
SEQRES  21 A  393  PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN          
SEQRES  22 A  393  VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE          
SEQRES  23 A  393  GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS          
SEQRES  24 A  393  PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER          
SEQRES  25 A  393  LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY          
SEQRES  26 A  393  TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR          
SEQRES  27 A  393  GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET          
SEQRES  28 A  393  PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS          
SEQRES  29 A  393  PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG          
SEQRES  30 A  393  GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS          
SEQRES  31 A  393  VAL LEU SER                                                  
SEQRES   1 B  393  SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 B  393  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 B  393  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 B  393  GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA          
SEQRES   5 B  393  PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER          
SEQRES   6 B  393  HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS          
SEQRES   7 B  393  VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET          
SEQRES   8 B  393  ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL          
SEQRES   9 B  393  VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU          
SEQRES  10 B  393  HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE          
SEQRES  11 B  393  ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU          
SEQRES  12 B  393  GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU          
SEQRES  13 B  393  LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE          
SEQRES  14 B  393  VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA          
SEQRES  15 B  393  GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU          
SEQRES  16 B  393  ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS          
SEQRES  17 B  393  PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER          
SEQRES  18 B  393  GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY          
SEQRES  19 B  393  ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE          
SEQRES  20 B  393  LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET          
SEQRES  21 B  393  PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN          
SEQRES  22 B  393  VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE          
SEQRES  23 B  393  GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS          
SEQRES  24 B  393  PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER          
SEQRES  25 B  393  LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY          
SEQRES  26 B  393  TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR          
SEQRES  27 B  393  GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET          
SEQRES  28 B  393  PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS          
SEQRES  29 B  393  PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG          
SEQRES  30 B  393  GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS          
SEQRES  31 B  393  VAL LEU SER                                                  
HET     MG  A 501       1                                                       
HET     MG  B 502       1                                                       
HET    GDP  A 513      28                                                       
HET    GDP  B 514      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   *446(H2 O)                                                    
HELIX    1   1 LYS A   24  TYR A   39  1                                  16    
HELIX    2   2 PHE A   46  ASP A   50  1                                   5    
HELIX    3   3 HIS A   84  ILE A   92  1                                   9    
HELIX    4   4 PRO A  113  VAL A  125  1                                  13    
HELIX    5   5 GLU A  143  TYR A  160  1                                  18    
HELIX    6   6 GLY A  164  ASP A  166  5                                   3    
HELIX    7   7 ALA A  174  LEU A  178  1                                   5    
HELIX    8   8 ALA A  182  TYR A  198  1                                  17    
HELIX    9   9 ALA A  205  ASP A  207  5                                   3    
HELIX   10  10 ARG A  283  GLU A  285  5                                   3    
HELIX   11  11 LYS A  313  GLU A  315  5                                   3    
HELIX   12  12 LYS B   24  TYR B   39  1                                  16    
HELIX   13  13 PHE B   46  ASP B   50  1                                   5    
HELIX   14  14 HIS B   84  ILE B   92  1                                   9    
HELIX   15  15 PRO B  113  VAL B  125  1                                  13    
HELIX   16  16 CYS B  137  MET B  139  5                                   3    
HELIX   17  17 GLU B  143  GLN B  159  1                                  17    
HELIX   18  18 GLY B  164  ASP B  166  5                                   3    
HELIX   19  19 ALA B  174  LEU B  178  1                                   5    
HELIX   20  20 ALA B  182  TYR B  198  1                                  17    
HELIX   21  21 ALA B  205  ASP B  207  5                                   3    
HELIX   22  22 ARG B  283  GLU B  285  5                                   3    
HELIX   23  23 LYS B  313  GLU B  315  5                                   3    
SHEET    1   A 6 ILE A 169  ARG A 171  0                                        
SHEET    2   A 6 ILE A 130  ASN A 135  1  N  VAL A 132   O  VAL A 170           
SHEET    3   A 6 GLY A 100  ALA A 106  1  N  ALA A 101   O  ILE A 131           
SHEET    4   A 6 PRO A  10  ILE A  17  1  N  GLY A  15   O  GLY A 100           
SHEET    5   A 6 ARG A  74  ASP A  80  1  N  HIS A  75   O  PRO A  10           
SHEET    6   A 6 SER A  65  ASP A  70 -1  N  TYR A  69   O  TYR A  76           
SHEET    1   B 2 GLU A  54  ALA A  57  0                                        
SHEET    2   B 2 ILE A  60  ASN A  63 -1  N  ILE A  62   O  GLU A  55           
SHEET    1   C 4 LEU A 211  PRO A 213  0                                        
SHEET    2   C 4 VAL A 291  ALA A 293 -1  N  LEU A 292   O  LEU A 212           
SHEET    3   C 4 GLU A 241  VAL A 245 -1  N  VAL A 245   O  VAL A 291           
SHEET    4   C 4 GLN A 251  THR A 254 -1  N  SER A 253   O  VAL A 242           
SHEET    1   D 5 ASP A 216  SER A 219  0                                        
SHEET    2   D 5 THR A 225  ARG A 230 -1  N  THR A 228   O  ASP A 216           
SHEET    3   D 5 ASN A 273  LEU A 278 -1  N  LEU A 278   O  THR A 225           
SHEET    4   D 5 CYS A 255  MET A 260 -1  N  GLU A 259   O  GLY A 275           
SHEET    5   D 5 LYS A 263  LEU A 265 -1  N  LEU A 265   O  VAL A 258           
SHEET    1   E 2 ILE A 235  LYS A 237  0                                        
SHEET    2   E 2 GLU A 267  ARG A 269 -1  N  GLY A 268   O  ILE A 236           
SHEET    1   F 2 LYS A 299  HIS A 301  0                                        
SHEET    2   F 2 ILE A 366  MET A 368 -1  N  MET A 368   O  LYS A 299           
SHEET    1   G 7 THR A 335  THR A 338  0                                        
SHEET    2   G 7 GLN A 329  PHE A 332 -1  N  PHE A 332   O  THR A 335           
SHEET    3   G 7 ARG A 373  GLU A 378 -1  N  ARG A 377   O  GLN A 329           
SHEET    4   G 7 ARG A 381  VAL A 388 -1  N  GLY A 386   O  PHE A 374           
SHEET    5   G 7 LYS A 303  ILE A 310 -1  N  TYR A 309   O  ALA A 385           
SHEET    6   G 7 ASN A 355  LEU A 362 -1  N  VAL A 360   O  PHE A 304           
SHEET    7   G 7 GLY A 339  LEU A 343 -1  N  GLU A 342   O  VAL A 359           
SHEET    1   H 2 LYS A 303  GLU A 305  0                                        
SHEET    2   H 2 LYS A 390  SER A 393 -1  N  SER A 393   O  LYS A 303           
SHEET    1   I 3 PRO B  10  GLY B  15  0                                        
SHEET    2   I 3 ARG B  74  ASP B  80  1  N  HIS B  75   O  PRO B  10           
SHEET    3   I 3 SER B  65  ASP B  70 -1  N  TYR B  69   O  TYR B  76           
SHEET    1   J 2 GLU B  54  ALA B  57  0                                        
SHEET    2   J 2 ILE B  60  ASN B  63 -1  N  ILE B  62   O  GLU B  55           
SHEET    1   K 3 ALA B 101  ALA B 106  0                                        
SHEET    2   K 3 ILE B 130  ASN B 135  1  N  ILE B 131   O  ALA B 101           
SHEET    3   K 3 ILE B 169  ARG B 171  1  N  VAL B 170   O  VAL B 132           
SHEET    1   L 7 LEU B 211  PRO B 213  0                                        
SHEET    2   L 7 VAL B 291  ALA B 293 -1  N  LEU B 292   O  LEU B 212           
SHEET    3   L 7 GLU B 241  VAL B 245 -1  N  VAL B 245   O  VAL B 291           
SHEET    4   L 7 GLN B 251  GLU B 259 -1  N  SER B 253   O  VAL B 242           
SHEET    5   L 7 ASN B 273  ARG B 279 -1  N  ARG B 279   O  THR B 254           
SHEET    6   L 7 GLY B 224  ARG B 230 -1  N  GLY B 229   O  VAL B 274           
SHEET    7   L 7 ASP B 216  ILE B 220 -1  N  ILE B 220   O  GLY B 224           
SHEET    1   M 2 ILE B 235  LYS B 237  0                                        
SHEET    2   M 2 GLU B 267  ARG B 269 -1  N  GLY B 268   O  ILE B 236           
SHEET    1   N 2 VAL B 258  MET B 260  0                                        
SHEET    2   N 2 LYS B 263  LEU B 265 -1  N  LEU B 265   O  VAL B 258           
SHEET    1   O 7 THR B 335  THR B 338  0                                        
SHEET    2   O 7 GLN B 329  PHE B 332 -1  N  PHE B 332   O  THR B 335           
SHEET    3   O 7 ARG B 373  GLU B 378 -1  N  ARG B 377   O  GLN B 329           
SHEET    4   O 7 ARG B 381  VAL B 388 -1  N  GLY B 386   O  PHE B 374           
SHEET    5   O 7 LYS B 303  ILE B 310 -1  N  TYR B 309   O  ALA B 385           
SHEET    6   O 7 ASN B 355  LEU B 362 -1  N  VAL B 360   O  PHE B 304           
SHEET    7   O 7 GLY B 339  LEU B 343 -1  N  GLU B 342   O  VAL B 359           
SHEET    1   P 2 LYS B 303  GLU B 305  0                                        
SHEET    2   P 2 LYS B 390  SER B 393 -1  N  SER B 393   O  LYS B 303           
LINK        MG    MG A 501                 OG1 THR A  25     1555   1555  1.94  
LINK        MG    MG A 501                 O2B GDP A 513     1555   1555  1.99  
LINK        MG    MG A 501                 O   HOH A 514     1555   1555  2.26  
LINK        MG    MG A 501                 O   HOH A 518     1555   1555  1.99  
LINK        MG    MG A 501                 O   HOH A 523     1555   1555  2.32  
LINK        MG    MG A 501                 O   HOH A 525     1555   1555  2.29  
LINK        MG    MG B 502                 O   HOH B 521     1555   1555  2.07  
LINK        MG    MG B 502                 O   HOH B 523     1555   1555  2.10  
LINK        MG    MG B 502                 O   HOH B 520     1555   1555  2.11  
LINK        MG    MG B 502                 O   HOH B 522     1555   1555  2.23  
LINK        MG    MG B 502                 O2B GDP B 514     1555   1555  1.97  
LINK        MG    MG B 502                 OG1 THR B  25     1555   1555  2.01  
SITE     1 AC1  6 THR A  25  GDP A 513  HOH A 514  HOH A 518                    
SITE     2 AC1  6 HOH A 523  HOH A 525                                          
SITE     1 AC2  6 THR B  25  GDP B 514  HOH B 520  HOH B 521                    
SITE     2 AC2  6 HOH B 522  HOH B 523                                          
SITE     1 AC3 23 ASP A  21  HIS A  22  GLY A  23  LYS A  24                    
SITE     2 AC3 23 THR A  25  THR A  26  PHE A  46  ASN A 135                    
SITE     3 AC3 23 LYS A 136  ASP A 138  MET A 139  SER A 173                    
SITE     4 AC3 23 ALA A 174  LEU A 175   MG A 501  HOH A 518                    
SITE     5 AC3 23 HOH A 523  HOH A 551  HOH A 613  HOH A 621                    
SITE     6 AC3 23 HOH A 643  HOH A 698  HOH A 717                               
SITE     1 AC4 23 ASP B  21  HIS B  22  GLY B  23  LYS B  24                    
SITE     2 AC4 23 THR B  25  THR B  26  PHE B  46  ASN B 135                    
SITE     3 AC4 23 LYS B 136  ASP B 138  MET B 139  SER B 173                    
SITE     4 AC4 23 ALA B 174  LEU B 175   MG B 502  HOH B 515                    
SITE     5 AC4 23 HOH B 516  HOH B 517  HOH B 518  HOH B 521                    
SITE     6 AC4 23 HOH B 522  HOH B 523  HOH B 621                               
CRYST1  243.120   61.080   66.910  90.00  90.00  90.00 P 21 21 2     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      0.004113  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016372  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014945        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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